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HEADER    TRANSFERASE/DNA                         11-JUL-11   3SUO              
TITLE     RB69 DNA POLYMERASE (Y567A) TERNARY COMPLEX WITH DTTP OPPOSITE 2AP (GC
TITLE    2 RICH 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, RB69POL, TRANSFERASE-DNA COMPLEX              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.XIA,W.H.KONIGSBERG,J.WANG                                           
REVDAT   3   30-NOV-11 3SUO    1       JRNL                                     
REVDAT   2   16-NOV-11 3SUO    1       JRNL                                     
REVDAT   1   09-NOV-11 3SUO    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) : 88.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 52104                          
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) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2800                            
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) : 3498                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.85                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4190                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 197                          
REMARK   3   BIN FREE R VALUE                    : 0.4740                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7337                                    
REMARK   3   NUCLEIC ACID ATOMS       : 591                                     
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 254                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.43                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.84000                                             
REMARK   3    B22 (A**2) : 2.43000                                              
REMARK   3    B33 (A**2) : -0.59000                                             
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): 0.313         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.234         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.176         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.601        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.898                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8222 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11242 ; 1.132 ; 2.057       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   903 ; 5.201 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   373 ;35.600 ;24.155       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1348 ;14.981 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    47 ;13.299 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1191 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6075 ; 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):  4497 ; 1.481 ; 4.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7292 ; 2.586 ; 6.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3725 ; 2.881 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3948 ; 4.272 ; 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   901        A   901                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.2730  -2.2210 -35.6960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1475 T22:   0.2264                                     
REMARK   3      T33:   0.1934 T12:   0.0450                                     
REMARK   3      T13:  -0.0075 T23:  -0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6832 L22:   0.0929                                     
REMARK   3      L33:   0.0510 L12:  -0.2202                                     
REMARK   3      L13:   0.2818 L23:  -0.0506                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1692 S12:  -0.1281 S13:   0.2121                       
REMARK   3      S21:   0.0048 S22:   0.1262 S23:  -0.0003                       
REMARK   3      S31:  -0.0186 S32:  -0.0434 S33:   0.0430                       
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):  24.7710   2.4680 -33.5120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1098 T22:   0.1103                                     
REMARK   3      T33:   0.0901 T12:   0.0007                                     
REMARK   3      T13:  -0.0036 T23:   0.0189                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2162 L22:   1.2247                                     
REMARK   3      L33:   0.4415 L12:   0.3026                                     
REMARK   3      L13:  -0.0789 L23:  -0.3747                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0094 S12:  -0.0210 S13:   0.0302                       
REMARK   3      S21:   0.0161 S22:  -0.0287 S23:  -0.1034                       
REMARK   3      S31:  -0.0302 S32:   0.0716 S33:   0.0194                       
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):  10.3110 -21.9930 -14.8020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1214 T22:   0.0921                                     
REMARK   3      T33:   0.0400 T12:   0.0006                                     
REMARK   3      T13:  -0.0117 T23:   0.0071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4420 L22:   1.0468                                     
REMARK   3      L33:   1.3929 L12:   0.2287                                     
REMARK   3      L13:   0.1694 L23:   0.0343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0536 S12:  -0.0499 S13:   0.0323                       
REMARK   3      S21:   0.0997 S22:  -0.0735 S23:   0.0029                       
REMARK   3      S31:   0.0799 S32:  -0.1023 S33:   0.0200                       
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):  -3.6410  -6.5650 -60.2870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1711 T22:   0.1631                                     
REMARK   3      T33:   0.0170 T12:  -0.0398                                     
REMARK   3      T13:  -0.0163 T23:   0.0278                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7876 L22:   0.7801                                     
REMARK   3      L33:   0.1712 L12:   0.5278                                     
REMARK   3      L13:  -0.2244 L23:  -0.1311                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0958 S12:   0.2257 S13:   0.0634                       
REMARK   3      S21:  -0.1399 S22:   0.1304 S23:   0.0283                       
REMARK   3      S31:   0.0138 S32:  -0.0960 S33:  -0.0345                       
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):   9.4380 -25.8670 -47.0350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1816 T22:   0.1177                                     
REMARK   3      T33:   0.0554 T12:   0.0126                                     
REMARK   3      T13:   0.0199 T23:  -0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5004 L22:   3.8241                                     
REMARK   3      L33:   0.3588 L12:   0.0419                                     
REMARK   3      L13:  -0.0803 L23:   0.6943                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0890 S12:   0.0675 S13:  -0.1156                       
REMARK   3      S21:   0.1456 S22:   0.0012 S23:   0.0856                       
REMARK   3      S31:   0.0826 S32:   0.0677 S33:   0.0878                       
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):  -9.4770 -22.7690 -48.0370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2009 T22:   0.1796                                     
REMARK   3      T33:   0.0709 T12:  -0.0178                                     
REMARK   3      T13:  -0.0027 T23:  -0.0151                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4320 L22:   0.9822                                     
REMARK   3      L33:   0.2290 L12:  -0.3025                                     
REMARK   3      L13:  -0.2904 L23:   0.3314                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1115 S12:  -0.0062 S13:  -0.1002                       
REMARK   3      S21:  -0.0346 S22:   0.0658 S23:   0.0861                       
REMARK   3      S31:   0.0519 S32:   0.0531 S33:   0.0457                       
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   900                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.2390 -20.5310 -27.8210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0992 T22:   0.1859                                     
REMARK   3      T33:   0.0478 T12:   0.0418                                     
REMARK   3      T13:   0.0064 T23:   0.0676                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9194 L22:   0.3936                                     
REMARK   3      L33:   1.2812 L12:  -0.1558                                     
REMARK   3      L13:   0.2817 L23:   0.1686                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1587 S12:  -0.4112 S13:  -0.1203                       
REMARK   3      S21:   0.0173 S22:   0.1356 S23:   0.0675                       
REMARK   3      S31:   0.0245 S32:  -0.1439 S33:   0.0231                       
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 3SUO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB066673.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-APR-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                  : SI(220)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52104                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.230                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 88.480                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.600                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
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) : 2.29                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9                               
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   (%): 52.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
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       37.20050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.44250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.03650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.44250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.20050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.03650            
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: 6920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 42640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 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     DT T   5   O4' -  C1' -  N1  ANGL. DEV. =   3.1 DEGREES          
REMARK 500     DC T   6   O4' -  C1' -  N1  ANGL. DEV. =   3.1 DEGREES          
REMARK 500     DC T   8   O4' -  C1' -  N1  ANGL. DEV. =   1.8 DEGREES          
REMARK 500     DC T   9   O4' -  C4' -  C3' ANGL. DEV. =  -2.5 DEGREES          
REMARK 500     DG T  15   O4' -  C1' -  N9  ANGL. DEV. =   2.9 DEGREES          
REMARK 500     DC P 103   O4' -  C1' -  N1  ANGL. DEV. =   3.2 DEGREES          
REMARK 500     DG P 104   O4' -  C1' -  N9  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DC P 105   O4' -  C1' -  N1  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DG P 112   O4' -  C1' -  N9  ANGL. DEV. =   4.0 DEGREES          
REMARK 500     DC P 113   O4' -  C1' -  N1  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    SER A  44       39.89    -98.35                                   
REMARK 500    ASN A  98       46.55    -84.57                                   
REMARK 500    ASP A 121       39.62    -96.40                                   
REMARK 500    PHE A 221      -71.34   -124.24                                   
REMARK 500    ASN A 255     -138.96   -141.15                                   
REMARK 500    MET A 256       12.86   -147.85                                   
REMARK 500    TYR A 257      -65.66   -126.08                                   
REMARK 500    ASN A 316       68.34   -152.67                                   
REMARK 500    ASN A 424       49.32     71.76                                   
REMARK 500    PRO A 458        2.75    -63.08                                   
REMARK 500    ASP A 579      108.66   -167.26                                   
REMARK 500    THR A 622      -64.44     70.44                                   
REMARK 500    LEU A 680       16.12   -140.76                                   
REMARK 500    GLU A 716       48.88     29.86                                   
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 A1099        DISTANCE =  6.39 ANGSTROMS                       
REMARK 525    HOH A1146        DISTANCE =  6.25 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 902  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 623   OD1                                                    
REMARK 620 2 TTP A 901   O2B  89.1                                              
REMARK 620 3 TTP A 901   O1G 162.8  75.9                                        
REMARK 620 4 LEU A 412   O    84.3  85.3 102.6                                  
REMARK 620 5 TTP A 901   O2A  86.0  80.1  83.2 162.6                            
REMARK 620 6 ASP A 411   OD1 118.1 143.0  79.1  73.9 123.5                      
REMARK 620 7 ASP A 411   OD2  89.8 161.9 101.8 112.5  81.9  51.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 904  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 505   O                                                      
REMARK 620 2 LYS A 531   O   156.7                                              
REMARK 620 3 ASN A 507   OD1  86.1  77.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 903  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 411   OD2                                                    
REMARK 620 2 TTP A 901   O2A  75.5                                              
REMARK 620 3 ASP A 623   OD2  90.3  79.5                                        
REMARK 620 4 HOH A 979   O    60.4  85.9 149.9                                  
REMARK 620 N                    1     2     3                                   
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 GLU A 116   OE1                                                    
REMARK 620 2 GLU A 116   OE2  46.0                                              
REMARK 620 3 HOH A1128   O   151.2 136.3                                        
REMARK 620 4 HOH A 986   O    78.2  68.1  79.1                                  
REMARK 620 N                    1     2     3                                   
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 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 903                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 904                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 905                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 906                  
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: 3SQ4   RELATED DB: PDB                                   
REMARK 900 RB69 DNA POLYMERASE TERNARY COMPLEX WITH DTTP OPPOSITE 2AP           
REMARK 900 (GC 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: 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  3SUO A    1   900  UNP    Q38087   DPOL_BPR69       1    900             
DBREF  3SUO T    3    18  PDB    3SUO     3SUO             3     18             
DBREF  3SUO P  103   115  PDB    3SUO     3SUO           103    115             
SEQADV 3SUO ALA A  222  UNP  Q38087    ASP   222 ENGINEERED MUTATION            
SEQADV 3SUO ALA A  327  UNP  Q38087    ASP   327 ENGINEERED MUTATION            
SEQADV 3SUO ALA A  567  UNP  Q38087    TYR   567 ENGINEERED MUTATION            
SEQRES   1 A  900  MET LYS GLU PHE TYR LEU THR VAL GLU GLN ILE GLY ASP          
SEQRES   2 A  900  SER ILE PHE GLU ARG TYR ILE ASP SER ASN GLY ARG GLU          
SEQRES   3 A  900  ARG THR ARG GLU VAL GLU TYR LYS PRO SER LEU PHE ALA          
SEQRES   4 A  900  HIS CYS PRO GLU SER GLN ALA THR LYS TYR PHE ASP ILE          
SEQRES   5 A  900  TYR GLY LYS PRO CYS THR ARG LYS LEU PHE ALA ASN MET          
SEQRES   6 A  900  ARG ASP ALA SER GLN TRP ILE LYS ARG MET GLU ASP ILE          
SEQRES   7 A  900  GLY LEU GLU ALA LEU GLY MET ASP ASP PHE LYS LEU ALA          
SEQRES   8 A  900  TYR LEU SER ASP THR TYR ASN TYR GLU ILE LYS TYR ASP          
SEQRES   9 A  900  HIS THR LYS ILE ARG VAL ALA ASN PHE ASP ILE GLU VAL          
SEQRES  10 A  900  THR SER PRO ASP GLY PHE PRO GLU PRO SER GLN ALA LYS          
SEQRES  11 A  900  HIS PRO ILE ASP ALA ILE THR HIS TYR ASP SER ILE ASP          
SEQRES  12 A  900  ASP ARG PHE TYR VAL PHE ASP LEU LEU ASN SER PRO TYR          
SEQRES  13 A  900  GLY ASN VAL GLU GLU TRP SER ILE GLU ILE ALA ALA LYS          
SEQRES  14 A  900  LEU GLN GLU GLN GLY GLY ASP GLU VAL PRO SER GLU ILE          
SEQRES  15 A  900  ILE ASP LYS ILE ILE TYR MET PRO PHE ASP ASN GLU LYS          
SEQRES  16 A  900  GLU LEU LEU MET GLU TYR LEU ASN PHE TRP GLN GLN LYS          
SEQRES  17 A  900  THR PRO VAL ILE LEU THR GLY TRP ASN VAL GLU SER PHE          
SEQRES  18 A  900  ALA ILE PRO TYR VAL TYR ASN ARG ILE LYS ASN ILE PHE          
SEQRES  19 A  900  GLY GLU SER THR ALA LYS ARG LEU SER PRO HIS ARG LYS          
SEQRES  20 A  900  THR ARG VAL LYS VAL ILE GLU ASN MET TYR GLY SER ARG          
SEQRES  21 A  900  GLU ILE ILE THR LEU PHE GLY ILE SER VAL LEU ASP TYR          
SEQRES  22 A  900  ILE ASP LEU TYR LYS LYS PHE SER PHE THR ASN GLN PRO          
SEQRES  23 A  900  SER TYR SER LEU ASP TYR ILE SER GLU PHE GLU LEU ASN          
SEQRES  24 A  900  VAL GLY LYS LEU LYS TYR ASP GLY PRO ILE SER LYS LEU          
SEQRES  25 A  900  ARG GLU SER ASN HIS GLN ARG TYR ILE SER TYR ASN ILE          
SEQRES  26 A  900  ILE ALA VAL TYR ARG VAL LEU GLN ILE ASP ALA LYS ARG          
SEQRES  27 A  900  GLN PHE ILE ASN LEU SER LEU ASP MET GLY TYR TYR ALA          
SEQRES  28 A  900  LYS ILE GLN ILE GLN SER VAL PHE SER PRO ILE LYS THR          
SEQRES  29 A  900  TRP ASP ALA ILE ILE PHE ASN SER LEU LYS GLU GLN ASN          
SEQRES  30 A  900  LYS VAL ILE PRO GLN GLY ARG SER HIS PRO VAL GLN PRO          
SEQRES  31 A  900  TYR PRO GLY ALA PHE VAL LYS GLU PRO ILE PRO ASN ARG          
SEQRES  32 A  900  TYR LYS TYR VAL MET SER PHE ASP LEU THR SER LEU TYR          
SEQRES  33 A  900  PRO SER ILE ILE ARG GLN VAL ASN ILE SER PRO GLU THR          
SEQRES  34 A  900  ILE ALA GLY THR PHE LYS VAL ALA PRO LEU HIS ASP TYR          
SEQRES  35 A  900  ILE ASN ALA VAL ALA GLU ARG PRO SER ASP VAL TYR SER          
SEQRES  36 A  900  CYS SER PRO ASN GLY MET MET TYR TYR LYS ASP ARG ASP          
SEQRES  37 A  900  GLY VAL VAL PRO THR GLU ILE THR LYS VAL PHE ASN GLN          
SEQRES  38 A  900  ARG LYS GLU HIS LYS GLY TYR MET LEU ALA ALA GLN ARG          
SEQRES  39 A  900  ASN GLY GLU ILE ILE LYS GLU ALA LEU HIS ASN PRO ASN          
SEQRES  40 A  900  LEU SER VAL ASP GLU PRO LEU ASP VAL ASP TYR ARG PHE          
SEQRES  41 A  900  ASP PHE SER ASP GLU ILE LYS GLU LYS ILE LYS LYS LEU          
SEQRES  42 A  900  SER ALA LYS SER LEU ASN GLU MET LEU PHE ARG ALA GLN          
SEQRES  43 A  900  ARG THR GLU VAL ALA GLY MET THR ALA GLN ILE ASN ARG          
SEQRES  44 A  900  LYS LEU LEU ILE ASN SER LEU ALA GLY ALA LEU GLY ASN          
SEQRES  45 A  900  VAL TRP PHE ARG TYR TYR ASP LEU ARG ASN ALA THR ALA          
SEQRES  46 A  900  ILE THR THR PHE GLY GLN MET ALA LEU GLN TRP ILE GLU          
SEQRES  47 A  900  ARG LYS VAL ASN GLU TYR LEU ASN GLU VAL CYS GLY THR          
SEQRES  48 A  900  GLU GLY GLU ALA PHE VAL LEU TYR GLY ASP THR ASP SER          
SEQRES  49 A  900  ILE TYR VAL SER ALA ASP LYS ILE ILE ASP LYS VAL GLY          
SEQRES  50 A  900  GLU SER LYS PHE ARG ASP THR ASN HIS TRP VAL ASP PHE          
SEQRES  51 A  900  LEU ASP LYS PHE ALA ARG GLU ARG MET GLU PRO ALA ILE          
SEQRES  52 A  900  ASP ARG GLY PHE ARG GLU MET CYS GLU TYR MET ASN ASN          
SEQRES  53 A  900  LYS GLN HIS LEU MET PHE MET ASP ARG GLU ALA ILE ALA          
SEQRES  54 A  900  GLY PRO PRO LEU GLY SER LYS GLY ILE GLY GLY PHE TRP          
SEQRES  55 A  900  THR GLY LYS LYS ARG TYR ALA LEU ASN VAL TRP ASP MET          
SEQRES  56 A  900  GLU GLY THR ARG TYR ALA GLU PRO LYS LEU LYS ILE MET          
SEQRES  57 A  900  GLY LEU GLU THR GLN LYS SER SER THR PRO LYS ALA VAL          
SEQRES  58 A  900  GLN LYS ALA LEU LYS GLU CYS ILE ARG ARG MET LEU GLN          
SEQRES  59 A  900  GLU GLY GLU GLU SER LEU GLN GLU TYR PHE LYS GLU PHE          
SEQRES  60 A  900  GLU LYS GLU PHE ARG GLN LEU ASN TYR ILE SER ILE ALA          
SEQRES  61 A  900  SER VAL SER SER ALA ASN ASN ILE ALA LYS TYR ASP VAL          
SEQRES  62 A  900  GLY GLY PHE PRO GLY PRO LYS CYS PRO PHE HIS ILE ARG          
SEQRES  63 A  900  GLY ILE LEU THR TYR ASN ARG ALA ILE LYS GLY ASN ILE          
SEQRES  64 A  900  ASP ALA PRO GLN VAL VAL GLU GLY GLU LYS VAL TYR VAL          
SEQRES  65 A  900  LEU PRO LEU ARG GLU GLY ASN PRO PHE GLY ASP LYS CYS          
SEQRES  66 A  900  ILE ALA TRP PRO SER GLY THR GLU ILE THR ASP LEU ILE          
SEQRES  67 A  900  LYS ASP ASP VAL LEU HIS TRP MET ASP TYR THR VAL LEU          
SEQRES  68 A  900  LEU GLU LYS THR PHE ILE LYS PRO LEU GLU GLY PHE THR          
SEQRES  69 A  900  SER ALA ALA LYS LEU ASP TYR GLU LYS LYS ALA SER LEU          
SEQRES  70 A  900  PHE ASP MET                                                  
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 3SUO 2PR T    4   DG  2-AMINOPURINE-2'-DEOXYRIBO-5'-MONOPHOSPHA          
MODRES 3SUO 2DA P  115   DA  2',3'-DIDEOXYADENOSINE-5'-MONOPHOSPHATE            
HET    2PR  T   4      21                                                       
HET    2DA  P 115      20                                                       
HET    TTP  A 901      29                                                       
HET     CA  A 902       1                                                       
HET     CA  A 903       1                                                       
HET     CA  A 904       1                                                       
HET     CA  A 905       1                                                       
HET     CA  A 906       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   *254(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  SER A  310  5                                   3    
HELIX   14  14 LYS A  311  GLN A  339  1                                  29    
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 PRO A  438  ASN A  444  1                                   7    
HELIX   20  20 GLY A  469  LEU A  503  1                                  35    
HELIX   21  21 SER A  523  LYS A  531  1                                   9    
HELIX   22  22 SER A  534  LEU A  570  1                                  37    
HELIX   23  23 ASP A  579  GLY A  610  1                                  32    
HELIX   24  24 ALA A  629  GLY A  637  1                                   9    
HELIX   25  25 GLU A  638  PHE A  641  5                                   4    
HELIX   26  26 ASP A  643  ARG A  658  1                                  16    
HELIX   27  27 ARG A  658  MET A  674  1                                  17    
HELIX   28  28 LEU A  730  LYS A  734  5                                   5    
HELIX   29  29 PRO A  738  GLU A  755  1                                  18    
HELIX   30  30 GLY A  756  PHE A  771  1                                  16    
HELIX   31  31 ARG A  772  LEU A  774  5                                   3    
HELIX   32  32 ASN A  787  LYS A  790  5                                   4    
HELIX   33  33 PRO A  802  LYS A  816  1                                  15    
HELIX   34  34 THR A  855  MET A  866  1                                  12    
HELIX   35  35 ASP A  867  PHE A  876  1                                  10    
HELIX   36  36 PHE A  876  ALA A  887  1                                  12    
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 ALA A 135  ASP A 140 -1  N  ILE A 136   O  PHE A 149           
SHEET    4   C 6 VAL A 110  GLU A 116 -1  N  ASN A 112   O  TYR A 139           
SHEET    5   C 6 ILE A 212  THR A 214  1  O  ILE A 212   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 THR A 248  VAL A 252  0                                        
SHEET    2   D 2 GLU A 261  LEU A 265 -1  O  ILE A 262   N  LYS A 251           
SHEET    1   E 7 ASN A 402  ARG A 403  0                                        
SHEET    2   E 7 GLY A 700  GLY A 704 -1  O  TRP A 702   N  ASN A 402           
SHEET    3   E 7 ARG A 707  MET A 715 -1  O  ARG A 707   N  THR A 703           
SHEET    4   E 7 MET A 683  ALA A 689 -1  N  ILE A 688   O  TRP A 713           
SHEET    5   E 7 VAL A 407  LEU A 412 -1  N  VAL A 407   O  ALA A 689           
SHEET    6   E 7 SER A 624  SER A 628 -1  O  VAL A 627   N  MET A 408           
SHEET    7   E 7 VAL A 617  ASP A 621 -1  N  TYR A 619   O  TYR A 626           
SHEET    1   F 4 ASN A 402  ARG A 403  0                                        
SHEET    2   F 4 GLY A 700  GLY A 704 -1  O  TRP A 702   N  ASN A 402           
SHEET    3   F 4 ARG A 707  MET A 715 -1  O  ARG A 707   N  THR A 703           
SHEET    4   F 4 THR A 718  MET A 728 -1  O  LYS A 724   N  VAL A 712           
SHEET    1   G 3 ILE A 430  THR A 433  0                                        
SHEET    2   G 3 MET A 461  TYR A 463 -1  O  MET A 462   N  ALA A 431           
SHEET    3   G 3 SER A 455  SER A 457 -1  N  SER A 455   O  TYR A 463           
SHEET    1   H 3 SER A 781  SER A 784  0                                        
SHEET    2   H 3 LYS A 829  PRO A 834 -1  O  VAL A 830   N  SER A 783           
SHEET    3   H 3 CYS A 845  PRO A 849 -1  O  TRP A 848   N  TYR A 831           
SHEET    1   I 2 ASP A 792  VAL A 793  0                                        
SHEET    2   I 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  1.61  
LINK         O3' 2PR T   4                 P    DT T   5     1555   1555  1.59  
LINK         O3'  DG P 114                 P   2DA P 115     1555   1555  1.60  
LINK         OD1 ASP A 623                CA    CA A 902     1555   1555  2.24  
LINK         O2B TTP A 901                CA    CA A 902     1555   1555  2.24  
LINK         O1G TTP A 901                CA    CA A 902     1555   1555  2.31  
LINK         O   ASN A 505                CA    CA A 904     1555   1555  2.36  
LINK         O   LYS A 531                CA    CA A 904     1555   1555  2.37  
LINK         OD1 ASN A 507                CA    CA A 904     1555   1555  2.37  
LINK         O   LEU A 412                CA    CA A 902     1555   1555  2.40  
LINK         O2A TTP A 901                CA    CA A 902     1555   1555  2.42  
LINK         OD1 ASP A 411                CA    CA A 902     1555   1555  2.48  
LINK         OD2 ASP A 411                CA    CA A 903     1555   1555  2.56  
LINK         OE1 GLU A 116                CA    CA A 906     1555   1555  2.56  
LINK         OD2 ASP A 411                CA    CA A 902     1555   1555  2.59  
LINK         O2A TTP A 901                CA    CA A 903     1555   1555  2.80  
LINK         OD2 ASP A 623                CA    CA A 903     1555   1555  2.83  
LINK         OE2 GLU A 116                CA    CA A 906     1555   1555  2.95  
LINK        CA    CA A 906                 O   HOH A1128     1555   1555  2.62  
LINK        CA    CA A 906                 O   HOH A 986     1555   1555  2.76  
LINK        CA    CA A 905                 O   HOH A 982     1555   1555  2.97  
LINK        CA    CA A 903                 O   HOH A 979     1555   1555  3.09  
SITE     1 AC1 18 ASP A 411  LEU A 412  THR A 413  SER A 414                    
SITE     2 AC1 18 LEU A 415  TYR A 416  ARG A 482  LYS A 486                    
SITE     3 AC1 18 LYS A 560  ASN A 564  THR A 622  ASP A 623                    
SITE     4 AC1 18  CA A 902   CA A 903  HOH A 982  HOH A1014                    
SITE     5 AC1 18 2DA P 115  2PR T   4                                          
SITE     1 AC2  4 ASP A 411  LEU A 412  ASP A 623  TTP A 901                    
SITE     1 AC3  5 ASP A 411  ASP A 623  SER A 624  TTP A 901                    
SITE     2 AC3  5 HOH A 979                                                     
SITE     1 AC4  3 ASN A 505  ASN A 507  LYS A 531                               
SITE     1 AC5  2 GLU A 716  HOH A 982                                          
SITE     1 AC6  3 GLU A 116  HOH A 986  HOH A1128                               
CRYST1   74.401  120.073  130.885  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      0.013441  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008328  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007640        0.00000                         
ATOM      1  N   MET A   1      37.816 -17.806 -35.400  1.00 65.01           N  
ANISOU    1  N   MET A   1     7856   7963   8880    575    525    593       N  
ATOM      2  CA  MET A   1      36.496 -17.395 -35.952  1.00 64.68           C  
ANISOU    2  CA  MET A   1     7928   7943   8706    538    522    528       C  
ATOM      3  C   MET A   1      36.302 -15.878 -35.887  1.00 61.99           C  
ANISOU    3  C   MET A   1     7569   7648   8336    491    471    514       C  
ATOM      4  O   MET A   1      37.068 -15.172 -35.222  1.00 60.49           O  
ANISOU    4  O   MET A   1     7287   7480   8215    480    420    551       O  
ATOM      5  CB  MET A   1      35.359 -18.125 -35.222  1.00 66.36           C  
ANISOU    5  CB  MET A   1     8205   8171   8838    523    452    503       C  
ATOM      6  CG  MET A   1      35.010 -17.581 -33.823  1.00 72.89           C  
ANISOU    6  CG  MET A   1     8995   9051   9648    484    324    512       C  
ATOM      7  SD  MET A   1      33.461 -18.243 -33.129  1.00 78.25           S  
ANISOU    7  SD  MET A   1     9765   9750  10216    457    258    474       S  
ATOM      8  CE  MET A   1      32.274 -17.757 -34.389  1.00 77.64           C  
ANISOU    8  CE  MET A   1     9791   9674  10035    433    306    414       C  
ATOM      9  N   LYS A   2      35.286 -15.387 -36.596  1.00 59.58           N  
ANISOU    9  N   LYS A   2     7353   7353   7931    463    484    464       N  
ATOM     10  CA  LYS A   2      34.890 -13.985 -36.505  1.00 57.61           C  
ANISOU   10  CA  LYS A   2     7100   7146   7643    418    432    447       C  
ATOM     11  C   LYS A   2      34.121 -13.746 -35.206  1.00 53.51           C  
ANISOU   11  C   LYS A   2     6579   6671   7081    384    317    439       C  
ATOM     12  O   LYS A   2      33.125 -14.422 -34.929  1.00 51.83           O  
ANISOU   12  O   LYS A   2     6429   6462   6804    379    291    415       O  
ATOM     13  CB  LYS A   2      34.045 -13.563 -37.714  1.00 58.14           C  
ANISOU   13  CB  LYS A   2     7262   7204   7623    398    481    401       C  
ATOM     14  CG  LYS A   2      34.842 -13.189 -38.962  1.00 64.68           C  
ANISOU   14  CG  LYS A   2     8092   7999   8484    413    584    407       C  
ATOM     15  CD  LYS A   2      35.923 -12.147 -38.655  1.00 69.21           C  
ANISOU   15  CD  LYS A   2     8563   8591   9145    407    572    442       C  
ATOM     16  CE  LYS A   2      36.431 -11.442 -39.910  1.00 71.29           C  
ANISOU   16  CE  LYS A   2     8839   8829   9417    406    663    438       C  
ATOM     17  NZ  LYS A   2      35.656 -10.203 -40.210  1.00 68.99           N  
ANISOU   17  NZ  LYS A   2     8593   8568   9051    359    623    407       N  
ATOM     18  N   GLU A   3      34.600 -12.795 -34.411  1.00 48.93           N  
ANISOU   18  N   GLU A   3     5933   6121   6538    360    252    461       N  
ATOM     19  CA  GLU A   3      33.949 -12.434 -33.156  1.00 47.13           C  
ANISOU   19  CA  GLU A   3     5710   5930   6267    324    150    454       C  
ATOM     20  C   GLU A   3      32.519 -11.939 -33.381  1.00 43.81           C  
ANISOU   20  C   GLU A   3     5372   5529   5746    295    137    404       C  
ATOM     21  O   GLU A   3      32.214 -11.349 -34.418  1.00 43.63           O  
ANISOU   21  O   GLU A   3     5382   5501   5693    289    184    380       O  
ATOM     22  CB  GLU A   3      34.761 -11.373 -32.407  1.00 46.60           C  
ANISOU   22  CB  GLU A   3     5569   5885   6252    296     89    485       C  
ATOM     23  CG  GLU A   3      36.238 -11.715 -32.259  1.00 51.23           C  
ANISOU   23  CG  GLU A   3     6059   6451   6955    321     98    545       C  
ATOM     24  CD  GLU A   3      36.932 -10.943 -31.150  1.00 53.58           C  
ANISOU   24  CD  GLU A   3     6290   6770   7299    284      4    583       C  
ATOM     25  OE1 GLU A   3      37.957 -11.449 -30.640  1.00 58.61           O  
ANISOU   25  OE1 GLU A   3     6849   7393   8026    298    -23    639       O  
ATOM     26  OE2 GLU A   3      36.462  -9.845 -30.778  1.00 51.33           O  
ANISOU   26  OE2 GLU A   3     6031   6512   6961    239    -46    560       O  
ATOM     27  N   PHE A   4      31.641 -12.216 -32.423  1.00 38.73           N  
ANISOU   27  N   PHE A   4     4761   4904   5052    277     75    390       N  
ATOM     28  CA  PHE A   4      30.300 -11.646 -32.429  1.00 35.88           C  
ANISOU   28  CA  PHE A   4     4462   4563   4610    248     54    351       C  
ATOM     29  C   PHE A   4      29.833 -11.330 -31.021  1.00 35.13           C  
ANISOU   29  C   PHE A   4     4368   4493   4488    218    -24    349       C  
ATOM     30  O   PHE A   4      30.148 -12.048 -30.074  1.00 36.92           O  
ANISOU   30  O   PHE A   4     4577   4717   4732    222    -63    371       O  
ATOM     31  CB  PHE A   4      29.305 -12.556 -33.152  1.00 34.61           C  
ANISOU   31  CB  PHE A   4     4371   4385   4394    259     92    325       C  
ATOM     32  CG  PHE A   4      29.154 -13.925 -32.543  1.00 33.40           C  
ANISOU   32  CG  PHE A   4     4231   4219   4239    277     79    334       C  
ATOM     33  CD1 PHE A   4      30.023 -14.955 -32.884  1.00 34.16           C  
ANISOU   33  CD1 PHE A   4     4309   4285   4385    314    123    357       C  
ATOM     34  CD2 PHE A   4      28.116 -14.195 -31.663  1.00 30.33           C  
ANISOU   34  CD2 PHE A   4     3875   3847   3800    257     29    321       C  
ATOM     35  CE1 PHE A   4      29.871 -16.238 -32.338  1.00 32.58           C  
ANISOU   35  CE1 PHE A   4     4126   4071   4184    332    112    367       C  
ATOM     36  CE2 PHE A   4      27.951 -15.474 -31.113  1.00 33.46           C  
ANISOU   36  CE2 PHE A   4     4289   4232   4192    272     17    329       C  
ATOM     37  CZ  PHE A   4      28.832 -16.498 -31.457  1.00 32.99           C  
ANISOU   37  CZ  PHE A   4     4213   4141   4181    308     56    352       C  
ATOM     38  N   TYR A   5      29.089 -10.241 -30.890  1.00 35.25           N  
ANISOU   38  N   TYR A   5     4407   4526   4461    188    -45    325       N  
ATOM     39  CA  TYR A   5      28.526  -9.845 -29.604  1.00 34.01           C  
ANISOU   39  CA  TYR A   5     4266   4386   4269    158   -105    317       C  
ATOM     40  C   TYR A   5      27.457 -10.817 -29.120  1.00 32.03           C  
ANISOU   40  C   TYR A   5     4063   4135   3971    160   -114    303       C  
ATOM     41  O   TYR A   5      26.847 -11.550 -29.900  1.00 31.49           O  
ANISOU   41  O   TYR A   5     4025   4057   3885    178    -77    291       O  
ATOM     42  CB  TYR A   5      27.957  -8.414 -29.666  1.00 33.84           C  
ANISOU   42  CB  TYR A   5     4261   4377   4218    130   -112    294       C  
ATOM     43  CG  TYR A   5      26.708  -8.261 -30.512  1.00 34.36           C  
ANISOU   43  CG  TYR A   5     4372   4442   4241    132    -77    265       C  
ATOM     44  CD1 TYR A   5      26.800  -7.971 -31.876  1.00 34.66           C  
ANISOU   44  CD1 TYR A   5     4411   4471   4287    142    -31    260       C  
ATOM     45  CD2 TYR A   5      25.431  -8.390 -29.948  1.00 33.27           C  
ANISOU   45  CD2 TYR A   5     4275   4309   4056    120    -91    245       C  
ATOM     46  CE1 TYR A   5      25.653  -7.820 -32.657  1.00 35.51           C  
ANISOU   46  CE1 TYR A   5     4562   4576   4356    138    -11    239       C  
ATOM     47  CE2 TYR A   5      24.273  -8.236 -30.727  1.00 32.88           C  
ANISOU   47  CE2 TYR A   5     4257   4257   3978    119    -67    227       C  
ATOM     48  CZ  TYR A   5      24.400  -7.954 -32.079  1.00 34.27           C  
ANISOU   48  CZ  TYR A   5     4435   4425   4162    127    -33    225       C  
ATOM     49  OH  TYR A   5      23.287  -7.800 -32.862  1.00 37.53           O  
ANISOU   49  OH  TYR A   5     4881   4832   4548    121    -20    213       O  
ATOM     50  N   LEU A   6      27.246 -10.814 -27.813  1.00 31.65           N  
ANISOU   50  N   LEU A   6     4028   4095   3902    138   -165    306       N  
ATOM     51  CA  LEU A   6      26.163 -11.551 -27.207  1.00 29.25           C  
ANISOU   51  CA  LEU A   6     3771   3792   3551    134   -174    292       C  
ATOM     52  C   LEU A   6      25.117 -10.555 -26.723  1.00 29.88           C  
ANISOU   52  C   LEU A   6     3886   3882   3585    105   -181    265       C  
ATOM     53  O   LEU A   6      23.964 -10.602 -27.152  1.00 29.55           O  
ANISOU   53  O   LEU A   6     3872   3840   3515    107   -154    245       O  
ATOM     54  CB  LEU A   6      26.686 -12.416 -26.069  1.00 28.83           C  
ANISOU   54  CB  LEU A   6     3714   3734   3505    131   -219    318       C  
ATOM     55  CG  LEU A   6      27.624 -13.575 -26.442  1.00 30.40           C  
ANISOU   55  CG  LEU A   6     3879   3917   3756    165   -209    348       C  
ATOM     56  CD1 LEU A   6      28.220 -14.143 -25.185  1.00 32.27           C  
ANISOU   56  CD1 LEU A   6     4107   4149   4005    155   -270    380       C  
ATOM     57  CD2 LEU A   6      26.902 -14.677 -27.199  1.00 30.77           C  
ANISOU   57  CD2 LEU A   6     3957   3949   3783    191   -164    334       C  
ATOM     58  N   THR A   7      25.526  -9.644 -25.843  1.00 29.45           N  
ANISOU   58  N   THR A   7     3830   3832   3528     77   -217    269       N  
ATOM     59  CA  THR A   7      24.640  -8.612 -25.334  1.00 28.92           C  
ANISOU   59  CA  THR A   7     3800   3768   3422     51   -216    244       C  
ATOM     60  C   THR A   7      25.399  -7.311 -25.254  1.00 30.47           C  
ANISOU   60  C   THR A   7     3978   3965   3635     30   -234    246       C  
ATOM     61  O   THR A   7      26.625  -7.312 -25.159  1.00 34.38           O  
ANISOU   61  O   THR A   7     4436   4460   4166     26   -264    273       O  
ATOM     62  CB  THR A   7      24.176  -8.924 -23.912  1.00 32.09           C  
ANISOU   62  CB  THR A   7     4248   4164   3781     27   -244    241       C  
ATOM     63  OG1 THR A   7      25.320  -8.984 -23.047  1.00 33.85           O  
ANISOU   63  OG1 THR A   7     4463   4384   4015      7   -300    267       O  
ATOM     64  CG2 THR A   7      23.395 -10.238 -23.858  1.00 29.21           C  
ANISOU   64  CG2 THR A   7     3903   3797   3399     44   -229    240       C  
ATOM     65  N   VAL A   8      24.673  -6.198 -25.261  1.00 30.82           N  
ANISOU   65  N   VAL A   8     4046   4007   3656     15   -215    223       N  
ATOM     66  CA  VAL A   8      25.289  -4.884 -25.145  1.00 31.64           C  
ANISOU   66  CA  VAL A   8     4144   4108   3768     -9   -231    222       C  
ATOM     67  C   VAL A   8      24.392  -3.976 -24.313  1.00 32.20           C  
ANISOU   67  C   VAL A   8     4270   4167   3795    -35   -224    196       C  
ATOM     68  O   VAL A   8      23.176  -4.000 -24.470  1.00 35.57           O  
ANISOU   68  O   VAL A   8     4719   4590   4204    -23   -185    177       O  
ATOM     69  CB  VAL A   8      25.599  -4.268 -26.542  1.00 32.52           C  
ANISOU   69  CB  VAL A   8     4216   4225   3917      8   -200    222       C  
ATOM     70  CG1 VAL A   8      24.323  -4.099 -27.372  1.00 34.20           C  
ANISOU   70  CG1 VAL A   8     4445   4436   4115     25   -154    200       C  
ATOM     71  CG2 VAL A   8      26.336  -2.951 -26.408  1.00 31.62           C  
ANISOU   71  CG2 VAL A   8     4092   4107   3816    -19   -219    225       C  
ATOM     72  N   GLU A   9      25.001  -3.203 -23.416  1.00 32.84           N  
ANISOU   72  N   GLU A   9     4377   4240   3862    -72   -261    199       N  
ATOM     73  CA  GLU A   9      24.285  -2.253 -22.566  1.00 34.28           C  
ANISOU   73  CA  GLU A   9     4624   4403   4000    -99   -249    173       C  
ATOM     74  C   GLU A   9      25.056  -0.951 -22.389  1.00 33.07           C  
ANISOU   74  C   GLU A   9     4479   4238   3849   -133   -275    174       C  
ATOM     75  O   GLU A   9      26.278  -0.965 -22.311  1.00 34.87           O  
ANISOU   75  O   GLU A   9     4677   4473   4101   -151   -326    200       O  
ATOM     76  CB  GLU A   9      24.040  -2.856 -21.174  1.00 33.06           C  
ANISOU   76  CB  GLU A   9     4531   4235   3796   -124   -272    172       C  
ATOM     77  CG  GLU A   9      23.313  -4.197 -21.170  1.00 38.82           C  
ANISOU   77  CG  GLU A   9     5258   4973   4518    -97   -252    174       C  
ATOM     78  CD  GLU A   9      21.829  -4.101 -21.513  1.00 40.92           C  
ANISOU   78  CD  GLU A   9     5538   5233   4777    -75   -185    150       C  
ATOM     79  OE1 GLU A   9      21.325  -2.986 -21.784  1.00 41.70           O  
ANISOU   79  OE1 GLU A   9     5645   5321   4880    -75   -151    132       O  
ATOM     80  OE2 GLU A   9      21.160  -5.157 -21.505  1.00 40.99           O  
ANISOU   80  OE2 GLU A   9     5546   5247   4781    -57   -169    152       O  
ATOM     81  N   GLN A  10      24.343   0.168 -22.315  1.00 34.11           N  
ANISOU   81  N   GLN A  10     4649   4352   3960   -142   -239    147       N  
ATOM     82  CA  GLN A  10      24.947   1.417 -21.871  1.00 34.80           C  
ANISOU   82  CA  GLN A  10     4769   4420   4035   -182   -263    143       C  
ATOM     83  C   GLN A  10      24.606   1.627 -20.401  1.00 37.84           C  
ANISOU   83  C   GLN A  10     5248   4775   4354   -222   -273    127       C  
ATOM     84  O   GLN A  10      23.431   1.639 -20.026  1.00 40.85           O  
ANISOU   84  O   GLN A  10     5675   5138   4706   -211   -218    102       O  
ATOM     85  CB  GLN A  10      24.472   2.619 -22.692  1.00 34.78           C  
ANISOU   85  CB  GLN A  10     4758   4408   4050   -170   -217    125       C  
ATOM     86  CG  GLN A  10      25.088   3.937 -22.204  1.00 35.41           C  
ANISOU   86  CG  GLN A  10     4879   4464   4113   -215   -242    119       C  
ATOM     87  CD  GLN A  10      24.468   5.203 -22.791  1.00 39.35           C  
ANISOU   87  CD  GLN A  10     5387   4943   4620   -205   -192     98       C  
ATOM     88  OE1 GLN A  10      23.717   5.165 -23.769  1.00 36.41           O  
ANISOU   88  OE1 GLN A  10     4978   4580   4278   -164   -146     94       O  
ATOM     89  NE2 GLN A  10      24.795   6.344 -22.181  1.00 38.00           N  
ANISOU   89  NE2 GLN A  10     5272   4742   4423   -246   -204     87       N  
ATOM     90  N   ILE A  11      25.634   1.766 -19.572  1.00 39.89           N  
ANISOU   90  N   ILE A  11     5536   5026   4593   -271   -342    144       N  
ATOM     91  CA  ILE A  11      25.457   2.159 -18.180  1.00 41.72           C  
ANISOU   91  CA  ILE A  11     5876   5222   4753   -322   -357    128       C  
ATOM     92  C   ILE A  11      26.296   3.411 -17.955  1.00 42.07           C  
ANISOU   92  C   ILE A  11     5950   5246   4790   -372   -399    131       C  
ATOM     93  O   ILE A  11      27.535   3.353 -17.890  1.00 41.98           O  
ANISOU   93  O   ILE A  11     5905   5245   4801   -403   -478    165       O  
ATOM     94  CB  ILE A  11      25.822   1.015 -17.195  1.00 43.30           C  
ANISOU   94  CB  ILE A  11     6106   5423   4921   -346   -414    150       C  
ATOM     95  CG1 ILE A  11      24.865  -0.174 -17.385  1.00 45.22           C  
ANISOU   95  CG1 ILE A  11     6330   5683   5169   -299   -366    144       C  
ATOM     96  CG2 ILE A  11      25.770   1.508 -15.751  1.00 45.34           C  
ANISOU   96  CG2 ILE A  11     6491   5640   5097   -410   -438    136       C  
ATOM     97  CD1 ILE A  11      25.406  -1.516 -16.909  1.00 46.73           C  
ANISOU   97  CD1 ILE A  11     6509   5888   5359   -304   -424    176       C  
ATOM     98  N   GLY A  12      25.606   4.545 -17.868  1.00 43.27           N  
ANISOU   98  N   GLY A  12     6160   5366   4914   -378   -344     97       N  
ATOM     99  CA  GLY A  12      26.256   5.847 -17.761  1.00 44.22           C  
ANISOU   99  CA  GLY A  12     6313   5462   5025   -423   -372     94       C  
ATOM    100  C   GLY A  12      27.199   6.075 -18.929  1.00 44.34           C  
ANISOU  100  C   GLY A  12     6223   5510   5115   -409   -403    122       C  
ATOM    101  O   GLY A  12      26.770   6.134 -20.088  1.00 44.58           O  
ANISOU  101  O   GLY A  12     6185   5559   5193   -357   -350    117       O  
ATOM    102  N   ASP A  13      28.490   6.176 -18.629  1.00 42.84           N  
ANISOU  102  N   ASP A  13     6018   5322   4936   -457   -490    155       N  
ATOM    103  CA  ASP A  13      29.486   6.436 -19.664  1.00 43.22           C  
ANISOU  103  CA  ASP A  13     5967   5397   5059   -449   -517    186       C  
ATOM    104  C   ASP A  13      30.220   5.190 -20.121  1.00 40.71           C  
ANISOU  104  C   ASP A  13     5551   5117   4801   -422   -551    228       C  
ATOM    105  O   ASP A  13      31.243   5.275 -20.790  1.00 40.51           O  
ANISOU  105  O   ASP A  13     5443   5108   4840   -423   -582    262       O  
ATOM    106  CB  ASP A  13      30.469   7.512 -19.202  1.00 44.25           C  
ANISOU  106  CB  ASP A  13     6130   5503   5180   -519   -583    201       C  
ATOM    107  CG  ASP A  13      29.843   8.876 -19.181  1.00 44.08           C  
ANISOU  107  CG  ASP A  13     6183   5446   5121   -533   -534    161       C  
ATOM    108  OD1 ASP A  13      29.971   9.582 -18.157  1.00 48.16           O  
ANISOU  108  OD1 ASP A  13     6802   5921   5575   -596   -567    149       O  
ATOM    109  OD2 ASP A  13      29.196   9.226 -20.188  1.00 43.59           O  
ANISOU  109  OD2 ASP A  13     6082   5391   5088   -482   -461    141       O  
ATOM    110  N   SER A  14      29.674   4.033 -19.782  1.00 40.92           N  
ANISOU  110  N   SER A  14     5585   5152   4809   -396   -540    226       N  
ATOM    111  CA  SER A  14      30.294   2.777 -20.156  1.00 40.47           C  
ANISOU  111  CA  SER A  14     5444   5126   4807   -367   -566    264       C  
ATOM    112  C   SER A  14      29.388   1.919 -21.016  1.00 38.68           C  
ANISOU  112  C   SER A  14     5180   4919   4596   -298   -492    247       C  
ATOM    113  O   SER A  14      28.187   1.809 -20.767  1.00 40.18           O  
ANISOU  113  O   SER A  14     5426   5101   4741   -282   -442    212       O  
ATOM    114  CB  SER A  14      30.729   2.009 -18.907  1.00 41.33           C  
ANISOU  114  CB  SER A  14     5592   5225   4885   -406   -643    290       C  
ATOM    115  OG  SER A  14      32.007   2.449 -18.473  1.00 40.21           O  
ANISOU  115  OG  SER A  14     5435   5075   4767   -463   -734    331       O  
ATOM    116  N   ILE A  15      29.968   1.343 -22.058  1.00 37.98           N  
ANISOU  116  N   ILE A  15     4999   4855   4576   -260   -482    272       N  
ATOM    117  CA  ILE A  15      29.333   0.245 -22.760  1.00 35.02           C  
ANISOU  117  CA  ILE A  15     4592   4497   4216   -204   -431    266       C  
ATOM    118  C   ILE A  15      29.778  -1.024 -22.048  1.00 35.45           C  
ANISOU  118  C   ILE A  15     4638   4557   4275   -206   -479    295       C  
ATOM    119  O   ILE A  15      30.973  -1.249 -21.848  1.00 36.04           O  
ANISOU  119  O   ILE A  15     4666   4634   4395   -223   -538    338       O  
ATOM    120  CB  ILE A  15      29.724   0.203 -24.270  1.00 34.90           C  
ANISOU  120  CB  ILE A  15     4497   4499   4264   -163   -389    277       C  
ATOM    121  CG1 ILE A  15      29.148   1.407 -25.043  1.00 29.60           C  
ANISOU  121  CG1 ILE A  15     3840   3822   3586   -159   -340    248       C  
ATOM    122  CG2 ILE A  15      29.296  -1.108 -24.916  1.00 33.55           C  
ANISOU  122  CG2 ILE A  15     4299   4341   4109   -113   -350    278       C  
ATOM    123  CD1 ILE A  15      27.644   1.636 -24.882  1.00 29.46           C  
ANISOU  123  CD1 ILE A  15     3884   3794   3515   -147   -295    208       C  
ATOM    124  N   PHE A  16      28.813  -1.826 -21.614  1.00 36.40           N  
ANISOU  124  N   PHE A  16     4802   4676   4353   -190   -457    277       N  
ATOM    125  CA  PHE A  16      29.109  -3.169 -21.131  1.00 35.27           C  
ANISOU  125  CA  PHE A  16     4646   4537   4217   -181   -491    304       C  
ATOM    126  C   PHE A  16      28.744  -4.133 -22.249  1.00 35.03           C  
ANISOU  126  C   PHE A  16     4566   4523   4223   -121   -434    302       C  
ATOM    127  O   PHE A  16      27.600  -4.143 -22.719  1.00 35.82           O  
ANISOU  127  O   PHE A  16     4690   4625   4297    -97   -375    269       O  
ATOM    128  CB  PHE A  16      28.325  -3.475 -19.859  1.00 35.54           C  
ANISOU  128  CB  PHE A  16     4770   4555   4176   -208   -505    286       C  
ATOM    129  CG  PHE A  16      28.869  -2.794 -18.637  1.00 42.30           C  
ANISOU  129  CG  PHE A  16     5688   5390   4992   -273   -575    296       C  
ATOM    130  CD1 PHE A  16      29.570  -3.518 -17.681  1.00 47.95           C  
ANISOU  130  CD1 PHE A  16     6418   6099   5701   -305   -654    333       C  
ATOM    131  CD2 PHE A  16      28.691  -1.424 -18.441  1.00 43.80           C  
ANISOU  131  CD2 PHE A  16     5928   5563   5150   -307   -566    271       C  
ATOM    132  CE1 PHE A  16      30.088  -2.889 -16.542  1.00 50.33           C  
ANISOU  132  CE1 PHE A  16     6788   6377   5959   -375   -729    346       C  
ATOM    133  CE2 PHE A  16      29.200  -0.789 -17.310  1.00 47.06           C  
ANISOU  133  CE2 PHE A  16     6413   5951   5518   -375   -632    279       C  
ATOM    134  CZ  PHE A  16      29.900  -1.523 -16.358  1.00 49.33           C  
ANISOU  134  CZ  PHE A  16     6718   6231   5793   -412   -717    317       C  
ATOM    135  N   GLU A  17      29.724  -4.911 -22.696  1.00 33.69           N  
ANISOU  135  N   GLU A  17     4327   4360   4115    -99   -451    339       N  
ATOM    136  CA  GLU A  17      29.506  -5.868 -23.765  1.00 33.17           C  
ANISOU  136  CA  GLU A  17     4221   4302   4080    -46   -396    339       C  
ATOM    137  C   GLU A  17      29.917  -7.272 -23.339  1.00 33.84           C  
ANISOU  137  C   GLU A  17     4288   4384   4186    -30   -424    370       C  
ATOM    138  O   GLU A  17      31.026  -7.472 -22.842  1.00 33.68           O  
ANISOU  138  O   GLU A  17     4230   4358   4209    -45   -481    413       O  
ATOM    139  CB  GLU A  17      30.286  -5.469 -25.029  1.00 33.39           C  
ANISOU  139  CB  GLU A  17     4181   4333   4171    -24   -362    352       C  
ATOM    140  CG  GLU A  17      29.938  -6.336 -26.253  1.00 35.15           C  
ANISOU  140  CG  GLU A  17     4385   4558   4413     27   -294    344       C  
ATOM    141  CD  GLU A  17      30.958  -6.261 -27.394  1.00 37.89           C  
ANISOU  141  CD  GLU A  17     4665   4901   4829     51   -259    367       C  
ATOM    142  OE1 GLU A  17      30.750  -6.950 -28.413  1.00 36.57           O  
ANISOU  142  OE1 GLU A  17     4493   4728   4672     88   -201    361       O  
ATOM    143  OE2 GLU A  17      31.966  -5.537 -27.282  1.00 36.58           O  
ANISOU  143  OE2 GLU A  17     4456   4736   4708     30   -287    393       O  
ATOM    144  N   ARG A  18      29.022  -8.235 -23.547  1.00 31.85           N  
ANISOU  144  N   ARG A  18     4062   4132   3908     -1   -386    352       N  
ATOM    145  CA  ARG A  18      29.385  -9.643 -23.496  1.00 31.06           C  
ANISOU  145  CA  ARG A  18     3939   4027   3837     27   -394    380       C  
ATOM    146  C   ARG A  18      29.520 -10.099 -24.940  1.00 31.98           C  
ANISOU  146  C   ARG A  18     4013   4141   3997     74   -327    378       C  
ATOM    147  O   ARG A  18      28.704  -9.722 -25.778  1.00 28.93           O  
ANISOU  147  O   ARG A  18     3647   3759   3585     84   -275    345       O  
ATOM    148  CB  ARG A  18      28.320 -10.472 -22.771  1.00 31.09           C  
ANISOU  148  CB  ARG A  18     4006   4027   3780     24   -395    362       C  
ATOM    149  CG  ARG A  18      28.123 -10.104 -21.298  1.00 32.21           C  
ANISOU  149  CG  ARG A  18     4207   4164   3868    -25   -452    361       C  
ATOM    150  CD  ARG A  18      26.855 -10.756 -20.736  1.00 33.95           C  
ANISOU  150  CD  ARG A  18     4494   4380   4024    -27   -431    335       C  
ATOM    151  NE  ARG A  18      26.990 -12.206 -20.620  1.00 30.33           N  
ANISOU  151  NE  ARG A  18     4028   3917   3581     -4   -441    358       N  
ATOM    152  CZ  ARG A  18      25.979 -13.055 -20.459  1.00 28.89           C  
ANISOU  152  CZ  ARG A  18     3886   3732   3361      7   -414    341       C  
ATOM    153  NH1 ARG A  18      24.728 -12.605 -20.384  1.00 23.92           N  
ANISOU  153  NH1 ARG A  18     3303   3105   2682     -3   -373    304       N  
ATOM    154  NH2 ARG A  18      26.220 -14.363 -20.376  1.00 24.88           N  
ANISOU  154  NH2 ARG A  18     3369   3215   2869     27   -427    365       N  
ATOM    155  N   TYR A  19      30.549 -10.901 -25.229  1.00 33.20           N  
ANISOU  155  N   TYR A  19     4112   4286   4218    101   -328    417       N  
ATOM    156  CA  TYR A  19      30.860 -11.283 -26.605  1.00 31.79           C  
ANISOU  156  CA  TYR A  19     3897   4097   4083    144   -257    418       C  
ATOM    157  C   TYR A  19      31.618 -12.607 -26.680  1.00 32.71           C  
ANISOU  157  C   TYR A  19     3976   4194   4257    181   -249    455       C  
ATOM    158  O   TYR A  19      32.166 -13.092 -25.686  1.00 30.51           O  
ANISOU  158  O   TYR A  19     3678   3911   4004    172   -309    490       O  
ATOM    159  CB  TYR A  19      31.656 -10.166 -27.302  1.00 32.52           C  
ANISOU  159  CB  TYR A  19     3941   4193   4221    139   -240    426       C  
ATOM    160  CG  TYR A  19      33.083 -10.003 -26.805  1.00 35.00           C  
ANISOU  160  CG  TYR A  19     4183   4502   4614    129   -288    479       C  
ATOM    161  CD1 TYR A  19      33.360  -9.337 -25.610  1.00 36.56           C  
ANISOU  161  CD1 TYR A  19     4384   4707   4799     80   -372    495       C  
ATOM    162  CD2 TYR A  19      34.158 -10.528 -27.530  1.00 34.66           C  
ANISOU  162  CD2 TYR A  19     4069   4442   4659    166   -249    517       C  
ATOM    163  CE1 TYR A  19      34.683  -9.190 -25.152  1.00 37.41           C  
ANISOU  163  CE1 TYR A  19     4422   4809   4984     65   -429    551       C  
ATOM    164  CE2 TYR A  19      35.476 -10.380 -27.090  1.00 34.94           C  
ANISOU  164  CE2 TYR A  19     4024   4470   4780    157   -295    574       C  
ATOM    165  CZ  TYR A  19      35.733  -9.713 -25.904  1.00 36.46           C  
ANISOU  165  CZ  TYR A  19     4218   4674   4962    104   -391    593       C  
ATOM    166  OH  TYR A  19      37.037  -9.587 -25.468  1.00 33.58           O  
ANISOU  166  OH  TYR A  19     3772   4302   4687     89   -448    656       O  
ATOM    167  N   ILE A  20      31.622 -13.188 -27.872  1.00 33.52           N  
ANISOU  167  N   ILE A  20     4075   4282   4381    221   -174    447       N  
ATOM    168  CA  ILE A  20      32.415 -14.363 -28.165  1.00 36.38           C  
ANISOU  168  CA  ILE A  20     4399   4617   4807    263   -145    481       C  
ATOM    169  C   ILE A  20      33.679 -13.917 -28.913  1.00 39.18           C  
ANISOU  169  C   ILE A  20     4678   4959   5251    282   -107    513       C  
ATOM    170  O   ILE A  20      33.588 -13.330 -29.992  1.00 37.38           O  
ANISOU  170  O   ILE A  20     4459   4729   5016    288    -45    490       O  
ATOM    171  CB  ILE A  20      31.598 -15.392 -29.003  1.00 36.66           C  
ANISOU  171  CB  ILE A  20     4492   4633   4804    294    -79    452       C  
ATOM    172  CG1 ILE A  20      30.413 -15.947 -28.192  1.00 34.72           C  
ANISOU  172  CG1 ILE A  20     4311   4399   4484    275   -118    429       C  
ATOM    173  CG2 ILE A  20      32.495 -16.511 -29.529  1.00 37.77           C  
ANISOU  173  CG2 ILE A  20     4598   4738   5017    343    -27    484       C  
ATOM    174  CD1 ILE A  20      30.797 -16.723 -26.924  1.00 32.38           C  
ANISOU  174  CD1 ILE A  20     4000   4097   4206    272   -182    464       C  
ATOM    175  N   ASP A  21      34.849 -14.192 -28.330  1.00 40.44           N  
ANISOU  175  N   ASP A  21     4763   5107   5495    290   -145    569       N  
ATOM    176  CA  ASP A  21      36.122 -13.801 -28.935  1.00 42.10           C  
ANISOU  176  CA  ASP A  21     4887   5303   5805    308   -110    608       C  
ATOM    177  C   ASP A  21      36.541 -14.715 -30.097  1.00 44.48           C  
ANISOU  177  C   ASP A  21     5174   5567   6160    366     -3    615       C  
ATOM    178  O   ASP A  21      35.876 -15.715 -30.390  1.00 43.58           O  
ANISOU  178  O   ASP A  21     5119   5436   6004    392     36    591       O  
ATOM    179  CB  ASP A  21      37.232 -13.699 -27.873  1.00 42.29           C  
ANISOU  179  CB  ASP A  21     4830   5328   5911    289   -198    674       C  
ATOM    180  CG  ASP A  21      37.564 -15.034 -27.213  1.00 41.97           C  
ANISOU  180  CG  ASP A  21     4768   5265   5914    315   -228    715       C  
ATOM    181  OD1 ASP A  21      37.232 -16.114 -27.761  1.00 43.81           O  
ANISOU  181  OD1 ASP A  21     5031   5474   6141    360   -161    701       O  
ATOM    182  OD2 ASP A  21      38.169 -14.999 -26.122  1.00 41.11           O  
ANISOU  182  OD2 ASP A  21     4617   5159   5845    288   -324    764       O  
ATOM    183  N   SER A  22      37.653 -14.368 -30.742  1.00 47.65           N  
ANISOU  183  N   SER A  22     5500   5951   6655    386     47    649       N  
ATOM    184  CA  SER A  22      38.173 -15.120 -31.890  1.00 50.68           C  
ANISOU  184  CA  SER A  22     5870   6291   7095    442    164    658       C  
ATOM    185  C   SER A  22      38.420 -16.600 -31.593  1.00 51.80           C  
ANISOU  185  C   SER A  22     6002   6398   7282    486    177    687       C  
ATOM    186  O   SER A  22      38.491 -17.414 -32.516  1.00 50.17           O  
ANISOU  186  O   SER A  22     5822   6151   7090    532    279    678       O  
ATOM    187  CB  SER A  22      39.456 -14.472 -32.413  1.00 52.51           C  
ANISOU  187  CB  SER A  22     6005   6508   7436    453    208    702       C  
ATOM    188  OG  SER A  22      40.438 -14.393 -31.393  1.00 57.81           O  
ANISOU  188  OG  SER A  22     6575   7185   8204    443    124    769       O  
ATOM    189  N   ASN A  23      38.533 -16.937 -30.308  1.00 52.88           N  
ANISOU  189  N   ASN A  23     6109   6548   7435    470     75    721       N  
ATOM    190  CA  ASN A  23      38.768 -18.316 -29.866  1.00 55.39           C  
ANISOU  190  CA  ASN A  23     6415   6835   7797    508     71    754       C  
ATOM    191  C   ASN A  23      37.482 -19.082 -29.558  1.00 55.02           C  
ANISOU  191  C   ASN A  23     6473   6793   7638    500     53    707       C  
ATOM    192  O   ASN A  23      37.517 -20.281 -29.245  1.00 55.39           O  
ANISOU  192  O   ASN A  23     6527   6812   7705    530     54    726       O  
ATOM    193  CB  ASN A  23      39.705 -18.332 -28.650  1.00 57.54           C  
ANISOU  193  CB  ASN A  23     6594   7111   8159    493    -35    828       C  
ATOM    194  CG  ASN A  23      41.059 -17.699 -28.949  1.00 58.52           C  
ANISOU  194  CG  ASN A  23     6599   7224   8413    503    -18    886       C  
ATOM    195  OD1 ASN A  23      41.746 -18.108 -29.878  1.00 58.20           O  
ANISOU  195  OD1 ASN A  23     6513   7143   8458    556     88    907       O  
ATOM    196  ND2 ASN A  23      41.438 -16.690 -28.163  1.00 58.85           N  
ANISOU  196  ND2 ASN A  23     6594   7296   8469    449   -120    914       N  
ATOM    197  N   GLY A  24      36.351 -18.387 -29.654  1.00 52.65           N  
ANISOU  197  N   GLY A  24     6252   6527   7226    460     38    648       N  
ATOM    198  CA  GLY A  24      35.051 -18.997 -29.397  1.00 50.80           C  
ANISOU  198  CA  GLY A  24     6113   6300   6887    448     22    603       C  
ATOM    199  C   GLY A  24      34.714 -19.060 -27.920  1.00 48.98           C  
ANISOU  199  C   GLY A  24     5890   6096   6624    411    -90    617       C  
ATOM    200  O   GLY A  24      33.980 -19.938 -27.477  1.00 49.36           O  
ANISOU  200  O   GLY A  24     5994   6138   6621    411   -107    603       O  
ATOM    201  N   ARG A  25      35.242 -18.113 -27.158  1.00 48.35           N  
ANISOU  201  N   ARG A  25     5761   6040   6570    375   -165    643       N  
ATOM    202  CA  ARG A  25      35.002 -18.075 -25.725  1.00 47.27           C  
ANISOU  202  CA  ARG A  25     5641   5922   6397    332   -273    658       C  
ATOM    203  C   ARG A  25      34.210 -16.845 -25.311  1.00 44.27           C  
ANISOU  203  C   ARG A  25     5311   5580   5932    277   -314    617       C  
ATOM    204  O   ARG A  25      34.360 -15.770 -25.891  1.00 43.31           O  
ANISOU  204  O   ARG A  25     5171   5471   5815    265   -290    602       O  
ATOM    205  CB  ARG A  25      36.332 -18.129 -24.977  1.00 49.80           C  
ANISOU  205  CB  ARG A  25     5871   6231   6819    329   -343    733       C  
ATOM    206  CG  ARG A  25      37.032 -19.477 -25.094  1.00 48.28           C  
ANISOU  206  CG  ARG A  25     5632   5997   6714    384   -317    781       C  
ATOM    207  CD  ARG A  25      38.511 -19.270 -25.176  1.00 49.91           C  
ANISOU  207  CD  ARG A  25     5721   6186   7058    401   -327    852       C  
ATOM    208  NE  ARG A  25      39.263 -20.396 -24.641  1.00 47.71           N  
ANISOU  208  NE  ARG A  25     5387   5873   6868    432   -360    919       N  
ATOM    209  CZ  ARG A  25      40.577 -20.392 -24.466  1.00 45.31           C  
ANISOU  209  CZ  ARG A  25     4970   5549   6699    446   -390    998       C  
ATOM    210  NH1 ARG A  25      41.282 -19.315 -24.794  1.00 42.84           N  
ANISOU  210  NH1 ARG A  25     4588   5248   6443    429   -389   1017       N  
ATOM    211  NH2 ARG A  25      41.184 -21.461 -23.958  1.00 41.98           N  
ANISOU  211  NH2 ARG A  25     4500   5093   6359    476   -423   1061       N  
ATOM    212  N   GLU A  26      33.360 -17.011 -24.308  1.00 42.98           N  
ANISOU  212  N   GLU A  26     5212   5428   5689    244   -370    599       N  
ATOM    213  CA  GLU A  26      32.602 -15.888 -23.787  1.00 42.47           C  
ANISOU  213  CA  GLU A  26     5198   5391   5546    193   -405    563       C  
ATOM    214  C   GLU A  26      33.490 -14.956 -22.961  1.00 43.37           C  
ANISOU  214  C   GLU A  26     5273   5514   5691    150   -487    600       C  
ATOM    215  O   GLU A  26      34.194 -15.391 -22.046  1.00 43.56           O  
ANISOU  215  O   GLU A  26     5273   5527   5751    135   -561    649       O  
ATOM    216  CB  GLU A  26      31.385 -16.352 -22.978  1.00 40.82           C  
ANISOU  216  CB  GLU A  26     5075   5189   5245    171   -427    533       C  
ATOM    217  CG  GLU A  26      30.486 -15.189 -22.566  1.00 40.70           C  
ANISOU  217  CG  GLU A  26     5116   5196   5152    125   -440    490       C  
ATOM    218  CD  GLU A  26      29.203 -15.605 -21.877  1.00 40.39           C  
ANISOU  218  CD  GLU A  26     5158   5160   5028    107   -443    459       C  
ATOM    219  OE1 GLU A  26      28.693 -16.717 -22.144  1.00 41.82           O  
ANISOU  219  OE1 GLU A  26     5359   5331   5199    134   -412    453       O  
ATOM    220  OE2 GLU A  26      28.693 -14.796 -21.074  1.00 40.51           O  
ANISOU  220  OE2 GLU A  26     5221   5186   4987     64   -472    440       O  
ATOM    221  N   ARG A  27      33.460 -13.673 -23.312  1.00 42.40           N  
ANISOU  221  N   ARG A  27     5147   5407   5556    126   -476    577       N  
ATOM    222  CA  ARG A  27      34.164 -12.650 -22.558  1.00 44.77           C  
ANISOU  222  CA  ARG A  27     5426   5714   5871     76   -553    604       C  
ATOM    223  C   ARG A  27      33.221 -11.489 -22.271  1.00 44.30           C  
ANISOU  223  C   ARG A  27     5440   5672   5721     34   -556    553       C  
ATOM    224  O   ARG A  27      32.139 -11.397 -22.854  1.00 44.47           O  
ANISOU  224  O   ARG A  27     5507   5701   5689     49   -491    502       O  
ATOM    225  CB  ARG A  27      35.382 -12.141 -23.333  1.00 47.12           C  
ANISOU  225  CB  ARG A  27     5628   6007   6269     91   -536    641       C  
ATOM    226  CG  ARG A  27      36.281 -13.207 -23.933  1.00 54.60           C  
ANISOU  226  CG  ARG A  27     6495   6931   7319    147   -499    688       C  
ATOM    227  CD  ARG A  27      37.306 -13.732 -22.934  1.00 62.98           C  
ANISOU  227  CD  ARG A  27     7501   7978   8451    133   -592    761       C  
ATOM    228  NE  ARG A  27      38.603 -13.904 -23.581  1.00 70.16           N  
ANISOU  228  NE  ARG A  27     8297   8868   9494    169   -565    819       N  
ATOM    229  CZ  ARG A  27      39.483 -12.920 -23.767  1.00 72.99           C  
ANISOU  229  CZ  ARG A  27     8587   9231   9917    146   -584    850       C  
ATOM    230  NH1 ARG A  27      39.217 -11.688 -23.342  1.00 70.03           N  
ANISOU  230  NH1 ARG A  27     8252   8877   9480     87   -635    826       N  
ATOM    231  NH2 ARG A  27      40.635 -13.172 -24.375  1.00 75.84           N  
ANISOU  231  NH2 ARG A  27     8840   9570  10407    184   -549    906       N  
ATOM    232  N   THR A  28      33.646 -10.608 -21.374  1.00 44.31           N  
ANISOU  232  N   THR A  28     5452   5675   5710    -22   -632    569       N  
ATOM    233  CA  THR A  28      32.902  -9.405 -21.030  1.00 44.78           C  
ANISOU  233  CA  THR A  28     5580   5743   5692    -64   -635    525       C  
ATOM    234  C   THR A  28      33.907  -8.270 -20.943  1.00 44.76           C  
ANISOU  234  C   THR A  28     5537   5740   5731   -103   -683    552       C  
ATOM    235  O   THR A  28      35.054  -8.480 -20.549  1.00 45.61           O  
ANISOU  235  O   THR A  28     5586   5839   5904   -118   -751    611       O  
ATOM    236  CB  THR A  28      32.170  -9.555 -19.666  1.00 46.78           C  
ANISOU  236  CB  THR A  28     5929   5989   5855   -108   -685    510       C  
ATOM    237  OG1 THR A  28      31.437 -10.789 -19.637  1.00 49.92           O  
ANISOU  237  OG1 THR A  28     6353   6385   6229    -75   -653    499       O  
ATOM    238  CG2 THR A  28      31.207  -8.383 -19.404  1.00 43.21           C  
ANISOU  238  CG2 THR A  28     5556   5539   5321   -142   -662    457       C  
ATOM    239  N   ARG A  29      33.479  -7.070 -21.314  1.00 43.18           N  
ANISOU  239  N   ARG A  29     5364   5547   5496   -120   -651    514       N  
ATOM    240  CA  ARG A  29      34.338  -5.895 -21.229  1.00 43.23           C  
ANISOU  240  CA  ARG A  29     5341   5551   5533   -162   -695    535       C  
ATOM    241  C   ARG A  29      33.539  -4.620 -21.011  1.00 44.51           C  
ANISOU  241  C   ARG A  29     5582   5713   5617   -198   -681    485       C  
ATOM    242  O   ARG A  29      32.376  -4.512 -21.423  1.00 44.10           O  
ANISOU  242  O   ARG A  29     5576   5665   5513   -174   -612    434       O  
ATOM    243  CB  ARG A  29      35.210  -5.762 -22.480  1.00 43.48           C  
ANISOU  243  CB  ARG A  29     5271   5587   5661   -125   -649    560       C  
ATOM    244  CG  ARG A  29      34.441  -5.560 -23.788  1.00 40.32           C  
ANISOU  244  CG  ARG A  29     4877   5197   5247    -80   -543    512       C  
ATOM    245  CD  ARG A  29      35.396  -5.589 -24.951  1.00 40.97           C  
ANISOU  245  CD  ARG A  29     4866   5277   5423    -45   -496    541       C  
ATOM    246  NE  ARG A  29      34.724  -5.834 -26.216  1.00 37.29           N  
ANISOU  246  NE  ARG A  29     4410   4814   4946      4   -397    504       N  
ATOM    247  CZ  ARG A  29      35.318  -6.357 -27.283  1.00 40.34           C  
ANISOU  247  CZ  ARG A  29     4737   5192   5399     48   -333    523       C  
ATOM    248  NH1 ARG A  29      36.597  -6.708 -27.231  1.00 44.03           N  
ANISOU  248  NH1 ARG A  29     5119   5648   5962     56   -353    581       N  
ATOM    249  NH2 ARG A  29      34.628  -6.553 -28.397  1.00 36.26           N  
ANISOU  249  NH2 ARG A  29     4248   4673   4856     83   -250    487       N  
ATOM    250  N   GLU A  30      34.176  -3.663 -20.353  1.00 46.12           N  
ANISOU  250  N   GLU A  30     5799   5907   5816   -257   -750    503       N  
ATOM    251  CA  GLU A  30      33.606  -2.347 -20.147  1.00 48.38           C  
ANISOU  251  CA  GLU A  30     6158   6186   6039   -295   -739    461       C  
ATOM    252  C   GLU A  30      34.404  -1.394 -21.020  1.00 48.83           C  
ANISOU  252  C   GLU A  30     6146   6247   6159   -298   -729    476       C  
ATOM    253  O   GLU A  30      35.628  -1.333 -20.912  1.00 50.36           O  
ANISOU  253  O   GLU A  30     6274   6439   6421   -322   -791    530       O  
ATOM    254  CB  GLU A  30      33.720  -1.963 -18.677  1.00 50.42           C  
ANISOU  254  CB  GLU A  30     6503   6423   6233   -369   -827    469       C  
ATOM    255  CG  GLU A  30      33.012  -0.678 -18.285  1.00 53.64           C  
ANISOU  255  CG  GLU A  30     7007   6813   6561   -409   -809    420       C  
ATOM    256  CD  GLU A  30      33.201  -0.317 -16.812  1.00 57.02           C  
ANISOU  256  CD  GLU A  30     7535   7211   6918   -489   -896    429       C  
ATOM    257  OE1 GLU A  30      33.512  -1.217 -15.994  1.00 56.74           O  
ANISOU  257  OE1 GLU A  30     7516   7171   6873   -508   -961    462       O  
ATOM    258  OE2 GLU A  30      33.031   0.875 -16.474  1.00 58.28           O  
ANISOU  258  OE2 GLU A  30     7766   7350   7028   -534   -898    403       O  
ATOM    259  N   VAL A  31      33.717  -0.676 -21.904  1.00 47.79           N  
ANISOU  259  N   VAL A  31     6026   6121   6011   -274   -652    432       N  
ATOM    260  CA  VAL A  31      34.384   0.251 -22.816  1.00 46.67           C  
ANISOU  260  CA  VAL A  31     5827   5983   5924   -276   -632    442       C  
ATOM    261  C   VAL A  31      33.891   1.674 -22.586  1.00 44.56           C  
ANISOU  261  C   VAL A  31     5630   5702   5599   -316   -629    405       C  
ATOM    262  O   VAL A  31      32.689   1.928 -22.606  1.00 42.40           O  
ANISOU  262  O   VAL A  31     5423   5424   5262   -302   -577    356       O  
ATOM    263  CB  VAL A  31      34.182  -0.156 -24.297  1.00 46.97           C  
ANISOU  263  CB  VAL A  31     5806   6035   6006   -209   -540    432       C  
ATOM    264  CG1 VAL A  31      34.888   0.821 -25.231  1.00 51.57           C  
ANISOU  264  CG1 VAL A  31     6334   6618   6642   -214   -516    443       C  
ATOM    265  CG2 VAL A  31      34.695  -1.573 -24.547  1.00 49.20           C  
ANISOU  265  CG2 VAL A  31     6023   6323   6347   -167   -534    468       C  
ATOM    266  N   GLU A  32      34.827   2.593 -22.351  1.00 45.75           N  
ANISOU  266  N   GLU A  32     5765   5843   5775   -367   -685    432       N  
ATOM    267  CA  GLU A  32      34.500   4.017 -22.240  1.00 49.14           C  
ANISOU  267  CA  GLU A  32     6258   6256   6159   -405   -679    400       C  
ATOM    268  C   GLU A  32      34.385   4.587 -23.657  1.00 48.22           C  
ANISOU  268  C   GLU A  32     6092   6149   6080   -366   -601    384       C  
ATOM    269  O   GLU A  32      35.275   5.290 -24.148  1.00 48.85           O  
ANISOU  269  O   GLU A  32     6119   6228   6213   -385   -614    410       O  
ATOM    270  CB  GLU A  32      35.539   4.768 -21.399  1.00 50.70           C  
ANISOU  270  CB  GLU A  32     6467   6434   6363   -483   -777    435       C  
ATOM    271  CG  GLU A  32      35.474   4.462 -19.896  1.00 56.86           C  
ANISOU  271  CG  GLU A  32     7332   7194   7077   -537   -857    442       C  
ATOM    272  CD  GLU A  32      36.800   4.714 -19.169  1.00 61.80           C  
ANISOU  272  CD  GLU A  32     7936   7807   7738   -610   -976    503       C  
ATOM    273  OE1 GLU A  32      37.388   5.807 -19.332  1.00 61.40           O  
ANISOU  273  OE1 GLU A  32     7877   7745   7706   -653  -1002    513       O  
ATOM    274  OE2 GLU A  32      37.253   3.815 -18.424  1.00 63.53           O  
ANISOU  274  OE2 GLU A  32     8145   8026   7967   -628  -1048    543       O  
ATOM    275  N   TYR A  33      33.270   4.251 -24.300  1.00 46.45           N  
ANISOU  275  N   TYR A  33     5886   5933   5830   -313   -523    345       N  
ATOM    276  CA  TYR A  33      33.043   4.519 -25.712  1.00 44.35           C  
ANISOU  276  CA  TYR A  33     5579   5677   5595   -270   -448    333       C  
ATOM    277  C   TYR A  33      32.872   6.011 -25.961  1.00 45.16           C  
ANISOU  277  C   TYR A  33     5716   5764   5679   -298   -435    311       C  
ATOM    278  O   TYR A  33      32.086   6.672 -25.283  1.00 45.25           O  
ANISOU  278  O   TYR A  33     5808   5756   5628   -320   -436    278       O  
ATOM    279  CB  TYR A  33      31.806   3.748 -26.172  1.00 41.18           C  
ANISOU  279  CB  TYR A  33     5201   5283   5161   -218   -384    300       C  
ATOM    280  CG  TYR A  33      31.422   3.916 -27.623  1.00 38.26           C  
ANISOU  280  CG  TYR A  33     4805   4921   4812   -177   -312    287       C  
ATOM    281  CD1 TYR A  33      32.318   3.616 -28.648  1.00 37.86           C  
ANISOU  281  CD1 TYR A  33     4681   4878   4824   -156   -288    316       C  
ATOM    282  CD2 TYR A  33      30.140   4.338 -27.974  1.00 35.80           C  
ANISOU  282  CD2 TYR A  33     4543   4602   4457   -160   -266    249       C  
ATOM    283  CE1 TYR A  33      31.951   3.751 -29.988  1.00 34.96           C  
ANISOU  283  CE1 TYR A  33     4305   4512   4464   -124   -222    303       C  
ATOM    284  CE2 TYR A  33      29.768   4.473 -29.312  1.00 34.89           C  
ANISOU  284  CE2 TYR A  33     4410   4490   4356   -128   -210    241       C  
ATOM    285  CZ  TYR A  33      30.674   4.180 -30.306  1.00 33.71           C  
ANISOU  285  CZ  TYR A  33     4201   4349   4257   -113   -190    267       C  
ATOM    286  OH  TYR A  33      30.302   4.325 -31.618  1.00 34.18           O  
ANISOU  286  OH  TYR A  33     4258   4408   4322    -88   -136    258       O  
ATOM    287  N   LYS A  34      33.640   6.530 -26.919  1.00 45.11           N  
ANISOU  287  N   LYS A  34     5650   5762   5728   -296   -418    331       N  
ATOM    288  CA  LYS A  34      33.546   7.929 -27.334  1.00 44.53           C  
ANISOU  288  CA  LYS A  34     5601   5674   5645   -318   -400    314       C  
ATOM    289  C   LYS A  34      32.646   7.979 -28.567  1.00 41.44           C  
ANISOU  289  C   LYS A  34     5211   5287   5247   -268   -319    287       C  
ATOM    290  O   LYS A  34      33.065   7.624 -29.671  1.00 41.79           O  
ANISOU  290  O   LYS A  34     5197   5343   5337   -239   -281    304       O  
ATOM    291  CB  LYS A  34      34.931   8.511 -27.655  1.00 45.62           C  
ANISOU  291  CB  LYS A  34     5674   5811   5849   -352   -431    356       C  
ATOM    292  CG  LYS A  34      36.081   7.955 -26.818  1.00 49.41           C  
ANISOU  292  CG  LYS A  34     6106   6294   6371   -386   -510    405       C  
ATOM    293  CD  LYS A  34      36.465   8.851 -25.656  1.00 53.41           C  
ANISOU  293  CD  LYS A  34     6666   6779   6847   -461   -594    412       C  
ATOM    294  CE  LYS A  34      37.456   9.925 -26.102  1.00 60.33           C  
ANISOU  294  CE  LYS A  34     7499   7647   7775   -501   -613    440       C  
ATOM    295  NZ  LYS A  34      38.547  10.145 -25.101  1.00 60.38           N  
ANISOU  295  NZ  LYS A  34     7492   7642   7806   -573   -719    488       N  
ATOM    296  N   PRO A  35      31.395   8.405 -28.386  1.00 40.01           N  
ANISOU  296  N   PRO A  35     5099   5093   5011   -259   -293    248       N  
ATOM    297  CA  PRO A  35      30.486   8.374 -29.513  1.00 37.84           C  
ANISOU  297  CA  PRO A  35     4824   4821   4733   -215   -228    229       C  
ATOM    298  C   PRO A  35      30.674   9.596 -30.412  1.00 37.75           C  
ANISOU  298  C   PRO A  35     4808   4798   4738   -225   -205    228       C  
ATOM    299  O   PRO A  35      31.243  10.618 -29.985  1.00 33.34           O  
ANISOU  299  O   PRO A  35     4262   4223   4181   -268   -235    232       O  
ATOM    300  CB  PRO A  35      29.119   8.412 -28.841  1.00 37.76           C  
ANISOU  300  CB  PRO A  35     4881   4797   4669   -206   -214    195       C  
ATOM    301  CG  PRO A  35      29.344   9.171 -27.583  1.00 38.30           C  
ANISOU  301  CG  PRO A  35     5003   4843   4706   -254   -256    187       C  
ATOM    302  CD  PRO A  35      30.788   9.037 -27.202  1.00 39.53           C  
ANISOU  302  CD  PRO A  35     5119   5007   4893   -292   -316    222       C  
ATOM    303  N   SER A  36      30.216   9.483 -31.654  1.00 37.08           N  
ANISOU  303  N   SER A  36     4710   4718   4662   -191   -155    225       N  
ATOM    304  CA  SER A  36      30.184  10.642 -32.532  1.00 39.00           C  
ANISOU  304  CA  SER A  36     4959   4946   4912   -199   -130    222       C  
ATOM    305  C   SER A  36      28.768  11.018 -32.912  1.00 39.37           C  
ANISOU  305  C   SER A  36     5052   4979   4929   -175    -99    197       C  
ATOM    306  O   SER A  36      27.892  10.153 -33.065  1.00 38.50           O  
ANISOU  306  O   SER A  36     4947   4876   4804   -143    -81    189       O  
ATOM    307  CB  SER A  36      31.026  10.424 -33.786  1.00 38.33           C  
ANISOU  307  CB  SER A  36     4823   4872   4869   -188   -100    246       C  
ATOM    308  OG  SER A  36      32.408  10.465 -33.482  1.00 40.47           O  
ANISOU  308  OG  SER A  36     5045   5148   5184   -216   -127    276       O  
ATOM    309  N   LEU A  37      28.554  12.326 -33.030  1.00 38.94           N  
ANISOU  309  N   LEU A  37     5026   4901   4869   -193    -94    188       N  
ATOM    310  CA  LEU A  37      27.352  12.873 -33.637  1.00 37.83           C  
ANISOU  310  CA  LEU A  37     4916   4742   4717   -171    -64    175       C  
ATOM    311  C   LEU A  37      27.748  13.920 -34.678  1.00 38.55           C  
ANISOU  311  C   LEU A  37     5003   4820   4826   -184    -50    186       C  
ATOM    312  O   LEU A  37      28.930  14.241 -34.822  1.00 39.51           O  
ANISOU  312  O   LEU A  37     5098   4945   4967   -211    -61    201       O  
ATOM    313  CB  LEU A  37      26.418  13.445 -32.577  1.00 35.89           C  
ANISOU  313  CB  LEU A  37     4721   4469   4446   -174    -65    151       C  
ATOM    314  CG  LEU A  37      25.765  12.413 -31.668  1.00 38.67           C  
ANISOU  314  CG  LEU A  37     5085   4830   4777   -158    -67    140       C  
ATOM    315  CD1 LEU A  37      24.970  13.114 -30.589  1.00 37.64           C  
ANISOU  315  CD1 LEU A  37     5013   4666   4622   -165    -57    116       C  
ATOM    316  CD2 LEU A  37      24.899  11.418 -32.450  1.00 39.72           C  
ANISOU  316  CD2 LEU A  37     5197   4980   4916   -118    -45    145       C  
ATOM    317  N   PHE A  38      26.776  14.428 -35.426  1.00 37.59           N  
ANISOU  317  N   PHE A  38     4902   4680   4699   -166    -28    182       N  
ATOM    318  CA  PHE A  38      27.095  15.273 -36.567  1.00 37.54           C  
ANISOU  318  CA  PHE A  38     4895   4662   4706   -176    -14    196       C  
ATOM    319  C   PHE A  38      26.253  16.531 -36.636  1.00 38.18           C  
ANISOU  319  C   PHE A  38     5014   4707   4786   -177     -8    189       C  
ATOM    320  O   PHE A  38      25.093  16.538 -36.227  1.00 38.55           O  
ANISOU  320  O   PHE A  38     5081   4739   4827   -155     -2    178       O  
ATOM    321  CB  PHE A  38      26.958  14.483 -37.863  1.00 35.33           C  
ANISOU  321  CB  PHE A  38     4602   4396   4427   -155      7    211       C  
ATOM    322  CG  PHE A  38      27.829  13.258 -37.920  1.00 36.19           C  
ANISOU  322  CG  PHE A  38     4675   4534   4544   -150     13    220       C  
ATOM    323  CD1 PHE A  38      27.443  12.082 -37.285  1.00 36.00           C  
ANISOU  323  CD1 PHE A  38     4643   4526   4509   -130      5    213       C  
ATOM    324  CD2 PHE A  38      29.026  13.276 -38.622  1.00 33.80           C  
ANISOU  324  CD2 PHE A  38     4345   4236   4262   -164     31    238       C  
ATOM    325  CE1 PHE A  38      28.238  10.948 -37.339  1.00 36.27           C  
ANISOU  325  CE1 PHE A  38     4644   4582   4554   -122     12    223       C  
ATOM    326  CE2 PHE A  38      29.827  12.145 -38.685  1.00 37.85           C  
ANISOU  326  CE2 PHE A  38     4821   4770   4791   -155     44    250       C  
ATOM    327  CZ  PHE A  38      29.433  10.976 -38.035  1.00 37.65           C  
ANISOU  327  CZ  PHE A  38     4789   4760   4756   -133     33    242       C  
ATOM    328  N   ALA A  39      26.864  17.594 -37.147  1.00 38.23           N  
ANISOU  328  N   ALA A  39     5026   4697   4802   -202     -6    197       N  
ATOM    329  CA  ALA A  39      26.162  18.833 -37.425  1.00 39.41           C  
ANISOU  329  CA  ALA A  39     5209   4809   4955   -202      2    195       C  
ATOM    330  C   ALA A  39      26.430  19.237 -38.869  1.00 39.91           C  
ANISOU  330  C   ALA A  39     5270   4869   5027   -208     13    217       C  
ATOM    331  O   ALA A  39      27.507  18.967 -39.398  1.00 39.29           O  
ANISOU  331  O   ALA A  39     5168   4809   4953   -225     18    229       O  
ATOM    332  CB  ALA A  39      26.627  19.924 -36.469  1.00 38.86           C  
ANISOU  332  CB  ALA A  39     5168   4713   4884   -234     -9    181       C  
ATOM    333  N   HIS A  40      25.453  19.875 -39.507  1.00 42.00           N  
ANISOU  333  N   HIS A  40     5558   5106   5296   -194     18    225       N  
ATOM    334  CA  HIS A  40      25.670  20.469 -40.823  1.00 44.75           C  
ANISOU  334  CA  HIS A  40     5917   5440   5645   -206     25    247       C  
ATOM    335  C   HIS A  40      26.798  21.491 -40.764  1.00 45.83           C  
ANISOU  335  C   HIS A  40     6059   5566   5790   -244     27    247       C  
ATOM    336  O   HIS A  40      26.948  22.197 -39.768  1.00 46.97           O  
ANISOU  336  O   HIS A  40     6214   5693   5938   -258     18    232       O  
ATOM    337  CB  HIS A  40      24.392  21.135 -41.341  1.00 44.68           C  
ANISOU  337  CB  HIS A  40     5933   5397   5646   -187     20    260       C  
ATOM    338  CG  HIS A  40      23.343  20.163 -41.778  1.00 45.78           C  
ANISOU  338  CG  HIS A  40     6066   5546   5782   -159     12    271       C  
ATOM    339  ND1 HIS A  40      22.056  20.185 -41.286  1.00 47.68           N  
ANISOU  339  ND1 HIS A  40     6305   5768   6043   -130      6    272       N  
ATOM    340  CD2 HIS A  40      23.394  19.129 -42.652  1.00 44.94           C  
ANISOU  340  CD2 HIS A  40     5957   5463   5656   -157      9    284       C  
ATOM    341  CE1 HIS A  40      21.358  19.211 -41.842  1.00 48.39           C  
ANISOU  341  CE1 HIS A  40     6386   5872   6128   -115     -7    288       C  
ATOM    342  NE2 HIS A  40      22.146  18.558 -42.677  1.00 46.91           N  
ANISOU  342  NE2 HIS A  40     6203   5708   5912   -132     -7    294       N  
ATOM    343  N   CYS A  41      27.598  21.543 -41.823  1.00 48.57           N  
ANISOU  343  N   CYS A  41     6400   5920   6136   -262     40    266       N  
ATOM    344  CA  CYS A  41      28.652  22.550 -41.955  1.00 53.59           C  
ANISOU  344  CA  CYS A  41     7036   6542   6783   -301     44    272       C  
ATOM    345  C   CYS A  41      28.552  23.256 -43.318  1.00 56.67           C  
ANISOU  345  C   CYS A  41     7455   6909   7168   -311     59    294       C  
ATOM    346  O   CYS A  41      27.802  22.803 -44.186  1.00 55.34           O  
ANISOU  346  O   CYS A  41     7304   6739   6984   -291     62    305       O  
ATOM    347  CB  CYS A  41      30.033  21.916 -41.743  1.00 53.65           C  
ANISOU  347  CB  CYS A  41     6999   6581   6806   -321     52    278       C  
ATOM    348  SG  CYS A  41      30.467  20.605 -42.911  1.00 53.33           S  
ANISOU  348  SG  CYS A  41     6935   6568   6761   -305     90    295       S  
ATOM    349  N   PRO A  42      29.282  24.382 -43.503  1.00 62.16           N  
ANISOU  349  N   PRO A  42     8161   7583   7874   -345     62    301       N  
ATOM    350  CA  PRO A  42      29.273  25.063 -44.807  1.00 64.50           C  
ANISOU  350  CA  PRO A  42     8489   7856   8163   -359     77    323       C  
ATOM    351  C   PRO A  42      29.817  24.187 -45.933  1.00 67.50           C  
ANISOU  351  C   PRO A  42     8863   8255   8527   -362    110    340       C  
ATOM    352  O   PRO A  42      30.720  23.369 -45.709  1.00 67.04           O  
ANISOU  352  O   PRO A  42     8765   8227   8481   -365    130    338       O  
ATOM    353  CB  PRO A  42      30.201  26.265 -44.592  1.00 64.73           C  
ANISOU  353  CB  PRO A  42     8521   7865   8209   -400     77    327       C  
ATOM    354  CG  PRO A  42      30.207  26.494 -43.128  1.00 65.22           C  
ANISOU  354  CG  PRO A  42     8573   7926   8282   -404     52    304       C  
ATOM    355  CD  PRO A  42      30.063  25.136 -42.500  1.00 63.64           C  
ANISOU  355  CD  PRO A  42     8339   7762   8078   -377     48    291       C  
ATOM    356  N   GLU A  43      29.260  24.369 -47.130  1.00 71.31           N  
ANISOU  356  N   GLU A  43     9391   8718   8986   -361    115    358       N  
ATOM    357  CA  GLU A  43      29.686  23.656 -48.340  1.00 75.61           C  
ANISOU  357  CA  GLU A  43     9954   9269   9505   -369    152    373       C  
ATOM    358  C   GLU A  43      31.166  23.902 -48.619  1.00 77.08           C  
ANISOU  358  C   GLU A  43    10118   9460   9709   -401    197    382       C  
ATOM    359  O   GLU A  43      31.801  23.143 -49.352  1.00 76.40           O  
ANISOU  359  O   GLU A  43    10033   9383   9613   -404    244    390       O  
ATOM    360  CB  GLU A  43      28.867  24.115 -49.558  1.00 78.42           C  
ANISOU  360  CB  GLU A  43    10376   9591   9827   -376    141    395       C  
ATOM    361  CG  GLU A  43      27.410  24.538 -49.270  1.00 82.45           C  
ANISOU  361  CG  GLU A  43    10904  10081  10343   -354     88    398       C  
ATOM    362  CD  GLU A  43      26.490  23.365 -48.939  1.00 85.22           C  
ANISOU  362  CD  GLU A  43    11242  10452  10687   -321     67    391       C  
ATOM    363  OE1 GLU A  43      26.423  22.406 -49.743  1.00 84.90           O  
ANISOU  363  OE1 GLU A  43    11226  10420  10612   -322     77    399       O  
ATOM    364  OE2 GLU A  43      25.826  23.413 -47.877  1.00 85.98           O  
ANISOU  364  OE2 GLU A  43    11309  10552  10810   -295     43    377       O  
ATOM    365  N   SER A  44      31.695  24.969 -48.017  1.00 79.15           N  
ANISOU  365  N   SER A  44    10361   9711  10000   -425    185    381       N  
ATOM    366  CA  SER A  44      33.065  25.427 -48.234  1.00 81.09           C  
ANISOU  366  CA  SER A  44    10581   9957  10273   -461    220    395       C  
ATOM    367  C   SER A  44      34.039  24.961 -47.141  1.00 81.53           C  
ANISOU  367  C   SER A  44    10562  10042  10372   -466    217    390       C  
ATOM    368  O   SER A  44      34.912  25.724 -46.705  1.00 82.12           O  
ANISOU  368  O   SER A  44    10610  10113  10481   -501    210    398       O  
ATOM    369  CB  SER A  44      33.089  26.957 -48.365  1.00 82.06           C  
ANISOU  369  CB  SER A  44    10735  10044  10400   -493    203    403       C  
ATOM    370  OG  SER A  44      32.430  27.573 -47.267  1.00 82.62           O  
ANISOU  370  OG  SER A  44    10808  10104  10479   -485    154    385       O  
ATOM    371  N   GLN A  45      33.876  23.714 -46.695  1.00 80.51           N  
ANISOU  371  N   GLN A  45    10404   9942  10244   -435    217    379       N  
ATOM    372  CA  GLN A  45      34.862  23.063 -45.824  1.00 79.19           C  
ANISOU  372  CA  GLN A  45    10165   9804  10120   -438    216    382       C  
ATOM    373  C   GLN A  45      34.947  21.559 -46.105  1.00 78.01           C  
ANISOU  373  C   GLN A  45     9993   9678   9969   -405    252    383       C  
ATOM    374  O   GLN A  45      33.928  20.905 -46.374  1.00 77.24           O  
ANISOU  374  O   GLN A  45     9933   9583   9832   -374    248    369       O  
ATOM    375  CB  GLN A  45      34.606  23.355 -44.335  1.00 78.52           C  
ANISOU  375  CB  GLN A  45    10065   9725  10045   -442    154    364       C  
ATOM    376  CG  GLN A  45      33.499  22.543 -43.685  1.00 77.94           C  
ANISOU  376  CG  GLN A  45    10005   9665   9945   -403    128    340       C  
ATOM    377  CD  GLN A  45      33.725  22.335 -42.193  1.00 78.56           C  
ANISOU  377  CD  GLN A  45    10051   9757  10039   -409     84    328       C  
ATOM    378  OE1 GLN A  45      34.187  21.273 -41.771  1.00 77.18           O  
ANISOU  378  OE1 GLN A  45     9831   9610   9882   -398     84    332       O  
ATOM    379  NE2 GLN A  45      33.405  23.350 -41.390  1.00 76.27           N  
ANISOU  379  NE2 GLN A  45     9792   9445   9741   -430     47    314       N  
ATOM    380  N   ALA A  46      36.169  21.029 -46.043  1.00 75.87           N  
ANISOU  380  N   ALA A  46     9658   9422   9747   -412    285    402       N  
ATOM    381  CA  ALA A  46      36.451  19.646 -46.434  1.00 73.38           C  
ANISOU  381  CA  ALA A  46     9321   9123   9439   -381    335    407       C  
ATOM    382  C   ALA A  46      35.885  18.627 -45.449  1.00 70.50           C  
ANISOU  382  C   ALA A  46     8936   8782   9067   -349    295    389       C  
ATOM    383  O   ALA A  46      36.162  18.684 -44.246  1.00 70.91           O  
ANISOU  383  O   ALA A  46     8944   8850   9149   -358    245    387       O  
ATOM    384  CB  ALA A  46      37.957  19.436 -46.621  1.00 74.48           C  
ANISOU  384  CB  ALA A  46     9389   9265   9647   -396    388    438       C  
ATOM    385  N   THR A  47      35.089  17.699 -45.975  1.00 65.72           N  
ANISOU  385  N   THR A  47     8372   8178   8419   -317    314    376       N  
ATOM    386  CA  THR A  47      34.522  16.623 -45.172  1.00 61.81           C  
ANISOU  386  CA  THR A  47     7864   7706   7916   -285    285    360       C  
ATOM    387  C   THR A  47      34.196  15.392 -46.014  1.00 59.26           C  
ANISOU  387  C   THR A  47     7572   7382   7563   -256    332    357       C  
ATOM    388  O   THR A  47      33.973  15.491 -47.223  1.00 59.29           O  
ANISOU  388  O   THR A  47     7634   7363   7531   -261    373    360       O  
ATOM    389  CB  THR A  47      33.261  17.088 -44.388  1.00 62.13           C  
ANISOU  389  CB  THR A  47     7937   7747   7923   -280    219    336       C  
ATOM    390  OG1 THR A  47      32.833  16.050 -43.494  1.00 55.80           O  
ANISOU  390  OG1 THR A  47     7116   6966   7118   -254    192    322       O  
ATOM    391  CG2 THR A  47      32.122  17.464 -45.340  1.00 59.82           C  
ANISOU  391  CG2 THR A  47     7717   7431   7579   -276    220    330       C  
ATOM    392  N   LYS A  48      34.178  14.233 -45.365  1.00 55.13           N  
ANISOU  392  N   LYS A  48     7017   6879   7052   -228    325    351       N  
ATOM    393  CA  LYS A  48      33.758  13.001 -46.020  1.00 52.39           C  
ANISOU  393  CA  LYS A  48     6705   6528   6671   -200    363    344       C  
ATOM    394  C   LYS A  48      32.398  12.510 -45.506  1.00 49.42           C  
ANISOU  394  C   LYS A  48     6362   6163   6252   -181    309    322       C  
ATOM    395  O   LYS A  48      31.925  11.445 -45.913  1.00 49.72           O  
ANISOU  395  O   LYS A  48     6432   6200   6261   -161    326    316       O  
ATOM    396  CB  LYS A  48      34.835  11.913 -45.886  1.00 52.92           C  
ANISOU  396  CB  LYS A  48     6715   6603   6787   -181    412    359       C  
ATOM    397  CG  LYS A  48      35.064  11.371 -44.472  1.00 53.54           C  
ANISOU  397  CG  LYS A  48     6725   6710   6907   -167    363    360       C  
ATOM    398  CD  LYS A  48      35.953  10.125 -44.519  1.00 52.81           C  
ANISOU  398  CD  LYS A  48     6585   6620   6862   -141    416    377       C  
ATOM    399  CE  LYS A  48      36.428   9.719 -43.139  1.00 51.62           C  
ANISOU  399  CE  LYS A  48     6357   6494   6764   -135    363    388       C  
ATOM    400  NZ  LYS A  48      37.344   8.545 -43.198  1.00 51.74           N  
ANISOU  400  NZ  LYS A  48     6317   6507   6837   -107    415    412       N  
ATOM    401  N   TYR A  49      31.782  13.292 -44.619  1.00 45.29           N  
ANISOU  401  N   TYR A  49     5833   5647   5729   -189    247    312       N  
ATOM    402  CA  TYR A  49      30.475  12.961 -44.036  1.00 43.08           C  
ANISOU  402  CA  TYR A  49     5576   5374   5418   -172    200    294       C  
ATOM    403  C   TYR A  49      29.377  13.841 -44.617  1.00 42.45           C  
ANISOU  403  C   TYR A  49     5552   5272   5305   -181    177    292       C  
ATOM    404  O   TYR A  49      29.501  15.065 -44.646  1.00 42.57           O  
ANISOU  404  O   TYR A  49     5572   5274   5330   -202    167    296       O  
ATOM    405  CB  TYR A  49      30.499  13.105 -42.511  1.00 40.39           C  
ANISOU  405  CB  TYR A  49     5194   5051   5103   -171    153    284       C  
ATOM    406  CG  TYR A  49      31.627  12.351 -41.841  1.00 39.84           C  
ANISOU  406  CG  TYR A  49     5063   5001   5073   -167    161    293       C  
ATOM    407  CD1 TYR A  49      32.771  13.018 -41.393  1.00 37.54           C  
ANISOU  407  CD1 TYR A  49     4725   4711   4826   -193    154    308       C  
ATOM    408  CD2 TYR A  49      31.551  10.972 -41.655  1.00 36.47           C  
ANISOU  408  CD2 TYR A  49     4625   4588   4645   -140    171    291       C  
ATOM    409  CE1 TYR A  49      33.805  12.332 -40.777  1.00 33.40           C  
ANISOU  409  CE1 TYR A  49     4140   4203   4350   -192    153    325       C  
ATOM    410  CE2 TYR A  49      32.577  10.275 -41.051  1.00 38.66           C  
ANISOU  410  CE2 TYR A  49     4844   4880   4966   -135    175    305       C  
ATOM    411  CZ  TYR A  49      33.704  10.956 -40.613  1.00 39.08           C  
ANISOU  411  CZ  TYR A  49     4845   4934   5068   -161    164    324       C  
ATOM    412  OH  TYR A  49      34.717  10.249 -40.001  1.00 38.20           O  
ANISOU  412  OH  TYR A  49     4669   4836   5010   -157    160    346       O  
ATOM    413  N   PHE A  50      28.311  13.200 -45.084  1.00 41.87           N  
ANISOU  413  N   PHE A  50     5519   5194   5197   -167    167    290       N  
ATOM    414  CA  PHE A  50      27.183  13.884 -45.713  1.00 40.89           C  
ANISOU  414  CA  PHE A  50     5443   5046   5046   -174    139    296       C  
ATOM    415  C   PHE A  50      25.887  13.270 -45.231  1.00 39.80           C  
ANISOU  415  C   PHE A  50     5309   4914   4898   -153    100    290       C  
ATOM    416  O   PHE A  50      25.807  12.047 -45.034  1.00 38.10           O  
ANISOU  416  O   PHE A  50     5089   4716   4674   -137    106    284       O  
ATOM    417  CB  PHE A  50      27.243  13.746 -47.242  1.00 41.39           C  
ANISOU  417  CB  PHE A  50     5568   5087   5071   -191    168    312       C  
ATOM    418  CG  PHE A  50      28.471  14.340 -47.857  1.00 41.05           C  
ANISOU  418  CG  PHE A  50     5526   5033   5037   -213    217    320       C  
ATOM    419  CD1 PHE A  50      29.639  13.594 -47.967  1.00 40.44           C  
ANISOU  419  CD1 PHE A  50     5424   4965   4975   -208    274    320       C  
ATOM    420  CD2 PHE A  50      28.462  15.651 -48.324  1.00 42.69           C  
ANISOU  420  CD2 PHE A  50     5756   5219   5245   -237    208    332       C  
ATOM    421  CE1 PHE A  50      30.780  14.145 -48.532  1.00 42.92           C  
ANISOU  421  CE1 PHE A  50     5732   5267   5307   -228    326    332       C  
ATOM    422  CE2 PHE A  50      29.601  16.215 -48.892  1.00 43.94           C  
ANISOU  422  CE2 PHE A  50     5915   5367   5414   -260    256    342       C  
ATOM    423  CZ  PHE A  50      30.761  15.459 -48.998  1.00 42.21           C  
ANISOU  423  CZ  PHE A  50     5667   5157   5212   -255    316    343       C  
ATOM    424  N   ASP A  51      24.866  14.105 -45.056  1.00 36.26           N  
ANISOU  424  N   ASP A  51     4871   4450   4457   -153     63    295       N  
ATOM    425  CA  ASP A  51      23.543  13.584 -44.738  1.00 35.08           C  
ANISOU  425  CA  ASP A  51     4723   4301   4306   -134     29    297       C  
ATOM    426  C   ASP A  51      22.944  12.926 -45.977  1.00 35.42           C  
ANISOU  426  C   ASP A  51     4815   4331   4312   -143     19    316       C  
ATOM    427  O   ASP A  51      23.562  12.928 -47.045  1.00 38.76           O  
ANISOU  427  O   ASP A  51     5278   4743   4707   -164     43    325       O  
ATOM    428  CB  ASP A  51      22.632  14.655 -44.121  1.00 33.70           C  
ANISOU  428  CB  ASP A  51     4536   4108   4160   -127      2    300       C  
ATOM    429  CG  ASP A  51      22.163  15.704 -45.115  1.00 32.74           C  
ANISOU  429  CG  ASP A  51     4447   3953   4038   -143    -15    325       C  
ATOM    430  OD1 ASP A  51      22.212  15.501 -46.347  1.00 31.06           O  
ANISOU  430  OD1 ASP A  51     4276   3730   3796   -161    -18    343       O  
ATOM    431  OD2 ASP A  51      21.715  16.758 -44.634  1.00 37.14           O  
ANISOU  431  OD2 ASP A  51     4994   4490   4626   -137    -26    327       O  
ATOM    432  N   ILE A  52      21.757  12.353 -45.842  1.00 35.61           N  
ANISOU  432  N   ILE A  52     4840   4354   4336   -132    -16    325       N  
ATOM    433  CA  ILE A  52      21.190  11.539 -46.924  1.00 34.46           C  
ANISOU  433  CA  ILE A  52     4744   4196   4151   -146    -34    343       C  
ATOM    434  C   ILE A  52      20.846  12.353 -48.181  1.00 36.59           C  
ANISOU  434  C   ILE A  52     5068   4432   4402   -175    -58    373       C  
ATOM    435  O   ILE A  52      20.780  11.805 -49.284  1.00 36.65           O  
ANISOU  435  O   ILE A  52     5139   4425   4363   -199    -64    387       O  
ATOM    436  CB  ILE A  52      19.987  10.706 -46.443  1.00 32.28           C  
ANISOU  436  CB  ILE A  52     4451   3927   3885   -131    -71    350       C  
ATOM    437  CG1 ILE A  52      18.894  11.609 -45.856  1.00 31.76           C  
ANISOU  437  CG1 ILE A  52     4350   3849   3870   -118   -106    365       C  
ATOM    438  CG2 ILE A  52      20.457   9.663 -45.434  1.00 33.45           C  
ANISOU  438  CG2 ILE A  52     4566   4106   4037   -108    -44    322       C  
ATOM    439  CD1 ILE A  52      17.556  10.907 -45.607  1.00 32.77           C  
ANISOU  439  CD1 ILE A  52     4461   3976   4016   -108   -145    383       C  
ATOM    440  N   TYR A  53      20.667  13.660 -47.998  1.00 37.47           N  
ANISOU  440  N   TYR A  53     5161   4529   4546   -175    -71    382       N  
ATOM    441  CA  TYR A  53      20.364  14.583 -49.085  1.00 39.25           C  
ANISOU  441  CA  TYR A  53     5433   4721   4761   -202    -97    412       C  
ATOM    442  C   TYR A  53      21.632  15.144 -49.740  1.00 41.57           C  
ANISOU  442  C   TYR A  53     5760   5007   5028   -225    -52    405       C  
ATOM    443  O   TYR A  53      21.552  15.995 -50.625  1.00 40.96           O  
ANISOU  443  O   TYR A  53     5725   4901   4937   -250    -67    428       O  
ATOM    444  CB  TYR A  53      19.471  15.713 -48.564  1.00 39.45           C  
ANISOU  444  CB  TYR A  53     5420   4727   4840   -188   -132    429       C  
ATOM    445  CG  TYR A  53      18.306  15.197 -47.750  1.00 42.85           C  
ANISOU  445  CG  TYR A  53     5806   5164   5310   -161   -161    435       C  
ATOM    446  CD1 TYR A  53      18.256  15.375 -46.366  1.00 44.76           C  
ANISOU  446  CD1 TYR A  53     5992   5420   5593   -129   -138    410       C  
ATOM    447  CD2 TYR A  53      17.272  14.497 -48.360  1.00 43.69           C  
ANISOU  447  CD2 TYR A  53     5930   5261   5408   -171   -210    466       C  
ATOM    448  CE1 TYR A  53      17.188  14.879 -45.615  1.00 46.20           C  
ANISOU  448  CE1 TYR A  53     6136   5607   5812   -105   -154    415       C  
ATOM    449  CE2 TYR A  53      16.208  14.001 -47.626  1.00 47.73           C  
ANISOU  449  CE2 TYR A  53     6396   5779   5962   -148   -234    475       C  
ATOM    450  CZ  TYR A  53      16.170  14.194 -46.258  1.00 48.54           C  
ANISOU  450  CZ  TYR A  53     6440   5894   6107   -113   -201    449       C  
ATOM    451  OH  TYR A  53      15.104  13.696 -45.549  1.00 51.41           O  
ANISOU  451  OH  TYR A  53     6761   6261   6513    -90   -216    459       O  
ATOM    452  N   GLY A  54      22.796  14.656 -49.309  1.00 42.24           N  
ANISOU  452  N   GLY A  54     5824   5117   5110   -217      3    377       N  
ATOM    453  CA  GLY A  54      24.077  15.116 -49.844  1.00 43.30           C  
ANISOU  453  CA  GLY A  54     5977   5246   5231   -236     54    372       C  
ATOM    454  C   GLY A  54      24.548  16.453 -49.288  1.00 43.98           C  
ANISOU  454  C   GLY A  54     6025   5328   5356   -238     59    368       C  
ATOM    455  O   GLY A  54      25.389  17.124 -49.887  1.00 43.51           O  
ANISOU  455  O   GLY A  54     5986   5255   5289   -261     90    374       O  
ATOM    456  N   LYS A  55      23.998  16.850 -48.146  1.00 44.98           N  
ANISOU  456  N   LYS A  55     6103   5463   5523   -216     31    359       N  
ATOM    457  CA  LYS A  55      24.482  18.035 -47.442  1.00 45.07           C  
ANISOU  457  CA  LYS A  55     6085   5470   5570   -219     38    351       C  
ATOM    458  C   LYS A  55      25.656  17.643 -46.547  1.00 42.91           C  
ANISOU  458  C   LYS A  55     5766   5227   5312   -215     71    327       C  
ATOM    459  O   LYS A  55      25.584  16.636 -45.841  1.00 43.79           O  
ANISOU  459  O   LYS A  55     5849   5362   5426   -195     71    313       O  
ATOM    460  CB  LYS A  55      23.363  18.713 -46.639  1.00 45.66           C  
ANISOU  460  CB  LYS A  55     6141   5531   5679   -199      1    352       C  
ATOM    461  CG  LYS A  55      22.238  19.275 -47.510  1.00 51.73           C  
ANISOU  461  CG  LYS A  55     6943   6264   6448   -204    -38    385       C  
ATOM    462  CD  LYS A  55      21.340  20.251 -46.746  1.00 60.05           C  
ANISOU  462  CD  LYS A  55     7972   7293   7549   -184    -59    390       C  
ATOM    463  CE  LYS A  55      21.842  21.706 -46.833  1.00 65.48           C  
ANISOU  463  CE  LYS A  55     8674   7953   8251   -200    -49    392       C  
ATOM    464  NZ  LYS A  55      21.831  22.270 -48.229  1.00 65.38           N  
ANISOU  464  NZ  LYS A  55     8711   7913   8218   -228    -66    425       N  
ATOM    465  N   PRO A  56      26.748  18.430 -46.591  1.00 41.40           N  
ANISOU  465  N   PRO A  56     5566   5031   5134   -236     96    327       N  
ATOM    466  CA  PRO A  56      27.972  18.122 -45.860  1.00 41.09           C  
ANISOU  466  CA  PRO A  56     5479   5016   5117   -240    122    314       C  
ATOM    467  C   PRO A  56      27.814  18.271 -44.350  1.00 40.02           C  
ANISOU  467  C   PRO A  56     5307   4893   5008   -229     94    295       C  
ATOM    468  O   PRO A  56      27.128  19.189 -43.880  1.00 38.09           O  
ANISOU  468  O   PRO A  56     5074   4629   4771   -228     69    291       O  
ATOM    469  CB  PRO A  56      28.966  19.158 -46.398  1.00 41.98           C  
ANISOU  469  CB  PRO A  56     5597   5112   5240   -272    146    326       C  
ATOM    470  CG  PRO A  56      28.122  20.311 -46.810  1.00 41.79           C  
ANISOU  470  CG  PRO A  56     5614   5056   5208   -281    119    335       C  
ATOM    471  CD  PRO A  56      26.867  19.689 -47.353  1.00 42.45           C  
ANISOU  471  CD  PRO A  56     5732   5132   5264   -262     96    343       C  
ATOM    472  N   CYS A  57      28.446  17.366 -43.608  1.00 38.64           N  
ANISOU  472  N   CYS A  57     5091   4746   4844   -220    100    286       N  
ATOM    473  CA  CYS A  57      28.382  17.366 -42.148  1.00 39.95           C  
ANISOU  473  CA  CYS A  57     5231   4923   5025   -215     73    268       C  
ATOM    474  C   CYS A  57      29.771  17.292 -41.540  1.00 39.76           C  
ANISOU  474  C   CYS A  57     5163   4915   5028   -236     77    271       C  
ATOM    475  O   CYS A  57      30.681  16.712 -42.116  1.00 41.61           O  
ANISOU  475  O   CYS A  57     5372   5162   5277   -239    107    285       O  
ATOM    476  CB  CYS A  57      27.543  16.195 -41.626  1.00 39.44           C  
ANISOU  476  CB  CYS A  57     5162   4875   4948   -185     62    257       C  
ATOM    477  SG  CYS A  57      25.813  16.183 -42.143  1.00 44.66           S  
ANISOU  477  SG  CYS A  57     5861   5518   5591   -162     46    260       S  
ATOM    478  N   THR A  58      29.922  17.885 -40.367  1.00 40.11           N  
ANISOU  478  N   THR A  58     5201   4956   5083   -252     47    260       N  
ATOM    479  CA  THR A  58      31.153  17.758 -39.605  1.00 40.65           C  
ANISOU  479  CA  THR A  58     5227   5040   5180   -276     33    267       C  
ATOM    480  C   THR A  58      30.923  16.764 -38.466  1.00 39.17           C  
ANISOU  480  C   THR A  58     5025   4872   4987   -260      8    255       C  
ATOM    481  O   THR A  58      29.843  16.748 -37.866  1.00 39.06           O  
ANISOU  481  O   THR A  58     5043   4850   4947   -244     -5    235       O  
ATOM    482  CB  THR A  58      31.655  19.138 -39.077  1.00 42.06           C  
ANISOU  482  CB  THR A  58     5416   5196   5369   -317      9    267       C  
ATOM    483  OG1 THR A  58      32.759  18.939 -38.188  1.00 45.63           O  
ANISOU  483  OG1 THR A  58     5827   5662   5848   -346    -19    278       O  
ATOM    484  CG2 THR A  58      30.551  19.898 -38.335  1.00 37.93           C  
ANISOU  484  CG2 THR A  58     4946   4647   4820   -314    -11    243       C  
ATOM    485  N   ARG A  59      31.922  15.924 -38.195  1.00 38.10           N  
ANISOU  485  N   ARG A  59     4840   4759   4879   -264      5    270       N  
ATOM    486  CA  ARG A  59      31.833  14.937 -37.118  1.00 37.44           C  
ANISOU  486  CA  ARG A  59     4741   4693   4790   -253    -22    263       C  
ATOM    487  C   ARG A  59      32.202  15.559 -35.777  1.00 39.17           C  
ANISOU  487  C   ARG A  59     4968   4904   5009   -290    -73    259       C  
ATOM    488  O   ARG A  59      33.236  16.224 -35.658  1.00 39.33           O  
ANISOU  488  O   ARG A  59     4965   4919   5059   -328    -92    277       O  
ATOM    489  CB  ARG A  59      32.740  13.725 -37.391  1.00 37.10           C  
ANISOU  489  CB  ARG A  59     4641   4674   4782   -239     -5    286       C  
ATOM    490  CG  ARG A  59      32.782  12.740 -36.237  1.00 40.42           C  
ANISOU  490  CG  ARG A  59     5044   5112   5203   -231    -40    285       C  
ATOM    491  CD  ARG A  59      33.169  11.341 -36.654  1.00 43.19           C  
ANISOU  491  CD  ARG A  59     5354   5480   5576   -200    -12    300       C  
ATOM    492  NE  ARG A  59      34.609  11.172 -36.789  1.00 45.00           N  
ANISOU  492  NE  ARG A  59     5515   5713   5868   -213     -5    336       N  
ATOM    493  CZ  ARG A  59      35.382  10.522 -35.928  1.00 44.93           C  
ANISOU  493  CZ  ARG A  59     5458   5717   5898   -220    -41    358       C  
ATOM    494  NH1 ARG A  59      34.866   9.960 -34.844  1.00 44.95           N  
ANISOU  494  NH1 ARG A  59     5479   5728   5872   -217    -85    346       N  
ATOM    495  NH2 ARG A  59      36.682  10.425 -36.164  1.00 49.06           N  
ANISOU  495  NH2 ARG A  59     5910   6241   6491   -230    -30    398       N  
ATOM    496  N   LYS A  60      31.360  15.331 -34.772  1.00 40.29           N  
ANISOU  496  N   LYS A  60     5147   5043   5118   -282    -95    236       N  
ATOM    497  CA  LYS A  60      31.652  15.775 -33.417  1.00 41.70           C  
ANISOU  497  CA  LYS A  60     5350   5210   5285   -320   -144    229       C  
ATOM    498  C   LYS A  60      31.917  14.599 -32.493  1.00 42.11           C  
ANISOU  498  C   LYS A  60     5383   5283   5336   -318   -175    235       C  
ATOM    499  O   LYS A  60      31.011  13.837 -32.149  1.00 40.76           O  
ANISOU  499  O   LYS A  60     5232   5117   5136   -288   -165    218       O  
ATOM    500  CB  LYS A  60      30.551  16.689 -32.891  1.00 43.86           C  
ANISOU  500  CB  LYS A  60     5697   5451   5517   -322   -139    198       C  
ATOM    501  CG  LYS A  60      30.482  18.016 -33.650  1.00 49.76           C  
ANISOU  501  CG  LYS A  60     6464   6171   6271   -335   -119    197       C  
ATOM    502  CD  LYS A  60      29.771  19.088 -32.858  1.00 53.65           C  
ANISOU  502  CD  LYS A  60     7030   6623   6733   -350   -122    171       C  
ATOM    503  CE  LYS A  60      29.538  20.333 -33.706  1.00 60.57           C  
ANISOU  503  CE  LYS A  60     7925   7469   7618   -353    -97    171       C  
ATOM    504  NZ  LYS A  60      30.643  21.333 -33.616  1.00 62.85           N  
ANISOU  504  NZ  LYS A  60     8218   7743   7918   -407   -124    183       N  
ATOM    505  N   LEU A  61      33.189  14.455 -32.128  1.00 44.65           N  
ANISOU  505  N   LEU A  61     5659   5614   5693   -351   -214    265       N  
ATOM    506  CA  LEU A  61      33.674  13.390 -31.259  1.00 46.25           C  
ANISOU  506  CA  LEU A  61     5833   5834   5904   -356   -255    281       C  
ATOM    507  C   LEU A  61      33.600  13.850 -29.800  1.00 45.89           C  
ANISOU  507  C   LEU A  61     5849   5769   5819   -402   -315    269       C  
ATOM    508  O   LEU A  61      34.164  14.887 -29.447  1.00 46.94           O  
ANISOU  508  O   LEU A  61     6002   5881   5952   -453   -349    276       O  
ATOM    509  CB  LEU A  61      35.117  13.024 -31.658  1.00 47.08           C  
ANISOU  509  CB  LEU A  61     5851   5955   6081   -368   -268    328       C  
ATOM    510  CG  LEU A  61      35.858  11.780 -31.123  1.00 50.11           C  
ANISOU  510  CG  LEU A  61     6177   6358   6503   -363   -302    361       C  
ATOM    511  CD1 LEU A  61      36.668  12.103 -29.874  1.00 54.46           C  
ANISOU  511  CD1 LEU A  61     6728   6900   7063   -424   -390    385       C  
ATOM    512  CD2 LEU A  61      34.953  10.559 -30.891  1.00 43.16           C  
ANISOU  512  CD2 LEU A  61     5318   5491   5590   -318   -284    340       C  
ATOM    513  N   PHE A  62      32.910  13.073 -28.965  1.00 42.33           N  
ANISOU  513  N   PHE A  62     5434   5321   5329   -388   -325    252       N  
ATOM    514  CA  PHE A  62      32.666  13.443 -27.568  1.00 41.97           C  
ANISOU  514  CA  PHE A  62     5467   5250   5231   -430   -369    234       C  
ATOM    515  C   PHE A  62      33.488  12.634 -26.570  1.00 42.20           C  
ANISOU  515  C   PHE A  62     5479   5290   5266   -462   -441    263       C  
ATOM    516  O   PHE A  62      33.709  11.433 -26.763  1.00 40.55           O  
ANISOU  516  O   PHE A  62     5212   5108   5087   -430   -440    283       O  
ATOM    517  CB  PHE A  62      31.169  13.329 -27.232  1.00 40.22           C  
ANISOU  517  CB  PHE A  62     5314   5014   4953   -396   -324    192       C  
ATOM    518  CG  PHE A  62      30.312  14.275 -28.015  1.00 40.63           C  
ANISOU  518  CG  PHE A  62     5391   5047   5001   -373   -266    168       C  
ATOM    519  CD1 PHE A  62      29.625  13.837 -29.145  1.00 40.21           C  
ANISOU  519  CD1 PHE A  62     5300   5010   4967   -318   -214    166       C  
ATOM    520  CD2 PHE A  62      30.215  15.618 -27.641  1.00 38.88           C  
ANISOU  520  CD2 PHE A  62     5233   4786   4755   -408   -268    151       C  
ATOM    521  CE1 PHE A  62      28.835  14.720 -29.890  1.00 41.10           C  
ANISOU  521  CE1 PHE A  62     5433   5103   5079   -298   -169    150       C  
ATOM    522  CE2 PHE A  62      29.440  16.511 -28.382  1.00 40.47           C  
ANISOU  522  CE2 PHE A  62     5453   4966   4958   -384   -217    133       C  
ATOM    523  CZ  PHE A  62      28.746  16.063 -29.509  1.00 38.63           C  
ANISOU  523  CZ  PHE A  62     5177   4752   4749   -329   -170    135       C  
ATOM    524  N   ALA A  63      33.915  13.302 -25.497  1.00 39.74           N  
ANISOU  524  N   ALA A  63     5224   4952   4923   -527   -503    266       N  
ATOM    525  CA  ALA A  63      34.732  12.687 -24.457  1.00 41.41           C  
ANISOU  525  CA  ALA A  63     5431   5166   5137   -571   -588    298       C  
ATOM    526  C   ALA A  63      34.057  11.468 -23.843  1.00 40.50           C  
ANISOU  526  C   ALA A  63     5338   5061   4987   -541   -583    287       C  
ATOM    527  O   ALA A  63      34.728  10.560 -23.365  1.00 41.68           O  
ANISOU  527  O   ALA A  63     5450   5226   5160   -552   -639    322       O  
ATOM    528  CB  ALA A  63      35.079  13.716 -23.361  1.00 42.06           C  
ANISOU  528  CB  ALA A  63     5602   5209   5171   -653   -655    295       C  
ATOM    529  N   ASN A  64      32.727  11.469 -23.856  1.00 40.69           N  
ANISOU  529  N   ASN A  64     5423   5077   4961   -502   -517    241       N  
ATOM    530  CA  ASN A  64      31.918  10.396 -23.284  1.00 41.55           C  
ANISOU  530  CA  ASN A  64     5562   5192   5033   -473   -502    225       C  
ATOM    531  C   ASN A  64      30.460  10.534 -23.723  1.00 40.43           C  
ANISOU  531  C   ASN A  64     5456   5043   4863   -421   -414    181       C  
ATOM    532  O   ASN A  64      30.066  11.564 -24.276  1.00 39.11           O  
ANISOU  532  O   ASN A  64     5306   4859   4697   -415   -374    162       O  
ATOM    533  CB  ASN A  64      32.021  10.403 -21.752  1.00 42.20           C  
ANISOU  533  CB  ASN A  64     5736   5247   5052   -533   -565    222       C  
ATOM    534  CG  ASN A  64      31.760  11.773 -21.163  1.00 45.84           C  
ANISOU  534  CG  ASN A  64     6299   5662   5456   -582   -564    192       C  
ATOM    535  OD1 ASN A  64      30.718  12.379 -21.422  1.00 46.51           O  
ANISOU  535  OD1 ASN A  64     6429   5726   5515   -553   -490    152       O  
ATOM    536  ND2 ASN A  64      32.712  12.277 -20.375  1.00 44.50           N  
ANISOU  536  ND2 ASN A  64     6168   5471   5271   -659   -649    215       N  
ATOM    537  N   MET A  65      29.665   9.504 -23.449  1.00 40.08           N  
ANISOU  537  N   MET A  65     5421   5008   4797   -387   -390    169       N  
ATOM    538  CA  MET A  65      28.289   9.434 -23.935  1.00 40.17           C  
ANISOU  538  CA  MET A  65     5448   5017   4797   -334   -311    138       C  
ATOM    539  C   MET A  65      27.342  10.473 -23.329  1.00 41.40           C  
ANISOU  539  C   MET A  65     5696   5129   4904   -347   -272    101       C  
ATOM    540  O   MET A  65      26.439  10.968 -24.011  1.00 42.73           O  
ANISOU  540  O   MET A  65     5861   5287   5085   -311   -210     83       O  
ATOM    541  CB  MET A  65      27.742   8.022 -23.754  1.00 37.29           C  
ANISOU  541  CB  MET A  65     5068   4673   4426   -299   -300    139       C  
ATOM    542  CG  MET A  65      28.405   7.023 -24.687  1.00 37.46           C  
ANISOU  542  CG  MET A  65     4996   4733   4503   -268   -310    170       C  
ATOM    543  SD  MET A  65      27.759   5.359 -24.498  1.00 39.06           S  
ANISOU  543  SD  MET A  65     5188   4957   4697   -228   -296    172       S  
ATOM    544  CE  MET A  65      28.615   4.794 -23.033  1.00 39.56           C  
ANISOU  544  CE  MET A  65     5281   5015   4734   -277   -377    193       C  
ATOM    545  N   ARG A  66      27.543  10.796 -22.057  1.00 43.91           N  
ANISOU  545  N   ARG A  66     6099   5416   5168   -399   -305     91       N  
ATOM    546  CA  ARG A  66      26.740  11.821 -21.403  1.00 47.53           C  
ANISOU  546  CA  ARG A  66     6657   5824   5578   -415   -261     55       C  
ATOM    547  C   ARG A  66      26.945  13.199 -22.044  1.00 45.31           C  
ANISOU  547  C   ARG A  66     6376   5521   5317   -425   -246     49       C  
ATOM    548  O   ARG A  66      25.986  13.936 -22.224  1.00 44.86           O  
ANISOU  548  O   ARG A  66     6355   5434   5257   -401   -179     23       O  
ATOM    549  CB  ARG A  66      27.006  11.849 -19.896  1.00 51.27           C  
ANISOU  549  CB  ARG A  66     7237   6264   5981   -477   -303     46       C  
ATOM    550  CG  ARG A  66      26.291  10.717 -19.140  1.00 61.69           C  
ANISOU  550  CG  ARG A  66     8589   7587   7264   -460   -284     37       C  
ATOM    551  CD  ARG A  66      26.650  10.711 -17.654  1.00 69.90           C  
ANISOU  551  CD  ARG A  66     9743   8592   8226   -529   -334     33       C  
ATOM    552  NE  ARG A  66      26.003   9.616 -16.932  1.00 73.93           N  
ANISOU  552  NE  ARG A  66    10287   9104   8700   -516   -316     26       N  
ATOM    553  CZ  ARG A  66      26.335   9.216 -15.704  1.00 77.87           C  
ANISOU  553  CZ  ARG A  66    10872   9582   9132   -571   -368     30       C  
ATOM    554  NH1 ARG A  66      27.322   9.815 -15.042  1.00 78.93           N  
ANISOU  554  NH1 ARG A  66    11068   9692   9229   -647   -448     43       N  
ATOM    555  NH2 ARG A  66      25.681   8.207 -15.136  1.00 78.63           N  
ANISOU  555  NH2 ARG A  66    10996   9681   9199   -554   -343     24       N  
ATOM    556  N   ASP A  67      28.187  13.523 -22.401  1.00 44.66           N  
ANISOU  556  N   ASP A  67     6252   5454   5265   -460   -308     77       N  
ATOM    557  CA  ASP A  67      28.487  14.754 -23.131  1.00 47.39           C  
ANISOU  557  CA  ASP A  67     6586   5784   5635   -471   -297     77       C  
ATOM    558  C   ASP A  67      27.743  14.776 -24.462  1.00 46.51           C  
ANISOU  558  C   ASP A  67     6410   5691   5572   -405   -232     74       C  
ATOM    559  O   ASP A  67      27.159  15.794 -24.833  1.00 45.93           O  
ANISOU  559  O   ASP A  67     6365   5587   5501   -394   -187     56       O  
ATOM    560  CB  ASP A  67      29.993  14.897 -23.382  1.00 49.49           C  
ANISOU  560  CB  ASP A  67     6797   6070   5937   -516   -373    115       C  
ATOM    561  CG  ASP A  67      30.751  15.468 -22.184  1.00 52.47           C  
ANISOU  561  CG  ASP A  67     7254   6413   6268   -598   -445    119       C  
ATOM    562  OD1 ASP A  67      30.149  15.726 -21.116  1.00 54.02           O  
ANISOU  562  OD1 ASP A  67     7561   6569   6396   -623   -434     89       O  
ATOM    563  OD2 ASP A  67      31.977  15.654 -22.322  1.00 56.81           O  
ANISOU  563  OD2 ASP A  67     7757   6976   6853   -641   -513    156       O  
ATOM    564  N   ALA A  68      27.762  13.642 -25.165  1.00 45.10           N  
ANISOU  564  N   ALA A  68     6151   5557   5429   -364   -230     93       N  
ATOM    565  CA  ALA A  68      27.048  13.492 -26.435  1.00 43.80           C  
ANISOU  565  CA  ALA A  68     5931   5409   5302   -307   -177     94       C  
ATOM    566  C   ALA A  68      25.547  13.763 -26.293  1.00 43.18           C  
ANISOU  566  C   ALA A  68     5898   5301   5206   -272   -113     66       C  
ATOM    567  O   ALA A  68      24.964  14.480 -27.112  1.00 41.26           O  
ANISOU  567  O   ALA A  68     5645   5044   4987   -247    -75     63       O  
ATOM    568  CB  ALA A  68      27.294  12.112 -27.022  1.00 41.68           C  
ANISOU  568  CB  ALA A  68     5589   5185   5061   -275   -186    116       C  
ATOM    569  N   SER A  69      24.945  13.192 -25.245  1.00 42.33           N  
ANISOU  569  N   SER A  69     5839   5183   5062   -271   -103     50       N  
ATOM    570  CA  SER A  69      23.533  13.406 -24.909  1.00 42.31           C  
ANISOU  570  CA  SER A  69     5880   5148   5048   -241    -36     26       C  
ATOM    571  C   SER A  69      23.181  14.861 -24.586  1.00 41.73           C  
ANISOU  571  C   SER A  69     5875   5018   4961   -256      0      5       C  
ATOM    572  O   SER A  69      22.140  15.361 -25.007  1.00 39.77           O  
ANISOU  572  O   SER A  69     5625   4745   4739   -219     59     -2       O  
ATOM    573  CB  SER A  69      23.128  12.513 -23.732  1.00 42.02           C  
ANISOU  573  CB  SER A  69     5890   5107   4969   -246    -32     14       C  
ATOM    574  OG  SER A  69      22.748  11.231 -24.190  1.00 47.39           O  
ANISOU  574  OG  SER A  69     6509   5826   5671   -208    -29     29       O  
ATOM    575  N   GLN A  70      24.045  15.521 -23.821  1.00 43.11           N  
ANISOU  575  N   GLN A  70     6112   5169   5098   -313    -37     -3       N  
ATOM    576  CA  GLN A  70      23.848  16.919 -23.456  1.00 43.98           C  
ANISOU  576  CA  GLN A  70     6300   5220   5189   -335     -6    -25       C  
ATOM    577  C   GLN A  70      23.978  17.836 -24.672  1.00 42.37           C  
ANISOU  577  C   GLN A  70     6049   5017   5035   -320      2    -13       C  
ATOM    578  O   GLN A  70      23.339  18.889 -24.740  1.00 42.47           O  
ANISOU  578  O   GLN A  70     6101   4981   5053   -309     52    -28       O  
ATOM    579  CB  GLN A  70      24.851  17.332 -22.374  1.00 45.58           C  
ANISOU  579  CB  GLN A  70     6585   5399   5334   -410    -62    -32       C  
ATOM    580  CG  GLN A  70      24.616  16.679 -21.011  1.00 53.31           C  
ANISOU  580  CG  GLN A  70     7646   6360   6250   -434    -64    -49       C  
ATOM    581  CD  GLN A  70      23.286  17.084 -20.383  1.00 59.86           C  
ANISOU  581  CD  GLN A  70     8558   7133   7054   -409     31    -83       C  
ATOM    582  OE1 GLN A  70      22.393  16.250 -20.198  1.00 60.00           O  
ANISOU  582  OE1 GLN A  70     8562   7159   7075   -369     77    -87       O  
ATOM    583  NE2 GLN A  70      23.146  18.372 -20.066  1.00 59.75           N  
ANISOU  583  NE2 GLN A  70     8628   7057   7018   -431     67   -106       N  
ATOM    584  N   TRP A  71      24.810  17.433 -25.629  1.00 41.20           N  
ANISOU  584  N   TRP A  71     5817   4918   4921   -319    -44     15       N  
ATOM    585  CA  TRP A  71      24.969  18.196 -26.860  1.00 41.47           C  
ANISOU  585  CA  TRP A  71     5804   4953   4998   -306    -37     30       C  
ATOM    586  C   TRP A  71      23.666  18.159 -27.639  1.00 40.25           C  
ANISOU  586  C   TRP A  71     5620   4794   4879   -246     22     30       C  
ATOM    587  O   TRP A  71      23.201  19.180 -28.128  1.00 39.05           O  
ANISOU  587  O   TRP A  71     5480   4608   4749   -233     54     28       O  
ATOM    588  CB  TRP A  71      26.132  17.661 -27.696  1.00 40.75           C  
ANISOU  588  CB  TRP A  71     5634   4913   4936   -318    -88     60       C  
ATOM    589  CG  TRP A  71      26.336  18.423 -28.974  1.00 40.98           C  
ANISOU  589  CG  TRP A  71     5624   4943   5004   -309    -77     75       C  
ATOM    590  CD1 TRP A  71      26.897  19.668 -29.109  1.00 41.73           C  
ANISOU  590  CD1 TRP A  71     5745   5010   5102   -344    -87     76       C  
ATOM    591  CD2 TRP A  71      25.982  17.996 -30.294  1.00 37.16           C  
ANISOU  591  CD2 TRP A  71     5076   4487   4558   -266    -57     93       C  
ATOM    592  NE1 TRP A  71      26.908  20.038 -30.435  1.00 43.65           N  
ANISOU  592  NE1 TRP A  71     5941   5261   5381   -324    -72     93       N  
ATOM    593  CE2 TRP A  71      26.350  19.034 -31.182  1.00 38.66           C  
ANISOU  593  CE2 TRP A  71     5257   4663   4769   -277    -53    104       C  
ATOM    594  CE3 TRP A  71      25.385  16.840 -30.814  1.00 38.87           C  
ANISOU  594  CE3 TRP A  71     5249   4735   4786   -224    -42    102       C  
ATOM    595  CZ2 TRP A  71      26.142  18.951 -32.560  1.00 37.02           C  
ANISOU  595  CZ2 TRP A  71     5004   4470   4591   -249    -37    123       C  
ATOM    596  CZ3 TRP A  71      25.173  16.759 -32.194  1.00 36.90           C  
ANISOU  596  CZ3 TRP A  71     4955   4500   4566   -197    -28    120       C  
ATOM    597  CH2 TRP A  71      25.553  17.808 -33.046  1.00 39.19           C  
ANISOU  597  CH2 TRP A  71     5243   4775   4874   -210    -25    130       C  
ATOM    598  N   ILE A  72      23.062  16.978 -27.720  1.00 42.94           N  
ANISOU  598  N   ILE A  72     5924   5164   5228   -210     32     36       N  
ATOM    599  CA  ILE A  72      21.740  16.830 -28.332  1.00 44.31           C  
ANISOU  599  CA  ILE A  72     6069   5331   5436   -157     80     41       C  
ATOM    600  C   ILE A  72      20.753  17.843 -27.733  1.00 45.00           C  
ANISOU  600  C   ILE A  72     6216   5356   5526   -145    140     22       C  
ATOM    601  O   ILE A  72      20.110  18.594 -28.466  1.00 45.85           O  
ANISOU  601  O   ILE A  72     6308   5439   5675   -119    169     32       O  
ATOM    602  CB  ILE A  72      21.211  15.384 -28.198  1.00 43.39           C  
ANISOU  602  CB  ILE A  72     5919   5248   5319   -130     82     47       C  
ATOM    603  CG1 ILE A  72      22.034  14.439 -29.081  1.00 43.55           C  
ANISOU  603  CG1 ILE A  72     5875   5323   5350   -131     37     69       C  
ATOM    604  CG2 ILE A  72      19.732  15.304 -28.573  1.00 46.51           C  
ANISOU  604  CG2 ILE A  72     6293   5626   5752    -82    131     53       C  
ATOM    605  CD1 ILE A  72      21.652  12.951 -28.952  1.00 40.73           C  
ANISOU  605  CD1 ILE A  72     5488   4998   4988   -108     33     75       C  
ATOM    606  N   LYS A  73      20.660  17.872 -26.404  1.00 46.87           N  
ANISOU  606  N   LYS A  73     6526   5563   5719   -165    160     -4       N  
ATOM    607  CA  LYS A  73      19.786  18.817 -25.695  1.00 48.95           C  
ANISOU  607  CA  LYS A  73     6861   5758   5980   -156    229    -26       C  
ATOM    608  C   LYS A  73      20.103  20.281 -26.018  1.00 48.06           C  
ANISOU  608  C   LYS A  73     6781   5603   5876   -173    236    -30       C  
ATOM    609  O   LYS A  73      19.195  21.069 -26.275  1.00 47.86           O  
ANISOU  609  O   LYS A  73     6762   5533   5890   -139    293    -30       O  
ATOM    610  CB  LYS A  73      19.825  18.577 -24.184  1.00 49.16           C  
ANISOU  610  CB  LYS A  73     6979   5758   5943   -187    245    -55       C  
ATOM    611  CG  LYS A  73      19.047  17.335 -23.738  1.00 58.31           C  
ANISOU  611  CG  LYS A  73     8120   6936   7101   -158    271    -54       C  
ATOM    612  CD  LYS A  73      19.456  16.893 -22.329  1.00 66.53           C  
ANISOU  612  CD  LYS A  73     9248   7964   8065   -203    260    -78       C  
ATOM    613  CE  LYS A  73      18.729  15.622 -21.888  1.00 69.56           C  
ANISOU  613  CE  LYS A  73     9615   8368   8445   -177    283    -76       C  
ATOM    614  NZ  LYS A  73      17.353  15.911 -21.371  1.00 71.54           N  
ANISOU  614  NZ  LYS A  73     9904   8565   8714   -141    386    -90       N  
ATOM    615  N   ARG A  74      21.386  20.637 -26.024  1.00 48.04           N  
ANISOU  615  N   ARG A  74     6795   5613   5844   -225    176    -31       N  
ATOM    616  CA  ARG A  74      21.783  22.005 -26.366  1.00 49.94           C  
ANISOU  616  CA  ARG A  74     7067   5816   6091   -247    176    -33       C  
ATOM    617  C   ARG A  74      21.421  22.368 -27.804  1.00 49.12           C  
ANISOU  617  C   ARG A  74     6889   5724   6051   -208    183     -6       C  
ATOM    618  O   ARG A  74      21.083  23.514 -28.079  1.00 49.08           O  
ANISOU  618  O   ARG A  74     6910   5671   6068   -200    215     -7       O  
ATOM    619  CB  ARG A  74      23.274  22.234 -26.123  1.00 50.64           C  
ANISOU  619  CB  ARG A  74     7178   5921   6143   -314    104    -32       C  
ATOM    620  CG  ARG A  74      23.652  22.356 -24.660  1.00 53.02           C  
ANISOU  620  CG  ARG A  74     7582   6187   6375   -368     92    -58       C  
ATOM    621  CD  ARG A  74      25.105  22.790 -24.517  1.00 58.44           C  
ANISOU  621  CD  ARG A  74     8286   6881   7036   -440     14    -49       C  
ATOM    622  NE  ARG A  74      25.795  21.997 -23.501  1.00 63.11           N  
ANISOU  622  NE  ARG A  74     8909   7490   7578   -487    -43    -50       N  
ATOM    623  CZ  ARG A  74      26.673  21.030 -23.760  1.00 62.67           C  
ANISOU  623  CZ  ARG A  74     8777   7495   7538   -500   -110    -21       C  
ATOM    624  NH1 ARG A  74      27.002  20.728 -25.016  1.00 57.58           N  
ANISOU  624  NH1 ARG A  74     8026   6900   6953   -470   -122      7       N  
ATOM    625  NH2 ARG A  74      27.236  20.371 -22.754  1.00 64.34           N  
ANISOU  625  NH2 ARG A  74     9024   7715   7705   -544   -163    -19       N  
ATOM    626  N   MET A  75      21.479  21.387 -28.708  1.00 49.08           N  
ANISOU  626  N   MET A  75     6798   5777   6071   -185    153     20       N  
ATOM    627  CA  MET A  75      21.131  21.611 -30.115  1.00 49.28           C  
ANISOU  627  CA  MET A  75     6762   5815   6149   -154    153     48       C  
ATOM    628  C   MET A  75      19.639  21.855 -30.274  1.00 51.58           C  
ANISOU  628  C   MET A  75     7044   6068   6485   -102    210     55       C  
ATOM    629  O   MET A  75      19.214  22.536 -31.208  1.00 51.99           O  
ANISOU  629  O   MET A  75     7072   6102   6581    -81    217     76       O  
ATOM    630  CB  MET A  75      21.578  20.443 -31.004  1.00 47.67           C  
ANISOU  630  CB  MET A  75     6483   5676   5952   -148    111     71       C  
ATOM    631  CG  MET A  75      23.083  20.358 -31.223  1.00 46.15           C  
ANISOU  631  CG  MET A  75     6277   5517   5740   -193     60     77       C  
ATOM    632  SD  MET A  75      23.827  21.818 -32.000  1.00 45.13           S  
ANISOU  632  SD  MET A  75     6160   5363   5625   -223     49     87       S  
ATOM    633  CE  MET A  75      23.629  21.392 -33.731  1.00 35.65           C  
ANISOU  633  CE  MET A  75     4889   4195   4461   -192     44    121       C  
ATOM    634  N   GLU A  76      18.854  21.289 -29.357  1.00 54.03           N  
ANISOU  634  N   GLU A  76     7374   6367   6790    -82    249     41       N  
ATOM    635  CA  GLU A  76      17.410  21.514 -29.323  1.00 56.07           C  
ANISOU  635  CA  GLU A  76     7622   6583   7099    -32    312     50       C  
ATOM    636  C   GLU A  76      17.128  22.942 -28.847  1.00 54.82           C  
ANISOU  636  C   GLU A  76     7530   6349   6950    -31    366     34       C  
ATOM    637  O   GLU A  76      16.324  23.652 -29.453  1.00 55.35           O  
ANISOU  637  O   GLU A  76     7573   6379   7079      4    397     55       O  
ATOM    638  CB  GLU A  76      16.713  20.478 -28.427  1.00 57.18           C  
ANISOU  638  CB  GLU A  76     7765   6730   7230    -13    344     39       C  
ATOM    639  CG  GLU A  76      15.187  20.424 -28.581  1.00 62.05           C  
ANISOU  639  CG  GLU A  76     8342   7317   7918     42    402     61       C  
ATOM    640  CD  GLU A  76      14.484  19.647 -27.464  1.00 66.72           C  
ANISOU  640  CD  GLU A  76     8956   7899   8498     56    454     45       C  
ATOM    641  OE1 GLU A  76      13.264  19.859 -27.283  1.00 68.78           O  
ANISOU  641  OE1 GLU A  76     9201   8116   8817     98    522     58       O  
ATOM    642  OE2 GLU A  76      15.133  18.830 -26.769  1.00 65.85           O  
ANISOU  642  OE2 GLU A  76     8875   7820   8324     26    429     24       O  
ATOM    643  N   ASP A  77      17.816  23.356 -27.781  1.00 53.57           N  
ANISOU  643  N   ASP A  77     7459   6164   6731    -74    373     -2       N  
ATOM    644  CA  ASP A  77      17.711  24.715 -27.240  1.00 53.74           C  
ANISOU  644  CA  ASP A  77     7563   6109   6747    -84    424    -23       C  
ATOM    645  C   ASP A  77      18.176  25.811 -28.218  1.00 52.50           C  
ANISOU  645  C   ASP A  77     7395   5939   6615    -94    397     -7       C  
ATOM    646  O   ASP A  77      17.678  26.941 -28.166  1.00 54.25           O  
ANISOU  646  O   ASP A  77     7657   6093   6865    -78    449    -10       O  
ATOM    647  CB  ASP A  77      18.492  24.837 -25.929  1.00 54.04           C  
ANISOU  647  CB  ASP A  77     7707   6126   6702   -140    420    -63       C  
ATOM    648  CG  ASP A  77      17.966  23.924 -24.837  1.00 57.49           C  
ANISOU  648  CG  ASP A  77     8178   6560   7107   -133    458    -82       C  
ATOM    649  OD1 ASP A  77      16.776  23.536 -24.887  1.00 59.71           O  
ANISOU  649  OD1 ASP A  77     8419   6830   7437    -78    518    -71       O  
ATOM    650  OD2 ASP A  77      18.749  23.603 -23.913  1.00 58.30           O  
ANISOU  650  OD2 ASP A  77     8347   6670   7136   -186    426   -105       O  
ATOM    651  N   ILE A  78      19.139  25.487 -29.080  1.00 49.28           N  
ANISOU  651  N   ILE A  78     6936   5590   6199   -120    322     11       N  
ATOM    652  CA  ILE A  78      19.576  26.415 -30.132  1.00 48.73           C  
ANISOU  652  CA  ILE A  78     6848   5513   6153   -130    296     31       C  
ATOM    653  C   ILE A  78      18.585  26.403 -31.298  1.00 47.59           C  
ANISOU  653  C   ILE A  78     6631   5371   6081    -77    306     69       C  
ATOM    654  O   ILE A  78      18.258  27.450 -31.843  1.00 47.87           O  
ANISOU  654  O   ILE A  78     6671   5362   6154    -63    323     84       O  
ATOM    655  CB  ILE A  78      21.026  26.135 -30.631  1.00 47.58           C  
ANISOU  655  CB  ILE A  78     6678   5424   5974   -181    220     38       C  
ATOM    656  CG1 ILE A  78      22.036  26.327 -29.496  1.00 47.63           C  
ANISOU  656  CG1 ILE A  78     6758   5421   5919   -241    198      8       C  
ATOM    657  CG2 ILE A  78      21.392  27.067 -31.777  1.00 47.64           C  
ANISOU  657  CG2 ILE A  78     6667   5423   6010   -189    201     61       C  
ATOM    658  CD1 ILE A  78      23.382  25.682 -29.744  1.00 45.32           C  
ANISOU  658  CD1 ILE A  78     6427   5191   5603   -286    126     20       C  
ATOM    659  N   GLY A  79      18.100  25.216 -31.658  1.00 47.42           N  
ANISOU  659  N   GLY A  79     6544   5397   6078    -50    292     88       N  
ATOM    660  CA  GLY A  79      17.139  25.064 -32.751  1.00 48.05           C  
ANISOU  660  CA  GLY A  79     6555   5480   6221     -6    289    129       C  
ATOM    661  C   GLY A  79      17.741  24.466 -34.011  1.00 47.54           C  
ANISOU  661  C   GLY A  79     6437   5475   6151    -21    224    156       C  
ATOM    662  O   GLY A  79      17.319  24.790 -35.129  1.00 48.13           O  
ANISOU  662  O   GLY A  79     6479   5544   6266     -6    207    191       O  
ATOM    663  N   LEU A  80      18.720  23.585 -33.826  1.00 44.23           N  
ANISOU  663  N   LEU A  80     6014   5110   5681    -52    190    141       N  
ATOM    664  CA  LEU A  80      19.450  22.988 -34.940  1.00 43.88           C  
ANISOU  664  CA  LEU A  80     5929   5119   5626    -69    139    162       C  
ATOM    665  C   LEU A  80      19.460  21.482 -34.816  1.00 42.73           C  
ANISOU  665  C   LEU A  80     5750   5026   5462    -62    123    161       C  
ATOM    666  O   LEU A  80      19.497  20.949 -33.703  1.00 43.69           O  
ANISOU  666  O   LEU A  80     5888   5153   5559    -64    136    136       O  
ATOM    667  CB  LEU A  80      20.897  23.488 -34.974  1.00 43.92           C  
ANISOU  667  CB  LEU A  80     5958   5135   5595   -117    114    149       C  
ATOM    668  CG  LEU A  80      21.167  24.938 -35.364  1.00 43.65           C  
ANISOU  668  CG  LEU A  80     5955   5056   5572   -134    119    154       C  
ATOM    669  CD1 LEU A  80      22.556  25.331 -34.893  1.00 39.22           C  
ANISOU  669  CD1 LEU A  80     5426   4503   4974   -187     98    135       C  
ATOM    670  CD2 LEU A  80      21.010  25.127 -36.875  1.00 40.02           C  
ANISOU  670  CD2 LEU A  80     5463   4604   5139   -126     99    191       C  
ATOM    671  N   GLU A  81      19.454  20.809 -35.964  1.00 38.69           N  
ANISOU  671  N   GLU A  81     5197   4548   4957    -56     93    187       N  
ATOM    672  CA  GLU A  81      19.425  19.362 -36.019  1.00 37.46           C  
ANISOU  672  CA  GLU A  81     5010   4437   4785    -49     77    190       C  
ATOM    673  C   GLU A  81      20.721  18.729 -35.506  1.00 38.06           C  
ANISOU  673  C   GLU A  81     5091   4552   4819    -78     62    169       C  
ATOM    674  O   GLU A  81      21.829  19.129 -35.903  1.00 38.66           O  
ANISOU  674  O   GLU A  81     5170   4636   4882   -108     46    170       O  
ATOM    675  CB  GLU A  81      19.161  18.906 -37.451  1.00 37.94           C  
ANISOU  675  CB  GLU A  81     5042   4517   4857    -43     50    224       C  
ATOM    676  CG  GLU A  81      18.989  17.394 -37.602  1.00 37.50           C  
ANISOU  676  CG  GLU A  81     4961   4502   4786    -34     36    228       C  
ATOM    677  CD  GLU A  81      18.711  16.981 -39.030  1.00 36.80           C  
ANISOU  677  CD  GLU A  81     4860   4423   4699    -34      8    261       C  
ATOM    678  OE1 GLU A  81      18.661  17.860 -39.915  1.00 38.47           O  
ANISOU  678  OE1 GLU A  81     5083   4611   4924    -43     -3    281       O  
ATOM    679  OE2 GLU A  81      18.531  15.775 -39.265  1.00 38.33           O  
ANISOU  679  OE2 GLU A  81     5040   4644   4879    -30     -5    266       O  
ATOM    680  N   ALA A  82      20.565  17.750 -34.614  1.00 35.83           N  
ANISOU  680  N   ALA A  82     4804   4288   4520    -70     66    154       N  
ATOM    681  CA  ALA A  82      21.669  16.925 -34.133  1.00 33.85           C  
ANISOU  681  CA  ALA A  82     4549   4075   4237    -93     45    143       C  
ATOM    682  C   ALA A  82      21.584  15.593 -34.855  1.00 33.67           C  
ANISOU  682  C   ALA A  82     4488   4092   4214    -77     31    158       C  
ATOM    683  O   ALA A  82      20.703  14.780 -34.571  1.00 36.18           O  
ANISOU  683  O   ALA A  82     4797   4415   4535    -54     39    159       O  
ATOM    684  CB  ALA A  82      21.574  16.730 -32.622  1.00 31.78           C  
ANISOU  684  CB  ALA A  82     4320   3804   3953   -100     55    117       C  
ATOM    685  N   LEU A  83      22.485  15.380 -35.806  1.00 32.64           N  
ANISOU  685  N   LEU A  83     4338   3983   4079    -91     16    172       N  
ATOM    686  CA  LEU A  83      22.421  14.200 -36.655  1.00 33.45           C  
ANISOU  686  CA  LEU A  83     4417   4114   4177    -78     10    187       C  
ATOM    687  C   LEU A  83      23.242  13.039 -36.092  1.00 33.35           C  
ANISOU  687  C   LEU A  83     4388   4135   4150    -82      2    179       C  
ATOM    688  O   LEU A  83      24.154  13.242 -35.283  1.00 33.99           O  
ANISOU  688  O   LEU A  83     4469   4221   4226   -103     -7    169       O  
ATOM    689  CB  LEU A  83      22.882  14.534 -38.074  1.00 32.77           C  
ANISOU  689  CB  LEU A  83     4330   4028   4094    -89      9    207       C  
ATOM    690  CG  LEU A  83      22.116  15.584 -38.880  1.00 33.87           C  
ANISOU  690  CG  LEU A  83     4486   4134   4249    -86      8    223       C  
ATOM    691  CD1 LEU A  83      22.679  16.977 -38.611  1.00 32.39           C  
ANISOU  691  CD1 LEU A  83     4315   3923   4071   -107     14    216       C  
ATOM    692  CD2 LEU A  83      22.196  15.274 -40.370  1.00 33.00           C  
ANISOU  692  CD2 LEU A  83     4381   4028   4128    -92      3    246       C  
ATOM    693  N   GLY A  84      22.911  11.825 -36.526  1.00 32.90           N  
ANISOU  693  N   GLY A  84     4317   4098   4085    -65      1    187       N  
ATOM    694  CA  GLY A  84      23.680  10.647 -36.163  1.00 31.47           C  
ANISOU  694  CA  GLY A  84     4117   3945   3894    -64     -4    184       C  
ATOM    695  C   GLY A  84      22.921   9.737 -35.227  1.00 33.09           C  
ANISOU  695  C   GLY A  84     4325   4159   4090    -48     -8    174       C  
ATOM    696  O   GLY A  84      21.856  10.098 -34.705  1.00 32.46           O  
ANISOU  696  O   GLY A  84     4260   4061   4013    -38     -2    167       O  
ATOM    697  N   MET A  85      23.472   8.546 -35.023  1.00 32.50           N  
ANISOU  697  N   MET A  85     4234   4108   4007    -44    -14    175       N  
ATOM    698  CA  MET A  85      22.840   7.536 -34.192  1.00 32.23           C  
ANISOU  698  CA  MET A  85     4203   4083   3961    -30    -18    168       C  
ATOM    699  C   MET A  85      22.895   7.957 -32.738  1.00 31.83           C  
ANISOU  699  C   MET A  85     4170   4024   3900    -43    -26    151       C  
ATOM    700  O   MET A  85      23.951   7.914 -32.112  1.00 33.23           O  
ANISOU  700  O   MET A  85     4342   4209   4073    -62    -45    151       O  
ATOM    701  CB  MET A  85      23.509   6.176 -34.401  1.00 31.02           C  
ANISOU  701  CB  MET A  85     4031   3953   3803    -22    -21    176       C  
ATOM    702  CG  MET A  85      22.971   5.059 -33.509  1.00 32.44           C  
ANISOU  702  CG  MET A  85     4215   4143   3969    -10    -29    169       C  
ATOM    703  SD  MET A  85      21.177   4.915 -33.488  1.00 31.93           S  
ANISOU  703  SD  MET A  85     4167   4065   3900      7    -19    166       S  
ATOM    704  CE  MET A  85      20.896   4.183 -35.107  1.00 30.37           C  
ANISOU  704  CE  MET A  85     3967   3871   3702     17    -17    185       C  
ATOM    705  N   ASP A  86      21.745   8.361 -32.210  1.00 32.89           N  
ANISOU  705  N   ASP A  86     4327   4137   4033    -34    -11    141       N  
ATOM    706  CA  ASP A  86      21.642   8.773 -30.813  1.00 35.02           C  
ANISOU  706  CA  ASP A  86     4631   4391   4286    -48     -8    122       C  
ATOM    707  C   ASP A  86      21.483   7.593 -29.844  1.00 34.95           C  
ANISOU  707  C   ASP A  86     4631   4395   4255    -45    -14    116       C  
ATOM    708  O   ASP A  86      21.520   7.791 -28.631  1.00 34.85           O  
ANISOU  708  O   ASP A  86     4656   4368   4218    -62    -15    101       O  
ATOM    709  CB  ASP A  86      20.499   9.775 -30.633  1.00 37.78           C  
ANISOU  709  CB  ASP A  86     5005   4704   4647    -38     25    114       C  
ATOM    710  CG  ASP A  86      19.153   9.217 -31.082  1.00 44.31           C  
ANISOU  710  CG  ASP A  86     5812   5529   5496     -7     44    126       C  
ATOM    711  OD1 ASP A  86      18.233   9.185 -30.241  1.00 47.87           O  
ANISOU  711  OD1 ASP A  86     6280   5960   5948      4     73    117       O  
ATOM    712  OD2 ASP A  86      19.017   8.808 -32.264  1.00 43.82           O  
ANISOU  712  OD2 ASP A  86     5721   5481   5448      4     32    146       O  
ATOM    713  N   ASP A  87      21.290   6.379 -30.371  1.00 34.92           N  
ANISOU  713  N   ASP A  87     4600   4414   4254    -26    -18    128       N  
ATOM    714  CA  ASP A  87      21.314   5.170 -29.527  1.00 35.93           C  
ANISOU  714  CA  ASP A  87     4733   4556   4362    -24    -29    125       C  
ATOM    715  C   ASP A  87      22.744   4.613 -29.553  1.00 35.43           C  
ANISOU  715  C   ASP A  87     4649   4515   4299    -37    -62    136       C  
ATOM    716  O   ASP A  87      23.136   3.868 -30.462  1.00 35.06           O  
ANISOU  716  O   ASP A  87     4570   4485   4265    -23    -63    150       O  
ATOM    717  CB  ASP A  87      20.260   4.133 -29.958  1.00 37.37           C  
ANISOU  717  CB  ASP A  87     4902   4746   4549      2    -16    133       C  
ATOM    718  CG  ASP A  87      20.163   2.924 -28.992  1.00 41.92           C  
ANISOU  718  CG  ASP A  87     5490   5334   5104      3    -23    129       C  
ATOM    719  OD1 ASP A  87      21.064   2.710 -28.154  1.00 41.04           O  
ANISOU  719  OD1 ASP A  87     5391   5228   4973    -15    -46    125       O  
ATOM    720  OD2 ASP A  87      19.167   2.176 -29.074  1.00 45.41           O  
ANISOU  720  OD2 ASP A  87     5929   5777   5548     19    -10    133       O  
ATOM    721  N   PHE A  88      23.515   5.006 -28.543  1.00 34.08           N  
ANISOU  721  N   PHE A  88     4497   4338   4113    -66    -86    131       N  
ATOM    722  CA  PHE A  88      24.962   4.857 -28.551  1.00 35.20           C  
ANISOU  722  CA  PHE A  88     4611   4494   4270    -84   -122    149       C  
ATOM    723  C   PHE A  88      25.439   3.415 -28.587  1.00 35.91           C  
ANISOU  723  C   PHE A  88     4670   4606   4368    -69   -137    165       C  
ATOM    724  O   PHE A  88      26.545   3.142 -29.044  1.00 38.16           O  
ANISOU  724  O   PHE A  88     4913   4902   4683    -70   -151    186       O  
ATOM    725  CB  PHE A  88      25.595   5.617 -27.378  1.00 34.70           C  
ANISOU  725  CB  PHE A  88     4582   4415   4186   -126   -156    144       C  
ATOM    726  CG  PHE A  88      25.354   7.106 -27.425  1.00 36.63           C  
ANISOU  726  CG  PHE A  88     4858   4634   4426   -143   -141    129       C  
ATOM    727  CD1 PHE A  88      25.501   7.807 -28.621  1.00 32.04           C  
ANISOU  727  CD1 PHE A  88     4246   4053   3875   -134   -122    136       C  
ATOM    728  CD2 PHE A  88      24.979   7.803 -26.280  1.00 34.63           C  
ANISOU  728  CD2 PHE A  88     4671   4351   4136   -170   -141    109       C  
ATOM    729  CE1 PHE A  88      25.276   9.165 -28.682  1.00 34.92           C  
ANISOU  729  CE1 PHE A  88     4640   4391   4237   -148   -109    124       C  
ATOM    730  CE2 PHE A  88      24.756   9.179 -26.329  1.00 40.39           C  
ANISOU  730  CE2 PHE A  88     5434   5051   4863   -183   -122     95       C  
ATOM    731  CZ  PHE A  88      24.903   9.861 -27.539  1.00 34.97           C  
ANISOU  731  CZ  PHE A  88     4710   4367   4211   -172   -107    103       C  
ATOM    732  N   LYS A  89      24.612   2.490 -28.125  1.00 34.11           N  
ANISOU  732  N   LYS A  89     4460   4381   4119    -54   -130    158       N  
ATOM    733  CA  LYS A  89      25.003   1.098 -28.213  1.00 36.92           C  
ANISOU  733  CA  LYS A  89     4791   4754   4484    -37   -140    174       C  
ATOM    734  C   LYS A  89      24.836   0.498 -29.620  1.00 35.88           C  
ANISOU  734  C   LYS A  89     4630   4630   4372     -7   -110    182       C  
ATOM    735  O   LYS A  89      25.534  -0.448 -29.968  1.00 37.56           O  
ANISOU  735  O   LYS A  89     4815   4852   4603      7   -112    198       O  
ATOM    736  CB  LYS A  89      24.375   0.247 -27.104  1.00 36.99           C  
ANISOU  736  CB  LYS A  89     4832   4760   4460    -38   -150    167       C  
ATOM    737  CG  LYS A  89      22.888   0.219 -27.047  1.00 37.76           C  
ANISOU  737  CG  LYS A  89     4960   4850   4538    -25   -115    149       C  
ATOM    738  CD  LYS A  89      22.459  -0.072 -25.608  1.00 37.15           C  
ANISOU  738  CD  LYS A  89     4930   4761   4423    -41   -123    138       C  
ATOM    739  CE  LYS A  89      20.950  -0.251 -25.511  1.00 36.29           C  
ANISOU  739  CE  LYS A  89     4842   4642   4303    -25    -81    125       C  
ATOM    740  NZ  LYS A  89      20.238   0.984 -25.876  1.00 28.14           N  
ANISOU  740  NZ  LYS A  89     3816   3591   3284    -22    -47    114       N  
ATOM    741  N   LEU A  90      23.944   1.067 -30.428  1.00 35.18           N  
ANISOU  741  N   LEU A  90     4552   4534   4281      2    -82    172       N  
ATOM    742  CA  LEU A  90      23.862   0.700 -31.844  1.00 35.71           C  
ANISOU  742  CA  LEU A  90     4605   4603   4360     21    -59    180       C  
ATOM    743  C   LEU A  90      25.076   1.220 -32.618  1.00 34.70           C  
ANISOU  743  C   LEU A  90     4450   4475   4258     15    -52    193       C  
ATOM    744  O   LEU A  90      25.567   0.551 -33.526  1.00 36.91           O  
ANISOU  744  O   LEU A  90     4716   4757   4551     29    -32    204       O  
ATOM    745  CB  LEU A  90      22.559   1.197 -32.495  1.00 36.91           C  
ANISOU  745  CB  LEU A  90     4776   4744   4505     26    -42    173       C  
ATOM    746  CG  LEU A  90      21.190   0.692 -32.008  1.00 36.79           C  
ANISOU  746  CG  LEU A  90     4779   4725   4476     34    -39    167       C  
ATOM    747  CD1 LEU A  90      20.109   1.164 -32.964  1.00 32.25           C  
ANISOU  747  CD1 LEU A  90     4207   4137   3908     39    -28    173       C  
ATOM    748  CD2 LEU A  90      21.125  -0.833 -31.837  1.00 36.32           C  
ANISOU  748  CD2 LEU A  90     4720   4676   4404     46    -44    172       C  
ATOM    749  N   ALA A  91      25.564   2.404 -32.253  1.00 34.20           N  
ANISOU  749  N   ALA A  91     4383   4407   4204     -7    -65    191       N  
ATOM    750  CA  ALA A  91      26.786   2.955 -32.860  1.00 33.53           C  
ANISOU  750  CA  ALA A  91     4267   4322   4150    -17    -60    206       C  
ATOM    751  C   ALA A  91      28.016   2.152 -32.440  1.00 32.71           C  
ANISOU  751  C   ALA A  91     4124   4228   4075    -17    -76    227       C  
ATOM    752  O   ALA A  91      28.897   1.878 -33.257  1.00 31.77           O  
ANISOU  752  O   ALA A  91     3971   4109   3989     -7    -52    246       O  
ATOM    753  CB  ALA A  91      26.960   4.438 -32.509  1.00 31.35           C  
ANISOU  753  CB  ALA A  91     4000   4036   3876    -46    -74    200       C  
ATOM    754  N   TYR A  92      28.064   1.778 -31.163  1.00 33.07           N  
ANISOU  754  N   TYR A  92     4175   4278   4111    -28   -114    228       N  
ATOM    755  CA  TYR A  92      29.113   0.905 -30.648  1.00 33.60           C  
ANISOU  755  CA  TYR A  92     4205   4353   4210    -27   -139    254       C  
ATOM    756  C   TYR A  92      29.187  -0.413 -31.421  1.00 33.76           C  
ANISOU  756  C   TYR A  92     4206   4375   4245     10   -105    263       C  
ATOM    757  O   TYR A  92      30.280  -0.865 -31.767  1.00 34.99           O  
ANISOU  757  O   TYR A  92     4315   4531   4449     20    -95    290       O  
ATOM    758  CB  TYR A  92      28.917   0.604 -29.154  1.00 34.44           C  
ANISOU  758  CB  TYR A  92     4338   4461   4289    -46   -188    251       C  
ATOM    759  CG  TYR A  92      29.899  -0.436 -28.640  1.00 36.96           C  
ANISOU  759  CG  TYR A  92     4617   4785   4642    -43   -220    283       C  
ATOM    760  CD1 TYR A  92      29.525  -1.781 -28.487  1.00 38.12           C  
ANISOU  760  CD1 TYR A  92     4770   4936   4780    -17   -214    285       C  
ATOM    761  CD2 TYR A  92      31.216  -0.082 -28.347  1.00 36.33           C  
ANISOU  761  CD2 TYR A  92     4492   4705   4609    -67   -259    316       C  
ATOM    762  CE1 TYR A  92      30.453  -2.735 -28.027  1.00 39.95           C  
ANISOU  762  CE1 TYR A  92     4962   5168   5049    -11   -244    318       C  
ATOM    763  CE2 TYR A  92      32.130  -1.014 -27.893  1.00 39.21           C  
ANISOU  763  CE2 TYR A  92     4811   5070   5016    -63   -292    353       C  
ATOM    764  CZ  TYR A  92      31.755  -2.330 -27.739  1.00 40.02           C  
ANISOU  764  CZ  TYR A  92     4921   5176   5110    -33   -284    354       C  
ATOM    765  OH  TYR A  92      32.702  -3.219 -27.289  1.00 43.82           O  
ANISOU  765  OH  TYR A  92     5355   5655   5641    -28   -318    395       O  
ATOM    766  N   LEU A  93      28.032  -1.028 -31.670  1.00 31.70           N  
ANISOU  766  N   LEU A  93     3982   4114   3947     28    -85    244       N  
ATOM    767  CA  LEU A  93      27.984  -2.335 -32.325  1.00 31.54           C  
ANISOU  767  CA  LEU A  93     3960   4091   3931     59    -54    250       C  
ATOM    768  C   LEU A  93      28.409  -2.231 -33.779  1.00 32.67           C  
ANISOU  768  C   LEU A  93     4095   4225   4094     72     -4    256       C  
ATOM    769  O   LEU A  93      29.083  -3.123 -34.306  1.00 34.76           O  
ANISOU  769  O   LEU A  93     4342   4481   4385     94     28    271       O  
ATOM    770  CB  LEU A  93      26.590  -2.962 -32.219  1.00 30.75           C  
ANISOU  770  CB  LEU A  93     3905   3991   3786     67    -52    230       C  
ATOM    771  CG  LEU A  93      26.208  -3.679 -30.921  1.00 32.64           C  
ANISOU  771  CG  LEU A  93     4157   4237   4007     64    -85    228       C  
ATOM    772  CD1 LEU A  93      24.843  -4.351 -31.079  1.00 29.66           C  
ANISOU  772  CD1 LEU A  93     3817   3857   3594     75    -72    213       C  
ATOM    773  CD2 LEU A  93      27.256  -4.713 -30.520  1.00 32.07           C  
ANISOU  773  CD2 LEU A  93     4054   4166   3966     76    -99    253       C  
ATOM    774  N   SER A  94      28.035  -1.120 -34.407  1.00 32.11           N  
ANISOU  774  N   SER A  94     4041   4150   4009     58      8    244       N  
ATOM    775  CA  SER A  94      28.382  -0.848 -35.794  1.00 33.92           C  
ANISOU  775  CA  SER A  94     4274   4366   4247     63     55    249       C  
ATOM    776  C   SER A  94      29.883  -0.624 -35.964  1.00 35.74           C  
ANISOU  776  C   SER A  94     4452   4593   4533     63     73    273       C  
ATOM    777  O   SER A  94      30.451  -1.006 -36.987  1.00 35.62           O  
ANISOU  777  O   SER A  94     4434   4564   4537     79    127    283       O  
ATOM    778  CB  SER A  94      27.621   0.381 -36.288  1.00 35.72           C  
ANISOU  778  CB  SER A  94     4532   4589   4449     45     52    235       C  
ATOM    779  OG  SER A  94      27.736   0.519 -37.696  1.00 39.29           O  
ANISOU  779  OG  SER A  94     5006   5027   4896     47     96    238       O  
ATOM    780  N   ASP A  95      30.508   0.001 -34.960  1.00 35.50           N  
ANISOU  780  N   ASP A  95     4383   4573   4530     43     30    285       N  
ATOM    781  CA  ASP A  95      31.941   0.279 -34.962  1.00 34.83           C  
ANISOU  781  CA  ASP A  95     4238   4487   4510     36     35    316       C  
ATOM    782  C   ASP A  95      32.744  -0.986 -34.662  1.00 36.65           C  
ANISOU  782  C   ASP A  95     4424   4714   4787     61     41    343       C  
ATOM    783  O   ASP A  95      33.804  -1.221 -35.241  1.00 37.16           O  
ANISOU  783  O   ASP A  95     4441   4768   4910     75     82    370       O  
ATOM    784  CB  ASP A  95      32.276   1.353 -33.921  1.00 32.70           C  
ANISOU  784  CB  ASP A  95     3950   4224   4249     -1    -26    321       C  
ATOM    785  CG  ASP A  95      32.003   2.763 -34.418  1.00 34.26           C  
ANISOU  785  CG  ASP A  95     4171   4417   4429    -25    -19    307       C  
ATOM    786  OD1 ASP A  95      31.599   3.623 -33.599  1.00 31.52           O  
ANISOU  786  OD1 ASP A  95     3848   4072   4057    -53    -62    293       O  
ATOM    787  OD2 ASP A  95      32.198   3.010 -35.625  1.00 28.39           O  
ANISOU  787  OD2 ASP A  95     3428   3664   3695    -16     33    309       O  
ATOM    788  N   THR A  96      32.222  -1.801 -33.756  1.00 35.46           N  
ANISOU  788  N   THR A  96     4289   4572   4613     67      3    337       N  
ATOM    789  CA  THR A  96      32.935  -2.978 -33.285  1.00 34.71           C  
ANISOU  789  CA  THR A  96     4153   4473   4562     88     -4    366       C  
ATOM    790  C   THR A  96      32.821  -4.137 -34.274  1.00 33.35           C  
ANISOU  790  C   THR A  96     3997   4284   4391    129     65    363       C  
ATOM    791  O   THR A  96      33.755  -4.910 -34.435  1.00 36.34           O  
ANISOU  791  O   THR A  96     4330   4649   4830    154     94    392       O  
ATOM    792  CB  THR A  96      32.449  -3.359 -31.875  1.00 33.72           C  
ANISOU  792  CB  THR A  96     4046   4360   4408     74    -73    362       C  
ATOM    793  OG1 THR A  96      32.442  -2.175 -31.061  1.00 31.76           O  
ANISOU  793  OG1 THR A  96     3804   4120   4144     32   -128    358       O  
ATOM    794  CG2 THR A  96      33.347  -4.425 -31.241  1.00 30.79           C  
ANISOU  794  CG2 THR A  96     3624   3984   4091     89    -97    401       C  
ATOM    795  N   TYR A  97      31.687  -4.237 -34.953  1.00 33.21           N  
ANISOU  795  N   TYR A  97     4045   4262   4309    133     92    329       N  
ATOM    796  CA  TYR A  97      31.473  -5.306 -35.928  1.00 34.26           C  
ANISOU  796  CA  TYR A  97     4213   4374   4429    164    154    323       C  
ATOM    797  C   TYR A  97      31.196  -4.693 -37.304  1.00 36.63           C  
ANISOU  797  C   TYR A  97     4557   4661   4701    158    208    307       C  
ATOM    798  O   TYR A  97      30.069  -4.698 -37.793  1.00 36.44           O  
ANISOU  798  O   TYR A  97     4596   4633   4616    150    207    282       O  
ATOM    799  CB  TYR A  97      30.365  -6.259 -35.449  1.00 32.11           C  
ANISOU  799  CB  TYR A  97     3988   4106   4106    170    129    304       C  
ATOM    800  CG  TYR A  97      30.658  -6.788 -34.062  1.00 33.15           C  
ANISOU  800  CG  TYR A  97     4084   4250   4261    171     73    322       C  
ATOM    801  CD1 TYR A  97      30.220  -6.107 -32.933  1.00 29.87           C  
ANISOU  801  CD1 TYR A  97     3671   3856   3824    142      8    314       C  
ATOM    802  CD2 TYR A  97      31.428  -7.939 -33.877  1.00 33.50           C  
ANISOU  802  CD2 TYR A  97     4097   4281   4352    199     88    347       C  
ATOM    803  CE1 TYR A  97      30.521  -6.562 -31.650  1.00 32.82           C  
ANISOU  803  CE1 TYR A  97     4022   4237   4210    136    -47    332       C  
ATOM    804  CE2 TYR A  97      31.732  -8.403 -32.601  1.00 33.86           C  
ANISOU  804  CE2 TYR A  97     4111   4335   4418    196     29    368       C  
ATOM    805  CZ  TYR A  97      31.273  -7.704 -31.490  1.00 34.31           C  
ANISOU  805  CZ  TYR A  97     4177   4414   4444    162    -41    360       C  
ATOM    806  OH  TYR A  97      31.554  -8.150 -30.218  1.00 33.70           O  
ANISOU  806  OH  TYR A  97     4083   4343   4379    152   -102    381       O  
ATOM    807  N   ASN A  98      32.249  -4.147 -37.907  1.00 39.00           N  
ANISOU  807  N   ASN A  98     4821   4950   5050    159    250    325       N  
ATOM    808  CA  ASN A  98      32.139  -3.441 -39.182  1.00 44.62           C  
ANISOU  808  CA  ASN A  98     5572   5645   5736    148    301    314       C  
ATOM    809  C   ASN A  98      32.199  -4.420 -40.353  1.00 46.10           C  
ANISOU  809  C   ASN A  98     5811   5797   5906    172    381    310       C  
ATOM    810  O   ASN A  98      32.909  -4.207 -41.339  1.00 48.76           O  
ANISOU  810  O   ASN A  98     6153   6110   6263    176    453    319       O  
ATOM    811  CB  ASN A  98      33.214  -2.350 -39.296  1.00 45.88           C  
ANISOU  811  CB  ASN A  98     5675   5806   5952    134    313    336       C  
ATOM    812  CG  ASN A  98      32.834  -1.252 -40.277  1.00 53.11           C  
ANISOU  812  CG  ASN A  98     6636   6715   6829    110    334    321       C  
ATOM    813  OD1 ASN A  98      31.737  -1.262 -40.849  1.00 57.38           O  
ANISOU  813  OD1 ASN A  98     7250   7250   7301    103    332    296       O  
ATOM    814  ND2 ASN A  98      33.742  -0.295 -40.480  1.00 52.44           N  
ANISOU  814  ND2 ASN A  98     6507   6628   6789     96    350    339       N  
ATOM    815  N   TYR A  99      31.428  -5.494 -40.218  1.00 44.86           N  
ANISOU  815  N   TYR A  99     5699   5636   5710    184    372    296       N  
ATOM    816  CA  TYR A  99      31.381  -6.589 -41.172  1.00 44.88           C  
ANISOU  816  CA  TYR A  99     5763   5601   5688    204    440    290       C  
ATOM    817  C   TYR A  99      30.080  -7.360 -40.952  1.00 44.70           C  
ANISOU  817  C   TYR A  99     5801   5582   5599    198    398    269       C  
ATOM    818  O   TYR A  99      29.428  -7.205 -39.911  1.00 41.18           O  
ANISOU  818  O   TYR A  99     5333   5167   5145    188    325    265       O  
ATOM    819  CB  TYR A  99      32.594  -7.524 -40.999  1.00 45.65           C  
ANISOU  819  CB  TYR A  99     5808   5678   5859    243    495    316       C  
ATOM    820  CG  TYR A  99      32.839  -8.011 -39.575  1.00 46.53           C  
ANISOU  820  CG  TYR A  99     5848   5813   6017    256    433    335       C  
ATOM    821  CD1 TYR A  99      33.673  -7.302 -38.709  1.00 48.02           C  
ANISOU  821  CD1 TYR A  99     5946   6025   6274    249    391    362       C  
ATOM    822  CD2 TYR A  99      32.251  -9.187 -39.100  1.00 45.96           C  
ANISOU  822  CD2 TYR A  99     5804   5737   5920    271    412    327       C  
ATOM    823  CE1 TYR A  99      33.908  -7.740 -37.407  1.00 46.03           C  
ANISOU  823  CE1 TYR A  99     5639   5791   6059    255    327    382       C  
ATOM    824  CE2 TYR A  99      32.482  -9.638 -37.799  1.00 45.43           C  
ANISOU  824  CE2 TYR A  99     5680   5690   5891    280    354    346       C  
ATOM    825  CZ  TYR A  99      33.310  -8.905 -36.960  1.00 46.76           C  
ANISOU  825  CZ  TYR A  99     5764   5880   6123    271    310    374       C  
ATOM    826  OH  TYR A  99      33.548  -9.335 -35.675  1.00 45.05           O  
ANISOU  826  OH  TYR A  99     5499   5679   5938    273    245    396       O  
ATOM    827  N   GLU A 100      29.705  -8.171 -41.937  1.00 43.86           N  
ANISOU  827  N   GLU A 100     5778   5442   5447    201    446    257       N  
ATOM    828  CA  GLU A 100      28.557  -9.056 -41.823  1.00 45.12           C  
ANISOU  828  CA  GLU A 100     5996   5598   5549    194    411    242       C  
ATOM    829  C   GLU A 100      28.835 -10.046 -40.699  1.00 43.98           C  
ANISOU  829  C   GLU A 100     5804   5464   5444    222    392    252       C  
ATOM    830  O   GLU A 100      29.873 -10.715 -40.701  1.00 46.37           O  
ANISOU  830  O   GLU A 100     6077   5744   5797    255    445    268       O  
ATOM    831  CB  GLU A 100      28.351  -9.793 -43.147  1.00 47.54           C  
ANISOU  831  CB  GLU A 100     6405   5856   5801    190    473    230       C  
ATOM    832  CG  GLU A 100      27.090 -10.635 -43.247  1.00 53.32           C  
ANISOU  832  CG  GLU A 100     7212   6579   6467    172    434    216       C  
ATOM    833  CD  GLU A 100      27.125 -11.582 -44.445  1.00 61.31           C  
ANISOU  833  CD  GLU A 100     8330   7535   7429    170    502    207       C  
ATOM    834  OE1 GLU A 100      27.018 -12.812 -44.231  1.00 63.59           O  
ANISOU  834  OE1 GLU A 100     8646   7804   7710    186    514    204       O  
ATOM    835  OE2 GLU A 100      27.279 -11.102 -45.596  1.00 61.96           O  
ANISOU  835  OE2 GLU A 100     8475   7588   7477    150    546    203       O  
ATOM    836  N   ILE A 101      27.922 -10.128 -39.737  1.00 40.94           N  
ANISOU  836  N   ILE A 101     5409   5107   5038    210    318    246       N  
ATOM    837  CA  ILE A 101      28.118 -10.988 -38.573  1.00 40.86           C  
ANISOU  837  CA  ILE A 101     5357   5108   5059    231    290    256       C  
ATOM    838  C   ILE A 101      27.871 -12.449 -38.896  1.00 42.58           C  
ANISOU  838  C   ILE A 101     5631   5295   5253    248    321    252       C  
ATOM    839  O   ILE A 101      26.786 -12.824 -39.353  1.00 43.26           O  
ANISOU  839  O   ILE A 101     5789   5372   5278    228    308    235       O  
ATOM    840  CB  ILE A 101      27.223 -10.576 -37.384  1.00 39.93           C  
ANISOU  840  CB  ILE A 101     5218   5029   4925    211    209    250       C  
ATOM    841  CG1 ILE A 101      27.667  -9.212 -36.848  1.00 41.85           C  
ANISOU  841  CG1 ILE A 101     5404   5299   5200    197    180    257       C  
ATOM    842  CG2 ILE A 101      27.269 -11.643 -36.289  1.00 39.12           C  
ANISOU  842  CG2 ILE A 101     5095   4931   4837    227    182    260       C  
ATOM    843  CD1 ILE A 101      26.728  -8.588 -35.887  1.00 39.77           C  
ANISOU  843  CD1 ILE A 101     5136   5064   4912    174    116    246       C  
ATOM    844  N   LYS A 102      28.889 -13.268 -38.659  1.00 44.03           N  
ANISOU  844  N   LYS A 102     5780   5459   5490    284    360    270       N  
ATOM    845  CA  LYS A 102      28.714 -14.707 -38.656  1.00 46.43           C  
ANISOU  845  CA  LYS A 102     6127   5734   5781    304    381    269       C  
ATOM    846  C   LYS A 102      28.704 -15.171 -37.208  1.00 45.23           C  
ANISOU  846  C   LYS A 102     5920   5607   5658    313    319    284       C  
ATOM    847  O   LYS A 102      29.686 -14.998 -36.483  1.00 46.41           O  
ANISOU  847  O   LYS A 102     5990   5767   5875    331    308    311       O  
ATOM    848  CB  LYS A 102      29.825 -15.396 -39.453  1.00 49.86           C  
ANISOU  848  CB  LYS A 102     6569   6119   6257    341    478    281       C  
ATOM    849  CG  LYS A 102      29.296 -16.365 -40.502  1.00 57.42           C  
ANISOU  849  CG  LYS A 102     7638   7028   7151    339    532    261       C  
ATOM    850  CD  LYS A 102      28.575 -15.600 -41.625  1.00 61.95           C  
ANISOU  850  CD  LYS A 102     8290   7595   7652    298    538    238       C  
ATOM    851  CE  LYS A 102      27.611 -16.493 -42.406  1.00 66.17           C  
ANISOU  851  CE  LYS A 102     8945   8092   8103    276    547    217       C  
ATOM    852  NZ  LYS A 102      26.996 -15.758 -43.558  1.00 67.82           N  
ANISOU  852  NZ  LYS A 102     9234   8290   8244    233    549    202       N  
ATOM    853  N   TYR A 103      27.578 -15.723 -36.775  1.00 44.55           N  
ANISOU  853  N   TYR A 103     5876   5531   5520    296    273    270       N  
ATOM    854  CA  TYR A 103      27.435 -16.166 -35.391  1.00 42.88           C  
ANISOU  854  CA  TYR A 103     5627   5341   5323    299    214    282       C  
ATOM    855  C   TYR A 103      27.385 -17.684 -35.332  1.00 42.78           C  
ANISOU  855  C   TYR A 103     5651   5298   5307    322    234    286       C  
ATOM    856  O   TYR A 103      27.012 -18.345 -36.307  1.00 44.56           O  
ANISOU  856  O   TYR A 103     5949   5489   5494    323    279    272       O  
ATOM    857  CB  TYR A 103      26.219 -15.512 -34.709  1.00 40.05           C  
ANISOU  857  CB  TYR A 103     5278   5020   4919    263    147    266       C  
ATOM    858  CG  TYR A 103      24.858 -16.030 -35.152  1.00 40.62           C  
ANISOU  858  CG  TYR A 103     5423   5084   4927    241    138    246       C  
ATOM    859  CD1 TYR A 103      24.174 -15.453 -36.230  1.00 38.26           C  
ANISOU  859  CD1 TYR A 103     5169   4779   4588    217    150    231       C  
ATOM    860  CD2 TYR A 103      24.245 -17.079 -34.476  1.00 39.13           C  
ANISOU  860  CD2 TYR A 103     5255   4892   4718    241    113    247       C  
ATOM    861  CE1 TYR A 103      22.910 -15.920 -36.620  1.00 34.18           C  
ANISOU  861  CE1 TYR A 103     4715   4254   4019    192    131    221       C  
ATOM    862  CE2 TYR A 103      22.999 -17.557 -34.864  1.00 38.04           C  
ANISOU  862  CE2 TYR A 103     5179   4747   4528    217    100    234       C  
ATOM    863  CZ  TYR A 103      22.337 -16.978 -35.928  1.00 38.02           C  
ANISOU  863  CZ  TYR A 103     5217   4739   4492    192    107    222       C  
ATOM    864  OH  TYR A 103      21.104 -17.479 -36.283  1.00 36.58           O  
ANISOU  864  OH  TYR A 103     5089   4546   4263    164     84    217       O  
ATOM    865  N   ASP A 104      27.805 -18.232 -34.198  1.00 40.54           N  
ANISOU  865  N   ASP A 104     5321   5020   5060    337    200    308       N  
ATOM    866  CA  ASP A 104      27.774 -19.667 -33.977  1.00 39.68           C  
ANISOU  866  CA  ASP A 104     5242   4883   4952    359    211    316       C  
ATOM    867  C   ASP A 104      26.814 -19.927 -32.829  1.00 38.55           C  
ANISOU  867  C   ASP A 104     5109   4768   4771    335    138    312       C  
ATOM    868  O   ASP A 104      27.156 -19.660 -31.674  1.00 39.86           O  
ANISOU  868  O   ASP A 104     5222   4957   4964    331     87    330       O  
ATOM    869  CB  ASP A 104      29.175 -20.166 -33.640  1.00 40.13           C  
ANISOU  869  CB  ASP A 104     5235   4918   5095    401    235    353       C  
ATOM    870  CG  ASP A 104      29.224 -21.660 -33.377  1.00 45.71           C  
ANISOU  870  CG  ASP A 104     5968   5590   5811    429    248    365       C  
ATOM    871  OD1 ASP A 104      28.165 -22.330 -33.386  1.00 44.96           O  
ANISOU  871  OD1 ASP A 104     5943   5490   5651    412    235    344       O  
ATOM    872  OD2 ASP A 104      30.343 -22.170 -33.161  1.00 49.89           O  
ANISOU  872  OD2 ASP A 104     6444   6094   6418    468    272    400       O  
ATOM    873  N   HIS A 105      25.619 -20.436 -33.136  1.00 36.68           N  
ANISOU  873  N   HIS A 105     4942   4525   4471    314    134    290       N  
ATOM    874  CA  HIS A 105      24.575 -20.578 -32.111  1.00 38.90           C  
ANISOU  874  CA  HIS A 105     5233   4832   4715    287     73    284       C  
ATOM    875  C   HIS A 105      25.000 -21.464 -30.944  1.00 38.61           C  
ANISOU  875  C   HIS A 105     5174   4791   4703    303     44    307       C  
ATOM    876  O   HIS A 105      24.535 -21.275 -29.822  1.00 38.43           O  
ANISOU  876  O   HIS A 105     5140   4796   4666    282     -9    310       O  
ATOM    877  CB  HIS A 105      23.229 -21.044 -32.699  1.00 38.13           C  
ANISOU  877  CB  HIS A 105     5208   4725   4555    260     73    263       C  
ATOM    878  CG  HIS A 105      23.225 -22.465 -33.172  1.00 39.53           C  
ANISOU  878  CG  HIS A 105     5442   4858   4718    275    105    264       C  
ATOM    879  ND1 HIS A 105      22.978 -23.529 -32.331  1.00 40.31           N  
ANISOU  879  ND1 HIS A 105     5554   4950   4813    279     82    274       N  
ATOM    880  CD2 HIS A 105      23.419 -22.995 -34.403  1.00 41.59           C  
ANISOU  880  CD2 HIS A 105     5761   5076   4964    284    161    256       C  
ATOM    881  CE1 HIS A 105      23.027 -24.655 -33.023  1.00 44.53           C  
ANISOU  881  CE1 HIS A 105     6147   5439   5333    292    121    271       C  
ATOM    882  NE2 HIS A 105      23.297 -24.360 -34.283  1.00 41.37           N  
ANISOU  882  NE2 HIS A 105     5779   5015   4924    295    172    259       N  
ATOM    883  N   THR A 106      25.896 -22.412 -31.216  1.00 41.60           N  
ANISOU  883  N   THR A 106     5311   5534   4962    397    421    205       N  
ATOM    884  CA  THR A 106      26.374 -23.351 -30.193  1.00 42.24           C  
ANISOU  884  CA  THR A 106     5343   5616   5092    460    387    193       C  
ATOM    885  C   THR A 106      27.184 -22.662 -29.091  1.00 40.90           C  
ANISOU  885  C   THR A 106     5071   5486   4984    432    352    216       C  
ATOM    886  O   THR A 106      27.300 -23.194 -27.991  1.00 38.96           O  
ANISOU  886  O   THR A 106     4800   5228   4774    464    296    215       O  
ATOM    887  CB  THR A 106      27.198 -24.522 -30.801  1.00 41.97           C  
ANISOU  887  CB  THR A 106     5289   5599   5058    547    448    164       C  
ATOM    888  OG1 THR A 106      28.391 -24.015 -31.409  1.00 44.35           O  
ANISOU  888  OG1 THR A 106     5501   5973   5376    539    523    170       O  
ATOM    889  CG2 THR A 106      26.383 -25.279 -31.854  1.00 45.39           C  
ANISOU  889  CG2 THR A 106     5838   5985   5423    572    477    137       C  
ATOM    890  N   LYS A 107      27.726 -21.479 -29.393  1.00 41.06           N  
ANISOU  890  N   LYS A 107     5041   5549   5011    365    381    239       N  
ATOM    891  CA  LYS A 107      28.485 -20.690 -28.414  1.00 42.09           C  
ANISOU  891  CA  LYS A 107     5081   5717   5194    320    346    262       C  
ATOM    892  C   LYS A 107      27.594 -19.770 -27.567  1.00 40.71           C  
ANISOU  892  C   LYS A 107     4956   5498   5015    256    274    279       C  
ATOM    893  O   LYS A 107      28.049 -19.198 -26.567  1.00 41.41           O  
ANISOU  893  O   LYS A 107     4991   5602   5141    219    228    294       O  
ATOM    894  CB  LYS A 107      29.569 -19.851 -29.101  1.00 43.71           C  
ANISOU  894  CB  LYS A 107     5207   5990   5409    268    412    279       C  
ATOM    895  CG  LYS A 107      30.520 -20.616 -30.021  1.00 49.22           C  
ANISOU  895  CG  LYS A 107     5846   6746   6110    328    500    260       C  
ATOM    896  CD  LYS A 107      31.442 -21.531 -29.245  1.00 55.51           C  
ANISOU  896  CD  LYS A 107     6541   7580   6969    407    480    248       C  
ATOM    897  CE  LYS A 107      32.448 -22.209 -30.157  1.00 59.16           C  
ANISOU  897  CE  LYS A 107     6932   8106   7440    474    574    226       C  
ATOM    898  NZ  LYS A 107      33.335 -23.099 -29.355  1.00 63.14           N  
ANISOU  898  NZ  LYS A 107     7335   8645   8011    564    545    215       N  
ATOM    899  N   ILE A 108      26.337 -19.619 -27.976  1.00 38.35           N  
ANISOU  899  N   ILE A 108     4757   5145   4668    244    264    274       N  
ATOM    900  CA  ILE A 108      25.394 -18.724 -27.297  1.00 35.73           C  
ANISOU  900  CA  ILE A 108     4476   4771   4329    193    206    284       C  
ATOM    901  C   ILE A 108      24.598 -19.505 -26.260  1.00 36.24           C  
ANISOU  901  C   ILE A 108     4572   4798   4399    230    146    268       C  
ATOM    902  O   ILE A 108      24.001 -20.540 -26.576  1.00 38.30           O  
ANISOU  902  O   ILE A 108     4880   5037   4637    277    150    250       O  
ATOM    903  CB  ILE A 108      24.444 -18.031 -28.301  1.00 36.25           C  
ANISOU  903  CB  ILE A 108     4626   4804   4344    161    222    290       C  
ATOM    904  CG1 ILE A 108      25.262 -17.270 -29.353  1.00 36.22           C  
ANISOU  904  CG1 ILE A 108     4602   4834   4325    116    285    310       C  
ATOM    905  CG2 ILE A 108      23.466 -17.109 -27.568  1.00 34.97           C  
ANISOU  905  CG2 ILE A 108     4510   4598   4178    124    163    297       C  
ATOM    906  CD1 ILE A 108      24.481 -16.712 -30.541  1.00 33.63           C  
ANISOU  906  CD1 ILE A 108     4364   4476   3938     91    306    319       C  
ATOM    907  N   ARG A 109      24.606 -19.016 -25.020  1.00 34.31           N  
ANISOU  907  N   ARG A 109     4308   4547   4179    201     91    276       N  
ATOM    908  CA  ARG A 109      23.930 -19.695 -23.922  1.00 30.82           C  
ANISOU  908  CA  ARG A 109     3897   4075   3739    225     37    263       C  
ATOM    909  C   ARG A 109      22.459 -19.320 -23.859  1.00 31.13           C  
ANISOU  909  C   ARG A 109     4013   4071   3744    205     16    254       C  
ATOM    910  O   ARG A 109      22.107 -18.191 -23.488  1.00 32.54           O  
ANISOU  910  O   ARG A 109     4205   4236   3922    160     -3    261       O  
ATOM    911  CB  ARG A 109      24.616 -19.406 -22.576  1.00 32.23           C  
ANISOU  911  CB  ARG A 109     4025   4267   3953    203    -14    273       C  
ATOM    912  CG  ARG A 109      24.090 -20.278 -21.425  1.00 33.66           C  
ANISOU  912  CG  ARG A 109     4239   4421   4130    229    -66    262       C  
ATOM    913  CD  ARG A 109      24.808 -20.011 -20.100  1.00 34.62           C  
ANISOU  913  CD  ARG A 109     4319   4556   4279    206   -122    274       C  
ATOM    914  NE  ARG A 109      26.256 -20.171 -20.212  1.00 34.24           N  
ANISOU  914  NE  ARG A 109     4178   4559   4273    223   -117    287       N  
ATOM    915  CZ  ARG A 109      26.898 -21.333 -20.099  1.00 35.59           C  
ANISOU  915  CZ  ARG A 109     4314   4743   4464    290   -126    286       C  
ATOM    916  NH1 ARG A 109      26.228 -22.454 -19.852  1.00 31.47           N  
ANISOU  916  NH1 ARG A 109     3856   4180   3920    338   -142    274       N  
ATOM    917  NH2 ARG A 109      28.217 -21.371 -20.229  1.00 32.21           N  
ANISOU  917  NH2 ARG A 109     3788   4371   4080    308   -119    297       N  
ATOM    918  N   VAL A 110      21.608 -20.281 -24.214  1.00 29.69           N  
ANISOU  918  N   VAL A 110     3879   3866   3534    240     20    238       N  
ATOM    919  CA  VAL A 110      20.163 -20.095 -24.199  1.00 27.89           C  
ANISOU  919  CA  VAL A 110     3712   3609   3277    226      1    227       C  
ATOM    920  C   VAL A 110      19.601 -20.846 -23.000  1.00 31.79           C  
ANISOU  920  C   VAL A 110     4223   4086   3770    233    -39    215       C  
ATOM    921  O   VAL A 110      19.701 -22.076 -22.908  1.00 32.18           O  
ANISOU  921  O   VAL A 110     4286   4128   3814    265    -42    207       O  
ATOM    922  CB  VAL A 110      19.499 -20.546 -25.543  1.00 28.54           C  
ANISOU  922  CB  VAL A 110     3841   3682   3321    243     30    219       C  
ATOM    923  CG1 VAL A 110      17.978 -20.404 -25.491  1.00 23.93           C  
ANISOU  923  CG1 VAL A 110     3304   3077   2712    230      3    208       C  
ATOM    924  CG2 VAL A 110      20.047 -19.712 -26.710  1.00 28.59           C  
ANISOU  924  CG2 VAL A 110     3840   3703   3318    228     71    235       C  
ATOM    925  N   ALA A 111      19.032 -20.087 -22.067  1.00 31.47           N  
ANISOU  925  N   ALA A 111     4189   4036   3731    202    -69    213       N  
ATOM    926  CA  ALA A 111      18.470 -20.659 -20.862  1.00 32.88           C  
ANISOU  926  CA  ALA A 111     4388   4202   3902    197   -102    202       C  
ATOM    927  C   ALA A 111      16.956 -20.684 -20.965  1.00 32.17           C  
ANISOU  927  C   ALA A 111     4338   4102   3784    187   -103    185       C  
ATOM    928  O   ALA A 111      16.331 -19.706 -21.365  1.00 30.93           O  
ANISOU  928  O   ALA A 111     4185   3945   3624    176    -97    182       O  
ATOM    929  CB  ALA A 111      18.908 -19.873 -19.639  1.00 31.81           C  
ANISOU  929  CB  ALA A 111     4233   4069   3783    168   -132    207       C  
ATOM    930  N   ASN A 112      16.386 -21.825 -20.600  1.00 33.35           N  
ANISOU  930  N   ASN A 112     4516   4242   3913    190   -113    175       N  
ATOM    931  CA  ASN A 112      14.953 -22.031 -20.612  1.00 34.40           C  
ANISOU  931  CA  ASN A 112     4677   4375   4020    173   -115    158       C  
ATOM    932  C   ASN A 112      14.585 -22.473 -19.213  1.00 33.54           C  
ANISOU  932  C   ASN A 112     4584   4262   3899    149   -135    151       C  
ATOM    933  O   ASN A 112      15.003 -23.548 -18.765  1.00 33.04           O  
ANISOU  933  O   ASN A 112     4544   4183   3826    153   -148    156       O  
ATOM    934  CB  ASN A 112      14.611 -23.121 -21.636  1.00 36.71           C  
ANISOU  934  CB  ASN A 112     4999   4659   4289    186   -104    154       C  
ATOM    935  CG  ASN A 112      13.172 -23.057 -22.118  1.00 43.63           C  
ANISOU  935  CG  ASN A 112     5888   5545   5142    167   -105    141       C  
ATOM    936  OD1 ASN A 112      12.223 -23.191 -21.333  1.00 47.92           O  
ANISOU  936  OD1 ASN A 112     6434   6099   5675    139   -116    129       O  
ATOM    937  ND2 ASN A 112      13.000 -22.888 -23.429  1.00 40.46           N  
ANISOU  937  ND2 ASN A 112     5495   5147   4732    179    -95    143       N  
ATOM    938  N   PHE A 113      13.832 -21.648 -18.497  1.00 32.93           N  
ANISOU  938  N   PHE A 113     4499   4194   3817    127   -137    138       N  
ATOM    939  CA  PHE A 113      13.490 -22.012 -17.125  1.00 33.38           C  
ANISOU  939  CA  PHE A 113     4577   4251   3855     97   -150    130       C  
ATOM    940  C   PHE A 113      12.031 -21.800 -16.771  1.00 34.56           C  
ANISOU  940  C   PHE A 113     4727   4421   3984     72   -136    107       C  
ATOM    941  O   PHE A 113      11.300 -21.119 -17.485  1.00 36.05           O  
ANISOU  941  O   PHE A 113     4892   4625   4181     85   -124     96       O  
ATOM    942  CB  PHE A 113      14.443 -21.354 -16.105  1.00 31.39           C  
ANISOU  942  CB  PHE A 113     4319   3992   3616     91   -169    137       C  
ATOM    943  CG  PHE A 113      14.050 -19.955 -15.680  1.00 29.36           C  
ANISOU  943  CG  PHE A 113     4051   3740   3363     80   -163    122       C  
ATOM    944  CD1 PHE A 113      13.898 -18.935 -16.609  1.00 29.58           C  
ANISOU  944  CD1 PHE A 113     4059   3769   3411     98   -149    120       C  
ATOM    945  CD2 PHE A 113      13.877 -19.659 -14.334  1.00 29.80           C  
ANISOU  945  CD2 PHE A 113     4128   3794   3399     52   -172    109       C  
ATOM    946  CE1 PHE A 113      13.546 -17.640 -16.203  1.00 30.51           C  
ANISOU  946  CE1 PHE A 113     4179   3880   3532     95   -147    105       C  
ATOM    947  CE2 PHE A 113      13.540 -18.372 -13.916  1.00 32.19           C  
ANISOU  947  CE2 PHE A 113     4432   4094   3703     48   -164     90       C  
ATOM    948  CZ  PHE A 113      13.370 -17.362 -14.856  1.00 29.52           C  
ANISOU  948  CZ  PHE A 113     4076   3752   3390     72   -152     87       C  
ATOM    949  N   ASP A 114      11.615 -22.421 -15.675  1.00 36.48           N  
ANISOU  949  N   ASP A 114     4997   4667   4199     38   -139     99       N  
ATOM    950  CA  ASP A 114      10.325 -22.126 -15.061  1.00 38.85           C  
ANISOU  950  CA  ASP A 114     5288   4996   4478     10   -118     74       C  
ATOM    951  C   ASP A 114      10.396 -22.393 -13.569  1.00 38.09           C  
ANISOU  951  C   ASP A 114     5228   4895   4350    -28   -121     70       C  
ATOM    952  O   ASP A 114      11.247 -23.159 -13.104  1.00 38.66           O  
ANISOU  952  O   ASP A 114     5338   4940   4409    -38   -147     90       O  
ATOM    953  CB  ASP A 114       9.193 -22.942 -15.694  1.00 38.57           C  
ANISOU  953  CB  ASP A 114     5247   4982   4425    -11   -107     66       C  
ATOM    954  CG  ASP A 114       7.813 -22.352 -15.406  1.00 48.45           C  
ANISOU  954  CG  ASP A 114     6458   6279   5671    -26    -81     37       C  
ATOM    955  OD1 ASP A 114       7.709 -21.186 -14.916  1.00 50.22           O  
ANISOU  955  OD1 ASP A 114     6662   6512   5908     -4    -69     21       O  
ATOM    956  OD2 ASP A 114       6.823 -23.065 -15.670  1.00 52.36           O  
ANISOU  956  OD2 ASP A 114     6943   6802   6149    -58    -72     30       O  
ATOM    957  N   ILE A 115       9.497 -21.758 -12.821  1.00 37.72           N  
ANISOU  957  N   ILE A 115     5170   4875   4287    -47    -95     43       N  
ATOM    958  CA  ILE A 115       9.474 -21.908 -11.372  1.00 35.82           C  
ANISOU  958  CA  ILE A 115     4970   4634   4006    -88    -91     35       C  
ATOM    959  C   ILE A 115       8.110 -22.380 -10.877  1.00 36.53           C  
ANISOU  959  C   ILE A 115     5058   4764   4059   -135    -52     12       C  
ATOM    960  O   ILE A 115       7.096 -22.204 -11.563  1.00 37.51           O  
ANISOU  960  O   ILE A 115     5130   4925   4197   -126    -28     -5       O  
ATOM    961  CB  ILE A 115       9.896 -20.603 -10.655  1.00 36.35           C  
ANISOU  961  CB  ILE A 115     5040   4693   4079    -74    -91     19       C  
ATOM    962  CG1 ILE A 115       8.803 -19.526 -10.776  1.00 34.35           C  
ANISOU  962  CG1 ILE A 115     4746   4468   3835    -51    -52    -18       C  
ATOM    963  CG2 ILE A 115      11.262 -20.118 -11.187  1.00 33.00           C  
ANISOU  963  CG2 ILE A 115     4610   4236   3693    -40   -129     44       C  
ATOM    964  CD1 ILE A 115       8.966 -18.350  -9.812  1.00 33.26           C  
ANISOU  964  CD1 ILE A 115     4632   4318   3687    -46    -43    -43       C  
ATOM    965  N   GLU A 116       8.105 -23.012  -9.704  1.00 33.52           N  
ANISOU  965  N   GLU A 116     4730   4378   3627   -188    -50     15       N  
ATOM    966  CA  GLU A 116       6.876 -23.359  -9.005  1.00 34.02           C  
ANISOU  966  CA  GLU A 116     4795   4485   3646   -244     -5     -8       C  
ATOM    967  C   GLU A 116       6.794 -22.583  -7.698  1.00 33.91           C  
ANISOU  967  C   GLU A 116     4805   4480   3598   -260     21    -33       C  
ATOM    968  O   GLU A 116       7.802 -22.411  -7.012  1.00 34.41           O  
ANISOU  968  O   GLU A 116     4923   4506   3648   -260    -12    -20       O  
ATOM    969  CB  GLU A 116       6.811 -24.860  -8.710  1.00 34.66           C  
ANISOU  969  CB  GLU A 116     4937   4550   3681   -309    -17     17       C  
ATOM    970  CG  GLU A 116       6.884 -25.779  -9.932  1.00 39.19           C  
ANISOU  970  CG  GLU A 116     5507   5105   4278   -300    -43     39       C  
ATOM    971  CD  GLU A 116       5.825 -25.478 -10.979  1.00 44.40           C  
ANISOU  971  CD  GLU A 116     6088   5814   4967   -289    -17     19       C  
ATOM    972  OE1 GLU A 116       4.774 -24.897 -10.638  1.00 50.09           O  
ANISOU  972  OE1 GLU A 116     6757   6592   5683   -304     27    -12       O  
ATOM    973  OE2 GLU A 116       6.040 -25.818 -12.159  1.00 47.64           O  
ANISOU  973  OE2 GLU A 116     6488   6207   5405   -261    -41     32       O  
ATOM    974  N   VAL A 117       5.594 -22.107  -7.367  1.00 33.92           N  
ANISOU  974  N   VAL A 117     4766   4537   3587   -272     79    -72       N  
ATOM    975  CA  VAL A 117       5.348 -21.360  -6.133  1.00 33.39           C  
ANISOU  975  CA  VAL A 117     4722   4483   3480   -285    118   -106       C  
ATOM    976  C   VAL A 117       4.006 -21.821  -5.566  1.00 35.23           C  
ANISOU  976  C   VAL A 117     4935   4783   3669   -344    185   -133       C  
ATOM    977  O   VAL A 117       2.953 -21.537  -6.144  1.00 35.73           O  
ANISOU  977  O   VAL A 117     4913   4902   3762   -323    224   -159       O  
ATOM    978  CB  VAL A 117       5.305 -19.816  -6.375  1.00 31.84           C  
ANISOU  978  CB  VAL A 117     4484   4287   3326   -210    131   -139       C  
ATOM    979  CG1 VAL A 117       5.043 -19.054  -5.066  1.00 30.65           C  
ANISOU  979  CG1 VAL A 117     4372   4146   3129   -222    174   -181       C  
ATOM    980  CG2 VAL A 117       6.585 -19.312  -7.033  1.00 29.97           C  
ANISOU  980  CG2 VAL A 117     4261   3993   3135   -162     70   -112       C  
ATOM    981  N   THR A 118       4.045 -22.534  -4.444  1.00 35.93           N  
ANISOU  981  N   THR A 118     5099   4868   3686   -420    197   -125       N  
ATOM    982  CA  THR A 118       2.823 -22.936  -3.739  1.00 39.10           C  
ANISOU  982  CA  THR A 118     5488   5336   4034   -490    271   -151       C  
ATOM    983  C   THR A 118       2.208 -21.725  -3.035  1.00 42.01           C  
ANISOU  983  C   THR A 118     5825   5747   4392   -459    337   -209       C  
ATOM    984  O   THR A 118       2.900 -20.991  -2.324  1.00 42.40           O  
ANISOU  984  O   THR A 118     5933   5756   4420   -436    326   -220       O  
ATOM    985  CB  THR A 118       3.109 -24.069  -2.718  1.00 39.72           C  
ANISOU  985  CB  THR A 118     5675   5388   4027   -587    262   -121       C  
ATOM    986  OG1 THR A 118       3.523 -25.246  -3.428  1.00 37.62           O  
ANISOU  986  OG1 THR A 118     5438   5084   3773   -610    205    -73       O  
ATOM    987  CG2 THR A 118       1.865 -24.392  -1.864  1.00 36.38           C  
ANISOU  987  CG2 THR A 118     5246   5039   3538   -672    348   -150       C  
ATOM    988  N   SER A 119       0.911 -21.520  -3.247  1.00 45.26           N  
ANISOU  988  N   SER A 119     6142   6238   4817   -456    405   -246       N  
ATOM    989  CA  SER A 119       0.212 -20.347  -2.725  1.00 49.86           C  
ANISOU  989  CA  SER A 119     6680   6866   5400   -407    474   -307       C  
ATOM    990  C   SER A 119      -1.233 -20.682  -2.342  1.00 54.27           C  
ANISOU  990  C   SER A 119     7165   7528   5929   -459    565   -343       C  
ATOM    991  O   SER A 119      -2.061 -20.953  -3.220  1.00 55.21           O  
ANISOU  991  O   SER A 119     7180   7705   6094   -452    574   -344       O  
ATOM    992  CB  SER A 119       0.236 -19.206  -3.749  1.00 48.91           C  
ANISOU  992  CB  SER A 119     6486   6733   5364   -292    450   -324       C  
ATOM    993  OG  SER A 119      -0.528 -18.103  -3.297  1.00 51.78           O  
ANISOU  993  OG  SER A 119     6806   7137   5731   -234    517   -386       O  
ATOM    994  N   PRO A 120      -1.541 -20.668  -1.029  1.00 57.38           N  
ANISOU  994  N   PRO A 120     7610   7949   6244   -514    635   -373       N  
ATOM    995  CA  PRO A 120      -2.913 -20.935  -0.600  1.00 59.04           C  
ANISOU  995  CA  PRO A 120     7743   8267   6423   -568    734   -411       C  
ATOM    996  C   PRO A 120      -3.858 -19.755  -0.844  1.00 60.30           C  
ANISOU  996  C   PRO A 120     7780   8495   6637   -467    796   -476       C  
ATOM    997  O   PRO A 120      -5.026 -19.974  -1.156  1.00 61.66           O  
ANISOU  997  O   PRO A 120     7832   8765   6831   -481    850   -497       O  
ATOM    998  CB  PRO A 120      -2.766 -21.202   0.903  1.00 60.48           C  
ANISOU  998  CB  PRO A 120     8038   8444   6496   -654    785   -421       C  
ATOM    999  CG  PRO A 120      -1.554 -20.426   1.308  1.00 60.07           C  
ANISOU  999  CG  PRO A 120     8091   8296   6435   -598    731   -419       C  
ATOM   1000  CD  PRO A 120      -0.631 -20.448   0.115  1.00 58.12           C  
ANISOU 1000  CD  PRO A 120     7836   7978   6268   -538    624   -371       C  
ATOM   1001  N   ASP A 121      -3.357 -18.526  -0.724  1.00 59.65           N  
ANISOU 1001  N   ASP A 121     7727   8360   6578   -367    785   -505       N  
ATOM   1002  CA  ASP A 121      -4.219 -17.344  -0.767  1.00 61.99           C  
ANISOU 1002  CA  ASP A 121     7930   8707   6915   -263    848   -573       C  
ATOM   1003  C   ASP A 121      -4.308 -16.671  -2.138  1.00 61.48           C  
ANISOU 1003  C   ASP A 121     7776   8630   6955   -150    790   -568       C  
ATOM   1004  O   ASP A 121      -4.339 -15.441  -2.238  1.00 61.52           O  
ANISOU 1004  O   ASP A 121     7769   8608   6997    -39    795   -607       O  
ATOM   1005  CB  ASP A 121      -3.834 -16.335   0.329  1.00 64.57           C  
ANISOU 1005  CB  ASP A 121     8352   8989   7192   -224    887   -621       C  
ATOM   1006  CG  ASP A 121      -2.402 -15.826   0.201  1.00 67.03           C  
ANISOU 1006  CG  ASP A 121     8779   9177   7514   -190    793   -590       C  
ATOM   1007  OD1 ASP A 121      -1.856 -15.362   1.225  1.00 67.90           O  
ANISOU 1007  OD1 ASP A 121     8999   9239   7560   -203    806   -612       O  
ATOM   1008  OD2 ASP A 121      -1.825 -15.877  -0.911  1.00 68.94           O  
ANISOU 1008  OD2 ASP A 121     9001   9373   7822   -155    707   -544       O  
ATOM   1009  N   GLY A 122      -4.366 -17.482  -3.188  1.00 61.02           N  
ANISOU 1009  N   GLY A 122     7663   8584   6937   -180    733   -519       N  
ATOM   1010  CA  GLY A 122      -4.581 -16.969  -4.537  1.00 60.48           C  
ANISOU 1010  CA  GLY A 122     7506   8515   6959    -85    679   -511       C  
ATOM   1011  C   GLY A 122      -3.321 -16.919  -5.369  1.00 58.68           C  
ANISOU 1011  C   GLY A 122     7351   8181   6762    -60    578   -458       C  
ATOM   1012  O   GLY A 122      -2.299 -17.505  -5.002  1.00 58.58           O  
ANISOU 1012  O   GLY A 122     7445   8106   6709   -124    542   -420       O  
ATOM   1013  N   PHE A 123      -3.404 -16.220  -6.499  1.00 57.17           N  
ANISOU 1013  N   PHE A 123     7104   7974   6645     34    531   -454       N  
ATOM   1014  CA  PHE A 123      -2.285 -16.091  -7.429  1.00 54.73           C  
ANISOU 1014  CA  PHE A 123     6851   7575   6369     62    441   -406       C  
ATOM   1015  C   PHE A 123      -1.107 -15.353  -6.785  1.00 51.54           C  
ANISOU 1015  C   PHE A 123     6564   7077   5942     82    423   -407       C  
ATOM   1016  O   PHE A 123      -1.285 -14.248  -6.262  1.00 50.73           O  
ANISOU 1016  O   PHE A 123     6475   6961   5840    147    456   -452       O  
ATOM   1017  CB  PHE A 123      -2.736 -15.373  -8.701  1.00 56.09           C  
ANISOU 1017  CB  PHE A 123     6943   7753   6615    160    402   -406       C  
ATOM   1018  CG  PHE A 123      -1.635 -15.138  -9.690  1.00 58.58           C  
ANISOU 1018  CG  PHE A 123     7316   7980   6962    189    320   -359       C  
ATOM   1019  CD1 PHE A 123      -1.315 -16.110 -10.634  1.00 58.56           C  
ANISOU 1019  CD1 PHE A 123     7309   7973   6968    142    269   -310       C  
ATOM   1020  CD2 PHE A 123      -0.924 -13.935  -9.687  1.00 60.44           C  
ANISOU 1020  CD2 PHE A 123     7613   8137   7214    261    297   -367       C  
ATOM   1021  CE1 PHE A 123      -0.292 -15.898 -11.560  1.00 61.48           C  
ANISOU 1021  CE1 PHE A 123     7728   8267   7363    169    202   -269       C  
ATOM   1022  CE2 PHE A 123       0.101 -13.712 -10.605  1.00 62.28           C  
ANISOU 1022  CE2 PHE A 123     7895   8295   7473    278    228   -323       C  
ATOM   1023  CZ  PHE A 123       0.415 -14.696 -11.549  1.00 62.23           C  
ANISOU 1023  CZ  PHE A 123     7877   8293   7475    234    184   -274       C  
ATOM   1024  N   PRO A 124       0.098 -15.960  -6.836  1.00 48.11           N  
ANISOU 1024  N   PRO A 124     6213   6579   5489     28    368   -357       N  
ATOM   1025  CA  PRO A 124       1.278 -15.405  -6.177  1.00 46.89           C  
ANISOU 1025  CA  PRO A 124     6164   6345   5309     28    343   -352       C  
ATOM   1026  C   PRO A 124       1.816 -14.201  -6.934  1.00 46.74           C  
ANISOU 1026  C   PRO A 124     6154   6262   5342    115    298   -351       C  
ATOM   1027  O   PRO A 124       2.471 -14.365  -7.959  1.00 47.44           O  
ANISOU 1027  O   PRO A 124     6241   6316   5468    124    239   -307       O  
ATOM   1028  CB  PRO A 124       2.278 -16.559  -6.229  1.00 44.19           C  
ANISOU 1028  CB  PRO A 124     5879   5969   4944    -48    291   -296       C  
ATOM   1029  CG  PRO A 124       1.896 -17.336  -7.436  1.00 45.13           C  
ANISOU 1029  CG  PRO A 124     5929   6117   5101    -52    267   -265       C  
ATOM   1030  CD  PRO A 124       0.420 -17.169  -7.619  1.00 46.48           C  
ANISOU 1030  CD  PRO A 124     6001   6372   5289    -28    321   -304       C  
ATOM   1031  N   GLU A 125       1.533 -13.003  -6.435  1.00 48.95           N  
ANISOU 1031  N   GLU A 125     6452   6524   5622    176    329   -399       N  
ATOM   1032  CA  GLU A 125       1.964 -11.773  -7.098  1.00 50.45           C  
ANISOU 1032  CA  GLU A 125     6665   6647   5857    256    289   -400       C  
ATOM   1033  C   GLU A 125       3.483 -11.598  -7.071  1.00 49.30           C  
ANISOU 1033  C   GLU A 125     6612   6418   5703    220    228   -361       C  
ATOM   1034  O   GLU A 125       4.082 -11.503  -5.996  1.00 51.25           O  
ANISOU 1034  O   GLU A 125     6936   6635   5900    176    233   -372       O  
ATOM   1035  CB  GLU A 125       1.256 -10.544  -6.510  1.00 52.87           C  
ANISOU 1035  CB  GLU A 125     6980   6947   6161    333    339   -465       C  
ATOM   1036  CG  GLU A 125      -0.161 -10.313  -7.060  1.00 58.88           C  
ANISOU 1036  CG  GLU A 125     7628   7779   6966    412    376   -498       C  
ATOM   1037  CD  GLU A 125      -0.191 -10.093  -8.576  1.00 63.09           C  
ANISOU 1037  CD  GLU A 125     8111   8296   7565    469    313   -460       C  
ATOM   1038  OE1 GLU A 125       0.732  -9.438  -9.112  1.00 64.55           O  
ANISOU 1038  OE1 GLU A 125     8363   8395   7768    489    256   -433       O  
ATOM   1039  OE2 GLU A 125      -1.143 -10.574  -9.232  1.00 64.73           O  
ANISOU 1039  OE2 GLU A 125     8214   8577   7802    486    319   -458       O  
ATOM   1040  N   PRO A 126       4.109 -11.563  -8.261  1.00 46.53           N  
ANISOU 1040  N   PRO A 126     6248   6033   5397    236    169   -315       N  
ATOM   1041  CA  PRO A 126       5.547 -11.352  -8.392  1.00 45.00           C  
ANISOU 1041  CA  PRO A 126     6122   5771   5205    206    113   -277       C  
ATOM   1042  C   PRO A 126       6.065 -10.146  -7.616  1.00 45.18           C  
ANISOU 1042  C   PRO A 126     6229   5728   5207    217    109   -306       C  
ATOM   1043  O   PRO A 126       7.129 -10.240  -7.005  1.00 44.59           O  
ANISOU 1043  O   PRO A 126     6217   5619   5105    160     79   -288       O  
ATOM   1044  CB  PRO A 126       5.728 -11.134  -9.897  1.00 45.54           C  
ANISOU 1044  CB  PRO A 126     6154   5821   5328    247     72   -241       C  
ATOM   1045  CG  PRO A 126       4.635 -11.941 -10.507  1.00 46.74           C  
ANISOU 1045  CG  PRO A 126     6220   6043   5496    260     93   -241       C  
ATOM   1046  CD  PRO A 126       3.464 -11.751  -9.577  1.00 46.45           C  
ANISOU 1046  CD  PRO A 126     6158   6056   5437    280    155   -297       C  
ATOM   1047  N   SER A 127       5.321  -9.037  -7.614  1.00 43.66           N  
ANISOU 1047  N   SER A 127     6042   5519   5029    291    135   -350       N  
ATOM   1048  CA  SER A 127       5.778  -7.819  -6.932  1.00 44.58           C  
ANISOU 1048  CA  SER A 127     6253   5561   5124    305    130   -381       C  
ATOM   1049  C   SER A 127       5.729  -7.937  -5.409  1.00 45.35           C  
ANISOU 1049  C   SER A 127     6409   5669   5154    260    170   -422       C  
ATOM   1050  O   SER A 127       6.375  -7.164  -4.699  1.00 47.49           O  
ANISOU 1050  O   SER A 127     6774   5877   5393    241    155   -440       O  
ATOM   1051  CB  SER A 127       4.998  -6.589  -7.398  1.00 43.89           C  
ANISOU 1051  CB  SER A 127     6167   5441   5069    407    143   -418       C  
ATOM   1052  OG  SER A 127       3.712  -6.577  -6.813  1.00 48.81           O  
ANISOU 1052  OG  SER A 127     6747   6120   5680    457    213   -476       O  
ATOM   1053  N   GLN A 128       4.960  -8.903  -4.913  1.00 45.35           N  
ANISOU 1053  N   GLN A 128     6359   5746   5127    236    221   -436       N  
ATOM   1054  CA  GLN A 128       4.912  -9.179  -3.481  1.00 46.32           C  
ANISOU 1054  CA  GLN A 128     6541   5885   5175    181    262   -469       C  
ATOM   1055  C   GLN A 128       5.916 -10.272  -3.117  1.00 43.21           C  
ANISOU 1055  C   GLN A 128     6177   5494   4748     84    217   -417       C  
ATOM   1056  O   GLN A 128       6.683 -10.117  -2.170  1.00 41.71           O  
ANISOU 1056  O   GLN A 128     6075   5265   4506     32    196   -420       O  
ATOM   1057  CB  GLN A 128       3.489  -9.560  -3.028  1.00 49.26           C  
ANISOU 1057  CB  GLN A 128     6849   6342   5527    202    350   -517       C  
ATOM   1058  CG  GLN A 128       2.413  -8.481  -3.266  1.00 54.98           C  
ANISOU 1058  CG  GLN A 128     7534   7071   6283    312    399   -576       C  
ATOM   1059  CD  GLN A 128       2.764  -7.119  -2.655  1.00 60.28           C  
ANISOU 1059  CD  GLN A 128     8314   7658   6932    354    400   -621       C  
ATOM   1060  OE1 GLN A 128       3.081  -6.165  -3.374  1.00 60.17           O  
ANISOU 1060  OE1 GLN A 128     8325   7574   6962    414    356   -615       O  
ATOM   1061  NE2 GLN A 128       2.714  -7.029  -1.324  1.00 60.44           N  
ANISOU 1061  NE2 GLN A 128     8409   7678   6877    317    449   -667       N  
ATOM   1062  N   ALA A 129       5.908 -11.360  -3.891  1.00 40.32           N  
ANISOU 1062  N   ALA A 129     5741   5169   4412     63    198   -371       N  
ATOM   1063  CA  ALA A 129       6.769 -12.525  -3.669  1.00 38.80           C  
ANISOU 1063  CA  ALA A 129     5568   4979   4194    -15    155   -320       C  
ATOM   1064  C   ALA A 129       6.820 -12.937  -2.188  1.00 39.51           C  
ANISOU 1064  C   ALA A 129     5734   5079   4201    -83    178   -338       C  
ATOM   1065  O   ALA A 129       7.882 -12.956  -1.557  1.00 39.14           O  
ANISOU 1065  O   ALA A 129     5761   4990   4121   -131    127   -318       O  
ATOM   1066  CB  ALA A 129       8.175 -12.286  -4.250  1.00 35.13           C  
ANISOU 1066  CB  ALA A 129     5127   4456   3765    -24     75   -273       C  
ATOM   1067  N   LYS A 130       5.650 -13.251  -1.644  1.00 40.88           N  
ANISOU 1067  N   LYS A 130     5885   5310   4337    -90    254   -376       N  
ATOM   1068  CA  LYS A 130       5.523 -13.531  -0.220  1.00 44.32           C  
ANISOU 1068  CA  LYS A 130     6398   5758   4683   -153    291   -401       C  
ATOM   1069  C   LYS A 130       5.544 -15.025   0.081  1.00 43.65           C  
ANISOU 1069  C   LYS A 130     6319   5709   4558   -233    284   -360       C  
ATOM   1070  O   LYS A 130       5.560 -15.423   1.248  1.00 43.74           O  
ANISOU 1070  O   LYS A 130     6407   5727   4487   -300    303   -368       O  
ATOM   1071  CB  LYS A 130       4.275 -12.850   0.369  1.00 46.16           C  
ANISOU 1071  CB  LYS A 130     6620   6033   4888   -116    389   -475       C  
ATOM   1072  CG  LYS A 130       2.945 -13.234  -0.277  1.00 53.42           C  
ANISOU 1072  CG  LYS A 130     7419   7034   5845    -81    453   -492       C  
ATOM   1073  CD  LYS A 130       1.797 -12.380   0.282  1.00 59.40           C  
ANISOU 1073  CD  LYS A 130     8155   7831   6583    -26    549   -571       C  
ATOM   1074  CE  LYS A 130       0.423 -12.921  -0.122  1.00 60.72           C  
ANISOU 1074  CE  LYS A 130     8196   8100   6776    -12    619   -589       C  
ATOM   1075  NZ  LYS A 130      -0.703 -12.043   0.339  1.00 61.92           N  
ANISOU 1075  NZ  LYS A 130     8308   8298   6921     60    715   -669       N  
ATOM   1076  N   HIS A 131       5.562 -15.842  -0.974  1.00 41.57           N  
ANISOU 1076  N   HIS A 131     5986   5462   4347   -229    255   -316       N  
ATOM   1077  CA  HIS A 131       5.614 -17.297  -0.827  1.00 41.54           C  
ANISOU 1077  CA  HIS A 131     5994   5479   4311   -301    241   -273       C  
ATOM   1078  C   HIS A 131       6.928 -17.892  -1.337  1.00 38.75           C  
ANISOU 1078  C   HIS A 131     5664   5074   3986   -310    146   -210       C  
ATOM   1079  O   HIS A 131       7.524 -17.375  -2.284  1.00 38.22           O  
ANISOU 1079  O   HIS A 131     5558   4977   3985   -256    104   -195       O  
ATOM   1080  CB  HIS A 131       4.420 -17.956  -1.519  1.00 42.52           C  
ANISOU 1080  CB  HIS A 131     6026   5670   4459   -301    292   -278       C  
ATOM   1081  CG  HIS A 131       3.103 -17.374  -1.119  1.00 44.83           C  
ANISOU 1081  CG  HIS A 131     6271   6026   4735   -282    386   -340       C  
ATOM   1082  ND1 HIS A 131       2.321 -16.640  -1.983  1.00 47.80           N  
ANISOU 1082  ND1 HIS A 131     6550   6435   5178   -203    415   -371       N  
ATOM   1083  CD2 HIS A 131       2.447 -17.385   0.064  1.00 49.37           C  
ANISOU 1083  CD2 HIS A 131     6882   6640   5235   -328    460   -380       C  
ATOM   1084  CE1 HIS A 131       1.231 -16.239  -1.354  1.00 48.00           C  
ANISOU 1084  CE1 HIS A 131     6543   6519   5174   -193    502   -428       C  
ATOM   1085  NE2 HIS A 131       1.283 -16.678  -0.110  1.00 50.56           N  
ANISOU 1085  NE2 HIS A 131     6947   6851   5412   -271    536   -436       N  
ATOM   1086  N   PRO A 132       7.397 -18.970  -0.684  1.00 38.14           N  
ANISOU 1086  N   PRO A 132     5653   4984   3855   -378    114   -174       N  
ATOM   1087  CA  PRO A 132       8.624 -19.651  -1.094  1.00 36.26           C  
ANISOU 1087  CA  PRO A 132     5433   4701   3642   -380     26   -116       C  
ATOM   1088  C   PRO A 132       8.606 -20.110  -2.547  1.00 33.85           C  
ANISOU 1088  C   PRO A 132     5047   4401   3411   -337     10    -90       C  
ATOM   1089  O   PRO A 132       7.576 -20.560  -3.030  1.00 33.93           O  
ANISOU 1089  O   PRO A 132     5010   4454   3430   -342     58   -100       O  
ATOM   1090  CB  PRO A 132       8.665 -20.868  -0.170  1.00 33.44           C  
ANISOU 1090  CB  PRO A 132     5158   4341   3209   -457     13    -88       C  
ATOM   1091  CG  PRO A 132       8.001 -20.381   1.080  1.00 38.91           C  
ANISOU 1091  CG  PRO A 132     5907   5056   3821   -500     74   -133       C  
ATOM   1092  CD  PRO A 132       6.922 -19.440   0.636  1.00 38.43           C  
ANISOU 1092  CD  PRO A 132     5765   5040   3795   -453    155   -189       C  
ATOM   1093  N   ILE A 133       9.739 -19.971  -3.233  1.00 33.81           N  
ANISOU 1093  N   ILE A 133     5028   4360   3460   -299    -54    -58       N  
ATOM   1094  CA  ILE A 133       9.949 -20.668  -4.494  1.00 35.90           C  
ANISOU 1094  CA  ILE A 133     5239   4621   3779   -269    -77    -26       C  
ATOM   1095  C   ILE A 133      10.324 -22.108  -4.146  1.00 34.94           C  
ANISOU 1095  C   ILE A 133     5172   4481   3621   -312   -114     14       C  
ATOM   1096  O   ILE A 133      11.349 -22.346  -3.509  1.00 36.56           O  
ANISOU 1096  O   ILE A 133     5432   4652   3806   -324   -172     41       O  
ATOM   1097  CB  ILE A 133      11.075 -20.037  -5.331  1.00 34.25           C  
ANISOU 1097  CB  ILE A 133     4996   4383   3634   -217   -126     -6       C  
ATOM   1098  CG1 ILE A 133      10.732 -18.586  -5.685  1.00 32.31           C  
ANISOU 1098  CG1 ILE A 133     4713   4142   3421   -177    -96    -42       C  
ATOM   1099  CG2 ILE A 133      11.332 -20.888  -6.583  1.00 35.73           C  
ANISOU 1099  CG2 ILE A 133     5140   4567   3867   -189   -145     26       C  
ATOM   1100  CD1 ILE A 133      11.910 -17.763  -6.164  1.00 23.24           C  
ANISOU 1100  CD1 ILE A 133     3552   2961   2318   -148   -143    -25       C  
ATOM   1101  N   ASP A 134       9.502 -23.067  -4.548  1.00 34.09           N  
ANISOU 1101  N   ASP A 134     5055   4393   3503   -335    -86     19       N  
ATOM   1102  CA  ASP A 134       9.764 -24.461  -4.156  1.00 32.84           C  
ANISOU 1102  CA  ASP A 134     4968   4208   3302   -381   -119     56       C  
ATOM   1103  C   ASP A 134      10.274 -25.385  -5.259  1.00 31.58           C  
ANISOU 1103  C   ASP A 134     4795   4019   3185   -347   -159     90       C  
ATOM   1104  O   ASP A 134      10.431 -26.584  -5.048  1.00 33.49           O  
ANISOU 1104  O   ASP A 134     5101   4230   3394   -378   -187    119       O  
ATOM   1105  CB  ASP A 134       8.558 -25.081  -3.427  1.00 34.41           C  
ANISOU 1105  CB  ASP A 134     5205   4438   3431   -459    -64     41       C  
ATOM   1106  CG  ASP A 134       7.230 -24.814  -4.118  1.00 32.81           C  
ANISOU 1106  CG  ASP A 134     4919   4296   3251   -460      6      6       C  
ATOM   1107  OD1 ASP A 134       7.174 -24.795  -5.366  1.00 35.71           O  
ANISOU 1107  OD1 ASP A 134     5221   4667   3679   -413     -1     10       O  
ATOM   1108  OD2 ASP A 134       6.227 -24.642  -3.393  1.00 30.34           O  
ANISOU 1108  OD2 ASP A 134     4606   4029   2892   -508     69    -25       O  
ATOM   1109  N   ALA A 135      10.536 -24.831  -6.435  1.00 30.04           N  
ANISOU 1109  N   ALA A 135     4525   3830   3058   -285   -160     85       N  
ATOM   1110  CA  ALA A 135      11.058 -25.624  -7.546  1.00 29.69           C  
ANISOU 1110  CA  ALA A 135     4468   3759   3053   -248   -190    112       C  
ATOM   1111  C   ALA A 135      11.495 -24.716  -8.672  1.00 31.18           C  
ANISOU 1111  C   ALA A 135     4580   3956   3309   -182   -189    105       C  
ATOM   1112  O   ALA A 135      10.763 -23.808  -9.074  1.00 29.73           O  
ANISOU 1112  O   ALA A 135     4344   3807   3145   -172   -150     77       O  
ATOM   1113  CB  ALA A 135      10.024 -26.605  -8.051  1.00 26.88           C  
ANISOU 1113  CB  ALA A 135     4121   3414   2677   -284   -162    110       C  
ATOM   1114  N   ILE A 136      12.708 -24.945  -9.158  1.00 31.11           N  
ANISOU 1114  N   ILE A 136     4567   3919   3336   -138   -233    132       N  
ATOM   1115  CA  ILE A 136      13.154 -24.300 -10.375  1.00 28.72           C  
ANISOU 1115  CA  ILE A 136     4198   3623   3092    -84   -228    131       C  
ATOM   1116  C   ILE A 136      13.740 -25.374 -11.250  1.00 29.21           C  
ANISOU 1116  C   ILE A 136     4268   3659   3172    -50   -249    154       C  
ATOM   1117  O   ILE A 136      14.573 -26.152 -10.794  1.00 29.08           O  
ANISOU 1117  O   ILE A 136     4290   3612   3147    -41   -290    177       O  
ATOM   1118  CB  ILE A 136      14.241 -23.231 -10.118  1.00 27.40           C  
ANISOU 1118  CB  ILE A 136     4003   3452   2954    -61   -254    136       C  
ATOM   1119  CG1 ILE A 136      13.813 -22.276  -8.999  1.00 24.43           C  
ANISOU 1119  CG1 ILE A 136     3646   3087   2548    -97   -243    112       C  
ATOM   1120  CG2 ILE A 136      14.583 -22.491 -11.422  1.00 23.14           C  
ANISOU 1120  CG2 ILE A 136     3401   2923   2469    -17   -240    135       C  
ATOM   1121  CD1 ILE A 136      14.856 -21.235  -8.640  1.00 26.31           C  
ANISOU 1121  CD1 ILE A 136     3872   3318   2808    -90   -275    117       C  
ATOM   1122  N   THR A 137      13.275 -25.426 -12.496  1.00 30.39           N  
ANISOU 1122  N   THR A 137     4386   3820   3343    -29   -222    146       N  
ATOM   1123  CA  THR A 137      13.924 -26.207 -13.533  1.00 29.64           C  
ANISOU 1123  CA  THR A 137     4292   3701   3270     14   -233    161       C  
ATOM   1124  C   THR A 137      14.485 -25.216 -14.529  1.00 30.41           C  
ANISOU 1124  C   THR A 137     4324   3816   3414     57   -219    159       C  
ATOM   1125  O   THR A 137      13.753 -24.394 -15.088  1.00 28.91           O  
ANISOU 1125  O   THR A 137     4102   3651   3233     53   -191    143       O  
ATOM   1126  CB  THR A 137      12.964 -27.196 -14.218  1.00 28.72           C  
ANISOU 1126  CB  THR A 137     4208   3577   3128     -6   -216    154       C  
ATOM   1127  OG1 THR A 137      12.576 -28.190 -13.270  1.00 30.81           O  
ANISOU 1127  OG1 THR A 137     4542   3818   3345    -54   -231    161       O  
ATOM   1128  CG2 THR A 137      13.645 -27.889 -15.389  1.00 29.84           C  
ANISOU 1128  CG2 THR A 137     4356   3691   3289     45   -221    163       C  
ATOM   1129  N   HIS A 138      15.796 -25.302 -14.724  1.00 31.66           N  
ANISOU 1129  N   HIS A 138     4465   3963   3602     99   -241    177       N  
ATOM   1130  CA  HIS A 138      16.539 -24.383 -15.568  1.00 31.35           C  
ANISOU 1130  CA  HIS A 138     4365   3941   3604    130   -228    180       C  
ATOM   1131  C   HIS A 138      17.342 -25.192 -16.595  1.00 32.28           C  
ANISOU 1131  C   HIS A 138     4475   4047   3741    182   -222    190       C  
ATOM   1132  O   HIS A 138      18.368 -25.788 -16.254  1.00 32.39           O  
ANISOU 1132  O   HIS A 138     4487   4049   3769    213   -250    206       O  
ATOM   1133  CB  HIS A 138      17.453 -23.536 -14.673  1.00 31.07           C  
ANISOU 1133  CB  HIS A 138     4302   3914   3587    122   -256    190       C  
ATOM   1134  CG  HIS A 138      18.309 -22.555 -15.411  1.00 32.37           C  
ANISOU 1134  CG  HIS A 138     4408   4098   3793    139   -245    197       C  
ATOM   1135  ND1 HIS A 138      18.216 -21.194 -15.212  1.00 33.13           N  
ANISOU 1135  ND1 HIS A 138     4485   4205   3897    112   -240    190       N  
ATOM   1136  CD2 HIS A 138      19.284 -22.736 -16.334  1.00 32.30           C  
ANISOU 1136  CD2 HIS A 138     4357   4099   3816    178   -235    210       C  
ATOM   1137  CE1 HIS A 138      19.090 -20.579 -15.988  1.00 33.29           C  
ANISOU 1137  CE1 HIS A 138     4459   4238   3950    124   -230    202       C  
ATOM   1138  NE2 HIS A 138      19.756 -21.493 -16.673  1.00 33.90           N  
ANISOU 1138  NE2 HIS A 138     4516   4322   4043    163   -223    213       N  
ATOM   1139  N   TYR A 139      16.863 -25.230 -17.841  1.00 32.76           N  
ANISOU 1139  N   TYR A 139     4534   4113   3801    194   -189    181       N  
ATOM   1140  CA  TYR A 139      17.600 -25.888 -18.931  1.00 31.75           C  
ANISOU 1140  CA  TYR A 139     4402   3976   3686    243   -172    184       C  
ATOM   1141  C   TYR A 139      18.691 -24.959 -19.480  1.00 33.15           C  
ANISOU 1141  C   TYR A 139     4512   4182   3902    267   -155    194       C  
ATOM   1142  O   TYR A 139      18.458 -23.771 -19.704  1.00 34.83           O  
ANISOU 1142  O   TYR A 139     4696   4414   4122    242   -141    193       O  
ATOM   1143  CB  TYR A 139      16.659 -26.371 -20.052  1.00 29.60           C  
ANISOU 1143  CB  TYR A 139     4166   3694   3386    240   -146    170       C  
ATOM   1144  CG  TYR A 139      17.391 -26.928 -21.271  1.00 31.53           C  
ANISOU 1144  CG  TYR A 139     4414   3929   3636    291   -120    168       C  
ATOM   1145  CD1 TYR A 139      17.670 -26.116 -22.375  1.00 31.29           C  
ANISOU 1145  CD1 TYR A 139     4347   3924   3617    302    -86    168       C  
ATOM   1146  CD2 TYR A 139      17.825 -28.257 -21.308  1.00 31.06           C  
ANISOU 1146  CD2 TYR A 139     4401   3832   3566    329   -129    166       C  
ATOM   1147  CE1 TYR A 139      18.349 -26.615 -23.489  1.00 30.93           C  
ANISOU 1147  CE1 TYR A 139     4307   3874   3570    347    -53    163       C  
ATOM   1148  CE2 TYR A 139      18.506 -28.765 -22.412  1.00 31.02           C  
ANISOU 1148  CE2 TYR A 139     4403   3820   3565    383    -98    158       C  
ATOM   1149  CZ  TYR A 139      18.770 -27.940 -23.498  1.00 30.98           C  
ANISOU 1149  CZ  TYR A 139     4355   3847   3568    390    -56    156       C  
ATOM   1150  OH  TYR A 139      19.456 -28.435 -24.592  1.00 29.86           O  
ANISOU 1150  OH  TYR A 139     4222   3700   3423    442    -17    145       O  
ATOM   1151  N   ASP A 140      19.879 -25.516 -19.692  1.00 32.73           N  
ANISOU 1151  N   ASP A 140     4434   4129   3872    315   -155    203       N  
ATOM   1152  CA  ASP A 140      21.000 -24.784 -20.257  1.00 31.48           C  
ANISOU 1152  CA  ASP A 140     4203   4006   3750    334   -133    212       C  
ATOM   1153  C   ASP A 140      21.379 -25.385 -21.615  1.00 34.05           C  
ANISOU 1153  C   ASP A 140     4530   4334   4075    382    -86    204       C  
ATOM   1154  O   ASP A 140      21.729 -26.565 -21.694  1.00 35.43           O  
ANISOU 1154  O   ASP A 140     4729   4486   4248    433    -89    198       O  
ATOM   1155  CB  ASP A 140      22.189 -24.851 -19.302  1.00 31.18           C  
ANISOU 1155  CB  ASP A 140     4117   3983   3748    351   -171    228       C  
ATOM   1156  CG  ASP A 140      23.367 -24.046 -19.789  1.00 33.87           C  
ANISOU 1156  CG  ASP A 140     4370   4370   4128    357   -149    239       C  
ATOM   1157  OD1 ASP A 140      24.102 -24.549 -20.676  1.00 32.71           O  
ANISOU 1157  OD1 ASP A 140     4192   4240   3998    408   -113    237       O  
ATOM   1158  OD2 ASP A 140      23.554 -22.913 -19.283  1.00 33.65           O  
ANISOU 1158  OD2 ASP A 140     4310   4362   4114    307   -165    249       O  
ATOM   1159  N   SER A 141      21.311 -24.574 -22.672  1.00 32.25           N  
ANISOU 1159  N   SER A 141     4283   4127   3844    367    -44    202       N  
ATOM   1160  CA  SER A 141      21.508 -25.063 -24.045  1.00 34.38           C  
ANISOU 1160  CA  SER A 141     4567   4397   4097    403      7    191       C  
ATOM   1161  C   SER A 141      22.933 -25.544 -24.315  1.00 35.37           C  
ANISOU 1161  C   SER A 141     4638   4547   4255    462     33    193       C  
ATOM   1162  O   SER A 141      23.139 -26.466 -25.105  1.00 35.83           O  
ANISOU 1162  O   SER A 141     4724   4591   4298    513     66    176       O  
ATOM   1163  CB  SER A 141      21.143 -23.984 -25.068  1.00 34.49           C  
ANISOU 1163  CB  SER A 141     4580   4429   4096    366     42    195       C  
ATOM   1164  OG  SER A 141      22.045 -22.886 -24.989  1.00 37.09           O  
ANISOU 1164  OG  SER A 141     4840   4795   4456    344     54    212       O  
ATOM   1165  N   ILE A 142      23.908 -24.907 -23.669  1.00 35.85           N  
ANISOU 1165  N   ILE A 142     4618   4646   4359    454     19    210       N  
ATOM   1166  CA  ILE A 142      25.311 -25.283 -23.832  1.00 36.15           C  
ANISOU 1166  CA  ILE A 142     4579   4720   4436    511     40    212       C  
ATOM   1167  C   ILE A 142      25.641 -26.636 -23.160  1.00 37.68           C  
ANISOU 1167  C   ILE A 142     4791   4884   4642    582      2    206       C  
ATOM   1168  O   ILE A 142      26.241 -27.514 -23.788  1.00 37.69           O  
ANISOU 1168  O   ILE A 142     4787   4884   4649    656     35    191       O  
ATOM   1169  CB  ILE A 142      26.255 -24.136 -23.387  1.00 36.01           C  
ANISOU 1169  CB  ILE A 142     4463   4758   4461    469     32    234       C  
ATOM   1170  CG1 ILE A 142      26.208 -23.005 -24.428  1.00 30.80           C  
ANISOU 1170  CG1 ILE A 142     3790   4126   3787    416     88    239       C  
ATOM   1171  CG2 ILE A 142      27.692 -24.654 -23.169  1.00 35.63           C  
ANISOU 1171  CG2 ILE A 142     4319   4755   4464    530     31    238       C  
ATOM   1172  CD1 ILE A 142      27.153 -21.839 -24.175  1.00 33.40           C  
ANISOU 1172  CD1 ILE A 142     4030   4507   4152    362     89    261       C  
ATOM   1173  N   ASP A 143      25.219 -26.810 -21.909  1.00 37.10           N  
ANISOU 1173  N   ASP A 143     4749   4781   4566    562    -66    216       N  
ATOM   1174  CA  ASP A 143      25.400 -28.088 -21.203  1.00 38.90           C  
ANISOU 1174  CA  ASP A 143     5017   4967   4796    621   -112    215       C  
ATOM   1175  C   ASP A 143      24.453 -29.165 -21.715  1.00 37.65           C  
ANISOU 1175  C   ASP A 143     4970   4745   4589    641    -99    195       C  
ATOM   1176  O   ASP A 143      24.753 -30.355 -21.603  1.00 37.44           O  
ANISOU 1176  O   ASP A 143     4985   4678   4561    708   -117    189       O  
ATOM   1177  CB  ASP A 143      25.182 -27.923 -19.690  1.00 40.20           C  
ANISOU 1177  CB  ASP A 143     5195   5117   4960    581   -188    235       C  
ATOM   1178  CG  ASP A 143      26.217 -27.027 -19.038  1.00 41.54           C  
ANISOU 1178  CG  ASP A 143     5264   5343   5177    563   -217    255       C  
ATOM   1179  OD1 ASP A 143      27.211 -26.647 -19.698  1.00 44.37           O  
ANISOU 1179  OD1 ASP A 143     5530   5755   5573    587   -181    256       O  
ATOM   1180  OD2 ASP A 143      26.030 -26.706 -17.850  1.00 40.90           O  
ANISOU 1180  OD2 ASP A 143     5198   5254   5090    519   -276    269       O  
ATOM   1181  N   ASP A 144      23.311 -28.734 -22.265  1.00 37.53           N  
ANISOU 1181  N   ASP A 144     5004   4721   4535    581    -75    186       N  
ATOM   1182  CA  ASP A 144      22.241 -29.631 -22.714  1.00 36.37           C  
ANISOU 1182  CA  ASP A 144     4963   4519   4338    576    -70    168       C  
ATOM   1183  C   ASP A 144      21.725 -30.440 -21.525  1.00 35.91           C  
ANISOU 1183  C   ASP A 144     4973   4411   4261    562   -131    175       C  
ATOM   1184  O   ASP A 144      21.619 -31.668 -21.579  1.00 38.36           O  
ANISOU 1184  O   ASP A 144     5361   4666   4549    599   -144    167       O  
ATOM   1185  CB  ASP A 144      22.733 -30.541 -23.859  1.00 37.35           C  
ANISOU 1185  CB  ASP A 144     5116   4624   4453    649    -24    146       C  
ATOM   1186  CG  ASP A 144      21.611 -31.310 -24.532  1.00 36.63           C  
ANISOU 1186  CG  ASP A 144     5135   4479   4303    629    -15    125       C  
ATOM   1187  OD1 ASP A 144      20.447 -30.847 -24.514  1.00 37.44           O  
ANISOU 1187  OD1 ASP A 144     5267   4583   4377    554    -26    127       O  
ATOM   1188  OD2 ASP A 144      21.904 -32.379 -25.102  1.00 41.13           O  
ANISOU 1188  OD2 ASP A 144     5763   5008   4857    690      2    105       O  
ATOM   1189  N   ARG A 145      21.426 -29.736 -20.439  1.00 33.90           N  
ANISOU 1189  N   ARG A 145     4696   4173   4012    507   -168    192       N  
ATOM   1190  CA  ARG A 145      21.035 -30.378 -19.185  1.00 33.04           C  
ANISOU 1190  CA  ARG A 145     4648   4024   3882    485   -225    203       C  
ATOM   1191  C   ARG A 145      19.892 -29.622 -18.539  1.00 31.34           C  
ANISOU 1191  C   ARG A 145     4446   3823   3641    398   -234    204       C  
ATOM   1192  O   ARG A 145      19.821 -28.395 -18.644  1.00 29.22           O  
ANISOU 1192  O   ARG A 145     4117   3598   3389    366   -216    204       O  
ATOM   1193  CB  ARG A 145      22.216 -30.435 -18.210  1.00 32.21           C  
ANISOU 1193  CB  ARG A 145     4497   3929   3814    526   -273    224       C  
ATOM   1194  CG  ARG A 145      23.397 -31.308 -18.662  1.00 33.48           C  
ANISOU 1194  CG  ARG A 145     4639   4077   4006    628   -273    223       C  
ATOM   1195  CD  ARG A 145      23.029 -32.787 -18.675  1.00 32.03           C  
ANISOU 1195  CD  ARG A 145     4571   3814   3786    665   -292    216       C  
ATOM   1196  NE  ARG A 145      24.155 -33.668 -18.986  1.00 35.50           N  
ANISOU 1196  NE  ARG A 145     4999   4232   4256    776   -297    213       N  
ATOM   1197  CZ  ARG A 145      24.534 -34.002 -20.220  1.00 40.98           C  
ANISOU 1197  CZ  ARG A 145     5683   4927   4959    840   -239    188       C  
ATOM   1198  NH1 ARG A 145      23.892 -33.514 -21.279  1.00 37.40           N  
ANISOU 1198  NH1 ARG A 145     5232   4494   4482    797   -177    168       N  
ATOM   1199  NH2 ARG A 145      25.564 -34.826 -20.397  1.00 38.73           N  
ANISOU 1199  NH2 ARG A 145     5388   4623   4703    951   -244    182       N  
ATOM   1200  N   PHE A 146      18.997 -30.362 -17.890  1.00 30.56           N  
ANISOU 1200  N   PHE A 146     4428   3684   3499    359   -259    204       N  
ATOM   1201  CA  PHE A 146      17.921 -29.774 -17.093  1.00 32.02           C  
ANISOU 1201  CA  PHE A 146     4625   3884   3657    279   -266    203       C  
ATOM   1202  C   PHE A 146      18.380 -29.751 -15.635  1.00 31.95           C  
ANISOU 1202  C   PHE A 146     4624   3869   3646    266   -315    222       C  
ATOM   1203  O   PHE A 146      18.491 -30.800 -14.998  1.00 31.46           O  
ANISOU 1203  O   PHE A 146     4631   3761   3560    274   -352    235       O  
ATOM   1204  CB  PHE A 146      16.626 -30.598 -17.218  1.00 32.35           C  
ANISOU 1204  CB  PHE A 146     4748   3896   3649    230   -259    192       C  
ATOM   1205  CG  PHE A 146      16.011 -30.591 -18.598  1.00 33.62           C  
ANISOU 1205  CG  PHE A 146     4908   4064   3802    229   -220    173       C  
ATOM   1206  CD1 PHE A 146      16.449 -31.476 -19.576  1.00 30.91           C  
ANISOU 1206  CD1 PHE A 146     4603   3685   3455    280   -209    165       C  
ATOM   1207  CD2 PHE A 146      14.976 -29.713 -18.909  1.00 34.04           C  
ANISOU 1207  CD2 PHE A 146     4927   4159   3849    180   -197    161       C  
ATOM   1208  CE1 PHE A 146      15.882 -31.479 -20.847  1.00 31.12           C  
ANISOU 1208  CE1 PHE A 146     4640   3718   3466    273   -177    147       C  
ATOM   1209  CE2 PHE A 146      14.406 -29.699 -20.180  1.00 33.40           C  
ANISOU 1209  CE2 PHE A 146     4849   4085   3758    178   -171    146       C  
ATOM   1210  CZ  PHE A 146      14.858 -30.589 -21.152  1.00 33.61           C  
ANISOU 1210  CZ  PHE A 146     4920   4076   3775    220   -162    140       C  
ATOM   1211  N   TYR A 147      18.676 -28.561 -15.123  1.00 31.35           N  
ANISOU 1211  N   TYR A 147     4486   3833   3592    246   -319    226       N  
ATOM   1212  CA  TYR A 147      19.039 -28.404 -13.715  1.00 33.27           C  
ANISOU 1212  CA  TYR A 147     4741   4074   3826    223   -368    242       C  
ATOM   1213  C   TYR A 147      17.792 -28.153 -12.876  1.00 31.91           C  
ANISOU 1213  C   TYR A 147     4616   3903   3604    146   -361    232       C  
ATOM   1214  O   TYR A 147      17.119 -27.127 -13.025  1.00 32.57           O  
ANISOU 1214  O   TYR A 147     4666   4020   3690    113   -327    215       O  
ATOM   1215  CB  TYR A 147      20.065 -27.275 -13.522  1.00 34.33           C  
ANISOU 1215  CB  TYR A 147     4791   4248   4003    235   -381    250       C  
ATOM   1216  CG  TYR A 147      21.390 -27.517 -14.220  1.00 35.44           C  
ANISOU 1216  CG  TYR A 147     4869   4400   4194    307   -387    261       C  
ATOM   1217  CD1 TYR A 147      21.600 -27.086 -15.536  1.00 36.90           C  
ANISOU 1217  CD1 TYR A 147     4999   4613   4410    333   -334    250       C  
ATOM   1218  CD2 TYR A 147      22.432 -28.171 -13.568  1.00 36.88           C  
ANISOU 1218  CD2 TYR A 147     5049   4571   4394    352   -444    282       C  
ATOM   1219  CE1 TYR A 147      22.822 -27.299 -16.185  1.00 35.72           C  
ANISOU 1219  CE1 TYR A 147     4785   4482   4304    399   -328    257       C  
ATOM   1220  CE2 TYR A 147      23.663 -28.389 -14.202  1.00 38.55           C  
ANISOU 1220  CE2 TYR A 147     5188   4803   4656    426   -445    289       C  
ATOM   1221  CZ  TYR A 147      23.845 -27.953 -15.509  1.00 41.22           C  
ANISOU 1221  CZ  TYR A 147     5466   5172   5023    447   -381    275       C  
ATOM   1222  OH  TYR A 147      25.050 -28.170 -16.134  1.00 41.10           O  
ANISOU 1222  OH  TYR A 147     5375   5185   5056    518   -371    278       O  
ATOM   1223  N   VAL A 148      17.497 -29.104 -11.997  1.00 31.45           N  
ANISOU 1223  N   VAL A 148     4639   3807   3502    120   -392    244       N  
ATOM   1224  CA  VAL A 148      16.287 -29.083 -11.176  1.00 30.39           C  
ANISOU 1224  CA  VAL A 148     4557   3676   3313     42   -378    234       C  
ATOM   1225  C   VAL A 148      16.625 -28.722  -9.726  1.00 32.36           C  
ANISOU 1225  C   VAL A 148     4832   3927   3538      9   -418    246       C  
ATOM   1226  O   VAL A 148      17.423 -29.404  -9.072  1.00 31.49           O  
ANISOU 1226  O   VAL A 148     4766   3783   3417     29   -475    272       O  
ATOM   1227  CB  VAL A 148      15.544 -30.448 -11.229  1.00 29.53           C  
ANISOU 1227  CB  VAL A 148     4539   3525   3159     14   -378    238       C  
ATOM   1228  CG1 VAL A 148      14.201 -30.369 -10.507  1.00 29.01           C  
ANISOU 1228  CG1 VAL A 148     4509   3477   3038    -76   -350    225       C  
ATOM   1229  CG2 VAL A 148      15.334 -30.893 -12.685  1.00 27.11           C  
ANISOU 1229  CG2 VAL A 148     4219   3210   2873     48   -348    226       C  
ATOM   1230  N   PHE A 149      16.011 -27.646  -9.237  1.00 32.15           N  
ANISOU 1230  N   PHE A 149     4781   3936   3497    -37   -389    226       N  
ATOM   1231  CA  PHE A 149      16.208 -27.173  -7.860  1.00 31.59           C  
ANISOU 1231  CA  PHE A 149     4742   3869   3393    -76   -419    231       C  
ATOM   1232  C   PHE A 149      14.919 -27.395  -7.107  1.00 32.58           C  
ANISOU 1232  C   PHE A 149     4929   3999   3451   -150   -385    215       C  
ATOM   1233  O   PHE A 149      13.908 -26.771  -7.409  1.00 35.21           O  
ANISOU 1233  O   PHE A 149     5228   4367   3783   -174   -327    185       O  
ATOM   1234  CB  PHE A 149      16.564 -25.682  -7.838  1.00 30.46           C  
ANISOU 1234  CB  PHE A 149     4532   3760   3282    -72   -410    215       C  
ATOM   1235  CG  PHE A 149      17.816 -25.340  -8.599  1.00 33.20           C  
ANISOU 1235  CG  PHE A 149     4807   4113   3694    -13   -435    229       C  
ATOM   1236  CD1 PHE A 149      17.845 -25.404  -9.994  1.00 33.87           C  
ANISOU 1236  CD1 PHE A 149     4839   4206   3822     32   -401    225       C  
ATOM   1237  CD2 PHE A 149      18.960 -24.941  -7.925  1.00 32.56           C  
ANISOU 1237  CD2 PHE A 149     4710   4034   3626     -8   -492    247       C  
ATOM   1238  CE1 PHE A 149      18.994 -25.084 -10.698  1.00 34.51           C  
ANISOU 1238  CE1 PHE A 149     4852   4300   3959     80   -414    237       C  
ATOM   1239  CE2 PHE A 149      20.119 -24.612  -8.622  1.00 35.10           C  
ANISOU 1239  CE2 PHE A 149     4954   4373   4010     39   -511    260       C  
ATOM   1240  CZ  PHE A 149      20.134 -24.688 -10.012  1.00 36.92           C  
ANISOU 1240  CZ  PHE A 149     5132   4614   4283     83   -467    254       C  
ATOM   1241  N   ASP A 150      14.957 -28.276  -6.121  1.00 34.00           N  
ANISOU 1241  N   ASP A 150     5198   4145   3575   -187   -420    237       N  
ATOM   1242  CA  ASP A 150      13.740 -28.766  -5.493  1.00 34.80           C  
ANISOU 1242  CA  ASP A 150     5366   4249   3607   -265   -383    227       C  
ATOM   1243  C   ASP A 150      13.742 -28.478  -3.994  1.00 33.71           C  
ANISOU 1243  C   ASP A 150     5293   4112   3405   -321   -400    230       C  
ATOM   1244  O   ASP A 150      14.653 -28.898  -3.294  1.00 34.11           O  
ANISOU 1244  O   ASP A 150     5401   4125   3436   -313   -470    261       O  
ATOM   1245  CB  ASP A 150      13.625 -30.272  -5.744  1.00 33.69           C  
ANISOU 1245  CB  ASP A 150     5301   4059   3441   -273   -405    253       C  
ATOM   1246  CG  ASP A 150      12.396 -30.883  -5.104  1.00 39.36           C  
ANISOU 1246  CG  ASP A 150     6093   4780   4084   -368   -368    248       C  
ATOM   1247  OD1 ASP A 150      11.505 -30.131  -4.625  1.00 35.64           O  
ANISOU 1247  OD1 ASP A 150     5595   4360   3586   -421   -312    219       O  
ATOM   1248  OD2 ASP A 150      12.325 -32.132  -5.088  1.00 39.07           O  
ANISOU 1248  OD2 ASP A 150     6141   4691   4012   -390   -393    273       O  
ATOM   1249  N   LEU A 151      12.722 -27.770  -3.509  1.00 32.69           N  
ANISOU 1249  N   LEU A 151     5156   4025   3241   -375   -338    196       N  
ATOM   1250  CA  LEU A 151      12.632 -27.464  -2.088  1.00 33.74           C  
ANISOU 1250  CA  LEU A 151     5357   4161   3303   -433   -342    192       C  
ATOM   1251  C   LEU A 151      11.937 -28.596  -1.337  1.00 36.28           C  
ANISOU 1251  C   LEU A 151     5782   4464   3539   -512   -333    208       C  
ATOM   1252  O   LEU A 151      10.811 -28.985  -1.666  1.00 36.32           O  
ANISOU 1252  O   LEU A 151     5779   4494   3528   -555   -271    192       O  
ATOM   1253  CB  LEU A 151      11.921 -26.130  -1.852  1.00 32.17           C  
ANISOU 1253  CB  LEU A 151     5108   4013   3101   -447   -276    143       C  
ATOM   1254  CG  LEU A 151      11.819 -25.668  -0.397  1.00 29.90           C  
ANISOU 1254  CG  LEU A 151     4893   3730   2736   -504   -271    130       C  
ATOM   1255  CD1 LEU A 151      13.204 -25.621   0.243  1.00 26.07           C  
ANISOU 1255  CD1 LEU A 151     4457   3204   2244   -489   -366    163       C  
ATOM   1256  CD2 LEU A 151      11.113 -24.314  -0.270  1.00 29.28           C  
ANISOU 1256  CD2 LEU A 151     4765   3698   2662   -502   -201     75       C  
ATOM   1257  N   LEU A 152      12.617 -29.132  -0.333  1.00 39.74           N  
ANISOU 1257  N   LEU A 152     6319   4858   3923   -536   -398    243       N  
ATOM   1258  CA  LEU A 152      12.072 -30.268   0.418  1.00 42.73           C  
ANISOU 1258  CA  LEU A 152     6816   5206   4213   -617   -399    266       C  
ATOM   1259  C   LEU A 152      11.277 -29.839   1.631  1.00 41.15           C  
ANISOU 1259  C   LEU A 152     6671   5041   3924   -706   -345    243       C  
ATOM   1260  O   LEU A 152      10.334 -30.522   2.024  1.00 41.05           O  
ANISOU 1260  O   LEU A 152     6720   5035   3843   -790   -298    244       O  
ATOM   1261  CB  LEU A 152      13.159 -31.275   0.812  1.00 42.55           C  
ANISOU 1261  CB  LEU A 152     6889   5108   4171   -594   -503    322       C  
ATOM   1262  CG  LEU A 152      13.805 -32.088  -0.319  1.00 44.39           C  
ANISOU 1262  CG  LEU A 152     7097   5296   4473   -513   -549    347       C  
ATOM   1263  CD1 LEU A 152      14.385 -33.381   0.253  1.00 43.48           C  
ANISOU 1263  CD1 LEU A 152     7113   5099   4309   -518   -634    400       C  
ATOM   1264  CD2 LEU A 152      12.840 -32.411  -1.461  1.00 41.82           C  
ANISOU 1264  CD2 LEU A 152     6722   4991   4179   -521   -479    324       C  
ATOM   1265  N   ASN A 153      11.657 -28.701   2.202  1.00 39.92           N  
ANISOU 1265  N   ASN A 153     6495   4908   3767   -692   -348    220       N  
ATOM   1266  CA  ASN A 153      11.021 -28.178   3.406  1.00 42.88           C  
ANISOU 1266  CA  ASN A 153     6927   5312   4053   -768   -296    192       C  
ATOM   1267  C   ASN A 153      10.527 -26.746   3.207  1.00 44.27           C  
ANISOU 1267  C   ASN A 153     7008   5547   4265   -741   -223    132       C  
ATOM   1268  O   ASN A 153      11.269 -25.867   2.749  1.00 40.44           O  
ANISOU 1268  O   ASN A 153     6458   5059   3849   -671   -257    123       O  
ATOM   1269  CB  ASN A 153      11.969 -28.247   4.608  1.00 43.81           C  
ANISOU 1269  CB  ASN A 153     7156   5385   4103   -791   -381    223       C  
ATOM   1270  CG  ASN A 153      12.542 -29.645   4.832  1.00 50.01           C  
ANISOU 1270  CG  ASN A 153     8044   6102   4854   -804   -467    287       C  
ATOM   1271  OD1 ASN A 153      11.853 -30.655   4.678  1.00 52.66           O  
ANISOU 1271  OD1 ASN A 153     8426   6424   5157   -851   -438    303       O  
ATOM   1272  ND2 ASN A 153      13.814 -29.703   5.201  1.00 53.36           N  
ANISOU 1272  ND2 ASN A 153     8506   6483   5287   -763   -577    324       N  
ATOM   1273  N   SER A 154       9.267 -26.527   3.570  1.00 45.00           N  
ANISOU 1273  N   SER A 154     7096   5692   4310   -797   -123     91       N  
ATOM   1274  CA  SER A 154       8.585 -25.266   3.337  1.00 44.65           C  
ANISOU 1274  CA  SER A 154     6962   5705   4299   -766    -43     30       C  
ATOM   1275  C   SER A 154       7.535 -25.065   4.421  1.00 45.33           C  
ANISOU 1275  C   SER A 154     7096   5837   4291   -844     48    -10       C  
ATOM   1276  O   SER A 154       7.078 -26.038   5.015  1.00 46.30           O  
ANISOU 1276  O   SER A 154     7295   5961   4335   -928     67     11       O  
ATOM   1277  CB  SER A 154       7.930 -25.301   1.953  1.00 43.72           C  
ANISOU 1277  CB  SER A 154     6723   5622   4268   -720     -3     17       C  
ATOM   1278  OG  SER A 154       6.924 -24.320   1.821  1.00 44.79           O  
ANISOU 1278  OG  SER A 154     6779   5820   4420   -703     87    -42       O  
ATOM   1279  N   PRO A 155       7.143 -23.804   4.690  1.00 46.69           N  
ANISOU 1279  N   PRO A 155     7230   6046   4465   -817    109    -68       N  
ATOM   1280  CA  PRO A 155       6.011 -23.596   5.600  1.00 47.16           C  
ANISOU 1280  CA  PRO A 155     7316   6162   4441   -880    215   -116       C  
ATOM   1281  C   PRO A 155       4.703 -24.202   5.064  1.00 48.62           C  
ANISOU 1281  C   PRO A 155     7422   6414   4637   -914    301   -129       C  
ATOM   1282  O   PRO A 155       3.726 -24.301   5.803  1.00 51.31           O  
ANISOU 1282  O   PRO A 155     7782   6811   4905   -983    393   -160       O  
ATOM   1283  CB  PRO A 155       5.905 -22.067   5.689  1.00 47.08           C  
ANISOU 1283  CB  PRO A 155     7262   6169   4458   -815    256   -178       C  
ATOM   1284  CG  PRO A 155       6.616 -21.561   4.454  1.00 45.42           C  
ANISOU 1284  CG  PRO A 155     6963   5929   4364   -720    192   -165       C  
ATOM   1285  CD  PRO A 155       7.722 -22.529   4.225  1.00 44.57           C  
ANISOU 1285  CD  PRO A 155     6902   5764   4269   -730     85    -94       C  
ATOM   1286  N   TYR A 156       4.687 -24.608   3.793  1.00 48.72           N  
ANISOU 1286  N   TYR A 156     7348   6425   4738   -871    273   -106       N  
ATOM   1287  CA  TYR A 156       3.501 -25.232   3.200  1.00 48.61           C  
ANISOU 1287  CA  TYR A 156     7257   6474   4738   -908    339   -114       C  
ATOM   1288  C   TYR A 156       3.612 -26.749   3.067  1.00 49.32           C  
ANISOU 1288  C   TYR A 156     7414   6529   4796   -983    295    -55       C  
ATOM   1289  O   TYR A 156       2.710 -27.403   2.531  1.00 50.23           O  
ANISOU 1289  O   TYR A 156     7477   6687   4921  -1027    336    -54       O  
ATOM   1290  CB  TYR A 156       3.144 -24.576   1.861  1.00 47.64           C  
ANISOU 1290  CB  TYR A 156     6991   6385   4727   -816    350   -138       C  
ATOM   1291  CG  TYR A 156       2.913 -23.092   1.992  1.00 48.46           C  
ANISOU 1291  CG  TYR A 156     7036   6516   4858   -743    397   -198       C  
ATOM   1292  CD1 TYR A 156       2.020 -22.588   2.940  1.00 52.36           C  
ANISOU 1292  CD1 TYR A 156     7533   7071   5292   -775    495   -252       C  
ATOM   1293  CD2 TYR A 156       3.599 -22.188   1.188  1.00 46.32           C  
ANISOU 1293  CD2 TYR A 156     6717   6210   4672   -642    347   -202       C  
ATOM   1294  CE1 TYR A 156       1.813 -21.218   3.080  1.00 53.04           C  
ANISOU 1294  CE1 TYR A 156     7578   7174   5402   -699    538   -311       C  
ATOM   1295  CE2 TYR A 156       3.394 -20.816   1.315  1.00 48.72           C  
ANISOU 1295  CE2 TYR A 156     6985   6529   4999   -575    386   -255       C  
ATOM   1296  CZ  TYR A 156       2.501 -20.340   2.262  1.00 51.64           C  
ANISOU 1296  CZ  TYR A 156     7362   6951   5309   -599    479   -311       C  
ATOM   1297  OH  TYR A 156       2.295 -18.988   2.397  1.00 52.80           O  
ANISOU 1297  OH  TYR A 156     7483   7104   5476   -525    517   -368       O  
ATOM   1298  N   GLY A 157       4.709 -27.308   3.568  1.00 48.73           N  
ANISOU 1298  N   GLY A 157     7458   6375   4683   -997    207     -6       N  
ATOM   1299  CA  GLY A 157       4.848 -28.757   3.628  1.00 48.89           C  
ANISOU 1299  CA  GLY A 157     7570   6348   4657  -1068    162     51       C  
ATOM   1300  C   GLY A 157       6.259 -29.280   3.463  1.00 48.24           C  
ANISOU 1300  C   GLY A 157     7562   6171   4597  -1020     39    107       C  
ATOM   1301  O   GLY A 157       7.045 -28.764   2.664  1.00 47.85           O  
ANISOU 1301  O   GLY A 157     7446   6100   4635   -921    -13    108       O  
ATOM   1302  N   ASN A 158       6.571 -30.312   4.237  1.00 47.42           N  
ANISOU 1302  N   ASN A 158     7596   6012   4409  -1091     -7    153       N  
ATOM   1303  CA  ASN A 158       7.816 -31.046   4.096  1.00 47.79           C  
ANISOU 1303  CA  ASN A 158     7718   5967   4471  -1047   -126    211       C  
ATOM   1304  C   ASN A 158       7.565 -32.308   3.289  1.00 48.16           C  
ANISOU 1304  C   ASN A 158     7785   5978   4534  -1067   -144    245       C  
ATOM   1305  O   ASN A 158       6.627 -33.062   3.575  1.00 50.80           O  
ANISOU 1305  O   ASN A 158     8174   6327   4802  -1171    -93    250       O  
ATOM   1306  CB  ASN A 158       8.403 -31.385   5.468  1.00 47.00           C  
ANISOU 1306  CB  ASN A 158     7772   5817   4268  -1103   -182    246       C  
ATOM   1307  CG  ASN A 158       8.704 -30.149   6.290  1.00 47.56           C  
ANISOU 1307  CG  ASN A 158     7838   5917   4315  -1088   -171    211       C  
ATOM   1308  OD1 ASN A 158       8.960 -29.070   5.747  1.00 45.58           O  
ANISOU 1308  OD1 ASN A 158     7479   5695   4144  -1008   -162    176       O  
ATOM   1309  ND2 ASN A 158       8.651 -30.291   7.606  1.00 45.07           N  
ANISOU 1309  ND2 ASN A 158     7650   5590   3883  -1170   -170    221       N  
ATOM   1310  N   VAL A 159       8.412 -32.528   2.287  1.00 46.47           N  
ANISOU 1310  N   VAL A 159     7532   5718   4406   -972   -214    265       N  
ATOM   1311  CA  VAL A 159       8.199 -33.569   1.284  1.00 46.73           C  
ANISOU 1311  CA  VAL A 159     7567   5717   4470   -971   -228    286       C  
ATOM   1312  C   VAL A 159       9.432 -34.464   1.116  1.00 47.55           C  
ANISOU 1312  C   VAL A 159     7758   5721   4590   -909   -340    339       C  
ATOM   1313  O   VAL A 159      10.530 -34.108   1.549  1.00 48.74           O  
ANISOU 1313  O   VAL A 159     7925   5842   4752   -847   -409    356       O  
ATOM   1314  CB  VAL A 159       7.800 -32.946  -0.093  1.00 45.35           C  
ANISOU 1314  CB  VAL A 159     7238   5597   4397   -905   -184    247       C  
ATOM   1315  CG1 VAL A 159       6.471 -32.202   0.011  1.00 43.83           C  
ANISOU 1315  CG1 VAL A 159     6958   5503   4192   -962    -76    196       C  
ATOM   1316  CG2 VAL A 159       8.876 -32.016  -0.607  1.00 42.35           C  
ANISOU 1316  CG2 VAL A 159     6778   5212   4102   -785   -228    239       C  
ATOM   1317  N   GLU A 160       9.240 -35.627   0.495  1.00 48.44           N  
ANISOU 1317  N   GLU A 160     7924   5781   4700   -926   -358    363       N  
ATOM   1318  CA  GLU A 160      10.346 -36.522   0.137  1.00 47.27           C  
ANISOU 1318  CA  GLU A 160     7847   5535   4576   -850   -457    406       C  
ATOM   1319  C   GLU A 160      11.013 -36.072  -1.167  1.00 43.28           C  
ANISOU 1319  C   GLU A 160     7219   5040   4187   -724   -472    388       C  
ATOM   1320  O   GLU A 160      10.452 -35.268  -1.916  1.00 40.43           O  
ANISOU 1320  O   GLU A 160     6734   4750   3878   -711   -407    347       O  
ATOM   1321  CB  GLU A 160       9.857 -37.970  -0.002  1.00 49.85           C  
ANISOU 1321  CB  GLU A 160     8300   5792   4849   -920   -470    437       C  
ATOM   1322  CG  GLU A 160       9.054 -38.506   1.185  1.00 59.60           C  
ANISOU 1322  CG  GLU A 160     9662   7020   5963  -1065   -442    456       C  
ATOM   1323  CD  GLU A 160       9.928 -38.980   2.338  1.00 67.18           C  
ANISOU 1323  CD  GLU A 160    10770   7900   6853  -1066   -531    507       C  
ATOM   1324  OE1 GLU A 160       9.998 -40.214   2.557  1.00 69.28           O  
ANISOU 1324  OE1 GLU A 160    11188   8073   7061  -1107   -583    552       O  
ATOM   1325  OE2 GLU A 160      10.540 -38.126   3.022  1.00 67.90           O  
ANISOU 1325  OE2 GLU A 160    10834   8019   6945  -1028   -555    503       O  
ATOM   1326  N   GLU A 161      12.209 -36.594  -1.429  1.00 40.96           N  
ANISOU 1326  N   GLU A 161     6960   4674   3928   -630   -559    420       N  
ATOM   1327  CA  GLU A 161      12.935 -36.294  -2.655  1.00 40.46           C  
ANISOU 1327  CA  GLU A 161     6792   4615   3967   -512   -572    406       C  
ATOM   1328  C   GLU A 161      12.183 -36.803  -3.874  1.00 40.09           C  
ANISOU 1328  C   GLU A 161     6720   4567   3944   -522   -525    386       C  
ATOM   1329  O   GLU A 161      11.421 -37.762  -3.794  1.00 40.31           O  
ANISOU 1329  O   GLU A 161     6844   4559   3914   -603   -513    397       O  
ATOM   1330  CB  GLU A 161      14.325 -36.934  -2.630  1.00 41.52           C  
ANISOU 1330  CB  GLU A 161     6977   4672   4128   -412   -672    444       C  
ATOM   1331  CG  GLU A 161      15.423 -36.033  -2.104  1.00 43.73           C  
ANISOU 1331  CG  GLU A 161     7193   4978   4443   -348   -722    451       C  
ATOM   1332  CD  GLU A 161      16.791 -36.699  -2.102  1.00 46.03           C  
ANISOU 1332  CD  GLU A 161     7519   5203   4767   -244   -824    488       C  
ATOM   1333  OE1 GLU A 161      17.099 -37.472  -3.031  1.00 47.52           O  
ANISOU 1333  OE1 GLU A 161     7714   5345   4996   -173   -836    492       O  
ATOM   1334  OE2 GLU A 161      17.570 -36.432  -1.168  1.00 51.27           O  
ANISOU 1334  OE2 GLU A 161     8201   5862   5416   -229   -892    513       O  
ATOM   1335  N   TRP A 162      12.408 -36.146  -5.003  1.00 39.93           N  
ANISOU 1335  N   TRP A 162     6578   4587   4007   -445   -500    359       N  
ATOM   1336  CA  TRP A 162      11.837 -36.568  -6.269  1.00 38.71           C  
ANISOU 1336  CA  TRP A 162     6398   4430   3879   -441   -465    340       C  
ATOM   1337  C   TRP A 162      12.579 -37.796  -6.755  1.00 39.56           C  
ANISOU 1337  C   TRP A 162     6598   4441   3992   -380   -524    365       C  
ATOM   1338  O   TRP A 162      13.797 -37.888  -6.606  1.00 39.54           O  
ANISOU 1338  O   TRP A 162     6603   4399   4021   -287   -585    386       O  
ATOM   1339  CB  TRP A 162      11.972 -35.431  -7.265  1.00 37.62           C  
ANISOU 1339  CB  TRP A 162     6111   4360   3822   -374   -427    306       C  
ATOM   1340  CG  TRP A 162      11.609 -35.732  -8.675  1.00 37.63           C  
ANISOU 1340  CG  TRP A 162     6078   4361   3858   -350   -400    287       C  
ATOM   1341  CD1 TRP A 162      10.353 -35.810  -9.205  1.00 36.42           C  
ANISOU 1341  CD1 TRP A 162     5906   4244   3687   -424   -349    264       C  
ATOM   1342  CD2 TRP A 162      12.518 -35.929  -9.760  1.00 37.53           C  
ANISOU 1342  CD2 TRP A 162     6040   4316   3903   -246   -422    286       C  
ATOM   1343  NE1 TRP A 162      10.427 -36.055 -10.557  1.00 38.77           N  
ANISOU 1343  NE1 TRP A 162     6177   4529   4024   -374   -345    251       N  
ATOM   1344  CE2 TRP A 162      11.745 -36.132 -10.923  1.00 37.03           C  
ANISOU 1344  CE2 TRP A 162     5957   4266   3849   -265   -384    263       C  
ATOM   1345  CE3 TRP A 162      13.916 -35.963  -9.861  1.00 38.17           C  
ANISOU 1345  CE3 TRP A 162     6112   4364   4029   -140   -470    302       C  
ATOM   1346  CZ2 TRP A 162      12.323 -36.377 -12.171  1.00 38.32           C  
ANISOU 1346  CZ2 TRP A 162     6101   4403   4054   -182   -388    254       C  
ATOM   1347  CZ3 TRP A 162      14.492 -36.193 -11.107  1.00 36.75           C  
ANISOU 1347  CZ3 TRP A 162     5901   4165   3898    -54   -467    291       C  
ATOM   1348  CH2 TRP A 162      13.696 -36.401 -12.244  1.00 37.46           C  
ANISOU 1348  CH2 TRP A 162     5983   4262   3987    -77   -425    267       C  
ATOM   1349  N   SER A 163      11.836 -38.740  -7.324  1.00 40.73           N  
ANISOU 1349  N   SER A 163     6816   4551   4111   -432   -509    363       N  
ATOM   1350  CA  SER A 163      12.408 -39.987  -7.809  1.00 41.03           C  
ANISOU 1350  CA  SER A 163     6961   4483   4144   -379   -561    382       C  
ATOM   1351  C   SER A 163      12.451 -39.988  -9.327  1.00 40.78           C  
ANISOU 1351  C   SER A 163     6867   4458   4169   -314   -534    352       C  
ATOM   1352  O   SER A 163      11.410 -39.939  -9.985  1.00 41.60           O  
ANISOU 1352  O   SER A 163     6943   4599   4263   -382   -484    328       O  
ATOM   1353  CB  SER A 163      11.598 -41.176  -7.295  1.00 40.93           C  
ANISOU 1353  CB  SER A 163     7106   4403   4042   -493   -572    404       C  
ATOM   1354  OG  SER A 163      12.028 -42.372  -7.916  1.00 45.89           O  
ANISOU 1354  OG  SER A 163     7845   4924   4666   -442   -616    416       O  
ATOM   1355  N   ILE A 164      13.660 -40.038  -9.877  1.00 40.91           N  
ANISOU 1355  N   ILE A 164     6858   4442   4243   -183   -567    354       N  
ATOM   1356  CA  ILE A 164      13.848 -40.059 -11.323  1.00 41.55           C  
ANISOU 1356  CA  ILE A 164     6889   4525   4374   -113   -541    325       C  
ATOM   1357  C   ILE A 164      13.327 -41.370 -11.915  1.00 43.91           C  
ANISOU 1357  C   ILE A 164     7319   4737   4627   -148   -548    323       C  
ATOM   1358  O   ILE A 164      12.891 -41.405 -13.071  1.00 44.29           O  
ANISOU 1358  O   ILE A 164     7342   4798   4688   -149   -512    294       O  
ATOM   1359  CB  ILE A 164      15.334 -39.779 -11.742  1.00 40.94           C  
ANISOU 1359  CB  ILE A 164     6744   4442   4369     37   -567    326       C  
ATOM   1360  CG1 ILE A 164      15.456 -39.599 -13.267  1.00 42.20           C  
ANISOU 1360  CG1 ILE A 164     6837   4622   4574     99   -522    292       C  
ATOM   1361  CG2 ILE A 164      16.279 -40.881 -11.244  1.00 42.15           C  
ANISOU 1361  CG2 ILE A 164     7011   4494   4510    110   -640    356       C  
ATOM   1362  CD1 ILE A 164      16.742 -38.900 -13.726  1.00 40.93           C  
ANISOU 1362  CD1 ILE A 164     6562   4498   4490    222   -521    286       C  
ATOM   1363  N   GLU A 165      13.353 -42.434 -11.112  1.00 45.10           N  
ANISOU 1363  N   GLU A 165     7619   4797   4719   -182   -598    354       N  
ATOM   1364  CA  GLU A 165      12.895 -43.750 -11.555  1.00 47.32           C  
ANISOU 1364  CA  GLU A 165     8051   4980   4949   -223   -614    356       C  
ATOM   1365  C   GLU A 165      11.396 -43.730 -11.812  1.00 45.78           C  
ANISOU 1365  C   GLU A 165     7854   4831   4710   -373   -564    339       C  
ATOM   1366  O   GLU A 165      10.931 -44.220 -12.848  1.00 46.40           O  
ANISOU 1366  O   GLU A 165     7966   4885   4781   -392   -548    316       O  
ATOM   1367  CB  GLU A 165      13.244 -44.847 -10.533  1.00 51.23           C  
ANISOU 1367  CB  GLU A 165     8717   5361   5386   -233   -684    398       C  
ATOM   1368  CG  GLU A 165      14.734 -44.974 -10.204  1.00 58.29           C  
ANISOU 1368  CG  GLU A 165     9618   6206   6324    -80   -748    419       C  
ATOM   1369  CD  GLU A 165      15.208 -43.988  -9.124  1.00 64.93           C  
ANISOU 1369  CD  GLU A 165    10366   7121   7184    -71   -765    440       C  
ATOM   1370  OE1 GLU A 165      14.635 -42.879  -8.998  1.00 65.15           O  
ANISOU 1370  OE1 GLU A 165    10273   7257   7224   -136   -711    423       O  
ATOM   1371  OE2 GLU A 165      16.168 -44.322  -8.397  1.00 68.96           O  
ANISOU 1371  OE2 GLU A 165    10928   7578   7697      3   -837    473       O  
ATOM   1372  N   ILE A 166      10.648 -43.157 -10.869  1.00 44.55           N  
ANISOU 1372  N   ILE A 166     7657   4746   4523   -478   -539    348       N  
ATOM   1373  CA  ILE A 166       9.187 -43.061 -10.984  1.00 43.66           C  
ANISOU 1373  CA  ILE A 166     7521   4697   4372   -623   -488    332       C  
ATOM   1374  C   ILE A 166       8.788 -42.083 -12.100  1.00 41.69           C  
ANISOU 1374  C   ILE A 166     7114   4544   4181   -597   -437    292       C  
ATOM   1375  O   ILE A 166       7.807 -42.304 -12.804  1.00 41.31           O  
ANISOU 1375  O   ILE A 166     7059   4520   4115   -676   -411    273       O  
ATOM   1376  CB  ILE A 166       8.525 -42.679  -9.631  1.00 43.96           C  
ANISOU 1376  CB  ILE A 166     7552   4792   4361   -735   -467    349       C  
ATOM   1377  CG1 ILE A 166       8.672 -43.828  -8.629  1.00 43.00           C  
ANISOU 1377  CG1 ILE A 166     7615   4565   4160   -793   -517    392       C  
ATOM   1378  CG2 ILE A 166       7.049 -42.343  -9.817  1.00 44.31           C  
ANISOU 1378  CG2 ILE A 166     7522   4929   4382   -866   -403    325       C  
ATOM   1379  CD1 ILE A 166       8.338 -43.448  -7.197  1.00 44.82           C  
ANISOU 1379  CD1 ILE A 166     7853   4838   4338   -879   -504    413       C  
ATOM   1380  N   ALA A 167       9.575 -41.024 -12.262  1.00 38.80           N  
ANISOU 1380  N   ALA A 167     6628   4232   3883   -489   -428    281       N  
ATOM   1381  CA  ALA A 167       9.338 -40.030 -13.285  1.00 38.53           C  
ANISOU 1381  CA  ALA A 167     6454   4281   3905   -454   -385    248       C  
ATOM   1382  C   ALA A 167       9.455 -40.600 -14.710  1.00 40.40           C  
ANISOU 1382  C   ALA A 167     6723   4473   4154   -409   -389    229       C  
ATOM   1383  O   ALA A 167       8.752 -40.148 -15.619  1.00 39.97           O  
ANISOU 1383  O   ALA A 167     6595   4478   4115   -435   -358    204       O  
ATOM   1384  CB  ALA A 167      10.279 -38.849 -13.095  1.00 36.61           C  
ANISOU 1384  CB  ALA A 167     6096   4088   3724   -352   -381    247       C  
ATOM   1385  N   ALA A 168      10.335 -41.582 -14.900  1.00 40.85           N  
ANISOU 1385  N   ALA A 168     6892   4425   4203   -338   -429    240       N  
ATOM   1386  CA  ALA A 168      10.506 -42.219 -16.210  1.00 44.31           C  
ANISOU 1386  CA  ALA A 168     7381   4809   4644   -291   -431    218       C  
ATOM   1387  C   ALA A 168       9.404 -43.225 -16.544  1.00 46.54           C  
ANISOU 1387  C   ALA A 168     7776   5045   4860   -412   -436    212       C  
ATOM   1388  O   ALA A 168       9.095 -43.440 -17.722  1.00 48.87           O  
ANISOU 1388  O   ALA A 168     8083   5334   5153   -413   -425    186       O  
ATOM   1389  CB  ALA A 168      11.873 -42.887 -16.312  1.00 45.53           C  
ANISOU 1389  CB  ALA A 168     7612   4870   4819   -159   -467    226       C  
ATOM   1390  N   LYS A 169       8.819 -43.837 -15.514  1.00 47.38           N  
ANISOU 1390  N   LYS A 169     7972   5121   4910   -520   -455    237       N  
ATOM   1391  CA  LYS A 169       7.801 -44.879 -15.696  1.00 48.00           C  
ANISOU 1391  CA  LYS A 169     8171   5149   4919   -651   -465    237       C  
ATOM   1392  C   LYS A 169       6.545 -44.327 -16.347  1.00 47.46           C  
ANISOU 1392  C   LYS A 169     7998   5184   4850   -751   -426    212       C  
ATOM   1393  O   LYS A 169       6.247 -43.131 -16.231  1.00 47.48           O  
ANISOU 1393  O   LYS A 169     7843   5301   4894   -746   -390    203       O  
ATOM   1394  CB  LYS A 169       7.460 -45.568 -14.367  1.00 48.64           C  
ANISOU 1394  CB  LYS A 169     8364   5183   4934   -755   -488    274       C  
ATOM   1395  CG  LYS A 169       8.616 -46.349 -13.762  1.00 52.41           C  
ANISOU 1395  CG  LYS A 169     8977   5537   5399   -665   -544    303       C  
ATOM   1396  CD  LYS A 169       8.151 -47.481 -12.852  1.00 56.88           C  
ANISOU 1396  CD  LYS A 169     9722   6012   5878   -785   -579    339       C  
ATOM   1397  CE  LYS A 169       9.321 -48.408 -12.514  1.00 60.61           C  
ANISOU 1397  CE  LYS A 169    10350   6339   6339   -676   -646    365       C  
ATOM   1398  NZ  LYS A 169       8.902 -49.795 -12.131  1.00 64.66           N  
ANISOU 1398  NZ  LYS A 169    11083   6723   6763   -779   -689    392       N  
ATOM   1399  N   LEU A 170       5.819 -45.198 -17.043  1.00 49.34           N  
ANISOU 1399  N   LEU A 170     8327   5379   5041   -839   -439    201       N  
ATOM   1400  CA  LEU A 170       4.561 -44.817 -17.692  1.00 49.70           C  
ANISOU 1400  CA  LEU A 170     8282   5519   5081   -944   -414    179       C  
ATOM   1401  C   LEU A 170       3.533 -44.377 -16.661  1.00 47.94           C  
ANISOU 1401  C   LEU A 170     7979   5394   4841  -1070   -385    192       C  
ATOM   1402  O   LEU A 170       3.555 -44.844 -15.520  1.00 49.47           O  
ANISOU 1402  O   LEU A 170     8251   5550   4994  -1127   -391    220       O  
ATOM   1403  CB  LEU A 170       3.991 -45.992 -18.488  1.00 51.51           C  
ANISOU 1403  CB  LEU A 170     8649   5671   5253  -1034   -444    169       C  
ATOM   1404  CG  LEU A 170       4.812 -46.642 -19.602  1.00 55.01           C  
ANISOU 1404  CG  LEU A 170     9202   6006   5694   -932   -469    149       C  
ATOM   1405  CD1 LEU A 170       4.001 -47.783 -20.194  1.00 59.36           C  
ANISOU 1405  CD1 LEU A 170     9894   6488   6174  -1058   -499    139       C  
ATOM   1406  CD2 LEU A 170       5.215 -45.644 -20.683  1.00 53.91           C  
ANISOU 1406  CD2 LEU A 170     8933   5935   5615   -817   -445    120       C  
ATOM   1407  N   GLN A 171       2.629 -43.489 -17.062  1.00 47.29           N  
ANISOU 1407  N   GLN A 171     7743   5437   4787  -1112   -353    171       N  
ATOM   1408  CA  GLN A 171       1.539 -43.060 -16.182  1.00 49.55           C  
ANISOU 1408  CA  GLN A 171     7939   5829   5059  -1231   -317    176       C  
ATOM   1409  C   GLN A 171       0.724 -44.248 -15.669  1.00 48.47           C  
ANISOU 1409  C   GLN A 171     7924   5651   4841  -1401   -327    194       C  
ATOM   1410  O   GLN A 171       0.197 -44.219 -14.561  1.00 48.08           O  
ANISOU 1410  O   GLN A 171     7862   5645   4760  -1494   -299    209       O  
ATOM   1411  CB  GLN A 171       0.631 -42.042 -16.876  1.00 51.02           C  
ANISOU 1411  CB  GLN A 171     7947   6149   5289  -1244   -289    148       C  
ATOM   1412  CG  GLN A 171       1.306 -40.695 -17.122  1.00 58.11           C  
ANISOU 1412  CG  GLN A 171     8716   7101   6262  -1096   -270    135       C  
ATOM   1413  CD  GLN A 171       0.448 -39.509 -16.705  1.00 63.55           C  
ANISOU 1413  CD  GLN A 171     9232   7928   6985  -1118   -226    121       C  
ATOM   1414  OE1 GLN A 171      -0.515 -39.653 -15.943  1.00 68.13           O  
ANISOU 1414  OE1 GLN A 171     9785   8569   7534  -1235   -199    122       O  
ATOM   1415  NE2 GLN A 171       0.808 -38.324 -17.189  1.00 63.14           N  
ANISOU 1415  NE2 GLN A 171     9068   7926   6996  -1005   -215    106       N  
ATOM   1416  N   GLU A 172       0.659 -45.296 -16.482  1.00 47.56           N  
ANISOU 1416  N   GLU A 172     7937   5445   4688  -1442   -368    191       N  
ATOM   1417  CA  GLU A 172      -0.071 -46.509 -16.162  1.00 48.95           C  
ANISOU 1417  CA  GLU A 172     8251   5565   4784  -1609   -386    208       C  
ATOM   1418  C   GLU A 172       0.682 -47.355 -15.130  1.00 49.54           C  
ANISOU 1418  C   GLU A 172     8501   5512   4808  -1605   -409    244       C  
ATOM   1419  O   GLU A 172       0.131 -48.301 -14.568  1.00 50.66           O  
ANISOU 1419  O   GLU A 172     8767   5604   4876  -1751   -420    267       O  
ATOM   1420  CB  GLU A 172      -0.324 -47.307 -17.449  1.00 51.56           C  
ANISOU 1420  CB  GLU A 172     8671   5831   5090  -1645   -427    189       C  
ATOM   1421  CG  GLU A 172      -1.343 -46.668 -18.409  1.00 54.25           C  
ANISOU 1421  CG  GLU A 172     8856   6298   5459  -1696   -417    160       C  
ATOM   1422  CD  GLU A 172      -0.771 -45.559 -19.293  1.00 58.88           C  
ANISOU 1422  CD  GLU A 172     9314   6936   6121  -1532   -409    135       C  
ATOM   1423  OE1 GLU A 172      -1.551 -44.947 -20.064  1.00 58.48           O  
ANISOU 1423  OE1 GLU A 172     9135   6988   6097  -1558   -406    114       O  
ATOM   1424  OE2 GLU A 172       0.451 -45.299 -19.231  1.00 59.32           O  
ANISOU 1424  OE2 GLU A 172     9398   6932   6211  -1380   -408    138       O  
ATOM   1425  N   GLN A 173       1.946 -47.016 -14.891  1.00 47.95           N  
ANISOU 1425  N   GLN A 173     8311   5261   4647  -1442   -420    251       N  
ATOM   1426  CA  GLN A 173       2.730 -47.641 -13.827  1.00 49.36           C  
ANISOU 1426  CA  GLN A 173     8634   5333   4788  -1419   -448    288       C  
ATOM   1427  C   GLN A 173       2.785 -46.748 -12.591  1.00 46.82           C  
ANISOU 1427  C   GLN A 173     8213   5097   4479  -1414   -412    304       C  
ATOM   1428  O   GLN A 173       3.525 -47.029 -11.652  1.00 47.27           O  
ANISOU 1428  O   GLN A 173     8364   5084   4514  -1376   -437    335       O  
ATOM   1429  CB  GLN A 173       4.154 -47.918 -14.302  1.00 50.95           C  
ANISOU 1429  CB  GLN A 173     8916   5420   5023  -1238   -491    287       C  
ATOM   1430  CG  GLN A 173       4.323 -49.135 -15.198  1.00 56.29           C  
ANISOU 1430  CG  GLN A 173     9764   5960   5662  -1237   -535    279       C  
ATOM   1431  CD  GLN A 173       5.740 -49.238 -15.723  1.00 59.09           C  
ANISOU 1431  CD  GLN A 173    10161   6226   6062  -1039   -564    270       C  
ATOM   1432  OE1 GLN A 173       6.149 -48.470 -16.605  1.00 58.50           O  
ANISOU 1432  OE1 GLN A 173     9966   6210   6053   -929   -542    240       O  
ATOM   1433  NE2 GLN A 173       6.508 -50.176 -15.170  1.00 57.61           N  
ANISOU 1433  NE2 GLN A 173    10146   5900   5842   -991   -612    297       N  
ATOM   1434  N   GLY A 174       2.002 -45.674 -12.597  1.00 44.91           N  
ANISOU 1434  N   GLY A 174     7787   5004   4272  -1449   -357    281       N  
ATOM   1435  CA  GLY A 174       2.027 -44.698 -11.511  1.00 45.19           C  
ANISOU 1435  CA  GLY A 174     7719   5128   4323  -1435   -316    287       C  
ATOM   1436  C   GLY A 174       3.096 -43.640 -11.720  1.00 43.92           C  
ANISOU 1436  C   GLY A 174     7457   4988   4242  -1256   -318    274       C  
ATOM   1437  O   GLY A 174       3.328 -42.802 -10.846  1.00 43.40           O  
ANISOU 1437  O   GLY A 174     7319   4979   4191  -1223   -293    277       O  
ATOM   1438  N   GLY A 175       3.740 -43.681 -12.884  1.00 44.23           N  
ANISOU 1438  N   GLY A 175     7495   4983   4328  -1145   -345    258       N  
ATOM   1439  CA  GLY A 175       4.846 -42.778 -13.197  1.00 42.45           C  
ANISOU 1439  CA  GLY A 175     7183   4769   4175   -979   -349    248       C  
ATOM   1440  C   GLY A 175       4.395 -41.454 -13.775  1.00 41.28           C  
ANISOU 1440  C   GLY A 175     6848   4747   4089   -947   -306    217       C  
ATOM   1441  O   GLY A 175       3.205 -41.165 -13.823  1.00 41.04           O  
ANISOU 1441  O   GLY A 175     6740   4805   4048  -1046   -272    202       O  
ATOM   1442  N   ASP A 176       5.354 -40.653 -14.224  1.00 41.39           N  
ANISOU 1442  N   ASP A 176     6789   4770   4167   -808   -308    207       N  
ATOM   1443  CA  ASP A 176       5.071 -39.308 -14.701  1.00 43.46           C  
ANISOU 1443  CA  ASP A 176     6885   5139   4487   -764   -272    182       C  
ATOM   1444  C   ASP A 176       5.325 -39.185 -16.193  1.00 44.92           C  
ANISOU 1444  C   ASP A 176     7041   5316   4709   -692   -281    161       C  
ATOM   1445  O   ASP A 176       5.025 -38.152 -16.797  1.00 44.51           O  
ANISOU 1445  O   ASP A 176     6866   5345   4702   -659   -258    142       O  
ATOM   1446  CB  ASP A 176       5.917 -38.286 -13.942  1.00 42.53           C  
ANISOU 1446  CB  ASP A 176     6700   5050   4410   -677   -263    188       C  
ATOM   1447  CG  ASP A 176       5.704 -38.353 -12.439  1.00 46.20           C  
ANISOU 1447  CG  ASP A 176     7201   5523   4830   -748   -254    206       C  
ATOM   1448  OD1 ASP A 176       4.539 -38.464 -11.994  1.00 47.16           O  
ANISOU 1448  OD1 ASP A 176     7310   5698   4912   -865   -222    201       O  
ATOM   1449  OD2 ASP A 176       6.704 -38.286 -11.701  1.00 47.53           O  
ANISOU 1449  OD2 ASP A 176     7408   5648   5001   -687   -279    226       O  
ATOM   1450  N   GLU A 177       5.896 -40.239 -16.774  1.00 47.65           N  
ANISOU 1450  N   GLU A 177     7510   5561   5035   -663   -314    166       N  
ATOM   1451  CA  GLU A 177       6.074 -40.332 -18.215  1.00 50.04           C  
ANISOU 1451  CA  GLU A 177     7814   5846   5355   -609   -320    145       C  
ATOM   1452  C   GLU A 177       6.882 -39.131 -18.726  1.00 47.74           C  
ANISOU 1452  C   GLU A 177     7406   5601   5131   -485   -301    134       C  
ATOM   1453  O   GLU A 177       6.581 -38.564 -19.778  1.00 48.79           O  
ANISOU 1453  O   GLU A 177     7470   5781   5285   -467   -289    115       O  
ATOM   1454  CB  GLU A 177       4.700 -40.410 -18.887  1.00 52.24           C  
ANISOU 1454  CB  GLU A 177     8060   6180   5609   -719   -314    128       C  
ATOM   1455  CG  GLU A 177       4.601 -41.283 -20.116  1.00 57.50           C  
ANISOU 1455  CG  GLU A 177     8820   6783   6245   -731   -339    112       C  
ATOM   1456  CD  GLU A 177       3.154 -41.418 -20.577  1.00 64.41           C  
ANISOU 1456  CD  GLU A 177     9662   7719   7090   -863   -343    100       C  
ATOM   1457  OE1 GLU A 177       2.777 -40.742 -21.564  1.00 65.23           O  
ANISOU 1457  OE1 GLU A 177     9678   7888   7219   -844   -340     81       O  
ATOM   1458  OE2 GLU A 177       2.387 -42.175 -19.931  1.00 64.65           O  
ANISOU 1458  OE2 GLU A 177     9753   7739   7071   -990   -351    111       O  
ATOM   1459  N   VAL A 178       7.889 -38.735 -17.948  1.00 46.42           N  
ANISOU 1459  N   VAL A 178     7222   5423   4994   -408   -303    150       N  
ATOM   1460  CA  VAL A 178       8.908 -37.783 -18.397  1.00 43.66           C  
ANISOU 1460  CA  VAL A 178     6786   5098   4704   -289   -290    144       C  
ATOM   1461  C   VAL A 178       9.636 -38.433 -19.578  1.00 43.55           C  
ANISOU 1461  C   VAL A 178     6837   5019   4693   -213   -298    132       C  
ATOM   1462  O   VAL A 178      10.194 -39.523 -19.427  1.00 43.86           O  
ANISOU 1462  O   VAL A 178     6990   4966   4707   -188   -324    140       O  
ATOM   1463  CB  VAL A 178       9.899 -37.433 -17.259  1.00 41.66           C  
ANISOU 1463  CB  VAL A 178     6518   4837   4475   -232   -301    165       C  
ATOM   1464  CG1 VAL A 178      11.042 -36.573 -17.763  1.00 40.25           C  
ANISOU 1464  CG1 VAL A 178     6257   4678   4356   -117   -291    161       C  
ATOM   1465  CG2 VAL A 178       9.174 -36.721 -16.131  1.00 41.55           C  
ANISOU 1465  CG2 VAL A 178     6446   4890   4453   -305   -286    171       C  
ATOM   1466  N   PRO A 179       9.607 -37.784 -20.762  1.00 42.94           N  
ANISOU 1466  N   PRO A 179     6693   4983   4639   -176   -276    113       N  
ATOM   1467  CA  PRO A 179      10.088 -38.417 -22.003  1.00 41.02           C  
ANISOU 1467  CA  PRO A 179     6518   4683   4384   -121   -275     95       C  
ATOM   1468  C   PRO A 179      11.491 -38.990 -21.826  1.00 42.18           C  
ANISOU 1468  C   PRO A 179     6722   4757   4548    -14   -282    101       C  
ATOM   1469  O   PRO A 179      12.365 -38.310 -21.279  1.00 42.85           O  
ANISOU 1469  O   PRO A 179     6732   4869   4679     53   -277    114       O  
ATOM   1470  CB  PRO A 179      10.106 -37.262 -23.001  1.00 40.15           C  
ANISOU 1470  CB  PRO A 179     6302   4645   4308    -83   -245     81       C  
ATOM   1471  CG  PRO A 179       9.126 -36.268 -22.471  1.00 43.11           C  
ANISOU 1471  CG  PRO A 179     6576   5107   4697   -151   -240     87       C  
ATOM   1472  CD  PRO A 179       9.223 -36.375 -20.975  1.00 42.91           C  
ANISOU 1472  CD  PRO A 179     6555   5076   4674   -175   -250    106       C  
ATOM   1473  N   SER A 180      11.694 -40.232 -22.265  1.00 43.43           N  
ANISOU 1473  N   SER A 180     7011   4822   4669      3   -298     91       N  
ATOM   1474  CA  SER A 180      12.965 -40.950 -22.061  1.00 45.59           C  
ANISOU 1474  CA  SER A 180     7350   5016   4956    111   -311     95       C  
ATOM   1475  C   SER A 180      14.205 -40.214 -22.592  1.00 45.28           C  
ANISOU 1475  C   SER A 180     7215   5015   4976    237   -279     87       C  
ATOM   1476  O   SER A 180      15.290 -40.328 -22.022  1.00 46.14           O  
ANISOU 1476  O   SER A 180     7311   5102   5119    324   -291    100       O  
ATOM   1477  CB  SER A 180      12.895 -42.373 -22.648  1.00 47.77           C  
ANISOU 1477  CB  SER A 180     7791   5181   5178    113   -329     78       C  
ATOM   1478  OG  SER A 180      12.816 -42.358 -24.065  1.00 48.49           O  
ANISOU 1478  OG  SER A 180     7893   5275   5256    134   -299     44       O  
ATOM   1479  N   GLU A 181      14.038 -39.447 -23.665  1.00 43.99           N  
ANISOU 1479  N   GLU A 181     6981   4911   4823    241   -240     67       N  
ATOM   1480  CA  GLU A 181      15.169 -38.754 -24.281  1.00 44.44           C  
ANISOU 1480  CA  GLU A 181     6951   5005   4927    345   -201     59       C  
ATOM   1481  C   GLU A 181      15.771 -37.615 -23.433  1.00 41.86           C  
ANISOU 1481  C   GLU A 181     6494   4751   4660    369   -199     83       C  
ATOM   1482  O   GLU A 181      16.810 -37.064 -23.794  1.00 42.70           O  
ANISOU 1482  O   GLU A 181     6524   4890   4810    450   -170     81       O  
ATOM   1483  CB  GLU A 181      14.827 -38.280 -25.711  1.00 45.40           C  
ANISOU 1483  CB  GLU A 181     7052   5163   5032    336   -160     34       C  
ATOM   1484  CG  GLU A 181      13.838 -37.106 -25.812  1.00 46.80           C  
ANISOU 1484  CG  GLU A 181     7140   5426   5215    253   -156     42       C  
ATOM   1485  CD  GLU A 181      12.378 -37.534 -25.784  1.00 46.46           C  
ANISOU 1485  CD  GLU A 181     7155   5376   5123    139   -186     39       C  
ATOM   1486  OE1 GLU A 181      12.093 -38.719 -25.512  1.00 49.93           O  
ANISOU 1486  OE1 GLU A 181     7707   5742   5522    107   -213     36       O  
ATOM   1487  OE2 GLU A 181      11.508 -36.678 -26.041  1.00 46.41           O  
ANISOU 1487  OE2 GLU A 181     7080   5437   5117     80   -185     41       O  
ATOM   1488  N   ILE A 182      15.127 -37.261 -22.325  1.00 38.47           N  
ANISOU 1488  N   ILE A 182     6041   4347   4230    295   -227    105       N  
ATOM   1489  CA  ILE A 182      15.683 -36.241 -21.435  1.00 37.90           C  
ANISOU 1489  CA  ILE A 182     5862   4331   4205    313   -231    126       C  
ATOM   1490  C   ILE A 182      16.063 -36.748 -20.037  1.00 39.15           C  
ANISOU 1490  C   ILE A 182     6058   4452   4364    317   -278    151       C  
ATOM   1491  O   ILE A 182      16.705 -36.027 -19.273  1.00 40.89           O  
ANISOU 1491  O   ILE A 182     6203   4711   4623    340   -289    168       O  
ATOM   1492  CB  ILE A 182      14.781 -34.970 -21.325  1.00 36.98           C  
ANISOU 1492  CB  ILE A 182     5658   4297   4097    238   -215    127       C  
ATOM   1493  CG1 ILE A 182      13.578 -35.221 -20.405  1.00 35.15           C  
ANISOU 1493  CG1 ILE A 182     5465   4063   3827    137   -239    135       C  
ATOM   1494  CG2 ILE A 182      14.368 -34.469 -22.721  1.00 34.20           C  
ANISOU 1494  CG2 ILE A 182     5277   3977   3739    234   -179    107       C  
ATOM   1495  CD1 ILE A 182      12.999 -33.947 -19.801  1.00 32.76           C  
ANISOU 1495  CD1 ILE A 182     5068   3837   3543     89   -229    140       C  
ATOM   1496  N   ILE A 183      15.683 -37.986 -19.716  1.00 40.38           N  
ANISOU 1496  N   ILE A 183     6338   4529   4474    290   -309    154       N  
ATOM   1497  CA  ILE A 183      15.978 -38.580 -18.407  1.00 42.63           C  
ANISOU 1497  CA  ILE A 183     6684   4767   4747    287   -360    182       C  
ATOM   1498  C   ILE A 183      17.464 -38.478 -18.026  1.00 44.15           C  
ANISOU 1498  C   ILE A 183     6828   4955   4991    401   -382    196       C  
ATOM   1499  O   ILE A 183      17.800 -38.071 -16.909  1.00 45.10           O  
ANISOU 1499  O   ILE A 183     6913   5097   5126    394   -415    221       O  
ATOM   1500  CB  ILE A 183      15.501 -40.062 -18.327  1.00 43.71           C  
ANISOU 1500  CB  ILE A 183     6984   4801   4824    254   -391    183       C  
ATOM   1501  CG1 ILE A 183      13.968 -40.141 -18.294  1.00 44.13           C  
ANISOU 1501  CG1 ILE A 183     7075   4869   4823    115   -381    179       C  
ATOM   1502  CG2 ILE A 183      16.106 -40.770 -17.120  1.00 41.70           C  
ANISOU 1502  CG2 ILE A 183     6805   4481   4560    282   -449    215       C  
ATOM   1503  CD1 ILE A 183      13.307 -39.501 -17.060  1.00 46.82           C  
ANISOU 1503  CD1 ILE A 183     7371   5266   5153     24   -387    199       C  
ATOM   1504  N   ASP A 184      18.340 -38.833 -18.963  1.00 44.53           N  
ANISOU 1504  N   ASP A 184     6871   4981   5066    504   -363    178       N  
ATOM   1505  CA  ASP A 184      19.780 -38.824 -18.735  1.00 44.10           C  
ANISOU 1505  CA  ASP A 184     6760   4930   5066    620   -380    188       C  
ATOM   1506  C   ASP A 184      20.324 -37.397 -18.688  1.00 41.73           C  
ANISOU 1506  C   ASP A 184     6302   4733   4822    628   -356    193       C  
ATOM   1507  O   ASP A 184      21.494 -37.192 -18.387  1.00 43.34           O  
ANISOU 1507  O   ASP A 184     6434   4960   5075    706   -374    204       O  
ATOM   1508  CB  ASP A 184      20.508 -39.625 -19.830  1.00 46.87           C  
ANISOU 1508  CB  ASP A 184     7147   5233   5427    731   -354    161       C  
ATOM   1509  CG  ASP A 184      20.065 -41.093 -19.897  1.00 52.18           C  
ANISOU 1509  CG  ASP A 184     7994   5788   6043    731   -383    154       C  
ATOM   1510  OD1 ASP A 184      20.034 -41.771 -18.850  1.00 55.19           O  
ANISOU 1510  OD1 ASP A 184     8460   6107   6403    720   -445    180       O  
ATOM   1511  OD2 ASP A 184      19.757 -41.578 -21.009  1.00 55.44           O  
ANISOU 1511  OD2 ASP A 184     8469   6167   6429    740   -345    121       O  
ATOM   1512  N   LYS A 185      19.473 -36.420 -18.989  1.00 39.54           N  
ANISOU 1512  N   LYS A 185     5972   4516   4536    545   -320    185       N  
ATOM   1513  CA  LYS A 185      19.873 -35.008 -19.042  1.00 36.42           C  
ANISOU 1513  CA  LYS A 185     5443   4208   4185    541   -295    188       C  
ATOM   1514  C   LYS A 185      19.436 -34.202 -17.811  1.00 36.02           C  
ANISOU 1514  C   LYS A 185     5361   4194   4132    464   -324    208       C  
ATOM   1515  O   LYS A 185      19.594 -32.983 -17.774  1.00 34.94           O  
ANISOU 1515  O   LYS A 185     5129   4121   4024    446   -307    210       O  
ATOM   1516  CB  LYS A 185      19.333 -34.356 -20.316  1.00 35.48           C  
ANISOU 1516  CB  LYS A 185     5288   4131   4063    515   -234    164       C  
ATOM   1517  CG  LYS A 185      19.926 -34.931 -21.591  1.00 38.91           C  
ANISOU 1517  CG  LYS A 185     5740   4544   4501    594   -194    141       C  
ATOM   1518  CD  LYS A 185      19.273 -34.367 -22.838  1.00 35.99           C  
ANISOU 1518  CD  LYS A 185     5358   4207   4112    558   -141    121       C  
ATOM   1519  CE  LYS A 185      19.921 -34.970 -24.080  1.00 42.52           C  
ANISOU 1519  CE  LYS A 185     6211   5011   4934    636    -97     95       C  
ATOM   1520  NZ  LYS A 185      19.750 -34.123 -25.294  1.00 44.12           N  
ANISOU 1520  NZ  LYS A 185     6370   5264   5129    618    -41     81       N  
ATOM   1521  N   ILE A 186      18.895 -34.887 -16.807  1.00 36.00           N  
ANISOU 1521  N   ILE A 186     5446   4145   4089    418   -367    223       N  
ATOM   1522  CA  ILE A 186      18.444 -34.230 -15.584  1.00 36.04           C  
ANISOU 1522  CA  ILE A 186     5437   4179   4079    344   -391    239       C  
ATOM   1523  C   ILE A 186      19.511 -34.275 -14.489  1.00 36.78           C  
ANISOU 1523  C   ILE A 186     5518   4264   4192    386   -450    266       C  
ATOM   1524  O   ILE A 186      20.046 -35.334 -14.155  1.00 35.69           O  
ANISOU 1524  O   ILE A 186     5451   4065   4046    436   -496    281       O  
ATOM   1525  CB  ILE A 186      17.103 -34.821 -15.070  1.00 35.75           C  
ANISOU 1525  CB  ILE A 186     5497   4109   3976    249   -396    239       C  
ATOM   1526  CG1 ILE A 186      15.985 -34.548 -16.085  1.00 34.19           C  
ANISOU 1526  CG1 ILE A 186     5287   3939   3763    198   -344    213       C  
ATOM   1527  CG2 ILE A 186      16.756 -34.256 -13.693  1.00 35.10           C  
ANISOU 1527  CG2 ILE A 186     5412   4053   3873    181   -419    255       C  
ATOM   1528  CD1 ILE A 186      14.709 -35.337 -15.857  1.00 33.84           C  
ANISOU 1528  CD1 ILE A 186     5335   3863   3658    107   -346    210       C  
ATOM   1529  N   ILE A 187      19.819 -33.100 -13.957  1.00 35.91           N  
ANISOU 1529  N   ILE A 187     5322   4213   4108    365   -454    272       N  
ATOM   1530  CA  ILE A 187      20.721 -32.964 -12.838  1.00 34.43           C  
ANISOU 1530  CA  ILE A 187     5117   4029   3934    385   -516    298       C  
ATOM   1531  C   ILE A 187      19.854 -32.458 -11.703  1.00 34.22           C  
ANISOU 1531  C   ILE A 187     5128   4015   3861    287   -527    304       C  
ATOM   1532  O   ILE A 187      19.393 -31.314 -11.720  1.00 34.21           O  
ANISOU 1532  O   ILE A 187     5068   4066   3865    239   -491    289       O  
ATOM   1533  CB  ILE A 187      21.916 -32.019 -13.178  1.00 35.51           C  
ANISOU 1533  CB  ILE A 187     5126   4228   4139    438   -512    299       C  
ATOM   1534  CG1 ILE A 187      22.744 -32.639 -14.319  1.00 35.55           C  
ANISOU 1534  CG1 ILE A 187     5098   4223   4185    538   -491    291       C  
ATOM   1535  CG2 ILE A 187      22.779 -31.761 -11.939  1.00 35.18           C  
ANISOU 1535  CG2 ILE A 187     5061   4198   4109    442   -585    327       C  
ATOM   1536  CD1 ILE A 187      23.985 -31.873 -14.731  1.00 40.18           C  
ANISOU 1536  CD1 ILE A 187     5554   4874   4838    592   -481    292       C  
ATOM   1537  N   TYR A 188      19.609 -33.340 -10.736  1.00 33.66           N  
ANISOU 1537  N   TYR A 188     5161   3890   3739    259   -573    324       N  
ATOM   1538  CA  TYR A 188      18.626 -33.107  -9.696  1.00 34.21           C  
ANISOU 1538  CA  TYR A 188     5287   3964   3748    159   -573    326       C  
ATOM   1539  C   TYR A 188      19.277 -32.689  -8.381  1.00 36.03           C  
ANISOU 1539  C   TYR A 188     5519   4202   3967    146   -633    349       C  
ATOM   1540  O   TYR A 188      20.148 -33.388  -7.866  1.00 37.40           O  
ANISOU 1540  O   TYR A 188     5734   4335   4141    194   -703    378       O  
ATOM   1541  CB  TYR A 188      17.779 -34.369  -9.493  1.00 35.18           C  
ANISOU 1541  CB  TYR A 188     5538   4021   3807    114   -578    333       C  
ATOM   1542  CG  TYR A 188      16.835 -34.279  -8.311  1.00 38.33           C  
ANISOU 1542  CG  TYR A 188     6004   4424   4135      8   -576    339       C  
ATOM   1543  CD1 TYR A 188      15.703 -33.460  -8.358  1.00 36.04           C  
ANISOU 1543  CD1 TYR A 188     5672   4192   3829    -68   -511    311       C  
ATOM   1544  CD2 TYR A 188      17.078 -35.005  -7.142  1.00 39.21           C  
ANISOU 1544  CD2 TYR A 188     6221   4484   4194    -15   -638    372       C  
ATOM   1545  CE1 TYR A 188      14.831 -33.371  -7.267  1.00 36.05           C  
ANISOU 1545  CE1 TYR A 188     5728   4205   3765   -163   -499    312       C  
ATOM   1546  CE2 TYR A 188      16.209 -34.928  -6.048  1.00 38.41           C  
ANISOU 1546  CE2 TYR A 188     6186   4389   4019   -120   -629    376       C  
ATOM   1547  CZ  TYR A 188      15.091 -34.103  -6.118  1.00 37.26           C  
ANISOU 1547  CZ  TYR A 188     5990   4308   3861   -193   -554    344       C  
ATOM   1548  OH  TYR A 188      14.234 -34.023  -5.042  1.00 33.34           O  
ANISOU 1548  OH  TYR A 188     5552   3825   3291   -293   -534    344       O  
ATOM   1549  N   MET A 189      18.842 -31.558  -7.835  1.00 36.04           N  
ANISOU 1549  N   MET A 189     5483   4254   3955     84   -610    336       N  
ATOM   1550  CA  MET A 189      19.430 -31.021  -6.605  1.00 38.42           C  
ANISOU 1550  CA  MET A 189     5789   4567   4241     62   -665    353       C  
ATOM   1551  C   MET A 189      18.343 -30.632  -5.619  1.00 37.74           C  
ANISOU 1551  C   MET A 189     5763   4492   4084    -38   -639    341       C  
ATOM   1552  O   MET A 189      17.715 -29.591  -5.794  1.00 37.77           O  
ANISOU 1552  O   MET A 189     5714   4543   4094    -72   -582    311       O  
ATOM   1553  CB  MET A 189      20.312 -29.794  -6.899  1.00 39.48           C  
ANISOU 1553  CB  MET A 189     5805   4757   4440     95   -667    345       C  
ATOM   1554  CG  MET A 189      21.464 -30.051  -7.859  1.00 44.72           C  
ANISOU 1554  CG  MET A 189     6391   5426   5177    191   -684    354       C  
ATOM   1555  SD  MET A 189      22.104 -28.552  -8.636  1.00 47.54           S  
ANISOU 1555  SD  MET A 189     6605   5855   5604    205   -648    336       S  
ATOM   1556  CE  MET A 189      20.768 -28.155  -9.776  1.00 39.48           C  
ANISOU 1556  CE  MET A 189     5577   4847   4577    176   -548    301       C  
ATOM   1557  N   PRO A 190      18.107 -31.473  -4.588  1.00 38.93           N  
ANISOU 1557  N   PRO A 190     6029   4598   4164    -82   -679    365       N  
ATOM   1558  CA  PRO A 190      17.157 -31.138  -3.526  1.00 39.02           C  
ANISOU 1558  CA  PRO A 190     6103   4623   4099   -180   -652    354       C  
ATOM   1559  C   PRO A 190      17.771 -30.217  -2.474  1.00 40.06           C  
ANISOU 1559  C   PRO A 190     6228   4778   4216   -199   -694    358       C  
ATOM   1560  O   PRO A 190      18.976 -30.259  -2.241  1.00 39.10           O  
ANISOU 1560  O   PRO A 190     6091   4643   4123   -148   -772    384       O  
ATOM   1561  CB  PRO A 190      16.827 -32.500  -2.911  1.00 40.05           C  
ANISOU 1561  CB  PRO A 190     6369   4689   4158   -219   -684    384       C  
ATOM   1562  CG  PRO A 190      18.048 -33.323  -3.138  1.00 41.21           C  
ANISOU 1562  CG  PRO A 190     6534   4784   4342   -129   -767    419       C  
ATOM   1563  CD  PRO A 190      18.647 -32.839  -4.438  1.00 40.54           C  
ANISOU 1563  CD  PRO A 190     6319   4731   4352    -41   -744    401       C  
ATOM   1564  N   PHE A 191      16.939 -29.404  -1.832  1.00 40.47           N  
ANISOU 1564  N   PHE A 191     6291   4864   4222   -271   -644    330       N  
ATOM   1565  CA  PHE A 191      17.413 -28.460  -0.819  1.00 41.03           C  
ANISOU 1565  CA  PHE A 191     6369   4954   4269   -298   -677    326       C  
ATOM   1566  C   PHE A 191      16.576 -28.520   0.447  1.00 43.25           C  
ANISOU 1566  C   PHE A 191     6757   5231   4446   -391   -657    319       C  
ATOM   1567  O   PHE A 191      15.351 -28.649   0.387  1.00 42.35           O  
ANISOU 1567  O   PHE A 191     6661   5133   4295   -442   -577    295       O  
ATOM   1568  CB  PHE A 191      17.440 -27.032  -1.379  1.00 39.44           C  
ANISOU 1568  CB  PHE A 191     6059   4801   4123   -280   -633    289       C  
ATOM   1569  CG  PHE A 191      18.465 -26.831  -2.457  1.00 38.46           C  
ANISOU 1569  CG  PHE A 191     5834   4686   4093   -200   -660    300       C  
ATOM   1570  CD1 PHE A 191      18.139 -27.046  -3.794  1.00 37.93           C  
ANISOU 1570  CD1 PHE A 191     5705   4628   4080   -156   -608    289       C  
ATOM   1571  CD2 PHE A 191      19.767 -26.456  -2.135  1.00 39.53           C  
ANISOU 1571  CD2 PHE A 191     5936   4825   4260   -172   -737    321       C  
ATOM   1572  CE1 PHE A 191      19.089 -26.871  -4.795  1.00 39.12           C  
ANISOU 1572  CE1 PHE A 191     5765   4789   4310    -85   -624    297       C  
ATOM   1573  CE2 PHE A 191      20.726 -26.287  -3.126  1.00 37.58           C  
ANISOU 1573  CE2 PHE A 191     5587   4594   4097   -103   -754    330       C  
ATOM   1574  CZ  PHE A 191      20.384 -26.497  -4.461  1.00 39.02           C  
ANISOU 1574  CZ  PHE A 191     5712   4784   4328    -58   -693    318       C  
ATOM   1575  N   ASP A 192      17.251 -28.432   1.590  1.00 46.61           N  
ANISOU 1575  N   ASP A 192     7249   5638   4822   -416   -730    341       N  
ATOM   1576  CA  ASP A 192      16.593 -28.503   2.898  1.00 50.27           C  
ANISOU 1576  CA  ASP A 192     7830   6095   5175   -508   -717    338       C  
ATOM   1577  C   ASP A 192      15.888 -27.201   3.276  1.00 47.68           C  
ANISOU 1577  C   ASP A 192     7477   5816   4823   -553   -640    284       C  
ATOM   1578  O   ASP A 192      14.988 -27.197   4.123  1.00 49.05           O  
ANISOU 1578  O   ASP A 192     7728   6000   4910   -629   -587    265       O  
ATOM   1579  CB  ASP A 192      17.602 -28.887   3.990  1.00 55.79           C  
ANISOU 1579  CB  ASP A 192     8620   6753   5824   -518   -832    382       C  
ATOM   1580  CG  ASP A 192      18.133 -30.303   3.825  1.00 63.45           C  
ANISOU 1580  CG  ASP A 192     9647   7664   6798   -477   -907    436       C  
ATOM   1581  OD1 ASP A 192      17.309 -31.248   3.757  1.00 66.50           O  
ANISOU 1581  OD1 ASP A 192    10105   8021   7140   -514   -868    444       O  
ATOM   1582  OD2 ASP A 192      19.374 -30.470   3.769  1.00 66.52           O  
ANISOU 1582  OD2 ASP A 192    10007   8033   7234   -409  -1006    469       O  
ATOM   1583  N   ASN A 193      16.309 -26.097   2.667  1.00 43.14           N  
ANISOU 1583  N   ASN A 193     6799   5270   4323   -505   -632    259       N  
ATOM   1584  CA  ASN A 193      15.665 -24.807   2.904  1.00 41.81           C  
ANISOU 1584  CA  ASN A 193     6606   5138   4140   -533   -560    205       C  
ATOM   1585  C   ASN A 193      15.768 -23.867   1.697  1.00 39.53           C  
ANISOU 1585  C   ASN A 193     6193   4876   3950   -470   -526    179       C  
ATOM   1586  O   ASN A 193      16.679 -23.986   0.879  1.00 38.66           O  
ANISOU 1586  O   ASN A 193     6015   4759   3915   -412   -575    205       O  
ATOM   1587  CB  ASN A 193      16.201 -24.146   4.180  1.00 42.39           C  
ANISOU 1587  CB  ASN A 193     6756   5202   4148   -578   -611    202       C  
ATOM   1588  CG  ASN A 193      17.653 -23.739   4.060  1.00 45.71           C  
ANISOU 1588  CG  ASN A 193     7131   5610   4625   -537   -713    228       C  
ATOM   1589  OD1 ASN A 193      17.964 -22.605   3.676  1.00 46.88           O  
ANISOU 1589  OD1 ASN A 193     7212   5777   4824   -517   -704    202       O  
ATOM   1590  ND2 ASN A 193      18.555 -24.668   4.357  1.00 47.06           N  
ANISOU 1590  ND2 ASN A 193     7339   5752   4790   -524   -812    281       N  
ATOM   1591  N   GLU A 194      14.816 -22.946   1.597  1.00 39.02           N  
ANISOU 1591  N   GLU A 194     6101   4842   3881   -481   -440    129       N  
ATOM   1592  CA  GLU A 194      14.688 -22.053   0.450  1.00 37.98           C  
ANISOU 1592  CA  GLU A 194     5865   4732   3833   -427   -399    103       C  
ATOM   1593  C   GLU A 194      15.894 -21.135   0.279  1.00 39.99           C  
ANISOU 1593  C   GLU A 194     6081   4976   4138   -399   -461    110       C  
ATOM   1594  O   GLU A 194      16.268 -20.797  -0.848  1.00 40.53           O  
ANISOU 1594  O   GLU A 194     6063   5051   4286   -348   -460    115       O  
ATOM   1595  CB  GLU A 194      13.413 -21.217   0.579  1.00 37.93           C  
ANISOU 1595  CB  GLU A 194     5851   4757   3803   -442   -303     46       C  
ATOM   1596  CG  GLU A 194      13.029 -20.470  -0.688  1.00 36.72           C  
ANISOU 1596  CG  GLU A 194     5597   4624   3730   -383   -256     22       C  
ATOM   1597  CD  GLU A 194      12.120 -19.286  -0.433  1.00 37.82           C  
ANISOU 1597  CD  GLU A 194     5732   4784   3854   -381   -184    -36       C  
ATOM   1598  OE1 GLU A 194      11.798 -18.576  -1.406  1.00 41.69           O  
ANISOU 1598  OE1 GLU A 194     6150   5284   4406   -330   -153    -55       O  
ATOM   1599  OE2 GLU A 194      11.715 -19.062   0.727  1.00 40.50           O  
ANISOU 1599  OE2 GLU A 194     6143   5126   4118   -426   -158    -63       O  
ATOM   1600  N   LYS A 195      16.488 -20.721   1.397  1.00 40.96           N  
ANISOU 1600  N   LYS A 195     6270   5083   4209   -440   -514    111       N  
ATOM   1601  CA  LYS A 195      17.646 -19.846   1.363  1.00 41.45           C  
ANISOU 1601  CA  LYS A 195     6301   5137   4311   -431   -579    119       C  
ATOM   1602  C   LYS A 195      18.802 -20.513   0.634  1.00 41.70           C  
ANISOU 1602  C   LYS A 195     6264   5168   4413   -385   -650    169       C  
ATOM   1603  O   LYS A 195      19.399 -19.909  -0.261  1.00 40.23           O  
ANISOU 1603  O   LYS A 195     5992   4992   4301   -351   -656    172       O  
ATOM   1604  CB  LYS A 195      18.067 -19.415   2.767  1.00 42.75           C  
ANISOU 1604  CB  LYS A 195     6561   5285   4399   -492   -632    114       C  
ATOM   1605  CG  LYS A 195      17.188 -18.330   3.360  1.00 48.07           C  
ANISOU 1605  CG  LYS A 195     7289   5958   5019   -525   -562     54       C  
ATOM   1606  CD  LYS A 195      17.909 -17.576   4.460  1.00 51.87           C  
ANISOU 1606  CD  LYS A 195     7847   6417   5444   -578   -628     47       C  
ATOM   1607  CE  LYS A 195      16.925 -16.868   5.372  1.00 54.86           C  
ANISOU 1607  CE  LYS A 195     8318   6789   5736   -618   -555    -13       C  
ATOM   1608  NZ  LYS A 195      16.407 -17.793   6.423  1.00 57.66           N  
ANISOU 1608  NZ  LYS A 195     8770   7146   5990   -668   -545     -6       N  
ATOM   1609  N   GLU A 196      19.109 -21.759   0.999  1.00 41.93           N  
ANISOU 1609  N   GLU A 196     6332   5182   4417   -384   -701    208       N  
ATOM   1610  CA  GLU A 196      20.223 -22.443   0.357  1.00 42.92           C  
ANISOU 1610  CA  GLU A 196     6393   5306   4608   -329   -769    253       C  
ATOM   1611  C   GLU A 196      19.910 -22.700  -1.122  1.00 40.57           C  
ANISOU 1611  C   GLU A 196     6009   5022   4384   -269   -708    248       C  
ATOM   1612  O   GLU A 196      20.787 -22.556  -1.972  1.00 40.18           O  
ANISOU 1612  O   GLU A 196     5872   4987   4409   -222   -731    263       O  
ATOM   1613  CB  GLU A 196      20.698 -23.685   1.134  1.00 44.21           C  
ANISOU 1613  CB  GLU A 196     6628   5441   4727   -332   -850    297       C  
ATOM   1614  CG  GLU A 196      19.824 -24.930   1.062  1.00 54.16           C  
ANISOU 1614  CG  GLU A 196     7950   6678   5950   -331   -813    306       C  
ATOM   1615  CD  GLU A 196      20.388 -26.109   1.881  1.00 61.18           C  
ANISOU 1615  CD  GLU A 196     8927   7528   6792   -333   -905    355       C  
ATOM   1616  OE1 GLU A 196      20.133 -27.285   1.501  1.00 57.31           O  
ANISOU 1616  OE1 GLU A 196     8466   7009   6301   -306   -901    376       O  
ATOM   1617  OE2 GLU A 196      21.082 -25.855   2.900  1.00 61.31           O  
ANISOU 1617  OE2 GLU A 196     8990   7538   6769   -363   -986    372       O  
ATOM   1618  N   LEU A 197      18.651 -23.017  -1.421  1.00 37.94           N  
ANISOU 1618  N   LEU A 197     5698   4689   4027   -277   -628    225       N  
ATOM   1619  CA  LEU A 197      18.205 -23.197  -2.800  1.00 38.14           C  
ANISOU 1619  CA  LEU A 197     5652   4727   4111   -229   -569    217       C  
ATOM   1620  C   LEU A 197      18.488 -21.947  -3.651  1.00 36.75           C  
ANISOU 1620  C   LEU A 197     5391   4575   3999   -205   -544    197       C  
ATOM   1621  O   LEU A 197      19.105 -22.036  -4.714  1.00 35.93           O  
ANISOU 1621  O   LEU A 197     5213   4478   3960   -156   -548    212       O  
ATOM   1622  CB  LEU A 197      16.713 -23.575  -2.851  1.00 36.68           C  
ANISOU 1622  CB  LEU A 197     5504   4548   3884   -256   -491    191       C  
ATOM   1623  CG  LEU A 197      16.099 -23.915  -4.215  1.00 37.03           C  
ANISOU 1623  CG  LEU A 197     5490   4605   3976   -217   -436    183       C  
ATOM   1624  CD1 LEU A 197      14.935 -24.890  -4.070  1.00 35.05           C  
ANISOU 1624  CD1 LEU A 197     5292   4352   3675   -254   -395    178       C  
ATOM   1625  CD2 LEU A 197      15.646 -22.656  -4.960  1.00 35.41           C  
ANISOU 1625  CD2 LEU A 197     5216   4427   3812   -200   -381    149       C  
ATOM   1626  N   LEU A 198      18.042 -20.787  -3.180  1.00 35.82           N  
ANISOU 1626  N   LEU A 198     5290   4462   3857   -240   -515    163       N  
ATOM   1627  CA  LEU A 198      18.217 -19.566  -3.951  1.00 36.59           C  
ANISOU 1627  CA  LEU A 198     5326   4570   4007   -222   -491    145       C  
ATOM   1628  C   LEU A 198      19.678 -19.150  -4.061  1.00 36.51           C  
ANISOU 1628  C   LEU A 198     5269   4563   4041   -218   -559    172       C  
ATOM   1629  O   LEU A 198      20.098 -18.664  -5.108  1.00 35.95           O  
ANISOU 1629  O   LEU A 198     5126   4503   4030   -190   -545    177       O  
ATOM   1630  CB  LEU A 198      17.341 -18.429  -3.416  1.00 35.39           C  
ANISOU 1630  CB  LEU A 198     5214   4415   3818   -252   -444     99       C  
ATOM   1631  CG  LEU A 198      15.835 -18.567  -3.697  1.00 35.55           C  
ANISOU 1631  CG  LEU A 198     5239   4449   3819   -242   -361     67       C  
ATOM   1632  CD1 LEU A 198      15.026 -17.584  -2.867  1.00 29.97           C  
ANISOU 1632  CD1 LEU A 198     4583   3739   3064   -269   -318     19       C  
ATOM   1633  CD2 LEU A 198      15.511 -18.400  -5.193  1.00 31.13           C  
ANISOU 1633  CD2 LEU A 198     4602   3902   3324   -191   -322     66       C  
ATOM   1634  N   MET A 199      20.442 -19.338  -2.991  1.00 39.09           N  
ANISOU 1634  N   MET A 199     5635   4881   4335   -250   -632    191       N  
ATOM   1635  CA  MET A 199      21.868 -18.991  -2.992  1.00 41.20           C  
ANISOU 1635  CA  MET A 199     5849   5160   4644   -253   -706    218       C  
ATOM   1636  C   MET A 199      22.630 -19.855  -3.990  1.00 41.67           C  
ANISOU 1636  C   MET A 199     5824   5239   4771   -191   -722    252       C  
ATOM   1637  O   MET A 199      23.461 -19.351  -4.761  1.00 41.15           O  
ANISOU 1637  O   MET A 199     5673   5197   4766   -176   -728    262       O  
ATOM   1638  CB  MET A 199      22.475 -19.125  -1.589  1.00 42.54           C  
ANISOU 1638  CB  MET A 199     6083   5320   4760   -300   -792    234       C  
ATOM   1639  CG  MET A 199      22.120 -17.971  -0.662  1.00 44.58           C  
ANISOU 1639  CG  MET A 199     6416   5562   4961   -365   -788    199       C  
ATOM   1640  SD  MET A 199      22.945 -18.017   0.940  1.00 51.28           S  
ANISOU 1640  SD  MET A 199     7345   6399   5742   -429   -899    217       S  
ATOM   1641  CE  MET A 199      22.235 -19.494   1.680  1.00 47.42           C  
ANISOU 1641  CE  MET A 199     6945   5891   5179   -423   -900    233       C  
ATOM   1642  N   GLU A 200      22.327 -21.151  -3.984  1.00 40.89           N  
ANISOU 1642  N   GLU A 200     5752   5127   4656   -158   -723    267       N  
ATOM   1643  CA  GLU A 200      22.905 -22.067  -4.953  1.00 42.40           C  
ANISOU 1643  CA  GLU A 200     5878   5328   4903    -89   -728    292       C  
ATOM   1644  C   GLU A 200      22.479 -21.697  -6.381  1.00 40.77           C  
ANISOU 1644  C   GLU A 200     5610   5137   4744    -59   -647    274       C  
ATOM   1645  O   GLU A 200      23.307 -21.709  -7.300  1.00 40.95           O  
ANISOU 1645  O   GLU A 200     5550   5183   4827    -18   -647    288       O  
ATOM   1646  CB  GLU A 200      22.543 -23.516  -4.615  1.00 44.33           C  
ANISOU 1646  CB  GLU A 200     6190   5543   5112    -65   -745    309       C  
ATOM   1647  CG  GLU A 200      23.111 -24.552  -5.578  1.00 51.20           C  
ANISOU 1647  CG  GLU A 200     7009   6411   6034     14   -750    330       C  
ATOM   1648  CD  GLU A 200      24.633 -24.522  -5.682  1.00 58.71           C  
ANISOU 1648  CD  GLU A 200     7873   7390   7044     56   -816    357       C  
ATOM   1649  OE1 GLU A 200      25.308 -24.330  -4.639  1.00 58.18           O  
ANISOU 1649  OE1 GLU A 200     7819   7327   6960     28   -896    375       O  
ATOM   1650  OE2 GLU A 200      25.147 -24.702  -6.816  1.00 60.70           O  
ANISOU 1650  OE2 GLU A 200     8042   7663   7357    115   -788    360       O  
ATOM   1651  N   TYR A 201      21.206 -21.347  -6.561  1.00 37.40           N  
ANISOU 1651  N   TYR A 201     5222   4700   4288    -78   -581    243       N  
ATOM   1652  CA  TYR A 201      20.721 -20.916  -7.876  1.00 37.87           C  
ANISOU 1652  CA  TYR A 201     5233   4771   4384    -53   -512    227       C  
ATOM   1653  C   TYR A 201      21.527 -19.738  -8.422  1.00 38.04           C  
ANISOU 1653  C   TYR A 201     5188   4813   4453    -60   -514    229       C  
ATOM   1654  O   TYR A 201      22.021 -19.787  -9.555  1.00 38.20           O  
ANISOU 1654  O   TYR A 201     5142   4850   4522    -24   -493    240       O  
ATOM   1655  CB  TYR A 201      19.223 -20.588  -7.852  1.00 37.30           C  
ANISOU 1655  CB  TYR A 201     5207   4692   4275    -74   -451    193       C  
ATOM   1656  CG  TYR A 201      18.640 -20.352  -9.230  1.00 37.07           C  
ANISOU 1656  CG  TYR A 201     5133   4672   4279    -42   -391    181       C  
ATOM   1657  CD1 TYR A 201      18.657 -21.366 -10.192  1.00 37.40           C  
ANISOU 1657  CD1 TYR A 201     5153   4715   4341      0   -377    194       C  
ATOM   1658  CD2 TYR A 201      18.078 -19.114  -9.580  1.00 36.11           C  
ANISOU 1658  CD2 TYR A 201     5002   4553   4165    -52   -353    156       C  
ATOM   1659  CE1 TYR A 201      18.137 -21.161 -11.468  1.00 34.51           C  
ANISOU 1659  CE1 TYR A 201     4755   4358   3999     25   -328    184       C  
ATOM   1660  CE2 TYR A 201      17.546 -18.900 -10.864  1.00 35.78           C  
ANISOU 1660  CE2 TYR A 201     4926   4519   4150    -22   -308    149       C  
ATOM   1661  CZ  TYR A 201      17.578 -19.939 -11.797  1.00 35.24           C  
ANISOU 1661  CZ  TYR A 201     4835   4456   4098     13   -296    164       C  
ATOM   1662  OH  TYR A 201      17.064 -19.770 -13.061  1.00 32.27           O  
ANISOU 1662  OH  TYR A 201     4434   4087   3741     39   -256    158       O  
ATOM   1663  N   LEU A 202      21.671 -18.694  -7.610  1.00 36.17           N  
ANISOU 1663  N   LEU A 202     4975   4570   4196   -110   -537    218       N  
ATOM   1664  CA  LEU A 202      22.437 -17.522  -8.010  1.00 38.29           C  
ANISOU 1664  CA  LEU A 202     5195   4851   4502   -134   -544    221       C  
ATOM   1665  C   LEU A 202      23.891 -17.859  -8.350  1.00 39.85           C  
ANISOU 1665  C   LEU A 202     5309   5082   4751   -118   -590    255       C  
ATOM   1666  O   LEU A 202      24.429 -17.336  -9.329  1.00 39.81           O  
ANISOU 1666  O   LEU A 202     5236   5098   4791   -114   -566    263       O  
ATOM   1667  CB  LEU A 202      22.363 -16.423  -6.950  1.00 36.19           C  
ANISOU 1667  CB  LEU A 202     4987   4565   4198   -196   -570    201       C  
ATOM   1668  CG  LEU A 202      21.012 -15.718  -6.776  1.00 37.90           C  
ANISOU 1668  CG  LEU A 202     5271   4753   4375   -206   -514    160       C  
ATOM   1669  CD1 LEU A 202      21.048 -14.805  -5.559  1.00 33.49           C  
ANISOU 1669  CD1 LEU A 202     4783   4170   3770   -263   -546    139       C  
ATOM   1670  CD2 LEU A 202      20.584 -14.931  -8.032  1.00 35.06           C  
ANISOU 1670  CD2 LEU A 202     4881   4390   4052   -183   -458    149       C  
ATOM   1671  N   ASN A 203      24.512 -18.738  -7.558  1.00 40.63           N  
ANISOU 1671  N   ASN A 203     5409   5186   4841   -108   -654    276       N  
ATOM   1672  CA  ASN A 203      25.882 -19.186  -7.833  1.00 41.25           C  
ANISOU 1672  CA  ASN A 203     5397   5304   4974    -79   -700    308       C  
ATOM   1673  C   ASN A 203      25.969 -19.921  -9.160  1.00 39.85           C  
ANISOU 1673  C   ASN A 203     5159   5141   4839     -8   -647    314       C  
ATOM   1674  O   ASN A 203      26.887 -19.696  -9.952  1.00 40.91           O  
ANISOU 1674  O   ASN A 203     5202   5316   5027      7   -637    326       O  
ATOM   1675  CB  ASN A 203      26.422 -20.076  -6.710  1.00 40.91           C  
ANISOU 1675  CB  ASN A 203     5378   5256   4910    -70   -786    330       C  
ATOM   1676  CG  ASN A 203      26.905 -19.279  -5.510  1.00 42.69           C  
ANISOU 1676  CG  ASN A 203     5631   5484   5107   -142   -858    334       C  
ATOM   1677  OD1 ASN A 203      26.845 -19.753  -4.374  1.00 46.52           O  
ANISOU 1677  OD1 ASN A 203     6185   5948   5543   -158   -919    342       O  
ATOM   1678  ND2 ASN A 203      27.407 -18.079  -5.755  1.00 39.55           N  
ANISOU 1678  ND2 ASN A 203     5186   5106   4734   -193   -856    329       N  
ATOM   1679  N   PHE A 204      25.001 -20.804  -9.377  1.00 38.17           N  
ANISOU 1679  N   PHE A 204     5004   4900   4600     29   -611    303       N  
ATOM   1680  CA  PHE A 204      24.827 -21.517 -10.631  1.00 35.93           C  
ANISOU 1680  CA  PHE A 204     4691   4619   4342     90   -556    301       C  
ATOM   1681  C   PHE A 204      24.638 -20.525 -11.786  1.00 34.75           C  
ANISOU 1681  C   PHE A 204     4501   4486   4215     76   -490    289       C  
ATOM   1682  O   PHE A 204      25.286 -20.660 -12.821  1.00 34.70           O  
ANISOU 1682  O   PHE A 204     4426   4508   4251    112   -460    297       O  
ATOM   1683  CB  PHE A 204      23.648 -22.496 -10.488  1.00 34.36           C  
ANISOU 1683  CB  PHE A 204     4579   4380   4097    108   -536    290       C  
ATOM   1684  CG  PHE A 204      23.004 -22.890 -11.787  1.00 35.80           C  
ANISOU 1684  CG  PHE A 204     4757   4557   4288    145   -467    277       C  
ATOM   1685  CD1 PHE A 204      23.456 -23.999 -12.492  1.00 35.91           C  
ANISOU 1685  CD1 PHE A 204     4752   4567   4324    211   -461    286       C  
ATOM   1686  CD2 PHE A 204      21.918 -22.170 -12.289  1.00 31.84           C  
ANISOU 1686  CD2 PHE A 204     4278   4051   3770    116   -412    254       C  
ATOM   1687  CE1 PHE A 204      22.849 -24.376 -13.690  1.00 35.30           C  
ANISOU 1687  CE1 PHE A 204     4684   4483   4247    240   -401    272       C  
ATOM   1688  CE2 PHE A 204      21.310 -22.542 -13.485  1.00 31.42           C  
ANISOU 1688  CE2 PHE A 204     4224   3994   3719    146   -358    243       C  
ATOM   1689  CZ  PHE A 204      21.779 -23.648 -14.184  1.00 30.51           C  
ANISOU 1689  CZ  PHE A 204     4096   3875   3621    203   -353    252       C  
ATOM   1690  N   TRP A 205      23.772 -19.527 -11.580  1.00 34.73           N  
ANISOU 1690  N   TRP A 205     4545   4465   4185     27   -468    269       N  
ATOM   1691  CA  TRP A 205      23.471 -18.478 -12.569  1.00 34.13           C  
ANISOU 1691  CA  TRP A 205     4452   4393   4122     10   -414    258       C  
ATOM   1692  C   TRP A 205      24.731 -17.707 -12.918  1.00 37.76           C  
ANISOU 1692  C   TRP A 205     4837   4887   4625    -16   -426    277       C  
ATOM   1693  O   TRP A 205      24.943 -17.344 -14.077  1.00 37.50           O  
ANISOU 1693  O   TRP A 205     4762   4869   4615     -9   -380    281       O  
ATOM   1694  CB  TRP A 205      22.409 -17.517 -12.014  1.00 33.31           C  
ANISOU 1694  CB  TRP A 205     4418   4259   3981    -32   -403    233       C  
ATOM   1695  CG  TRP A 205      21.857 -16.463 -12.969  1.00 32.34           C  
ANISOU 1695  CG  TRP A 205     4298   4125   3864    -41   -354    221       C  
ATOM   1696  CD1 TRP A 205      22.472 -15.298 -13.372  1.00 35.38           C  
ANISOU 1696  CD1 TRP A 205     4660   4512   4270    -77   -352    229       C  
ATOM   1697  CD2 TRP A 205      20.556 -16.453 -13.582  1.00 33.73           C  
ANISOU 1697  CD2 TRP A 205     4509   4285   4023    -16   -307    201       C  
ATOM   1698  NE1 TRP A 205      21.640 -14.581 -14.219  1.00 32.94           N  
ANISOU 1698  NE1 TRP A 205     4378   4182   3955    -70   -308    217       N  
ATOM   1699  CE2 TRP A 205      20.461 -15.266 -14.359  1.00 34.35           C  
ANISOU 1699  CE2 TRP A 205     4586   4351   4112    -30   -282    199       C  
ATOM   1700  CE3 TRP A 205      19.465 -17.338 -13.565  1.00 34.07           C  
ANISOU 1700  CE3 TRP A 205     4583   4322   4040     12   -287    186       C  
ATOM   1701  CZ2 TRP A 205      19.320 -14.947 -15.101  1.00 34.51           C  
ANISOU 1701  CZ2 TRP A 205     4633   4356   4122     -7   -244    184       C  
ATOM   1702  CZ3 TRP A 205      18.327 -17.017 -14.311  1.00 32.27           C  
ANISOU 1702  CZ3 TRP A 205     4372   4086   3805     28   -247    169       C  
ATOM   1703  CH2 TRP A 205      18.267 -15.829 -15.062  1.00 31.90           C  
ANISOU 1703  CH2 TRP A 205     4321   4029   3772     24   -228    168       C  
ATOM   1704  N   GLN A 206      25.567 -17.475 -11.907  1.00 39.35           N  
ANISOU 1704  N   GLN A 206     5020   5101   4830    -52   -490    289       N  
ATOM   1705  CA  GLN A 206      26.856 -16.832 -12.092  1.00 43.70           C  
ANISOU 1705  CA  GLN A 206     5489   5693   5422    -87   -511    309       C  
ATOM   1706  C   GLN A 206      27.782 -17.642 -12.996  1.00 44.01           C  
ANISOU 1706  C   GLN A 206     5430   5781   5510    -30   -492    327       C  
ATOM   1707  O   GLN A 206      28.510 -17.067 -13.802  1.00 44.51           O  
ANISOU 1707  O   GLN A 206     5423   5883   5607    -51   -462    337       O  
ATOM   1708  CB  GLN A 206      27.538 -16.605 -10.746  1.00 45.66           C  
ANISOU 1708  CB  GLN A 206     5739   5949   5663   -134   -596    318       C  
ATOM   1709  CG  GLN A 206      28.135 -15.221 -10.584  1.00 53.36           C  
ANISOU 1709  CG  GLN A 206     6697   6932   6645   -220   -616    322       C  
ATOM   1710  CD  GLN A 206      27.107 -14.206 -10.082  1.00 60.16           C  
ANISOU 1710  CD  GLN A 206     7667   7734   7455   -269   -606    294       C  
ATOM   1711  OE1 GLN A 206      26.130 -13.879 -10.775  1.00 59.92           O  
ANISOU 1711  OE1 GLN A 206     7681   7673   7412   -250   -544    276       O  
ATOM   1712  NE2 GLN A 206      27.326 -13.703  -8.868  1.00 57.02           N  
ANISOU 1712  NE2 GLN A 206     7315   7321   7028   -327   -670    290       N  
ATOM   1713  N   GLN A 207      27.765 -18.966 -12.851  1.00 44.56           N  
ANISOU 1713  N   GLN A 207     5501   5849   5581     40   -506    330       N  
ATOM   1714  CA  GLN A 207      28.613 -19.848 -13.665  1.00 46.93           C  
ANISOU 1714  CA  GLN A 207     5717   6189   5925    110   -485    341       C  
ATOM   1715  C   GLN A 207      28.081 -19.990 -15.089  1.00 44.15           C  
ANISOU 1715  C   GLN A 207     5370   5831   5572    144   -397    328       C  
ATOM   1716  O   GLN A 207      28.844 -20.159 -16.039  1.00 45.72           O  
ANISOU 1716  O   GLN A 207     5491   6072   5806    176   -356    333       O  
ATOM   1717  CB  GLN A 207      28.728 -21.239 -13.035  1.00 48.92           C  
ANISOU 1717  CB  GLN A 207     5988   6425   6174    180   -534    348       C  
ATOM   1718  CG  GLN A 207      29.731 -21.346 -11.895  1.00 61.59           C  
ANISOU 1718  CG  GLN A 207     7549   8055   7797    172   -627    370       C  
ATOM   1719  CD  GLN A 207      31.179 -21.222 -12.365  1.00 70.11           C  
ANISOU 1719  CD  GLN A 207     8486   9209   8942    191   -634    387       C  
ATOM   1720  OE1 GLN A 207      31.745 -22.162 -12.932  1.00 73.65           O  
ANISOU 1720  OE1 GLN A 207     8875   9681   9427    277   -618    390       O  
ATOM   1721  NE2 GLN A 207      31.784 -20.059 -12.123  1.00 71.39           N  
ANISOU 1721  NE2 GLN A 207     8594   9410   9120    108   -655    396       N  
ATOM   1722  N   LYS A 208      26.765 -19.940 -15.222  1.00 40.97           N  
ANISOU 1722  N   LYS A 208     5059   5381   5127    137   -369    309       N  
ATOM   1723  CA  LYS A 208      26.109 -20.205 -16.491  1.00 38.71           C  
ANISOU 1723  CA  LYS A 208     4794   5083   4830    170   -298    297       C  
ATOM   1724  C   LYS A 208      25.088 -19.099 -16.703  1.00 36.49           C  
ANISOU 1724  C   LYS A 208     4569   4774   4519    116   -272    285       C  
ATOM   1725  O   LYS A 208      23.878 -19.332 -16.660  1.00 37.65           O  
ANISOU 1725  O   LYS A 208     4788   4886   4633    123   -261    268       O  
ATOM   1726  CB  LYS A 208      25.442 -21.588 -16.471  1.00 36.76           C  
ANISOU 1726  CB  LYS A 208     4604   4803   4561    230   -298    286       C  
ATOM   1727  CG  LYS A 208      26.392 -22.731 -16.138  1.00 38.31           C  
ANISOU 1727  CG  LYS A 208     4761   5011   4783    294   -334    298       C  
ATOM   1728  CD  LYS A 208      25.653 -24.046 -15.934  1.00 40.56           C  
ANISOU 1728  CD  LYS A 208     5128   5246   5036    341   -345    290       C  
ATOM   1729  CE  LYS A 208      26.534 -25.077 -15.221  1.00 42.00           C  
ANISOU 1729  CE  LYS A 208     5294   5426   5239    399   -405    305       C  
ATOM   1730  NZ  LYS A 208      27.695 -25.521 -16.056  1.00 42.02           N  
ANISOU 1730  NZ  LYS A 208     5208   5467   5290    472   -381    308       N  
ATOM   1731  N   THR A 209      25.595 -17.888 -16.910  1.00 34.99           N  
ANISOU 1731  N   THR A 209     4347   4602   4344     62   -265    294       N  
ATOM   1732  CA  THR A 209      24.761 -16.710 -17.073  1.00 34.51           C  
ANISOU 1732  CA  THR A 209     4343   4510   4260     15   -249    284       C  
ATOM   1733  C   THR A 209      24.073 -16.775 -18.433  1.00 34.02           C  
ANISOU 1733  C   THR A 209     4303   4438   4185     43   -188    279       C  
ATOM   1734  O   THR A 209      24.732 -16.864 -19.464  1.00 32.04           O  
ANISOU 1734  O   THR A 209     4006   4218   3950     54   -148    290       O  
ATOM   1735  CB  THR A 209      25.581 -15.399 -16.950  1.00 35.65           C  
ANISOU 1735  CB  THR A 209     4457   4667   4420    -57   -262    299       C  
ATOM   1736  OG1 THR A 209      26.445 -15.470 -15.807  1.00 36.93           O  
ANISOU 1736  OG1 THR A 209     4583   4851   4599    -83   -324    308       O  
ATOM   1737  CG2 THR A 209      24.653 -14.181 -16.827  1.00 31.26           C  
ANISOU 1737  CG2 THR A 209     3981   4062   3836    -99   -260    286       C  
ATOM   1738  N   PRO A 210      22.734 -16.752 -18.432  1.00 35.73           N  
ANISOU 1738  N   PRO A 210     4588   4617   4369     53   -181    260       N  
ATOM   1739  CA  PRO A 210      21.982 -16.761 -19.684  1.00 34.62           C  
ANISOU 1739  CA  PRO A 210     4475   4467   4212     76   -136    255       C  
ATOM   1740  C   PRO A 210      22.344 -15.561 -20.559  1.00 35.26           C  
ANISOU 1740  C   PRO A 210     4550   4549   4297     39   -110    270       C  
ATOM   1741  O   PRO A 210      22.580 -14.464 -20.043  1.00 34.82           O  
ANISOU 1741  O   PRO A 210     4504   4480   4246    -10   -131    275       O  
ATOM   1742  CB  PRO A 210      20.535 -16.646 -19.212  1.00 34.29           C  
ANISOU 1742  CB  PRO A 210     4495   4391   4141     79   -147    234       C  
ATOM   1743  CG  PRO A 210      20.551 -17.241 -17.820  1.00 34.66           C  
ANISOU 1743  CG  PRO A 210     4549   4437   4185     77   -187    226       C  
ATOM   1744  CD  PRO A 210      21.855 -16.829 -17.246  1.00 35.00           C  
ANISOU 1744  CD  PRO A 210     4548   4497   4253     47   -215    242       C  
ATOM   1745  N   VAL A 211      22.421 -15.791 -21.866  1.00 33.94           N  
ANISOU 1745  N   VAL A 211     4378   4394   4124     57    -65    277       N  
ATOM   1746  CA  VAL A 211      22.537 -14.710 -22.838  1.00 32.65           C  
ANISOU 1746  CA  VAL A 211     4232   4224   3951     22    -37    293       C  
ATOM   1747  C   VAL A 211      21.128 -14.439 -23.329  1.00 33.75           C  
ANISOU 1747  C   VAL A 211     4441   4323   4058     41    -37    282       C  
ATOM   1748  O   VAL A 211      20.618 -13.314 -23.221  1.00 32.73           O  
ANISOU 1748  O   VAL A 211     4357   4159   3920     16    -53    284       O  
ATOM   1749  CB  VAL A 211      23.445 -15.108 -24.014  1.00 34.86           C  
ANISOU 1749  CB  VAL A 211     4468   4544   4234     28     17    307       C  
ATOM   1750  CG1 VAL A 211      23.291 -14.130 -25.191  1.00 33.80           C  
ANISOU 1750  CG1 VAL A 211     4375   4394   4072     -7     50    324       C  
ATOM   1751  CG2 VAL A 211      24.901 -15.177 -23.550  1.00 34.81           C  
ANISOU 1751  CG2 VAL A 211     4374   4586   4265      6     17    319       C  
ATOM   1752  N   ILE A 212      20.508 -15.490 -23.864  1.00 32.11           N  
ANISOU 1752  N   ILE A 212     4246   4121   3834     87    -22    270       N  
ATOM   1753  CA  ILE A 212      19.090 -15.488 -24.189  1.00 30.55           C  
ANISOU 1753  CA  ILE A 212     4101   3897   3609    109    -32    257       C  
ATOM   1754  C   ILE A 212      18.343 -16.162 -23.059  1.00 30.05           C  
ANISOU 1754  C   ILE A 212     4040   3828   3548    127    -61    234       C  
ATOM   1755  O   ILE A 212      18.630 -17.308 -22.690  1.00 28.63           O  
ANISOU 1755  O   ILE A 212     3841   3665   3373    146    -62    227       O  
ATOM   1756  CB  ILE A 212      18.787 -16.243 -25.508  1.00 30.29           C  
ANISOU 1756  CB  ILE A 212     4087   3872   3550    136     -2    257       C  
ATOM   1757  CG1 ILE A 212      19.687 -15.752 -26.652  1.00 29.54           C  
ANISOU 1757  CG1 ILE A 212     3989   3790   3445    115     39    280       C  
ATOM   1758  CG2 ILE A 212      17.297 -16.129 -25.858  1.00 28.95           C  
ANISOU 1758  CG2 ILE A 212     3965   3680   3353    153    -22    246       C  
ATOM   1759  CD1 ILE A 212      19.471 -14.275 -27.077  1.00 31.10           C  
ANISOU 1759  CD1 ILE A 212     4227   3958   3630     78     32    299       C  
ATOM   1760  N   LEU A 213      17.369 -15.448 -22.516  1.00 30.94           N  
ANISOU 1760  N   LEU A 213     4182   3919   3656    123    -84    221       N  
ATOM   1761  CA  LEU A 213      16.571 -15.983 -21.437  1.00 30.06           C  
ANISOU 1761  CA  LEU A 213     4075   3808   3540    133   -104    198       C  
ATOM   1762  C   LEU A 213      15.121 -16.125 -21.897  1.00 31.63           C  
ANISOU 1762  C   LEU A 213     4295   4003   3719    155   -105    183       C  
ATOM   1763  O   LEU A 213      14.487 -15.159 -22.313  1.00 32.25           O  
ANISOU 1763  O   LEU A 213     4393   4066   3794    163   -110    182       O  
ATOM   1764  CB  LEU A 213      16.699 -15.101 -20.192  1.00 28.47           C  
ANISOU 1764  CB  LEU A 213     3879   3590   3347    108   -126    190       C  
ATOM   1765  CG  LEU A 213      16.071 -15.628 -18.897  1.00 27.10           C  
ANISOU 1765  CG  LEU A 213     3714   3420   3164    108   -142    167       C  
ATOM   1766  CD1 LEU A 213      16.541 -17.056 -18.570  1.00 25.00           C  
ANISOU 1766  CD1 LEU A 213     3431   3174   2896    112   -146    171       C  
ATOM   1767  CD2 LEU A 213      16.364 -14.669 -17.760  1.00 27.00           C  
ANISOU 1767  CD2 LEU A 213     3716   3389   3153     80   -162    158       C  
ATOM   1768  N   THR A 214      14.613 -17.348 -21.852  1.00 31.72           N  
ANISOU 1768  N   THR A 214     4305   4031   3718    166   -103    172       N  
ATOM   1769  CA  THR A 214      13.285 -17.614 -22.378  1.00 31.11           C  
ANISOU 1769  CA  THR A 214     4239   3961   3622    179   -107    159       C  
ATOM   1770  C   THR A 214      12.542 -18.603 -21.484  1.00 30.64           C  
ANISOU 1770  C   THR A 214     4177   3916   3551    169   -113    139       C  
ATOM   1771  O   THR A 214      13.065 -19.017 -20.449  1.00 29.55           O  
ANISOU 1771  O   THR A 214     4037   3775   3415    156   -116    137       O  
ATOM   1772  CB  THR A 214      13.322 -18.033 -23.893  1.00 30.42           C  
ANISOU 1772  CB  THR A 214     4167   3875   3517    191    -95    172       C  
ATOM   1773  OG1 THR A 214      11.988 -18.127 -24.397  1.00 30.03           O  
ANISOU 1773  OG1 THR A 214     4125   3834   3450    199   -110    161       O  
ATOM   1774  CG2 THR A 214      14.048 -19.356 -24.111  1.00 29.08           C  
ANISOU 1774  CG2 THR A 214     4000   3710   3339    193    -80    174       C  
ATOM   1775  N   GLY A 215      11.314 -18.939 -21.876  1.00 30.76           N  
ANISOU 1775  N   GLY A 215     4192   3946   3550    172   -117    126       N  
ATOM   1776  CA  GLY A 215      10.412 -19.772 -21.077  1.00 31.14           C  
ANISOU 1776  CA  GLY A 215     4235   4014   3584    151   -119    107       C  
ATOM   1777  C   GLY A 215       8.999 -19.281 -21.299  1.00 31.85           C  
ANISOU 1777  C   GLY A 215     4301   4130   3672    158   -125     90       C  
ATOM   1778  O   GLY A 215       8.770 -18.446 -22.170  1.00 35.14           O  
ANISOU 1778  O   GLY A 215     4713   4541   4096    184   -135     97       O  
ATOM   1779  N   TRP A 216       8.048 -19.785 -20.522  1.00 32.22           N  
ANISOU 1779  N   TRP A 216     4331   4204   3707    134   -121     70       N  
ATOM   1780  CA  TRP A 216       6.641 -19.435 -20.721  1.00 33.03           C  
ANISOU 1780  CA  TRP A 216     4394   4345   3812    142   -125     51       C  
ATOM   1781  C   TRP A 216       6.136 -18.454 -19.649  1.00 31.48           C  
ANISOU 1781  C   TRP A 216     4170   4162   3629    158   -111     27       C  
ATOM   1782  O   TRP A 216       6.003 -18.813 -18.484  1.00 31.15           O  
ANISOU 1782  O   TRP A 216     4128   4133   3574    129    -91     12       O  
ATOM   1783  CB  TRP A 216       5.776 -20.704 -20.795  1.00 34.26           C  
ANISOU 1783  CB  TRP A 216     4540   4534   3943     97   -127     44       C  
ATOM   1784  CG  TRP A 216       4.457 -20.480 -21.491  1.00 36.45           C  
ANISOU 1784  CG  TRP A 216     4770   4855   4224    105   -144     33       C  
ATOM   1785  CD1 TRP A 216       3.244 -20.285 -20.899  1.00 37.97           C  
ANISOU 1785  CD1 TRP A 216     4903   5101   4422     98   -135      8       C  
ATOM   1786  CD2 TRP A 216       4.227 -20.410 -22.909  1.00 37.50           C  
ANISOU 1786  CD2 TRP A 216     4906   4987   4355    123   -174     46       C  
ATOM   1787  NE1 TRP A 216       2.270 -20.105 -21.855  1.00 39.12           N  
ANISOU 1787  NE1 TRP A 216     5006   5282   4575    113   -163      6       N  
ATOM   1788  CE2 TRP A 216       2.845 -20.176 -23.096  1.00 39.11           C  
ANISOU 1788  CE2 TRP A 216     5049   5246   4567    127   -192     31       C  
ATOM   1789  CE3 TRP A 216       5.052 -20.525 -24.037  1.00 38.30           C  
ANISOU 1789  CE3 TRP A 216     5057   5051   4445    135   -188     70       C  
ATOM   1790  CZ2 TRP A 216       2.267 -20.050 -24.366  1.00 39.16           C  
ANISOU 1790  CZ2 TRP A 216     5044   5266   4569    142   -232     41       C  
ATOM   1791  CZ3 TRP A 216       4.476 -20.398 -25.304  1.00 42.24           C  
ANISOU 1791  CZ3 TRP A 216     5555   5561   4934    146   -221     78       C  
ATOM   1792  CH2 TRP A 216       3.094 -20.162 -25.455  1.00 38.42           C  
ANISOU 1792  CH2 TRP A 216     5012   5128   4457    149   -248     65       C  
ATOM   1793  N   ASN A 217       5.875 -17.211 -20.055  1.00 33.13           N  
ANISOU 1793  N   ASN A 217     4366   4362   3859    206   -120     24       N  
ATOM   1794  CA  ASN A 217       5.525 -16.129 -19.127  1.00 33.68           C  
ANISOU 1794  CA  ASN A 217     4424   4431   3943    235   -106     -2       C  
ATOM   1795  C   ASN A 217       6.644 -15.753 -18.162  1.00 33.48           C  
ANISOU 1795  C   ASN A 217     4442   4366   3914    221    -95     -1       C  
ATOM   1796  O   ASN A 217       6.384 -15.252 -17.069  1.00 35.81           O  
ANISOU 1796  O   ASN A 217     4737   4663   4205    224    -76    -28       O  
ATOM   1797  CB  ASN A 217       4.279 -16.480 -18.309  1.00 37.80           C  
ANISOU 1797  CB  ASN A 217     4896   5010   4457    223    -82    -36       C  
ATOM   1798  CG  ASN A 217       3.006 -16.110 -19.001  1.00 45.70           C  
ANISOU 1798  CG  ASN A 217     5837   6053   5476    263    -95    -49       C  
ATOM   1799  OD1 ASN A 217       2.845 -14.980 -19.484  1.00 46.55           O  
ANISOU 1799  OD1 ASN A 217     5944   6139   5606    325   -114    -50       O  
ATOM   1800  ND2 ASN A 217       2.068 -17.061 -19.049  1.00 47.64           N  
ANISOU 1800  ND2 ASN A 217     6033   6357   5709    226    -90    -58       N  
ATOM   1801  N   VAL A 218       7.889 -15.982 -18.544  1.00 32.82           N  
ANISOU 1801  N   VAL A 218     4391   4249   3831    204   -106     29       N  
ATOM   1802  CA  VAL A 218       8.983 -15.651 -17.640  1.00 34.10           C  
ANISOU 1802  CA  VAL A 218     4585   4380   3991    185   -104     32       C  
ATOM   1803  C   VAL A 218       9.115 -14.143 -17.392  1.00 35.65           C  
ANISOU 1803  C   VAL A 218     4803   4541   4201    212   -108     22       C  
ATOM   1804  O   VAL A 218       9.495 -13.735 -16.299  1.00 36.49           O  
ANISOU 1804  O   VAL A 218     4933   4631   4299    196   -104      8       O  
ATOM   1805  CB  VAL A 218      10.319 -16.285 -18.073  1.00 33.48           C  
ANISOU 1805  CB  VAL A 218     4523   4284   3914    163   -115     65       C  
ATOM   1806  CG1 VAL A 218      10.211 -17.815 -17.994  1.00 32.41           C  
ANISOU 1806  CG1 VAL A 218     4384   4170   3759    138   -112     69       C  
ATOM   1807  CG2 VAL A 218      10.718 -15.833 -19.487  1.00 31.09           C  
ANISOU 1807  CG2 VAL A 218     4224   3965   3625    185   -124     89       C  
ATOM   1808  N   GLU A 219       8.770 -13.318 -18.381  1.00 36.47           N  
ANISOU 1808  N   GLU A 219     4907   4628   4320    251   -121     29       N  
ATOM   1809  CA  GLU A 219       8.899 -11.866 -18.218  1.00 39.71           C  
ANISOU 1809  CA  GLU A 219     5354   4993   4742    278   -129     21       C  
ATOM   1810  C   GLU A 219       7.873 -11.333 -17.229  1.00 39.93           C  
ANISOU 1810  C   GLU A 219     5375   5029   4767    310   -112    -23       C  
ATOM   1811  O   GLU A 219       8.184 -10.473 -16.411  1.00 40.78           O  
ANISOU 1811  O   GLU A 219     5524   5100   4872    311   -108    -41       O  
ATOM   1812  CB  GLU A 219       8.794 -11.121 -19.552  1.00 40.98           C  
ANISOU 1812  CB  GLU A 219     5531   5126   4915    313   -151     44       C  
ATOM   1813  CG  GLU A 219       9.163  -9.635 -19.437  1.00 48.41           C  
ANISOU 1813  CG  GLU A 219     6529   6003   5863    330   -164     44       C  
ATOM   1814  CD  GLU A 219       9.342  -8.954 -20.787  1.00 53.63           C  
ANISOU 1814  CD  GLU A 219     7224   6627   6527    347   -189     78       C  
ATOM   1815  OE1 GLU A 219      10.504  -8.734 -21.190  1.00 55.73           O  
ANISOU 1815  OE1 GLU A 219     7521   6865   6788    304   -191    109       O  
ATOM   1816  OE2 GLU A 219       8.324  -8.645 -21.447  1.00 56.26           O  
ANISOU 1816  OE2 GLU A 219     7549   6962   6865    401   -206     74       O  
ATOM   1817  N   SER A 220       6.656 -11.863 -17.299  1.00 40.15           N  
ANISOU 1817  N   SER A 220     5350   5109   4796    332    -99    -43       N  
ATOM   1818  CA  SER A 220       5.569 -11.394 -16.442  1.00 39.11           C  
ANISOU 1818  CA  SER A 220     5197   4999   4664    369    -73    -89       C  
ATOM   1819  C   SER A 220       5.491 -12.133 -15.104  1.00 35.53           C  
ANISOU 1819  C   SER A 220     4737   4581   4183    322    -37   -114       C  
ATOM   1820  O   SER A 220       4.933 -11.602 -14.143  1.00 36.11           O  
ANISOU 1820  O   SER A 220     4813   4660   4246    342     -8   -155       O  
ATOM   1821  CB  SER A 220       4.226 -11.453 -17.191  1.00 39.71           C  
ANISOU 1821  CB  SER A 220     5207   5122   4758    419    -78   -100       C  
ATOM   1822  OG  SER A 220       4.083 -12.683 -17.883  1.00 45.60           O  
ANISOU 1822  OG  SER A 220     5916   5912   5497    380    -88    -76       O  
ATOM   1823  N   PHE A 221       6.053 -13.341 -15.037  1.00 32.84           N  
ANISOU 1823  N   PHE A 221     4396   4258   3825    262    -39    -90       N  
ATOM   1824  CA  PHE A 221       6.018 -14.126 -13.801  1.00 33.26           C  
ANISOU 1824  CA  PHE A 221     4456   4338   3845    211    -12   -106       C  
ATOM   1825  C   PHE A 221       7.364 -14.590 -13.238  1.00 34.81           C  
ANISOU 1825  C   PHE A 221     4703   4502   4021    159    -29    -81       C  
ATOM   1826  O   PHE A 221       7.791 -14.104 -12.185  1.00 37.41           O  
ANISOU 1826  O   PHE A 221     5075   4808   4332    143    -24    -97       O  
ATOM   1827  CB  PHE A 221       5.078 -15.335 -13.904  1.00 33.15           C  
ANISOU 1827  CB  PHE A 221     4391   4388   3818    182      6   -110       C  
ATOM   1828  CG  PHE A 221       4.981 -16.120 -12.618  1.00 36.72           C  
ANISOU 1828  CG  PHE A 221     4860   4864   4228    123     36   -124       C  
ATOM   1829  CD1 PHE A 221       5.521 -17.397 -12.523  1.00 35.05           C  
ANISOU 1829  CD1 PHE A 221     4674   4652   3993     65     23    -96       C  
ATOM   1830  CD2 PHE A 221       4.387 -15.556 -11.484  1.00 36.70           C  
ANISOU 1830  CD2 PHE A 221     4861   4879   4204    128     78   -166       C  
ATOM   1831  CE1 PHE A 221       5.445 -18.114 -11.327  1.00 36.33           C  
ANISOU 1831  CE1 PHE A 221     4865   4828   4109      7     46   -104       C  
ATOM   1832  CE2 PHE A 221       4.309 -16.265 -10.286  1.00 34.44           C  
ANISOU 1832  CE2 PHE A 221     4602   4614   3869     67    107   -178       C  
ATOM   1833  CZ  PHE A 221       4.839 -17.540 -10.208  1.00 37.84           C  
ANISOU 1833  CZ  PHE A 221     5061   5042   4276      4     88   -144       C  
ATOM   1834  N   ALA A 222       8.003 -15.550 -13.906  1.00 30.02           N  
ANISOU 1834  N   ALA A 222     4093   3894   3418    134    -51    -45       N  
ATOM   1835  CA  ALA A 222       9.192 -16.196 -13.351  1.00 31.75           C  
ANISOU 1835  CA  ALA A 222     4348   4094   3623     92    -70    -22       C  
ATOM   1836  C   ALA A 222      10.310 -15.209 -13.018  1.00 32.57           C  
ANISOU 1836  C   ALA A 222     4486   4153   3735     92    -92    -14       C  
ATOM   1837  O   ALA A 222      10.843 -15.239 -11.915  1.00 33.33           O  
ANISOU 1837  O   ALA A 222     4617   4238   3808     59   -100    -19       O  
ATOM   1838  CB  ALA A 222       9.705 -17.315 -14.279  1.00 29.36           C  
ANISOU 1838  CB  ALA A 222     4034   3794   3327     83    -88     12       C  
ATOM   1839  N   ILE A 223      10.668 -14.342 -13.963  1.00 31.43           N  
ANISOU 1839  N   ILE A 223     4338   3983   3620    120   -104     -2       N  
ATOM   1840  CA  ILE A 223      11.748 -13.375 -13.713  1.00 32.92           C  
ANISOU 1840  CA  ILE A 223     4561   4130   3817    107   -126      8       C  
ATOM   1841  C   ILE A 223      11.427 -12.447 -12.535  1.00 32.18           C  
ANISOU 1841  C   ILE A 223     4509   4014   3702    104   -118    -29       C  
ATOM   1842  O   ILE A 223      12.189 -12.412 -11.575  1.00 33.65           O  
ANISOU 1842  O   ILE A 223     4729   4187   3870     65   -135    -28       O  
ATOM   1843  CB  ILE A 223      12.181 -12.589 -14.982  1.00 30.54           C  
ANISOU 1843  CB  ILE A 223     4257   3802   3546    128   -138     31       C  
ATOM   1844  CG1 ILE A 223      12.849 -13.538 -15.986  1.00 32.23           C  
ANISOU 1844  CG1 ILE A 223     4440   4035   3773    121   -144     67       C  
ATOM   1845  CG2 ILE A 223      13.136 -11.457 -14.606  1.00 33.58           C  
ANISOU 1845  CG2 ILE A 223     4683   4142   3935    104   -159     36       C  
ATOM   1846  CD1 ILE A 223      12.736 -13.092 -17.439  1.00 28.73           C  
ANISOU 1846  CD1 ILE A 223     3989   3582   3345    148   -143     86       C  
ATOM   1847  N   PRO A 224      10.283 -11.729 -12.583  1.00 32.65           N  
ANISOU 1847  N   PRO A 224     4568   4073   3763    149    -94    -62       N  
ATOM   1848  CA  PRO A 224       9.994 -10.820 -11.459  1.00 31.59           C  
ANISOU 1848  CA  PRO A 224     4483   3914   3606    153    -80   -103       C  
ATOM   1849  C   PRO A 224       9.762 -11.501 -10.108  1.00 33.30           C  
ANISOU 1849  C   PRO A 224     4715   4159   3779    116    -58   -127       C  
ATOM   1850  O   PRO A 224      10.068 -10.912  -9.066  1.00 30.73           O  
ANISOU 1850  O   PRO A 224     4447   3805   3424     94    -60   -150       O  
ATOM   1851  CB  PRO A 224       8.741 -10.053 -11.911  1.00 32.82           C  
ANISOU 1851  CB  PRO A 224     4622   4069   3778    224    -55   -134       C  
ATOM   1852  CG  PRO A 224       8.189 -10.805 -13.082  1.00 32.86           C  
ANISOU 1852  CG  PRO A 224     4561   4116   3807    246    -56   -112       C  
ATOM   1853  CD  PRO A 224       9.320 -11.576 -13.691  1.00 30.73           C  
ANISOU 1853  CD  PRO A 224     4286   3845   3544    202    -84    -64       C  
ATOM   1854  N   TYR A 225       9.239 -12.728 -10.111  1.00 34.98           N  
ANISOU 1854  N   TYR A 225     4886   4423   3981    101    -41   -121       N  
ATOM   1855  CA  TYR A 225       9.070 -13.452  -8.852  1.00 35.33           C  
ANISOU 1855  CA  TYR A 225     4956   4492   3977     55    -22   -136       C  
ATOM   1856  C   TYR A 225      10.421 -13.799  -8.223  1.00 35.75           C  
ANISOU 1856  C   TYR A 225     5055   4518   4010      2    -67   -107       C  
ATOM   1857  O   TYR A 225      10.640 -13.559  -7.029  1.00 35.59           O  
ANISOU 1857  O   TYR A 225     5090   4484   3947    -31    -68   -126       O  
ATOM   1858  CB  TYR A 225       8.201 -14.718  -8.983  1.00 33.48           C  
ANISOU 1858  CB  TYR A 225     4677   4315   3731     39      5   -134       C  
ATOM   1859  CG  TYR A 225       7.623 -15.084  -7.640  1.00 35.39           C  
ANISOU 1859  CG  TYR A 225     4948   4583   3916      0     43   -164       C  
ATOM   1860  CD1 TYR A 225       8.357 -15.850  -6.727  1.00 36.24           C  
ANISOU 1860  CD1 TYR A 225     5110   4680   3979    -61     21   -144       C  
ATOM   1861  CD2 TYR A 225       6.372 -14.606  -7.245  1.00 34.42           C  
ANISOU 1861  CD2 TYR A 225     4802   4496   3780     25    101   -213       C  
ATOM   1862  CE1 TYR A 225       7.847 -16.149  -5.463  1.00 37.41           C  
ANISOU 1862  CE1 TYR A 225     5298   4849   4065   -105     57   -170       C  
ATOM   1863  CE2 TYR A 225       5.852 -14.906  -5.991  1.00 35.98           C  
ANISOU 1863  CE2 TYR A 225     5029   4722   3918    -17    146   -243       C  
ATOM   1864  CZ  TYR A 225       6.595 -15.677  -5.104  1.00 39.96           C  
ANISOU 1864  CZ  TYR A 225     5598   5212   4372    -86    124   -220       C  
ATOM   1865  OH  TYR A 225       6.087 -15.977  -3.858  1.00 40.40           O  
ANISOU 1865  OH  TYR A 225     5696   5295   4361   -135    169   -248       O  
ATOM   1866  N   VAL A 226      11.312 -14.365  -9.030  1.00 32.78           N  
ANISOU 1866  N   VAL A 226     4654   4137   3664     -4   -104    -63       N  
ATOM   1867  CA  VAL A 226      12.633 -14.741  -8.554  1.00 33.60           C  
ANISOU 1867  CA  VAL A 226     4783   4223   3760    -44   -152    -32       C  
ATOM   1868  C   VAL A 226      13.389 -13.510  -8.036  1.00 33.14           C  
ANISOU 1868  C   VAL A 226     4768   4125   3699    -61   -178    -41       C  
ATOM   1869  O   VAL A 226      13.923 -13.535  -6.927  1.00 31.79           O  
ANISOU 1869  O   VAL A 226     4644   3943   3491   -103   -204    -44       O  
ATOM   1870  CB  VAL A 226      13.434 -15.504  -9.633  1.00 31.36           C  
ANISOU 1870  CB  VAL A 226     4455   3945   3515    -35   -178     12       C  
ATOM   1871  CG1 VAL A 226      14.894 -15.638  -9.235  1.00 33.99           C  
ANISOU 1871  CG1 VAL A 226     4798   4263   3852    -64   -231     42       C  
ATOM   1872  CG2 VAL A 226      12.831 -16.887  -9.844  1.00 30.34           C  
ANISOU 1872  CG2 VAL A 226     4309   3846   3374    -35   -163     20       C  
ATOM   1873  N   TYR A 227      13.395 -12.435  -8.823  1.00 32.70           N  
ANISOU 1873  N   TYR A 227     4705   4044   3677    -32   -175    -46       N  
ATOM   1874  CA  TYR A 227      14.077 -11.202  -8.440  1.00 32.23           C  
ANISOU 1874  CA  TYR A 227     4694   3938   3614    -53   -200    -54       C  
ATOM   1875  C   TYR A 227      13.527 -10.622  -7.135  1.00 33.96           C  
ANISOU 1875  C   TYR A 227     4983   4139   3783    -65   -183   -101       C  
ATOM   1876  O   TYR A 227      14.294 -10.186  -6.275  1.00 35.16           O  
ANISOU 1876  O   TYR A 227     5189   4263   3907   -111   -218   -104       O  
ATOM   1877  CB  TYR A 227      13.979 -10.167  -9.562  1.00 33.19           C  
ANISOU 1877  CB  TYR A 227     4808   4029   3774    -17   -195    -51       C  
ATOM   1878  CG  TYR A 227      14.648  -8.844  -9.248  1.00 33.19           C  
ANISOU 1878  CG  TYR A 227     4869   3971   3769    -45   -222    -58       C  
ATOM   1879  CD1 TYR A 227      16.008  -8.650  -9.497  1.00 33.32           C  
ANISOU 1879  CD1 TYR A 227     4879   3976   3804    -96   -266    -21       C  
ATOM   1880  CD2 TYR A 227      13.917  -7.781  -8.723  1.00 34.00           C  
ANISOU 1880  CD2 TYR A 227     5037   4031   3850    -21   -202   -104       C  
ATOM   1881  CE1 TYR A 227      16.625  -7.434  -9.218  1.00 35.98           C  
ANISOU 1881  CE1 TYR A 227     5277   4260   4135   -136   -294    -26       C  
ATOM   1882  CE2 TYR A 227      14.524  -6.559  -8.433  1.00 37.70           C  
ANISOU 1882  CE2 TYR A 227     5577   4436   4309    -52   -230   -113       C  
ATOM   1883  CZ  TYR A 227      15.875  -6.394  -8.684  1.00 39.19           C  
ANISOU 1883  CZ  TYR A 227     5762   4614   4514   -115   -278    -72       C  
ATOM   1884  OH  TYR A 227      16.472  -5.185  -8.410  1.00 44.35           O  
ANISOU 1884  OH  TYR A 227     6490   5204   5157   -158   -308    -79       O  
ATOM   1885  N   ASN A 228      12.203 -10.624  -6.998  1.00 33.90           N  
ANISOU 1885  N   ASN A 228     4971   4150   3761    -24   -129   -140       N  
ATOM   1886  CA  ASN A 228      11.539 -10.045  -5.832  1.00 33.80           C  
ANISOU 1886  CA  ASN A 228     5021   4124   3698    -24    -96   -193       C  
ATOM   1887  C   ASN A 228      11.597 -10.911  -4.591  1.00 35.30           C  
ANISOU 1887  C   ASN A 228     5244   4340   3828    -78    -94   -198       C  
ATOM   1888  O   ASN A 228      11.648 -10.382  -3.481  1.00 36.34           O  
ANISOU 1888  O   ASN A 228     5451   4448   3908   -105    -91   -231       O  
ATOM   1889  CB  ASN A 228      10.098  -9.651  -6.154  1.00 32.95           C  
ANISOU 1889  CB  ASN A 228     4885   4034   3600     45    -35   -235       C  
ATOM   1890  CG  ASN A 228      10.017  -8.363  -6.958  1.00 36.89           C  
ANISOU 1890  CG  ASN A 228     5397   4482   4138    100    -42   -244       C  
ATOM   1891  OD1 ASN A 228      10.471  -7.316  -6.509  1.00 41.31           O  
ANISOU 1891  OD1 ASN A 228     6031   4981   4682     91    -60   -263       O  
ATOM   1892  ND2 ASN A 228       9.454  -8.440  -8.159  1.00 37.27           N  
ANISOU 1892  ND2 ASN A 228     5380   4548   4232    153    -34   -230       N  
ATOM   1893  N   ARG A 229      11.605 -12.232  -4.779  1.00 33.12           N  
ANISOU 1893  N   ARG A 229     4923   4107   3553    -96    -98   -166       N  
ATOM   1894  CA  ARG A 229      11.754 -13.169  -3.670  1.00 33.89           C  
ANISOU 1894  CA  ARG A 229     5061   4223   3592   -151   -106   -160       C  
ATOM   1895  C   ARG A 229      13.148 -13.070  -3.072  1.00 34.31           C  
ANISOU 1895  C   ARG A 229     5163   4244   3630   -201   -180   -132       C  
ATOM   1896  O   ARG A 229      13.314 -13.008  -1.855  1.00 36.54           O  
ANISOU 1896  O   ARG A 229     5519   4516   3851   -246   -192   -148       O  
ATOM   1897  CB  ARG A 229      11.485 -14.608  -4.129  1.00 32.40           C  
ANISOU 1897  CB  ARG A 229     4823   4076   3413   -157   -101   -127       C  
ATOM   1898  CG  ARG A 229      11.544 -15.630  -3.003  1.00 34.02           C  
ANISOU 1898  CG  ARG A 229     5080   4295   3552   -215   -109   -118       C  
ATOM   1899  CD  ARG A 229      10.357 -15.474  -2.070  1.00 31.63           C  
ANISOU 1899  CD  ARG A 229     4814   4017   3189   -231    -39   -168       C  
ATOM   1900  NE  ARG A 229      10.436 -16.373  -0.928  1.00 32.48           N  
ANISOU 1900  NE  ARG A 229     4988   4132   3222   -296    -47   -158       N  
ATOM   1901  CZ  ARG A 229       9.737 -16.223   0.197  1.00 34.86           C  
ANISOU 1901  CZ  ARG A 229     5348   4448   3448   -331      5   -197       C  
ATOM   1902  NH1 ARG A 229       8.901 -15.198   0.341  1.00 32.24           N  
ANISOU 1902  NH1 ARG A 229     5010   4128   3113   -296     70   -255       N  
ATOM   1903  NH2 ARG A 229       9.883 -17.095   1.188  1.00 32.87           N  
ANISOU 1903  NH2 ARG A 229     5166   4199   3123   -397     -9   -180       N  
ATOM   1904  N   ILE A 230      14.148 -13.056  -3.945  1.00 36.31           N  
ANISOU 1904  N   ILE A 230     5372   4486   3938   -195   -229    -91       N  
ATOM   1905  CA  ILE A 230      15.534 -12.867  -3.540  1.00 34.99           C  
ANISOU 1905  CA  ILE A 230     5227   4296   3770   -239   -303    -62       C  
ATOM   1906  C   ILE A 230      15.712 -11.495  -2.886  1.00 36.32           C  
ANISOU 1906  C   ILE A 230     5467   4421   3913   -264   -312    -97       C  
ATOM   1907  O   ILE A 230      16.371 -11.393  -1.848  1.00 38.21           O  
ANISOU 1907  O   ILE A 230     5767   4645   4107   -318   -360    -96       O  
ATOM   1908  CB  ILE A 230      16.502 -13.111  -4.718  1.00 34.46           C  
ANISOU 1908  CB  ILE A 230     5085   4238   3773   -224   -339    -15       C  
ATOM   1909  CG1 ILE A 230      16.497 -14.605  -5.065  1.00 31.74           C  
ANISOU 1909  CG1 ILE A 230     4695   3927   3438   -208   -342     17       C  
ATOM   1910  CG2 ILE A 230      17.922 -12.617  -4.389  1.00 34.98           C  
ANISOU 1910  CG2 ILE A 230     5158   4285   3846   -271   -412      9       C  
ATOM   1911  CD1 ILE A 230      17.164 -14.952  -6.365  1.00 28.18           C  
ANISOU 1911  CD1 ILE A 230     4167   3489   3052   -178   -354     54       C  
ATOM   1912  N   LYS A 231      15.091 -10.463  -3.460  1.00 36.15           N  
ANISOU 1912  N   LYS A 231     5447   4375   3913   -223   -271   -128       N  
ATOM   1913  CA  LYS A 231      15.114  -9.125  -2.869  1.00 38.00           C  
ANISOU 1913  CA  LYS A 231     5764   4557   4120   -238   -274   -167       C  
ATOM   1914  C   LYS A 231      14.520  -9.118  -1.456  1.00 38.26           C  
ANISOU 1914  C   LYS A 231     5881   4586   4071   -261   -247   -214       C  
ATOM   1915  O   LYS A 231      15.088  -8.509  -0.549  1.00 36.04           O  
ANISOU 1915  O   LYS A 231     5682   4267   3744   -311   -284   -229       O  
ATOM   1916  CB  LYS A 231      14.401  -8.099  -3.760  1.00 38.49           C  
ANISOU 1916  CB  LYS A 231     5819   4588   4219   -176   -232   -193       C  
ATOM   1917  CG  LYS A 231      14.522  -6.656  -3.246  1.00 46.18           C  
ANISOU 1917  CG  LYS A 231     6889   5490   5166   -188   -241   -232       C  
ATOM   1918  CD  LYS A 231      13.787  -5.634  -4.122  1.00 49.39           C  
ANISOU 1918  CD  LYS A 231     7300   5857   5608   -117   -205   -256       C  
ATOM   1919  CE  LYS A 231      12.281  -5.647  -3.872  1.00 55.24           C  
ANISOU 1919  CE  LYS A 231     8038   6618   6332    -43   -129   -310       C  
ATOM   1920  NZ  LYS A 231      11.601  -4.432  -4.410  1.00 59.58           N  
ANISOU 1920  NZ  LYS A 231     8619   7113   6904     31   -104   -344       N  
ATOM   1921  N   ASN A 232      13.393  -9.809  -1.271  1.00 39.13           N  
ANISOU 1921  N   ASN A 232     5972   4738   4160   -231   -183   -236       N  
ATOM   1922  CA  ASN A 232      12.756  -9.898   0.056  1.00 43.56           C  
ANISOU 1922  CA  ASN A 232     6608   5305   4636   -256   -144   -280       C  
ATOM   1923  C   ASN A 232      13.589 -10.637   1.116  1.00 42.85           C  
ANISOU 1923  C   ASN A 232     6575   5220   4487   -334   -202   -253       C  
ATOM   1924  O   ASN A 232      13.644 -10.209   2.269  1.00 46.08           O  
ANISOU 1924  O   ASN A 232     7081   5605   4822   -376   -206   -286       O  
ATOM   1925  CB  ASN A 232      11.349 -10.507  -0.035  1.00 43.97           C  
ANISOU 1925  CB  ASN A 232     6616   5412   4681   -215    -58   -307       C  
ATOM   1926  CG  ASN A 232      10.350  -9.584  -0.713  1.00 46.26           C  
ANISOU 1926  CG  ASN A 232     6871   5695   5010   -135      3   -351       C  
ATOM   1927  OD1 ASN A 232      10.624  -8.399  -0.937  1.00 48.03           O  
ANISOU 1927  OD1 ASN A 232     7132   5863   5253   -109    -13   -369       O  
ATOM   1928  ND2 ASN A 232       9.180 -10.125  -1.050  1.00 42.49           N  
ANISOU 1928  ND2 ASN A 232     6325   5274   4544    -95     68   -366       N  
ATOM   1929  N   ILE A 233      14.234 -11.733   0.716  1.00 42.32           N  
ANISOU 1929  N   ILE A 233     6451   5180   4449   -350   -251   -195       N  
ATOM   1930  CA  ILE A 233      15.030 -12.565   1.627  1.00 40.49           C  
ANISOU 1930  CA  ILE A 233     6264   4953   4166   -413   -316   -161       C  
ATOM   1931  C   ILE A 233      16.430 -12.003   1.897  1.00 41.94           C  
ANISOU 1931  C   ILE A 233     6476   5104   4357   -458   -411   -136       C  
ATOM   1932  O   ILE A 233      16.889 -12.003   3.046  1.00 43.67           O  
ANISOU 1932  O   ILE A 233     6778   5308   4507   -516   -459   -138       O  
ATOM   1933  CB  ILE A 233      15.152 -14.020   1.105  1.00 40.50           C  
ANISOU 1933  CB  ILE A 233     6201   4992   4197   -404   -332   -109       C  
ATOM   1934  CG1 ILE A 233      13.779 -14.712   1.087  1.00 40.89           C  
ANISOU 1934  CG1 ILE A 233     6239   5077   4222   -386   -246   -131       C  
ATOM   1935  CG2 ILE A 233      16.146 -14.816   1.943  1.00 37.98           C  
ANISOU 1935  CG2 ILE A 233     5926   4668   3837   -457   -418    -66       C  
ATOM   1936  CD1 ILE A 233      13.735 -16.009   0.261  1.00 38.50           C  
ANISOU 1936  CD1 ILE A 233     5867   4802   3960   -367   -252    -86       C  
ATOM   1937  N   PHE A 234      17.102 -11.521   0.851  1.00 40.55           N  
ANISOU 1937  N   PHE A 234     6230   4918   4258   -436   -440   -112       N  
ATOM   1938  CA  PHE A 234      18.521 -11.167   0.956  1.00 41.54           C  
ANISOU 1938  CA  PHE A 234     6353   5028   4401   -484   -533    -79       C  
ATOM   1939  C   PHE A 234      18.817  -9.678   0.753  1.00 41.87           C  
ANISOU 1939  C   PHE A 234     6427   5024   4459   -501   -541   -104       C  
ATOM   1940  O   PHE A 234      19.856  -9.192   1.184  1.00 41.51           O  
ANISOU 1940  O   PHE A 234     6409   4960   4404   -562   -616    -91       O  
ATOM   1941  CB  PHE A 234      19.358 -11.976  -0.044  1.00 40.19           C  
ANISOU 1941  CB  PHE A 234     6071   4891   4307   -462   -573    -20       C  
ATOM   1942  CG  PHE A 234      19.264 -13.470   0.129  1.00 42.41           C  
ANISOU 1942  CG  PHE A 234     6331   5206   4577   -448   -582     11       C  
ATOM   1943  CD1 PHE A 234      18.523 -14.241  -0.769  1.00 41.18           C  
ANISOU 1943  CD1 PHE A 234     6116   5074   4455   -391   -523     18       C  
ATOM   1944  CD2 PHE A 234      19.937 -14.114   1.173  1.00 41.68           C  
ANISOU 1944  CD2 PHE A 234     6284   5117   4435   -492   -657     37       C  
ATOM   1945  CE1 PHE A 234      18.444 -15.640  -0.629  1.00 40.35           C  
ANISOU 1945  CE1 PHE A 234     6004   4990   4337   -382   -534     47       C  
ATOM   1946  CE2 PHE A 234      19.865 -15.504   1.321  1.00 43.23           C  
ANISOU 1946  CE2 PHE A 234     6474   5334   4619   -477   -671     68       C  
ATOM   1947  CZ  PHE A 234      19.118 -16.270   0.417  1.00 41.32           C  
ANISOU 1947  CZ  PHE A 234     6178   5109   4412   -423   -607     73       C  
ATOM   1948  N   GLY A 235      17.916  -8.960   0.089  1.00 42.65           N  
ANISOU 1948  N   GLY A 235     6523   5103   4581   -449   -469   -140       N  
ATOM   1949  CA  GLY A 235      18.149  -7.548  -0.223  1.00 43.28           C  
ANISOU 1949  CA  GLY A 235     6641   5127   4677   -458   -475   -161       C  
ATOM   1950  C   GLY A 235      18.381  -7.333  -1.707  1.00 43.89           C  
ANISOU 1950  C   GLY A 235     6628   5208   4838   -422   -467   -129       C  
ATOM   1951  O   GLY A 235      18.548  -8.294  -2.465  1.00 42.62           O  
ANISOU 1951  O   GLY A 235     6374   5096   4725   -395   -465    -89       O  
ATOM   1952  N   GLU A 236      18.399  -6.069  -2.121  1.00 45.36           N  
ANISOU 1952  N   GLU A 236     6856   5340   5040   -422   -462   -148       N  
ATOM   1953  CA  GLU A 236      18.502  -5.720  -3.537  1.00 47.47           C  
ANISOU 1953  CA  GLU A 236     7058   5601   5376   -389   -448   -121       C  
ATOM   1954  C   GLU A 236      19.787  -6.207  -4.209  1.00 47.46           C  
ANISOU 1954  C   GLU A 236     6967   5640   5426   -431   -501    -59       C  
ATOM   1955  O   GLU A 236      19.729  -6.780  -5.301  1.00 47.12           O  
ANISOU 1955  O   GLU A 236     6837   5633   5434   -389   -476    -29       O  
ATOM   1956  CB  GLU A 236      18.319  -4.215  -3.757  1.00 51.11           C  
ANISOU 1956  CB  GLU A 236     7602   5983   5834   -388   -440   -151       C  
ATOM   1957  CG  GLU A 236      16.870  -3.814  -4.005  1.00 57.73           C  
ANISOU 1957  CG  GLU A 236     8471   6796   6669   -296   -366   -199       C  
ATOM   1958  CD  GLU A 236      16.711  -2.505  -4.781  1.00 64.67           C  
ANISOU 1958  CD  GLU A 236     9400   7599   7571   -271   -360   -209       C  
ATOM   1959  OE1 GLU A 236      17.701  -1.747  -4.943  1.00 65.98           O  
ANISOU 1959  OE1 GLU A 236     9605   7721   7743   -340   -411   -187       O  
ATOM   1960  OE2 GLU A 236      15.575  -2.234  -5.230  1.00 66.70           O  
ANISOU 1960  OE2 GLU A 236     9660   7843   7841   -182   -307   -238       O  
ATOM   1961  N   SER A 237      20.933  -5.978  -3.562  1.00 46.48           N  
ANISOU 1961  N   SER A 237     6861   5512   5287   -514   -572    -42       N  
ATOM   1962  CA  SER A 237      22.238  -6.287  -4.154  1.00 44.74           C  
ANISOU 1962  CA  SER A 237     6547   5333   5117   -558   -623     14       C  
ATOM   1963  C   SER A 237      22.359  -7.763  -4.526  1.00 43.63           C  
ANISOU 1963  C   SER A 237     6304   5264   5009   -512   -617     48       C  
ATOM   1964  O   SER A 237      22.993  -8.115  -5.531  1.00 42.92           O  
ANISOU 1964  O   SER A 237     6120   5212   4977   -503   -618     88       O  
ATOM   1965  CB  SER A 237      23.379  -5.893  -3.212  1.00 45.71           C  
ANISOU 1965  CB  SER A 237     6703   5451   5214   -656   -709     24       C  
ATOM   1966  OG  SER A 237      23.679  -6.944  -2.298  1.00 47.47           O  
ANISOU 1966  OG  SER A 237     6909   5717   5410   -664   -753     36       O  
ATOM   1967  N   THR A 238      21.761  -8.624  -3.707  1.00 40.36           N  
ANISOU 1967  N   THR A 238     5916   4865   4554   -487   -610     33       N  
ATOM   1968  CA  THR A 238      21.720 -10.040  -4.023  1.00 39.12           C  
ANISOU 1968  CA  THR A 238     5683   4761   4418   -441   -602     61       C  
ATOM   1969  C   THR A 238      20.754 -10.300  -5.189  1.00 37.26           C  
ANISOU 1969  C   THR A 238     5407   4533   4216   -367   -525     56       C  
ATOM   1970  O   THR A 238      21.043 -11.127  -6.043  1.00 38.13           O  
ANISOU 1970  O   THR A 238     5437   4681   4371   -334   -518     88       O  
ATOM   1971  CB  THR A 238      21.363 -10.893  -2.788  1.00 38.30           C  
ANISOU 1971  CB  THR A 238     5633   4666   4253   -447   -619     50       C  
ATOM   1972  OG1 THR A 238      22.189 -10.497  -1.687  1.00 42.74           O  
ANISOU 1972  OG1 THR A 238     6249   5216   4776   -519   -695     52       O  
ATOM   1973  CG2 THR A 238      21.585 -12.377  -3.059  1.00 34.65           C  
ANISOU 1973  CG2 THR A 238     5101   4250   3814   -410   -631     88       C  
ATOM   1974  N   ALA A 239      19.629  -9.586  -5.237  1.00 35.37           N  
ANISOU 1974  N   ALA A 239     5224   4257   3956   -338   -470     14       N  
ATOM   1975  CA  ALA A 239      18.678  -9.769  -6.340  1.00 37.27           C  
ANISOU 1975  CA  ALA A 239     5425   4507   4228   -270   -407      9       C  
ATOM   1976  C   ALA A 239      19.303  -9.363  -7.673  1.00 36.98           C  
ANISOU 1976  C   ALA A 239     5332   4471   4250   -265   -408     41       C  
ATOM   1977  O   ALA A 239      19.099 -10.028  -8.696  1.00 34.77           O  
ANISOU 1977  O   ALA A 239     4988   4220   4003   -222   -380     61       O  
ATOM   1978  CB  ALA A 239      17.380  -9.004  -6.090  1.00 37.03           C  
ANISOU 1978  CB  ALA A 239     5459   4441   4168   -234   -354    -43       C  
ATOM   1979  N   LYS A 240      20.093  -8.289  -7.633  1.00 37.47           N  
ANISOU 1979  N   LYS A 240     5422   4500   4316   -319   -441     47       N  
ATOM   1980  CA  LYS A 240      20.775  -7.758  -8.813  1.00 37.96           C  
ANISOU 1980  CA  LYS A 240     5441   4559   4423   -333   -442     78       C  
ATOM   1981  C   LYS A 240      21.845  -8.685  -9.405  1.00 37.01           C  
ANISOU 1981  C   LYS A 240     5218   4500   4345   -343   -461    125       C  
ATOM   1982  O   LYS A 240      22.285  -8.485 -10.536  1.00 37.91           O  
ANISOU 1982  O   LYS A 240     5284   4626   4496   -344   -444    151       O  
ATOM   1983  CB  LYS A 240      21.327  -6.363  -8.522  1.00 39.14           C  
ANISOU 1983  CB  LYS A 240     5658   4653   4561   -401   -474     71       C  
ATOM   1984  CG  LYS A 240      20.214  -5.344  -8.298  1.00 38.66           C  
ANISOU 1984  CG  LYS A 240     5699   4522   4469   -369   -444     25       C  
ATOM   1985  CD  LYS A 240      20.759  -3.968  -8.028  1.00 39.65           C  
ANISOU 1985  CD  LYS A 240     5908   4579   4577   -437   -478     17       C  
ATOM   1986  CE  LYS A 240      19.654  -2.947  -8.004  1.00 39.65           C  
ANISOU 1986  CE  LYS A 240     6009   4503   4554   -388   -445    -28       C  
ATOM   1987  NZ  LYS A 240      20.251  -1.592  -7.887  1.00 46.09           N  
ANISOU 1987  NZ  LYS A 240     6916   5241   5354   -458   -481    -31       N  
ATOM   1988  N   ARG A 241      22.222  -9.721  -8.663  1.00 36.81           N  
ANISOU 1988  N   ARG A 241     5162   4513   4311   -345   -492    134       N  
ATOM   1989  CA  ARG A 241      23.131 -10.747  -9.174  1.00 36.15           C  
ANISOU 1989  CA  ARG A 241     4981   4487   4267   -333   -507    173       C  
ATOM   1990  C   ARG A 241      22.572 -11.526 -10.381  1.00 35.02           C  
ANISOU 1990  C   ARG A 241     4790   4365   4150   -263   -450    181       C  
ATOM   1991  O   ARG A 241      23.301 -12.274 -11.038  1.00 35.72           O  
ANISOU 1991  O   ARG A 241     4801   4496   4275   -244   -450    209       O  
ATOM   1992  CB  ARG A 241      23.563 -11.694  -8.046  1.00 35.91           C  
ANISOU 1992  CB  ARG A 241     4945   4481   4217   -341   -561    180       C  
ATOM   1993  CG  ARG A 241      24.613 -11.079  -7.105  1.00 37.75           C  
ANISOU 1993  CG  ARG A 241     5190   4714   4440   -419   -636    189       C  
ATOM   1994  CD  ARG A 241      25.007 -12.021  -5.993  1.00 36.09           C  
ANISOU 1994  CD  ARG A 241     4982   4526   4205   -423   -697    199       C  
ATOM   1995  NE  ARG A 241      25.467 -13.313  -6.502  1.00 34.54           N  
ANISOU 1995  NE  ARG A 241     4699   4376   4047   -368   -702    230       N  
ATOM   1996  CZ  ARG A 241      25.468 -14.444  -5.806  1.00 34.30           C  
ANISOU 1996  CZ  ARG A 241     4680   4357   3997   -340   -737    240       C  
ATOM   1997  NH1 ARG A 241      25.038 -14.456  -4.548  1.00 39.98           N  
ANISOU 1997  NH1 ARG A 241     5490   5049   4653   -370   -769    224       N  
ATOM   1998  NH2 ARG A 241      25.911 -15.565  -6.363  1.00 32.31           N  
ANISOU 1998  NH2 ARG A 241     4354   4138   3783   -282   -739    267       N  
ATOM   1999  N   LEU A 242      21.290 -11.334 -10.679  1.00 34.56           N  
ANISOU 1999  N   LEU A 242     4778   4279   4074   -223   -404    154       N  
ATOM   2000  CA  LEU A 242      20.682 -11.918 -11.878  1.00 35.22           C  
ANISOU 2000  CA  LEU A 242     4826   4378   4177   -165   -355    160       C  
ATOM   2001  C   LEU A 242      21.100 -11.159 -13.137  1.00 35.31           C  
ANISOU 2001  C   LEU A 242     4814   4385   4219   -174   -333    180       C  
ATOM   2002  O   LEU A 242      20.928 -11.644 -14.255  1.00 31.57           O  
ANISOU 2002  O   LEU A 242     4304   3929   3762   -136   -299    192       O  
ATOM   2003  CB  LEU A 242      19.157 -11.958 -11.755  1.00 36.49           C  
ANISOU 2003  CB  LEU A 242     5036   4520   4311   -124   -318    126       C  
ATOM   2004  CG  LEU A 242      18.588 -12.958 -10.747  1.00 34.12           C  
ANISOU 2004  CG  LEU A 242     4753   4233   3976   -114   -322    110       C  
ATOM   2005  CD1 LEU A 242      17.115 -12.665 -10.514  1.00 35.28           C  
ANISOU 2005  CD1 LEU A 242     4943   4365   4095    -86   -282     71       C  
ATOM   2006  CD2 LEU A 242      18.789 -14.383 -11.261  1.00 33.92           C  
ANISOU 2006  CD2 LEU A 242     4678   4243   3967    -84   -318    134       C  
ATOM   2007  N   SER A 243      21.651  -9.965 -12.943  1.00 33.87           N  
ANISOU 2007  N   SER A 243     4660   4174   4036   -230   -355    182       N  
ATOM   2008  CA  SER A 243      22.298  -9.242 -14.023  1.00 36.11           C  
ANISOU 2008  CA  SER A 243     4923   4455   4343   -259   -341    208       C  
ATOM   2009  C   SER A 243      23.826  -9.405 -13.944  1.00 36.86           C  
ANISOU 2009  C   SER A 243     4944   4596   4466   -315   -371    239       C  
ATOM   2010  O   SER A 243      24.416  -9.137 -12.892  1.00 40.81           O  
ANISOU 2010  O   SER A 243     5453   5095   4959   -367   -421    237       O  
ATOM   2011  CB  SER A 243      21.936  -7.759 -13.954  1.00 33.86           C  
ANISOU 2011  CB  SER A 243     4724   4103   4040   -292   -346    194       C  
ATOM   2012  OG  SER A 243      22.885  -6.992 -14.672  1.00 35.90           O  
ANISOU 2012  OG  SER A 243     4969   4358   4315   -353   -348    224       O  
ATOM   2013  N   PRO A 244      24.474  -9.812 -15.058  1.00 35.74           N  
ANISOU 2013  N   PRO A 244     4728   4498   4354   -307   -341    267       N  
ATOM   2014  CA  PRO A 244      25.939  -9.976 -15.090  1.00 36.16           C  
ANISOU 2014  CA  PRO A 244     4692   4608   4441   -354   -362    296       C  
ATOM   2015  C   PRO A 244      26.699  -8.681 -14.827  1.00 37.34           C  
ANISOU 2015  C   PRO A 244     4859   4740   4590   -453   -392    307       C  
ATOM   2016  O   PRO A 244      27.881  -8.726 -14.499  1.00 39.63           O  
ANISOU 2016  O   PRO A 244     5076   5079   4904   -505   -425    327       O  
ATOM   2017  CB  PRO A 244      26.215 -10.456 -16.519  1.00 37.73           C  
ANISOU 2017  CB  PRO A 244     4828   4846   4661   -322   -303    316       C  
ATOM   2018  CG  PRO A 244      25.032 -10.014 -17.308  1.00 36.62           C  
ANISOU 2018  CG  PRO A 244     4764   4654   4495   -291   -263    304       C  
ATOM   2019  CD  PRO A 244      23.868 -10.117 -16.365  1.00 34.51           C  
ANISOU 2019  CD  PRO A 244     4568   4344   4201   -255   -285    272       C  
ATOM   2020  N   HIS A 245      26.024  -7.543 -14.974  1.00 36.88           N  
ANISOU 2020  N   HIS A 245     4896   4612   4503   -478   -383    295       N  
ATOM   2021  CA  HIS A 245      26.616  -6.232 -14.695  1.00 36.77           C  
ANISOU 2021  CA  HIS A 245     4927   4562   4481   -577   -414    303       C  
ATOM   2022  C   HIS A 245      26.054  -5.629 -13.418  1.00 37.59           C  
ANISOU 2022  C   HIS A 245     5131   4602   4548   -593   -459    269       C  
ATOM   2023  O   HIS A 245      26.302  -4.467 -13.127  1.00 37.86           O  
ANISOU 2023  O   HIS A 245     5234   4585   4565   -668   -486    267       O  
ATOM   2024  CB  HIS A 245      26.354  -5.261 -15.846  1.00 35.87           C  
ANISOU 2024  CB  HIS A 245     4868   4403   4358   -599   -374    316       C  
ATOM   2025  CG  HIS A 245      26.589  -5.848 -17.201  1.00 35.31           C  
ANISOU 2025  CG  HIS A 245     4726   4383   4308   -569   -316    342       C  
ATOM   2026  ND1 HIS A 245      27.795  -6.402 -17.575  1.00 36.90           N  
ANISOU 2026  ND1 HIS A 245     4810   4668   4543   -600   -304    369       N  
ATOM   2027  CD2 HIS A 245      25.781  -5.942 -18.283  1.00 34.23           C  
ANISOU 2027  CD2 HIS A 245     4619   4226   4160   -511   -268    344       C  
ATOM   2028  CE1 HIS A 245      27.710  -6.833 -18.821  1.00 37.25           C  
ANISOU 2028  CE1 HIS A 245     4822   4739   4591   -561   -243    383       C  
ATOM   2029  NE2 HIS A 245      26.502  -6.557 -19.277  1.00 33.32           N  
ANISOU 2029  NE2 HIS A 245     4416   4178   4065   -511   -224    370       N  
ATOM   2030  N   ARG A 246      25.279  -6.419 -12.678  1.00 40.34           N  
ANISOU 2030  N   ARG A 246     5495   4952   4881   -526   -464    242       N  
ATOM   2031  CA  ARG A 246      24.652  -5.990 -11.408  1.00 43.63           C  
ANISOU 2031  CA  ARG A 246     6006   5314   5255   -532   -497    204       C  
ATOM   2032  C   ARG A 246      23.804  -4.710 -11.495  1.00 44.18           C  
ANISOU 2032  C   ARG A 246     6195   5296   5297   -534   -481    177       C  
ATOM   2033  O   ARG A 246      23.694  -3.955 -10.523  1.00 43.04           O  
ANISOU 2033  O   ARG A 246     6138   5098   5118   -571   -513    150       O  
ATOM   2034  CB  ARG A 246      25.691  -5.863 -10.284  1.00 44.92           C  
ANISOU 2034  CB  ARG A 246     6161   5496   5411   -614   -567    210       C  
ATOM   2035  CG  ARG A 246      26.672  -7.029 -10.170  1.00 48.27           C  
ANISOU 2035  CG  ARG A 246     6464   6006   5869   -611   -595    239       C  
ATOM   2036  CD  ARG A 246      25.993  -8.342  -9.820  1.00 50.71           C  
ANISOU 2036  CD  ARG A 246     6757   6339   6170   -524   -583    228       C  
ATOM   2037  NE  ARG A 246      26.975  -9.410  -9.642  1.00 56.20           N  
ANISOU 2037  NE  ARG A 246     7351   7106   6897   -517   -619    256       N  
ATOM   2038  CZ  ARG A 246      27.287 -10.320 -10.562  1.00 59.56           C  
ANISOU 2038  CZ  ARG A 246     7683   7584   7363   -463   -586    278       C  
ATOM   2039  NH1 ARG A 246      26.693 -10.317 -11.752  1.00 59.59           N  
ANISOU 2039  NH1 ARG A 246     7685   7578   7377   -419   -517    277       N  
ATOM   2040  NH2 ARG A 246      28.202 -11.239 -10.289  1.00 60.70           N  
ANISOU 2040  NH2 ARG A 246     7740   7787   7535   -450   -626    301       N  
ATOM   2041  N   LYS A 247      23.210  -4.465 -12.659  1.00 44.46           N  
ANISOU 2041  N   LYS A 247     6239   5310   5343   -489   -434    185       N  
ATOM   2042  CA  LYS A 247      22.253  -3.369 -12.792  1.00 47.10           C  
ANISOU 2042  CA  LYS A 247     6684   5558   5653   -464   -421    159       C  
ATOM   2043  C   LYS A 247      20.899  -3.881 -13.272  1.00 45.64           C  
ANISOU 2043  C   LYS A 247     6499   5375   5468   -356   -376    139       C  
ATOM   2044  O   LYS A 247      20.828  -4.707 -14.182  1.00 43.90           O  
ANISOU 2044  O   LYS A 247     6205   5204   5271   -318   -347    161       O  
ATOM   2045  CB  LYS A 247      22.776  -2.253 -13.707  1.00 47.78           C  
ANISOU 2045  CB  LYS A 247     6811   5599   5744   -524   -421    187       C  
ATOM   2046  CG  LYS A 247      21.763  -1.109 -13.896  1.00 51.83           C  
ANISOU 2046  CG  LYS A 247     7449   6012   6233   -486   -413    162       C  
ATOM   2047  CD  LYS A 247      22.381   0.180 -14.421  1.00 55.29           C  
ANISOU 2047  CD  LYS A 247     7965   6381   6663   -569   -431    187       C  
ATOM   2048  CE  LYS A 247      21.338   1.297 -14.527  1.00 58.29           C  
ANISOU 2048  CE  LYS A 247     8480   6651   7017   -517   -430    160       C  
ATOM   2049  NZ  LYS A 247      20.550   1.494 -13.264  1.00 60.39           N  
ANISOU 2049  NZ  LYS A 247     8813   6874   7257   -468   -441    100       N  
ATOM   2050  N   THR A 248      19.838  -3.397 -12.630  1.00 46.08           N  
ANISOU 2050  N   THR A 248     6633   5377   5497   -309   -370     94       N  
ATOM   2051  CA  THR A 248      18.471  -3.714 -13.020  1.00 48.77           C  
ANISOU 2051  CA  THR A 248     6973   5719   5838   -210   -331     71       C  
ATOM   2052  C   THR A 248      17.598  -2.470 -12.955  1.00 54.55           C  
ANISOU 2052  C   THR A 248     7809   6364   6552   -171   -328     38       C  
ATOM   2053  O   THR A 248      17.950  -1.484 -12.301  1.00 55.58           O  
ANISOU 2053  O   THR A 248     8026   6431   6661   -217   -354     22       O  
ATOM   2054  CB  THR A 248      17.825  -4.775 -12.102  1.00 46.74           C  
ANISOU 2054  CB  THR A 248     6681   5510   5568   -170   -317     41       C  
ATOM   2055  OG1 THR A 248      17.677  -4.240 -10.782  1.00 46.19           O  
ANISOU 2055  OG1 THR A 248     6686   5402   5461   -190   -333      0       O  
ATOM   2056  CG2 THR A 248      18.640  -6.071 -12.060  1.00 43.88           C  
ANISOU 2056  CG2 THR A 248     6228   5224   5221   -197   -327     71       C  
ATOM   2057  N   ARG A 249      16.451  -2.530 -13.624  1.00 59.70           N  
ANISOU 2057  N   ARG A 249     8455   7013   7213    -82   -299     27       N  
ATOM   2058  CA  ARG A 249      15.442  -1.488 -13.517  1.00 65.82           C  
ANISOU 2058  CA  ARG A 249     9317   7714   7976    -18   -294    -10       C  
ATOM   2059  C   ARG A 249      14.069  -2.134 -13.338  1.00 68.69           C  
ANISOU 2059  C   ARG A 249     9636   8120   8343     78   -258    -47       C  
ATOM   2060  O   ARG A 249      13.818  -3.223 -13.859  1.00 67.77           O  
ANISOU 2060  O   ARG A 249     9430   8075   8243     99   -241    -29       O  
ATOM   2061  CB  ARG A 249      15.466  -0.595 -14.762  1.00 67.92           C  
ANISOU 2061  CB  ARG A 249     9632   7921   8255     -9   -306     22       C  
ATOM   2062  CG  ARG A 249      15.187   0.883 -14.493  1.00 74.20           C  
ANISOU 2062  CG  ARG A 249    10558   8604   9030      6   -326     -4       C  
ATOM   2063  CD  ARG A 249      16.353   1.565 -13.752  1.00 80.41           C  
ANISOU 2063  CD  ARG A 249    11416   9343   9794   -104   -358     -1       C  
ATOM   2064  NE  ARG A 249      17.524   1.764 -14.610  1.00 83.03           N  
ANISOU 2064  NE  ARG A 249    11739   9673  10135   -198   -378     59       N  
ATOM   2065  CZ  ARG A 249      17.787   2.881 -15.287  1.00 85.53           C  
ANISOU 2065  CZ  ARG A 249    12149   9904  10443   -231   -398     83       C  
ATOM   2066  NH1 ARG A 249      16.968   3.925 -15.214  1.00 86.97           N  
ANISOU 2066  NH1 ARG A 249    12449   9986  10610   -167   -408     53       N  
ATOM   2067  NH2 ARG A 249      18.877   2.959 -16.041  1.00 86.27           N  
ANISOU 2067  NH2 ARG A 249    12223  10013  10542   -327   -407    137       N  
ATOM   2068  N   VAL A 250      13.198  -1.465 -12.585  1.00 74.42           N  
ANISOU 2068  N   VAL A 250    10423   8803   9051    133   -246   -100       N  
ATOM   2069  CA  VAL A 250      11.817  -1.911 -12.389  1.00 80.07           C  
ANISOU 2069  CA  VAL A 250    11094   9559   9769    225   -207   -140       C  
ATOM   2070  C   VAL A 250      10.883  -0.972 -13.168  1.00 86.18           C  
ANISOU 2070  C   VAL A 250    11905  10277  10560    318   -209   -151       C  
ATOM   2071  O   VAL A 250      10.567   0.133 -12.709  1.00 86.46           O  
ANISOU 2071  O   VAL A 250    12034  10236  10583    355   -212   -188       O  
ATOM   2072  CB  VAL A 250      11.435  -1.964 -10.881  1.00 79.94           C  
ANISOU 2072  CB  VAL A 250    11106   9550   9717    227   -181   -198       C  
ATOM   2073  CG1 VAL A 250      10.110  -2.688 -10.682  1.00 79.50           C  
ANISOU 2073  CG1 VAL A 250    10978   9564   9665    302   -133   -233       C  
ATOM   2074  CG2 VAL A 250      12.532  -2.641 -10.060  1.00 78.39           C  
ANISOU 2074  CG2 VAL A 250    10902   9386   9497    128   -198   -183       C  
ATOM   2075  N   LYS A 251      10.448  -1.423 -14.347  1.00 92.86           N  
ANISOU 2075  N   LYS A 251    12687  11162  11435    358   -210   -120       N  
ATOM   2076  CA  LYS A 251       9.793  -0.549 -15.331  1.00100.44           C  
ANISOU 2076  CA  LYS A 251    13686  12065  12412    434   -230   -112       C  
ATOM   2077  C   LYS A 251       8.486  -1.117 -15.907  1.00104.46           C  
ANISOU 2077  C   LYS A 251    14108  12638  12945    527   -215   -122       C  
ATOM   2078  O   LYS A 251       8.298  -2.335 -15.966  1.00104.30           O  
ANISOU 2078  O   LYS A 251    13992  12707  12930    510   -194   -115       O  
ATOM   2079  CB  LYS A 251      10.771  -0.225 -16.474  1.00100.97           C  
ANISOU 2079  CB  LYS A 251    13788  12093  12482    375   -265    -48       C  
ATOM   2080  CG  LYS A 251      10.422   1.020 -17.290  1.00102.51           C  
ANISOU 2080  CG  LYS A 251    14076  12194  12680    429   -297    -35       C  
ATOM   2081  CD  LYS A 251      11.057   0.974 -18.672  1.00102.43           C  
ANISOU 2081  CD  LYS A 251    14068  12178  12671    383   -320     31       C  
ATOM   2082  CE  LYS A 251      10.571   2.129 -19.538  1.00104.04           C  
ANISOU 2082  CE  LYS A 251    14368  12289  12874    444   -358     48       C  
ATOM   2083  NZ  LYS A 251      11.171   2.110 -20.905  1.00103.10           N  
ANISOU 2083  NZ  LYS A 251    14264  12163  12747    393   -377    115       N  
ATOM   2084  N   VAL A 252       7.604  -0.213 -16.340  1.00110.45           N  
ANISOU 2084  N   VAL A 252    14905  13345  13717    623   -231   -137       N  
ATOM   2085  CA  VAL A 252       6.302  -0.559 -16.929  1.00115.57           C  
ANISOU 2085  CA  VAL A 252    15472  14049  14392    719   -228   -148       C  
ATOM   2086  C   VAL A 252       6.254  -0.454 -18.456  1.00118.89           C  
ANISOU 2086  C   VAL A 252    15893  14454  14825    737   -273    -93       C  
ATOM   2087  O   VAL A 252       7.041   0.274 -19.071  1.00119.52           O  
ANISOU 2087  O   VAL A 252    16063  14455  14894    701   -306    -53       O  
ATOM   2088  CB  VAL A 252       5.149   0.321 -16.365  1.00116.66           C  
ANISOU 2088  CB  VAL A 252    15633  14154  14541    837   -216   -208       C  
ATOM   2089  CG1 VAL A 252       4.550  -0.305 -15.121  1.00117.40           C  
ANISOU 2089  CG1 VAL A 252    15658  14323  14626    847   -156   -267       C  
ATOM   2090  CG2 VAL A 252       5.614   1.761 -16.112  1.00118.02           C  
ANISOU 2090  CG2 VAL A 252    15951  14194  14697    850   -241   -219       C  
ATOM   2091  N   ILE A 253       5.310  -1.186 -19.048  1.00122.51           N  
ANISOU 2091  N   ILE A 253    16254  14990  15303    788   -274    -90       N  
ATOM   2092  CA  ILE A 253       4.996  -1.088 -20.473  1.00125.87           C  
ANISOU 2092  CA  ILE A 253    16679  15408  15738    822   -321    -45       C  
ATOM   2093  C   ILE A 253       3.871  -0.066 -20.659  1.00129.04           C  
ANISOU 2093  C   ILE A 253    17106  15763  16161    951   -352    -70       C  
ATOM   2094  O   ILE A 253       2.846  -0.127 -19.970  1.00129.63           O  
ANISOU 2094  O   ILE A 253    17114  15882  16255   1027   -327   -123       O  
ATOM   2095  CB  ILE A 253       4.546  -2.465 -21.072  1.00125.32           C  
ANISOU 2095  CB  ILE A 253    16494  15448  15676    804   -314    -29       C  
ATOM   2096  CG1 ILE A 253       5.406  -3.634 -20.547  1.00124.19           C  
ANISOU 2096  CG1 ILE A 253    16308  15362  15516    700   -274    -24       C  
ATOM   2097  CG2 ILE A 253       4.498  -2.417 -22.611  1.00125.55           C  
ANISOU 2097  CG2 ILE A 253    16540  15463  15700    814   -366     25       C  
ATOM   2098  CD1 ILE A 253       6.842  -3.694 -21.078  1.00123.53           C  
ANISOU 2098  CD1 ILE A 253    16281  15243  15413    608   -281     26       C  
ATOM   2099  N   GLU A 254       4.072   0.877 -21.581  1.00131.93           N  
ANISOU 2099  N   GLU A 254    17568  16039  16521    976   -405    -31       N  
ATOM   2100  CA  GLU A 254       3.048   1.872 -21.914  1.00134.93           C  
ANISOU 2100  CA  GLU A 254    17982  16363  16921   1107   -449    -46       C  
ATOM   2101  C   GLU A 254       1.930   1.252 -22.755  1.00136.00           C  
ANISOU 2101  C   GLU A 254    18010  16584  17082   1175   -479    -36       C  
ATOM   2102  O   GLU A 254       2.191   0.632 -23.791  1.00135.72           O  
ANISOU 2102  O   GLU A 254    17956  16581  17032   1122   -505     15       O  
ATOM   2103  CB  GLU A 254       3.660   3.075 -22.645  1.00135.84           C  
ANISOU 2103  CB  GLU A 254    18252  16346  17016   1103   -503     -1       C  
ATOM   2104  CG  GLU A 254       4.381   4.077 -21.738  1.00136.38           C  
ANISOU 2104  CG  GLU A 254    18444  16307  17066   1076   -488    -25       C  
ATOM   2105  CD  GLU A 254       4.618   5.431 -22.403  1.00136.89           C  
ANISOU 2105  CD  GLU A 254    18670  16229  17115   1104   -549      9       C  
ATOM   2106  OE1 GLU A 254       4.373   5.567 -23.623  1.00136.77           O  
ANISOU 2106  OE1 GLU A 254    18676  16196  17096   1131   -602     59       O  
ATOM   2107  OE2 GLU A 254       5.052   6.367 -21.697  1.00136.71           O  
ANISOU 2107  OE2 GLU A 254    18761  16105  17077   1095   -545    -14       O  
ATOM   2108  N   ASN A 255       0.690   1.421 -22.295  1.00137.52           N  
ANISOU 2108  N   ASN A 255    18129  16815  17308   1290   -475    -87       N  
ATOM   2109  CA  ASN A 255      -0.488   0.891 -22.990  1.00138.44           C  
ANISOU 2109  CA  ASN A 255    18129  17021  17453   1360   -508    -84       C  
ATOM   2110  C   ASN A 255      -1.689   1.848 -22.952  1.00139.62           C  
ANISOU 2110  C   ASN A 255    18266  17143  17640   1523   -543   -119       C  
ATOM   2111  O   ASN A 255      -1.523   3.060 -23.117  1.00140.33           O  
ANISOU 2111  O   ASN A 255    18480  17112  17727   1585   -582   -112       O  
ATOM   2112  CB  ASN A 255      -0.855  -0.518 -22.479  1.00138.29           C  
ANISOU 2112  CB  ASN A 255    17962  17141  17441   1304   -452   -110       C  
ATOM   2113  CG  ASN A 255      -1.082  -0.566 -20.971  1.00139.16           C  
ANISOU 2113  CG  ASN A 255    18033  17284  17559   1315   -375   -179       C  
ATOM   2114  OD1 ASN A 255      -2.223  -0.597 -20.508  1.00140.12           O  
ANISOU 2114  OD1 ASN A 255    18056  17471  17710   1399   -354   -228       O  
ATOM   2115  ND2 ASN A 255       0.005  -0.582 -20.203  1.00138.63           N  
ANISOU 2115  ND2 ASN A 255    18038  17174  17462   1226   -333   -184       N  
ATOM   2116  N   MET A 256      -2.888   1.301 -22.744  1.00139.89           N  
ANISOU 2116  N   MET A 256    18151  17291  17712   1590   -530   -157       N  
ATOM   2117  CA  MET A 256      -4.123   2.089 -22.740  1.00141.00           C  
ANISOU 2117  CA  MET A 256    18248  17429  17896   1755   -563   -193       C  
ATOM   2118  C   MET A 256      -5.178   1.520 -21.772  1.00140.56           C  
ANISOU 2118  C   MET A 256    18029  17503  17876   1803   -495   -264       C  
ATOM   2119  O   MET A 256      -6.347   1.920 -21.808  1.00141.90           O  
ANISOU 2119  O   MET A 256    18115  17711  18091   1938   -516   -297       O  
ATOM   2120  CB  MET A 256      -4.682   2.186 -24.169  1.00141.94           C  
ANISOU 2120  CB  MET A 256    18352  17551  18028   1811   -664   -139       C  
ATOM   2121  CG  MET A 256      -5.560   3.409 -24.443  1.00143.69           C  
ANISOU 2121  CG  MET A 256    18604  17705  18285   1988   -730   -153       C  
ATOM   2122  SD  MET A 256      -6.010   3.594 -26.185  1.00144.59           S  
ANISOU 2122  SD  MET A 256    18738  17800  18400   2039   -865    -76       S  
ATOM   2123  CE  MET A 256      -7.055   2.159 -26.451  1.00144.10           C  
ANISOU 2123  CE  MET A 256    18447  17937  18366   2015   -865    -85       C  
ATOM   2124  N   TYR A 257      -4.759   0.598 -20.904  1.00138.25           N  
ANISOU 2124  N   TYR A 257    17690  17277  17561   1692   -414   -287       N  
ATOM   2125  CA  TYR A 257      -5.674  -0.044 -19.954  1.00137.13           C  
ANISOU 2125  CA  TYR A 257    17399  17262  17440   1710   -339   -350       C  
ATOM   2126  C   TYR A 257      -5.182   0.073 -18.510  1.00135.25           C  
ANISOU 2126  C   TYR A 257    17211  17002  17176   1671   -247   -404       C  
ATOM   2127  O   TYR A 257      -5.816   0.733 -17.684  1.00136.14           O  
ANISOU 2127  O   TYR A 257    17309  17111  17306   1771   -203   -470       O  
ATOM   2128  CB  TYR A 257      -5.909  -1.517 -20.326  1.00137.07           C  
ANISOU 2128  CB  TYR A 257    17266  17385  17429   1607   -333   -325       C  
ATOM   2129  CG  TYR A 257      -6.141  -1.764 -21.804  1.00138.10           C  
ANISOU 2129  CG  TYR A 257    17375  17528  17569   1610   -428   -263       C  
ATOM   2130  CD1 TYR A 257      -5.172  -2.399 -22.584  1.00137.71           C  
ANISOU 2130  CD1 TYR A 257    17391  17453  17481   1491   -457   -201       C  
ATOM   2131  CD2 TYR A 257      -7.324  -1.357 -22.425  1.00139.67           C  
ANISOU 2131  CD2 TYR A 257    17489  17768  17813   1734   -489   -268       C  
ATOM   2132  CE1 TYR A 257      -5.377  -2.628 -23.945  1.00137.96           C  
ANISOU 2132  CE1 TYR A 257    17414  17495  17511   1490   -541   -146       C  
ATOM   2133  CE2 TYR A 257      -7.539  -1.579 -23.784  1.00139.92           C  
ANISOU 2133  CE2 TYR A 257    17508  17809  17845   1733   -583   -210       C  
ATOM   2134  CZ  TYR A 257      -6.563  -2.214 -24.537  1.00138.94           C  
ANISOU 2134  CZ  TYR A 257    17461  17655  17675   1608   -607   -150       C  
ATOM   2135  OH  TYR A 257      -6.773  -2.435 -25.879  1.00138.76           O  
ANISOU 2135  OH  TYR A 257    17437  17641  17643   1603   -697    -95       O  
ATOM   2136  N   GLY A 258      -4.053  -0.570 -18.217  1.00132.04           N  
ANISOU 2136  N   GLY A 258    16862  16580  16725   1529   -220   -378       N  
ATOM   2137  CA  GLY A 258      -3.453  -0.539 -16.884  1.00128.87           C  
ANISOU 2137  CA  GLY A 258    16518  16155  16290   1473   -144   -421       C  
ATOM   2138  C   GLY A 258      -1.940  -0.454 -16.946  1.00125.66           C  
ANISOU 2138  C   GLY A 258    16248  15653  15842   1363   -161   -376       C  
ATOM   2139  O   GLY A 258      -1.388   0.306 -17.747  1.00125.86           O  
ANISOU 2139  O   GLY A 258    16375  15578  15867   1377   -224   -334       O  
ATOM   2140  N   SER A 259      -1.272  -1.236 -16.097  1.00122.20           N  
ANISOU 2140  N   SER A 259    15811  15250  15371   1250   -108   -383       N  
ATOM   2141  CA  SER A 259       0.194  -1.285 -16.051  1.00118.06           C  
ANISOU 2141  CA  SER A 259    15393  14654  14810   1138   -122   -343       C  
ATOM   2142  C   SER A 259       0.718  -2.522 -15.319  1.00114.22           C  
ANISOU 2142  C   SER A 259    14865  14241  14294   1019    -74   -341       C  
ATOM   2143  O   SER A 259       0.105  -2.995 -14.357  1.00114.07           O  
ANISOU 2143  O   SER A 259    14782  14293  14265   1019    -14   -389       O  
ATOM   2144  CB  SER A 259       0.766  -0.013 -15.405  1.00118.96           C  
ANISOU 2144  CB  SER A 259    15649  14647  14905   1162   -121   -369       C  
ATOM   2145  OG  SER A 259       0.231   0.200 -14.108  1.00119.22           O  
ANISOU 2145  OG  SER A 259    15674  14699  14926   1202    -56   -442       O  
ATOM   2146  N   ARG A 260       1.848  -3.044 -15.794  1.00109.70           N  
ANISOU 2146  N   ARG A 260    14327  13648  13703    919   -101   -286       N  
ATOM   2147  CA  ARG A 260       2.580  -4.103 -15.089  1.00105.26           C  
ANISOU 2147  CA  ARG A 260    13752  13131  13111    808    -68   -279       C  
ATOM   2148  C   ARG A 260       4.094  -3.844 -15.088  1.00100.59           C  
ANISOU 2148  C   ARG A 260    13260  12463  12498    726    -94   -241       C  
ATOM   2149  O   ARG A 260       4.695  -3.586 -16.136  1.00100.13           O  
ANISOU 2149  O   ARG A 260    13237  12361  12448    711   -139   -192       O  
ATOM   2150  CB  ARG A 260       2.236  -5.508 -15.627  1.00105.49           C  
ANISOU 2150  CB  ARG A 260    13676  13258  13146    764    -65   -252       C  
ATOM   2151  CG  ARG A 260       2.504  -5.750 -17.114  1.00106.35           C  
ANISOU 2151  CG  ARG A 260    13778  13360  13271    755   -120   -193       C  
ATOM   2152  CD  ARG A 260       2.315  -7.220 -17.472  1.00106.69           C  
ANISOU 2152  CD  ARG A 260    13738  13491  13309    696   -113   -173       C  
ATOM   2153  NE  ARG A 260       2.512  -7.473 -18.901  1.00108.69           N  
ANISOU 2153  NE  ARG A 260    13989  13738  13570    689   -162   -122       N  
ATOM   2154  CZ  ARG A 260       3.595  -8.037 -19.435  1.00108.73           C  
ANISOU 2154  CZ  ARG A 260    14029  13726  13558    617   -175    -78       C  
ATOM   2155  NH1 ARG A 260       4.604  -8.428 -18.666  1.00108.34           N  
ANISOU 2155  NH1 ARG A 260    14012  13664  13490    548   -150    -76       N  
ATOM   2156  NH2 ARG A 260       3.669  -8.218 -20.747  1.00107.83           N  
ANISOU 2156  NH2 ARG A 260    13918  13609  13446    617   -214    -38       N  
ATOM   2157  N   GLU A 261       4.692  -3.890 -13.898  1.00 95.39           N  
ANISOU 2157  N   GLU A 261    12645  11792  11808    670    -65   -265       N  
ATOM   2158  CA  GLU A 261       6.124  -3.639 -13.731  1.00 89.16           C  
ANISOU 2158  CA  GLU A 261    11938  10940  10998    587    -90   -234       C  
ATOM   2159  C   GLU A 261       6.954  -4.903 -13.939  1.00 82.91           C  
ANISOU 2159  C   GLU A 261    11101  10203  10200    495    -95   -190       C  
ATOM   2160  O   GLU A 261       6.818  -5.889 -13.204  1.00 81.71           O  
ANISOU 2160  O   GLU A 261    10902  10113  10030    459    -65   -204       O  
ATOM   2161  CB  GLU A 261       6.416  -2.989 -12.372  1.00 90.62           C  
ANISOU 2161  CB  GLU A 261    12204  11079  11150    570    -68   -280       C  
ATOM   2162  CG  GLU A 261       6.328  -1.458 -12.398  1.00 92.07           C  
ANISOU 2162  CG  GLU A 261    12490  11158  11335    631    -87   -303       C  
ATOM   2163  CD  GLU A 261       5.939  -0.844 -11.061  1.00 92.62           C  
ANISOU 2163  CD  GLU A 261    12620  11199  11374    661    -48   -373       C  
ATOM   2164  OE1 GLU A 261       6.115  -1.505 -10.015  1.00 93.28           O  
ANISOU 2164  OE1 GLU A 261    12690  11328  11424    604    -15   -395       O  
ATOM   2165  OE2 GLU A 261       5.456   0.309 -11.059  1.00 91.53           O  
ANISOU 2165  OE2 GLU A 261    12549  10986  11241    744    -52   -407       O  
ATOM   2166  N   ILE A 262       7.793  -4.864 -14.970  1.00 75.05           N  
ANISOU 2166  N   ILE A 262    10121   9179   9216    462   -132   -137       N  
ATOM   2167  CA  ILE A 262       8.686  -5.972 -15.293  1.00 67.61           C  
ANISOU 2167  CA  ILE A 262     9139   8279   8270    387   -138    -95       C  
ATOM   2168  C   ILE A 262      10.123  -5.604 -14.931  1.00 60.76           C  
ANISOU 2168  C   ILE A 262     8332   7365   7390    311   -158    -73       C  
ATOM   2169  O   ILE A 262      10.446  -4.428 -14.733  1.00 59.00           O  
ANISOU 2169  O   ILE A 262     8187   7069   7162    311   -174    -81       O  
ATOM   2170  CB  ILE A 262       8.578  -6.411 -16.787  1.00 68.61           C  
ANISOU 2170  CB  ILE A 262     9224   8428   8416    400   -157    -52       C  
ATOM   2171  CG1 ILE A 262       8.928  -5.257 -17.737  1.00 71.87           C  
ANISOU 2171  CG1 ILE A 262     9703   8767   8838    418   -190    -24       C  
ATOM   2172  CG2 ILE A 262       7.184  -6.956 -17.088  1.00 67.94           C  
ANISOU 2172  CG2 ILE A 262     9068   8404   8344    460   -144    -72       C  
ATOM   2173  CD1 ILE A 262       9.440  -5.710 -19.108  1.00 73.54           C  
ANISOU 2173  CD1 ILE A 262     9898   8991   9053    392   -208     29       C  
ATOM   2174  N   ILE A 263      10.980  -6.613 -14.836  1.00 53.00           N  
ANISOU 2174  N   ILE A 263     7312   6423   6403    247   -160    -46       N  
ATOM   2175  CA  ILE A 263      12.352  -6.384 -14.416  1.00 48.77           C  
ANISOU 2175  CA  ILE A 263     6813   5859   5858    173   -181    -25       C  
ATOM   2176  C   ILE A 263      13.287  -6.438 -15.617  1.00 47.11           C  
ANISOU 2176  C   ILE A 263     6587   5645   5666    140   -199     27       C  
ATOM   2177  O   ILE A 263      13.367  -7.451 -16.324  1.00 44.23           O  
ANISOU 2177  O   ILE A 263     6163   5332   5312    140   -191     51       O  
ATOM   2178  CB  ILE A 263      12.802  -7.368 -13.294  1.00 45.77           C  
ANISOU 2178  CB  ILE A 263     6408   5523   5459    124   -177    -33       C  
ATOM   2179  CG1 ILE A 263      11.786  -7.400 -12.145  1.00 46.72           C  
ANISOU 2179  CG1 ILE A 263     6544   5656   5553    152   -149    -86       C  
ATOM   2180  CG2 ILE A 263      14.190  -7.010 -12.768  1.00 45.26           C  
ANISOU 2180  CG2 ILE A 263     6378   5431   5386     50   -209    -15       C  
ATOM   2181  CD1 ILE A 263      11.483  -6.042 -11.525  1.00 45.04           C  
ANISOU 2181  CD1 ILE A 263     6411   5378   5325    175   -147   -125       C  
ATOM   2182  N   THR A 264      13.979  -5.327 -15.852  1.00 44.11           N  
ANISOU 2182  N   THR A 264     6269   5205   5287    108   -220     43       N  
ATOM   2183  CA  THR A 264      14.997  -5.289 -16.886  1.00 42.20           C  
ANISOU 2183  CA  THR A 264     6016   4962   5055     62   -231     92       C  
ATOM   2184  C   THR A 264      16.317  -5.749 -16.292  1.00 40.29           C  
ANISOU 2184  C   THR A 264     5744   4749   4815    -16   -241    109       C  
ATOM   2185  O   THR A 264      16.839  -5.136 -15.360  1.00 40.36           O  
ANISOU 2185  O   THR A 264     5796   4726   4811    -62   -262     96       O  
ATOM   2186  CB  THR A 264      15.160  -3.889 -17.498  1.00 42.28           C  
ANISOU 2186  CB  THR A 264     6109   4893   5062     53   -249    107       C  
ATOM   2187  OG1 THR A 264      13.893  -3.433 -17.986  1.00 40.76           O  
ANISOU 2187  OG1 THR A 264     5945   4670   4870    137   -248     90       O  
ATOM   2188  CG2 THR A 264      16.167  -3.938 -18.651  1.00 41.27           C  
ANISOU 2188  CG2 THR A 264     5964   4776   4941     -2   -249    160       C  
ATOM   2189  N   LEU A 265      16.834  -6.844 -16.833  1.00 36.89           N  
ANISOU 2189  N   LEU A 265     5240   4378   4397    -27   -230    136       N  
ATOM   2190  CA  LEU A 265      18.115  -7.371 -16.429  1.00 34.00           C  
ANISOU 2190  CA  LEU A 265     4830   4049   4040    -88   -242    156       C  
ATOM   2191  C   LEU A 265      19.140  -6.941 -17.452  1.00 34.52           C  
ANISOU 2191  C   LEU A 265     4883   4113   4118   -135   -240    197       C  
ATOM   2192  O   LEU A 265      19.197  -7.508 -18.547  1.00 33.96           O  
ANISOU 2192  O   LEU A 265     4773   4074   4057   -116   -215    219       O  
ATOM   2193  CB  LEU A 265      18.066  -8.894 -16.355  1.00 32.81           C  
ANISOU 2193  CB  LEU A 265     4608   3962   3895    -62   -230    157       C  
ATOM   2194  CG  LEU A 265      17.018  -9.529 -15.446  1.00 31.60           C  
ANISOU 2194  CG  LEU A 265     4461   3821   3725    -23   -224    122       C  
ATOM   2195  CD1 LEU A 265      17.134 -11.043 -15.499  1.00 28.74           C  
ANISOU 2195  CD1 LEU A 265     4041   3513   3367    -10   -216    132       C  
ATOM   2196  CD2 LEU A 265      17.169  -9.026 -14.014  1.00 28.59           C  
ANISOU 2196  CD2 LEU A 265     4125   3416   3323    -56   -247     97       C  
ATOM   2197  N   PHE A 266      19.938  -5.939 -17.095  1.00 33.01           N  
ANISOU 2197  N   PHE A 266     4731   3887   3925   -203   -264    205       N  
ATOM   2198  CA  PHE A 266      21.030  -5.471 -17.943  1.00 36.20           C  
ANISOU 2198  CA  PHE A 266     5121   4296   4339   -268   -259    246       C  
ATOM   2199  C   PHE A 266      22.029  -6.591 -18.205  1.00 35.18           C  
ANISOU 2199  C   PHE A 266     4885   4248   4233   -285   -245    269       C  
ATOM   2200  O   PHE A 266      22.458  -7.276 -17.279  1.00 33.75           O  
ANISOU 2200  O   PHE A 266     4658   4104   4061   -292   -266    260       O  
ATOM   2201  CB  PHE A 266      21.734  -4.272 -17.304  1.00 36.85           C  
ANISOU 2201  CB  PHE A 266     5261   4327   4411   -352   -294    248       C  
ATOM   2202  CG  PHE A 266      20.979  -2.977 -17.450  1.00 40.99           C  
ANISOU 2202  CG  PHE A 266     5901   4758   4913   -342   -303    235       C  
ATOM   2203  CD1 PHE A 266      19.797  -2.758 -16.750  1.00 38.45           C  
ANISOU 2203  CD1 PHE A 266     5638   4393   4577   -273   -309    192       C  
ATOM   2204  CD2 PHE A 266      21.455  -1.973 -18.289  1.00 46.25           C  
ANISOU 2204  CD2 PHE A 266     6621   5378   5572   -399   -304    267       C  
ATOM   2205  CE1 PHE A 266      19.091  -1.564 -16.884  1.00 43.23           C  
ANISOU 2205  CE1 PHE A 266     6351   4909   5165   -249   -319    177       C  
ATOM   2206  CE2 PHE A 266      20.756  -0.766 -18.432  1.00 49.15           C  
ANISOU 2206  CE2 PHE A 266     7109   5648   5917   -382   -318    257       C  
ATOM   2207  CZ  PHE A 266      19.568  -0.566 -17.726  1.00 46.70           C  
ANISOU 2207  CZ  PHE A 266     6854   5293   5598   -300   -327    211       C  
ATOM   2208  N   GLY A 267      22.365  -6.786 -19.476  1.00 34.81           N  
ANISOU 2208  N   GLY A 267     4807   4228   4193   -286   -210    297       N  
ATOM   2209  CA  GLY A 267      23.337  -7.796 -19.872  1.00 34.17           C  
ANISOU 2209  CA  GLY A 267     4626   4222   4134   -293   -187    317       C  
ATOM   2210  C   GLY A 267      22.716  -9.135 -20.209  1.00 34.96           C  
ANISOU 2210  C   GLY A 267     4690   4359   4237   -212   -163    305       C  
ATOM   2211  O   GLY A 267      23.436 -10.093 -20.499  1.00 38.25           O  
ANISOU 2211  O   GLY A 267     5030   4832   4671   -200   -144    315       O  
ATOM   2212  N   ILE A 268      21.385  -9.206 -20.160  1.00 31.55           N  
ANISOU 2212  N   ILE A 268     4310   3892   3786   -155   -166    282       N  
ATOM   2213  CA  ILE A 268      20.647 -10.384 -20.613  1.00 29.41           C  
ANISOU 2213  CA  ILE A 268     4017   3647   3511    -87   -144    271       C  
ATOM   2214  C   ILE A 268      19.589  -9.976 -21.642  1.00 31.64           C  
ANISOU 2214  C   ILE A 268     4353   3898   3773    -53   -129    271       C  
ATOM   2215  O   ILE A 268      19.023  -8.875 -21.572  1.00 32.71           O  
ANISOU 2215  O   ILE A 268     4551   3980   3897    -57   -146    267       O  
ATOM   2216  CB  ILE A 268      20.060 -11.174 -19.417  1.00 30.23           C  
ANISOU 2216  CB  ILE A 268     4114   3758   3613    -55   -166    242       C  
ATOM   2217  CG1 ILE A 268      21.215 -11.802 -18.616  1.00 29.15           C  
ANISOU 2217  CG1 ILE A 268     3920   3660   3496    -81   -185    250       C  
ATOM   2218  CG2 ILE A 268      19.073 -12.263 -19.873  1.00 26.60           C  
ANISOU 2218  CG2 ILE A 268     3649   3315   3143      5   -148    229       C  
ATOM   2219  CD1 ILE A 268      20.890 -12.127 -17.224  1.00 25.20           C  
ANISOU 2219  CD1 ILE A 268     3434   3153   2986    -79   -219    228       C  
ATOM   2220  N   SER A 269      19.375 -10.838 -22.631  1.00 29.75           N  
ANISOU 2220  N   SER A 269     4093   3686   3526    -19   -101    278       N  
ATOM   2221  CA  SER A 269      18.315 -10.628 -23.608  1.00 31.14           C  
ANISOU 2221  CA  SER A 269     4315   3839   3679     17    -96    278       C  
ATOM   2222  C   SER A 269      17.188 -11.590 -23.305  1.00 30.10           C  
ANISOU 2222  C   SER A 269     4172   3721   3543     71   -103    251       C  
ATOM   2223  O   SER A 269      17.292 -12.797 -23.557  1.00 29.54           O  
ANISOU 2223  O   SER A 269     4067   3686   3470     88    -87    248       O  
ATOM   2224  CB  SER A 269      18.829 -10.818 -25.031  1.00 29.88           C  
ANISOU 2224  CB  SER A 269     4153   3697   3503      6    -61    305       C  
ATOM   2225  OG  SER A 269      19.755  -9.794 -25.342  1.00 33.70           O  
ANISOU 2225  OG  SER A 269     4653   4164   3986    -54    -52    332       O  
ATOM   2226  N   VAL A 270      16.122 -11.045 -22.734  1.00 30.18           N  
ANISOU 2226  N   VAL A 270     4212   3703   3550     95   -127    229       N  
ATOM   2227  CA  VAL A 270      14.940 -11.822 -22.393  1.00 28.98           C  
ANISOU 2227  CA  VAL A 270     4047   3570   3394    137   -132    202       C  
ATOM   2228  C   VAL A 270      14.044 -11.904 -23.610  1.00 29.69           C  
ANISOU 2228  C   VAL A 270     4152   3660   3467    170   -133    208       C  
ATOM   2229  O   VAL A 270      13.613 -10.879 -24.144  1.00 29.05           O  
ANISOU 2229  O   VAL A 270     4112   3545   3381    184   -148    217       O  
ATOM   2230  CB  VAL A 270      14.178 -11.207 -21.198  1.00 29.01           C  
ANISOU 2230  CB  VAL A 270     4067   3554   3402    151   -149    172       C  
ATOM   2231  CG1 VAL A 270      12.867 -11.943 -20.956  1.00 28.05           C  
ANISOU 2231  CG1 VAL A 270     3924   3459   3274    189   -148    145       C  
ATOM   2232  CG2 VAL A 270      15.047 -11.243 -19.949  1.00 23.58           C  
ANISOU 2232  CG2 VAL A 270     3371   2867   2722    113   -154    165       C  
ATOM   2233  N   LEU A 271      13.806 -13.128 -24.072  1.00 30.23           N  
ANISOU 2233  N   LEU A 271     4197   3764   3526    182   -122    206       N  
ATOM   2234  CA  LEU A 271      12.827 -13.368 -25.128  1.00 32.30           C  
ANISOU 2234  CA  LEU A 271     4472   4033   3769    209   -131    208       C  
ATOM   2235  C   LEU A 271      11.798 -14.343 -24.595  1.00 31.00           C  
ANISOU 2235  C   LEU A 271     4277   3898   3602    225   -138    180       C  
ATOM   2236  O   LEU A 271      11.927 -15.550 -24.814  1.00 32.05           O  
ANISOU 2236  O   LEU A 271     4398   4055   3724    217   -126    178       O  
ATOM   2237  CB  LEU A 271      13.467 -13.961 -26.400  1.00 29.90           C  
ANISOU 2237  CB  LEU A 271     4180   3739   3442    198   -110    230       C  
ATOM   2238  CG  LEU A 271      14.675 -13.376 -27.141  1.00 31.76           C  
ANISOU 2238  CG  LEU A 271     4436   3960   3670    168    -85    260       C  
ATOM   2239  CD1 LEU A 271      15.109 -14.346 -28.236  1.00 24.61           C  
ANISOU 2239  CD1 LEU A 271     3534   3078   2738    166    -55    268       C  
ATOM   2240  CD2 LEU A 271      14.364 -12.030 -27.755  1.00 32.48           C  
ANISOU 2240  CD2 LEU A 271     4580   4012   3750    167   -105    280       C  
ATOM   2241  N   ASP A 272      10.786 -13.826 -23.899  1.00 30.89           N  
ANISOU 2241  N   ASP A 272     4254   3884   3599    247   -154    158       N  
ATOM   2242  CA  ASP A 272       9.685 -14.661 -23.397  1.00 31.93           C  
ANISOU 2242  CA  ASP A 272     4351   4053   3727    255   -157    132       C  
ATOM   2243  C   ASP A 272       9.067 -15.425 -24.577  1.00 31.20           C  
ANISOU 2243  C   ASP A 272     4257   3983   3615    259   -168    139       C  
ATOM   2244  O   ASP A 272       8.772 -14.822 -25.610  1.00 28.07           O  
ANISOU 2244  O   ASP A 272     3880   3573   3210    280   -188    154       O  
ATOM   2245  CB  ASP A 272       8.623 -13.784 -22.713  1.00 32.02           C  
ANISOU 2245  CB  ASP A 272     4348   4066   3753    288   -168    106       C  
ATOM   2246  CG  ASP A 272       7.663 -14.585 -21.827  1.00 35.51           C  
ANISOU 2246  CG  ASP A 272     4747   4553   4193    281   -157     75       C  
ATOM   2247  OD1 ASP A 272       7.445 -15.794 -22.073  1.00 35.28           O  
ANISOU 2247  OD1 ASP A 272     4702   4554   4148    255   -154     76       O  
ATOM   2248  OD2 ASP A 272       7.109 -13.990 -20.876  1.00 36.87           O  
ANISOU 2248  OD2 ASP A 272     4905   4729   4374    299   -149     48       O  
ATOM   2249  N   TYR A 273       8.875 -16.737 -24.435  1.00 30.81           N  
ANISOU 2249  N   TYR A 273     4193   3961   3552    236   -160    130       N  
ATOM   2250  CA  TYR A 273       8.390 -17.533 -25.570  1.00 30.51           C  
ANISOU 2250  CA  TYR A 273     4165   3939   3489    231   -173    136       C  
ATOM   2251  C   TYR A 273       6.951 -17.221 -25.956  1.00 33.50           C  
ANISOU 2251  C   TYR A 273     4518   4344   3867    250   -206    126       C  
ATOM   2252  O   TYR A 273       6.584 -17.331 -27.128  1.00 34.11           O  
ANISOU 2252  O   TYR A 273     4613   4424   3923    254   -231    138       O  
ATOM   2253  CB  TYR A 273       8.594 -19.046 -25.383  1.00 31.13           C  
ANISOU 2253  CB  TYR A 273     4250   4029   3550    199   -160    129       C  
ATOM   2254  CG  TYR A 273       8.913 -19.682 -26.712  1.00 30.72           C  
ANISOU 2254  CG  TYR A 273     4238   3967   3467    194   -161    142       C  
ATOM   2255  CD1 TYR A 273       7.894 -20.136 -27.560  1.00 28.58           C  
ANISOU 2255  CD1 TYR A 273     3975   3715   3171    185   -188    138       C  
ATOM   2256  CD2 TYR A 273      10.237 -19.767 -27.162  1.00 32.55           C  
ANISOU 2256  CD2 TYR A 273     4498   4176   3695    199   -134    158       C  
ATOM   2257  CE1 TYR A 273       8.193 -20.681 -28.814  1.00 29.70           C  
ANISOU 2257  CE1 TYR A 273     4165   3844   3276    179   -188    148       C  
ATOM   2258  CE2 TYR A 273      10.545 -20.313 -28.415  1.00 28.21           C  
ANISOU 2258  CE2 TYR A 273     3990   3617   3111    198   -125    166       C  
ATOM   2259  CZ  TYR A 273       9.519 -20.766 -29.234  1.00 30.80           C  
ANISOU 2259  CZ  TYR A 273     4339   3957   3408    188   -153    160       C  
ATOM   2260  OH  TYR A 273       9.819 -21.309 -30.468  1.00 31.39           O  
ANISOU 2260  OH  TYR A 273     4467   4020   3441    185   -145    165       O  
ATOM   2261  N   ILE A 274       6.134 -16.837 -24.976  1.00 33.88           N  
ANISOU 2261  N   ILE A 274     4522   4415   3936    262   -207    103       N  
ATOM   2262  CA  ILE A 274       4.768 -16.417 -25.259  1.00 34.26           C  
ANISOU 2262  CA  ILE A 274     4528   4496   3992    291   -238     91       C  
ATOM   2263  C   ILE A 274       4.775 -15.206 -26.216  1.00 34.08           C  
ANISOU 2263  C   ILE A 274     4535   4440   3974    338   -270    112       C  
ATOM   2264  O   ILE A 274       3.987 -15.145 -27.165  1.00 36.96           O  
ANISOU 2264  O   ILE A 274     4892   4822   4330    356   -310    120       O  
ATOM   2265  CB  ILE A 274       3.979 -16.135 -23.948  1.00 35.96           C  
ANISOU 2265  CB  ILE A 274     4688   4743   4231    303   -221     57       C  
ATOM   2266  CG1 ILE A 274       2.471 -16.195 -24.208  1.00 41.31           C  
ANISOU 2266  CG1 ILE A 274     5300   5480   4917    320   -247     41       C  
ATOM   2267  CG2 ILE A 274       4.397 -14.798 -23.320  1.00 35.37           C  
ANISOU 2267  CG2 ILE A 274     4632   4629   4179    345   -211     52       C  
ATOM   2268  CD1 ILE A 274       1.627 -16.303 -22.942  1.00 46.69           C  
ANISOU 2268  CD1 ILE A 274     5917   6212   5612    314   -216      4       C  
ATOM   2269  N   ASP A 275       5.689 -14.269 -25.978  1.00 33.33           N  
ANISOU 2269  N   ASP A 275     4478   4296   3889    353   -256    123       N  
ATOM   2270  CA  ASP A 275       5.849 -13.089 -26.822  1.00 32.35           C  
ANISOU 2270  CA  ASP A 275     4400   4128   3764    388   -284    147       C  
ATOM   2271  C   ASP A 275       6.480 -13.464 -28.163  1.00 31.99           C  
ANISOU 2271  C   ASP A 275     4406   4068   3683    362   -291    180       C  
ATOM   2272  O   ASP A 275       6.107 -12.919 -29.198  1.00 27.87           O  
ANISOU 2272  O   ASP A 275     3915   3530   3145    385   -328    201       O  
ATOM   2273  CB  ASP A 275       6.699 -12.029 -26.121  1.00 31.76           C  
ANISOU 2273  CB  ASP A 275     4359   4002   3705    394   -265    149       C  
ATOM   2274  CG  ASP A 275       5.991 -11.387 -24.936  1.00 37.51           C  
ANISOU 2274  CG  ASP A 275     5055   4734   4462    432   -262    115       C  
ATOM   2275  OD1 ASP A 275       4.743 -11.350 -24.924  1.00 39.80           O  
ANISOU 2275  OD1 ASP A 275     5299   5060   4764    473   -282     95       O  
ATOM   2276  OD2 ASP A 275       6.691 -10.912 -24.006  1.00 41.82           O  
ANISOU 2276  OD2 ASP A 275     5622   5250   5017    420   -239    106       O  
ATOM   2277  N   LEU A 276       7.449 -14.381 -28.147  1.00 30.38           N  
ANISOU 2277  N   LEU A 276     4213   3867   3464    318   -254    185       N  
ATOM   2278  CA  LEU A 276       7.972 -14.910 -29.403  1.00 30.55           C  
ANISOU 2278  CA  LEU A 276     4279   3881   3446    296   -251    207       C  
ATOM   2279  C   LEU A 276       6.822 -15.543 -30.194  1.00 30.47           C  
ANISOU 2279  C   LEU A 276     4262   3903   3413    299   -290    203       C  
ATOM   2280  O   LEU A 276       6.617 -15.227 -31.365  1.00 31.06           O  
ANISOU 2280  O   LEU A 276     4378   3966   3457    306   -321    224       O  
ATOM   2281  CB  LEU A 276       9.105 -15.922 -29.168  1.00 29.13           C  
ANISOU 2281  CB  LEU A 276     4103   3706   3260    260   -203    205       C  
ATOM   2282  CG  LEU A 276      10.488 -15.444 -28.703  1.00 29.27           C  
ANISOU 2282  CG  LEU A 276     4128   3699   3293    247   -166    217       C  
ATOM   2283  CD1 LEU A 276      11.379 -16.651 -28.460  1.00 25.29           C  
ANISOU 2283  CD1 LEU A 276     3613   3208   2786    226   -130    210       C  
ATOM   2284  CD2 LEU A 276      11.176 -14.469 -29.682  1.00 27.01           C  
ANISOU 2284  CD2 LEU A 276     3891   3381   2989    242   -161    249       C  
ATOM   2285  N   TYR A 277       6.061 -16.415 -29.537  1.00 29.78           N  
ANISOU 2285  N   TYR A 277     4123   3856   3335    287   -293    176       N  
ATOM   2286  CA  TYR A 277       4.943 -17.102 -30.181  1.00 31.42           C  
ANISOU 2286  CA  TYR A 277     4314   4101   3522    276   -333    170       C  
ATOM   2287  C   TYR A 277       3.862 -16.147 -30.724  1.00 32.92           C  
ANISOU 2287  C   TYR A 277     4487   4303   3720    320   -392    178       C  
ATOM   2288  O   TYR A 277       3.362 -16.342 -31.834  1.00 34.46           O  
ANISOU 2288  O   TYR A 277     4704   4506   3882    315   -437    191       O  
ATOM   2289  CB  TYR A 277       4.349 -18.141 -29.226  1.00 31.12           C  
ANISOU 2289  CB  TYR A 277     4223   4105   3495    244   -321    141       C  
ATOM   2290  CG  TYR A 277       3.334 -19.077 -29.837  1.00 31.77           C  
ANISOU 2290  CG  TYR A 277     4292   4228   3552    211   -358    133       C  
ATOM   2291  CD1 TYR A 277       3.705 -20.341 -30.302  1.00 29.78           C  
ANISOU 2291  CD1 TYR A 277     4088   3966   3259    164   -347    132       C  
ATOM   2292  CD2 TYR A 277       1.992 -18.707 -29.924  1.00 32.77           C  
ANISOU 2292  CD2 TYR A 277     4357   4401   3694    228   -405    125       C  
ATOM   2293  CE1 TYR A 277       2.760 -21.203 -30.859  1.00 28.70           C  
ANISOU 2293  CE1 TYR A 277     3948   3862   3095    123   -386    124       C  
ATOM   2294  CE2 TYR A 277       1.047 -19.557 -30.462  1.00 30.50           C  
ANISOU 2294  CE2 TYR A 277     4049   4157   3383    188   -444    119       C  
ATOM   2295  CZ  TYR A 277       1.430 -20.796 -30.927  1.00 29.09           C  
ANISOU 2295  CZ  TYR A 277     3928   3964   3160    130   -436    119       C  
ATOM   2296  OH  TYR A 277       0.464 -21.611 -31.449  1.00 26.81           O  
ANISOU 2296  OH  TYR A 277     3626   3714   2845     82   -479    112       O  
ATOM   2297  N   LYS A 278       3.501 -15.122 -29.959  1.00 33.39           N  
ANISOU 2297  N   LYS A 278     4508   4358   3820    365   -397    169       N  
ATOM   2298  CA  LYS A 278       2.454 -14.174 -30.396  1.00 32.38           C  
ANISOU 2298  CA  LYS A 278     4359   4239   3707    423   -456    174       C  
ATOM   2299  C   LYS A 278       2.859 -13.336 -31.619  1.00 33.53           C  
ANISOU 2299  C   LYS A 278     4587   4331   3823    444   -492    213       C  
ATOM   2300  O   LYS A 278       2.020 -12.993 -32.446  1.00 34.58           O  
ANISOU 2300  O   LYS A 278     4721   4472   3945    476   -556    227       O  
ATOM   2301  CB  LYS A 278       2.031 -13.246 -29.255  1.00 29.96           C  
ANISOU 2301  CB  LYS A 278     4003   3933   3449    476   -446    150       C  
ATOM   2302  CG  LYS A 278       1.045 -13.869 -28.287  1.00 31.49           C  
ANISOU 2302  CG  LYS A 278     4100   4196   3667    470   -432    112       C  
ATOM   2303  CD  LYS A 278       0.947 -13.080 -26.996  1.00 31.17           C  
ANISOU 2303  CD  LYS A 278     4027   4149   3665    511   -397     83       C  
ATOM   2304  CE  LYS A 278      -0.103 -13.671 -26.058  1.00 31.62           C  
ANISOU 2304  CE  LYS A 278     3986   4285   3743    502   -377     44       C  
ATOM   2305  NZ  LYS A 278      -0.341 -12.783 -24.873  1.00 34.29           N  
ANISOU 2305  NZ  LYS A 278     4296   4620   4114    554   -343     11       N  
ATOM   2306  N   LYS A 279       4.135 -12.994 -31.727  1.00 33.74           N  
ANISOU 2306  N   LYS A 279     4681   4304   3834    425   -452    232       N  
ATOM   2307  CA  LYS A 279       4.583 -12.161 -32.831  1.00 35.95           C  
ANISOU 2307  CA  LYS A 279     5047   4533   4081    433   -477    272       C  
ATOM   2308  C   LYS A 279       4.854 -12.972 -34.086  1.00 35.33           C  
ANISOU 2308  C   LYS A 279     5021   4461   3943    390   -483    291       C  
ATOM   2309  O   LYS A 279       4.565 -12.521 -35.193  1.00 38.02           O  
ANISOU 2309  O   LYS A 279     5418   4781   4246    401   -532    320       O  
ATOM   2310  CB  LYS A 279       5.839 -11.376 -32.452  1.00 37.08           C  
ANISOU 2310  CB  LYS A 279     5239   4621   4231    421   -431    286       C  
ATOM   2311  CG  LYS A 279       6.061 -10.168 -33.354  1.00 38.37           C  
ANISOU 2311  CG  LYS A 279     5490   4723   4368    438   -465    326       C  
ATOM   2312  CD  LYS A 279       7.472  -9.608 -33.236  1.00 43.08           C  
ANISOU 2312  CD  LYS A 279     6142   5272   4956    397   -413    346       C  
ATOM   2313  CE  LYS A 279       7.770  -8.631 -34.385  1.00 45.99           C  
ANISOU 2313  CE  LYS A 279     6613   5581   5279    391   -441    392       C  
ATOM   2314  NZ  LYS A 279       6.881  -7.418 -34.355  1.00 48.68           N  
ANISOU 2314  NZ  LYS A 279     6983   5874   5637    458   -509    402       N  
ATOM   2315  N   PHE A 280       5.393 -14.173 -33.914  1.00 33.27           N  
ANISOU 2315  N   PHE A 280     4749   4224   3669    342   -435    275       N  
ATOM   2316  CA  PHE A 280       5.973 -14.897 -35.037  1.00 33.90           C  
ANISOU 2316  CA  PHE A 280     4894   4297   3688    302   -419    289       C  
ATOM   2317  C   PHE A 280       5.184 -16.115 -35.532  1.00 34.69           C  
ANISOU 2317  C   PHE A 280     4985   4438   3758    276   -449    273       C  
ATOM   2318  O   PHE A 280       5.448 -16.620 -36.631  1.00 38.05           O  
ANISOU 2318  O   PHE A 280     5479   4855   4124    248   -450    284       O  
ATOM   2319  CB  PHE A 280       7.412 -15.303 -34.702  1.00 31.78           C  
ANISOU 2319  CB  PHE A 280     4642   4014   3419    270   -339    286       C  
ATOM   2320  CG  PHE A 280       8.358 -14.139 -34.492  1.00 31.12           C  
ANISOU 2320  CG  PHE A 280     4583   3890   3350    275   -311    308       C  
ATOM   2321  CD1 PHE A 280       9.313 -14.184 -33.480  1.00 26.75           C  
ANISOU 2321  CD1 PHE A 280     3996   3334   2833    263   -257    297       C  
ATOM   2322  CD2 PHE A 280       8.311 -13.012 -35.319  1.00 32.55           C  
ANISOU 2322  CD2 PHE A 280     4829   4032   3506    286   -343    343       C  
ATOM   2323  CE1 PHE A 280      10.205 -13.134 -33.292  1.00 31.85           C  
ANISOU 2323  CE1 PHE A 280     4665   3945   3491    254   -234    318       C  
ATOM   2324  CE2 PHE A 280       9.200 -11.953 -35.139  1.00 30.30           C  
ANISOU 2324  CE2 PHE A 280     4576   3706   3230    277   -317    365       C  
ATOM   2325  CZ  PHE A 280      10.149 -12.015 -34.125  1.00 32.38           C  
ANISOU 2325  CZ  PHE A 280     4799   3972   3532    258   -261    351       C  
ATOM   2326  N   SER A 281       4.222 -16.586 -34.744  1.00 33.26           N  
ANISOU 2326  N   SER A 281     4725   4299   3611    280   -470    246       N  
ATOM   2327  CA  SER A 281       3.516 -17.824 -35.087  1.00 34.07           C  
ANISOU 2327  CA  SER A 281     4818   4441   3687    240   -495    229       C  
ATOM   2328  C   SER A 281       2.386 -17.637 -36.101  1.00 35.56           C  
ANISOU 2328  C   SER A 281     5013   4652   3847    246   -581    242       C  
ATOM   2329  O   SER A 281       1.989 -18.596 -36.767  1.00 35.92           O  
ANISOU 2329  O   SER A 281     5084   4716   3848    202   -607    235       O  
ATOM   2330  CB  SER A 281       2.972 -18.509 -33.835  1.00 31.85           C  
ANISOU 2330  CB  SER A 281     4452   4201   3448    225   -479    196       C  
ATOM   2331  OG  SER A 281       1.720 -17.959 -33.477  1.00 34.89           O  
ANISOU 2331  OG  SER A 281     4758   4629   3869    254   -529    189       O  
ATOM   2332  N   PHE A 282       1.867 -16.414 -36.197  1.00 35.40           N  
ANISOU 2332  N   PHE A 282     4974   4626   3850    301   -628    260       N  
ATOM   2333  CA  PHE A 282       0.723 -16.097 -37.060  1.00 37.87           C  
ANISOU 2333  CA  PHE A 282     5281   4964   4146    321   -723    275       C  
ATOM   2334  C   PHE A 282      -0.507 -16.953 -36.746  1.00 39.10           C  
ANISOU 2334  C   PHE A 282     5344   5193   4319    296   -763    248       C  
ATOM   2335  O   PHE A 282      -1.145 -17.532 -37.635  1.00 36.47           O  
ANISOU 2335  O   PHE A 282     5028   4886   3943    261   -824    253       O  
ATOM   2336  CB  PHE A 282       1.120 -16.127 -38.541  1.00 36.81           C  
ANISOU 2336  CB  PHE A 282     5261   4793   3931    296   -751    307       C  
ATOM   2337  CG  PHE A 282       1.923 -14.932 -38.958  1.00 42.03           C  
ANISOU 2337  CG  PHE A 282     6000   5391   4578    329   -739    342       C  
ATOM   2338  CD1 PHE A 282       1.295 -13.810 -39.494  1.00 46.88           C  
ANISOU 2338  CD1 PHE A 282     6635   5987   5191    381   -818    372       C  
ATOM   2339  CD2 PHE A 282       3.301 -14.903 -38.772  1.00 41.60           C  
ANISOU 2339  CD2 PHE A 282     5997   5296   4514    307   -651    345       C  
ATOM   2340  CE1 PHE A 282       2.030 -12.691 -39.857  1.00 46.09           C  
ANISOU 2340  CE1 PHE A 282     6618   5820   5073    403   -808    408       C  
ATOM   2341  CE2 PHE A 282       4.041 -13.793 -39.132  1.00 40.85           C  
ANISOU 2341  CE2 PHE A 282     5972   5146   4405    323   -638    379       C  
ATOM   2342  CZ  PHE A 282       3.407 -12.684 -39.676  1.00 45.95           C  
ANISOU 2342  CZ  PHE A 282     6651   5765   5043    368   -715    411       C  
ATOM   2343  N   THR A 283      -0.794 -17.038 -35.446  1.00 39.87           N  
ANISOU 2343  N   THR A 283     5348   5324   4476    305   -726    219       N  
ATOM   2344  CA  THR A 283      -2.024 -17.614 -34.918  1.00 40.14           C  
ANISOU 2344  CA  THR A 283     5274   5437   4540    286   -755    193       C  
ATOM   2345  C   THR A 283      -2.671 -16.593 -33.980  1.00 41.58           C  
ANISOU 2345  C   THR A 283     5358   5648   4792    361   -758    179       C  
ATOM   2346  O   THR A 283      -2.007 -15.657 -33.527  1.00 42.00           O  
ANISOU 2346  O   THR A 283     5438   5651   4869    412   -722    185       O  
ATOM   2347  CB  THR A 283      -1.744 -18.899 -34.111  1.00 40.45           C  
ANISOU 2347  CB  THR A 283     5298   5494   4576    213   -692    164       C  
ATOM   2348  OG1 THR A 283      -0.997 -18.574 -32.924  1.00 34.30           O  
ANISOU 2348  OG1 THR A 283     4506   4690   3835    236   -616    152       O  
ATOM   2349  CG2 THR A 283      -0.989 -19.942 -34.959  1.00 34.36           C  
ANISOU 2349  CG2 THR A 283     4635   4684   3737    150   -678    171       C  
ATOM   2350  N   ASN A 284      -3.971 -16.742 -33.731  1.00 42.78           N  
ANISOU 2350  N   ASN A 284     5399   5880   4975    366   -801    161       N  
ATOM   2351  CA  ASN A 284      -4.598 -16.154 -32.544  1.00 43.20           C  
ANISOU 2351  CA  ASN A 284     5342   5977   5096    420   -775    132       C  
ATOM   2352  C   ASN A 284      -5.341 -17.281 -31.871  1.00 42.58           C  
ANISOU 2352  C   ASN A 284     5171   5981   5025    347   -753    102       C  
ATOM   2353  O   ASN A 284      -6.163 -17.963 -32.490  1.00 43.51           O  
ANISOU 2353  O   ASN A 284     5251   6156   5125    298   -810    103       O  
ATOM   2354  CB  ASN A 284      -5.540 -14.974 -32.851  1.00 44.99           C  
ANISOU 2354  CB  ASN A 284     5508   6226   5362    520   -847    139       C  
ATOM   2355  CG  ASN A 284      -5.778 -14.040 -31.620  1.00 47.98           C  
ANISOU 2355  CG  ASN A 284     5814   6611   5803    602   -801    110       C  
ATOM   2356  OD1 ASN A 284      -5.088 -14.134 -30.598  1.00 46.63           O  
ANISOU 2356  OD1 ASN A 284     5659   6417   5642    583   -718     90       O  
ATOM   2357  ND2 ASN A 284      -6.756 -13.134 -31.738  1.00 42.57           N  
ANISOU 2357  ND2 ASN A 284     5056   5959   5162    696   -859    106       N  
ATOM   2358  N   GLN A 285      -5.034 -17.475 -30.600  1.00 40.50           N  
ANISOU 2358  N   GLN A 285     4879   5722   4785    332   -672     75       N  
ATOM   2359  CA  GLN A 285      -5.476 -18.649 -29.891  1.00 38.73           C  
ANISOU 2359  CA  GLN A 285     4599   5560   4557    245   -636     50       C  
ATOM   2360  C   GLN A 285      -6.563 -18.300 -28.896  1.00 39.32           C  
ANISOU 2360  C   GLN A 285     4535   5720   4684    273   -617     17       C  
ATOM   2361  O   GLN A 285      -6.568 -17.195 -28.347  1.00 42.82           O  
ANISOU 2361  O   GLN A 285     4950   6153   5169    363   -597      5       O  
ATOM   2362  CB  GLN A 285      -4.280 -19.301 -29.196  1.00 36.27           C  
ANISOU 2362  CB  GLN A 285     4371   5190   4222    194   -559     47       C  
ATOM   2363  CG  GLN A 285      -3.199 -19.769 -30.160  1.00 37.41           C  
ANISOU 2363  CG  GLN A 285     4643   5259   4314    165   -568     74       C  
ATOM   2364  CD  GLN A 285      -3.551 -21.046 -30.910  1.00 41.07           C  
ANISOU 2364  CD  GLN A 285     5133   5741   4729     77   -603     77       C  
ATOM   2365  OE1 GLN A 285      -4.711 -21.473 -30.948  1.00 44.33           O  
ANISOU 2365  OE1 GLN A 285     5466   6229   5146     37   -641     65       O  
ATOM   2366  NE2 GLN A 285      -2.540 -21.661 -31.529  1.00 40.46           N  
ANISOU 2366  NE2 GLN A 285     5170   5598   4603     47   -590     90       N  
ATOM   2367  N   PRO A 286      -7.507 -19.231 -28.677  1.00 38.96           N  
ANISOU 2367  N   PRO A 286     4404   5762   4636    195   -622      0       N  
ATOM   2368  CA  PRO A 286      -8.499 -19.090 -27.604  1.00 38.26           C  
ANISOU 2368  CA  PRO A 286     4178   5767   4592    203   -583    -36       C  
ATOM   2369  C   PRO A 286      -7.862 -19.019 -26.212  1.00 37.26           C  
ANISOU 2369  C   PRO A 286     4073   5613   4471    202   -484    -59       C  
ATOM   2370  O   PRO A 286      -8.458 -18.469 -25.289  1.00 36.63           O  
ANISOU 2370  O   PRO A 286     3901   5588   4430    245   -442    -91       O  
ATOM   2371  CB  PRO A 286      -9.326 -20.367 -27.721  1.00 37.21           C  
ANISOU 2371  CB  PRO A 286     3986   5715   4435     83   -601    -43       C  
ATOM   2372  CG  PRO A 286      -9.126 -20.822 -29.118  1.00 39.01           C  
ANISOU 2372  CG  PRO A 286     4296   5907   4621     48   -681    -10       C  
ATOM   2373  CD  PRO A 286      -7.747 -20.426 -29.504  1.00 36.11           C  
ANISOU 2373  CD  PRO A 286     4072   5419   4228     94   -668     13       C  
ATOM   2374  N   SER A 287      -6.661 -19.573 -26.074  1.00 38.56           N  
ANISOU 2374  N   SER A 287     4359   5695   4597    154   -450    -45       N  
ATOM   2375  CA  SER A 287      -5.962 -19.649 -24.788  1.00 38.75           C  
ANISOU 2375  CA  SER A 287     4417   5688   4618    140   -366    -61       C  
ATOM   2376  C   SER A 287      -4.457 -19.658 -24.995  1.00 39.54           C  
ANISOU 2376  C   SER A 287     4653   5680   4691    145   -354    -37       C  
ATOM   2377  O   SER A 287      -3.963 -20.186 -25.999  1.00 40.02           O  
ANISOU 2377  O   SER A 287     4787   5700   4720    116   -392    -11       O  
ATOM   2378  CB  SER A 287      -6.377 -20.916 -24.036  1.00 40.41           C  
ANISOU 2378  CB  SER A 287     4600   5952   4803     25   -326    -76       C  
ATOM   2379  OG  SER A 287      -5.535 -21.173 -22.920  1.00 42.82           O  
ANISOU 2379  OG  SER A 287     4968   6212   5090     -1   -257    -83       O  
ATOM   2380  N   TYR A 288      -3.735 -19.094 -24.030  1.00 38.86           N  
ANISOU 2380  N   TYR A 288     4596   5551   4616    180   -301    -47       N  
ATOM   2381  CA  TYR A 288      -2.273 -19.077 -24.064  1.00 38.45           C  
ANISOU 2381  CA  TYR A 288     4657   5407   4544    182   -284    -25       C  
ATOM   2382  C   TYR A 288      -1.592 -19.776 -22.892  1.00 37.55           C  
ANISOU 2382  C   TYR A 288     4583   5274   4411    126   -226    -34       C  
ATOM   2383  O   TYR A 288      -0.433 -19.502 -22.595  1.00 38.38           O  
ANISOU 2383  O   TYR A 288     4756   5313   4512    144   -206    -23       O  
ATOM   2384  CB  TYR A 288      -1.739 -17.652 -24.259  1.00 37.23           C  
ANISOU 2384  CB  TYR A 288     4531   5198   4415    276   -294    -18       C  
ATOM   2385  CG  TYR A 288      -1.925 -17.190 -25.681  1.00 38.89           C  
ANISOU 2385  CG  TYR A 288     4757   5395   4626    316   -360      8       C  
ATOM   2386  CD1 TYR A 288      -2.980 -16.359 -26.023  1.00 38.28           C  
ANISOU 2386  CD1 TYR A 288     4607   5357   4579    383   -402      0       C  
ATOM   2387  CD2 TYR A 288      -1.079 -17.628 -26.691  1.00 37.02           C  
ANISOU 2387  CD2 TYR A 288     4605   5106   4353    289   -382     39       C  
ATOM   2388  CE1 TYR A 288      -3.175 -15.946 -27.327  1.00 37.83           C  
ANISOU 2388  CE1 TYR A 288     4572   5285   4516    419   -472     27       C  
ATOM   2389  CE2 TYR A 288      -1.275 -17.226 -28.011  1.00 39.84           C  
ANISOU 2389  CE2 TYR A 288     4987   5451   4701    319   -443     64       C  
ATOM   2390  CZ  TYR A 288      -2.322 -16.382 -28.316  1.00 38.02           C  
ANISOU 2390  CZ  TYR A 288     4692   5256   4499    382   -492     60       C  
ATOM   2391  OH  TYR A 288      -2.527 -15.967 -29.614  1.00 40.25           O  
ANISOU 2391  OH  TYR A 288     5005   5522   4765    412   -561     88       O  
ATOM   2392  N   SER A 289      -2.300 -20.703 -22.254  1.00 38.54           N  
ANISOU 2392  N   SER A 289     4666   5456   4521     54   -203    -51       N  
ATOM   2393  CA  SER A 289      -1.668 -21.607 -21.300  1.00 39.20           C  
ANISOU 2393  CA  SER A 289     4806   5514   4574    -13   -160    -51       C  
ATOM   2394  C   SER A 289      -0.770 -22.557 -22.076  1.00 39.23           C  
ANISOU 2394  C   SER A 289     4904   5457   4546    -50   -185    -23       C  
ATOM   2395  O   SER A 289      -1.053 -22.887 -23.234  1.00 40.40           O  
ANISOU 2395  O   SER A 289     5057   5608   4683    -60   -228    -11       O  
ATOM   2396  CB  SER A 289      -2.709 -22.408 -20.531  1.00 40.92           C  
ANISOU 2396  CB  SER A 289     4965   5806   4775    -93   -131    -72       C  
ATOM   2397  OG  SER A 289      -3.418 -23.269 -21.406  1.00 47.05           O  
ANISOU 2397  OG  SER A 289     5722   6619   5537   -153   -171    -64       O  
ATOM   2398  N   LEU A 290       0.306 -22.995 -21.434  1.00 38.37           N  
ANISOU 2398  N   LEU A 290     4868   5292   4419    -67   -159    -14       N  
ATOM   2399  CA  LEU A 290       1.284 -23.861 -22.078  1.00 37.08           C  
ANISOU 2399  CA  LEU A 290     4793   5065   4229    -86   -175      9       C  
ATOM   2400  C   LEU A 290       0.691 -25.222 -22.439  1.00 36.74           C  
ANISOU 2400  C   LEU A 290     4773   5036   4149   -168   -192     10       C  
ATOM   2401  O   LEU A 290       1.119 -25.846 -23.407  1.00 37.60           O  
ANISOU 2401  O   LEU A 290     4944   5106   4236   -177   -217     23       O  
ATOM   2402  CB  LEU A 290       2.531 -24.008 -21.200  1.00 35.55           C  
ANISOU 2402  CB  LEU A 290     4660   4816   4030    -80   -147     17       C  
ATOM   2403  CG  LEU A 290       3.687 -24.866 -21.734  1.00 34.95           C  
ANISOU 2403  CG  LEU A 290     4672   4675   3934    -83   -157     37       C  
ATOM   2404  CD1 LEU A 290       4.183 -24.392 -23.105  1.00 34.00           C  
ANISOU 2404  CD1 LEU A 290     4567   4530   3821    -33   -178     51       C  
ATOM   2405  CD2 LEU A 290       4.818 -24.890 -20.731  1.00 32.70           C  
ANISOU 2405  CD2 LEU A 290     4425   4349   3651    -71   -136     45       C  
ATOM   2406  N   ASP A 291      -0.294 -25.667 -21.660  1.00 38.17           N  
ANISOU 2406  N   ASP A 291     4908   5274   4320   -233   -175     -6       N  
ATOM   2407  CA  ASP A 291      -1.066 -26.876 -21.954  1.00 41.08           C  
ANISOU 2407  CA  ASP A 291     5288   5667   4654   -326   -193     -7       C  
ATOM   2408  C   ASP A 291      -1.753 -26.746 -23.294  1.00 38.02           C  
ANISOU 2408  C   ASP A 291     4865   5310   4270   -321   -243     -5       C  
ATOM   2409  O   ASP A 291      -1.707 -27.649 -24.115  1.00 36.16           O  
ANISOU 2409  O   ASP A 291     4692   5046   4001   -366   -275      4       O  
ATOM   2410  CB  ASP A 291      -2.152 -27.090 -20.901  1.00 45.59           C  
ANISOU 2410  CB  ASP A 291     5789   6313   5220   -395   -161    -26       C  
ATOM   2411  CG  ASP A 291      -1.754 -28.078 -19.834  1.00 52.66           C  
ANISOU 2411  CG  ASP A 291     6759   7173   6075   -466   -129    -21       C  
ATOM   2412  OD1 ASP A 291      -0.708 -28.749 -19.988  1.00 55.51           O  
ANISOU 2412  OD1 ASP A 291     7228   7450   6413   -464   -141     -2       O  
ATOM   2413  OD2 ASP A 291      -2.509 -28.187 -18.839  1.00 60.52           O  
ANISOU 2413  OD2 ASP A 291     7709   8227   7061   -524    -91    -35       O  
ATOM   2414  N   TYR A 292      -2.402 -25.606 -23.493  1.00 37.24           N  
ANISOU 2414  N   TYR A 292     4672   5267   4211   -263   -254    -14       N  
ATOM   2415  CA  TYR A 292      -3.153 -25.356 -24.699  1.00 36.10           C  
ANISOU 2415  CA  TYR A 292     4484   5160   4073   -252   -310    -11       C  
ATOM   2416  C   TYR A 292      -2.230 -25.231 -25.909  1.00 34.97           C  
ANISOU 2416  C   TYR A 292     4428   4945   3915   -205   -344     10       C  
ATOM   2417  O   TYR A 292      -2.457 -25.886 -26.933  1.00 35.09           O  
ANISOU 2417  O   TYR A 292     4481   4953   3897   -245   -387     18       O  
ATOM   2418  CB  TYR A 292      -4.027 -24.112 -24.538  1.00 37.03           C  
ANISOU 2418  CB  TYR A 292     4481   5349   4239   -186   -315    -26       C  
ATOM   2419  CG  TYR A 292      -5.077 -24.017 -25.603  1.00 40.07           C  
ANISOU 2419  CG  TYR A 292     4800   5794   4631   -190   -380    -24       C  
ATOM   2420  CD1 TYR A 292      -4.813 -23.388 -26.818  1.00 38.20           C  
ANISOU 2420  CD1 TYR A 292     4594   5523   4396   -126   -435     -5       C  
ATOM   2421  CD2 TYR A 292      -6.331 -24.588 -25.411  1.00 40.05           C  
ANISOU 2421  CD2 TYR A 292     4707   5883   4628   -266   -391    -39       C  
ATOM   2422  CE1 TYR A 292      -5.796 -23.315 -27.812  1.00 42.79           C  
ANISOU 2422  CE1 TYR A 292     5120   6160   4979   -131   -506      0       C  
ATOM   2423  CE2 TYR A 292      -7.308 -24.524 -26.393  1.00 42.62           C  
ANISOU 2423  CE2 TYR A 292     4964   6269   4959   -274   -461    -36       C  
ATOM   2424  CZ  TYR A 292      -7.041 -23.884 -27.584  1.00 41.85           C  
ANISOU 2424  CZ  TYR A 292     4902   6135   4864   -204   -521    -16       C  
ATOM   2425  OH  TYR A 292      -8.023 -23.832 -28.548  1.00 44.02           O  
ANISOU 2425  OH  TYR A 292     5113   6471   5142   -213   -600    -11       O  
ATOM   2426  N   ILE A 293      -1.185 -24.408 -25.791  1.00 33.07           N  
ANISOU 2426  N   ILE A 293     4221   4651   3693   -129   -321     19       N  
ATOM   2427  CA  ILE A 293      -0.253 -24.199 -26.910  1.00 32.28           C  
ANISOU 2427  CA  ILE A 293     4199   4489   3578    -86   -342     40       C  
ATOM   2428  C   ILE A 293       0.538 -25.488 -27.224  1.00 33.51           C  
ANISOU 2428  C   ILE A 293     4459   4586   3689   -134   -333     46       C  
ATOM   2429  O   ILE A 293       0.742 -25.813 -28.396  1.00 34.11           O  
ANISOU 2429  O   ILE A 293     4593   4634   3733   -138   -362     55       O  
ATOM   2430  CB  ILE A 293       0.662 -22.953 -26.691  1.00 31.20           C  
ANISOU 2430  CB  ILE A 293     4068   4314   3473     -2   -318     49       C  
ATOM   2431  CG1 ILE A 293      -0.186 -21.692 -26.466  1.00 29.73           C  
ANISOU 2431  CG1 ILE A 293     3793   4175   3328     53   -332     40       C  
ATOM   2432  CG2 ILE A 293       1.625 -22.733 -27.867  1.00 31.10           C  
ANISOU 2432  CG2 ILE A 293     4132   4244   3441     32   -332     71       C  
ATOM   2433  CD1 ILE A 293      -1.165 -21.355 -27.605  1.00 27.68           C  
ANISOU 2433  CD1 ILE A 293     3496   3955   3068     69   -395     46       C  
ATOM   2434  N   SER A 294       0.939 -26.231 -26.191  1.00 31.80           N  
ANISOU 2434  N   SER A 294     4269   4348   3464   -171   -296     40       N  
ATOM   2435  CA  SER A 294       1.572 -27.546 -26.390  1.00 35.83           C  
ANISOU 2435  CA  SER A 294     4880   4800   3933   -214   -292     43       C  
ATOM   2436  C   SER A 294       0.693 -28.534 -27.144  1.00 35.81           C  
ANISOU 2436  C   SER A 294     4905   4812   3889   -290   -332     37       C  
ATOM   2437  O   SER A 294       1.169 -29.236 -28.031  1.00 34.11           O  
ANISOU 2437  O   SER A 294     4779   4545   3635   -298   -346     40       O  
ATOM   2438  CB  SER A 294       1.997 -28.186 -25.064  1.00 36.17           C  
ANISOU 2438  CB  SER A 294     4950   4821   3974   -243   -256     40       C  
ATOM   2439  OG  SER A 294       3.058 -27.463 -24.488  1.00 40.50           O  
ANISOU 2439  OG  SER A 294     5497   5341   4551   -177   -226     47       O  
ATOM   2440  N   GLU A 295      -0.583 -28.605 -26.777  1.00 38.46           N  
ANISOU 2440  N   GLU A 295     5164   5220   4230   -349   -348     27       N  
ATOM   2441  CA  GLU A 295      -1.511 -29.518 -27.452  1.00 39.62           C  
ANISOU 2441  CA  GLU A 295     5326   5389   4337   -437   -392     22       C  
ATOM   2442  C   GLU A 295      -1.683 -29.117 -28.918  1.00 36.97           C  
ANISOU 2442  C   GLU A 295     5001   5057   3990   -407   -444     29       C  
ATOM   2443  O   GLU A 295      -1.734 -29.969 -29.814  1.00 36.25           O  
ANISOU 2443  O   GLU A 295     4989   4934   3849   -455   -478     28       O  
ATOM   2444  CB  GLU A 295      -2.851 -29.588 -26.698  1.00 43.98           C  
ANISOU 2444  CB  GLU A 295     5773   6032   4903   -509   -394     10       C  
ATOM   2445  CG  GLU A 295      -4.124 -29.683 -27.566  1.00 56.13           C  
ANISOU 2445  CG  GLU A 295     7250   7643   6433   -564   -455      6       C  
ATOM   2446  CD  GLU A 295      -4.464 -31.087 -28.048  1.00 64.90           C  
ANISOU 2446  CD  GLU A 295     8444   8730   7484   -678   -489      4       C  
ATOM   2447  OE1 GLU A 295      -3.548 -31.931 -28.193  1.00 69.23           O  
ANISOU 2447  OE1 GLU A 295     9126   9186   7994   -689   -477      8       O  
ATOM   2448  OE2 GLU A 295      -5.665 -31.340 -28.299  1.00 68.27           O  
ANISOU 2448  OE2 GLU A 295     8801   9233   7905   -757   -530     -1       O  
ATOM   2449  N   PHE A 296      -1.738 -27.814 -29.160  1.00 35.05           N  
ANISOU 2449  N   PHE A 296     4689   4844   3786   -327   -452     35       N  
ATOM   2450  CA  PHE A 296      -1.939 -27.316 -30.503  1.00 37.06           C  
ANISOU 2450  CA  PHE A 296     4952   5102   4026   -297   -506     45       C  
ATOM   2451  C   PHE A 296      -0.707 -27.597 -31.360  1.00 35.55           C  
ANISOU 2451  C   PHE A 296     4886   4826   3796   -266   -493     55       C  
ATOM   2452  O   PHE A 296      -0.824 -28.129 -32.463  1.00 32.76           O  
ANISOU 2452  O   PHE A 296     4601   4453   3392   -298   -532     56       O  
ATOM   2453  CB  PHE A 296      -2.277 -25.822 -30.479  1.00 37.21           C  
ANISOU 2453  CB  PHE A 296     4877   5166   4096   -214   -518     52       C  
ATOM   2454  CG  PHE A 296      -2.444 -25.216 -31.840  1.00 39.23           C  
ANISOU 2454  CG  PHE A 296     5152   5419   4335   -177   -578     69       C  
ATOM   2455  CD1 PHE A 296      -3.711 -25.088 -32.407  1.00 42.56           C  
ANISOU 2455  CD1 PHE A 296     5503   5910   4757   -200   -650     69       C  
ATOM   2456  CD2 PHE A 296      -1.338 -24.767 -32.557  1.00 39.85           C  
ANISOU 2456  CD2 PHE A 296     5317   5430   4394   -122   -565     85       C  
ATOM   2457  CE1 PHE A 296      -3.873 -24.519 -33.672  1.00 43.92           C  
ANISOU 2457  CE1 PHE A 296     5703   6078   4908   -166   -714     88       C  
ATOM   2458  CE2 PHE A 296      -1.491 -24.203 -33.827  1.00 42.42           C  
ANISOU 2458  CE2 PHE A 296     5673   5751   4695    -94   -621    104       C  
ATOM   2459  CZ  PHE A 296      -2.758 -24.078 -34.383  1.00 41.51           C  
ANISOU 2459  CZ  PHE A 296     5497   5698   4576   -114   -699    106       C  
ATOM   2460  N   GLU A 297       0.467 -27.251 -30.838  1.00 35.69           N  
ANISOU 2460  N   GLU A 297     4930   4796   3833   -208   -438     60       N  
ATOM   2461  CA  GLU A 297       1.711 -27.337 -31.610  1.00 34.16           C  
ANISOU 2461  CA  GLU A 297     4835   4534   3612   -167   -415     68       C  
ATOM   2462  C   GLU A 297       2.247 -28.759 -31.774  1.00 34.63           C  
ANISOU 2462  C   GLU A 297     5000   4535   3624   -209   -399     56       C  
ATOM   2463  O   GLU A 297       2.783 -29.091 -32.826  1.00 35.48           O  
ANISOU 2463  O   GLU A 297     5194   4600   3688   -199   -401     56       O  
ATOM   2464  CB  GLU A 297       2.797 -26.453 -30.994  1.00 29.32           C  
ANISOU 2464  CB  GLU A 297     4203   3897   3040    -94   -365     77       C  
ATOM   2465  CG  GLU A 297       2.509 -24.967 -31.065  1.00 31.30           C  
ANISOU 2465  CG  GLU A 297     4383   4181   3329    -40   -380     90       C  
ATOM   2466  CD  GLU A 297       2.527 -24.420 -32.482  1.00 33.91           C  
ANISOU 2466  CD  GLU A 297     4753   4501   3629    -15   -415    106       C  
ATOM   2467  OE1 GLU A 297       3.322 -24.919 -33.312  1.00 33.84           O  
ANISOU 2467  OE1 GLU A 297     4833   4447   3577    -17   -399    109       O  
ATOM   2468  OE2 GLU A 297       1.752 -23.479 -32.765  1.00 32.94           O  
ANISOU 2468  OE2 GLU A 297     4577   4415   3525     10   -457    116       O  
ATOM   2469  N   LEU A 298       2.103 -29.583 -30.740  1.00 33.43           N  
ANISOU 2469  N   LEU A 298     4849   4378   3477   -256   -383     46       N  
ATOM   2470  CA  LEU A 298       2.808 -30.863 -30.673  1.00 36.32           C  
ANISOU 2470  CA  LEU A 298     5322   4673   3806   -278   -362     37       C  
ATOM   2471  C   LEU A 298       1.888 -32.080 -30.581  1.00 38.23           C  
ANISOU 2471  C   LEU A 298     5606   4914   4007   -379   -394     25       C  
ATOM   2472  O   LEU A 298       2.365 -33.214 -30.701  1.00 36.67           O  
ANISOU 2472  O   LEU A 298     5518   4647   3769   -402   -387     16       O  
ATOM   2473  CB  LEU A 298       3.755 -30.878 -29.468  1.00 35.17           C  
ANISOU 2473  CB  LEU A 298     5171   4498   3694   -238   -313     41       C  
ATOM   2474  CG  LEU A 298       4.630 -29.652 -29.210  1.00 35.87           C  
ANISOU 2474  CG  LEU A 298     5203   4594   3830   -154   -280     54       C  
ATOM   2475  CD1 LEU A 298       5.060 -29.589 -27.737  1.00 30.24           C  
ANISOU 2475  CD1 LEU A 298     4458   3880   3154   -144   -250     57       C  
ATOM   2476  CD2 LEU A 298       5.828 -29.657 -30.151  1.00 37.97           C  
ANISOU 2476  CD2 LEU A 298     5536   4812   4080    -95   -256     56       C  
ATOM   2477  N   ASN A 299       0.590 -31.832 -30.360  1.00 39.44           N  
ANISOU 2477  N   ASN A 299     5672   5142   4171   -440   -429     25       N  
ATOM   2478  CA AASN A 299      -0.419 -32.881 -30.150  0.50 42.71           C  
ANISOU 2478  CA AASN A 299     6102   5572   4552   -554   -460     15       C  
ATOM   2479  CA BASN A 299      -0.407 -32.902 -30.172  0.50 43.27           C  
ANISOU 2479  CA BASN A 299     6177   5642   4622   -554   -460     15       C  
ATOM   2480  C   ASN A 299      -0.137 -33.784 -28.937  1.00 45.28           C  
ANISOU 2480  C   ASN A 299     6473   5858   4871   -597   -425     14       C  
ATOM   2481  O   ASN A 299      -0.445 -34.984 -28.934  1.00 46.91           O  
ANISOU 2481  O   ASN A 299     6765   6028   5032   -684   -442      7       O  
ATOM   2482  CB AASN A 299      -0.676 -33.678 -31.438  0.50 41.84           C  
ANISOU 2482  CB AASN A 299     6091   5428   4378   -605   -507      6       C  
ATOM   2483  CB BASN A 299      -0.563 -33.754 -31.445  0.50 43.11           C  
ANISOU 2483  CB BASN A 299     6264   5579   4535   -602   -504      6       C  
ATOM   2484  CG AASN A 299      -1.319 -32.829 -32.525  0.50 42.44           C  
ANISOU 2484  CG AASN A 299     6109   5562   4454   -589   -558     11       C  
ATOM   2485  CG BASN A 299      -1.829 -34.598 -31.438  0.50 46.25           C  
ANISOU 2485  CG BASN A 299     6659   6014   4900   -732   -552     -2       C  
ATOM   2486  OD1AASN A 299      -2.493 -32.461 -32.431  0.50 41.03           O  
ANISOU 2486  OD1AASN A 299     5826   5468   4294   -635   -598     13       O  
ATOM   2487  OD1BASN A 299      -2.776 -34.313 -30.700  0.50 47.19           O  
ANISOU 2487  OD1BASN A 299     6664   6214   5051   -781   -558      1       O  
ATOM   2488  ND2AASN A 299      -0.544 -32.500 -33.556  0.50 42.23           N  
ANISOU 2488  ND2AASN A 299     6149   5492   4404   -523   -556     14       N  
ATOM   2489  ND2BASN A 299      -1.848 -35.646 -32.259  0.50 45.15           N  
ANISOU 2489  ND2BASN A 299     6645   5815   4695   -792   -584    -13       N  
ATOM   2490  N   VAL A 300       0.434 -33.187 -27.892  1.00 45.50           N  
ANISOU 2490  N   VAL A 300     6452   5891   4944   -541   -381     21       N  
ATOM   2491  CA  VAL A 300       0.660 -33.899 -26.634  1.00 48.82           C  
ANISOU 2491  CA  VAL A 300     6908   6281   5359   -579   -352     23       C  
ATOM   2492  C   VAL A 300      -0.493 -33.613 -25.678  1.00 51.27           C  
ANISOU 2492  C   VAL A 300     7113   6680   5688   -648   -346     21       C  
ATOM   2493  O   VAL A 300      -1.076 -32.526 -25.707  1.00 50.73           O  
ANISOU 2493  O   VAL A 300     6925   6691   5660   -618   -347     19       O  
ATOM   2494  CB  VAL A 300       2.019 -33.538 -25.960  1.00 48.07           C  
ANISOU 2494  CB  VAL A 300     6834   6137   5294   -485   -310     32       C  
ATOM   2495  CG1 VAL A 300       3.181 -34.093 -26.762  1.00 48.44           C  
ANISOU 2495  CG1 VAL A 300     6991   6097   5319   -426   -308     31       C  
ATOM   2496  CG2 VAL A 300       2.168 -32.022 -25.741  1.00 46.62           C  
ANISOU 2496  CG2 VAL A 300     6536   6010   5166   -408   -291     37       C  
ATOM   2497  N   GLY A 301      -0.822 -34.593 -24.840  1.00 54.07           N  
ANISOU 2497  N   GLY A 301     7514   7019   6012   -740   -338     23       N  
ATOM   2498  CA  GLY A 301      -1.905 -34.448 -23.872  1.00 57.44           C  
ANISOU 2498  CA  GLY A 301     7846   7532   6448   -819   -321     19       C  
ATOM   2499  C   GLY A 301      -1.594 -33.428 -22.791  1.00 59.02           C  
ANISOU 2499  C   GLY A 301     7966   7768   6693   -752   -274     20       C  
ATOM   2500  O   GLY A 301      -0.431 -33.207 -22.448  1.00 57.73           O  
ANISOU 2500  O   GLY A 301     7851   7543   6542   -673   -254     28       O  
ATOM   2501  N   LYS A 302      -2.645 -32.793 -22.276  1.00 62.59           N  
ANISOU 2501  N   LYS A 302     8292   8322   7169   -783   -257      9       N  
ATOM   2502  CA  LYS A 302      -2.554 -31.902 -21.114  1.00 65.99           C  
ANISOU 2502  CA  LYS A 302     8649   8791   7632   -738   -207      4       C  
ATOM   2503  C   LYS A 302      -1.963 -32.624 -19.891  1.00 67.39           C  
ANISOU 2503  C   LYS A 302     8917   8913   7776   -779   -175     14       C  
ATOM   2504  O   LYS A 302      -2.214 -33.822 -19.682  1.00 67.05           O  
ANISOU 2504  O   LYS A 302     8953   8839   7683   -881   -182     22       O  
ATOM   2505  CB  LYS A 302      -3.942 -31.304 -20.812  1.00 67.60           C  
ANISOU 2505  CB  LYS A 302     8707   9118   7860   -776   -192    -15       C  
ATOM   2506  CG  LYS A 302      -4.435 -31.400 -19.357  1.00 72.51           C  
ANISOU 2506  CG  LYS A 302     9291   9790   8469   -840   -133    -24       C  
ATOM   2507  CD  LYS A 302      -5.928 -31.061 -19.228  1.00 76.33           C  
ANISOU 2507  CD  LYS A 302     9627  10406   8971   -894   -118    -46       C  
ATOM   2508  CE  LYS A 302      -6.818 -32.160 -19.813  1.00 80.57           C  
ANISOU 2508  CE  LYS A 302    10169  10973   9472  -1024   -154    -41       C  
ATOM   2509  NZ  LYS A 302      -8.239 -31.731 -19.958  1.00 82.21           N  
ANISOU 2509  NZ  LYS A 302    10210  11318   9710  -1061   -154    -62       N  
ATOM   2510  N   LEU A 303      -1.159 -31.899 -19.113  1.00 67.73           N  
ANISOU 2510  N   LEU A 303     8955   8936   7841   -703   -144     16       N  
ATOM   2511  CA  LEU A 303      -0.616 -32.426 -17.860  1.00 69.93           C  
ANISOU 2511  CA  LEU A 303     9310   9169   8089   -735   -118     27       C  
ATOM   2512  C   LEU A 303      -1.746 -32.626 -16.850  1.00 71.63           C  
ANISOU 2512  C   LEU A 303     9476   9461   8278   -840    -79     17       C  
ATOM   2513  O   LEU A 303      -2.421 -31.668 -16.456  1.00 72.53           O  
ANISOU 2513  O   LEU A 303     9475   9663   8421   -822    -44     -3       O  
ATOM   2514  CB  LEU A 303       0.473 -31.508 -17.284  1.00 69.14           C  
ANISOU 2514  CB  LEU A 303     9210   9041   8021   -633   -101     31       C  
ATOM   2515  CG  LEU A 303       1.885 -31.412 -17.897  1.00 69.32           C  
ANISOU 2515  CG  LEU A 303     9296   8981   8063   -537   -128     45       C  
ATOM   2516  CD1 LEU A 303       2.273 -32.622 -18.753  1.00 67.82           C  
ANISOU 2516  CD1 LEU A 303     9209   8717   7843   -557   -163     58       C  
ATOM   2517  CD2 LEU A 303       2.083 -30.101 -18.662  1.00 70.08           C  
ANISOU 2517  CD2 LEU A 303     9310   9106   8212   -442   -130     36       C  
ATOM   2518  N   LYS A 304      -1.945 -33.880 -16.445  1.00 71.99           N  
ANISOU 2518  N   LYS A 304     9614   9472   8266   -949    -83     31       N  
ATOM   2519  CA  LYS A 304      -3.112 -34.279 -15.668  1.00 73.10           C  
ANISOU 2519  CA  LYS A 304     9716   9687   8371  -1075    -46     24       C  
ATOM   2520  C   LYS A 304      -2.776 -34.434 -14.184  1.00 71.99           C  
ANISOU 2520  C   LYS A 304     9633   9526   8192  -1108     -4     33       C  
ATOM   2521  O   LYS A 304      -1.863 -35.181 -13.826  1.00 72.51           O  
ANISOU 2521  O   LYS A 304     9836   9491   8223  -1111    -26     58       O  
ATOM   2522  CB  LYS A 304      -3.669 -35.591 -16.241  1.00 74.94           C  
ANISOU 2522  CB  LYS A 304    10021   9897   8558  -1196    -80     35       C  
ATOM   2523  CG  LYS A 304      -5.186 -35.766 -16.149  1.00 79.06           C  
ANISOU 2523  CG  LYS A 304    10440  10532   9066  -1321    -58     20       C  
ATOM   2524  CD  LYS A 304      -5.599 -36.686 -14.995  1.00 82.00           C  
ANISOU 2524  CD  LYS A 304    10880  10904   9370  -1464    -21     33       C  
ATOM   2525  CE  LYS A 304      -6.000 -35.899 -13.751  1.00 81.89           C  
ANISOU 2525  CE  LYS A 304    10774  10978   9361  -1466     54     17       C  
ATOM   2526  NZ  LYS A 304      -5.847 -36.703 -12.509  1.00 81.22           N  
ANISOU 2526  NZ  LYS A 304    10806  10851   9203  -1566     87     37       N  
ATOM   2527  N   TYR A 305      -3.512 -33.721 -13.330  1.00 70.89           N  
ANISOU 2527  N   TYR A 305     9394   9483   8058  -1129     54     12       N  
ATOM   2528  CA  TYR A 305      -3.400 -33.873 -11.870  1.00 69.55           C  
ANISOU 2528  CA  TYR A 305     9277   9309   7839  -1182    102     17       C  
ATOM   2529  C   TYR A 305      -4.721 -33.605 -11.138  1.00 68.73           C  
ANISOU 2529  C   TYR A 305     9065   9331   7719  -1270    173     -8       C  
ATOM   2530  O   TYR A 305      -5.606 -32.928 -11.669  1.00 67.67           O  
ANISOU 2530  O   TYR A 305     8785   9295   7630  -1249    189    -36       O  
ATOM   2531  CB  TYR A 305      -2.284 -32.987 -11.302  1.00 69.60           C  
ANISOU 2531  CB  TYR A 305     9306   9271   7868  -1064    105     17       C  
ATOM   2532  CG  TYR A 305      -2.421 -31.508 -11.608  1.00 70.34           C  
ANISOU 2532  CG  TYR A 305     9268   9429   8030   -953    125    -14       C  
ATOM   2533  CD1 TYR A 305      -3.177 -30.670 -10.786  1.00 70.08           C  
ANISOU 2533  CD1 TYR A 305     9140   9488   8000   -958    191    -46       C  
ATOM   2534  CD2 TYR A 305      -1.778 -30.945 -12.710  1.00 71.41           C  
ANISOU 2534  CD2 TYR A 305     9382   9529   8222   -843     79    -12       C  
ATOM   2535  CE1 TYR A 305      -3.301 -29.310 -11.059  1.00 71.44           C  
ANISOU 2535  CE1 TYR A 305     9203   9707   8233   -849    205    -75       C  
ATOM   2536  CE2 TYR A 305      -1.891 -29.583 -12.994  1.00 73.52           C  
ANISOU 2536  CE2 TYR A 305     9543   9844   8547   -744     92    -37       C  
ATOM   2537  CZ  TYR A 305      -2.653 -28.772 -12.162  1.00 73.86           C  
ANISOU 2537  CZ  TYR A 305     9499   9970   8595   -745    152    -68       C  
ATOM   2538  OH  TYR A 305      -2.765 -27.428 -12.441  1.00 75.22           O  
ANISOU 2538  OH  TYR A 305     9579  10179   8823   -641    162    -94       O  
ATOM   2539  N   ASP A 306      -4.837 -34.139  -9.920  1.00 68.00           N  
ANISOU 2539  N   ASP A 306     9043   9235   7559  -1366    215      1       N  
ATOM   2540  CA  ASP A 306      -6.034 -33.979  -9.083  1.00 68.41           C  
ANISOU 2540  CA  ASP A 306     9004   9407   7583  -1462    297    -23       C  
ATOM   2541  C   ASP A 306      -5.905 -32.811  -8.106  1.00 66.30           C  
ANISOU 2541  C   ASP A 306     8683   9184   7325  -1386    359    -52       C  
ATOM   2542  O   ASP A 306      -4.815 -32.519  -7.612  1.00 65.02           O  
ANISOU 2542  O   ASP A 306     8609   8940   7154  -1314    342    -40       O  
ATOM   2543  CB  ASP A 306      -6.321 -35.262  -8.289  1.00 71.00           C  
ANISOU 2543  CB  ASP A 306     9450   9710   7818  -1629    315      4       C  
ATOM   2544  CG  ASP A 306      -6.648 -36.454  -9.180  1.00 74.73           C  
ANISOU 2544  CG  ASP A 306     9978  10145   8271  -1728    261     28       C  
ATOM   2545  OD1 ASP A 306      -6.204 -37.574  -8.845  1.00 75.43           O  
ANISOU 2545  OD1 ASP A 306    10233  10135   8293  -1809    233     64       O  
ATOM   2546  OD2 ASP A 306      -7.350 -36.279 -10.204  1.00 74.88           O  
ANISOU 2546  OD2 ASP A 306     9883  10231   8338  -1725    243     11       O  
ATOM   2547  N   GLY A 307      -7.029 -32.159  -7.821  1.00 65.42           N  
ANISOU 2547  N   GLY A 307     8423   9202   7229  -1403    430    -92       N  
ATOM   2548  CA  GLY A 307      -7.073 -31.052  -6.867  1.00 64.56           C  
ANISOU 2548  CA  GLY A 307     8261   9143   7124  -1338    500   -128       C  
ATOM   2549  C   GLY A 307      -6.441 -29.774  -7.390  1.00 62.50           C  
ANISOU 2549  C   GLY A 307     7949   8857   6940  -1165    471   -147       C  
ATOM   2550  O   GLY A 307      -5.916 -29.749  -8.508  1.00 61.74           O  
ANISOU 2550  O   GLY A 307     7859   8704   6893  -1096    397   -130       O  
ATOM   2551  N   PRO A 308      -6.482 -28.696  -6.587  1.00 61.42           N  
ANISOU 2551  N   PRO A 308     7769   8759   6809  -1098    530   -184       N  
ATOM   2552  CA  PRO A 308      -5.866 -27.446  -7.040  1.00 60.21           C  
ANISOU 2552  CA  PRO A 308     7580   8572   6723   -940    501   -202       C  
ATOM   2553  C   PRO A 308      -4.338 -27.515  -7.028  1.00 58.32           C  
ANISOU 2553  C   PRO A 308     7481   8201   6477   -889    435   -166       C  
ATOM   2554  O   PRO A 308      -3.752 -28.272  -6.248  1.00 56.68           O  
ANISOU 2554  O   PRO A 308     7398   7933   6203   -958    430   -139       O  
ATOM   2555  CB  PRO A 308      -6.367 -26.410  -6.026  1.00 60.98           C  
ANISOU 2555  CB  PRO A 308     7615   8740   6814   -902    589   -253       C  
ATOM   2556  CG  PRO A 308      -6.677 -27.195  -4.794  1.00 62.31           C  
ANISOU 2556  CG  PRO A 308     7851   8935   6890  -1035    654   -250       C  
ATOM   2557  CD  PRO A 308      -7.104 -28.567  -5.255  1.00 62.59           C  
ANISOU 2557  CD  PRO A 308     7905   8978   6897  -1165    628   -214       C  
ATOM   2558  N   ILE A 309      -3.719 -26.722  -7.898  1.00 56.84           N  
ANISOU 2558  N   ILE A 309     7269   7971   6356   -769    384   -166       N  
ATOM   2559  CA  ILE A 309      -2.264 -26.600  -7.989  1.00 55.93           C  
ANISOU 2559  CA  ILE A 309     7259   7745   6247   -706    325   -137       C  
ATOM   2560  C   ILE A 309      -1.651 -26.163  -6.646  1.00 54.97           C  
ANISOU 2560  C   ILE A 309     7213   7593   6081   -702    354   -145       C  
ATOM   2561  O   ILE A 309      -0.495 -26.478  -6.346  1.00 53.88           O  
ANISOU 2561  O   ILE A 309     7183   7368   5920   -697    309   -114       O  
ATOM   2562  CB  ILE A 309      -1.866 -25.622  -9.148  1.00 56.11           C  
ANISOU 2562  CB  ILE A 309     7223   7746   6349   -582    280   -141       C  
ATOM   2563  CG1 ILE A 309      -0.473 -25.952  -9.720  1.00 58.50           C  
ANISOU 2563  CG1 ILE A 309     7620   7945   6664   -543    207   -100       C  
ATOM   2564  CG2 ILE A 309      -2.055 -24.148  -8.739  1.00 56.75           C  
ANISOU 2564  CG2 ILE A 309     7240   7860   6461   -493    319   -183       C  
ATOM   2565  CD1 ILE A 309       0.691 -25.188  -9.112  1.00 60.22           C  
ANISOU 2565  CD1 ILE A 309     7895   8100   6884   -479    194    -98       C  
ATOM   2566  N   SER A 310      -2.446 -25.458  -5.842  1.00 53.69           N  
ANISOU 2566  N   SER A 310     6992   7505   5903   -704    430   -190       N  
ATOM   2567  CA  SER A 310      -2.011 -24.980  -4.537  1.00 53.17           C  
ANISOU 2567  CA  SER A 310     6997   7419   5786   -705    466   -206       C  
ATOM   2568  C   SER A 310      -1.884 -26.110  -3.520  1.00 52.08           C  
ANISOU 2568  C   SER A 310     6972   7261   5556   -828    480   -179       C  
ATOM   2569  O   SER A 310      -1.332 -25.913  -2.438  1.00 51.51           O  
ANISOU 2569  O   SER A 310     6989   7154   5429   -841    491   -180       O  
ATOM   2570  CB  SER A 310      -2.963 -23.899  -4.016  1.00 55.39           C  
ANISOU 2570  CB  SER A 310     7184   7786   6074   -666    551   -267       C  
ATOM   2571  OG  SER A 310      -4.290 -24.386  -3.882  1.00 59.66           O  
ANISOU 2571  OG  SER A 310     7640   8431   6595   -744    619   -288       O  
ATOM   2572  N   LYS A 311      -2.391 -27.288  -3.875  1.00 50.85           N  
ANISOU 2572  N   LYS A 311     6821   7121   5379   -921    473   -153       N  
ATOM   2573  CA  LYS A 311      -2.270 -28.472  -3.025  1.00 51.29           C  
ANISOU 2573  CA  LYS A 311     6999   7145   5346  -1044    476   -119       C  
ATOM   2574  C   LYS A 311      -1.439 -29.595  -3.665  1.00 49.71           C  
ANISOU 2574  C   LYS A 311     6896   6846   5144  -1063    386    -63       C  
ATOM   2575  O   LYS A 311      -1.235 -30.643  -3.046  1.00 49.63           O  
ANISOU 2575  O   LYS A 311     7004   6790   5061  -1157    373    -28       O  
ATOM   2576  CB  LYS A 311      -3.656 -28.986  -2.621  1.00 53.08           C  
ANISOU 2576  CB  LYS A 311     7169   7473   5525  -1163    559   -139       C  
ATOM   2577  CG  LYS A 311      -4.360 -28.112  -1.588  1.00 58.92           C  
ANISOU 2577  CG  LYS A 311     7853   8300   6234  -1165    661   -192       C  
ATOM   2578  CD  LYS A 311      -5.813 -28.535  -1.389  1.00 66.50           C  
ANISOU 2578  CD  LYS A 311     8720   9382   7165  -1274    749   -216       C  
ATOM   2579  CE  LYS A 311      -6.605 -27.484  -0.603  1.00 70.41           C  
ANISOU 2579  CE  LYS A 311     9122   9979   7652  -1243    858   -282       C  
ATOM   2580  NZ  LYS A 311      -8.086 -27.612  -0.801  1.00 72.62           N  
ANISOU 2580  NZ  LYS A 311     9246  10400   7945  -1304    938   -315       N  
ATOM   2581  N   LEU A 312      -0.944 -29.365  -4.884  1.00 45.46           N  
ANISOU 2581  N   LEU A 312     6316   6273   4682   -973    326    -54       N  
ATOM   2582  CA  LEU A 312      -0.256 -30.408  -5.649  1.00 43.99           C  
ANISOU 2582  CA  LEU A 312     6210   6003   4502   -980    250     -9       C  
ATOM   2583  C   LEU A 312       1.074 -30.837  -5.045  1.00 42.08           C  
ANISOU 2583  C   LEU A 312     6106   5657   4226   -964    192     29       C  
ATOM   2584  O   LEU A 312       1.353 -32.038  -4.952  1.00 39.13           O  
ANISOU 2584  O   LEU A 312     5840   5219   3807  -1026    155     67       O  
ATOM   2585  CB  LEU A 312      -0.067 -30.008  -7.121  1.00 43.72           C  
ANISOU 2585  CB  LEU A 312     6097   5963   4553   -886    207    -13       C  
ATOM   2586  CG  LEU A 312       0.484 -31.103  -8.049  1.00 46.43           C  
ANISOU 2586  CG  LEU A 312     6512   6228   4901   -894    139     25       C  
ATOM   2587  CD1 LEU A 312      -0.375 -32.375  -8.023  1.00 47.75           C  
ANISOU 2587  CD1 LEU A 312     6722   6406   5013  -1025    149     38       C  
ATOM   2588  CD2 LEU A 312       0.628 -30.601  -9.476  1.00 47.65           C  
ANISOU 2588  CD2 LEU A 312     6589   6384   5131   -803    107     17       C  
ATOM   2589  N   ARG A 313       1.893 -29.862  -4.651  1.00 40.11           N  
ANISOU 2589  N   ARG A 313     5856   5387   3998   -880    180     20       N  
ATOM   2590  CA  ARG A 313       3.174 -30.154  -4.003  1.00 41.76           C  
ANISOU 2590  CA  ARG A 313     6182   5509   4178   -861    121     54       C  
ATOM   2591  C   ARG A 313       2.961 -31.031  -2.763  1.00 43.67           C  
ANISOU 2591  C   ARG A 313     6540   5732   4319   -973    135     75       C  
ATOM   2592  O   ARG A 313       3.654 -32.031  -2.572  1.00 43.88           O  
ANISOU 2592  O   ARG A 313     6683   5679   4311   -997     75    119       O  
ATOM   2593  CB  ARG A 313       3.913 -28.859  -3.638  1.00 41.84           C  
ANISOU 2593  CB  ARG A 313     6164   5516   4218   -774    114     35       C  
ATOM   2594  CG  ARG A 313       5.281 -29.079  -3.014  1.00 41.05           C  
ANISOU 2594  CG  ARG A 313     6167   5333   4095   -749     44     71       C  
ATOM   2595  CD  ARG A 313       5.968 -27.771  -2.672  1.00 40.65           C  
ANISOU 2595  CD  ARG A 313     6087   5284   4073   -677     35     51       C  
ATOM   2596  NE  ARG A 313       7.178 -27.985  -1.874  1.00 38.32           N  
ANISOU 2596  NE  ARG A 313     5890   4924   3747   -672    -32     84       N  
ATOM   2597  CZ  ARG A 313       7.206 -28.050  -0.544  1.00 37.96           C  
ANISOU 2597  CZ  ARG A 313     5932   4871   3620   -732    -27     87       C  
ATOM   2598  NH1 ARG A 313       6.094 -27.911   0.166  1.00 38.32           N  
ANISOU 2598  NH1 ARG A 313     5981   4974   3606   -805     53     56       N  
ATOM   2599  NH2 ARG A 313       8.355 -28.248   0.082  1.00 39.52           N  
ANISOU 2599  NH2 ARG A 313     6213   5009   3794   -720   -103    121       N  
ATOM   2600  N   GLU A 314       1.975 -30.653  -1.952  1.00 46.37           N  
ANISOU 2600  N   GLU A 314     6853   6152   4615  -1040    217     43       N  
ATOM   2601  CA  GLU A 314       1.621 -31.356  -0.716  1.00 48.52           C  
ANISOU 2601  CA  GLU A 314     7230   6423   4781  -1159    248     58       C  
ATOM   2602  C   GLU A 314       1.098 -32.776  -0.976  1.00 47.30           C  
ANISOU 2602  C   GLU A 314     7138   6248   4585  -1267    240     91       C  
ATOM   2603  O   GLU A 314       1.562 -33.737  -0.359  1.00 47.26           O  
ANISOU 2603  O   GLU A 314     7278   6169   4511  -1328    198    134       O  
ATOM   2604  CB  GLU A 314       0.582 -30.532   0.059  1.00 50.60           C  
ANISOU 2604  CB  GLU A 314     7423   6789   5012  -1199    353      6       C  
ATOM   2605  CG  GLU A 314       0.293 -30.990   1.486  1.00 57.91           C  
ANISOU 2605  CG  GLU A 314     8460   7722   5820  -1316    399     14       C  
ATOM   2606  CD  GLU A 314      -0.548 -29.977   2.273  1.00 65.53           C  
ANISOU 2606  CD  GLU A 314     9355   8786   6758  -1327    506    -46       C  
ATOM   2607  OE1 GLU A 314      -0.556 -30.046   3.525  1.00 66.50           O  
ANISOU 2607  OE1 GLU A 314     9575   8908   6783  -1398    542    -47       O  
ATOM   2608  OE2 GLU A 314      -1.196 -29.107   1.644  1.00 67.46           O  
ANISOU 2608  OE2 GLU A 314     9452   9105   7073  -1262    554    -93       O  
ATOM   2609  N   SER A 315       0.143 -32.905  -1.890  1.00 45.25           N  
ANISOU 2609  N   SER A 315     6777   6050   4365  -1290    273     72       N  
ATOM   2610  CA  SER A 315      -0.482 -34.199  -2.149  1.00 46.23           C  
ANISOU 2610  CA  SER A 315     6955   6163   4447  -1408    270     98       C  
ATOM   2611  C   SER A 315       0.384 -35.142  -2.991  1.00 45.68           C  
ANISOU 2611  C   SER A 315     6976   5981   4400  -1373    175    141       C  
ATOM   2612  O   SER A 315       0.365 -36.361  -2.783  1.00 46.09           O  
ANISOU 2612  O   SER A 315     7153   5971   4390  -1464    147    179       O  
ATOM   2613  CB  SER A 315      -1.869 -34.023  -2.783  1.00 46.33           C  
ANISOU 2613  CB  SER A 315     6823   6290   4491  -1458    337     62       C  
ATOM   2614  OG  SER A 315      -1.829 -33.171  -3.913  1.00 44.91           O  
ANISOU 2614  OG  SER A 315     6514   6141   4411  -1339    321     35       O  
ATOM   2615  N   ASN A 316       1.148 -34.570  -3.922  1.00 44.27           N  
ANISOU 2615  N   ASN A 316     6739   5775   4306  -1240    127    135       N  
ATOM   2616  CA  ASN A 316       1.904 -35.350  -4.899  1.00 42.65           C  
ANISOU 2616  CA  ASN A 316     6595   5478   4134  -1191     49    165       C  
ATOM   2617  C   ASN A 316       3.150 -34.622  -5.391  1.00 40.09           C  
ANISOU 2617  C   ASN A 316     6242   5111   3881  -1042     -2    165       C  
ATOM   2618  O   ASN A 316       3.231 -34.238  -6.554  1.00 39.53           O  
ANISOU 2618  O   ASN A 316     6087   5052   3880   -968    -14    150       O  
ATOM   2619  CB  ASN A 316       1.007 -35.695  -6.091  1.00 42.70           C  
ANISOU 2619  CB  ASN A 316     6528   5523   4171  -1225     61    150       C  
ATOM   2620  CG  ASN A 316       1.482 -36.927  -6.854  1.00 44.93           C  
ANISOU 2620  CG  ASN A 316     6921   5704   4447  -1232     -7    183       C  
ATOM   2621  OD1 ASN A 316       2.675 -37.255  -6.879  1.00 42.90           O  
ANISOU 2621  OD1 ASN A 316     6753   5350   4196  -1156    -69    209       O  
ATOM   2622  ND2 ASN A 316       0.541 -37.616  -7.482  1.00 45.45           N  
ANISOU 2622  ND2 ASN A 316     6979   5792   4498  -1323      3    179       N  
ATOM   2623  N   HIS A 317       4.127 -34.451  -4.508  1.00 40.33           N  
ANISOU 2623  N   HIS A 317     6342   5091   3889  -1005    -36    185       N  
ATOM   2624  CA  HIS A 317       5.372 -33.758  -4.841  1.00 37.21           C  
ANISOU 2624  CA  HIS A 317     5919   4660   3557   -875    -85    188       C  
ATOM   2625  C   HIS A 317       6.109 -34.387  -6.038  1.00 38.17           C  
ANISOU 2625  C   HIS A 317     6058   4714   3729   -803   -144    207       C  
ATOM   2626  O   HIS A 317       6.726 -33.678  -6.844  1.00 36.38           O  
ANISOU 2626  O   HIS A 317     5755   4494   3575   -702   -159    195       O  
ATOM   2627  CB  HIS A 317       6.275 -33.691  -3.610  1.00 35.22           C  
ANISOU 2627  CB  HIS A 317     5756   4364   3262   -867   -123    211       C  
ATOM   2628  CG  HIS A 317       7.631 -33.115  -3.877  1.00 34.11           C  
ANISOU 2628  CG  HIS A 317     5592   4186   3182   -748   -182    220       C  
ATOM   2629  ND1 HIS A 317       8.760 -33.899  -3.984  1.00 32.10           N  
ANISOU 2629  ND1 HIS A 317     5418   3844   2934   -696   -262    259       N  
ATOM   2630  CD2 HIS A 317       8.041 -31.836  -4.062  1.00 32.51           C  
ANISOU 2630  CD2 HIS A 317     5294   4022   3038   -672   -173    195       C  
ATOM   2631  CE1 HIS A 317       9.807 -33.127  -4.214  1.00 34.51           C  
ANISOU 2631  CE1 HIS A 317     5666   4146   3300   -598   -297    258       C  
ATOM   2632  NE2 HIS A 317       9.398 -31.872  -4.267  1.00 31.19           N  
ANISOU 2632  NE2 HIS A 317     5143   3798   2909   -587   -245    221       N  
ATOM   2633  N   GLN A 318       6.038 -35.712  -6.143  1.00 38.52           N  
ANISOU 2633  N   GLN A 318     6212   4692   3731   -857   -174    234       N  
ATOM   2634  CA  GLN A 318       6.630 -36.448  -7.257  1.00 39.84           C  
ANISOU 2634  CA  GLN A 318     6413   4789   3934   -795   -224    248       C  
ATOM   2635  C   GLN A 318       6.217 -35.857  -8.606  1.00 39.80           C  
ANISOU 2635  C   GLN A 318     6287   4839   3996   -751   -196    216       C  
ATOM   2636  O   GLN A 318       7.065 -35.494  -9.415  1.00 43.05           O  
ANISOU 2636  O   GLN A 318     6658   5231   4467   -645   -221    212       O  
ATOM   2637  CB  GLN A 318       6.237 -37.930  -7.182  1.00 39.98           C  
ANISOU 2637  CB  GLN A 318     6568   4736   3885   -886   -246    274       C  
ATOM   2638  CG  GLN A 318       6.676 -38.775  -8.390  1.00 41.15           C  
ANISOU 2638  CG  GLN A 318     6765   4809   4062   -832   -289    280       C  
ATOM   2639  CD  GLN A 318       8.184 -38.841  -8.566  1.00 39.70           C  
ANISOU 2639  CD  GLN A 318     6613   4552   3920   -698   -349    298       C  
ATOM   2640  OE1 GLN A 318       8.933 -38.928  -7.595  1.00 39.19           O  
ANISOU 2640  OE1 GLN A 318     6609   4448   3834   -675   -388    325       O  
ATOM   2641  NE2 GLN A 318       8.635 -38.808  -9.815  1.00 38.69           N  
ANISOU 2641  NE2 GLN A 318     6441   4410   3850   -609   -359    283       N  
ATOM   2642  N   ARG A 319       4.911 -35.757  -8.822  1.00 41.13           N  
ANISOU 2642  N   ARG A 319     6397   5080   4151   -834   -145    193       N  
ATOM   2643  CA  ARG A 319       4.331 -35.234 -10.053  1.00 39.83           C  
ANISOU 2643  CA  ARG A 319     6121   4972   4040   -806   -124    164       C  
ATOM   2644  C   ARG A 319       4.565 -33.728 -10.213  1.00 37.38           C  
ANISOU 2644  C   ARG A 319     5686   4724   3792   -717   -101    139       C  
ATOM   2645  O   ARG A 319       4.756 -33.237 -11.330  1.00 32.65           O  
ANISOU 2645  O   ARG A 319     5020   4136   3249   -645   -109    127       O  
ATOM   2646  CB  ARG A 319       2.834 -35.548 -10.086  1.00 40.85           C  
ANISOU 2646  CB  ARG A 319     6216   5169   4135   -927    -80    148       C  
ATOM   2647  CG  ARG A 319       2.170 -35.282 -11.422  1.00 45.02           C  
ANISOU 2647  CG  ARG A 319     6649   5747   4708   -913    -75    125       C  
ATOM   2648  CD  ARG A 319       0.992 -36.209 -11.648  1.00 52.45           C  
ANISOU 2648  CD  ARG A 319     7610   6712   5605  -1043    -65    124       C  
ATOM   2649  NE  ARG A 319       1.400 -37.509 -12.179  1.00 55.04           N  
ANISOU 2649  NE  ARG A 319     8073   6938   5901  -1068   -115    147       N  
ATOM   2650  CZ  ARG A 319       0.630 -38.595 -12.160  1.00 60.14           C  
ANISOU 2650  CZ  ARG A 319     8792   7568   6491  -1196   -119    157       C  
ATOM   2651  NH1 ARG A 319      -0.584 -38.543 -11.623  1.00 60.20           N  
ANISOU 2651  NH1 ARG A 319     8739   7666   6468  -1315    -72    147       N  
ATOM   2652  NH2 ARG A 319       1.074 -39.741 -12.663  1.00 59.75           N  
ANISOU 2652  NH2 ARG A 319     8877   7411   6412  -1208   -168    176       N  
ATOM   2653  N   TYR A 320       4.537 -33.015  -9.090  1.00 35.78           N  
ANISOU 2653  N   TYR A 320     5463   4557   3573   -727    -73    132       N  
ATOM   2654  CA  TYR A 320       4.795 -31.574  -9.037  1.00 34.57           C  
ANISOU 2654  CA  TYR A 320     5215   4451   3470   -649    -53    108       C  
ATOM   2655  C   TYR A 320       6.115 -31.226  -9.697  1.00 33.91           C  
ANISOU 2655  C   TYR A 320     5128   4316   3442   -540   -100    121       C  
ATOM   2656  O   TYR A 320       6.167 -30.350 -10.569  1.00 33.41           O  
ANISOU 2656  O   TYR A 320     4978   4281   3434   -474    -93    104       O  
ATOM   2657  CB  TYR A 320       4.834 -31.133  -7.581  1.00 34.22           C  
ANISOU 2657  CB  TYR A 320     5197   4423   3383   -681    -29    105       C  
ATOM   2658  CG  TYR A 320       4.796 -29.645  -7.324  1.00 36.60           C  
ANISOU 2658  CG  TYR A 320     5409   4778   3719   -625      4     72       C  
ATOM   2659  CD1 TYR A 320       3.623 -28.915  -7.502  1.00 34.94           C  
ANISOU 2659  CD1 TYR A 320     5098   4652   3525   -638     63     34       C  
ATOM   2660  CD2 TYR A 320       5.917 -28.979  -6.832  1.00 36.66           C  
ANISOU 2660  CD2 TYR A 320     5438   4751   3741   -564    -27     80       C  
ATOM   2661  CE1 TYR A 320       3.575 -27.560  -7.226  1.00 39.08           C  
ANISOU 2661  CE1 TYR A 320     5556   5215   4078   -582     93      3       C  
ATOM   2662  CE2 TYR A 320       5.878 -27.615  -6.546  1.00 38.14           C  
ANISOU 2662  CE2 TYR A 320     5560   4977   3953   -520      2     49       C  
ATOM   2663  CZ  TYR A 320       4.705 -26.915  -6.743  1.00 39.16           C  
ANISOU 2663  CZ  TYR A 320     5601   5180   4096   -526     63     10       C  
ATOM   2664  OH  TYR A 320       4.655 -25.567  -6.461  1.00 40.65           O  
ANISOU 2664  OH  TYR A 320     5738   5398   4308   -476     90    -23       O  
ATOM   2665  N   ILE A 321       7.177 -31.918  -9.278  1.00 34.48           N  
ANISOU 2665  N   ILE A 321     5292   4312   3495   -521   -148    152       N  
ATOM   2666  CA  ILE A 321       8.505 -31.729  -9.865  1.00 32.89           C  
ANISOU 2666  CA  ILE A 321     5086   4066   3344   -420   -192    166       C  
ATOM   2667  C   ILE A 321       8.547 -32.206 -11.329  1.00 34.43           C  
ANISOU 2667  C   ILE A 321     5268   4240   3572   -382   -202    164       C  
ATOM   2668  O   ILE A 321       9.107 -31.524 -12.194  1.00 33.32           O  
ANISOU 2668  O   ILE A 321     5064   4109   3486   -305   -204    157       O  
ATOM   2669  CB  ILE A 321       9.614 -32.402  -9.018  1.00 32.40           C  
ANISOU 2669  CB  ILE A 321     5120   3934   3256   -403   -247    200       C  
ATOM   2670  CG1 ILE A 321       9.692 -31.783  -7.611  1.00 30.62           C  
ANISOU 2670  CG1 ILE A 321     4909   3729   2997   -435   -244    200       C  
ATOM   2671  CG2 ILE A 321      10.972 -32.321  -9.717  1.00 29.98           C  
ANISOU 2671  CG2 ILE A 321     4795   3589   3007   -298   -290    213       C  
ATOM   2672  CD1 ILE A 321       9.874 -30.262  -7.576  1.00 34.77           C  
ANISOU 2672  CD1 ILE A 321     5337   4308   3566   -391   -221    175       C  
ATOM   2673  N   SER A 322       7.937 -33.355 -11.616  1.00 34.20           N  
ANISOU 2673  N   SER A 322     5306   4183   3505   -442   -206    170       N  
ATOM   2674  CA  SER A 322       7.966 -33.886 -12.982  1.00 35.20           C  
ANISOU 2674  CA  SER A 322     5439   4283   3652   -412   -217    166       C  
ATOM   2675  C   SER A 322       7.292 -32.955 -13.980  1.00 35.38           C  
ANISOU 2675  C   SER A 322     5353   4376   3715   -396   -185    139       C  
ATOM   2676  O   SER A 322       7.776 -32.774 -15.095  1.00 36.55           O  
ANISOU 2676  O   SER A 322     5476   4512   3899   -330   -194    135       O  
ATOM   2677  CB  SER A 322       7.315 -35.260 -13.054  1.00 35.35           C  
ANISOU 2677  CB  SER A 322     5559   4258   3616   -495   -228    175       C  
ATOM   2678  OG  SER A 322       8.138 -36.237 -12.458  1.00 39.29           O  
ANISOU 2678  OG  SER A 322     6175   4669   4084   -484   -270    203       O  
ATOM   2679  N   TYR A 323       6.172 -32.373 -13.573  1.00 37.95           N  
ANISOU 2679  N   TYR A 323     5614   4773   4030   -455   -149    121       N  
ATOM   2680  CA  TYR A 323       5.416 -31.474 -14.434  1.00 39.32           C  
ANISOU 2680  CA  TYR A 323     5683   5016   4241   -439   -125     97       C  
ATOM   2681  C   TYR A 323       6.129 -30.146 -14.609  1.00 38.55           C  
ANISOU 2681  C   TYR A 323     5516   4934   4196   -348   -121     90       C  
ATOM   2682  O   TYR A 323       5.908 -29.457 -15.596  1.00 40.88           O  
ANISOU 2682  O   TYR A 323     5747   5259   4526   -308   -117     78       O  
ATOM   2683  CB  TYR A 323       3.994 -31.281 -13.893  1.00 41.12           C  
ANISOU 2683  CB  TYR A 323     5857   5321   4445   -523    -87     77       C  
ATOM   2684  CG  TYR A 323       3.064 -32.448 -14.193  1.00 44.75           C  
ANISOU 2684  CG  TYR A 323     6358   5783   4863   -621    -91     79       C  
ATOM   2685  CD1 TYR A 323       1.692 -32.356 -13.931  1.00 46.61           C  
ANISOU 2685  CD1 TYR A 323     6526   6101   5082   -703    -56     61       C  
ATOM   2686  CD2 TYR A 323       3.550 -33.641 -14.756  1.00 46.18           C  
ANISOU 2686  CD2 TYR A 323     6643   5884   5021   -632   -129     98       C  
ATOM   2687  CE1 TYR A 323       0.831 -33.421 -14.210  1.00 48.44           C  
ANISOU 2687  CE1 TYR A 323     6792   6340   5275   -807    -62     64       C  
ATOM   2688  CE2 TYR A 323       2.695 -34.712 -15.041  1.00 47.51           C  
ANISOU 2688  CE2 TYR A 323     6860   6047   5146   -731   -136    100       C  
ATOM   2689  CZ  TYR A 323       1.338 -34.590 -14.767  1.00 50.80           C  
ANISOU 2689  CZ  TYR A 323     7206   6550   5546   -825   -104     84       C  
ATOM   2690  OH  TYR A 323       0.485 -35.641 -15.039  1.00 58.19           O  
ANISOU 2690  OH  TYR A 323     8186   7485   6437   -937   -113     87       O  
ATOM   2691  N   ASN A 324       6.982 -29.792 -13.651  1.00 36.93           N  
ANISOU 2691  N   ASN A 324     5331   4708   3992   -321   -127    100       N  
ATOM   2692  CA  ASN A 324       7.818 -28.604 -13.774  1.00 35.89           C  
ANISOU 2692  CA  ASN A 324     5148   4582   3907   -244   -129     97       C  
ATOM   2693  C   ASN A 324       8.912 -28.829 -14.813  1.00 33.94           C  
ANISOU 2693  C   ASN A 324     4913   4290   3691   -176   -156    112       C  
ATOM   2694  O   ASN A 324       9.152 -27.975 -15.665  1.00 31.70           O  
ANISOU 2694  O   ASN A 324     4574   4023   3447   -125   -150    106       O  
ATOM   2695  CB  ASN A 324       8.419 -28.207 -12.420  1.00 34.89           C  
ANISOU 2695  CB  ASN A 324     5043   4445   3767   -246   -134    103       C  
ATOM   2696  CG  ASN A 324       9.313 -26.972 -12.510  1.00 40.05           C  
ANISOU 2696  CG  ASN A 324     5649   5102   4467   -179   -141    101       C  
ATOM   2697  OD1 ASN A 324      10.489 -27.023 -12.154  1.00 43.52           O  
ANISOU 2697  OD1 ASN A 324     6116   5507   4915   -148   -172    121       O  
ATOM   2698  ND2 ASN A 324       8.755 -25.858 -12.976  1.00 40.77           N  
ANISOU 2698  ND2 ASN A 324     5669   5235   4586   -157   -115     79       N  
ATOM   2699  N   ILE A 325       9.564 -29.987 -14.737  1.00 32.49           N  
ANISOU 2699  N   ILE A 325     4808   4049   3488   -174   -183    132       N  
ATOM   2700  CA  ILE A 325      10.552 -30.386 -15.725  1.00 32.07           C  
ANISOU 2700  CA  ILE A 325     4772   3954   3459   -108   -201    142       C  
ATOM   2701  C   ILE A 325       9.917 -30.461 -17.129  1.00 34.64           C  
ANISOU 2701  C   ILE A 325     5078   4293   3789   -107   -187    127       C  
ATOM   2702  O   ILE A 325      10.440 -29.876 -18.089  1.00 34.88           O  
ANISOU 2702  O   ILE A 325     5068   4331   3852    -50   -180    125       O  
ATOM   2703  CB  ILE A 325      11.211 -31.746 -15.350  1.00 33.06           C  
ANISOU 2703  CB  ILE A 325     4995   4008   3557   -104   -235    162       C  
ATOM   2704  CG1 ILE A 325      11.973 -31.633 -14.016  1.00 30.69           C  
ANISOU 2704  CG1 ILE A 325     4715   3693   3252    -97   -261    180       C  
ATOM   2705  CG2 ILE A 325      12.136 -32.224 -16.478  1.00 28.65           C  
ANISOU 2705  CG2 ILE A 325     4453   3410   3023    -28   -244    164       C  
ATOM   2706  CD1 ILE A 325      12.314 -32.987 -13.350  1.00 27.44           C  
ANISOU 2706  CD1 ILE A 325     4414   3212   2800   -111   -301    203       C  
ATOM   2707  N   ILE A 326       8.789 -31.168 -17.235  1.00 33.88           N  
ANISOU 2707  N   ILE A 326     5013   4203   3656   -177   -184    119       N  
ATOM   2708  CA  ILE A 326       8.115 -31.369 -18.519  1.00 33.23           C  
ANISOU 2708  CA  ILE A 326     4923   4133   3569   -188   -181    107       C  
ATOM   2709  C   ILE A 326       7.698 -30.047 -19.158  1.00 32.53           C  
ANISOU 2709  C   ILE A 326     4740   4106   3516   -161   -164     94       C  
ATOM   2710  O   ILE A 326       7.810 -29.885 -20.374  1.00 36.05           O  
ANISOU 2710  O   ILE A 326     5176   4549   3972   -127   -166     90       O  
ATOM   2711  CB  ILE A 326       6.898 -32.323 -18.405  1.00 32.92           C  
ANISOU 2711  CB  ILE A 326     4927   4098   3482   -284   -185    101       C  
ATOM   2712  CG1 ILE A 326       7.378 -33.755 -18.142  1.00 29.89           C  
ANISOU 2712  CG1 ILE A 326     4664   3633   3060   -304   -208    115       C  
ATOM   2713  CG2 ILE A 326       6.066 -32.282 -19.693  1.00 34.57           C  
ANISOU 2713  CG2 ILE A 326     5108   4337   3690   -302   -187     86       C  
ATOM   2714  CD1 ILE A 326       6.299 -34.706 -17.688  1.00 31.36           C  
ANISOU 2714  CD1 ILE A 326     4907   3816   3193   -415   -213    116       C  
ATOM   2715  N   ALA A 327       7.246 -29.105 -18.339  1.00 31.16           N  
ANISOU 2715  N   ALA A 327     4503   3979   3356   -172   -148     87       N  
ATOM   2716  CA  ALA A 327       6.856 -27.783 -18.827  1.00 32.81           C  
ANISOU 2716  CA  ALA A 327     4630   4238   3599   -139   -136     75       C  
ATOM   2717  C   ALA A 327       7.999 -27.064 -19.537  1.00 33.10           C  
ANISOU 2717  C   ALA A 327     4655   4252   3670    -64   -139     85       C  
ATOM   2718  O   ALA A 327       7.789 -26.458 -20.590  1.00 36.16           O  
ANISOU 2718  O   ALA A 327     5011   4655   4072    -37   -140     82       O  
ATOM   2719  CB  ALA A 327       6.299 -26.926 -17.697  1.00 32.71           C  
ANISOU 2719  CB  ALA A 327     4566   4269   3593   -155   -115     62       C  
ATOM   2720  N   VAL A 328       9.202 -27.137 -18.972  1.00 32.18           N  
ANISOU 2720  N   VAL A 328     4563   4100   3563    -34   -143     98       N  
ATOM   2721  CA  VAL A 328      10.395 -26.554 -19.613  1.00 32.94           C  
ANISOU 2721  CA  VAL A 328     4646   4180   3692     29   -142    109       C  
ATOM   2722  C   VAL A 328      10.672 -27.189 -20.984  1.00 32.36           C  
ANISOU 2722  C   VAL A 328     4602   4083   3609     53   -142    111       C  
ATOM   2723  O   VAL A 328      10.890 -26.484 -21.980  1.00 32.07           O  
ANISOU 2723  O   VAL A 328     4539   4057   3587     84   -132    112       O  
ATOM   2724  CB  VAL A 328      11.660 -26.654 -18.703  1.00 33.34           C  
ANISOU 2724  CB  VAL A 328     4710   4204   3755     53   -152    124       C  
ATOM   2725  CG1 VAL A 328      12.916 -26.281 -19.476  1.00 31.31           C  
ANISOU 2725  CG1 VAL A 328     4433   3935   3529    111   -148    135       C  
ATOM   2726  CG2 VAL A 328      11.511 -25.757 -17.468  1.00 34.69           C  
ANISOU 2726  CG2 VAL A 328     4852   4396   3931     34   -152    120       C  
ATOM   2727  N   TYR A 329      10.651 -28.518 -21.022  1.00 30.37           N  
ANISOU 2727  N   TYR A 329     4416   3796   3328     35   -152    111       N  
ATOM   2728  CA  TYR A 329      10.955 -29.282 -22.234  1.00 30.49           C  
ANISOU 2728  CA  TYR A 329     4478   3779   3326     59   -150    108       C  
ATOM   2729  C   TYR A 329       9.959 -29.016 -23.349  1.00 30.50           C  
ANISOU 2729  C   TYR A 329     4469   3807   3311     35   -149     97       C  
ATOM   2730  O   TYR A 329      10.314 -29.028 -24.521  1.00 33.90           O  
ANISOU 2730  O   TYR A 329     4918   4227   3736     66   -141     95       O  
ATOM   2731  CB  TYR A 329      10.992 -30.778 -21.906  1.00 30.24           C  
ANISOU 2731  CB  TYR A 329     4534   3695   3261     38   -166    108       C  
ATOM   2732  CG  TYR A 329      11.308 -31.699 -23.071  1.00 30.78           C  
ANISOU 2732  CG  TYR A 329     4670   3719   3306     64   -163    100       C  
ATOM   2733  CD1 TYR A 329      12.342 -31.414 -23.958  1.00 29.66           C  
ANISOU 2733  CD1 TYR A 329     4516   3570   3183    135   -141     98       C  
ATOM   2734  CD2 TYR A 329      10.592 -32.880 -23.255  1.00 33.93           C  
ANISOU 2734  CD2 TYR A 329     5153   4081   3659     13   -180     91       C  
ATOM   2735  CE1 TYR A 329      12.642 -32.269 -25.016  1.00 32.03           C  
ANISOU 2735  CE1 TYR A 329     4885   3829   3456    162   -131     85       C  
ATOM   2736  CE2 TYR A 329      10.888 -33.747 -24.304  1.00 38.97           C  
ANISOU 2736  CE2 TYR A 329     5868   4669   4269     38   -177     79       C  
ATOM   2737  CZ  TYR A 329      11.915 -33.432 -25.178  1.00 37.75           C  
ANISOU 2737  CZ  TYR A 329     5700   4510   4133    117   -151     74       C  
ATOM   2738  OH  TYR A 329      12.211 -34.284 -26.217  1.00 42.43           O  
ANISOU 2738  OH  TYR A 329     6374   5055   4694    145   -141     57       O  
ATOM   2739  N   ARG A 330       8.705 -28.782 -22.982  1.00 32.03           N  
ANISOU 2739  N   ARG A 330     4633   4040   3497    -19   -159     90       N  
ATOM   2740  CA  ARG A 330       7.678 -28.493 -23.964  1.00 31.88           C  
ANISOU 2740  CA  ARG A 330     4592   4054   3466    -41   -169     81       C  
ATOM   2741  C   ARG A 330       7.951 -27.203 -24.739  1.00 30.97           C  
ANISOU 2741  C   ARG A 330     4429   3961   3377      9   -163     86       C  
ATOM   2742  O   ARG A 330       7.738 -27.150 -25.952  1.00 33.06           O  
ANISOU 2742  O   ARG A 330     4709   4227   3625     15   -172     86       O  
ATOM   2743  CB  ARG A 330       6.295 -28.530 -23.320  1.00 34.05           C  
ANISOU 2743  CB  ARG A 330     4829   4375   3731   -107   -179     71       C  
ATOM   2744  CG  ARG A 330       5.868 -29.953 -23.046  1.00 39.11           C  
ANISOU 2744  CG  ARG A 330     5538   4991   4331   -175   -191     68       C  
ATOM   2745  CD  ARG A 330       4.439 -30.071 -22.598  1.00 47.65           C  
ANISOU 2745  CD  ARG A 330     6578   6128   5399   -254   -197     57       C  
ATOM   2746  NE  ARG A 330       4.061 -31.484 -22.527  1.00 54.14           N  
ANISOU 2746  NE  ARG A 330     7479   6918   6174   -330   -211     57       N  
ATOM   2747  CZ  ARG A 330       2.845 -31.936 -22.230  1.00 55.89           C  
ANISOU 2747  CZ  ARG A 330     7682   7181   6372   -420   -218     49       C  
ATOM   2748  NH1 ARG A 330       1.846 -31.090 -21.963  1.00 55.10           N  
ANISOU 2748  NH1 ARG A 330     7476   7165   6295   -438   -209     39       N  
ATOM   2749  NH2 ARG A 330       2.630 -33.244 -22.201  1.00 53.05           N  
ANISOU 2749  NH2 ARG A 330     7412   6779   5966   -494   -233     51       N  
ATOM   2750  N   VAL A 331       8.450 -26.177 -24.059  1.00 28.35           N  
ANISOU 2750  N   VAL A 331     4051   3641   3081     40   -150     93       N  
ATOM   2751  CA  VAL A 331       8.896 -24.961 -24.755  1.00 28.33           C  
ANISOU 2751  CA  VAL A 331     4018   3646   3101     84   -143    102       C  
ATOM   2752  C   VAL A 331      10.064 -25.262 -25.708  1.00 29.73           C  
ANISOU 2752  C   VAL A 331     4236   3790   3270    119   -127    111       C  
ATOM   2753  O   VAL A 331      10.112 -24.746 -26.821  1.00 29.87           O  
ANISOU 2753  O   VAL A 331     4259   3811   3279    135   -124    117       O  
ATOM   2754  CB  VAL A 331       9.307 -23.856 -23.785  1.00 27.88           C  
ANISOU 2754  CB  VAL A 331     3916   3598   3079    103   -134    106       C  
ATOM   2755  CG1 VAL A 331       9.477 -22.555 -24.534  1.00 28.03           C  
ANISOU 2755  CG1 VAL A 331     3912   3623   3116    136   -133    116       C  
ATOM   2756  CG2 VAL A 331       8.270 -23.705 -22.685  1.00 27.86           C  
ANISOU 2756  CG2 VAL A 331     3880   3626   3080     72   -139     91       C  
ATOM   2757  N   LEU A 332      10.984 -26.122 -25.275  1.00 30.71           N  
ANISOU 2757  N   LEU A 332     4391   3884   3394    131   -115    112       N  
ATOM   2758  CA  LEU A 332      12.085 -26.564 -26.119  1.00 30.86           C  
ANISOU 2758  CA  LEU A 332     4443   3876   3405    170    -92    115       C  
ATOM   2759  C   LEU A 332      11.565 -27.290 -27.363  1.00 31.89           C  
ANISOU 2759  C   LEU A 332     4633   3993   3491    159    -95    104       C  
ATOM   2760  O   LEU A 332      12.077 -27.085 -28.461  1.00 32.90           O  
ANISOU 2760  O   LEU A 332     4778   4116   3605    184    -73    106       O  
ATOM   2761  CB  LEU A 332      13.031 -27.474 -25.339  1.00 29.52           C  
ANISOU 2761  CB  LEU A 332     4295   3676   3246    193    -87    116       C  
ATOM   2762  CG  LEU A 332      13.944 -26.877 -24.267  1.00 32.47           C  
ANISOU 2762  CG  LEU A 332     4619   4059   3661    213    -86    129       C  
ATOM   2763  CD1 LEU A 332      14.801 -27.995 -23.701  1.00 34.26           C  
ANISOU 2763  CD1 LEU A 332     4878   4251   3890    241    -92    131       C  
ATOM   2764  CD2 LEU A 332      14.829 -25.752 -24.817  1.00 30.67           C  
ANISOU 2764  CD2 LEU A 332     4341   3853   3460    241    -61    141       C  
ATOM   2765  N   GLN A 333      10.533 -28.112 -27.173  1.00 31.51           N  
ANISOU 2765  N   GLN A 333     4617   3939   3415    112   -121     93       N  
ATOM   2766  CA  GLN A 333       9.912 -28.864 -28.247  1.00 32.03           C  
ANISOU 2766  CA  GLN A 333     4746   3991   3434     87   -134     81       C  
ATOM   2767  C   GLN A 333       9.143 -27.973 -29.215  1.00 32.44           C  
ANISOU 2767  C   GLN A 333     4773   4078   3474     75   -150     84       C  
ATOM   2768  O   GLN A 333       9.196 -28.183 -30.428  1.00 32.41           O  
ANISOU 2768  O   GLN A 333     4820   4061   3433     79   -149     80       O  
ATOM   2769  CB  GLN A 333       8.987 -29.922 -27.672  1.00 32.13           C  
ANISOU 2769  CB  GLN A 333     4795   3992   3422     26   -162     71       C  
ATOM   2770  CG  GLN A 333       9.708 -31.145 -27.157  1.00 33.63           C  
ANISOU 2770  CG  GLN A 333     5054   4123   3600     38   -154     66       C  
ATOM   2771  CD  GLN A 333       8.762 -32.123 -26.501  1.00 35.41           C  
ANISOU 2771  CD  GLN A 333     5323   4335   3798    -36   -182     61       C  
ATOM   2772  OE1 GLN A 333       8.648 -33.271 -26.925  1.00 39.90           O  
ANISOU 2772  OE1 GLN A 333     5982   4854   4324    -59   -193     50       O  
ATOM   2773  NE2 GLN A 333       8.064 -31.668 -25.468  1.00 36.28           N  
ANISOU 2773  NE2 GLN A 333     5372   4486   3926    -77   -191     67       N  
ATOM   2774  N   ILE A 334       8.420 -26.989 -28.681  1.00 32.71           N  
ANISOU 2774  N   ILE A 334     4736   4154   3537     63   -168     91       N  
ATOM   2775  CA  ILE A 334       7.792 -25.985 -29.527  1.00 31.75           C  
ANISOU 2775  CA  ILE A 334     4588   4063   3413     67   -189     99       C  
ATOM   2776  C   ILE A 334       8.876 -25.273 -30.339  1.00 33.19           C  
ANISOU 2776  C   ILE A 334     4786   4229   3596    113   -160    113       C  
ATOM   2777  O   ILE A 334       8.742 -25.137 -31.557  1.00 34.69           O  
ANISOU 2777  O   ILE A 334     5015   4417   3751    113   -168    117       O  
ATOM   2778  CB  ILE A 334       6.918 -24.984 -28.722  1.00 30.22           C  
ANISOU 2778  CB  ILE A 334     4312   3913   3257     62   -208    101       C  
ATOM   2779  CG1 ILE A 334       5.710 -25.698 -28.093  1.00 29.04           C  
ANISOU 2779  CG1 ILE A 334     4141   3793   3100      7   -231     86       C  
ATOM   2780  CG2 ILE A 334       6.443 -23.832 -29.610  1.00 27.25           C  
ANISOU 2780  CG2 ILE A 334     3915   3558   2883     85   -233    113       C  
ATOM   2781  CD1 ILE A 334       5.108 -24.931 -26.891  1.00 26.92           C  
ANISOU 2781  CD1 ILE A 334     3792   3565   2870      7   -228     81       C  
ATOM   2782  N   ASP A 335       9.959 -24.850 -29.681  1.00 34.01           N  
ANISOU 2782  N   ASP A 335     4864   4324   3734    144   -126    121       N  
ATOM   2783  CA  ASP A 335      11.029 -24.164 -30.409  1.00 34.32           C  
ANISOU 2783  CA  ASP A 335     4910   4354   3774    177    -93    135       C  
ATOM   2784  C   ASP A 335      11.705 -25.033 -31.469  1.00 33.86           C  
ANISOU 2784  C   ASP A 335     4919   4272   3674    189    -63    127       C  
ATOM   2785  O   ASP A 335      11.962 -24.552 -32.569  1.00 34.47           O  
ANISOU 2785  O   ASP A 335     5023   4350   3724    196    -48    136       O  
ATOM   2786  CB  ASP A 335      12.092 -23.548 -29.507  1.00 32.17           C  
ANISOU 2786  CB  ASP A 335     4592   4084   3549    199    -67    146       C  
ATOM   2787  CG  ASP A 335      12.930 -22.517 -30.254  1.00 37.56           C  
ANISOU 2787  CG  ASP A 335     5269   4768   4233    215    -39    165       C  
ATOM   2788  OD1 ASP A 335      12.333 -21.553 -30.800  1.00 34.73           O  
ANISOU 2788  OD1 ASP A 335     4915   4417   3866    208    -59    177       O  
ATOM   2789  OD2 ASP A 335      14.168 -22.681 -30.329  1.00 36.62           O  
ANISOU 2789  OD2 ASP A 335     5144   4645   4123    234      2    168       O  
ATOM   2790  N   ALA A 336      11.994 -26.291 -31.138  1.00 30.43           N  
ANISOU 2790  N   ALA A 336     4517   3813   3231    193    -53    110       N  
ATOM   2791  CA  ALA A 336      12.525 -27.240 -32.126  1.00 31.68           C  
ANISOU 2791  CA  ALA A 336     4749   3942   3345    211    -25     95       C  
ATOM   2792  C   ALA A 336      11.691 -27.246 -33.405  1.00 32.02           C  
ANISOU 2792  C   ALA A 336     4850   3985   3330    182    -46     91       C  
ATOM   2793  O   ALA A 336      12.220 -27.410 -34.504  1.00 31.90           O  
ANISOU 2793  O   ALA A 336     4891   3958   3274    198    -14     85       O  
ATOM   2794  CB  ALA A 336      12.603 -28.638 -31.541  1.00 31.52           C  
ANISOU 2794  CB  ALA A 336     4772   3885   3318    213    -29     76       C  
ATOM   2795  N   LYS A 337      10.383 -27.058 -33.247  1.00 33.74           N  
ANISOU 2795  N   LYS A 337     5054   4223   3544    138   -101     93       N  
ATOM   2796  CA  LYS A 337       9.445 -27.022 -34.367  1.00 31.22           C  
ANISOU 2796  CA  LYS A 337     4778   3910   3172    106   -139     92       C  
ATOM   2797  C   LYS A 337       9.379 -25.631 -35.035  1.00 31.63           C  
ANISOU 2797  C   LYS A 337     4807   3987   3225    117   -148    117       C  
ATOM   2798  O   LYS A 337       9.566 -25.510 -36.257  1.00 31.23           O  
ANISOU 2798  O   LYS A 337     4817   3927   3123    118   -140    121       O  
ATOM   2799  CB  LYS A 337       8.063 -27.459 -33.879  1.00 31.21           C  
ANISOU 2799  CB  LYS A 337     4759   3928   3171     53   -198     85       C  
ATOM   2800  CG  LYS A 337       7.001 -27.449 -34.948  1.00 36.11           C  
ANISOU 2800  CG  LYS A 337     5414   4564   3743     14   -251     85       C  
ATOM   2801  CD  LYS A 337       5.614 -27.704 -34.376  1.00 36.81           C  
ANISOU 2801  CD  LYS A 337     5455   4688   3843    -41   -308     80       C  
ATOM   2802  CE  LYS A 337       4.552 -27.512 -35.475  1.00 38.91           C  
ANISOU 2802  CE  LYS A 337     5738   4981   4067    -76   -372     84       C  
ATOM   2803  NZ  LYS A 337       3.160 -27.392 -34.941  1.00 37.83           N  
ANISOU 2803  NZ  LYS A 337     5518   4900   3955   -119   -429     83       N  
ATOM   2804  N   ARG A 338       9.117 -24.587 -34.242  1.00 29.40           N  
ANISOU 2804  N   ARG A 338     4447   3730   2995    126   -163    133       N  
ATOM   2805  CA  ARG A 338       8.870 -23.252 -34.802  1.00 26.89           C  
ANISOU 2805  CA  ARG A 338     4114   3425   2677    137   -184    158       C  
ATOM   2806  C   ARG A 338      10.140 -22.523 -35.165  1.00 29.07           C  
ANISOU 2806  C   ARG A 338     4402   3688   2955    163   -131    176       C  
ATOM   2807  O   ARG A 338      10.167 -21.781 -36.152  1.00 30.57           O  
ANISOU 2807  O   ARG A 338     4629   3874   3112    162   -137    195       O  
ATOM   2808  CB  ARG A 338       8.026 -22.390 -33.862  1.00 26.81           C  
ANISOU 2808  CB  ARG A 338     4024   3442   2718    141   -223    165       C  
ATOM   2809  CG  ARG A 338       6.565 -22.828 -33.772  1.00 26.92           C  
ANISOU 2809  CG  ARG A 338     4015   3486   2727    111   -282    152       C  
ATOM   2810  CD  ARG A 338       5.804 -22.567 -35.071  1.00 25.56           C  
ANISOU 2810  CD  ARG A 338     3882   3322   2508    101   -335    164       C  
ATOM   2811  NE  ARG A 338       4.379 -22.718 -34.842  1.00 26.55           N  
ANISOU 2811  NE  ARG A 338     3954   3489   2643     77   -397    155       N  
ATOM   2812  CZ  ARG A 338       3.423 -22.085 -35.514  1.00 30.07           C  
ANISOU 2812  CZ  ARG A 338     4386   3961   3079     82   -462    168       C  
ATOM   2813  NH1 ARG A 338       3.720 -21.237 -36.493  1.00 31.49           N  
ANISOU 2813  NH1 ARG A 338     4614   4119   3231    109   -477    194       N  
ATOM   2814  NH2 ARG A 338       2.154 -22.306 -35.196  1.00 26.96           N  
ANISOU 2814  NH2 ARG A 338     3927   3616   2702     59   -513    157       N  
ATOM   2815  N   GLN A 339      11.180 -22.725 -34.361  1.00 30.45           N  
ANISOU 2815  N   GLN A 339     4545   3858   3167    181    -82    170       N  
ATOM   2816  CA  GLN A 339      12.502 -22.137 -34.592  1.00 34.82           C  
ANISOU 2816  CA  GLN A 339     5095   4407   3729    198    -26    185       C  
ATOM   2817  C   GLN A 339      12.520 -20.601 -34.431  1.00 36.38           C  
ANISOU 2817  C   GLN A 339     5261   4610   3953    197    -39    213       C  
ATOM   2818  O   GLN A 339      13.217 -19.890 -35.164  1.00 37.12           O  
ANISOU 2818  O   GLN A 339     5378   4699   4027    193     -8    234       O  
ATOM   2819  CB  GLN A 339      13.094 -22.618 -35.937  1.00 34.40           C  
ANISOU 2819  CB  GLN A 339     5115   4344   3613    199     17    181       C  
ATOM   2820  CG  GLN A 339      13.484 -24.105 -35.894  1.00 39.54           C  
ANISOU 2820  CG  GLN A 339     5796   4980   4249    215     46    149       C  
ATOM   2821  CD  GLN A 339      13.763 -24.748 -37.260  1.00 43.01           C  
ANISOU 2821  CD  GLN A 339     6324   5403   4614    216     81    134       C  
ATOM   2822  OE1 GLN A 339      13.545 -25.947 -37.435  1.00 43.88           O  
ANISOU 2822  OE1 GLN A 339     6487   5490   4694    218     78    107       O  
ATOM   2823  NE2 GLN A 339      14.257 -23.966 -38.213  1.00 42.26           N  
ANISOU 2823  NE2 GLN A 339     6254   5317   4485    211    115    152       N  
ATOM   2824  N   PHE A 340      11.763 -20.109 -33.448  1.00 35.93           N  
ANISOU 2824  N   PHE A 340     5037   4500   4113    -36   -172    285       N  
ATOM   2825  CA  PHE A 340      11.681 -18.668 -33.182  1.00 35.56           C  
ANISOU 2825  CA  PHE A 340     4934   4478   4101    -28   -167    285       C  
ATOM   2826  C   PHE A 340      12.966 -18.090 -32.595  1.00 34.16           C  
ANISOU 2826  C   PHE A 340     4734   4317   3929     10   -136    264       C  
ATOM   2827  O   PHE A 340      13.306 -16.938 -32.864  1.00 34.62           O  
ANISOU 2827  O   PHE A 340     4767   4385   4001     18   -129    258       O  
ATOM   2828  CB  PHE A 340      10.470 -18.313 -32.298  1.00 33.60           C  
ANISOU 2828  CB  PHE A 340     4636   4244   3887    -41   -175    301       C  
ATOM   2829  CG  PHE A 340       9.134 -18.607 -32.936  1.00 32.77           C  
ANISOU 2829  CG  PHE A 340     4533   4124   3794    -81   -213    332       C  
ATOM   2830  CD1 PHE A 340       8.951 -18.481 -34.315  1.00 33.69           C  
ANISOU 2830  CD1 PHE A 340     4681   4223   3899   -107   -245    344       C  
ATOM   2831  CD2 PHE A 340       8.048 -18.996 -32.155  1.00 34.19           C  
ANISOU 2831  CD2 PHE A 340     4684   4306   4001    -97   -217    351       C  
ATOM   2832  CE1 PHE A 340       7.713 -18.756 -34.903  1.00 31.29           C  
ANISOU 2832  CE1 PHE A 340     4379   3902   3608   -151   -292    378       C  
ATOM   2833  CE2 PHE A 340       6.802 -19.270 -32.732  1.00 33.89           C  
ANISOU 2833  CE2 PHE A 340     4639   4254   3985   -138   -257    387       C  
ATOM   2834  CZ  PHE A 340       6.640 -19.154 -34.110  1.00 32.63           C  
ANISOU 2834  CZ  PHE A 340     4509   4076   3813   -166   -300    402       C  
ATOM   2835  N   ILE A 341      13.674 -18.878 -31.792  1.00 33.94           N  
ANISOU 2835  N   ILE A 341     4716   4290   3891     30   -122    255       N  
ATOM   2836  CA  ILE A 341      14.952 -18.424 -31.231  1.00 35.42           C  
ANISOU 2836  CA  ILE A 341     4881   4490   4088     61   -103    243       C  
ATOM   2837  C   ILE A 341      15.967 -18.217 -32.363  1.00 35.32           C  
ANISOU 2837  C   ILE A 341     4884   4463   4072     75    -85    236       C  
ATOM   2838  O   ILE A 341      16.620 -17.170 -32.441  1.00 36.77           O  
ANISOU 2838  O   ILE A 341     5038   4660   4273     87    -75    230       O  
ATOM   2839  CB  ILE A 341      15.511 -19.388 -30.148  1.00 36.50           C  
ANISOU 2839  CB  ILE A 341     5024   4625   4219     77   -100    243       C  
ATOM   2840  CG1 ILE A 341      14.473 -19.663 -29.037  1.00 35.80           C  
ANISOU 2840  CG1 ILE A 341     4931   4546   4128     60   -111    249       C  
ATOM   2841  CG2 ILE A 341      16.819 -18.851 -29.571  1.00 36.88           C  
ANISOU 2841  CG2 ILE A 341     5044   4685   4284    103    -92    237       C  
ATOM   2842  CD1 ILE A 341      14.210 -18.515 -28.106  1.00 41.20           C  
ANISOU 2842  CD1 ILE A 341     5578   5249   4825     56   -106    245       C  
ATOM   2843  N   ASN A 342      16.065 -19.209 -33.247  1.00 35.10           N  
ANISOU 2843  N   ASN A 342     4908   4407   4021     72    -78    237       N  
ATOM   2844  CA  ASN A 342      16.906 -19.135 -34.447  1.00 34.20           C  
ANISOU 2844  CA  ASN A 342     4826   4271   3898     82    -50    230       C  
ATOM   2845  C   ASN A 342      16.584 -17.912 -35.306  1.00 31.72           C  
ANISOU 2845  C   ASN A 342     4505   3962   3584     64    -57    230       C  
ATOM   2846  O   ASN A 342      17.482 -17.194 -35.731  1.00 29.58           O  
ANISOU 2846  O   ASN A 342     4221   3692   3325     80    -32    224       O  
ATOM   2847  CB  ASN A 342      16.758 -20.419 -35.272  1.00 37.33           C  
ANISOU 2847  CB  ASN A 342     5297   4627   4259     72    -41    231       C  
ATOM   2848  CG  ASN A 342      17.630 -20.419 -36.519  1.00 41.32           C  
ANISOU 2848  CG  ASN A 342     5849   5101   4750     81      1    222       C  
ATOM   2849  OD1 ASN A 342      18.840 -20.629 -36.438  1.00 45.17           O  
ANISOU 2849  OD1 ASN A 342     6327   5579   5258    118     43    218       O  
ATOM   2850  ND2 ASN A 342      17.015 -20.185 -37.681  1.00 40.01           N  
ANISOU 2850  ND2 ASN A 342     5736   4916   4551     47    -10    223       N  
ATOM   2851  N   LEU A 343      15.293 -17.683 -35.539  1.00 30.69           N  
ANISOU 2851  N   LEU A 343     4380   3835   3448     30    -92    241       N  
ATOM   2852  CA  LEU A 343      14.809 -16.514 -36.273  1.00 28.61           C  
ANISOU 2852  CA  LEU A 343     4105   3576   3190     10   -109    248       C  
ATOM   2853  C   LEU A 343      15.213 -15.205 -35.608  1.00 29.36           C  
ANISOU 2853  C   LEU A 343     4136   3700   3320     29    -99    242       C  
ATOM   2854  O   LEU A 343      15.642 -14.270 -36.283  1.00 32.85           O  
ANISOU 2854  O   LEU A 343     4575   4141   3766     30    -90    239       O  
ATOM   2855  CB  LEU A 343      13.285 -16.569 -36.425  1.00 28.45           C  
ANISOU 2855  CB  LEU A 343     4085   3552   3172    -29   -154    270       C  
ATOM   2856  CG  LEU A 343      12.605 -15.308 -36.989  1.00 28.09           C  
ANISOU 2856  CG  LEU A 343     4014   3512   3148    -49   -180    286       C  
ATOM   2857  CD1 LEU A 343      12.915 -15.100 -38.496  1.00 23.09           C  
ANISOU 2857  CD1 LEU A 343     3440   2852   2479    -69   -185    287       C  
ATOM   2858  CD2 LEU A 343      11.126 -15.414 -36.742  1.00 27.42           C  
ANISOU 2858  CD2 LEU A 343     3904   3428   3087    -78   -221    313       C  
ATOM   2859  N   SER A 344      15.077 -15.151 -34.285  1.00 29.25           N  
ANISOU 2859  N   SER A 344     4080   3707   3327     41   -100    240       N  
ATOM   2860  CA  SER A 344      15.452 -13.978 -33.498  1.00 28.07           C  
ANISOU 2860  CA  SER A 344     3882   3581   3205     56    -91    233       C  
ATOM   2861  C   SER A 344      16.928 -13.654 -33.614  1.00 28.41           C  
ANISOU 2861  C   SER A 344     3918   3626   3252     79    -67    222       C  
ATOM   2862  O   SER A 344      17.295 -12.504 -33.884  1.00 28.39           O  
ANISOU 2862  O   SER A 344     3893   3631   3264     81    -61    219       O  
ATOM   2863  CB  SER A 344      15.078 -14.174 -32.031  1.00 27.92           C  
ANISOU 2863  CB  SER A 344     3839   3576   3195     60    -93    232       C  
ATOM   2864  OG  SER A 344      13.673 -14.144 -31.895  1.00 27.93           O  
ANISOU 2864  OG  SER A 344     3830   3575   3205     39   -107    246       O  
ATOM   2865  N   LEU A 345      17.768 -14.671 -33.429  1.00 27.38           N  
ANISOU 2865  N   LEU A 345     3802   3487   3115     97    -53    220       N  
ATOM   2866  CA  LEU A 345      19.205 -14.515 -33.579  1.00 27.46           C  
ANISOU 2866  CA  LEU A 345     3798   3494   3141    121    -28    217       C  
ATOM   2867  C   LEU A 345      19.581 -14.025 -34.994  1.00 30.20           C  
ANISOU 2867  C   LEU A 345     4167   3826   3483    119     -4    215       C  
ATOM   2868  O   LEU A 345      20.309 -13.036 -35.127  1.00 30.54           O  
ANISOU 2868  O   LEU A 345     4181   3876   3546    125      8    213       O  
ATOM   2869  CB  LEU A 345      19.925 -15.817 -33.211  1.00 28.12           C  
ANISOU 2869  CB  LEU A 345     3894   3565   3227    143    -16    222       C  
ATOM   2870  CG  LEU A 345      19.895 -16.266 -31.738  1.00 31.05           C  
ANISOU 2870  CG  LEU A 345     4244   3950   3605    147    -40    226       C  
ATOM   2871  CD1 LEU A 345      20.384 -17.714 -31.603  1.00 27.90           C  
ANISOU 2871  CD1 LEU A 345     3867   3529   3204    166    -30    234       C  
ATOM   2872  CD2 LEU A 345      20.707 -15.330 -30.826  1.00 27.52           C  
ANISOU 2872  CD2 LEU A 345     3749   3523   3183    153    -52    229       C  
ATOM   2873  N   ASP A 346      19.067 -14.695 -36.033  1.00 30.58           N  
ANISOU 2873  N   ASP A 346     4272   3848   3500    104      1    216       N  
ATOM   2874  CA  ASP A 346      19.253 -14.271 -37.429  1.00 34.55           C  
ANISOU 2874  CA  ASP A 346     4814   4329   3984     93     21    214       C  
ATOM   2875  C   ASP A 346      18.950 -12.789 -37.649  1.00 34.92           C  
ANISOU 2875  C   ASP A 346     4832   4392   4043     78      5    216       C  
ATOM   2876  O   ASP A 346      19.800 -12.065 -38.154  1.00 37.69           O  
ANISOU 2876  O   ASP A 346     5175   4741   4404     86     32    213       O  
ATOM   2877  CB  ASP A 346      18.354 -15.071 -38.380  1.00 37.46           C  
ANISOU 2877  CB  ASP A 346     5257   4667   4307     63      8    218       C  
ATOM   2878  CG  ASP A 346      18.894 -16.449 -38.701  1.00 44.57           C  
ANISOU 2878  CG  ASP A 346     6213   5535   5187     76     43    213       C  
ATOM   2879  OD1 ASP A 346      19.994 -16.808 -38.235  1.00 47.52           O  
ANISOU 2879  OD1 ASP A 346     6560   5907   5587    112     80    209       O  
ATOM   2880  OD2 ASP A 346      18.203 -17.178 -39.443  1.00 48.88           O  
ANISOU 2880  OD2 ASP A 346     6830   6051   5690     48     31    215       O  
ATOM   2881  N   MET A 347      17.731 -12.359 -37.302  1.00 34.58           N  
ANISOU 2881  N   MET A 347     4773   4363   4003     57    -36    223       N  
ATOM   2882  CA  MET A 347      17.290 -10.964 -37.499  1.00 34.93           C  
ANISOU 2882  CA  MET A 347     4790   4419   4064     44    -53    228       C  
ATOM   2883  C   MET A 347      18.111 -10.020 -36.637  1.00 33.72           C  
ANISOU 2883  C   MET A 347     4582   4288   3942     65    -38    219       C  
ATOM   2884  O   MET A 347      18.494  -8.938 -37.083  1.00 33.67           O  
ANISOU 2884  O   MET A 347     4564   4283   3945     63    -31    219       O  
ATOM   2885  CB  MET A 347      15.808 -10.777 -37.135  1.00 36.98           C  
ANISOU 2885  CB  MET A 347     5032   4684   4334     23    -93    243       C  
ATOM   2886  CG  MET A 347      14.781 -11.482 -38.033  1.00 47.51           C  
ANISOU 2886  CG  MET A 347     6413   5995   5642     -9   -125    261       C  
ATOM   2887  SD  MET A 347      13.036 -11.219 -37.512  1.00 55.24           S  
ANISOU 2887  SD  MET A 347     7351   6982   6657    -31   -170    288       S  
ATOM   2888  CE  MET A 347      12.952  -9.428 -37.345  1.00 50.54           C  
ANISOU 2888  CE  MET A 347     6701   6399   6105    -22   -166    291       C  
ATOM   2889  N   GLY A 348      18.357 -10.432 -35.391  1.00 31.20           N  
ANISOU 2889  N   GLY A 348     4235   3984   3636     80    -39    215       N  
ATOM   2890  CA  GLY A 348      19.107  -9.629 -34.440  1.00 28.81           C  
ANISOU 2890  CA  GLY A 348     3890   3700   3358     93    -35    208       C  
ATOM   2891  C   GLY A 348      20.503  -9.327 -34.934  1.00 30.38           C  
ANISOU 2891  C   GLY A 348     4079   3895   3569    106     -9    207       C  
ATOM   2892  O   GLY A 348      20.915  -8.159 -34.982  1.00 31.45           O  
ANISOU 2892  O   GLY A 348     4190   4037   3721    103     -6    205       O  
ATOM   2893  N   TYR A 349      21.231 -10.373 -35.319  1.00 28.53           N  
ANISOU 2893  N   TYR A 349     3862   3646   3332    121     14    210       N  
ATOM   2894  CA  TYR A 349      22.585 -10.192 -35.838  1.00 30.02           C  
ANISOU 2894  CA  TYR A 349     4037   3826   3544    137     49    213       C  
ATOM   2895  C   TYR A 349      22.642  -9.459 -37.188  1.00 31.04           C  
ANISOU 2895  C   TYR A 349     4192   3941   3661    126     74    212       C  
ATOM   2896  O   TYR A 349      23.571  -8.696 -37.441  1.00 32.25           O  
ANISOU 2896  O   TYR A 349     4319   4094   3839    131     95    214       O  
ATOM   2897  CB  TYR A 349      23.367 -11.510 -35.866  1.00 28.00           C  
ANISOU 2897  CB  TYR A 349     3790   3552   3297    162     77    220       C  
ATOM   2898  CG  TYR A 349      23.776 -11.975 -34.490  1.00 28.06           C  
ANISOU 2898  CG  TYR A 349     3758   3575   3329    175     53    228       C  
ATOM   2899  CD1 TYR A 349      24.615 -11.200 -33.692  1.00 30.39           C  
ANISOU 2899  CD1 TYR A 349     4000   3888   3661    176     36    237       C  
ATOM   2900  CD2 TYR A 349      23.317 -13.184 -33.979  1.00 28.51           C  
ANISOU 2900  CD2 TYR A 349     3837   3626   3370    180     41    229       C  
ATOM   2901  CE1 TYR A 349      24.974 -11.612 -32.421  1.00 30.56           C  
ANISOU 2901  CE1 TYR A 349     3994   3920   3699    181      4    248       C  
ATOM   2902  CE2 TYR A 349      23.681 -13.616 -32.707  1.00 29.27           C  
ANISOU 2902  CE2 TYR A 349     3903   3733   3484    188     14    239       C  
ATOM   2903  CZ  TYR A 349      24.507 -12.826 -31.933  1.00 30.90           C  
ANISOU 2903  CZ  TYR A 349     4062   3957   3724    188     -6    249       C  
ATOM   2904  OH  TYR A 349      24.873 -13.250 -30.672  1.00 29.02           O  
ANISOU 2904  OH  TYR A 349     3803   3726   3499    189    -41    263       O  
ATOM   2905  N   TYR A 350      21.637  -9.667 -38.034  1.00 32.76           N  
ANISOU 2905  N   TYR A 350     4462   4143   3842    106     65    210       N  
ATOM   2906  CA  TYR A 350      21.578  -8.997 -39.337  1.00 33.27           C  
ANISOU 2906  CA  TYR A 350     4565   4191   3887     88     80    211       C  
ATOM   2907  C   TYR A 350      21.488  -7.466 -39.171  1.00 33.07           C  
ANISOU 2907  C   TYR A 350     4501   4183   3882     78     62    212       C  
ATOM   2908  O   TYR A 350      22.188  -6.711 -39.845  1.00 32.36           O  
ANISOU 2908  O   TYR A 350     4411   4085   3797     76     87    213       O  
ATOM   2909  CB  TYR A 350      20.410  -9.556 -40.162  1.00 33.68           C  
ANISOU 2909  CB  TYR A 350     4683   4221   3893     61     58    215       C  
ATOM   2910  CG  TYR A 350      20.304  -8.980 -41.553  1.00 33.59           C  
ANISOU 2910  CG  TYR A 350     4726   4185   3852     36     66    219       C  
ATOM   2911  CD1 TYR A 350      21.071  -9.492 -42.595  1.00 33.37           C  
ANISOU 2911  CD1 TYR A 350     4759   4123   3795     36    118    214       C  
ATOM   2912  CD2 TYR A 350      19.442  -7.909 -41.825  1.00 29.18           C  
ANISOU 2912  CD2 TYR A 350     4161   3633   3293     11     24    229       C  
ATOM   2913  CE1 TYR A 350      20.993  -8.957 -43.879  1.00 37.12           C  
ANISOU 2913  CE1 TYR A 350     5297   4572   4235      8    127    218       C  
ATOM   2914  CE2 TYR A 350      19.356  -7.365 -43.102  1.00 35.41           C  
ANISOU 2914  CE2 TYR A 350     5004   4398   4052    -16     25    237       C  
ATOM   2915  CZ  TYR A 350      20.132  -7.896 -44.127  1.00 37.15           C  
ANISOU 2915  CZ  TYR A 350     5294   4585   4235    -20     75    230       C  
ATOM   2916  OH  TYR A 350      20.054  -7.370 -45.394  1.00 40.17           O  
ANISOU 2916  OH  TYR A 350     5743   4940   4580    -51     78    237       O  
ATOM   2917  N   ALA A 351      20.648  -7.028 -38.240  1.00 34.35           N  
ANISOU 2917  N   ALA A 351     4631   4365   4055     73     23    213       N  
ATOM   2918  CA  ALA A 351      20.411  -5.610 -37.987  1.00 35.08           C  
ANISOU 2918  CA  ALA A 351     4693   4469   4168     64      7    213       C  
ATOM   2919  C   ALA A 351      21.494  -4.997 -37.114  1.00 35.64           C  
ANISOU 2919  C   ALA A 351     4716   4556   4268     77     17    207       C  
ATOM   2920  O   ALA A 351      21.710  -3.775 -37.134  1.00 36.32           O  
ANISOU 2920  O   ALA A 351     4785   4646   4370     69     16    207       O  
ATOM   2921  CB  ALA A 351      19.040  -5.422 -37.330  1.00 35.30           C  
ANISOU 2921  CB  ALA A 351     4708   4504   4199     55    -28    217       C  
ATOM   2922  N   LYS A 352      22.168  -5.862 -36.357  1.00 36.86           N  
ANISOU 2922  N   LYS A 352     4855   4718   4433     93     23    206       N  
ATOM   2923  CA  LYS A 352      23.128  -5.467 -35.324  1.00 36.27           C  
ANISOU 2923  CA  LYS A 352     4736   4658   4388     99     18    207       C  
ATOM   2924  C   LYS A 352      22.418  -4.695 -34.218  1.00 34.66           C  
ANISOU 2924  C   LYS A 352     4519   4466   4182     87    -13    200       C  
ATOM   2925  O   LYS A 352      22.728  -3.541 -33.930  1.00 35.40           O  
ANISOU 2925  O   LYS A 352     4597   4565   4290     77    -18    197       O  
ATOM   2926  CB  LYS A 352      24.310  -4.696 -35.924  1.00 39.24           C  
ANISOU 2926  CB  LYS A 352     5091   5030   4789    100     42    213       C  
ATOM   2927  CG  LYS A 352      25.153  -5.560 -36.834  1.00 38.93           C  
ANISOU 2927  CG  LYS A 352     5061   4973   4757    116     85    221       C  
ATOM   2928  CD  LYS A 352      26.142  -4.758 -37.636  1.00 39.12           C  
ANISOU 2928  CD  LYS A 352     5071   4989   4804    114    120    228       C  
ATOM   2929  CE  LYS A 352      26.941  -5.689 -38.523  1.00 37.68           C  
ANISOU 2929  CE  LYS A 352     4904   4782   4631    134    177    236       C  
ATOM   2930  NZ  LYS A 352      27.818  -4.975 -39.469  1.00 37.37           N  
ANISOU 2930  NZ  LYS A 352     4859   4728   4611    131    224    243       N  
ATOM   2931  N   ILE A 353      21.436  -5.360 -33.620  1.00 34.14           N  
ANISOU 2931  N   ILE A 353     4468   4403   4101     87    -27    196       N  
ATOM   2932  CA  ILE A 353      20.642  -4.802 -32.532  1.00 33.16           C  
ANISOU 2932  CA  ILE A 353     4341   4285   3975     78    -42    189       C  
ATOM   2933  C   ILE A 353      20.724  -5.757 -31.345  1.00 33.24           C  
ANISOU 2933  C   ILE A 353     4354   4301   3975     82    -55    188       C  
ATOM   2934  O   ILE A 353      21.134  -6.918 -31.499  1.00 31.29           O  
ANISOU 2934  O   ILE A 353     4110   4053   3724     93    -54    195       O  
ATOM   2935  CB  ILE A 353      19.151  -4.656 -32.942  1.00 32.57           C  
ANISOU 2935  CB  ILE A 353     4279   4201   3893     72    -43    191       C  
ATOM   2936  CG1 ILE A 353      18.602  -5.993 -33.480  1.00 32.20           C  
ANISOU 2936  CG1 ILE A 353     4254   4150   3832     75    -46    199       C  
ATOM   2937  CG2 ILE A 353      18.980  -3.548 -33.973  1.00 30.22           C  
ANISOU 2937  CG2 ILE A 353     3981   3894   3606     65    -39    195       C  
ATOM   2938  CD1 ILE A 353      17.138  -5.969 -33.900  1.00 26.56           C  
ANISOU 2938  CD1 ILE A 353     3547   3426   3119     64    -57    209       C  
ATOM   2939  N   GLN A 354      20.322  -5.281 -30.169  1.00 30.78           N  
ANISOU 2939  N   GLN A 354     4047   3992   3657     72    -64    180       N  
ATOM   2940  CA  GLN A 354      20.076  -6.188 -29.057  1.00 30.74           C  
ANISOU 2940  CA  GLN A 354     4057   3989   3635     70    -74    179       C  
ATOM   2941  C   GLN A 354      19.083  -7.222 -29.576  1.00 31.15           C  
ANISOU 2941  C   GLN A 354     4119   4037   3679     78    -66    184       C  
ATOM   2942  O   GLN A 354      18.146  -6.860 -30.300  1.00 31.73           O  
ANISOU 2942  O   GLN A 354     4193   4104   3758     76    -57    186       O  
ATOM   2943  CB  GLN A 354      19.484  -5.441 -27.868  1.00 30.14           C  
ANISOU 2943  CB  GLN A 354     3998   3907   3546     55    -72    168       C  
ATOM   2944  CG  GLN A 354      20.333  -4.294 -27.330  1.00 32.14           C  
ANISOU 2944  CG  GLN A 354     4253   4159   3800     40    -83    161       C  
ATOM   2945  CD  GLN A 354      19.820  -3.790 -25.982  1.00 41.03           C  
ANISOU 2945  CD  GLN A 354     5416   5271   4901     21    -77    148       C  
ATOM   2946  OE1 GLN A 354      20.456  -3.995 -24.942  1.00 42.99           O  
ANISOU 2946  OE1 GLN A 354     5687   5519   5128      4   -102    148       O  
ATOM   2947  NE2 GLN A 354      18.653  -3.153 -25.991  1.00 40.91           N  
ANISOU 2947  NE2 GLN A 354     5410   5243   4890     24    -44    138       N  
ATOM   2948  N   ILE A 355      19.288  -8.500 -29.250  1.00 30.99           N  
ANISOU 2948  N   ILE A 355     4109   4018   3648     85    -74    190       N  
ATOM   2949  CA  ILE A 355      18.402  -9.564 -29.777  1.00 30.02           C  
ANISOU 2949  CA  ILE A 355     4002   3890   3516     88    -70    195       C  
ATOM   2950  C   ILE A 355      16.928  -9.308 -29.421  1.00 28.60           C  
ANISOU 2950  C   ILE A 355     3826   3705   3334     77    -64    195       C  
ATOM   2951  O   ILE A 355      16.041  -9.529 -30.238  1.00 28.77           O  
ANISOU 2951  O   ILE A 355     3849   3720   3361     72    -64    204       O  
ATOM   2952  CB  ILE A 355      18.840 -11.000 -29.334  1.00 29.08           C  
ANISOU 2952  CB  ILE A 355     3896   3768   3384     97    -78    202       C  
ATOM   2953  CG1 ILE A 355      20.329 -11.247 -29.628  1.00 31.54           C  
ANISOU 2953  CG1 ILE A 355     4194   4079   3712    113    -79    209       C  
ATOM   2954  CG2 ILE A 355      17.952 -12.089 -29.976  1.00 23.11           C  
ANISOU 2954  CG2 ILE A 355     3163   3002   2616     96    -75    207       C  
ATOM   2955  CD1 ILE A 355      20.739 -11.118 -31.111  1.00 36.70           C  
ANISOU 2955  CD1 ILE A 355     4845   4723   4375    122    -56    210       C  
ATOM   2956  N   GLN A 356      16.670  -8.816 -28.214  1.00 29.03           N  
ANISOU 2956  N   GLN A 356     3884   3761   3385     70    -58    187       N  
ATOM   2957  CA  GLN A 356      15.289  -8.595 -27.783  1.00 29.77           C  
ANISOU 2957  CA  GLN A 356     3978   3846   3487     63    -40    189       C  
ATOM   2958  C   GLN A 356      14.583  -7.485 -28.576  1.00 29.25           C  
ANISOU 2958  C   GLN A 356     3890   3773   3451     63    -29    194       C  
ATOM   2959  O   GLN A 356      13.363  -7.330 -28.476  1.00 32.76           O  
ANISOU 2959  O   GLN A 356     4323   4208   3918     60    -13    204       O  
ATOM   2960  CB  GLN A 356      15.199  -8.354 -26.265  1.00 27.92           C  
ANISOU 2960  CB  GLN A 356     3765   3607   3235     55    -25    178       C  
ATOM   2961  CG  GLN A 356      15.784  -7.014 -25.773  1.00 30.37           C  
ANISOU 2961  CG  GLN A 356     4082   3913   3544     49    -18    163       C  
ATOM   2962  CD  GLN A 356      17.270  -7.091 -25.448  1.00 33.92           C  
ANISOU 2962  CD  GLN A 356     4540   4372   3976     44    -49    161       C  
ATOM   2963  OE1 GLN A 356      17.978  -7.992 -25.904  1.00 33.09           O  
ANISOU 2963  OE1 GLN A 356     4425   4277   3872     52    -71    171       O  
ATOM   2964  NE2 GLN A 356      17.749  -6.142 -24.651  1.00 34.87           N  
ANISOU 2964  NE2 GLN A 356     4680   4485   4082     28    -51    150       N  
ATOM   2965  N   SER A 357      15.340  -6.732 -29.370  1.00 28.74           N  
ANISOU 2965  N   SER A 357     3817   3711   3393     65    -36    191       N  
ATOM   2966  CA  SER A 357      14.752  -5.698 -30.235  1.00 30.41           C  
ANISOU 2966  CA  SER A 357     4009   3913   3631     64    -32    200       C  
ATOM   2967  C   SER A 357      14.084  -6.234 -31.504  1.00 30.11           C  
ANISOU 2967  C   SER A 357     3968   3870   3602     59    -51    220       C  
ATOM   2968  O   SER A 357      13.504  -5.443 -32.275  1.00 29.81           O  
ANISOU 2968  O   SER A 357     3916   3822   3588     54    -57    234       O  
ATOM   2969  CB  SER A 357      15.794  -4.656 -30.631  1.00 29.48           C  
ANISOU 2969  CB  SER A 357     3888   3798   3515     65    -34    191       C  
ATOM   2970  OG  SER A 357      16.206  -3.913 -29.511  1.00 31.70           O  
ANISOU 2970  OG  SER A 357     4176   4077   3791     62    -21    175       O  
ATOM   2971  N   VAL A 358      14.160  -7.549 -31.734  1.00 27.77           N  
ANISOU 2971  N   VAL A 358     3690   3576   3284     56    -64    225       N  
ATOM   2972  CA  VAL A 358      13.441  -8.166 -32.875  1.00 30.00           C  
ANISOU 2972  CA  VAL A 358     3982   3849   3566     43    -87    245       C  
ATOM   2973  C   VAL A 358      11.926  -7.971 -32.764  1.00 29.75           C  
ANISOU 2973  C   VAL A 358     3926   3808   3570     32    -93    268       C  
ATOM   2974  O   VAL A 358      11.227  -7.976 -33.763  1.00 33.34           O  
ANISOU 2974  O   VAL A 358     4379   4251   4037     16   -121    292       O  
ATOM   2975  CB  VAL A 358      13.764  -9.677 -33.085  1.00 31.66           C  
ANISOU 2975  CB  VAL A 358     4226   4058   3745     41    -96    244       C  
ATOM   2976  CG1 VAL A 358      15.240  -9.871 -33.379  1.00 29.59           C  
ANISOU 2976  CG1 VAL A 358     3981   3799   3461     54    -85    229       C  
ATOM   2977  CG2 VAL A 358      13.297 -10.540 -31.874  1.00 29.71           C  
ANISOU 2977  CG2 VAL A 358     3977   3816   3495     43    -90    243       C  
ATOM   2978  N   PHE A 359      11.426  -7.804 -31.544  1.00 30.00           N  
ANISOU 2978  N   PHE A 359     3938   3840   3619     40    -68    264       N  
ATOM   2979  CA  PHE A 359      10.018  -7.492 -31.321  1.00 29.48           C  
ANISOU 2979  CA  PHE A 359     3837   3761   3601     35    -60    288       C  
ATOM   2980  C   PHE A 359       9.621  -6.143 -31.937  1.00 31.17           C  
ANISOU 2980  C   PHE A 359     4022   3963   3856     37    -61    303       C  
ATOM   2981  O   PHE A 359       8.430  -5.859 -32.093  1.00 31.63           O  
ANISOU 2981  O   PHE A 359     4044   4007   3967     32    -64    333       O  
ATOM   2982  CB  PHE A 359       9.699  -7.481 -29.824  1.00 29.97           C  
ANISOU 2982  CB  PHE A 359     3895   3822   3670     44    -17    276       C  
ATOM   2983  CG  PHE A 359       9.740  -8.851 -29.182  1.00 32.87           C  
ANISOU 2983  CG  PHE A 359     4287   4198   4006     39    -18    271       C  
ATOM   2984  CD1 PHE A 359       8.888  -9.867 -29.619  1.00 28.19           C  
ANISOU 2984  CD1 PHE A 359     3687   3600   3424     24    -41    296       C  
ATOM   2985  CD2 PHE A 359      10.618  -9.118 -28.133  1.00 32.71           C  
ANISOU 2985  CD2 PHE A 359     4297   4185   3946     45     -1    244       C  
ATOM   2986  CE1 PHE A 359       8.911 -11.123 -29.041  1.00 29.92           C  
ANISOU 2986  CE1 PHE A 359     3930   3823   3614     18    -42    292       C  
ATOM   2987  CE2 PHE A 359      10.651 -10.389 -27.535  1.00 31.44           C  
ANISOU 2987  CE2 PHE A 359     4160   4029   3758     40     -5    243       C  
ATOM   2988  CZ  PHE A 359       9.796 -11.396 -27.995  1.00 28.37           C  
ANISOU 2988  CZ  PHE A 359     3765   3636   3380     28    -22    265       C  
ATOM   2989  N   SER A 360      10.615  -5.333 -32.302  1.00 27.82           N  
ANISOU 2989  N   SER A 360     3611   3543   3415     43    -61    285       N  
ATOM   2990  CA  SER A 360      10.365  -3.977 -32.779  1.00 28.19           C  
ANISOU 2990  CA  SER A 360     3636   3577   3498     46    -58    296       C  
ATOM   2991  C   SER A 360      10.942  -3.737 -34.187  1.00 29.04           C  
ANISOU 2991  C   SER A 360     3762   3684   3587     34    -94    303       C  
ATOM   2992  O   SER A 360      12.153  -3.518 -34.350  1.00 30.09           O  
ANISOU 2992  O   SER A 360     3918   3827   3686     38    -87    279       O  
ATOM   2993  CB  SER A 360      10.936  -2.974 -31.782  1.00 26.37           C  
ANISOU 2993  CB  SER A 360     3408   3346   3267     62    -17    268       C  
ATOM   2994  OG  SER A 360      11.217  -1.743 -32.415  1.00 28.84           O  
ANISOU 2994  OG  SER A 360     3713   3649   3595     64    -20    270       O  
ATOM   2995  N   PRO A 361      10.078  -3.782 -35.215  1.00 31.60           N  
ANISOU 2995  N   PRO A 361     4078   3995   3934     17   -132    338       N  
ATOM   2996  CA  PRO A 361      10.556  -3.587 -36.593  1.00 30.71           C  
ANISOU 2996  CA  PRO A 361     3996   3876   3796     -1   -166    346       C  
ATOM   2997  C   PRO A 361      11.113  -2.185 -36.839  1.00 30.30           C  
ANISOU 2997  C   PRO A 361     3939   3820   3755      8   -152    338       C  
ATOM   2998  O   PRO A 361      11.998  -2.026 -37.687  1.00 28.92           O  
ANISOU 2998  O   PRO A 361     3798   3645   3544      0   -159    329       O  
ATOM   2999  CB  PRO A 361       9.308  -3.834 -37.448  1.00 29.65           C  
ANISOU 2999  CB  PRO A 361     3852   3724   3690    -27   -216    392       C  
ATOM   3000  CG  PRO A 361       8.154  -3.600 -36.522  1.00 32.61           C  
ANISOU 3000  CG  PRO A 361     4168   4093   4131    -15   -200    413       C  
ATOM   3001  CD  PRO A 361       8.634  -4.087 -35.173  1.00 32.24           C  
ANISOU 3001  CD  PRO A 361     4123   4063   4065      7   -150    376       C  
ATOM   3002  N   ILE A 362      10.602  -1.187 -36.113  1.00 30.30           N  
ANISOU 3002  N   ILE A 362     3899   3811   3802     24   -127    342       N  
ATOM   3003  CA  ILE A 362      11.136   0.184 -36.203  1.00 30.55           C  
ANISOU 3003  CA  ILE A 362     3927   3835   3845     33   -111    332       C  
ATOM   3004  C   ILE A 362      12.603   0.211 -35.764  1.00 32.27           C  
ANISOU 3004  C   ILE A 362     4173   4072   4017     40    -85    291       C  
ATOM   3005  O   ILE A 362      13.455   0.751 -36.472  1.00 35.48           O  
ANISOU 3005  O   ILE A 362     4598   4479   4405     34    -90    285       O  
ATOM   3006  CB  ILE A 362      10.253   1.222 -35.430  1.00 29.95           C  
ANISOU 3006  CB  ILE A 362     3809   3740   3832     52    -80    342       C  
ATOM   3007  CG1 ILE A 362       9.009   1.571 -36.255  1.00 28.26           C  
ANISOU 3007  CG1 ILE A 362     3560   3501   3676     44   -116    393       C  
ATOM   3008  CG2 ILE A 362      11.034   2.504 -35.077  1.00 27.63           C  
ANISOU 3008  CG2 ILE A 362     3524   3439   3536     63    -49    317       C  
ATOM   3009  CD1 ILE A 362       7.880   2.287 -35.477  1.00 24.52           C  
ANISOU 3009  CD1 ILE A 362     3033   3001   3281     66    -80    413       C  
ATOM   3010  N   LYS A 363      12.901  -0.392 -34.616  1.00 32.76           N  
ANISOU 3010  N   LYS A 363     4237   4147   4063     50    -60    268       N  
ATOM   3011  CA  LYS A 363      14.278  -0.461 -34.122  1.00 33.70           C  
ANISOU 3011  CA  LYS A 363     4376   4283   4147     54    -46    238       C  
ATOM   3012  C   LYS A 363      15.152  -1.269 -35.087  1.00 31.50           C  
ANISOU 3012  C   LYS A 363     4122   4015   3833     46    -63    237       C  
ATOM   3013  O   LYS A 363      16.278  -0.875 -35.408  1.00 30.54           O  
ANISOU 3013  O   LYS A 363     4009   3898   3698     45    -56    226       O  
ATOM   3014  CB  LYS A 363      14.318  -1.054 -32.695  1.00 34.52           C  
ANISOU 3014  CB  LYS A 363     4482   4395   4239     61    -25    220       C  
ATOM   3015  CG  LYS A 363      15.712  -1.216 -32.074  1.00 36.95           C  
ANISOU 3015  CG  LYS A 363     4807   4719   4515     61    -21    196       C  
ATOM   3016  CD  LYS A 363      16.480   0.102 -31.927  1.00 38.90           C  
ANISOU 3016  CD  LYS A 363     5054   4959   4765     57    -13    184       C  
ATOM   3017  CE  LYS A 363      15.980   0.943 -30.770  1.00 41.15           C  
ANISOU 3017  CE  LYS A 363     5347   5228   5060     58     13    172       C  
ATOM   3018  NZ  LYS A 363      16.879   2.111 -30.493  1.00 42.69           N  
ANISOU 3018  NZ  LYS A 363     5553   5416   5250     48     17    157       N  
ATOM   3019  N   THR A 364      14.615  -2.388 -35.560  1.00 30.59           N  
ANISOU 3019  N   THR A 364     4018   3899   3706     39    -81    251       N  
ATOM   3020  CA  THR A 364      15.315  -3.225 -36.523  1.00 29.06           C  
ANISOU 3020  CA  THR A 364     3859   3706   3477     31    -89    250       C  
ATOM   3021  C   THR A 364      15.640  -2.451 -37.797  1.00 30.97           C  
ANISOU 3021  C   THR A 364     4120   3935   3712     18    -96    260       C  
ATOM   3022  O   THR A 364      16.791  -2.414 -38.229  1.00 33.11           O  
ANISOU 3022  O   THR A 364     4408   4208   3964     20    -78    248       O  
ATOM   3023  CB  THR A 364      14.504  -4.497 -36.865  1.00 29.36           C  
ANISOU 3023  CB  THR A 364     3917   3738   3501     19   -111    265       C  
ATOM   3024  OG1 THR A 364      14.165  -5.189 -35.651  1.00 27.69           O  
ANISOU 3024  OG1 THR A 364     3688   3537   3296     30   -102    258       O  
ATOM   3025  CG2 THR A 364      15.318  -5.431 -37.769  1.00 27.55           C  
ANISOU 3025  CG2 THR A 364     3736   3504   3230     13   -108    260       C  
ATOM   3026  N   TRP A 365      14.638  -1.821 -38.396  1.00 30.55           N  
ANISOU 3026  N   TRP A 365     4062   3867   3680      5   -122    284       N  
ATOM   3027  CA  TRP A 365      14.877  -1.091 -39.628  1.00 31.12           C  
ANISOU 3027  CA  TRP A 365     4159   3923   3742    -12   -134    296       C  
ATOM   3028  C   TRP A 365      15.754   0.125 -39.410  1.00 31.89           C  
ANISOU 3028  C   TRP A 365     4241   4024   3851     -1   -109    281       C  
ATOM   3029  O   TRP A 365      16.549   0.469 -40.287  1.00 31.46           O  
ANISOU 3029  O   TRP A 365     4214   3963   3775    -11   -100    279       O  
ATOM   3030  CB  TRP A 365      13.576  -0.735 -40.358  1.00 30.21           C  
ANISOU 3030  CB  TRP A 365     4042   3787   3649    -33   -180    333       C  
ATOM   3031  CG  TRP A 365      13.047  -1.906 -41.139  1.00 32.39           C  
ANISOU 3031  CG  TRP A 365     4360   4052   3895    -58   -215    352       C  
ATOM   3032  CD1 TRP A 365      11.885  -2.596 -40.909  1.00 27.13           C  
ANISOU 3032  CD1 TRP A 365     3678   3383   3249    -69   -247    375       C  
ATOM   3033  CD2 TRP A 365      13.676  -2.539 -42.264  1.00 30.69           C  
ANISOU 3033  CD2 TRP A 365     4216   3824   3621    -80   -217    348       C  
ATOM   3034  NE1 TRP A 365      11.750  -3.607 -41.831  1.00 30.83           N  
ANISOU 3034  NE1 TRP A 365     4204   3836   3672    -99   -278    387       N  
ATOM   3035  CE2 TRP A 365      12.831  -3.598 -42.673  1.00 30.05           C  
ANISOU 3035  CE2 TRP A 365     4166   3731   3523   -106   -257    369       C  
ATOM   3036  CE3 TRP A 365      14.872  -2.312 -42.968  1.00 30.37           C  
ANISOU 3036  CE3 TRP A 365     4218   3778   3543    -82   -185    330       C  
ATOM   3037  CZ2 TRP A 365      13.144  -4.437 -43.752  1.00 27.17           C  
ANISOU 3037  CZ2 TRP A 365     3883   3344   3095   -135   -266    369       C  
ATOM   3038  CZ3 TRP A 365      15.188  -3.146 -44.038  1.00 27.44           C  
ANISOU 3038  CZ3 TRP A 365     3925   3386   3115   -106   -185    331       C  
ATOM   3039  CH2 TRP A 365      14.321  -4.197 -44.421  1.00 30.39           C  
ANISOU 3039  CH2 TRP A 365     4339   3745   3465   -133   -225    348       C  
ATOM   3040  N   ASP A 366      15.629   0.760 -38.244  1.00 31.41           N  
ANISOU 3040  N   ASP A 366     4142   3970   3821     15    -93    270       N  
ATOM   3041  CA  ASP A 366      16.450   1.925 -37.940  1.00 32.36           C  
ANISOU 3041  CA  ASP A 366     4252   4092   3951     20    -72    255       C  
ATOM   3042  C   ASP A 366      17.925   1.528 -37.928  1.00 32.29           C  
ANISOU 3042  C   ASP A 366     4255   4098   3916     22    -52    235       C  
ATOM   3043  O   ASP A 366      18.767   2.254 -38.446  1.00 34.18           O  
ANISOU 3043  O   ASP A 366     4500   4334   4153     16    -41    233       O  
ATOM   3044  CB  ASP A 366      16.039   2.581 -36.608  1.00 33.27           C  
ANISOU 3044  CB  ASP A 366     4339   4206   4095     34    -56    244       C  
ATOM   3045  CG  ASP A 366      16.655   3.963 -36.420  1.00 34.85           C  
ANISOU 3045  CG  ASP A 366     4535   4398   4307     33    -41    233       C  
ATOM   3046  OD1 ASP A 366      16.647   4.773 -37.367  1.00 39.76           O  
ANISOU 3046  OD1 ASP A 366     5164   5006   4938     25    -50    247       O  
ATOM   3047  OD2 ASP A 366      17.163   4.245 -35.323  1.00 36.27           O  
ANISOU 3047  OD2 ASP A 366     4713   4583   4485     37    -23    212       O  
ATOM   3048  N   ALA A 367      18.223   0.359 -37.366  1.00 31.93           N  
ANISOU 3048  N   ALA A 367     4210   4067   3856     30    -46    226       N  
ATOM   3049  CA  ALA A 367      19.600  -0.120 -37.278  1.00 31.13           C  
ANISOU 3049  CA  ALA A 367     4109   3976   3742     36    -26    214       C  
ATOM   3050  C   ALA A 367      20.149  -0.663 -38.595  1.00 31.47           C  
ANISOU 3050  C   ALA A 367     4185   4010   3764     30    -13    221       C  
ATOM   3051  O   ALA A 367      21.332  -0.479 -38.908  1.00 32.52           O  
ANISOU 3051  O   ALA A 367     4315   4143   3899     32     12    217       O  
ATOM   3052  CB  ALA A 367      19.727  -1.151 -36.189  1.00 31.92           C  
ANISOU 3052  CB  ALA A 367     4199   4091   3838     48    -26    205       C  
ATOM   3053  N   ILE A 368      19.307  -1.348 -39.358  1.00 30.53           N  
ANISOU 3053  N   ILE A 368     4099   3878   3622     21    -27    232       N  
ATOM   3054  CA  ILE A 368      19.692  -1.801 -40.692  1.00 30.47           C  
ANISOU 3054  CA  ILE A 368     4142   3852   3583      9    -13    238       C  
ATOM   3055  C   ILE A 368      20.078  -0.592 -41.560  1.00 32.09           C  
ANISOU 3055  C   ILE A 368     4359   4045   3789     -5     -5    244       C  
ATOM   3056  O   ILE A 368      21.175  -0.537 -42.112  1.00 31.37           O  
ANISOU 3056  O   ILE A 368     4282   3948   3691     -4     33    239       O  
ATOM   3057  CB  ILE A 368      18.576  -2.619 -41.358  1.00 30.88           C  
ANISOU 3057  CB  ILE A 368     4237   3887   3607     -9    -42    252       C  
ATOM   3058  CG1 ILE A 368      18.343  -3.915 -40.568  1.00 32.55           C  
ANISOU 3058  CG1 ILE A 368     4442   4109   3815      4    -44    245       C  
ATOM   3059  CG2 ILE A 368      18.932  -2.927 -42.825  1.00 34.57           C  
ANISOU 3059  CG2 ILE A 368     4776   4327   4031    -29    -28    257       C  
ATOM   3060  CD1 ILE A 368      17.184  -4.784 -41.062  1.00 33.46           C  
ANISOU 3060  CD1 ILE A 368     4597   4210   3908    -17    -79    261       C  
ATOM   3061  N   ILE A 369      19.185   0.389 -41.635  1.00 30.23           N  
ANISOU 3061  N   ILE A 369     4114   3804   3568    -16    -36    256       N  
ATOM   3062  CA  ILE A 369      19.411   1.567 -42.452  1.00 31.19           C  
ANISOU 3062  CA  ILE A 369     4250   3912   3691    -31    -35    265       C  
ATOM   3063  C   ILE A 369      20.672   2.336 -42.014  1.00 32.29           C  
ANISOU 3063  C   ILE A 369     4357   4061   3849    -21      0    250       C  
ATOM   3064  O   ILE A 369      21.499   2.716 -42.853  1.00 30.38           O  
ANISOU 3064  O   ILE A 369     4138   3809   3597    -30     26    252       O  
ATOM   3065  CB  ILE A 369      18.143   2.462 -42.503  1.00 30.26           C  
ANISOU 3065  CB  ILE A 369     4119   3782   3595    -41    -77    286       C  
ATOM   3066  CG1 ILE A 369      17.020   1.713 -43.232  1.00 29.35           C  
ANISOU 3066  CG1 ILE A 369     4040   3652   3461    -61   -118    310       C  
ATOM   3067  CG2 ILE A 369      18.438   3.777 -43.207  1.00 27.47           C  
ANISOU 3067  CG2 ILE A 369     3776   3414   3247    -54    -76    295       C  
ATOM   3068  CD1 ILE A 369      15.606   2.183 -42.896  1.00 33.17           C  
ANISOU 3068  CD1 ILE A 369     4488   4128   3986    -62   -162    335       C  
ATOM   3069  N   PHE A 370      20.829   2.522 -40.703  1.00 32.69           N  
ANISOU 3069  N   PHE A 370     4361   4131   3928     -5     -1    238       N  
ATOM   3070  CA  PHE A 370      21.985   3.228 -40.153  1.00 30.95           C  
ANISOU 3070  CA  PHE A 370     4110   3921   3729     -1     19    228       C  
ATOM   3071  C   PHE A 370      23.304   2.570 -40.529  1.00 30.01           C  
ANISOU 3071  C   PHE A 370     3991   3805   3607      3     56    226       C  
ATOM   3072  O   PHE A 370      24.244   3.263 -40.908  1.00 31.09           O  
ANISOU 3072  O   PHE A 370     4120   3937   3756     -4     78    229       O  
ATOM   3073  CB  PHE A 370      21.860   3.383 -38.630  1.00 32.40           C  
ANISOU 3073  CB  PHE A 370     4257   4119   3933      9      6    215       C  
ATOM   3074  CG  PHE A 370      23.185   3.536 -37.914  1.00 32.87           C  
ANISOU 3074  CG  PHE A 370     4289   4192   4009      9     18    208       C  
ATOM   3075  CD1 PHE A 370      23.616   2.562 -37.020  1.00 37.26           C  
ANISOU 3075  CD1 PHE A 370     4826   4762   4568     19     15    203       C  
ATOM   3076  CD2 PHE A 370      23.990   4.651 -38.128  1.00 35.24           C  
ANISOU 3076  CD2 PHE A 370     4579   4487   4325     -5     26    210       C  
ATOM   3077  CE1 PHE A 370      24.834   2.698 -36.349  1.00 38.69           C  
ANISOU 3077  CE1 PHE A 370     4977   4953   4770     16     15    204       C  
ATOM   3078  CE2 PHE A 370      25.205   4.791 -37.474  1.00 38.62           C  
ANISOU 3078  CE2 PHE A 370     4975   4925   4773    -10     28    209       C  
ATOM   3079  CZ  PHE A 370      25.627   3.813 -36.580  1.00 39.77           C  
ANISOU 3079  CZ  PHE A 370     5100   5085   4925      0     20    208       C  
ATOM   3080  N   ASN A 371      23.379   1.244 -40.405  1.00 29.95           N  
ANISOU 3080  N   ASN A 371     3991   3802   3589     16     65    223       N  
ATOM   3081  CA  ASN A 371      24.569   0.486 -40.817  1.00 31.65           C  
ANISOU 3081  CA  ASN A 371     4205   4012   3807     27    108    225       C  
ATOM   3082  C   ASN A 371      24.855   0.593 -42.321  1.00 33.29           C  
ANISOU 3082  C   ASN A 371     4464   4194   3990     14    145    231       C  
ATOM   3083  O   ASN A 371      26.008   0.749 -42.733  1.00 37.11           O  
ANISOU 3083  O   ASN A 371     4938   4671   4492     17    190    236       O  
ATOM   3084  CB  ASN A 371      24.478  -0.978 -40.372  1.00 28.63           C  
ANISOU 3084  CB  ASN A 371     3826   3635   3417     45    111    221       C  
ATOM   3085  CG  ASN A 371      24.916  -1.173 -38.929  1.00 33.72           C  
ANISOU 3085  CG  ASN A 371     4417   4302   4093     58     93    219       C  
ATOM   3086  OD1 ASN A 371      26.110  -1.173 -38.636  1.00 36.15           O  
ANISOU 3086  OD1 ASN A 371     4687   4613   4433     65    111    225       O  
ATOM   3087  ND2 ASN A 371      23.956  -1.337 -38.019  1.00 30.01           N  
ANISOU 3087  ND2 ASN A 371     3944   3843   3615     58     56    212       N  
ATOM   3088  N   SER A 372      23.807   0.537 -43.131  1.00 33.06           N  
ANISOU 3088  N   SER A 372     4490   4149   3922     -3    125    236       N  
ATOM   3089  CA  SER A 372      23.958   0.649 -44.573  1.00 35.72           C  
ANISOU 3089  CA  SER A 372     4892   4456   4223    -22    153    243       C  
ATOM   3090  C   SER A 372      24.505   2.024 -44.943  1.00 37.48           C  
ANISOU 3090  C   SER A 372     5104   4676   4462    -35    165    248       C  
ATOM   3091  O   SER A 372      25.410   2.121 -45.761  1.00 38.62           O  
ANISOU 3091  O   SER A 372     5272   4801   4599    -41    217    251       O  
ATOM   3092  CB  SER A 372      22.628   0.409 -45.274  1.00 36.41           C  
ANISOU 3092  CB  SER A 372     5041   4526   4268    -46    110    252       C  
ATOM   3093  OG  SER A 372      22.785   0.349 -46.687  1.00 38.32           O  
ANISOU 3093  OG  SER A 372     5364   4734   4462    -71    135    259       O  
ATOM   3094  N   LEU A 373      23.978   3.074 -44.310  1.00 38.05           N  
ANISOU 3094  N   LEU A 373     5140   4761   4558    -40    123    250       N  
ATOM   3095  CA  LEU A 373      24.374   4.451 -44.622  1.00 38.48           C  
ANISOU 3095  CA  LEU A 373     5185   4809   4626    -54    127    256       C  
ATOM   3096  C   LEU A 373      25.769   4.793 -44.098  1.00 38.63           C  
ANISOU 3096  C   LEU A 373     5152   4840   4684    -45    164    252       C  
ATOM   3097  O   LEU A 373      26.520   5.511 -44.756  1.00 38.17           O  
ANISOU 3097  O   LEU A 373     5101   4771   4632    -59    195    258       O  
ATOM   3098  CB  LEU A 373      23.337   5.450 -44.084  1.00 37.84           C  
ANISOU 3098  CB  LEU A 373     5086   4732   4561    -59     75    260       C  
ATOM   3099  CG  LEU A 373      21.962   5.484 -44.755  1.00 37.10           C  
ANISOU 3099  CG  LEU A 373     5033   4620   4443    -74     32    276       C  
ATOM   3100  CD1 LEU A 373      21.006   6.382 -43.982  1.00 39.48           C  
ANISOU 3100  CD1 LEU A 373     5298   4924   4778    -69     -8    281       C  
ATOM   3101  CD2 LEU A 373      22.062   5.949 -46.203  1.00 38.65           C  
ANISOU 3101  CD2 LEU A 373     5292   4787   4605   -102     39    292       C  
ATOM   3102  N   LYS A 374      26.095   4.276 -42.913  1.00 40.01           N  
ANISOU 3102  N   LYS A 374     5276   5038   4888    -26    156    244       N  
ATOM   3103  CA  LYS A 374      27.410   4.445 -42.294  1.00 42.14           C  
ANISOU 3103  CA  LYS A 374     5490   5320   5203    -21    177    247       C  
ATOM   3104  C   LYS A 374      28.536   3.858 -43.147  1.00 44.10           C  
ANISOU 3104  C   LYS A 374     5741   5554   5460    -14    242    257       C  
ATOM   3105  O   LYS A 374      29.617   4.436 -43.225  1.00 45.01           O  
ANISOU 3105  O   LYS A 374     5822   5668   5613    -20    270    267       O  
ATOM   3106  CB  LYS A 374      27.427   3.834 -40.887  1.00 41.36           C  
ANISOU 3106  CB  LYS A 374     5345   5243   5124     -5    147    241       C  
ATOM   3107  CG  LYS A 374      28.789   3.857 -40.224  1.00 41.41           C  
ANISOU 3107  CG  LYS A 374     5292   5261   5180     -3    158    251       C  
ATOM   3108  CD  LYS A 374      28.714   3.572 -38.739  1.00 39.20           C  
ANISOU 3108  CD  LYS A 374     4979   5001   4914      1    112    247       C  
ATOM   3109  CE  LYS A 374      30.053   3.089 -38.242  1.00 37.14           C  
ANISOU 3109  CE  LYS A 374     4662   4748   4703      7    120    266       C  
ATOM   3110  NZ  LYS A 374      30.323   1.721 -38.746  1.00 40.59           N  
ANISOU 3110  NZ  LYS A 374     5101   5178   5145     34    161    273       N  
ATOM   3111  N   GLU A 375      28.277   2.716 -43.781  1.00 46.00           N  
ANISOU 3111  N   GLU A 375     6027   5780   5671     -3    270    254       N  
ATOM   3112  CA  GLU A 375      29.213   2.120 -44.741  1.00 48.78           C  
ANISOU 3112  CA  GLU A 375     6402   6109   6025      4    346    261       C  
ATOM   3113  C   GLU A 375      29.672   3.100 -45.830  1.00 46.25           C  
ANISOU 3113  C   GLU A 375     6112   5766   5697    -18    386    269       C  
ATOM   3114  O   GLU A 375      30.790   2.999 -46.328  1.00 45.66           O  
ANISOU 3114  O   GLU A 375     6025   5675   5649    -12    455    279       O  
ATOM   3115  CB  GLU A 375      28.603   0.867 -45.391  1.00 51.74           C  
ANISOU 3115  CB  GLU A 375     6847   6462   6350     11    365    253       C  
ATOM   3116  CG  GLU A 375      29.309  -0.450 -45.029  1.00 62.55           C  
ANISOU 3116  CG  GLU A 375     8192   7828   7747     43    407    255       C  
ATOM   3117  CD  GLU A 375      30.591  -0.700 -45.855  1.00 71.56           C  
ANISOU 3117  CD  GLU A 375     9336   8939   8915     55    503    266       C  
ATOM   3118  OE1 GLU A 375      30.557  -0.549 -47.102  1.00 71.06           O  
ANISOU 3118  OE1 GLU A 375     9351   8843   8807     38    552    263       O  
ATOM   3119  OE2 GLU A 375      31.634  -1.057 -45.255  1.00 74.94           O  
ANISOU 3119  OE2 GLU A 375     9691   9374   9410     80    532    279       O  
ATOM   3120  N   GLN A 376      28.805   4.043 -46.185  1.00 43.16           N  
ANISOU 3120  N   GLN A 376     5757   5371   5271    -43    344    267       N  
ATOM   3121  CA  GLN A 376      29.095   5.004 -47.246  1.00 43.02           C  
ANISOU 3121  CA  GLN A 376     5779   5330   5236    -69    374    275       C  
ATOM   3122  C   GLN A 376      29.472   6.383 -46.685  1.00 41.43           C  
ANISOU 3122  C   GLN A 376     5521   5144   5076    -81    348    281       C  
ATOM   3123  O   GLN A 376      29.511   7.372 -47.427  1.00 39.66           O  
ANISOU 3123  O   GLN A 376     5328   4903   4838   -105    356    288       O  
ATOM   3124  CB  GLN A 376      27.891   5.120 -48.183  1.00 44.48           C  
ANISOU 3124  CB  GLN A 376     6054   5493   5354    -93    343    275       C  
ATOM   3125  CG  GLN A 376      27.309   3.781 -48.653  1.00 49.81           C  
ANISOU 3125  CG  GLN A 376     6794   6151   5980    -89    349    270       C  
ATOM   3126  CD  GLN A 376      25.842   3.882 -49.056  1.00 54.51           C  
ANISOU 3126  CD  GLN A 376     7448   6737   6526   -113    280    275       C  
ATOM   3127  OE1 GLN A 376      25.000   3.126 -48.566  1.00 58.27           O  
ANISOU 3127  OE1 GLN A 376     7922   7224   6994   -105    238    271       O  
ATOM   3128  NE2 GLN A 376      25.528   4.824 -49.944  1.00 56.65           N  
ANISOU 3128  NE2 GLN A 376     7769   6986   6768   -145    264    288       N  
ATOM   3129  N   ASN A 377      29.754   6.427 -45.379  1.00 39.05           N  
ANISOU 3129  N   ASN A 377     5145   4871   4822    -67    316    279       N  
ATOM   3130  CA  ASN A 377      30.011   7.672 -44.628  1.00 38.79           C  
ANISOU 3130  CA  ASN A 377     5064   4851   4823    -82    280    282       C  
ATOM   3131  C   ASN A 377      28.852   8.685 -44.675  1.00 38.86           C  
ANISOU 3131  C   ASN A 377     5108   4855   4803    -98    229    276       C  
ATOM   3132  O   ASN A 377      29.051   9.907 -44.630  1.00 38.31           O  
ANISOU 3132  O   ASN A 377     5028   4779   4748   -117    218    280       O  
ATOM   3133  CB  ASN A 377      31.353   8.312 -45.029  1.00 40.48           C  
ANISOU 3133  CB  ASN A 377     5246   5056   5077    -95    328    298       C  
ATOM   3134  CG  ASN A 377      32.556   7.427 -44.692  1.00 43.09           C  
ANISOU 3134  CG  ASN A 377     5517   5394   5462    -76    371    311       C  
ATOM   3135  OD1 ASN A 377      32.706   6.937 -43.564  1.00 38.47           O  
ANISOU 3135  OD1 ASN A 377     4879   4830   4906    -63    336    312       O  
ATOM   3136  ND2 ASN A 377      33.419   7.225 -45.677  1.00 38.95           N  
ANISOU 3136  ND2 ASN A 377     5000   4848   4952    -75    449    325       N  
ATOM   3137  N   LYS A 378      27.634   8.162 -44.760  1.00 38.79           N  
ANISOU 3137  N   LYS A 378     5137   4844   4759    -91    199    269       N  
ATOM   3138  CA  LYS A 378      26.459   9.004 -44.693  1.00 37.85           C  
ANISOU 3138  CA  LYS A 378     5038   4717   4626   -100    150    269       C  
ATOM   3139  C   LYS A 378      25.932   9.079 -43.268  1.00 38.70           C  
ANISOU 3139  C   LYS A 378     5104   4844   4757    -86    110    258       C  
ATOM   3140  O   LYS A 378      26.137   8.166 -42.458  1.00 38.06           O  
ANISOU 3140  O   LYS A 378     4994   4781   4685    -70    109    249       O  
ATOM   3141  CB  LYS A 378      25.387   8.536 -45.673  1.00 40.47           C  
ANISOU 3141  CB  LYS A 378     5434   5031   4913   -106    136    277       C  
ATOM   3142  CG  LYS A 378      25.767   8.768 -47.124  1.00 41.37           C  
ANISOU 3142  CG  LYS A 378     5609   5117   4993   -130    170    290       C  
ATOM   3143  CD  LYS A 378      24.713   8.231 -48.077  1.00 44.21           C  
ANISOU 3143  CD  LYS A 378     6041   5455   5302   -144    145    300       C  
ATOM   3144  CE  LYS A 378      25.119   8.462 -49.533  1.00 48.98           C  
ANISOU 3144  CE  LYS A 378     6722   6025   5862   -173    180    312       C  
ATOM   3145  NZ  LYS A 378      23.968   8.225 -50.463  1.00 51.28           N  
ANISOU 3145  NZ  LYS A 378     7093   6291   6101   -199    135    329       N  
ATOM   3146  N   VAL A 379      25.272  10.191 -42.970  1.00 37.84           N  
ANISOU 3146  N   VAL A 379     4996   4725   4656    -94     80    258       N  
ATOM   3147  CA  VAL A 379      24.818  10.494 -41.625  1.00 37.03           C  
ANISOU 3147  CA  VAL A 379     4864   4632   4573    -85     53    245       C  
ATOM   3148  C   VAL A 379      23.288  10.549 -41.568  1.00 35.08           C  
ANISOU 3148  C   VAL A 379     4634   4373   4320    -74     24    249       C  
ATOM   3149  O   VAL A 379      22.660  11.262 -42.351  1.00 36.12           O  
ANISOU 3149  O   VAL A 379     4790   4483   4450    -83     13    264       O  
ATOM   3150  CB  VAL A 379      25.448  11.817 -41.147  1.00 39.11           C  
ANISOU 3150  CB  VAL A 379     5113   4887   4858   -102     51    242       C  
ATOM   3151  CG1 VAL A 379      24.836  12.268 -39.849  1.00 39.05           C  
ANISOU 3151  CG1 VAL A 379     5096   4878   4862    -96     28    227       C  
ATOM   3152  CG2 VAL A 379      26.963  11.652 -41.000  1.00 37.99           C  
ANISOU 3152  CG2 VAL A 379     4939   4759   4734   -113     72    244       C  
ATOM   3153  N   ILE A 380      22.701   9.788 -40.644  1.00 33.18           N  
ANISOU 3153  N   ILE A 380     4378   4146   4083    -57     13    239       N  
ATOM   3154  CA  ILE A 380      21.242   9.688 -40.522  1.00 31.46           C  
ANISOU 3154  CA  ILE A 380     4165   3917   3870    -45    -10    246       C  
ATOM   3155  C   ILE A 380      20.640  10.964 -39.928  1.00 32.04           C  
ANISOU 3155  C   ILE A 380     4232   3970   3972    -43    -15    245       C  
ATOM   3156  O   ILE A 380      21.304  11.659 -39.156  1.00 31.66           O  
ANISOU 3156  O   ILE A 380     4176   3921   3931    -48     -5    230       O  
ATOM   3157  CB  ILE A 380      20.803   8.435 -39.705  1.00 30.59           C  
ANISOU 3157  CB  ILE A 380     4042   3826   3756    -28    -14    237       C  
ATOM   3158  CG1 ILE A 380      21.181   8.555 -38.223  1.00 28.76           C  
ANISOU 3158  CG1 ILE A 380     3789   3605   3535    -22     -7    216       C  
ATOM   3159  CG2 ILE A 380      21.398   7.152 -40.313  1.00 31.40           C  
ANISOU 3159  CG2 ILE A 380     4155   3942   3831    -28     -4    238       C  
ATOM   3160  CD1 ILE A 380      20.897   7.278 -37.412  1.00 26.31           C  
ANISOU 3160  CD1 ILE A 380     3469   3313   3215     -8    -10    207       C  
ATOM   3161  N   PRO A 381      19.392  11.294 -40.311  1.00 32.61           N  
ANISOU 3161  N   PRO A 381     4309   4021   4062    -36    -32    265       N  
ATOM   3162  CA  PRO A 381      18.779  12.512 -39.766  1.00 33.38           C  
ANISOU 3162  CA  PRO A 381     4398   4091   4194    -28    -29    266       C  
ATOM   3163  C   PRO A 381      18.365  12.306 -38.320  1.00 33.23           C  
ANISOU 3163  C   PRO A 381     4365   4074   4188    -11    -12    246       C  
ATOM   3164  O   PRO A 381      18.224  11.165 -37.880  1.00 34.39           O  
ANISOU 3164  O   PRO A 381     4502   4242   4322     -3    -12    239       O  
ATOM   3165  CB  PRO A 381      17.535  12.714 -40.648  1.00 30.48           C  
ANISOU 3165  CB  PRO A 381     4032   3700   3850    -24    -55    302       C  
ATOM   3166  CG  PRO A 381      17.190  11.349 -41.151  1.00 32.26           C  
ANISOU 3166  CG  PRO A 381     4260   3943   4054    -26    -75    313       C  
ATOM   3167  CD  PRO A 381      18.497  10.590 -41.251  1.00 32.46           C  
ANISOU 3167  CD  PRO A 381     4300   3997   4036    -37    -58    291       C  
ATOM   3168  N   GLN A 382      18.173  13.397 -37.587  1.00 33.80           N  
ANISOU 3168  N   GLN A 382     4441   4120   4282     -6      7    236       N  
ATOM   3169  CA  GLN A 382      17.602  13.300 -36.252  1.00 35.98           C  
ANISOU 3169  CA  GLN A 382     4715   4388   4569     10     31    219       C  
ATOM   3170  C   GLN A 382      16.156  12.855 -36.362  1.00 37.51           C  
ANISOU 3170  C   GLN A 382     4885   4569   4798     34     31    242       C  
ATOM   3171  O   GLN A 382      15.453  13.243 -37.289  1.00 38.75           O  
ANISOU 3171  O   GLN A 382     5029   4708   4986     38     13    274       O  
ATOM   3172  CB  GLN A 382      17.676  14.649 -35.526  1.00 37.32           C  
ANISOU 3172  CB  GLN A 382     4907   4522   4752      8     57    203       C  
ATOM   3173  CG  GLN A 382      17.215  14.617 -34.056  1.00 37.44           C  
ANISOU 3173  CG  GLN A 382     4939   4520   4767     19     93    179       C  
ATOM   3174  CD  GLN A 382      17.590  15.880 -33.281  1.00 40.93           C  
ANISOU 3174  CD  GLN A 382     5422   4926   5204      6    119    157       C  
ATOM   3175  OE1 GLN A 382      17.542  16.999 -33.810  1.00 38.63           O  
ANISOU 3175  OE1 GLN A 382     5137   4605   4934      5    123    166       O  
ATOM   3176  NE2 GLN A 382      17.966  15.699 -32.015  1.00 41.35           N  
ANISOU 3176  NE2 GLN A 382     5509   4977   5223     -7    134    128       N  
ATOM   3177  N   GLY A 383      15.717  12.040 -35.410  1.00 39.75           N  
ANISOU 3177  N   GLY A 383     5161   4862   5079     46     47    230       N  
ATOM   3178  CA  GLY A 383      14.297  11.758 -35.253  1.00 42.79           C  
ANISOU 3178  CA  GLY A 383     5519   5230   5509     69     58    252       C  
ATOM   3179  C   GLY A 383      13.547  13.016 -34.855  1.00 44.84           C  
ANISOU 3179  C   GLY A 383     5776   5441   5819     87     94    259       C  
ATOM   3180  O   GLY A 383      14.003  13.776 -34.003  1.00 43.40           O  
ANISOU 3180  O   GLY A 383     5626   5241   5625     85    128    230       O  
ATOM   3181  N   ARG A 384      12.394  13.234 -35.479  1.00 48.39           N  
ANISOU 3181  N   ARG A 384     6190   5867   6328    104     85    299       N  
ATOM   3182  CA  ARG A 384      11.572  14.406 -35.195  1.00 50.82           C  
ANISOU 3182  CA  ARG A 384     6486   6123   6700    127    123    314       C  
ATOM   3183  C   ARG A 384      10.228  14.047 -34.564  1.00 50.31           C  
ANISOU 3183  C   ARG A 384     6382   6036   6698    157    160    334       C  
ATOM   3184  O   ARG A 384       9.826  12.876 -34.523  1.00 50.12           O  
ANISOU 3184  O   ARG A 384     6335   6038   6670    156    144    344       O  
ATOM   3185  CB  ARG A 384      11.364  15.228 -36.465  1.00 53.18           C  
ANISOU 3185  CB  ARG A 384     6770   6402   7034    124     85    353       C  
ATOM   3186  CG  ARG A 384      12.555  16.081 -36.827  1.00 59.39           C  
ANISOU 3186  CG  ARG A 384     7598   7189   7777    101     76    331       C  
ATOM   3187  CD  ARG A 384      12.499  16.564 -38.272  1.00 67.79           C  
ANISOU 3187  CD  ARG A 384     8657   8245   8856     88     25    371       C  
ATOM   3188  NE  ARG A 384      13.289  17.786 -38.446  1.00 75.87           N  
ANISOU 3188  NE  ARG A 384     9713   9248   9866     77     35    357       N  
ATOM   3189  CZ  ARG A 384      14.608  17.824 -38.636  1.00 78.45           C  
ANISOU 3189  CZ  ARG A 384    10075   9601  10133     48     26    330       C  
ATOM   3190  NH1 ARG A 384      15.320  16.699 -38.690  1.00 78.79           N  
ANISOU 3190  NH1 ARG A 384    10123   9690  10124     31     11    313       N  
ATOM   3191  NH2 ARG A 384      15.218  18.997 -38.773  1.00 78.88           N  
ANISOU 3191  NH2 ARG A 384    10156   9632  10183     36     35    322       N  
ATOM   3192  N   SER A 385       9.548  15.071 -34.064  1.00 48.87           N  
ANISOU 3192  N   SER A 385     6194   5802   6574    183    214    341       N  
ATOM   3193  CA  SER A 385       8.230  14.916 -33.481  1.00 48.85           C  
ANISOU 3193  CA  SER A 385     6148   5766   6646    216    263    365       C  
ATOM   3194  C   SER A 385       7.157  15.128 -34.556  1.00 47.14           C  
ANISOU 3194  C   SER A 385     5862   5529   6520    230    222    434       C  
ATOM   3195  O   SER A 385       7.204  16.110 -35.306  1.00 45.46           O  
ANISOU 3195  O   SER A 385     5647   5292   6335    230    200    456       O  
ATOM   3196  CB  SER A 385       8.060  15.916 -32.331  1.00 50.81           C  
ANISOU 3196  CB  SER A 385     6431   5961   6915    239    354    337       C  
ATOM   3197  OG  SER A 385       7.031  15.511 -31.447  1.00 53.59           O  
ANISOU 3197  OG  SER A 385     6759   6289   7316    266    420    345       O  
ATOM   3198  N   HIS A 386       6.201  14.205 -34.638  1.00 46.69           N  
ANISOU 3198  N   HIS A 386     5751   5481   6509    237    208    470       N  
ATOM   3199  CA  HIS A 386       5.100  14.328 -35.604  1.00 46.50           C  
ANISOU 3199  CA  HIS A 386     5656   5435   6578    245    160    543       C  
ATOM   3200  C   HIS A 386       3.764  13.969 -34.973  1.00 46.29           C  
ANISOU 3200  C   HIS A 386     5562   5380   6646    276    207    579       C  
ATOM   3201  O   HIS A 386       3.692  13.008 -34.196  1.00 46.55           O  
ANISOU 3201  O   HIS A 386     5599   5435   6651    275    237    556       O  
ATOM   3202  CB  HIS A 386       5.314  13.422 -36.820  1.00 46.53           C  
ANISOU 3202  CB  HIS A 386     5656   5481   6540    206     58    569       C  
ATOM   3203  CG  HIS A 386       6.678  13.520 -37.426  1.00 47.51           C  
ANISOU 3203  CG  HIS A 386     5847   5638   6566    175     20    533       C  
ATOM   3204  ND1 HIS A 386       7.056  14.563 -38.245  1.00 48.81           N  
ANISOU 3204  ND1 HIS A 386     6030   5784   6732    166     -8    546       N  
ATOM   3205  CD2 HIS A 386       7.749  12.695 -37.345  1.00 46.64           C  
ANISOU 3205  CD2 HIS A 386     5785   5575   6360    150      7    487       C  
ATOM   3206  CE1 HIS A 386       8.304  14.378 -38.637  1.00 50.27           C  
ANISOU 3206  CE1 HIS A 386     6271   6003   6826    137    -31    509       C  
ATOM   3207  NE2 HIS A 386       8.748  13.252 -38.105  1.00 48.68           N  
ANISOU 3207  NE2 HIS A 386     6086   5842   6568    128    -22    474       N  
ATOM   3208  N   PRO A 387       2.699  14.729 -35.310  1.00 45.35           N  
ANISOU 3208  N   PRO A 387     5377   5210   6645    303    214    640       N  
ATOM   3209  CA  PRO A 387       1.344  14.349 -34.909  1.00 45.38           C  
ANISOU 3209  CA  PRO A 387     5298   5186   6758    330    249    691       C  
ATOM   3210  C   PRO A 387       0.855  13.151 -35.722  1.00 44.53           C  
ANISOU 3210  C   PRO A 387     5145   5116   6659    299    153    739       C  
ATOM   3211  O   PRO A 387       1.134  13.065 -36.922  1.00 42.41           O  
ANISOU 3211  O   PRO A 387     4884   4867   6361    265     52    766       O  
ATOM   3212  CB  PRO A 387       0.511  15.593 -35.248  1.00 45.82           C  
ANISOU 3212  CB  PRO A 387     5296   5176   6938    365    267    749       C  
ATOM   3213  CG  PRO A 387       1.272  16.263 -36.353  1.00 47.53           C  
ANISOU 3213  CG  PRO A 387     5550   5401   7108    339    188    752       C  
ATOM   3214  CD  PRO A 387       2.720  16.019 -36.029  1.00 46.45           C  
ANISOU 3214  CD  PRO A 387     5512   5310   6826    312    194    668       C  
ATOM   3215  N   VAL A 388       0.146  12.239 -35.064  1.00 43.47           N  
ANISOU 3215  N   VAL A 388     4970   4987   6559    306    185    750       N  
ATOM   3216  CA  VAL A 388      -0.444  11.088 -35.736  1.00 43.70           C  
ANISOU 3216  CA  VAL A 388     4953   5044   6605    275     99    800       C  
ATOM   3217  C   VAL A 388      -1.508  11.569 -36.712  1.00 44.72           C  
ANISOU 3217  C   VAL A 388     4997   5136   6858    276     32    894       C  
ATOM   3218  O   VAL A 388      -2.380  12.351 -36.340  1.00 47.15           O  
ANISOU 3218  O   VAL A 388     5236   5390   7287    318     92    935       O  
ATOM   3219  CB  VAL A 388      -1.051  10.082 -34.724  1.00 43.95           C  
ANISOU 3219  CB  VAL A 388     4956   5084   6660    286    158    794       C  
ATOM   3220  CG1 VAL A 388      -1.678   8.891 -35.444  1.00 44.75           C  
ANISOU 3220  CG1 VAL A 388     5012   5212   6780    249     64    848       C  
ATOM   3221  CG2 VAL A 388       0.013   9.599 -33.730  1.00 43.53           C  
ANISOU 3221  CG2 VAL A 388     4992   5065   6483    281    217    704       C  
ATOM   3222  N   GLN A 389      -1.409  11.122 -37.963  1.00 44.46           N  
ANISOU 3222  N   GLN A 389     4972   5128   6792    229    -91    931       N  
ATOM   3223  CA  GLN A 389      -2.387  11.457 -39.005  1.00 45.62           C  
ANISOU 3223  CA  GLN A 389     5046   5243   7046    216   -180   1028       C  
ATOM   3224  C   GLN A 389      -2.902  10.195 -39.725  1.00 44.91           C  
ANISOU 3224  C   GLN A 389     4935   5179   6950    165   -287   1077       C  
ATOM   3225  O   GLN A 389      -2.107   9.330 -40.098  1.00 42.39           O  
ANISOU 3225  O   GLN A 389     4693   4906   6507    124   -334   1035       O  
ATOM   3226  CB  GLN A 389      -1.790  12.434 -40.023  1.00 45.73           C  
ANISOU 3226  CB  GLN A 389     5103   5244   7026    201   -240   1035       C  
ATOM   3227  CG  GLN A 389      -1.617  13.874 -39.537  1.00 52.23           C  
ANISOU 3227  CG  GLN A 389     5926   6025   7896    250   -155   1016       C  
ATOM   3228  CD  GLN A 389      -1.211  14.834 -40.664  1.00 57.95           C  
ANISOU 3228  CD  GLN A 389     6682   6731   8604    231   -227   1041       C  
ATOM   3229  OE1 GLN A 389      -0.062  14.832 -41.129  1.00 58.99           O  
ANISOU 3229  OE1 GLN A 389     6903   6896   8613    200   -256    989       O  
ATOM   3230  NE2 GLN A 389      -2.156  15.664 -41.099  1.00 56.73           N  
ANISOU 3230  NE2 GLN A 389     6452   6523   8580    250   -253   1122       N  
ATOM   3231  N   PRO A 390      -4.234  10.080 -39.907  1.00 40.57           N  
ANISOU 3231  N   PRO A 390     5741   4729   4945   -206    513   -101       N  
ATOM   3232  CA  PRO A 390      -4.779   8.976 -40.707  1.00 40.24           C  
ANISOU 3232  CA  PRO A 390     5676   4732   4881   -174    454    -47       C  
ATOM   3233  C   PRO A 390      -4.440   9.128 -42.186  1.00 38.65           C  
ANISOU 3233  C   PRO A 390     5433   4546   4705   -131    403     23       C  
ATOM   3234  O   PRO A 390      -4.367  10.247 -42.696  1.00 39.08           O  
ANISOU 3234  O   PRO A 390     5455   4560   4833   -112    430     45       O  
ATOM   3235  CB  PRO A 390      -6.296   9.093 -40.497  1.00 40.32           C  
ANISOU 3235  CB  PRO A 390     5652   4709   4958   -160    510    -44       C  
ATOM   3236  CG  PRO A 390      -6.451   9.888 -39.227  1.00 42.62           C  
ANISOU 3236  CG  PRO A 390     5971   4949   5275   -200    598   -118       C  
ATOM   3237  CD  PRO A 390      -5.308  10.867 -39.273  1.00 42.75           C  
ANISOU 3237  CD  PRO A 390     6000   4943   5300   -212    605   -134       C  
ATOM   3238  N   TYR A 391      -4.220   8.003 -42.857  1.00 37.94           N  
ANISOU 3238  N   TYR A 391     5346   4513   4556   -121    334     56       N  
ATOM   3239  CA  TYR A 391      -3.925   7.997 -44.285  1.00 35.45           C  
ANISOU 3239  CA  TYR A 391     4998   4221   4251    -90    285    119       C  
ATOM   3240  C   TYR A 391      -4.538   6.771 -44.956  1.00 35.82           C  
ANISOU 3240  C   TYR A 391     5032   4318   4261    -77    236    155       C  
ATOM   3241  O   TYR A 391      -4.822   5.782 -44.273  1.00 33.11           O  
ANISOU 3241  O   TYR A 391     4714   3997   3869    -94    228    127       O  
ATOM   3242  CB  TYR A 391      -2.411   8.086 -44.530  1.00 35.30           C  
ANISOU 3242  CB  TYR A 391     5005   4219   4190   -102    253    111       C  
ATOM   3243  CG  TYR A 391      -1.589   6.875 -44.130  1.00 33.13           C  
ANISOU 3243  CG  TYR A 391     4771   3989   3828   -126    206     85       C  
ATOM   3244  CD1 TYR A 391      -1.114   6.726 -42.827  1.00 36.31           C  
ANISOU 3244  CD1 TYR A 391     5217   4387   4191   -164    218     29       C  
ATOM   3245  CD2 TYR A 391      -1.253   5.898 -45.066  1.00 31.09           C  
ANISOU 3245  CD2 TYR A 391     4507   3777   3529   -115    150    117       C  
ATOM   3246  CE1 TYR A 391      -0.338   5.624 -42.464  1.00 33.56           C  
ANISOU 3246  CE1 TYR A 391     4901   4078   3773   -186    170     16       C  
ATOM   3247  CE2 TYR A 391      -0.483   4.801 -44.718  1.00 30.59           C  
ANISOU 3247  CE2 TYR A 391     4475   3746   3402   -134    111     97       C  
ATOM   3248  CZ  TYR A 391      -0.030   4.668 -43.412  1.00 33.97           C  
ANISOU 3248  CZ  TYR A 391     4940   4167   3799   -168    118     51       C  
ATOM   3249  OH  TYR A 391       0.737   3.578 -43.065  1.00 35.44           O  
ANISOU 3249  OH  TYR A 391     5150   4383   3932   -187     75     40       O  
ATOM   3250  N   PRO A 392      -4.756   6.834 -46.293  1.00 35.85           N  
ANISOU 3250  N   PRO A 392     4996   4340   4284    -53    203    219       N  
ATOM   3251  CA  PRO A 392      -5.443   5.758 -47.024  1.00 35.18           C  
ANISOU 3251  CA  PRO A 392     4897   4303   4169    -46    159    254       C  
ATOM   3252  C   PRO A 392      -4.609   4.508 -47.258  1.00 34.45           C  
ANISOU 3252  C   PRO A 392     4839   4262   3990    -61    109    239       C  
ATOM   3253  O   PRO A 392      -3.396   4.601 -47.460  1.00 33.87           O  
ANISOU 3253  O   PRO A 392     4785   4195   3889    -69     94    228       O  
ATOM   3254  CB  PRO A 392      -5.785   6.407 -48.370  1.00 34.18           C  
ANISOU 3254  CB  PRO A 392     4721   4178   4088    -25    140    328       C  
ATOM   3255  CG  PRO A 392      -4.767   7.461 -48.544  1.00 34.95           C  
ANISOU 3255  CG  PRO A 392     4823   4249   4209    -23    154    328       C  
ATOM   3256  CD  PRO A 392      -4.526   8.008 -47.155  1.00 35.06           C  
ANISOU 3256  CD  PRO A 392     4863   4215   4244    -34    210    264       C  
ATOM   3257  N   GLY A 393      -5.281   3.355 -47.254  1.00 34.34           N  
ANISOU 3257  N   GLY A 393     4826   4280   3942    -66     88    239       N  
ATOM   3258  CA  GLY A 393      -4.637   2.064 -47.483  1.00 33.13           C  
ANISOU 3258  CA  GLY A 393     4699   4170   3718    -80     46    226       C  
ATOM   3259  C   GLY A 393      -5.083   1.390 -48.769  1.00 34.32           C  
ANISOU 3259  C   GLY A 393     4827   4364   3849    -77      8    268       C  
ATOM   3260  O   GLY A 393      -5.210   2.037 -49.815  1.00 32.96           O  
ANISOU 3260  O   GLY A 393     4626   4197   3699    -69     -2    314       O  
ATOM   3261  N   ALA A 394      -5.343   0.085 -48.695  1.00 33.41           N  
ANISOU 3261  N   ALA A 394     4725   4280   3691    -88    -13    253       N  
ATOM   3262  CA  ALA A 394      -5.623  -0.693 -49.903  1.00 31.61           C  
ANISOU 3262  CA  ALA A 394     4482   4096   3433    -95    -48    282       C  
ATOM   3263  C   ALA A 394      -7.030  -0.474 -50.468  1.00 31.89           C  
ANISOU 3263  C   ALA A 394     4476   4140   3499    -88    -54    329       C  
ATOM   3264  O   ALA A 394      -7.905   0.070 -49.797  1.00 34.73           O  
ANISOU 3264  O   ALA A 394     4817   4470   3909    -75    -27    334       O  
ATOM   3265  CB  ALA A 394      -5.370  -2.169 -49.653  1.00 29.43           C  
ANISOU 3265  CB  ALA A 394     4231   3843   3107   -111    -65    248       C  
ATOM   3266  N   PHE A 395      -7.225  -0.889 -51.717  1.00 32.36           N  
ANISOU 3266  N   PHE A 395     4521   4243   3530   -102    -88    363       N  
ATOM   3267  CA  PHE A 395      -8.549  -1.010 -52.294  1.00 33.65           C  
ANISOU 3267  CA  PHE A 395     4647   4428   3710   -104   -106    408       C  
ATOM   3268  C   PHE A 395      -9.077  -2.421 -52.086  1.00 33.84           C  
ANISOU 3268  C   PHE A 395     4683   4480   3696   -120   -118    381       C  
ATOM   3269  O   PHE A 395      -8.332  -3.400 -52.222  1.00 34.91           O  
ANISOU 3269  O   PHE A 395     4850   4636   3778   -137   -128    345       O  
ATOM   3270  CB  PHE A 395      -8.526  -0.680 -53.788  1.00 33.12           C  
ANISOU 3270  CB  PHE A 395     4560   4399   3627   -121   -141    465       C  
ATOM   3271  CG  PHE A 395      -9.846  -0.869 -54.470  1.00 36.70           C  
ANISOU 3271  CG  PHE A 395     4973   4883   4090   -132   -171    519       C  
ATOM   3272  CD1 PHE A 395     -10.850   0.088 -54.349  1.00 40.48           C  
ANISOU 3272  CD1 PHE A 395     5402   5332   4647   -111   -166    572       C  
ATOM   3273  CD2 PHE A 395     -10.087  -2.004 -55.243  1.00 39.72           C  
ANISOU 3273  CD2 PHE A 395     5364   5319   4409   -166   -204    517       C  
ATOM   3274  CE1 PHE A 395     -12.080  -0.089 -54.980  1.00 41.24           C  
ANISOU 3274  CE1 PHE A 395     5454   5456   4760   -123   -200    629       C  
ATOM   3275  CE2 PHE A 395     -11.312  -2.191 -55.871  1.00 41.14           C  
ANISOU 3275  CE2 PHE A 395     5505   5530   4595   -182   -237    568       C  
ATOM   3276  CZ  PHE A 395     -12.308  -1.233 -55.742  1.00 42.44           C  
ANISOU 3276  CZ  PHE A 395     5617   5669   4840   -160   -239    627       C  
ATOM   3277  N   VAL A 396     -10.363  -2.501 -51.745  1.00 33.07           N  
ANISOU 3277  N   VAL A 396     4557   4376   3634   -113   -114    398       N  
ATOM   3278  CA  VAL A 396     -11.118  -3.755 -51.687  1.00 33.78           C  
ANISOU 3278  CA  VAL A 396     4647   4493   3695   -128   -128    384       C  
ATOM   3279  C   VAL A 396     -12.379  -3.614 -52.551  1.00 34.31           C  
ANISOU 3279  C   VAL A 396     4664   4586   3787   -136   -156    445       C  
ATOM   3280  O   VAL A 396     -13.158  -2.669 -52.385  1.00 31.74           O  
ANISOU 3280  O   VAL A 396     4298   4232   3532   -116   -145    485       O  
ATOM   3281  CB  VAL A 396     -11.521  -4.137 -50.238  1.00 33.44           C  
ANISOU 3281  CB  VAL A 396     4618   4417   3672   -117    -93    341       C  
ATOM   3282  CG1 VAL A 396     -12.059  -5.560 -50.190  1.00 33.66           C  
ANISOU 3282  CG1 VAL A 396     4653   4472   3663   -135   -107    321       C  
ATOM   3283  CG2 VAL A 396     -10.338  -4.001 -49.291  1.00 36.04           C  
ANISOU 3283  CG2 VAL A 396     4991   4718   3986   -112    -68    294       C  
ATOM   3284  N   LYS A 397     -12.545  -4.545 -53.491  1.00 33.83           N  
ANISOU 3284  N   LYS A 397     4605   4576   3672   -167   -193    452       N  
ATOM   3285  CA  LYS A 397     -13.697  -4.581 -54.376  1.00 33.84           C  
ANISOU 3285  CA  LYS A 397     4562   4612   3682   -186   -230    510       C  
ATOM   3286  C   LYS A 397     -14.902  -5.198 -53.663  1.00 34.52           C  
ANISOU 3286  C   LYS A 397     4627   4689   3800   -180   -221    502       C  
ATOM   3287  O   LYS A 397     -14.757  -6.193 -52.948  1.00 36.34           O  
ANISOU 3287  O   LYS A 397     4889   4916   4003   -183   -202    446       O  
ATOM   3288  CB  LYS A 397     -13.366  -5.386 -55.638  1.00 34.48           C  
ANISOU 3288  CB  LYS A 397     4661   4756   3683   -233   -268    513       C  
ATOM   3289  CG  LYS A 397     -14.522  -5.485 -56.649  1.00 35.68           C  
ANISOU 3289  CG  LYS A 397     4770   4955   3830   -265   -316    576       C  
ATOM   3290  CD  LYS A 397     -14.136  -6.295 -57.879  1.00 33.95           C  
ANISOU 3290  CD  LYS A 397     4578   4801   3522   -322   -348    568       C  
ATOM   3291  CE  LYS A 397     -15.320  -6.483 -58.820  1.00 35.68           C  
ANISOU 3291  CE  LYS A 397     4757   5073   3728   -363   -401    628       C  
ATOM   3292  NZ  LYS A 397     -15.694  -5.208 -59.534  1.00 35.08           N  
ANISOU 3292  NZ  LYS A 397     4636   5005   3686   -364   -437    722       N  
ATOM   3293  N   GLU A 398     -16.078  -4.603 -53.861  1.00 33.03           N  
ANISOU 3293  N   GLU A 398     4381   4495   3674   -172   -233    562       N  
ATOM   3294  CA  GLU A 398     -17.337  -5.180 -53.400  1.00 34.51           C  
ANISOU 3294  CA  GLU A 398     4538   4679   3896   -171   -230    564       C  
ATOM   3295  C   GLU A 398     -17.788  -6.352 -54.296  1.00 34.34           C  
ANISOU 3295  C   GLU A 398     4516   4719   3812   -215   -276    570       C  
ATOM   3296  O   GLU A 398     -18.162  -6.138 -55.447  1.00 36.60           O  
ANISOU 3296  O   GLU A 398     4772   5049   4087   -243   -325    630       O  
ATOM   3297  CB  GLU A 398     -18.429  -4.097 -53.341  1.00 35.57           C  
ANISOU 3297  CB  GLU A 398     4602   4779   4133   -147   -226    630       C  
ATOM   3298  CG  GLU A 398     -19.700  -4.520 -52.578  1.00 37.53           C  
ANISOU 3298  CG  GLU A 398     4817   5006   4438   -138   -203    624       C  
ATOM   3299  CD  GLU A 398     -19.547  -4.462 -51.053  1.00 40.22           C  
ANISOU 3299  CD  GLU A 398     5186   5288   4809   -111   -132    558       C  
ATOM   3300  OE1 GLU A 398     -19.273  -3.366 -50.505  1.00 39.74           O  
ANISOU 3300  OE1 GLU A 398     5119   5176   4805    -84    -90    557       O  
ATOM   3301  OE2 GLU A 398     -19.721  -5.515 -50.400  1.00 38.00           O  
ANISOU 3301  OE2 GLU A 398     4933   5012   4492   -121   -116    507       O  
ATOM   3302  N   PRO A 399     -17.769  -7.594 -53.772  1.00 32.28           N  
ANISOU 3302  N   PRO A 399     4288   4465   3511   -227   -262    510       N  
ATOM   3303  CA  PRO A 399     -18.263  -8.686 -54.617  1.00 32.18           C  
ANISOU 3303  CA  PRO A 399     4272   4508   3445   -271   -301    512       C  
ATOM   3304  C   PRO A 399     -19.789  -8.778 -54.642  1.00 34.73           C  
ANISOU 3304  C   PRO A 399     4537   4838   3820   -276   -320    556       C  
ATOM   3305  O   PRO A 399     -20.465  -8.323 -53.721  1.00 36.74           O  
ANISOU 3305  O   PRO A 399     4763   5046   4151   -241   -288    563       O  
ATOM   3306  CB  PRO A 399     -17.692  -9.937 -53.947  1.00 32.19           C  
ANISOU 3306  CB  PRO A 399     4325   4503   3401   -277   -273    434       C  
ATOM   3307  CG  PRO A 399     -17.625  -9.567 -52.476  1.00 32.63           C  
ANISOU 3307  CG  PRO A 399     4390   4499   3509   -234   -222    406       C  
ATOM   3308  CD  PRO A 399     -17.332  -8.067 -52.442  1.00 32.01           C  
ANISOU 3308  CD  PRO A 399     4294   4391   3477   -205   -213    442       C  
ATOM   3309  N   ILE A 400     -20.318  -9.368 -55.704  1.00 36.67           N  
ANISOU 3309  N   ILE A 400     4766   5142   4024   -323   -370    584       N  
ATOM   3310  CA  ILE A 400     -21.717  -9.732 -55.763  1.00 37.88           C  
ANISOU 3310  CA  ILE A 400     4869   5309   4216   -336   -393    618       C  
ATOM   3311  C   ILE A 400     -21.855 -11.043 -54.990  1.00 38.67           C  
ANISOU 3311  C   ILE A 400     5000   5400   4293   -341   -361    546       C  
ATOM   3312  O   ILE A 400     -21.307 -12.068 -55.411  1.00 38.71           O  
ANISOU 3312  O   ILE A 400     5048   5439   4223   -376   -368    500       O  
ATOM   3313  CB  ILE A 400     -22.179  -9.909 -57.224  1.00 38.49           C  
ANISOU 3313  CB  ILE A 400     4921   5458   4247   -395   -463    674       C  
ATOM   3314  CG1 ILE A 400     -22.131  -8.562 -57.949  1.00 39.19           C  
ANISOU 3314  CG1 ILE A 400     4972   5552   4365   -391   -498    759       C  
ATOM   3315  CG2 ILE A 400     -23.579 -10.544 -57.286  1.00 36.49           C  
ANISOU 3315  CG2 ILE A 400     4618   5224   4021   -418   -490    699       C  
ATOM   3316  CD1 ILE A 400     -22.109  -8.680 -59.466  1.00 45.09           C  
ANISOU 3316  CD1 ILE A 400     5717   6378   5035   -460   -567    806       C  
ATOM   3317  N   PRO A 401     -22.561 -11.012 -53.840  1.00 38.22           N  
ANISOU 3317  N   PRO A 401     4922   5295   4304   -306   -322    534       N  
ATOM   3318  CA  PRO A 401     -22.646 -12.255 -53.076  1.00 38.39           C  
ANISOU 3318  CA  PRO A 401     4977   5308   4303   -312   -292    469       C  
ATOM   3319  C   PRO A 401     -23.304 -13.325 -53.937  1.00 36.99           C  
ANISOU 3319  C   PRO A 401     4786   5185   4083   -363   -334    473       C  
ATOM   3320  O   PRO A 401     -24.366 -13.091 -54.512  1.00 40.08           O  
ANISOU 3320  O   PRO A 401     5121   5600   4508   -380   -372    531       O  
ATOM   3321  CB  PRO A 401     -23.524 -11.885 -51.873  1.00 37.27           C  
ANISOU 3321  CB  PRO A 401     4803   5111   4246   -274   -247    472       C  
ATOM   3322  CG  PRO A 401     -23.491 -10.382 -51.808  1.00 40.31           C  
ANISOU 3322  CG  PRO A 401     5156   5464   4697   -241   -237    518       C  
ATOM   3323  CD  PRO A 401     -23.361  -9.933 -53.234  1.00 37.44           C  
ANISOU 3323  CD  PRO A 401     4768   5148   4308   -266   -300    578       C  
ATOM   3324  N   ASN A 402     -22.651 -14.470 -54.052  1.00 33.56           N  
ANISOU 3324  N   ASN A 402     4403   4769   3581   -390   -327    414       N  
ATOM   3325  CA  ASN A 402     -23.112 -15.528 -54.927  1.00 34.33           C  
ANISOU 3325  CA  ASN A 402     4497   4918   3630   -446   -360    406       C  
ATOM   3326  C   ASN A 402     -22.269 -16.769 -54.717  1.00 33.99           C  
ANISOU 3326  C   ASN A 402     4512   4871   3532   -463   -331    329       C  
ATOM   3327  O   ASN A 402     -21.211 -16.713 -54.101  1.00 32.93           O  
ANISOU 3327  O   ASN A 402     4418   4703   3392   -434   -296    293       O  
ATOM   3328  CB  ASN A 402     -22.995 -15.084 -56.391  1.00 34.64           C  
ANISOU 3328  CB  ASN A 402     4523   5016   3621   -491   -416    452       C  
ATOM   3329  CG  ASN A 402     -24.049 -15.725 -57.300  1.00 38.27           C  
ANISOU 3329  CG  ASN A 402     4950   5533   4057   -551   -465    478       C  
ATOM   3330  OD1 ASN A 402     -24.535 -16.832 -57.048  1.00 41.14           O  
ANISOU 3330  OD1 ASN A 402     5318   5899   4412   -571   -454    438       O  
ATOM   3331  ND2 ASN A 402     -24.393 -15.024 -58.375  1.00 37.02           N  
ANISOU 3331  ND2 ASN A 402     4759   5422   3886   -585   -523    548       N  
ATOM   3332  N   ARG A 403     -22.749 -17.895 -55.223  1.00 35.47           N  
ANISOU 3332  N   ARG A 403     4700   5091   3687   -510   -344    305       N  
ATOM   3333  CA  ARG A 403     -21.881 -19.024 -55.474  1.00 37.52           C  
ANISOU 3333  CA  ARG A 403     5008   5356   3891   -540   -324    239       C  
ATOM   3334  C   ARG A 403     -21.021 -18.685 -56.690  1.00 40.12           C  
ANISOU 3334  C   ARG A 403     5359   5726   4160   -577   -345    242       C  
ATOM   3335  O   ARG A 403     -21.426 -17.888 -57.552  1.00 41.98           O  
ANISOU 3335  O   ARG A 403     5566   6002   4381   -599   -390    298       O  
ATOM   3336  CB  ARG A 403     -22.697 -20.297 -55.731  1.00 39.66           C  
ANISOU 3336  CB  ARG A 403     5272   5651   4148   -587   -329    212       C  
ATOM   3337  CG  ARG A 403     -23.552 -20.264 -56.993  1.00 38.40           C  
ANISOU 3337  CG  ARG A 403     5079   5557   3954   -648   -384    250       C  
ATOM   3338  CD  ARG A 403     -24.285 -21.572 -57.191  1.00 42.36           C  
ANISOU 3338  CD  ARG A 403     5577   6078   4440   -697   -384    214       C  
ATOM   3339  NE  ARG A 403     -25.491 -21.652 -56.381  1.00 46.25           N  
ANISOU 3339  NE  ARG A 403     6026   6550   4998   -671   -384    239       N  
ATOM   3340  CZ  ARG A 403     -26.346 -22.670 -56.398  1.00 49.30           C  
ANISOU 3340  CZ  ARG A 403     6397   6947   5387   -706   -385    218       C  
ATOM   3341  NH1 ARG A 403     -26.133 -23.719 -57.180  1.00 49.13           N  
ANISOU 3341  NH1 ARG A 403     6402   6958   5307   -769   -386    169       N  
ATOM   3342  NH2 ARG A 403     -27.419 -22.643 -55.622  1.00 53.03           N  
ANISOU 3342  NH2 ARG A 403     6828   7396   5924   -679   -382    243       N  
ATOM   3343  N   TYR A 404     -19.831 -19.277 -56.745  1.00 40.54           N  
ANISOU 3343  N   TYR A 404     5459   5765   4179   -584   -313    184       N  
ATOM   3344  CA  TYR A 404     -18.918 -19.134 -57.884  1.00 37.48           C  
ANISOU 3344  CA  TYR A 404     5099   5412   3732   -625   -320    171       C  
ATOM   3345  C   TYR A 404     -18.257 -20.488 -58.112  1.00 37.95           C  
ANISOU 3345  C   TYR A 404     5195   5464   3759   -661   -282     94       C  
ATOM   3346  O   TYR A 404     -17.529 -20.988 -57.242  1.00 34.69           O  
ANISOU 3346  O   TYR A 404     4804   4998   3378   -625   -241     53       O  
ATOM   3347  CB  TYR A 404     -17.874 -18.049 -57.604  1.00 33.96           C  
ANISOU 3347  CB  TYR A 404     4667   4937   3299   -579   -308    187       C  
ATOM   3348  CG  TYR A 404     -18.446 -16.655 -57.574  1.00 32.53           C  
ANISOU 3348  CG  TYR A 404     4448   4763   3150   -551   -342    263       C  
ATOM   3349  CD1 TYR A 404     -18.582 -15.911 -58.749  1.00 32.27           C  
ANISOU 3349  CD1 TYR A 404     4399   4780   3080   -587   -385    314       C  
ATOM   3350  CD2 TYR A 404     -18.864 -16.078 -56.374  1.00 32.28           C  
ANISOU 3350  CD2 TYR A 404     4395   4684   3187   -490   -328    285       C  
ATOM   3351  CE1 TYR A 404     -19.111 -14.626 -58.729  1.00 32.64           C  
ANISOU 3351  CE1 TYR A 404     4405   4826   3170   -560   -415    390       C  
ATOM   3352  CE2 TYR A 404     -19.402 -14.791 -56.340  1.00 31.33           C  
ANISOU 3352  CE2 TYR A 404     4235   4561   3110   -464   -350    352       C  
ATOM   3353  CZ  TYR A 404     -19.521 -14.074 -57.519  1.00 35.59           C  
ANISOU 3353  CZ  TYR A 404     4754   5145   3622   -496   -395    407       C  
ATOM   3354  OH  TYR A 404     -20.050 -12.804 -57.491  1.00 37.35           O  
ANISOU 3354  OH  TYR A 404     4931   5359   3900   -467   -416    479       O  
ATOM   3355  N   LYS A 405     -18.535 -21.087 -59.269  1.00 39.14           N  
ANISOU 3355  N   LYS A 405     5352   5667   3853   -735   -296     75       N  
ATOM   3356  CA  LYS A 405     -18.175 -22.480 -59.521  1.00 40.26           C  
ANISOU 3356  CA  LYS A 405     5522   5802   3975   -778   -256     -2       C  
ATOM   3357  C   LYS A 405     -16.674 -22.661 -59.776  1.00 40.34           C  
ANISOU 3357  C   LYS A 405     5571   5786   3971   -780   -211    -53       C  
ATOM   3358  O   LYS A 405     -15.987 -23.319 -58.994  1.00 40.62           O  
ANISOU 3358  O   LYS A 405     5621   5764   4051   -747   -166    -95       O  
ATOM   3359  CB  LYS A 405     -19.006 -23.047 -60.674  1.00 41.03           C  
ANISOU 3359  CB  LYS A 405     5613   5964   4012   -865   -283     -9       C  
ATOM   3360  CG  LYS A 405     -18.956 -24.572 -60.786  1.00 45.72           C  
ANISOU 3360  CG  LYS A 405     6227   6545   4599   -910   -239    -89       C  
ATOM   3361  CD  LYS A 405     -19.883 -25.087 -61.887  1.00 48.72           C  
ANISOU 3361  CD  LYS A 405     6601   6994   4917  -1002   -269    -96       C  
ATOM   3362  CE  LYS A 405     -19.880 -26.623 -61.959  1.00 52.22           C  
ANISOU 3362  CE  LYS A 405     7062   7418   5360  -1047   -219   -180       C  
ATOM   3363  NZ  LYS A 405     -20.487 -27.158 -63.227  1.00 53.32           N  
ANISOU 3363  NZ  LYS A 405     7209   7628   5422  -1156   -238   -205       N  
ATOM   3364  N   TYR A 406     -16.179 -22.077 -60.865  1.00 39.98           N  
ANISOU 3364  N   TYR A 406     5540   5782   3869   -822   -222    -46       N  
ATOM   3365  CA  TYR A 406     -14.772 -22.158 -61.225  1.00 39.90           C  
ANISOU 3365  CA  TYR A 406     5564   5751   3846   -829   -177    -93       C  
ATOM   3366  C   TYR A 406     -14.088 -20.819 -60.962  1.00 40.91           C  
ANISOU 3366  C   TYR A 406     5690   5865   3989   -776   -191    -45       C  
ATOM   3367  O   TYR A 406     -14.561 -19.766 -61.408  1.00 40.86           O  
ANISOU 3367  O   TYR A 406     5667   5900   3956   -782   -238     18       O  
ATOM   3368  CB  TYR A 406     -14.611 -22.606 -62.691  1.00 40.42           C  
ANISOU 3368  CB  TYR A 406     5655   5871   3831   -926   -166   -134       C  
ATOM   3369  CG  TYR A 406     -15.049 -24.050 -62.926  1.00 42.78           C  
ANISOU 3369  CG  TYR A 406     5962   6172   4122   -981   -136   -200       C  
ATOM   3370  CD1 TYR A 406     -16.266 -24.348 -63.551  1.00 41.59           C  
ANISOU 3370  CD1 TYR A 406     5798   6082   3922  -1046   -175   -186       C  
ATOM   3371  CD2 TYR A 406     -14.253 -25.120 -62.502  1.00 40.02           C  
ANISOU 3371  CD2 TYR A 406     5627   5758   3819   -970    -68   -273       C  
ATOM   3372  CE1 TYR A 406     -16.671 -25.681 -63.756  1.00 39.14           C  
ANISOU 3372  CE1 TYR A 406     5496   5771   3606  -1099   -144   -251       C  
ATOM   3373  CE2 TYR A 406     -14.644 -26.443 -62.707  1.00 37.71           C  
ANISOU 3373  CE2 TYR A 406     5339   5460   3527  -1020    -34   -335       C  
ATOM   3374  CZ  TYR A 406     -15.847 -26.719 -63.327  1.00 40.42           C  
ANISOU 3374  CZ  TYR A 406     5675   5866   3818  -1085    -71   -327       C  
ATOM   3375  OH  TYR A 406     -16.219 -28.037 -63.507  1.00 41.62           O  
ANISOU 3375  OH  TYR A 406     5832   6009   3973  -1136    -34   -392       O  
ATOM   3376  N   VAL A 407     -12.979 -20.862 -60.224  1.00 39.06           N  
ANISOU 3376  N   VAL A 407     5469   5570   3801   -726   -151    -72       N  
ATOM   3377  CA  VAL A 407     -12.268 -19.646 -59.815  1.00 36.74           C  
ANISOU 3377  CA  VAL A 407     5174   5255   3529   -673   -160    -33       C  
ATOM   3378  C   VAL A 407     -10.764 -19.835 -59.918  1.00 36.93           C  
ANISOU 3378  C   VAL A 407     5224   5243   3565   -668   -112    -81       C  
ATOM   3379  O   VAL A 407     -10.217 -20.827 -59.419  1.00 34.47           O  
ANISOU 3379  O   VAL A 407     4919   4883   3292   -658    -71   -130       O  
ATOM   3380  CB  VAL A 407     -12.628 -19.213 -58.362  1.00 35.52           C  
ANISOU 3380  CB  VAL A 407     5001   5058   3439   -597   -172      2       C  
ATOM   3381  CG1 VAL A 407     -11.801 -17.989 -57.917  1.00 29.80           C  
ANISOU 3381  CG1 VAL A 407     4279   4308   2738   -547   -174     33       C  
ATOM   3382  CG2 VAL A 407     -14.115 -18.924 -58.230  1.00 34.95           C  
ANISOU 3382  CG2 VAL A 407     4897   5015   3368   -597   -213     52       C  
ATOM   3383  N   MET A 408     -10.114 -18.881 -60.583  1.00 37.55           N  
ANISOU 3383  N   MET A 408     5312   5341   3613   -677   -118    -61       N  
ATOM   3384  CA  MET A 408      -8.659 -18.764 -60.582  1.00 37.77           C  
ANISOU 3384  CA  MET A 408     5358   5331   3663   -661    -77    -93       C  
ATOM   3385  C   MET A 408      -8.267 -17.443 -59.952  1.00 35.72           C  
ANISOU 3385  C   MET A 408     5089   5052   3431   -601    -99    -41       C  
ATOM   3386  O   MET A 408      -8.707 -16.375 -60.407  1.00 33.53           O  
ANISOU 3386  O   MET A 408     4804   4813   3124   -606   -136     13       O  
ATOM   3387  CB  MET A 408      -8.100 -18.749 -62.000  1.00 40.14           C  
ANISOU 3387  CB  MET A 408     5682   5671   3900   -731    -55   -122       C  
ATOM   3388  CG  MET A 408      -8.638 -19.783 -62.944  1.00 50.92           C  
ANISOU 3388  CG  MET A 408     7060   7075   5212   -812    -39   -168       C  
ATOM   3389  SD  MET A 408      -7.556 -19.847 -64.388  1.00 61.05           S  
ANISOU 3389  SD  MET A 408     8378   8383   6435   -890     12   -221       S  
ATOM   3390  CE  MET A 408      -6.168 -20.667 -63.595  1.00 52.59           C  
ANISOU 3390  CE  MET A 408     7306   7216   5460   -842     87   -288       C  
ATOM   3391  N   SER A 409      -7.407 -17.501 -58.942  1.00 33.68           N  
ANISOU 3391  N   SER A 409     4831   4734   3231   -550    -78    -55       N  
ATOM   3392  CA  SER A 409      -6.899 -16.280 -58.335  1.00 31.50           C  
ANISOU 3392  CA  SER A 409     4550   4437   2982   -499    -92    -15       C  
ATOM   3393  C   SER A 409      -5.484 -15.979 -58.801  1.00 32.55           C  
ANISOU 3393  C   SER A 409     4698   4553   3119   -503    -62    -38       C  
ATOM   3394  O   SER A 409      -4.710 -16.890 -59.111  1.00 33.55           O  
ANISOU 3394  O   SER A 409     4834   4658   3256   -526    -21    -91       O  
ATOM   3395  CB  SER A 409      -6.966 -16.348 -56.801  1.00 28.50           C  
ANISOU 3395  CB  SER A 409     4161   4008   2659   -441    -97     -5       C  
ATOM   3396  OG  SER A 409      -5.987 -17.226 -56.283  1.00 27.20           O  
ANISOU 3396  OG  SER A 409     4004   3796   2536   -430    -65    -46       O  
ATOM   3397  N   PHE A 410      -5.163 -14.689 -58.860  1.00 32.70           N  
ANISOU 3397  N   PHE A 410     4715   4577   3134   -482    -79      3       N  
ATOM   3398  CA  PHE A 410      -3.808 -14.225 -59.128  1.00 32.91           C  
ANISOU 3398  CA  PHE A 410     4751   4582   3172   -478    -54    -12       C  
ATOM   3399  C   PHE A 410      -3.376 -13.259 -58.031  1.00 33.71           C  
ANISOU 3399  C   PHE A 410     4844   4645   3320   -418    -68     20       C  
ATOM   3400  O   PHE A 410      -4.200 -12.553 -57.453  1.00 33.25           O  
ANISOU 3400  O   PHE A 410     4774   4592   3268   -390    -99     63       O  
ATOM   3401  CB  PHE A 410      -3.717 -13.571 -60.511  1.00 30.90           C  
ANISOU 3401  CB  PHE A 410     4508   4377   2857   -526    -55      3       C  
ATOM   3402  CG  PHE A 410      -4.043 -14.511 -61.648  1.00 31.26           C  
ANISOU 3402  CG  PHE A 410     4568   4464   2846   -598    -37    -36       C  
ATOM   3403  CD1 PHE A 410      -5.355 -14.902 -61.894  1.00 30.78           C  
ANISOU 3403  CD1 PHE A 410     4501   4444   2748   -627    -67    -20       C  
ATOM   3404  CD2 PHE A 410      -3.035 -15.000 -62.477  1.00 29.72           C  
ANISOU 3404  CD2 PHE A 410     4393   4264   2636   -641     15    -90       C  
ATOM   3405  CE1 PHE A 410      -5.657 -15.774 -62.932  1.00 36.79           C  
ANISOU 3405  CE1 PHE A 410     5278   5246   3453   -701    -50    -58       C  
ATOM   3406  CE2 PHE A 410      -3.327 -15.867 -63.517  1.00 34.97           C  
ANISOU 3406  CE2 PHE A 410     5075   4966   3246   -716     39   -133       C  
ATOM   3407  CZ  PHE A 410      -4.642 -16.255 -63.750  1.00 34.46           C  
ANISOU 3407  CZ  PHE A 410     5007   4948   3138   -748      5   -118       C  
ATOM   3408  N   ASP A 411      -2.076 -13.231 -57.757  1.00 35.15           N  
ANISOU 3408  N   ASP A 411     5030   4787   3538   -401    -43     -3       N  
ATOM   3409  CA  ASP A 411      -1.542 -12.496 -56.623  1.00 37.86           C  
ANISOU 3409  CA  ASP A 411     5368   5091   3927   -351    -54     18       C  
ATOM   3410  C   ASP A 411      -0.165 -11.892 -56.944  1.00 38.47           C  
ANISOU 3410  C   ASP A 411     5448   5148   4022   -348    -34     10       C  
ATOM   3411  O   ASP A 411       0.714 -12.559 -57.493  1.00 40.80           O  
ANISOU 3411  O   ASP A 411     5746   5429   4328   -370      0    -29       O  
ATOM   3412  CB  ASP A 411      -1.469 -13.431 -55.402  1.00 38.84           C  
ANISOU 3412  CB  ASP A 411     5487   5175   4096   -327    -53      1       C  
ATOM   3413  CG  ASP A 411      -0.737 -12.818 -54.239  1.00 41.44           C  
ANISOU 3413  CG  ASP A 411     5814   5464   4466   -288    -64     16       C  
ATOM   3414  OD1 ASP A 411       0.511 -12.794 -54.255  1.00 47.18           O  
ANISOU 3414  OD1 ASP A 411     6539   6163   5224   -284    -48      1       O  
ATOM   3415  OD2 ASP A 411      -1.401 -12.353 -53.295  1.00 48.42           O  
ANISOU 3415  OD2 ASP A 411     6698   6345   5353   -264    -86     41       O  
ATOM   3416  N   LEU A 412       0.009 -10.625 -56.586  1.00 37.92           N  
ANISOU 3416  N   LEU A 412     5376   5072   3960   -321    -51     45       N  
ATOM   3417  CA  LEU A 412       1.273  -9.934 -56.773  1.00 38.21           C  
ANISOU 3417  CA  LEU A 412     5414   5088   4017   -314    -35     42       C  
ATOM   3418  C   LEU A 412       2.272 -10.340 -55.700  1.00 37.59           C  
ANISOU 3418  C   LEU A 412     5328   4957   3996   -287    -29     23       C  
ATOM   3419  O   LEU A 412       1.973 -10.264 -54.506  1.00 39.90           O  
ANISOU 3419  O   LEU A 412     5618   5231   4309   -259    -52     37       O  
ATOM   3420  CB  LEU A 412       1.051  -8.421 -56.749  1.00 38.71           C  
ANISOU 3420  CB  LEU A 412     5474   5160   4072   -296    -55     88       C  
ATOM   3421  CG  LEU A 412       0.490  -7.833 -58.046  1.00 39.64           C  
ANISOU 3421  CG  LEU A 412     5595   5326   4139   -328    -61    116       C  
ATOM   3422  CD1 LEU A 412      -0.342  -6.590 -57.778  1.00 40.43           C  
ANISOU 3422  CD1 LEU A 412     5683   5434   4242   -305    -90    172       C  
ATOM   3423  CD2 LEU A 412       1.626  -7.526 -59.003  1.00 38.53           C  
ANISOU 3423  CD2 LEU A 412     5463   5188   3988   -353    -33    103       C  
ATOM   3424  N   THR A 413       3.445 -10.791 -56.139  1.00 34.90           N  
ANISOU 3424  N   THR A 413     4983   4593   3683   -300      2     -8       N  
ATOM   3425  CA  THR A 413       4.547 -11.143 -55.252  1.00 34.03           C  
ANISOU 3425  CA  THR A 413     4859   4432   3637   -278      5    -20       C  
ATOM   3426  C   THR A 413       4.968  -9.934 -54.431  1.00 32.88           C  
ANISOU 3426  C   THR A 413     4713   4271   3507   -249    -20     11       C  
ATOM   3427  O   THR A 413       5.302  -8.882 -54.986  1.00 31.16           O  
ANISOU 3427  O   THR A 413     4499   4064   3276   -251    -14     22       O  
ATOM   3428  CB  THR A 413       5.761 -11.614 -56.065  1.00 35.05           C  
ANISOU 3428  CB  THR A 413     4978   4537   3800   -298     49    -55       C  
ATOM   3429  OG1 THR A 413       5.369 -12.711 -56.892  1.00 40.91           O  
ANISOU 3429  OG1 THR A 413     5725   5293   4527   -333     81    -91       O  
ATOM   3430  CG2 THR A 413       6.901 -12.052 -55.153  1.00 30.78           C  
ANISOU 3430  CG2 THR A 413     4415   3941   3339   -276     48    -60       C  
ATOM   3431  N   SER A 414       4.929 -10.097 -53.108  1.00 32.61           N  
ANISOU 3431  N   SER A 414     4677   4215   3499   -227    -47     23       N  
ATOM   3432  CA  SER A 414       5.451  -9.109 -52.161  1.00 32.20           C  
ANISOU 3432  CA  SER A 414     4625   4144   3465   -207    -69     43       C  
ATOM   3433  C   SER A 414       5.124  -7.667 -52.564  1.00 30.79           C  
ANISOU 3433  C   SER A 414     4456   3986   3257   -203    -69     63       C  
ATOM   3434  O   SER A 414       6.022  -6.888 -52.879  1.00 31.87           O  
ANISOU 3434  O   SER A 414     4589   4111   3409   -201    -60     65       O  
ATOM   3435  CB  SER A 414       6.959  -9.308 -52.013  1.00 31.65           C  
ANISOU 3435  CB  SER A 414     4537   4035   3452   -206    -62     34       C  
ATOM   3436  OG  SER A 414       7.466  -8.575 -50.926  1.00 42.71           O  
ANISOU 3436  OG  SER A 414     5939   5418   4870   -193    -90     52       O  
ATOM   3437  N   LEU A 415       3.840  -7.316 -52.548  1.00 29.01           N  
ANISOU 3437  N   LEU A 415     4239   3787   2997   -200    -78     81       N  
ATOM   3438  CA  LEU A 415       3.391  -6.073 -53.180  1.00 27.70           C  
ANISOU 3438  CA  LEU A 415     4075   3641   2808   -198    -76    106       C  
ATOM   3439  C   LEU A 415       4.064  -4.789 -52.683  1.00 27.44           C  
ANISOU 3439  C   LEU A 415     4042   3584   2799   -182    -77    118       C  
ATOM   3440  O   LEU A 415       4.707  -4.084 -53.466  1.00 26.59           O  
ANISOU 3440  O   LEU A 415     3931   3478   2694   -187    -64    125       O  
ATOM   3441  CB  LEU A 415       1.866  -5.928 -53.170  1.00 26.64           C  
ANISOU 3441  CB  LEU A 415     3942   3534   2648   -195    -87    128       C  
ATOM   3442  CG  LEU A 415       1.447  -4.628 -53.890  1.00 31.62           C  
ANISOU 3442  CG  LEU A 415     4566   4180   3269   -193    -87    163       C  
ATOM   3443  CD1 LEU A 415       1.781  -4.673 -55.384  1.00 25.73           C  
ANISOU 3443  CD1 LEU A 415     3819   3462   2494   -221    -77    167       C  
ATOM   3444  CD2 LEU A 415      -0.012  -4.263 -53.668  1.00 30.84           C  
ANISOU 3444  CD2 LEU A 415     4458   4095   3165   -184    -99    193       C  
ATOM   3445  N   TYR A 416       3.912  -4.471 -51.403  1.00 27.43           N  
ANISOU 3445  N   TYR A 416     4047   3564   2812   -169    -90    120       N  
ATOM   3446  CA  TYR A 416       4.405  -3.192 -50.911  1.00 27.51           C  
ANISOU 3446  CA  TYR A 416     4059   3553   2841   -159    -88    128       C  
ATOM   3447  C   TYR A 416       5.924  -3.045 -51.039  1.00 27.19           C  
ANISOU 3447  C   TYR A 416     4014   3491   2828   -164    -84    117       C  
ATOM   3448  O   TYR A 416       6.385  -1.981 -51.439  1.00 24.75           O  
ANISOU 3448  O   TYR A 416     3701   3175   2529   -161    -73    126       O  
ATOM   3449  CB  TYR A 416       3.906  -2.899 -49.485  1.00 27.55           C  
ANISOU 3449  CB  TYR A 416     4076   3542   2849   -154    -97    126       C  
ATOM   3450  CG  TYR A 416       2.470  -2.423 -49.433  1.00 24.68           C  
ANISOU 3450  CG  TYR A 416     3712   3190   2476   -145    -88    142       C  
ATOM   3451  CD1 TYR A 416       1.622  -2.591 -50.523  1.00 25.01           C  
ANISOU 3451  CD1 TYR A 416     3742   3260   2503   -144    -86    161       C  
ATOM   3452  CD2 TYR A 416       1.954  -1.820 -48.289  1.00 27.82           C  
ANISOU 3452  CD2 TYR A 416     4119   3570   2881   -142    -81    137       C  
ATOM   3453  CE1 TYR A 416       0.303  -2.169 -50.486  1.00 25.04           C  
ANISOU 3453  CE1 TYR A 416     3736   3270   2508   -136    -82    182       C  
ATOM   3454  CE2 TYR A 416       0.623  -1.402 -48.238  1.00 30.81           C  
ANISOU 3454  CE2 TYR A 416     4491   3952   3264   -133    -67    151       C  
ATOM   3455  CZ  TYR A 416      -0.192  -1.586 -49.348  1.00 26.92           C  
ANISOU 3455  CZ  TYR A 416     3980   3485   2765   -128    -70    177       C  
ATOM   3456  OH  TYR A 416      -1.505  -1.179 -49.329  1.00 28.95           O  
ANISOU 3456  OH  TYR A 416     4222   3743   3036   -119    -60    197       O  
ATOM   3457  N   PRO A 417       6.701  -4.110 -50.719  1.00 28.43           N  
ANISOU 3457  N   PRO A 417     4165   3635   3003   -170    -93     99       N  
ATOM   3458  CA  PRO A 417       8.149  -3.997 -50.909  1.00 29.43           C  
ANISOU 3458  CA  PRO A 417     4279   3738   3166   -174    -88     91       C  
ATOM   3459  C   PRO A 417       8.529  -3.841 -52.380  1.00 30.21           C  
ANISOU 3459  C   PRO A 417     4369   3847   3261   -182    -58     87       C  
ATOM   3460  O   PRO A 417       9.476  -3.111 -52.694  1.00 29.25           O  
ANISOU 3460  O   PRO A 417     4241   3711   3162   -183    -47     87       O  
ATOM   3461  CB  PRO A 417       8.685  -5.321 -50.346  1.00 29.35           C  
ANISOU 3461  CB  PRO A 417     4258   3711   3184   -179   -103     80       C  
ATOM   3462  CG  PRO A 417       7.659  -5.750 -49.368  1.00 27.35           C  
ANISOU 3462  CG  PRO A 417     4019   3468   2906   -178   -124     86       C  
ATOM   3463  CD  PRO A 417       6.356  -5.352 -49.997  1.00 30.32           C  
ANISOU 3463  CD  PRO A 417     4406   3873   3241   -174   -109     91       C  
ATOM   3464  N   SER A 418       7.786  -4.510 -53.263  1.00 29.86           N  
ANISOU 3464  N   SER A 418     4329   3830   3187   -192    -45     83       N  
ATOM   3465  CA  SER A 418       8.001  -4.397 -54.701  1.00 28.90           C  
ANISOU 3465  CA  SER A 418     4207   3728   3048   -211    -16     79       C  
ATOM   3466  C   SER A 418       7.617  -3.018 -55.230  1.00 30.05           C  
ANISOU 3466  C   SER A 418     4358   3890   3170   -209    -15    110       C  
ATOM   3467  O   SER A 418       8.208  -2.555 -56.189  1.00 32.21           O  
ANISOU 3467  O   SER A 418     4631   4169   3439   -223      7    112       O  
ATOM   3468  CB  SER A 418       7.229  -5.478 -55.453  1.00 28.69           C  
ANISOU 3468  CB  SER A 418     4185   3730   2987   -231     -6     65       C  
ATOM   3469  OG  SER A 418       7.635  -6.759 -55.009  1.00 30.68           O  
ANISOU 3469  OG  SER A 418     4428   3960   3272   -232     -2     38       O  
ATOM   3470  N   ILE A 419       6.623  -2.371 -54.617  1.00 31.92           N  
ANISOU 3470  N   ILE A 419     4599   4132   3396   -193    -34    134       N  
ATOM   3471  CA  ILE A 419       6.231  -1.023 -55.020  1.00 30.94           C  
ANISOU 3471  CA  ILE A 419     4474   4016   3267   -187    -33    169       C  
ATOM   3472  C   ILE A 419       7.362  -0.069 -54.637  1.00 31.81           C  
ANISOU 3472  C   ILE A 419     4581   4092   3414   -178    -24    166       C  
ATOM   3473  O   ILE A 419       7.764   0.780 -55.430  1.00 31.78           O  
ANISOU 3473  O   ILE A 419     4574   4089   3412   -184    -10    184       O  
ATOM   3474  CB  ILE A 419       4.886  -0.573 -54.388  1.00 32.36           C  
ANISOU 3474  CB  ILE A 419     4653   4200   3443   -171    -48    194       C  
ATOM   3475  CG1 ILE A 419       3.719  -1.388 -54.963  1.00 30.57           C  
ANISOU 3475  CG1 ILE A 419     4426   4011   3179   -183    -58    204       C  
ATOM   3476  CG2 ILE A 419       4.633   0.926 -54.641  1.00 31.81           C  
ANISOU 3476  CG2 ILE A 419     4575   4122   3389   -161    -43    231       C  
ATOM   3477  CD1 ILE A 419       2.380  -1.130 -54.278  1.00 31.03           C  
ANISOU 3477  CD1 ILE A 419     4479   4071   3242   -167    -71    224       C  
ATOM   3478  N   ILE A 420       7.883  -0.249 -53.429  1.00 29.42           N  
ANISOU 3478  N   ILE A 420     4279   3761   3139   -168    -35    146       N  
ATOM   3479  CA  ILE A 420       9.043   0.496 -52.944  1.00 30.44           C  
ANISOU 3479  CA  ILE A 420     4404   3858   3305   -165    -32    138       C  
ATOM   3480  C   ILE A 420      10.230   0.402 -53.909  1.00 31.08           C  
ANISOU 3480  C   ILE A 420     4474   3934   3401   -178    -12    129       C  
ATOM   3481  O   ILE A 420      10.891   1.406 -54.189  1.00 27.47           O  
ANISOU 3481  O   ILE A 420     4012   3461   2962   -178      1    137       O  
ATOM   3482  CB  ILE A 420       9.463   0.029 -51.519  1.00 28.35           C  
ANISOU 3482  CB  ILE A 420     4141   3570   3059   -164    -55    119       C  
ATOM   3483  CG1 ILE A 420       8.408   0.475 -50.488  1.00 27.87           C  
ANISOU 3483  CG1 ILE A 420     4095   3510   2985   -157    -65    124       C  
ATOM   3484  CG2 ILE A 420      10.863   0.563 -51.160  1.00 27.95           C  
ANISOU 3484  CG2 ILE A 420     4081   3490   3047   -168    -57    110       C  
ATOM   3485  CD1 ILE A 420       8.619  -0.040 -49.050  1.00 25.10           C  
ANISOU 3485  CD1 ILE A 420     3753   3146   2637   -165    -90    109       C  
ATOM   3486  N   ARG A 421      10.475  -0.802 -54.422  1.00 29.85           N  
ANISOU 3486  N   ARG A 421     4314   3787   3241   -190     -3    110       N  
ATOM   3487  CA  ARG A 421      11.592  -1.041 -55.326  1.00 30.87           C  
ANISOU 3487  CA  ARG A 421     4432   3907   3390   -205     26     93       C  
ATOM   3488  C   ARG A 421      11.293  -0.521 -56.740  1.00 32.70           C  
ANISOU 3488  C   ARG A 421     4674   4169   3583   -224     52    108       C  
ATOM   3489  O   ARG A 421      12.130   0.147 -57.343  1.00 32.81           O  
ANISOU 3489  O   ARG A 421     4684   4174   3611   -233     75    110       O  
ATOM   3490  CB  ARG A 421      11.953  -2.528 -55.360  1.00 28.06           C  
ANISOU 3490  CB  ARG A 421     4066   3543   3053   -214     34     64       C  
ATOM   3491  CG  ARG A 421      12.370  -3.122 -54.010  1.00 32.49           C  
ANISOU 3491  CG  ARG A 421     4613   4074   3656   -201      4     58       C  
ATOM   3492  CD  ARG A 421      12.371  -4.640 -54.071  1.00 33.33           C  
ANISOU 3492  CD  ARG A 421     4708   4174   3780   -208     11     37       C  
ATOM   3493  NE  ARG A 421      13.300  -5.128 -55.089  1.00 32.75           N  
ANISOU 3493  NE  ARG A 421     4618   4085   3740   -224     55     11       N  
ATOM   3494  CZ  ARG A 421      13.157  -6.263 -55.769  1.00 34.99           C  
ANISOU 3494  CZ  ARG A 421     4899   4372   4025   -241     86    -16       C  
ATOM   3495  NH1 ARG A 421      12.110  -7.058 -55.556  1.00 32.28           N  
ANISOU 3495  NH1 ARG A 421     4566   4047   3651   -242     73    -17       N  
ATOM   3496  NH2 ARG A 421      14.065  -6.598 -56.677  1.00 32.49           N  
ANISOU 3496  NH2 ARG A 421     4566   4036   3742   -259    136    -44       N  
ATOM   3497  N   GLN A 422      10.102  -0.824 -57.255  1.00 31.55           N  
ANISOU 3497  N   GLN A 422     4539   4060   3386   -233     46    122       N  
ATOM   3498  CA  GLN A 422       9.688  -0.359 -58.577  1.00 30.25           C  
ANISOU 3498  CA  GLN A 422     4385   3933   3176   -259     61    146       C  
ATOM   3499  C   GLN A 422       9.711   1.167 -58.682  1.00 30.97           C  
ANISOU 3499  C   GLN A 422     4475   4017   3276   -248     57    186       C  
ATOM   3500  O   GLN A 422      10.259   1.722 -59.629  1.00 33.78           O  
ANISOU 3500  O   GLN A 422     4833   4380   3622   -268     79    197       O  
ATOM   3501  CB  GLN A 422       8.281  -0.870 -58.913  1.00 29.38           C  
ANISOU 3501  CB  GLN A 422     4284   3864   3015   -270     43    162       C  
ATOM   3502  CG  GLN A 422       7.659  -0.236 -60.181  1.00 29.21           C  
ANISOU 3502  CG  GLN A 422     4270   3886   2942   -299     43    203       C  
ATOM   3503  CD  GLN A 422       6.756  -1.201 -60.935  1.00 31.97           C  
ANISOU 3503  CD  GLN A 422     4630   4282   3233   -333     38    200       C  
ATOM   3504  OE1 GLN A 422       6.853  -2.417 -60.760  1.00 31.75           O  
ANISOU 3504  OE1 GLN A 422     4606   4252   3205   -342     50    156       O  
ATOM   3505  NE2 GLN A 422       5.865  -0.662 -61.769  1.00 27.75           N  
ANISOU 3505  NE2 GLN A 422     4099   3790   2652   -356     19    249       N  
ATOM   3506  N   VAL A 423       9.096   1.833 -57.710  1.00 30.14           N  
ANISOU 3506  N   VAL A 423     4364   3896   3190   -219     33    206       N  
ATOM   3507  CA  VAL A 423       8.924   3.279 -57.756  1.00 32.84           C  
ANISOU 3507  CA  VAL A 423     4701   4227   3549   -207     32    246       C  
ATOM   3508  C   VAL A 423      10.185   3.996 -57.276  1.00 33.71           C  
ANISOU 3508  C   VAL A 423     4806   4297   3707   -198     47    230       C  
ATOM   3509  O   VAL A 423      10.417   5.135 -57.653  1.00 35.17           O  
ANISOU 3509  O   VAL A 423     4986   4470   3907   -197     58    257       O  
ATOM   3510  CB  VAL A 423       7.686   3.742 -56.928  1.00 31.02           C  
ANISOU 3510  CB  VAL A 423     4466   3991   3329   -183     11    270       C  
ATOM   3511  CG1 VAL A 423       7.553   5.260 -56.945  1.00 33.90           C  
ANISOU 3511  CG1 VAL A 423     4820   4334   3727   -170     18    310       C  
ATOM   3512  CG2 VAL A 423       6.411   3.103 -57.466  1.00 31.54           C  
ANISOU 3512  CG2 VAL A 423     4533   4099   3353   -194     -6    292       C  
ATOM   3513  N   ASN A 424      10.993   3.304 -56.472  1.00 33.27           N  
ANISOU 3513  N   ASN A 424     4747   4218   3677   -194     44    190       N  
ATOM   3514  CA  ASN A 424      12.174   3.869 -55.811  1.00 34.99           C  
ANISOU 3514  CA  ASN A 424     4957   4396   3942   -187     49    173       C  
ATOM   3515  C   ASN A 424      11.791   4.831 -54.679  1.00 35.46           C  
ANISOU 3515  C   ASN A 424     5018   4432   4024   -169     35    181       C  
ATOM   3516  O   ASN A 424      12.302   5.950 -54.584  1.00 35.36           O  
ANISOU 3516  O   ASN A 424     5000   4394   4040   -166     47    189       O  
ATOM   3517  CB  ASN A 424      13.161   4.505 -56.809  1.00 34.82           C  
ANISOU 3517  CB  ASN A 424     4930   4368   3934   -201     79    179       C  
ATOM   3518  CG  ASN A 424      14.579   4.634 -56.238  1.00 38.29           C  
ANISOU 3518  CG  ASN A 424     5354   4769   4425   -200     84    153       C  
ATOM   3519  OD1 ASN A 424      15.052   3.774 -55.487  1.00 38.44           O  
ANISOU 3519  OD1 ASN A 424     5364   4773   4466   -198     69    127       O  
ATOM   3520  ND2 ASN A 424      15.256   5.714 -56.593  1.00 38.20           N  
ANISOU 3520  ND2 ASN A 424     5337   4740   4438   -203    103    164       N  
ATOM   3521  N   ILE A 425      10.891   4.365 -53.816  1.00 36.34           N  
ANISOU 3521  N   ILE A 425     5136   4549   4121   -160     15    176       N  
ATOM   3522  CA  ILE A 425      10.380   5.155 -52.698  1.00 35.76           C  
ANISOU 3522  CA  ILE A 425     5068   4454   4064   -150     10    176       C  
ATOM   3523  C   ILE A 425      11.365   5.115 -51.529  1.00 35.92           C  
ANISOU 3523  C   ILE A 425     5092   4449   4109   -158     -3    145       C  
ATOM   3524  O   ILE A 425      11.600   4.058 -50.939  1.00 36.20           O  
ANISOU 3524  O   ILE A 425     5128   4489   4136   -164    -25    127       O  
ATOM   3525  CB  ILE A 425       8.954   4.686 -52.280  1.00 35.68           C  
ANISOU 3525  CB  ILE A 425     5066   4462   4029   -142     -1    183       C  
ATOM   3526  CG1 ILE A 425       7.947   5.029 -53.380  1.00 34.05           C  
ANISOU 3526  CG1 ILE A 425     4852   4279   3808   -137      7    223       C  
ATOM   3527  CG2 ILE A 425       8.502   5.344 -50.964  1.00 33.66           C  
ANISOU 3527  CG2 ILE A 425     4819   4181   3790   -137      1    170       C  
ATOM   3528  CD1 ILE A 425       6.714   4.136 -53.405  1.00 33.33           C  
ANISOU 3528  CD1 ILE A 425     4763   4217   3686   -135     -8    230       C  
ATOM   3529  N   SER A 426      11.936   6.277 -51.215  1.00 34.00           N  
ANISOU 3529  N   SER A 426     4846   4177   3894   -160      9    143       N  
ATOM   3530  CA  SER A 426      12.950   6.421 -50.168  1.00 34.50           C  
ANISOU 3530  CA  SER A 426     4911   4217   3980   -175     -5    117       C  
ATOM   3531  C   SER A 426      12.992   7.882 -49.710  1.00 35.12           C  
ANISOU 3531  C   SER A 426     4994   4266   4084   -178     15    114       C  
ATOM   3532  O   SER A 426      12.660   8.778 -50.488  1.00 36.27           O  
ANISOU 3532  O   SER A 426     5133   4403   4244   -166     42    136       O  
ATOM   3533  CB  SER A 426      14.328   6.004 -50.701  1.00 35.57           C  
ANISOU 3533  CB  SER A 426     5028   4347   4139   -182     -9    112       C  
ATOM   3534  OG  SER A 426      15.212   5.604 -49.660  1.00 36.26           O  
ANISOU 3534  OG  SER A 426     5111   4421   4244   -199    -39     94       O  
ATOM   3535  N   PRO A 427      13.381   8.131 -48.444  1.00 34.80           N  
ANISOU 3535  N   PRO A 427     4965   4209   4048   -199      2     87       N  
ATOM   3536  CA  PRO A 427      13.492   9.495 -47.919  1.00 35.39           C  
ANISOU 3536  CA  PRO A 427     5046   4252   4148   -209     27     74       C  
ATOM   3537  C   PRO A 427      14.347  10.430 -48.778  1.00 37.10           C  
ANISOU 3537  C   PRO A 427     5245   4447   4404   -204     49     86       C  
ATOM   3538  O   PRO A 427      14.012  11.608 -48.931  1.00 38.04           O  
ANISOU 3538  O   PRO A 427     5363   4541   4549   -198     83     92       O  
ATOM   3539  CB  PRO A 427      14.166   9.296 -46.549  1.00 36.56           C  
ANISOU 3539  CB  PRO A 427     5209   4396   4286   -244     -2     42       C  
ATOM   3540  CG  PRO A 427      14.549   7.814 -46.483  1.00 35.91           C  
ANISOU 3540  CG  PRO A 427     5120   4340   4183   -247    -45     49       C  
ATOM   3541  CD  PRO A 427      13.571   7.135 -47.377  1.00 35.66           C  
ANISOU 3541  CD  PRO A 427     5085   4330   4134   -218    -35     69       C  
ATOM   3542  N   GLU A 428      15.444   9.912 -49.325  1.00 35.48           N  
ANISOU 3542  N   GLU A 428     5024   4248   4208   -207     34     90       N  
ATOM   3543  CA  GLU A 428      16.405  10.762 -50.018  1.00 37.17           C  
ANISOU 3543  CA  GLU A 428     5222   4440   4460   -209     55     97       C  
ATOM   3544  C   GLU A 428      16.205  10.767 -51.534  1.00 37.45           C  
ANISOU 3544  C   GLU A 428     5245   4489   4494   -190     78    130       C  
ATOM   3545  O   GLU A 428      16.936  11.456 -52.254  1.00 38.72           O  
ANISOU 3545  O   GLU A 428     5395   4635   4683   -191    100    141       O  
ATOM   3546  CB  GLU A 428      17.850  10.382 -49.641  1.00 36.16           C  
ANISOU 3546  CB  GLU A 428     5080   4305   4355   -229     30     80       C  
ATOM   3547  CG  GLU A 428      18.430   9.149 -50.348  1.00 31.86           C  
ANISOU 3547  CG  GLU A 428     4516   3777   3812   -223     17     87       C  
ATOM   3548  CD  GLU A 428      17.873   7.834 -49.816  1.00 32.37           C  
ANISOU 3548  CD  GLU A 428     4588   3866   3846   -222    -15     84       C  
ATOM   3549  OE1 GLU A 428      16.750   7.826 -49.278  1.00 32.31           O  
ANISOU 3549  OE1 GLU A 428     4602   3870   3803   -219    -19     82       O  
ATOM   3550  OE2 GLU A 428      18.557   6.801 -49.936  1.00 35.14           O  
ANISOU 3550  OE2 GLU A 428     4919   4219   4212   -225    -33     83       O  
ATOM   3551  N   THR A 429      15.219  10.003 -52.011  1.00 36.23           N  
ANISOU 3551  N   THR A 429     5098   4365   4304   -177     74    147       N  
ATOM   3552  CA  THR A 429      14.933   9.935 -53.454  1.00 34.53           C  
ANISOU 3552  CA  THR A 429     4875   4170   4074   -170     91    180       C  
ATOM   3553  C   THR A 429      13.748  10.800 -53.871  1.00 31.92           C  
ANISOU 3553  C   THR A 429     4546   3839   3741   -156    107    217       C  
ATOM   3554  O   THR A 429      13.392  10.826 -55.039  1.00 34.00           O  
ANISOU 3554  O   THR A 429     4805   4125   3988   -155    116    253       O  
ATOM   3555  CB  THR A 429      14.739   8.487 -53.978  1.00 33.96           C  
ANISOU 3555  CB  THR A 429     4804   4134   3964   -172     77    177       C  
ATOM   3556  OG1 THR A 429      13.659   7.856 -53.279  1.00 36.51           O  
ANISOU 3556  OG1 THR A 429     5139   4472   4260   -165     57    172       O  
ATOM   3557  CG2 THR A 429      16.009   7.682 -53.803  1.00 32.39           C  
ANISOU 3557  CG2 THR A 429     4594   3927   3784   -184     69    148       C  
ATOM   3558  N   ILE A 430      13.148  11.512 -52.923  1.00 33.63           N  
ANISOU 3558  N   ILE A 430     4767   4031   3979   -150    112    210       N  
ATOM   3559  CA  ILE A 430      12.038  12.407 -53.244  1.00 34.07           C  
ANISOU 3559  CA  ILE A 430     4815   4076   4053   -135    131    248       C  
ATOM   3560  C   ILE A 430      12.522  13.485 -54.208  1.00 34.78           C  
ANISOU 3560  C   ILE A 430     4891   4149   4176   -134    155    284       C  
ATOM   3561  O   ILE A 430      13.426  14.265 -53.882  1.00 39.79           O  
ANISOU 3561  O   ILE A 430     5523   4749   4847   -141    172    265       O  
ATOM   3562  CB  ILE A 430      11.399  13.024 -51.981  1.00 35.12           C  
ANISOU 3562  CB  ILE A 430     4954   4176   4214   -131    145    224       C  
ATOM   3563  CG1 ILE A 430      10.714  11.930 -51.147  1.00 34.57           C  
ANISOU 3563  CG1 ILE A 430     4899   4129   4106   -133    123    198       C  
ATOM   3564  CG2 ILE A 430      10.392  14.108 -52.360  1.00 33.21           C  
ANISOU 3564  CG2 ILE A 430     4694   3908   4016   -114    173    267       C  
ATOM   3565  CD1 ILE A 430      10.404  12.331 -49.716  1.00 29.20           C  
ANISOU 3565  CD1 ILE A 430     4234   3421   3441   -144    136    158       C  
ATOM   3566  N   ALA A 431      11.925  13.502 -55.399  1.00 34.02           N  
ANISOU 3566  N   ALA A 431     4786   4077   4063   -130    154    337       N  
ATOM   3567  CA  ALA A 431      12.292  14.439 -56.470  1.00 33.75           C  
ANISOU 3567  CA  ALA A 431     4740   4035   4051   -134    172    383       C  
ATOM   3568  C   ALA A 431      11.354  15.643 -56.559  1.00 33.16           C  
ANISOU 3568  C   ALA A 431     4644   3928   4026   -118    188    433       C  
ATOM   3569  O   ALA A 431      11.731  16.694 -57.079  1.00 35.05           O  
ANISOU 3569  O   ALA A 431     4871   4141   4305   -118    209    467       O  
ATOM   3570  CB  ALA A 431      12.332  13.712 -57.805  1.00 32.05           C  
ANISOU 3570  CB  ALA A 431     4529   3870   3780   -151    161    413       C  
ATOM   3571  N   GLY A 432      10.130  15.479 -56.071  1.00 32.93           N  
ANISOU 3571  N   GLY A 432     4610   3899   4003   -103    181    442       N  
ATOM   3572  CA  GLY A 432       9.119  16.535 -56.168  1.00 33.94           C  
ANISOU 3572  CA  GLY A 432     4710   3993   4191    -85    197    495       C  
ATOM   3573  C   GLY A 432       7.714  15.984 -56.282  1.00 34.44           C  
ANISOU 3573  C   GLY A 432     4762   4083   4240    -74    175    528       C  
ATOM   3574  O   GLY A 432       7.474  14.821 -55.960  1.00 31.74           O  
ANISOU 3574  O   GLY A 432     4439   3778   3845    -79    153    495       O  
ATOM   3575  N   THR A 433       6.789  16.826 -56.741  1.00 36.37           N  
ANISOU 3575  N   THR A 433     4974   4307   4539    -60    181    597       N  
ATOM   3576  CA  THR A 433       5.384  16.440 -56.902  1.00 37.40           C  
ANISOU 3576  CA  THR A 433     5084   4458   4670    -49    159    640       C  
ATOM   3577  C   THR A 433       4.837  16.778 -58.292  1.00 38.45           C  
ANISOU 3577  C   THR A 433     5189   4617   4802    -56    132    740       C  
ATOM   3578  O   THR A 433       5.346  17.667 -58.977  1.00 38.34           O  
ANISOU 3578  O   THR A 433     5164   4587   4816    -61    141    786       O  
ATOM   3579  CB  THR A 433       4.456  17.104 -55.836  1.00 38.39           C  
ANISOU 3579  CB  THR A 433     5185   4522   4879    -24    194    628       C  
ATOM   3580  OG1 THR A 433       4.389  18.526 -56.049  1.00 38.60           O  
ANISOU 3580  OG1 THR A 433     5178   4490   5000    -11    226    676       O  
ATOM   3581  CG2 THR A 433       4.949  16.820 -54.413  1.00 38.23           C  
ANISOU 3581  CG2 THR A 433     5195   4478   4851    -28    220    531       C  
ATOM   3582  N   PHE A 434       3.802  16.055 -58.701  1.00 37.65           N  
ANISOU 3582  N   PHE A 434     5078   4560   4667    -60     97    777       N  
ATOM   3583  CA  PHE A 434       3.031  16.429 -59.880  1.00 40.09           C  
ANISOU 3583  CA  PHE A 434     5354   4893   4984    -68     65    882       C  
ATOM   3584  C   PHE A 434       1.572  16.661 -59.491  1.00 38.88           C  
ANISOU 3584  C   PHE A 434     5157   4714   4901    -43     60    924       C  
ATOM   3585  O   PHE A 434       1.152  16.347 -58.369  1.00 39.21           O  
ANISOU 3585  O   PHE A 434     5201   4729   4967    -24     82    865       O  
ATOM   3586  CB  PHE A 434       3.154  15.381 -61.008  1.00 39.01           C  
ANISOU 3586  CB  PHE A 434     5243   4841   4737   -108     20    902       C  
ATOM   3587  CG  PHE A 434       2.553  14.042 -60.670  1.00 40.38           C  
ANISOU 3587  CG  PHE A 434     5433   5057   4851   -113     -2    859       C  
ATOM   3588  CD1 PHE A 434       3.313  13.064 -60.042  1.00 36.10           C  
ANISOU 3588  CD1 PHE A 434     4931   4528   4258   -118     11    766       C  
ATOM   3589  CD2 PHE A 434       1.228  13.757 -60.988  1.00 41.01           C  
ANISOU 3589  CD2 PHE A 434     5485   5164   4933   -115    -37    917       C  
ATOM   3590  CE1 PHE A 434       2.768  11.829 -59.736  1.00 37.76           C  
ANISOU 3590  CE1 PHE A 434     5155   4774   4418   -123     -8    729       C  
ATOM   3591  CE2 PHE A 434       0.672  12.523 -60.675  1.00 36.94           C  
ANISOU 3591  CE2 PHE A 434     4984   4686   4365   -121    -56    876       C  
ATOM   3592  CZ  PHE A 434       1.441  11.557 -60.054  1.00 38.00           C  
ANISOU 3592  CZ  PHE A 434     5160   4830   4447   -124    -40    782       C  
ATOM   3593  N   LYS A 435       0.817  17.221 -60.427  1.00 39.36           N  
ANISOU 3593  N   LYS A 435     5176   4782   4996    -47     31   1031       N  
ATOM   3594  CA  LYS A 435      -0.592  17.520 -60.243  1.00 40.23           C  
ANISOU 3594  CA  LYS A 435     5232   4866   5187    -24     23   1090       C  
ATOM   3595  C   LYS A 435      -1.401  16.248 -60.472  1.00 39.95           C  
ANISOU 3595  C   LYS A 435     5204   4899   5075    -41    -24   1091       C  
ATOM   3596  O   LYS A 435      -1.396  15.697 -61.572  1.00 39.67           O  
ANISOU 3596  O   LYS A 435     5181   4935   4956    -78    -73   1136       O  
ATOM   3597  CB  LYS A 435      -1.018  18.629 -61.208  1.00 40.44           C  
ANISOU 3597  CB  LYS A 435     5205   4874   5285    -25      3   1215       C  
ATOM   3598  CG  LYS A 435      -2.326  19.315 -60.847  1.00 44.12           C  
ANISOU 3598  CG  LYS A 435     5602   5282   5881      9     12   1277       C  
ATOM   3599  CD  LYS A 435      -2.418  20.724 -61.475  1.00 45.05           C  
ANISOU 3599  CD  LYS A 435     5665   5347   6106     18     16   1384       C  
ATOM   3600  CE  LYS A 435      -2.732  20.686 -62.968  1.00 42.23           C  
ANISOU 3600  CE  LYS A 435     5289   5058   5700    -19    -60   1510       C  
ATOM   3601  NZ  LYS A 435      -2.724  22.062 -63.553  1.00 44.21           N  
ANISOU 3601  NZ  LYS A 435     5487   5256   6055    -11    -57   1617       N  
ATOM   3602  N   VAL A 436      -2.079  15.790 -59.419  1.00 38.59           N  
ANISOU 3602  N   VAL A 436     5028   4704   4931    -19     -4   1037       N  
ATOM   3603  CA  VAL A 436      -2.812  14.533 -59.439  1.00 39.16           C  
ANISOU 3603  CA  VAL A 436     5110   4834   4936    -32    -40   1022       C  
ATOM   3604  C   VAL A 436      -4.178  14.683 -60.085  1.00 41.09           C  
ANISOU 3604  C   VAL A 436     5297   5092   5225    -32    -82   1126       C  
ATOM   3605  O   VAL A 436      -4.908  15.638 -59.819  1.00 42.98           O  
ANISOU 3605  O   VAL A 436     5479   5270   5583     -3    -63   1178       O  
ATOM   3606  CB  VAL A 436      -2.997  13.927 -58.011  1.00 38.97           C  
ANISOU 3606  CB  VAL A 436     5106   4781   4919    -11     -2    923       C  
ATOM   3607  CG1 VAL A 436      -1.679  13.800 -57.318  1.00 39.27           C  
ANISOU 3607  CG1 VAL A 436     5196   4805   4919    -14     33    829       C  
ATOM   3608  CG2 VAL A 436      -3.946  14.777 -57.163  1.00 40.87           C  
ANISOU 3608  CG2 VAL A 436     5297   4945   5286     25     40    936       C  
ATOM   3609  N   ALA A 437      -4.505  13.730 -60.947  1.00 41.61           N  
ANISOU 3609  N   ALA A 437     5374   5238   5197    -69   -139   1155       N  
ATOM   3610  CA  ALA A 437      -5.845  13.593 -61.479  1.00 42.35           C  
ANISOU 3610  CA  ALA A 437     5417   5357   5316    -76   -188   1243       C  
ATOM   3611  C   ALA A 437      -6.557  12.561 -60.590  1.00 42.61           C  
ANISOU 3611  C   ALA A 437     5457   5396   5337    -64   -179   1176       C  
ATOM   3612  O   ALA A 437      -5.896  11.824 -59.870  1.00 39.40           O  
ANISOU 3612  O   ALA A 437     5103   4994   4874    -62   -150   1073       O  
ATOM   3613  CB  ALA A 437      -5.779  13.123 -62.915  1.00 41.47           C  
ANISOU 3613  CB  ALA A 437     5320   5334   5101   -133   -254   1308       C  
ATOM   3614  N   PRO A 438      -7.904  12.528 -60.610  1.00 44.37           N  
ANISOU 3614  N   PRO A 438     5625   5616   5619    -55   -204   1236       N  
ATOM   3615  CA  PRO A 438      -8.591  11.491 -59.838  1.00 45.09           C  
ANISOU 3615  CA  PRO A 438     5724   5717   5691    -48   -198   1175       C  
ATOM   3616  C   PRO A 438      -8.046  10.110 -60.172  1.00 44.37           C  
ANISOU 3616  C   PRO A 438     5697   5704   5457    -88   -225   1113       C  
ATOM   3617  O   PRO A 438      -7.722   9.841 -61.329  1.00 43.73           O  
ANISOU 3617  O   PRO A 438     5633   5688   5295   -131   -270   1154       O  
ATOM   3618  CB  PRO A 438     -10.040  11.616 -60.295  1.00 46.87           C  
ANISOU 3618  CB  PRO A 438     5878   5949   5982    -48   -242   1275       C  
ATOM   3619  CG  PRO A 438     -10.180  13.080 -60.648  1.00 48.52           C  
ANISOU 3619  CG  PRO A 438     6027   6102   6307    -28   -237   1370       C  
ATOM   3620  CD  PRO A 438      -8.840  13.525 -61.167  1.00 45.76           C  
ANISOU 3620  CD  PRO A 438     5722   5763   5901    -45   -231   1361       C  
ATOM   3621  N   LEU A 439      -7.936   9.256 -59.157  1.00 42.90           N  
ANISOU 3621  N   LEU A 439     5546   5510   5244    -76   -193   1015       N  
ATOM   3622  CA  LEU A 439      -7.318   7.941 -59.303  1.00 44.05           C  
ANISOU 3622  CA  LEU A 439     5752   5716   5271   -107   -206    946       C  
ATOM   3623  C   LEU A 439      -7.883   7.096 -60.457  1.00 45.06           C  
ANISOU 3623  C   LEU A 439     5877   5925   5319   -155   -268    994       C  
ATOM   3624  O   LEU A 439      -7.123   6.412 -61.149  1.00 45.37           O  
ANISOU 3624  O   LEU A 439     5961   6017   5259   -194   -283    966       O  
ATOM   3625  CB  LEU A 439      -7.389   7.171 -57.981  1.00 43.87           C  
ANISOU 3625  CB  LEU A 439     5753   5668   5247    -86   -169    852       C  
ATOM   3626  CG  LEU A 439      -6.751   5.781 -57.931  1.00 42.28           C  
ANISOU 3626  CG  LEU A 439     5609   5515   4943   -111   -176    776       C  
ATOM   3627  CD1 LEU A 439      -5.242   5.862 -57.714  1.00 39.78           C  
ANISOU 3627  CD1 LEU A 439     5338   5184   4592   -113   -148    716       C  
ATOM   3628  CD2 LEU A 439      -7.409   4.952 -56.843  1.00 43.91           C  
ANISOU 3628  CD2 LEU A 439     5820   5708   5157    -97   -159    721       C  
ATOM   3629  N   HIS A 440      -9.199   7.146 -60.665  1.00 46.17           N  
ANISOU 3629  N   HIS A 440     5965   6074   5505   -154   -302   1062       N  
ATOM   3630  CA  HIS A 440      -9.827   6.423 -61.785  1.00 50.16           C  
ANISOU 3630  CA  HIS A 440     6464   6659   5937   -207   -366   1116       C  
ATOM   3631  C   HIS A 440      -9.267   6.803 -63.159  1.00 48.40           C  
ANISOU 3631  C   HIS A 440     6252   6488   5651   -255   -406   1180       C  
ATOM   3632  O   HIS A 440      -9.270   5.986 -64.083  1.00 48.28           O  
ANISOU 3632  O   HIS A 440     6263   6548   5533   -313   -445   1186       O  
ATOM   3633  CB  HIS A 440     -11.361   6.537 -61.756  1.00 53.57           C  
ANISOU 3633  CB  HIS A 440     6827   7085   6443   -197   -399   1190       C  
ATOM   3634  CG  HIS A 440     -12.033   5.323 -61.187  1.00 61.71           C  
ANISOU 3634  CG  HIS A 440     7867   8134   7445   -200   -398   1132       C  
ATOM   3635  ND1 HIS A 440     -12.352   5.202 -59.850  1.00 66.13           N  
ANISOU 3635  ND1 HIS A 440     8421   8635   8070   -153   -347   1069       N  
ATOM   3636  CD2 HIS A 440     -12.415   4.160 -61.770  1.00 64.15           C  
ANISOU 3636  CD2 HIS A 440     8194   8515   7665   -247   -440   1124       C  
ATOM   3637  CE1 HIS A 440     -12.912   4.024 -59.638  1.00 66.37           C  
ANISOU 3637  CE1 HIS A 440     8464   8699   8056   -169   -358   1030       C  
ATOM   3638  NE2 HIS A 440     -12.960   3.372 -60.786  1.00 65.96           N  
ANISOU 3638  NE2 HIS A 440     8425   8725   7913   -224   -414   1061       N  
ATOM   3639  N   ASP A 441      -8.772   8.036 -63.272  1.00 47.43           N  
ANISOU 3639  N   ASP A 441     6112   6322   5586   -235   -390   1225       N  
ATOM   3640  CA  ASP A 441      -8.126   8.514 -64.492  1.00 46.58           C  
ANISOU 3640  CA  ASP A 441     6018   6256   5423   -280   -419   1284       C  
ATOM   3641  C   ASP A 441      -6.833   7.766 -64.785  1.00 45.63           C  
ANISOU 3641  C   ASP A 441     5973   6173   5190   -313   -396   1197       C  
ATOM   3642  O   ASP A 441      -6.503   7.517 -65.949  1.00 48.55           O  
ANISOU 3642  O   ASP A 441     6370   6610   5469   -375   -427   1226       O  
ATOM   3643  CB  ASP A 441      -7.854  10.016 -64.407  1.00 46.04           C  
ANISOU 3643  CB  ASP A 441     5913   6122   5456   -244   -399   1345       C  
ATOM   3644  CG  ASP A 441      -9.107  10.854 -64.605  1.00 47.96           C  
ANISOU 3644  CG  ASP A 441     6074   6340   5808   -228   -436   1465       C  
ATOM   3645  OD1 ASP A 441     -10.234  10.302 -64.591  1.00 44.73           O  
ANISOU 3645  OD1 ASP A 441     5632   5955   5410   -235   -471   1493       O  
ATOM   3646  OD2 ASP A 441      -8.956  12.079 -64.781  1.00 48.97           O  
ANISOU 3646  OD2 ASP A 441     6166   6422   6018   -209   -429   1534       O  
ATOM   3647  N   TYR A 442      -6.099   7.415 -63.733  1.00 42.29           N  
ANISOU 3647  N   TYR A 442     5583   5707   4777   -277   -340   1093       N  
ATOM   3648  CA  TYR A 442      -4.889   6.621 -63.894  1.00 40.29           C  
ANISOU 3648  CA  TYR A 442     5393   5481   4433   -304   -314   1006       C  
ATOM   3649  C   TYR A 442      -5.261   5.167 -64.132  1.00 41.05           C  
ANISOU 3649  C   TYR A 442     5515   5636   4445   -343   -333    962       C  
ATOM   3650  O   TYR A 442      -4.654   4.492 -64.962  1.00 41.20           O  
ANISOU 3650  O   TYR A 442     5575   5707   4371   -396   -335    934       O  
ATOM   3651  CB  TYR A 442      -3.951   6.782 -62.690  1.00 37.98           C  
ANISOU 3651  CB  TYR A 442     5122   5122   4186   -255   -255    920       C  
ATOM   3652  CG  TYR A 442      -3.471   8.205 -62.501  1.00 33.33           C  
ANISOU 3652  CG  TYR A 442     4512   4476   3675   -224   -231    956       C  
ATOM   3653  CD1 TYR A 442      -2.632   8.811 -63.439  1.00 34.10           C  
ANISOU 3653  CD1 TYR A 442     4623   4590   3744   -252   -233    990       C  
ATOM   3654  CD2 TYR A 442      -3.868   8.952 -61.399  1.00 33.49           C  
ANISOU 3654  CD2 TYR A 442     4500   4425   3800   -171   -202    952       C  
ATOM   3655  CE1 TYR A 442      -2.194  10.123 -63.274  1.00 31.27           C  
ANISOU 3655  CE1 TYR A 442     4244   4175   3461   -224   -210   1024       C  
ATOM   3656  CE2 TYR A 442      -3.436  10.269 -61.229  1.00 34.00           C  
ANISOU 3656  CE2 TYR A 442     4545   4432   3941   -145   -175    981       C  
ATOM   3657  CZ  TYR A 442      -2.603  10.841 -62.170  1.00 29.81           C  
ANISOU 3657  CZ  TYR A 442     4026   3918   3383   -170   -181   1018       C  
ATOM   3658  OH  TYR A 442      -2.188  12.143 -62.006  1.00 35.70           O  
ANISOU 3658  OH  TYR A 442     4751   4605   4210   -145   -154   1048       O  
ATOM   3659  N   ILE A 443      -6.284   4.699 -63.422  1.00 42.56           N  
ANISOU 3659  N   ILE A 443     5682   5816   4673   -319   -341    954       N  
ATOM   3660  CA  ILE A 443      -6.765   3.333 -63.585  1.00 43.28           C  
ANISOU 3660  CA  ILE A 443     5793   5958   4695   -353   -359    914       C  
ATOM   3661  C   ILE A 443      -7.160   3.075 -65.039  1.00 44.20           C  
ANISOU 3661  C   ILE A 443     5911   6156   4729   -427   -412    977       C  
ATOM   3662  O   ILE A 443      -6.793   2.048 -65.609  1.00 44.76           O  
ANISOU 3662  O   ILE A 443     6024   6277   4706   -478   -410    926       O  
ATOM   3663  CB  ILE A 443      -7.929   3.007 -62.608  1.00 42.34           C  
ANISOU 3663  CB  ILE A 443     5638   5811   4637   -316   -362    909       C  
ATOM   3664  CG1 ILE A 443      -7.407   2.986 -61.162  1.00 44.06           C  
ANISOU 3664  CG1 ILE A 443     5872   5961   4908   -260   -306    828       C  
ATOM   3665  CG2 ILE A 443      -8.569   1.661 -62.959  1.00 41.70           C  
ANISOU 3665  CG2 ILE A 443     5570   5788   4485   -358   -389    885       C  
ATOM   3666  CD1 ILE A 443      -8.460   3.204 -60.096  1.00 42.90           C  
ANISOU 3666  CD1 ILE A 443     5685   5768   4849   -215   -295    835       C  
ATOM   3667  N   ASN A 444      -7.874   4.023 -65.640  1.00 45.82           N  
ANISOU 3667  N   ASN A 444     6069   6370   4969   -435   -457   1086       N  
ATOM   3668  CA  ASN A 444      -8.376   3.858 -67.008  1.00 48.73           C  
ANISOU 3668  CA  ASN A 444     6435   6821   5258   -512   -518   1161       C  
ATOM   3669  C   ASN A 444      -7.457   4.405 -68.102  1.00 49.82           C  
ANISOU 3669  C   ASN A 444     6603   6993   5332   -562   -522   1194       C  
ATOM   3670  O   ASN A 444      -7.821   4.421 -69.284  1.00 51.27           O  
ANISOU 3670  O   ASN A 444     6786   7247   5446   -633   -574   1267       O  
ATOM   3671  CB  ASN A 444      -9.805   4.410 -67.122  1.00 49.88           C  
ANISOU 3671  CB  ASN A 444     6510   6969   5474   -504   -576   1272       C  
ATOM   3672  CG  ASN A 444     -10.779   3.672 -66.210  1.00 51.80           C  
ANISOU 3672  CG  ASN A 444     6728   7193   5762   -471   -573   1236       C  
ATOM   3673  OD1 ASN A 444     -11.058   2.487 -66.413  1.00 52.31           O  
ANISOU 3673  OD1 ASN A 444     6818   7306   5750   -512   -586   1190       O  
ATOM   3674  ND2 ASN A 444     -11.275   4.360 -65.183  1.00 48.73           N  
ANISOU 3674  ND2 ASN A 444     6290   6728   5496   -400   -550   1251       N  
ATOM   3675  N   ALA A 445      -6.267   4.845 -67.693  1.00 48.86           N  
ANISOU 3675  N   ALA A 445     6508   6824   5233   -528   -467   1142       N  
ATOM   3676  CA  ALA A 445      -5.220   5.319 -68.600  1.00 49.44           C  
ANISOU 3676  CA  ALA A 445     6615   6920   5250   -570   -456   1156       C  
ATOM   3677  C   ALA A 445      -5.605   6.572 -69.396  1.00 50.98           C  
ANISOU 3677  C   ALA A 445     6770   7126   5472   -588   -503   1288       C  
ATOM   3678  O   ALA A 445      -5.170   6.742 -70.536  1.00 51.98           O  
ANISOU 3678  O   ALA A 445     6923   7307   5518   -655   -521   1327       O  
ATOM   3679  CB  ALA A 445      -4.760   4.187 -69.542  1.00 48.92           C  
ANISOU 3679  CB  ALA A 445     6608   6930   5051   -653   -452   1100       C  
ATOM   3680  N   VAL A 446      -6.407   7.448 -68.793  1.00 51.59           N  
ANISOU 3680  N   VAL A 446     6785   7150   5668   -530   -520   1357       N  
ATOM   3681  CA  VAL A 446      -6.853   8.674 -69.477  1.00 52.98           C  
ANISOU 3681  CA  VAL A 446     6912   7326   5893   -540   -567   1493       C  
ATOM   3682  C   VAL A 446      -6.199   9.956 -68.949  1.00 52.09           C  
ANISOU 3682  C   VAL A 446     6777   7129   5884   -479   -524   1509       C  
ATOM   3683  O   VAL A 446      -6.298  11.015 -69.572  1.00 50.85           O  
ANISOU 3683  O   VAL A 446     6587   6968   5766   -489   -553   1616       O  
ATOM   3684  CB  VAL A 446      -8.400   8.815 -69.488  1.00 54.69           C  
ANISOU 3684  CB  VAL A 446     7057   7550   6174   -534   -630   1592       C  
ATOM   3685  CG1 VAL A 446      -9.033   7.706 -70.325  1.00 56.68           C  
ANISOU 3685  CG1 VAL A 446     7328   7898   6309   -614   -686   1601       C  
ATOM   3686  CG2 VAL A 446      -8.972   8.827 -68.071  1.00 54.85           C  
ANISOU 3686  CG2 VAL A 446     7038   7489   6313   -450   -593   1545       C  
ATOM   3687  N   ALA A 447      -5.531   9.855 -67.804  1.00 51.89           N  
ANISOU 3687  N   ALA A 447     6771   7040   5903   -420   -457   1404       N  
ATOM   3688  CA  ALA A 447      -4.803  10.990 -67.240  1.00 51.55           C  
ANISOU 3688  CA  ALA A 447     6717   6919   5952   -368   -410   1400       C  
ATOM   3689  C   ALA A 447      -3.497  11.236 -67.992  1.00 50.45           C  
ANISOU 3689  C   ALA A 447     6626   6802   5742   -406   -390   1386       C  
ATOM   3690  O   ALA A 447      -2.906  10.304 -68.550  1.00 47.88           O  
ANISOU 3690  O   ALA A 447     6355   6536   5303   -458   -386   1329       O  
ATOM   3691  CB  ALA A 447      -4.533  10.766 -65.762  1.00 50.18           C  
ANISOU 3691  CB  ALA A 447     6552   6676   5840   -303   -350   1293       C  
ATOM   3692  N   GLU A 448      -3.060  12.496 -68.008  1.00 50.80           N  
ANISOU 3692  N   GLU A 448     6648   6795   5861   -381   -373   1436       N  
ATOM   3693  CA  GLU A 448      -1.773  12.849 -68.596  1.00 50.42           C  
ANISOU 3693  CA  GLU A 448     6640   6754   5762   -410   -345   1420       C  
ATOM   3694  C   GLU A 448      -0.633  12.151 -67.852  1.00 48.53           C  
ANISOU 3694  C   GLU A 448     6453   6494   5492   -391   -284   1281       C  
ATOM   3695  O   GLU A 448      -0.732  11.880 -66.650  1.00 47.02           O  
ANISOU 3695  O   GLU A 448     6256   6254   5356   -339   -254   1210       O  
ATOM   3696  CB  GLU A 448      -1.567  14.374 -68.667  1.00 52.23           C  
ANISOU 3696  CB  GLU A 448     6830   6924   6091   -382   -336   1501       C  
ATOM   3697  CG  GLU A 448      -1.313  15.106 -67.341  1.00 55.95           C  
ANISOU 3697  CG  GLU A 448     7277   7294   6689   -303   -279   1451       C  
ATOM   3698  CD  GLU A 448      -1.114  16.629 -67.518  1.00 64.16           C  
ANISOU 3698  CD  GLU A 448     8276   8272   7828   -281   -267   1534       C  
ATOM   3699  OE1 GLU A 448      -1.040  17.106 -68.679  1.00 65.67           O  
ANISOU 3699  OE1 GLU A 448     8463   8503   7986   -327   -303   1631       O  
ATOM   3700  OE2 GLU A 448      -1.029  17.353 -66.494  1.00 63.24           O  
ANISOU 3700  OE2 GLU A 448     8134   8070   7825   -223   -220   1504       O  
ATOM   3701  N   ARG A 449       0.430  11.831 -68.583  1.00 47.11           N  
ANISOU 3701  N   ARG A 449     6323   6353   5224   -439   -265   1245       N  
ATOM   3702  CA  ARG A 449       1.601  11.200 -67.995  1.00 45.26           C  
ANISOU 3702  CA  ARG A 449     6132   6098   4968   -426   -209   1123       C  
ATOM   3703  C   ARG A 449       2.188  12.103 -66.893  1.00 41.96           C  
ANISOU 3703  C   ARG A 449     5696   5591   4658   -359   -165   1092       C  
ATOM   3704  O   ARG A 449       2.404  13.297 -67.122  1.00 40.25           O  
ANISOU 3704  O   ARG A 449     5457   5341   4496   -349   -160   1154       O  
ATOM   3705  CB  ARG A 449       2.628  10.894 -69.083  1.00 47.83           C  
ANISOU 3705  CB  ARG A 449     6504   6472   5195   -492   -191   1103       C  
ATOM   3706  CG  ARG A 449       3.631   9.830 -68.702  1.00 48.96           C  
ANISOU 3706  CG  ARG A 449     6690   6613   5297   -495   -143    980       C  
ATOM   3707  CD  ARG A 449       4.087   9.042 -69.927  1.00 51.90           C  
ANISOU 3707  CD  ARG A 449     7109   7059   5552   -578   -135    960       C  
ATOM   3708  NE  ARG A 449       5.109   8.056 -69.573  1.00 49.13           N  
ANISOU 3708  NE  ARG A 449     6792   6695   5180   -579    -82    843       N  
ATOM   3709  CZ  ARG A 449       6.416   8.307 -69.550  1.00 47.63           C  
ANISOU 3709  CZ  ARG A 449     6618   6473   5007   -575    -31    796       C  
ATOM   3710  NH1 ARG A 449       6.874   9.507 -69.873  1.00 47.13           N  
ANISOU 3710  NH1 ARG A 449     6545   6388   4975   -572    -25    851       N  
ATOM   3711  NH2 ARG A 449       7.272   7.350 -69.218  1.00 48.13           N  
ANISOU 3711  NH2 ARG A 449     6704   6522   5062   -575     14    696       N  
ATOM   3712  N   PRO A 450       2.399  11.544 -65.683  1.00 39.95           N  
ANISOU 3712  N   PRO A 450     5449   5297   4432   -317   -135    999       N  
ATOM   3713  CA  PRO A 450       2.894  12.330 -64.548  1.00 38.98           C  
ANISOU 3713  CA  PRO A 450     5313   5095   4404   -261    -95    962       C  
ATOM   3714  C   PRO A 450       4.245  12.991 -64.799  1.00 39.88           C  
ANISOU 3714  C   PRO A 450     5444   5185   4524   -268    -59    945       C  
ATOM   3715  O   PRO A 450       4.403  14.191 -64.547  1.00 39.66           O  
ANISOU 3715  O   PRO A 450     5391   5103   4576   -241    -43    980       O  
ATOM   3716  CB  PRO A 450       3.012  11.285 -63.436  1.00 38.00           C  
ANISOU 3716  CB  PRO A 450     5208   4958   4271   -238    -77    862       C  
ATOM   3717  CG  PRO A 450       1.970  10.295 -63.760  1.00 35.38           C  
ANISOU 3717  CG  PRO A 450     4875   4681   3886   -260   -115    876       C  
ATOM   3718  CD  PRO A 450       1.977  10.195 -65.257  1.00 36.60           C  
ANISOU 3718  CD  PRO A 450     5042   4903   3962   -321   -143    935       C  
ATOM   3719  N   SER A 451       5.210  12.216 -65.287  1.00 41.03           N  
ANISOU 3719  N   SER A 451     5630   5366   4593   -304    -44    890       N  
ATOM   3720  CA  SER A 451       6.559  12.729 -65.520  1.00 41.27           C  
ANISOU 3720  CA  SER A 451     5678   5374   4630   -313     -6    866       C  
ATOM   3721  C   SER A 451       7.260  12.011 -66.654  1.00 42.22           C  
ANISOU 3721  C   SER A 451     5835   5553   4654   -374      3    848       C  
ATOM   3722  O   SER A 451       7.059  10.810 -66.867  1.00 39.46           O  
ANISOU 3722  O   SER A 451     5508   5249   4238   -401     -5    807       O  
ATOM   3723  CB  SER A 451       7.429  12.627 -64.260  1.00 38.26           C  
ANISOU 3723  CB  SER A 451     5302   4936   4298   -273     31    775       C  
ATOM   3724  OG  SER A 451       8.704  13.217 -64.486  1.00 34.26           O  
ANISOU 3724  OG  SER A 451     4806   4404   3807   -281     66    758       O  
ATOM   3725  N   ASP A 452       8.096  12.777 -67.350  1.00 42.47           N  
ANISOU 3725  N   ASP A 452     5874   5579   4684   -397     24    875       N  
ATOM   3726  CA  ASP A 452       8.996  12.279 -68.381  1.00 44.72           C  
ANISOU 3726  CA  ASP A 452     6196   5907   4890   -456     49    849       C  
ATOM   3727  C   ASP A 452      10.433  12.177 -67.843  1.00 40.50           C  
ANISOU 3727  C   ASP A 452     5673   5327   4389   -438    103    762       C  
ATOM   3728  O   ASP A 452      11.374  11.893 -68.587  1.00 38.85           O  
ANISOU 3728  O   ASP A 452     5489   5137   4134   -481    137    733       O  
ATOM   3729  CB  ASP A 452       8.964  13.230 -69.584  1.00 48.28           C  
ANISOU 3729  CB  ASP A 452     6646   6385   5313   -500     38    944       C  
ATOM   3730  CG  ASP A 452       7.864  12.894 -70.576  1.00 55.84           C  
ANISOU 3730  CG  ASP A 452     7609   7418   6190   -553    -12   1017       C  
ATOM   3731  OD1 ASP A 452       7.726  11.704 -70.927  1.00 61.56           O  
ANISOU 3731  OD1 ASP A 452     8363   8194   6834   -594    -13    970       O  
ATOM   3732  OD2 ASP A 452       7.155  13.824 -71.027  1.00 60.46           O  
ANISOU 3732  OD2 ASP A 452     8168   8009   6796   -559    -51   1124       O  
ATOM   3733  N   VAL A 453      10.596  12.428 -66.550  1.00 38.17           N  
ANISOU 3733  N   VAL A 453     5358   4971   4173   -380    110    724       N  
ATOM   3734  CA  VAL A 453      11.923  12.518 -65.942  1.00 37.17           C  
ANISOU 3734  CA  VAL A 453     5234   4796   4092   -361    151    655       C  
ATOM   3735  C   VAL A 453      12.074  11.564 -64.760  1.00 36.67           C  
ANISOU 3735  C   VAL A 453     5171   4713   4050   -330    152    575       C  
ATOM   3736  O   VAL A 453      13.085  10.860 -64.650  1.00 38.48           O  
ANISOU 3736  O   VAL A 453     5411   4934   4275   -339    180    509       O  
ATOM   3737  CB  VAL A 453      12.234  13.965 -65.465  1.00 36.56           C  
ANISOU 3737  CB  VAL A 453     5132   4659   4098   -328    162    688       C  
ATOM   3738  CG1 VAL A 453      13.590  14.033 -64.777  1.00 34.70           C  
ANISOU 3738  CG1 VAL A 453     4899   4377   3910   -312    199    617       C  
ATOM   3739  CG2 VAL A 453      12.175  14.940 -66.625  1.00 36.01           C  
ANISOU 3739  CG2 VAL A 453     5060   4606   4015   -359    161    773       C  
ATOM   3740  N   TYR A 454      11.069  11.551 -63.888  1.00 34.22           N  
ANISOU 3740  N   TYR A 454     4846   4390   3767   -295    123    584       N  
ATOM   3741  CA  TYR A 454      11.152  10.857 -62.608  1.00 34.10           C  
ANISOU 3741  CA  TYR A 454     4829   4348   3779   -264    121    517       C  
ATOM   3742  C   TYR A 454      10.146   9.718 -62.523  1.00 33.67           C  
ANISOU 3742  C   TYR A 454     4781   4332   3678   -268     95    508       C  
ATOM   3743  O   TYR A 454       9.239   9.619 -63.343  1.00 33.24           O  
ANISOU 3743  O   TYR A 454     4728   4322   3580   -291     73    558       O  
ATOM   3744  CB  TYR A 454      10.912  11.833 -61.448  1.00 32.68           C  
ANISOU 3744  CB  TYR A 454     4629   4113   3675   -221    120    522       C  
ATOM   3745  CG  TYR A 454      11.810  13.051 -61.437  1.00 32.05           C  
ANISOU 3745  CG  TYR A 454     4540   3988   3649   -215    147    532       C  
ATOM   3746  CD1 TYR A 454      13.192  12.925 -61.276  1.00 35.44           C  
ANISOU 3746  CD1 TYR A 454     4976   4398   4091   -223    172    481       C  
ATOM   3747  CD2 TYR A 454      11.276  14.329 -61.571  1.00 33.24           C  
ANISOU 3747  CD2 TYR A 454     4671   4114   3847   -202    148    595       C  
ATOM   3748  CE1 TYR A 454      14.021  14.042 -61.257  1.00 36.80           C  
ANISOU 3748  CE1 TYR A 454     5140   4530   4314   -219    196    488       C  
ATOM   3749  CE2 TYR A 454      12.097  15.456 -61.556  1.00 37.28           C  
ANISOU 3749  CE2 TYR A 454     5173   4581   4411   -197    175    603       C  
ATOM   3750  CZ  TYR A 454      13.464  15.304 -61.392  1.00 39.65           C  
ANISOU 3750  CZ  TYR A 454     5483   4865   4715   -207    199    548       C  
ATOM   3751  OH  TYR A 454      14.279  16.414 -61.374  1.00 48.07           O  
ANISOU 3751  OH  TYR A 454     6541   5889   5836   -205    226    555       O  
ATOM   3752  N   SER A 455      10.324   8.872 -61.514  1.00 34.43           N  
ANISOU 3752  N   SER A 455     4881   4413   3787   -249     94    446       N  
ATOM   3753  CA  SER A 455       9.462   7.729 -61.265  1.00 35.89           C  
ANISOU 3753  CA  SER A 455     5072   4627   3937   -250     72    428       C  
ATOM   3754  C   SER A 455       8.311   8.125 -60.326  1.00 35.99           C  
ANISOU 3754  C   SER A 455     5069   4622   3984   -216     49    451       C  
ATOM   3755  O   SER A 455       8.532   8.749 -59.282  1.00 35.81           O  
ANISOU 3755  O   SER A 455     5037   4552   4016   -187     57    434       O  
ATOM   3756  CB  SER A 455      10.298   6.587 -60.679  1.00 33.97           C  
ANISOU 3756  CB  SER A 455     4838   4374   3696   -250     84    355       C  
ATOM   3757  OG  SER A 455       9.474   5.604 -60.088  1.00 36.51           O  
ANISOU 3757  OG  SER A 455     5162   4709   4000   -241     63    336       O  
ATOM   3758  N   CYS A 456       7.089   7.744 -60.687  1.00 35.94           N  
ANISOU 3758  N   CYS A 456     5058   4652   3946   -223     24    485       N  
ATOM   3759  CA  CYS A 456       5.909   8.301 -60.029  1.00 35.05           C  
ANISOU 3759  CA  CYS A 456     4924   4521   3874   -193      7    520       C  
ATOM   3760  C   CYS A 456       4.953   7.319 -59.356  1.00 33.96           C  
ANISOU 3760  C   CYS A 456     4787   4396   3722   -184    -11    497       C  
ATOM   3761  O   CYS A 456       4.846   6.151 -59.738  1.00 34.10           O  
ANISOU 3761  O   CYS A 456     4819   4453   3685   -206    -22    474       O  
ATOM   3762  CB  CYS A 456       5.124   9.167 -61.019  1.00 36.60           C  
ANISOU 3762  CB  CYS A 456     5099   4734   4071   -205    -10    607       C  
ATOM   3763  SG  CYS A 456       6.106  10.439 -61.837  1.00 40.03           S  
ANISOU 3763  SG  CYS A 456     5531   5152   4527   -217     10    648       S  
ATOM   3764  N   SER A 457       4.254   7.838 -58.350  1.00 33.30           N  
ANISOU 3764  N   SER A 457     4686   4275   3690   -152    -10    502       N  
ATOM   3765  CA  SER A 457       3.097   7.192 -57.752  1.00 32.43           C  
ANISOU 3765  CA  SER A 457     4569   4175   3578   -141    -25    497       C  
ATOM   3766  C   SER A 457       1.909   8.139 -57.913  1.00 32.17           C  
ANISOU 3766  C   SER A 457     4501   4129   3593   -125    -33    565       C  
ATOM   3767  O   SER A 457       2.078   9.347 -57.765  1.00 31.87           O  
ANISOU 3767  O   SER A 457     4446   4049   3614   -109    -14    590       O  
ATOM   3768  CB  SER A 457       3.354   6.938 -56.270  1.00 31.07           C  
ANISOU 3768  CB  SER A 457     4409   3965   3432   -120     -9    434       C  
ATOM   3769  OG  SER A 457       2.153   6.597 -55.609  1.00 32.28           O  
ANISOU 3769  OG  SER A 457     4553   4117   3596   -107    -17    435       O  
ATOM   3770  N   PRO A 458       0.704   7.598 -58.205  1.00 33.44           N  
ANISOU 3770  N   PRO A 458     4647   4321   3736   -131    -60    597       N  
ATOM   3771  CA  PRO A 458      -0.523   8.378 -58.442  1.00 32.54           C  
ANISOU 3771  CA  PRO A 458     4491   4197   3674   -118    -73    672       C  
ATOM   3772  C   PRO A 458      -1.023   9.208 -57.243  1.00 34.91           C  
ANISOU 3772  C   PRO A 458     4768   4432   4065    -80    -41    662       C  
ATOM   3773  O   PRO A 458      -2.074   9.848 -57.333  1.00 34.12           O  
ANISOU 3773  O   PRO A 458     4626   4313   4026    -65    -45    721       O  
ATOM   3774  CB  PRO A 458      -1.552   7.296 -58.789  1.00 32.69           C  
ANISOU 3774  CB  PRO A 458     4506   4268   3647   -136   -107    684       C  
ATOM   3775  CG  PRO A 458      -1.028   6.070 -58.152  1.00 32.77           C  
ANISOU 3775  CG  PRO A 458     4553   4289   3608   -141    -98    601       C  
ATOM   3776  CD  PRO A 458       0.444   6.157 -58.370  1.00 32.95           C  
ANISOU 3776  CD  PRO A 458     4604   4307   3608   -152    -79    566       C  
ATOM   3777  N   ASN A 459      -0.292   9.199 -56.133  1.00 35.31           N  
ANISOU 3777  N   ASN A 459     4843   4446   4127    -67     -8    590       N  
ATOM   3778  CA  ASN A 459      -0.596  10.119 -55.045  1.00 35.12           C  
ANISOU 3778  CA  ASN A 459     4804   4357   4184    -41     31    574       C  
ATOM   3779  C   ASN A 459       0.019  11.490 -55.302  1.00 35.39           C  
ANISOU 3779  C   ASN A 459     4822   4348   4276    -33     56    602       C  
ATOM   3780  O   ASN A 459      -0.213  12.432 -54.542  1.00 35.22           O  
ANISOU 3780  O   ASN A 459     4783   4266   4331    -14     95    594       O  
ATOM   3781  CB  ASN A 459      -0.141   9.558 -53.693  1.00 35.73           C  
ANISOU 3781  CB  ASN A 459     4915   4417   4244    -40     54    488       C  
ATOM   3782  CG  ASN A 459       1.358   9.689 -53.469  1.00 34.33           C  
ANISOU 3782  CG  ASN A 459     4769   4230   4044    -51     64    442       C  
ATOM   3783  OD1 ASN A 459       2.160   9.512 -54.384  1.00 37.05           O  
ANISOU 3783  OD1 ASN A 459     5122   4602   4352    -65     46    456       O  
ATOM   3784  ND2 ASN A 459       1.740   9.990 -52.230  1.00 35.35           N  
ANISOU 3784  ND2 ASN A 459     4915   4320   4197    -49     94    386       N  
ATOM   3785  N   GLY A 460       0.803  11.598 -56.374  1.00 34.34           N  
ANISOU 3785  N   GLY A 460     4697   4244   4106    -51     37    632       N  
ATOM   3786  CA  GLY A 460       1.453  12.864 -56.725  1.00 32.87           C  
ANISOU 3786  CA  GLY A 460     4498   4021   3971    -46     58    663       C  
ATOM   3787  C   GLY A 460       2.947  12.948 -56.484  1.00 32.47           C  
ANISOU 3787  C   GLY A 460     4481   3959   3897    -56     77    607       C  
ATOM   3788  O   GLY A 460       3.556  13.970 -56.773  1.00 35.57           O  
ANISOU 3788  O   GLY A 460     4864   4321   4330    -54     96    628       O  
ATOM   3789  N   MET A 461       3.551  11.884 -55.965  1.00 32.28           N  
ANISOU 3789  N   MET A 461     4492   3959   3815    -67     71    539       N  
ATOM   3790  CA  MET A 461       4.980  11.919 -55.634  1.00 32.46           C  
ANISOU 3790  CA  MET A 461     4540   3968   3825    -77     86    485       C  
ATOM   3791  C   MET A 461       5.875  11.525 -56.811  1.00 33.94           C  
ANISOU 3791  C   MET A 461     4740   4196   3959   -100     70    499       C  
ATOM   3792  O   MET A 461       5.500  10.698 -57.649  1.00 34.14           O  
ANISOU 3792  O   MET A 461     4770   4273   3930   -117     45    521       O  
ATOM   3793  CB  MET A 461       5.275  11.038 -54.411  1.00 31.82           C  
ANISOU 3793  CB  MET A 461     4486   3886   3720    -79     86    410       C  
ATOM   3794  CG  MET A 461       4.699  11.580 -53.083  1.00 33.61           C  
ANISOU 3794  CG  MET A 461     4710   4065   3996    -65    114    380       C  
ATOM   3795  SD  MET A 461       5.352  13.205 -52.574  1.00 38.60           S  
ANISOU 3795  SD  MET A 461     5333   4629   4704    -61    160    369       S  
ATOM   3796  CE  MET A 461       7.034  12.778 -52.142  1.00 37.35           C  
ANISOU 3796  CE  MET A 461     5207   4477   4505    -83    151    309       C  
ATOM   3797  N   MET A 462       7.059  12.127 -56.868  1.00 33.55           N  
ANISOU 3797  N   MET A 462     4698   4123   3928   -105     90    483       N  
ATOM   3798  CA  MET A 462       8.049  11.807 -57.897  1.00 35.00           C  
ANISOU 3798  CA  MET A 462     4893   4337   4068   -130     87    486       C  
ATOM   3799  C   MET A 462       9.345  11.417 -57.214  1.00 35.35           C  
ANISOU 3799  C   MET A 462     4956   4365   4111   -135     99    418       C  
ATOM   3800  O   MET A 462       9.671  11.948 -56.144  1.00 34.94           O  
ANISOU 3800  O   MET A 462     4903   4271   4102   -123    113    385       O  
ATOM   3801  CB  MET A 462       8.289  13.002 -58.830  1.00 36.97           C  
ANISOU 3801  CB  MET A 462     5127   4573   4345   -135     99    546       C  
ATOM   3802  CG  MET A 462       7.039  13.476 -59.558  1.00 39.75           C  
ANISOU 3802  CG  MET A 462     5455   4941   4708   -133     81    629       C  
ATOM   3803  SD  MET A 462       7.350  14.668 -60.868  1.00 42.80           S  
ANISOU 3803  SD  MET A 462     5825   5325   5111   -150     86    713       S  
ATOM   3804  CE  MET A 462       8.062  16.045 -59.959  1.00 44.54           C  
ANISOU 3804  CE  MET A 462     6032   5463   5429   -123    129    690       C  
ATOM   3805  N   TYR A 463      10.074  10.481 -57.818  1.00 33.58           N  
ANISOU 3805  N   TYR A 463     4745   4173   3841   -156     94    396       N  
ATOM   3806  CA  TYR A 463      11.319   9.982 -57.226  1.00 34.26           C  
ANISOU 3806  CA  TYR A 463     4840   4243   3934   -161    101    338       C  
ATOM   3807  C   TYR A 463      12.438   9.900 -58.247  1.00 35.00           C  
ANISOU 3807  C   TYR A 463     4936   4347   4015   -184    119    336       C  
ATOM   3808  O   TYR A 463      12.186   9.659 -59.434  1.00 33.85           O  
ANISOU 3808  O   TYR A 463     4795   4238   3827   -204    122    365       O  
ATOM   3809  CB  TYR A 463      11.102   8.611 -56.573  1.00 31.66           C  
ANISOU 3809  CB  TYR A 463     4521   3932   3576   -161     82    297       C  
ATOM   3810  CG  TYR A 463      10.032   8.613 -55.507  1.00 31.89           C  
ANISOU 3810  CG  TYR A 463     4551   3952   3615   -143     68    293       C  
ATOM   3811  CD1 TYR A 463       8.689   8.417 -55.844  1.00 31.28           C  
ANISOU 3811  CD1 TYR A 463     4470   3900   3516   -137     56    327       C  
ATOM   3812  CD2 TYR A 463      10.357   8.823 -54.164  1.00 31.41           C  
ANISOU 3812  CD2 TYR A 463     4494   3857   3582   -136     68    256       C  
ATOM   3813  CE1 TYR A 463       7.700   8.419 -54.883  1.00 30.57           C  
ANISOU 3813  CE1 TYR A 463     4378   3798   3440   -122     50    322       C  
ATOM   3814  CE2 TYR A 463       9.372   8.826 -53.182  1.00 31.02           C  
ANISOU 3814  CE2 TYR A 463     4449   3799   3537   -126     63    248       C  
ATOM   3815  CZ  TYR A 463       8.044   8.626 -53.553  1.00 32.59           C  
ANISOU 3815  CZ  TYR A 463     4642   4020   3721   -116     57    280       C  
ATOM   3816  OH  TYR A 463       7.060   8.627 -52.602  1.00 30.54           O  
ANISOU 3816  OH  TYR A 463     4384   3748   3471   -107     59    270       O  
ATOM   3817  N   TYR A 464      13.670  10.097 -57.778  1.00 34.54           N  
ANISOU 3817  N   TYR A 464     4875   4258   3992   -185    132    300       N  
ATOM   3818  CA  TYR A 464      14.842  10.007 -58.645  1.00 33.67           C  
ANISOU 3818  CA  TYR A 464     4763   4149   3881   -206    156    291       C  
ATOM   3819  C   TYR A 464      14.940   8.621 -59.297  1.00 33.48           C  
ANISOU 3819  C   TYR A 464     4747   4161   3812   -226    159    269       C  
ATOM   3820  O   TYR A 464      14.538   7.617 -58.705  1.00 33.20           O  
ANISOU 3820  O   TYR A 464     4715   4135   3764   -219    139    244       O  
ATOM   3821  CB  TYR A 464      16.125  10.334 -57.868  1.00 31.91           C  
ANISOU 3821  CB  TYR A 464     4530   3884   3711   -202    165    255       C  
ATOM   3822  CG  TYR A 464      16.175  11.729 -57.272  1.00 34.37           C  
ANISOU 3822  CG  TYR A 464     4834   4156   4068   -190    171    268       C  
ATOM   3823  CD1 TYR A 464      16.518  11.916 -55.942  1.00 37.09           C  
ANISOU 3823  CD1 TYR A 464     5176   4469   4446   -183    159    234       C  
ATOM   3824  CD2 TYR A 464      15.872  12.861 -58.036  1.00 38.22           C  
ANISOU 3824  CD2 TYR A 464     5319   4638   4566   -190    189    315       C  
ATOM   3825  CE1 TYR A 464      16.559  13.185 -55.377  1.00 39.81           C  
ANISOU 3825  CE1 TYR A 464     5516   4776   4832   -177    171    237       C  
ATOM   3826  CE2 TYR A 464      15.914  14.139 -57.481  1.00 38.66           C  
ANISOU 3826  CE2 TYR A 464     5366   4651   4674   -179    201    325       C  
ATOM   3827  CZ  TYR A 464      16.257  14.292 -56.145  1.00 41.18           C  
ANISOU 3827  CZ  TYR A 464     5684   4937   5024   -173    195    281       C  
ATOM   3828  OH  TYR A 464      16.304  15.548 -55.569  1.00 42.96           O  
ANISOU 3828  OH  TYR A 464     5903   5118   5300   -168    213    281       O  
ATOM   3829  N   LYS A 465      15.449   8.586 -60.523  1.00 34.10           N  
ANISOU 3829  N   LYS A 465     4830   4258   3867   -254    186    277       N  
ATOM   3830  CA  LYS A 465      15.656   7.339 -61.258  1.00 36.78           C  
ANISOU 3830  CA  LYS A 465     5179   4627   4169   -282    202    249       C  
ATOM   3831  C   LYS A 465      17.145   7.001 -61.434  1.00 38.35           C  
ANISOU 3831  C   LYS A 465     5368   4800   4406   -295    239    206       C  
ATOM   3832  O   LYS A 465      17.486   5.925 -61.938  1.00 37.91           O  
ANISOU 3832  O   LYS A 465     5314   4756   4335   -317    262    171       O  
ATOM   3833  CB  LYS A 465      14.975   7.398 -62.633  1.00 36.69           C  
ANISOU 3833  CB  LYS A 465     5185   4665   4089   -316    211    287       C  
ATOM   3834  CG  LYS A 465      13.455   7.373 -62.588  1.00 38.71           C  
ANISOU 3834  CG  LYS A 465     5448   4954   4307   -309    174    328       C  
ATOM   3835  CD  LYS A 465      12.833   7.288 -63.979  1.00 38.99           C  
ANISOU 3835  CD  LYS A 465     5500   5045   4270   -354    175    368       C  
ATOM   3836  CE  LYS A 465      12.828   5.847 -64.500  1.00 39.48           C  
ANISOU 3836  CE  LYS A 465     5579   5141   4280   -388    190    322       C  
ATOM   3837  NZ  LYS A 465      11.959   5.689 -65.704  1.00 41.18           N  
ANISOU 3837  NZ  LYS A 465     5814   5419   4413   -437    180    362       N  
ATOM   3838  N   ASP A 466      18.028   7.908 -61.017  1.00 39.29           N  
ANISOU 3838  N   ASP A 466     5471   4879   4578   -283    246    206       N  
ATOM   3839  CA  ASP A 466      19.461   7.729 -61.258  1.00 42.94           C  
ANISOU 3839  CA  ASP A 466     5917   5313   5085   -296    282    172       C  
ATOM   3840  C   ASP A 466      20.103   6.669 -60.365  1.00 45.44           C  
ANISOU 3840  C   ASP A 466     6212   5604   5449   -285    272    127       C  
ATOM   3841  O   ASP A 466      21.020   5.967 -60.794  1.00 48.04           O  
ANISOU 3841  O   ASP A 466     6528   5920   5807   -301    306     94       O  
ATOM   3842  CB  ASP A 466      20.209   9.055 -61.135  1.00 44.06           C  
ANISOU 3842  CB  ASP A 466     6047   5421   5271   -291    293    188       C  
ATOM   3843  CG  ASP A 466      20.183   9.614 -59.726  1.00 49.17           C  
ANISOU 3843  CG  ASP A 466     6683   6037   5963   -260    256    186       C  
ATOM   3844  OD1 ASP A 466      19.126   9.531 -59.059  1.00 49.47           O  
ANISOU 3844  OD1 ASP A 466     6731   6086   5979   -243    223    197       O  
ATOM   3845  OD2 ASP A 466      21.224  10.139 -59.285  1.00 54.70           O  
ANISOU 3845  OD2 ASP A 466     7365   6700   6719   -258    263    172       O  
ATOM   3846  N   ARG A 467      19.614   6.550 -59.133  1.00 46.40           N  
ANISOU 3846  N   ARG A 467     6331   5717   5582   -259    227    127       N  
ATOM   3847  CA  ARG A 467      20.199   5.642 -58.147  1.00 48.03           C  
ANISOU 3847  CA  ARG A 467     6515   5899   5835   -249    205     96       C  
ATOM   3848  C   ARG A 467      19.146   5.115 -57.172  1.00 46.81           C  
ANISOU 3848  C   ARG A 467     6372   5759   5654   -232    161    100       C  
ATOM   3849  O   ARG A 467      18.162   5.802 -56.872  1.00 46.29           O  
ANISOU 3849  O   ARG A 467     6325   5708   5557   -221    142    124       O  
ATOM   3850  CB  ARG A 467      21.323   6.344 -57.372  1.00 50.12           C  
ANISOU 3850  CB  ARG A 467     6755   6121   6165   -243    196     91       C  
ATOM   3851  CG  ARG A 467      20.893   7.659 -56.702  1.00 59.84           C  
ANISOU 3851  CG  ARG A 467     8000   7347   7391   -232    173    113       C  
ATOM   3852  CD  ARG A 467      22.024   8.317 -55.904  1.00 68.28           C  
ANISOU 3852  CD  ARG A 467     9045   8376   8521   -233    163    103       C  
ATOM   3853  NE  ARG A 467      21.857   9.773 -55.826  1.00 73.40           N  
ANISOU 3853  NE  ARG A 467     9704   9012   9170   -231    170    121       N  
ATOM   3854  CZ  ARG A 467      21.187  10.415 -54.869  1.00 76.17           C  
ANISOU 3854  CZ  ARG A 467    10069   9359   9512   -223    145    126       C  
ATOM   3855  NH1 ARG A 467      20.609   9.743 -53.877  1.00 74.56           N  
ANISOU 3855  NH1 ARG A 467     9874   9166   9290   -219    109    115       N  
ATOM   3856  NH2 ARG A 467      21.097  11.739 -54.904  1.00 77.10           N  
ANISOU 3856  NH2 ARG A 467    10192   9458   9642   -222    162    140       N  
ATOM   3857  N   ASP A 468      19.367   3.898 -56.682  1.00 44.39           N  
ANISOU 3857  N   ASP A 468     6052   5446   5370   -230    147     78       N  
ATOM   3858  CA  ASP A 468      18.505   3.289 -55.678  1.00 43.19           C  
ANISOU 3858  CA  ASP A 468     5907   5304   5197   -217    105     80       C  
ATOM   3859  C   ASP A 468      18.650   3.978 -54.338  1.00 40.18           C  
ANISOU 3859  C   ASP A 468     5525   4904   4838   -208     66     86       C  
ATOM   3860  O   ASP A 468      19.760   4.226 -53.877  1.00 40.84           O  
ANISOU 3860  O   ASP A 468     5586   4957   4973   -213     58     80       O  
ATOM   3861  CB  ASP A 468      18.833   1.804 -55.517  1.00 46.18           C  
ANISOU 3861  CB  ASP A 468     6268   5674   5604   -220    102     58       C  
ATOM   3862  CG  ASP A 468      18.293   0.959 -56.654  1.00 51.23           C  
ANISOU 3862  CG  ASP A 468     6918   6340   6207   -233    137     45       C  
ATOM   3863  OD1 ASP A 468      17.402   1.445 -57.384  1.00 54.05           O  
ANISOU 3863  OD1 ASP A 468     7302   6731   6503   -240    148     60       O  
ATOM   3864  OD2 ASP A 468      18.753  -0.195 -56.812  1.00 54.86           O  
ANISOU 3864  OD2 ASP A 468     7359   6784   6700   -240    154     21       O  
ATOM   3865  N   GLY A 469      17.514   4.291 -53.723  1.00 42.75           N  
ANISOU 3865  N   GLY A 469     6458   5121   4663   -556    304    345       N  
ATOM   3866  CA  GLY A 469      17.483   4.732 -52.338  1.00 37.29           C  
ANISOU 3866  CA  GLY A 469     5597   4480   4092   -526    197    320       C  
ATOM   3867  C   GLY A 469      17.869   3.621 -51.378  1.00 36.58           C  
ANISOU 3867  C   GLY A 469     5348   4459   4094   -490    159    267       C  
ATOM   3868  O   GLY A 469      17.851   2.429 -51.733  1.00 33.71           O  
ANISOU 3868  O   GLY A 469     4999   4121   3688   -475    185    255       O  
ATOM   3869  N   VAL A 470      18.225   4.018 -50.158  1.00 34.15           N  
ANISOU 3869  N   VAL A 470     4904   4168   3904   -473     88    233       N  
ATOM   3870  CA  VAL A 470      18.603   3.088 -49.103  1.00 33.49           C  
ANISOU 3870  CA  VAL A 470     4694   4130   3899   -433     21    184       C  
ATOM   3871  C   VAL A 470      17.434   2.171 -48.694  1.00 34.55           C  
ANISOU 3871  C   VAL A 470     4870   4331   3928   -378    -79    197       C  
ATOM   3872  O   VAL A 470      17.643   0.995 -48.377  1.00 36.36           O  
ANISOU 3872  O   VAL A 470     5054   4592   4171   -350    -92    171       O  
ATOM   3873  CB  VAL A 470      19.220   3.853 -47.884  1.00 34.60           C  
ANISOU 3873  CB  VAL A 470     4719   4253   4172   -427    -55    145       C  
ATOM   3874  CG1 VAL A 470      18.236   4.870 -47.296  1.00 33.90           C  
ANISOU 3874  CG1 VAL A 470     4683   4174   4023   -413   -148    172       C  
ATOM   3875  CG2 VAL A 470      19.730   2.905 -46.827  1.00 30.53           C  
ANISOU 3875  CG2 VAL A 470     4105   3760   3733   -383   -143     93       C  
ATOM   3876  N   VAL A 471      16.208   2.693 -48.728  1.00 33.02           N  
ANISOU 3876  N   VAL A 471     4755   4145   3646   -365   -144    233       N  
ATOM   3877  CA  VAL A 471      15.030   1.868 -48.434  1.00 31.26           C  
ANISOU 3877  CA  VAL A 471     4560   3963   3352   -320   -217    237       C  
ATOM   3878  C   VAL A 471      14.860   0.743 -49.480  1.00 29.62           C  
ANISOU 3878  C   VAL A 471     4413   3767   3073   -319   -172    246       C  
ATOM   3879  O   VAL A 471      14.882  -0.427 -49.109  1.00 29.74           O  
ANISOU 3879  O   VAL A 471     4388   3818   3092   -292   -179    223       O  
ATOM   3880  CB  VAL A 471      13.735   2.720 -48.177  1.00 32.20           C  
ANISOU 3880  CB  VAL A 471     4722   4067   3443   -305   -297    259       C  
ATOM   3881  CG1 VAL A 471      12.490   1.861 -48.210  1.00 28.45           C  
ANISOU 3881  CG1 VAL A 471     4274   3610   2926   -268   -347    258       C  
ATOM   3882  CG2 VAL A 471      13.826   3.452 -46.824  1.00 32.01           C  
ANISOU 3882  CG2 VAL A 471     4639   4041   3485   -294   -342    234       C  
ATOM   3883  N   PRO A 472      14.750   1.084 -50.785  1.00 28.68           N  
ANISOU 3883  N   PRO A 472     4408   3608   2882   -351   -124    279       N  
ATOM   3884  CA  PRO A 472      14.733   0.011 -51.804  1.00 29.36           C  
ANISOU 3884  CA  PRO A 472     4572   3693   2889   -354    -73    281       C  
ATOM   3885  C   PRO A 472      15.905  -0.968 -51.696  1.00 30.08           C  
ANISOU 3885  C   PRO A 472     4581   3802   3046   -362     25    242       C  
ATOM   3886  O   PRO A 472      15.711  -2.188 -51.765  1.00 32.91           O  
ANISOU 3886  O   PRO A 472     4933   4192   3379   -338     21    226       O  
ATOM   3887  CB  PRO A 472      14.808   0.779 -53.131  1.00 28.37           C  
ANISOU 3887  CB  PRO A 472     4610   3495   2676   -398    -14    320       C  
ATOM   3888  CG  PRO A 472      14.176   2.110 -52.830  1.00 24.29           C  
ANISOU 3888  CG  PRO A 472     4110   2951   2167   -395   -100    348       C  
ATOM   3889  CD  PRO A 472      14.521   2.416 -51.384  1.00 27.11           C  
ANISOU 3889  CD  PRO A 472     4299   3351   2649   -380   -126    317       C  
ATOM   3890  N   THR A 473      17.106  -0.440 -51.511  1.00 30.58           N  
ANISOU 3890  N   THR A 473     4570   3835   3213   -395    108    222       N  
ATOM   3891  CA  THR A 473      18.303  -1.263 -51.412  1.00 31.54           C  
ANISOU 3891  CA  THR A 473     4589   3950   3443   -402    197    175       C  
ATOM   3892  C   THR A 473      18.238  -2.256 -50.256  1.00 31.98           C  
ANISOU 3892  C   THR A 473     4537   4061   3551   -347     95    144       C  
ATOM   3893  O   THR A 473      18.457  -3.460 -50.456  1.00 34.06           O  
ANISOU 3893  O   THR A 473     4783   4340   3819   -331    127    123       O  
ATOM   3894  CB  THR A 473      19.553  -0.388 -51.300  1.00 30.60           C  
ANISOU 3894  CB  THR A 473     4381   3770   3475   -445    285    148       C  
ATOM   3895  OG1 THR A 473      19.699   0.345 -52.517  1.00 37.11           O  
ANISOU 3895  OG1 THR A 473     5335   4527   4239   -504    421    177       O  
ATOM   3896  CG2 THR A 473      20.798  -1.238 -51.096  1.00 34.03           C  
ANISOU 3896  CG2 THR A 473     4674   4181   4074   -446    354     85       C  
ATOM   3897  N   GLU A 474      17.924  -1.762 -49.061  1.00 28.29           N  
ANISOU 3897  N   GLU A 474     4020   3614   3113   -317    -22    141       N  
ATOM   3898  CA  GLU A 474      17.914  -2.625 -47.883  1.00 31.33           C  
ANISOU 3898  CA  GLU A 474     4342   4030   3530   -266   -116    114       C  
ATOM   3899  C   GLU A 474      16.733  -3.577 -47.842  1.00 31.43           C  
ANISOU 3899  C   GLU A 474     4421   4087   3435   -231   -155    131       C  
ATOM   3900  O   GLU A 474      16.889  -4.737 -47.451  1.00 31.74           O  
ANISOU 3900  O   GLU A 474     4432   4142   3485   -199   -171    110       O  
ATOM   3901  CB  GLU A 474      18.030  -1.813 -46.591  1.00 30.74           C  
ANISOU 3901  CB  GLU A 474     4227   3945   3508   -248   -219    100       C  
ATOM   3902  CG  GLU A 474      19.400  -1.145 -46.426  1.00 32.10           C  
ANISOU 3902  CG  GLU A 474     4296   4063   3837   -273   -206     62       C  
ATOM   3903  CD  GLU A 474      20.570  -2.126 -46.554  1.00 36.72           C  
ANISOU 3903  CD  GLU A 474     4780   4621   4552   -267   -173     14       C  
ATOM   3904  OE1 GLU A 474      21.551  -1.769 -47.235  1.00 38.52           O  
ANISOU 3904  OE1 GLU A 474     4934   4795   4907   -310    -68    -12       O  
ATOM   3905  OE2 GLU A 474      20.514  -3.244 -45.986  1.00 36.55           O  
ANISOU 3905  OE2 GLU A 474     4751   4618   4518   -220   -242      0       O  
ATOM   3906  N   ILE A 475      15.566  -3.096 -48.272  1.00 31.50           N  
ANISOU 3906  N   ILE A 475     4512   4102   3356   -236   -171    164       N  
ATOM   3907  CA  ILE A 475      14.375  -3.939 -48.362  1.00 30.42           C  
ANISOU 3907  CA  ILE A 475     4422   3988   3148   -208   -204    172       C  
ATOM   3908  C   ILE A 475      14.560  -5.099 -49.377  1.00 31.76           C  
ANISOU 3908  C   ILE A 475     4620   4166   3280   -213   -143    166       C  
ATOM   3909  O   ILE A 475      14.021  -6.188 -49.162  1.00 30.51           O  
ANISOU 3909  O   ILE A 475     4461   4028   3102   -183   -163    154       O  
ATOM   3910  CB  ILE A 475      13.086  -3.100 -48.654  1.00 30.31           C  
ANISOU 3910  CB  ILE A 475     4470   3956   3090   -210   -254    198       C  
ATOM   3911  CG1 ILE A 475      11.847  -3.777 -48.063  1.00 29.66           C  
ANISOU 3911  CG1 ILE A 475     4384   3880   3004   -174   -301    185       C  
ATOM   3912  CG2 ILE A 475      12.886  -2.877 -50.148  1.00 28.35           C  
ANISOU 3912  CG2 ILE A 475     4316   3682   2775   -238   -232    223       C  
ATOM   3913  CD1 ILE A 475      10.575  -2.916 -48.116  1.00 27.00           C  
ANISOU 3913  CD1 ILE A 475     4070   3508   2681   -171   -359    194       C  
ATOM   3914  N   THR A 476      15.327  -4.860 -50.453  1.00 31.51           N  
ANISOU 3914  N   THR A 476     4623   4107   3240   -253    -55    171       N  
ATOM   3915  CA  THR A 476      15.598  -5.875 -51.492  1.00 31.64           C  
ANISOU 3915  CA  THR A 476     4690   4118   3215   -265     26    161       C  
ATOM   3916  C   THR A 476      16.400  -7.071 -50.943  1.00 34.32           C  
ANISOU 3916  C   THR A 476     4929   4475   3636   -242     54    122       C  
ATOM   3917  O   THR A 476      16.161  -8.230 -51.325  1.00 33.25           O  
ANISOU 3917  O   THR A 476     4816   4352   3464   -227     73    110       O  
ATOM   3918  CB  THR A 476      16.354  -5.264 -52.700  1.00 34.26           C  
ANISOU 3918  CB  THR A 476     5103   4393   3521   -321    150    170       C  
ATOM   3919  OG1 THR A 476      15.545  -4.260 -53.334  1.00 28.51           O  
ANISOU 3919  OG1 THR A 476     4503   3634   2694   -338    107    211       O  
ATOM   3920  CG2 THR A 476      16.753  -6.334 -53.730  1.00 30.88           C  
ANISOU 3920  CG2 THR A 476     4739   3945   3050   -338    260    151       C  
ATOM   3921  N   LYS A 477      17.350  -6.773 -50.055  1.00 34.87           N  
ANISOU 3921  N   LYS A 477     4890   4535   3823   -236     43     99       N  
ATOM   3922  CA  LYS A 477      18.210  -7.786 -49.445  1.00 33.65           C  
ANISOU 3922  CA  LYS A 477     4636   4378   3771   -207     38     59       C  
ATOM   3923  C   LYS A 477      17.402  -8.761 -48.595  1.00 33.35           C  
ANISOU 3923  C   LYS A 477     4612   4377   3684   -155    -54     62       C  
ATOM   3924  O   LYS A 477      17.568  -9.971 -48.710  1.00 32.79           O  
ANISOU 3924  O   LYS A 477     4526   4310   3624   -135    -33     44       O  
ATOM   3925  CB  LYS A 477      19.308  -7.124 -48.606  1.00 34.40           C  
ANISOU 3925  CB  LYS A 477     4621   4438   4013   -206      0     30       C  
ATOM   3926  CG  LYS A 477      20.512  -6.648 -49.423  1.00 33.84           C  
ANISOU 3926  CG  LYS A 477     4486   4306   4066   -257    132      1       C  
ATOM   3927  CD  LYS A 477      21.375  -5.670 -48.633  1.00 35.75           C  
ANISOU 3927  CD  LYS A 477     4621   4503   4458   -262     76    -27       C  
ATOM   3928  CE  LYS A 477      22.326  -4.903 -49.553  1.00 45.07           C  
ANISOU 3928  CE  LYS A 477     5757   5612   5755   -327    237    -50       C  
ATOM   3929  NZ  LYS A 477      23.035  -3.777 -48.857  1.00 45.97           N  
ANISOU 3929  NZ  LYS A 477     5770   5678   6019   -339    183    -77       N  
ATOM   3930  N   VAL A 478      16.521  -8.229 -47.750  1.00 33.30           N  
ANISOU 3930  N   VAL A 478     4640   4384   3627   -136   -138     82       N  
ATOM   3931  CA  VAL A 478      15.703  -9.078 -46.897  1.00 31.75           C  
ANISOU 3931  CA  VAL A 478     4474   4202   3386    -94   -195     83       C  
ATOM   3932  C   VAL A 478      14.659  -9.803 -47.745  1.00 31.05           C  
ANISOU 3932  C   VAL A 478     4439   4132   3226    -97   -158     93       C  
ATOM   3933  O   VAL A 478      14.403 -10.989 -47.521  1.00 34.54           O  
ANISOU 3933  O   VAL A 478     4885   4579   3658    -70   -156     81       O  
ATOM   3934  CB  VAL A 478      15.047  -8.306 -45.729  1.00 30.94           C  
ANISOU 3934  CB  VAL A 478     4406   4089   3259    -78   -265     93       C  
ATOM   3935  CG1 VAL A 478      14.194  -9.245 -44.900  1.00 29.80           C  
ANISOU 3935  CG1 VAL A 478     4314   3939   3069    -42   -282     91       C  
ATOM   3936  CG2 VAL A 478      16.104  -7.658 -44.848  1.00 28.01           C  
ANISOU 3936  CG2 VAL A 478     3996   3690   2956    -71   -327     77       C  
ATOM   3937  N   PHE A 479      14.090  -9.105 -48.727  1.00 29.90           N  
ANISOU 3937  N   PHE A 479     4341   3985   3033   -127   -140    111       N  
ATOM   3938  CA  PHE A 479      13.192  -9.724 -49.713  1.00 30.69           C  
ANISOU 3938  CA  PHE A 479     4501   4086   3072   -131   -131    113       C  
ATOM   3939  C   PHE A 479      13.793 -10.964 -50.385  1.00 32.46           C  
ANISOU 3939  C   PHE A 479     4726   4315   3291   -131    -66     92       C  
ATOM   3940  O   PHE A 479      13.113 -11.992 -50.508  1.00 31.16           O  
ANISOU 3940  O   PHE A 479     4578   4156   3106   -112    -77     80       O  
ATOM   3941  CB  PHE A 479      12.749  -8.745 -50.809  1.00 29.42           C  
ANISOU 3941  CB  PHE A 479     4421   3902   2855   -162   -141    135       C  
ATOM   3942  CG  PHE A 479      12.036  -9.426 -51.961  1.00 32.68           C  
ANISOU 3942  CG  PHE A 479     4919   4299   3199   -165   -153    131       C  
ATOM   3943  CD1 PHE A 479      10.703  -9.820 -51.841  1.00 31.28           C  
ANISOU 3943  CD1 PHE A 479     4743   4111   3032   -140   -233    120       C  
ATOM   3944  CD2 PHE A 479      12.714  -9.729 -53.139  1.00 32.06           C  
ANISOU 3944  CD2 PHE A 479     4920   4202   3058   -194    -78    128       C  
ATOM   3945  CE1 PHE A 479      10.053 -10.472 -52.898  1.00 38.29           C  
ANISOU 3945  CE1 PHE A 479     5707   4973   3869   -140   -271    106       C  
ATOM   3946  CE2 PHE A 479      12.074 -10.378 -54.198  1.00 33.88           C  
ANISOU 3946  CE2 PHE A 479     5256   4406   3208   -196   -102    120       C  
ATOM   3947  CZ  PHE A 479      10.741 -10.750 -54.080  1.00 32.83           C  
ANISOU 3947  CZ  PHE A 479     5120   4266   3087   -166   -215    108       C  
ATOM   3948  N   ASN A 480      15.036 -10.844 -50.850  1.00 33.98           N  
ANISOU 3948  N   ASN A 480     4897   4495   3518   -156     11     82       N  
ATOM   3949  CA  ASN A 480      15.756 -11.974 -51.447  1.00 36.25           C  
ANISOU 3949  CA  ASN A 480     5172   4774   3825   -159     94     54       C  
ATOM   3950  C   ASN A 480      15.926 -13.141 -50.466  1.00 36.16           C  
ANISOU 3950  C   ASN A 480     5087   4777   3876   -113     58     33       C  
ATOM   3951  O   ASN A 480      15.734 -14.288 -50.842  1.00 37.79           O  
ANISOU 3951  O   ASN A 480     5308   4986   4063   -101     85     17       O  
ATOM   3952  CB  ASN A 480      17.112 -11.535 -52.014  1.00 37.18           C  
ANISOU 3952  CB  ASN A 480     5260   4855   4013   -198    206     37       C  
ATOM   3953  CG  ASN A 480      16.985 -10.762 -53.333  1.00 41.66           C  
ANISOU 3953  CG  ASN A 480     5957   5386   4484   -250    285     56       C  
ATOM   3954  OD1 ASN A 480      16.045 -10.967 -54.109  1.00 42.45           O  
ANISOU 3954  OD1 ASN A 480     6183   5485   4462   -253    259     71       O  
ATOM   3955  ND2 ASN A 480      17.949  -9.878 -53.594  1.00 38.73           N  
ANISOU 3955  ND2 ASN A 480     5568   4972   4175   -290    379     51       N  
ATOM   3956  N   GLN A 481      16.278 -12.842 -49.215  1.00 35.64           N  
ANISOU 3956  N   GLN A 481     4959   4710   3874    -86     -9     33       N  
ATOM   3957  CA  GLN A 481      16.320 -13.858 -48.167  1.00 36.47           C  
ANISOU 3957  CA  GLN A 481     5037   4810   4008    -38    -64     22       C  
ATOM   3958  C   GLN A 481      14.950 -14.524 -48.041  1.00 35.59           C  
ANISOU 3958  C   GLN A 481     4990   4714   3817    -22    -79     34       C  
ATOM   3959  O   GLN A 481      14.855 -15.752 -47.992  1.00 34.68           O  
ANISOU 3959  O   GLN A 481     4876   4596   3705      1    -65     20       O  
ATOM   3960  CB  GLN A 481      16.685 -13.255 -46.810  1.00 34.88           C  
ANISOU 3960  CB  GLN A 481     4815   4590   3849    -12   -157     25       C  
ATOM   3961  CG  GLN A 481      18.091 -12.713 -46.673  1.00 38.50           C  
ANISOU 3961  CG  GLN A 481     5183   5014   4429    -18   -174      0       C  
ATOM   3962  CD  GLN A 481      18.308 -12.008 -45.325  1.00 44.62           C  
ANISOU 3962  CD  GLN A 481     5966   5763   5226      9   -295      1       C  
ATOM   3963  OE1 GLN A 481      17.548 -12.201 -44.365  1.00 42.32           O  
ANISOU 3963  OE1 GLN A 481     5760   5468   4852     38   -356     18       O  
ATOM   3964  NE2 GLN A 481      19.342 -11.176 -45.257  1.00 48.82           N  
ANISOU 3964  NE2 GLN A 481     6417   6262   5872     -5   -321    -22       N  
ATOM   3965  N   ARG A 482      13.896 -13.708 -47.990  1.00 32.08           N  
ANISOU 3965  N   ARG A 482     4589   4277   3324    -34   -105     53       N  
ATOM   3966  CA  ARG A 482      12.545 -14.234 -47.860  1.00 32.82           C  
ANISOU 3966  CA  ARG A 482     4719   4364   3385    -22   -113     52       C  
ATOM   3967  C   ARG A 482      12.246 -15.233 -48.980  1.00 34.18           C  
ANISOU 3967  C   ARG A 482     4907   4542   3539    -29    -78     35       C  
ATOM   3968  O   ARG A 482      11.780 -16.351 -48.720  1.00 33.13           O  
ANISOU 3968  O   ARG A 482     4774   4399   3414     -8    -66     20       O  
ATOM   3969  CB  ARG A 482      11.524 -13.095 -47.851  1.00 32.82           C  
ANISOU 3969  CB  ARG A 482     4741   4355   3373    -38   -146     65       C  
ATOM   3970  CG  ARG A 482      10.091 -13.542 -47.588  1.00 32.58           C  
ANISOU 3970  CG  ARG A 482     4721   4297   3362    -27   -149     51       C  
ATOM   3971  CD  ARG A 482       9.308 -13.775 -48.876  1.00 33.87           C  
ANISOU 3971  CD  ARG A 482     4896   4451   3522    -40   -172     38       C  
ATOM   3972  NE  ARG A 482       7.944 -14.238 -48.613  1.00 31.53           N  
ANISOU 3972  NE  ARG A 482     4579   4111   3290    -30   -179     10       N  
ATOM   3973  CZ  ARG A 482       6.881 -13.881 -49.328  1.00 34.45           C  
ANISOU 3973  CZ  ARG A 482     4942   4442   3703    -37   -242     -7       C  
ATOM   3974  NH1 ARG A 482       7.007 -13.033 -50.351  1.00 33.12           N  
ANISOU 3974  NH1 ARG A 482     4818   4277   3489    -53   -310      9       N  
ATOM   3975  NH2 ARG A 482       5.683 -14.357 -49.007  1.00 32.84           N  
ANISOU 3975  NH2 ARG A 482     4693   4183   3602    -27   -238    -45       N  
ATOM   3976  N   LYS A 483      12.545 -14.824 -50.213  1.00 34.14           N  
ANISOU 3976  N   LYS A 483     4931   4542   3501    -61    -55     36       N  
ATOM   3977  CA  LYS A 483      12.271 -15.611 -51.408  1.00 36.52           C  
ANISOU 3977  CA  LYS A 483     5282   4835   3758    -73    -29     18       C  
ATOM   3978  C   LYS A 483      12.921 -16.992 -51.361  1.00 37.52           C  
ANISOU 3978  C   LYS A 483     5376   4965   3914    -55     27     -7       C  
ATOM   3979  O   LYS A 483      12.284 -17.991 -51.693  1.00 37.88           O  
ANISOU 3979  O   LYS A 483     5441   5003   3948    -46     26    -27       O  
ATOM   3980  CB  LYS A 483      12.701 -14.842 -52.663  1.00 38.14           C  
ANISOU 3980  CB  LYS A 483     5564   5026   3900   -113      4     27       C  
ATOM   3981  CG  LYS A 483      12.321 -15.523 -53.977  1.00 44.23           C  
ANISOU 3981  CG  LYS A 483     6438   5772   4594   -127     16      7       C  
ATOM   3982  CD  LYS A 483      12.548 -14.613 -55.184  1.00 53.04           C  
ANISOU 3982  CD  LYS A 483     7688   6852   5614   -168     39     23       C  
ATOM   3983  CE  LYS A 483      12.120 -15.313 -56.482  1.00 58.30           C  
ANISOU 3983  CE  LYS A 483     8498   7477   6177   -180     34      1       C  
ATOM   3984  NZ  LYS A 483      12.268 -14.444 -57.698  1.00 62.06           N  
ANISOU 3984  NZ  LYS A 483     9160   7895   6525   -220     52     19       N  
ATOM   3985  N   GLU A 484      14.181 -17.042 -50.940  1.00 39.77           N  
ANISOU 3985  N   GLU A 484     5603   5251   4257    -50     67    -11       N  
ATOM   3986  CA  GLU A 484      14.890 -18.304 -50.786  1.00 41.81           C  
ANISOU 3986  CA  GLU A 484     5815   5500   4571    -27    107    -36       C  
ATOM   3987  C   GLU A 484      14.118 -19.254 -49.871  1.00 41.76           C  
ANISOU 3987  C   GLU A 484     5808   5490   4567     12     62    -36       C  
ATOM   3988  O   GLU A 484      13.878 -20.415 -50.231  1.00 40.11           O  
ANISOU 3988  O   GLU A 484     5608   5274   4357     22     92    -56       O  
ATOM   3989  CB  GLU A 484      16.294 -18.067 -50.221  1.00 43.28           C  
ANISOU 3989  CB  GLU A 484     5918   5669   4860    -17    116    -46       C  
ATOM   3990  CG  GLU A 484      17.149 -19.335 -50.151  1.00 48.87           C  
ANISOU 3990  CG  GLU A 484     6565   6350   5654      9    149    -79       C  
ATOM   3991  CD  GLU A 484      18.471 -19.133 -49.427  1.00 56.22           C  
ANISOU 3991  CD  GLU A 484     7393   7242   6725     30    115    -98       C  
ATOM   3992  OE1 GLU A 484      18.708 -18.032 -48.881  1.00 59.77           O  
ANISOU 3992  OE1 GLU A 484     7823   7689   7196     26     60    -84       O  
ATOM   3993  OE2 GLU A 484      19.280 -20.082 -49.396  1.00 58.53           O  
ANISOU 3993  OE2 GLU A 484     7618   7498   7121     54    133   -132       O  
ATOM   3994  N   HIS A 485      13.735 -18.752 -48.694  1.00 39.24           N  
ANISOU 3994  N   HIS A 485     5491   5166   4250     32      4    -14       N  
ATOM   3995  CA  HIS A 485      13.081 -19.577 -47.680  1.00 37.00           C  
ANISOU 3995  CA  HIS A 485     5234   4859   3967     65    -12    -12       C  
ATOM   3996  C   HIS A 485      11.691 -20.020 -48.092  1.00 35.71           C  
ANISOU 3996  C   HIS A 485     5096   4687   3785     55      9    -23       C  
ATOM   3997  O   HIS A 485      11.282 -21.137 -47.775  1.00 37.93           O  
ANISOU 3997  O   HIS A 485     5388   4943   4080     73     34    -35       O  
ATOM   3998  CB  HIS A 485      13.041 -18.858 -46.334  1.00 36.41           C  
ANISOU 3998  CB  HIS A 485     5189   4762   3884     83    -62     10       C  
ATOM   3999  CG  HIS A 485      14.369 -18.811 -45.651  1.00 36.14           C  
ANISOU 3999  CG  HIS A 485     5134   4710   3888    109   -116     12       C  
ATOM   4000  ND1 HIS A 485      14.922 -19.911 -45.033  1.00 36.77           N  
ANISOU 4000  ND1 HIS A 485     5227   4750   3992    150   -143      5       N  
ATOM   4001  CD2 HIS A 485      15.264 -17.805 -45.507  1.00 37.17           C  
ANISOU 4001  CD2 HIS A 485     5226   4842   4055    103   -162     13       C  
ATOM   4002  CE1 HIS A 485      16.100 -19.584 -44.531  1.00 37.45           C  
ANISOU 4002  CE1 HIS A 485     5281   4811   4137    172   -221     -1       C  
ATOM   4003  NE2 HIS A 485      16.329 -18.310 -44.800  1.00 40.83           N  
ANISOU 4003  NE2 HIS A 485     5671   5264   4580    142   -229      1       N  
ATOM   4004  N   LYS A 486      10.975 -19.157 -48.808  1.00 33.82           N  
ANISOU 4004  N   LYS A 486     4865   4458   3528     26    -11    -23       N  
ATOM   4005  CA  LYS A 486       9.671 -19.526 -49.352  1.00 32.06           C  
ANISOU 4005  CA  LYS A 486     4650   4211   3319     18    -20    -47       C  
ATOM   4006  C   LYS A 486       9.831 -20.671 -50.357  1.00 31.21           C  
ANISOU 4006  C   LYS A 486     4553   4105   3199     16      3    -75       C  
ATOM   4007  O   LYS A 486       8.984 -21.561 -50.427  1.00 31.41           O  
ANISOU 4007  O   LYS A 486     4573   4102   3262     23      8   -102       O  
ATOM   4008  CB  LYS A 486       8.957 -18.322 -49.980  1.00 31.21           C  
ANISOU 4008  CB  LYS A 486     4556   4099   3204     -5    -79    -43       C  
ATOM   4009  CG  LYS A 486       7.529 -18.632 -50.413  1.00 31.94           C  
ANISOU 4009  CG  LYS A 486     4637   4144   3353     -7   -121    -78       C  
ATOM   4010  CD  LYS A 486       6.726 -17.407 -50.840  1.00 35.42           C  
ANISOU 4010  CD  LYS A 486     5083   4559   3815    -20   -205    -78       C  
ATOM   4011  CE  LYS A 486       5.323 -17.854 -51.282  1.00 39.04           C  
ANISOU 4011  CE  LYS A 486     5509   4950   4373    -16   -269   -127       C  
ATOM   4012  NZ  LYS A 486       4.391 -16.765 -51.721  1.00 41.70           N  
ANISOU 4012  NZ  LYS A 486     5838   5237   4768    -20   -381   -138       N  
ATOM   4013  N   GLY A 487      10.925 -20.639 -51.118  1.00 31.03           N  
ANISOU 4013  N   GLY A 487     4546   4107   3138      3     30    -73       N  
ATOM   4014  CA  GLY A 487      11.283 -21.720 -52.044  1.00 31.86           C  
ANISOU 4014  CA  GLY A 487     4671   4207   3226     -1     75   -103       C  
ATOM   4015  C   GLY A 487      11.464 -23.048 -51.321  1.00 33.05           C  
ANISOU 4015  C   GLY A 487     4782   4346   3430     30    110   -115       C  
ATOM   4016  O   GLY A 487      10.953 -24.080 -51.763  1.00 31.62           O  
ANISOU 4016  O   GLY A 487     4613   4146   3256     33    124   -145       O  
ATOM   4017  N   TYR A 488      12.169 -23.018 -50.189  1.00 33.21           N  
ANISOU 4017  N   TYR A 488     4767   4366   3485     56    112    -94       N  
ATOM   4018  CA  TYR A 488      12.368 -24.216 -49.382  1.00 33.22           C  
ANISOU 4018  CA  TYR A 488     4756   4339   3526     92    129    -98       C  
ATOM   4019  C   TYR A 488      11.039 -24.714 -48.861  1.00 33.84           C  
ANISOU 4019  C   TYR A 488     4860   4385   3612     99    133   -102       C  
ATOM   4020  O   TYR A 488      10.790 -25.923 -48.860  1.00 34.06           O  
ANISOU 4020  O   TYR A 488     4892   4386   3665    112    168   -121       O  
ATOM   4021  CB  TYR A 488      13.339 -23.977 -48.219  1.00 30.51           C  
ANISOU 4021  CB  TYR A 488     4400   3982   3211    124     94    -74       C  
ATOM   4022  CG  TYR A 488      14.732 -23.568 -48.649  1.00 34.93           C  
ANISOU 4022  CG  TYR A 488     4902   4553   3817    119     96    -83       C  
ATOM   4023  CD1 TYR A 488      15.264 -23.992 -49.870  1.00 36.47           C  
ANISOU 4023  CD1 TYR A 488     5069   4754   4033     97    166   -116       C  
ATOM   4024  CD2 TYR A 488      15.526 -22.760 -47.832  1.00 36.52           C  
ANISOU 4024  CD2 TYR A 488     5079   4744   4053    134     35    -67       C  
ATOM   4025  CE1 TYR A 488      16.549 -23.611 -50.273  1.00 37.25           C  
ANISOU 4025  CE1 TYR A 488     5106   4843   4205     85    203   -134       C  
ATOM   4026  CE2 TYR A 488      16.814 -22.373 -48.224  1.00 37.22           C  
ANISOU 4026  CE2 TYR A 488     5090   4825   4226    126     45    -87       C  
ATOM   4027  CZ  TYR A 488      17.318 -22.804 -49.444  1.00 38.81           C  
ANISOU 4027  CZ  TYR A 488     5254   5027   4466    100    142   -122       C  
ATOM   4028  OH  TYR A 488      18.590 -22.430 -49.841  1.00 39.88           O  
ANISOU 4028  OH  TYR A 488     5305   5136   4713     86    186   -151       O  
ATOM   4029  N   MET A 489      10.189 -23.772 -48.440  1.00 34.79           N  
ANISOU 4029  N   MET A 489     4992   4499   3727     86    111    -90       N  
ATOM   4030  CA  MET A 489       8.914 -24.090 -47.806  1.00 35.41           C  
ANISOU 4030  CA  MET A 489     5083   4525   3847     87    140   -101       C  
ATOM   4031  C   MET A 489       7.954 -24.766 -48.773  1.00 35.33           C  
ANISOU 4031  C   MET A 489     5044   4494   3885     72    143   -146       C  
ATOM   4032  O   MET A 489       7.366 -25.798 -48.452  1.00 34.28           O  
ANISOU 4032  O   MET A 489     4908   4313   3805     79    194   -168       O  
ATOM   4033  CB  MET A 489       8.254 -22.830 -47.223  1.00 36.63           C  
ANISOU 4033  CB  MET A 489     5243   4666   4009     75    125    -87       C  
ATOM   4034  CG  MET A 489       6.874 -23.100 -46.629  1.00 36.86           C  
ANISOU 4034  CG  MET A 489     5269   4621   4116     68    184   -112       C  
ATOM   4035  SD  MET A 489       5.889 -21.627 -46.314  1.00 48.64           S  
ANISOU 4035  SD  MET A 489     6737   6083   5661     46    172   -117       S  
ATOM   4036  CE  MET A 489       5.375 -21.175 -47.971  1.00 40.38           C  
ANISOU 4036  CE  MET A 489     5625   5063   4656     27     64   -148       C  
ATOM   4037  N   LEU A 490       7.787 -24.170 -49.951  1.00 35.87           N  
ANISOU 4037  N   LEU A 490     5106   4589   3936     50     83   -161       N  
ATOM   4038  CA  LEU A 490       6.855 -24.704 -50.936  1.00 36.56           C  
ANISOU 4038  CA  LEU A 490     5183   4644   4065     37     46   -209       C  
ATOM   4039  C   LEU A 490       7.276 -26.085 -51.427  1.00 34.77           C  
ANISOU 4039  C   LEU A 490     4967   4416   3829     45     86   -234       C  
ATOM   4040  O   LEU A 490       6.428 -26.946 -51.653  1.00 33.14           O  
ANISOU 4040  O   LEU A 490     4739   4162   3692     45     86   -277       O  
ATOM   4041  CB  LEU A 490       6.702 -23.743 -52.109  1.00 36.32           C  
ANISOU 4041  CB  LEU A 490     5187   4626   3985     17    -47   -215       C  
ATOM   4042  CG  LEU A 490       5.854 -22.497 -51.861  1.00 38.88           C  
ANISOU 4042  CG  LEU A 490     5489   4927   4358      9   -112   -209       C  
ATOM   4043  CD1 LEU A 490       5.698 -21.751 -53.168  1.00 37.61           C  
ANISOU 4043  CD1 LEU A 490     5393   4761   4136     -6   -223   -216       C  
ATOM   4044  CD2 LEU A 490       4.490 -22.852 -51.295  1.00 38.84           C  
ANISOU 4044  CD2 LEU A 490     5408   4845   4503     14   -108   -251       C  
ATOM   4045  N   ALA A 491       8.589 -26.273 -51.585  1.00 33.94           N  
ANISOU 4045  N   ALA A 491     4885   4353   3659     52    121   -213       N  
ATOM   4046  CA  ALA A 491       9.167 -27.547 -52.017  1.00 33.80           C  
ANISOU 4046  CA  ALA A 491     4872   4331   3639     61    170   -237       C  
ATOM   4047  C   ALA A 491       8.921 -28.647 -50.985  1.00 33.89           C  
ANISOU 4047  C   ALA A 491     4859   4302   3716     87    221   -238       C  
ATOM   4048  O   ALA A 491       8.658 -29.788 -51.346  1.00 36.15           O  
ANISOU 4048  O   ALA A 491     5141   4560   4034     90    249   -272       O  
ATOM   4049  CB  ALA A 491      10.649 -27.388 -52.280  1.00 30.88           C  
ANISOU 4049  CB  ALA A 491     4509   3996   3227     62    208   -221       C  
ATOM   4050  N   ALA A 492       9.000 -28.291 -49.701  1.00 33.27           N  
ANISOU 4050  N   ALA A 492     4784   4212   3647    105    236   -199       N  
ATOM   4051  CA  ALA A 492       8.732 -29.235 -48.621  1.00 33.75           C  
ANISOU 4051  CA  ALA A 492     4863   4214   3745    129    293   -192       C  
ATOM   4052  C   ALA A 492       7.266 -29.661 -48.627  1.00 33.67           C  
ANISOU 4052  C   ALA A 492     4834   4144   3817    111    329   -230       C  
ATOM   4053  O   ALA A 492       6.927 -30.821 -48.336  1.00 35.44           O  
ANISOU 4053  O   ALA A 492     5064   4312   4089    119    391   -248       O  
ATOM   4054  CB  ALA A 492       9.125 -28.635 -47.280  1.00 31.67           C  
ANISOU 4054  CB  ALA A 492     4649   3935   3447    149    292   -144       C  
ATOM   4055  N   GLN A 493       6.418 -28.708 -48.993  1.00 31.54           N  
ANISOU 4055  N   GLN A 493     4531   3873   3578     86    286   -248       N  
ATOM   4056  CA  GLN A 493       4.977 -28.880 -49.105  1.00 33.33           C  
ANISOU 4056  CA  GLN A 493     4707   4029   3927     67    298   -298       C  
ATOM   4057  C   GLN A 493       4.624 -29.776 -50.302  1.00 34.63           C  
ANISOU 4057  C   GLN A 493     4841   4181   4136     60    255   -356       C  
ATOM   4058  O   GLN A 493       3.806 -30.692 -50.182  1.00 33.64           O  
ANISOU 4058  O   GLN A 493     4678   3983   4122     55    303   -400       O  
ATOM   4059  CB  GLN A 493       4.341 -27.483 -49.227  1.00 34.43           C  
ANISOU 4059  CB  GLN A 493     4816   4170   4097     50    234   -301       C  
ATOM   4060  CG  GLN A 493       2.823 -27.393 -49.324  1.00 35.12           C  
ANISOU 4060  CG  GLN A 493     4822   4167   4353     32    226   -363       C  
ATOM   4061  CD  GLN A 493       2.349 -25.949 -49.496  1.00 39.13           C  
ANISOU 4061  CD  GLN A 493     5299   4676   4891     21    143   -362       C  
ATOM   4062  OE1 GLN A 493       1.904 -25.555 -50.576  1.00 39.22           O  
ANISOU 4062  OE1 GLN A 493     5284   4682   4934     16     12   -396       O  
ATOM   4063  NE2 GLN A 493       2.472 -25.150 -48.438  1.00 35.70           N  
ANISOU 4063  NE2 GLN A 493     4888   4242   4436     21    209   -324       N  
ATOM   4064  N   ARG A 494       5.240 -29.518 -51.454  1.00 35.25           N  
ANISOU 4064  N   ARG A 494     4948   4318   4126     55    174   -359       N  
ATOM   4065  CA  ARG A 494       5.031 -30.380 -52.616  1.00 38.18           C  
ANISOU 4065  CA  ARG A 494     5328   4672   4507     48    131   -414       C  
ATOM   4066  C   ARG A 494       5.482 -31.812 -52.326  1.00 39.79           C  
ANISOU 4066  C   ARG A 494     5533   4861   4725     63    223   -421       C  
ATOM   4067  O   ARG A 494       4.759 -32.753 -52.634  1.00 41.81           O  
ANISOU 4067  O   ARG A 494     5761   5060   5068     59    226   -474       O  
ATOM   4068  CB  ARG A 494       5.733 -29.833 -53.850  1.00 37.54           C  
ANISOU 4068  CB  ARG A 494     5322   4642   4299     37     58   -411       C  
ATOM   4069  CG  ARG A 494       5.135 -28.536 -54.373  1.00 38.85           C  
ANISOU 4069  CG  ARG A 494     5508   4802   4450     23    -58   -412       C  
ATOM   4070  CD  ARG A 494       5.723 -28.223 -55.740  1.00 37.61           C  
ANISOU 4070  CD  ARG A 494     5469   4667   4153      7   -118   -418       C  
ATOM   4071  NE  ARG A 494       7.153 -27.951 -55.650  1.00 32.54           N  
ANISOU 4071  NE  ARG A 494     4867   4090   3408      5    -23   -370       N  
ATOM   4072  CZ  ARG A 494       7.676 -26.746 -55.438  1.00 30.85           C  
ANISOU 4072  CZ  ARG A 494     4669   3914   3141     -3    -23   -323       C  
ATOM   4073  NH1 ARG A 494       6.889 -25.689 -55.310  1.00 27.51           N  
ANISOU 4073  NH1 ARG A 494     4236   3475   2740     -6   -112   -312       N  
ATOM   4074  NH2 ARG A 494       8.992 -26.598 -55.372  1.00 29.95           N  
ANISOU 4074  NH2 ARG A 494     4569   3842   2971     -6     67   -293       N  
ATOM   4075  N   ASN A 495       6.662 -31.959 -51.717  1.00 39.58           N  
ANISOU 4075  N   ASN A 495     5533   4874   4629     83    285   -370       N  
ATOM   4076  CA  ASN A 495       7.172 -33.258 -51.282  1.00 41.20           C  
ANISOU 4076  CA  ASN A 495     5745   5056   4853    106    362   -369       C  
ATOM   4077  C   ASN A 495       6.211 -33.981 -50.332  1.00 42.33           C  
ANISOU 4077  C   ASN A 495     5871   5115   5096    109    433   -379       C  
ATOM   4078  O   ASN A 495       6.048 -35.205 -50.412  1.00 43.27           O  
ANISOU 4078  O   ASN A 495     5985   5189   5268    115    482   -408       O  
ATOM   4079  CB  ASN A 495       8.551 -33.105 -50.620  1.00 41.85           C  
ANISOU 4079  CB  ASN A 495     5853   5176   4873    134    384   -313       C  
ATOM   4080  CG  ASN A 495       9.662 -32.779 -51.618  1.00 42.25           C  
ANISOU 4080  CG  ASN A 495     5907   5284   4862    128    363   -319       C  
ATOM   4081  OD1 ASN A 495       9.622 -33.191 -52.780  1.00 43.49           O  
ANISOU 4081  OD1 ASN A 495     6077   5443   5003    109    362   -363       O  
ATOM   4082  ND2 ASN A 495      10.669 -32.044 -51.157  1.00 39.98           N  
ANISOU 4082  ND2 ASN A 495     5617   5029   4545    141    352   -278       N  
ATOM   4083  N   GLY A 496       5.583 -33.213 -49.437  1.00 43.53           N  
ANISOU 4083  N   GLY A 496     6023   5238   5279    103    455   -357       N  
ATOM   4084  CA  GLY A 496       4.572 -33.729 -48.513  1.00 41.95           C  
ANISOU 4084  CA  GLY A 496     5819   4937   5184     96    557   -372       C  
ATOM   4085  C   GLY A 496       3.393 -34.363 -49.232  1.00 43.62           C  
ANISOU 4085  C   GLY A 496     5948   5082   5543     71    556   -452       C  
ATOM   4086  O   GLY A 496       2.921 -35.436 -48.839  1.00 45.86           O  
ANISOU 4086  O   GLY A 496     6227   5284   5915     69    652   -478       O  
ATOM   4087  N   GLU A 497       2.934 -33.705 -50.298  1.00 43.24           N  
ANISOU 4087  N   GLU A 497     5846   5060   5525     55    436   -495       N  
ATOM   4088  CA  GLU A 497       1.797 -34.177 -51.094  1.00 43.58           C  
ANISOU 4088  CA  GLU A 497     5808   5030   5721     36    383   -582       C  
ATOM   4089  C   GLU A 497       2.124 -35.468 -51.838  1.00 43.44           C  
ANISOU 4089  C   GLU A 497     5806   5011   5689     42    377   -617       C  
ATOM   4090  O   GLU A 497       1.258 -36.327 -52.008  1.00 43.25           O  
ANISOU 4090  O   GLU A 497     5720   4899   5813     30    396   -684       O  
ATOM   4091  CB  GLU A 497       1.316 -33.096 -52.066  1.00 43.08           C  
ANISOU 4091  CB  GLU A 497     5716   4983   5670     25    219   -614       C  
ATOM   4092  CG  GLU A 497       0.791 -31.823 -51.392  1.00 43.19           C  
ANISOU 4092  CG  GLU A 497     5692   4980   5740     18    219   -594       C  
ATOM   4093  CD  GLU A 497      -0.297 -32.078 -50.341  1.00 44.64           C  
ANISOU 4093  CD  GLU A 497     5793   5044   6126      3    354   -629       C  
ATOM   4094  OE1 GLU A 497      -1.308 -32.747 -50.648  1.00 45.66           O  
ANISOU 4094  OE1 GLU A 497     5828   5072   6449    -11    349   -712       O  
ATOM   4095  OE2 GLU A 497      -0.142 -31.588 -49.205  1.00 44.63           O  
ANISOU 4095  OE2 GLU A 497     5826   5037   6093      2    470   -580       O  
ATOM   4096  N   ILE A 498       3.381 -35.598 -52.261  1.00 43.32           N  
ANISOU 4096  N   ILE A 498     5865   5082   5512     58    361   -577       N  
ATOM   4097  CA  ILE A 498       3.881 -36.833 -52.871  1.00 45.62           C  
ANISOU 4097  CA  ILE A 498     6181   5373   5778     66    380   -605       C  
ATOM   4098  C   ILE A 498       3.834 -37.995 -51.873  1.00 45.49           C  
ANISOU 4098  C   ILE A 498     6157   5293   5835     78    515   -594       C  
ATOM   4099  O   ILE A 498       3.481 -39.118 -52.236  1.00 48.05           O  
ANISOU 4099  O   ILE A 498     6458   5563   6236     74    539   -647       O  
ATOM   4100  CB  ILE A 498       5.317 -36.644 -53.438  1.00 45.94           C  
ANISOU 4100  CB  ILE A 498     6295   5505   5656     78    364   -567       C  
ATOM   4101  CG1 ILE A 498       5.296 -35.675 -54.624  1.00 46.74           C  
ANISOU 4101  CG1 ILE A 498     6440   5645   5675     59    246   -587       C  
ATOM   4102  CG2 ILE A 498       5.922 -37.979 -53.868  1.00 44.69           C  
ANISOU 4102  CG2 ILE A 498     6157   5336   5489     89    417   -593       C  
ATOM   4103  CD1 ILE A 498       6.624 -34.976 -54.886  1.00 48.11           C  
ANISOU 4103  CD1 ILE A 498     6674   5897   5706     63    261   -537       C  
ATOM   4104  N   ILE A 499       4.183 -37.718 -50.617  1.00 45.04           N  
ANISOU 4104  N   ILE A 499     6135   5233   5745     94    597   -527       N  
ATOM   4105  CA  ILE A 499       4.127 -38.723 -49.564  1.00 44.42           C  
ANISOU 4105  CA  ILE A 499     6092   5074   5711    107    725   -507       C  
ATOM   4106  C   ILE A 499       2.677 -39.089 -49.235  1.00 47.25           C  
ANISOU 4106  C   ILE A 499     6391   5314   6246     76    808   -563       C  
ATOM   4107  O   ILE A 499       2.362 -40.270 -49.076  1.00 48.00           O  
ANISOU 4107  O   ILE A 499     6483   5331   6425     73    895   -592       O  
ATOM   4108  CB  ILE A 499       4.903 -38.291 -48.301  1.00 44.44           C  
ANISOU 4108  CB  ILE A 499     6190   5087   5610    134    771   -421       C  
ATOM   4109  CG1 ILE A 499       6.386 -38.092 -48.638  1.00 42.32           C  
ANISOU 4109  CG1 ILE A 499     5950   4912   5218    166    691   -381       C  
ATOM   4110  CG2 ILE A 499       4.761 -39.333 -47.186  1.00 43.62           C  
ANISOU 4110  CG2 ILE A 499     6167   4875   5533    147    901   -397       C  
ATOM   4111  CD1 ILE A 499       7.130 -37.243 -47.628  1.00 39.12           C  
ANISOU 4111  CD1 ILE A 499     5616   4529   4720    190    672   -309       C  
ATOM   4112  N   LYS A 500       1.800 -38.086 -49.159  1.00 47.85           N  
ANISOU 4112  N   LYS A 500     6410   5369   6403     52    787   -586       N  
ATOM   4113  CA  LYS A 500       0.364 -38.333 -48.960  1.00 49.77           C  
ANISOU 4113  CA  LYS A 500     6560   5483   6866     19    862   -659       C  
ATOM   4114  C   LYS A 500      -0.218 -39.282 -50.022  1.00 53.39           C  
ANISOU 4114  C   LYS A 500     6930   5897   7459      7    801   -751       C  
ATOM   4115  O   LYS A 500      -0.878 -40.264 -49.679  1.00 55.18           O  
ANISOU 4115  O   LYS A 500     7119   6011   7836     -9    918   -795       O  
ATOM   4116  CB  LYS A 500      -0.423 -37.021 -48.918  1.00 47.57           C  
ANISOU 4116  CB  LYS A 500     6211   5190   6674     -1    815   -681       C  
ATOM   4117  CG  LYS A 500      -0.270 -36.238 -47.629  1.00 46.62           C  
ANISOU 4117  CG  LYS A 500     6169   5056   6487      0    930   -614       C  
ATOM   4118  CD  LYS A 500      -0.706 -34.795 -47.815  1.00 47.88           C  
ANISOU 4118  CD  LYS A 500     6268   5242   6684    -11    840   -624       C  
ATOM   4119  CE  LYS A 500      -0.494 -33.971 -46.552  1.00 48.87           C  
ANISOU 4119  CE  LYS A 500     6485   5357   6727    -11    950   -559       C  
ATOM   4120  NZ  LYS A 500      -1.119 -32.612 -46.664  1.00 49.32           N  
ANISOU 4120  NZ  LYS A 500     6465   5412   6864    -26    888   -581       N  
ATOM   4121  N   GLU A 501       0.055 -38.993 -51.297  1.00 55.38           N  
ANISOU 4121  N   GLU A 501     7168   6226   7648     13    623   -779       N  
ATOM   4122  CA  GLU A 501      -0.363 -39.840 -52.421  1.00 58.08           C  
ANISOU 4122  CA  GLU A 501     7462   6531   8076      5    531   -866       C  
ATOM   4123  C   GLU A 501       0.124 -41.275 -52.254  1.00 58.21           C  
ANISOU 4123  C   GLU A 501     7517   6525   8075     14    639   -863       C  
ATOM   4124  O   GLU A 501      -0.640 -42.220 -52.445  1.00 59.20           O  
ANISOU 4124  O   GLU A 501     7574   6552   8367     -1    669   -937       O  
ATOM   4125  CB  GLU A 501       0.162 -39.282 -53.752  1.00 60.18           C  
ANISOU 4125  CB  GLU A 501     7782   6888   8196     13    341   -876       C  
ATOM   4126  CG  GLU A 501      -0.507 -37.984 -54.239  1.00 66.25           C  
ANISOU 4126  CG  GLU A 501     8514   7653   9004      4    185   -901       C  
ATOM   4127  CD  GLU A 501      -1.805 -38.212 -55.017  1.00 71.52           C  
ANISOU 4127  CD  GLU A 501     9085   8205   9884    -10     44  -1016       C  
ATOM   4128  OE1 GLU A 501      -2.120 -39.380 -55.357  1.00 73.10           O  
ANISOU 4128  OE1 GLU A 501     9255   8340  10181    -16     54  -1082       O  
ATOM   4129  OE2 GLU A 501      -2.508 -37.210 -55.294  1.00 71.40           O  
ANISOU 4129  OE2 GLU A 501     9022   8157   9952    -13    -90  -1046       O  
ATOM   4130  N   ALA A 502       1.396 -41.424 -51.889  1.00 57.49           N  
ANISOU 4130  N   ALA A 502     7526   6516   7801     42    690   -780       N  
ATOM   4131  CA  ALA A 502       2.019 -42.735 -51.710  1.00 57.47           C  
ANISOU 4131  CA  ALA A 502     7569   6495   7772     59    778   -768       C  
ATOM   4132  C   ALA A 502       1.387 -43.530 -50.567  1.00 59.52           C  
ANISOU 4132  C   ALA A 502     7826   6631   8159     51    950   -764       C  
ATOM   4133  O   ALA A 502       1.325 -44.764 -50.613  1.00 60.01           O  
ANISOU 4133  O   ALA A 502     7886   6629   8284     52   1017   -794       O  
ATOM   4134  CB  ALA A 502       3.505 -42.581 -51.481  1.00 54.98           C  
ANISOU 4134  CB  ALA A 502     7345   6275   7268     95    779   -685       C  
ATOM   4135  N   LEU A 503       0.911 -42.814 -49.551  1.00 60.70           N  
ANISOU 4135  N   LEU A 503     7986   6736   8342     40   1032   -731       N  
ATOM   4136  CA  LEU A 503       0.283 -43.429 -48.386  1.00 61.84           C  
ANISOU 4136  CA  LEU A 503     8162   6743   8592     25   1228   -724       C  
ATOM   4137  C   LEU A 503      -1.021 -44.157 -48.704  1.00 64.42           C  
ANISOU 4137  C   LEU A 503     8364   6938   9176    -15   1291   -830       C  
ATOM   4138  O   LEU A 503      -1.530 -44.904 -47.868  1.00 66.42           O  
ANISOU 4138  O   LEU A 503     8644   7059   9535    -33   1479   -835       O  
ATOM   4139  CB  LEU A 503       0.057 -42.389 -47.288  1.00 59.38           C  
ANISOU 4139  CB  LEU A 503     7907   6405   8249     17   1311   -672       C  
ATOM   4140  CG  LEU A 503       1.274 -42.136 -46.400  1.00 55.86           C  
ANISOU 4140  CG  LEU A 503     7631   6016   7577     57   1323   -561       C  
ATOM   4141  CD1 LEU A 503       1.220 -40.743 -45.800  1.00 52.31           C  
ANISOU 4141  CD1 LEU A 503     7216   5596   7064     52   1314   -521       C  
ATOM   4142  CD2 LEU A 503       1.370 -43.202 -45.318  1.00 56.38           C  
ANISOU 4142  CD2 LEU A 503     7839   5962   7622     66   1491   -520       C  
ATOM   4143  N   HIS A 504      -1.552 -43.945 -49.907  1.00 65.70           N  
ANISOU 4143  N   HIS A 504     8400   7120   9442    -28   1132   -916       N  
ATOM   4144  CA  HIS A 504      -2.741 -44.664 -50.353  1.00 68.50           C  
ANISOU 4144  CA  HIS A 504     8619   7345  10064    -61   1147  -1032       C  
ATOM   4145  C   HIS A 504      -2.417 -46.120 -50.681  1.00 69.73           C  
ANISOU 4145  C   HIS A 504     8800   7472  10221    -54   1185  -1054       C  
ATOM   4146  O   HIS A 504      -3.310 -46.967 -50.708  1.00 71.09           O  
ANISOU 4146  O   HIS A 504     8882   7512  10618    -82   1261  -1137       O  
ATOM   4147  CB  HIS A 504      -3.394 -43.966 -51.549  1.00 68.62           C  
ANISOU 4147  CB  HIS A 504     8515   7376  10182    -70    923  -1120       C  
ATOM   4148  CG  HIS A 504      -3.809 -42.552 -51.273  1.00 69.74           C  
ANISOU 4148  CG  HIS A 504     8615   7529  10354    -77    878  -1108       C  
ATOM   4149  ND1 HIS A 504      -4.276 -42.137 -50.043  1.00 70.25           N  
ANISOU 4149  ND1 HIS A 504     8670   7514  10508    -97   1067  -1081       N  
ATOM   4150  CD2 HIS A 504      -3.842 -41.461 -52.074  1.00 69.17           C  
ANISOU 4150  CD2 HIS A 504     8521   7528  10234    -68    670  -1121       C  
ATOM   4151  CE1 HIS A 504      -4.565 -40.850 -50.095  1.00 69.73           C  
ANISOU 4151  CE1 HIS A 504     8561   7476  10458    -98    977  -1080       C  
ATOM   4152  NE2 HIS A 504      -4.313 -40.416 -51.317  1.00 68.83           N  
ANISOU 4152  NE2 HIS A 504     8436   7453  10263    -79    730  -1102       N  
ATOM   4153  N   ASN A 505      -1.136 -46.401 -50.919  1.00 70.24           N  
ANISOU 4153  N   ASN A 505     8978   7652  10056    -17   1137   -986       N  
ATOM   4154  CA  ASN A 505      -0.668 -47.766 -51.164  1.00 71.88           C  
ANISOU 4154  CA  ASN A 505     9223   7839  10249     -4   1181   -997       C  
ATOM   4155  C   ASN A 505       0.635 -48.107 -50.432  1.00 70.53           C  
ANISOU 4155  C   ASN A 505     9197   7723   9878     38   1255   -887       C  
ATOM   4156  O   ASN A 505       1.676 -48.269 -51.073  1.00 71.22           O  
ANISOU 4156  O   ASN A 505     9326   7909   9826     67   1164   -867       O  
ATOM   4157  CB  ASN A 505      -0.516 -48.016 -52.670  1.00 73.06           C  
ANISOU 4157  CB  ASN A 505     9334   8046  10378     -1   1000  -1072       C  
ATOM   4158  CG  ASN A 505      -1.851 -48.131 -53.378  1.00 77.72           C  
ANISOU 4158  CG  ASN A 505     9789   8536  11206    -36    915  -1198       C  
ATOM   4159  OD1 ASN A 505      -2.286 -47.202 -54.063  1.00 80.64           O  
ANISOU 4159  OD1 ASN A 505    10113   8932  11597    -44    750  -1240       O  
ATOM   4160  ND2 ASN A 505      -2.520 -49.269 -53.204  1.00 79.51           N  
ANISOU 4160  ND2 ASN A 505     9950   8632  11627    -57   1018  -1262       N  
ATOM   4161  N   PRO A 506       0.587 -48.216 -49.088  1.00 70.36           N  
ANISOU 4161  N   PRO A 506     9262   7622   9849     41   1418   -820       N  
ATOM   4162  CA  PRO A 506       1.796 -48.608 -48.361  1.00 70.08           C  
ANISOU 4162  CA  PRO A 506     9376   7613   9638     88   1455   -721       C  
ATOM   4163  C   PRO A 506       2.177 -50.059 -48.636  1.00 71.34           C  
ANISOU 4163  C   PRO A 506     9554   7727   9825    105   1490   -739       C  
ATOM   4164  O   PRO A 506       1.303 -50.925 -48.697  1.00 73.17           O  
ANISOU 4164  O   PRO A 506     9734   7845  10222     74   1587   -803       O  
ATOM   4165  CB  PRO A 506       1.402 -48.424 -46.889  1.00 70.18           C  
ANISOU 4165  CB  PRO A 506     9505   7514   9646     79   1623   -660       C  
ATOM   4166  CG  PRO A 506      -0.083 -48.520 -46.871  1.00 71.07           C  
ANISOU 4166  CG  PRO A 506     9510   7502   9991     21   1742   -746       C  
ATOM   4167  CD  PRO A 506      -0.547 -47.957 -48.179  1.00 70.79           C  
ANISOU 4167  CD  PRO A 506     9297   7545  10053      2   1573   -836       C  
ATOM   4168  N   ASN A 507       3.473 -50.310 -48.816  1.00 72.39           N  
ANISOU 4168  N   ASN A 507     9747   7938   9818    153   1415   -690       N  
ATOM   4169  CA  ASN A 507       3.987 -51.660 -49.046  1.00 73.59           C  
ANISOU 4169  CA  ASN A 507     9921   8048   9991    177   1442   -702       C  
ATOM   4170  C   ASN A 507       4.265 -52.356 -47.721  1.00 75.91           C  
ANISOU 4170  C   ASN A 507    10366   8228  10249    207   1560   -621       C  
ATOM   4171  O   ASN A 507       4.859 -51.761 -46.821  1.00 76.13           O  
ANISOU 4171  O   ASN A 507    10509   8265  10150    239   1543   -535       O  
ATOM   4172  CB  ASN A 507       5.264 -51.618 -49.892  1.00 72.49           C  
ANISOU 4172  CB  ASN A 507     9766   8027   9748    214   1317   -698       C  
ATOM   4173  CG  ASN A 507       5.071 -50.893 -51.215  1.00 71.35           C  
ANISOU 4173  CG  ASN A 507     9526   7984   9599    184   1205   -769       C  
ATOM   4174  OD1 ASN A 507       4.523 -49.783 -51.264  1.00 64.62           O  
ANISOU 4174  OD1 ASN A 507     8644   7172   8737    160   1158   -773       O  
ATOM   4175  ND2 ASN A 507       5.534 -51.516 -52.300  1.00 69.01           N  
ANISOU 4175  ND2 ASN A 507     9200   7719   9302    187   1162   -827       N  
ATOM   4176  N   LEU A 508       3.840 -53.612 -47.598  1.00 78.27           N  
ANISOU 4176  N   LEU A 508    10679   8407  10652    197   1671   -651       N  
ATOM   4177  CA  LEU A 508       3.990 -54.339 -46.333  1.00 79.83           C  
ANISOU 4177  CA  LEU A 508    11053   8467  10812    222   1795   -574       C  
ATOM   4178  C   LEU A 508       5.404 -54.882 -46.135  1.00 79.49           C  
ANISOU 4178  C   LEU A 508    11104   8444  10654    296   1703   -508       C  
ATOM   4179  O   LEU A 508       5.747 -55.961 -46.627  1.00 80.93           O  
ANISOU 4179  O   LEU A 508    11254   8600  10895    313   1700   -540       O  
ATOM   4180  CB  LEU A 508       2.927 -55.436 -46.187  1.00 81.41           C  
ANISOU 4180  CB  LEU A 508    11243   8509  11180    179   1972   -629       C  
ATOM   4181  CG  LEU A 508       1.520 -54.943 -45.816  1.00 84.49           C  
ANISOU 4181  CG  LEU A 508    11589   8809  11706    111   2117   -674       C  
ATOM   4182  CD1 LEU A 508       0.520 -56.098 -45.803  1.00 86.03           C  
ANISOU 4182  CD1 LEU A 508    11741   8838  12108     65   2294   -745       C  
ATOM   4183  CD2 LEU A 508       1.503 -54.192 -44.472  1.00 83.45           C  
ANISOU 4183  CD2 LEU A 508    11642   8616  11451    115   2212   -582       C  
ATOM   4184  N   SER A 509       6.216 -54.112 -45.410  1.00 78.31           N  
ANISOU 4184  N   SER A 509    11064   8330  10358    339   1619   -424       N  
ATOM   4185  CA  SER A 509       7.630 -54.420 -45.206  1.00 78.26           C  
ANISOU 4185  CA  SER A 509    11125   8340  10270    415   1494   -367       C  
ATOM   4186  C   SER A 509       8.208 -53.675 -44.005  1.00 78.26           C  
ANISOU 4186  C   SER A 509    11302   8312  10122    459   1428   -269       C  
ATOM   4187  O   SER A 509       7.605 -52.721 -43.500  1.00 78.79           O  
ANISOU 4187  O   SER A 509    11419   8384  10132    427   1471   -248       O  
ATOM   4188  CB  SER A 509       8.434 -54.058 -46.458  1.00 77.43           C  
ANISOU 4188  CB  SER A 509    10846   8388  10184    425   1362   -420       C  
ATOM   4189  OG  SER A 509       8.357 -52.666 -46.716  1.00 77.93           O  
ANISOU 4189  OG  SER A 509    10850   8568  10192    402   1298   -422       O  
ATOM   4190  N   VAL A 510       9.376 -54.125 -43.551  1.00 78.42           N  
ANISOU 4190  N   VAL A 510    11416   8289  10090    534   1314   -214       N  
ATOM   4191  CA  VAL A 510      10.157 -53.401 -42.549  1.00 78.32           C  
ANISOU 4191  CA  VAL A 510    11558   8255   9945    588   1188   -131       C  
ATOM   4192  C   VAL A 510      11.254 -52.623 -43.283  1.00 76.43           C  
ANISOU 4192  C   VAL A 510    11152   8162   9724    618   1015   -153       C  
ATOM   4193  O   VAL A 510      12.124 -53.214 -43.935  1.00 75.98           O  
ANISOU 4193  O   VAL A 510    10985   8129   9755    654    941   -186       O  
ATOM   4194  CB  VAL A 510      10.768 -54.341 -41.467  1.00 80.26           C  
ANISOU 4194  CB  VAL A 510    12037   8329  10128    661   1139    -55       C  
ATOM   4195  CG1 VAL A 510      11.499 -53.533 -40.391  1.00 80.47           C  
ANISOU 4195  CG1 VAL A 510    12249   8318  10009    718    983     26       C  
ATOM   4196  CG2 VAL A 510       9.690 -55.204 -40.828  1.00 81.69           C  
ANISOU 4196  CG2 VAL A 510    12390   8350  10298    625   1344    -37       C  
ATOM   4197  N   ASP A 511      11.186 -51.296 -43.188  1.00 73.64           N  
ANISOU 4197  N   ASP A 511    10779   7899   9302    597    970   -141       N  
ATOM   4198  CA  ASP A 511      12.118 -50.408 -43.880  1.00 71.21           C  
ANISOU 4198  CA  ASP A 511    10317   7725   9014    612    835   -165       C  
ATOM   4199  C   ASP A 511      12.298 -49.092 -43.132  1.00 69.96           C  
ANISOU 4199  C   ASP A 511    10240   7596   8746    620    751   -113       C  
ATOM   4200  O   ASP A 511      11.587 -48.808 -42.166  1.00 70.80           O  
ANISOU 4200  O   ASP A 511    10518   7629   8753    605    813    -66       O  
ATOM   4201  CB  ASP A 511      11.656 -50.149 -45.320  1.00 69.85           C  
ANISOU 4201  CB  ASP A 511     9939   7681   8918    549    898   -251       C  
ATOM   4202  CG  ASP A 511      10.183 -49.776 -45.409  1.00 69.88           C  
ANISOU 4202  CG  ASP A 511     9942   7695   8913    476   1025   -275       C  
ATOM   4203  OD1 ASP A 511       9.675 -49.094 -44.493  1.00 69.33           O  
ANISOU 4203  OD1 ASP A 511     9986   7590   8765    465   1053   -227       O  
ATOM   4204  OD2 ASP A 511       9.534 -50.163 -46.405  1.00 68.33           O  
ANISOU 4204  OD2 ASP A 511     9630   7532   8799    431   1092   -348       O  
ATOM   4205  N   GLU A 512      13.253 -48.294 -43.590  1.00 68.03           N  
ANISOU 4205  N   GLU A 512     9875   7449   8525    639    625   -127       N  
ATOM   4206  CA  GLU A 512      13.581 -47.032 -42.950  1.00 66.05           C  
ANISOU 4206  CA  GLU A 512     9681   7228   8186    651    524    -85       C  
ATOM   4207  C   GLU A 512      13.191 -45.848 -43.840  1.00 62.89           C  
ANISOU 4207  C   GLU A 512     9130   6977   7790    588    559   -127       C  
ATOM   4208  O   GLU A 512      13.110 -45.995 -45.066  1.00 61.68           O  
ANISOU 4208  O   GLU A 512     8816   6905   7714    553    610   -191       O  
ATOM   4209  CB  GLU A 512      15.074 -46.992 -42.602  1.00 67.92           C  
ANISOU 4209  CB  GLU A 512     9911   7430   8466    730    328    -66       C  
ATOM   4210  CG  GLU A 512      15.485 -47.936 -41.458  1.00 73.94           C  
ANISOU 4210  CG  GLU A 512    10879   8020   9194    805    238     -9       C  
ATOM   4211  CD  GLU A 512      14.980 -47.480 -40.084  1.00 77.97           C  
ANISOU 4211  CD  GLU A 512    11666   8435   9526    814    222     68       C  
ATOM   4212  OE1 GLU A 512      14.417 -48.318 -39.342  1.00 77.54           O  
ANISOU 4212  OE1 GLU A 512    11821   8246   9393    822    299    109       O  
ATOM   4213  OE2 GLU A 512      15.143 -46.284 -39.747  1.00 79.10           O  
ANISOU 4213  OE2 GLU A 512    11828   8627   9601    809    145     85       O  
ATOM   4214  N   PRO A 513      12.921 -44.675 -43.226  1.00 60.45           N  
ANISOU 4214  N   PRO A 513     8891   6692   7386    574    532    -91       N  
ATOM   4215  CA  PRO A 513      12.701 -43.458 -44.000  1.00 57.86           C  
ANISOU 4215  CA  PRO A 513     8430   6494   7058    524    536   -123       C  
ATOM   4216  C   PRO A 513      13.941 -43.081 -44.811  1.00 57.34           C  
ANISOU 4216  C   PRO A 513     8212   6509   7065    544    436   -154       C  
ATOM   4217  O   PRO A 513      15.069 -43.307 -44.364  1.00 59.51           O  
ANISOU 4217  O   PRO A 513     8499   6732   7380    605    320   -137       O  
ATOM   4218  CB  PRO A 513      12.435 -42.398 -42.922  1.00 57.23           C  
ANISOU 4218  CB  PRO A 513     8485   6393   6866    524    504    -68       C  
ATOM   4219  CG  PRO A 513      12.979 -42.968 -41.668  1.00 58.76           C  
ANISOU 4219  CG  PRO A 513     8876   6452   6997    589    427     -9       C  
ATOM   4220  CD  PRO A 513      12.726 -44.432 -41.786  1.00 60.31           C  
ANISOU 4220  CD  PRO A 513     9102   6567   7246    599    508    -20       C  
ATOM   4221  N   LEU A 514      13.720 -42.527 -45.997  1.00 54.79           N  
ANISOU 4221  N   LEU A 514     7755   6294   6770    492    483   -205       N  
ATOM   4222  CA  LEU A 514      14.798 -42.081 -46.869  1.00 54.52           C  
ANISOU 4222  CA  LEU A 514     7586   6327   6801    495    435   -242       C  
ATOM   4223  C   LEU A 514      15.502 -40.869 -46.282  1.00 54.70           C  
ANISOU 4223  C   LEU A 514     7613   6371   6798    514    327   -208       C  
ATOM   4224  O   LEU A 514      14.853 -39.950 -45.785  1.00 52.46           O  
ANISOU 4224  O   LEU A 514     7395   6113   6424    492    321   -175       O  
ATOM   4225  CB  LEU A 514      14.241 -41.721 -48.249  1.00 53.24           C  
ANISOU 4225  CB  LEU A 514     7336   6258   6636    429    519   -299       C  
ATOM   4226  CG  LEU A 514      14.184 -42.753 -49.376  1.00 52.80           C  
ANISOU 4226  CG  LEU A 514     7221   6201   6640    411    599   -364       C  
ATOM   4227  CD1 LEU A 514      13.833 -44.154 -48.898  1.00 55.46           C  
ANISOU 4227  CD1 LEU A 514     7609   6446   7015    438    635   -361       C  
ATOM   4228  CD2 LEU A 514      13.204 -42.289 -50.431  1.00 51.64           C  
ANISOU 4228  CD2 LEU A 514     7057   6120   6443    346    651   -407       C  
ATOM   4229  N   ASP A 515      16.830 -40.872 -46.339  1.00 56.24           N  
ANISOU 4229  N   ASP A 515     7728   6547   7095    555    244   -223       N  
ATOM   4230  CA  ASP A 515      17.603 -39.710 -45.925  1.00 57.78           C  
ANISOU 4230  CA  ASP A 515     7895   6758   7301    571    136   -206       C  
ATOM   4231  C   ASP A 515      17.602 -38.692 -47.065  1.00 55.26           C  
ANISOU 4231  C   ASP A 515     7465   6546   6984    509    209   -244       C  
ATOM   4232  O   ASP A 515      18.405 -38.787 -48.001  1.00 56.43           O  
ANISOU 4232  O   ASP A 515     7492   6708   7240    498    254   -298       O  
ATOM   4233  CB  ASP A 515      19.031 -40.111 -45.535  1.00 61.68           C  
ANISOU 4233  CB  ASP A 515     8327   7165   7944    641      7   -219       C  
ATOM   4234  CG  ASP A 515      19.739 -39.039 -44.711  1.00 68.29           C  
ANISOU 4234  CG  ASP A 515     9175   7981   8792    672   -149   -194       C  
ATOM   4235  OD1 ASP A 515      20.918 -38.748 -45.010  1.00 72.18           O  
ANISOU 4235  OD1 ASP A 515     9522   8455   9449    692   -211   -237       O  
ATOM   4236  OD2 ASP A 515      19.123 -38.487 -43.766  1.00 69.52           O  
ANISOU 4236  OD2 ASP A 515     9483   8128   8805    675   -202   -138       O  
ATOM   4237  N   VAL A 516      16.680 -37.737 -46.991  1.00 50.77           N  
ANISOU 4237  N   VAL A 516     6952   6040   6300    466    231   -219       N  
ATOM   4238  CA  VAL A 516      16.520 -36.732 -48.037  1.00 48.05           C  
ANISOU 4238  CA  VAL A 516     6539   5787   5930    407    290   -246       C  
ATOM   4239  C   VAL A 516      16.523 -35.308 -47.484  1.00 46.92           C  
ANISOU 4239  C   VAL A 516     6418   5679   5732    398    222   -210       C  
ATOM   4240  O   VAL A 516      16.256 -35.085 -46.299  1.00 45.92           O  
ANISOU 4240  O   VAL A 516     6386   5514   5548    426    150   -163       O  
ATOM   4241  CB  VAL A 516      15.219 -36.956 -48.860  1.00 47.38           C  
ANISOU 4241  CB  VAL A 516     6482   5745   5774    354    387   -267       C  
ATOM   4242  CG1 VAL A 516      15.364 -38.145 -49.784  1.00 51.71           C  
ANISOU 4242  CG1 VAL A 516     6991   6274   6381    349    463   -321       C  
ATOM   4243  CG2 VAL A 516      14.023 -37.139 -47.945  1.00 45.12           C  
ANISOU 4243  CG2 VAL A 516     6297   5426   5421    356    388   -230       C  
ATOM   4244  N   ASP A 517      16.823 -34.344 -48.349  1.00 45.43           N  
ANISOU 4244  N   ASP A 517     6159   5554   5550    357    253   -233       N  
ATOM   4245  CA  ASP A 517      16.672 -32.944 -47.989  1.00 43.24           C  
ANISOU 4245  CA  ASP A 517     5899   5316   5213    338    205   -203       C  
ATOM   4246  C   ASP A 517      15.303 -32.493 -48.496  1.00 42.71           C  
ANISOU 4246  C   ASP A 517     5882   5304   5041    288    262   -198       C  
ATOM   4247  O   ASP A 517      15.074 -32.378 -49.706  1.00 41.83           O  
ANISOU 4247  O   ASP A 517     5746   5234   4915    245    327   -232       O  
ATOM   4248  CB  ASP A 517      17.810 -32.091 -48.566  1.00 41.42           C  
ANISOU 4248  CB  ASP A 517     5568   5106   5065    323    205   -229       C  
ATOM   4249  CG  ASP A 517      17.818 -30.665 -48.014  1.00 41.79           C  
ANISOU 4249  CG  ASP A 517     5629   5181   5069    313    136   -197       C  
ATOM   4250  OD1 ASP A 517      18.912 -30.095 -47.850  1.00 43.10           O  
ANISOU 4250  OD1 ASP A 517     5718   5324   5333    326     87   -209       O  
ATOM   4251  OD2 ASP A 517      16.738 -30.103 -47.735  1.00 41.28           O  
ANISOU 4251  OD2 ASP A 517     5643   5150   4890    292    133   -164       O  
ATOM   4252  N   TYR A 518      14.387 -32.252 -47.562  1.00 40.38           N  
ANISOU 4252  N   TYR A 518     5668   4994   4681    293    236   -161       N  
ATOM   4253  CA  TYR A 518      13.013 -31.899 -47.911  1.00 37.90           C  
ANISOU 4253  CA  TYR A 518     5382   4706   4311    251    282   -165       C  
ATOM   4254  C   TYR A 518      12.861 -30.486 -48.506  1.00 35.91           C  
ANISOU 4254  C   TYR A 518     5105   4517   4022    211    264   -164       C  
ATOM   4255  O   TYR A 518      11.827 -30.170 -49.075  1.00 35.90           O  
ANISOU 4255  O   TYR A 518     5110   4534   3996    177    281   -179       O  
ATOM   4256  CB  TYR A 518      12.088 -32.102 -46.707  1.00 38.14           C  
ANISOU 4256  CB  TYR A 518     5503   4679   4310    263    293   -134       C  
ATOM   4257  CG  TYR A 518      12.030 -33.533 -46.215  1.00 35.55           C  
ANISOU 4257  CG  TYR A 518     5225   4276   4006    295    329   -134       C  
ATOM   4258  CD1 TYR A 518      12.914 -33.988 -45.248  1.00 39.79           C  
ANISOU 4258  CD1 TYR A 518     5826   4753   4541    347    270   -103       C  
ATOM   4259  CD2 TYR A 518      11.096 -34.432 -46.722  1.00 33.78           C  
ANISOU 4259  CD2 TYR A 518     4990   4030   3816    273    407   -168       C  
ATOM   4260  CE1 TYR A 518      12.876 -35.302 -44.797  1.00 40.00           C  
ANISOU 4260  CE1 TYR A 518     5916   4699   4583    379    297    -98       C  
ATOM   4261  CE2 TYR A 518      11.043 -35.747 -46.267  1.00 32.66           C  
ANISOU 4261  CE2 TYR A 518     4897   3813   3699    300    450   -166       C  
ATOM   4262  CZ  TYR A 518      11.938 -36.174 -45.308  1.00 35.56           C  
ANISOU 4262  CZ  TYR A 518     5340   4122   4050    352    398   -128       C  
ATOM   4263  OH  TYR A 518      11.908 -37.472 -44.843  1.00 36.72           O  
ANISOU 4263  OH  TYR A 518     5555   4183   4215    382    433   -122       O  
ATOM   4264  N   ARG A 519      13.896 -29.657 -48.392  1.00 34.42           N  
ANISOU 4264  N   ARG A 519     4885   4349   3844    218    221   -151       N  
ATOM   4265  CA  ARG A 519      13.884 -28.304 -48.966  1.00 37.28           C  
ANISOU 4265  CA  ARG A 519     5230   4763   4174    181    212   -148       C  
ATOM   4266  C   ARG A 519      13.984 -28.303 -50.494  1.00 39.22           C  
ANISOU 4266  C   ARG A 519     5458   5036   4407    141    269   -186       C  
ATOM   4267  O   ARG A 519      13.889 -27.245 -51.119  1.00 41.43           O  
ANISOU 4267  O   ARG A 519     5752   5348   4643    107    267   -183       O  
ATOM   4268  CB  ARG A 519      15.025 -27.452 -48.392  1.00 37.39           C  
ANISOU 4268  CB  ARG A 519     5210   4776   4223    197    156   -130       C  
ATOM   4269  CG  ARG A 519      14.965 -27.206 -46.869  1.00 38.87           C  
ANISOU 4269  CG  ARG A 519     5453   4924   4390    234     76    -91       C  
ATOM   4270  CD  ARG A 519      16.216 -26.479 -46.371  1.00 40.03           C  
ANISOU 4270  CD  ARG A 519     5558   5058   4596    255     -6    -86       C  
ATOM   4271  NE  ARG A 519      17.431 -27.256 -46.641  1.00 43.08           N  
ANISOU 4271  NE  ARG A 519     5862   5408   5101    283    -15   -119       N  
ATOM   4272  CZ  ARG A 519      18.673 -26.771 -46.641  1.00 43.02           C  
ANISOU 4272  CZ  ARG A 519     5762   5377   5207    293    -62   -140       C  
ATOM   4273  NH1 ARG A 519      18.911 -25.482 -46.389  1.00 38.52           N  
ANISOU 4273  NH1 ARG A 519     5178   4823   4636    277   -107   -130       N  
ATOM   4274  NH2 ARG A 519      19.684 -27.583 -46.914  1.00 40.14           N  
ANISOU 4274  NH2 ARG A 519     5307   4963   4980    318    -58   -180       N  
ATOM   4275  N   PHE A 520      14.182 -29.480 -51.089  1.00 39.93           N  
ANISOU 4275  N   PHE A 520     5540   5107   4526    146    322   -221       N  
ATOM   4276  CA  PHE A 520      14.341 -29.609 -52.538  1.00 42.05           C  
ANISOU 4276  CA  PHE A 520     5827   5384   4767    108    389   -262       C  
ATOM   4277  C   PHE A 520      13.416 -30.682 -53.089  1.00 42.73           C  
ANISOU 4277  C   PHE A 520     5953   5452   4831    103    405   -295       C  
ATOM   4278  O   PHE A 520      13.256 -31.746 -52.476  1.00 41.77           O  
ANISOU 4278  O   PHE A 520     5810   5300   4759    134    409   -298       O  
ATOM   4279  CB  PHE A 520      15.802 -29.907 -52.902  1.00 43.24           C  
ANISOU 4279  CB  PHE A 520     5921   5512   4998    112    462   -290       C  
ATOM   4280  CG  PHE A 520      16.753 -28.846 -52.438  1.00 45.46           C  
ANISOU 4280  CG  PHE A 520     6144   5796   5333    114    443   -271       C  
ATOM   4281  CD1 PHE A 520      16.926 -27.670 -53.185  1.00 46.38           C  
ANISOU 4281  CD1 PHE A 520     6289   5932   5401     68    483   -270       C  
ATOM   4282  CD2 PHE A 520      17.435 -28.988 -51.229  1.00 40.98           C  
ANISOU 4282  CD2 PHE A 520     5508   5200   4862    163    371   -254       C  
ATOM   4283  CE1 PHE A 520      17.788 -26.658 -52.745  1.00 45.31           C  
ANISOU 4283  CE1 PHE A 520     6091   5792   5332     67    468   -257       C  
ATOM   4284  CE2 PHE A 520      18.296 -27.987 -50.777  1.00 44.56           C  
ANISOU 4284  CE2 PHE A 520     5902   5646   5381    167    332   -244       C  
ATOM   4285  CZ  PHE A 520      18.477 -26.816 -51.538  1.00 45.52           C  
ANISOU 4285  CZ  PHE A 520     6030   5793   5473    116    388   -248       C  
ATOM   4286  N   ASP A 521      12.803 -30.387 -54.238  1.00 41.18           N  
ANISOU 4286  N   ASP A 521     5826   5262   4559     65    405   -321       N  
ATOM   4287  CA  ASP A 521      11.862 -31.296 -54.893  1.00 40.53           C  
ANISOU 4287  CA  ASP A 521     5787   5153   4460     57    394   -363       C  
ATOM   4288  C   ASP A 521      12.439 -32.700 -55.042  1.00 39.46           C  
ANISOU 4288  C   ASP A 521     5628   4987   4376     74    469   -397       C  
ATOM   4289  O   ASP A 521      13.598 -32.869 -55.431  1.00 39.99           O  
ANISOU 4289  O   ASP A 521     5684   5049   4462     71    549   -413       O  
ATOM   4290  CB  ASP A 521      11.432 -30.727 -56.249  1.00 42.40           C  
ANISOU 4290  CB  ASP A 521     6132   5385   4594     17    366   -390       C  
ATOM   4291  CG  ASP A 521      10.551 -29.490 -56.102  1.00 46.56           C  
ANISOU 4291  CG  ASP A 521     6679   5925   5088      7    263   -362       C  
ATOM   4292  OD1 ASP A 521       9.333 -29.653 -55.880  1.00 47.89           O  
ANISOU 4292  OD1 ASP A 521     6828   6070   5299     13    184   -376       O  
ATOM   4293  OD2 ASP A 521      11.071 -28.356 -56.192  1.00 47.84           O  
ANISOU 4293  OD2 ASP A 521     6865   6110   5203     -9    268   -331       O  
ATOM   4294  N   PHE A 522      11.643 -33.705 -54.694  1.00 38.11           N  
ANISOU 4294  N   PHE A 522     5441   4788   4251     91    453   -413       N  
ATOM   4295  CA  PHE A 522      12.096 -35.085 -54.800  1.00 38.96           C  
ANISOU 4295  CA  PHE A 522     5528   4861   4413    109    518   -446       C  
ATOM   4296  C   PHE A 522      12.435 -35.423 -56.242  1.00 40.07           C  
ANISOU 4296  C   PHE A 522     5737   4988   4499     78    575   -503       C  
ATOM   4297  O   PHE A 522      11.648 -35.157 -57.152  1.00 40.84           O  
ANISOU 4297  O   PHE A 522     5920   5079   4518     47    528   -532       O  
ATOM   4298  CB  PHE A 522      11.040 -36.065 -54.277  1.00 39.25           C  
ANISOU 4298  CB  PHE A 522     5550   4858   4506    124    500   -458       C  
ATOM   4299  CG  PHE A 522      10.855 -36.035 -52.783  1.00 38.10           C  
ANISOU 4299  CG  PHE A 522     5371   4698   4410    156    488   -405       C  
ATOM   4300  CD1 PHE A 522      11.876 -35.610 -51.939  1.00 38.44           C  
ANISOU 4300  CD1 PHE A 522     5395   4753   4459    185    483   -358       C  
ATOM   4301  CD2 PHE A 522       9.661 -36.466 -52.220  1.00 36.70           C  
ANISOU 4301  CD2 PHE A 522     5191   4474   4277    156    486   -410       C  
ATOM   4302  CE1 PHE A 522      11.696 -35.591 -50.556  1.00 37.25           C  
ANISOU 4302  CE1 PHE A 522     5258   4571   4325    215    463   -310       C  
ATOM   4303  CE2 PHE A 522       9.481 -36.465 -50.844  1.00 33.23           C  
ANISOU 4303  CE2 PHE A 522     4761   4001   3863    180    502   -363       C  
ATOM   4304  CZ  PHE A 522      10.498 -36.027 -50.012  1.00 35.78           C  
ANISOU 4304  CZ  PHE A 522     5098   4338   4158    211    484   -310       C  
ATOM   4305  N   SER A 523      13.625 -35.987 -56.434  1.00 41.44           N  
ANISOU 4305  N   SER A 523     5881   5144   4720     87    670   -522       N  
ATOM   4306  CA  SER A 523      14.042 -36.551 -57.714  1.00 44.55           C  
ANISOU 4306  CA  SER A 523     6346   5505   5076     58    763   -585       C  
ATOM   4307  C   SER A 523      13.149 -37.730 -58.097  1.00 44.23           C  
ANISOU 4307  C   SER A 523     6344   5430   5032     59    742   -630       C  
ATOM   4308  O   SER A 523      12.462 -38.293 -57.248  1.00 44.43           O  
ANISOU 4308  O   SER A 523     6309   5450   5124     87    687   -614       O  
ATOM   4309  CB  SER A 523      15.495 -37.035 -57.619  1.00 45.33           C  
ANISOU 4309  CB  SER A 523     6366   5574   5283     74    881   -603       C  
ATOM   4310  OG  SER A 523      15.585 -38.181 -56.788  1.00 44.22           O  
ANISOU 4310  OG  SER A 523     6139   5407   5256    121    868   -601       O  
ATOM   4311  N   ASP A 524      13.176 -38.105 -59.372  1.00 46.46           N  
ANISOU 4311  N   ASP A 524     6738   5679   5237     26    794   -691       N  
ATOM   4312  CA  ASP A 524      12.447 -39.279 -59.849  1.00 49.72           C  
ANISOU 4312  CA  ASP A 524     7191   6048   5652     26    775   -747       C  
ATOM   4313  C   ASP A 524      12.858 -40.558 -59.111  1.00 50.80           C  
ANISOU 4313  C   ASP A 524     7214   6161   5926     64    835   -753       C  
ATOM   4314  O   ASP A 524      12.014 -41.418 -58.826  1.00 52.07           O  
ANISOU 4314  O   ASP A 524     7351   6297   6138     78    789   -770       O  
ATOM   4315  CB  ASP A 524      12.626 -39.447 -61.366  1.00 51.08           C  
ANISOU 4315  CB  ASP A 524     7533   6175   5701    -16    834   -814       C  
ATOM   4316  CG  ASP A 524      11.884 -38.380 -62.170  1.00 54.80           C  
ANISOU 4316  CG  ASP A 524     8161   6644   6017    -50    726   -814       C  
ATOM   4317  OD1 ASP A 524      11.038 -37.659 -61.592  1.00 56.82           O  
ANISOU 4317  OD1 ASP A 524     8370   6932   6288    -38    592   -774       O  
ATOM   4318  OD2 ASP A 524      12.145 -38.258 -63.388  1.00 56.56           O  
ANISOU 4318  OD2 ASP A 524     8568   6820   6101    -87    776   -857       O  
ATOM   4319  N   GLU A 525      14.150 -40.662 -58.800  1.00 50.85           N  
ANISOU 4319  N   GLU A 525     7148   6162   6009     82    934   -743       N  
ATOM   4320  CA  GLU A 525      14.716 -41.796 -58.070  1.00 52.48           C  
ANISOU 4320  CA  GLU A 525     7250   6333   6355    127    977   -744       C  
ATOM   4321  C   GLU A 525      14.103 -41.921 -56.674  1.00 52.17           C  
ANISOU 4321  C   GLU A 525     7144   6303   6373    168    880   -682       C  
ATOM   4322  O   GLU A 525      13.731 -43.022 -56.251  1.00 51.53           O  
ANISOU 4322  O   GLU A 525     7040   6182   6356    193    879   -690       O  
ATOM   4323  CB  GLU A 525      16.234 -41.632 -57.973  1.00 54.66           C  
ANISOU 4323  CB  GLU A 525     7449   6591   6730    140   1071   -748       C  
ATOM   4324  CG  GLU A 525      17.007 -42.798 -57.361  1.00 60.66           C  
ANISOU 4324  CG  GLU A 525     8102   7293   7655    191   1107   -760       C  
ATOM   4325  CD  GLU A 525      18.459 -42.425 -57.035  1.00 65.29           C  
ANISOU 4325  CD  GLU A 525     8575   7849   8383    213   1154   -760       C  
ATOM   4326  OE1 GLU A 525      18.931 -41.354 -57.492  1.00 64.95           O  
ANISOU 4326  OE1 GLU A 525     8543   7826   8310    178   1204   -764       O  
ATOM   4327  OE2 GLU A 525      19.128 -43.202 -56.317  1.00 66.96           O  
ANISOU 4327  OE2 GLU A 525     8686   8005   8749    267   1136   -759       O  
ATOM   4328  N   ILE A 526      13.999 -40.788 -55.971  1.00 49.73           N  
ANISOU 4328  N   ILE A 526     6820   6039   6038    173    812   -623       N  
ATOM   4329  CA  ILE A 526      13.395 -40.746 -54.637  1.00 47.58           C  
ANISOU 4329  CA  ILE A 526     6519   5764   5795    205    738   -564       C  
ATOM   4330  C   ILE A 526      11.903 -41.086 -54.684  1.00 46.90           C  
ANISOU 4330  C   ILE A 526     6469   5663   5688    186    704   -580       C  
ATOM   4331  O   ILE A 526      11.416 -41.858 -53.854  1.00 47.48           O  
ANISOU 4331  O   ILE A 526     6528   5691   5821    210    707   -565       O  
ATOM   4332  CB  ILE A 526      13.631 -39.380 -53.944  1.00 47.94           C  
ANISOU 4332  CB  ILE A 526     6553   5854   5809    209    680   -505       C  
ATOM   4333  CG1 ILE A 526      15.109 -39.224 -53.576  1.00 46.52           C  
ANISOU 4333  CG1 ILE A 526     6307   5662   5704    240    696   -491       C  
ATOM   4334  CG2 ILE A 526      12.769 -39.245 -52.697  1.00 46.08           C  
ANISOU 4334  CG2 ILE A 526     6328   5606   5573    229    621   -452       C  
ATOM   4335  CD1 ILE A 526      15.574 -37.782 -53.501  1.00 48.49           C  
ANISOU 4335  CD1 ILE A 526     6545   5957   5922    225    666   -462       C  
ATOM   4336  N   LYS A 527      11.191 -40.528 -55.662  1.00 46.86           N  
ANISOU 4336  N   LYS A 527     6515   5679   5611    144    668   -615       N  
ATOM   4337  CA  LYS A 527       9.772 -40.843 -55.862  1.00 49.11           C  
ANISOU 4337  CA  LYS A 527     6814   5932   5914    126    616   -650       C  
ATOM   4338  C   LYS A 527       9.500 -42.352 -55.958  1.00 50.95           C  
ANISOU 4338  C   LYS A 527     7032   6102   6224    135    662   -697       C  
ATOM   4339  O   LYS A 527       8.596 -42.862 -55.300  1.00 51.80           O  
ANISOU 4339  O   LYS A 527     7106   6163   6412    141    659   -698       O  
ATOM   4340  CB  LYS A 527       9.212 -40.111 -57.088  1.00 49.24           C  
ANISOU 4340  CB  LYS A 527     6906   5961   5842     86    542   -693       C  
ATOM   4341  CG  LYS A 527       8.785 -38.674 -56.800  1.00 50.86           C  
ANISOU 4341  CG  LYS A 527     7113   6204   6006     76    464   -651       C  
ATOM   4342  CD  LYS A 527       8.225 -37.963 -58.032  1.00 52.18           C  
ANISOU 4342  CD  LYS A 527     7378   6366   6081     43    367   -690       C  
ATOM   4343  CE  LYS A 527       9.284 -37.109 -58.704  1.00 53.42           C  
ANISOU 4343  CE  LYS A 527     7623   6563   6111     25    406   -670       C  
ATOM   4344  NZ  LYS A 527       8.692 -35.984 -59.475  1.00 52.57           N  
ANISOU 4344  NZ  LYS A 527     7617   6453   5905      0    293   -675       N  
ATOM   4345  N   GLU A 528      10.295 -43.057 -56.760  1.00 53.32           N  
ANISOU 4345  N   GLU A 528     7359   6391   6509    134    722   -740       N  
ATOM   4346  CA  GLU A 528      10.120 -44.499 -56.949  1.00 56.31           C  
ANISOU 4346  CA  GLU A 528     7728   6709   6959    142    769   -790       C  
ATOM   4347  C   GLU A 528      10.352 -45.285 -55.660  1.00 55.62           C  
ANISOU 4347  C   GLU A 528     7579   6583   6970    185    814   -743       C  
ATOM   4348  O   GLU A 528       9.609 -46.226 -55.370  1.00 54.95           O  
ANISOU 4348  O   GLU A 528     7480   6439   6959    188    831   -763       O  
ATOM   4349  CB  GLU A 528      11.021 -45.029 -58.075  1.00 58.90           C  
ANISOU 4349  CB  GLU A 528     8105   7026   7248    130    841   -847       C  
ATOM   4350  CG  GLU A 528      10.771 -44.386 -59.441  1.00 65.43           C  
ANISOU 4350  CG  GLU A 528     9050   7864   7946     85    805   -898       C  
ATOM   4351  CD  GLU A 528       9.372 -44.658 -59.977  1.00 71.08           C  
ANISOU 4351  CD  GLU A 528     9812   8540   8656     63    697   -954       C  
ATOM   4352  OE1 GLU A 528       8.524 -43.735 -59.932  1.00 72.33           O  
ANISOU 4352  OE1 GLU A 528     9981   8713   8788     50    586   -940       O  
ATOM   4353  OE2 GLU A 528       9.122 -45.798 -60.431  1.00 73.54           O  
ANISOU 4353  OE2 GLU A 528    10139   8795   9007     60    717  -1018       O  
ATOM   4354  N   LYS A 529      11.371 -44.894 -54.892  1.00 55.43           N  
ANISOU 4354  N   LYS A 529     7530   6581   6951    219    826   -682       N  
ATOM   4355  CA  LYS A 529      11.647 -45.526 -53.604  1.00 56.41           C  
ANISOU 4355  CA  LYS A 529     7634   6655   7145    266    840   -629       C  
ATOM   4356  C   LYS A 529      10.485 -45.332 -52.629  1.00 55.45           C  
ANISOU 4356  C   LYS A 529     7535   6504   7028    262    821   -590       C  
ATOM   4357  O   LYS A 529      10.095 -46.267 -51.932  1.00 56.10           O  
ANISOU 4357  O   LYS A 529     7636   6512   7169    280    862   -580       O  
ATOM   4358  CB  LYS A 529      12.948 -44.996 -52.998  1.00 58.37           C  
ANISOU 4358  CB  LYS A 529     7857   6919   7401    305    817   -579       C  
ATOM   4359  CG  LYS A 529      14.213 -45.617 -53.578  1.00 60.80           C  
ANISOU 4359  CG  LYS A 529     8118   7206   7779    325    866   -619       C  
ATOM   4360  CD  LYS A 529      15.461 -44.967 -52.995  1.00 61.34           C  
ANISOU 4360  CD  LYS A 529     8136   7277   7894    362    825   -581       C  
ATOM   4361  CE  LYS A 529      16.680 -45.193 -53.882  1.00 61.74           C  
ANISOU 4361  CE  LYS A 529     8117   7311   8030    361    899   -641       C  
ATOM   4362  NZ  LYS A 529      17.789 -44.255 -53.533  1.00 62.43           N  
ANISOU 4362  NZ  LYS A 529     8137   7407   8179    380    862   -621       N  
ATOM   4363  N   ILE A 530       9.936 -44.118 -52.602  1.00 54.93           N  
ANISOU 4363  N   ILE A 530     7475   6487   6909    236    774   -573       N  
ATOM   4364  CA  ILE A 530       8.775 -43.779 -51.774  1.00 55.66           C  
ANISOU 4364  CA  ILE A 530     7581   6545   7024    224    776   -549       C  
ATOM   4365  C   ILE A 530       7.561 -44.660 -52.101  1.00 56.75           C  
ANISOU 4365  C   ILE A 530     7697   6614   7253    196    813   -612       C  
ATOM   4366  O   ILE A 530       6.819 -45.063 -51.204  1.00 55.79           O  
ANISOU 4366  O   ILE A 530     7587   6415   7198    196    875   -597       O  
ATOM   4367  CB  ILE A 530       8.422 -42.269 -51.899  1.00 54.96           C  
ANISOU 4367  CB  ILE A 530     7487   6520   6877    198    712   -534       C  
ATOM   4368  CG1 ILE A 530       9.414 -41.422 -51.100  1.00 52.94           C  
ANISOU 4368  CG1 ILE A 530     7254   6304   6558    228    686   -462       C  
ATOM   4369  CG2 ILE A 530       7.002 -41.976 -51.421  1.00 54.93           C  
ANISOU 4369  CG2 ILE A 530     7469   6467   6934    172    723   -544       C  
ATOM   4370  CD1 ILE A 530       9.377 -39.955 -51.456  1.00 53.55           C  
ANISOU 4370  CD1 ILE A 530     7322   6453   6570    204    624   -451       C  
ATOM   4371  N   LYS A 531       7.385 -44.970 -53.384  1.00 59.19           N  
ANISOU 4371  N   LYS A 531     7986   6937   7568    172    782   -686       N  
ATOM   4372  CA  LYS A 531       6.328 -45.882 -53.843  1.00 61.61           C  
ANISOU 4372  CA  LYS A 531     8263   7170   7977    148    794   -761       C  
ATOM   4373  C   LYS A 531       6.506 -47.330 -53.358  1.00 61.80           C  
ANISOU 4373  C   LYS A 531     8289   7116   8074    170    888   -763       C  
ATOM   4374  O   LYS A 531       5.605 -48.160 -53.523  1.00 63.09           O  
ANISOU 4374  O   LYS A 531     8422   7203   8347    150    918   -821       O  
ATOM   4375  CB  LYS A 531       6.216 -45.851 -55.372  1.00 62.94           C  
ANISOU 4375  CB  LYS A 531     8446   7364   8106    121    715   -841       C  
ATOM   4376  CG  LYS A 531       5.659 -44.550 -55.940  1.00 65.66           C  
ANISOU 4376  CG  LYS A 531     8801   7748   8398     95    602   -854       C  
ATOM   4377  CD  LYS A 531       5.305 -44.712 -57.408  1.00 69.60           C  
ANISOU 4377  CD  LYS A 531     9351   8231   8862     70    508   -941       C  
ATOM   4378  CE  LYS A 531       4.486 -43.538 -57.919  1.00 72.77           C  
ANISOU 4378  CE  LYS A 531     9769   8639   9243     48    366   -962       C  
ATOM   4379  NZ  LYS A 531       4.002 -43.761 -59.319  1.00 75.31           N  
ANISOU 4379  NZ  LYS A 531    10169   8917   9530     28    240  -1054       N  
ATOM   4380  N   LYS A 532       7.656 -47.630 -52.757  1.00 60.33           N  
ANISOU 4380  N   LYS A 532     8137   6940   7846    212    925   -703       N  
ATOM   4381  CA  LYS A 532       7.940 -48.981 -52.276  1.00 60.17           C  
ANISOU 4381  CA  LYS A 532     8133   6839   7889    241   1000   -698       C  
ATOM   4382  C   LYS A 532       8.039 -49.052 -50.748  1.00 59.72           C  
ANISOU 4382  C   LYS A 532     8142   6720   7828    274   1045   -612       C  
ATOM   4383  O   LYS A 532       8.418 -50.083 -50.192  1.00 59.44           O  
ANISOU 4383  O   LYS A 532     8151   6609   7825    308   1093   -589       O  
ATOM   4384  CB  LYS A 532       9.209 -49.543 -52.944  1.00 60.48           C  
ANISOU 4384  CB  LYS A 532     8166   6904   7910    268    998   -716       C  
ATOM   4385  CG  LYS A 532       9.072 -49.735 -54.454  1.00 63.59           C  
ANISOU 4385  CG  LYS A 532     8540   7327   8294    232    983   -808       C  
ATOM   4386  CD  LYS A 532      10.262 -50.475 -55.077  1.00 67.44           C  
ANISOU 4386  CD  LYS A 532     9025   7812   8789    254   1025   -839       C  
ATOM   4387  CE  LYS A 532      10.067 -50.641 -56.590  1.00 68.45           C  
ANISOU 4387  CE  LYS A 532     9177   7953   8879    212   1022   -934       C  
ATOM   4388  NZ  LYS A 532      11.205 -51.330 -57.275  1.00 69.05           N  
ANISOU 4388  NZ  LYS A 532     9257   8014   8965    225   1094   -975       N  
ATOM   4389  N   LEU A 533       7.672 -47.962 -50.073  1.00 58.73           N  
ANISOU 4389  N   LEU A 533     8044   6615   7657    265   1028   -566       N  
ATOM   4390  CA  LEU A 533       7.830 -47.870 -48.620  1.00 57.93           C  
ANISOU 4390  CA  LEU A 533     8047   6450   7515    296   1063   -482       C  
ATOM   4391  C   LEU A 533       6.578 -48.197 -47.797  1.00 57.31           C  
ANISOU 4391  C   LEU A 533     8020   6258   7499    267   1183   -480       C  
ATOM   4392  O   LEU A 533       5.442 -48.066 -48.265  1.00 57.44           O  
ANISOU 4392  O   LEU A 533     7959   6258   7608    218   1222   -543       O  
ATOM   4393  CB  LEU A 533       8.377 -46.490 -48.223  1.00 57.47           C  
ANISOU 4393  CB  LEU A 533     8012   6468   7358    308    983   -428       C  
ATOM   4394  CG  LEU A 533       9.844 -46.179 -48.536  1.00 58.67           C  
ANISOU 4394  CG  LEU A 533     8140   6692   7461    348    888   -408       C  
ATOM   4395  CD1 LEU A 533      10.133 -44.713 -48.259  1.00 59.40           C  
ANISOU 4395  CD1 LEU A 533     8237   6857   7476    346    817   -369       C  
ATOM   4396  CD2 LEU A 533      10.806 -47.082 -47.756  1.00 61.05           C  
ANISOU 4396  CD2 LEU A 533     8511   6915   7771    411    870   -364       C  
ATOM   4397  N   SER A 534       6.820 -48.615 -46.558  1.00 56.16           N  
ANISOU 4397  N   SER A 534     8014   6015   7308    299   1240   -411       N  
ATOM   4398  CA  SER A 534       5.774 -48.941 -45.600  1.00 55.99           C  
ANISOU 4398  CA  SER A 534     8088   5859   7328    273   1392   -398       C  
ATOM   4399  C   SER A 534       5.136 -47.681 -45.034  1.00 57.00           C  
ANISOU 4399  C   SER A 534     8241   5994   7423    243   1421   -378       C  
ATOM   4400  O   SER A 534       5.724 -46.597 -45.098  1.00 55.41           O  
ANISOU 4400  O   SER A 534     8028   5894   7131    258   1309   -349       O  
ATOM   4401  CB  SER A 534       6.371 -49.744 -44.447  1.00 56.37           C  
ANISOU 4401  CB  SER A 534     8329   5791   7299    322   1431   -320       C  
ATOM   4402  OG  SER A 534       7.177 -48.911 -43.627  1.00 52.82           O  
ANISOU 4402  OG  SER A 534     8001   5363   6707    364   1338   -242       O  
ATOM   4403  N   ALA A 535       3.947 -47.843 -44.453  1.00 57.38           N  
ANISOU 4403  N   ALA A 535     8324   5920   7559    198   1586   -398       N  
ATOM   4404  CA  ALA A 535       3.239 -46.749 -43.800  1.00 57.43           C  
ANISOU 4404  CA  ALA A 535     8363   5899   7557    166   1655   -387       C  
ATOM   4405  C   ALA A 535       4.060 -46.104 -42.679  1.00 57.56           C  
ANISOU 4405  C   ALA A 535     8578   5912   7380    207   1617   -288       C  
ATOM   4406  O   ALA A 535       4.028 -44.886 -42.509  1.00 56.36           O  
ANISOU 4406  O   ALA A 535     8419   5820   7176    198   1571   -273       O  
ATOM   4407  CB  ALA A 535       1.899 -47.226 -43.275  1.00 59.53           C  
ANISOU 4407  CB  ALA A 535     8644   5998   7975    111   1878   -431       C  
ATOM   4408  N   LYS A 536       4.800 -46.923 -41.933  1.00 58.02           N  
ANISOU 4408  N   LYS A 536     8817   5891   7336    254   1620   -224       N  
ATOM   4409  CA  LYS A 536       5.623 -46.438 -40.826  1.00 57.90           C  
ANISOU 4409  CA  LYS A 536     9018   5846   7135    302   1553   -133       C  
ATOM   4410  C   LYS A 536       6.709 -45.470 -41.305  1.00 55.41           C  
ANISOU 4410  C   LYS A 536     8613   5691   6749    340   1334   -116       C  
ATOM   4411  O   LYS A 536       6.937 -44.432 -40.684  1.00 53.45           O  
ANISOU 4411  O   LYS A 536     8451   5460   6396    349   1283    -75       O  
ATOM   4412  CB  LYS A 536       6.240 -47.609 -40.053  1.00 60.80           C  
ANISOU 4412  CB  LYS A 536     9597   6084   7421    354   1559    -74       C  
ATOM   4413  CG  LYS A 536       6.887 -47.208 -38.721  1.00 66.51           C  
ANISOU 4413  CG  LYS A 536    10605   6721   7946    402   1498     18       C  
ATOM   4414  CD  LYS A 536       7.362 -48.419 -37.924  1.00 69.52           C  
ANISOU 4414  CD  LYS A 536    11227   6941   8245    454   1501     77       C  
ATOM   4415  CE  LYS A 536       7.931 -47.994 -36.572  1.00 74.06           C  
ANISOU 4415  CE  LYS A 536    12126   7407   8606    503   1421    166       C  
ATOM   4416  NZ  LYS A 536       8.041 -49.137 -35.603  1.00 77.94           N  
ANISOU 4416  NZ  LYS A 536    12929   7689   8996    540   1477    227       N  
ATOM   4417  N   SER A 537       7.366 -45.815 -42.412  1.00 52.89           N  
ANISOU 4417  N   SER A 537     8125   5477   6492    359   1221   -153       N  
ATOM   4418  CA  SER A 537       8.411 -44.973 -42.980  1.00 49.82           C  
ANISOU 4418  CA  SER A 537     7637   5227   6065    387   1045   -148       C  
ATOM   4419  C   SER A 537       7.843 -43.752 -43.707  1.00 47.49           C  
ANISOU 4419  C   SER A 537     7198   5045   5800    337   1034   -190       C  
ATOM   4420  O   SER A 537       8.438 -42.675 -43.666  1.00 44.31           O  
ANISOU 4420  O   SER A 537     6783   4722   5331    350    930   -165       O  
ATOM   4421  CB  SER A 537       9.303 -45.782 -43.917  1.00 49.77           C  
ANISOU 4421  CB  SER A 537     7515   5272   6122    419    963   -180       C  
ATOM   4422  OG  SER A 537       9.973 -46.806 -43.209  1.00 54.68           O  
ANISOU 4422  OG  SER A 537     8267   5788   6722    476    938   -137       O  
ATOM   4423  N   LEU A 538       6.703 -43.929 -44.373  1.00 46.70           N  
ANISOU 4423  N   LEU A 538     6990   4941   5812    283   1129   -256       N  
ATOM   4424  CA  LEU A 538       6.063 -42.840 -45.109  1.00 45.66           C  
ANISOU 4424  CA  LEU A 538     6728   4895   5726    239   1100   -301       C  
ATOM   4425  C   LEU A 538       5.517 -41.801 -44.147  1.00 46.53           C  
ANISOU 4425  C   LEU A 538     6919   4968   5792    221   1154   -268       C  
ATOM   4426  O   LEU A 538       5.681 -40.600 -44.368  1.00 46.19           O  
ANISOU 4426  O   LEU A 538     6829   5013   5709    215   1071   -261       O  
ATOM   4427  CB  LEU A 538       4.958 -43.355 -46.035  1.00 43.91           C  
ANISOU 4427  CB  LEU A 538     6374   4652   5656    193   1158   -389       C  
ATOM   4428  CG  LEU A 538       5.396 -44.170 -47.260  1.00 47.02           C  
ANISOU 4428  CG  LEU A 538     6676   5100   6090    201   1091   -440       C  
ATOM   4429  CD1 LEU A 538       4.221 -44.942 -47.849  1.00 47.80           C  
ANISOU 4429  CD1 LEU A 538     6687   5128   6348    160   1160   -525       C  
ATOM   4430  CD2 LEU A 538       6.064 -43.313 -48.330  1.00 45.21           C  
ANISOU 4430  CD2 LEU A 538     6370   5005   5801    202    955   -455       C  
ATOM   4431  N   ASN A 539       4.895 -42.264 -43.067  1.00 46.56           N  
ANISOU 4431  N   ASN A 539     7060   4831   5800    211   1305   -247       N  
ATOM   4432  CA  ASN A 539       4.382 -41.357 -42.049  1.00 49.22           C  
ANISOU 4432  CA  ASN A 539     7508   5107   6087    191   1388   -217       C  
ATOM   4433  C   ASN A 539       5.492 -40.576 -41.358  1.00 48.70           C  
ANISOU 4433  C   ASN A 539     7574   5086   5843    238   1264   -141       C  
ATOM   4434  O   ASN A 539       5.336 -39.389 -41.094  1.00 47.65           O  
ANISOU 4434  O   ASN A 539     7447   4989   5671    223   1245   -131       O  
ATOM   4435  CB  ASN A 539       3.510 -42.092 -41.024  1.00 50.38           C  
ANISOU 4435  CB  ASN A 539     7806   5067   6268    166   1611   -213       C  
ATOM   4436  CG  ASN A 539       2.075 -42.267 -41.496  1.00 52.65           C  
ANISOU 4436  CG  ASN A 539     7937   5290   6778    101   1760   -304       C  
ATOM   4437  OD1 ASN A 539       1.566 -43.385 -41.563  1.00 55.84           O  
ANISOU 4437  OD1 ASN A 539     8329   5595   7291     83   1878   -339       O  
ATOM   4438  ND2 ASN A 539       1.416 -41.161 -41.830  1.00 54.26           N  
ANISOU 4438  ND2 ASN A 539     8012   5538   7068     67   1745   -347       N  
ATOM   4439  N   GLU A 540       6.609 -41.243 -41.072  1.00 49.84           N  
ANISOU 4439  N   GLU A 540     7819   5220   5897    295   1169    -94       N  
ATOM   4440  CA  GLU A 540       7.763 -40.564 -40.485  1.00 51.07           C  
ANISOU 4440  CA  GLU A 540     8079   5409   5916    347   1013    -33       C  
ATOM   4441  C   GLU A 540       8.357 -39.535 -41.461  1.00 49.08           C  
ANISOU 4441  C   GLU A 540     7637   5321   5688    345    869    -56       C  
ATOM   4442  O   GLU A 540       8.712 -38.429 -41.050  1.00 49.39           O  
ANISOU 4442  O   GLU A 540     7715   5397   5652    353    793    -28       O  
ATOM   4443  CB  GLU A 540       8.811 -41.573 -39.991  1.00 51.24           C  
ANISOU 4443  CB  GLU A 540     8233   5361   5876    414    923     12       C  
ATOM   4444  CG  GLU A 540      10.097 -40.954 -39.410  1.00 58.40           C  
ANISOU 4444  CG  GLU A 540     9230   6283   6676    476    723     64       C  
ATOM   4445  CD  GLU A 540       9.871 -40.052 -38.191  1.00 63.90           C  
ANISOU 4445  CD  GLU A 540    10142   6906   7230    475    733    111       C  
ATOM   4446  OE1 GLU A 540       9.053 -40.407 -37.313  1.00 68.09           O  
ANISOU 4446  OE1 GLU A 540    10878   7300   7693    454    892    132       O  
ATOM   4447  OE2 GLU A 540      10.530 -38.991 -38.102  1.00 62.51           O  
ANISOU 4447  OE2 GLU A 540     9941   6799   7010    492    593    123       O  
ATOM   4448  N   MET A 541       8.441 -39.892 -42.746  1.00 46.49           N  
ANISOU 4448  N   MET A 541     7124   5082   5460    333    841   -108       N  
ATOM   4449  CA  MET A 541       8.884 -38.948 -43.779  1.00 43.69           C  
ANISOU 4449  CA  MET A 541     6612   4866   5124    321    738   -135       C  
ATOM   4450  C   MET A 541       7.944 -37.748 -43.895  1.00 41.51           C  
ANISOU 4450  C   MET A 541     6289   4627   4858    273    772   -152       C  
ATOM   4451  O   MET A 541       8.400 -36.617 -44.056  1.00 42.00           O  
ANISOU 4451  O   MET A 541     6314   4767   4876    273    685   -139       O  
ATOM   4452  CB  MET A 541       9.042 -39.630 -45.141  1.00 43.32           C  
ANISOU 4452  CB  MET A 541     6420   4880   5162    311    725   -192       C  
ATOM   4453  CG  MET A 541      10.283 -40.508 -45.265  1.00 45.27           C  
ANISOU 4453  CG  MET A 541     6666   5119   5416    362    661   -183       C  
ATOM   4454  SD  MET A 541      10.493 -41.239 -46.903  1.00 45.68           S  
ANISOU 4454  SD  MET A 541     6567   5234   5554    343    670   -258       S  
ATOM   4455  CE  MET A 541      10.932 -39.806 -47.901  1.00 43.42           C  
ANISOU 4455  CE  MET A 541     6184   5076   5239    316    598   -277       C  
ATOM   4456  N   LEU A 542       6.640 -38.006 -43.808  1.00 39.47           N  
ANISOU 4456  N   LEU A 542     6022   4298   4678    232    901   -186       N  
ATOM   4457  CA  LEU A 542       5.633 -36.959 -43.886  1.00 38.95           C  
ANISOU 4457  CA  LEU A 542     5895   4240   4662    188    939   -214       C  
ATOM   4458  C   LEU A 542       5.792 -35.996 -42.715  1.00 38.76           C  
ANISOU 4458  C   LEU A 542     6005   4187   4536    196    950   -160       C  
ATOM   4459  O   LEU A 542       5.739 -34.784 -42.907  1.00 36.01           O  
ANISOU 4459  O   LEU A 542     5603   3905   4175    182    892   -161       O  
ATOM   4460  CB  LEU A 542       4.213 -37.549 -43.934  1.00 38.47           C  
ANISOU 4460  CB  LEU A 542     5786   4078   4753    144   1085   -274       C  
ATOM   4461  CG  LEU A 542       3.004 -36.598 -43.962  1.00 38.24           C  
ANISOU 4461  CG  LEU A 542     5674   4019   4836     98   1140   -318       C  
ATOM   4462  CD1 LEU A 542       3.048 -35.595 -45.127  1.00 38.01           C  
ANISOU 4462  CD1 LEU A 542     5503   4110   4827     89    984   -348       C  
ATOM   4463  CD2 LEU A 542       1.689 -37.377 -43.979  1.00 38.76           C  
ANISOU 4463  CD2 LEU A 542     5673   3958   5096     58   1289   -389       C  
ATOM   4464  N   PHE A 543       5.993 -36.548 -41.516  1.00 38.08           N  
ANISOU 4464  N   PHE A 543     6110   3992   4367    220   1018   -113       N  
ATOM   4465  CA  PHE A 543       6.305 -35.749 -40.331  1.00 39.64           C  
ANISOU 4465  CA  PHE A 543     6483   4145   4432    235   1009    -59       C  
ATOM   4466  C   PHE A 543       7.529 -34.871 -40.568  1.00 39.74           C  
ANISOU 4466  C   PHE A 543     6459   4273   4368    271    815    -29       C  
ATOM   4467  O   PHE A 543       7.537 -33.699 -40.197  1.00 39.87           O  
ANISOU 4467  O   PHE A 543     6502   4314   4333    262    782    -14       O  
ATOM   4468  CB  PHE A 543       6.533 -36.644 -39.103  1.00 41.75           C  
ANISOU 4468  CB  PHE A 543     7002   4266   4594    266   1076     -9       C  
ATOM   4469  CG  PHE A 543       6.870 -35.877 -37.840  1.00 44.45           C  
ANISOU 4469  CG  PHE A 543     7573   4541   4775    286   1053     46       C  
ATOM   4470  CD1 PHE A 543       5.863 -35.346 -37.042  1.00 45.91           C  
ANISOU 4470  CD1 PHE A 543     7879   4625   4940    242   1229     40       C  
ATOM   4471  CD2 PHE A 543       8.198 -35.688 -37.452  1.00 45.62           C  
ANISOU 4471  CD2 PHE A 543     7815   4713   4804    348    852     95       C  
ATOM   4472  CE1 PHE A 543       6.171 -34.637 -35.878  1.00 46.91           C  
ANISOU 4472  CE1 PHE A 543     8244   4681   4900    258   1211     87       C  
ATOM   4473  CE2 PHE A 543       8.516 -34.984 -36.294  1.00 42.65           C  
ANISOU 4473  CE2 PHE A 543     7665   4266   4276    369    805    140       C  
ATOM   4474  CZ  PHE A 543       7.502 -34.461 -35.507  1.00 45.61           C  
ANISOU 4474  CZ  PHE A 543     8187   4545   4600    323    986    138       C  
ATOM   4475  N   ARG A 544       8.558 -35.443 -41.190  1.00 39.20           N  
ANISOU 4475  N   ARG A 544     6320   4264   4309    308    697    -27       N  
ATOM   4476  CA  ARG A 544       9.795 -34.713 -41.447  1.00 38.84           C  
ANISOU 4476  CA  ARG A 544     6220   4309   4229    339    529    -10       C  
ATOM   4477  C   ARG A 544       9.596 -33.638 -42.515  1.00 38.96           C  
ANISOU 4477  C   ARG A 544     6062   4446   4295    300    502    -44       C  
ATOM   4478  O   ARG A 544      10.126 -32.533 -42.396  1.00 38.65           O  
ANISOU 4478  O   ARG A 544     6013   4457   4215    304    417    -27       O  
ATOM   4479  CB  ARG A 544      10.916 -35.674 -41.831  1.00 37.16           C  
ANISOU 4479  CB  ARG A 544     5967   4104   4049    386    439    -10       C  
ATOM   4480  CG  ARG A 544      11.403 -36.528 -40.669  1.00 39.91           C  
ANISOU 4480  CG  ARG A 544     6511   4326   4329    441    402     35       C  
ATOM   4481  CD  ARG A 544      12.307 -37.654 -41.126  1.00 41.32           C  
ANISOU 4481  CD  ARG A 544     6628   4494   4578    485    334     23       C  
ATOM   4482  NE  ARG A 544      12.753 -38.460 -39.992  1.00 49.92           N  
ANISOU 4482  NE  ARG A 544     7920   5445   5600    544    276     69       N  
ATOM   4483  CZ  ARG A 544      13.683 -39.412 -40.045  1.00 49.92           C  
ANISOU 4483  CZ  ARG A 544     7910   5400   5656    600    179     70       C  
ATOM   4484  NH1 ARG A 544      14.302 -39.707 -41.187  1.00 46.70           N  
ANISOU 4484  NH1 ARG A 544     7290   5073   5379    601    153     22       N  
ATOM   4485  NH2 ARG A 544      13.997 -40.072 -38.943  1.00 50.00           N  
ANISOU 4485  NH2 ARG A 544     8139   5267   5590    656    110    117       N  
ATOM   4486  N   ALA A 545       8.824 -33.974 -43.547  1.00 38.66           N  
ANISOU 4486  N   ALA A 545     5903   4441   4345    263    565    -94       N  
ATOM   4487  CA  ALA A 545       8.487 -33.033 -44.605  1.00 38.20           C  
ANISOU 4487  CA  ALA A 545     5712   4474   4326    226    532   -127       C  
ATOM   4488  C   ALA A 545       7.754 -31.830 -44.013  1.00 38.52           C  
ANISOU 4488  C   ALA A 545     5784   4501   4350    201    558   -116       C  
ATOM   4489  O   ALA A 545       8.093 -30.675 -44.301  1.00 37.15           O  
ANISOU 4489  O   ALA A 545     5567   4398   4148    194    483   -108       O  
ATOM   4490  CB  ALA A 545       7.630 -33.718 -45.679  1.00 35.83           C  
ANISOU 4490  CB  ALA A 545     5314   4176   4122    196    580   -187       C  
ATOM   4491  N   GLN A 546       6.771 -32.123 -43.163  1.00 38.31           N  
ANISOU 4491  N   GLN A 546     5836   4372   4348    186    680   -119       N  
ATOM   4492  CA  GLN A 546       5.937 -31.104 -42.550  1.00 40.70           C  
ANISOU 4492  CA  GLN A 546     6169   4636   4661    158    742   -121       C  
ATOM   4493  C   GLN A 546       6.730 -30.228 -41.585  1.00 39.81           C  
ANISOU 4493  C   GLN A 546     6182   4526   4418    182    682    -66       C  
ATOM   4494  O   GLN A 546       6.435 -29.031 -41.458  1.00 40.94           O  
ANISOU 4494  O   GLN A 546     6306   4692   4557    162    672    -67       O  
ATOM   4495  CB  GLN A 546       4.715 -31.734 -41.862  1.00 41.49           C  
ANISOU 4495  CB  GLN A 546     6328   4599   4839    131    925   -147       C  
ATOM   4496  CG  GLN A 546       3.620 -32.187 -42.842  1.00 45.01           C  
ANISOU 4496  CG  GLN A 546     6608   5029   5465     95    973   -221       C  
ATOM   4497  CD  GLN A 546       2.507 -33.021 -42.196  1.00 50.66           C  
ANISOU 4497  CD  GLN A 546     7364   5591   6295     67   1172   -257       C  
ATOM   4498  OE1 GLN A 546       1.429 -33.178 -42.778  1.00 51.27           O  
ANISOU 4498  OE1 GLN A 546     7300   5624   6558     33   1222   -328       O  
ATOM   4499  NE2 GLN A 546       2.765 -33.561 -40.997  1.00 48.53           N  
ANISOU 4499  NE2 GLN A 546     7292   5223   5922     81   1283   -211       N  
ATOM   4500  N   ARG A 547       7.733 -30.812 -40.924  1.00 36.84           N  
ANISOU 4500  N   ARG A 547     5931   4120   3946    227    628    -24       N  
ATOM   4501  CA  ARG A 547       8.637 -30.034 -40.074  1.00 38.35           C  
ANISOU 4501  CA  ARG A 547     6240   4309   4023    259    524     21       C  
ATOM   4502  C   ARG A 547       9.520 -29.091 -40.884  1.00 36.50           C  
ANISOU 4502  C   ARG A 547     5864   4199   3804    263    382     18       C  
ATOM   4503  O   ARG A 547       9.679 -27.924 -40.531  1.00 37.93           O  
ANISOU 4503  O   ARG A 547     6067   4402   3944    258    334     31       O  
ATOM   4504  CB  ARG A 547       9.487 -30.932 -39.177  1.00 38.89           C  
ANISOU 4504  CB  ARG A 547     6483   4293   4002    313    468     60       C  
ATOM   4505  CG  ARG A 547       8.760 -31.414 -37.934  1.00 42.47           C  
ANISOU 4505  CG  ARG A 547     7173   4592   4372    310    604     82       C  
ATOM   4506  CD  ARG A 547       8.369 -30.245 -37.029  1.00 42.59           C  
ANISOU 4506  CD  ARG A 547     7320   4561   4301    290    644     96       C  
ATOM   4507  NE  ARG A 547       7.519 -30.666 -35.918  1.00 46.96           N  
ANISOU 4507  NE  ARG A 547     8109   4951   4780    272    829    107       N  
ATOM   4508  CZ  ARG A 547       7.975 -31.089 -34.743  1.00 51.11           C  
ANISOU 4508  CZ  ARG A 547     8925   5349   5145    310    805    154       C  
ATOM   4509  NH1 ARG A 547       9.283 -31.154 -34.517  1.00 54.12           N  
ANISOU 4509  NH1 ARG A 547     9371   5747   5445    374    576    188       N  
ATOM   4510  NH2 ARG A 547       7.125 -31.447 -33.793  1.00 52.26           N  
ANISOU 4510  NH2 ARG A 547     9303   5333   5219    284   1010    161       N  
ATOM   4511  N   THR A 548      10.080 -29.587 -41.977  1.00 36.11           N  
ANISOU 4511  N   THR A 548     5680   4221   3818    270    331     -3       N  
ATOM   4512  CA  THR A 548      10.824 -28.724 -42.891  1.00 36.70           C  
ANISOU 4512  CA  THR A 548     5624   4399   3920    262    239    -13       C  
ATOM   4513  C   THR A 548       9.936 -27.584 -43.404  1.00 34.22           C  
ANISOU 4513  C   THR A 548     5242   4134   3625    215    271    -30       C  
ATOM   4514  O   THR A 548      10.342 -26.418 -43.381  1.00 34.61           O  
ANISOU 4514  O   THR A 548     5274   4227   3651    209    208    -17       O  
ATOM   4515  CB  THR A 548      11.431 -29.517 -44.052  1.00 37.79           C  
ANISOU 4515  CB  THR A 548     5649   4587   4122    267    223    -42       C  
ATOM   4516  OG1 THR A 548      12.173 -30.618 -43.520  1.00 36.36           O  
ANISOU 4516  OG1 THR A 548     5526   4345   3944    314    193    -30       O  
ATOM   4517  CG2 THR A 548      12.355 -28.632 -44.878  1.00 35.31           C  
ANISOU 4517  CG2 THR A 548     5233   4354   3831    258    153    -51       C  
ATOM   4518  N   GLU A 549       8.714 -27.919 -43.819  1.00 34.43           N  
ANISOU 4518  N   GLU A 549     5231   4139   3710    184    359    -62       N  
ATOM   4519  CA  GLU A 549       7.736 -26.898 -44.220  1.00 35.13           C  
ANISOU 4519  CA  GLU A 549     5257   4246   3844    146    376    -84       C  
ATOM   4520  C   GLU A 549       7.518 -25.816 -43.152  1.00 33.01           C  
ANISOU 4520  C   GLU A 549     5067   3944   3532    141    391    -59       C  
ATOM   4521  O   GLU A 549       7.613 -24.636 -43.456  1.00 35.27           O  
ANISOU 4521  O   GLU A 549     5307   4281   3812    127    333    -55       O  
ATOM   4522  CB  GLU A 549       6.397 -27.526 -44.616  1.00 36.35           C  
ANISOU 4522  CB  GLU A 549     5359   4348   4107    119    460   -132       C  
ATOM   4523  CG  GLU A 549       5.456 -26.516 -45.267  1.00 39.28           C  
ANISOU 4523  CG  GLU A 549     5638   4732   4555     86    434   -165       C  
ATOM   4524  CD  GLU A 549       4.047 -27.027 -45.466  1.00 42.19           C  
ANISOU 4524  CD  GLU A 549     5940   5017   5074     62    507   -225       C  
ATOM   4525  OE1 GLU A 549       3.845 -28.265 -45.508  1.00 45.43           O  
ANISOU 4525  OE1 GLU A 549     6352   5383   5528     66    567   -247       O  
ATOM   4526  OE2 GLU A 549       3.139 -26.173 -45.595  1.00 38.72           O  
ANISOU 4526  OE2 GLU A 549     5436   4548   4728     40    500   -255       O  
ATOM   4527  N   VAL A 550       7.245 -26.225 -41.911  1.00 33.42           N  
ANISOU 4527  N   VAL A 550     5255   3899   3545    152    475    -43       N  
ATOM   4528  CA  VAL A 550       7.073 -25.288 -40.786  1.00 33.14           C  
ANISOU 4528  CA  VAL A 550     5336   3811   3446    148    504    -22       C  
ATOM   4529  C   VAL A 550       8.296 -24.395 -40.588  1.00 34.45           C  
ANISOU 4529  C   VAL A 550     5526   4038   3526    172    363     12       C  
ATOM   4530  O   VAL A 550       8.156 -23.178 -40.405  1.00 34.30           O  
ANISOU 4530  O   VAL A 550     5501   4037   3496    156    343     15       O  
ATOM   4531  CB  VAL A 550       6.725 -26.004 -39.444  1.00 32.63           C  
ANISOU 4531  CB  VAL A 550     5471   3610   3316    157    626     -6       C  
ATOM   4532  CG1 VAL A 550       6.816 -25.020 -38.270  1.00 33.14           C  
ANISOU 4532  CG1 VAL A 550     5698   3618   3276    158    635     19       C  
ATOM   4533  CG2 VAL A 550       5.325 -26.624 -39.496  1.00 28.88           C  
ANISOU 4533  CG2 VAL A 550     4963   3048   2960    119    807    -51       C  
ATOM   4534  N   ALA A 551       9.482 -25.005 -40.619  1.00 34.19           N  
ANISOU 4534  N   ALA A 551     5510   4026   3455    211    265     32       N  
ATOM   4535  CA  ALA A 551      10.746 -24.271 -40.504  1.00 34.57           C  
ANISOU 4535  CA  ALA A 551     5550   4118   3467    237    121     51       C  
ATOM   4536  C   ALA A 551      10.835 -23.200 -41.596  1.00 34.26           C  
ANISOU 4536  C   ALA A 551     5354   4180   3484    205     85     36       C  
ATOM   4537  O   ALA A 551      11.191 -22.051 -41.325  1.00 35.92           O  
ANISOU 4537  O   ALA A 551     5567   4409   3672    200     26     47       O  
ATOM   4538  CB  ALA A 551      11.938 -25.244 -40.594  1.00 33.96           C  
ANISOU 4538  CB  ALA A 551     5466   4036   3401    282     29     57       C  
ATOM   4539  N   GLY A 552      10.494 -23.592 -42.825  1.00 33.83           N  
ANISOU 4539  N   GLY A 552     5181   4178   3496    183    121     11       N  
ATOM   4540  CA  GLY A 552      10.483 -22.684 -43.967  1.00 31.77           C  
ANISOU 4540  CA  GLY A 552     4808   3995   3270    151     93     -2       C  
ATOM   4541  C   GLY A 552       9.445 -21.592 -43.804  1.00 31.89           C  
ANISOU 4541  C   GLY A 552     4824   4001   3293    122    121     -5       C  
ATOM   4542  O   GLY A 552       9.721 -20.419 -44.094  1.00 30.63           O  
ANISOU 4542  O   GLY A 552     4628   3883   3126    107     71      3       O  
ATOM   4543  N   MET A 553       8.256 -21.976 -43.332  1.00 30.40           N  
ANISOU 4543  N   MET A 553     4670   3744   3135    112    211    -22       N  
ATOM   4544  CA  MET A 553       7.196 -21.016 -43.036  1.00 32.29           C  
ANISOU 4544  CA  MET A 553     4903   3949   3416     85    256    -35       C  
ATOM   4545  C   MET A 553       7.669 -19.958 -42.035  1.00 32.31           C  
ANISOU 4545  C   MET A 553     4989   3940   3346     92    230     -6       C  
ATOM   4546  O   MET A 553       7.445 -18.764 -42.255  1.00 32.28           O  
ANISOU 4546  O   MET A 553     4941   3961   3363     73    200     -8       O  
ATOM   4547  CB  MET A 553       5.924 -21.722 -42.549  1.00 35.10           C  
ANISOU 4547  CB  MET A 553     5282   4207   3848     72    387    -67       C  
ATOM   4548  CG  MET A 553       4.787 -20.787 -42.087  1.00 40.93           C  
ANISOU 4548  CG  MET A 553     6007   4880   4665     45    462    -92       C  
ATOM   4549  SD  MET A 553       4.119 -19.719 -43.385  1.00 48.14           S  
ANISOU 4549  SD  MET A 553     6759   5840   5693     22    368   -123       S  
ATOM   4550  CE  MET A 553       2.945 -20.783 -44.210  1.00 44.88           C  
ANISOU 4550  CE  MET A 553     6237   5369   5445     10    401   -187       C  
ATOM   4551  N   THR A 554       8.345 -20.381 -40.965  1.00 29.72           N  
ANISOU 4551  N   THR A 554     4793   3568   2932    121    224     18       N  
ATOM   4552  CA  THR A 554       8.820 -19.420 -39.952  1.00 31.35           C  
ANISOU 4552  CA  THR A 554     5104   3748   3059    130    180     40       C  
ATOM   4553  C   THR A 554       9.796 -18.409 -40.553  1.00 31.07           C  
ANISOU 4553  C   THR A 554     4978   3800   3029    130     55     50       C  
ATOM   4554  O   THR A 554       9.639 -17.190 -40.382  1.00 31.99           O  
ANISOU 4554  O   THR A 554     5088   3924   3143    112     39     51       O  
ATOM   4555  CB  THR A 554       9.491 -20.106 -38.747  1.00 30.23           C  
ANISOU 4555  CB  THR A 554     5146   3528   2811    169    153     63       C  
ATOM   4556  OG1 THR A 554       8.520 -20.884 -38.025  1.00 32.22           O  
ANISOU 4556  OG1 THR A 554     5525   3675   3041    162    302     56       O  
ATOM   4557  CG2 THR A 554      10.093 -19.061 -37.816  1.00 30.66           C  
ANISOU 4557  CG2 THR A 554     5312   3556   2782    182     68     79       C  
ATOM   4558  N   ALA A 555      10.789 -18.937 -41.262  1.00 29.55           N  
ANISOU 4558  N   ALA A 555     4712   3660   2857    147    -17     52       N  
ATOM   4559  CA  ALA A 555      11.829 -18.133 -41.857  1.00 31.30           C  
ANISOU 4559  CA  ALA A 555     4844   3945   3104    143   -108     56       C  
ATOM   4560  C   ALA A 555      11.278 -17.135 -42.881  1.00 31.38           C  
ANISOU 4560  C   ALA A 555     4760   4010   3152    102    -87     49       C  
ATOM   4561  O   ALA A 555      11.677 -15.961 -42.880  1.00 32.19           O  
ANISOU 4561  O   ALA A 555     4842   4135   3256     90   -134     57       O  
ATOM   4562  CB  ALA A 555      12.880 -19.026 -42.482  1.00 33.48           C  
ANISOU 4562  CB  ALA A 555     5053   4245   3421    164   -149     48       C  
ATOM   4563  N   GLN A 556      10.340 -17.590 -43.714  1.00 28.16           N  
ANISOU 4563  N   GLN A 556     4307   3613   2779     84    -29     33       N  
ATOM   4564  CA  GLN A 556       9.836 -16.770 -44.816  1.00 27.08           C  
ANISOU 4564  CA  GLN A 556     4101   3514   2674     52    -38     26       C  
ATOM   4565  C   GLN A 556       8.766 -15.761 -44.403  1.00 30.61           C  
ANISOU 4565  C   GLN A 556     4556   3927   3147     35    -22     22       C  
ATOM   4566  O   GLN A 556       8.820 -14.600 -44.824  1.00 32.29           O  
ANISOU 4566  O   GLN A 556     4741   4165   3365     17    -65     31       O  
ATOM   4567  CB  GLN A 556       9.373 -17.631 -46.011  1.00 24.00           C  
ANISOU 4567  CB  GLN A 556     3667   3139   2313     42    -21      4       C  
ATOM   4568  CG  GLN A 556       8.022 -18.326 -45.867  1.00 25.38           C  
ANISOU 4568  CG  GLN A 556     3839   3260   2545     41     31    -24       C  
ATOM   4569  CD  GLN A 556       6.829 -17.419 -46.183  1.00 27.39           C  
ANISOU 4569  CD  GLN A 556     4054   3485   2867     20     15    -43       C  
ATOM   4570  OE1 GLN A 556       6.980 -16.346 -46.772  1.00 28.14           O  
ANISOU 4570  OE1 GLN A 556     4134   3609   2948      6    -48    -31       O  
ATOM   4571  NE2 GLN A 556       5.639 -17.854 -45.789  1.00 23.60           N  
ANISOU 4571  NE2 GLN A 556     3555   2934   2478     17     75    -77       N  
ATOM   4572  N   ILE A 557       7.800 -16.190 -43.585  1.00 32.38           N  
ANISOU 4572  N   ILE A 557     4820   4083   3398     38     53      5       N  
ATOM   4573  CA  ILE A 557       6.659 -15.330 -43.277  1.00 33.12           C  
ANISOU 4573  CA  ILE A 557     4900   4127   3557     19     93    -13       C  
ATOM   4574  C   ILE A 557       7.055 -14.159 -42.387  1.00 33.82           C  
ANISOU 4574  C   ILE A 557     5047   4206   3596     17     78      6       C  
ATOM   4575  O   ILE A 557       6.480 -13.065 -42.482  1.00 35.30           O  
ANISOU 4575  O   ILE A 557     5198   4381   3833      0     71     -2       O  
ATOM   4576  CB  ILE A 557       5.434 -16.107 -42.715  1.00 34.11           C  
ANISOU 4576  CB  ILE A 557     5038   4159   3763     14    212    -49       C  
ATOM   4577  CG1 ILE A 557       4.159 -15.261 -42.880  1.00 31.51           C  
ANISOU 4577  CG1 ILE A 557     4631   3773   3567     -8    238    -86       C  
ATOM   4578  CG2 ILE A 557       5.669 -16.582 -41.265  1.00 33.57           C  
ANISOU 4578  CG2 ILE A 557     5115   4026   3616     28    302    -37       C  
ATOM   4579  CD1 ILE A 557       2.864 -16.019 -42.641  1.00 34.41           C  
ANISOU 4579  CD1 ILE A 557     4959   4037   4077    -19    357   -140       C  
ATOM   4580  N   ASN A 558       8.060 -14.380 -41.551  1.00 31.24           N  
ANISOU 4580  N   ASN A 558     4812   3880   3179     39     56     28       N  
ATOM   4581  CA  ASN A 558       8.514 -13.327 -40.656  1.00 30.62           C  
ANISOU 4581  CA  ASN A 558     4804   3783   3046     40     24     41       C  
ATOM   4582  C   ASN A 558       9.487 -12.367 -41.323  1.00 30.72           C  
ANISOU 4582  C   ASN A 558     4745   3868   3060     34    -81     57       C  
ATOM   4583  O   ASN A 558       9.629 -11.225 -40.882  1.00 32.53           O  
ANISOU 4583  O   ASN A 558     4995   4089   3278     25   -110     62       O  
ATOM   4584  CB  ASN A 558       9.061 -13.923 -39.376  1.00 27.73           C  
ANISOU 4584  CB  ASN A 558     4594   3357   2585     69     25     51       C  
ATOM   4585  CG  ASN A 558       7.972 -14.523 -38.536  1.00 30.88           C  
ANISOU 4585  CG  ASN A 558     5103   3656   2973     64    167     34       C  
ATOM   4586  OD1 ASN A 558       7.086 -13.809 -38.074  1.00 31.00           O  
ANISOU 4586  OD1 ASN A 558     5147   3615   3017     40    255     15       O  
ATOM   4587  ND2 ASN A 558       8.003 -15.847 -38.356  1.00 29.19           N  
ANISOU 4587  ND2 ASN A 558     4948   3410   2734     82    206     36       N  
ATOM   4588  N   ARG A 559      10.123 -12.809 -42.408  1.00 29.50           N  
ANISOU 4588  N   ARG A 559     4509   3773   2924     34   -121     63       N  
ATOM   4589  CA  ARG A 559      10.928 -11.887 -43.202  1.00 31.04           C  
ANISOU 4589  CA  ARG A 559     4637   4021   3135     17   -181     74       C  
ATOM   4590  C   ARG A 559       9.990 -11.043 -44.048  1.00 30.77           C  
ANISOU 4590  C   ARG A 559     4558   3995   3137    -12   -170     73       C  
ATOM   4591  O   ARG A 559      10.230  -9.851 -44.262  1.00 30.66           O  
ANISOU 4591  O   ARG A 559     4527   3994   3129    -29   -204     85       O  
ATOM   4592  CB  ARG A 559      11.980 -12.619 -44.036  1.00 30.95           C  
ANISOU 4592  CB  ARG A 559     4574   4049   3136     22   -199     74       C  
ATOM   4593  CG  ARG A 559      13.196 -12.999 -43.208  1.00 32.45           C  
ANISOU 4593  CG  ARG A 559     4783   4221   3327     52   -255     71       C  
ATOM   4594  CD  ARG A 559      14.149 -13.902 -43.963  1.00 34.77           C  
ANISOU 4594  CD  ARG A 559     5011   4534   3665     60   -254     59       C  
ATOM   4595  NE  ARG A 559      15.343 -14.185 -43.169  1.00 33.83           N  
ANISOU 4595  NE  ARG A 559     4889   4379   3584     94   -335     48       N  
ATOM   4596  CZ  ARG A 559      15.428 -15.136 -42.240  1.00 35.26           C  
ANISOU 4596  CZ  ARG A 559     5146   4513   3739    136   -377     47       C  
ATOM   4597  NH1 ARG A 559      14.389 -15.920 -41.973  1.00 29.39           N  
ANISOU 4597  NH1 ARG A 559     4481   3754   2930    143   -315     57       N  
ATOM   4598  NH2 ARG A 559      16.563 -15.306 -41.577  1.00 33.89           N  
ANISOU 4598  NH2 ARG A 559     4970   4293   3613    172   -486     34       N  
ATOM   4599  N   LYS A 560       8.904 -11.677 -44.492  1.00 30.20           N  
ANISOU 4599  N   LYS A 560     4469   3904   3100    -14   -134     56       N  
ATOM   4600  CA  LYS A 560       7.816 -10.987 -45.161  1.00 30.17           C  
ANISOU 4600  CA  LYS A 560     4427   3881   3156    -31   -149     46       C  
ATOM   4601  C   LYS A 560       7.232  -9.916 -44.237  1.00 28.99           C  
ANISOU 4601  C   LYS A 560     4290   3685   3041    -37   -130     41       C  
ATOM   4602  O   LYS A 560       7.027  -8.777 -44.653  1.00 27.66           O  
ANISOU 4602  O   LYS A 560     4097   3515   2899    -51   -175     48       O  
ATOM   4603  CB  LYS A 560       6.730 -11.983 -45.598  1.00 30.39           C  
ANISOU 4603  CB  LYS A 560     4424   3873   3249    -27   -124     14       C  
ATOM   4604  CG  LYS A 560       5.431 -11.320 -46.033  1.00 30.25           C  
ANISOU 4604  CG  LYS A 560     4354   3801   3337    -36   -156    -11       C  
ATOM   4605  CD  LYS A 560       4.363 -12.328 -46.387  1.00 29.89           C  
ANISOU 4605  CD  LYS A 560     4261   3703   3391    -31   -141    -56       C  
ATOM   4606  CE  LYS A 560       3.008 -11.641 -46.478  1.00 32.03           C  
ANISOU 4606  CE  LYS A 560     4460   3890   3820    -36   -169    -96       C  
ATOM   4607  NZ  LYS A 560       1.931 -12.560 -46.994  1.00 33.43           N  
ANISOU 4607  NZ  LYS A 560     4567   4001   4134    -30   -185   -151       N  
ATOM   4608  N   LEU A 561       6.963 -10.289 -42.987  1.00 28.82           N  
ANISOU 4608  N   LEU A 561     4324   3612   3013    -27    -56     27       N  
ATOM   4609  CA  LEU A 561       6.425  -9.339 -42.019  1.00 31.64           C  
ANISOU 4609  CA  LEU A 561     4718   3911   3395    -35    -11     15       C  
ATOM   4610  C   LEU A 561       7.384  -8.168 -41.845  1.00 31.66           C  
ANISOU 4610  C   LEU A 561     4740   3949   3340    -40    -82     41       C  
ATOM   4611  O   LEU A 561       6.964  -7.008 -41.891  1.00 34.26           O  
ANISOU 4611  O   LEU A 561     5042   4260   3714    -55    -94     38       O  
ATOM   4612  CB  LEU A 561       6.113 -10.018 -40.674  1.00 32.32           C  
ANISOU 4612  CB  LEU A 561     4911   3921   3448    -26     99     -2       C  
ATOM   4613  CG  LEU A 561       5.637  -9.145 -39.504  1.00 35.83           C  
ANISOU 4613  CG  LEU A 561     5438   4286   3891    -37    176    -19       C  
ATOM   4614  CD1 LEU A 561       4.275  -8.493 -39.774  1.00 37.84           C  
ANISOU 4614  CD1 LEU A 561     5596   4477   4303    -58    239    -58       C  
ATOM   4615  CD2 LEU A 561       5.590  -9.969 -38.223  1.00 42.58           C  
ANISOU 4615  CD2 LEU A 561     6457   5059   4664    -28    283    -27       C  
ATOM   4616  N   LEU A 562       8.669  -8.473 -41.670  1.00 29.89           N  
ANISOU 4616  N   LEU A 562     4551   3768   3039    -27   -132     61       N  
ATOM   4617  CA  LEU A 562       9.681  -7.433 -41.546  1.00 30.53           C  
ANISOU 4617  CA  LEU A 562     4632   3874   3094    -33   -204     76       C  
ATOM   4618  C   LEU A 562       9.702  -6.457 -42.731  1.00 31.25           C  
ANISOU 4618  C   LEU A 562     4642   4003   3229    -58   -242     91       C  
ATOM   4619  O   LEU A 562       9.725  -5.239 -42.519  1.00 33.87           O  
ANISOU 4619  O   LEU A 562     4973   4322   3574    -72   -264     95       O  
ATOM   4620  CB  LEU A 562      11.070  -8.031 -41.293  1.00 30.35           C  
ANISOU 4620  CB  LEU A 562     4628   3874   3030    -12   -264     83       C  
ATOM   4621  CG  LEU A 562      12.203  -7.030 -41.024  1.00 30.66           C  
ANISOU 4621  CG  LEU A 562     4655   3919   3075    -16   -345     86       C  
ATOM   4622  CD1 LEU A 562      12.008  -6.264 -39.686  1.00 31.24           C  
ANISOU 4622  CD1 LEU A 562     4833   3932   3105    -10   -362     75       C  
ATOM   4623  CD2 LEU A 562      13.552  -7.741 -41.048  1.00 28.31           C  
ANISOU 4623  CD2 LEU A 562     4331   3634   2794      5   -410     80       C  
ATOM   4624  N   ILE A 563       9.691  -6.961 -43.966  1.00 28.73           N  
ANISOU 4624  N   ILE A 563     4276   3719   2922    -64   -249     99       N  
ATOM   4625  CA  ILE A 563       9.719  -6.039 -45.119  1.00 28.98           C  
ANISOU 4625  CA  ILE A 563     4276   3767   2967    -89   -285    117       C  
ATOM   4626  C   ILE A 563       8.420  -5.246 -45.279  1.00 30.40           C  
ANISOU 4626  C   ILE A 563     4445   3903   3204    -95   -300    110       C  
ATOM   4627  O   ILE A 563       8.457  -4.057 -45.603  1.00 30.14           O  
ANISOU 4627  O   ILE A 563     4409   3861   3182   -111   -336    126       O  
ATOM   4628  CB  ILE A 563      10.185  -6.688 -46.463  1.00 30.24           C  
ANISOU 4628  CB  ILE A 563     4430   3961   3100    -98   -287    127       C  
ATOM   4629  CG1 ILE A 563       9.330  -7.902 -46.841  1.00 26.51           C  
ANISOU 4629  CG1 ILE A 563     3956   3480   2635    -84   -274    109       C  
ATOM   4630  CG2 ILE A 563      11.677  -7.032 -46.397  1.00 28.69           C  
ANISOU 4630  CG2 ILE A 563     4219   3794   2888   -100   -269    130       C  
ATOM   4631  CD1 ILE A 563       9.810  -8.648 -48.073  1.00 23.37           C  
ANISOU 4631  CD1 ILE A 563     3575   3108   2196    -92   -269    113       C  
ATOM   4632  N   ASN A 564       7.282  -5.897 -45.029  1.00 27.76           N  
ANISOU 4632  N   ASN A 564     4095   3527   2925    -82   -270     82       N  
ATOM   4633  CA  ASN A 564       6.002  -5.193 -44.985  1.00 27.93           C  
ANISOU 4633  CA  ASN A 564     4080   3482   3049    -84   -279     60       C  
ATOM   4634  C   ASN A 564       5.899  -4.131 -43.871  1.00 29.88           C  
ANISOU 4634  C   ASN A 564     4342   3692   3318    -90   -242     52       C  
ATOM   4635  O   ASN A 564       5.252  -3.093 -44.058  1.00 30.04           O  
ANISOU 4635  O   ASN A 564     4330   3670   3415    -96   -274     46       O  
ATOM   4636  CB  ASN A 564       4.855  -6.188 -44.897  1.00 26.00           C  
ANISOU 4636  CB  ASN A 564     3797   3185   2897    -72   -236     18       C  
ATOM   4637  CG  ASN A 564       4.604  -6.901 -46.219  1.00 28.57           C  
ANISOU 4637  CG  ASN A 564     4101   3523   3232    -67   -309     16       C  
ATOM   4638  OD1 ASN A 564       5.003  -6.427 -47.283  1.00 27.72           O  
ANISOU 4638  OD1 ASN A 564     4019   3442   3071    -74   -395     44       O  
ATOM   4639  ND2 ASN A 564       3.926  -8.034 -46.157  1.00 26.86           N  
ANISOU 4639  ND2 ASN A 564     3853   3274   3079    -57   -270    -20       N  
ATOM   4640  N   SER A 565       6.549  -4.393 -42.733  1.00 28.75           N  
ANISOU 4640  N   SER A 565     4261   3555   3106    -85   -188     51       N  
ATOM   4641  CA  SER A 565       6.627  -3.431 -41.621  1.00 30.94           C  
ANISOU 4641  CA  SER A 565     4588   3795   3374    -91   -158     43       C  
ATOM   4642  C   SER A 565       7.402  -2.164 -41.958  1.00 31.48           C  
ANISOU 4642  C   SER A 565     4643   3895   3423   -105   -234     69       C  
ATOM   4643  O   SER A 565       7.177  -1.116 -41.337  1.00 32.29           O  
ANISOU 4643  O   SER A 565     4762   3957   3550   -114   -223     59       O  
ATOM   4644  CB  SER A 565       7.254  -4.077 -40.391  1.00 30.12           C  
ANISOU 4644  CB  SER A 565     4591   3679   3176    -78   -116     37       C  
ATOM   4645  OG  SER A 565       6.562  -5.264 -40.056  1.00 36.34           O  
ANISOU 4645  OG  SER A 565     5407   4425   3974    -68    -29     15       O  
ATOM   4646  N   LEU A 566       8.333  -2.265 -42.908  1.00 30.26           N  
ANISOU 4646  N   LEU A 566     4465   3803   3229   -111   -293     99       N  
ATOM   4647  CA  LEU A 566       9.044  -1.089 -43.389  1.00 32.82           C  
ANISOU 4647  CA  LEU A 566     4774   4145   3550   -131   -343    124       C  
ATOM   4648  C   LEU A 566       8.079  -0.137 -44.085  1.00 33.14           C  
ANISOU 4648  C   LEU A 566     4788   4149   3656   -141   -372    131       C  
ATOM   4649  O   LEU A 566       8.167   1.072 -43.896  1.00 35.04           O  
ANISOU 4649  O   LEU A 566     5028   4367   3918   -154   -391    137       O  
ATOM   4650  CB  LEU A 566      10.208  -1.460 -44.319  1.00 31.79           C  
ANISOU 4650  CB  LEU A 566     4631   4069   3381   -142   -364    147       C  
ATOM   4651  CG  LEU A 566      11.109  -0.294 -44.748  1.00 33.29           C  
ANISOU 4651  CG  LEU A 566     4810   4262   3577   -170   -385    168       C  
ATOM   4652  CD1 LEU A 566      11.547   0.550 -43.547  1.00 32.13           C  
ANISOU 4652  CD1 LEU A 566     4667   4092   3447   -170   -403    151       C  
ATOM   4653  CD2 LEU A 566      12.317  -0.775 -45.532  1.00 32.96           C  
ANISOU 4653  CD2 LEU A 566     4751   4251   3520   -185   -365    177       C  
ATOM   4654  N   ALA A 567       7.166  -0.693 -44.881  1.00 33.95           N  
ANISOU 4654  N   ALA A 567     4868   4234   3798   -132   -390    125       N  
ATOM   4655  CA  ALA A 567       6.129   0.089 -45.555  1.00 33.07           C  
ANISOU 4655  CA  ALA A 567     4730   4065   3770   -131   -451    124       C  
ATOM   4656  C   ALA A 567       5.183   0.735 -44.543  1.00 32.28           C  
ANISOU 4656  C   ALA A 567     4593   3894   3778   -126   -411     86       C  
ATOM   4657  O   ALA A 567       4.766   1.884 -44.715  1.00 32.23           O  
ANISOU 4657  O   ALA A 567     4567   3840   3837   -130   -455     89       O  
ATOM   4658  CB  ALA A 567       5.355  -0.785 -46.525  1.00 32.76           C  
ANISOU 4658  CB  ALA A 567     4676   4007   3764   -117   -500    114       C  
ATOM   4659  N   GLY A 568       4.852  -0.005 -43.486  1.00 31.78           N  
ANISOU 4659  N   GLY A 568     4532   3811   3734   -119   -315     50       N  
ATOM   4660  CA  GLY A 568       4.000   0.514 -42.417  1.00 30.37           C  
ANISOU 4660  CA  GLY A 568     4340   3548   3650   -120   -233      5       C  
ATOM   4661  C   GLY A 568       4.708   1.545 -41.553  1.00 32.34           C  
ANISOU 4661  C   GLY A 568     4649   3803   3837   -134   -214     14       C  
ATOM   4662  O   GLY A 568       4.116   2.564 -41.177  1.00 32.65           O  
ANISOU 4662  O   GLY A 568     4668   3776   3962   -140   -193     -8       O  
ATOM   4663  N   ALA A 569       5.978   1.286 -41.244  1.00 30.29           N  
ANISOU 4663  N   ALA A 569     4455   3610   3445   -136   -229     40       N  
ATOM   4664  CA  ALA A 569       6.768   2.162 -40.385  1.00 31.24           C  
ANISOU 4664  CA  ALA A 569     4635   3728   3506   -146   -234     41       C  
ATOM   4665  C   ALA A 569       6.838   3.591 -40.925  1.00 33.18           C  
ANISOU 4665  C   ALA A 569     4837   3966   3802   -162   -294     59       C  
ATOM   4666  O   ALA A 569       6.826   4.550 -40.154  1.00 34.02           O  
ANISOU 4666  O   ALA A 569     4973   4031   3921   -171   -276     41       O  
ATOM   4667  CB  ALA A 569       8.160   1.594 -40.187  1.00 30.84           C  
ANISOU 4667  CB  ALA A 569     4632   3739   3347   -141   -277     60       C  
ATOM   4668  N   LEU A 570       6.889   3.721 -42.249  1.00 32.53           N  
ANISOU 4668  N   LEU A 570     4706   3915   3741   -166   -363     94       N  
ATOM   4669  CA  LEU A 570       6.846   5.016 -42.923  1.00 32.03           C  
ANISOU 4669  CA  LEU A 570     4619   3829   3720   -180   -422    118       C  
ATOM   4670  C   LEU A 570       5.587   5.799 -42.544  1.00 32.42           C  
ANISOU 4670  C   LEU A 570     4632   3790   3895   -174   -406     85       C  
ATOM   4671  O   LEU A 570       5.535   7.020 -42.715  1.00 33.54           O  
ANISOU 4671  O   LEU A 570     4765   3899   4081   -183   -444     96       O  
ATOM   4672  CB  LEU A 570       6.925   4.835 -44.449  1.00 31.88           C  
ANISOU 4672  CB  LEU A 570     4597   3833   3683   -182   -493    160       C  
ATOM   4673  CG  LEU A 570       8.204   4.287 -45.094  1.00 28.65           C  
ANISOU 4673  CG  LEU A 570     4220   3493   3172   -197   -492    192       C  
ATOM   4674  CD1 LEU A 570       7.950   3.967 -46.557  1.00 23.78           C  
ANISOU 4674  CD1 LEU A 570     3634   2872   2527   -197   -543    223       C  
ATOM   4675  CD2 LEU A 570       9.377   5.279 -44.979  1.00 27.77           C  
ANISOU 4675  CD2 LEU A 570     4121   3393   3038   -225   -487    210       C  
ATOM   4676  N   GLY A 571       4.585   5.086 -42.028  1.00 32.56           N  
ANISOU 4676  N   GLY A 571     4625   3760   3987   -159   -339     40       N  
ATOM   4677  CA  GLY A 571       3.354   5.701 -41.509  1.00 33.49           C  
ANISOU 4677  CA  GLY A 571     4693   3773   4260   -155   -286    -10       C  
ATOM   4678  C   GLY A 571       3.222   5.751 -39.987  1.00 33.48           C  
ANISOU 4678  C   GLY A 571     4751   3720   4248   -165   -146    -58       C  
ATOM   4679  O   GLY A 571       2.158   6.097 -39.467  1.00 32.92           O  
ANISOU 4679  O   GLY A 571     4642   3548   4319   -166    -59   -112       O  
ATOM   4680  N   ASN A 572       4.299   5.409 -39.274  1.00 34.25           N  
ANISOU 4680  N   ASN A 572     4953   3874   4186   -171   -125    -44       N  
ATOM   4681  CA  ASN A 572       4.342   5.525 -37.809  1.00 34.66           C  
ANISOU 4681  CA  ASN A 572     5119   3870   4180   -179    -15    -84       C  
ATOM   4682  C   ASN A 572       5.284   6.629 -37.342  1.00 33.65           C  
ANISOU 4682  C   ASN A 572     5053   3758   3977   -192    -71    -73       C  
ATOM   4683  O   ASN A 572       6.461   6.633 -37.710  1.00 33.73           O  
ANISOU 4683  O   ASN A 572     5069   3846   3900   -192   -173    -35       O  
ATOM   4684  CB  ASN A 572       4.710   4.191 -37.139  1.00 33.25           C  
ANISOU 4684  CB  ASN A 572     5047   3707   3881   -170     43    -90       C  
ATOM   4685  CG  ASN A 572       4.867   4.325 -35.622  1.00 35.25           C  
ANISOU 4685  CG  ASN A 572     5473   3887   4032   -177    137   -125       C  
ATOM   4686  OD1 ASN A 572       5.765   5.009 -35.142  1.00 32.78           O  
ANISOU 4686  OD1 ASN A 572     5238   3590   3628   -181     66   -118       O  
ATOM   4687  ND2 ASN A 572       3.981   3.680 -34.869  1.00 32.04           N  
ANISOU 4687  ND2 ASN A 572     5142   3388   3645   -181    299   -169       N  
ATOM   4688  N   VAL A 573       4.765   7.540 -36.511  1.00 34.54           N  
ANISOU 4688  N   VAL A 573     5206   3782   4136   -204      5   -115       N  
ATOM   4689  CA  VAL A 573       5.469   8.787 -36.145  1.00 35.24           C  
ANISOU 4689  CA  VAL A 573     5333   3868   4188   -218    -52   -112       C  
ATOM   4690  C   VAL A 573       6.805   8.587 -35.419  1.00 36.36           C  
ANISOU 4690  C   VAL A 573     5600   4050   4166   -217   -118   -106       C  
ATOM   4691  O   VAL A 573       7.649   9.478 -35.441  1.00 36.26           O  
ANISOU 4691  O   VAL A 573     5582   4058   4137   -227   -207    -95       O  
ATOM   4692  CB  VAL A 573       4.579   9.791 -35.330  1.00 35.76           C  
ANISOU 4692  CB  VAL A 573     5427   3818   4342   -232     57   -168       C  
ATOM   4693  CG1 VAL A 573       3.375  10.255 -36.156  1.00 34.97           C  
ANISOU 4693  CG1 VAL A 573     5170   3666   4451   -228     75   -178       C  
ATOM   4694  CG2 VAL A 573       4.146   9.210 -33.954  1.00 31.31           C  
ANISOU 4694  CG2 VAL A 573     5027   3162   3706   -236    220   -225       C  
ATOM   4695  N   TRP A 574       6.986   7.423 -34.795  1.00 34.35           N  
ANISOU 4695  N   TRP A 574     5453   3793   3806   -203    -83   -116       N  
ATOM   4696  CA  TRP A 574       8.223   7.111 -34.072  1.00 38.17           C  
ANISOU 4696  CA  TRP A 574     6064   4295   4147   -193   -175   -115       C  
ATOM   4697  C   TRP A 574       9.393   6.656 -34.961  1.00 34.90           C  
ANISOU 4697  C   TRP A 574     5554   3982   3724   -183   -311    -72       C  
ATOM   4698  O   TRP A 574      10.543   6.695 -34.537  1.00 34.72           O  
ANISOU 4698  O   TRP A 574     5582   3968   3641   -176   -421    -77       O  
ATOM   4699  CB  TRP A 574       7.948   6.129 -32.916  1.00 39.02           C  
ANISOU 4699  CB  TRP A 574     6366   4330   4130   -180    -87   -145       C  
ATOM   4700  CG  TRP A 574       7.002   6.735 -31.934  1.00 46.66           C  
ANISOU 4700  CG  TRP A 574     7456   5177   5098   -197     64   -196       C  
ATOM   4701  CD1 TRP A 574       5.656   6.506 -31.842  1.00 49.17           C  
ANISOU 4701  CD1 TRP A 574     7758   5418   5505   -209    253   -227       C  
ATOM   4702  CD2 TRP A 574       7.310   7.729 -30.944  1.00 49.81           C  
ANISOU 4702  CD2 TRP A 574     7999   5501   5424   -208     50   -232       C  
ATOM   4703  NE1 TRP A 574       5.112   7.282 -30.846  1.00 49.85           N  
ANISOU 4703  NE1 TRP A 574     7973   5385   5581   -229    378   -280       N  
ATOM   4704  CE2 TRP A 574       6.103   8.040 -30.276  1.00 50.65           C  
ANISOU 4704  CE2 TRP A 574     8187   5488   5568   -228    254   -282       C  
ATOM   4705  CE3 TRP A 574       8.490   8.379 -30.550  1.00 53.75           C  
ANISOU 4705  CE3 TRP A 574     8564   6012   5845   -203   -115   -235       C  
ATOM   4706  CZ2 TRP A 574       6.039   8.977 -29.231  1.00 53.14           C  
ANISOU 4706  CZ2 TRP A 574     8669   5700   5822   -245    307   -330       C  
ATOM   4707  CZ3 TRP A 574       8.427   9.314 -29.503  1.00 56.19           C  
ANISOU 4707  CZ3 TRP A 574     9036   6220   6091   -217    -86   -283       C  
ATOM   4708  CH2 TRP A 574       7.208   9.600 -28.859  1.00 54.35           C  
ANISOU 4708  CH2 TRP A 574     8902   5874   5874   -238    128   -328       C  
ATOM   4709  N   PHE A 575       9.095   6.250 -36.194  1.00 35.64           N  
ANISOU 4709  N   PHE A 575     5512   4138   3892   -184   -305    -37       N  
ATOM   4710  CA  PHE A 575      10.122   5.921 -37.191  1.00 33.69           C  
ANISOU 4710  CA  PHE A 575     5172   3975   3653   -183   -398      1       C  
ATOM   4711  C   PHE A 575      10.904   7.164 -37.619  1.00 35.76           C  
ANISOU 4711  C   PHE A 575     5367   4250   3969   -206   -469     13       C  
ATOM   4712  O   PHE A 575      10.311   8.192 -37.960  1.00 37.66           O  
ANISOU 4712  O   PHE A 575     5567   4467   4276   -223   -445     19       O  
ATOM   4713  CB  PHE A 575       9.466   5.282 -38.411  1.00 32.86           C  
ANISOU 4713  CB  PHE A 575     4972   3914   3601   -182   -363     32       C  
ATOM   4714  CG  PHE A 575      10.418   4.558 -39.325  1.00 28.28           C  
ANISOU 4714  CG  PHE A 575     4335   3406   3004   -180   -418     63       C  
ATOM   4715  CD1 PHE A 575      11.465   3.792 -38.818  1.00 30.45           C  
ANISOU 4715  CD1 PHE A 575     4648   3699   3222   -165   -466     53       C  
ATOM   4716  CD2 PHE A 575      10.226   4.598 -40.699  1.00 29.61           C  
ANISOU 4716  CD2 PHE A 575     4424   3609   3216   -191   -422     98       C  
ATOM   4717  CE1 PHE A 575      12.327   3.104 -39.672  1.00 27.61           C  
ANISOU 4717  CE1 PHE A 575     4222   3394   2874   -164   -497     73       C  
ATOM   4718  CE2 PHE A 575      11.070   3.908 -41.560  1.00 27.26           C  
ANISOU 4718  CE2 PHE A 575     4091   3366   2900   -194   -443    121       C  
ATOM   4719  CZ  PHE A 575      12.123   3.164 -41.046  1.00 29.02           C  
ANISOU 4719  CZ  PHE A 575     4326   3609   3090   -182   -470    106       C  
ATOM   4720  N   ARG A 576      12.233   7.055 -37.595  1.00 33.49           N  
ANISOU 4720  N   ARG A 576     5033   4099   3591   -531   -128   -103       N  
ATOM   4721  CA  ARG A 576      13.141   8.133 -37.991  1.00 32.54           C  
ANISOU 4721  CA  ARG A 576     4897   3953   3514   -532   -113   -114       C  
ATOM   4722  C   ARG A 576      12.825   8.648 -39.399  1.00 35.38           C  
ANISOU 4722  C   ARG A 576     5223   4286   3932   -465    -69   -100       C  
ATOM   4723  O   ARG A 576      12.960   9.852 -39.685  1.00 33.15           O  
ANISOU 4723  O   ARG A 576     4937   3973   3686   -462    -25   -119       O  
ATOM   4724  CB  ARG A 576      14.590   7.626 -37.936  1.00 31.85           C  
ANISOU 4724  CB  ARG A 576     4787   3878   3435   -552   -183    -85       C  
ATOM   4725  CG  ARG A 576      15.666   8.701 -38.091  1.00 31.80           C  
ANISOU 4725  CG  ARG A 576     4767   3848   3465   -568   -177    -98       C  
ATOM   4726  CD  ARG A 576      17.070   8.101 -38.131  1.00 26.31           C  
ANISOU 4726  CD  ARG A 576     4041   3164   2793   -581   -247    -64       C  
ATOM   4727  NE  ARG A 576      17.413   7.396 -36.897  1.00 27.83           N  
ANISOU 4727  NE  ARG A 576     4253   3388   2935   -643   -312    -52       N  
ATOM   4728  CZ  ARG A 576      17.934   7.967 -35.818  1.00 33.55           C  
ANISOU 4728  CZ  ARG A 576     5002   4121   3623   -717   -334    -74       C  
ATOM   4729  NH1 ARG A 576      18.200   9.275 -35.812  1.00 32.90           N  
ANISOU 4729  NH1 ARG A 576     4930   4014   3555   -736   -292   -114       N  
ATOM   4730  NH2 ARG A 576      18.195   7.226 -34.741  1.00 31.49           N  
ANISOU 4730  NH2 ARG A 576     4759   3894   3311   -776   -401    -54       N  
ATOM   4731  N   TYR A 577      12.392   7.731 -40.268  1.00 33.26           N  
ANISOU 4731  N   TYR A 577     4932   4031   3672   -417    -80    -66       N  
ATOM   4732  CA  TYR A 577      12.096   8.071 -41.654  1.00 33.19           C  
ANISOU 4732  CA  TYR A 577     4894   4008   3709   -361    -47    -46       C  
ATOM   4733  C   TYR A 577      10.595   8.177 -41.947  1.00 32.93           C  
ANISOU 4733  C   TYR A 577     4866   3971   3677   -332     -4    -45       C  
ATOM   4734  O   TYR A 577      10.174   8.087 -43.108  1.00 32.23           O  
ANISOU 4734  O   TYR A 577     4752   3882   3611   -288      9    -17       O  
ATOM   4735  CB  TYR A 577      12.822   7.112 -42.606  1.00 33.26           C  
ANISOU 4735  CB  TYR A 577     4871   4032   3735   -333    -85    -11       C  
ATOM   4736  CG  TYR A 577      14.295   6.986 -42.274  1.00 33.55           C  
ANISOU 4736  CG  TYR A 577     4897   4067   3785   -361   -128     -8       C  
ATOM   4737  CD1 TYR A 577      14.778   5.881 -41.573  1.00 32.59           C  
ANISOU 4737  CD1 TYR A 577     4775   3966   3642   -386   -184      5       C  
ATOM   4738  CD2 TYR A 577      15.195   7.979 -42.640  1.00 32.67           C  
ANISOU 4738  CD2 TYR A 577     4770   3932   3711   -364   -114    -13       C  
ATOM   4739  CE1 TYR A 577      16.124   5.768 -41.245  1.00 31.02           C  
ANISOU 4739  CE1 TYR A 577     4558   3764   3465   -413   -228     15       C  
ATOM   4740  CE2 TYR A 577      16.545   7.873 -42.324  1.00 35.80           C  
ANISOU 4740  CE2 TYR A 577     5151   4326   4126   -391   -154     -9       C  
ATOM   4741  CZ  TYR A 577      17.001   6.763 -41.625  1.00 35.76           C  
ANISOU 4741  CZ  TYR A 577     5142   4341   4103   -415   -213      7       C  
ATOM   4742  OH  TYR A 577      18.338   6.657 -41.313  1.00 34.68           O  
ANISOU 4742  OH  TYR A 577     4983   4201   3994   -443   -258     19       O  
ATOM   4743  N   TYR A 578       9.803   8.372 -40.888  1.00 32.36           N  
ANISOU 4743  N   TYR A 578     4824   3896   3577   -361     20    -76       N  
ATOM   4744  CA  TYR A 578       8.382   8.723 -41.011  1.00 31.84           C  
ANISOU 4744  CA  TYR A 578     4758   3815   3525   -339     72    -81       C  
ATOM   4745  C   TYR A 578       8.167   9.773 -42.077  1.00 31.06           C  
ANISOU 4745  C   TYR A 578     4630   3685   3488   -300    113    -64       C  
ATOM   4746  O   TYR A 578       8.808  10.814 -42.070  1.00 33.75           O  
ANISOU 4746  O   TYR A 578     4967   3996   3860   -311    135    -78       O  
ATOM   4747  CB  TYR A 578       7.831   9.277 -39.695  1.00 32.01           C  
ANISOU 4747  CB  TYR A 578     4816   3821   3525   -386    111   -130       C  
ATOM   4748  CG  TYR A 578       6.385   9.745 -39.769  1.00 31.87           C  
ANISOU 4748  CG  TYR A 578     4793   3778   3539   -364    174   -139       C  
ATOM   4749  CD1 TYR A 578       6.074  11.103 -39.832  1.00 30.37           C  
ANISOU 4749  CD1 TYR A 578     4593   3539   3407   -360    240   -159       C  
ATOM   4750  CD2 TYR A 578       5.328   8.826 -39.776  1.00 32.57           C  
ANISOU 4750  CD2 TYR A 578     4881   3887   3608   -346    170   -125       C  
ATOM   4751  CE1 TYR A 578       4.751  11.541 -39.898  1.00 32.66           C  
ANISOU 4751  CE1 TYR A 578     4869   3799   3741   -338    299   -162       C  
ATOM   4752  CE2 TYR A 578       3.997   9.249 -39.841  1.00 32.25           C  
ANISOU 4752  CE2 TYR A 578     4828   3820   3604   -326    227   -129       C  
ATOM   4753  CZ  TYR A 578       3.719  10.610 -39.900  1.00 33.40           C  
ANISOU 4753  CZ  TYR A 578     4961   3915   3814   -321    291   -146       C  
ATOM   4754  OH  TYR A 578       2.418  11.045 -39.955  1.00 34.10           O  
ANISOU 4754  OH  TYR A 578     5029   3972   3954   -300    349   -147       O  
ATOM   4755  N   ASP A 579       7.261   9.482 -42.994  1.00 32.40           N  
ANISOU 4755  N   ASP A 579     4775   3860   3674   -257    121    -30       N  
ATOM   4756  CA  ASP A 579       6.898  10.413 -44.045  1.00 33.43           C  
ANISOU 4756  CA  ASP A 579     4874   3964   3863   -221    155     -1       C  
ATOM   4757  C   ASP A 579       5.637   9.891 -44.701  1.00 33.41           C  
ANISOU 4757  C   ASP A 579     4853   3976   3864   -188    157     34       C  
ATOM   4758  O   ASP A 579       5.667   8.868 -45.403  1.00 32.74           O  
ANISOU 4758  O   ASP A 579     4759   3928   3751   -173    118     61       O  
ATOM   4759  CB  ASP A 579       8.020  10.567 -45.083  1.00 32.56           C  
ANISOU 4759  CB  ASP A 579     4745   3859   3767   -207    132     27       C  
ATOM   4760  CG  ASP A 579       7.815  11.780 -45.991  1.00 35.88           C  
ANISOU 4760  CG  ASP A 579     5137   4246   4249   -182    170     56       C  
ATOM   4761  OD1 ASP A 579       8.815  12.333 -46.493  1.00 35.86           O  
ANISOU 4761  OD1 ASP A 579     5126   4233   4267   -182    168     63       O  
ATOM   4762  OD2 ASP A 579       6.655  12.196 -46.189  1.00 38.70           O  
ANISOU 4762  OD2 ASP A 579     5480   4586   4639   -161    201     74       O  
ATOM   4763  N   LEU A 580       4.535  10.590 -44.443  1.00 31.48           N  
ANISOU 4763  N   LEU A 580     4599   3700   3660   -180    206     30       N  
ATOM   4764  CA  LEU A 580       3.230  10.242 -44.991  1.00 33.46           C  
ANISOU 4764  CA  LEU A 580     4826   3960   3927   -150    211     65       C  
ATOM   4765  C   LEU A 580       3.147  10.331 -46.518  1.00 34.30           C  
ANISOU 4765  C   LEU A 580     4896   4079   4056   -116    191    128       C  
ATOM   4766  O   LEU A 580       2.307   9.662 -47.129  1.00 32.64           O  
ANISOU 4766  O   LEU A 580     4669   3896   3836    -98    172    162       O  
ATOM   4767  CB  LEU A 580       2.137  11.094 -44.350  1.00 35.26           C  
ANISOU 4767  CB  LEU A 580     5045   4141   4210   -150    274     47       C  
ATOM   4768  CG  LEU A 580       1.016  10.406 -43.566  1.00 37.74           C  
ANISOU 4768  CG  LEU A 580     5371   4463   4505   -158    288     26       C  
ATOM   4769  CD1 LEU A 580       1.440   9.136 -42.798  1.00 32.92           C  
ANISOU 4769  CD1 LEU A 580     4802   3898   3809   -189    246     -3       C  
ATOM   4770  CD2 LEU A 580       0.397  11.417 -42.630  1.00 40.96           C  
ANISOU 4770  CD2 LEU A 580     5782   4815   4966   -175    364    -15       C  
ATOM   4771  N   ARG A 581       4.010  11.149 -47.121  1.00 33.29           N  
ANISOU 4771  N   ARG A 581     4758   3935   3956   -112    195    143       N  
ATOM   4772  CA  ARG A 581       4.138  11.208 -48.585  1.00 33.88           C  
ANISOU 4772  CA  ARG A 581     4806   4028   4039    -90    173    202       C  
ATOM   4773  C   ARG A 581       4.628   9.861 -49.127  1.00 32.68           C  
ANISOU 4773  C   ARG A 581     4665   3931   3820    -96    124    207       C  
ATOM   4774  O   ARG A 581       4.136   9.378 -50.148  1.00 31.97           O  
ANISOU 4774  O   ARG A 581     4559   3872   3715    -84    103    248       O  
ATOM   4775  CB  ARG A 581       5.108  12.308 -49.021  1.00 32.36           C  
ANISOU 4775  CB  ARG A 581     4605   3807   3884    -91    190    211       C  
ATOM   4776  CG  ARG A 581       4.706  13.734 -48.655  1.00 36.26           C  
ANISOU 4776  CG  ARG A 581     5081   4239   4457    -85    244    210       C  
ATOM   4777  CD  ARG A 581       5.834  14.730 -48.960  1.00 36.97           C  
ANISOU 4777  CD  ARG A 581     5167   4300   4578    -90    259    211       C  
ATOM   4778  NE  ARG A 581       7.026  14.491 -48.136  1.00 38.18           N  
ANISOU 4778  NE  ARG A 581     5354   4458   4694   -121    249    152       N  
ATOM   4779  CZ  ARG A 581       8.200  15.104 -48.299  1.00 38.25           C  
ANISOU 4779  CZ  ARG A 581     5365   4452   4717   -132    252    144       C  
ATOM   4780  NH1 ARG A 581       8.370  16.003 -49.258  1.00 39.67           N  
ANISOU 4780  NH1 ARG A 581     5518   4609   4945   -115    269    187       N  
ATOM   4781  NH2 ARG A 581       9.213  14.816 -47.500  1.00 35.99           N  
ANISOU 4781  NH2 ARG A 581     5105   4172   4398   -163    237     95       N  
ATOM   4782  N   ASN A 582       5.600   9.260 -48.446  1.00 32.40           N  
ANISOU 4782  N   ASN A 582     4656   3905   3749   -117    106    165       N  
ATOM   4783  CA  ASN A 582       6.105   7.955 -48.861  1.00 33.34           C  
ANISOU 4783  CA  ASN A 582     4783   4067   3819   -122     66    165       C  
ATOM   4784  C   ASN A 582       5.137   6.806 -48.528  1.00 30.31           C  
ANISOU 4784  C   ASN A 582     4406   3710   3400   -121     49    161       C  
ATOM   4785  O   ASN A 582       4.946   5.916 -49.352  1.00 32.00           O  
ANISOU 4785  O   ASN A 582     4613   3957   3588   -115     27    181       O  
ATOM   4786  CB  ASN A 582       7.511   7.681 -48.300  1.00 34.59           C  
ANISOU 4786  CB  ASN A 582     4958   4222   3964   -143     48    132       C  
ATOM   4787  CG  ASN A 582       8.596   8.545 -48.952  1.00 38.36           C  
ANISOU 4787  CG  ASN A 582     5424   4682   4471   -143     58    141       C  
ATOM   4788  OD1 ASN A 582       8.407   9.116 -50.032  1.00 36.35           O  
ANISOU 4788  OD1 ASN A 582     5151   4426   4235   -128     72    177       O  
ATOM   4789  ND2 ASN A 582       9.742   8.640 -48.284  1.00 33.91           N  
ANISOU 4789  ND2 ASN A 582     4870   4105   3910   -164     49    112       N  
ATOM   4790  N   ALA A 583       4.512   6.838 -47.352  1.00 28.65           N  
ANISOU 4790  N   ALA A 583     4210   3485   3190   -130     64    134       N  
ATOM   4791  CA  ALA A 583       3.588   5.751 -46.953  1.00 31.15           C  
ANISOU 4791  CA  ALA A 583     4535   3825   3475   -131     51    129       C  
ATOM   4792  C   ALA A 583       2.366   5.699 -47.861  1.00 31.75           C  
ANISOU 4792  C   ALA A 583     4585   3915   3564   -108     55    169       C  
ATOM   4793  O   ALA A 583       1.913   4.616 -48.241  1.00 31.25           O  
ANISOU 4793  O   ALA A 583     4520   3885   3469   -106     31    180       O  
ATOM   4794  CB  ALA A 583       3.165   5.872 -45.489  1.00 26.32           C  
ANISOU 4794  CB  ALA A 583     3947   3195   2858   -151     72     89       C  
ATOM   4795  N   THR A 584       1.858   6.883 -48.208  1.00 31.60           N  
ANISOU 4795  N   THR A 584     4543   3867   3597    -93     84    194       N  
ATOM   4796  CA  THR A 584       0.705   7.023 -49.083  1.00 33.84           C  
ANISOU 4796  CA  THR A 584     4794   4159   3905    -74     85    244       C  
ATOM   4797  C   THR A 584       1.072   6.732 -50.555  1.00 35.18           C  
ANISOU 4797  C   THR A 584     4950   4365   4051    -71     53    288       C  
ATOM   4798  O   THR A 584       0.267   6.165 -51.297  1.00 36.97           O  
ANISOU 4798  O   THR A 584     5162   4625   4261    -69     32    322       O  
ATOM   4799  CB  THR A 584       0.036   8.408 -48.884  1.00 36.41           C  
ANISOU 4799  CB  THR A 584     5093   4434   4307    -59    129    261       C  
ATOM   4800  OG1 THR A 584      -0.403   8.527 -47.516  1.00 38.74           O  
ANISOU 4800  OG1 THR A 584     5405   4700   4616    -69    165    213       O  
ATOM   4801  CG2 THR A 584      -1.160   8.577 -49.784  1.00 38.69           C  
ANISOU 4801  CG2 THR A 584     5340   4730   4630    -40    123    324       C  
ATOM   4802  N   ALA A 585       2.287   7.093 -50.970  1.00 33.38           N  
ANISOU 4802  N   ALA A 585     4730   4135   3819    -78     50    285       N  
ATOM   4803  CA  ALA A 585       2.768   6.740 -52.309  1.00 31.86           C  
ANISOU 4803  CA  ALA A 585     4532   3978   3595    -84     27    315       C  
ATOM   4804  C   ALA A 585       2.720   5.226 -52.540  1.00 32.95           C  
ANISOU 4804  C   ALA A 585     4683   4159   3676    -97     -1    299       C  
ATOM   4805  O   ALA A 585       2.409   4.786 -53.638  1.00 33.72           O  
ANISOU 4805  O   ALA A 585     4773   4294   3746   -105    -17    329       O  
ATOM   4806  CB  ALA A 585       4.185   7.258 -52.535  1.00 27.09           C  
ANISOU 4806  CB  ALA A 585     3937   3360   2998    -92     34    302       C  
ATOM   4807  N   ILE A 586       3.042   4.443 -51.508  1.00 30.72           N  
ANISOU 4807  N   ILE A 586     4421   3872   3377   -103     -5    252       N  
ATOM   4808  CA  ILE A 586       2.980   2.983 -51.598  1.00 31.92           C  
ANISOU 4808  CA  ILE A 586     4585   4058   3487   -113    -27    235       C  
ATOM   4809  C   ILE A 586       1.539   2.503 -51.731  1.00 32.96           C  
ANISOU 4809  C   ILE A 586     4706   4211   3607   -109    -34    255       C  
ATOM   4810  O   ILE A 586       1.232   1.714 -52.619  1.00 36.35           O  
ANISOU 4810  O   ILE A 586     5131   4676   4005   -119    -51    269       O  
ATOM   4811  CB  ILE A 586       3.612   2.284 -50.355  1.00 31.65           C  
ANISOU 4811  CB  ILE A 586     4571   4010   3443   -121    -34    190       C  
ATOM   4812  CG1 ILE A 586       5.101   2.619 -50.239  1.00 32.78           C  
ANISOU 4812  CG1 ILE A 586     4720   4135   3599   -129    -33    172       C  
ATOM   4813  CG2 ILE A 586       3.411   0.772 -50.415  1.00 26.76           C  
ANISOU 4813  CG2 ILE A 586     3958   3419   2791   -129    -53    177       C  
ATOM   4814  CD1 ILE A 586       5.634   2.399 -48.852  1.00 32.48           C  
ANISOU 4814  CD1 ILE A 586     4700   4079   3563   -140    -41    140       C  
ATOM   4815  N   THR A 587       0.662   2.963 -50.842  1.00 32.64           N  
ANISOU 4815  N   THR A 587     4661   4148   3594    -98    -19    254       N  
ATOM   4816  CA  THR A 587      -0.706   2.428 -50.798  1.00 33.00           C  
ANISOU 4816  CA  THR A 587     4694   4209   3635    -94    -25    268       C  
ATOM   4817  C   THR A 587      -1.583   2.875 -51.968  1.00 32.43           C  
ANISOU 4817  C   THR A 587     4590   4156   3577    -88    -34    326       C  
ATOM   4818  O   THR A 587      -2.388   2.082 -52.473  1.00 31.15           O  
ANISOU 4818  O   THR A 587     4419   4027   3390    -96    -54    343       O  
ATOM   4819  CB  THR A 587      -1.421   2.714 -49.469  1.00 32.90           C  
ANISOU 4819  CB  THR A 587     4686   4165   3650    -87      0    246       C  
ATOM   4820  OG1 THR A 587      -1.577   4.127 -49.293  1.00 28.89           O  
ANISOU 4820  OG1 THR A 587     4162   3618   3199    -75     32    259       O  
ATOM   4821  CG2 THR A 587      -0.639   2.092 -48.292  1.00 31.91           C  
ANISOU 4821  CG2 THR A 587     4595   4032   3497   -102     -1    194       C  
ATOM   4822  N   THR A 588      -1.412   4.123 -52.406  1.00 30.03           N  
ANISOU 4822  N   THR A 588     4268   3830   3313    -79    -22    360       N  
ATOM   4823  CA  THR A 588      -2.165   4.632 -53.554  1.00 28.87           C  
ANISOU 4823  CA  THR A 588     4087   3700   3181    -78    -37    427       C  
ATOM   4824  C   THR A 588      -1.758   3.890 -54.829  1.00 29.83           C  
ANISOU 4824  C   THR A 588     4218   3876   3241   -104    -68    443       C  
ATOM   4825  O   THR A 588      -2.620   3.452 -55.593  1.00 31.05           O  
ANISOU 4825  O   THR A 588     4357   4068   3373   -117    -93    480       O  
ATOM   4826  CB  THR A 588      -2.005   6.151 -53.708  1.00 28.49           C  
ANISOU 4826  CB  THR A 588     4017   3612   3197    -63    -15    462       C  
ATOM   4827  OG1 THR A 588      -2.259   6.774 -52.442  1.00 31.82           O  
ANISOU 4827  OG1 THR A 588     4436   3980   3673    -46     24    431       O  
ATOM   4828  CG2 THR A 588      -2.988   6.703 -54.726  1.00 28.99           C  
ANISOU 4828  CG2 THR A 588     4037   3687   3289    -61    -35    543       C  
ATOM   4829  N   PHE A 589      -0.450   3.735 -55.038  1.00 29.56           N  
ANISOU 4829  N   PHE A 589     4208   3844   3179   -116    -63    413       N  
ATOM   4830  CA  PHE A 589       0.079   2.932 -56.141  1.00 29.25           C  
ANISOU 4830  CA  PHE A 589     4184   3851   3081   -145    -79    411       C  
ATOM   4831  C   PHE A 589      -0.540   1.534 -56.114  1.00 29.14           C  
ANISOU 4831  C   PHE A 589     4177   3869   3025   -159    -95    388       C  
ATOM   4832  O   PHE A 589      -0.876   0.981 -57.156  1.00 31.19           O  
ANISOU 4832  O   PHE A 589     4437   4174   3241   -188   -113    407       O  
ATOM   4833  CB  PHE A 589       1.617   2.839 -56.065  1.00 27.99           C  
ANISOU 4833  CB  PHE A 589     4047   3677   2912   -152    -63    368       C  
ATOM   4834  CG  PHE A 589       2.264   2.272 -57.320  1.00 27.81           C  
ANISOU 4834  CG  PHE A 589     4035   3692   2839   -185    -66    367       C  
ATOM   4835  CD1 PHE A 589       2.324   0.893 -57.535  1.00 25.71           C  
ANISOU 4835  CD1 PHE A 589     3784   3453   2531   -206    -69    331       C  
ATOM   4836  CD2 PHE A 589       2.818   3.120 -58.277  1.00 28.78           C  
ANISOU 4836  CD2 PHE A 589     4156   3821   2959   -198    -59    399       C  
ATOM   4837  CE1 PHE A 589       2.911   0.366 -58.695  1.00 28.47           C  
ANISOU 4837  CE1 PHE A 589     4146   3835   2836   -243    -62    321       C  
ATOM   4838  CE2 PHE A 589       3.409   2.607 -59.444  1.00 30.06           C  
ANISOU 4838  CE2 PHE A 589     4332   4019   3070   -237    -55    394       C  
ATOM   4839  CZ  PHE A 589       3.451   1.229 -59.652  1.00 29.18           C  
ANISOU 4839  CZ  PHE A 589     4236   3934   2917   -260    -53    352       C  
ATOM   4840  N   GLY A 590      -0.701   0.976 -54.916  1.00 28.24           N  
ANISOU 4840  N   GLY A 590     4072   3734   2923   -144    -88    348       N  
ATOM   4841  CA  GLY A 590      -1.295  -0.348 -54.753  1.00 29.63           C  
ANISOU 4841  CA  GLY A 590     4255   3935   3068   -155   -100    325       C  
ATOM   4842  C   GLY A 590      -2.728  -0.387 -55.247  1.00 31.93           C  
ANISOU 4842  C   GLY A 590     4523   4254   3356   -160   -119    368       C  
ATOM   4843  O   GLY A 590      -3.144  -1.350 -55.910  1.00 31.69           O  
ANISOU 4843  O   GLY A 590     4495   4263   3283   -185   -136    368       O  
ATOM   4844  N   GLN A 591      -3.474   0.678 -54.947  1.00 31.65           N  
ANISOU 4844  N   GLN A 591     4461   4194   3370   -139   -115    407       N  
ATOM   4845  CA  GLN A 591      -4.874   0.779 -55.344  1.00 33.50           C  
ANISOU 4845  CA  GLN A 591     4663   4447   3620   -140   -134    458       C  
ATOM   4846  C   GLN A 591      -4.999   0.882 -56.851  1.00 35.22           C  
ANISOU 4846  C   GLN A 591     4869   4713   3802   -170   -165    511       C  
ATOM   4847  O   GLN A 591      -5.936   0.341 -57.442  1.00 34.12           O  
ANISOU 4847  O   GLN A 591     4714   4613   3639   -191   -193    540       O  
ATOM   4848  CB  GLN A 591      -5.539   1.995 -54.694  1.00 35.89           C  
ANISOU 4848  CB  GLN A 591     4933   4702   4000   -109   -115    489       C  
ATOM   4849  CG  GLN A 591      -5.809   1.847 -53.197  1.00 38.33           C  
ANISOU 4849  CG  GLN A 591     5252   4971   4341    -88    -83    440       C  
ATOM   4850  CD  GLN A 591      -6.841   2.842 -52.680  1.00 45.35           C  
ANISOU 4850  CD  GLN A 591     6102   5817   5310    -64    -59    470       C  
ATOM   4851  OE1 GLN A 591      -7.172   3.826 -53.349  1.00 47.94           O  
ANISOU 4851  OE1 GLN A 591     6395   6136   5686    -56    -64    530       O  
ATOM   4852  NE2 GLN A 591      -7.352   2.589 -51.478  1.00 46.88           N  
ANISOU 4852  NE2 GLN A 591     6303   5984   5526    -55    -30    431       N  
ATOM   4853  N   MET A 592      -4.048   1.591 -57.457  1.00 35.45           N  
ANISOU 4853  N   MET A 592     4905   4739   3824   -177   -160    525       N  
ATOM   4854  CA  MET A 592      -4.000   1.752 -58.896  1.00 35.65           C  
ANISOU 4854  CA  MET A 592     4927   4811   3807   -214   -186    574       C  
ATOM   4855  C   MET A 592      -3.642   0.429 -59.544  1.00 35.08           C  
ANISOU 4855  C   MET A 592     4885   4787   3655   -256   -192    533       C  
ATOM   4856  O   MET A 592      -4.299   0.017 -60.487  1.00 36.25           O  
ANISOU 4856  O   MET A 592     5028   4986   3758   -294   -222    565       O  
ATOM   4857  CB  MET A 592      -2.987   2.825 -59.299  1.00 34.33           C  
ANISOU 4857  CB  MET A 592     4764   4625   3654   -211   -171    593       C  
ATOM   4858  CG  MET A 592      -2.821   2.971 -60.807  1.00 33.89           C  
ANISOU 4858  CG  MET A 592     4711   4621   3544   -258   -195    642       C  
ATOM   4859  SD  MET A 592      -1.486   4.081 -61.291  1.00 36.86           S  
ANISOU 4859  SD  MET A 592     5099   4977   3931   -259   -173    655       S  
ATOM   4860  CE  MET A 592      -0.042   3.156 -60.765  1.00 39.47           C  
ANISOU 4860  CE  MET A 592     5472   5292   4233   -260   -134    552       C  
ATOM   4861  N   ALA A 593      -2.609  -0.232 -59.027  1.00 35.34           N  
ANISOU 4861  N   ALA A 593     4949   4803   3677   -252   -165    463       N  
ATOM   4862  CA  ALA A 593      -2.105  -1.467 -59.629  1.00 36.26           C  
ANISOU 4862  CA  ALA A 593     5092   4952   3731   -290   -159    416       C  
ATOM   4863  C   ALA A 593      -3.199  -2.522 -59.712  1.00 36.77           C  
ANISOU 4863  C   ALA A 593     5152   5050   3767   -310   -179    412       C  
ATOM   4864  O   ALA A 593      -3.410  -3.113 -60.771  1.00 38.79           O  
ANISOU 4864  O   ALA A 593     5418   5356   3965   -358   -191    416       O  
ATOM   4865  CB  ALA A 593      -0.889  -1.996 -58.864  1.00 34.45           C  
ANISOU 4865  CB  ALA A 593     4886   4687   3518   -274   -127    348       C  
ATOM   4866  N   LEU A 594      -3.900  -2.730 -58.597  1.00 35.57           N  
ANISOU 4866  N   LEU A 594     4988   4872   3655   -276   -180    402       N  
ATOM   4867  CA  LEU A 594      -4.997  -3.692 -58.511  1.00 36.12           C  
ANISOU 4867  CA  LEU A 594     5051   4966   3708   -289   -197    398       C  
ATOM   4868  C   LEU A 594      -6.125  -3.423 -59.524  1.00 37.70           C  
ANISOU 4868  C   LEU A 594     5225   5214   3885   -319   -235    464       C  
ATOM   4869  O   LEU A 594      -6.495  -4.309 -60.302  1.00 39.52           O  
ANISOU 4869  O   LEU A 594     5464   5492   4061   -364   -251    457       O  
ATOM   4870  CB  LEU A 594      -5.561  -3.722 -57.082  1.00 36.33           C  
ANISOU 4870  CB  LEU A 594     5066   4950   3787   -246   -187    383       C  
ATOM   4871  CG  LEU A 594      -6.744  -4.663 -56.840  1.00 37.30           C  
ANISOU 4871  CG  LEU A 594     5178   5092   3903   -254   -201    379       C  
ATOM   4872  CD1 LEU A 594      -6.298  -6.103 -57.013  1.00 39.78           C  
ANISOU 4872  CD1 LEU A 594     5520   5424   4172   -282   -193    322       C  
ATOM   4873  CD2 LEU A 594      -7.331  -4.450 -55.464  1.00 38.70           C  
ANISOU 4873  CD2 LEU A 594     5343   5225   4134   -214   -187    372       C  
ATOM   4874  N   GLN A 595      -6.657  -2.202 -59.507  1.00 36.86           N  
ANISOU 4874  N   GLN A 595     5086   5093   3826   -297   -250    529       N  
ATOM   4875  CA  GLN A 595      -7.775  -1.818 -60.367  1.00 38.78           C  
ANISOU 4875  CA  GLN A 595     5294   5376   4064   -321   -293    607       C  
ATOM   4876  C   GLN A 595      -7.384  -1.747 -61.847  1.00 38.42           C  
ANISOU 4876  C   GLN A 595     5263   5387   3947   -380   -317    638       C  
ATOM   4877  O   GLN A 595      -8.185  -2.082 -62.718  1.00 39.33           O  
ANISOU 4877  O   GLN A 595     5366   5557   4019   -426   -356    678       O  
ATOM   4878  CB  GLN A 595      -8.412  -0.511 -59.869  1.00 37.58           C  
ANISOU 4878  CB  GLN A 595     5097   5182   4001   -278   -297    669       C  
ATOM   4879  CG  GLN A 595      -9.246  -0.733 -58.603  1.00 41.22           C  
ANISOU 4879  CG  GLN A 595     5539   5602   4522   -238   -279    647       C  
ATOM   4880  CD  GLN A 595      -9.546   0.538 -57.829  1.00 40.77           C  
ANISOU 4880  CD  GLN A 595     5448   5484   4561   -190   -257    678       C  
ATOM   4881  OE1 GLN A 595     -10.668   1.041 -57.860  1.00 41.35           O  
ANISOU 4881  OE1 GLN A 595     5471   5548   4692   -179   -273    738       O  
ATOM   4882  NE2 GLN A 595      -8.545   1.055 -57.119  1.00 39.73           N  
ANISOU 4882  NE2 GLN A 595     5339   5307   4450   -164   -218    637       N  
ATOM   4883  N   TRP A 596      -6.147  -1.326 -62.111  1.00 37.64           N  
ANISOU 4883  N   TRP A 596     5190   5277   3834   -382   -291    618       N  
ATOM   4884  CA  TRP A 596      -5.561  -1.345 -63.453  1.00 34.77           C  
ANISOU 4884  CA  TRP A 596     4850   4964   3396   -442   -300    632       C  
ATOM   4885  C   TRP A 596      -5.540  -2.759 -64.043  1.00 35.61           C  
ANISOU 4885  C   TRP A 596     4988   5119   3422   -499   -296    576       C  
ATOM   4886  O   TRP A 596      -5.847  -2.945 -65.221  1.00 38.94           O  
ANISOU 4886  O   TRP A 596     5418   5603   3774   -565   -322    606       O  
ATOM   4887  CB  TRP A 596      -4.136  -0.776 -63.409  1.00 32.31           C  
ANISOU 4887  CB  TRP A 596     4562   4619   3093   -428   -261    603       C  
ATOM   4888  CG  TRP A 596      -3.369  -0.891 -64.701  1.00 32.01           C  
ANISOU 4888  CG  TRP A 596     4555   4628   2978   -491   -255    600       C  
ATOM   4889  CD1 TRP A 596      -2.797  -2.017 -65.213  1.00 30.45           C  
ANISOU 4889  CD1 TRP A 596     4395   4459   2717   -538   -229    532       C  
ATOM   4890  CD2 TRP A 596      -3.076   0.164 -65.628  1.00 31.99           C  
ANISOU 4890  CD2 TRP A 596     4550   4646   2959   -517   -269    665       C  
ATOM   4891  NE1 TRP A 596      -2.177  -1.737 -66.403  1.00 29.58           N  
ANISOU 4891  NE1 TRP A 596     4308   4387   2545   -595   -222    546       N  
ATOM   4892  CE2 TRP A 596      -2.331  -0.405 -66.683  1.00 32.15           C  
ANISOU 4892  CE2 TRP A 596     4611   4710   2894   -584   -249    630       C  
ATOM   4893  CE3 TRP A 596      -3.374   1.534 -65.672  1.00 34.30           C  
ANISOU 4893  CE3 TRP A 596     4810   4921   3304   -492   -292    750       C  
ATOM   4894  CZ2 TRP A 596      -1.888   0.346 -67.786  1.00 34.26           C  
ANISOU 4894  CZ2 TRP A 596     4889   5010   3117   -630   -255    679       C  
ATOM   4895  CZ3 TRP A 596      -2.928   2.284 -66.765  1.00 33.37           C  
ANISOU 4895  CZ3 TRP A 596     4700   4833   3148   -533   -302    804       C  
ATOM   4896  CH2 TRP A 596      -2.190   1.685 -67.805  1.00 35.17           C  
ANISOU 4896  CH2 TRP A 596     4972   5109   3281   -603   -285    768       C  
ATOM   4897  N   ILE A 597      -5.148  -3.746 -63.241  1.00 33.95           N  
ANISOU 4897  N   ILE A 597     4797   4879   3222   -479   -261    496       N  
ATOM   4898  CA  ILE A 597      -5.024  -5.108 -63.746  1.00 34.94           C  
ANISOU 4898  CA  ILE A 597     4952   5040   3286   -530   -247    435       C  
ATOM   4899  C   ILE A 597      -6.380  -5.792 -63.831  1.00 37.34           C  
ANISOU 4899  C   ILE A 597     5238   5379   3570   -553   -282    453       C  
ATOM   4900  O   ILE A 597      -6.571  -6.668 -64.663  1.00 38.89           O  
ANISOU 4900  O   ILE A 597     5454   5625   3699   -616   -285    429       O  
ATOM   4901  CB  ILE A 597      -3.936  -5.960 -63.006  1.00 35.36           C  
ANISOU 4901  CB  ILE A 597     5029   5045   3359   -507   -194    346       C  
ATOM   4902  CG1 ILE A 597      -3.281  -6.945 -63.980  1.00 31.89           C  
ANISOU 4902  CG1 ILE A 597     4623   4637   2856   -572   -163    288       C  
ATOM   4903  CG2 ILE A 597      -4.474  -6.665 -61.732  1.00 29.98           C  
ANISOU 4903  CG2 ILE A 597     4337   4329   2727   -463   -192    316       C  
ATOM   4904  CD1 ILE A 597      -2.521  -6.269 -65.099  1.00 30.63           C  
ANISOU 4904  CD1 ILE A 597     4482   4505   2651   -615   -152    306       C  
ATOM   4905  N   GLU A 598      -7.323  -5.354 -62.997  1.00 38.95           N  
ANISOU 4905  N   GLU A 598     5406   5559   3836   -505   -305    494       N  
ATOM   4906  CA  GLU A 598      -8.711  -5.771 -63.117  1.00 38.72           C  
ANISOU 4906  CA  GLU A 598     5350   5563   3800   -524   -345    528       C  
ATOM   4907  C   GLU A 598      -9.216  -5.399 -64.499  1.00 39.96           C  
ANISOU 4907  C   GLU A 598     5498   5788   3896   -589   -393    597       C  
ATOM   4908  O   GLU A 598      -9.807  -6.232 -65.190  1.00 40.42           O  
ANISOU 4908  O   GLU A 598     5562   5900   3893   -649   -415    592       O  
ATOM   4909  CB  GLU A 598      -9.581  -5.099 -62.052  1.00 38.85           C  
ANISOU 4909  CB  GLU A 598     5323   5535   3904   -460   -357    569       C  
ATOM   4910  CG  GLU A 598     -11.060  -5.471 -62.145  1.00 39.74           C  
ANISOU 4910  CG  GLU A 598     5399   5677   4023   -476   -397    610       C  
ATOM   4911  CD  GLU A 598     -11.944  -4.701 -61.172  1.00 43.85           C  
ANISOU 4911  CD  GLU A 598     5871   6151   4639   -417   -402    654       C  
ATOM   4912  OE1 GLU A 598     -11.506  -3.656 -60.635  1.00 43.33           O  
ANISOU 4912  OE1 GLU A 598     5796   6036   4631   -371   -381    670       O  
ATOM   4913  OE2 GLU A 598     -13.089  -5.150 -60.950  1.00 43.55           O  
ANISOU 4913  OE2 GLU A 598     5805   6123   4621   -419   -422    670       O  
ATOM   4914  N   ARG A 599      -8.967  -4.149 -64.894  1.00 38.11           N  
ANISOU 4914  N   ARG A 599     5249   5552   3679   -582   -409    664       N  
ATOM   4915  CA  ARG A 599      -9.399  -3.642 -66.194  1.00 39.87           C  
ANISOU 4915  CA  ARG A 599     5462   5840   3848   -645   -460    745       C  
ATOM   4916  C   ARG A 599      -8.798  -4.462 -67.332  1.00 39.97           C  
ANISOU 4916  C   ARG A 599     5525   5913   3748   -732   -449    699       C  
ATOM   4917  O   ARG A 599      -9.509  -4.879 -68.237  1.00 43.05           O  
ANISOU 4917  O   ARG A 599     5916   6372   4070   -804   -490    729       O  
ATOM   4918  CB  ARG A 599      -9.059  -2.153 -66.348  1.00 36.80           C  
ANISOU 4918  CB  ARG A 599     5051   5427   3503   -618   -471    820       C  
ATOM   4919  CG  ARG A 599      -9.553  -1.564 -67.658  1.00 39.23           C  
ANISOU 4919  CG  ARG A 599     5344   5802   3761   -684   -531    919       C  
ATOM   4920  CD  ARG A 599      -9.314  -0.056 -67.764  1.00 41.07           C  
ANISOU 4920  CD  ARG A 599     5546   6004   4052   -652   -543   1003       C  
ATOM   4921  NE  ARG A 599      -7.903   0.330 -67.637  1.00 41.19           N  
ANISOU 4921  NE  ARG A 599     5599   5985   4066   -632   -489    953       N  
ATOM   4922  CZ  ARG A 599      -7.003   0.268 -68.617  1.00 43.87           C  
ANISOU 4922  CZ  ARG A 599     5983   6365   4321   -692   -476    938       C  
ATOM   4923  NH1 ARG A 599      -7.336  -0.191 -69.821  1.00 41.99           N  
ANISOU 4923  NH1 ARG A 599     5763   6208   3982   -783   -513    965       N  
ATOM   4924  NH2 ARG A 599      -5.759   0.665 -68.390  1.00 42.60           N  
ANISOU 4924  NH2 ARG A 599     5847   6162   4175   -666   -425    894       N  
ATOM   4925  N   LYS A 600      -7.490  -4.699 -67.258  1.00 41.16           N  
ANISOU 4925  N   LYS A 600     5717   6038   3884   -727   -391    625       N  
ATOM   4926  CA  LYS A 600      -6.759  -5.458 -68.272  1.00 41.00           C  
ANISOU 4926  CA  LYS A 600     5746   6062   3768   -807   -362    567       C  
ATOM   4927  C   LYS A 600      -7.203  -6.915 -68.362  1.00 41.17           C  
ANISOU 4927  C   LYS A 600     5786   6111   3746   -850   -350    500       C  
ATOM   4928  O   LYS A 600      -7.405  -7.439 -69.456  1.00 43.03           O  
ANISOU 4928  O   LYS A 600     6046   6412   3889   -940   -361    493       O  
ATOM   4929  CB  LYS A 600      -5.248  -5.376 -68.016  1.00 40.84           C  
ANISOU 4929  CB  LYS A 600     5757   5994   3767   -781   -296    501       C  
ATOM   4930  CG  LYS A 600      -4.645  -3.980 -68.211  1.00 39.35           C  
ANISOU 4930  CG  LYS A 600     5560   5790   3602   -759   -301    561       C  
ATOM   4931  CD  LYS A 600      -4.486  -3.642 -69.677  1.00 42.02           C  
ANISOU 4931  CD  LYS A 600     5922   6196   3847   -847   -317    602       C  
ATOM   4932  CE  LYS A 600      -3.771  -2.319 -69.875  1.00 43.15           C  
ANISOU 4932  CE  LYS A 600     6060   6319   4016   -826   -315    655       C  
ATOM   4933  NZ  LYS A 600      -3.242  -2.217 -71.277  1.00 45.94           N  
ANISOU 4933  NZ  LYS A 600     6452   6734   4269   -919   -308    666       N  
ATOM   4934  N   VAL A 601      -7.364  -7.566 -67.215  1.00 41.50           N  
ANISOU 4934  N   VAL A 601     5817   6102   3850   -791   -328    450       N  
ATOM   4935  CA  VAL A 601      -7.798  -8.954 -67.194  1.00 42.41           C  
ANISOU 4935  CA  VAL A 601     5945   6232   3936   -825   -315    387       C  
ATOM   4936  C   VAL A 601      -9.199  -9.065 -67.791  1.00 43.92           C  
ANISOU 4936  C   VAL A 601     6113   6488   4085   -877   -379    447       C  
ATOM   4937  O   VAL A 601      -9.464  -9.962 -68.595  1.00 44.61           O  
ANISOU 4937  O   VAL A 601     6225   6630   4097   -957   -379    414       O  
ATOM   4938  CB  VAL A 601      -7.693  -9.585 -65.779  1.00 41.53           C  
ANISOU 4938  CB  VAL A 601     5823   6051   3905   -750   -282    331       C  
ATOM   4939  CG1 VAL A 601      -8.330 -10.972 -65.751  1.00 41.67           C  
ANISOU 4939  CG1 VAL A 601     5848   6086   3900   -784   -274    278       C  
ATOM   4940  CG2 VAL A 601      -6.234  -9.689 -65.370  1.00 39.47           C  
ANISOU 4940  CG2 VAL A 601     5587   5735   3673   -719   -220    266       C  
ATOM   4941  N   ASN A 602     -10.074  -8.127 -67.435  1.00 45.64           N  
ANISOU 4941  N   ASN A 602     6284   6701   4355   -835   -432    538       N  
ATOM   4942  CA  ASN A 602     -11.419  -8.073 -68.022  1.00 46.67           C  
ANISOU 4942  CA  ASN A 602     6383   6892   4459   -882   -502    613       C  
ATOM   4943  C   ASN A 602     -11.392  -7.833 -69.515  1.00 47.65           C  
ANISOU 4943  C   ASN A 602     6527   7098   4480   -981   -538    657       C  
ATOM   4944  O   ASN A 602     -12.099  -8.507 -70.271  1.00 49.66           O  
ANISOU 4944  O   ASN A 602     6787   7418   4662  -1061   -572    662       O  
ATOM   4945  CB  ASN A 602     -12.285  -7.014 -67.338  1.00 46.39           C  
ANISOU 4945  CB  ASN A 602     6284   6824   4517   -813   -545    705       C  
ATOM   4946  CG  ASN A 602     -12.908  -7.516 -66.053  1.00 45.26           C  
ANISOU 4946  CG  ASN A 602     6116   6629   4454   -747   -529    672       C  
ATOM   4947  OD1 ASN A 602     -13.024  -8.727 -65.835  1.00 45.22           O  
ANISOU 4947  OD1 ASN A 602     6132   6628   4424   -765   -506    600       O  
ATOM   4948  ND2 ASN A 602     -13.322  -6.588 -65.195  1.00 39.76           N  
ANISOU 4948  ND2 ASN A 602     5375   5880   3854   -673   -536    723       N  
ATOM   4949  N   GLU A 603     -10.574  -6.874 -69.942  1.00 47.08           N  
ANISOU 4949  N   GLU A 603     6467   7023   4398   -981   -532    690       N  
ATOM   4950  CA  GLU A 603     -10.452  -6.566 -71.365  1.00 45.83           C  
ANISOU 4950  CA  GLU A 603     6333   6943   4137  -1079   -563    736       C  
ATOM   4951  C   GLU A 603      -9.896  -7.768 -72.125  1.00 46.61           C  
ANISOU 4951  C   GLU A 603     6494   7085   4131  -1169   -516    637       C  
ATOM   4952  O   GLU A 603     -10.357  -8.065 -73.224  1.00 49.48           O  
ANISOU 4952  O   GLU A 603     6875   7530   4394  -1272   -553    660       O  
ATOM   4953  CB  GLU A 603      -9.608  -5.307 -71.598  1.00 44.64           C  
ANISOU 4953  CB  GLU A 603     6184   6774   4003  -1057   -557    786       C  
ATOM   4954  CG  GLU A 603     -10.328  -4.005 -71.242  1.00 47.48           C  
ANISOU 4954  CG  GLU A 603     6481   7110   4450   -998   -616    907       C  
ATOM   4955  CD  GLU A 603      -9.443  -2.748 -71.326  1.00 51.37           C  
ANISOU 4955  CD  GLU A 603     6972   7570   4975   -965   -601    950       C  
ATOM   4956  OE1 GLU A 603      -8.236  -2.855 -71.659  1.00 45.74           O  
ANISOU 4956  OE1 GLU A 603     6310   6854   4216   -987   -547    888       O  
ATOM   4957  OE2 GLU A 603      -9.973  -1.639 -71.055  1.00 51.31           O  
ANISOU 4957  OE2 GLU A 603     6912   7537   5048   -917   -642   1048       O  
ATOM   4958  N   TYR A 604      -8.939  -8.479 -71.524  1.00 46.03           N  
ANISOU 4958  N   TYR A 604     6450   6954   4084  -1133   -436    528       N  
ATOM   4959  CA  TYR A 604      -8.314  -9.637 -72.177  1.00 45.27           C  
ANISOU 4959  CA  TYR A 604     6409   6883   3909  -1212   -376    424       C  
ATOM   4960  C   TYR A 604      -9.280 -10.810 -72.358  1.00 45.62           C  
ANISOU 4960  C   TYR A 604     6455   6968   3911  -1268   -392    389       C  
ATOM   4961  O   TYR A 604      -9.383 -11.371 -73.450  1.00 47.88           O  
ANISOU 4961  O   TYR A 604     6777   7323   4092  -1378   -390    364       O  
ATOM   4962  CB  TYR A 604      -7.050 -10.090 -71.429  1.00 43.97           C  
ANISOU 4962  CB  TYR A 604     6264   6638   3803  -1153   -287    324       C  
ATOM   4963  CG  TYR A 604      -6.430 -11.357 -71.985  1.00 44.48           C  
ANISOU 4963  CG  TYR A 604     6377   6712   3811  -1225   -215    211       C  
ATOM   4964  CD1 TYR A 604      -6.529 -12.573 -71.296  1.00 45.23           C  
ANISOU 4964  CD1 TYR A 604     6470   6766   3949  -1202   -175    130       C  
ATOM   4965  CD2 TYR A 604      -5.749 -11.345 -73.207  1.00 45.12           C  
ANISOU 4965  CD2 TYR A 604     6503   6840   3799  -1320   -181    184       C  
ATOM   4966  CE1 TYR A 604      -5.966 -13.748 -71.816  1.00 45.33           C  
ANISOU 4966  CE1 TYR A 604     6522   6780   3922  -1269   -102     25       C  
ATOM   4967  CE2 TYR A 604      -5.185 -12.509 -73.734  1.00 45.26           C  
ANISOU 4967  CE2 TYR A 604     6565   6862   3771  -1391   -104     73       C  
ATOM   4968  CZ  TYR A 604      -5.296 -13.702 -73.038  1.00 47.85           C  
ANISOU 4968  CZ  TYR A 604     6886   7144   4152  -1363    -64     -6       C  
ATOM   4969  OH  TYR A 604      -4.731 -14.839 -73.571  1.00 50.36           O  
ANISOU 4969  OH  TYR A 604     7242   7458   4436  -1433     19   -116       O  
ATOM   4970  N   LEU A 605      -9.979 -11.173 -71.288  1.00 42.75           N  
ANISOU 4970  N   LEU A 605     6054   6562   3628  -1197   -404    387       N  
ATOM   4971  CA  LEU A 605     -10.894 -12.312 -71.308  1.00 43.80           C  
ANISOU 4971  CA  LEU A 605     6185   6722   3736  -1239   -415    351       C  
ATOM   4972  C   LEU A 605     -12.148 -12.095 -72.172  1.00 45.31           C  
ANISOU 4972  C   LEU A 605     6356   7001   3859  -1317   -503    438       C  
ATOM   4973  O   LEU A 605     -12.642 -13.036 -72.800  1.00 44.94           O  
ANISOU 4973  O   LEU A 605     6329   7007   3739  -1405   -507    400       O  
ATOM   4974  CB  LEU A 605     -11.269 -12.718 -69.876  1.00 41.10           C  
ANISOU 4974  CB  LEU A 605     5807   6306   3501  -1140   -403    328       C  
ATOM   4975  CG  LEU A 605     -10.139 -13.358 -69.057  1.00 40.16           C  
ANISOU 4975  CG  LEU A 605     5712   6109   3438  -1084   -318    230       C  
ATOM   4976  CD1 LEU A 605     -10.556 -13.534 -67.608  1.00 41.27           C  
ANISOU 4976  CD1 LEU A 605     5816   6183   3680   -987   -318    229       C  
ATOM   4977  CD2 LEU A 605      -9.653 -14.688 -69.636  1.00 34.27           C  
ANISOU 4977  CD2 LEU A 605     5010   5375   2637  -1158   -255    124       C  
ATOM   4978  N   ASN A 606     -12.660 -10.864 -72.188  1.00 46.58           N  
ANISOU 4978  N   ASN A 606     6474   7174   4051  -1287   -572    556       N  
ATOM   4979  CA  ASN A 606     -13.761 -10.487 -73.076  1.00 50.34           C  
ANISOU 4979  CA  ASN A 606     6924   7733   4468  -1363   -664    658       C  
ATOM   4980  C   ASN A 606     -13.393 -10.712 -74.546  1.00 54.43           C  
ANISOU 4980  C   ASN A 606     7498   8340   4843  -1498   -667    645       C  
ATOM   4981  O   ASN A 606     -14.226 -11.145 -75.343  1.00 55.43           O  
ANISOU 4981  O   ASN A 606     7627   8546   4888  -1595   -720    671       O  
ATOM   4982  CB  ASN A 606     -14.165  -9.020 -72.849  1.00 49.64           C  
ANISOU 4982  CB  ASN A 606     6778   7629   4453  -1301   -727    788       C  
ATOM   4983  CG  ASN A 606     -15.240  -8.863 -71.778  1.00 48.79           C  
ANISOU 4983  CG  ASN A 606     6602   7475   4461  -1216   -760    835       C  
ATOM   4984  OD1 ASN A 606     -16.401  -9.203 -72.007  1.00 47.72           O  
ANISOU 4984  OD1 ASN A 606     6433   7383   4315  -1255   -819    879       O  
ATOM   4985  ND2 ASN A 606     -14.860  -8.333 -70.608  1.00 41.68           N  
ANISOU 4985  ND2 ASN A 606     5679   6486   3671  -1102   -721    825       N  
ATOM   4986  N   GLU A 607     -12.137 -10.422 -74.882  1.00 58.53           N  
ANISOU 4986  N   GLU A 607     8062   8845   5331  -1507   -608    603       N  
ATOM   4987  CA  GLU A 607     -11.593 -10.626 -76.222  1.00 62.34           C  
ANISOU 4987  CA  GLU A 607     8606   9402   5678  -1634   -591    575       C  
ATOM   4988  C   GLU A 607     -11.468 -12.115 -76.540  1.00 63.18           C  
ANISOU 4988  C   GLU A 607     8760   9527   5717  -1711   -529    447       C  
ATOM   4989  O   GLU A 607     -11.832 -12.552 -77.632  1.00 65.20           O  
ANISOU 4989  O   GLU A 607     9051   9870   5854  -1840   -550    442       O  
ATOM   4990  CB  GLU A 607     -10.233  -9.927 -76.343  1.00 63.85           C  
ANISOU 4990  CB  GLU A 607     8828   9558   5875  -1609   -533    556       C  
ATOM   4991  CG  GLU A 607      -9.339 -10.395 -77.504  1.00 71.10           C  
ANISOU 4991  CG  GLU A 607     9820  10525   6668  -1728   -472    479       C  
ATOM   4992  CD  GLU A 607      -7.848 -10.258 -77.188  1.00 74.90           C  
ANISOU 4992  CD  GLU A 607    10329  10935   7194  -1676   -375    402       C  
ATOM   4993  OE1 GLU A 607      -7.133 -11.288 -77.208  1.00 75.56           O  
ANISOU 4993  OE1 GLU A 607    10453  10992   7266  -1701   -285    277       O  
ATOM   4994  OE2 GLU A 607      -7.395  -9.124 -76.905  1.00 76.25           O  
ANISOU 4994  OE2 GLU A 607    10479  11072   7420  -1609   -389    466       O  
ATOM   4995  N   VAL A 608     -10.953 -12.884 -75.585  1.00 63.23           N  
ANISOU 4995  N   VAL A 608     8770   9451   5804  -1637   -451    346       N  
ATOM   4996  CA  VAL A 608     -10.814 -14.336 -75.735  1.00 64.43           C  
ANISOU 4996  CA  VAL A 608     8960   9602   5919  -1694   -383    222       C  
ATOM   4997  C   VAL A 608     -12.167 -15.010 -76.001  1.00 65.36           C  
ANISOU 4997  C   VAL A 608     9061   9780   5992  -1759   -443    241       C  
ATOM   4998  O   VAL A 608     -12.259 -15.930 -76.816  1.00 65.01           O  
ANISOU 4998  O   VAL A 608     9060   9789   5853  -1872   -417    172       O  
ATOM   4999  CB  VAL A 608     -10.127 -14.968 -74.490  1.00 62.82           C  
ANISOU 4999  CB  VAL A 608     8747   9290   5833  -1586   -302    132       C  
ATOM   5000  CG1 VAL A 608     -10.372 -16.481 -74.412  1.00 61.91           C  
ANISOU 5000  CG1 VAL A 608     8650   9165   5710  -1627   -251     27       C  
ATOM   5001  CG2 VAL A 608      -8.636 -14.665 -74.497  1.00 62.94           C  
ANISOU 5001  CG2 VAL A 608     8792   9255   5869  -1560   -223     80       C  
ATOM   5002  N   CYS A 609     -13.206 -14.527 -75.321  1.00 65.49           N  
ANISOU 5002  N   CYS A 609     9016   9789   6079  -1690   -522    334       N  
ATOM   5003  CA  CYS A 609     -14.535 -15.135 -75.373  1.00 65.95           C  
ANISOU 5003  CA  CYS A 609     9045   9891   6120  -1732   -582    359       C  
ATOM   5004  C   CYS A 609     -15.486 -14.455 -76.364  1.00 66.88           C  
ANISOU 5004  C   CYS A 609     9145  10111   6157  -1820   -691    480       C  
ATOM   5005  O   CYS A 609     -16.598 -14.932 -76.596  1.00 66.91           O  
ANISOU 5005  O   CYS A 609     9126  10165   6132  -1875   -749    507       O  
ATOM   5006  CB  CYS A 609     -15.145 -15.164 -73.968  1.00 65.65           C  
ANISOU 5006  CB  CYS A 609     8948   9778   6217  -1606   -593    378       C  
ATOM   5007  SG  CYS A 609     -14.103 -16.012 -72.754  1.00 61.81           S  
ANISOU 5007  SG  CYS A 609     8481   9178   5826  -1508   -478    248       S  
ATOM   5008  N   GLY A 610     -15.041 -13.345 -76.945  1.00 67.16           N  
ANISOU 5008  N   GLY A 610     9186  10174   6158  -1836   -720    557       N  
ATOM   5009  CA  GLY A 610     -15.818 -12.623 -77.949  1.00 69.51           C  
ANISOU 5009  CA  GLY A 610     9466  10568   6377  -1925   -826    683       C  
ATOM   5010  C   GLY A 610     -17.007 -11.863 -77.392  1.00 70.11           C  
ANISOU 5010  C   GLY A 610     9455  10635   6550  -1855   -924    816       C  
ATOM   5011  O   GLY A 610     -18.043 -11.757 -78.057  1.00 69.82           O  
ANISOU 5011  O   GLY A 610     9389  10677   6462  -1933  -1018    906       O  
ATOM   5012  N   THR A 611     -16.859 -11.333 -76.176  1.00 69.33           N  
ANISOU 5012  N   THR A 611     9312  10440   6592  -1711   -900    829       N  
ATOM   5013  CA  THR A 611     -17.921 -10.559 -75.525  1.00 69.92           C  
ANISOU 5013  CA  THR A 611     9300  10488   6779  -1632   -975    947       C  
ATOM   5014  C   THR A 611     -17.549  -9.082 -75.338  1.00 70.84           C  
ANISOU 5014  C   THR A 611     9383  10566   6967  -1560   -996   1045       C  
ATOM   5015  O   THR A 611     -16.521  -8.622 -75.843  1.00 69.39           O  
ANISOU 5015  O   THR A 611     9244  10390   6731  -1582   -965   1033       O  
ATOM   5016  CB  THR A 611     -18.342 -11.180 -74.171  1.00 69.24           C  
ANISOU 5016  CB  THR A 611     9181  10321   6809  -1529   -936    887       C  
ATOM   5017  OG1 THR A 611     -17.178 -11.521 -73.406  1.00 67.69           O  
ANISOU 5017  OG1 THR A 611     9025  10045   6648  -1459   -833    774       O  
ATOM   5018  CG2 THR A 611     -19.186 -12.429 -74.393  1.00 69.98           C  
ANISOU 5018  CG2 THR A 611     9278  10460   6851  -1602   -950    839       C  
ATOM   5019  N   GLU A 612     -18.406  -8.345 -74.629  1.00 72.39           N  
ANISOU 5019  N   GLU A 612     9499  10721   7286  -1476  -1046   1140       N  
ATOM   5020  CA  GLU A 612     -18.142  -6.948 -74.277  1.00 73.54           C  
ANISOU 5020  CA  GLU A 612     9603  10814   7525  -1394  -1058   1229       C  
ATOM   5021  C   GLU A 612     -18.780  -6.586 -72.937  1.00 71.95           C  
ANISOU 5021  C   GLU A 612     9331  10522   7484  -1268  -1050   1251       C  
ATOM   5022  O   GLU A 612     -19.939  -6.934 -72.669  1.00 72.03           O  
ANISOU 5022  O   GLU A 612     9289  10539   7539  -1266  -1093   1285       O  
ATOM   5023  CB  GLU A 612     -18.641  -5.990 -75.370  1.00 76.00           C  
ANISOU 5023  CB  GLU A 612     9881  11197   7797  -1466  -1158   1380       C  
ATOM   5024  CG  GLU A 612     -18.362  -4.507 -75.078  1.00 80.18           C  
ANISOU 5024  CG  GLU A 612    10366  11670   8428  -1385  -1169   1477       C  
ATOM   5025  CD  GLU A 612     -19.325  -3.547 -75.778  1.00 86.09           C  
ANISOU 5025  CD  GLU A 612    11043  12466   9203  -1423  -1282   1653       C  
ATOM   5026  OE1 GLU A 612     -20.358  -4.001 -76.326  1.00 88.75           O  
ANISOU 5026  OE1 GLU A 612    11352  12872   9498  -1499  -1359   1708       O  
ATOM   5027  OE2 GLU A 612     -19.047  -2.326 -75.771  1.00 86.90           O  
ANISOU 5027  OE2 GLU A 612    11113  12532   9373  -1377  -1295   1740       O  
ATOM   5028  N   GLY A 613     -18.006  -5.896 -72.101  1.00 69.73           N  
ANISOU 5028  N   GLY A 613     9049  10157   7288  -1170   -991   1229       N  
ATOM   5029  CA  GLY A 613     -18.508  -5.311 -70.862  1.00 68.00           C  
ANISOU 5029  CA  GLY A 613     8766   9849   7222  -1054   -978   1258       C  
ATOM   5030  C   GLY A 613     -18.776  -6.275 -69.720  1.00 65.66           C  
ANISOU 5030  C   GLY A 613     8472   9501   6977   -998   -924   1160       C  
ATOM   5031  O   GLY A 613     -19.207  -5.854 -68.647  1.00 66.29           O  
ANISOU 5031  O   GLY A 613     8502   9508   7177   -908   -906   1174       O  
ATOM   5032  N   GLU A 614     -18.525  -7.562 -69.935  1.00 63.03           N  
ANISOU 5032  N   GLU A 614     8193   9202   6553  -1053   -894   1060       N  
ATOM   5033  CA  GLU A 614     -18.757  -8.550 -68.890  1.00 61.70           C  
ANISOU 5033  CA  GLU A 614     8029   8987   6428  -1006   -844    969       C  
ATOM   5034  C   GLU A 614     -17.587  -8.637 -67.912  1.00 57.39           C  
ANISOU 5034  C   GLU A 614     7524   8363   5919   -929   -755    873       C  
ATOM   5035  O   GLU A 614     -16.423  -8.610 -68.314  1.00 56.10           O  
ANISOU 5035  O   GLU A 614     7413   8204   5697   -949   -718    827       O  
ATOM   5036  CB  GLU A 614     -19.057  -9.920 -69.485  1.00 63.88           C  
ANISOU 5036  CB  GLU A 614     8340   9325   6606  -1095   -849    905       C  
ATOM   5037  CG  GLU A 614     -19.899 -10.780 -68.557  1.00 70.63           C  
ANISOU 5037  CG  GLU A 614     9169  10147   7522  -1057   -834    863       C  
ATOM   5038  CD  GLU A 614     -19.744 -12.260 -68.820  1.00 72.64           C  
ANISOU 5038  CD  GLU A 614     9475  10432   7693  -1122   -800    757       C  
ATOM   5039  OE1 GLU A 614     -19.913 -12.678 -69.990  1.00 72.72           O  
ANISOU 5039  OE1 GLU A 614     9509  10524   7598  -1230   -837    762       O  
ATOM   5040  OE2 GLU A 614     -19.458 -13.000 -67.851  1.00 70.90           O  
ANISOU 5040  OE2 GLU A 614     9272  10153   7515  -1069   -736    669       O  
ATOM   5041  N   ALA A 615     -17.914  -8.736 -66.627  1.00 54.61           N  
ANISOU 5041  N   ALA A 615     7145   7940   5664   -845   -722    846       N  
ATOM   5042  CA  ALA A 615     -16.917  -8.777 -65.559  1.00 50.13           C  
ANISOU 5042  CA  ALA A 615     6609   7297   5140   -771   -645    766       C  
ATOM   5043  C   ALA A 615     -16.502 -10.213 -65.232  1.00 47.57           C  
ANISOU 5043  C   ALA A 615     6333   6967   4774   -787   -594    652       C  
ATOM   5044  O   ALA A 615     -17.331 -11.034 -64.857  1.00 48.81           O  
ANISOU 5044  O   ALA A 615     6475   7126   4946   -791   -599    631       O  
ATOM   5045  CB  ALA A 615     -17.452  -8.078 -64.319  1.00 49.76           C  
ANISOU 5045  CB  ALA A 615     6512   7178   5216   -679   -633    797       C  
ATOM   5046  N   PHE A 616     -15.216 -10.507 -65.389  1.00 44.43           N  
ANISOU 5046  N   PHE A 616     5990   6559   4331   -796   -544    581       N  
ATOM   5047  CA  PHE A 616     -14.670 -11.825 -65.083  1.00 39.54           C  
ANISOU 5047  CA  PHE A 616     5414   5923   3685   -808   -489    475       C  
ATOM   5048  C   PHE A 616     -14.076 -11.814 -63.690  1.00 38.55           C  
ANISOU 5048  C   PHE A 616     5292   5715   3639   -719   -437    429       C  
ATOM   5049  O   PHE A 616     -14.164 -12.802 -62.958  1.00 34.78           O  
ANISOU 5049  O   PHE A 616     4824   5209   3183   -702   -406    369       O  
ATOM   5050  CB  PHE A 616     -13.577 -12.198 -66.080  1.00 39.59           C  
ANISOU 5050  CB  PHE A 616     5474   5962   3605   -873   -459    422       C  
ATOM   5051  CG  PHE A 616     -14.090 -12.652 -67.417  1.00 39.36           C  
ANISOU 5051  CG  PHE A 616     5459   6019   3478   -981   -496    434       C  
ATOM   5052  CD1 PHE A 616     -14.163 -14.011 -67.722  1.00 39.25           C  
ANISOU 5052  CD1 PHE A 616     5474   6027   3413  -1040   -467    353       C  
ATOM   5053  CD2 PHE A 616     -14.481 -11.725 -68.380  1.00 38.99           C  
ANISOU 5053  CD2 PHE A 616     5395   6031   3387  -1028   -558    526       C  
ATOM   5054  CE1 PHE A 616     -14.630 -14.444 -68.972  1.00 39.78           C  
ANISOU 5054  CE1 PHE A 616     5558   6176   3380  -1151   -499    358       C  
ATOM   5055  CE2 PHE A 616     -14.946 -12.148 -69.632  1.00 41.41           C  
ANISOU 5055  CE2 PHE A 616     5717   6424   3591  -1139   -597    539       C  
ATOM   5056  CZ  PHE A 616     -15.015 -13.506 -69.928  1.00 39.22           C  
ANISOU 5056  CZ  PHE A 616     5473   6171   3256  -1202   -566    452       C  
ATOM   5057  N   VAL A 617     -13.450 -10.686 -63.352  1.00 38.73           N  
ANISOU 5057  N   VAL A 617     5310   5703   3703   -669   -429    461       N  
ATOM   5058  CA  VAL A 617     -12.900 -10.442 -62.030  1.00 38.33           C  
ANISOU 5058  CA  VAL A 617     5260   5577   3725   -589   -388    430       C  
ATOM   5059  C   VAL A 617     -14.074 -10.161 -61.107  1.00 38.24           C  
ANISOU 5059  C   VAL A 617     5204   5540   3787   -542   -405    470       C  
ATOM   5060  O   VAL A 617     -14.735  -9.133 -61.238  1.00 40.70           O  
ANISOU 5060  O   VAL A 617     5473   5854   4135   -527   -439    547       O  
ATOM   5061  CB  VAL A 617     -11.908  -9.245 -62.036  1.00 39.88           C  
ANISOU 5061  CB  VAL A 617     5464   5749   3941   -557   -376    454       C  
ATOM   5062  CG1 VAL A 617     -11.282  -9.041 -60.645  1.00 36.92           C  
ANISOU 5062  CG1 VAL A 617     5095   5300   3633   -484   -333    417       C  
ATOM   5063  CG2 VAL A 617     -10.819  -9.449 -63.084  1.00 35.02           C  
ANISOU 5063  CG2 VAL A 617     4890   5164   3252   -611   -359    421       C  
ATOM   5064  N   LEU A 618     -14.343 -11.099 -60.201  1.00 36.01           N  
ANISOU 5064  N   LEU A 618     4926   5228   3527   -521   -379    418       N  
ATOM   5065  CA  LEU A 618     -15.502 -11.034 -59.307  1.00 34.49           C  
ANISOU 5065  CA  LEU A 618     4694   5011   3400   -484   -387    444       C  
ATOM   5066  C   LEU A 618     -15.158 -10.335 -57.995  1.00 33.94           C  
ANISOU 5066  C   LEU A 618     4622   4874   3402   -413   -351    437       C  
ATOM   5067  O   LEU A 618     -16.036  -9.880 -57.271  1.00 33.78           O  
ANISOU 5067  O   LEU A 618     4565   4826   3445   -379   -351    468       O  
ATOM   5068  CB  LEU A 618     -16.019 -12.445 -59.024  1.00 33.48           C  
ANISOU 5068  CB  LEU A 618     4575   4890   3256   -506   -376    393       C  
ATOM   5069  CG  LEU A 618     -15.042 -13.442 -58.380  1.00 36.06           C  
ANISOU 5069  CG  LEU A 618     4947   5182   3573   -494   -327    309       C  
ATOM   5070  CD1 LEU A 618     -15.385 -13.636 -56.930  1.00 35.54           C  
ANISOU 5070  CD1 LEU A 618     4872   5063   3568   -442   -301    292       C  
ATOM   5071  CD2 LEU A 618     -15.058 -14.803 -59.095  1.00 35.42           C  
ANISOU 5071  CD2 LEU A 618     4887   5136   3434   -556   -322    258       C  
ATOM   5072  N   TYR A 619     -13.866 -10.260 -57.703  1.00 34.93           N  
ANISOU 5072  N   TYR A 619     4784   4971   3515   -396   -319    394       N  
ATOM   5073  CA  TYR A 619     -13.378  -9.787 -56.425  1.00 32.55           C  
ANISOU 5073  CA  TYR A 619     4492   4610   3267   -340   -283    374       C  
ATOM   5074  C   TYR A 619     -11.895  -9.494 -56.501  1.00 34.02           C  
ANISOU 5074  C   TYR A 619     4712   4779   3434   -333   -262    345       C  
ATOM   5075  O   TYR A 619     -11.176 -10.054 -57.339  1.00 31.93           O  
ANISOU 5075  O   TYR A 619     4473   4541   3117   -370   -261    318       O  
ATOM   5076  CB  TYR A 619     -13.610 -10.854 -55.348  1.00 32.49           C  
ANISOU 5076  CB  TYR A 619     4497   4575   3272   -326   -258    323       C  
ATOM   5077  CG  TYR A 619     -13.203 -10.437 -53.945  1.00 26.92           C  
ANISOU 5077  CG  TYR A 619     3804   3813   2613   -278   -224    303       C  
ATOM   5078  CD1 TYR A 619     -12.146 -11.062 -53.287  1.00 23.15           C  
ANISOU 5078  CD1 TYR A 619     3363   3309   2123   -271   -199    251       C  
ATOM   5079  CD2 TYR A 619     -13.885  -9.416 -53.280  1.00 24.98           C  
ANISOU 5079  CD2 TYR A 619     3529   3538   2425   -246   -216    337       C  
ATOM   5080  CE1 TYR A 619     -11.789 -10.684 -51.976  1.00 26.46           C  
ANISOU 5080  CE1 TYR A 619     3796   3682   2575   -237   -173    235       C  
ATOM   5081  CE2 TYR A 619     -13.532  -9.024 -51.996  1.00 24.99           C  
ANISOU 5081  CE2 TYR A 619     3545   3490   2459   -212   -181    314       C  
ATOM   5082  CZ  TYR A 619     -12.496  -9.656 -51.350  1.00 25.71           C  
ANISOU 5082  CZ  TYR A 619     3679   3564   2527   -210   -163    264       C  
ATOM   5083  OH  TYR A 619     -12.188  -9.249 -50.079  1.00 31.22           O  
ANISOU 5083  OH  TYR A 619     4393   4220   3250   -186   -134    244       O  
ATOM   5084  N   GLY A 620     -11.447  -8.638 -55.584  1.00 33.94           N  
ANISOU 5084  N   GLY A 620     4703   4722   3469   -289   -240    347       N  
ATOM   5085  CA  GLY A 620     -10.035  -8.366 -55.384  1.00 34.84           C  
ANISOU 5085  CA  GLY A 620     4849   4812   3578   -276   -218    316       C  
ATOM   5086  C   GLY A 620      -9.829  -7.657 -54.062  1.00 35.85           C  
ANISOU 5086  C   GLY A 620     4977   4886   3757   -231   -193    309       C  
ATOM   5087  O   GLY A 620     -10.705  -6.913 -53.610  1.00 36.58           O  
ANISOU 5087  O   GLY A 620     5042   4961   3894   -210   -191    342       O  
ATOM   5088  N   ASP A 621      -8.672  -7.893 -53.445  1.00 33.91           N  
ANISOU 5088  N   ASP A 621     4763   4614   3508   -221   -172    267       N  
ATOM   5089  CA  ASP A 621      -8.317  -7.273 -52.180  1.00 33.25           C  
ANISOU 5089  CA  ASP A 621     4689   4484   3461   -189   -150    254       C  
ATOM   5090  C   ASP A 621      -6.834  -6.918 -52.151  1.00 33.30           C  
ANISOU 5090  C   ASP A 621     4718   4473   3462   -185   -140    234       C  
ATOM   5091  O   ASP A 621      -5.984  -7.806 -52.093  1.00 32.66           O  
ANISOU 5091  O   ASP A 621     4658   4391   3362   -196   -137    200       O  
ATOM   5092  CB  ASP A 621      -8.649  -8.226 -51.031  1.00 34.72           C  
ANISOU 5092  CB  ASP A 621     4888   4653   3651   -186   -138    221       C  
ATOM   5093  CG  ASP A 621      -8.377  -7.624 -49.661  1.00 34.00           C  
ANISOU 5093  CG  ASP A 621     4811   4520   3587   -164   -115    207       C  
ATOM   5094  OD1 ASP A 621      -7.690  -6.590 -49.569  1.00 35.60           O  
ANISOU 5094  OD1 ASP A 621     5017   4703   3804   -152   -106    212       O  
ATOM   5095  OD2 ASP A 621      -8.852  -8.201 -48.668  1.00 29.66           O  
ANISOU 5095  OD2 ASP A 621     4270   3957   3040   -164   -104    188       O  
ATOM   5096  N   THR A 622      -6.533  -5.615 -52.188  1.00 33.38           N  
ANISOU 5096  N   THR A 622     4719   4466   3497   -169   -134    258       N  
ATOM   5097  CA  THR A 622      -5.152  -5.092 -52.101  1.00 30.54           C  
ANISOU 5097  CA  THR A 622     4378   4086   3139   -164   -124    243       C  
ATOM   5098  C   THR A 622      -4.278  -5.359 -53.334  1.00 32.57           C  
ANISOU 5098  C   THR A 622     4642   4368   3364   -186   -132    240       C  
ATOM   5099  O   THR A 622      -3.864  -4.409 -54.010  1.00 31.21           O  
ANISOU 5099  O   THR A 622     4463   4199   3195   -186   -132    266       O  
ATOM   5100  CB  THR A 622      -4.413  -5.591 -50.831  1.00 30.06           C  
ANISOU 5100  CB  THR A 622     4344   3996   3084   -157   -112    201       C  
ATOM   5101  OG1 THR A 622      -5.196  -5.282 -49.662  1.00 31.37           O  
ANISOU 5101  OG1 THR A 622     4508   4138   3272   -144    -99    199       O  
ATOM   5102  CG2 THR A 622      -3.033  -4.936 -50.715  1.00 30.22           C  
ANISOU 5102  CG2 THR A 622     4376   3994   3113   -152   -106    190       C  
ATOM   5103  N   ASP A 623      -4.006  -6.641 -53.608  1.00 33.40           N  
ANISOU 5103  N   ASP A 623     4760   4490   3441   -207   -133    209       N  
ATOM   5104  CA  ASP A 623      -3.041  -7.053 -54.627  1.00 35.23           C  
ANISOU 5104  CA  ASP A 623     5002   4737   3646   -232   -127    191       C  
ATOM   5105  C   ASP A 623      -3.400  -8.367 -55.323  1.00 37.32           C  
ANISOU 5105  C   ASP A 623     5270   5033   3877   -265   -128    169       C  
ATOM   5106  O   ASP A 623      -2.624  -8.878 -56.126  1.00 35.88           O  
ANISOU 5106  O   ASP A 623     5098   4859   3674   -292   -114    143       O  
ATOM   5107  CB  ASP A 623      -1.664  -7.226 -53.987  1.00 35.85           C  
ANISOU 5107  CB  ASP A 623     5095   4780   3747   -221   -112    158       C  
ATOM   5108  CG  ASP A 623      -1.579  -8.461 -53.091  1.00 37.07           C  
ANISOU 5108  CG  ASP A 623     5257   4916   3913   -219   -110    125       C  
ATOM   5109  OD1 ASP A 623      -0.491  -9.071 -53.028  1.00 38.51           O  
ANISOU 5109  OD1 ASP A 623     5444   5078   4109   -223   -100     98       O  
ATOM   5110  OD2 ASP A 623      -2.584  -8.820 -52.441  1.00 35.48           O  
ANISOU 5110  OD2 ASP A 623     5053   4716   3711   -212   -118    130       O  
ATOM   5111  N   SER A 624      -4.549  -8.937 -54.986  1.00 38.87           N  
ANISOU 5111  N   SER A 624     5458   5240   4070   -266   -139    173       N  
ATOM   5112  CA  SER A 624      -4.958 -10.188 -55.603  1.00 39.20           C  
ANISOU 5112  CA  SER A 624     5503   5309   4081   -301   -139    150       C  
ATOM   5113  C   SER A 624      -6.281 -10.007 -56.309  1.00 38.55           C  
ANISOU 5113  C   SER A 624     5404   5271   3973   -322   -164    187       C  
ATOM   5114  O   SER A 624      -7.112  -9.197 -55.888  1.00 39.40           O  
ANISOU 5114  O   SER A 624     5492   5375   4105   -299   -179    227       O  
ATOM   5115  CB  SER A 624      -5.105 -11.283 -54.551  1.00 40.81           C  
ANISOU 5115  CB  SER A 624     5713   5488   4307   -289   -131    118       C  
ATOM   5116  OG  SER A 624      -6.376 -11.185 -53.935  1.00 46.79           O  
ANISOU 5116  OG  SER A 624     6456   6249   5073   -276   -145    141       O  
ATOM   5117  N   ILE A 625      -6.477 -10.773 -57.375  1.00 34.75           N  
ANISOU 5117  N   ILE A 625     4928   4829   3448   -369   -166    173       N  
ATOM   5118  CA  ILE A 625      -7.748 -10.783 -58.078  1.00 33.75           C  
ANISOU 5118  CA  ILE A 625     4783   4749   3290   -398   -195    208       C  
ATOM   5119  C   ILE A 625      -8.305 -12.194 -58.169  1.00 33.14           C  
ANISOU 5119  C   ILE A 625     4711   4688   3193   -429   -191    171       C  
ATOM   5120  O   ILE A 625      -7.555 -13.169 -58.232  1.00 33.28           O  
ANISOU 5120  O   ILE A 625     4748   4691   3204   -445   -161    116       O  
ATOM   5121  CB  ILE A 625      -7.658 -10.146 -59.491  1.00 33.63           C  
ANISOU 5121  CB  ILE A 625     4769   4782   3227   -442   -213    242       C  
ATOM   5122  CG1 ILE A 625      -6.626 -10.865 -60.369  1.00 31.97           C  
ANISOU 5122  CG1 ILE A 625     4589   4586   2972   -488   -183    190       C  
ATOM   5123  CG2 ILE A 625      -7.365  -8.661 -59.387  1.00 34.83           C  
ANISOU 5123  CG2 ILE A 625     4908   4918   3407   -409   -222    292       C  
ATOM   5124  CD1 ILE A 625      -6.799 -10.597 -61.862  1.00 27.43           C  
ANISOU 5124  CD1 ILE A 625     4022   4074   2329   -552   -200    216       C  
ATOM   5125  N   TYR A 626      -9.628 -12.296 -58.165  1.00 32.52           N  
ANISOU 5125  N   TYR A 626     4610   4634   3113   -436   -218    201       N  
ATOM   5126  CA  TYR A 626     -10.288 -13.582 -58.291  1.00 30.85           C  
ANISOU 5126  CA  TYR A 626     4399   4439   2882   -469   -216    169       C  
ATOM   5127  C   TYR A 626     -11.084 -13.588 -59.583  1.00 32.23           C  
ANISOU 5127  C   TYR A 626     4565   4680   3002   -528   -249    198       C  
ATOM   5128  O   TYR A 626     -11.988 -12.776 -59.772  1.00 34.74           O  
ANISOU 5128  O   TYR A 626     4853   5021   3326   -525   -287    261       O  
ATOM   5129  CB  TYR A 626     -11.146 -13.870 -57.055  1.00 29.65           C  
ANISOU 5129  CB  TYR A 626     4231   4258   2777   -430   -218    173       C  
ATOM   5130  CG  TYR A 626     -10.300 -14.040 -55.819  1.00 30.46           C  
ANISOU 5130  CG  TYR A 626     4350   4304   2921   -386   -188    142       C  
ATOM   5131  CD1 TYR A 626      -9.700 -12.936 -55.211  1.00 29.75           C  
ANISOU 5131  CD1 TYR A 626     4261   4183   2860   -346   -184    162       C  
ATOM   5132  CD2 TYR A 626     -10.059 -15.304 -55.278  1.00 29.11           C  
ANISOU 5132  CD2 TYR A 626     4192   4108   2760   -389   -166     94       C  
ATOM   5133  CE1 TYR A 626      -8.896 -13.079 -54.107  1.00 30.35           C  
ANISOU 5133  CE1 TYR A 626     4352   4213   2966   -315   -163    136       C  
ATOM   5134  CE2 TYR A 626      -9.264 -15.456 -54.164  1.00 30.52           C  
ANISOU 5134  CE2 TYR A 626     4384   4238   2975   -354   -147     76       C  
ATOM   5135  CZ  TYR A 626      -8.682 -14.336 -53.585  1.00 33.84           C  
ANISOU 5135  CZ  TYR A 626     4807   4636   3416   -319   -148     97       C  
ATOM   5136  OH  TYR A 626      -7.883 -14.459 -52.471  1.00 39.48           O  
ANISOU 5136  OH  TYR A 626     5535   5307   4161   -292   -135     82       O  
ATOM   5137  N   VAL A 627     -10.697 -14.486 -60.484  1.00 34.05           N  
ANISOU 5137  N   VAL A 627     4820   4938   3180   -586   -232    151       N  
ATOM   5138  CA  VAL A 627     -11.247 -14.557 -61.835  1.00 34.71           C  
ANISOU 5138  CA  VAL A 627     4905   5091   3194   -660   -260    170       C  
ATOM   5139  C   VAL A 627     -12.138 -15.780 -61.981  1.00 36.20           C  
ANISOU 5139  C   VAL A 627     5091   5302   3363   -702   -263    139       C  
ATOM   5140  O   VAL A 627     -11.734 -16.900 -61.660  1.00 36.38           O  
ANISOU 5140  O   VAL A 627     5131   5296   3396   -706   -221     72       O  
ATOM   5141  CB  VAL A 627     -10.125 -14.610 -62.890  1.00 34.83           C  
ANISOU 5141  CB  VAL A 627     4954   5125   3154   -710   -231    135       C  
ATOM   5142  CG1 VAL A 627     -10.692 -14.789 -64.281  1.00 37.78           C  
ANISOU 5142  CG1 VAL A 627     5337   5576   3443   -800   -258    148       C  
ATOM   5143  CG2 VAL A 627      -9.278 -13.340 -62.830  1.00 37.18           C  
ANISOU 5143  CG2 VAL A 627     5253   5404   3471   -673   -231    170       C  
ATOM   5144  N   SER A 628     -13.358 -15.538 -62.450  1.00 37.60           N  
ANISOU 5144  N   SER A 628     5240   5528   3517   -732   -313    193       N  
ATOM   5145  CA  SER A 628     -14.316 -16.580 -62.766  1.00 39.34           C  
ANISOU 5145  CA  SER A 628     5455   5782   3709   -783   -326    174       C  
ATOM   5146  C   SER A 628     -13.942 -17.282 -64.075  1.00 41.01           C  
ANISOU 5146  C   SER A 628     5701   6045   3835   -876   -312    126       C  
ATOM   5147  O   SER A 628     -13.830 -16.645 -65.130  1.00 40.71           O  
ANISOU 5147  O   SER A 628     5672   6060   3736   -927   -338    161       O  
ATOM   5148  CB  SER A 628     -15.721 -15.976 -62.862  1.00 40.32           C  
ANISOU 5148  CB  SER A 628     5532   5942   3844   -785   -390    256       C  
ATOM   5149  OG  SER A 628     -16.649 -16.926 -63.337  1.00 41.29           O  
ANISOU 5149  OG  SER A 628     5649   6108   3932   -846   -409    241       O  
ATOM   5150  N   ALA A 629     -13.771 -18.601 -63.986  1.00 42.42           N  
ANISOU 5150  N   ALA A 629     5900   6207   4010   -901   -267     47       N  
ATOM   5151  CA  ALA A 629     -13.293 -19.438 -65.091  1.00 41.68           C  
ANISOU 5151  CA  ALA A 629     5845   6147   3846   -989   -232    -20       C  
ATOM   5152  C   ALA A 629     -14.398 -20.291 -65.725  1.00 42.69           C  
ANISOU 5152  C   ALA A 629     5969   6329   3923  -1068   -255    -33       C  
ATOM   5153  O   ALA A 629     -14.127 -21.126 -66.603  1.00 42.17           O  
ANISOU 5153  O   ALA A 629     5935   6290   3797  -1150   -220    -99       O  
ATOM   5154  CB  ALA A 629     -12.152 -20.330 -64.606  1.00 41.32           C  
ANISOU 5154  CB  ALA A 629     5823   6033   3843   -966   -154   -106       C  
ATOM   5155  N   ASP A 630     -15.636 -20.080 -65.279  1.00 42.28           N  
ANISOU 5155  N   ASP A 630     5877   6292   3897  -1045   -310     27       N  
ATOM   5156  CA  ASP A 630     -16.791 -20.813 -65.795  1.00 42.56           C  
ANISOU 5156  CA  ASP A 630     5900   6378   3891  -1115   -341     25       C  
ATOM   5157  C   ASP A 630     -16.778 -20.883 -67.311  1.00 43.76           C  
ANISOU 5157  C   ASP A 630     6081   6613   3934  -1230   -358     17       C  
ATOM   5158  O   ASP A 630     -16.869 -21.967 -67.890  1.00 44.80           O  
ANISOU 5158  O   ASP A 630     6238   6768   4017  -1307   -329    -53       O  
ATOM   5159  CB  ASP A 630     -18.095 -20.159 -65.334  1.00 43.05           C  
ANISOU 5159  CB  ASP A 630     5908   6456   3993  -1079   -411    116       C  
ATOM   5160  CG  ASP A 630     -18.399 -20.423 -63.880  1.00 41.99           C  
ANISOU 5160  CG  ASP A 630     5749   6250   3955   -990   -389    110       C  
ATOM   5161  OD1 ASP A 630     -17.473 -20.781 -63.118  1.00 38.41           O  
ANISOU 5161  OD1 ASP A 630     5318   5734   3543   -940   -331     56       O  
ATOM   5162  OD2 ASP A 630     -19.579 -20.273 -63.502  1.00 44.43           O  
ANISOU 5162  OD2 ASP A 630     6014   6568   4298   -974   -431    161       O  
ATOM   5163  N   LYS A 631     -16.662 -19.719 -67.944  1.00 42.82           N  
ANISOU 5163  N   LYS A 631     5959   6537   3775  -1244   -403     89       N  
ATOM   5164  CA  LYS A 631     -16.687 -19.626 -69.396  1.00 41.04           C  
ANISOU 5164  CA  LYS A 631     5760   6396   3436  -1359   -429     97       C  
ATOM   5165  C   LYS A 631     -15.516 -20.348 -70.049  1.00 41.39           C  
ANISOU 5165  C   LYS A 631     5865   6436   3425  -1420   -348     -7       C  
ATOM   5166  O   LYS A 631     -15.668 -20.893 -71.140  1.00 41.89           O  
ANISOU 5166  O   LYS A 631     5960   6564   3392  -1533   -346    -43       O  
ATOM   5167  CB  LYS A 631     -16.734 -18.167 -69.846  1.00 40.85           C  
ANISOU 5167  CB  LYS A 631     5718   6411   3392  -1353   -494    203       C  
ATOM   5168  CG  LYS A 631     -18.106 -17.563 -69.701  1.00 41.31           C  
ANISOU 5168  CG  LYS A 631     5715   6500   3480  -1339   -583    311       C  
ATOM   5169  CD  LYS A 631     -18.061 -16.057 -69.796  1.00 44.46           C  
ANISOU 5169  CD  LYS A 631     6085   6906   3902  -1300   -634    418       C  
ATOM   5170  CE  LYS A 631     -19.467 -15.497 -69.829  1.00 45.82           C  
ANISOU 5170  CE  LYS A 631     6191   7114   4106  -1301   -725    529       C  
ATOM   5171  NZ  LYS A 631     -20.200 -15.710 -68.543  1.00 46.18           N  
ANISOU 5171  NZ  LYS A 631     6189   7095   4262  -1212   -717    530       N  
ATOM   5172  N   ILE A 632     -14.356 -20.349 -69.387  1.00 40.56           N  
ANISOU 5172  N   ILE A 632     5774   6255   3381  -1349   -281    -55       N  
ATOM   5173  CA  ILE A 632     -13.180 -21.042 -69.921  1.00 40.76           C  
ANISOU 5173  CA  ILE A 632     5849   6262   3375  -1397   -195   -156       C  
ATOM   5174  C   ILE A 632     -13.433 -22.545 -69.895  1.00 42.42           C  
ANISOU 5174  C   ILE A 632     6072   6456   3590  -1441   -143   -249       C  
ATOM   5175  O   ILE A 632     -13.223 -23.226 -70.891  1.00 42.56           O  
ANISOU 5175  O   ILE A 632     6129   6510   3533  -1544   -102   -318       O  
ATOM   5176  CB  ILE A 632     -11.877 -20.692 -69.160  1.00 39.97           C  
ANISOU 5176  CB  ILE A 632     5753   6080   3354  -1307   -139   -179       C  
ATOM   5177  CG1 ILE A 632     -11.661 -19.172 -69.094  1.00 37.83           C  
ANISOU 5177  CG1 ILE A 632     5467   5819   3088  -1258   -189    -87       C  
ATOM   5178  CG2 ILE A 632     -10.668 -21.412 -69.781  1.00 39.18           C  
ANISOU 5178  CG2 ILE A 632     5697   5957   3231  -1361    -46   -282       C  
ATOM   5179  CD1 ILE A 632     -11.659 -18.454 -70.435  1.00 47.23           C  
ANISOU 5179  CD1 ILE A 632     6680   7092   4172  -1347   -223    -45       C  
ATOM   5180  N   ILE A 633     -13.908 -23.049 -68.757  1.00 42.51           N  
ANISOU 5180  N   ILE A 633     6051   6412   3688  -1367   -143   -251       N  
ATOM   5181  CA  ILE A 633     -14.310 -24.443 -68.661  1.00 44.82           C  
ANISOU 5181  CA  ILE A 633     6348   6687   3993  -1404   -103   -327       C  
ATOM   5182  C   ILE A 633     -15.373 -24.772 -69.716  1.00 46.60           C  
ANISOU 5182  C   ILE A 633     6581   7004   4119  -1519   -147   -322       C  
ATOM   5183  O   ILE A 633     -15.257 -25.776 -70.414  1.00 44.68           O  
ANISOU 5183  O   ILE A 633     6371   6777   3830  -1609    -95   -409       O  
ATOM   5184  CB  ILE A 633     -14.811 -24.813 -67.234  1.00 43.49           C  
ANISOU 5184  CB  ILE A 633     6141   6453   3930  -1306   -109   -311       C  
ATOM   5185  CG1 ILE A 633     -13.666 -24.740 -66.211  1.00 41.62           C  
ANISOU 5185  CG1 ILE A 633     5904   6126   3786  -1209    -58   -331       C  
ATOM   5186  CG2 ILE A 633     -15.489 -26.191 -67.224  1.00 45.36           C  
ANISOU 5186  CG2 ILE A 633     6378   6685   4172  -1354    -83   -375       C  
ATOM   5187  CD1 ILE A 633     -12.493 -25.669 -66.486  1.00 42.56           C  
ANISOU 5187  CD1 ILE A 633     6052   6194   3923  -1237     37   -431       C  
ATOM   5188  N   ASP A 634     -16.376 -23.901 -69.844  1.00 48.99           N  
ANISOU 5188  N   ASP A 634     6853   7367   4394  -1520   -241   -221       N  
ATOM   5189  CA  ASP A 634     -17.511 -24.139 -70.744  1.00 52.36           C  
ANISOU 5189  CA  ASP A 634     7276   7883   4735  -1625   -301   -197       C  
ATOM   5190  C   ASP A 634     -17.143 -24.143 -72.225  1.00 53.57           C  
ANISOU 5190  C   ASP A 634     7480   8115   4760  -1757   -293   -227       C  
ATOM   5191  O   ASP A 634     -17.795 -24.822 -73.017  1.00 54.25           O  
ANISOU 5191  O   ASP A 634     7581   8264   4767  -1867   -306   -257       O  
ATOM   5192  CB  ASP A 634     -18.660 -23.152 -70.477  1.00 52.49           C  
ANISOU 5192  CB  ASP A 634     7238   7937   4770  -1588   -406    -70       C  
ATOM   5193  CG  ASP A 634     -19.429 -23.469 -69.196  1.00 53.84           C  
ANISOU 5193  CG  ASP A 634     7360   8049   5046  -1497   -415    -53       C  
ATOM   5194  OD1 ASP A 634     -19.402 -24.634 -68.737  1.00 53.08           O  
ANISOU 5194  OD1 ASP A 634     7274   7909   4985  -1493   -358   -134       O  
ATOM   5195  OD2 ASP A 634     -20.064 -22.544 -68.643  1.00 55.99           O  
ANISOU 5195  OD2 ASP A 634     7584   8318   5371  -1430   -476     42       O  
ATOM   5196  N   LYS A 635     -16.103 -23.392 -72.591  1.00 53.97           N  
ANISOU 5196  N   LYS A 635     7557   8163   4786  -1751   -270   -222       N  
ATOM   5197  CA  LYS A 635     -15.664 -23.306 -73.985  1.00 56.96           C  
ANISOU 5197  CA  LYS A 635     7988   8616   5039  -1877   -257   -249       C  
ATOM   5198  C   LYS A 635     -15.087 -24.615 -74.534  1.00 56.94           C  
ANISOU 5198  C   LYS A 635     8036   8600   4997  -1965   -154   -390       C  
ATOM   5199  O   LYS A 635     -15.055 -24.822 -75.750  1.00 56.80           O  
ANISOU 5199  O   LYS A 635     8065   8658   4861  -2098   -144   -426       O  
ATOM   5200  CB  LYS A 635     -14.674 -22.155 -74.192  1.00 58.73           C  
ANISOU 5200  CB  LYS A 635     8226   8835   5255  -1845   -253   -207       C  
ATOM   5201  CG  LYS A 635     -15.244 -21.003 -75.007  1.00 65.71           C  
ANISOU 5201  CG  LYS A 635     9101   9811   6055  -1898   -353    -90       C  
ATOM   5202  CD  LYS A 635     -14.154 -20.321 -75.831  1.00 74.21           C  
ANISOU 5202  CD  LYS A 635    10222  10910   7063  -1943   -322    -94       C  
ATOM   5203  CE  LYS A 635     -14.725 -19.537 -77.024  1.00 79.36           C  
ANISOU 5203  CE  LYS A 635    10884  11677   7592  -2051   -412     -1       C  
ATOM   5204  NZ  LYS A 635     -15.327 -18.223 -76.628  1.00 81.34           N  
ANISOU 5204  NZ  LYS A 635    11076  11936   7894  -1973   -513    147       N  
ATOM   5205  N   VAL A 636     -14.632 -25.490 -73.639  1.00 55.53           N  
ANISOU 5205  N   VAL A 636     7851   8327   4922  -1895    -76   -468       N  
ATOM   5206  CA  VAL A 636     -14.192 -26.823 -74.041  1.00 56.38           C  
ANISOU 5206  CA  VAL A 636     7997   8409   5018  -1970     26   -601       C  
ATOM   5207  C   VAL A 636     -15.292 -27.848 -73.735  1.00 58.17           C  
ANISOU 5207  C   VAL A 636     8202   8637   5263  -1992     12   -626       C  
ATOM   5208  O   VAL A 636     -15.429 -28.855 -74.442  1.00 59.86           O  
ANISOU 5208  O   VAL A 636     8448   8873   5421  -2100     63   -717       O  
ATOM   5209  CB  VAL A 636     -12.814 -27.221 -73.417  1.00 55.32           C  
ANISOU 5209  CB  VAL A 636     7869   8163   4986  -1894    135   -679       C  
ATOM   5210  CG1 VAL A 636     -12.243 -26.094 -72.580  1.00 52.77           C  
ANISOU 5210  CG1 VAL A 636     7518   7797   4737  -1768    103   -599       C  
ATOM   5211  CG2 VAL A 636     -12.889 -28.520 -72.627  1.00 54.75           C  
ANISOU 5211  CG2 VAL A 636     7779   8009   5013  -1857    198   -755       C  
ATOM   5212  N   GLY A 637     -16.088 -27.567 -72.705  1.00 56.77           N  
ANISOU 5212  N   GLY A 637     7972   8437   5162  -1894    -54   -548       N  
ATOM   5213  CA  GLY A 637     -17.181 -28.445 -72.296  1.00 59.23           C  
ANISOU 5213  CA  GLY A 637     8256   8746   5502  -1902    -74   -560       C  
ATOM   5214  C   GLY A 637     -16.746 -29.397 -71.201  1.00 59.85           C  
ANISOU 5214  C   GLY A 637     8321   8714   5704  -1818      5   -627       C  
ATOM   5215  O   GLY A 637     -15.695 -30.026 -71.311  1.00 60.27           O  
ANISOU 5215  O   GLY A 637     8403   8711   5785  -1828    103   -719       O  
ATOM   5216  N   GLU A 638     -17.553 -29.502 -70.147  1.00 60.90           N  
ANISOU 5216  N   GLU A 638     8408   8815   5915  -1737    -36   -579       N  
ATOM   5217  CA  GLU A 638     -17.231 -30.358 -68.999  1.00 63.67           C  
ANISOU 5217  CA  GLU A 638     8742   9063   6385  -1653     26   -626       C  
ATOM   5218  C   GLU A 638     -17.143 -31.839 -69.354  1.00 65.70           C  
ANISOU 5218  C   GLU A 638     9022   9292   6647  -1728    111   -742       C  
ATOM   5219  O   GLU A 638     -16.394 -32.588 -68.723  1.00 66.83           O  
ANISOU 5219  O   GLU A 638     9165   9344   6883  -1678    190   -802       O  
ATOM   5220  CB  GLU A 638     -18.233 -30.152 -67.859  1.00 63.38           C  
ANISOU 5220  CB  GLU A 638     8655   9008   6418  -1565    -37   -548       C  
ATOM   5221  CG  GLU A 638     -17.823 -29.071 -66.865  1.00 65.24           C  
ANISOU 5221  CG  GLU A 638     8867   9202   6720  -1443    -66   -471       C  
ATOM   5222  CD  GLU A 638     -18.900 -28.761 -65.834  1.00 68.28           C  
ANISOU 5222  CD  GLU A 638     9204   9578   7163  -1370   -127   -394       C  
ATOM   5223  OE1 GLU A 638     -18.562 -28.598 -64.641  1.00 65.31           O  
ANISOU 5223  OE1 GLU A 638     8811   9130   6872  -1268   -113   -374       O  
ATOM   5224  OE2 GLU A 638     -20.087 -28.676 -66.217  1.00 73.97           O  
ANISOU 5224  OE2 GLU A 638     9902  10360   7842  -1417   -189   -352       O  
ATOM   5225  N   SER A 639     -17.907 -32.247 -70.366  1.00 67.84           N  
ANISOU 5225  N   SER A 639     9311   9642   6822  -1849     93   -771       N  
ATOM   5226  CA  SER A 639     -17.966 -33.639 -70.818  1.00 68.79           C  
ANISOU 5226  CA  SER A 639     9454   9745   6936  -1938    171   -884       C  
ATOM   5227  C   SER A 639     -16.616 -34.148 -71.306  1.00 68.12           C  
ANISOU 5227  C   SER A 639     9411   9609   6863  -1973    287   -990       C  
ATOM   5228  O   SER A 639     -16.324 -35.341 -71.212  1.00 68.57           O  
ANISOU 5228  O   SER A 639     9475   9601   6979  -1994    378  -1086       O  
ATOM   5229  CB  SER A 639     -18.998 -33.785 -71.942  1.00 71.00           C  
ANISOU 5229  CB  SER A 639     9751  10134   7090  -2076    120   -888       C  
ATOM   5230  OG  SER A 639     -20.305 -33.479 -71.484  1.00 73.23           O  
ANISOU 5230  OG  SER A 639     9988  10457   7379  -2047     20   -797       O  
ATOM   5231  N   LYS A 640     -15.801 -33.231 -71.822  1.00 66.56           N  
ANISOU 5231  N   LYS A 640     9237   9437   6617  -1979    286   -970       N  
ATOM   5232  CA  LYS A 640     -14.514 -33.566 -72.423  1.00 65.83           C  
ANISOU 5232  CA  LYS A 640     9183   9304   6523  -2022    395  -1066       C  
ATOM   5233  C   LYS A 640     -13.408 -33.931 -71.423  1.00 61.87           C  
ANISOU 5233  C   LYS A 640     8661   8678   6171  -1910    473  -1097       C  
ATOM   5234  O   LYS A 640     -12.390 -34.502 -71.819  1.00 61.44           O  
ANISOU 5234  O   LYS A 640     8629   8569   6146  -1944    579  -1190       O  
ATOM   5235  CB  LYS A 640     -14.051 -32.428 -73.353  1.00 69.29           C  
ANISOU 5235  CB  LYS A 640     9655   9818   6854  -2072    365  -1029       C  
ATOM   5236  CG  LYS A 640     -14.256 -32.676 -74.862  1.00 74.49           C  
ANISOU 5236  CG  LYS A 640    10368  10570   7365  -2244    385  -1093       C  
ATOM   5237  CD  LYS A 640     -15.710 -33.024 -75.239  1.00 80.51           C  
ANISOU 5237  CD  LYS A 640    11125  11417   8047  -2329    310  -1071       C  
ATOM   5238  CE  LYS A 640     -16.540 -31.786 -75.590  1.00 81.78           C  
ANISOU 5238  CE  LYS A 640    11274  11685   8112  -2345    173   -939       C  
ATOM   5239  NZ  LYS A 640     -16.228 -31.246 -76.948  1.00 81.31           N  
ANISOU 5239  NZ  LYS A 640    11268  11720   7906  -2473    167   -946       N  
ATOM   5240  N   PHE A 641     -13.606 -33.610 -70.141  1.00 57.20           N  
ANISOU 5240  N   PHE A 641     8025   8038   5671  -1782    422  -1018       N  
ATOM   5241  CA  PHE A 641     -12.595 -33.891 -69.107  1.00 53.05           C  
ANISOU 5241  CA  PHE A 641     7475   7398   5284  -1675    480  -1030       C  
ATOM   5242  C   PHE A 641     -12.720 -35.291 -68.510  1.00 53.17           C  
ANISOU 5242  C   PHE A 641     7471   7331   5401  -1662    544  -1093       C  
ATOM   5243  O   PHE A 641     -13.824 -35.777 -68.253  1.00 52.28           O  
ANISOU 5243  O   PHE A 641     7344   7238   5283  -1675    507  -1081       O  
ATOM   5244  CB  PHE A 641     -12.620 -32.837 -67.993  1.00 49.76           C  
ANISOU 5244  CB  PHE A 641     7026   6967   4915  -1549    399   -917       C  
ATOM   5245  CG  PHE A 641     -12.318 -31.444 -68.469  1.00 45.22           C  
ANISOU 5245  CG  PHE A 641     6464   6453   4264  -1546    346   -853       C  
ATOM   5246  CD1 PHE A 641     -13.340 -30.513 -68.618  1.00 43.38           C  
ANISOU 5246  CD1 PHE A 641     6223   6305   3955  -1553    243   -764       C  
ATOM   5247  CD2 PHE A 641     -11.016 -31.069 -68.788  1.00 44.94           C  
ANISOU 5247  CD2 PHE A 641     6447   6387   4241  -1540    401   -882       C  
ATOM   5248  CE1 PHE A 641     -13.073 -29.226 -69.078  1.00 43.36           C  
ANISOU 5248  CE1 PHE A 641     6230   6355   3888  -1552    195   -701       C  
ATOM   5249  CE2 PHE A 641     -10.731 -29.778 -69.242  1.00 41.94           C  
ANISOU 5249  CE2 PHE A 641     6080   6062   3792  -1540    354   -822       C  
ATOM   5250  CZ  PHE A 641     -11.763 -28.854 -69.385  1.00 40.86           C  
ANISOU 5250  CZ  PHE A 641     5937   6010   3580  -1546    250   -731       C  
ATOM   5251  N   ARG A 642     -11.571 -35.923 -68.294  1.00 53.81           N  
ANISOU 5251  N   ARG A 642     7548   7316   5582  -1636    641  -1158       N  
ATOM   5252  CA  ARG A 642     -11.499 -37.285 -67.774  1.00 55.37           C  
ANISOU 5252  CA  ARG A 642     7724   7421   5892  -1624    715  -1221       C  
ATOM   5253  C   ARG A 642     -11.840 -37.313 -66.290  1.00 54.67           C  
ANISOU 5253  C   ARG A 642     7591   7280   5901  -1505    662  -1140       C  
ATOM   5254  O   ARG A 642     -12.652 -38.134 -65.842  1.00 55.49           O  
ANISOU 5254  O   ARG A 642     7678   7366   6040  -1506    658  -1147       O  
ATOM   5255  CB  ARG A 642     -10.095 -37.854 -68.005  1.00 58.88           C  
ANISOU 5255  CB  ARG A 642     8170   7774   6426  -1629    834  -1304       C  
ATOM   5256  CG  ARG A 642      -9.813 -38.242 -69.456  1.00 65.52           C  
ANISOU 5256  CG  ARG A 642     9057   8650   7190  -1764    920  -1415       C  
ATOM   5257  CD  ARG A 642      -8.355 -38.649 -69.673  1.00 70.76           C  
ANISOU 5257  CD  ARG A 642     9718   9219   7950  -1762   1041  -1492       C  
ATOM   5258  NE  ARG A 642      -7.482 -37.505 -69.943  1.00 72.83           N  
ANISOU 5258  NE  ARG A 642     9993   9505   8175  -1738   1026  -1456       N  
ATOM   5259  CZ  ARG A 642      -6.591 -37.012 -69.085  1.00 73.70           C  
ANISOU 5259  CZ  ARG A 642    10070   9550   8383  -1627   1014  -1398       C  
ATOM   5260  NH1 ARG A 642      -6.440 -37.556 -67.885  1.00 77.12           N  
ANISOU 5260  NH1 ARG A 642    10455   9893   8953  -1531   1013  -1365       N  
ATOM   5261  NH2 ARG A 642      -5.845 -35.972 -69.430  1.00 71.76           N  
ANISOU 5261  NH2 ARG A 642     9839   9332   8095  -1617   1002  -1371       N  
ATOM   5262  N   ASP A 643     -11.214 -36.398 -65.547  1.00 49.99           N  
ANISOU 5262  N   ASP A 643     6983   6666   5346  -1409    621  -1065       N  
ATOM   5263  CA  ASP A 643     -11.374 -36.264 -64.108  1.00 47.95           C  
ANISOU 5263  CA  ASP A 643     6688   6359   5171  -1298    570   -985       C  
ATOM   5264  C   ASP A 643     -11.023 -34.826 -63.667  1.00 45.62           C  
ANISOU 5264  C   ASP A 643     6390   6092   4850  -1225    499   -895       C  
ATOM   5265  O   ASP A 643     -10.645 -33.994 -64.488  1.00 44.91           O  
ANISOU 5265  O   ASP A 643     6323   6054   4685  -1259    492   -895       O  
ATOM   5266  CB  ASP A 643     -10.501 -37.295 -63.376  1.00 47.70           C  
ANISOU 5266  CB  ASP A 643     6630   6209   5286  -1250    647  -1020       C  
ATOM   5267  CG  ASP A 643      -9.056 -37.299 -63.864  1.00 51.00           C  
ANISOU 5267  CG  ASP A 643     7052   6574   5752  -1257    726  -1072       C  
ATOM   5268  OD1 ASP A 643      -8.519 -36.230 -64.230  1.00 51.38           O  
ANISOU 5268  OD1 ASP A 643     7117   6662   5745  -1251    702  -1046       O  
ATOM   5269  OD2 ASP A 643      -8.449 -38.386 -63.887  1.00 56.07           O  
ANISOU 5269  OD2 ASP A 643     7679   7131   6494  -1271    816  -1140       O  
ATOM   5270  N   THR A 644     -11.141 -34.556 -62.371  1.00 43.34           N  
ANISOU 5270  N   THR A 644     6075   5769   4624  -1130    451   -822       N  
ATOM   5271  CA  THR A 644     -10.922 -33.227 -61.820  1.00 42.46           C  
ANISOU 5271  CA  THR A 644     5958   5679   4494  -1060    384   -737       C  
ATOM   5272  C   THR A 644      -9.520 -32.707 -62.132  1.00 43.77           C  
ANISOU 5272  C   THR A 644     6133   5818   4680  -1046    422   -752       C  
ATOM   5273  O   THR A 644      -9.365 -31.559 -62.546  1.00 44.19           O  
ANISOU 5273  O   THR A 644     6200   5923   4666  -1046    383   -716       O  
ATOM   5274  CB  THR A 644     -11.159 -33.208 -60.290  1.00 40.54           C  
ANISOU 5274  CB  THR A 644     5688   5391   4326   -967    344   -670       C  
ATOM   5275  OG1 THR A 644     -12.473 -33.707 -59.998  1.00 39.79           O  
ANISOU 5275  OG1 THR A 644     5584   5319   4216   -981    314   -658       O  
ATOM   5276  CG2 THR A 644     -11.025 -31.791 -59.738  1.00 39.33           C  
ANISOU 5276  CG2 THR A 644     5533   5264   4148   -903    277   -588       C  
ATOM   5277  N   ASN A 645      -8.507 -33.555 -61.954  1.00 43.97           N  
ANISOU 5277  N   ASN A 645     6146   5756   4803  -1035    497   -802       N  
ATOM   5278  CA  ASN A 645      -7.126 -33.151 -62.202  1.00 44.61           C  
ANISOU 5278  CA  ASN A 645     6229   5801   4921  -1019    539   -818       C  
ATOM   5279  C   ASN A 645      -6.893 -32.663 -63.636  1.00 43.96           C  
ANISOU 5279  C   ASN A 645     6182   5781   4741  -1102    567   -865       C  
ATOM   5280  O   ASN A 645      -6.049 -31.790 -63.873  1.00 45.80           O  
ANISOU 5280  O   ASN A 645     6422   6019   4960  -1086    566   -849       O  
ATOM   5281  CB  ASN A 645      -6.151 -34.276 -61.848  1.00 45.95           C  
ANISOU 5281  CB  ASN A 645     6371   5862   5225  -1001    622   -867       C  
ATOM   5282  CG  ASN A 645      -4.757 -33.756 -61.531  1.00 49.69           C  
ANISOU 5282  CG  ASN A 645     6829   6283   5769   -947    639   -846       C  
ATOM   5283  OD1 ASN A 645      -4.587 -32.923 -60.641  1.00 51.87           O  
ANISOU 5283  OD1 ASN A 645     7094   6560   6053   -876    573   -768       O  
ATOM   5284  ND2 ASN A 645      -3.754 -34.242 -62.261  1.00 49.63           N  
ANISOU 5284  ND2 ASN A 645     6820   6226   5813   -985    730   -920       N  
ATOM   5285  N   HIS A 646      -7.658 -33.219 -64.575  1.00 43.07           N  
ANISOU 5285  N   HIS A 646     6092   5717   4556  -1194    589   -922       N  
ATOM   5286  CA  HIS A 646      -7.578 -32.862 -65.994  1.00 44.09           C  
ANISOU 5286  CA  HIS A 646     6261   5916   4577  -1291    613   -970       C  
ATOM   5287  C   HIS A 646      -7.973 -31.400 -66.257  1.00 43.53           C  
ANISOU 5287  C   HIS A 646     6205   5935   4399  -1285    523   -890       C  
ATOM   5288  O   HIS A 646      -7.205 -30.669 -66.884  1.00 43.64           O  
ANISOU 5288  O   HIS A 646     6238   5968   4375  -1304    538   -893       O  
ATOM   5289  CB  HIS A 646      -8.403 -33.847 -66.835  1.00 46.02           C  
ANISOU 5289  CB  HIS A 646     6526   6195   4766  -1396    650  -1045       C  
ATOM   5290  CG  HIS A 646      -8.242 -33.686 -68.317  1.00 47.58           C  
ANISOU 5290  CG  HIS A 646     6768   6458   4853  -1513    690  -1109       C  
ATOM   5291  ND1 HIS A 646      -9.090 -34.292 -69.221  1.00 50.88           N  
ANISOU 5291  ND1 HIS A 646     7213   6935   5183  -1624    704  -1166       N  
ATOM   5292  CD2 HIS A 646      -7.345 -32.989 -69.055  1.00 49.72           C  
ANISOU 5292  CD2 HIS A 646     7064   6747   5080  -1542    719  -1124       C  
ATOM   5293  CE1 HIS A 646      -8.719 -33.980 -70.450  1.00 49.59           C  
ANISOU 5293  CE1 HIS A 646     7093   6827   4924  -1721    740  -1214       C  
ATOM   5294  NE2 HIS A 646      -7.664 -33.188 -70.378  1.00 51.04           N  
ANISOU 5294  NE2 HIS A 646     7276   6987   5133  -1672    751  -1189       N  
ATOM   5295  N   TRP A 647      -9.135 -30.958 -65.763  1.00 43.22           N  
ANISOU 5295  N   TRP A 647     6154   5946   4323  -1258    433   -816       N  
ATOM   5296  CA  TRP A 647      -9.488 -29.529 -65.876  1.00 43.22           C  
ANISOU 5296  CA  TRP A 647     6158   6017   4246  -1239    348   -730       C  
ATOM   5297  C   TRP A 647      -8.606 -28.617 -65.016  1.00 41.17           C  
ANISOU 5297  C   TRP A 647     5882   5712   4048  -1140    329   -673       C  
ATOM   5298  O   TRP A 647      -8.406 -27.450 -65.362  1.00 42.03           O  
ANISOU 5298  O   TRP A 647     6001   5865   4103  -1135    290   -626       O  
ATOM   5299  CB  TRP A 647     -10.995 -29.240 -65.680  1.00 44.37           C  
ANISOU 5299  CB  TRP A 647     6291   6227   4340  -1242    261   -666       C  
ATOM   5300  CG  TRP A 647     -11.572 -29.412 -64.274  1.00 43.34           C  
ANISOU 5300  CG  TRP A 647     6126   6052   4289  -1152    224   -616       C  
ATOM   5301  CD1 TRP A 647     -12.334 -30.452 -63.831  1.00 45.91           C  
ANISOU 5301  CD1 TRP A 647     6437   6356   4651  -1158    233   -639       C  
ATOM   5302  CD2 TRP A 647     -11.471 -28.495 -63.167  1.00 41.55           C  
ANISOU 5302  CD2 TRP A 647     5878   5802   4109  -1053    174   -537       C  
ATOM   5303  NE1 TRP A 647     -12.694 -30.259 -62.518  1.00 43.34           N  
ANISOU 5303  NE1 TRP A 647     6083   5995   4389  -1069    194   -578       N  
ATOM   5304  CE2 TRP A 647     -12.178 -29.067 -62.085  1.00 41.58           C  
ANISOU 5304  CE2 TRP A 647     5856   5771   4172  -1006    158   -517       C  
ATOM   5305  CE3 TRP A 647     -10.841 -27.255 -62.982  1.00 39.19           C  
ANISOU 5305  CE3 TRP A 647     5579   5507   3806  -1004    146   -484       C  
ATOM   5306  CZ2 TRP A 647     -12.270 -28.445 -60.835  1.00 41.89           C  
ANISOU 5306  CZ2 TRP A 647     5875   5781   4261   -916    118   -450       C  
ATOM   5307  CZ3 TRP A 647     -10.932 -26.637 -61.744  1.00 38.44           C  
ANISOU 5307  CZ3 TRP A 647     5461   5381   3764   -913    105   -419       C  
ATOM   5308  CH2 TRP A 647     -11.644 -27.231 -60.685  1.00 40.73           C  
ANISOU 5308  CH2 TRP A 647     5730   5639   4107   -873     92   -403       C  
ATOM   5309  N   VAL A 648      -8.070 -29.148 -63.914  1.00 39.90           N  
ANISOU 5309  N   VAL A 648     5696   5465   3999  -1066    355   -675       N  
ATOM   5310  CA  VAL A 648      -7.113 -28.388 -63.104  1.00 37.25           C  
ANISOU 5310  CA  VAL A 648     5345   5083   3724   -981    343   -629       C  
ATOM   5311  C   VAL A 648      -5.835 -28.130 -63.908  1.00 38.01           C  
ANISOU 5311  C   VAL A 648     5457   5164   3819  -1010    402   -673       C  
ATOM   5312  O   VAL A 648      -5.346 -26.999 -63.944  1.00 37.95           O  
ANISOU 5312  O   VAL A 648     5455   5176   3789   -982    373   -629       O  
ATOM   5313  CB  VAL A 648      -6.800 -29.057 -61.750  1.00 35.24           C  
ANISOU 5313  CB  VAL A 648     5060   4743   3586   -905    353   -617       C  
ATOM   5314  CG1 VAL A 648      -5.696 -28.295 -61.027  1.00 30.35           C  
ANISOU 5314  CG1 VAL A 648     4427   4079   3024   -832    343   -576       C  
ATOM   5315  CG2 VAL A 648      -8.048 -29.101 -60.881  1.00 34.18           C  
ANISOU 5315  CG2 VAL A 648     4913   4628   3448   -872    290   -564       C  
ATOM   5316  N   ASP A 649      -5.317 -29.172 -64.560  1.00 39.49           N  
ANISOU 5316  N   ASP A 649     5653   5316   4034  -1068    489   -762       N  
ATOM   5317  CA  ASP A 649      -4.200 -29.033 -65.511  1.00 42.72           C  
ANISOU 5317  CA  ASP A 649     6082   5716   4435  -1114    560   -819       C  
ATOM   5318  C   ASP A 649      -4.542 -28.014 -66.584  1.00 41.78           C  
ANISOU 5318  C   ASP A 649     5997   5694   4181  -1177    524   -799       C  
ATOM   5319  O   ASP A 649      -3.723 -27.152 -66.903  1.00 42.35           O  
ANISOU 5319  O   ASP A 649     6079   5773   4239  -1169    529   -784       O  
ATOM   5320  CB  ASP A 649      -3.845 -30.380 -66.192  1.00 45.03           C  
ANISOU 5320  CB  ASP A 649     6381   5964   4766  -1186    667   -928       C  
ATOM   5321  CG  ASP A 649      -2.999 -31.303 -65.304  1.00 48.80           C  
ANISOU 5321  CG  ASP A 649     6816   6324   5400  -1125    724   -951       C  
ATOM   5322  OD1 ASP A 649      -2.507 -30.863 -64.242  1.00 49.85           O  
ANISOU 5322  OD1 ASP A 649     6920   6414   5606  -1033    685   -886       O  
ATOM   5323  OD2 ASP A 649      -2.828 -32.484 -65.675  1.00 52.07           O  
ANISOU 5323  OD2 ASP A 649     7227   6690   5867  -1172    810  -1034       O  
ATOM   5324  N   PHE A 650      -5.750 -28.116 -67.135  1.00 41.08           N  
ANISOU 5324  N   PHE A 650     5928   5683   3999  -1240    485   -795       N  
ATOM   5325  CA  PHE A 650      -6.190 -27.207 -68.192  1.00 42.13           C  
ANISOU 5325  CA  PHE A 650     6092   5914   4001  -1310    441   -767       C  
ATOM   5326  C   PHE A 650      -6.188 -25.746 -67.732  1.00 41.12           C  
ANISOU 5326  C   PHE A 650     5952   5813   3859  -1239    360   -665       C  
ATOM   5327  O   PHE A 650      -5.712 -24.871 -68.455  1.00 42.01           O  
ANISOU 5327  O   PHE A 650     6086   5964   3912  -1268    356   -649       O  
ATOM   5328  CB  PHE A 650      -7.564 -27.609 -68.732  1.00 41.63           C  
ANISOU 5328  CB  PHE A 650     6041   5926   3851  -1386    401   -768       C  
ATOM   5329  CG  PHE A 650      -8.151 -26.617 -69.694  1.00 45.55           C  
ANISOU 5329  CG  PHE A 650     6561   6528   4217  -1452    336   -716       C  
ATOM   5330  CD1 PHE A 650      -7.654 -26.502 -70.988  1.00 51.10           C  
ANISOU 5330  CD1 PHE A 650     7307   7278   4831  -1553    380   -765       C  
ATOM   5331  CD2 PHE A 650      -9.205 -25.798 -69.309  1.00 48.26           C  
ANISOU 5331  CD2 PHE A 650     6884   6923   4531  -1415    232   -616       C  
ATOM   5332  CE1 PHE A 650      -8.197 -25.584 -71.887  1.00 52.48           C  
ANISOU 5332  CE1 PHE A 650     7504   7554   4883  -1619    314   -707       C  
ATOM   5333  CE2 PHE A 650      -9.752 -24.875 -70.198  1.00 50.12           C  
ANISOU 5333  CE2 PHE A 650     7135   7253   4657  -1475    167   -557       C  
ATOM   5334  CZ  PHE A 650      -9.242 -24.767 -71.490  1.00 51.59           C  
ANISOU 5334  CZ  PHE A 650     7364   7489   4749  -1578    204   -599       C  
ATOM   5335  N   LEU A 651      -6.699 -25.487 -66.531  1.00 41.30           N  
ANISOU 5335  N   LEU A 651     5942   5811   3938  -1150    300   -599       N  
ATOM   5336  CA  LEU A 651      -6.702 -24.121 -65.992  1.00 41.59           C  
ANISOU 5336  CA  LEU A 651     5965   5863   3973  -1081    231   -508       C  
ATOM   5337  C   LEU A 651      -5.298 -23.633 -65.647  1.00 41.21           C  
ANISOU 5337  C   LEU A 651     5913   5757   3988  -1027    266   -511       C  
ATOM   5338  O   LEU A 651      -4.950 -22.488 -65.952  1.00 41.40           O  
ANISOU 5338  O   LEU A 651     5944   5809   3975  -1019    240   -467       O  
ATOM   5339  CB  LEU A 651      -7.657 -23.975 -64.800  1.00 40.94           C  
ANISOU 5339  CB  LEU A 651     5852   5771   3933  -1008    165   -443       C  
ATOM   5340  CG  LEU A 651      -9.164 -24.072 -65.059  1.00 39.78           C  
ANISOU 5340  CG  LEU A 651     5700   5689   3724  -1048    108   -412       C  
ATOM   5341  CD1 LEU A 651      -9.922 -23.771 -63.783  1.00 39.09           C  
ANISOU 5341  CD1 LEU A 651     5580   5581   3692   -965     54   -347       C  
ATOM   5342  CD2 LEU A 651      -9.608 -23.119 -66.170  1.00 41.89           C  
ANISOU 5342  CD2 LEU A 651     5983   6046   3889  -1110     60   -368       C  
ATOM   5343  N   ASP A 652      -4.496 -24.511 -65.042  1.00 41.72           N  
ANISOU 5343  N   ASP A 652     5963   5738   4150   -993    326   -560       N  
ATOM   5344  CA  ASP A 652      -3.082 -24.230 -64.762  1.00 42.93           C  
ANISOU 5344  CA  ASP A 652     6108   5829   4375   -949    368   -571       C  
ATOM   5345  C   ASP A 652      -2.349 -23.812 -66.043  1.00 43.81           C  
ANISOU 5345  C   ASP A 652     6249   5972   4425  -1018    414   -609       C  
ATOM   5346  O   ASP A 652      -1.653 -22.793 -66.069  1.00 39.93           O  
ANISOU 5346  O   ASP A 652     5759   5482   3932   -990    402   -574       O  
ATOM   5347  CB  ASP A 652      -2.410 -25.457 -64.119  1.00 44.30           C  
ANISOU 5347  CB  ASP A 652     6258   5911   4664   -922    431   -624       C  
ATOM   5348  CG  ASP A 652      -0.943 -25.215 -63.758  1.00 48.68           C  
ANISOU 5348  CG  ASP A 652     6794   6396   5306   -875    469   -629       C  
ATOM   5349  OD1 ASP A 652      -0.615 -24.167 -63.161  1.00 48.75           O  
ANISOU 5349  OD1 ASP A 652     6794   6405   5324   -816    420   -566       O  
ATOM   5350  OD2 ASP A 652      -0.106 -26.087 -64.073  1.00 52.85           O  
ANISOU 5350  OD2 ASP A 652     7314   6865   5901   -898    552   -698       O  
ATOM   5351  N   LYS A 653      -2.532 -24.595 -67.106  1.00 45.27           N  
ANISOU 5351  N   LYS A 653     6459   6183   4557  -1112    469   -682       N  
ATOM   5352  CA  LYS A 653      -1.927 -24.294 -68.404  1.00 46.82           C  
ANISOU 5352  CA  LYS A 653     6691   6417   4682  -1194    520   -726       C  
ATOM   5353  C   LYS A 653      -2.476 -22.985 -68.980  1.00 46.32           C  
ANISOU 5353  C   LYS A 653     6648   6445   4506  -1219    444   -651       C  
ATOM   5354  O   LYS A 653      -1.713 -22.147 -69.438  1.00 46.74           O  
ANISOU 5354  O   LYS A 653     6715   6509   4537  -1225    455   -638       O  
ATOM   5355  CB  LYS A 653      -2.128 -25.455 -69.380  1.00 46.81           C  
ANISOU 5355  CB  LYS A 653     6716   6428   4641  -1300    595   -823       C  
ATOM   5356  CG  LYS A 653      -1.358 -25.306 -70.693  1.00 52.14           C  
ANISOU 5356  CG  LYS A 653     7431   7130   5251  -1393    669   -886       C  
ATOM   5357  CD  LYS A 653      -1.523 -26.536 -71.599  1.00 54.79           C  
ANISOU 5357  CD  LYS A 653     7794   7470   5552  -1503    756   -994       C  
ATOM   5358  CE  LYS A 653      -0.752 -26.368 -72.914  1.00 59.63           C  
ANISOU 5358  CE  LYS A 653     8452   8112   6094  -1604    837  -1062       C  
ATOM   5359  NZ  LYS A 653      -0.752 -27.611 -73.755  1.00 64.24           N  
ANISOU 5359  NZ  LYS A 653     9063   8686   6658  -1714    941  -1183       N  
ATOM   5360  N   PHE A 654      -3.794 -22.808 -68.934  1.00 46.64           N  
ANISOU 5360  N   PHE A 654     6688   6548   4486  -1230    366   -598       N  
ATOM   5361  CA  PHE A 654      -4.409 -21.574 -69.411  1.00 47.89           C  
ANISOU 5361  CA  PHE A 654     6856   6787   4553  -1248    287   -515       C  
ATOM   5362  C   PHE A 654      -3.935 -20.318 -68.645  1.00 46.91           C  
ANISOU 5362  C   PHE A 654     6709   6637   4476  -1153    242   -437       C  
ATOM   5363  O   PHE A 654      -3.725 -19.265 -69.248  1.00 47.02           O  
ANISOU 5363  O   PHE A 654     6736   6694   4434  -1173    218   -393       O  
ATOM   5364  CB  PHE A 654      -5.942 -21.679 -69.400  1.00 47.89           C  
ANISOU 5364  CB  PHE A 654     6847   6849   4499  -1271    211   -469       C  
ATOM   5365  CG  PHE A 654      -6.629 -20.488 -70.013  1.00 48.75           C  
ANISOU 5365  CG  PHE A 654     6962   7043   4518  -1300    130   -380       C  
ATOM   5366  CD1 PHE A 654      -7.132 -19.468 -69.211  1.00 48.46           C  
ANISOU 5366  CD1 PHE A 654     6891   7005   4516  -1218     53   -283       C  
ATOM   5367  CD2 PHE A 654      -6.752 -20.376 -71.391  1.00 50.75           C  
ANISOU 5367  CD2 PHE A 654     7252   7376   4655  -1415    132   -392       C  
ATOM   5368  CE1 PHE A 654      -7.754 -18.363 -69.773  1.00 47.60           C  
ANISOU 5368  CE1 PHE A 654     6779   6966   4340  -1242    -21   -196       C  
ATOM   5369  CE2 PHE A 654      -7.374 -19.272 -71.959  1.00 51.27           C  
ANISOU 5369  CE2 PHE A 654     7318   7519   4643  -1443     50   -299       C  
ATOM   5370  CZ  PHE A 654      -7.871 -18.265 -71.148  1.00 47.45           C  
ANISOU 5370  CZ  PHE A 654     6794   7026   4207  -1354    -26   -199       C  
ATOM   5371  N   ALA A 655      -3.770 -20.434 -67.330  1.00 44.98           N  
ANISOU 5371  N   ALA A 655     6432   6324   4334  -1057    233   -421       N  
ATOM   5372  CA  ALA A 655      -3.286 -19.316 -66.515  1.00 45.05           C  
ANISOU 5372  CA  ALA A 655     6420   6303   4393   -970    197   -357       C  
ATOM   5373  C   ALA A 655      -1.811 -19.039 -66.762  1.00 45.27           C  
ANISOU 5373  C   ALA A 655     6456   6290   4454   -964    257   -390       C  
ATOM   5374  O   ALA A 655      -1.411 -17.886 -66.892  1.00 44.10           O  
ANISOU 5374  O   ALA A 655     6310   6156   4290   -945    233   -343       O  
ATOM   5375  CB  ALA A 655      -3.531 -19.573 -65.039  1.00 41.79           C  
ANISOU 5375  CB  ALA A 655     5975   5833   4070   -881    172   -333       C  
ATOM   5376  N   ARG A 656      -1.013 -20.100 -66.846  1.00 46.68           N  
ANISOU 5376  N   ARG A 656     6636   6414   4685   -982    337   -472       N  
ATOM   5377  CA  ARG A 656       0.422 -19.964 -67.059  1.00 49.67           C  
ANISOU 5377  CA  ARG A 656     7016   6744   5113   -976    402   -510       C  
ATOM   5378  C   ARG A 656       0.811 -19.532 -68.480  1.00 49.54           C  
ANISOU 5378  C   ARG A 656     7037   6780   5007  -1064    439   -536       C  
ATOM   5379  O   ARG A 656       1.842 -18.891 -68.657  1.00 51.47           O  
ANISOU 5379  O   ARG A 656     7282   7002   5271  -1051    467   -536       O  
ATOM   5380  CB  ARG A 656       1.154 -21.254 -66.656  1.00 52.10           C  
ANISOU 5380  CB  ARG A 656     7304   6968   5524   -964    478   -584       C  
ATOM   5381  CG  ARG A 656       2.688 -21.179 -66.733  1.00 60.32           C  
ANISOU 5381  CG  ARG A 656     8334   7944   6642   -949    547   -621       C  
ATOM   5382  CD  ARG A 656       3.363 -22.522 -66.418  1.00 66.55           C  
ANISOU 5382  CD  ARG A 656     9096   8645   7543   -942    626   -692       C  
ATOM   5383  NE  ARG A 656       2.930 -23.597 -67.315  1.00 69.44           N  
ANISOU 5383  NE  ARG A 656     9485   9027   7871  -1029    690   -772       N  
ATOM   5384  CZ  ARG A 656       2.097 -24.574 -66.965  1.00 67.77           C  
ANISOU 5384  CZ  ARG A 656     9267   8809   7675  -1034    684   -789       C  
ATOM   5385  NH1 ARG A 656       1.614 -24.626 -65.732  1.00 67.02           N  
ANISOU 5385  NH1 ARG A 656     9142   8690   7631   -957    619   -730       N  
ATOM   5386  NH2 ARG A 656       1.752 -25.503 -67.846  1.00 68.65           N  
ANISOU 5386  NH2 ARG A 656     9401   8935   7748  -1121    747   -867       N  
ATOM   5387  N   GLU A 657      -0.002 -19.864 -69.483  1.00 49.00           N  
ANISOU 5387  N   GLU A 657     7000   6782   4836  -1156    439   -558       N  
ATOM   5388  CA  GLU A 657       0.387 -19.620 -70.880  1.00 49.88           C  
ANISOU 5388  CA  GLU A 657     7153   6946   4854  -1256    484   -593       C  
ATOM   5389  C   GLU A 657      -0.395 -18.519 -71.596  1.00 48.97           C  
ANISOU 5389  C   GLU A 657     7060   6928   4619  -1300    406   -514       C  
ATOM   5390  O   GLU A 657       0.070 -17.989 -72.595  1.00 48.58           O  
ANISOU 5390  O   GLU A 657     7041   6918   4497  -1366    430   -519       O  
ATOM   5391  CB  GLU A 657       0.341 -20.919 -71.697  1.00 52.28           C  
ANISOU 5391  CB  GLU A 657     7484   7254   5128  -1353    566   -696       C  
ATOM   5392  CG  GLU A 657       1.516 -21.849 -71.432  1.00 56.26           C  
ANISOU 5392  CG  GLU A 657     7971   7658   5747  -1334    673   -786       C  
ATOM   5393  CD  GLU A 657       1.378 -23.209 -72.094  1.00 60.98           C  
ANISOU 5393  CD  GLU A 657     8588   8247   6333  -1422    759   -891       C  
ATOM   5394  OE1 GLU A 657       0.651 -23.325 -73.108  1.00 63.49           O  
ANISOU 5394  OE1 GLU A 657     8949   8648   6528  -1526    755   -911       O  
ATOM   5395  OE2 GLU A 657       2.010 -24.168 -71.597  1.00 60.90           O  
ANISOU 5395  OE2 GLU A 657     8550   8147   6442  -1390    831   -953       O  
ATOM   5396  N   ARG A 658      -1.577 -18.183 -71.091  1.00 47.72           N  
ANISOU 5396  N   ARG A 658     6883   6805   4444  -1266    315   -438       N  
ATOM   5397  CA  ARG A 658      -2.406 -17.159 -71.717  1.00 48.28           C  
ANISOU 5397  CA  ARG A 658     6964   6963   4417  -1304    234   -352       C  
ATOM   5398  C   ARG A 658      -2.590 -15.941 -70.814  1.00 46.96           C  
ANISOU 5398  C   ARG A 658     6762   6780   4301  -1204    160   -253       C  
ATOM   5399  O   ARG A 658      -2.367 -14.802 -71.225  1.00 47.17           O  
ANISOU 5399  O   ARG A 658     6794   6836   4293  -1208    131   -193       O  
ATOM   5400  CB  ARG A 658      -3.771 -17.738 -72.113  1.00 48.82           C  
ANISOU 5400  CB  ARG A 658     7039   7098   4412  -1369    188   -343       C  
ATOM   5401  CG  ARG A 658      -3.711 -18.812 -73.186  1.00 54.40           C  
ANISOU 5401  CG  ARG A 658     7787   7837   5044  -1489    257   -438       C  
ATOM   5402  CD  ARG A 658      -3.659 -18.211 -74.593  1.00 60.19           C  
ANISOU 5402  CD  ARG A 658     8565   8659   5646  -1601    250   -421       C  
ATOM   5403  NE  ARG A 658      -3.530 -19.246 -75.618  1.00 67.48           N  
ANISOU 5403  NE  ARG A 658     9533   9611   6493  -1725    327   -523       N  
ATOM   5404  CZ  ARG A 658      -2.377 -19.619 -76.173  1.00 71.18           C  
ANISOU 5404  CZ  ARG A 658    10033  10048   6963  -1772    433   -615       C  
ATOM   5405  NH1 ARG A 658      -1.236 -19.043 -75.812  1.00 73.54           N  
ANISOU 5405  NH1 ARG A 658    10320  10286   7336  -1704    471   -613       N  
ATOM   5406  NH2 ARG A 658      -2.362 -20.571 -77.096  1.00 74.19           N  
ANISOU 5406  NH2 ARG A 658    10456  10457   7274  -1890    506   -711       N  
ATOM   5407  N   MET A 659      -2.991 -16.184 -69.575  1.00 45.29           N  
ANISOU 5407  N   MET A 659     6515   6519   4173  -1118    134   -236       N  
ATOM   5408  CA  MET A 659      -3.328 -15.084 -68.679  1.00 44.60           C  
ANISOU 5408  CA  MET A 659     6395   6418   4132  -1031     66   -148       C  
ATOM   5409  C   MET A 659      -2.124 -14.335 -68.114  1.00 44.67           C  
ANISOU 5409  C   MET A 659     6395   6368   4210   -963     90   -141       C  
ATOM   5410  O   MET A 659      -2.068 -13.099 -68.194  1.00 45.09           O  
ANISOU 5410  O   MET A 659     6442   6436   4252   -941     52    -73       O  
ATOM   5411  CB  MET A 659      -4.258 -15.565 -67.583  1.00 43.29           C  
ANISOU 5411  CB  MET A 659     6199   6227   4021   -973     30   -132       C  
ATOM   5412  CG  MET A 659      -5.641 -15.848 -68.118  1.00 44.90           C  
ANISOU 5412  CG  MET A 659     6403   6502   4157  -1032    -20   -104       C  
ATOM   5413  SD  MET A 659      -6.797 -16.179 -66.814  1.00 49.01           S  
ANISOU 5413  SD  MET A 659     6883   6994   4744   -960    -66    -72       S  
ATOM   5414  CE  MET A 659      -6.942 -14.562 -66.043  1.00 48.87           C  
ANISOU 5414  CE  MET A 659     6834   6961   4775   -873   -124     28       C  
ATOM   5415  N   GLU A 660      -1.161 -15.078 -67.572  1.00 43.73           N  
ANISOU 5415  N   GLU A 660     6273   6179   4165   -932    153   -209       N  
ATOM   5416  CA  GLU A 660       0.033 -14.469 -66.988  1.00 44.88           C  
ANISOU 5416  CA  GLU A 660     6406   6265   4382   -870    176   -206       C  
ATOM   5417  C   GLU A 660       0.812 -13.595 -67.990  1.00 45.90           C  
ANISOU 5417  C   GLU A 660     6557   6421   4463   -912    198   -198       C  
ATOM   5418  O   GLU A 660       1.198 -12.484 -67.634  1.00 45.07           O  
ANISOU 5418  O   GLU A 660     6440   6301   4384   -863    172   -146       O  
ATOM   5419  CB  GLU A 660       0.923 -15.507 -66.285  1.00 44.46           C  
ANISOU 5419  CB  GLU A 660     6340   6133   4422   -836    237   -276       C  
ATOM   5420  CG  GLU A 660       0.343 -15.996 -64.945  1.00 44.96           C  
ANISOU 5420  CG  GLU A 660     6375   6157   4552   -768    203   -260       C  
ATOM   5421  CD  GLU A 660       1.240 -16.989 -64.196  1.00 49.13           C  
ANISOU 5421  CD  GLU A 660     6884   6605   5178   -733    254   -314       C  
ATOM   5422  OE1 GLU A 660       2.456 -17.076 -64.482  1.00 51.61           O  
ANISOU 5422  OE1 GLU A 660     7198   6880   5533   -740    310   -353       O  
ATOM   5423  OE2 GLU A 660       0.724 -17.684 -63.297  1.00 51.97           O  
ANISOU 5423  OE2 GLU A 660     7227   6938   5582   -700    237   -313       O  
ATOM   5424  N   PRO A 661       1.014 -14.070 -69.245  1.00 48.09           N  
ANISOU 5424  N   PRO A 661     6868   6738   4667  -1006    246   -248       N  
ATOM   5425  CA  PRO A 661       1.632 -13.180 -70.249  1.00 47.76           C  
ANISOU 5425  CA  PRO A 661     6851   6730   4565  -1055    262   -232       C  
ATOM   5426  C   PRO A 661       0.839 -11.887 -70.491  1.00 48.81           C  
ANISOU 5426  C   PRO A 661     6981   6923   4641  -1053    178   -127       C  
ATOM   5427  O   PRO A 661       1.437 -10.813 -70.645  1.00 49.12           O  
ANISOU 5427  O   PRO A 661     7020   6959   4683  -1036    172    -86       O  
ATOM   5428  CB  PRO A 661       1.657 -14.039 -71.516  1.00 48.98           C  
ANISOU 5428  CB  PRO A 661     7047   6929   4636  -1169    321   -303       C  
ATOM   5429  CG  PRO A 661       1.698 -15.440 -71.019  1.00 49.37           C  
ANISOU 5429  CG  PRO A 661     7085   6927   4746  -1160    371   -383       C  
ATOM   5430  CD  PRO A 661       0.885 -15.454 -69.750  1.00 47.44           C  
ANISOU 5430  CD  PRO A 661     6804   6659   4563  -1073    303   -333       C  
ATOM   5431  N   ALA A 662      -0.490 -11.987 -70.510  1.00 48.28           N  
ANISOU 5431  N   ALA A 662     6907   6906   4531  -1069    114    -82       N  
ATOM   5432  CA  ALA A 662      -1.347 -10.811 -70.682  1.00 47.11           C  
ANISOU 5432  CA  ALA A 662     6745   6807   4345  -1063     31     24       C  
ATOM   5433  C   ALA A 662      -1.251  -9.861 -69.485  1.00 46.16           C  
ANISOU 5433  C   ALA A 662     6588   6632   4319   -954     -3     81       C  
ATOM   5434  O   ALA A 662      -1.229  -8.635 -69.654  1.00 46.09           O  
ANISOU 5434  O   ALA A 662     6570   6636   4306   -939    -38    154       O  
ATOM   5435  CB  ALA A 662      -2.801 -11.230 -70.927  1.00 47.00           C  
ANISOU 5435  CB  ALA A 662     6726   6854   4278  -1105    -28     57       C  
ATOM   5436  N   ILE A 663      -1.195 -10.444 -68.285  1.00 43.42           N  
ANISOU 5436  N   ILE A 663     6220   6224   4056   -884      9     46       N  
ATOM   5437  CA  ILE A 663      -1.050  -9.705 -67.037  1.00 38.77           C  
ANISOU 5437  CA  ILE A 663     5599   5578   3554   -787    -14     84       C  
ATOM   5438  C   ILE A 663       0.281  -8.941 -67.013  1.00 40.40           C  
ANISOU 5438  C   ILE A 663     5810   5746   3795   -762     21     78       C  
ATOM   5439  O   ILE A 663       0.317  -7.756 -66.669  1.00 40.80           O  
ANISOU 5439  O   ILE A 663     5844   5785   3872   -719    -10    138       O  
ATOM   5440  CB  ILE A 663      -1.212 -10.665 -65.818  1.00 39.12           C  
ANISOU 5440  CB  ILE A 663     5626   5569   3668   -733     -3     41       C  
ATOM   5441  CG1 ILE A 663      -2.692 -11.013 -65.630  1.00 36.07           C  
ANISOU 5441  CG1 ILE A 663     5226   5218   3261   -739    -53     73       C  
ATOM   5442  CG2 ILE A 663      -0.616 -10.076 -64.520  1.00 28.72           C  
ANISOU 5442  CG2 ILE A 663     4288   4186   2440   -645     -5     54       C  
ATOM   5443  CD1 ILE A 663      -2.933 -12.124 -64.649  1.00 39.56           C  
ANISOU 5443  CD1 ILE A 663     5658   5619   3754   -706    -39     27       C  
ATOM   5444  N   ASP A 664       1.362  -9.621 -67.394  1.00 40.53           N  
ANISOU 5444  N   ASP A 664     5846   5740   3815   -792     89      3       N  
ATOM   5445  CA  ASP A 664       2.676  -8.998 -67.526  1.00 40.63           C  
ANISOU 5445  CA  ASP A 664     5863   5719   3857   -779    129     -9       C  
ATOM   5446  C   ASP A 664       2.643  -7.784 -68.478  1.00 40.58           C  
ANISOU 5446  C   ASP A 664     5869   5761   3787   -817    105     54       C  
ATOM   5447  O   ASP A 664       3.105  -6.702 -68.114  1.00 41.49           O  
ANISOU 5447  O   ASP A 664     5971   5851   3943   -771     92     96       O  
ATOM   5448  CB  ASP A 664       3.726 -10.025 -67.981  1.00 41.59           C  
ANISOU 5448  CB  ASP A 664     6000   5812   3989   -819    212   -101       C  
ATOM   5449  CG  ASP A 664       3.912 -11.177 -66.985  1.00 46.25           C  
ANISOU 5449  CG  ASP A 664     6571   6342   4660   -776    236   -156       C  
ATOM   5450  OD1 ASP A 664       4.224 -12.300 -67.437  1.00 51.68           O  
ANISOU 5450  OD1 ASP A 664     7270   7019   5347   -822    295   -228       O  
ATOM   5451  OD2 ASP A 664       3.753 -10.979 -65.759  1.00 44.99           O  
ANISOU 5451  OD2 ASP A 664     6385   6144   4565   -702    199   -127       O  
ATOM   5452  N   ARG A 665       2.083  -7.955 -69.678  1.00 39.34           N  
ANISOU 5452  N   ARG A 665     5740   5677   3533   -903     98     63       N  
ATOM   5453  CA  ARG A 665       1.995  -6.857 -70.649  1.00 40.54           C  
ANISOU 5453  CA  ARG A 665     5904   5881   3617   -949     71    132       C  
ATOM   5454  C   ARG A 665       1.260  -5.649 -70.056  1.00 39.20           C  
ANISOU 5454  C   ARG A 665     5700   5709   3483   -887     -3    232       C  
ATOM   5455  O   ARG A 665       1.736  -4.513 -70.153  1.00 37.48           O  
ANISOU 5455  O   ARG A 665     5477   5481   3282   -867    -10    281       O  
ATOM   5456  CB  ARG A 665       1.320  -7.307 -71.955  1.00 42.16           C  
ANISOU 5456  CB  ARG A 665     6142   6172   3703  -1059     62    134       C  
ATOM   5457  CG  ARG A 665       2.196  -8.169 -72.861  1.00 47.08           C  
ANISOU 5457  CG  ARG A 665     6808   6805   4276  -1141    147     40       C  
ATOM   5458  CD  ARG A 665       1.544  -8.441 -74.218  1.00 49.66           C  
ANISOU 5458  CD  ARG A 665     7174   7225   4471  -1263    135     48       C  
ATOM   5459  NE  ARG A 665       0.382  -9.332 -74.132  1.00 55.47           N  
ANISOU 5459  NE  ARG A 665     7906   7995   5177  -1288    100     39       N  
ATOM   5460  CZ  ARG A 665       0.438 -10.667 -74.145  1.00 55.45           C  
ANISOU 5460  CZ  ARG A 665     7918   7978   5173  -1320    156    -57       C  
ATOM   5461  NH1 ARG A 665       1.606 -11.301 -74.233  1.00 54.16           N  
ANISOU 5461  NH1 ARG A 665     7771   7764   5042  -1331    252   -153       N  
ATOM   5462  NH2 ARG A 665      -0.683 -11.375 -74.071  1.00 52.56           N  
ANISOU 5462  NH2 ARG A 665     7547   7645   4779  -1343    118    -55       N  
ATOM   5463  N   GLY A 666       0.107  -5.910 -69.440  1.00 38.01           N  
ANISOU 5463  N   GLY A 666     5526   5564   3350   -858    -53    260       N  
ATOM   5464  CA  GLY A 666      -0.670  -4.889 -68.744  1.00 37.66           C  
ANISOU 5464  CA  GLY A 666     5444   5507   3357   -795   -113    346       C  
ATOM   5465  C   GLY A 666       0.120  -4.141 -67.679  1.00 38.47           C  
ANISOU 5465  C   GLY A 666     5528   5536   3554   -709    -96    345       C  
ATOM   5466  O   GLY A 666      -0.009  -2.919 -67.542  1.00 39.19           O  
ANISOU 5466  O   GLY A 666     5598   5618   3675   -678   -125    415       O  
ATOM   5467  N   PHE A 667       0.951  -4.863 -66.930  1.00 36.96           N  
ANISOU 5467  N   PHE A 667     5340   5291   3410   -676    -49    268       N  
ATOM   5468  CA  PHE A 667       1.731  -4.236 -65.858  1.00 35.61           C  
ANISOU 5468  CA  PHE A 667     5152   5053   3324   -602    -35    263       C  
ATOM   5469  C   PHE A 667       2.970  -3.513 -66.375  1.00 37.33           C  
ANISOU 5469  C   PHE A 667     5382   5256   3544   -613      0    259       C  
ATOM   5470  O   PHE A 667       3.358  -2.487 -65.808  1.00 34.74           O  
ANISOU 5470  O   PHE A 667     5038   4892   3270   -564     -7    290       O  
ATOM   5471  CB  PHE A 667       2.099  -5.238 -64.759  1.00 33.29           C  
ANISOU 5471  CB  PHE A 667     4853   4707   3087   -560    -10    195       C  
ATOM   5472  CG  PHE A 667       1.092  -5.315 -63.639  1.00 32.18           C  
ANISOU 5472  CG  PHE A 667     4691   4551   2987   -510    -48    218       C  
ATOM   5473  CD1 PHE A 667       0.654  -4.155 -62.990  1.00 26.99           C  
ANISOU 5473  CD1 PHE A 667     4011   3876   2370   -462    -80    276       C  
ATOM   5474  CD2 PHE A 667       0.595  -6.552 -63.214  1.00 30.35           C  
ANISOU 5474  CD2 PHE A 667     4459   4318   2756   -512    -45    176       C  
ATOM   5475  CE1 PHE A 667      -0.270  -4.220 -61.953  1.00 24.75           C  
ANISOU 5475  CE1 PHE A 667     3707   3574   2123   -420   -106    291       C  
ATOM   5476  CE2 PHE A 667      -0.322  -6.630 -62.163  1.00 23.79           C  
ANISOU 5476  CE2 PHE A 667     3609   3470   1960   -468    -75    195       C  
ATOM   5477  CZ  PHE A 667      -0.755  -5.456 -61.535  1.00 25.15           C  
ANISOU 5477  CZ  PHE A 667     3761   3627   2169   -424   -105    251       C  
ATOM   5478  N   ARG A 668       3.584  -4.042 -67.438  1.00 39.35           N  
ANISOU 5478  N   ARG A 668     5667   5540   3743   -679     42    217       N  
ATOM   5479  CA AARG A 668       4.712  -3.368 -68.083  0.50 41.01           C  
ANISOU 5479  CA AARG A 668     5890   5743   3947   -701     79    215       C  
ATOM   5480  CA BARG A 668       4.709  -3.367 -68.082  0.50 41.02           C  
ANISOU 5480  CA BARG A 668     5892   5744   3948   -701     79    215       C  
ATOM   5481  C   ARG A 668       4.273  -2.015 -68.629  1.00 41.76           C  
ANISOU 5481  C   ARG A 668     5981   5871   4014   -710     36    307       C  
ATOM   5482  O   ARG A 668       5.044  -1.050 -68.608  1.00 42.41           O  
ANISOU 5482  O   ARG A 668     6058   5926   4128   -689     49    329       O  
ATOM   5483  CB AARG A 668       5.311  -4.218 -69.207  0.50 42.88           C  
ANISOU 5483  CB AARG A 668     6162   6009   4121   -782    138    151       C  
ATOM   5484  CB BARG A 668       5.309  -4.226 -69.196  0.50 42.89           C  
ANISOU 5484  CB BARG A 668     6164   6010   4124   -781    138    151       C  
ATOM   5485  CG AARG A 668       5.918  -5.534 -68.747  0.50 44.49           C  
ANISOU 5485  CG AARG A 668     6366   6169   4370   -774    193     58       C  
ATOM   5486  CG BARG A 668       6.321  -5.244 -68.705  0.50 44.49           C  
ANISOU 5486  CG BARG A 668     6363   6155   4386   -764    202     59       C  
ATOM   5487  CD AARG A 668       6.919  -6.071 -69.752  0.50 45.39           C  
ANISOU 5487  CD AARG A 668     6508   6287   4453   -842    271    -10       C  
ATOM   5488  CD BARG A 668       7.142  -5.816 -69.846  0.50 45.41           C  
ANISOU 5488  CD BARG A 668     6511   6287   4457   -842    276     -5       C  
ATOM   5489  NE AARG A 668       6.476  -5.911 -71.135  0.50 49.19           N  
ANISOU 5489  NE AARG A 668     7024   6845   4820   -935    270     10       N  
ATOM   5490  NE BARG A 668       8.451  -6.278 -69.389  0.50 47.96           N  
ANISOU 5490  NE BARG A 668     6820   6538   4864   -813    340    -73       N  
ATOM   5491  CZ AARG A 668       5.843  -6.848 -71.833  0.50 49.62           C  
ANISOU 5491  CZ AARG A 668     7104   6949   4801  -1007    281    -24       C  
ATOM   5492  CZ BARG A 668       8.688  -7.487 -68.889  0.50 47.10           C  
ANISOU 5492  CZ BARG A 668     6699   6388   4808   -799    375   -139       C  
ATOM   5493  NH1AARG A 668       5.562  -8.019 -71.272  0.50 48.68           N  
ANISOU 5493  NH1AARG A 668     6975   6804   4716   -991    296    -80       N  
ATOM   5494  NH1BARG A 668       7.701  -8.368 -68.783  0.50 46.28           N  
ANISOU 5494  NH1BARG A 668     6600   6308   4677   -814    355   -152       N  
ATOM   5495  NH2AARG A 668       5.488  -6.611 -73.090  0.50 47.96           N  
ANISOU 5495  NH2AARG A 668     6929   6813   4480  -1099    276     -1       N  
ATOM   5496  NH2BARG A 668       9.913  -7.814 -68.499  0.50 44.10           N  
ANISOU 5496  NH2BARG A 668     6300   5942   4516   -773    430   -189       N  
ATOM   5497  N   GLU A 669       3.029  -1.954 -69.109  1.00 42.90           N  
ANISOU 5497  N   GLU A 669     6123   6072   4104   -743    -16    365       N  
ATOM   5498  CA  GLU A 669       2.436  -0.708 -69.613  1.00 44.10           C  
ANISOU 5498  CA  GLU A 669     6262   6255   4238   -752    -67    467       C  
ATOM   5499  C   GLU A 669       2.236   0.292 -68.472  1.00 41.23           C  
ANISOU 5499  C   GLU A 669     5859   5834   3971   -663    -93    513       C  
ATOM   5500  O   GLU A 669       2.463   1.483 -68.649  1.00 39.59           O  
ANISOU 5500  O   GLU A 669     5640   5616   3787   -650   -104    573       O  
ATOM   5501  CB  GLU A 669       1.106  -0.981 -70.349  1.00 46.49           C  
ANISOU 5501  CB  GLU A 669     6566   6632   4468   -809   -123    522       C  
ATOM   5502  CG  GLU A 669       0.453   0.250 -71.015  1.00 50.16           C  
ANISOU 5502  CG  GLU A 669     7012   7135   4913   -830   -182    640       C  
ATOM   5503  CD  GLU A 669      -0.872  -0.065 -71.723  1.00 53.16           C  
ANISOU 5503  CD  GLU A 669     7386   7588   5223   -890   -244    699       C  
ATOM   5504  OE1 GLU A 669      -0.905  -0.991 -72.562  1.00 58.24           O  
ANISOU 5504  OE1 GLU A 669     8067   8290   5773   -973   -232    657       O  
ATOM   5505  OE2 GLU A 669      -1.883   0.622 -71.453  1.00 51.56           O  
ANISOU 5505  OE2 GLU A 669     7142   7386   5063   -859   -304    788       O  
ATOM   5506  N   MET A 670       1.824  -0.203 -67.304  1.00 38.81           N  
ANISOU 5506  N   MET A 670     5534   5490   3721   -607    -99    483       N  
ATOM   5507  CA  MET A 670       1.596   0.661 -66.146  1.00 37.80           C  
ANISOU 5507  CA  MET A 670     5373   5308   3683   -529   -116    514       C  
ATOM   5508  C   MET A 670       2.911   1.265 -65.647  1.00 38.02           C  
ANISOU 5508  C   MET A 670     5404   5279   3765   -493    -76    483       C  
ATOM   5509  O   MET A 670       2.971   2.451 -65.293  1.00 39.84           O  
ANISOU 5509  O   MET A 670     5613   5476   4046   -456    -85    530       O  
ATOM   5510  CB  MET A 670       0.890  -0.103 -65.024  1.00 37.73           C  
ANISOU 5510  CB  MET A 670     5350   5275   3711   -488   -126    482       C  
ATOM   5511  CG  MET A 670       0.311   0.783 -63.943  1.00 36.38           C  
ANISOU 5511  CG  MET A 670     5145   5059   3619   -422   -147    522       C  
ATOM   5512  SD  MET A 670      -0.362  -0.176 -62.582  1.00 36.29           S  
ANISOU 5512  SD  MET A 670     5124   5019   3645   -380   -149    474       S  
ATOM   5513  CE  MET A 670       1.139  -0.797 -61.814  1.00 36.36           C  
ANISOU 5513  CE  MET A 670     5157   4982   3679   -359   -101    384       C  
ATOM   5514  N   CYS A 671       3.959   0.445 -65.643  1.00 37.69           N  
ANISOU 5514  N   CYS A 671     5383   5222   3714   -506    -30    406       N  
ATOM   5515  CA  CYS A 671       5.309   0.891 -65.304  1.00 37.86           C  
ANISOU 5515  CA  CYS A 671     5406   5194   3783   -481      9    374       C  
ATOM   5516  C   CYS A 671       5.776   2.065 -66.191  1.00 36.94           C  
ANISOU 5516  C   CYS A 671     5294   5089   3651   -505     14    425       C  
ATOM   5517  O   CYS A 671       6.311   3.060 -65.686  1.00 35.54           O  
ANISOU 5517  O   CYS A 671     5102   4869   3532   -466     20    443       O  
ATOM   5518  CB  CYS A 671       6.296  -0.285 -65.381  1.00 35.72           C  
ANISOU 5518  CB  CYS A 671     5154   4911   3507   -502     58    288       C  
ATOM   5519  SG  CYS A 671       8.028   0.150 -64.983  1.00 40.65           S  
ANISOU 5519  SG  CYS A 671     5773   5474   4198   -476    106    247       S  
ATOM   5520  N   GLU A 672       5.568   1.946 -67.502  1.00 37.00           N  
ANISOU 5520  N   GLU A 672     5323   5157   3578   -574     13    449       N  
ATOM   5521  CA  GLU A 672       5.933   3.011 -68.440  1.00 38.86           C  
ANISOU 5521  CA  GLU A 672     5565   5412   3789   -607     14    506       C  
ATOM   5522  C   GLU A 672       5.103   4.270 -68.214  1.00 37.47           C  
ANISOU 5522  C   GLU A 672     5358   5228   3652   -572    -36    601       C  
ATOM   5523  O   GLU A 672       5.614   5.385 -68.276  1.00 36.60           O  
ANISOU 5523  O   GLU A 672     5238   5092   3578   -556    -29    640       O  
ATOM   5524  CB  GLU A 672       5.776   2.545 -69.885  1.00 42.55           C  
ANISOU 5524  CB  GLU A 672     6066   5953   4150   -699     19    513       C  
ATOM   5525  CG  GLU A 672       6.950   1.728 -70.397  1.00 53.93           C  
ANISOU 5525  CG  GLU A 672     7539   7392   5560   -743     89    425       C  
ATOM   5526  CD  GLU A 672       7.172   1.885 -71.894  1.00 64.97           C  
ANISOU 5526  CD  GLU A 672     8973   8852   6862   -836    106    446       C  
ATOM   5527  OE1 GLU A 672       7.182   0.853 -72.605  1.00 67.18           O  
ANISOU 5527  OE1 GLU A 672     9284   9173   7070   -904    137    392       O  
ATOM   5528  OE2 GLU A 672       7.341   3.041 -72.359  1.00 69.54           O  
ANISOU 5528  OE2 GLU A 672     9548   9438   7435   -844     92    515       O  
ATOM   5529  N   TYR A 673       3.817   4.071 -67.956  1.00 36.23           N  
ANISOU 5529  N   TYR A 673     5181   5090   3493   -562    -82    639       N  
ATOM   5530  CA  TYR A 673       2.890   5.150 -67.690  1.00 35.00           C  
ANISOU 5530  CA  TYR A 673     4988   4923   3389   -528   -127    729       C  
ATOM   5531  C   TYR A 673       3.394   5.965 -66.500  1.00 35.39           C  
ANISOU 5531  C   TYR A 673     5015   4893   3538   -454   -105    714       C  
ATOM   5532  O   TYR A 673       3.552   7.183 -66.598  1.00 34.97           O  
ANISOU 5532  O   TYR A 673     4944   4815   3529   -438   -108    771       O  
ATOM   5533  CB  TYR A 673       1.505   4.553 -67.444  1.00 35.72           C  
ANISOU 5533  CB  TYR A 673     5060   5039   3471   -525   -170    750       C  
ATOM   5534  CG  TYR A 673       0.358   5.533 -67.304  1.00 40.17           C  
ANISOU 5534  CG  TYR A 673     5579   5596   4089   -498   -219    849       C  
ATOM   5535  CD1 TYR A 673       0.380   6.791 -67.939  1.00 39.75           C  
ANISOU 5535  CD1 TYR A 673     5507   5542   4056   -507   -236    939       C  
ATOM   5536  CD2 TYR A 673      -0.783   5.178 -66.579  1.00 34.61           C  
ANISOU 5536  CD2 TYR A 673     4846   4883   3421   -466   -245    857       C  
ATOM   5537  CE1 TYR A 673      -0.697   7.681 -67.813  1.00 38.68           C  
ANISOU 5537  CE1 TYR A 673     5321   5392   3985   -480   -278   1034       C  
ATOM   5538  CE2 TYR A 673      -1.866   6.052 -66.459  1.00 38.74           C  
ANISOU 5538  CE2 TYR A 673     5320   5393   4007   -441   -284    947       C  
ATOM   5539  CZ  TYR A 673      -1.815   7.300 -67.077  1.00 41.06           C  
ANISOU 5539  CZ  TYR A 673     5592   5682   4328   -447   -301   1037       C  
ATOM   5540  OH  TYR A 673      -2.891   8.152 -66.952  1.00 45.17           O  
ANISOU 5540  OH  TYR A 673     6056   6181   4924   -421   -337   1130       O  
ATOM   5541  N   MET A 674       3.703   5.275 -65.404  1.00 34.07           N  
ANISOU 5541  N   MET A 674     4852   4689   3405   -415    -83    637       N  
ATOM   5542  CA  MET A 674       4.235   5.914 -64.208  1.00 34.35           C  
ANISOU 5542  CA  MET A 674     4872   4654   3524   -355    -62    612       C  
ATOM   5543  C   MET A 674       5.731   6.249 -64.306  1.00 34.80           C  
ANISOU 5543  C   MET A 674     4945   4683   3594   -358    -20    573       C  
ATOM   5544  O   MET A 674       6.295   6.859 -63.387  1.00 33.78           O  
ANISOU 5544  O   MET A 674     4806   4499   3531   -316     -3    554       O  
ATOM   5545  CB  MET A 674       3.972   5.036 -62.976  1.00 33.67           C  
ANISOU 5545  CB  MET A 674     4785   4543   3464   -320    -59    550       C  
ATOM   5546  CG  MET A 674       2.505   4.930 -62.554  1.00 33.30           C  
ANISOU 5546  CG  MET A 674     4716   4506   3432   -302    -94    586       C  
ATOM   5547  SD  MET A 674       1.725   6.507 -62.093  1.00 39.43           S  
ANISOU 5547  SD  MET A 674     5449   5238   4294   -259   -107    663       S  
ATOM   5548  CE  MET A 674       0.660   6.778 -63.499  1.00 35.11           C  
ANISOU 5548  CE  MET A 674     4883   4752   3706   -303   -154    764       C  
ATOM   5549  N   ASN A 675       6.369   5.852 -65.412  1.00 34.56           N  
ANISOU 5549  N   ASN A 675     4939   4690   3500   -411     -1    561       N  
ATOM   5550  CA  ASN A 675       7.806   6.085 -65.613  1.00 35.03           C  
ANISOU 5550  CA  ASN A 675     5013   4725   3572   -419     43    523       C  
ATOM   5551  C   ASN A 675       8.659   5.534 -64.456  1.00 36.80           C  
ANISOU 5551  C   ASN A 675     5234   4898   3849   -381     69    444       C  
ATOM   5552  O   ASN A 675       9.618   6.170 -64.010  1.00 37.22           O  
ANISOU 5552  O   ASN A 675     5280   4906   3954   -358     91    428       O  
ATOM   5553  CB  ASN A 675       8.093   7.583 -65.839  1.00 33.27           C  
ANISOU 5553  CB  ASN A 675     4776   4479   3388   -408     44    584       C  
ATOM   5554  CG  ASN A 675       9.490   7.841 -66.401  1.00 32.69           C  
ANISOU 5554  CG  ASN A 675     4718   4393   3309   -433     89    557       C  
ATOM   5555  OD1 ASN A 675       9.999   7.082 -67.233  1.00 28.47           O  
ANISOU 5555  OD1 ASN A 675     4209   3893   2716   -483    115    522       O  
ATOM   5556  ND2 ASN A 675      10.109   8.927 -65.956  1.00 34.60           N  
ANISOU 5556  ND2 ASN A 675     4944   4585   3616   -401    102    571       N  
ATOM   5557  N   ASN A 676       8.308   4.347 -63.972  1.00 36.53           N  
ANISOU 5557  N   ASN A 676     5205   4872   3803   -377     63    398       N  
ATOM   5558  CA  ASN A 676       8.988   3.790 -62.810  1.00 35.98           C  
ANISOU 5558  CA  ASN A 676     5130   4757   3786   -342     77    336       C  
ATOM   5559  C   ASN A 676      10.419   3.330 -63.115  1.00 36.60           C  
ANISOU 5559  C   ASN A 676     5216   4817   3874   -360    121    281       C  
ATOM   5560  O   ASN A 676      10.795   3.156 -64.277  1.00 35.79           O  
ANISOU 5560  O   ASN A 676     5128   4743   3726   -407    149    277       O  
ATOM   5561  CB  ASN A 676       8.156   2.668 -62.185  1.00 35.00           C  
ANISOU 5561  CB  ASN A 676     5005   4643   3650   -331     57    310       C  
ATOM   5562  CG  ASN A 676       6.835   3.162 -61.613  1.00 35.54           C  
ANISOU 5562  CG  ASN A 676     5060   4715   3730   -304     18    357       C  
ATOM   5563  OD1 ASN A 676       5.800   2.499 -61.752  1.00 34.39           O  
ANISOU 5563  OD1 ASN A 676     4915   4601   3550   -315     -3    366       O  
ATOM   5564  ND2 ASN A 676       6.865   4.324 -60.950  1.00 32.63           N  
ANISOU 5564  ND2 ASN A 676     4676   4308   3414   -269     14    384       N  
ATOM   5565  N   LYS A 677      11.213   3.147 -62.066  1.00 36.13           N  
ANISOU 5565  N   LYS A 677     5144   4710   3875   -328    129    241       N  
ATOM   5566  CA  LYS A 677      12.622   2.808 -62.223  1.00 37.80           C  
ANISOU 5566  CA  LYS A 677     5352   4894   4117   -339    169    195       C  
ATOM   5567  C   LYS A 677      12.833   1.365 -62.708  1.00 38.40           C  
ANISOU 5567  C   LYS A 677     5436   4984   4172   -370    197    144       C  
ATOM   5568  O   LYS A 677      13.778   1.079 -63.443  1.00 39.59           O  
ANISOU 5568  O   LYS A 677     5588   5128   4325   -400    244    112       O  
ATOM   5569  CB  LYS A 677      13.367   3.053 -60.908  1.00 39.19           C  
ANISOU 5569  CB  LYS A 677     5507   5015   4366   -298    160    175       C  
ATOM   5570  CG  LYS A 677      14.870   2.865 -61.002  1.00 42.86           C  
ANISOU 5570  CG  LYS A 677     5960   5446   4880   -306    196    137       C  
ATOM   5571  CD  LYS A 677      15.594   3.313 -59.746  1.00 42.26           C  
ANISOU 5571  CD  LYS A 677     5863   5322   4872   -272    178    129       C  
ATOM   5572  CE  LYS A 677      17.092   3.195 -59.941  1.00 44.34           C  
ANISOU 5572  CE  LYS A 677     6107   5551   5188   -282    213     99       C  
ATOM   5573  NZ  LYS A 677      17.515   1.760 -60.016  1.00 45.90           N  
ANISOU 5573  NZ  LYS A 677     6293   5740   5406   -293    233     56       N  
ATOM   5574  N   GLN A 678      11.950   0.459 -62.303  1.00 38.06           N  
ANISOU 5574  N   GLN A 678     5395   4957   4111   -364    174    134       N  
ATOM   5575  CA  GLN A 678      12.138  -0.956 -62.600  1.00 38.19           C  
ANISOU 5575  CA  GLN A 678     5415   4977   4120   -389    203     82       C  
ATOM   5576  C   GLN A 678      10.797  -1.679 -62.492  1.00 37.59           C  
ANISOU 5576  C   GLN A 678     5348   4935   3999   -393    173     89       C  
ATOM   5577  O   GLN A 678      10.086  -1.535 -61.504  1.00 36.79           O  
ANISOU 5577  O   GLN A 678     5238   4826   3913   -356    132    110       O  
ATOM   5578  CB  GLN A 678      13.166  -1.545 -61.620  1.00 38.45           C  
ANISOU 5578  CB  GLN A 678     5423   4953   4234   -359    213     42       C  
ATOM   5579  CG  GLN A 678      13.791  -2.875 -62.019  1.00 42.15           C  
ANISOU 5579  CG  GLN A 678     5884   5405   4725   -385    260    -15       C  
ATOM   5580  CD  GLN A 678      14.499  -3.552 -60.846  1.00 43.89           C  
ANISOU 5580  CD  GLN A 678     6073   5571   5031   -350    251    -37       C  
ATOM   5581  OE1 GLN A 678      14.790  -2.923 -59.824  1.00 41.02           O  
ANISOU 5581  OE1 GLN A 678     5696   5182   4708   -314    215    -15       O  
ATOM   5582  NE2 GLN A 678      14.767  -4.839 -60.987  1.00 43.92           N  
ANISOU 5582  NE2 GLN A 678     6066   5557   5064   -364    283    -80       N  
ATOM   5583  N   HIS A 679      10.447  -2.436 -63.525  1.00 36.93           N  
ANISOU 5583  N   HIS A 679     5283   4891   3858   -443    196     69       N  
ATOM   5584  CA  HIS A 679       9.224  -3.231 -63.523  1.00 34.45           C  
ANISOU 5584  CA  HIS A 679     4977   4611   3500   -454    172     71       C  
ATOM   5585  C   HIS A 679       9.335  -4.434 -62.583  1.00 34.22           C  
ANISOU 5585  C   HIS A 679     4934   4547   3522   -429    175     26       C  
ATOM   5586  O   HIS A 679      10.166  -5.333 -62.778  1.00 32.93           O  
ANISOU 5586  O   HIS A 679     4765   4358   3388   -445    220    -27       O  
ATOM   5587  CB  HIS A 679       8.863  -3.682 -64.946  1.00 34.75           C  
ANISOU 5587  CB  HIS A 679     5041   4704   3457   -525    197     60       C  
ATOM   5588  CG  HIS A 679       7.950  -4.865 -64.985  1.00 32.22           C  
ANISOU 5588  CG  HIS A 679     4728   4410   3104   -546    189     35       C  
ATOM   5589  ND1 HIS A 679       6.649  -4.815 -64.538  1.00 29.91           N  
ANISOU 5589  ND1 HIS A 679     4431   4142   2791   -528    135     75       N  
ATOM   5590  CD2 HIS A 679       8.154  -6.134 -65.410  1.00 34.07           C  
ANISOU 5590  CD2 HIS A 679     4972   4645   3330   -584    233    -28       C  
ATOM   5591  CE1 HIS A 679       6.090  -6.002 -64.683  1.00 29.03           C  
ANISOU 5591  CE1 HIS A 679     4327   4048   2654   -554    143     40       C  
ATOM   5592  NE2 HIS A 679       6.979  -6.817 -65.223  1.00 33.86           N  
ANISOU 5592  NE2 HIS A 679     4948   4645   3272   -589    202    -23       N  
ATOM   5593  N   LEU A 680       8.492  -4.437 -61.556  1.00 33.31           N  
ANISOU 5593  N   LEU A 680     4810   4427   3418   -391    129     50       N  
ATOM   5594  CA  LEU A 680       8.530  -5.485 -60.547  1.00 32.03           C  
ANISOU 5594  CA  LEU A 680     4635   4232   3302   -366    124     19       C  
ATOM   5595  C   LEU A 680       7.139  -5.906 -60.096  1.00 29.98           C  
ANISOU 5595  C   LEU A 680     4379   3998   3012   -358     87     36       C  
ATOM   5596  O   LEU A 680       6.984  -6.555 -59.060  1.00 31.88           O  
ANISOU 5596  O   LEU A 680     4611   4215   3289   -331     71     25       O  
ATOM   5597  CB  LEU A 680       9.385  -5.057 -59.352  1.00 31.09           C  
ANISOU 5597  CB  LEU A 680     4497   4063   3255   -322    111     23       C  
ATOM   5598  CG  LEU A 680      10.893  -4.929 -59.582  1.00 32.98           C  
ANISOU 5598  CG  LEU A 680     4722   4264   3544   -326    148     -2       C  
ATOM   5599  CD1 LEU A 680      11.518  -4.099 -58.466  1.00 33.45           C  
ANISOU 5599  CD1 LEU A 680     4766   4286   3656   -287    121     19       C  
ATOM   5600  CD2 LEU A 680      11.564  -6.313 -59.707  1.00 28.24           C  
ANISOU 5600  CD2 LEU A 680     4108   3635   2988   -340    186    -53       C  
ATOM   5601  N   MET A 681       6.127  -5.542 -60.871  1.00 27.50           N  
ANISOU 5601  N   MET A 681     4079   3736   2636   -383     71     67       N  
ATOM   5602  CA  MET A 681       4.777  -6.022 -60.598  1.00 30.49           C  
ANISOU 5602  CA  MET A 681     4457   4140   2986   -382     40     82       C  
ATOM   5603  C   MET A 681       4.598  -7.419 -61.197  1.00 30.58           C  
ANISOU 5603  C   MET A 681     4478   4169   2971   -424     65     35       C  
ATOM   5604  O   MET A 681       4.286  -7.559 -62.380  1.00 32.74           O  
ANISOU 5604  O   MET A 681     4768   4488   3184   -476     77     33       O  
ATOM   5605  CB  MET A 681       3.734  -5.029 -61.112  1.00 30.54           C  
ANISOU 5605  CB  MET A 681     4465   4190   2949   -391      6    143       C  
ATOM   5606  CG  MET A 681       3.824  -3.630 -60.475  1.00 27.20           C  
ANISOU 5606  CG  MET A 681     4029   3742   2563   -349    -13    187       C  
ATOM   5607  SD  MET A 681       3.330  -3.542 -58.733  1.00 30.53           S  
ANISOU 5607  SD  MET A 681     4438   4124   3040   -292    -38    190       S  
ATOM   5608  CE  MET A 681       4.908  -3.522 -57.895  1.00 26.17           C  
ANISOU 5608  CE  MET A 681     3883   3516   2545   -268    -16    152       C  
ATOM   5609  N   PHE A 682       4.835  -8.447 -60.381  1.00 32.01           N  
ANISOU 5609  N   PHE A 682     4650   4314   3198   -404     75     -1       N  
ATOM   5610  CA  PHE A 682       4.802  -9.840 -60.850  1.00 33.36           C  
ANISOU 5610  CA  PHE A 682     4826   4488   3362   -440    108    -52       C  
ATOM   5611  C   PHE A 682       3.594 -10.586 -60.276  1.00 33.56           C  
ANISOU 5611  C   PHE A 682     4849   4526   3377   -432     79    -48       C  
ATOM   5612  O   PHE A 682       3.616 -11.047 -59.137  1.00 33.35           O  
ANISOU 5612  O   PHE A 682     4809   4462   3400   -395     66    -51       O  
ATOM   5613  CB  PHE A 682       6.095 -10.587 -60.480  1.00 34.93           C  
ANISOU 5613  CB  PHE A 682     5009   4627   3635   -429    149    -99       C  
ATOM   5614  CG  PHE A 682       7.357  -9.965 -61.025  1.00 37.08           C  
ANISOU 5614  CG  PHE A 682     5280   4881   3928   -437    184   -109       C  
ATOM   5615  CD1 PHE A 682       7.417  -9.479 -62.329  1.00 38.76           C  
ANISOU 5615  CD1 PHE A 682     5513   5133   4080   -486    210   -112       C  
ATOM   5616  CD2 PHE A 682       8.507  -9.916 -60.242  1.00 38.69           C  
ANISOU 5616  CD2 PHE A 682     5459   5027   4213   -402    192   -116       C  
ATOM   5617  CE1 PHE A 682       8.597  -8.921 -62.837  1.00 38.98           C  
ANISOU 5617  CE1 PHE A 682     5539   5142   4128   -496    248   -124       C  
ATOM   5618  CE2 PHE A 682       9.694  -9.367 -60.737  1.00 39.71           C  
ANISOU 5618  CE2 PHE A 682     5583   5136   4369   -410    227   -127       C  
ATOM   5619  CZ  PHE A 682       9.737  -8.868 -62.043  1.00 40.41           C  
ANISOU 5619  CZ  PHE A 682     5694   5263   4397   -456    258   -133       C  
ATOM   5620  N   MET A 683       2.538 -10.699 -61.070  1.00 35.15           N  
ANISOU 5620  N   MET A 683     5062   4781   3512   -471     67    -37       N  
ATOM   5621  CA  MET A 683       1.305 -11.314 -60.618  1.00 35.05           C  
ANISOU 5621  CA  MET A 683     5046   4785   3487   -467     38    -28       C  
ATOM   5622  C   MET A 683       1.168 -12.717 -61.181  1.00 36.32           C  
ANISOU 5622  C   MET A 683     5215   4953   3632   -513     73    -84       C  
ATOM   5623  O   MET A 683       0.884 -12.894 -62.353  1.00 36.28           O  
ANISOU 5623  O   MET A 683     5226   4993   3564   -572     87    -97       O  
ATOM   5624  CB  MET A 683       0.108 -10.445 -61.002  1.00 34.34           C  
ANISOU 5624  CB  MET A 683     4956   4747   3344   -476     -7     30       C  
ATOM   5625  CG  MET A 683      -1.242 -11.075 -60.718  1.00 35.87           C  
ANISOU 5625  CG  MET A 683     5144   4964   3522   -480    -34     39       C  
ATOM   5626  SD  MET A 683      -2.615  -9.954 -61.039  1.00 35.97           S  
ANISOU 5626  SD  MET A 683     5144   5027   3496   -483    -90    119       S  
ATOM   5627  CE  MET A 683      -2.878  -9.294 -59.384  1.00 31.29           C  
ANISOU 5627  CE  MET A 683     4530   4383   2974   -405   -110    147       C  
ATOM   5628  N   ASP A 684       1.377 -13.709 -60.323  1.00 38.12           N  
ANISOU 5628  N   ASP A 684     5432   5136   3918   -488     86   -114       N  
ATOM   5629  CA  ASP A 684       1.292 -15.109 -60.710  1.00 41.16           C  
ANISOU 5629  CA  ASP A 684     5819   5514   4305   -526    124   -169       C  
ATOM   5630  C   ASP A 684      -0.045 -15.683 -60.285  1.00 40.68           C  
ANISOU 5630  C   ASP A 684     5756   5475   4226   -525     92   -157       C  
ATOM   5631  O   ASP A 684      -0.685 -15.174 -59.351  1.00 40.29           O  
ANISOU 5631  O   ASP A 684     5698   5425   4187   -482     47   -112       O  
ATOM   5632  CB  ASP A 684       2.399 -15.920 -60.027  1.00 43.51           C  
ANISOU 5632  CB  ASP A 684     6098   5741   4693   -500    161   -206       C  
ATOM   5633  CG  ASP A 684       3.782 -15.569 -60.527  1.00 49.70           C  
ANISOU 5633  CG  ASP A 684     6880   6497   5508   -506    203   -228       C  
ATOM   5634  OD1 ASP A 684       3.918 -15.148 -61.701  1.00 52.14           O  
ANISOU 5634  OD1 ASP A 684     7208   6842   5760   -553    228   -241       O  
ATOM   5635  OD2 ASP A 684       4.740 -15.727 -59.737  1.00 55.19           O  
ANISOU 5635  OD2 ASP A 684     7553   7135   6284   -468    211   -230       O  
ATOM   5636  N   ARG A 685      -0.453 -16.759 -60.950  1.00 37.83           N  
ANISOU 5636  N   ARG A 685     5403   5130   3841   -575    121   -201       N  
ATOM   5637  CA  ARG A 685      -1.619 -17.520 -60.511  1.00 35.89           C  
ANISOU 5637  CA  ARG A 685     5153   4896   3590   -576     98   -199       C  
ATOM   5638  C   ARG A 685      -1.342 -18.057 -59.106  1.00 35.92           C  
ANISOU 5638  C   ARG A 685     5136   4837   3674   -519     94   -197       C  
ATOM   5639  O   ARG A 685      -0.226 -18.485 -58.817  1.00 36.69           O  
ANISOU 5639  O   ARG A 685     5225   4882   3835   -504    128   -224       O  
ATOM   5640  CB  ARG A 685      -1.919 -18.656 -61.492  1.00 32.42           C  
ANISOU 5640  CB  ARG A 685     4726   4477   3117   -645    139   -257       C  
ATOM   5641  CG  ARG A 685      -3.261 -19.358 -61.275  1.00 36.59           C  
ANISOU 5641  CG  ARG A 685     5250   5029   3623   -658    113   -253       C  
ATOM   5642  CD  ARG A 685      -3.162 -20.465 -60.218  1.00 34.41           C  
ANISOU 5642  CD  ARG A 685     4957   4692   3426   -623    131   -277       C  
ATOM   5643  NE  ARG A 685      -2.410 -21.604 -60.723  1.00 35.80           N  
ANISOU 5643  NE  ARG A 685     5135   4831   3638   -659    200   -348       N  
ATOM   5644  CZ  ARG A 685      -1.999 -22.630 -59.990  1.00 37.22           C  
ANISOU 5644  CZ  ARG A 685     5297   4947   3900   -635    229   -374       C  
ATOM   5645  NH1 ARG A 685      -2.254 -22.683 -58.677  1.00 36.28           N  
ANISOU 5645  NH1 ARG A 685     5159   4796   3828   -577    191   -333       N  
ATOM   5646  NH2 ARG A 685      -1.322 -23.603 -60.581  1.00 29.85           N  
ANISOU 5646  NH2 ARG A 685     4361   3976   3004   -672    298   -441       N  
ATOM   5647  N   GLU A 686      -2.349 -18.006 -58.239  1.00 36.48           N  
ANISOU 5647  N   GLU A 686     5201   4916   3745   -490     52   -161       N  
ATOM   5648  CA  GLU A 686      -2.233 -18.567 -56.907  1.00 39.28           C  
ANISOU 5648  CA  GLU A 686     5542   5220   4163   -446     45   -155       C  
ATOM   5649  C   GLU A 686      -3.143 -19.788 -56.731  1.00 39.57           C  
ANISOU 5649  C   GLU A 686     5574   5257   4203   -463     51   -176       C  
ATOM   5650  O   GLU A 686      -2.645 -20.899 -56.535  1.00 39.38           O  
ANISOU 5650  O   GLU A 686     5542   5189   4232   -468     84   -212       O  
ATOM   5651  CB  GLU A 686      -2.503 -17.504 -55.838  1.00 42.25           C  
ANISOU 5651  CB  GLU A 686     5914   5595   4544   -397      0   -101       C  
ATOM   5652  CG  GLU A 686      -1.685 -17.735 -54.574  1.00 51.20           C  
ANISOU 5652  CG  GLU A 686     7039   6672   5743   -357     -3    -94       C  
ATOM   5653  CD  GLU A 686      -1.870 -16.658 -53.527  1.00 59.84           C  
ANISOU 5653  CD  GLU A 686     8135   7765   6837   -318    -40    -49       C  
ATOM   5654  OE1 GLU A 686      -0.857 -16.256 -52.903  1.00 59.59           O  
ANISOU 5654  OE1 GLU A 686     8101   7701   6841   -295    -44    -39       O  
ATOM   5655  OE2 GLU A 686      -3.025 -16.215 -53.320  1.00 66.42           O  
ANISOU 5655  OE2 GLU A 686     8971   8627   7637   -314    -63    -25       O  
ATOM   5656  N   ALA A 687      -4.461 -19.601 -56.831  1.00 38.73           N  
ANISOU 5656  N   ALA A 687     5470   5196   4049   -475     20   -154       N  
ATOM   5657  CA  ALA A 687      -5.400 -20.718 -56.608  1.00 36.25           C  
ANISOU 5657  CA  ALA A 687     5152   4883   3740   -491     22   -171       C  
ATOM   5658  C   ALA A 687      -6.202 -21.161 -57.826  1.00 35.41           C  
ANISOU 5658  C   ALA A 687     5053   4828   3574   -554     31   -197       C  
ATOM   5659  O   ALA A 687      -6.583 -20.354 -58.684  1.00 35.04           O  
ANISOU 5659  O   ALA A 687     5013   4833   3466   -581     10   -177       O  
ATOM   5660  CB  ALA A 687      -6.328 -20.434 -55.436  1.00 34.96           C  
ANISOU 5660  CB  ALA A 687     4981   4719   3586   -451    -17   -127       C  
ATOM   5661  N   ILE A 688      -6.429 -22.467 -57.899  1.00 34.26           N  
ANISOU 5661  N   ILE A 688     4906   4664   3448   -581     61   -241       N  
ATOM   5662  CA  ILE A 688      -7.379 -23.026 -58.845  1.00 35.64           C  
ANISOU 5662  CA  ILE A 688     5087   4887   3568   -643     64   -267       C  
ATOM   5663  C   ILE A 688      -8.449 -23.717 -58.037  1.00 35.91           C  
ANISOU 5663  C   ILE A 688     5108   4913   3623   -629     46   -256       C  
ATOM   5664  O   ILE A 688      -8.170 -24.649 -57.277  1.00 38.71           O  
ANISOU 5664  O   ILE A 688     5455   5215   4040   -608     70   -276       O  
ATOM   5665  CB  ILE A 688      -6.731 -24.015 -59.821  1.00 35.51           C  
ANISOU 5665  CB  ILE A 688     5083   4859   3552   -702    128   -341       C  
ATOM   5666  CG1 ILE A 688      -5.719 -23.285 -60.709  1.00 38.53           C  
ANISOU 5666  CG1 ILE A 688     5480   5254   3906   -723    150   -354       C  
ATOM   5667  CG2 ILE A 688      -7.804 -24.680 -60.674  1.00 36.87           C  
ANISOU 5667  CG2 ILE A 688     5263   5081   3665   -772    129   -370       C  
ATOM   5668  CD1 ILE A 688      -4.984 -24.185 -61.682  1.00 41.97           C  
ANISOU 5668  CD1 ILE A 688     5928   5672   4344   -785    224   -433       C  
ATOM   5669  N   ALA A 689      -9.677 -23.242 -58.184  1.00 36.67           N  
ANISOU 5669  N   ALA A 689     5198   5061   3672   -640      2   -219       N  
ATOM   5670  CA  ALA A 689     -10.760 -23.721 -57.348  1.00 35.82           C  
ANISOU 5670  CA  ALA A 689     5076   4948   3586   -621    -18   -201       C  
ATOM   5671  C   ALA A 689     -11.957 -24.150 -58.170  1.00 35.47           C  
ANISOU 5671  C   ALA A 689     5027   4959   3492   -680    -32   -210       C  
ATOM   5672  O   ALA A 689     -12.230 -23.604 -59.238  1.00 35.28           O  
ANISOU 5672  O   ALA A 689     5009   4992   3406   -725    -53   -200       O  
ATOM   5673  CB  ALA A 689     -11.143 -22.666 -56.318  1.00 34.49           C  
ANISOU 5673  CB  ALA A 689     4895   4775   3434   -562    -57   -139       C  
ATOM   5674  N   GLY A 690     -12.649 -25.161 -57.666  1.00 35.41           N  
ANISOU 5674  N   GLY A 690     5011   4933   3511   -683    -24   -227       N  
ATOM   5675  CA  GLY A 690     -13.852 -25.660 -58.306  1.00 36.48           C  
ANISOU 5675  CA  GLY A 690     5138   5116   3606   -738    -40   -236       C  
ATOM   5676  C   GLY A 690     -14.385 -26.883 -57.598  1.00 36.77           C  
ANISOU 5676  C   GLY A 690     5166   5117   3689   -735    -19   -261       C  
ATOM   5677  O   GLY A 690     -13.713 -27.442 -56.735  1.00 35.65           O  
ANISOU 5677  O   GLY A 690     5025   4912   3607   -697     12   -277       O  
ATOM   5678  N   PRO A 691     -15.603 -27.311 -57.964  1.00 39.50           N  
ANISOU 5678  N   PRO A 691     5500   5502   4007   -777    -38   -262       N  
ATOM   5679  CA  PRO A 691     -16.177 -28.511 -57.384  1.00 38.69           C  
ANISOU 5679  CA  PRO A 691     5388   5368   3946   -780    -17   -289       C  
ATOM   5680  C   PRO A 691     -15.599 -29.771 -58.043  1.00 39.76           C  
ANISOU 5680  C   PRO A 691     5539   5479   4088   -834     42   -368       C  
ATOM   5681  O   PRO A 691     -15.153 -29.706 -59.197  1.00 39.56           O  
ANISOU 5681  O   PRO A 691     5531   5485   4014   -889     58   -403       O  
ATOM   5682  CB  PRO A 691     -17.660 -28.370 -57.717  1.00 40.05           C  
ANISOU 5682  CB  PRO A 691     5539   5597   4081   -813    -61   -260       C  
ATOM   5683  CG  PRO A 691     -17.689 -27.600 -58.995  1.00 40.81           C  
ANISOU 5683  CG  PRO A 691     5641   5761   4103   -864    -91   -248       C  
ATOM   5684  CD  PRO A 691     -16.448 -26.752 -59.039  1.00 40.28           C  
ANISOU 5684  CD  PRO A 691     5592   5678   4035   -832    -81   -239       C  
ATOM   5685  N   PRO A 692     -15.608 -30.913 -57.325  1.00 39.24           N  
ANISOU 5685  N   PRO A 692     5467   5357   4086   -820     77   -395       N  
ATOM   5686  CA  PRO A 692     -15.167 -32.173 -57.937  1.00 40.36           C  
ANISOU 5686  CA  PRO A 692     5618   5469   4249   -873    139   -473       C  
ATOM   5687  C   PRO A 692     -15.986 -32.484 -59.186  1.00 43.80           C  
ANISOU 5687  C   PRO A 692     6060   5969   4611   -962    136   -511       C  
ATOM   5688  O   PRO A 692     -17.201 -32.264 -59.185  1.00 44.93           O  
ANISOU 5688  O   PRO A 692     6190   6161   4721   -976     89   -477       O  
ATOM   5689  CB  PRO A 692     -15.442 -33.215 -56.838  1.00 38.16           C  
ANISOU 5689  CB  PRO A 692     5323   5127   4048   -841    160   -475       C  
ATOM   5690  CG  PRO A 692     -15.389 -32.424 -55.546  1.00 36.13           C  
ANISOU 5690  CG  PRO A 692     5058   4851   3819   -761    121   -403       C  
ATOM   5691  CD  PRO A 692     -15.982 -31.085 -55.904  1.00 37.49           C  
ANISOU 5691  CD  PRO A 692     5229   5092   3922   -759     66   -356       C  
ATOM   5692  N   LEU A 693     -15.326 -32.973 -60.240  1.00 45.09           N  
ANISOU 5692  N   LEU A 693     6245   6136   4753  -1027    187   -581       N  
ATOM   5693  CA  LEU A 693     -15.996 -33.295 -61.509  1.00 46.31           C  
ANISOU 5693  CA  LEU A 693     6413   6356   4827  -1127    188   -625       C  
ATOM   5694  C   LEU A 693     -17.095 -34.333 -61.302  1.00 46.17           C  
ANISOU 5694  C   LEU A 693     6381   6337   4826  -1157    191   -646       C  
ATOM   5695  O   LEU A 693     -16.863 -35.373 -60.686  1.00 47.45           O  
ANISOU 5695  O   LEU A 693     6534   6427   5067  -1137    242   -682       O  
ATOM   5696  CB  LEU A 693     -14.994 -33.822 -62.546  1.00 46.92           C  
ANISOU 5696  CB  LEU A 693     6518   6420   4889  -1193    263   -711       C  
ATOM   5697  CG  LEU A 693     -15.118 -33.445 -64.034  1.00 49.60           C  
ANISOU 5697  CG  LEU A 693     6886   6844   5115  -1293    256   -740       C  
ATOM   5698  CD1 LEU A 693     -14.676 -34.603 -64.928  1.00 49.26           C  
ANISOU 5698  CD1 LEU A 693     6867   6781   5068  -1383    346   -850       C  
ATOM   5699  CD2 LEU A 693     -16.508 -32.968 -64.448  1.00 51.37           C  
ANISOU 5699  CD2 LEU A 693     7103   7161   5256  -1337    175   -689       C  
ATOM   5700  N   GLY A 694     -18.285 -34.029 -61.813  1.00 46.22           N  
ANISOU 5700  N   GLY A 694     6380   6420   4763  -1205    135   -619       N  
ATOM   5701  CA  GLY A 694     -19.442 -34.923 -61.725  1.00 49.39           C  
ANISOU 5701  CA  GLY A 694     6764   6830   5170  -1242    130   -636       C  
ATOM   5702  C   GLY A 694     -20.260 -34.782 -60.453  1.00 49.86           C  
ANISOU 5702  C   GLY A 694     6792   6867   5286  -1166     90   -570       C  
ATOM   5703  O   GLY A 694     -21.257 -35.481 -60.271  1.00 51.62           O  
ANISOU 5703  O   GLY A 694     6998   7094   5522  -1190     84   -578       O  
ATOM   5704  N   SER A 695     -19.836 -33.874 -59.575  1.00 49.16           N  
ANISOU 5704  N   SER A 695     6696   6754   5230  -1080     67   -509       N  
ATOM   5705  CA  SER A 695     -20.485 -33.665 -58.283  1.00 47.93           C  
ANISOU 5705  CA  SER A 695     6514   6570   5126  -1007     38   -450       C  
ATOM   5706  C   SER A 695     -21.512 -32.535 -58.331  1.00 46.45           C  
ANISOU 5706  C   SER A 695     6304   6447   4899   -998    -35   -376       C  
ATOM   5707  O   SER A 695     -21.651 -31.844 -59.344  1.00 44.38           O  
ANISOU 5707  O   SER A 695     6044   6250   4570  -1043    -71   -362       O  
ATOM   5708  CB  SER A 695     -19.433 -33.334 -57.224  1.00 48.00           C  
ANISOU 5708  CB  SER A 695     6530   6514   5195   -924     57   -426       C  
ATOM   5709  OG  SER A 695     -18.923 -32.024 -57.432  1.00 48.50           O  
ANISOU 5709  OG  SER A 695     6600   6606   5223   -898     25   -385       O  
ATOM   5710  N   LYS A 696     -22.211 -32.338 -57.216  1.00 44.76           N  
ANISOU 5710  N   LYS A 696     6065   6210   4732   -941    -54   -328       N  
ATOM   5711  CA  LYS A 696     -23.172 -31.252 -57.101  1.00 44.85           C  
ANISOU 5711  CA  LYS A 696     6047   6266   4728   -922   -115   -256       C  
ATOM   5712  C   LYS A 696     -22.640 -30.092 -56.251  1.00 43.74           C  
ANISOU 5712  C   LYS A 696     5906   6100   4613   -842   -126   -204       C  
ATOM   5713  O   LYS A 696     -23.368 -29.138 -55.960  1.00 43.68           O  
ANISOU 5713  O   LYS A 696     5872   6114   4612   -814   -166   -143       O  
ATOM   5714  CB  LYS A 696     -24.507 -31.782 -56.572  1.00 47.42           C  
ANISOU 5714  CB  LYS A 696     6341   6592   5086   -926   -126   -242       C  
ATOM   5715  CG  LYS A 696     -25.216 -32.712 -57.549  1.00 50.25           C  
ANISOU 5715  CG  LYS A 696     6693   6990   5409  -1014   -129   -284       C  
ATOM   5716  CD  LYS A 696     -26.272 -33.564 -56.863  1.00 58.21           C  
ANISOU 5716  CD  LYS A 696     7676   7977   6465  -1013   -120   -288       C  
ATOM   5717  CE  LYS A 696     -26.918 -34.541 -57.852  1.00 61.70           C  
ANISOU 5717  CE  LYS A 696     8114   8458   6872  -1107   -120   -338       C  
ATOM   5718  NZ  LYS A 696     -27.820 -35.512 -57.161  1.00 64.39           N  
ANISOU 5718  NZ  LYS A 696     8433   8768   7265  -1107   -101   -350       N  
ATOM   5719  N   GLY A 697     -21.364 -30.166 -55.879  1.00 40.26           N  
ANISOU 5719  N   GLY A 697     5494   5612   4192   -809    -89   -227       N  
ATOM   5720  CA  GLY A 697     -20.710 -29.085 -55.132  1.00 41.34           C  
ANISOU 5720  CA  GLY A 697     5635   5725   4346   -742    -98   -184       C  
ATOM   5721  C   GLY A 697     -20.721 -27.754 -55.878  1.00 41.39           C  
ANISOU 5721  C   GLY A 697     5635   5783   4308   -746   -140   -142       C  
ATOM   5722  O   GLY A 697     -20.745 -27.721 -57.110  1.00 42.12           O  
ANISOU 5722  O   GLY A 697     5732   5927   4347   -806   -156   -155       O  
ATOM   5723  N   ILE A 698     -20.716 -26.654 -55.134  1.00 39.02           N  
ANISOU 5723  N   ILE A 698     5325   5471   4030   -688   -158    -90       N  
ATOM   5724  CA  ILE A 698     -20.815 -25.335 -55.756  1.00 38.04           C  
ANISOU 5724  CA  ILE A 698     5187   5389   3876   -687   -199    -41       C  
ATOM   5725  C   ILE A 698     -19.448 -24.683 -55.993  1.00 38.63           C  
ANISOU 5725  C   ILE A 698     5290   5453   3934   -669   -188    -47       C  
ATOM   5726  O   ILE A 698     -19.365 -23.634 -56.630  1.00 41.08           O  
ANISOU 5726  O   ILE A 698     5594   5797   4216   -673   -218    -10       O  
ATOM   5727  CB  ILE A 698     -21.774 -24.400 -54.982  1.00 37.34           C  
ANISOU 5727  CB  ILE A 698     5064   5297   3828   -642   -224     21       C  
ATOM   5728  CG1 ILE A 698     -21.241 -24.106 -53.571  1.00 37.80           C  
ANISOU 5728  CG1 ILE A 698     5135   5294   3932   -575   -193     25       C  
ATOM   5729  CG2 ILE A 698     -23.160 -25.028 -54.908  1.00 35.24           C  
ANISOU 5729  CG2 ILE A 698     4764   5046   3578   -667   -237     28       C  
ATOM   5730  CD1 ILE A 698     -21.894 -22.927 -52.889  1.00 33.34           C  
ANISOU 5730  CD1 ILE A 698     4542   4721   3403   -531   -207     79       C  
ATOM   5731  N   GLY A 699     -18.384 -25.315 -55.490  1.00 36.57           N  
ANISOU 5731  N   GLY A 699     5057   5142   3695   -650   -145    -89       N  
ATOM   5732  CA  GLY A 699     -17.012 -24.860 -55.735  1.00 33.14           C  
ANISOU 5732  CA  GLY A 699     4647   4693   3251   -637   -129   -102       C  
ATOM   5733  C   GLY A 699     -16.573 -23.740 -54.807  1.00 33.69           C  
ANISOU 5733  C   GLY A 699     4717   4736   3349   -572   -138    -60       C  
ATOM   5734  O   GLY A 699     -15.573 -23.863 -54.102  1.00 33.91           O  
ANISOU 5734  O   GLY A 699     4762   4717   3406   -539   -113    -75       O  
ATOM   5735  N   GLY A 700     -17.316 -22.639 -54.802  1.00 32.66           N  
ANISOU 5735  N   GLY A 700     4563   4631   3213   -556   -173     -7       N  
ATOM   5736  CA  GLY A 700     -16.977 -21.518 -53.943  1.00 33.46           C  
ANISOU 5736  CA  GLY A 700     4665   4707   3343   -500   -176     29       C  
ATOM   5737  C   GLY A 700     -18.139 -20.571 -53.777  1.00 34.42           C  
ANISOU 5737  C   GLY A 700     4751   4846   3480   -485   -204     84       C  
ATOM   5738  O   GLY A 700     -19.126 -20.667 -54.509  1.00 35.71           O  
ANISOU 5738  O   GLY A 700     4889   5051   3630   -520   -231    102       O  
ATOM   5739  N   PHE A 701     -18.026 -19.678 -52.794  1.00 34.01           N  
ANISOU 5739  N   PHE A 701     4696   4761   3463   -435   -197    109       N  
ATOM   5740  CA  PHE A 701     -18.962 -18.563 -52.621  1.00 33.53           C  
ANISOU 5740  CA  PHE A 701     4599   4707   3432   -414   -215    161       C  
ATOM   5741  C   PHE A 701     -18.288 -17.375 -51.922  1.00 35.35           C  
ANISOU 5741  C   PHE A 701     4839   4905   3686   -368   -201    179       C  
ATOM   5742  O   PHE A 701     -17.261 -17.542 -51.268  1.00 37.05           O  
ANISOU 5742  O   PHE A 701     5089   5089   3899   -351   -178    150       O  
ATOM   5743  CB  PHE A 701     -20.249 -18.981 -51.886  1.00 29.91           C  
ANISOU 5743  CB  PHE A 701     4115   4238   3012   -408   -207    169       C  
ATOM   5744  CG  PHE A 701     -20.049 -19.373 -50.424  1.00 27.68           C  
ANISOU 5744  CG  PHE A 701     3856   3906   2756   -378   -168    143       C  
ATOM   5745  CD1 PHE A 701     -19.837 -20.701 -50.068  1.00 26.48           C  
ANISOU 5745  CD1 PHE A 701     3727   3740   2594   -393   -151    103       C  
ATOM   5746  CD2 PHE A 701     -20.124 -18.423 -49.411  1.00 27.57           C  
ANISOU 5746  CD2 PHE A 701     3840   3859   2777   -339   -148    161       C  
ATOM   5747  CE1 PHE A 701     -19.678 -21.073 -48.724  1.00 27.61           C  
ANISOU 5747  CE1 PHE A 701     3892   3841   2758   -371   -120     88       C  
ATOM   5748  CE2 PHE A 701     -19.950 -18.783 -48.065  1.00 26.30           C  
ANISOU 5748  CE2 PHE A 701     3705   3658   2629   -322   -114    139       C  
ATOM   5749  CZ  PHE A 701     -19.719 -20.108 -47.726  1.00 24.64           C  
ANISOU 5749  CZ  PHE A 701     3519   3439   2405   -338   -104    106       C  
ATOM   5750  N   TRP A 702     -18.883 -16.194 -52.099  1.00 34.49           N  
ANISOU 5750  N   TRP A 702     4696   4802   3604   -353   -217    228       N  
ATOM   5751  CA  TRP A 702     -18.547 -14.960 -51.391  1.00 34.43           C  
ANISOU 5751  CA  TRP A 702     4689   4761   3633   -312   -200    247       C  
ATOM   5752  C   TRP A 702     -19.813 -14.474 -50.697  1.00 33.36           C  
ANISOU 5752  C   TRP A 702     4514   4605   3557   -292   -188    275       C  
ATOM   5753  O   TRP A 702     -20.883 -14.557 -51.286  1.00 36.09           O  
ANISOU 5753  O   TRP A 702     4817   4975   3919   -309   -212    307       O  
ATOM   5754  CB  TRP A 702     -18.106 -13.879 -52.396  1.00 34.00           C  
ANISOU 5754  CB  TRP A 702     4623   4729   3568   -314   -226    285       C  
ATOM   5755  CG  TRP A 702     -16.634 -13.741 -52.561  1.00 31.31           C  
ANISOU 5755  CG  TRP A 702     4322   4381   3194   -311   -218    259       C  
ATOM   5756  CD1 TRP A 702     -15.852 -12.762 -52.038  1.00 35.38           C  
ANISOU 5756  CD1 TRP A 702     4850   4865   3728   -279   -201    263       C  
ATOM   5757  CD2 TRP A 702     -15.759 -14.610 -53.296  1.00 30.26           C  
ANISOU 5757  CD2 TRP A 702     4219   4270   3008   -343   -222    223       C  
ATOM   5758  NE1 TRP A 702     -14.536 -12.960 -52.396  1.00 37.31           N  
ANISOU 5758  NE1 TRP A 702     5129   5112   3936   -287   -198    235       N  
ATOM   5759  CE2 TRP A 702     -14.451 -14.089 -53.168  1.00 34.19           C  
ANISOU 5759  CE2 TRP A 702     4744   4747   3499   -326   -208    210       C  
ATOM   5760  CE3 TRP A 702     -15.950 -15.780 -54.039  1.00 32.41           C  
ANISOU 5760  CE3 TRP A 702     4497   4575   3243   -387   -231    198       C  
ATOM   5761  CZ2 TRP A 702     -13.333 -14.694 -53.763  1.00 33.46           C  
ANISOU 5761  CZ2 TRP A 702     4681   4663   3370   -348   -202    174       C  
ATOM   5762  CZ3 TRP A 702     -14.840 -16.386 -54.633  1.00 36.53           C  
ANISOU 5762  CZ3 TRP A 702     5051   5103   3726   -412   -220    157       C  
ATOM   5763  CH2 TRP A 702     -13.546 -15.836 -54.494  1.00 33.42           C  
ANISOU 5763  CH2 TRP A 702     4680   4686   3333   -391   -205    147       C  
ATOM   5764  N   THR A 703     -19.705 -13.966 -49.468  1.00 31.32           N  
ANISOU 5764  N   THR A 703     4266   4300   3333   -260   -148    264       N  
ATOM   5765  CA  THR A 703     -20.833 -13.285 -48.823  1.00 30.94           C  
ANISOU 5765  CA  THR A 703     4180   4226   3352   -240   -125    288       C  
ATOM   5766  C   THR A 703     -20.649 -11.759 -48.842  1.00 31.79           C  
ANISOU 5766  C   THR A 703     4267   4310   3503   -212   -116    321       C  
ATOM   5767  O   THR A 703     -21.605 -11.003 -48.689  1.00 31.50           O  
ANISOU 5767  O   THR A 703     4182   4252   3534   -197   -103    355       O  
ATOM   5768  CB  THR A 703     -21.100 -13.766 -47.355  1.00 30.88           C  
ANISOU 5768  CB  THR A 703     4195   4179   3358   -231    -76    250       C  
ATOM   5769  OG1 THR A 703     -20.339 -12.987 -46.428  1.00 34.26           O  
ANISOU 5769  OG1 THR A 703     4655   4571   3792   -210    -41    232       O  
ATOM   5770  CG2 THR A 703     -20.768 -15.236 -47.163  1.00 32.67           C  
ANISOU 5770  CG2 THR A 703     4458   4419   3536   -253    -80    211       C  
ATOM   5771  N   GLY A 704     -19.412 -11.312 -49.024  1.00 34.76           N  
ANISOU 5771  N   GLY A 704     4676   4685   3847   -206   -120    311       N  
ATOM   5772  CA  GLY A 704     -19.082  -9.885 -48.959  1.00 34.66           C  
ANISOU 5772  CA  GLY A 704     4651   4646   3874   -181   -106    335       C  
ATOM   5773  C   GLY A 704     -17.580  -9.698 -48.978  1.00 34.42           C  
ANISOU 5773  C   GLY A 704     4668   4613   3796   -179   -107    310       C  
ATOM   5774  O   GLY A 704     -16.833 -10.657 -49.224  1.00 31.75           O  
ANISOU 5774  O   GLY A 704     4366   4298   3402   -197   -123    281       O  
ATOM   5775  N   LYS A 705     -17.131  -8.467 -48.734  1.00 32.57           N  
ANISOU 5775  N   LYS A 705     4431   4349   3594   -157    -88    321       N  
ATOM   5776  CA  LYS A 705     -15.696  -8.193 -48.646  1.00 31.74           C  
ANISOU 5776  CA  LYS A 705     4369   4237   3452   -154    -85    296       C  
ATOM   5777  C   LYS A 705     -15.046  -9.035 -47.552  1.00 31.05           C  
ANISOU 5777  C   LYS A 705     4332   4136   3329   -160    -65    243       C  
ATOM   5778  O   LYS A 705     -15.575  -9.158 -46.447  1.00 33.27           O  
ANISOU 5778  O   LYS A 705     4621   4392   3629   -157    -31    222       O  
ATOM   5779  CB  LYS A 705     -15.427  -6.711 -48.382  1.00 30.12           C  
ANISOU 5779  CB  LYS A 705     4153   3996   3295   -130    -60    313       C  
ATOM   5780  CG  LYS A 705     -15.703  -5.802 -49.573  1.00 31.53           C  
ANISOU 5780  CG  LYS A 705     4287   4189   3506   -125    -88    374       C  
ATOM   5781  CD  LYS A 705     -15.483  -4.329 -49.201  1.00 31.70           C  
ANISOU 5781  CD  LYS A 705     4294   4163   3587   -100    -56    388       C  
ATOM   5782  CE  LYS A 705     -15.861  -3.401 -50.359  1.00 32.22           C  
ANISOU 5782  CE  LYS A 705     4307   4239   3696    -94    -85    460       C  
ATOM   5783  NZ  LYS A 705     -15.887  -1.994 -49.899  1.00 32.77           N  
ANISOU 5783  NZ  LYS A 705     4353   4252   3845    -67    -44    475       N  
ATOM   5784  N   LYS A 706     -13.904  -9.623 -47.885  1.00 32.76           N  
ANISOU 5784  N   LYS A 706     4581   4368   3496   -171    -84    223       N  
ATOM   5785  CA  LYS A 706     -13.096 -10.408 -46.948  1.00 31.52           C  
ANISOU 5785  CA  LYS A 706     4468   4198   3310   -178    -74    182       C  
ATOM   5786  C   LYS A 706     -13.850 -11.612 -46.376  1.00 29.73           C  
ANISOU 5786  C   LYS A 706     4247   3975   3076   -191    -68    166       C  
ATOM   5787  O   LYS A 706     -13.510 -12.106 -45.305  1.00 29.48           O  
ANISOU 5787  O   LYS A 706     4245   3924   3030   -197    -54    141       O  
ATOM   5788  CB  LYS A 706     -12.539  -9.502 -45.827  1.00 31.50           C  
ANISOU 5788  CB  LYS A 706     4489   4160   3321   -167    -44    167       C  
ATOM   5789  CG  LYS A 706     -11.741  -8.288 -46.325  1.00 32.85           C  
ANISOU 5789  CG  LYS A 706     4656   4322   3503   -154    -47    181       C  
ATOM   5790  CD  LYS A 706     -10.853  -7.708 -45.239  1.00 35.07           C  
ANISOU 5790  CD  LYS A 706     4971   4573   3780   -154    -25    156       C  
ATOM   5791  CE  LYS A 706     -10.027  -6.520 -45.739  1.00 36.99           C  
ANISOU 5791  CE  LYS A 706     5210   4807   4038   -142    -26    168       C  
ATOM   5792  NZ  LYS A 706      -8.791  -6.941 -46.454  1.00 34.48           N  
ANISOU 5792  NZ  LYS A 706     4906   4508   3688   -147    -56    166       N  
ATOM   5793  N   ARG A 707     -14.868 -12.083 -47.096  1.00 31.10           N  
ANISOU 5793  N   ARG A 707     4403   4247   3165   -270   -290   -114       N  
ATOM   5794  CA  ARG A 707     -15.686 -13.214 -46.633  1.00 28.44           C  
ANISOU 5794  CA  ARG A 707     4047   3884   2874   -257   -271   -111       C  
ATOM   5795  C   ARG A 707     -16.032 -14.157 -47.772  1.00 29.35           C  
ANISOU 5795  C   ARG A 707     4172   3977   3002   -273   -287   -128       C  
ATOM   5796  O   ARG A 707     -16.922 -13.867 -48.581  1.00 27.98           O  
ANISOU 5796  O   ARG A 707     4000   3783   2849   -290   -329   -139       O  
ATOM   5797  CB  ARG A 707     -16.966 -12.716 -45.955  1.00 28.21           C  
ANISOU 5797  CB  ARG A 707     3993   3829   2895   -252   -276   -102       C  
ATOM   5798  CG  ARG A 707     -16.724 -12.031 -44.610  1.00 24.59           C  
ANISOU 5798  CG  ARG A 707     3525   3388   2428   -230   -250    -87       C  
ATOM   5799  CD  ARG A 707     -18.017 -11.708 -43.906  1.00 26.24           C  
ANISOU 5799  CD  ARG A 707     3712   3566   2693   -224   -244    -78       C  
ATOM   5800  NE  ARG A 707     -18.791 -12.908 -43.575  1.00 33.34           N  
ANISOU 5800  NE  ARG A 707     4596   4427   3644   -214   -210    -77       N  
ATOM   5801  CZ  ARG A 707     -18.768 -13.530 -42.397  1.00 33.16           C  
ANISOU 5801  CZ  ARG A 707     4574   4396   3628   -183   -154    -61       C  
ATOM   5802  NH1 ARG A 707     -18.007 -13.078 -41.407  1.00 28.44           N  
ANISOU 5802  NH1 ARG A 707     3990   3830   2985   -156   -135    -48       N  
ATOM   5803  NH2 ARG A 707     -19.511 -14.612 -42.209  1.00 34.99           N  
ANISOU 5803  NH2 ARG A 707     4794   4585   3914   -177   -116    -61       N  
ATOM   5804  N   TYR A 708     -15.315 -15.279 -47.844  1.00 29.35           N  
ANISOU 5804  N   TYR A 708     4179   3982   2990   -266   -257   -132       N  
ATOM   5805  CA  TYR A 708     -15.511 -16.242 -48.924  1.00 31.73           C  
ANISOU 5805  CA  TYR A 708     4491   4264   3300   -282   -269   -152       C  
ATOM   5806  C   TYR A 708     -14.917 -17.595 -48.583  1.00 31.70           C  
ANISOU 5806  C   TYR A 708     4485   4258   3302   -267   -221   -151       C  
ATOM   5807  O   TYR A 708     -14.151 -17.721 -47.637  1.00 35.28           O  
ANISOU 5807  O   TYR A 708     4936   4732   3738   -242   -185   -135       O  
ATOM   5808  CB  TYR A 708     -14.903 -15.730 -50.243  1.00 30.56           C  
ANISOU 5808  CB  TYR A 708     4380   4130   3100   -304   -302   -165       C  
ATOM   5809  CG  TYR A 708     -13.414 -15.468 -50.170  1.00 30.00           C  
ANISOU 5809  CG  TYR A 708     4328   4093   2979   -301   -276   -160       C  
ATOM   5810  CD1 TYR A 708     -12.928 -14.220 -49.803  1.00 27.51           C  
ANISOU 5810  CD1 TYR A 708     4014   3799   2639   -300   -278   -151       C  
ATOM   5811  CD2 TYR A 708     -12.495 -16.474 -50.463  1.00 27.57           C  
ANISOU 5811  CD2 TYR A 708     4031   3792   2654   -299   -246   -169       C  
ATOM   5812  CE1 TYR A 708     -11.570 -13.976 -49.722  1.00 26.49           C  
ANISOU 5812  CE1 TYR A 708     3893   3697   2475   -298   -253   -155       C  
ATOM   5813  CE2 TYR A 708     -11.138 -16.241 -50.393  1.00 25.84           C  
ANISOU 5813  CE2 TYR A 708     3820   3600   2399   -296   -222   -170       C  
ATOM   5814  CZ  TYR A 708     -10.680 -14.990 -50.020  1.00 30.25           C  
ANISOU 5814  CZ  TYR A 708     4376   4179   2939   -296   -226   -165       C  
ATOM   5815  OH  TYR A 708      -9.325 -14.749 -49.949  1.00 33.62           O  
ANISOU 5815  OH  TYR A 708     4804   4630   3342   -294   -202   -174       O  
ATOM   5816  N   ALA A 709     -15.276 -18.594 -49.382  1.00 31.36           N  
ANISOU 5816  N   ALA A 709     4443   4190   3281   -279   -224   -171       N  
ATOM   5817  CA  ALA A 709     -14.761 -19.950 -49.253  1.00 31.30           C  
ANISOU 5817  CA  ALA A 709     4436   4175   3283   -268   -179   -173       C  
ATOM   5818  C   ALA A 709     -14.556 -20.536 -50.643  1.00 31.97           C  
ANISOU 5818  C   ALA A 709     4542   4253   3353   -293   -199   -202       C  
ATOM   5819  O   ALA A 709     -15.387 -20.358 -51.528  1.00 33.43           O  
ANISOU 5819  O   ALA A 709     4730   4421   3553   -312   -245   -225       O  
ATOM   5820  CB  ALA A 709     -15.723 -20.811 -48.449  1.00 27.92           C  
ANISOU 5820  CB  ALA A 709     3979   3707   2923   -253   -141   -168       C  
ATOM   5821  N   LEU A 710     -13.440 -21.227 -50.833  1.00 33.47           N  
ANISOU 5821  N   LEU A 710     4748   4456   3512   -288   -169   -203       N  
ATOM   5822  CA  LEU A 710     -13.124 -21.840 -52.116  1.00 32.30           C  
ANISOU 5822  CA  LEU A 710     4625   4302   3346   -310   -179   -230       C  
ATOM   5823  C   LEU A 710     -12.648 -23.267 -51.923  1.00 32.54           C  
ANISOU 5823  C   LEU A 710     4648   4319   3397   -299   -128   -233       C  
ATOM   5824  O   LEU A 710     -11.994 -23.590 -50.933  1.00 32.23           O  
ANISOU 5824  O   LEU A 710     4599   4291   3356   -271    -85   -210       O  
ATOM   5825  CB  LEU A 710     -12.052 -21.038 -52.845  1.00 31.98           C  
ANISOU 5825  CB  LEU A 710     4621   4292   3239   -322   -194   -231       C  
ATOM   5826  CG  LEU A 710     -12.453 -19.709 -53.489  1.00 35.96           C  
ANISOU 5826  CG  LEU A 710     5148   4802   3713   -337   -245   -233       C  
ATOM   5827  CD1 LEU A 710     -11.212 -18.999 -54.006  1.00 35.53           C  
ANISOU 5827  CD1 LEU A 710     5128   4772   3598   -346   -235   -231       C  
ATOM   5828  CD2 LEU A 710     -13.444 -19.912 -54.627  1.00 36.56           C  
ANISOU 5828  CD2 LEU A 710     5241   4853   3796   -353   -293   -261       C  
ATOM   5829  N   ASN A 711     -12.996 -24.123 -52.871  1.00 32.61           N  
ANISOU 5829  N   ASN A 711     4664   4304   3424   -317   -134   -263       N  
ATOM   5830  CA  ASN A 711     -12.497 -25.475 -52.874  1.00 33.30           C  
ANISOU 5830  CA  ASN A 711     4748   4375   3529   -311    -85   -269       C  
ATOM   5831  C   ASN A 711     -11.272 -25.557 -53.791  1.00 33.31           C  
ANISOU 5831  C   ASN A 711     4785   4398   3473   -323    -82   -281       C  
ATOM   5832  O   ASN A 711     -11.397 -25.594 -55.012  1.00 33.77           O  
ANISOU 5832  O   ASN A 711     4870   4450   3511   -348   -112   -310       O  
ATOM   5833  CB  ASN A 711     -13.601 -26.440 -53.303  1.00 32.71           C  
ANISOU 5833  CB  ASN A 711     4653   4256   3519   -324    -86   -301       C  
ATOM   5834  CG  ASN A 711     -13.198 -27.879 -53.135  1.00 35.19           C  
ANISOU 5834  CG  ASN A 711     4960   4547   3864   -315    -24   -304       C  
ATOM   5835  OD1 ASN A 711     -12.779 -28.289 -52.052  1.00 30.59           O  
ANISOU 5835  OD1 ASN A 711     4367   3963   3292   -285     29   -272       O  
ATOM   5836  ND2 ASN A 711     -13.299 -28.655 -54.213  1.00 32.03           N  
ANISOU 5836  ND2 ASN A 711     4569   4128   3474   -338    -32   -343       N  
ATOM   5837  N   VAL A 712     -10.092 -25.576 -53.182  1.00 33.94           N  
ANISOU 5837  N   VAL A 712     4865   4502   3528   -303    -45   -260       N  
ATOM   5838  CA  VAL A 712      -8.829 -25.416 -53.901  1.00 34.11           C  
ANISOU 5838  CA  VAL A 712     4915   4544   3500   -314    -37   -269       C  
ATOM   5839  C   VAL A 712      -8.158 -26.758 -54.180  1.00 35.86           C  
ANISOU 5839  C   VAL A 712     5139   4753   3735   -311      9   -281       C  
ATOM   5840  O   VAL A 712      -8.044 -27.605 -53.285  1.00 35.53           O  
ANISOU 5840  O   VAL A 712     5074   4702   3725   -282     48   -265       O  
ATOM   5841  CB  VAL A 712      -7.866 -24.460 -53.146  1.00 33.73           C  
ANISOU 5841  CB  VAL A 712     4860   4533   3423   -296    -31   -248       C  
ATOM   5842  CG1 VAL A 712      -6.482 -24.442 -53.783  1.00 30.46           C  
ANISOU 5842  CG1 VAL A 712     4466   4134   2975   -305     -9   -262       C  
ATOM   5843  CG2 VAL A 712      -8.442 -23.050 -53.086  1.00 31.69           C  
ANISOU 5843  CG2 VAL A 712     4606   4286   3148   -305    -75   -241       C  
ATOM   5844  N   TRP A 713      -7.742 -26.934 -55.438  1.00 34.99           N  
ANISOU 5844  N   TRP A 713     5061   4637   3595   -337      5   -307       N  
ATOM   5845  CA  TRP A 713      -7.060 -28.140 -55.919  1.00 34.40           C  
ANISOU 5845  CA  TRP A 713     4994   4548   3528   -341     47   -324       C  
ATOM   5846  C   TRP A 713      -5.568 -27.915 -56.102  1.00 33.83           C  
ANISOU 5846  C   TRP A 713     4935   4498   3421   -339     76   -323       C  
ATOM   5847  O   TRP A 713      -4.791 -28.878 -56.171  1.00 33.69           O  
ANISOU 5847  O   TRP A 713     4914   4472   3416   -332    119   -330       O  
ATOM   5848  CB  TRP A 713      -7.664 -28.608 -57.252  1.00 33.26           C  
ANISOU 5848  CB  TRP A 713     4880   4379   3379   -371     26   -362       C  
ATOM   5849  CG  TRP A 713      -9.105 -28.962 -57.116  1.00 35.49           C  
ANISOU 5849  CG  TRP A 713     5140   4635   3711   -374     -1   -373       C  
ATOM   5850  CD1 TRP A 713     -10.169 -28.128 -57.305  1.00 35.92           C  
ANISOU 5850  CD1 TRP A 713     5195   4688   3764   -382    -59   -380       C  
ATOM   5851  CD2 TRP A 713      -9.648 -30.226 -56.721  1.00 33.62           C  
ANISOU 5851  CD2 TRP A 713     4871   4365   3539   -366     32   -382       C  
ATOM   5852  NE1 TRP A 713     -11.341 -28.792 -57.060  1.00 35.77           N  
ANISOU 5852  NE1 TRP A 713     5142   4637   3810   -382    -66   -396       N  
ATOM   5853  CE2 TRP A 713     -11.056 -30.083 -56.696  1.00 33.95           C  
ANISOU 5853  CE2 TRP A 713     4891   4384   3623   -374     -6   -398       C  
ATOM   5854  CE3 TRP A 713      -9.085 -31.463 -56.380  1.00 33.51           C  
ANISOU 5854  CE3 TRP A 713     4843   4332   3556   -353     95   -378       C  
ATOM   5855  CZ2 TRP A 713     -11.920 -31.136 -56.353  1.00 32.70           C  
ANISOU 5855  CZ2 TRP A 713     4697   4184   3543   -371     21   -413       C  
ATOM   5856  CZ3 TRP A 713      -9.942 -32.518 -56.039  1.00 36.44           C  
ANISOU 5856  CZ3 TRP A 713     5184   4663   4000   -349    123   -389       C  
ATOM   5857  CH2 TRP A 713     -11.348 -32.345 -56.033  1.00 36.34           C  
ANISOU 5857  CH2 TRP A 713     5148   4626   4033   -360     88   -408       C  
ATOM   5858  N   ASP A 714      -5.184 -26.644 -56.193  1.00 30.94           N  
ANISOU 5858  N   ASP A 714     4582   4155   3018   -346     55   -318       N  
ATOM   5859  CA  ASP A 714      -3.824 -26.261 -56.500  1.00 34.73           C  
ANISOU 5859  CA  ASP A 714     5073   4650   3472   -351     83   -325       C  
ATOM   5860  C   ASP A 714      -3.548 -24.852 -55.987  1.00 36.72           C  
ANISOU 5860  C   ASP A 714     5317   4929   3707   -346     64   -311       C  
ATOM   5861  O   ASP A 714      -4.234 -23.896 -56.350  1.00 37.19           O  
ANISOU 5861  O   ASP A 714     5399   4988   3744   -362     28   -308       O  
ATOM   5862  CB  ASP A 714      -3.553 -26.374 -58.017  1.00 33.56           C  
ANISOU 5862  CB  ASP A 714     4979   4485   3289   -385     91   -352       C  
ATOM   5863  CG  ASP A 714      -2.063 -26.332 -58.357  1.00 37.27           C  
ANISOU 5863  CG  ASP A 714     5456   4958   3747   -390    140   -364       C  
ATOM   5864  OD1 ASP A 714      -1.416 -25.292 -58.117  1.00 36.53           O  
ANISOU 5864  OD1 ASP A 714     5355   4881   3642   -390    144   -359       O  
ATOM   5865  OD2 ASP A 714      -1.535 -27.334 -58.872  1.00 40.73           O  
ANISOU 5865  OD2 ASP A 714     5903   5381   4194   -396    177   -381       O  
ATOM   5866  N   MET A 715      -2.540 -24.745 -55.130  1.00 38.31           N  
ANISOU 5866  N   MET A 715     5484   5150   3922   -322     86   -307       N  
ATOM   5867  CA  MET A 715      -2.161 -23.484 -54.522  1.00 40.19           C  
ANISOU 5867  CA  MET A 715     5704   5413   4152   -315     72   -301       C  
ATOM   5868  C   MET A 715      -0.683 -23.220 -54.819  1.00 40.50           C  
ANISOU 5868  C   MET A 715     5738   5460   4192   -322    108   -324       C  
ATOM   5869  O   MET A 715       0.188 -24.002 -54.423  1.00 39.58           O  
ANISOU 5869  O   MET A 715     5592   5347   4098   -300    136   -332       O  
ATOM   5870  CB  MET A 715      -2.424 -23.533 -53.009  1.00 41.95           C  
ANISOU 5870  CB  MET A 715     5885   5656   4398   -273     58   -280       C  
ATOM   5871  CG  MET A 715      -2.277 -22.207 -52.279  1.00 46.26           C  
ANISOU 5871  CG  MET A 715     6411   6228   4938   -264     35   -276       C  
ATOM   5872  SD  MET A 715      -3.462 -20.963 -52.830  1.00 51.63           S  
ANISOU 5872  SD  MET A 715     7122   6901   5597   -296     -4   -266       S  
ATOM   5873  CE  MET A 715      -3.732 -20.074 -51.295  1.00 54.33           C  
ANISOU 5873  CE  MET A 715     7424   7269   5949   -264    -29   -249       C  
ATOM   5874  N   GLU A 716      -0.425 -22.110 -55.512  1.00 39.93           N  
ANISOU 5874  N   GLU A 716     5691   5385   4097   -350    111   -333       N  
ATOM   5875  CA  GLU A 716       0.902 -21.745 -56.047  1.00 41.45           C  
ANISOU 5875  CA  GLU A 716     5884   5572   4293   -366    155   -359       C  
ATOM   5876  C   GLU A 716       1.828 -22.919 -56.421  1.00 40.03           C  
ANISOU 5876  C   GLU A 716     5699   5379   4132   -364    200   -379       C  
ATOM   5877  O   GLU A 716       3.008 -22.957 -56.047  1.00 39.31           O  
ANISOU 5877  O   GLU A 716     5568   5296   4073   -353    229   -400       O  
ATOM   5878  CB  GLU A 716       1.606 -20.697 -55.167  1.00 42.40           C  
ANISOU 5878  CB  GLU A 716     5960   5716   4436   -353    153   -369       C  
ATOM   5879  CG  GLU A 716       1.742 -21.069 -53.708  1.00 47.59           C  
ANISOU 5879  CG  GLU A 716     6558   6403   5121   -307    130   -364       C  
ATOM   5880  CD  GLU A 716       1.870 -19.861 -52.777  1.00 48.48           C  
ANISOU 5880  CD  GLU A 716     6635   6540   5244   -293    105   -368       C  
ATOM   5881  OE1 GLU A 716       1.570 -20.032 -51.576  1.00 45.04           O  
ANISOU 5881  OE1 GLU A 716     6168   6129   4815   -253     74   -356       O  
ATOM   5882  OE2 GLU A 716       2.263 -18.761 -53.235  1.00 49.68           O  
ANISOU 5882  OE2 GLU A 716     6794   6687   5397   -321    119   -385       O  
ATOM   5883  N   GLY A 717       1.280 -23.867 -57.173  1.00 35.64           N  
ANISOU 5883  N   GLY A 717     5180   4803   3561   -376    205   -376       N  
ATOM   5884  CA  GLY A 717       2.075 -24.965 -57.711  1.00 36.58           C  
ANISOU 5884  CA  GLY A 717     5301   4903   3693   -380    251   -396       C  
ATOM   5885  C   GLY A 717       2.056 -26.230 -56.882  1.00 34.58           C  
ANISOU 5885  C   GLY A 717     5009   4655   3473   -345    252   -388       C  
ATOM   5886  O   GLY A 717       2.607 -27.249 -57.294  1.00 34.87           O  
ANISOU 5886  O   GLY A 717     5048   4676   3526   -346    289   -401       O  
ATOM   5887  N   THR A 718       1.430 -26.170 -55.711  1.00 34.56           N  
ANISOU 5887  N   THR A 718     4975   4674   3483   -313    216   -364       N  
ATOM   5888  CA  THR A 718       1.233 -27.365 -54.895  1.00 37.50           C  
ANISOU 5888  CA  THR A 718     5320   5045   3882   -275    220   -350       C  
ATOM   5889  C   THR A 718      -0.068 -28.041 -55.291  1.00 37.07           C  
ANISOU 5889  C   THR A 718     5295   4968   3824   -288    209   -338       C  
ATOM   5890  O   THR A 718      -1.147 -27.545 -54.978  1.00 37.88           O  
ANISOU 5890  O   THR A 718     5401   5073   3918   -289    172   -322       O  
ATOM   5891  CB  THR A 718       1.204 -27.038 -53.392  1.00 38.04           C  
ANISOU 5891  CB  THR A 718     5348   5143   3963   -227    194   -330       C  
ATOM   5892  OG1 THR A 718       2.420 -26.370 -53.028  1.00 43.52           O  
ANISOU 5892  OG1 THR A 718     6009   5860   4666   -214    198   -350       O  
ATOM   5893  CG2 THR A 718       1.059 -28.311 -52.557  1.00 37.69           C  
ANISOU 5893  CG2 THR A 718     5286   5092   3941   -182    208   -311       C  
ATOM   5894  N   ARG A 719       0.041 -29.161 -55.992  1.00 36.50           N  
ANISOU 5894  N   ARG A 719     5238   4869   3761   -299    241   -351       N  
ATOM   5895  CA  ARG A 719      -1.132 -29.956 -56.342  1.00 39.07           C  
ANISOU 5895  CA  ARG A 719     5581   5169   4095   -310    233   -350       C  
ATOM   5896  C   ARG A 719      -1.496 -30.856 -55.164  1.00 38.91           C  
ANISOU 5896  C   ARG A 719     5527   5143   4114   -268    246   -326       C  
ATOM   5897  O   ARG A 719      -0.728 -31.749 -54.820  1.00 39.87           O  
ANISOU 5897  O   ARG A 719     5631   5259   4257   -242    284   -324       O  
ATOM   5898  CB  ARG A 719      -0.867 -30.796 -57.602  1.00 37.86           C  
ANISOU 5898  CB  ARG A 719     5461   4988   3937   -340    264   -379       C  
ATOM   5899  CG  ARG A 719      -2.110 -31.445 -58.212  1.00 36.81           C  
ANISOU 5899  CG  ARG A 719     5348   4827   3810   -360    248   -391       C  
ATOM   5900  CD  ARG A 719      -3.125 -30.400 -58.728  1.00 37.90           C  
ANISOU 5900  CD  ARG A 719     5516   4971   3915   -382    191   -395       C  
ATOM   5901  NE  ARG A 719      -2.570 -29.523 -59.758  1.00 37.08           N  
ANISOU 5901  NE  ARG A 719     5459   4872   3757   -408    186   -409       N  
ATOM   5902  CZ  ARG A 719      -2.512 -29.821 -61.057  1.00 40.77           C  
ANISOU 5902  CZ  ARG A 719     5978   5321   4194   -435    194   -438       C  
ATOM   5903  NH1 ARG A 719      -2.977 -30.980 -61.510  1.00 41.93           N  
ANISOU 5903  NH1 ARG A 719     6130   5443   4360   -442    201   -461       N  
ATOM   5904  NH2 ARG A 719      -1.990 -28.955 -61.910  1.00 37.36           N  
ANISOU 5904  NH2 ARG A 719     5595   4891   3711   -453    198   -446       N  
ATOM   5905  N   TYR A 720      -2.657 -30.613 -54.551  1.00 39.93           N  
ANISOU 5905  N   TYR A 720     5649   5270   4252   -259    218   -306       N  
ATOM   5906  CA  TYR A 720      -3.059 -31.345 -53.340  1.00 40.86           C  
ANISOU 5906  CA  TYR A 720     5742   5379   4405   -215    237   -278       C  
ATOM   5907  C   TYR A 720      -3.562 -32.746 -53.650  1.00 41.32           C  
ANISOU 5907  C   TYR A 720     5802   5395   4501   -219    274   -285       C  
ATOM   5908  O   TYR A 720      -4.285 -32.946 -54.620  1.00 43.27           O  
ANISOU 5908  O   TYR A 720     6066   5619   4755   -257    263   -310       O  
ATOM   5909  CB  TYR A 720      -4.153 -30.604 -52.567  1.00 39.22           C  
ANISOU 5909  CB  TYR A 720     5526   5177   4200   -205    204   -257       C  
ATOM   5910  CG  TYR A 720      -3.775 -29.240 -52.039  1.00 42.59           C  
ANISOU 5910  CG  TYR A 720     5946   5643   4595   -196    169   -247       C  
ATOM   5911  CD1 TYR A 720      -2.784 -29.089 -51.073  1.00 44.03           C  
ANISOU 5911  CD1 TYR A 720     6108   5852   4769   -152    177   -235       C  
ATOM   5912  CD2 TYR A 720      -4.439 -28.103 -52.482  1.00 40.53           C  
ANISOU 5912  CD2 TYR A 720     5696   5390   4314   -227    126   -253       C  
ATOM   5913  CE1 TYR A 720      -2.448 -27.836 -50.590  1.00 44.67           C  
ANISOU 5913  CE1 TYR A 720     6178   5967   4826   -145    145   -234       C  
ATOM   5914  CE2 TYR A 720      -4.121 -26.856 -51.997  1.00 42.41           C  
ANISOU 5914  CE2 TYR A 720     5926   5659   4528   -220     99   -246       C  
ATOM   5915  CZ  TYR A 720      -3.126 -26.724 -51.059  1.00 44.50           C  
ANISOU 5915  CZ  TYR A 720     6169   5951   4789   -181    109   -238       C  
ATOM   5916  OH  TYR A 720      -2.813 -25.473 -50.587  1.00 46.09           O  
ANISOU 5916  OH  TYR A 720     6359   6183   4972   -176     82   -238       O  
ATOM   5917  N   ALA A 721      -3.185 -33.707 -52.814  1.00 41.70           N  
ANISOU 5917  N   ALA A 721     5836   5431   4576   -175    317   -265       N  
ATOM   5918  CA  ALA A 721      -3.717 -35.062 -52.907  1.00 44.62           C  
ANISOU 5918  CA  ALA A 721     6205   5756   4993   -173    363   -267       C  
ATOM   5919  C   ALA A 721      -5.226 -35.054 -52.641  1.00 46.86           C  
ANISOU 5919  C   ALA A 721     6483   6012   5309   -182    354   -262       C  
ATOM   5920  O   ALA A 721      -5.982 -35.767 -53.300  1.00 49.59           O  
ANISOU 5920  O   ALA A 721     6829   6320   5692   -211    367   -286       O  
ATOM   5921  CB  ALA A 721      -2.994 -35.992 -51.928  1.00 42.85           C  
ANISOU 5921  CB  ALA A 721     5971   5524   4787   -114    413   -239       C  
ATOM   5922  N   GLU A 722      -5.642 -34.237 -51.673  1.00 48.04           N  
ANISOU 5922  N   GLU A 722     6625   6180   5448   -158    331   -234       N  
ATOM   5923  CA  GLU A 722      -7.051 -34.034 -51.337  1.00 49.45           C  
ANISOU 5923  CA  GLU A 722     6795   6334   5660   -166    321   -228       C  
ATOM   5924  C   GLU A 722      -7.359 -32.543 -51.412  1.00 47.09           C  
ANISOU 5924  C   GLU A 722     6497   6070   5325   -184    258   -230       C  
ATOM   5925  O   GLU A 722      -6.555 -31.733 -50.955  1.00 45.63           O  
ANISOU 5925  O   GLU A 722     6315   5925   5097   -164    239   -215       O  
ATOM   5926  CB  GLU A 722      -7.352 -34.544 -49.924  1.00 51.97           C  
ANISOU 5926  CB  GLU A 722     7108   6632   6007   -111    369   -187       C  
ATOM   5927  CG  GLU A 722      -7.139 -36.043 -49.717  1.00 58.21           C  
ANISOU 5927  CG  GLU A 722     7900   7380   6838    -85    442   -178       C  
ATOM   5928  CD  GLU A 722      -8.107 -36.902 -50.513  1.00 64.05           C  
ANISOU 5928  CD  GLU A 722     8628   8066   7641   -126    467   -212       C  
ATOM   5929  OE1 GLU A 722      -9.278 -36.490 -50.682  1.00 67.32           O  
ANISOU 5929  OE1 GLU A 722     9029   8463   8086   -155    443   -228       O  
ATOM   5930  OE2 GLU A 722      -7.694 -37.992 -50.968  1.00 67.97           O  
ANISOU 5930  OE2 GLU A 722     9127   8537   8162   -129    510   -225       O  
ATOM   5931  N   PRO A 723      -8.523 -32.172 -51.981  1.00 45.27           N  
ANISOU 5931  N   PRO A 723     6264   5823   5115   -220    224   -251       N  
ATOM   5932  CA  PRO A 723      -8.848 -30.751 -52.113  1.00 43.00           C  
ANISOU 5932  CA  PRO A 723     5980   5565   4794   -237    164   -252       C  
ATOM   5933  C   PRO A 723      -8.822 -30.053 -50.750  1.00 42.26           C  
ANISOU 5933  C   PRO A 723     5876   5492   4689   -198    165   -213       C  
ATOM   5934  O   PRO A 723      -9.125 -30.669 -49.723  1.00 39.93           O  
ANISOU 5934  O   PRO A 723     5572   5176   4426   -162    208   -188       O  
ATOM   5935  CB  PRO A 723     -10.267 -30.768 -52.686  1.00 42.72           C  
ANISOU 5935  CB  PRO A 723     5935   5497   4801   -269    136   -279       C  
ATOM   5936  CG  PRO A 723     -10.823 -32.092 -52.274  1.00 43.67           C  
ANISOU 5936  CG  PRO A 723     6035   5569   4990   -256    193   -280       C  
ATOM   5937  CD  PRO A 723      -9.656 -33.028 -52.378  1.00 45.37           C  
ANISOU 5937  CD  PRO A 723     6263   5785   5191   -241    240   -276       C  
ATOM   5938  N   LYS A 724      -8.439 -28.785 -50.741  1.00 42.38           N  
ANISOU 5938  N   LYS A 724     5896   5546   4659   -203    123   -210       N  
ATOM   5939  CA  LYS A 724      -8.270 -28.074 -49.486  1.00 44.37           C  
ANISOU 5939  CA  LYS A 724     6140   5823   4895   -165    121   -179       C  
ATOM   5940  C   LYS A 724      -9.125 -26.812 -49.474  1.00 43.48           C  
ANISOU 5940  C   LYS A 724     6024   5720   4778   -185     74   -179       C  
ATOM   5941  O   LYS A 724      -9.125 -26.042 -50.439  1.00 42.90           O  
ANISOU 5941  O   LYS A 724     5961   5659   4681   -220     32   -199       O  
ATOM   5942  CB  LYS A 724      -6.787 -27.762 -49.254  1.00 44.33           C  
ANISOU 5942  CB  LYS A 724     6139   5859   4847   -143    121   -177       C  
ATOM   5943  CG  LYS A 724      -6.459 -27.217 -47.865  1.00 54.61           C  
ANISOU 5943  CG  LYS A 724     7431   7188   6131    -94    119   -151       C  
ATOM   5944  CD  LYS A 724      -4.953 -27.026 -47.658  1.00 59.31           C  
ANISOU 5944  CD  LYS A 724     8020   7820   6694    -69    116   -159       C  
ATOM   5945  CE  LYS A 724      -4.650 -26.039 -46.524  1.00 62.99           C  
ANISOU 5945  CE  LYS A 724     8476   8323   7135    -32     91   -148       C  
ATOM   5946  NZ  LYS A 724      -5.110 -26.523 -45.185  1.00 65.12           N  
ANISOU 5946  NZ  LYS A 724     8751   8582   7407     26    114   -115       N  
ATOM   5947  N   LEU A 725      -9.852 -26.604 -48.380  1.00 41.67           N  
ANISOU 5947  N   LEU A 725     5782   5481   4569   -158     84   -155       N  
ATOM   5948  CA  LEU A 725     -10.725 -25.435 -48.262  1.00 39.44           C  
ANISOU 5948  CA  LEU A 725     5494   5204   4290   -174     43   -153       C  
ATOM   5949  C   LEU A 725      -9.931 -24.175 -47.950  1.00 38.12           C  
ANISOU 5949  C   LEU A 725     5331   5083   4072   -167     13   -147       C  
ATOM   5950  O   LEU A 725      -9.220 -24.104 -46.949  1.00 38.44           O  
ANISOU 5950  O   LEU A 725     5369   5146   4091   -127     29   -130       O  
ATOM   5951  CB  LEU A 725     -11.821 -25.662 -47.210  1.00 37.65           C  
ANISOU 5951  CB  LEU A 725     5252   4943   4108   -151     73   -132       C  
ATOM   5952  CG  LEU A 725     -12.711 -26.909 -47.360  1.00 39.20           C  
ANISOU 5952  CG  LEU A 725     5437   5084   4372   -157    115   -140       C  
ATOM   5953  CD1 LEU A 725     -13.691 -27.057 -46.197  1.00 36.97           C  
ANISOU 5953  CD1 LEU A 725     5144   4766   4137   -130    158   -116       C  
ATOM   5954  CD2 LEU A 725     -13.453 -26.938 -48.695  1.00 38.26           C  
ANISOU 5954  CD2 LEU A 725     5308   4945   4283   -207     75   -181       C  
ATOM   5955  N   LYS A 726     -10.030 -23.190 -48.833  1.00 37.36           N  
ANISOU 5955  N   LYS A 726     5241   4999   3955   -203    -32   -164       N  
ATOM   5956  CA  LYS A 726      -9.498 -21.872 -48.536  1.00 36.69           C  
ANISOU 5956  CA  LYS A 726     5156   4950   3834   -201    -58   -160       C  
ATOM   5957  C   LYS A 726     -10.654 -21.014 -48.054  1.00 34.60           C  
ANISOU 5957  C   LYS A 726     4881   4677   3589   -204    -82   -149       C  
ATOM   5958  O   LYS A 726     -11.512 -20.617 -48.842  1.00 35.17           O  
ANISOU 5958  O   LYS A 726     4957   4732   3674   -234   -114   -160       O  
ATOM   5959  CB  LYS A 726      -8.817 -21.240 -49.752  1.00 35.33           C  
ANISOU 5959  CB  LYS A 726     5004   4793   3628   -236    -82   -182       C  
ATOM   5960  CG  LYS A 726      -8.210 -19.860 -49.449  1.00 37.06           C  
ANISOU 5960  CG  LYS A 726     5219   5043   3818   -236   -100   -181       C  
ATOM   5961  CD  LYS A 726      -7.713 -19.184 -50.710  1.00 41.51           C  
ANISOU 5961  CD  LYS A 726     5810   5610   4353   -272   -114   -200       C  
ATOM   5962  CE  LYS A 726      -7.878 -17.667 -50.639  1.00 46.43           C  
ANISOU 5962  CE  LYS A 726     6435   6245   4961   -283   -140   -196       C  
ATOM   5963  NZ  LYS A 726      -6.707 -16.974 -50.066  1.00 45.25           N  
ANISOU 5963  NZ  LYS A 726     6269   6125   4801   -272   -126   -204       N  
ATOM   5964  N   ILE A 727     -10.684 -20.757 -46.752  1.00 32.46           N  
ANISOU 5964  N   ILE A 727     4599   4416   3320   -168    -67   -128       N  
ATOM   5965  CA  ILE A 727     -11.745 -19.965 -46.156  1.00 29.84           C  
ANISOU 5965  CA  ILE A 727     4256   4074   3008   -168    -81   -116       C  
ATOM   5966  C   ILE A 727     -11.147 -18.716 -45.545  1.00 31.39           C  
ANISOU 5966  C   ILE A 727     4449   4307   3169   -156   -100   -112       C  
ATOM   5967  O   ILE A 727     -10.168 -18.797 -44.803  1.00 31.64           O  
ANISOU 5967  O   ILE A 727     4480   4366   3174   -123    -86   -109       O  
ATOM   5968  CB  ILE A 727     -12.511 -20.746 -45.077  1.00 29.61           C  
ANISOU 5968  CB  ILE A 727     4219   4014   3017   -135    -38    -94       C  
ATOM   5969  CG1 ILE A 727     -13.039 -22.073 -45.641  1.00 28.44           C  
ANISOU 5969  CG1 ILE A 727     4069   3824   2913   -146    -10   -102       C  
ATOM   5970  CG2 ILE A 727     -13.669 -19.904 -44.548  1.00 28.00           C  
ANISOU 5970  CG2 ILE A 727     4003   3794   2842   -139    -49    -85       C  
ATOM   5971  CD1 ILE A 727     -13.428 -23.089 -44.592  1.00 28.88           C  
ANISOU 5971  CD1 ILE A 727     4125   3846   3002   -107     53    -79       C  
ATOM   5972  N   MET A 728     -11.732 -17.561 -45.859  1.00 30.13           N  
ANISOU 5972  N   MET A 728     4287   4149   3013   -182   -134   -116       N  
ATOM   5973  CA  MET A 728     -11.269 -16.312 -45.275  1.00 30.20           C  
ANISOU 5973  CA  MET A 728     4290   4188   2995   -174   -150   -115       C  
ATOM   5974  C   MET A 728     -12.433 -15.522 -44.688  1.00 29.67           C  
ANISOU 5974  C   MET A 728     4213   4106   2955   -174   -161   -103       C  
ATOM   5975  O   MET A 728     -13.489 -15.394 -45.312  1.00 30.04           O  
ANISOU 5975  O   MET A 728     4257   4124   3032   -200   -180   -104       O  
ATOM   5976  CB  MET A 728     -10.505 -15.457 -46.299  1.00 30.71           C  
ANISOU 5976  CB  MET A 728     4365   4271   3033   -206   -174   -134       C  
ATOM   5977  CG  MET A 728      -9.295 -16.124 -46.970  1.00 37.80           C  
ANISOU 5977  CG  MET A 728     5273   5181   3909   -211   -159   -151       C  
ATOM   5978  SD  MET A 728      -8.016 -16.805 -45.874  1.00 48.61           S  
ANISOU 5978  SD  MET A 728     6626   6579   5264   -163   -130   -155       S  
ATOM   5979  CE  MET A 728      -7.610 -15.394 -44.893  1.00 32.90           C  
ANISOU 5979  CE  MET A 728     4617   4622   3261   -147   -148   -162       C  
ATOM   5980  N   GLY A 729     -12.237 -15.004 -43.480  1.00 27.99           N  
ANISOU 5980  N   GLY A 729     3993   3912   2730   -144   -152    -94       N  
ATOM   5981  CA  GLY A 729     -13.182 -14.061 -42.878  1.00 30.00           C  
ANISOU 5981  CA  GLY A 729     4238   4157   3005   -145   -160    -84       C  
ATOM   5982  C   GLY A 729     -14.362 -14.703 -42.183  1.00 31.17           C  
ANISOU 5982  C   GLY A 729     4382   4266   3195   -127   -130    -65       C  
ATOM   5983  O   GLY A 729     -14.865 -14.168 -41.194  1.00 31.13           O  
ANISOU 5983  O   GLY A 729     4373   4257   3198   -109   -118    -54       O  
ATOM   5984  N   LEU A 730     -14.784 -15.864 -42.679  1.00 29.75           N  
ANISOU 5984  N   LEU A 730     4203   4056   3046   -134   -112    -65       N  
ATOM   5985  CA  LEU A 730     -15.946 -16.561 -42.139  1.00 30.00           C  
ANISOU 5985  CA  LEU A 730     4227   4041   3133   -122    -74    -52       C  
ATOM   5986  C   LEU A 730     -15.679 -17.071 -40.727  1.00 32.46           C  
ANISOU 5986  C   LEU A 730     4554   4352   3427    -70    -21    -28       C  
ATOM   5987  O   LEU A 730     -14.528 -17.159 -40.295  1.00 33.10           O  
ANISOU 5987  O   LEU A 730     4652   4471   3454    -39    -19    -26       O  
ATOM   5988  CB  LEU A 730     -16.373 -17.710 -43.061  1.00 30.15           C  
ANISOU 5988  CB  LEU A 730     4239   4025   3191   -143    -66    -64       C  
ATOM   5989  CG  LEU A 730     -16.593 -17.415 -44.555  1.00 29.24           C  
ANISOU 5989  CG  LEU A 730     4118   3908   3084   -188   -121    -90       C  
ATOM   5990  CD1 LEU A 730     -17.167 -18.660 -45.255  1.00 24.50           C  
ANISOU 5990  CD1 LEU A 730     3509   3269   2533   -202   -108   -107       C  
ATOM   5991  CD2 LEU A 730     -17.490 -16.190 -44.781  1.00 30.47           C  
ANISOU 5991  CD2 LEU A 730     4259   4057   3262   -210   -164    -95       C  
ATOM   5992  N   GLU A 731     -16.757 -17.408 -40.025  1.00 32.35           N  
ANISOU 5992  N   GLU A 731     4537   4293   3461    -56     23    -13       N  
ATOM   5993  CA  GLU A 731     -16.724 -17.734 -38.610  1.00 34.54           C  
ANISOU 5993  CA  GLU A 731     4839   4562   3721     -2     79     14       C  
ATOM   5994  C   GLU A 731     -15.793 -18.901 -38.253  1.00 35.77           C  
ANISOU 5994  C   GLU A 731     5024   4727   3840     41    114     27       C  
ATOM   5995  O   GLU A 731     -15.254 -18.959 -37.144  1.00 36.59           O  
ANISOU 5995  O   GLU A 731     5159   4849   3897     96    138     45       O  
ATOM   5996  CB  GLU A 731     -18.154 -17.968 -38.113  1.00 35.36           C  
ANISOU 5996  CB  GLU A 731     4933   4603   3897     -3    130     25       C  
ATOM   5997  CG  GLU A 731     -18.907 -16.657 -37.762  1.00 39.46           C  
ANISOU 5997  CG  GLU A 731     5437   5120   4435    -18    110     23       C  
ATOM   5998  CD  GLU A 731     -19.404 -15.854 -38.979  1.00 40.52           C  
ANISOU 5998  CD  GLU A 731     5535   5258   4605    -74     44     -4       C  
ATOM   5999  OE1 GLU A 731     -19.136 -16.242 -40.143  1.00 34.48           O  
ANISOU 5999  OE1 GLU A 731     4760   4498   3842   -103      9    -22       O  
ATOM   6000  OE2 GLU A 731     -20.083 -14.820 -38.760  1.00 41.52           O  
ANISOU 6000  OE2 GLU A 731     5646   5377   4754    -87     27     -6       O  
ATOM   6001  N   THR A 732     -15.596 -19.809 -39.203  1.00 32.98           N  
ANISOU 6001  N   THR A 732     4662   4362   3506     19    115     15       N  
ATOM   6002  CA  THR A 732     -14.665 -20.916 -39.052  1.00 33.32           C  
ANISOU 6002  CA  THR A 732     4728   4413   3518     55    143     25       C  
ATOM   6003  C   THR A 732     -13.241 -20.456 -38.759  1.00 35.29           C  
ANISOU 6003  C   THR A 732     4991   4726   3693     85    107     19       C  
ATOM   6004  O   THR A 732     -12.430 -21.230 -38.247  1.00 36.95           O  
ANISOU 6004  O   THR A 732     5224   4946   3868    133    130     31       O  
ATOM   6005  CB  THR A 732     -14.620 -21.764 -40.337  1.00 33.60           C  
ANISOU 6005  CB  THR A 732     4748   4431   3587     16    137      5       C  
ATOM   6006  OG1 THR A 732     -14.579 -20.898 -41.481  1.00 33.25           O  
ANISOU 6006  OG1 THR A 732     4682   4411   3542    -37     72    -24       O  
ATOM   6007  CG2 THR A 732     -15.834 -22.637 -40.434  1.00 31.90           C  
ANISOU 6007  CG2 THR A 732     4521   4149   3450      3    188      7       C  
ATOM   6008  N   GLN A 733     -12.937 -19.200 -39.095  1.00 36.15           N  
ANISOU 6008  N   GLN A 733     5082   4872   3780     57     51     -1       N  
ATOM   6009  CA  GLN A 733     -11.559 -18.692 -39.069  1.00 34.17           C  
ANISOU 6009  CA  GLN A 733     4831   4678   3474     72     12    -19       C  
ATOM   6010  C   GLN A 733     -11.272 -17.821 -37.854  1.00 35.05           C  
ANISOU 6010  C   GLN A 733     4951   4821   3545    114      0    -17       C  
ATOM   6011  O   GLN A 733     -10.146 -17.362 -37.665  1.00 36.30           O  
ANISOU 6011  O   GLN A 733     5104   5025   3662    132    -32    -38       O  
ATOM   6012  CB  GLN A 733     -11.252 -17.902 -40.353  1.00 34.81           C  
ANISOU 6012  CB  GLN A 733     4888   4778   3559     12    -37    -48       C  
ATOM   6013  CG  GLN A 733     -11.596 -18.641 -41.644  1.00 34.79           C  
ANISOU 6013  CG  GLN A 733     4881   4747   3591    -31    -35    -55       C  
ATOM   6014  CD  GLN A 733     -11.045 -20.057 -41.673  1.00 35.98           C  
ANISOU 6014  CD  GLN A 733     5043   4887   3739     -5      1    -49       C  
ATOM   6015  OE1 GLN A 733     -11.791 -21.026 -41.512  1.00 36.69           O  
ANISOU 6015  OE1 GLN A 733     5140   4935   3865      4     43    -34       O  
ATOM   6016  NE2 GLN A 733      -9.734 -20.183 -41.870  1.00 30.09           N  
ANISOU 6016  NE2 GLN A 733     4298   4176   2958      6    -12    -64       N  
ATOM   6017  N   LYS A 734     -12.292 -17.608 -37.031  1.00 35.39           N  
ANISOU 6017  N   LYS A 734     5007   4836   3604    129     29      4       N  
ATOM   6018  CA  LYS A 734     -12.213 -16.682 -35.914  1.00 35.19           C  
ANISOU 6018  CA  LYS A 734     4993   4836   3543    164     19      5       C  
ATOM   6019  C   LYS A 734     -11.994 -17.433 -34.619  1.00 34.51           C  
ANISOU 6019  C   LYS A 734     4951   4746   3416    243     60     29       C  
ATOM   6020  O   LYS A 734     -12.699 -18.404 -34.335  1.00 35.66           O  
ANISOU 6020  O   LYS A 734     5120   4844   3585    262    119     59       O  
ATOM   6021  CB  LYS A 734     -13.503 -15.872 -35.822  1.00 37.80           C  
ANISOU 6021  CB  LYS A 734     5312   5135   3915    132     27     12       C  
ATOM   6022  CG  LYS A 734     -13.711 -14.859 -36.947  1.00 44.21           C  
ANISOU 6022  CG  LYS A 734     6088   5954   4755     65    -22    -11       C  
ATOM   6023  CD  LYS A 734     -15.133 -14.273 -36.914  1.00 52.24           C  
ANISOU 6023  CD  LYS A 734     7093   6931   5826     37    -11     -2       C  
ATOM   6024  CE  LYS A 734     -15.288 -13.107 -35.928  1.00 56.80           C  
ANISOU 6024  CE  LYS A 734     7674   7525   6384     54    -17     -3       C  
ATOM   6025  NZ  LYS A 734     -14.798 -11.803 -36.485  1.00 57.58           N  
ANISOU 6025  NZ  LYS A 734     7748   7659   6471     19    -72    -29       N  
ATOM   6026  N   SER A 735     -11.021 -16.975 -33.832  1.00 34.26           N  
ANISOU 6026  N   SER A 735     4930   4763   3325    291     29     14       N  
ATOM   6027  CA  SER A 735     -10.726 -17.560 -32.528  1.00 32.59           C  
ANISOU 6027  CA  SER A 735     4769   4556   3059    377     57     35       C  
ATOM   6028  C   SER A 735     -11.877 -17.365 -31.539  1.00 33.60           C  
ANISOU 6028  C   SER A 735     4933   4645   3190    402    107     65       C  
ATOM   6029  O   SER A 735     -11.976 -18.088 -30.551  1.00 32.70           O  
ANISOU 6029  O   SER A 735     4873   4512   3041    470    155     95       O  
ATOM   6030  CB  SER A 735      -9.432 -16.979 -31.956  1.00 34.52           C  
ANISOU 6030  CB  SER A 735     5010   4865   3241    423     -2      0       C  
ATOM   6031  OG  SER A 735      -9.570 -15.594 -31.677  1.00 35.01           O  
ANISOU 6031  OG  SER A 735     5052   4950   3299    403    -37    -25       O  
ATOM   6032  N   SER A 736     -12.739 -16.387 -31.821  1.00 31.89           N  
ANISOU 6032  N   SER A 736     4687   4414   3014    347    100     57       N  
ATOM   6033  CA  SER A 736     -13.923 -16.112 -31.011  1.00 32.15           C  
ANISOU 6033  CA  SER A 736     4745   4404   3065    358    151     82       C  
ATOM   6034  C   SER A 736     -15.054 -17.139 -31.166  1.00 32.00           C  
ANISOU 6034  C   SER A 736     4738   4312   3110    347    229    116       C  
ATOM   6035  O   SER A 736     -15.914 -17.251 -30.296  1.00 34.39           O  
ANISOU 6035  O   SER A 736     5074   4570   3422    374    292    142       O  
ATOM   6036  CB  SER A 736     -14.469 -14.726 -31.338  1.00 30.81           C  
ANISOU 6036  CB  SER A 736     4536   4242   2929    301    115     60       C  
ATOM   6037  OG  SER A 736     -14.679 -14.608 -32.732  1.00 33.12           O  
ANISOU 6037  OG  SER A 736     4779   4527   3278    227     87     45       O  
ATOM   6038  N   THR A 737     -15.066 -17.863 -32.275  1.00 29.39           N  
ANISOU 6038  N   THR A 737     4378   3964   2824    304    227    111       N  
ATOM   6039  CA  THR A 737     -16.098 -18.851 -32.533  1.00 30.33           C  
ANISOU 6039  CA  THR A 737     4498   4013   3015    288    297    132       C  
ATOM   6040  C   THR A 737     -15.819 -20.131 -31.728  1.00 32.97           C  
ANISOU 6040  C   THR A 737     4889   4320   3317    359    366    166       C  
ATOM   6041  O   THR A 737     -14.683 -20.613 -31.709  1.00 32.33           O  
ANISOU 6041  O   THR A 737     4827   4278   3181    397    342    165       O  
ATOM   6042  CB  THR A 737     -16.156 -19.152 -34.042  1.00 31.41           C  
ANISOU 6042  CB  THR A 737     4585   4144   3207    219    264    109       C  
ATOM   6043  OG1 THR A 737     -16.388 -17.931 -34.757  1.00 29.18           O  
ANISOU 6043  OG1 THR A 737     4260   3884   2944    162    200     82       O  
ATOM   6044  CG2 THR A 737     -17.251 -20.139 -34.391  1.00 31.25           C  
ANISOU 6044  CG2 THR A 737     4554   4049   3271    196    329    120       C  
ATOM   6045  N   PRO A 738     -16.846 -20.678 -31.048  1.00 27.34           N  
ANISOU 6045  N   PRO A 738     3547   3890   2952    271     35    503       N  
ATOM   6046  CA  PRO A 738     -16.679 -21.950 -30.343  1.00 28.53           C  
ANISOU 6046  CA  PRO A 738     3664   4063   3111    306     72    579       C  
ATOM   6047  C   PRO A 738     -15.987 -23.013 -31.200  1.00 29.43           C  
ANISOU 6047  C   PRO A 738     3802   4096   3283    271     92    588       C  
ATOM   6048  O   PRO A 738     -16.189 -23.067 -32.416  1.00 28.99           O  
ANISOU 6048  O   PRO A 738     3782   3967   3266    210     86    556       O  
ATOM   6049  CB  PRO A 738     -18.113 -22.372 -30.042  1.00 28.53           C  
ANISOU 6049  CB  PRO A 738     3641   4076   3123    306     86    646       C  
ATOM   6050  CG  PRO A 738     -18.848 -21.107 -29.903  1.00 29.28           C  
ANISOU 6050  CG  PRO A 738     3732   4214   3178    318     54    596       C  
ATOM   6051  CD  PRO A 738     -18.200 -20.127 -30.860  1.00 27.14           C  
ANISOU 6051  CD  PRO A 738     3511   3887   2916    280     19    510       C  
ATOM   6052  N   LYS A 739     -15.159 -23.836 -30.570  1.00 31.66           N  
ANISOU 6052  N   LYS A 739     4063   4399   3569    317    113    627       N  
ATOM   6053  CA  LYS A 739     -14.445 -24.882 -31.297  1.00 37.70           C  
ANISOU 6053  CA  LYS A 739     4845   5087   4392    301    129    626       C  
ATOM   6054  C   LYS A 739     -15.360 -25.795 -32.111  1.00 38.25           C  
ANISOU 6054  C   LYS A 739     4935   5058   4539    249    142    655       C  
ATOM   6055  O   LYS A 739     -15.152 -25.967 -33.312  1.00 38.92           O  
ANISOU 6055  O   LYS A 739     5050   5078   4659    200    138    597       O  
ATOM   6056  CB  LYS A 739     -13.550 -25.698 -30.353  1.00 39.76           C  
ANISOU 6056  CB  LYS A 739     5075   5384   4650    374    146    680       C  
ATOM   6057  CG  LYS A 739     -12.170 -25.080 -30.175  1.00 46.98           C  
ANISOU 6057  CG  LYS A 739     5974   6365   5512    404    132    613       C  
ATOM   6058  CD  LYS A 739     -11.373 -25.121 -31.484  1.00 50.87           C  
ANISOU 6058  CD  LYS A 739     6494   6799   6036    356    130    532       C  
ATOM   6059  CE  LYS A 739     -10.318 -24.031 -31.536  1.00 54.94           C  
ANISOU 6059  CE  LYS A 739     6997   7385   6493    348    110    451       C  
ATOM   6060  NZ  LYS A 739     -10.896 -22.677 -31.792  1.00 56.50           N  
ANISOU 6060  NZ  LYS A 739     7215   7592   6660    295     85    409       N  
ATOM   6061  N   ALA A 740     -16.372 -26.363 -31.459  1.00 38.26           N  
ANISOU 6061  N   ALA A 740     4916   5060   4561    257    157    742       N  
ATOM   6062  CA  ALA A 740     -17.274 -27.312 -32.111  1.00 38.81           C  
ANISOU 6062  CA  ALA A 740     4997   5035   4713    203    169    774       C  
ATOM   6063  C   ALA A 740     -18.053 -26.655 -33.245  1.00 37.15           C  
ANISOU 6063  C   ALA A 740     4811   4801   4504    134    148    705       C  
ATOM   6064  O   ALA A 740     -18.330 -27.287 -34.259  1.00 39.02           O  
ANISOU 6064  O   ALA A 740     5067   4957   4803     81    148    676       O  
ATOM   6065  CB  ALA A 740     -18.212 -27.942 -31.103  1.00 37.70           C  
ANISOU 6065  CB  ALA A 740     4820   4916   4588    216    190    890       C  
ATOM   6066  N   VAL A 741     -18.371 -25.377 -33.070  1.00 35.97           N  
ANISOU 6066  N   VAL A 741     4658   4723   4285    141    127    675       N  
ATOM   6067  CA  VAL A 741     -19.042 -24.578 -34.090  1.00 33.65           C  
ANISOU 6067  CA  VAL A 741     4387   4416   3982     89    100    617       C  
ATOM   6068  C   VAL A 741     -18.157 -24.336 -35.319  1.00 34.02           C  
ANISOU 6068  C   VAL A 741     4473   4423   4031     51     87    537       C  
ATOM   6069  O   VAL A 741     -18.611 -24.535 -36.445  1.00 34.60           O  
ANISOU 6069  O   VAL A 741     4564   4453   4130     -4     78    505       O  
ATOM   6070  CB  VAL A 741     -19.541 -23.242 -33.514  1.00 32.77           C  
ANISOU 6070  CB  VAL A 741     4265   4383   3805    118     76    605       C  
ATOM   6071  CG1 VAL A 741     -20.159 -22.400 -34.597  1.00 29.42           C  
ANISOU 6071  CG1 VAL A 741     3867   3936   3374     72     43    554       C  
ATOM   6072  CG2 VAL A 741     -20.542 -23.501 -32.418  1.00 35.54           C  
ANISOU 6072  CG2 VAL A 741     4566   4793   4144    152     92    677       C  
ATOM   6073  N   GLN A 742     -16.911 -23.905 -35.104  1.00 31.95           N  
ANISOU 6073  N   GLN A 742     4216   4190   3734     78     85    505       N  
ATOM   6074  CA  GLN A 742     -15.941 -23.816 -36.186  1.00 32.85           C  
ANISOU 6074  CA  GLN A 742     4354   4283   3845     43     81    439       C  
ATOM   6075  C   GLN A 742     -15.984 -25.112 -36.988  1.00 34.29           C  
ANISOU 6075  C   GLN A 742     4541   4397   4091     17     99    426       C  
ATOM   6076  O   GLN A 742     -16.111 -25.092 -38.216  1.00 33.86           O  
ANISOU 6076  O   GLN A 742     4504   4321   4039    -36     89    375       O  
ATOM   6077  CB  GLN A 742     -14.509 -23.602 -35.663  1.00 32.53           C  
ANISOU 6077  CB  GLN A 742     4300   4285   3773     82     87    417       C  
ATOM   6078  CG  GLN A 742     -14.244 -22.306 -34.877  1.00 31.98           C  
ANISOU 6078  CG  GLN A 742     4223   4281   3645    106     65    407       C  
ATOM   6079  CD  GLN A 742     -12.801 -22.209 -34.384  1.00 33.99           C  
ANISOU 6079  CD  GLN A 742     4455   4586   3872    139     70    379       C  
ATOM   6080  OE1 GLN A 742     -12.142 -23.222 -34.166  1.00 35.49           O  
ANISOU 6080  OE1 GLN A 742     4626   4775   4082    175     93    393       O  
ATOM   6081  NE2 GLN A 742     -12.310 -20.988 -34.205  1.00 27.67           N  
ANISOU 6081  NE2 GLN A 742     3656   3828   3030    128     45    338       N  
ATOM   6082  N   LYS A 743     -15.899 -26.232 -36.273  1.00 34.12           N  
ANISOU 6082  N   LYS A 743     4501   4343   4121     57    121    475       N  
ATOM   6083  CA  LYS A 743     -15.800 -27.560 -36.876  1.00 35.64           C  
ANISOU 6083  CA  LYS A 743     4699   4452   4392     44    135    459       C  
ATOM   6084  C   LYS A 743     -17.034 -27.898 -37.708  1.00 35.28           C  
ANISOU 6084  C   LYS A 743     4660   4355   4389    -20    126    447       C  
ATOM   6085  O   LYS A 743     -16.907 -28.365 -38.842  1.00 36.10           O  
ANISOU 6085  O   LYS A 743     4776   4418   4521    -57    122    375       O  
ATOM   6086  CB  LYS A 743     -15.564 -28.604 -35.785  1.00 37.08           C  
ANISOU 6086  CB  LYS A 743     4862   4601   4627    103    156    537       C  
ATOM   6087  CG  LYS A 743     -15.168 -29.997 -36.266  1.00 39.29           C  
ANISOU 6087  CG  LYS A 743     5148   4779   5002    110    166    517       C  
ATOM   6088  CD  LYS A 743     -14.635 -30.821 -35.076  1.00 43.63           C  
ANISOU 6088  CD  LYS A 743     5680   5308   5589    186    182    606       C  
ATOM   6089  CE  LYS A 743     -14.963 -32.304 -35.203  1.00 47.42           C  
ANISOU 6089  CE  LYS A 743     6168   5654   6196    181    189    640       C  
ATOM   6090  NZ  LYS A 743     -14.333 -32.934 -36.398  1.00 48.59           N  
ANISOU 6090  NZ  LYS A 743     6333   5729   6401    174    181    525       N  
ATOM   6091  N   ALA A 744     -18.217 -27.638 -37.156  1.00 34.17           N  
ANISOU 6091  N   ALA A 744     4506   4231   4246    -32    123    508       N  
ATOM   6092  CA  ALA A 744     -19.477 -27.917 -37.855  1.00 35.08           C  
ANISOU 6092  CA  ALA A 744     4618   4312   4398    -94    113    500       C  
ATOM   6093  C   ALA A 744     -19.709 -26.986 -39.048  1.00 33.98           C  
ANISOU 6093  C   ALA A 744     4498   4210   4204   -139     84    426       C  
ATOM   6094  O   ALA A 744     -20.111 -27.443 -40.135  1.00 34.52           O  
ANISOU 6094  O   ALA A 744     4570   4246   4301   -190     74    372       O  
ATOM   6095  CB  ALA A 744     -20.652 -27.858 -36.886  1.00 33.89           C  
ANISOU 6095  CB  ALA A 744     4436   4190   4251    -91    119    588       C  
ATOM   6096  N   LEU A 745     -19.438 -25.694 -38.856  1.00 30.38           N  
ANISOU 6096  N   LEU A 745     4051   3820   3671   -119     69    425       N  
ATOM   6097  CA  LEU A 745     -19.510 -24.727 -39.952  1.00 30.51           C  
ANISOU 6097  CA  LEU A 745     4090   3869   3633   -158     41    373       C  
ATOM   6098  C   LEU A 745     -18.540 -25.068 -41.085  1.00 32.29           C  
ANISOU 6098  C   LEU A 745     4330   4085   3852   -186     45    300       C  
ATOM   6099  O   LEU A 745     -18.867 -24.902 -42.262  1.00 34.77           O  
ANISOU 6099  O   LEU A 745     4652   4414   4143   -233     27    256       O  
ATOM   6100  CB  LEU A 745     -19.275 -23.296 -39.452  1.00 29.86           C  
ANISOU 6100  CB  LEU A 745     4019   3839   3486   -130     21    389       C  
ATOM   6101  CG  LEU A 745     -20.351 -22.656 -38.562  1.00 30.59           C  
ANISOU 6101  CG  LEU A 745     4095   3963   3566    -99      7    437       C  
ATOM   6102  CD1 LEU A 745     -19.931 -21.249 -38.191  1.00 26.72           C  
ANISOU 6102  CD1 LEU A 745     3621   3507   3024    -71    -18    428       C  
ATOM   6103  CD2 LEU A 745     -21.720 -22.654 -39.245  1.00 20.49           C  
ANISOU 6103  CD2 LEU A 745     2806   2684   2297   -136    -14    438       C  
ATOM   6104  N   LYS A 746     -17.356 -25.559 -40.730  1.00 34.10           N  
ANISOU 6104  N   LYS A 746     4557   4304   4095   -152     67    287       N  
ATOM   6105  CA  LYS A 746     -16.398 -26.006 -41.726  1.00 36.50           C  
ANISOU 6105  CA  LYS A 746     4863   4610   4394   -169     75    211       C  
ATOM   6106  C   LYS A 746     -16.933 -27.191 -42.532  1.00 37.20           C  
ANISOU 6106  C   LYS A 746     4946   4644   4546   -198     77    160       C  
ATOM   6107  O   LYS A 746     -16.803 -27.217 -43.756  1.00 40.46           O  
ANISOU 6107  O   LYS A 746     5359   5084   4929   -236     68     86       O  
ATOM   6108  CB  LYS A 746     -15.045 -26.351 -41.098  1.00 38.24           C  
ANISOU 6108  CB  LYS A 746     5073   4836   4621   -115     98    205       C  
ATOM   6109  CG  LYS A 746     -13.985 -26.649 -42.145  1.00 39.13           C  
ANISOU 6109  CG  LYS A 746     5180   4977   4713   -127    107    118       C  
ATOM   6110  CD  LYS A 746     -12.594 -26.621 -41.582  1.00 42.76           C  
ANISOU 6110  CD  LYS A 746     5621   5472   5154    -78    123    110       C  
ATOM   6111  CE  LYS A 746     -11.584 -26.863 -42.690  1.00 43.48           C  
ANISOU 6111  CE  LYS A 746     5695   5611   5213    -92    134     18       C  
ATOM   6112  NZ  LYS A 746     -10.226 -27.079 -42.142  1.00 47.50           N  
ANISOU 6112  NZ  LYS A 746     6176   6155   5717    -34    151      1       N  
ATOM   6113  N   GLU A 747     -17.532 -28.160 -41.850  1.00 34.54           N  
ANISOU 6113  N   GLU A 747     4598   4232   4293   -183     87    200       N  
ATOM   6114  CA  GLU A 747     -18.108 -29.320 -42.530  1.00 35.34           C  
ANISOU 6114  CA  GLU A 747     4692   4261   4473   -216     84    150       C  
ATOM   6115  C   GLU A 747     -19.310 -28.929 -43.407  1.00 35.38           C  
ANISOU 6115  C   GLU A 747     4693   4299   4453   -281     57    125       C  
ATOM   6116  O   GLU A 747     -19.506 -29.498 -44.476  1.00 34.10           O  
ANISOU 6116  O   GLU A 747     4524   4123   4308   -319     46     40       O  
ATOM   6117  CB  GLU A 747     -18.472 -30.419 -41.520  1.00 35.47           C  
ANISOU 6117  CB  GLU A 747     4698   4182   4595   -194    100    217       C  
ATOM   6118  CG  GLU A 747     -19.045 -31.710 -42.108  1.00 36.53           C  
ANISOU 6118  CG  GLU A 747     4826   4216   4837   -233     94    168       C  
ATOM   6119  CD  GLU A 747     -18.154 -32.382 -43.136  1.00 36.28           C  
ANISOU 6119  CD  GLU A 747     4800   4156   4831   -225     91     43       C  
ATOM   6120  OE1 GLU A 747     -18.676 -33.236 -43.882  1.00 40.94           O  
ANISOU 6120  OE1 GLU A 747     5382   4680   5492   -266     77    -31       O  
ATOM   6121  OE2 GLU A 747     -16.947 -32.069 -43.213  1.00 35.12           O  
ANISOU 6121  OE2 GLU A 747     4657   4057   4630   -178    101     10       O  
ATOM   6122  N   CYS A 748     -20.095 -27.947 -42.967  1.00 34.45           N  
ANISOU 6122  N   CYS A 748     4574   4228   4287   -286     45    191       N  
ATOM   6123  CA  CYS A 748     -21.187 -27.436 -43.788  1.00 34.71           C  
ANISOU 6123  CA  CYS A 748     4599   4304   4283   -336     15    172       C  
ATOM   6124  C   CYS A 748     -20.654 -26.845 -45.095  1.00 33.17           C  
ANISOU 6124  C   CYS A 748     4418   4176   4007   -361     -2    101       C  
ATOM   6125  O   CYS A 748     -21.161 -27.149 -46.176  1.00 35.38           O  
ANISOU 6125  O   CYS A 748     4686   4477   4279   -405    -21     37       O  
ATOM   6126  CB  CYS A 748     -21.998 -26.387 -43.025  1.00 35.67           C  
ANISOU 6126  CB  CYS A 748     4717   4470   4365   -319      2    252       C  
ATOM   6127  SG  CYS A 748     -23.097 -27.062 -41.765  1.00 39.47           S  
ANISOU 6127  SG  CYS A 748     5163   4913   4921   -311     18    335       S  
ATOM   6128  N   ILE A 749     -19.626 -26.009 -44.981  1.00 31.79           N  
ANISOU 6128  N   ILE A 749     4264   4045   3771   -337      4    113       N  
ATOM   6129  CA  ILE A 749     -18.939 -25.424 -46.134  1.00 28.45           C  
ANISOU 6129  CA  ILE A 749     3850   3695   3266   -363     -5     63       C  
ATOM   6130  C   ILE A 749     -18.278 -26.489 -47.003  1.00 29.39           C  
ANISOU 6130  C   ILE A 749     3953   3813   3402   -374      9    -37       C  
ATOM   6131  O   ILE A 749     -18.366 -26.429 -48.231  1.00 34.25           O  
ANISOU 6131  O   ILE A 749     4559   4493   3962   -412     -5    -99       O  
ATOM   6132  CB  ILE A 749     -17.893 -24.371 -45.695  1.00 27.58           C  
ANISOU 6132  CB  ILE A 749     3758   3621   3101   -342      1    103       C  
ATOM   6133  CG1 ILE A 749     -18.589 -23.148 -45.092  1.00 27.38           C  
ANISOU 6133  CG1 ILE A 749     3749   3602   3050   -334    -24    180       C  
ATOM   6134  CG2 ILE A 749     -17.009 -23.952 -46.876  1.00 29.77           C  
ANISOU 6134  CG2 ILE A 749     4036   3977   3298   -377      2     56       C  
ATOM   6135  CD1 ILE A 749     -17.668 -22.234 -44.268  1.00 28.56           C  
ANISOU 6135  CD1 ILE A 749     3914   3761   3177   -306    -19    218       C  
ATOM   6136  N   ARG A 750     -17.625 -27.469 -46.386  1.00 30.63           N  
ANISOU 6136  N   ARG A 750     4103   3903   3632   -335     35    -57       N  
ATOM   6137  CA  ARG A 750     -17.041 -28.555 -47.158  1.00 33.72           C  
ANISOU 6137  CA  ARG A 750     4477   4279   4054   -333     45   -165       C  
ATOM   6138  C   ARG A 750     -18.129 -29.176 -48.024  1.00 35.16           C  
ANISOU 6138  C   ARG A 750     4645   4447   4267   -380     22   -229       C  
ATOM   6139  O   ARG A 750     -17.968 -29.290 -49.238  1.00 37.98           O  
ANISOU 6139  O   ARG A 750     4986   4872   4572   -406     12   -324       O  
ATOM   6140  CB  ARG A 750     -16.393 -29.624 -46.265  1.00 33.84           C  
ANISOU 6140  CB  ARG A 750     4490   4199   4170   -275     69   -166       C  
ATOM   6141  CG  ARG A 750     -15.518 -30.603 -47.055  1.00 33.18           C  
ANISOU 6141  CG  ARG A 750     4388   4107   4111   -255     78   -290       C  
ATOM   6142  CD  ARG A 750     -15.212 -31.890 -46.298  1.00 35.05           C  
ANISOU 6142  CD  ARG A 750     4625   4215   4477   -199     90   -294       C  
ATOM   6143  NE  ARG A 750     -16.419 -32.646 -45.966  1.00 38.49           N  
ANISOU 6143  NE  ARG A 750     5066   4539   5020   -228     77   -263       N  
ATOM   6144  CZ  ARG A 750     -17.094 -33.422 -46.815  1.00 40.99           C  
ANISOU 6144  CZ  ARG A 750     5372   4810   5394   -269     58   -354       C  
ATOM   6145  NH1 ARG A 750     -16.709 -33.555 -48.081  1.00 38.58           N  
ANISOU 6145  NH1 ARG A 750     5049   4570   5040   -281     48   -490       N  
ATOM   6146  NH2 ARG A 750     -18.175 -34.061 -46.395  1.00 43.06           N  
ANISOU 6146  NH2 ARG A 750     5635   4969   5757   -303     48   -312       N  
ATOM   6147  N   ARG A 751     -19.249 -29.527 -47.399  1.00 35.36           N  
ANISOU 6147  N   ARG A 751     4668   4398   4367   -393     13   -178       N  
ATOM   6148  CA  ARG A 751     -20.367 -30.170 -48.098  1.00 37.13           C  
ANISOU 6148  CA  ARG A 751     4872   4602   4634   -444    -11   -237       C  
ATOM   6149  C   ARG A 751     -20.986 -29.303 -49.187  1.00 37.89           C  
ANISOU 6149  C   ARG A 751     4958   4816   4623   -488    -42   -261       C  
ATOM   6150  O   ARG A 751     -21.271 -29.796 -50.279  1.00 40.97           O  
ANISOU 6150  O   ARG A 751     5324   5239   5002   -522    -60   -364       O  
ATOM   6151  CB  ARG A 751     -21.426 -30.648 -47.104  1.00 36.72           C  
ANISOU 6151  CB  ARG A 751     4813   4459   4681   -455    -10   -159       C  
ATOM   6152  CG  ARG A 751     -20.923 -31.781 -46.226  1.00 37.77           C  
ANISOU 6152  CG  ARG A 751     4951   4467   4934   -421     15   -142       C  
ATOM   6153  CD  ARG A 751     -21.868 -32.122 -45.102  1.00 38.61           C  
ANISOU 6153  CD  ARG A 751     5048   4502   5122   -432     22    -34       C  
ATOM   6154  NE  ARG A 751     -21.403 -33.324 -44.409  1.00 41.64           N  
ANISOU 6154  NE  ARG A 751     5437   4757   5629   -404     42    -14       N  
ATOM   6155  CZ  ARG A 751     -21.988 -34.519 -44.476  1.00 41.52           C  
ANISOU 6155  CZ  ARG A 751     5409   4626   5741   -445     36    -38       C  
ATOM   6156  NH1 ARG A 751     -23.099 -34.694 -45.184  1.00 41.85           N  
ANISOU 6156  NH1 ARG A 751     5425   4675   5803   -519     11    -90       N  
ATOM   6157  NH2 ARG A 751     -21.462 -35.544 -43.814  1.00 41.54           N  
ANISOU 6157  NH2 ARG A 751     5424   4504   5858   -411     51     -6       N  
ATOM   6158  N   MET A 752     -21.173 -28.016 -48.902  1.00 36.53           N  
ANISOU 6158  N   MET A 752     4802   4705   4373   -482    -50   -170       N  
ATOM   6159  CA  MET A 752     -21.647 -27.062 -49.912  1.00 36.11           C  
ANISOU 6159  CA  MET A 752     4745   4763   4212   -514    -82   -172       C  
ATOM   6160  C   MET A 752     -20.764 -27.059 -51.165  1.00 37.01           C  
ANISOU 6160  C   MET A 752     4852   4970   4242   -529    -81   -259       C  
ATOM   6161  O   MET A 752     -21.258 -27.189 -52.284  1.00 39.71           O  
ANISOU 6161  O   MET A 752     5168   5386   4532   -565   -106   -326       O  
ATOM   6162  CB  MET A 752     -21.701 -25.649 -49.323  1.00 35.91           C  
ANISOU 6162  CB  MET A 752     4747   4768   4129   -494    -91    -59       C  
ATOM   6163  CG  MET A 752     -22.865 -25.403 -48.379  1.00 33.81           C  
ANISOU 6163  CG  MET A 752     4476   4460   3910   -482   -103     17       C  
ATOM   6164  SD  MET A 752     -22.674 -23.863 -47.458  1.00 39.18           S  
ANISOU 6164  SD  MET A 752     5189   5152   4544   -438   -110    126       S  
ATOM   6165  CE  MET A 752     -23.171 -22.673 -48.680  1.00 34.29           C  
ANISOU 6165  CE  MET A 752     4580   4628   3821   -464   -158    141       C  
ATOM   6166  N   LEU A 753     -19.453 -26.939 -50.961  1.00 36.05           N  
ANISOU 6166  N   LEU A 753     4742   4855   4099   -502    -51   -260       N  
ATOM   6167  CA  LEU A 753     -18.521 -26.720 -52.052  1.00 34.30           C  
ANISOU 6167  CA  LEU A 753     4508   4746   3779   -515    -44   -323       C  
ATOM   6168  C   LEU A 753     -18.131 -28.004 -52.787  1.00 36.09           C  
ANISOU 6168  C   LEU A 753     4701   4977   4035   -511    -35   -470       C  
ATOM   6169  O   LEU A 753     -17.794 -27.969 -53.971  1.00 37.42           O  
ANISOU 6169  O   LEU A 753     4842   5265   4109   -532    -39   -547       O  
ATOM   6170  CB  LEU A 753     -17.263 -26.004 -51.544  1.00 33.93           C  
ANISOU 6170  CB  LEU A 753     4478   4718   3694   -493    -17   -266       C  
ATOM   6171  CG  LEU A 753     -17.357 -24.749 -50.658  1.00 32.13           C  
ANISOU 6171  CG  LEU A 753     4286   4470   3453   -487    -24   -137       C  
ATOM   6172  CD1 LEU A 753     -16.010 -24.018 -50.595  1.00 23.25           C  
ANISOU 6172  CD1 LEU A 753     3167   3399   2269   -487     -2   -110       C  
ATOM   6173  CD2 LEU A 753     -18.445 -23.802 -51.112  1.00 32.75           C  
ANISOU 6173  CD2 LEU A 753     4377   4589   3478   -518    -64    -74       C  
ATOM   6174  N   GLN A 754     -18.169 -29.129 -52.083  1.00 35.01           N  
ANISOU 6174  N   GLN A 754     4564   4713   4027   -483    -23   -508       N  
ATOM   6175  CA  GLN A 754     -17.696 -30.391 -52.628  1.00 35.96           C  
ANISOU 6175  CA  GLN A 754     4657   4807   4201   -466    -17   -652       C  
ATOM   6176  C   GLN A 754     -18.823 -31.326 -53.019  1.00 38.35           C  
ANISOU 6176  C   GLN A 754     4940   5048   4582   -498    -45   -733       C  
ATOM   6177  O   GLN A 754     -18.659 -32.141 -53.928  1.00 39.37           O  
ANISOU 6177  O   GLN A 754     5039   5201   4719   -501    -55   -879       O  
ATOM   6178  CB  GLN A 754     -16.765 -31.097 -51.638  1.00 37.18           C  
ANISOU 6178  CB  GLN A 754     4823   4850   4453   -403     14   -648       C  
ATOM   6179  CG  GLN A 754     -15.347 -30.509 -51.568  1.00 36.77           C  
ANISOU 6179  CG  GLN A 754     4768   4881   4321   -368     43   -633       C  
ATOM   6180  CD  GLN A 754     -14.488 -31.161 -50.495  1.00 39.46           C  
ANISOU 6180  CD  GLN A 754     5117   5118   4758   -298     68   -617       C  
ATOM   6181  OE1 GLN A 754     -14.807 -32.236 -49.982  1.00 42.40           O  
ANISOU 6181  OE1 GLN A 754     5496   5355   5260   -272     64   -637       O  
ATOM   6182  NE2 GLN A 754     -13.396 -30.508 -50.146  1.00 40.29           N  
ANISOU 6182  NE2 GLN A 754     5219   5288   4800   -271     91   -575       N  
ATOM   6183  N   GLU A 755     -19.972 -31.194 -52.357  1.00 39.59           N  
ANISOU 6183  N   GLU A 755     5110   5136   4798   -524    -61   -645       N  
ATOM   6184  CA  GLU A 755     -21.003 -32.228 -52.421  1.00 42.47           C  
ANISOU 6184  CA  GLU A 755     5454   5409   5274   -559    -83   -706       C  
ATOM   6185  C   GLU A 755     -22.399 -31.720 -52.796  1.00 42.07           C  
ANISOU 6185  C   GLU A 755     5383   5419   5182   -616   -119   -676       C  
ATOM   6186  O   GLU A 755     -23.152 -32.428 -53.457  1.00 44.57           O  
ANISOU 6186  O   GLU A 755     5666   5730   5537   -658   -146   -776       O  
ATOM   6187  CB  GLU A 755     -21.035 -33.029 -51.107  1.00 42.31           C  
ANISOU 6187  CB  GLU A 755     5453   5214   5409   -535    -64   -642       C  
ATOM   6188  CG  GLU A 755     -19.870 -34.016 -50.923  1.00 45.41           C  
ANISOU 6188  CG  GLU A 755     5854   5517   5885   -480    -42   -714       C  
ATOM   6189  CD  GLU A 755     -19.806 -34.622 -49.515  1.00 49.98           C  
ANISOU 6189  CD  GLU A 755     6456   5938   6597   -447    -22   -611       C  
ATOM   6190  OE1 GLU A 755     -18.735 -35.148 -49.135  1.00 49.41           O  
ANISOU 6190  OE1 GLU A 755     6396   5805   6574   -384     -2   -628       O  
ATOM   6191  OE2 GLU A 755     -20.821 -34.574 -48.783  1.00 48.80           O  
ANISOU 6191  OE2 GLU A 755     6307   5735   6499   -482    -25   -509       O  
ATOM   6192  N   GLY A 756     -22.751 -30.511 -52.376  1.00 40.98           N  
ANISOU 6192  N   GLY A 756     5262   5338   4969   -613   -121   -548       N  
ATOM   6193  CA  GLY A 756     -24.015 -29.915 -52.800  1.00 41.53           C  
ANISOU 6193  CA  GLY A 756     5310   5485   4986   -653   -159   -519       C  
ATOM   6194  C   GLY A 756     -25.038 -29.674 -51.711  1.00 43.67           C  
ANISOU 6194  C   GLY A 756     5581   5693   5320   -658   -161   -405       C  
ATOM   6195  O   GLY A 756     -24.777 -29.921 -50.525  1.00 44.33           O  
ANISOU 6195  O   GLY A 756     5684   5674   5484   -631   -132   -334       O  
ATOM   6196  N   GLU A 757     -26.213 -29.202 -52.133  1.00 44.54           N  
ANISOU 6196  N   GLU A 757     5662   5877   5384   -689   -198   -391       N  
ATOM   6197  CA  GLU A 757     -27.293 -28.778 -51.234  1.00 44.26           C  
ANISOU 6197  CA  GLU A 757     5615   5823   5381   -689   -205   -287       C  
ATOM   6198  C   GLU A 757     -27.839 -29.893 -50.338  1.00 45.36           C  
ANISOU 6198  C   GLU A 757     5731   5840   5665   -716   -187   -278       C  
ATOM   6199  O   GLU A 757     -28.043 -29.684 -49.132  1.00 42.70           O  
ANISOU 6199  O   GLU A 757     5401   5454   5368   -692   -165   -171       O  
ATOM   6200  CB  GLU A 757     -28.438 -28.137 -52.036  1.00 44.59           C  
ANISOU 6200  CB  GLU A 757     5618   5983   5341   -714   -254   -292       C  
ATOM   6201  CG  GLU A 757     -29.604 -27.627 -51.172  1.00 46.89           C  
ANISOU 6201  CG  GLU A 757     5887   6277   5653   -706   -265   -194       C  
ATOM   6202  CD  GLU A 757     -30.565 -26.720 -51.922  1.00 49.58           C  
ANISOU 6202  CD  GLU A 757     6197   6745   5895   -705   -316   -181       C  
ATOM   6203  OE1 GLU A 757     -30.990 -27.081 -53.042  1.00 52.63           O  
ANISOU 6203  OE1 GLU A 757     6545   7206   6245   -746   -349   -272       O  
ATOM   6204  OE2 GLU A 757     -30.903 -25.644 -51.380  1.00 48.06           O  
ANISOU 6204  OE2 GLU A 757     6018   6581   5663   -659   -327    -83       O  
ATOM   6205  N   GLU A 758     -28.083 -31.065 -50.927  1.00 45.19           N  
ANISOU 6205  N   GLU A 758     5679   5773   5720   -767   -197   -390       N  
ATOM   6206  CA  GLU A 758     -28.644 -32.186 -50.177  1.00 47.48           C  
ANISOU 6206  CA  GLU A 758     5946   5936   6160   -807   -184   -380       C  
ATOM   6207  C   GLU A 758     -27.693 -32.683 -49.085  1.00 45.19           C  
ANISOU 6207  C   GLU A 758     5697   5518   5956   -766   -139   -316       C  
ATOM   6208  O   GLU A 758     -28.134 -33.036 -47.990  1.00 44.63           O  
ANISOU 6208  O   GLU A 758     5617   5371   5969   -774   -118   -220       O  
ATOM   6209  CB  GLU A 758     -29.070 -33.336 -51.106  1.00 50.93           C  
ANISOU 6209  CB  GLU A 758     6342   6336   6672   -875   -211   -527       C  
ATOM   6210  CG  GLU A 758     -30.053 -34.326 -50.454  1.00 58.99           C  
ANISOU 6210  CG  GLU A 758     7324   7247   7844   -943   -209   -504       C  
ATOM   6211  CD  GLU A 758     -30.547 -35.423 -51.402  1.00 68.38           C  
ANISOU 6211  CD  GLU A 758     8468   8396   9116  -1020   -245   -663       C  
ATOM   6212  OE1 GLU A 758     -30.767 -36.558 -50.924  1.00 71.31           O  
ANISOU 6212  OE1 GLU A 758     8830   8616   9649  -1069   -236   -670       O  
ATOM   6213  OE2 GLU A 758     -30.725 -35.160 -52.616  1.00 71.95           O  
ANISOU 6213  OE2 GLU A 758     8895   8969   9475  -1033   -283   -779       O  
ATOM   6214  N   SER A 759     -26.393 -32.690 -49.369  1.00 44.89           N  
ANISOU 6214  N   SER A 759     5698   5471   5887   -718   -124   -362       N  
ATOM   6215  CA  SER A 759     -25.427 -33.141 -48.370  1.00 44.12           C  
ANISOU 6215  CA  SER A 759     5636   5265   5862   -668    -86   -305       C  
ATOM   6216  C   SER A 759     -25.383 -32.203 -47.178  1.00 41.39           C  
ANISOU 6216  C   SER A 759     5308   4948   5470   -623    -62   -154       C  
ATOM   6217  O   SER A 759     -25.251 -32.645 -46.036  1.00 40.57           O  
ANISOU 6217  O   SER A 759     5212   4760   5444   -602    -35    -67       O  
ATOM   6218  CB  SER A 759     -24.037 -33.285 -48.957  1.00 42.72           C  
ANISOU 6218  CB  SER A 759     5485   5093   5651   -622    -76   -393       C  
ATOM   6219  OG  SER A 759     -23.147 -33.725 -47.947  1.00 44.34           O  
ANISOU 6219  OG  SER A 759     5719   5200   5928   -568    -43   -333       O  
ATOM   6220  N   LEU A 760     -25.499 -30.910 -47.470  1.00 40.48           N  
ANISOU 6220  N   LEU A 760     5199   4954   5228   -607    -77   -127       N  
ATOM   6221  CA  LEU A 760     -25.514 -29.863 -46.458  1.00 39.88           C  
ANISOU 6221  CA  LEU A 760     5138   4917   5099   -562    -64     -6       C  
ATOM   6222  C   LEU A 760     -26.727 -29.976 -45.532  1.00 40.92           C  
ANISOU 6222  C   LEU A 760     5233   5033   5281   -580    -61     80       C  
ATOM   6223  O   LEU A 760     -26.586 -29.858 -44.312  1.00 41.82           O  
ANISOU 6223  O   LEU A 760     5352   5123   5414   -542    -34    176       O  
ATOM   6224  CB  LEU A 760     -25.432 -28.488 -47.133  1.00 37.04           C  
ANISOU 6224  CB  LEU A 760     4793   4675   4607   -546    -90     -7       C  
ATOM   6225  CG  LEU A 760     -25.396 -27.131 -46.410  1.00 37.72           C  
ANISOU 6225  CG  LEU A 760     4899   4812   4620   -498    -91     89       C  
ATOM   6226  CD1 LEU A 760     -26.672 -26.341 -46.666  1.00 39.73           C  
ANISOU 6226  CD1 LEU A 760     5128   5142   4827   -510   -128    117       C  
ATOM   6227  CD2 LEU A 760     -25.076 -27.186 -44.929  1.00 34.22           C  
ANISOU 6227  CD2 LEU A 760     4463   4316   4221   -452    -58    173       C  
ATOM   6228  N   GLN A 761     -27.903 -30.223 -46.110  1.00 41.94           N  
ANISOU 6228  N   GLN A 761     5318   5189   5426   -639    -88     44       N  
ATOM   6229  CA  GLN A 761     -29.137 -30.368 -45.342  1.00 41.56           C  
ANISOU 6229  CA  GLN A 761     5222   5147   5424   -668    -84    118       C  
ATOM   6230  C   GLN A 761     -29.074 -31.592 -44.439  1.00 44.54           C  
ANISOU 6230  C   GLN A 761     5589   5402   5930   -691    -50    167       C  
ATOM   6231  O   GLN A 761     -29.589 -31.563 -43.317  1.00 44.36           O  
ANISOU 6231  O   GLN A 761     5542   5385   5929   -684    -27    275       O  
ATOM   6232  CB  GLN A 761     -30.352 -30.470 -46.266  1.00 43.30           C  
ANISOU 6232  CB  GLN A 761     5388   5426   5637   -733   -123     54       C  
ATOM   6233  CG  GLN A 761     -30.632 -29.207 -47.072  1.00 42.89           C  
ANISOU 6233  CG  GLN A 761     5338   5503   5455   -707   -162     32       C  
ATOM   6234  CD  GLN A 761     -31.619 -29.414 -48.212  1.00 45.31           C  
ANISOU 6234  CD  GLN A 761     5593   5877   5745   -767   -206    -54       C  
ATOM   6235  OE1 GLN A 761     -31.963 -28.460 -48.922  1.00 47.70           O  
ANISOU 6235  OE1 GLN A 761     5890   6289   5945   -747   -243    -65       O  
ATOM   6236  NE2 GLN A 761     -32.083 -30.649 -48.394  1.00 40.41           N  
ANISOU 6236  NE2 GLN A 761     4933   5191   5229   -840   -206   -114       N  
ATOM   6237  N   GLU A 762     -28.437 -32.657 -44.936  1.00 45.21           N  
ANISOU 6237  N   GLU A 762     5694   5384   6100   -714    -47     90       N  
ATOM   6238  CA  GLU A 762     -28.267 -33.901 -44.187  1.00 47.87           C  
ANISOU 6238  CA  GLU A 762     6032   5581   6577   -733    -21    135       C  
ATOM   6239  C   GLU A 762     -27.409 -33.677 -42.938  1.00 46.85           C  
ANISOU 6239  C   GLU A 762     5934   5432   6436   -657     17    249       C  
ATOM   6240  O   GLU A 762     -27.706 -34.212 -41.868  1.00 46.48           O  
ANISOU 6240  O   GLU A 762     5869   5332   6458   -664     44    359       O  
ATOM   6241  CB  GLU A 762     -27.646 -34.981 -45.078  1.00 50.28           C  
ANISOU 6241  CB  GLU A 762     6356   5778   6971   -756    -34      7       C  
ATOM   6242  CG  GLU A 762     -27.794 -36.393 -44.543  1.00 56.74           C  
ANISOU 6242  CG  GLU A 762     7167   6429   7962   -799    -21     37       C  
ATOM   6243  CD  GLU A 762     -26.786 -37.380 -45.144  1.00 62.09           C  
ANISOU 6243  CD  GLU A 762     7880   6981   8730   -780    -29    -78       C  
ATOM   6244  OE1 GLU A 762     -25.574 -37.048 -45.235  1.00 59.19           O  
ANISOU 6244  OE1 GLU A 762     7553   6635   8302   -700    -19   -106       O  
ATOM   6245  OE2 GLU A 762     -27.214 -38.501 -45.507  1.00 61.77           O  
ANISOU 6245  OE2 GLU A 762     7823   6820   8828   -846    -47   -144       O  
ATOM   6246  N   TYR A 763     -26.363 -32.862 -43.075  1.00 45.06           N  
ANISOU 6246  N   TYR A 763     5748   5259   6114   -587     19    227       N  
ATOM   6247  CA  TYR A 763     -25.466 -32.597 -41.963  1.00 43.86           C  
ANISOU 6247  CA  TYR A 763     5622   5102   5941   -512     49    317       C  
ATOM   6248  C   TYR A 763     -26.070 -31.649 -40.941  1.00 43.25           C  
ANISOU 6248  C   TYR A 763     5521   5120   5790   -485     60    426       C  
ATOM   6249  O   TYR A 763     -26.029 -31.934 -39.746  1.00 44.74           O  
ANISOU 6249  O   TYR A 763     5700   5292   6009   -458     89    532       O  
ATOM   6250  CB  TYR A 763     -24.114 -32.075 -42.443  1.00 43.07           C  
ANISOU 6250  CB  TYR A 763     5565   5030   5770   -455     47    251       C  
ATOM   6251  CG  TYR A 763     -23.064 -32.078 -41.357  1.00 43.99           C  
ANISOU 6251  CG  TYR A 763     5702   5126   5885   -381     76    325       C  
ATOM   6252  CD1 TYR A 763     -22.697 -30.897 -40.705  1.00 42.62           C  
ANISOU 6252  CD1 TYR A 763     5537   5047   5610   -328     82    379       C  
ATOM   6253  CD2 TYR A 763     -22.450 -33.267 -40.962  1.00 43.80           C  
ANISOU 6253  CD2 TYR A 763     5688   4987   5967   -361     93    341       C  
ATOM   6254  CE1 TYR A 763     -21.732 -30.902 -39.695  1.00 40.07           C  
ANISOU 6254  CE1 TYR A 763     5225   4719   5280   -260    105    439       C  
ATOM   6255  CE2 TYR A 763     -21.491 -33.282 -39.953  1.00 44.77           C  
ANISOU 6255  CE2 TYR A 763     5825   5104   6083   -287    116    413       C  
ATOM   6256  CZ  TYR A 763     -21.134 -32.097 -39.328  1.00 43.68           C  
ANISOU 6256  CZ  TYR A 763     5688   5075   5832   -238    123    459       C  
ATOM   6257  OH  TYR A 763     -20.178 -32.116 -38.337  1.00 47.42           O  
ANISOU 6257  OH  TYR A 763     6169   5557   6293   -165    142    521       O  
ATOM   6258  N   PHE A 764     -26.630 -30.535 -41.408  1.00 42.01           N  
ANISOU 6258  N   PHE A 764     5355   5068   5538   -486     35    400       N  
ATOM   6259  CA  PHE A 764     -27.275 -29.567 -40.521  1.00 42.86           C  
ANISOU 6259  CA  PHE A 764     5437   5272   5577   -453     38    481       C  
ATOM   6260  C   PHE A 764     -28.287 -30.228 -39.597  1.00 43.84           C  
ANISOU 6260  C   PHE A 764     5506   5390   5763   -485     61    574       C  
ATOM   6261  O   PHE A 764     -28.254 -30.015 -38.388  1.00 43.21           O  
ANISOU 6261  O   PHE A 764     5410   5348   5660   -440     87    667       O  
ATOM   6262  CB  PHE A 764     -27.966 -28.458 -41.315  1.00 43.01           C  
ANISOU 6262  CB  PHE A 764     5447   5385   5511   -458      0    434       C  
ATOM   6263  CG  PHE A 764     -28.904 -27.609 -40.485  1.00 43.66           C  
ANISOU 6263  CG  PHE A 764     5489   5560   5541   -426     -3    502       C  
ATOM   6264  CD1 PHE A 764     -28.431 -26.490 -39.800  1.00 41.72           C  
ANISOU 6264  CD1 PHE A 764     5265   5369   5219   -350     -4    533       C  
ATOM   6265  CD2 PHE A 764     -30.260 -27.934 -40.387  1.00 40.83           C  
ANISOU 6265  CD2 PHE A 764     5065   5238   5210   -473     -6    527       C  
ATOM   6266  CE1 PHE A 764     -29.292 -25.703 -39.029  1.00 41.45           C  
ANISOU 6266  CE1 PHE A 764     5189   5422   5137   -310     -9    580       C  
ATOM   6267  CE2 PHE A 764     -31.125 -27.161 -39.623  1.00 40.85           C  
ANISOU 6267  CE2 PHE A 764     5021   5340   5159   -436     -8    581       C  
ATOM   6268  CZ  PHE A 764     -30.642 -26.038 -38.947  1.00 42.84           C  
ANISOU 6268  CZ  PHE A 764     5297   5644   5334   -349    -10    603       C  
ATOM   6269  N   LYS A 765     -29.184 -31.019 -40.183  1.00 45.61           N  
ANISOU 6269  N   LYS A 765     5694   5575   6060   -566     51    544       N  
ATOM   6270  CA  LYS A 765     -30.222 -31.722 -39.446  1.00 47.11           C  
ANISOU 6270  CA  LYS A 765     5823   5759   6318   -620     72    631       C  
ATOM   6271  C   LYS A 765     -29.615 -32.570 -38.323  1.00 48.30           C  
ANISOU 6271  C   LYS A 765     5983   5830   6538   -601    113    737       C  
ATOM   6272  O   LYS A 765     -30.147 -32.600 -37.207  1.00 47.61           O  
ANISOU 6272  O   LYS A 765     5851   5795   6443   -596    142    853       O  
ATOM   6273  CB  LYS A 765     -31.036 -32.601 -40.395  1.00 48.97           C  
ANISOU 6273  CB  LYS A 765     6026   5938   6642   -721     50    562       C  
ATOM   6274  CG  LYS A 765     -32.306 -33.205 -39.793  1.00 54.61           C  
ANISOU 6274  CG  LYS A 765     6664   6666   7422   -796     67    645       C  
ATOM   6275  CD  LYS A 765     -32.813 -34.395 -40.620  1.00 61.30           C  
ANISOU 6275  CD  LYS A 765     7488   7405   8397   -905     49    577       C  
ATOM   6276  CE  LYS A 765     -33.406 -33.962 -41.965  1.00 64.40           C  
ANISOU 6276  CE  LYS A 765     7861   7866   8742   -940      0    441       C  
ATOM   6277  NZ  LYS A 765     -33.222 -35.006 -43.023  1.00 67.64           N  
ANISOU 6277  NZ  LYS A 765     8285   8156   9257  -1010    -25    320       N  
ATOM   6278  N   GLU A 766     -28.497 -33.236 -38.617  1.00 46.90           N  
ANISOU 6278  N   GLU A 766     5860   5538   6421   -585    115    698       N  
ATOM   6279  CA  GLU A 766     -27.847 -34.091 -37.630  1.00 48.20           C  
ANISOU 6279  CA  GLU A 766     6039   5617   6658   -559    148    799       C  
ATOM   6280  C   GLU A 766     -27.186 -33.278 -36.523  1.00 47.33           C  
ANISOU 6280  C   GLU A 766     5936   5600   6446   -463    170    878       C  
ATOM   6281  O   GLU A 766     -27.331 -33.608 -35.352  1.00 46.63           O  
ANISOU 6281  O   GLU A 766     5820   5528   6369   -448    200   1006       O  
ATOM   6282  CB  GLU A 766     -26.841 -35.036 -38.285  1.00 49.31           C  
ANISOU 6282  CB  GLU A 766     6230   5609   6895   -557    139    724       C  
ATOM   6283  CG  GLU A 766     -26.622 -36.309 -37.489  1.00 50.30           C  
ANISOU 6283  CG  GLU A 766     6359   5603   7151   -566    163    829       C  
ATOM   6284  CD  GLU A 766     -27.905 -37.100 -37.294  1.00 53.56           C  
ANISOU 6284  CD  GLU A 766     6720   5967   7665   -670    169    898       C  
ATOM   6285  OE1 GLU A 766     -28.526 -37.500 -38.305  1.00 53.48           O  
ANISOU 6285  OE1 GLU A 766     6696   5903   7720   -751    142    797       O  
ATOM   6286  OE2 GLU A 766     -28.293 -37.323 -36.126  1.00 54.32           O  
ANISOU 6286  OE2 GLU A 766     6781   6087   7771   -675    201   1055       O  
ATOM   6287  N   PHE A 767     -26.490 -32.204 -36.897  1.00 46.12           N  
ANISOU 6287  N   PHE A 767     5817   5514   6192   -403    152    802       N  
ATOM   6288  CA  PHE A 767     -25.868 -31.310 -35.923  1.00 46.01           C  
ANISOU 6288  CA  PHE A 767     5808   5593   6079   -316    165    853       C  
ATOM   6289  C   PHE A 767     -26.885 -30.733 -34.940  1.00 47.32           C  
ANISOU 6289  C   PHE A 767     5916   5882   6183   -305    179    939       C  
ATOM   6290  O   PHE A 767     -26.668 -30.768 -33.733  1.00 46.98           O  
ANISOU 6290  O   PHE A 767     5851   5888   6110   -257    206   1036       O  
ATOM   6291  CB  PHE A 767     -25.069 -30.182 -36.601  1.00 45.78           C  
ANISOU 6291  CB  PHE A 767     5822   5612   5962   -272    139    752       C  
ATOM   6292  CG  PHE A 767     -24.266 -29.354 -35.632  1.00 44.40           C  
ANISOU 6292  CG  PHE A 767     5655   5514   5702   -187    149    788       C  
ATOM   6293  CD1 PHE A 767     -24.687 -28.083 -35.269  1.00 46.31           C  
ANISOU 6293  CD1 PHE A 767     5881   5867   5849   -153    135    785       C  
ATOM   6294  CD2 PHE A 767     -23.111 -29.868 -35.048  1.00 45.55           C  
ANISOU 6294  CD2 PHE A 767     5820   5621   5867   -137    168    821       C  
ATOM   6295  CE1 PHE A 767     -23.964 -27.321 -34.354  1.00 46.95           C  
ANISOU 6295  CE1 PHE A 767     5965   6018   5856    -77    140    804       C  
ATOM   6296  CE2 PHE A 767     -22.376 -29.117 -34.126  1.00 48.05           C  
ANISOU 6296  CE2 PHE A 767     6135   6020   6102    -61    173    847       C  
ATOM   6297  CZ  PHE A 767     -22.805 -27.839 -33.780  1.00 48.42           C  
ANISOU 6297  CZ  PHE A 767     6165   6176   6055    -34    159    834       C  
ATOM   6298  N   GLU A 768     -27.999 -30.231 -35.465  1.00 48.61           N  
ANISOU 6298  N   GLU A 768     6046   6102   6320   -347    159    901       N  
ATOM   6299  CA  GLU A 768     -29.079 -29.668 -34.655  1.00 48.80           C  
ANISOU 6299  CA  GLU A 768     6004   6254   6283   -336    169    965       C  
ATOM   6300  C   GLU A 768     -29.620 -30.661 -33.617  1.00 49.34           C  
ANISOU 6300  C   GLU A 768     6016   6326   6406   -369    211   1099       C  
ATOM   6301  O   GLU A 768     -29.940 -30.275 -32.489  1.00 50.31           O  
ANISOU 6301  O   GLU A 768     6091   6567   6460   -324    234   1179       O  
ATOM   6302  CB  GLU A 768     -30.202 -29.192 -35.573  1.00 50.28           C  
ANISOU 6302  CB  GLU A 768     6162   6486   6456   -383    137    896       C  
ATOM   6303  CG  GLU A 768     -31.281 -28.343 -34.919  1.00 52.96           C  
ANISOU 6303  CG  GLU A 768     6433   6973   6716   -353    136    929       C  
ATOM   6304  CD  GLU A 768     -32.298 -27.842 -35.932  1.00 54.87           C  
ANISOU 6304  CD  GLU A 768     6649   7256   6943   -388     97    854       C  
ATOM   6305  OE1 GLU A 768     -32.481 -26.611 -36.026  1.00 56.75           O  
ANISOU 6305  OE1 GLU A 768     6889   7575   7096   -325     67    809       O  
ATOM   6306  OE2 GLU A 768     -32.899 -28.676 -36.646  1.00 53.21           O  
ANISOU 6306  OE2 GLU A 768     6416   6995   6807   -477     91    836       O  
ATOM   6307  N   LYS A 769     -29.715 -31.932 -34.000  1.00 48.01           N  
ANISOU 6307  N   LYS A 769     5852   6029   6360   -448    219   1122       N  
ATOM   6308  CA  LYS A 769     -30.184 -32.982 -33.102  1.00 49.10           C  
ANISOU 6308  CA  LYS A 769     5944   6144   6570   -495    257   1263       C  
ATOM   6309  C   LYS A 769     -29.178 -33.314 -32.000  1.00 48.59           C  
ANISOU 6309  C   LYS A 769     5900   6068   6496   -425    287   1367       C  
ATOM   6310  O   LYS A 769     -29.564 -33.505 -30.847  1.00 48.96           O  
ANISOU 6310  O   LYS A 769     5892   6197   6514   -416    321   1501       O  
ATOM   6311  CB  LYS A 769     -30.498 -34.259 -33.884  1.00 51.28           C  
ANISOU 6311  CB  LYS A 769     6226   6258   7000   -601    250   1248       C  
ATOM   6312  CG  LYS A 769     -31.826 -34.252 -34.603  1.00 55.56           C  
ANISOU 6312  CG  LYS A 769     6712   6833   7565   -694    232   1197       C  
ATOM   6313  CD  LYS A 769     -32.158 -35.648 -35.121  1.00 62.35           C  
ANISOU 6313  CD  LYS A 769     7568   7529   8592   -807    229   1201       C  
ATOM   6314  CE  LYS A 769     -33.167 -35.592 -36.262  1.00 63.70           C  
ANISOU 6314  CE  LYS A 769     7703   7714   8787   -893    194   1087       C  
ATOM   6315  NZ  LYS A 769     -33.397 -36.935 -36.858  1.00 64.81           N  
ANISOU 6315  NZ  LYS A 769     7844   7683   9096  -1002    184   1061       N  
ATOM   6316  N   GLU A 770     -27.895 -33.381 -32.364  1.00 47.62           N  
ANISOU 6316  N   GLU A 770     5848   5857   6388   -373    272   1306       N  
ATOM   6317  CA  GLU A 770     -26.852 -33.919 -31.479  1.00 47.50           C  
ANISOU 6317  CA  GLU A 770     5856   5804   6387   -310    294   1398       C  
ATOM   6318  C   GLU A 770     -26.111 -32.836 -30.690  1.00 45.58           C  
ANISOU 6318  C   GLU A 770     5615   5700   6005   -201    297   1396       C  
ATOM   6319  O   GLU A 770     -25.396 -33.127 -29.734  1.00 44.33           O  
ANISOU 6319  O   GLU A 770     5455   5561   5827   -140    316   1487       O  
ATOM   6320  CB  GLU A 770     -25.851 -34.783 -32.268  1.00 48.13           C  
ANISOU 6320  CB  GLU A 770     6003   5705   6578   -313    278   1336       C  
ATOM   6321  CG  GLU A 770     -26.460 -35.791 -33.261  1.00 48.39           C  
ANISOU 6321  CG  GLU A 770     6042   5587   6756   -417    263   1290       C  
ATOM   6322  CD  GLU A 770     -27.367 -36.836 -32.624  1.00 53.45           C  
ANISOU 6322  CD  GLU A 770     6638   6173   7499   -496    288   1435       C  
ATOM   6323  OE1 GLU A 770     -28.278 -37.330 -33.326  1.00 56.02           O  
ANISOU 6323  OE1 GLU A 770     6941   6431   7912   -598    277   1396       O  
ATOM   6324  OE2 GLU A 770     -27.182 -37.169 -31.436  1.00 52.14           O  
ANISOU 6324  OE2 GLU A 770     6452   6034   7324   -461    319   1589       O  
ATOM   6325  N   PHE A 771     -26.326 -31.593 -31.093  1.00 44.37           N  
ANISOU 6325  N   PHE A 771     5460   5640   5757   -179    274   1294       N  
ATOM   6326  CA  PHE A 771     -25.655 -30.412 -30.555  1.00 45.84           C  
ANISOU 6326  CA  PHE A 771     5654   5943   5822    -85    265   1255       C  
ATOM   6327  C   PHE A 771     -25.609 -30.310 -29.018  1.00 45.93           C  
ANISOU 6327  C   PHE A 771     5613   6084   5754    -19    295   1371       C  
ATOM   6328  O   PHE A 771     -24.587 -29.930 -28.446  1.00 45.11           O  
ANISOU 6328  O   PHE A 771     5525   6026   5590     60    293   1365       O  
ATOM   6329  CB  PHE A 771     -26.301 -29.176 -31.201  1.00 45.41           C  
ANISOU 6329  CB  PHE A 771     5594   5959   5700    -90    234   1150       C  
ATOM   6330  CG  PHE A 771     -26.087 -27.902 -30.463  1.00 49.46           C  
ANISOU 6330  CG  PHE A 771     6093   6608   6094     -5    225   1123       C  
ATOM   6331  CD1 PHE A 771     -27.104 -27.371 -29.682  1.00 52.05           C  
ANISOU 6331  CD1 PHE A 771     6352   7073   6353     17    234   1161       C  
ATOM   6332  CD2 PHE A 771     -24.886 -27.202 -30.586  1.00 54.99           C  
ANISOU 6332  CD2 PHE A 771     6842   7301   6752     51    204   1049       C  
ATOM   6333  CE1 PHE A 771     -26.923 -26.181 -28.997  1.00 54.74           C  
ANISOU 6333  CE1 PHE A 771     6677   7534   6588    102    220   1119       C  
ATOM   6334  CE2 PHE A 771     -24.691 -25.998 -29.912  1.00 58.55           C  
ANISOU 6334  CE2 PHE A 771     7279   7865   7103    125    190   1012       C  
ATOM   6335  CZ  PHE A 771     -25.716 -25.486 -29.110  1.00 57.62           C  
ANISOU 6335  CZ  PHE A 771     7096   7876   6920    154    196   1042       C  
ATOM   6336  N   ARG A 772     -26.707 -30.665 -28.359  1.00 48.10           N  
ANISOU 6336  N   ARG A 772     5820   6431   6025    -54    322   1475       N  
ATOM   6337  CA  ARG A 772     -26.802 -30.581 -26.895  1.00 50.03           C  
ANISOU 6337  CA  ARG A 772     6001   6827   6179      5    354   1591       C  
ATOM   6338  C   ARG A 772     -25.863 -31.524 -26.135  1.00 47.47           C  
ANISOU 6338  C   ARG A 772     5690   6461   5885     40    376   1710       C  
ATOM   6339  O   ARG A 772     -25.745 -31.432 -24.920  1.00 50.29           O  
ANISOU 6339  O   ARG A 772     5999   6956   6154    101    400   1804       O  
ATOM   6340  CB  ARG A 772     -28.261 -30.744 -26.443  1.00 52.89           C  
ANISOU 6340  CB  ARG A 772     6277   7292   6526    -49    381   1677       C  
ATOM   6341  CG  ARG A 772     -29.074 -29.475 -26.654  1.00 56.92           C  
ANISOU 6341  CG  ARG A 772     6752   7926   6949    -27    359   1570       C  
ATOM   6342  CD  ARG A 772     -30.558 -29.735 -26.878  1.00 63.50           C  
ANISOU 6342  CD  ARG A 772     7517   8801   7811   -110    372   1604       C  
ATOM   6343  NE  ARG A 772     -31.128 -28.738 -27.791  1.00 68.31           N  
ANISOU 6343  NE  ARG A 772     8133   9426   8397   -110    332   1464       N  
ATOM   6344  CZ  ARG A 772     -31.607 -27.547 -27.425  1.00 70.75           C  
ANISOU 6344  CZ  ARG A 772     8399   9886   8598    -39    317   1401       C  
ATOM   6345  NH1 ARG A 772     -31.607 -27.179 -26.144  1.00 70.68           N  
ANISOU 6345  NH1 ARG A 772     8330  10040   8484     38    341   1453       N  
ATOM   6346  NH2 ARG A 772     -32.094 -26.718 -28.348  1.00 67.31           N  
ANISOU 6346  NH2 ARG A 772     7978   9440   8158    -39    275   1283       N  
ATOM   6347  N   GLN A 773     -25.185 -32.409 -26.858  1.00 44.47           N  
ANISOU 6347  N   GLN A 773     5373   5899   5624      9    367   1700       N  
ATOM   6348  CA  GLN A 773     -24.232 -33.347 -26.271  1.00 45.17           C  
ANISOU 6348  CA  GLN A 773     5481   5922   5758     50    380   1805       C  
ATOM   6349  C   GLN A 773     -22.810 -32.795 -26.228  1.00 42.20           C  
ANISOU 6349  C   GLN A 773     5146   5564   5323    146    359   1721       C  
ATOM   6350  O   GLN A 773     -21.922 -33.394 -25.617  1.00 40.85           O  
ANISOU 6350  O   GLN A 773     4984   5375   5162    204    366   1801       O  
ATOM   6351  CB  GLN A 773     -24.219 -34.655 -27.063  1.00 45.67           C  
ANISOU 6351  CB  GLN A 773     5588   5769   5996    -25    377   1830       C  
ATOM   6352  CG  GLN A 773     -25.506 -35.440 -27.015  1.00 51.08           C  
ANISOU 6352  CG  GLN A 773     6230   6414   6765   -130    400   1935       C  
ATOM   6353  CD  GLN A 773     -25.672 -36.370 -28.211  1.00 54.20           C  
ANISOU 6353  CD  GLN A 773     6671   6593   7330   -221    380   1876       C  
ATOM   6354  OE1 GLN A 773     -26.688 -36.317 -28.908  1.00 52.72           O  
ANISOU 6354  OE1 GLN A 773     6463   6388   7179   -310    374   1821       O  
ATOM   6355  NE2 GLN A 773     -24.666 -37.214 -28.463  1.00 51.43           N  
ANISOU 6355  NE2 GLN A 773     6378   6083   7080   -192    368   1876       N  
ATOM   6356  N   LEU A 774     -22.587 -31.666 -26.891  1.00 40.69           N  
ANISOU 6356  N   LEU A 774     4980   5408   5074    161    330   1565       N  
ATOM   6357  CA  LEU A 774     -21.243 -31.098 -26.972  1.00 41.74           C  
ANISOU 6357  CA  LEU A 774     5149   5553   5158    235    308   1475       C  
ATOM   6358  C   LEU A 774     -20.747 -30.616 -25.608  1.00 42.75           C  
ANISOU 6358  C   LEU A 774     5232   5848   5164    328    317   1532       C  
ATOM   6359  O   LEU A 774     -21.509 -30.030 -24.832  1.00 40.71           O  
ANISOU 6359  O   LEU A 774     4917   5735   4815    344    328   1565       O  
ATOM   6360  CB  LEU A 774     -21.174 -29.986 -28.023  1.00 39.41           C  
ANISOU 6360  CB  LEU A 774     4889   5252   4835    216    276   1309       C  
ATOM   6361  CG  LEU A 774     -21.421 -30.434 -29.474  1.00 40.97           C  
ANISOU 6361  CG  LEU A 774     5132   5297   5137    134    262   1234       C  
ATOM   6362  CD1 LEU A 774     -21.583 -29.249 -30.401  1.00 36.52           C  
ANISOU 6362  CD1 LEU A 774     4591   4758   4527    113    231   1099       C  
ATOM   6363  CD2 LEU A 774     -20.336 -31.384 -29.989  1.00 40.55           C  
ANISOU 6363  CD2 LEU A 774     5124   5112   5173    143    259   1217       C  
ATOM   6364  N   ASN A 775     -19.476 -30.905 -25.325  1.00 43.17           N  
ANISOU 6364  N   ASN A 775     5304   5887   5214    394    311   1538       N  
ATOM   6365  CA  ASN A 775     -18.805 -30.461 -24.106  1.00 43.63           C  
ANISOU 6365  CA  ASN A 775     5319   6105   5153    489    313   1574       C  
ATOM   6366  C   ASN A 775     -18.835 -28.937 -24.029  1.00 40.84           C  
ANISOU 6366  C   ASN A 775     4951   5878   4689    514    289   1442       C  
ATOM   6367  O   ASN A 775     -18.654 -28.255 -25.043  1.00 40.84           O  
ANISOU 6367  O   ASN A 775     4994   5811   4711    480    264   1309       O  
ATOM   6368  CB  ASN A 775     -17.358 -30.970 -24.083  1.00 44.60           C  
ANISOU 6368  CB  ASN A 775     5469   6177   5302    550    301   1571       C  
ATOM   6369  CG  ASN A 775     -16.571 -30.451 -22.888  1.00 46.83           C  
ANISOU 6369  CG  ASN A 775     5703   6635   5454    650    296   1588       C  
ATOM   6370  OD1 ASN A 775     -15.805 -29.494 -23.006  1.00 45.75           O  
ANISOU 6370  OD1 ASN A 775     5570   6558   5254    683    270   1461       O  
ATOM   6371  ND2 ASN A 775     -16.769 -31.071 -21.729  1.00 45.07           N  
ANISOU 6371  ND2 ASN A 775     5431   6503   5190    694    319   1748       N  
ATOM   6372  N   TYR A 776     -19.054 -28.409 -22.832  1.00 37.40           N  
ANISOU 6372  N   TYR A 776     4452   5623   4135    574    297   1479       N  
ATOM   6373  CA  TYR A 776     -19.289 -26.973 -22.672  1.00 39.35           C  
ANISOU 6373  CA  TYR A 776     4679   5986   4287    599    272   1354       C  
ATOM   6374  C   TYR A 776     -18.154 -26.065 -23.168  1.00 36.44           C  
ANISOU 6374  C   TYR A 776     4351   5593   3904    622    234   1204       C  
ATOM   6375  O   TYR A 776     -18.410 -24.957 -23.622  1.00 37.78           O  
ANISOU 6375  O   TYR A 776     4536   5766   4054    606    206   1086       O  
ATOM   6376  CB  TYR A 776     -19.652 -26.644 -21.223  1.00 40.03           C  
ANISOU 6376  CB  TYR A 776     4681   6285   4243    671    286   1413       C  
ATOM   6377  CG  TYR A 776     -18.499 -26.709 -20.253  1.00 39.77           C  
ANISOU 6377  CG  TYR A 776     4619   6361   4130    759    282   1438       C  
ATOM   6378  CD1 TYR A 776     -17.938 -25.536 -19.742  1.00 38.14           C  
ANISOU 6378  CD1 TYR A 776     4388   6283   3822    824    250   1312       C  
ATOM   6379  CD2 TYR A 776     -17.977 -27.942 -19.829  1.00 41.89           C  
ANISOU 6379  CD2 TYR A 776     4883   6605   4429    781    304   1586       C  
ATOM   6380  CE1 TYR A 776     -16.882 -25.579 -18.839  1.00 40.95           C  
ANISOU 6380  CE1 TYR A 776     4707   6756   4097    905    242   1326       C  
ATOM   6381  CE2 TYR A 776     -16.917 -27.999 -18.921  1.00 43.29           C  
ANISOU 6381  CE2 TYR A 776     5027   6898   4525    870    296   1612       C  
ATOM   6382  CZ  TYR A 776     -16.378 -26.809 -18.434  1.00 43.10           C  
ANISOU 6382  CZ  TYR A 776     4971   7016   4389    931    265   1478       C  
ATOM   6383  OH  TYR A 776     -15.340 -26.839 -17.545  1.00 45.36           O  
ANISOU 6383  OH  TYR A 776     5217   7429   4589   1018    254   1493       O  
ATOM   6384  N   ILE A 777     -16.917 -26.538 -23.068  1.00 38.01           N  
ANISOU 6384  N   ILE A 777     4562   5766   4112    658    230   1215       N  
ATOM   6385  CA  ILE A 777     -15.742 -25.805 -23.549  1.00 38.46           C  
ANISOU 6385  CA  ILE A 777     4650   5803   4161    670    198   1084       C  
ATOM   6386  C   ILE A 777     -15.801 -25.697 -25.075  1.00 38.86           C  
ANISOU 6386  C   ILE A 777     4767   5692   4304    587    186   1003       C  
ATOM   6387  O   ILE A 777     -15.618 -24.613 -25.645  1.00 35.85           O  
ANISOU 6387  O   ILE A 777     4410   5303   3908    563    158    884       O  
ATOM   6388  CB  ILE A 777     -14.424 -26.473 -23.041  1.00 41.36           C  
ANISOU 6388  CB  ILE A 777     5002   6197   4515    735    200   1126       C  
ATOM   6389  CG1 ILE A 777     -14.253 -26.201 -21.544  1.00 43.44           C  
ANISOU 6389  CG1 ILE A 777     5194   6658   4655    823    200   1171       C  
ATOM   6390  CG2 ILE A 777     -13.190 -25.976 -23.813  1.00 40.08           C  
ANISOU 6390  CG2 ILE A 777     4873   5984   4371    726    173    999       C  
ATOM   6391  CD1 ILE A 777     -13.634 -27.351 -20.765  1.00 51.38           C  
ANISOU 6391  CD1 ILE A 777     6168   7700   5652    888    218   1309       C  
ATOM   6392  N   SER A 778     -16.122 -26.817 -25.721  1.00 40.31           N  
ANISOU 6392  N   SER A 778     4979   5751   4585    542    207   1070       N  
ATOM   6393  CA  SER A 778     -16.230 -26.866 -27.178  1.00 39.54           C  
ANISOU 6393  CA  SER A 778     4939   5514   4572    465    198    997       C  
ATOM   6394  C   SER A 778     -17.330 -25.948 -27.731  1.00 39.18           C  
ANISOU 6394  C   SER A 778     4904   5469   4515    411    183    938       C  
ATOM   6395  O   SER A 778     -17.346 -25.665 -28.921  1.00 40.74           O  
ANISOU 6395  O   SER A 778     5144   5581   4753    354    167    861       O  
ATOM   6396  CB  SER A 778     -16.431 -28.308 -27.661  1.00 39.04           C  
ANISOU 6396  CB  SER A 778     4896   5320   4618    431    219   1074       C  
ATOM   6397  OG  SER A 778     -17.785 -28.700 -27.540  1.00 37.56           O  
ANISOU 6397  OG  SER A 778     4693   5118   4462    387    237   1152       O  
ATOM   6398  N   ILE A 779     -18.241 -25.478 -26.877  1.00 39.31           N  
ANISOU 6398  N   ILE A 779     4876   5590   4470    435    187    973       N  
ATOM   6399  CA  ILE A 779     -19.326 -24.602 -27.353  1.00 39.25           C  
ANISOU 6399  CA  ILE A 779     4873   5589   4453    398    169    917       C  
ATOM   6400  C   ILE A 779     -19.354 -23.195 -26.724  1.00 37.66           C  
ANISOU 6400  C   ILE A 779     4648   5500   4160    449    140    838       C  
ATOM   6401  O   ILE A 779     -20.265 -22.406 -26.990  1.00 36.70           O  
ANISOU 6401  O   ILE A 779     4525   5391   4028    436    121    792       O  
ATOM   6402  CB  ILE A 779     -20.724 -25.290 -27.290  1.00 40.68           C  
ANISOU 6402  CB  ILE A 779     5024   5765   4668    359    194   1006       C  
ATOM   6403  CG1 ILE A 779     -20.978 -25.914 -25.917  1.00 45.46           C  
ANISOU 6403  CG1 ILE A 779     5566   6481   5228    407    227   1130       C  
ATOM   6404  CG2 ILE A 779     -20.839 -26.341 -28.375  1.00 41.79           C  
ANISOU 6404  CG2 ILE A 779     5204   5756   4917    284    204   1027       C  
ATOM   6405  CD1 ILE A 779     -22.331 -26.602 -25.783  1.00 49.33           C  
ANISOU 6405  CD1 ILE A 779     6015   6978   5749    359    256   1229       C  
ATOM   6406  N   ALA A 780     -18.349 -22.885 -25.908  1.00 36.51           N  
ANISOU 6406  N   ALA A 780     4483   5434   3956    511    133    816       N  
ATOM   6407  CA  ALA A 780     -18.173 -21.531 -25.385  1.00 36.81           C  
ANISOU 6407  CA  ALA A 780     4504   5562   3921    557     98    717       C  
ATOM   6408  C   ALA A 780     -17.504 -20.611 -26.407  1.00 34.26           C  
ANISOU 6408  C   ALA A 780     4238   5146   3631    515     61    604       C  
ATOM   6409  O   ALA A 780     -16.551 -21.003 -27.080  1.00 35.12           O  
ANISOU 6409  O   ALA A 780     4381   5181   3780    481     64    595       O  
ATOM   6410  CB  ALA A 780     -17.376 -21.555 -24.090  1.00 35.90           C  
ANISOU 6410  CB  ALA A 780     4336   5581   3724    637    102    730       C  
ATOM   6411  N   SER A 781     -18.013 -19.391 -26.512  1.00 31.85           N  
ANISOU 6411  N   SER A 781     3942   4851   3310    518     25    522       N  
ATOM   6412  CA  SER A 781     -17.384 -18.353 -27.323  1.00 31.58           C  
ANISOU 6412  CA  SER A 781     3958   4740   3302    480    -16    424       C  
ATOM   6413  C   SER A 781     -16.114 -17.891 -26.629  1.00 31.34           C  
ANISOU 6413  C   SER A 781     3908   4770   3229    516    -32    364       C  
ATOM   6414  O   SER A 781     -15.871 -18.236 -25.473  1.00 28.24           O  
ANISOU 6414  O   SER A 781     3460   4493   2777    581    -18    389       O  
ATOM   6415  CB  SER A 781     -18.325 -17.157 -27.486  1.00 29.67           C  
ANISOU 6415  CB  SER A 781     3727   4487   3059    487    -56    360       C  
ATOM   6416  OG  SER A 781     -19.483 -17.531 -28.198  1.00 38.17           O  
ANISOU 6416  OG  SER A 781     4817   5515   4173    452    -46    409       O  
ATOM   6417  N   VAL A 782     -15.299 -17.107 -27.322  1.00 32.75           N  
ANISOU 6417  N   VAL A 782     4126   4881   3435    470    -63    288       N  
ATOM   6418  CA  VAL A 782     -14.090 -16.582 -26.701  1.00 33.79           C  
ANISOU 6418  CA  VAL A 782     4233   5072   3532    493    -83    219       C  
ATOM   6419  C   VAL A 782     -13.991 -15.097 -26.971  1.00 35.98           C  
ANISOU 6419  C   VAL A 782     4540   5302   3830    466   -136    115       C  
ATOM   6420  O   VAL A 782     -14.319 -14.645 -28.057  1.00 36.42           O  
ANISOU 6420  O   VAL A 782     4650   5248   3939    404   -152    110       O  
ATOM   6421  CB  VAL A 782     -12.829 -17.298 -27.208  1.00 34.73           C  
ANISOU 6421  CB  VAL A 782     4361   5166   3670    457    -61    238       C  
ATOM   6422  CG1 VAL A 782     -11.562 -16.712 -26.551  1.00 35.51           C  
ANISOU 6422  CG1 VAL A 782     4424   5339   3730    478    -85    161       C  
ATOM   6423  CG2 VAL A 782     -12.922 -18.795 -26.945  1.00 32.05           C  
ANISOU 6423  CG2 VAL A 782     3999   4851   3328    489    -14    343       C  
ATOM   6424  N   SER A 783     -13.578 -14.338 -25.965  1.00 39.29           N  
ANISOU 6424  N   SER A 783     4920   5803   4206    516   -167     33       N  
ATOM   6425  CA  SER A 783     -13.237 -12.940 -26.168  1.00 41.04           C  
ANISOU 6425  CA  SER A 783     5167   5966   4461    485   -223    -74       C  
ATOM   6426  C   SER A 783     -12.060 -12.507 -25.291  1.00 42.67           C  
ANISOU 6426  C   SER A 783     5326   6258   4629    508   -245   -161       C  
ATOM   6427  O   SER A 783     -11.660 -13.228 -24.374  1.00 42.81           O  
ANISOU 6427  O   SER A 783     5285   6404   4579    568   -221   -139       O  
ATOM   6428  CB  SER A 783     -14.445 -12.040 -25.920  1.00 40.33           C  
ANISOU 6428  CB  SER A 783     5086   5859   4381    527   -260   -122       C  
ATOM   6429  OG  SER A 783     -14.098 -10.694 -26.200  1.00 41.08           O  
ANISOU 6429  OG  SER A 783     5215   5867   4527    492   -319   -221       O  
ATOM   6430  N   SER A 784     -11.513 -11.329 -25.595  1.00 43.73           N  
ANISOU 6430  N   SER A 784     5486   6321   4810    456   -294   -254       N  
ATOM   6431  CA  SER A 784     -10.464 -10.706 -24.791  1.00 43.64           C  
ANISOU 6431  CA  SER A 784     5427   6380   4772    467   -328   -360       C  
ATOM   6432  C   SER A 784     -11.068  -9.819 -23.712  1.00 44.40           C  
ANISOU 6432  C   SER A 784     5491   6537   4842    548   -374   -466       C  
ATOM   6433  O   SER A 784     -12.005  -9.060 -23.971  1.00 45.83           O  
ANISOU 6433  O   SER A 784     5711   6633   5069    555   -406   -497       O  
ATOM   6434  CB  SER A 784      -9.527  -9.889 -25.677  1.00 42.67           C  
ANISOU 6434  CB  SER A 784     5344   6145   4722    358   -358   -406       C  
ATOM   6435  OG  SER A 784      -8.701 -10.738 -26.446  1.00 42.99           O  
ANISOU 6435  OG  SER A 784     5389   6181   4764    297   -314   -332       O  
ATOM   6436  N   ALA A 785     -10.508  -9.905 -22.510  1.00 43.93           N  
ANISOU 6436  N   ALA A 785     5354   6632   4704    615   -380   -529       N  
ATOM   6437  CA  ALA A 785     -11.024  -9.195 -21.342  1.00 45.43           C  
ANISOU 6437  CA  ALA A 785     5495   6922   4845    708   -420   -641       C  
ATOM   6438  C   ALA A 785     -10.461  -7.778 -21.205  1.00 46.95           C  
ANISOU 6438  C   ALA A 785     5694   7051   5095    675   -494   -804       C  
ATOM   6439  O   ALA A 785      -9.662  -7.509 -20.306  1.00 48.10           O  
ANISOU 6439  O   ALA A 785     5774   7310   5190    705   -520   -905       O  
ATOM   6440  CB  ALA A 785     -10.732 -10.001 -20.082  1.00 44.85           C  
ANISOU 6440  CB  ALA A 785     5329   7065   4646    800   -392   -626       C  
ATOM   6441  N   ASN A 786     -10.887  -6.869 -22.078  1.00 47.68           N  
ANISOU 6441  N   ASN A 786     5862   6961   5294    616   -532   -830       N  
ATOM   6442  CA  ASN A 786     -10.366  -5.502 -22.048  1.00 50.89           C  
ANISOU 6442  CA  ASN A 786     6284   7272   5779    572   -606   -974       C  
ATOM   6443  C   ASN A 786     -11.239  -4.514 -21.280  1.00 53.81           C  
ANISOU 6443  C   ASN A 786     6641   7646   6160    663   -666  -1110       C  
ATOM   6444  O   ASN A 786     -12.469  -4.578 -21.342  1.00 54.97           O  
ANISOU 6444  O   ASN A 786     6804   7780   6301    726   -659  -1074       O  
ATOM   6445  CB  ASN A 786     -10.112  -4.988 -23.464  1.00 49.37           C  
ANISOU 6445  CB  ASN A 786     6181   6869   5707    443   -620   -921       C  
ATOM   6446  CG  ASN A 786      -9.033  -5.768 -24.183  1.00 47.45           C  
ANISOU 6446  CG  ASN A 786     5939   6634   5456    348   -571   -826       C  
ATOM   6447  OD1 ASN A 786      -7.997  -6.093 -23.603  1.00 49.92           O  
ANISOU 6447  OD1 ASN A 786     6188   7063   5715    347   -562   -864       O  
ATOM   6448  ND2 ASN A 786      -9.267  -6.068 -25.457  1.00 42.23           N  
ANISOU 6448  ND2 ASN A 786     5345   5858   4842    274   -542   -707       N  
ATOM   6449  N   ASN A 787     -10.586  -3.600 -20.562  1.00 56.38           N  
ANISOU 6449  N   ASN A 787     6929   7991   6501    670   -727  -1275       N  
ATOM   6450  CA  ASN A 787     -11.256  -2.509 -19.837  1.00 58.28           C  
ANISOU 6450  CA  ASN A 787     7156   8220   6768    754   -797  -1440       C  
ATOM   6451  C   ASN A 787     -12.395  -2.941 -18.911  1.00 57.41           C  
ANISOU 6451  C   ASN A 787     6985   8284   6545    901   -775  -1452       C  
ATOM   6452  O   ASN A 787     -13.455  -2.309 -18.873  1.00 56.98           O  
ANISOU 6452  O   ASN A 787     6950   8172   6527    966   -810  -1509       O  
ATOM   6453  CB  ASN A 787     -11.739  -1.429 -20.815  1.00 60.16           C  
ANISOU 6453  CB  ASN A 787     7493   8205   7161    696   -853  -1456       C  
ATOM   6454  CG  ASN A 787     -10.616  -0.536 -21.294  1.00 65.12           C  
ANISOU 6454  CG  ASN A 787     8159   8679   7906    569   -905  -1519       C  
ATOM   6455  OD1 ASN A 787      -9.857   0.013 -20.490  1.00 68.30           O  
ANISOU 6455  OD1 ASN A 787     8508   9137   8307    572   -951  -1672       O  
ATOM   6456  ND2 ASN A 787     -10.509  -0.373 -22.610  1.00 64.07           N  
ANISOU 6456  ND2 ASN A 787     8113   8360   7872    454   -900  -1403       N  
ATOM   6457  N   ILE A 788     -12.171  -4.017 -18.164  1.00 56.99           N  
ANISOU 6457  N   ILE A 788     6854   8446   6354    954   -718  -1392       N  
ATOM   6458  CA  ILE A 788     -13.162  -4.495 -17.202  1.00 58.19           C  
ANISOU 6458  CA  ILE A 788     6934   8794   6382   1086   -689  -1389       C  
ATOM   6459  C   ILE A 788     -13.583  -3.374 -16.241  1.00 59.29           C  
ANISOU 6459  C   ILE A 788     7025   8995   6509   1187   -761  -1602       C  
ATOM   6460  O   ILE A 788     -14.771  -3.109 -16.078  1.00 59.18           O  
ANISOU 6460  O   ILE A 788     7005   8994   6486   1269   -769  -1629       O  
ATOM   6461  CB  ILE A 788     -12.649  -5.717 -16.405  1.00 58.37           C  
ANISOU 6461  CB  ILE A 788     6872   9048   6257   1126   -627  -1302       C  
ATOM   6462  CG1 ILE A 788     -12.166  -6.817 -17.358  1.00 56.71           C  
ANISOU 6462  CG1 ILE A 788     6710   8765   6072   1033   -563  -1109       C  
ATOM   6463  CG2 ILE A 788     -13.734  -6.235 -15.456  1.00 59.84           C  
ANISOU 6463  CG2 ILE A 788     6982   9441   6313   1252   -593  -1274       C  
ATOM   6464  CD1 ILE A 788     -11.590  -8.042 -16.656  1.00 58.87           C  
ANISOU 6464  CD1 ILE A 788     6911   9237   6220   1072   -507  -1011       C  
ATOM   6465  N   ALA A 789     -12.600  -2.707 -15.638  1.00 61.87           N  
ANISOU 6465  N   ALA A 789     7312   9357   6838   1179   -815  -1762       N  
ATOM   6466  CA  ALA A 789     -12.846  -1.660 -14.636  1.00 63.95           C  
ANISOU 6466  CA  ALA A 789     7519   9694   7087   1277   -889  -1993       C  
ATOM   6467  C   ALA A 789     -13.665  -0.482 -15.169  1.00 64.27           C  
ANISOU 6467  C   ALA A 789     7633   9517   7271   1287   -956  -2090       C  
ATOM   6468  O   ALA A 789     -14.365   0.178 -14.406  1.00 65.41           O  
ANISOU 6468  O   ALA A 789     7731   9733   7390   1403  -1002  -2250       O  
ATOM   6469  CB  ALA A 789     -11.525  -1.172 -14.036  1.00 64.61           C  
ANISOU 6469  CB  ALA A 789     7553   9832   7165   1244   -939  -2146       C  
ATOM   6470  N   LYS A 790     -13.572  -0.229 -16.473  1.00 63.73           N  
ANISOU 6470  N   LYS A 790     7674   9191   7349   1170   -963  -1994       N  
ATOM   6471  CA  LYS A 790     -14.326   0.845 -17.121  1.00 64.19           C  
ANISOU 6471  CA  LYS A 790     7814   9021   7556   1172  -1027  -2053       C  
ATOM   6472  C   LYS A 790     -15.838   0.624 -17.005  1.00 63.51           C  
ANISOU 6472  C   LYS A 790     7713   9000   7418   1291  -1005  -2016       C  
ATOM   6473  O   LYS A 790     -16.599   1.577 -16.832  1.00 63.49           O  
ANISOU 6473  O   LYS A 790     7720   8925   7479   1373  -1070  -2150       O  
ATOM   6474  CB  LYS A 790     -13.922   0.967 -18.598  1.00 64.21           C  
ANISOU 6474  CB  LYS A 790     7931   8766   7699   1019  -1025  -1914       C  
ATOM   6475  CG  LYS A 790     -14.581   2.124 -19.350  1.00 65.57           C  
ANISOU 6475  CG  LYS A 790     8196   8682   8037   1010  -1098  -1957       C  
ATOM   6476  CD  LYS A 790     -14.145   2.181 -20.802  1.00 65.60           C  
ANISOU 6476  CD  LYS A 790     8305   8462   8159    855  -1090  -1800       C  
ATOM   6477  CE  LYS A 790     -14.744   3.390 -21.509  1.00 68.00           C  
ANISOU 6477  CE  LYS A 790     8700   8508   8629    848  -1171  -1836       C  
ATOM   6478  NZ  LYS A 790     -14.305   3.469 -22.932  1.00 69.15           N  
ANISOU 6478  NZ  LYS A 790     8944   8453   8879    695  -1163  -1673       N  
ATOM   6479  N   TYR A 791     -16.252  -0.639 -17.094  1.00 62.30           N  
ANISOU 6479  N   TYR A 791     7534   8984   7155   1300   -916  -1838       N  
ATOM   6480  CA  TYR A 791     -17.663  -1.011 -17.113  1.00 61.51           C  
ANISOU 6480  CA  TYR A 791     7416   8951   7005   1388   -882  -1769       C  
ATOM   6481  C   TYR A 791     -18.117  -1.676 -15.814  1.00 63.01           C  
ANISOU 6481  C   TYR A 791     7481   9449   7012   1511   -837  -1795       C  
ATOM   6482  O   TYR A 791     -19.207  -2.251 -15.748  1.00 61.78           O  
ANISOU 6482  O   TYR A 791     7291   9396   6787   1571   -790  -1707       O  
ATOM   6483  CB  TYR A 791     -17.952  -1.927 -18.309  1.00 60.02           C  
ANISOU 6483  CB  TYR A 791     7295   8667   6844   1297   -816  -1539       C  
ATOM   6484  CG  TYR A 791     -17.724  -1.278 -19.654  1.00 59.06           C  
ANISOU 6484  CG  TYR A 791     7291   8260   6887   1187   -857  -1496       C  
ATOM   6485  CD1 TYR A 791     -16.628  -1.627 -20.438  1.00 57.99           C  
ANISOU 6485  CD1 TYR A 791     7210   8025   6798   1049   -834  -1397       C  
ATOM   6486  CD2 TYR A 791     -18.603  -0.309 -20.141  1.00 60.25           C  
ANISOU 6486  CD2 TYR A 791     7497   8252   7144   1225   -918  -1550       C  
ATOM   6487  CE1 TYR A 791     -16.413  -1.029 -21.686  1.00 57.65           C  
ANISOU 6487  CE1 TYR A 791     7270   7740   6896    943   -868  -1346       C  
ATOM   6488  CE2 TYR A 791     -18.399   0.297 -21.382  1.00 59.78           C  
ANISOU 6488  CE2 TYR A 791     7547   7937   7232   1124   -957  -1494       C  
ATOM   6489  CZ  TYR A 791     -17.305  -0.069 -22.147  1.00 59.38           C  
ANISOU 6489  CZ  TYR A 791     7545   7802   7216    980   -929  -1388       C  
ATOM   6490  OH  TYR A 791     -17.101   0.528 -23.371  1.00 60.04           O  
ANISOU 6490  OH  TYR A 791     7729   7651   7432    877   -964  -1322       O  
ATOM   6491  N   ASP A 792     -17.281  -1.599 -14.783  1.00 66.13           N  
ANISOU 6491  N   ASP A 792     7800  10003   7323   1544   -852  -1912       N  
ATOM   6492  CA  ASP A 792     -17.650  -2.117 -13.471  1.00 68.46           C  
ANISOU 6492  CA  ASP A 792     7969  10610   7433   1666   -817  -1949       C  
ATOM   6493  C   ASP A 792     -18.281  -1.013 -12.622  1.00 71.44           C  
ANISOU 6493  C   ASP A 792     8287  11061   7795   1799   -888  -2188       C  
ATOM   6494  O   ASP A 792     -17.628  -0.020 -12.279  1.00 73.11           O  
ANISOU 6494  O   ASP A 792     8498  11214   8066   1807   -967  -2388       O  
ATOM   6495  CB  ASP A 792     -16.440  -2.736 -12.757  1.00 69.14           C  
ANISOU 6495  CB  ASP A 792     7992  10867   7412   1643   -791  -1936       C  
ATOM   6496  CG  ASP A 792     -16.831  -3.544 -11.515  1.00 70.48           C  
ANISOU 6496  CG  ASP A 792     8033  11373   7374   1756   -737  -1904       C  
ATOM   6497  OD1 ASP A 792     -17.604  -3.040 -10.668  1.00 70.40           O  
ANISOU 6497  OD1 ASP A 792     7946  11517   7287   1880   -762  -2044       O  
ATOM   6498  OD2 ASP A 792     -16.352  -4.689 -11.382  1.00 68.85           O  
ANISOU 6498  OD2 ASP A 792     7800  11280   7080   1723   -670  -1738       O  
ATOM   6499  N   VAL A 793     -19.561  -1.194 -12.306  1.00 72.05           N  
ANISOU 6499  N   VAL A 793     8311  11267   7798   1903   -861  -2172       N  
ATOM   6500  CA  VAL A 793     -20.278  -0.331 -11.370  1.00 73.72           C  
ANISOU 6500  CA  VAL A 793     8441  11610   7958   2054   -915  -2393       C  
ATOM   6501  C   VAL A 793     -20.818  -1.213 -10.238  1.00 73.87           C  
ANISOU 6501  C   VAL A 793     8321  11994   7753   2156   -843  -2344       C  
ATOM   6502  O   VAL A 793     -21.829  -1.904 -10.403  1.00 73.23           O  
ANISOU 6502  O   VAL A 793     8216  11994   7615   2179   -779  -2197       O  
ATOM   6503  CB  VAL A 793     -21.427   0.460 -12.071  1.00 74.42           C  
ANISOU 6503  CB  VAL A 793     8588  11513   8174   2099   -961  -2441       C  
ATOM   6504  CG1 VAL A 793     -22.186   1.336 -11.075  1.00 77.82           C  
ANISOU 6504  CG1 VAL A 793     8927  12093   8550   2271  -1017  -2683       C  
ATOM   6505  CG2 VAL A 793     -20.883   1.318 -13.210  1.00 74.32           C  
ANISOU 6505  CG2 VAL A 793     8716  11141   8381   1993  -1031  -2463       C  
ATOM   6506  N   GLY A 794     -20.114  -1.211  -9.106  1.00 74.39           N  
ANISOU 6506  N   GLY A 794     8291  12282   7690   2210   -853  -2459       N  
ATOM   6507  CA  GLY A 794     -20.505  -1.990  -7.922  1.00 75.67           C  
ANISOU 6507  CA  GLY A 794     8312  12817   7624   2310   -790  -2418       C  
ATOM   6508  C   GLY A 794     -20.606  -3.500  -8.102  1.00 74.22           C  
ANISOU 6508  C   GLY A 794     8117  12734   7348   2246   -682  -2121       C  
ATOM   6509  O   GLY A 794     -21.189  -4.193  -7.266  1.00 75.12           O  
ANISOU 6509  O   GLY A 794     8121  13135   7287   2321   -621  -2045       O  
ATOM   6510  N   GLY A 795     -20.028  -4.011  -9.186  1.00 72.10           N  
ANISOU 6510  N   GLY A 795     7961  12234   7201   2107   -658  -1952       N  
ATOM   6511  CA  GLY A 795     -20.098  -5.436  -9.510  1.00 69.66           C  
ANISOU 6511  CA  GLY A 795     7659  11969   6840   2037   -563  -1674       C  
ATOM   6512  C   GLY A 795     -21.184  -5.765 -10.520  1.00 67.04           C  
ANISOU 6512  C   GLY A 795     7390  11485   6597   1992   -526  -1531       C  
ATOM   6513  O   GLY A 795     -21.441  -6.937 -10.813  1.00 64.91           O  
ANISOU 6513  O   GLY A 795     7123  11245   6294   1937   -448  -1307       O  
ATOM   6514  N   PHE A 796     -21.819  -4.720 -11.047  1.00 66.03           N  
ANISOU 6514  N   PHE A 796     7312  11192   6585   2017   -587  -1663       N  
ATOM   6515  CA  PHE A 796     -22.904  -4.855 -12.008  1.00 63.69           C  
ANISOU 6515  CA  PHE A 796     7069  10756   6374   1988   -566  -1557       C  
ATOM   6516  C   PHE A 796     -22.624  -4.029 -13.267  1.00 60.76           C  
ANISOU 6516  C   PHE A 796     6836  10043   6207   1907   -631  -1602       C  
ATOM   6517  O   PHE A 796     -21.997  -2.971 -13.184  1.00 61.54           O  
ANISOU 6517  O   PHE A 796     6966  10034   6381   1919   -710  -1783       O  
ATOM   6518  CB  PHE A 796     -24.227  -4.430 -11.371  1.00 66.42           C  
ANISOU 6518  CB  PHE A 796     7319  11275   6640   2123   -572  -1658       C  
ATOM   6519  CG  PHE A 796     -24.743  -5.397 -10.337  1.00 68.42           C  
ANISOU 6519  CG  PHE A 796     7438  11863   6694   2183   -492  -1556       C  
ATOM   6520  CD1 PHE A 796     -25.440  -6.542 -10.721  1.00 68.20           C  
ANISOU 6520  CD1 PHE A 796     7402  11875   6637   2125   -408  -1322       C  
ATOM   6521  CD2 PHE A 796     -24.544  -5.157  -8.983  1.00 69.07           C  
ANISOU 6521  CD2 PHE A 796     7401  12225   6618   2295   -501  -1692       C  
ATOM   6522  CE1 PHE A 796     -25.927  -7.436  -9.770  1.00 69.58           C  
ANISOU 6522  CE1 PHE A 796     7451  12353   6633   2170   -332  -1211       C  
ATOM   6523  CE2 PHE A 796     -25.022  -6.047  -8.024  1.00 71.63           C  
ANISOU 6523  CE2 PHE A 796     7596  12871   6747   2348   -425  -1582       C  
ATOM   6524  CZ  PHE A 796     -25.717  -7.188  -8.419  1.00 71.83           C  
ANISOU 6524  CZ  PHE A 796     7616  12924   6752   2282   -339  -1334       C  
ATOM   6525  N   PRO A 797     -23.091  -4.508 -14.439  1.00 57.42           N  
ANISOU 6525  N   PRO A 797     6492   9451   5874   1821   -600  -1437       N  
ATOM   6526  CA  PRO A 797     -22.729  -3.853 -15.696  1.00 54.64           C  
ANISOU 6526  CA  PRO A 797     6270   8788   5702   1730   -653  -1443       C  
ATOM   6527  C   PRO A 797     -23.125  -2.382 -15.729  1.00 55.68           C  
ANISOU 6527  C   PRO A 797     6427   8798   5930   1806   -749  -1647       C  
ATOM   6528  O   PRO A 797     -24.272  -2.042 -15.420  1.00 57.21           O  
ANISOU 6528  O   PRO A 797     6568   9075   6093   1914   -762  -1714       O  
ATOM   6529  CB  PRO A 797     -23.520  -4.644 -16.738  1.00 52.74           C  
ANISOU 6529  CB  PRO A 797     6076   8464   5500   1662   -599  -1247       C  
ATOM   6530  CG  PRO A 797     -23.742  -5.974 -16.108  1.00 53.08           C  
ANISOU 6530  CG  PRO A 797     6033   8735   5401   1667   -508  -1102       C  
ATOM   6531  CD  PRO A 797     -23.964  -5.675 -14.670  1.00 54.76           C  
ANISOU 6531  CD  PRO A 797     6124   9206   5476   1797   -515  -1235       C  
ATOM   6532  N   GLY A 798     -22.167  -1.525 -16.076  1.00 54.41           N  
ANISOU 6532  N   GLY A 798     6342   8442   5887   1751   -817  -1747       N  
ATOM   6533  CA  GLY A 798     -22.432  -0.109 -16.322  1.00 55.10           C  
ANISOU 6533  CA  GLY A 798     6481   8345   6109   1799   -917  -1920       C  
ATOM   6534  C   GLY A 798     -23.024   0.120 -17.708  1.00 54.50           C  
ANISOU 6534  C   GLY A 798     6511   8026   6170   1740   -934  -1810       C  
ATOM   6535  O   GLY A 798     -23.290  -0.845 -18.433  1.00 51.21           O  
ANISOU 6535  O   GLY A 798     6118   7606   5733   1666   -866  -1613       O  
ATOM   6536  N   PRO A 799     -23.236   1.400 -18.089  1.00 56.05           N  
ANISOU 6536  N   PRO A 799     6771   8017   6510   1773  -1028  -1937       N  
ATOM   6537  CA  PRO A 799     -23.768   1.738 -19.418  1.00 56.35           C  
ANISOU 6537  CA  PRO A 799     6912   7817   6680   1723  -1055  -1834       C  
ATOM   6538  C   PRO A 799     -22.857   1.261 -20.551  1.00 55.19           C  
ANISOU 6538  C   PRO A 799     6862   7510   6600   1547  -1024  -1659       C  
ATOM   6539  O   PRO A 799     -21.629   1.350 -20.441  1.00 56.09           O  
ANISOU 6539  O   PRO A 799     6997   7579   6737   1464  -1031  -1686       O  
ATOM   6540  CB  PRO A 799     -23.835   3.273 -19.396  1.00 57.48           C  
ANISOU 6540  CB  PRO A 799     7102   7768   6968   1789  -1172  -2024       C  
ATOM   6541  CG  PRO A 799     -23.898   3.632 -17.939  1.00 59.33           C  
ANISOU 6541  CG  PRO A 799     7227   8202   7113   1925  -1197  -2242       C  
ATOM   6542  CD  PRO A 799     -23.028   2.606 -17.263  1.00 59.07           C  
ANISOU 6542  CD  PRO A 799     7127   8380   6936   1868  -1118  -2188       C  
ATOM   6543  N   LYS A 800     -23.468   0.743 -21.612  1.00 53.64           N  
ANISOU 6543  N   LYS A 800     6713   7245   6425   1496   -989  -1488       N  
ATOM   6544  CA  LYS A 800     -22.759   0.273 -22.814  1.00 53.25           C  
ANISOU 6544  CA  LYS A 800     6751   7051   6432   1338   -959  -1319       C  
ATOM   6545  C   LYS A 800     -21.833  -0.934 -22.571  1.00 51.11           C  
ANISOU 6545  C   LYS A 800     6445   6913   6062   1253   -874  -1224       C  
ATOM   6546  O   LYS A 800     -20.971  -1.233 -23.400  1.00 52.07           O  
ANISOU 6546  O   LYS A 800     6630   6928   6228   1125   -854  -1122       O  
ATOM   6547  CB  LYS A 800     -22.009   1.430 -23.501  1.00 54.32           C  
ANISOU 6547  CB  LYS A 800     6988   6926   6726   1264  -1040  -1365       C  
ATOM   6548  CG  LYS A 800     -22.924   2.562 -23.970  1.00 59.46           C  
ANISOU 6548  CG  LYS A 800     7691   7405   7494   1337  -1126  -1420       C  
ATOM   6549  CD  LYS A 800     -22.152   3.797 -24.424  1.00 64.73           C  
ANISOU 6549  CD  LYS A 800     8451   7817   8325   1272  -1215  -1482       C  
ATOM   6550  CE  LYS A 800     -23.114   4.916 -24.832  1.00 69.87           C  
ANISOU 6550  CE  LYS A 800     9154   8294   9098   1362  -1306  -1533       C  
ATOM   6551  NZ  LYS A 800     -22.462   6.262 -24.897  1.00 71.50           N  
ANISOU 6551  NZ  LYS A 800     9433   8262   9471   1334  -1406  -1644       N  
ATOM   6552  N   CYS A 801     -22.038  -1.634 -21.453  1.00 49.39           N  
ANISOU 6552  N   CYS A 801     6124   6934   5708   1329   -824  -1251       N  
ATOM   6553  CA  CYS A 801     -21.211  -2.783 -21.082  1.00 48.65           C  
ANISOU 6553  CA  CYS A 801     5990   6980   5517   1271   -749  -1164       C  
ATOM   6554  C   CYS A 801     -21.289  -3.894 -22.134  1.00 46.88           C  
ANISOU 6554  C   CYS A 801     5807   6712   5292   1170   -681   -960       C  
ATOM   6555  O   CYS A 801     -22.375  -4.413 -22.402  1.00 45.83           O  
ANISOU 6555  O   CYS A 801     5656   6626   5131   1198   -648   -877       O  
ATOM   6556  CB  CYS A 801     -21.614  -3.332 -19.708  1.00 48.91           C  
ANISOU 6556  CB  CYS A 801     5900   7286   5397   1381   -709  -1209       C  
ATOM   6557  SG  CYS A 801     -20.618  -4.756 -19.133  1.00 51.61           S  
ANISOU 6557  SG  CYS A 801     6186   7808   5615   1328   -621  -1093       S  
ATOM   6558  N   PRO A 802     -20.138  -4.247 -22.742  1.00 44.97           N  
ANISOU 6558  N   PRO A 802     5617   6385   5086   1052   -661   -889       N  
ATOM   6559  CA  PRO A 802     -20.106  -5.342 -23.719  1.00 41.99           C  
ANISOU 6559  CA  PRO A 802     5274   5973   4706    959   -597   -713       C  
ATOM   6560  C   PRO A 802     -20.517  -6.680 -23.105  1.00 40.17           C  
ANISOU 6560  C   PRO A 802     4968   5935   4361    993   -518   -620       C  
ATOM   6561  O   PRO A 802     -20.370  -6.894 -21.889  1.00 38.62           O  
ANISOU 6561  O   PRO A 802     4690   5911   4071   1066   -503   -673       O  
ATOM   6562  CB  PRO A 802     -18.640  -5.378 -24.168  1.00 39.90           C  
ANISOU 6562  CB  PRO A 802     5054   5623   4481    849   -596   -695       C  
ATOM   6563  CG  PRO A 802     -18.147  -3.991 -23.931  1.00 43.87           C  
ANISOU 6563  CG  PRO A 802     5582   6026   5059    857   -677   -844       C  
ATOM   6564  CD  PRO A 802     -18.832  -3.565 -22.652  1.00 44.13           C  
ANISOU 6564  CD  PRO A 802     5539   6197   5033    996   -704   -977       C  
ATOM   6565  N   PHE A 803     -21.033  -7.555 -23.962  1.00 37.29           N  
ANISOU 6565  N   PHE A 803     4627   5536   4005    939   -472   -480       N  
ATOM   6566  CA  PHE A 803     -21.556  -8.856 -23.571  1.00 37.55           C  
ANISOU 6566  CA  PHE A 803     4598   5715   3954    954   -398   -371       C  
ATOM   6567  C   PHE A 803     -20.577  -9.679 -22.746  1.00 37.80           C  
ANISOU 6567  C   PHE A 803     4582   5869   3910    952   -354   -341       C  
ATOM   6568  O   PHE A 803     -20.945 -10.206 -21.696  1.00 40.68           O  
ANISOU 6568  O   PHE A 803     4864   6413   4179   1021   -319   -325       O  
ATOM   6569  CB  PHE A 803     -21.961  -9.638 -24.816  1.00 38.00           C  
ANISOU 6569  CB  PHE A 803     4705   5675   4058    868   -364   -237       C  
ATOM   6570  CG  PHE A 803     -22.777 -10.861 -24.527  1.00 37.30           C  
ANISOU 6570  CG  PHE A 803     4556   5708   3908    880   -298   -128       C  
ATOM   6571  CD1 PHE A 803     -24.130 -10.751 -24.228  1.00 37.08           C  
ANISOU 6571  CD1 PHE A 803     4476   5764   3851    945   -298   -133       C  
ATOM   6572  CD2 PHE A 803     -22.200 -12.122 -24.587  1.00 36.32           C  
ANISOU 6572  CD2 PHE A 803     4427   5609   3765    823   -238    -19       C  
ATOM   6573  CE1 PHE A 803     -24.898 -11.885 -23.973  1.00 39.27           C  
ANISOU 6573  CE1 PHE A 803     4692   6152   4077    941   -236    -25       C  
ATOM   6574  CE2 PHE A 803     -22.956 -13.267 -24.333  1.00 38.53           C  
ANISOU 6574  CE2 PHE A 803     4655   5983   4004    823   -180     90       C  
ATOM   6575  CZ  PHE A 803     -24.304 -13.148 -24.028  1.00 39.91           C  
ANISOU 6575  CZ  PHE A 803     4774   6242   4147    876   -178     91       C  
ATOM   6576  N   HIS A 804     -19.336  -9.782 -23.216  1.00 37.47           N  
ANISOU 6576  N   HIS A 804     4587   5742   3907    875   -354   -329       N  
ATOM   6577  CA  HIS A 804     -18.325 -10.604 -22.545  1.00 37.08           C  
ANISOU 6577  CA  HIS A 804     4496   5800   3793    872   -315   -293       C  
ATOM   6578  C   HIS A 804     -17.858  -9.998 -21.213  1.00 38.75           C  
ANISOU 6578  C   HIS A 804     4640   6152   3932    956   -345   -418       C  
ATOM   6579  O   HIS A 804     -17.533 -10.726 -20.282  1.00 37.85           O  
ANISOU 6579  O   HIS A 804     4458   6200   3725   1000   -309   -383       O  
ATOM   6580  CB  HIS A 804     -17.147 -10.912 -23.479  1.00 35.14           C  
ANISOU 6580  CB  HIS A 804     4311   5435   3607    769   -306   -249       C  
ATOM   6581  CG  HIS A 804     -16.362  -9.705 -23.896  1.00 37.16           C  
ANISOU 6581  CG  HIS A 804     4615   5572   3932    724   -367   -356       C  
ATOM   6582  ND1 HIS A 804     -16.860  -8.753 -24.760  1.00 35.82           N  
ANISOU 6582  ND1 HIS A 804     4511   5253   3848    691   -413   -390       N  
ATOM   6583  CD2 HIS A 804     -15.105  -9.307 -23.582  1.00 35.34           C  
ANISOU 6583  CD2 HIS A 804     4375   5350   3701    701   -390   -431       C  
ATOM   6584  CE1 HIS A 804     -15.950  -7.813 -24.946  1.00 37.46           C  
ANISOU 6584  CE1 HIS A 804     4750   5373   4111    644   -461   -474       C  
ATOM   6585  NE2 HIS A 804     -14.875  -8.126 -24.245  1.00 32.65           N  
ANISOU 6585  NE2 HIS A 804     4094   4860   3452    646   -447   -505       N  
ATOM   6586  N   ILE A 805     -17.856  -8.668 -21.121  1.00 40.33           N  
ANISOU 6586  N   ILE A 805     4857   6292   4176    980   -414   -565       N  
ATOM   6587  CA  ILE A 805     -17.518  -7.985 -19.868  1.00 40.90           C  
ANISOU 6587  CA  ILE A 805     4860   6496   4183   1066   -452   -712       C  
ATOM   6588  C   ILE A 805     -18.623  -8.194 -18.837  1.00 43.71           C  
ANISOU 6588  C   ILE A 805     5129   7045   4433   1181   -432   -724       C  
ATOM   6589  O   ILE A 805     -18.343  -8.404 -17.654  1.00 46.38           O  
ANISOU 6589  O   ILE A 805     5383   7580   4661   1252   -421   -764       O  
ATOM   6590  CB  ILE A 805     -17.227  -6.476 -20.084  1.00 40.65           C  
ANISOU 6590  CB  ILE A 805     4874   6324   4246   1057   -537   -875       C  
ATOM   6591  CG1 ILE A 805     -16.025  -6.279 -21.019  1.00 38.83           C  
ANISOU 6591  CG1 ILE A 805     4717   5929   4108    933   -552   -857       C  
ATOM   6592  CG2 ILE A 805     -16.970  -5.778 -18.764  1.00 40.14           C  
ANISOU 6592  CG2 ILE A 805     4733   6402   4116   1151   -581  -1048       C  
ATOM   6593  CD1 ILE A 805     -14.695  -6.876 -20.502  1.00 36.29           C  
ANISOU 6593  CD1 ILE A 805     4351   5713   3725    907   -527   -850       C  
ATOM   6594  N   ARG A 806     -19.875  -8.143 -19.293  1.00 44.68           N  
ANISOU 6594  N   ARG A 806     5265   7127   4584   1199   -427   -685       N  
ATOM   6595  CA  ARG A 806     -21.020  -8.557 -18.479  1.00 45.95           C  
ANISOU 6595  CA  ARG A 806     5338   7478   4643   1290   -392   -659       C  
ATOM   6596  C   ARG A 806     -20.784  -9.969 -17.915  1.00 46.60           C  
ANISOU 6596  C   ARG A 806     5362   7720   4625   1282   -314   -509       C  
ATOM   6597  O   ARG A 806     -21.008 -10.216 -16.736  1.00 48.56           O  
ANISOU 6597  O   ARG A 806     5514   8188   4750   1366   -292   -521       O  
ATOM   6598  CB  ARG A 806     -22.305  -8.523 -19.311  1.00 45.33           C  
ANISOU 6598  CB  ARG A 806     5290   7313   4622   1281   -389   -604       C  
ATOM   6599  CG  ARG A 806     -23.555  -8.979 -18.567  1.00 47.52           C  
ANISOU 6599  CG  ARG A 806     5469   7788   4798   1363   -348   -566       C  
ATOM   6600  CD  ARG A 806     -24.802  -8.956 -19.455  1.00 44.72           C  
ANISOU 6600  CD  ARG A 806     5139   7348   4503   1349   -347   -514       C  
ATOM   6601  NE  ARG A 806     -25.171  -7.598 -19.860  1.00 43.17           N  
ANISOU 6601  NE  ARG A 806     4986   7027   4390   1394   -428   -655       N  
ATOM   6602  CZ  ARG A 806     -25.883  -6.748 -19.120  1.00 43.31           C  
ANISOU 6602  CZ  ARG A 806     4941   7145   4370   1514   -468   -795       C  
ATOM   6603  NH1 ARG A 806     -26.326  -7.098 -17.912  1.00 42.88           N  
ANISOU 6603  NH1 ARG A 806     4769   7343   4180   1601   -431   -814       N  
ATOM   6604  NH2 ARG A 806     -26.142  -5.535 -19.588  1.00 39.44           N  
ANISOU 6604  NH2 ARG A 806     4504   6506   3976   1551   -546   -915       N  
ATOM   6605  N   GLY A 807     -20.314 -10.879 -18.768  1.00 45.37           N  
ANISOU 6605  N   GLY A 807     5264   7453   4522   1184   -274   -370       N  
ATOM   6606  CA  GLY A 807     -20.026 -12.249 -18.368  1.00 42.87           C  
ANISOU 6606  CA  GLY A 807     4908   7245   4137   1170   -206   -218       C  
ATOM   6607  C   GLY A 807     -18.957 -12.324 -17.303  1.00 44.27           C  
ANISOU 6607  C   GLY A 807     5027   7568   4223   1218   -209   -260       C  
ATOM   6608  O   GLY A 807     -19.060 -13.121 -16.363  1.00 45.33           O  
ANISOU 6608  O   GLY A 807     5084   7891   4250   1268   -165   -176       O  
ATOM   6609  N   ILE A 808     -17.929 -11.494 -17.446  1.00 43.34           N  
ANISOU 6609  N   ILE A 808     4945   7373   4150   1199   -262   -385       N  
ATOM   6610  CA  ILE A 808     -16.851 -11.444 -16.464  1.00 45.58           C  
ANISOU 6610  CA  ILE A 808     5171   7798   4351   1243   -275   -449       C  
ATOM   6611  C   ILE A 808     -17.381 -10.946 -15.118  1.00 48.08           C  
ANISOU 6611  C   ILE A 808     5385   8340   4542   1363   -292   -554       C  
ATOM   6612  O   ILE A 808     -17.061 -11.519 -14.072  1.00 51.60           O  
ANISOU 6612  O   ILE A 808     5748   8994   4863   1423   -265   -516       O  
ATOM   6613  CB  ILE A 808     -15.655 -10.585 -16.961  1.00 45.75           C  
ANISOU 6613  CB  ILE A 808     5247   7681   4456   1184   -332   -571       C  
ATOM   6614  CG1 ILE A 808     -14.929 -11.307 -18.106  1.00 43.78           C  
ANISOU 6614  CG1 ILE A 808     5071   7271   4290   1075   -302   -453       C  
ATOM   6615  CG2 ILE A 808     -14.685 -10.280 -15.817  1.00 44.13           C  
ANISOU 6615  CG2 ILE A 808     4966   7644   4158   1243   -360   -681       C  
ATOM   6616  CD1 ILE A 808     -14.214 -10.392 -19.075  1.00 42.84           C  
ANISOU 6616  CD1 ILE A 808     5030   6960   4289    987   -352   -541       C  
ATOM   6617  N   LEU A 809     -18.209  -9.902 -15.158  1.00 47.69           N  
ANISOU 6617  N   LEU A 809     5340   8255   4525   1403   -336   -683       N  
ATOM   6618  CA  LEU A 809     -18.775  -9.312 -13.946  1.00 47.11           C  
ANISOU 6618  CA  LEU A 809     5168   8393   4338   1525   -359   -812       C  
ATOM   6619  C   LEU A 809     -19.689 -10.291 -13.218  1.00 47.71           C  
ANISOU 6619  C   LEU A 809     5155   8687   4285   1583   -289   -675       C  
ATOM   6620  O   LEU A 809     -19.674 -10.353 -11.987  1.00 51.03           O  
ANISOU 6620  O   LEU A 809     5472   9357   4561   1674   -281   -715       O  
ATOM   6621  CB  LEU A 809     -19.508  -8.006 -14.264  1.00 46.63           C  
ANISOU 6621  CB  LEU A 809     5138   8221   4360   1559   -424   -977       C  
ATOM   6622  CG  LEU A 809     -18.682  -6.835 -14.807  1.00 46.19           C  
ANISOU 6622  CG  LEU A 809     5158   7961   4430   1513   -504  -1132       C  
ATOM   6623  CD1 LEU A 809     -19.568  -5.636 -15.038  1.00 47.78           C  
ANISOU 6623  CD1 LEU A 809     5385   8061   4710   1563   -567  -1276       C  
ATOM   6624  CD2 LEU A 809     -17.553  -6.462 -13.878  1.00 49.89           C  
ANISOU 6624  CD2 LEU A 809     5572   8547   4835   1544   -540  -1266       C  
ATOM   6625  N   THR A 810     -20.464 -11.066 -13.980  1.00 46.14           N  
ANISOU 6625  N   THR A 810     4993   8401   4136   1525   -239   -512       N  
ATOM   6626  CA  THR A 810     -21.269 -12.157 -13.422  1.00 46.52           C  
ANISOU 6626  CA  THR A 810     4965   8628   4081   1549   -165   -347       C  
ATOM   6627  C   THR A 810     -20.357 -13.159 -12.695  1.00 47.51           C  
ANISOU 6627  C   THR A 810     5046   8892   4113   1553   -124   -228       C  
ATOM   6628  O   THR A 810     -20.607 -13.517 -11.545  1.00 49.20           O  
ANISOU 6628  O   THR A 810     5155   9359   4179   1630    -94   -189       O  
ATOM   6629  CB  THR A 810     -22.100 -12.879 -14.518  1.00 46.11           C  
ANISOU 6629  CB  THR A 810     4972   8422   4125   1462   -123   -192       C  
ATOM   6630  OG1 THR A 810     -22.789 -11.915 -15.322  1.00 46.15           O  
ANISOU 6630  OG1 THR A 810     5029   8276   4228   1456   -169   -300       O  
ATOM   6631  CG2 THR A 810     -23.117 -13.834 -13.901  1.00 41.67           C  
ANISOU 6631  CG2 THR A 810     4321   8048   3465   1486    -53    -40       C  
ATOM   6632  N   TYR A 811     -19.288 -13.578 -13.368  1.00 46.13           N  
ANISOU 6632  N   TYR A 811     4948   8559   4021   1475   -125   -172       N  
ATOM   6633  CA  TYR A 811     -18.299 -14.472 -12.781  1.00 46.24           C  
ANISOU 6633  CA  TYR A 811     4929   8678   3963   1482    -97    -69       C  
ATOM   6634  C   TYR A 811     -17.681 -13.896 -11.510  1.00 48.53           C  
ANISOU 6634  C   TYR A 811     5128   9195   4118   1581   -131   -200       C  
ATOM   6635  O   TYR A 811     -17.535 -14.612 -10.520  1.00 48.74           O  
ANISOU 6635  O   TYR A 811     5071   9438   4011   1639    -96   -103       O  
ATOM   6636  CB  TYR A 811     -17.201 -14.800 -13.798  1.00 42.67           C  
ANISOU 6636  CB  TYR A 811     4572   8009   3631   1390   -104    -31       C  
ATOM   6637  CG  TYR A 811     -16.089 -15.678 -13.261  1.00 42.91           C  
ANISOU 6637  CG  TYR A 811     4571   8132   3599   1405    -83     63       C  
ATOM   6638  CD1 TYR A 811     -16.237 -17.062 -13.196  1.00 42.51           C  
ANISOU 6638  CD1 TYR A 811     4511   8107   3534   1391    -21    277       C  
ATOM   6639  CD2 TYR A 811     -14.888 -15.123 -12.819  1.00 42.96           C  
ANISOU 6639  CD2 TYR A 811     4555   8199   3569   1434   -128    -62       C  
ATOM   6640  CE1 TYR A 811     -15.222 -17.870 -12.702  1.00 42.87           C  
ANISOU 6640  CE1 TYR A 811     4529   8231   3527   1416     -6    370       C  
ATOM   6641  CE2 TYR A 811     -13.869 -15.918 -12.330  1.00 43.31           C  
ANISOU 6641  CE2 TYR A 811     4565   8338   3554   1456   -113     24       C  
ATOM   6642  CZ  TYR A 811     -14.038 -17.294 -12.273  1.00 46.09           C  
ANISOU 6642  CZ  TYR A 811     4911   8710   3890   1453    -52    243       C  
ATOM   6643  OH  TYR A 811     -13.022 -18.096 -11.779  1.00 46.83           O  
ANISOU 6643  OH  TYR A 811     4972   8893   3929   1487    -41    334       O  
ATOM   6644  N   ASN A 812     -17.313 -12.614 -11.544  1.00 50.90           N  
ANISOU 6644  N   ASN A 812     5443   9445   4453   1599   -201   -418       N  
ATOM   6645  CA  ASN A 812     -16.718 -11.958 -10.375  1.00 54.45           C  
ANISOU 6645  CA  ASN A 812     5806  10102   4782   1691   -244   -577       C  
ATOM   6646  C   ASN A 812     -17.640 -11.991  -9.159  1.00 58.11           C  
ANISOU 6646  C   ASN A 812     6147  10855   5077   1804   -222   -585       C  
ATOM   6647  O   ASN A 812     -17.186 -12.257  -8.043  1.00 61.55           O  
ANISOU 6647  O   ASN A 812     6487  11538   5361   1878   -216   -583       O  
ATOM   6648  CB  ASN A 812     -16.324 -10.510 -10.684  1.00 54.52           C  
ANISOU 6648  CB  ASN A 812     5856   9980   4881   1683   -329   -819       C  
ATOM   6649  CG  ASN A 812     -15.088 -10.403 -11.556  1.00 51.50           C  
ANISOU 6649  CG  ASN A 812     5559   9388   4621   1582   -356   -832       C  
ATOM   6650  OD1 ASN A 812     -14.396 -11.389 -11.827  1.00 52.13           O  
ANISOU 6650  OD1 ASN A 812     5657   9446   4704   1534   -316   -683       O  
ATOM   6651  ND2 ASN A 812     -14.798  -9.188 -11.996  1.00 50.42           N  
ANISOU 6651  ND2 ASN A 812     5471   9098   4588   1552   -425  -1013       N  
ATOM   6652  N   ARG A 813     -18.928 -11.720  -9.376  1.00 59.67           N  
ANISOU 6652  N   ARG A 813     6342  11037   5294   1819   -210   -594       N  
ATOM   6653  CA  ARG A 813     -19.913 -11.787  -8.296  1.00 61.31           C  
ANISOU 6653  CA  ARG A 813     6427  11528   5340   1922   -181   -592       C  
ATOM   6654  C   ARG A 813     -20.039 -13.207  -7.767  1.00 62.15           C  
ANISOU 6654  C   ARG A 813     6474  11804   5336   1918    -99   -340       C  
ATOM   6655  O   ARG A 813     -20.115 -13.415  -6.557  1.00 63.91           O  
ANISOU 6655  O   ARG A 813     6579  12324   5381   2007    -79   -325       O  
ATOM   6656  CB  ARG A 813     -21.281 -11.285  -8.747  1.00 61.11           C  
ANISOU 6656  CB  ARG A 813     6409  11441   5369   1933   -182   -639       C  
ATOM   6657  CG  ARG A 813     -21.372  -9.784  -8.925  1.00 62.29           C  
ANISOU 6657  CG  ARG A 813     6585  11490   5591   1978   -267   -903       C  
ATOM   6658  CD  ARG A 813     -22.820  -9.305  -9.000  1.00 60.86           C  
ANISOU 6658  CD  ARG A 813     6370  11342   5412   2033   -267   -959       C  
ATOM   6659  NE  ARG A 813     -23.653 -10.151  -9.853  1.00 58.75           N  
ANISOU 6659  NE  ARG A 813     6145  10966   5212   1953   -207   -756       N  
ATOM   6660  CZ  ARG A 813     -23.755 -10.040 -11.175  1.00 57.08           C  
ANISOU 6660  CZ  ARG A 813     6052  10464   5171   1860   -223   -722       C  
ATOM   6661  NH1 ARG A 813     -23.069  -9.113 -11.838  1.00 54.46           N  
ANISOU 6661  NH1 ARG A 813     5814   9910   4968   1830   -295   -861       N  
ATOM   6662  NH2 ARG A 813     -24.552 -10.870 -11.839  1.00 56.45           N  
ANISOU 6662  NH2 ARG A 813     5994  10323   5134   1794   -168   -544       N  
ATOM   6663  N   ALA A 814     -20.039 -14.177  -8.678  1.00 60.49           N  
ANISOU 6663  N   ALA A 814     6344  11404   5234   1816    -54   -143       N  
ATOM   6664  CA  ALA A 814     -20.162 -15.582  -8.304  1.00 61.45           C  
ANISOU 6664  CA  ALA A 814     6427  11637   5286   1798     20    112       C  
ATOM   6665  C   ALA A 814     -18.964 -16.085  -7.483  1.00 63.29           C  
ANISOU 6665  C   ALA A 814     6615  12018   5415   1840     20    166       C  
ATOM   6666  O   ALA A 814     -19.138 -16.905  -6.576  1.00 64.07           O  
ANISOU 6666  O   ALA A 814     6627  12340   5376   1884     69    324       O  
ATOM   6667  CB  ALA A 814     -20.380 -16.444  -9.536  1.00 58.33           C  
ANISOU 6667  CB  ALA A 814     6135  10979   5050   1678     57    282       C  
ATOM   6668  N   ILE A 815     -17.765 -15.583  -7.792  1.00 63.15           N  
ANISOU 6668  N   ILE A 815     6651  11884   5458   1825    -35     40       N  
ATOM   6669  CA  ILE A 815     -16.547 -15.983  -7.069  1.00 66.30           C  
ANISOU 6669  CA  ILE A 815     7006  12420   5764   1867    -44     71       C  
ATOM   6670  C   ILE A 815     -16.107 -15.028  -5.945  1.00 69.54           C  
ANISOU 6670  C   ILE A 815     7317  13077   6028   1974    -98   -138       C  
ATOM   6671  O   ILE A 815     -15.104 -15.289  -5.273  1.00 69.91           O  
ANISOU 6671  O   ILE A 815     7313  13267   5982   2018   -112   -128       O  
ATOM   6672  CB  ILE A 815     -15.330 -16.218  -8.015  1.00 63.87           C  
ANISOU 6672  CB  ILE A 815     6800  11870   5598   1787    -66     83       C  
ATOM   6673  CG1 ILE A 815     -14.924 -14.914  -8.716  1.00 61.97           C  
ANISOU 6673  CG1 ILE A 815     6624  11451   5472   1748   -136   -156       C  
ATOM   6674  CG2 ILE A 815     -15.609 -17.363  -8.987  1.00 63.29           C  
ANISOU 6674  CG2 ILE A 815     6810  11589   5648   1695    -11    301       C  
ATOM   6675  CD1 ILE A 815     -13.438 -14.787  -8.990  1.00 58.10           C  
ANISOU 6675  CD1 ILE A 815     6167  10878   5030   1716   -175   -221       C  
ATOM   6676  N   LYS A 816     -16.848 -13.936  -5.757  1.00 72.47           N  
ANISOU 6676  N   LYS A 816     7657  13495   6381   2018   -132   -332       N  
ATOM   6677  CA  LYS A 816     -16.517 -12.906  -4.764  1.00 76.16           C  
ANISOU 6677  CA  LYS A 816     8034  14175   6728   2119   -193   -569       C  
ATOM   6678  C   LYS A 816     -16.204 -13.500  -3.391  1.00 78.87           C  
ANISOU 6678  C   LYS A 816     8245  14875   6847   2216   -168   -491       C  
ATOM   6679  O   LYS A 816     -16.924 -14.379  -2.906  1.00 78.94           O  
ANISOU 6679  O   LYS A 816     8194  15050   6750   2242   -101   -292       O  
ATOM   6680  CB  LYS A 816     -17.649 -11.871  -4.658  1.00 77.64           C  
ANISOU 6680  CB  LYS A 816     8193  14395   6912   2171   -218   -749       C  
ATOM   6681  CG  LYS A 816     -17.469 -10.808  -3.565  1.00 81.97           C  
ANISOU 6681  CG  LYS A 816     8635  15179   7329   2289   -281  -1012       C  
ATOM   6682  CD  LYS A 816     -18.782 -10.066  -3.289  1.00 85.62           C  
ANISOU 6682  CD  LYS A 816     9044  15734   7754   2364   -288  -1144       C  
ATOM   6683  CE  LYS A 816     -18.838  -9.478  -1.875  1.00 88.56           C  
ANISOU 6683  CE  LYS A 816     9265  16464   7919   2507   -319  -1332       C  
ATOM   6684  NZ  LYS A 816     -18.027  -8.235  -1.715  1.00 89.76           N  
ANISOU 6684  NZ  LYS A 816     9423  16561   8118   2539   -419  -1635       N  
ATOM   6685  N   GLY A 817     -15.109 -13.028  -2.795  1.00 80.62           N  
ANISOU 6685  N   GLY A 817     8421  15211   7000   2264   -225   -640       N  
ATOM   6686  CA  GLY A 817     -14.717 -13.416  -1.446  1.00 84.02           C  
ANISOU 6686  CA  GLY A 817     8717  16002   7204   2368   -217   -603       C  
ATOM   6687  C   GLY A 817     -14.017 -14.759  -1.362  1.00 85.46           C  
ANISOU 6687  C   GLY A 817     8904  16216   7351   2347   -170   -334       C  
ATOM   6688  O   GLY A 817     -13.723 -15.241  -0.265  1.00 87.44           O  
ANISOU 6688  O   GLY A 817     9045  16769   7411   2433   -156   -255       O  
ATOM   6689  N   ASN A 818     -13.755 -15.364  -2.518  1.00 84.84           N  
ANISOU 6689  N   ASN A 818     8948  15831   7455   2239   -147   -196       N  
ATOM   6690  CA  ASN A 818     -13.060 -16.648  -2.581  1.00 85.56           C  
ANISOU 6690  CA  ASN A 818     9059  15902   7547   2218   -108     51       C  
ATOM   6691  C   ASN A 818     -11.635 -16.480  -3.084  1.00 85.07           C  
ANISOU 6691  C   ASN A 818     9051  15693   7579   2179   -159    -35       C  
ATOM   6692  O   ASN A 818     -11.412 -16.130  -4.247  1.00 83.91           O  
ANISOU 6692  O   ASN A 818     9013  15249   7618   2084   -178   -105       O  
ATOM   6693  CB  ASN A 818     -13.828 -17.649  -3.449  1.00 84.75           C  
ANISOU 6693  CB  ASN A 818     9043  15588   7571   2131    -40    292       C  
ATOM   6694  CG  ASN A 818     -15.113 -18.131  -2.791  1.00 88.94           C  
ANISOU 6694  CG  ASN A 818     9498  16313   7984   2168     23    442       C  
ATOM   6695  OD1 ASN A 818     -15.126 -18.509  -1.613  1.00 88.55           O  
ANISOU 6695  OD1 ASN A 818     9333  16572   7739   2256     42    530       O  
ATOM   6696  ND2 ASN A 818     -16.203 -18.126  -3.557  1.00 88.75           N  
ANISOU 6696  ND2 ASN A 818     9532  16118   8072   2099     55    477       N  
ATOM   6697  N   ILE A 819     -10.681 -16.737  -2.190  1.00 86.01           N  
ANISOU 6697  N   ILE A 819     9084  16037   7558   2255   -180    -25       N  
ATOM   6698  CA  ILE A 819      -9.256 -16.513  -2.451  1.00 85.86           C  
ANISOU 6698  CA  ILE A 819     9084  15947   7593   2236   -234   -129       C  
ATOM   6699  C   ILE A 819      -8.667 -17.388  -3.558  1.00 82.70           C  
ANISOU 6699  C   ILE A 819     8792  15270   7359   2149   -208     33       C  
ATOM   6700  O   ILE A 819      -7.807 -16.936  -4.312  1.00 81.42           O  
ANISOU 6700  O   ILE A 819     8688  14929   7320   2084   -248    -89       O  
ATOM   6701  CB  ILE A 819      -8.391 -16.651  -1.155  1.00 88.84           C  
ANISOU 6701  CB  ILE A 819     9328  16666   7761   2351   -264   -147       C  
ATOM   6702  CG1 ILE A 819      -8.884 -17.800  -0.260  1.00 90.49           C  
ANISOU 6702  CG1 ILE A 819     9462  17115   7806   2431   -203    121       C  
ATOM   6703  CG2 ILE A 819      -8.390 -15.347  -0.367  1.00 91.44           C  
ANISOU 6703  CG2 ILE A 819     9566  17197   7979   2413   -328   -441       C  
ATOM   6704  CD1 ILE A 819      -8.169 -19.124  -0.466  1.00 90.54           C  
ANISOU 6704  CD1 ILE A 819     9501  17056   7845   2427   -172    381       C  
ATOM   6705  N   ASP A 820      -9.148 -18.625  -3.664  1.00 81.18           N  
ANISOU 6705  N   ASP A 820     8625  15044   7177   2144   -143    303       N  
ATOM   6706  CA  ASP A 820      -8.521 -19.622  -4.536  1.00 78.76           C  
ANISOU 6706  CA  ASP A 820     8403  14515   7006   2086   -119    469       C  
ATOM   6707  C   ASP A 820      -9.083 -19.720  -5.962  1.00 74.05           C  
ANISOU 6707  C   ASP A 820     7940  13577   6621   1965    -92    499       C  
ATOM   6708  O   ASP A 820      -8.487 -20.392  -6.807  1.00 72.13           O  
ANISOU 6708  O   ASP A 820     7770  13135   6503   1913    -81    588       O  
ATOM   6709  CB  ASP A 820      -8.495 -21.002  -3.856  1.00 82.38           C  
ANISOU 6709  CB  ASP A 820     8817  15113   7370   2153    -73    750       C  
ATOM   6710  CG  ASP A 820      -9.860 -21.445  -3.366  1.00 87.31           C  
ANISOU 6710  CG  ASP A 820     9410  15842   7922   2168    -15    911       C  
ATOM   6711  OD1 ASP A 820     -10.414 -20.794  -2.451  1.00 91.62           O  
ANISOU 6711  OD1 ASP A 820     9862  16637   8312   2231    -23    818       O  
ATOM   6712  OD2 ASP A 820     -10.370 -22.461  -3.887  1.00 89.46           O  
ANISOU 6712  OD2 ASP A 820     9745  15953   8292   2117     38   1127       O  
ATOM   6713  N   ALA A 821     -10.213 -19.061  -6.229  1.00 69.86           N  
ANISOU 6713  N   ALA A 821     7433  12987   6124   1928    -84    420       N  
ATOM   6714  CA  ALA A 821     -10.822 -19.088  -7.562  1.00 64.78           C  
ANISOU 6714  CA  ALA A 821     6907  12039   5667   1818    -62    440       C  
ATOM   6715  C   ALA A 821      -9.989 -18.280  -8.545  1.00 61.39           C  
ANISOU 6715  C   ALA A 821     6551  11404   5371   1744   -111    259       C  
ATOM   6716  O   ALA A 821      -9.556 -17.177  -8.209  1.00 61.95           O  
ANISOU 6716  O   ALA A 821     6584  11552   5402   1765   -167     49       O  
ATOM   6717  CB  ALA A 821     -12.242 -18.553  -7.519  1.00 65.04           C  
ANISOU 6717  CB  ALA A 821     6933  12090   5688   1810    -45    399       C  
ATOM   6718  N   PRO A 822      -9.742 -18.834  -9.752  1.00 57.56           N  
ANISOU 6718  N   PRO A 822     6164  10662   5043   1657    -92    340       N  
ATOM   6719  CA  PRO A 822      -9.043 -18.096 -10.805  1.00 55.51           C  
ANISOU 6719  CA  PRO A 822     5976  10200   4913   1572   -130    189       C  
ATOM   6720  C   PRO A 822      -9.716 -16.752 -11.073  1.00 56.78           C  
ANISOU 6720  C   PRO A 822     6161  10300   5114   1537   -166      1       C  
ATOM   6721  O   PRO A 822     -10.895 -16.712 -11.417  1.00 56.18           O  
ANISOU 6721  O   PRO A 822     6121  10147   5078   1513   -141     40       O  
ATOM   6722  CB  PRO A 822      -9.184 -19.004 -12.028  1.00 52.96           C  
ANISOU 6722  CB  PRO A 822     5751   9633   4737   1491    -88    332       C  
ATOM   6723  CG  PRO A 822      -9.350 -20.364 -11.485  1.00 53.40           C  
ANISOU 6723  CG  PRO A 822     5777   9774   4739   1545    -40    555       C  
ATOM   6724  CD  PRO A 822     -10.034 -20.225 -10.152  1.00 56.69           C  
ANISOU 6724  CD  PRO A 822     6097  10450   4992   1634    -34    578       C  
ATOM   6725  N   GLN A 823      -8.975 -15.665 -10.876  1.00 58.67           N  
ANISOU 6725  N   GLN A 823     6374  10574   5342   1538   -227   -202       N  
ATOM   6726  CA  GLN A 823      -9.457 -14.329 -11.198  1.00 60.29           C  
ANISOU 6726  CA  GLN A 823     6611  10688   5609   1502   -272   -391       C  
ATOM   6727  C   GLN A 823      -9.276 -14.099 -12.694  1.00 60.72           C  
ANISOU 6727  C   GLN A 823     6780  10452   5841   1379   -275   -399       C  
ATOM   6728  O   GLN A 823      -8.373 -14.671 -13.309  1.00 60.39           O  
ANISOU 6728  O   GLN A 823     6770  10323   5855   1329   -262   -334       O  
ATOM   6729  CB  GLN A 823      -8.681 -13.268 -10.416  1.00 63.16           C  
ANISOU 6729  CB  GLN A 823     6904  11189   5905   1542   -340   -607       C  
ATOM   6730  CG  GLN A 823      -8.737 -13.409  -8.887  1.00 67.82           C  
ANISOU 6730  CG  GLN A 823     7368  12101   6301   1669   -344   -624       C  
ATOM   6731  CD  GLN A 823      -9.977 -12.779  -8.259  1.00 73.41           C  
ANISOU 6731  CD  GLN A 823     8036  12918   6940   1734   -351   -707       C  
ATOM   6732  OE1 GLN A 823     -10.664 -13.407  -7.450  1.00 75.85           O  
ANISOU 6732  OE1 GLN A 823     8278  13423   7119   1814   -310   -593       O  
ATOM   6733  NE2 GLN A 823     -10.260 -11.530  -8.620  1.00 75.23           N  
ANISOU 6733  NE2 GLN A 823     8303  13025   7257   1702   -404   -903       N  
ATOM   6734  N   VAL A 824     -10.143 -13.276 -13.277  1.00 59.86           N  
ANISOU 6734  N   VAL A 824     6727  10203   5813   1338   -292   -477       N  
ATOM   6735  CA  VAL A 824     -10.022 -12.899 -14.679  1.00 57.29           C  
ANISOU 6735  CA  VAL A 824     6505   9616   5645   1224   -302   -495       C  
ATOM   6736  C   VAL A 824      -8.967 -11.800 -14.808  1.00 58.06           C  
ANISOU 6736  C   VAL A 824     6604   9666   5790   1177   -367   -675       C  
ATOM   6737  O   VAL A 824      -9.094 -10.734 -14.207  1.00 59.64           O  
ANISOU 6737  O   VAL A 824     6770   9923   5967   1211   -420   -842       O  
ATOM   6738  CB  VAL A 824     -11.380 -12.418 -15.268  1.00 56.29           C  
ANISOU 6738  CB  VAL A 824     6437   9361   5589   1201   -301   -501       C  
ATOM   6739  CG1 VAL A 824     -11.213 -11.945 -16.716  1.00 52.15           C  
ANISOU 6739  CG1 VAL A 824     6017   8578   5218   1085   -318   -520       C  
ATOM   6740  CG2 VAL A 824     -12.425 -13.522 -15.189  1.00 53.00           C  
ANISOU 6740  CG2 VAL A 824     6014   8989   5134   1232   -237   -321       C  
ATOM   6741  N   VAL A 825      -7.929 -12.069 -15.593  1.00 58.06           N  
ANISOU 6741  N   VAL A 825     6640   9563   5859   1097   -362   -645       N  
ATOM   6742  CA  VAL A 825      -6.846 -11.109 -15.777  1.00 58.57           C  
ANISOU 6742  CA  VAL A 825     6700   9581   5972   1035   -417   -798       C  
ATOM   6743  C   VAL A 825      -7.164 -10.127 -16.904  1.00 56.82           C  
ANISOU 6743  C   VAL A 825     6571   9124   5894    931   -447   -862       C  
ATOM   6744  O   VAL A 825      -7.372 -10.529 -18.051  1.00 54.13           O  
ANISOU 6744  O   VAL A 825     6307   8623   5636    858   -413   -755       O  
ATOM   6745  CB  VAL A 825      -5.492 -11.809 -16.051  1.00 59.21           C  
ANISOU 6745  CB  VAL A 825     6759   9687   6050    998   -400   -744       C  
ATOM   6746  CG1 VAL A 825      -4.368 -10.778 -16.161  1.00 60.14           C  
ANISOU 6746  CG1 VAL A 825     6858   9780   6213    927   -458   -908       C  
ATOM   6747  CG2 VAL A 825      -5.177 -12.827 -14.951  1.00 61.18           C  
ANISOU 6747  CG2 VAL A 825     6920  10165   6161   1109   -374   -662       C  
ATOM   6748  N   GLU A 826      -7.201  -8.843 -16.552  1.00 57.28           N  
ANISOU 6748  N   GLU A 826     6619   9164   5979    929   -512  -1037       N  
ATOM   6749  CA  GLU A 826      -7.376  -7.750 -17.505  1.00 56.43           C  
ANISOU 6749  CA  GLU A 826     6595   8835   6012    833   -554  -1111       C  
ATOM   6750  C   GLU A 826      -6.510  -7.944 -18.748  1.00 55.72           C  
ANISOU 6750  C   GLU A 826     6562   8596   6013    705   -536  -1038       C  
ATOM   6751  O   GLU A 826      -5.283  -7.936 -18.663  1.00 56.25           O  
ANISOU 6751  O   GLU A 826     6588   8715   6072    662   -546  -1081       O  
ATOM   6752  CB  GLU A 826      -7.038  -6.415 -16.830  1.00 58.37           C  
ANISOU 6752  CB  GLU A 826     6804   9097   6276    841   -635  -1326       C  
ATOM   6753  CG  GLU A 826      -6.950  -5.203 -17.759  1.00 59.50           C  
ANISOU 6753  CG  GLU A 826     7028   9002   6577    730   -689  -1407       C  
ATOM   6754  CD  GLU A 826      -8.281  -4.845 -18.402  1.00 61.35           C  
ANISOU 6754  CD  GLU A 826     7345   9079   6886    737   -691  -1364       C  
ATOM   6755  OE1 GLU A 826      -8.276  -4.450 -19.588  1.00 62.16           O  
ANISOU 6755  OE1 GLU A 826     7534   8975   7108    633   -699  -1316       O  
ATOM   6756  OE2 GLU A 826      -9.330  -4.958 -17.728  1.00 61.84           O  
ANISOU 6756  OE2 GLU A 826     7381   9235   6882    848   -686  -1377       O  
ATOM   6757  N   GLY A 827      -7.161  -8.129 -19.894  1.00 53.12           N  
ANISOU 6757  N   GLY A 827     6320   8100   5763    647   -508   -932       N  
ATOM   6758  CA  GLY A 827      -6.468  -8.229 -21.170  1.00 52.38           C  
ANISOU 6758  CA  GLY A 827     6283   7867   5753    524   -490   -866       C  
ATOM   6759  C   GLY A 827      -6.319  -9.638 -21.714  1.00 51.89           C  
ANISOU 6759  C   GLY A 827     6227   7828   5660    521   -419   -707       C  
ATOM   6760  O   GLY A 827      -6.018  -9.814 -22.896  1.00 49.89           O  
ANISOU 6760  O   GLY A 827     6027   7456   5471    429   -397   -641       O  
ATOM   6761  N   GLU A 828      -6.515 -10.640 -20.858  1.00 50.92           N  
ANISOU 6761  N   GLU A 828     6049   7860   5439    623   -383   -645       N  
ATOM   6762  CA  GLU A 828      -6.398 -12.038 -21.277  1.00 51.33           C  
ANISOU 6762  CA  GLU A 828     6107   7927   5471    631   -320   -495       C  
ATOM   6763  C   GLU A 828      -7.730 -12.607 -21.789  1.00 47.83           C  
ANISOU 6763  C   GLU A 828     5720   7400   5052    643   -283   -381       C  
ATOM   6764  O   GLU A 828      -8.761 -11.948 -21.706  1.00 46.85           O  
ANISOU 6764  O   GLU A 828     5621   7233   4946    659   -305   -416       O  
ATOM   6765  CB  GLU A 828      -5.757 -12.889 -20.165  1.00 54.60           C  
ANISOU 6765  CB  GLU A 828     6432   8537   5776    725   -303   -469       C  
ATOM   6766  CG  GLU A 828      -4.213 -12.731 -20.136  1.00 63.58           C  
ANISOU 6766  CG  GLU A 828     7519   9733   6905    688   -322   -539       C  
ATOM   6767  CD  GLU A 828      -3.497 -13.563 -19.065  1.00 70.37           C  
ANISOU 6767  CD  GLU A 828     8286  10794   7655    786   -311   -511       C  
ATOM   6768  OE1 GLU A 828      -2.537 -13.030 -18.459  1.00 73.46           O  
ANISOU 6768  OE1 GLU A 828     8609  11296   8006    791   -350   -623       O  
ATOM   6769  OE2 GLU A 828      -3.870 -14.739 -18.835  1.00 71.01           O  
ANISOU 6769  OE2 GLU A 828     8362  10923   7695    856   -266   -376       O  
ATOM   6770  N   LYS A 829      -7.710 -13.817 -22.337  1.00 45.25           N  
ANISOU 6770  N   LYS A 829     5411   7049   4732    637   -230   -254       N  
ATOM   6771  CA  LYS A 829      -8.909 -14.365 -22.968  1.00 43.28           C  
ANISOU 6771  CA  LYS A 829     5217   6708   4521    628   -197   -153       C  
ATOM   6772  C   LYS A 829      -9.849 -15.088 -22.011  1.00 43.17           C  
ANISOU 6772  C   LYS A 829     5163   6803   4438    723   -170    -76       C  
ATOM   6773  O   LYS A 829      -9.413 -15.721 -21.049  1.00 42.43           O  
ANISOU 6773  O   LYS A 829     5006   6850   4267    795   -155    -42       O  
ATOM   6774  CB  LYS A 829      -8.549 -15.240 -24.172  1.00 44.21           C  
ANISOU 6774  CB  LYS A 829     5379   6724   4695    563   -158    -67       C  
ATOM   6775  CG  LYS A 829      -7.733 -14.478 -25.223  1.00 43.94           C  
ANISOU 6775  CG  LYS A 829     5382   6590   4723    459   -180   -131       C  
ATOM   6776  CD  LYS A 829      -8.192 -14.768 -26.623  1.00 44.98           C  
ANISOU 6776  CD  LYS A 829     5584   6585   4923    384   -158    -68       C  
ATOM   6777  CE  LYS A 829      -7.613 -13.761 -27.600  1.00 44.31           C  
ANISOU 6777  CE  LYS A 829     5536   6408   4890    278   -185   -128       C  
ATOM   6778  NZ  LYS A 829      -8.105 -14.018 -28.974  1.00 49.83           N  
ANISOU 6778  NZ  LYS A 829     6298   6993   5640    209   -165    -65       N  
ATOM   6779  N   VAL A 830     -11.147 -14.971 -22.284  1.00 41.12           N  
ANISOU 6779  N   VAL A 830     4937   6484   4204    721   -164    -44       N  
ATOM   6780  CA  VAL A 830     -12.177 -15.648 -21.505  1.00 38.32           C  
ANISOU 6780  CA  VAL A 830     4544   6226   3789    794   -133     40       C  
ATOM   6781  C   VAL A 830     -13.109 -16.469 -22.386  1.00 37.78           C  
ANISOU 6781  C   VAL A 830     4524   6050   3780    752    -94    156       C  
ATOM   6782  O   VAL A 830     -13.417 -16.069 -23.511  1.00 37.77           O  
ANISOU 6782  O   VAL A 830     4586   5908   3856    680   -105    136       O  
ATOM   6783  CB  VAL A 830     -13.031 -14.657 -20.667  1.00 38.66           C  
ANISOU 6783  CB  VAL A 830     4552   6355   3784    855   -167    -50       C  
ATOM   6784  CG1 VAL A 830     -12.249 -14.167 -19.461  1.00 36.39           C  
ANISOU 6784  CG1 VAL A 830     4191   6228   3408    924   -197   -149       C  
ATOM   6785  CG2 VAL A 830     -13.528 -13.489 -21.517  1.00 32.56           C  
ANISOU 6785  CG2 VAL A 830     3842   5437   3092    802   -209   -140       C  
ATOM   6786  N   TYR A 831     -13.535 -17.622 -21.873  1.00 36.80           N  
ANISOU 6786  N   TYR A 831     4366   5995   3621    793    -49    278       N  
ATOM   6787  CA  TYR A 831     -14.647 -18.366 -22.452  1.00 34.43           C  
ANISOU 6787  CA  TYR A 831     4094   5619   3368    761    -14    381       C  
ATOM   6788  C   TYR A 831     -15.950 -17.706 -22.009  1.00 35.37           C  
ANISOU 6788  C   TYR A 831     4189   5797   3453    794    -25    353       C  
ATOM   6789  O   TYR A 831     -16.051 -17.226 -20.877  1.00 35.25           O  
ANISOU 6789  O   TYR A 831     4111   5931   3351    869    -39    306       O  
ATOM   6790  CB  TYR A 831     -14.640 -19.818 -21.976  1.00 36.42           C  
ANISOU 6790  CB  TYR A 831     4315   5920   3601    790     34    528       C  
ATOM   6791  CG  TYR A 831     -13.573 -20.713 -22.578  1.00 34.65           C  
ANISOU 6791  CG  TYR A 831     4120   5613   3431    762     51    573       C  
ATOM   6792  CD1 TYR A 831     -13.405 -20.795 -23.961  1.00 32.13           C  
ANISOU 6792  CD1 TYR A 831     3869   5134   3205    680     50    550       C  
ATOM   6793  CD2 TYR A 831     -12.760 -21.509 -21.761  1.00 35.46           C  
ANISOU 6793  CD2 TYR A 831     4179   5807   3488    823     66    641       C  
ATOM   6794  CE1 TYR A 831     -12.451 -21.614 -24.519  1.00 32.39           C  
ANISOU 6794  CE1 TYR A 831     3921   5102   3283    662     64    578       C  
ATOM   6795  CE2 TYR A 831     -11.790 -22.349 -22.311  1.00 36.71           C  
ANISOU 6795  CE2 TYR A 831     4359   5889   3699    810     78    676       C  
ATOM   6796  CZ  TYR A 831     -11.640 -22.394 -23.696  1.00 39.56           C  
ANISOU 6796  CZ  TYR A 831     4786   6092   4154    729     78    638       C  
ATOM   6797  OH  TYR A 831     -10.691 -23.216 -24.271  1.00 39.64           O  
ANISOU 6797  OH  TYR A 831     4812   6035   4214    722     89    658       O  
ATOM   6798  N   VAL A 832     -16.941 -17.676 -22.900  1.00 35.61           N  
ANISOU 6798  N   VAL A 832     4261   5723   3546    743    -22    374       N  
ATOM   6799  CA  VAL A 832     -18.219 -17.009 -22.637  1.00 34.78           C  
ANISOU 6799  CA  VAL A 832     4133   5663   3418    774    -36    340       C  
ATOM   6800  C   VAL A 832     -19.390 -17.946 -22.959  1.00 36.04           C  
ANISOU 6800  C   VAL A 832     4286   5805   3603    745      6    459       C  
ATOM   6801  O   VAL A 832     -19.439 -18.547 -24.043  1.00 36.23           O  
ANISOU 6801  O   VAL A 832     4362   5696   3706    671     20    510       O  
ATOM   6802  CB  VAL A 832     -18.373 -15.701 -23.476  1.00 35.50           C  
ANISOU 6802  CB  VAL A 832     4281   5640   3568    742    -90    222       C  
ATOM   6803  CG1 VAL A 832     -19.711 -15.041 -23.184  1.00 33.88           C  
ANISOU 6803  CG1 VAL A 832     4046   5484   3341    789   -108    184       C  
ATOM   6804  CG2 VAL A 832     -17.222 -14.712 -23.207  1.00 31.12           C  
ANISOU 6804  CG2 VAL A 832     3733   5085   3004    754   -136    101       C  
ATOM   6805  N   LEU A 833     -20.326 -18.071 -22.019  1.00 35.74           N  
ANISOU 6805  N   LEU A 833     4176   5908   3495    802     26    497       N  
ATOM   6806  CA  LEU A 833     -21.528 -18.877 -22.238  1.00 36.78           C  
ANISOU 6806  CA  LEU A 833     4287   6039   3647    770     64    605       C  
ATOM   6807  C   LEU A 833     -22.801 -18.100 -21.947  1.00 38.00           C  
ANISOU 6807  C   LEU A 833     4396   6279   3763    811     49    553       C  
ATOM   6808  O   LEU A 833     -22.867 -17.363 -20.963  1.00 41.90           O  
ANISOU 6808  O   LEU A 833     4835   6914   4172    894     31    478       O  
ATOM   6809  CB  LEU A 833     -21.506 -20.166 -21.399  1.00 34.84           C  
ANISOU 6809  CB  LEU A 833     3987   5891   3359    783    119    754       C  
ATOM   6810  CG  LEU A 833     -20.715 -21.365 -21.924  1.00 35.30           C  
ANISOU 6810  CG  LEU A 833     4091   5833   3489    728    146    852       C  
ATOM   6811  CD1 LEU A 833     -20.823 -22.531 -20.963  1.00 32.42           C  
ANISOU 6811  CD1 LEU A 833     3667   5569   3082    753    194   1008       C  
ATOM   6812  CD2 LEU A 833     -21.182 -21.786 -23.327  1.00 33.89           C  
ANISOU 6812  CD2 LEU A 833     3976   5476   3426    634    149    869       C  
ATOM   6813  N   PRO A 834     -23.823 -18.267 -22.802  1.00 40.06           N  
ANISOU 6813  N   PRO A 834     4675   6463   4083    758     54    583       N  
ATOM   6814  CA  PRO A 834     -25.138 -17.705 -22.489  1.00 40.53           C  
ANISOU 6814  CA  PRO A 834     4676   6622   4103    801     46    550       C  
ATOM   6815  C   PRO A 834     -25.811 -18.485 -21.376  1.00 43.05           C  
ANISOU 6815  C   PRO A 834     4895   7124   4338    833    100    656       C  
ATOM   6816  O   PRO A 834     -25.596 -19.701 -21.241  1.00 44.30           O  
ANISOU 6816  O   PRO A 834     5045   7279   4509    787    147    791       O  
ATOM   6817  CB  PRO A 834     -25.917 -17.876 -23.793  1.00 39.51           C  
ANISOU 6817  CB  PRO A 834     4591   6356   4063    723     40    571       C  
ATOM   6818  CG  PRO A 834     -25.219 -19.021 -24.510  1.00 38.16           C  
ANISOU 6818  CG  PRO A 834     4476   6060   3965    635     69    663       C  
ATOM   6819  CD  PRO A 834     -23.778 -18.885 -24.145  1.00 37.89           C  
ANISOU 6819  CD  PRO A 834     4472   6013   3913    660     60    629       C  
ATOM   6820  N   LEU A 835     -26.621 -17.780 -20.594  1.00 43.01           N  
ANISOU 6820  N   LEU A 835     4812   7280   4250    912     91    595       N  
ATOM   6821  CA  LEU A 835     -27.311 -18.354 -19.444  1.00 45.72           C  
ANISOU 6821  CA  LEU A 835     5044   7836   4490    951    141    686       C  
ATOM   6822  C   LEU A 835     -28.818 -18.168 -19.570  1.00 47.11           C  
ANISOU 6822  C   LEU A 835     5158   8087   4656    955    149    685       C  
ATOM   6823  O   LEU A 835     -29.290 -17.065 -19.890  1.00 47.20           O  
ANISOU 6823  O   LEU A 835     5176   8081   4677   1002    100    552       O  
ATOM   6824  CB  LEU A 835     -26.805 -17.695 -18.154  1.00 46.44           C  
ANISOU 6824  CB  LEU A 835     5074   8112   4459   1062    128    604       C  
ATOM   6825  CG  LEU A 835     -25.841 -18.421 -17.209  1.00 46.98           C  
ANISOU 6825  CG  LEU A 835     5113   8283   4454   1083    160    692       C  
ATOM   6826  CD1 LEU A 835     -24.948 -19.455 -17.890  1.00 44.34           C  
ANISOU 6826  CD1 LEU A 835     4858   7775   4213    997    180    805       C  
ATOM   6827  CD2 LEU A 835     -25.014 -17.408 -16.424  1.00 46.32           C  
ANISOU 6827  CD2 LEU A 835     5011   8298   4290   1180    116    541       C  
ATOM   6828  N   ARG A 836     -29.563 -19.249 -19.327  1.00 47.78           N  
ANISOU 6828  N   ARG A 836     5178   8248   4726    903    209    836       N  
ATOM   6829  CA  ARG A 836     -31.025 -19.233 -19.438  1.00 48.74           C  
ANISOU 6829  CA  ARG A 836     5226   8457   4837    893    224    853       C  
ATOM   6830  C   ARG A 836     -31.641 -18.331 -18.384  1.00 50.64           C  
ANISOU 6830  C   ARG A 836     5361   8930   4948   1013    216    758       C  
ATOM   6831  O   ARG A 836     -31.084 -18.175 -17.294  1.00 51.91           O  
ANISOU 6831  O   ARG A 836     5477   9240   5006   1087    224    743       O  
ATOM   6832  CB  ARG A 836     -31.606 -20.639 -19.309  1.00 49.04           C  
ANISOU 6832  CB  ARG A 836     5212   8534   4889    801    293   1045       C  
ATOM   6833  CG  ARG A 836     -31.279 -21.543 -20.472  1.00 49.29           C  
ANISOU 6833  CG  ARG A 836     5336   8332   5061    681    297   1121       C  
ATOM   6834  CD  ARG A 836     -32.245 -22.701 -20.583  1.00 49.80           C  
ANISOU 6834  CD  ARG A 836     5344   8414   5165    582    350   1274       C  
ATOM   6835  NE  ARG A 836     -32.455 -23.384 -19.312  1.00 51.67           N  
ANISOU 6835  NE  ARG A 836     5481   8843   5308    595    409   1415       N  
ATOM   6836  CZ  ARG A 836     -31.610 -24.259 -18.783  1.00 53.67           C  
ANISOU 6836  CZ  ARG A 836     5751   9079   5561    579    441   1539       C  
ATOM   6837  NH1 ARG A 836     -30.473 -24.556 -19.406  1.00 51.03           N  
ANISOU 6837  NH1 ARG A 836     5527   8545   5315    554    418   1528       N  
ATOM   6838  NH2 ARG A 836     -31.901 -24.831 -17.619  1.00 53.06           N  
ANISOU 6838  NH2 ARG A 836     5576   9195   5390    592    494   1679       N  
ATOM   6839  N   GLU A 837     -32.786 -17.741 -18.720  1.00 51.05           N  
ANISOU 6839  N   GLU A 837     5371   9022   5004   1037    196    689       N  
ATOM   6840  CA  GLU A 837     -33.511 -16.843 -17.828  1.00 54.80           C  
ANISOU 6840  CA  GLU A 837     5739   9716   5365   1159    183    580       C  
ATOM   6841  C   GLU A 837     -33.853 -17.502 -16.479  1.00 56.60           C  
ANISOU 6841  C   GLU A 837     5834  10219   5451   1187    252    687       C  
ATOM   6842  O   GLU A 837     -34.275 -18.662 -16.431  1.00 56.93           O  
ANISOU 6842  O   GLU A 837     5834  10299   5498   1096    315    864       O  
ATOM   6843  CB  GLU A 837     -34.777 -16.337 -18.525  1.00 55.94           C  
ANISOU 6843  CB  GLU A 837     5855   9852   5549   1167    157    518       C  
ATOM   6844  CG  GLU A 837     -35.456 -15.151 -17.836  1.00 64.48           C  
ANISOU 6844  CG  GLU A 837     6849  11112   6540   1313    122    357       C  
ATOM   6845  CD  GLU A 837     -36.202 -14.249 -18.812  1.00 66.89           C  
ANISOU 6845  CD  GLU A 837     7185  11304   6924   1344     58    242       C  
ATOM   6846  OE1 GLU A 837     -37.432 -14.091 -18.661  1.00 67.71           O  
ANISOU 6846  OE1 GLU A 837     7185  11558   6983   1386     66    223       O  
ATOM   6847  OE2 GLU A 837     -35.554 -13.698 -19.731  1.00 68.69           O  
ANISOU 6847  OE2 GLU A 837     7539  11301   7257   1326     -1    176       O  
ATOM   6848  N   GLY A 838     -33.651 -16.757 -15.393  1.00 56.91           N  
ANISOU 6848  N   GLY A 838     5807  10451   5367   1311    239    579       N  
ATOM   6849  CA  GLY A 838     -33.980 -17.234 -14.051  1.00 58.69           C  
ANISOU 6849  CA  GLY A 838     5894  10973   5432   1355    300    666       C  
ATOM   6850  C   GLY A 838     -32.889 -18.069 -13.406  1.00 59.38           C  
ANISOU 6850  C   GLY A 838     5998  11088   5476   1327    336    796       C  
ATOM   6851  O   GLY A 838     -33.128 -18.748 -12.404  1.00 62.26           O  
ANISOU 6851  O   GLY A 838     6258  11679   5721   1334    397    927       O  
ATOM   6852  N   ASN A 839     -31.690 -18.017 -13.982  1.00 56.87           N  
ANISOU 6852  N   ASN A 839     5808  10548   5252   1298    298    764       N  
ATOM   6853  CA  ASN A 839     -30.516 -18.692 -13.426  1.00 55.30           C  
ANISOU 6853  CA  ASN A 839     5633  10360   5019   1287    320    862       C  
ATOM   6854  C   ASN A 839     -30.041 -18.018 -12.131  1.00 54.20           C  
ANISOU 6854  C   ASN A 839     5415  10461   4718   1418    305    758       C  
ATOM   6855  O   ASN A 839     -30.338 -16.845 -11.908  1.00 55.55           O  
ANISOU 6855  O   ASN A 839     5554  10709   4845   1514    259    564       O  
ATOM   6856  CB  ASN A 839     -29.391 -18.734 -14.469  1.00 51.27           C  
ANISOU 6856  CB  ASN A 839     5273   9554   4653   1225    280    836       C  
ATOM   6857  CG  ASN A 839     -28.866 -17.357 -14.816  1.00 50.20           C  
ANISOU 6857  CG  ASN A 839     5200   9323   4549   1291    201    610       C  
ATOM   6858  OD1 ASN A 839     -27.945 -16.853 -14.172  1.00 50.21           O  
ANISOU 6858  OD1 ASN A 839     5200   9387   4489   1360    172    519       O  
ATOM   6859  ND2 ASN A 839     -29.448 -16.740 -15.839  1.00 44.41           N  
ANISOU 6859  ND2 ASN A 839     4520   8438   3916   1267    162    522       N  
ATOM   6860  N   PRO A 840     -29.302 -18.756 -11.279  1.00 54.51           N  
ANISOU 6860  N   PRO A 840     5422  10618   4671   1426    341    882       N  
ATOM   6861  CA  PRO A 840     -28.826 -18.238  -9.991  1.00 54.05           C  
ANISOU 6861  CA  PRO A 840     5277  10816   4443   1548    330    797       C  
ATOM   6862  C   PRO A 840     -27.700 -17.197 -10.078  1.00 54.18           C  
ANISOU 6862  C   PRO A 840     5365  10737   4484   1611    253    586       C  
ATOM   6863  O   PRO A 840     -27.374 -16.551  -9.072  1.00 54.05           O  
ANISOU 6863  O   PRO A 840     5275  10929   4334   1720    230    463       O  
ATOM   6864  CB  PRO A 840     -28.312 -19.497  -9.290  1.00 54.89           C  
ANISOU 6864  CB  PRO A 840     5349  11027   4480   1516    390   1027       C  
ATOM   6865  CG  PRO A 840     -27.928 -20.402 -10.389  1.00 51.76           C  
ANISOU 6865  CG  PRO A 840     5073  10335   4259   1390    400   1161       C  
ATOM   6866  CD  PRO A 840     -28.954 -20.180 -11.445  1.00 53.69           C  
ANISOU 6866  CD  PRO A 840     5352  10427   4622   1324    394   1120       C  
ATOM   6867  N   PHE A 841     -27.109 -17.036 -11.258  1.00 52.77           N  
ANISOU 6867  N   PHE A 841     5321  10257   4471   1541    213    542       N  
ATOM   6868  CA  PHE A 841     -26.019 -16.074 -11.441  1.00 52.46           C  
ANISOU 6868  CA  PHE A 841     5353  10106   4473   1579    141    355       C  
ATOM   6869  C   PHE A 841     -26.547 -14.643 -11.589  1.00 52.63           C  
ANISOU 6869  C   PHE A 841     5371  10116   4511   1651     77    122       C  
ATOM   6870  O   PHE A 841     -25.788 -13.672 -11.472  1.00 52.82           O  
ANISOU 6870  O   PHE A 841     5424  10099   4544   1703     13    -59       O  
ATOM   6871  CB  PHE A 841     -25.132 -16.477 -12.624  1.00 49.79           C  
ANISOU 6871  CB  PHE A 841     5152   9469   4296   1474    126    407       C  
ATOM   6872  CG  PHE A 841     -24.453 -17.807 -12.441  1.00 49.48           C  
ANISOU 6872  CG  PHE A 841     5122   9429   4250   1421    177    610       C  
ATOM   6873  CD1 PHE A 841     -23.307 -17.917 -11.660  1.00 51.32           C  
ANISOU 6873  CD1 PHE A 841     5334   9764   4403   1471    168    607       C  
ATOM   6874  CD2 PHE A 841     -24.970 -18.955 -13.031  1.00 49.48           C  
ANISOU 6874  CD2 PHE A 841     5147   9328   4327   1325    230    802       C  
ATOM   6875  CE1 PHE A 841     -22.678 -19.150 -11.477  1.00 51.42           C  
ANISOU 6875  CE1 PHE A 841     5354   9772   4412   1435    210    799       C  
ATOM   6876  CE2 PHE A 841     -24.347 -20.194 -12.858  1.00 50.36           C  
ANISOU 6876  CE2 PHE A 841     5269   9419   4445   1283    271    990       C  
ATOM   6877  CZ  PHE A 841     -23.198 -20.290 -12.081  1.00 49.70           C  
ANISOU 6877  CZ  PHE A 841     5168   9434   4281   1342    261    992       C  
ATOM   6878  N   GLY A 842     -27.851 -14.531 -11.826  1.00 52.15           N  
ANISOU 6878  N   GLY A 842     5268  10091   4456   1655     93    128       N  
ATOM   6879  CA  GLY A 842     -28.535 -13.241 -11.883  1.00 54.92           C  
ANISOU 6879  CA  GLY A 842     5598  10455   4814   1741     35    -80       C  
ATOM   6880  C   GLY A 842     -28.257 -12.386 -13.111  1.00 56.38           C  
ANISOU 6880  C   GLY A 842     5914  10339   5170   1704    -36   -201       C  
ATOM   6881  O   GLY A 842     -28.438 -11.166 -13.054  1.00 58.34           O  
ANISOU 6881  O   GLY A 842     6162  10571   5433   1787   -101   -399       O  
ATOM   6882  N   ASP A 843     -27.817 -13.015 -14.210  1.00 53.94           N  
ANISOU 6882  N   ASP A 843     5713   9793   4987   1582    -25    -82       N  
ATOM   6883  CA  ASP A 843     -27.613 -12.329 -15.501  1.00 53.23           C  
ANISOU 6883  CA  ASP A 843     5747   9421   5056   1531    -84   -160       C  
ATOM   6884  C   ASP A 843     -27.665 -13.282 -16.705  1.00 52.48           C  
ANISOU 6884  C   ASP A 843     5733   9134   5072   1398    -50      4       C  
ATOM   6885  O   ASP A 843     -27.831 -14.491 -16.542  1.00 51.85           O  
ANISOU 6885  O   ASP A 843     5619   9119   4961   1343     17    176       O  
ATOM   6886  CB  ASP A 843     -26.304 -11.533 -15.512  1.00 54.21           C  
ANISOU 6886  CB  ASP A 843     5942   9435   5223   1543   -145   -295       C  
ATOM   6887  CG  ASP A 843     -26.443 -10.193 -16.222  1.00 56.25           C  
ANISOU 6887  CG  ASP A 843     6269   9515   5588   1567   -227   -464       C  
ATOM   6888  OD1 ASP A 843     -27.111 -10.123 -17.277  1.00 53.45           O  
ANISOU 6888  OD1 ASP A 843     5971   9009   5330   1519   -237   -427       O  
ATOM   6889  OD2 ASP A 843     -25.877  -9.202 -15.718  1.00 61.73           O  
ANISOU 6889  OD2 ASP A 843     6961  10220   6273   1634   -285   -634       O  
ATOM   6890  N   LYS A 844     -27.514 -12.737 -17.911  1.00 52.24           N  
ANISOU 6890  N   LYS A 844     5809   8867   5173   1347    -98    -48       N  
ATOM   6891  CA  LYS A 844     -27.728 -13.520 -19.131  1.00 52.01           C  
ANISOU 6891  CA  LYS A 844     5849   8667   5244   1231    -73     81       C  
ATOM   6892  C   LYS A 844     -26.505 -14.293 -19.640  1.00 50.39           C  
ANISOU 6892  C   LYS A 844     5723   8325   5096   1138    -54    170       C  
ATOM   6893  O   LYS A 844     -26.622 -15.091 -20.578  1.00 48.60           O  
ANISOU 6893  O   LYS A 844     5546   7974   4945   1043    -28    278       O  
ATOM   6894  CB  LYS A 844     -28.329 -12.657 -20.247  1.00 52.96           C  
ANISOU 6894  CB  LYS A 844     6033   8624   5465   1221   -129      3       C  
ATOM   6895  CG  LYS A 844     -27.384 -11.622 -20.849  1.00 56.27           C  
ANISOU 6895  CG  LYS A 844     6554   8859   5969   1215   -199   -115       C  
ATOM   6896  CD  LYS A 844     -28.086 -10.826 -21.942  1.00 55.32           C  
ANISOU 6896  CD  LYS A 844     6490   8586   5941   1208   -253   -166       C  
ATOM   6897  CE  LYS A 844     -27.411  -9.484 -22.173  1.00 54.95           C  
ANISOU 6897  CE  LYS A 844     6515   8404   5961   1240   -333   -310       C  
ATOM   6898  NZ  LYS A 844     -27.975  -8.784 -23.366  1.00 52.74           N  
ANISOU 6898  NZ  LYS A 844     6306   7953   5781   1222   -386   -329       N  
ATOM   6899  N   CYS A 845     -25.342 -14.050 -19.033  1.00 48.94           N  
ANISOU 6899  N   CYS A 845     5547   8172   4876   1169    -69    114       N  
ATOM   6900  CA  CYS A 845     -24.114 -14.719 -19.451  1.00 47.07           C  
ANISOU 6900  CA  CYS A 845     5376   7822   4687   1095    -55    183       C  
ATOM   6901  C   CYS A 845     -23.054 -14.739 -18.373  1.00 47.84           C  
ANISOU 6901  C   CYS A 845     5433   8045   4698   1149    -54    154       C  
ATOM   6902  O   CYS A 845     -23.120 -13.981 -17.406  1.00 50.27           O  
ANISOU 6902  O   CYS A 845     5677   8502   4921   1242    -80     42       O  
ATOM   6903  CB  CYS A 845     -23.532 -14.071 -20.707  1.00 46.40           C  
ANISOU 6903  CB  CYS A 845     5401   7509   4721   1031   -104    115       C  
ATOM   6904  SG  CYS A 845     -22.994 -12.376 -20.455  1.00 46.45           S  
ANISOU 6904  SG  CYS A 845     5429   7483   4737   1096   -188    -94       S  
ATOM   6905  N   ILE A 846     -22.066 -15.609 -18.573  1.00 45.61           N  
ANISOU 6905  N   ILE A 846     5186   7705   4440   1095    -28    247       N  
ATOM   6906  CA  ILE A 846     -20.972 -15.798 -17.641  1.00 42.05           C  
ANISOU 6906  CA  ILE A 846     4697   7369   3910   1139    -25    242       C  
ATOM   6907  C   ILE A 846     -19.684 -16.071 -18.418  1.00 40.54           C  
ANISOU 6907  C   ILE A 846     4586   7016   3800   1070    -34    253       C  
ATOM   6908  O   ILE A 846     -19.694 -16.780 -19.418  1.00 39.34           O  
ANISOU 6908  O   ILE A 846     4494   6715   3736    989    -11    344       O  
ATOM   6909  CB  ILE A 846     -21.294 -16.917 -16.594  1.00 42.87           C  
ANISOU 6909  CB  ILE A 846     4713   7669   3908   1176     37    394       C  
ATOM   6910  CG1 ILE A 846     -20.390 -16.786 -15.359  1.00 42.80           C  
ANISOU 6910  CG1 ILE A 846     4638   7846   3779   1259     28    353       C  
ATOM   6911  CG2 ILE A 846     -21.264 -18.321 -17.221  1.00 37.65           C  
ANISOU 6911  CG2 ILE A 846     4090   6898   3317   1092     89    580       C  
ATOM   6912  CD1 ILE A 846     -20.718 -17.747 -14.248  1.00 44.49           C  
ANISOU 6912  CD1 ILE A 846     4757   8276   3872   1306     84    503       C  
ATOM   6913  N   ALA A 847     -18.587 -15.474 -17.969  1.00 41.01           N  
ANISOU 6913  N   ALA A 847     4640   7114   3829   1102    -71    149       N  
ATOM   6914  CA  ALA A 847     -17.290 -15.662 -18.604  1.00 41.04           C  
ANISOU 6914  CA  ALA A 847     4702   6995   3895   1043    -81    147       C  
ATOM   6915  C   ALA A 847     -16.257 -16.090 -17.577  1.00 41.91           C  
ANISOU 6915  C   ALA A 847     4752   7257   3914   1098    -73    164       C  
ATOM   6916  O   ALA A 847     -16.274 -15.608 -16.450  1.00 40.09           O  
ANISOU 6916  O   ALA A 847     4447   7206   3579   1181    -90     92       O  
ATOM   6917  CB  ALA A 847     -16.842 -14.378 -19.299  1.00 40.60           C  
ANISOU 6917  CB  ALA A 847     4707   6805   3915   1007   -143     -8       C  
ATOM   6918  N   TRP A 848     -15.362 -16.992 -17.973  1.00 40.77           N  
ANISOU 6918  N   TRP A 848     4636   7048   3806   1058    -49    254       N  
ATOM   6919  CA  TRP A 848     -14.244 -17.386 -17.118  1.00 41.61           C  
ANISOU 6919  CA  TRP A 848     4689   7284   3834   1110    -48    269       C  
ATOM   6920  C   TRP A 848     -12.932 -17.496 -17.912  1.00 42.24           C  
ANISOU 6920  C   TRP A 848     4822   7241   3989   1053    -62    244       C  
ATOM   6921  O   TRP A 848     -12.970 -17.583 -19.140  1.00 41.01           O  
ANISOU 6921  O   TRP A 848     4741   6901   3939    970    -57    256       O  
ATOM   6922  CB  TRP A 848     -14.565 -18.688 -16.391  1.00 42.21           C  
ANISOU 6922  CB  TRP A 848     4714   7478   3845   1154      6    450       C  
ATOM   6923  CG  TRP A 848     -14.581 -19.903 -17.260  1.00 38.85           C  
ANISOU 6923  CG  TRP A 848     4346   6900   3516   1090     47    599       C  
ATOM   6924  CD1 TRP A 848     -13.604 -20.855 -17.352  1.00 37.19           C  
ANISOU 6924  CD1 TRP A 848     4146   6657   3328   1091     63    686       C  
ATOM   6925  CD2 TRP A 848     -15.632 -20.318 -18.139  1.00 35.91           C  
ANISOU 6925  CD2 TRP A 848     4023   6389   3231   1023     74    671       C  
ATOM   6926  NE1 TRP A 848     -13.980 -21.837 -18.236  1.00 35.44           N  
ANISOU 6926  NE1 TRP A 848     3980   6276   3209   1028     97    800       N  
ATOM   6927  CE2 TRP A 848     -15.218 -21.529 -18.741  1.00 35.36           C  
ANISOU 6927  CE2 TRP A 848     3994   6202   3240    981    105    792       C  
ATOM   6928  CE3 TRP A 848     -16.879 -19.780 -18.488  1.00 38.15           C  
ANISOU 6928  CE3 TRP A 848     4317   6640   3537    997     72    637       C  
ATOM   6929  CZ2 TRP A 848     -16.013 -22.218 -19.664  1.00 32.44           C  
ANISOU 6929  CZ2 TRP A 848     3673   5683   2968    908    133    874       C  
ATOM   6930  CZ3 TRP A 848     -17.666 -20.462 -19.414  1.00 34.01           C  
ANISOU 6930  CZ3 TRP A 848     3839   5978   3106    924    101    726       C  
ATOM   6931  CH2 TRP A 848     -17.228 -21.671 -19.987  1.00 34.07           C  
ANISOU 6931  CH2 TRP A 848     3885   5870   3188    877    130    840       C  
ATOM   6932  N   PRO A 849     -11.769 -17.474 -17.218  1.00 44.19           N  
ANISOU 6932  N   PRO A 849     5019   7601   4171   1097    -80    203       N  
ATOM   6933  CA  PRO A 849     -10.488 -17.546 -17.922  1.00 43.87           C  
ANISOU 6933  CA  PRO A 849     5012   7466   4191   1046    -93    170       C  
ATOM   6934  C   PRO A 849     -10.430 -18.708 -18.898  1.00 44.59           C  
ANISOU 6934  C   PRO A 849     5160   7413   4368    994    -50    302       C  
ATOM   6935  O   PRO A 849     -10.834 -19.827 -18.565  1.00 44.27           O  
ANISOU 6935  O   PRO A 849     5104   7406   4310   1029    -10    448       O  
ATOM   6936  CB  PRO A 849      -9.482 -17.740 -16.790  1.00 46.16           C  
ANISOU 6936  CB  PRO A 849     5218   7946   4374   1127   -105    157       C  
ATOM   6937  CG  PRO A 849     -10.096 -16.997 -15.646  1.00 47.19           C  
ANISOU 6937  CG  PRO A 849     5282   8249   4398   1200   -128     79       C  
ATOM   6938  CD  PRO A 849     -11.580 -17.243 -15.771  1.00 44.57           C  
ANISOU 6938  CD  PRO A 849     4971   7884   4080   1197    -95    163       C  
ATOM   6939  N   SER A 850      -9.945 -18.426 -20.104  1.00 43.85           N  
ANISOU 6939  N   SER A 850     5130   7162   4369    910    -61    250       N  
ATOM   6940  CA  SER A 850      -9.863 -19.427 -21.160  1.00 45.29           C  
ANISOU 6940  CA  SER A 850     5367   7203   4637    857    -26    345       C  
ATOM   6941  C   SER A 850      -8.758 -20.451 -20.907  1.00 47.50           C  
ANISOU 6941  C   SER A 850     5616   7530   4902    900     -9    411       C  
ATOM   6942  O   SER A 850      -7.816 -20.196 -20.148  1.00 47.06           O  
ANISOU 6942  O   SER A 850     5502   7601   4777    950    -31    360       O  
ATOM   6943  CB  SER A 850      -9.654 -18.755 -22.515  1.00 43.59           C  
ANISOU 6943  CB  SER A 850     5220   6831   4511    757    -44    264       C  
ATOM   6944  OG  SER A 850      -8.332 -18.266 -22.650  1.00 39.98           O  
ANISOU 6944  OG  SER A 850     4747   6394   4050    737    -69    174       O  
ATOM   6945  N   GLY A 851      -8.897 -21.608 -21.550  1.00 51.68           N  
ANISOU 6945  N   GLY A 851     6181   7954   5499    882     26    519       N  
ATOM   6946  CA  GLY A 851      -7.923 -22.699 -21.467  1.00 55.80           C  
ANISOU 6946  CA  GLY A 851     6685   8487   6030    926     42    589       C  
ATOM   6947  C   GLY A 851      -8.117 -23.567 -20.246  1.00 59.92           C  
ANISOU 6947  C   GLY A 851     7152   9127   6485   1021     60    720       C  
ATOM   6948  O   GLY A 851      -7.518 -24.637 -20.135  1.00 62.83           O  
ANISOU 6948  O   GLY A 851     7511   9488   6873   1068     74    811       O  
ATOM   6949  N   THR A 852      -8.958 -23.101 -19.327  1.00 61.69           N  
ANISOU 6949  N   THR A 852     7340   9468   6631   1053     57    732       N  
ATOM   6950  CA  THR A 852      -9.182 -23.792 -18.062  1.00 63.32           C  
ANISOU 6950  CA  THR A 852     7485   9825   6751   1143     74    860       C  
ATOM   6951  C   THR A 852     -10.622 -24.265 -17.938  1.00 63.64           C  
ANISOU 6951  C   THR A 852     7536   9837   6806   1124    109    978       C  
ATOM   6952  O   THR A 852     -11.547 -23.683 -18.528  1.00 61.47           O  
ANISOU 6952  O   THR A 852     7298   9487   6572   1060    110    924       O  
ATOM   6953  CB  THR A 852      -8.885 -22.893 -16.838  1.00 61.88           C  
ANISOU 6953  CB  THR A 852     7220   9863   6428   1213     43    777       C  
ATOM   6954  OG1 THR A 852      -9.837 -21.830 -16.807  1.00 61.21           O  
ANISOU 6954  OG1 THR A 852     7140   9795   6323   1182     31    683       O  
ATOM   6955  CG2 THR A 852      -7.468 -22.312 -16.894  1.00 62.41           C  
ANISOU 6955  CG2 THR A 852     7265   9974   6476   1223      4    646       C  
ATOM   6956  N   GLU A 853     -10.783 -25.341 -17.173  1.00 64.43           N  
ANISOU 6956  N   GLU A 853     7601  10003   6875   1181    137   1147       N  
ATOM   6957  CA  GLU A 853     -12.062 -25.710 -16.605  1.00 63.00           C  
ANISOU 6957  CA  GLU A 853     7396   9878   6663   1182    170   1270       C  
ATOM   6958  C   GLU A 853     -12.447 -24.588 -15.637  1.00 60.83           C  
ANISOU 6958  C   GLU A 853     7052   9812   6250   1228    153   1180       C  
ATOM   6959  O   GLU A 853     -11.590 -24.012 -14.948  1.00 56.88           O  
ANISOU 6959  O   GLU A 853     6501   9457   5654   1293    121   1094       O  
ATOM   6960  CB  GLU A 853     -11.944 -27.044 -15.851  1.00 66.09           C  
ANISOU 6960  CB  GLU A 853     7755  10317   7038   1239    199   1478       C  
ATOM   6961  CG  GLU A 853     -11.548 -28.255 -16.717  1.00 68.90           C  
ANISOU 6961  CG  GLU A 853     8176  10461   7540   1208    212   1569       C  
ATOM   6962  CD  GLU A 853     -12.732 -28.911 -17.441  1.00 71.02           C  
ANISOU 6962  CD  GLU A 853     8496  10562   7926   1119    245   1656       C  
ATOM   6963  OE1 GLU A 853     -13.890 -28.771 -16.989  1.00 69.38           O  
ANISOU 6963  OE1 GLU A 853     8257  10429   7674   1097    268   1715       O  
ATOM   6964  OE2 GLU A 853     -12.499 -29.586 -18.466  1.00 73.51           O  
ANISOU 6964  OE2 GLU A 853     8877  10677   8378   1073    247   1659       O  
ATOM   6965  N   ILE A 854     -13.733 -24.264 -15.613  1.00 60.47           N  
ANISOU 6965  N   ILE A 854     7000   9782   6194   1197    169   1186       N  
ATOM   6966  CA  ILE A 854     -14.263 -23.297 -14.668  1.00 62.29           C  
ANISOU 6966  CA  ILE A 854     7158  10214   6294   1249    156   1105       C  
ATOM   6967  C   ILE A 854     -14.182 -23.913 -13.267  1.00 62.94           C  
ANISOU 6967  C   ILE A 854     7150  10526   6241   1340    177   1242       C  
ATOM   6968  O   ILE A 854     -14.356 -25.125 -13.113  1.00 63.20           O  
ANISOU 6968  O   ILE A 854     7181  10532   6299   1337    216   1437       O  
ATOM   6969  CB  ILE A 854     -15.710 -22.857 -15.069  1.00 63.16           C  
ANISOU 6969  CB  ILE A 854     7280  10281   6435   1196    170   1081       C  
ATOM   6970  CG1 ILE A 854     -16.224 -21.725 -14.169  1.00 65.11           C  
ANISOU 6970  CG1 ILE A 854     7454  10730   6555   1260    149    962       C  
ATOM   6971  CG2 ILE A 854     -16.673 -24.054 -15.114  1.00 64.95           C  
ANISOU 6971  CG2 ILE A 854     7507  10467   6706   1157    224   1282       C  
ATOM   6972  CD1 ILE A 854     -17.357 -20.924 -14.785  1.00 64.55           C  
ANISOU 6972  CD1 ILE A 854     7409  10587   6532   1215    140    868       C  
ATOM   6973  N   THR A 855     -13.873 -23.089 -12.266  1.00 62.74           N  
ANISOU 6973  N   THR A 855     7047  10719   6073   1420    149   1138       N  
ATOM   6974  CA  THR A 855     -13.793 -23.551 -10.873  1.00 64.64           C  
ANISOU 6974  CA  THR A 855     7189  11216   6156   1514    166   1256       C  
ATOM   6975  C   THR A 855     -14.983 -24.422 -10.473  1.00 65.09           C  
ANISOU 6975  C   THR A 855     7213  11328   6189   1502    224   1461       C  
ATOM   6976  O   THR A 855     -16.130 -24.106 -10.802  1.00 62.93           O  
ANISOU 6976  O   THR A 855     6947  11018   5945   1452    242   1438       O  
ATOM   6977  CB  THR A 855     -13.631 -22.378  -9.870  1.00 65.28           C  
ANISOU 6977  CB  THR A 855     7182  11543   6079   1596    127   1085       C  
ATOM   6978  OG1 THR A 855     -13.659 -22.886  -8.530  1.00 65.82           O  
ANISOU 6978  OG1 THR A 855     7147  11880   5981   1688    148   1214       O  
ATOM   6979  CG2 THR A 855     -14.730 -21.332 -10.042  1.00 63.98           C  
ANISOU 6979  CG2 THR A 855     7014  11385   5912   1573    119    945       C  
ATOM   6980  N   ASP A 856     -14.696 -25.519  -9.770  1.00 68.56           N  
ANISOU 6980  N   ASP A 856     7614  11855   6578   1546    251   1665       N  
ATOM   6981  CA  ASP A 856     -15.718 -26.500  -9.361  1.00 72.18           C  
ANISOU 6981  CA  ASP A 856     8042  12359   7024   1525    309   1896       C  
ATOM   6982  C   ASP A 856     -16.892 -25.894  -8.583  1.00 73.16           C  
ANISOU 6982  C   ASP A 856     8075  12710   7012   1546    331   1875       C  
ATOM   6983  O   ASP A 856     -17.983 -26.476  -8.539  1.00 72.54           O  
ANISOU 6983  O   ASP A 856     7978  12634   6949   1496    380   2024       O  
ATOM   6984  CB  ASP A 856     -15.087 -27.657  -8.568  1.00 75.45           C  
ANISOU 6984  CB  ASP A 856     8421  12862   7387   1586    326   2118       C  
ATOM   6985  CG  ASP A 856     -14.565 -28.780  -9.469  1.00 78.50           C  
ANISOU 6985  CG  ASP A 856     8902  12969   7956   1536    331   2236       C  
ATOM   6986  OD1 ASP A 856     -13.487 -29.340  -9.166  1.00 81.02           O  
ANISOU 6986  OD1 ASP A 856     9220  13301   8265   1601    313   2306       O  
ATOM   6987  OD2 ASP A 856     -15.233 -29.107 -10.476  1.00 79.72           O  
ANISOU 6987  OD2 ASP A 856     9129  12897   8263   1436    350   2253       O  
ATOM   6988  N   LEU A 857     -16.657 -24.721  -7.995  1.00 73.71           N  
ANISOU 6988  N   LEU A 857     8086  12968   6954   1618    293   1680       N  
ATOM   6989  CA  LEU A 857     -17.675 -23.969  -7.252  1.00 76.09           C  
ANISOU 6989  CA  LEU A 857     8294  13499   7117   1657    304   1610       C  
ATOM   6990  C   LEU A 857     -18.974 -23.716  -8.032  1.00 74.75           C  
ANISOU 6990  C   LEU A 857     8158  13201   7042   1574    327   1579       C  
ATOM   6991  O   LEU A 857     -20.074 -23.846  -7.481  1.00 76.05           O  
ANISOU 6991  O   LEU A 857     8246  13526   7124   1578    368   1663       O  
ATOM   6992  CB  LEU A 857     -17.094 -22.628  -6.775  1.00 77.53           C  
ANISOU 6992  CB  LEU A 857     8433  13831   7194   1738    245   1351       C  
ATOM   6993  CG  LEU A 857     -16.226 -22.619  -5.510  1.00 80.22           C  
ANISOU 6993  CG  LEU A 857     8677  14452   7352   1851    226   1356       C  
ATOM   6994  CD1 LEU A 857     -15.469 -21.299  -5.376  1.00 79.43           C  
ANISOU 6994  CD1 LEU A 857     8563  14409   7209   1903    155   1070       C  
ATOM   6995  CD2 LEU A 857     -17.069 -22.897  -4.262  1.00 82.20           C  
ANISOU 6995  CD2 LEU A 857     8800  15023   7410   1917    270   1483       C  
ATOM   6996  N   ILE A 858     -18.834 -23.364  -9.309  1.00 70.42           N  
ANISOU 6996  N   ILE A 858     7717  12379   6662   1500    299   1464       N  
ATOM   6997  CA  ILE A 858     -19.961 -22.904 -10.118  1.00 66.94           C  
ANISOU 6997  CA  ILE A 858     7309  11818   6307   1432    305   1392       C  
ATOM   6998  C   ILE A 858     -20.158 -23.698 -11.418  1.00 62.82           C  
ANISOU 6998  C   ILE A 858     6892  10999   5978   1316    323   1486       C  
ATOM   6999  O   ILE A 858     -21.092 -23.431 -12.177  1.00 60.07           O  
ANISOU 6999  O   ILE A 858     6573  10541   5709   1253    328   1443       O  
ATOM   7000  CB  ILE A 858     -19.844 -21.384 -10.417  1.00 66.78           C  
ANISOU 7000  CB  ILE A 858     7307  11780   6287   1461    244   1118       C  
ATOM   7001  CG1 ILE A 858     -18.494 -21.063 -11.070  1.00 63.53           C  
ANISOU 7001  CG1 ILE A 858     6979  11198   5963   1447    195   1006       C  
ATOM   7002  CG2 ILE A 858     -20.070 -20.570  -9.125  1.00 68.37           C  
ANISOU 7002  CG2 ILE A 858     7389  12290   6298   1573    231   1011       C  
ATOM   7003  CD1 ILE A 858     -18.322 -19.622 -11.468  1.00 64.53           C  
ANISOU 7003  CD1 ILE A 858     7135  11267   6118   1456    133    755       C  
ATOM   7004  N   LYS A 859     -19.286 -24.676 -11.651  1.00 60.70           N  
ANISOU 7004  N   LYS A 859     6672  10610   5779   1296    331   1609       N  
ATOM   7005  CA  LYS A 859     -19.338 -25.518 -12.849  1.00 59.24           C  
ANISOU 7005  CA  LYS A 859     6584  10148   5777   1195    344   1691       C  
ATOM   7006  C   LYS A 859     -20.699 -26.187 -13.035  1.00 59.04           C  
ANISOU 7006  C   LYS A 859     6542  10092   5800   1120    393   1832       C  
ATOM   7007  O   LYS A 859     -21.329 -26.028 -14.083  1.00 58.97           O  
ANISOU 7007  O   LYS A 859     6587   9914   5904   1040    390   1772       O  
ATOM   7008  CB  LYS A 859     -18.212 -26.567 -12.831  1.00 59.26           C  
ANISOU 7008  CB  LYS A 859     6622  10066   5830   1208    347   1816       C  
ATOM   7009  CG  LYS A 859     -18.164 -27.463 -14.065  1.00 57.13           C  
ANISOU 7009  CG  LYS A 859     6449   9506   5750   1115    356   1880       C  
ATOM   7010  CD  LYS A 859     -17.022 -28.459 -13.996  1.00 58.85           C  
ANISOU 7010  CD  LYS A 859     6696   9647   6015   1146    353   1990       C  
ATOM   7011  CE  LYS A 859     -17.066 -29.407 -15.187  1.00 60.87           C  
ANISOU 7011  CE  LYS A 859     7042   9622   6462   1058    363   2048       C  
ATOM   7012  NZ  LYS A 859     -15.769 -30.106 -15.413  1.00 58.68           N  
ANISOU 7012  NZ  LYS A 859     6808   9236   6250   1097    344   2079       N  
ATOM   7013  N   ASP A 860     -21.143 -26.921 -12.016  1.00 59.55           N  
ANISOU 7013  N   ASP A 860     6525  10328   5774   1142    438   2021       N  
ATOM   7014  CA  ASP A 860     -22.410 -27.655 -12.057  1.00 61.00           C  
ANISOU 7014  CA  ASP A 860     6676  10505   5996   1063    490   2181       C  
ATOM   7015  C   ASP A 860     -23.586 -26.750 -12.390  1.00 59.45           C  
ANISOU 7015  C   ASP A 860     6451  10354   5784   1036    489   2050       C  
ATOM   7016  O   ASP A 860     -24.496 -27.150 -13.122  1.00 58.65           O  
ANISOU 7016  O   ASP A 860     6370  10125   5788    941    510   2099       O  
ATOM   7017  CB  ASP A 860     -22.668 -28.368 -10.722  1.00 65.08           C  
ANISOU 7017  CB  ASP A 860     7090  11258   6380   1105    537   2396       C  
ATOM   7018  CG  ASP A 860     -21.778 -29.586 -10.521  1.00 69.90           C  
ANISOU 7018  CG  ASP A 860     7736  11778   7045   1109    546   2588       C  
ATOM   7019  OD1 ASP A 860     -21.132 -30.034 -11.497  1.00 72.96           O  
ANISOU 7019  OD1 ASP A 860     8227  11902   7594   1066    524   2568       O  
ATOM   7020  OD2 ASP A 860     -21.729 -30.100  -9.381  1.00 75.85           O  
ANISOU 7020  OD2 ASP A 860     8410  12731   7677   1161    575   2763       O  
ATOM   7021  N   ASP A 861     -23.559 -25.534 -11.851  1.00 58.58           N  
ANISOU 7021  N   ASP A 861     6289  10424   5546   1123    460   1878       N  
ATOM   7022  CA  ASP A 861     -24.616 -24.561 -12.104  1.00 59.03           C  
ANISOU 7022  CA  ASP A 861     6314  10533   5582   1120    450   1735       C  
ATOM   7023  C   ASP A 861     -24.515 -23.957 -13.495  1.00 56.44           C  
ANISOU 7023  C   ASP A 861     6093   9949   5401   1066    405   1574       C  
ATOM   7024  O   ASP A 861     -25.528 -23.624 -14.093  1.00 57.05           O  
ANISOU 7024  O   ASP A 861     6170   9978   5526   1022    405   1524       O  
ATOM   7025  CB  ASP A 861     -24.625 -23.467 -11.039  1.00 59.69           C  
ANISOU 7025  CB  ASP A 861     6305  10890   5486   1240    430   1596       C  
ATOM   7026  CG  ASP A 861     -25.290 -23.919  -9.749  1.00 65.51           C  
ANISOU 7026  CG  ASP A 861     6907  11924   6058   1282    484   1747       C  
ATOM   7027  OD1 ASP A 861     -24.818 -23.522  -8.658  1.00 67.04           O  
ANISOU 7027  OD1 ASP A 861     7026  12356   6091   1386    475   1705       O  
ATOM   7028  OD2 ASP A 861     -26.288 -24.672  -9.828  1.00 65.38           O  
ANISOU 7028  OD2 ASP A 861     6855  11915   6071   1208    536   1907       O  
ATOM   7029  N   VAL A 862     -23.295 -23.827 -14.008  1.00 55.27           N  
ANISOU 7029  N   VAL A 862     6032   9650   5320   1071    366   1499       N  
ATOM   7030  CA  VAL A 862     -23.099 -23.324 -15.365  1.00 52.80           C  
ANISOU 7030  CA  VAL A 862     5822   9097   5143   1013    326   1365       C  
ATOM   7031  C   VAL A 862     -23.627 -24.340 -16.374  1.00 51.92           C  
ANISOU 7031  C   VAL A 862     5766   8786   5177    900    354   1483       C  
ATOM   7032  O   VAL A 862     -24.359 -23.975 -17.292  1.00 50.59           O  
ANISOU 7032  O   VAL A 862     5630   8510   5083    845    341   1412       O  
ATOM   7033  CB  VAL A 862     -21.616 -22.953 -15.651  1.00 52.24           C  
ANISOU 7033  CB  VAL A 862     5818   8930   5100   1040    281   1260       C  
ATOM   7034  CG1 VAL A 862     -21.375 -22.760 -17.152  1.00 50.27           C  
ANISOU 7034  CG1 VAL A 862     5677   8421   5001    960    253   1176       C  
ATOM   7035  CG2 VAL A 862     -21.231 -21.682 -14.892  1.00 49.69           C  
ANISOU 7035  CG2 VAL A 862     5450   8772   4660   1135    239   1090       C  
ATOM   7036  N   LEU A 863     -23.286 -25.612 -16.171  1.00 52.87           N  
ANISOU 7036  N   LEU A 863     5891   8863   5334    871    389   1662       N  
ATOM   7037  CA  LEU A 863     -23.672 -26.688 -17.095  1.00 54.24           C  
ANISOU 7037  CA  LEU A 863     6118   8832   5657    764    412   1771       C  
ATOM   7038  C   LEU A 863     -25.172 -26.919 -17.133  1.00 54.16           C  
ANISOU 7038  C   LEU A 863     6052   8870   5657    700    446   1842       C  
ATOM   7039  O   LEU A 863     -25.718 -27.338 -18.159  1.00 53.85           O  
ANISOU 7039  O   LEU A 863     6057   8660   5742    607    448   1850       O  
ATOM   7040  CB  LEU A 863     -22.975 -28.011 -16.738  1.00 56.35           C  
ANISOU 7040  CB  LEU A 863     6398   9045   5967    758    438   1953       C  
ATOM   7041  CG  LEU A 863     -21.448 -28.118 -16.704  1.00 56.54           C  
ANISOU 7041  CG  LEU A 863     6472   9014   5998    816    410   1922       C  
ATOM   7042  CD1 LEU A 863     -21.025 -29.580 -16.842  1.00 59.57           C  
ANISOU 7042  CD1 LEU A 863     6892   9252   6490    782    432   2096       C  
ATOM   7043  CD2 LEU A 863     -20.805 -27.282 -17.782  1.00 53.49           C  
ANISOU 7043  CD2 LEU A 863     6165   8487   5674    805    363   1723       C  
ATOM   7044  N   HIS A 864     -25.823 -26.654 -16.005  1.00 54.18           N  
ANISOU 7044  N   HIS A 864     5948   9118   5519    753    473   1889       N  
ATOM   7045  CA  HIS A 864     -27.261 -26.832 -15.867  1.00 56.07           C  
ANISOU 7045  CA  HIS A 864     6110   9453   5742    701    510   1961       C  
ATOM   7046  C   HIS A 864     -28.027 -25.639 -16.443  1.00 54.46           C  
ANISOU 7046  C   HIS A 864     5901   9263   5529    712    477   1774       C  
ATOM   7047  O   HIS A 864     -29.168 -25.785 -16.899  1.00 52.81           O  
ANISOU 7047  O   HIS A 864     5662   9039   5365    644    493   1796       O  
ATOM   7048  CB  HIS A 864     -27.620 -27.040 -14.391  1.00 59.22           C  
ANISOU 7048  CB  HIS A 864     6386  10135   5980    758    555   2091       C  
ATOM   7049  CG  HIS A 864     -29.051 -27.412 -14.159  1.00 65.15           C  
ANISOU 7049  CG  HIS A 864     7044  11000   6710    695    603   2201       C  
ATOM   7050  ND1 HIS A 864     -30.025 -26.480 -13.868  1.00 66.47           N  
ANISOU 7050  ND1 HIS A 864     7125  11355   6776    737    604   2094       N  
ATOM   7051  CD2 HIS A 864     -29.672 -28.615 -14.172  1.00 68.71           C  
ANISOU 7051  CD2 HIS A 864     7470  11405   7233    591    653   2405       C  
ATOM   7052  CE1 HIS A 864     -31.184 -27.093 -13.714  1.00 70.04           C  
ANISOU 7052  CE1 HIS A 864     7496  11887   7229    661    654   2229       C  
ATOM   7053  NE2 HIS A 864     -30.998 -28.388 -13.894  1.00 71.63           N  
ANISOU 7053  NE2 HIS A 864     7734  11945   7537    565    684   2422       N  
ATOM   7054  N   TRP A 865     -27.396 -24.466 -16.424  1.00 51.44           N  
ANISOU 7054  N   TRP A 865     5545   8906   5095    796    428   1593       N  
ATOM   7055  CA  TRP A 865     -28.057 -23.241 -16.872  1.00 50.89           C  
ANISOU 7055  CA  TRP A 865     5470   8851   5013    825    389   1414       C  
ATOM   7056  C   TRP A 865     -27.578 -22.691 -18.228  1.00 49.49           C  
ANISOU 7056  C   TRP A 865     5410   8433   4959    788    335   1278       C  
ATOM   7057  O   TRP A 865     -28.093 -21.674 -18.702  1.00 49.53           O  
ANISOU 7057  O   TRP A 865     5424   8425   4971    810    297   1139       O  
ATOM   7058  CB  TRP A 865     -28.002 -22.173 -15.772  1.00 50.48           C  
ANISOU 7058  CB  TRP A 865     5342   9033   4805    950    371   1300       C  
ATOM   7059  CG  TRP A 865     -28.885 -22.514 -14.615  1.00 50.72           C  
ANISOU 7059  CG  TRP A 865     5238   9329   4705    982    424   1409       C  
ATOM   7060  CD1 TRP A 865     -28.515 -23.136 -13.450  1.00 51.58           C  
ANISOU 7060  CD1 TRP A 865     5278   9617   4702   1020    463   1543       C  
ATOM   7061  CD2 TRP A 865     -30.294 -22.280 -14.513  1.00 51.51           C  
ANISOU 7061  CD2 TRP A 865     5249   9560   4764    977    445   1405       C  
ATOM   7062  NE1 TRP A 865     -29.604 -23.294 -12.632  1.00 52.99           N  
ANISOU 7062  NE1 TRP A 865     5330  10035   4770   1034    511   1626       N  
ATOM   7063  CE2 TRP A 865     -30.711 -22.779 -13.257  1.00 54.06           C  
ANISOU 7063  CE2 TRP A 865     5447  10147   4946   1008    501   1539       C  
ATOM   7064  CE3 TRP A 865     -31.248 -21.695 -15.358  1.00 51.22           C  
ANISOU 7064  CE3 TRP A 865     5219   9453   4789    953    421   1304       C  
ATOM   7065  CZ2 TRP A 865     -32.041 -22.707 -12.825  1.00 54.37           C  
ANISOU 7065  CZ2 TRP A 865     5364  10387   4905   1012    538   1569       C  
ATOM   7066  CZ3 TRP A 865     -32.572 -21.623 -14.925  1.00 51.82           C  
ANISOU 7066  CZ3 TRP A 865     5175   9724   4790    963    453   1328       C  
ATOM   7067  CH2 TRP A 865     -32.953 -22.128 -13.671  1.00 52.81           C  
ANISOU 7067  CH2 TRP A 865     5174  10117   4776    990    513   1458       C  
ATOM   7068  N   MET A 866     -26.606 -23.368 -18.846  1.00 49.23           N  
ANISOU 7068  N   MET A 866     5465   8220   5022    737    331   1322       N  
ATOM   7069  CA  MET A 866     -26.156 -23.046 -20.206  1.00 46.31           C  
ANISOU 7069  CA  MET A 866     5201   7626   4768    687    290   1220       C  
ATOM   7070  C   MET A 866     -27.336 -22.977 -21.147  1.00 44.52           C  
ANISOU 7070  C   MET A 866     4979   7326   4611    619    285   1201       C  
ATOM   7071  O   MET A 866     -28.165 -23.890 -21.172  1.00 45.75           O  
ANISOU 7071  O   MET A 866     5094   7488   4799    554    325   1321       O  
ATOM   7072  CB  MET A 866     -25.281 -24.158 -20.763  1.00 46.90           C  
ANISOU 7072  CB  MET A 866     5346   7532   4943    624    304   1309       C  
ATOM   7073  CG  MET A 866     -23.894 -24.274 -20.241  1.00 47.27           C  
ANISOU 7073  CG  MET A 866     5413   7589   4956    679    297   1312       C  
ATOM   7074  SD  MET A 866     -23.219 -25.779 -20.960  1.00 45.05           S  
ANISOU 7074  SD  MET A 866     5202   7106   4811    602    318   1434       S  
ATOM   7075  CE  MET A 866     -23.107 -25.289 -22.674  1.00 41.81           C  
ANISOU 7075  CE  MET A 866     4887   6485   4513    532    278   1291       C  
ATOM   7076  N   ASP A 867     -27.388 -21.913 -21.943  1.00 42.86           N  
ANISOU 7076  N   ASP A 867     4818   7040   4428    629    235   1054       N  
ATOM   7077  CA  ASP A 867     -28.452 -21.746 -22.923  1.00 40.92           C  
ANISOU 7077  CA  ASP A 867     4580   6724   4244    574    221   1024       C  
ATOM   7078  C   ASP A 867     -27.989 -22.258 -24.278  1.00 39.43           C  
ANISOU 7078  C   ASP A 867     4486   6318   4177    484    208   1024       C  
ATOM   7079  O   ASP A 867     -27.375 -21.521 -25.050  1.00 37.03           O  
ANISOU 7079  O   ASP A 867     4255   5909   3905    488    164    920       O  
ATOM   7080  CB  ASP A 867     -28.893 -20.285 -23.014  1.00 38.22           C  
ANISOU 7080  CB  ASP A 867     4230   6430   3860    645    170    874       C  
ATOM   7081  CG  ASP A 867     -30.258 -20.128 -23.653  1.00 37.64           C  
ANISOU 7081  CG  ASP A 867     4125   6362   3817    613    162    862       C  
ATOM   7082  OD1 ASP A 867     -30.626 -20.947 -24.526  1.00 38.23           O  
ANISOU 7082  OD1 ASP A 867     4222   6330   3973    517    177    928       O  
ATOM   7083  OD2 ASP A 867     -30.974 -19.176 -23.283  1.00 35.52           O  
ANISOU 7083  OD2 ASP A 867     3803   6205   3488    689    138    779       O  
ATOM   7084  N   TYR A 868     -28.279 -23.532 -24.539  1.00 39.78           N  
ANISOU 7084  N   TYR A 868     4524   6301   4288    401    246   1143       N  
ATOM   7085  CA  TYR A 868     -27.929 -24.185 -25.796  1.00 39.45           C  
ANISOU 7085  CA  TYR A 868     4560   6066   4362    314    238   1142       C  
ATOM   7086  C   TYR A 868     -28.643 -23.580 -26.998  1.00 39.32           C  
ANISOU 7086  C   TYR A 868     4571   5980   4387    276    199   1051       C  
ATOM   7087  O   TYR A 868     -28.050 -23.454 -28.059  1.00 40.18           O  
ANISOU 7087  O   TYR A 868     4758   5956   4554    243    171    987       O  
ATOM   7088  CB  TYR A 868     -28.269 -25.672 -25.734  1.00 40.73           C  
ANISOU 7088  CB  TYR A 868     4699   6181   4595    236    283   1284       C  
ATOM   7089  CG  TYR A 868     -27.368 -26.500 -24.855  1.00 44.75           C  
ANISOU 7089  CG  TYR A 868     5207   6701   5097    260    316   1391       C  
ATOM   7090  CD1 TYR A 868     -26.239 -27.129 -25.374  1.00 44.05           C  
ANISOU 7090  CD1 TYR A 868     5192   6460   5083    242    310   1393       C  
ATOM   7091  CD2 TYR A 868     -27.660 -26.681 -23.508  1.00 48.67           C  
ANISOU 7091  CD2 TYR A 868     5621   7367   5505    306    352   1494       C  
ATOM   7092  CE1 TYR A 868     -25.417 -27.915 -24.565  1.00 47.29           C  
ANISOU 7092  CE1 TYR A 868     5599   6880   5491    274    335   1497       C  
ATOM   7093  CE2 TYR A 868     -26.841 -27.458 -22.688  1.00 52.36           C  
ANISOU 7093  CE2 TYR A 868     6085   7851   5960    333    379   1607       C  
ATOM   7094  CZ  TYR A 868     -25.724 -28.070 -23.224  1.00 49.79           C  
ANISOU 7094  CZ  TYR A 868     5837   7362   5718    319    368   1609       C  
ATOM   7095  OH  TYR A 868     -24.923 -28.835 -22.409  1.00 54.82           O  
ANISOU 7095  OH  TYR A 868     6468   8017   6345    357    390   1723       O  
ATOM   7096  N   THR A 869     -29.923 -23.243 -26.835  1.00 41.69           N  
ANISOU 7096  N   THR A 869     4801   6383   4654    281    200   1049       N  
ATOM   7097  CA  THR A 869     -30.733 -22.667 -27.912  1.00 40.26           C  
ANISOU 7097  CA  THR A 869     4633   6159   4504    253    161    971       C  
ATOM   7098  C   THR A 869     -30.132 -21.347 -28.402  1.00 38.28           C  
ANISOU 7098  C   THR A 869     4449   5861   4234    312    104    846       C  
ATOM   7099  O   THR A 869     -29.970 -21.152 -29.600  1.00 37.67           O  
ANISOU 7099  O   THR A 869     4437   5666   4211    269     71    795       O  
ATOM   7100  CB  THR A 869     -32.215 -22.472 -27.476  1.00 41.75           C  
ANISOU 7100  CB  THR A 869     4719   6498   4647    266    171    989       C  
ATOM   7101  OG1 THR A 869     -32.775 -23.732 -27.085  1.00 47.38           O  
ANISOU 7101  OG1 THR A 869     5369   7246   5388    193    225   1117       O  
ATOM   7102  CG2 THR A 869     -33.053 -21.897 -28.606  1.00 38.22           C  
ANISOU 7102  CG2 THR A 869     4281   6010   4231    245    126    912       C  
ATOM   7103  N   VAL A 870     -29.784 -20.456 -27.475  1.00 39.64           N  
ANISOU 7103  N   VAL A 870     4604   6126   4331    406     91    797       N  
ATOM   7104  CA  VAL A 870     -29.131 -19.194 -27.835  1.00 42.60           C  
ANISOU 7104  CA  VAL A 870     5043   6444   4698    457     36    683       C  
ATOM   7105  C   VAL A 870     -27.791 -19.491 -28.501  1.00 43.56           C  
ANISOU 7105  C   VAL A 870     5254   6426   4872    410     32    678       C  
ATOM   7106  O   VAL A 870     -27.434 -18.889 -29.520  1.00 42.39           O  
ANISOU 7106  O   VAL A 870     5174   6173   4761    387     -8    615       O  
ATOM   7107  CB  VAL A 870     -28.936 -18.274 -26.608  1.00 43.32           C  
ANISOU 7107  CB  VAL A 870     5093   6662   4705    566     23    623       C  
ATOM   7108  CG1 VAL A 870     -27.957 -17.146 -26.917  1.00 42.64           C  
ANISOU 7108  CG1 VAL A 870     5083   6489   4630    601    -31    515       C  
ATOM   7109  CG2 VAL A 870     -30.283 -17.698 -26.154  1.00 45.56           C  
ANISOU 7109  CG2 VAL A 870     5294   7080   4937    628     13    592       C  
ATOM   7110  N   LEU A 871     -27.071 -20.441 -27.919  1.00 43.70           N  
ANISOU 7110  N   LEU A 871     5264   6451   4889    397     74    750       N  
ATOM   7111  CA  LEU A 871     -25.800 -20.897 -28.440  1.00 44.88           C  
ANISOU 7111  CA  LEU A 871     5482   6487   5084    358     77    751       C  
ATOM   7112  C   LEU A 871     -25.946 -21.342 -29.896  1.00 45.49           C  
ANISOU 7112  C   LEU A 871     5611   6432   5242    271     67    745       C  
ATOM   7113  O   LEU A 871     -25.228 -20.866 -30.780  1.00 44.98           O  
ANISOU 7113  O   LEU A 871     5611   6279   5199    250     38    683       O  
ATOM   7114  CB  LEU A 871     -25.309 -22.054 -27.574  1.00 48.27           C  
ANISOU 7114  CB  LEU A 871     5881   6952   5508    360    126    852       C  
ATOM   7115  CG  LEU A 871     -23.827 -22.250 -27.291  1.00 52.98           C  
ANISOU 7115  CG  LEU A 871     6512   7517   6100    384    130    848       C  
ATOM   7116  CD1 LEU A 871     -23.681 -23.137 -26.056  1.00 55.39           C  
ANISOU 7116  CD1 LEU A 871     6760   7916   6368    419    173    959       C  
ATOM   7117  CD2 LEU A 871     -23.115 -22.850 -28.514  1.00 56.38           C  
ANISOU 7117  CD2 LEU A 871     7013   7794   6616    314    127    837       C  
ATOM   7118  N   LEU A 872     -26.886 -22.246 -30.142  1.00 46.51           N  
ANISOU 7118  N   LEU A 872     5707   6557   5410    216     92    809       N  
ATOM   7119  CA  LEU A 872     -27.124 -22.753 -31.484  1.00 47.53           C  
ANISOU 7119  CA  LEU A 872     5873   6577   5611    133     82    795       C  
ATOM   7120  C   LEU A 872     -27.570 -21.649 -32.440  1.00 48.82           C  
ANISOU 7120  C   LEU A 872     6064   6722   5762    134     31    713       C  
ATOM   7121  O   LEU A 872     -27.117 -21.603 -33.586  1.00 50.89           O  
ANISOU 7121  O   LEU A 872     6383   6894   6057     89     10    670       O  
ATOM   7122  CB  LEU A 872     -28.152 -23.884 -31.462  1.00 46.18           C  
ANISOU 7122  CB  LEU A 872     5647   6412   5486     72    114    874       C  
ATOM   7123  CG  LEU A 872     -28.477 -24.522 -32.813  1.00 48.30           C  
ANISOU 7123  CG  LEU A 872     5944   6576   5832    -18    103    850       C  
ATOM   7124  CD1 LEU A 872     -27.324 -25.409 -33.291  1.00 48.87           C  
ANISOU 7124  CD1 LEU A 872     6073   6528   5967    -53    116    850       C  
ATOM   7125  CD2 LEU A 872     -29.787 -25.303 -32.751  1.00 50.99           C  
ANISOU 7125  CD2 LEU A 872     6215   6949   6210    -77    123    910       C  
ATOM   7126  N   GLU A 873     -28.451 -20.766 -31.978  1.00 49.27           N  
ANISOU 7126  N   GLU A 873     6078   6871   5771    189     11    691       N  
ATOM   7127  CA  GLU A 873     -28.948 -19.686 -32.833  1.00 50.90           C  
ANISOU 7127  CA  GLU A 873     6310   7060   5971    201    -43    623       C  
ATOM   7128  C   GLU A 873     -27.887 -18.641 -33.201  1.00 50.59           C  
ANISOU 7128  C   GLU A 873     6345   6954   5923    227    -82    558       C  
ATOM   7129  O   GLU A 873     -27.774 -18.256 -34.368  1.00 52.83           O  
ANISOU 7129  O   GLU A 873     6680   7165   6228    190   -116    527       O  
ATOM   7130  CB  GLU A 873     -30.192 -19.020 -32.232  1.00 52.01           C  
ANISOU 7130  CB  GLU A 873     6379   7314   6067    264    -59    611       C  
ATOM   7131  CG  GLU A 873     -31.478 -19.839 -32.387  1.00 55.95           C  
ANISOU 7131  CG  GLU A 873     6807   7869   6584    215    -37    661       C  
ATOM   7132  CD  GLU A 873     -31.878 -20.088 -33.844  1.00 60.45           C  
ANISOU 7132  CD  GLU A 873     7406   8361   7202    140    -63    644       C  
ATOM   7133  OE1 GLU A 873     -32.640 -21.054 -34.086  1.00 59.66           O  
ANISOU 7133  OE1 GLU A 873     7257   8276   7136     72    -39    685       O  
ATOM   7134  OE2 GLU A 873     -31.435 -19.323 -34.740  1.00 59.56           O  
ANISOU 7134  OE2 GLU A 873     7361   8178   7092    145   -107    590       O  
ATOM   7135  N   LYS A 874     -27.106 -18.201 -32.221  1.00 49.24           N  
ANISOU 7135  N   LYS A 874     6175   6816   5719    285    -78    540       N  
ATOM   7136  CA  LYS A 874     -26.157 -17.101 -32.420  1.00 48.51           C  
ANISOU 7136  CA  LYS A 874     6143   6669   5621    309   -118    474       C  
ATOM   7137  C   LYS A 874     -24.860 -17.482 -33.115  1.00 48.00           C  
ANISOU 7137  C   LYS A 874     6138   6516   5585    249   -108    475       C  
ATOM   7138  O   LYS A 874     -24.358 -16.720 -33.951  1.00 49.20           O  
ANISOU 7138  O   LYS A 874     6346   6598   5748    226   -144    437       O  
ATOM   7139  CB  LYS A 874     -25.838 -16.411 -31.089  1.00 48.77           C  
ANISOU 7139  CB  LYS A 874     6145   6779   5606    396   -124    436       C  
ATOM   7140  CG  LYS A 874     -26.541 -15.077 -30.889  1.00 50.35           C  
ANISOU 7140  CG  LYS A 874     6336   7004   5789    467   -178    367       C  
ATOM   7141  CD  LYS A 874     -26.677 -14.693 -29.418  1.00 50.15           C  
ANISOU 7141  CD  LYS A 874     6248   7102   5706    562   -173    329       C  
ATOM   7142  CE  LYS A 874     -25.374 -14.840 -28.650  1.00 48.28           C  
ANISOU 7142  CE  LYS A 874     6017   6882   5444    572   -155    318       C  
ATOM   7143  NZ  LYS A 874     -25.549 -14.473 -27.220  1.00 48.19           N  
ANISOU 7143  NZ  LYS A 874     5936   7012   5362    667   -152    276       N  
ATOM   7144  N   THR A 875     -24.306 -18.641 -32.770  1.00 45.78           N  
ANISOU 7144  N   THR A 875     5842   6238   5313    227    -61    521       N  
ATOM   7145  CA  THR A 875     -22.959 -18.981 -33.237  1.00 44.59           C  
ANISOU 7145  CA  THR A 875     5737   6023   5182    189    -50    511       C  
ATOM   7146  C   THR A 875     -22.951 -19.908 -34.441  1.00 42.60           C  
ANISOU 7146  C   THR A 875     5510   5700   4976    112    -36    528       C  
ATOM   7147  O   THR A 875     -21.943 -20.011 -35.144  1.00 42.36           O  
ANISOU 7147  O   THR A 875     5519   5617   4957     77    -35    502       O  
ATOM   7148  CB  THR A 875     -22.079 -19.617 -32.125  1.00 43.73           C  
ANISOU 7148  CB  THR A 875     5603   5958   5056    225    -14    540       C  
ATOM   7149  OG1 THR A 875     -22.496 -20.969 -31.892  1.00 46.55           O  
ANISOU 7149  OG1 THR A 875     5927   6320   5441    206     29    616       O  
ATOM   7150  CG2 THR A 875     -22.164 -18.819 -30.836  1.00 44.49           C  
ANISOU 7150  CG2 THR A 875     5660   6149   5095    306    -26    519       C  
ATOM   7151  N   PHE A 876     -24.062 -20.596 -34.670  1.00 40.32           N  
ANISOU 7151  N   PHE A 876     5190   5417   4711     85    -24    563       N  
ATOM   7152  CA  PHE A 876     -24.092 -21.587 -35.727  1.00 38.31           C  
ANISOU 7152  CA  PHE A 876     4951   5098   4506     14    -12    566       C  
ATOM   7153  C   PHE A 876     -25.086 -21.223 -36.814  1.00 39.56           C  
ANISOU 7153  C   PHE A 876     5114   5250   4667    -24    -44    542       C  
ATOM   7154  O   PHE A 876     -24.700 -21.029 -37.963  1.00 42.01           O  
ANISOU 7154  O   PHE A 876     5464   5519   4977    -65    -64    504       O  
ATOM   7155  CB  PHE A 876     -24.388 -22.976 -35.159  1.00 37.00           C  
ANISOU 7155  CB  PHE A 876     4746   4928   4385     -1     32    629       C  
ATOM   7156  CG  PHE A 876     -24.388 -24.056 -36.186  1.00 33.20           C  
ANISOU 7156  CG  PHE A 876     4279   4368   3968    -71     41    619       C  
ATOM   7157  CD1 PHE A 876     -23.195 -24.515 -36.730  1.00 31.85           C  
ANISOU 7157  CD1 PHE A 876     4146   4135   3819    -86     50    585       C  
ATOM   7158  CD2 PHE A 876     -25.581 -24.625 -36.607  1.00 33.80           C  
ANISOU 7158  CD2 PHE A 876     4323   4439   4081   -121     41    633       C  
ATOM   7159  CE1 PHE A 876     -23.196 -25.519 -37.695  1.00 35.44           C  
ANISOU 7159  CE1 PHE A 876     4611   4520   4334   -144     55    557       C  
ATOM   7160  CE2 PHE A 876     -25.593 -25.633 -37.568  1.00 37.06           C  
ANISOU 7160  CE2 PHE A 876     4746   4776   4558   -187     45    606       C  
ATOM   7161  CZ  PHE A 876     -24.399 -26.079 -38.115  1.00 36.42           C  
ANISOU 7161  CZ  PHE A 876     4707   4631   4500   -195     51    564       C  
ATOM   7162  N   ILE A 877     -26.360 -21.123 -36.442  1.00 40.02           N  
ANISOU 7162  N   ILE A 877     5125   5363   4719     -9    -50    565       N  
ATOM   7163  CA  ILE A 877     -27.435 -20.958 -37.407  1.00 38.35           C  
ANISOU 7163  CA  ILE A 877     4902   5159   4512    -43    -80    548       C  
ATOM   7164  C   ILE A 877     -27.336 -19.630 -38.147  1.00 38.30           C  
ANISOU 7164  C   ILE A 877     4939   5144   4469    -24   -133    507       C  
ATOM   7165  O   ILE A 877     -27.423 -19.597 -39.383  1.00 35.80           O  
ANISOU 7165  O   ILE A 877     4648   4802   4153    -71   -156    485       O  
ATOM   7166  CB  ILE A 877     -28.826 -21.157 -36.763  1.00 39.08           C  
ANISOU 7166  CB  ILE A 877     4919   5327   4602    -28    -73    583       C  
ATOM   7167  CG1 ILE A 877     -28.985 -22.616 -36.314  1.00 41.58           C  
ANISOU 7167  CG1 ILE A 877     5197   5633   4971    -75    -23    638       C  
ATOM   7168  CG2 ILE A 877     -29.954 -20.779 -37.749  1.00 39.77           C  
ANISOU 7168  CG2 ILE A 877     4989   5438   4683    -50   -114    557       C  
ATOM   7169  CD1 ILE A 877     -30.369 -22.953 -35.755  1.00 47.13           C  
ANISOU 7169  CD1 ILE A 877     5816   6416   5676    -82     -9    683       C  
ATOM   7170  N   LYS A 878     -27.137 -18.545 -37.403  1.00 38.48           N  
ANISOU 7170  N   LYS A 878     4971   5188   4461     44   -153    497       N  
ATOM   7171  CA  LYS A 878     -27.055 -17.234 -38.034  1.00 40.78           C  
ANISOU 7171  CA  LYS A 878     5308   5455   4733     63   -207    468       C  
ATOM   7172  C   LYS A 878     -25.894 -17.168 -39.034  1.00 39.73           C  
ANISOU 7172  C   LYS A 878     5236   5257   4601      7   -211    455       C  
ATOM   7173  O   LYS A 878     -26.099 -16.750 -40.166  1.00 41.96           O  
ANISOU 7173  O   LYS A 878     5546   5523   4872    -24   -244    451       O  
ATOM   7174  CB  LYS A 878     -26.998 -16.090 -37.012  1.00 43.38           C  
ANISOU 7174  CB  LYS A 878     5636   5804   5044    147   -232    446       C  
ATOM   7175  CG  LYS A 878     -27.707 -14.844 -37.511  1.00 49.15           C  
ANISOU 7175  CG  LYS A 878     6384   6522   5768    186   -295    427       C  
ATOM   7176  CD  LYS A 878     -27.210 -13.566 -36.860  1.00 58.21           C  
ANISOU 7176  CD  LYS A 878     7562   7641   6916    250   -332    388       C  
ATOM   7177  CE  LYS A 878     -27.635 -12.343 -37.690  1.00 61.25           C  
ANISOU 7177  CE  LYS A 878     7989   7971   7312    270   -401    381       C  
ATOM   7178  NZ  LYS A 878     -27.313 -11.052 -37.016  1.00 62.65           N  
ANISOU 7178  NZ  LYS A 878     8193   8105   7506    339   -446    335       N  
ATOM   7179  N   PRO A 879     -24.678 -17.600 -38.635  1.00 40.48           N  
ANISOU 7179  N   PRO A 879     5347   5330   4702     -5   -177    450       N  
ATOM   7180  CA  PRO A 879     -23.629 -17.658 -39.653  1.00 38.45           C  
ANISOU 7180  CA  PRO A 879     5136   5033   4442    -62   -175    435       C  
ATOM   7181  C   PRO A 879     -23.995 -18.566 -40.827  1.00 36.26           C  
ANISOU 7181  C   PRO A 879     4852   4753   4171   -125   -167    430       C  
ATOM   7182  O   PRO A 879     -23.763 -18.190 -41.966  1.00 33.43           O  
ANISOU 7182  O   PRO A 879     4524   4389   3789   -165   -189    420       O  
ATOM   7183  CB  PRO A 879     -22.432 -18.227 -38.891  1.00 39.51           C  
ANISOU 7183  CB  PRO A 879     5267   5161   4585    -54   -134    430       C  
ATOM   7184  CG  PRO A 879     -22.662 -17.814 -37.486  1.00 39.77           C  
ANISOU 7184  CG  PRO A 879     5273   5228   4611     16   -134    437       C  
ATOM   7185  CD  PRO A 879     -24.141 -17.886 -37.287  1.00 40.47           C  
ANISOU 7185  CD  PRO A 879     5322   5352   4701     40   -144    456       C  
ATOM   7186  N   LEU A 880     -24.569 -19.737 -40.555  1.00 36.37           N  
ANISOU 7186  N   LEU A 880     4825   4776   4218   -135   -136    438       N  
ATOM   7187  CA  LEU A 880     -24.915 -20.674 -41.629  1.00 36.16           C  
ANISOU 7187  CA  LEU A 880     4788   4742   4207   -197   -131    416       C  
ATOM   7188  C   LEU A 880     -25.942 -20.109 -42.622  1.00 36.90           C  
ANISOU 7188  C   LEU A 880     4878   4870   4273   -215   -176    410       C  
ATOM   7189  O   LEU A 880     -25.774 -20.250 -43.840  1.00 36.82           O  
ANISOU 7189  O   LEU A 880     4882   4866   4241   -262   -189    381       O  
ATOM   7190  CB  LEU A 880     -25.385 -22.017 -41.066  1.00 35.98           C  
ANISOU 7190  CB  LEU A 880     4722   4707   4242   -210    -94    430       C  
ATOM   7191  CG  LEU A 880     -25.723 -23.078 -42.120  1.00 35.94           C  
ANISOU 7191  CG  LEU A 880     4703   4681   4270   -276    -91    392       C  
ATOM   7192  CD1 LEU A 880     -24.458 -23.518 -42.862  1.00 36.54           C  
ANISOU 7192  CD1 LEU A 880     4814   4724   4347   -302    -77    343       C  
ATOM   7193  CD2 LEU A 880     -26.393 -24.259 -41.468  1.00 35.13           C  
ANISOU 7193  CD2 LEU A 880     4555   4556   4237   -294    -62    419       C  
ATOM   7194  N   GLU A 881     -26.995 -19.475 -42.101  1.00 38.34           N  
ANISOU 7194  N   GLU A 881     5034   5085   4448   -171   -201    434       N  
ATOM   7195  CA  GLU A 881     -27.975 -18.770 -42.932  1.00 40.83           C  
ANISOU 7195  CA  GLU A 881     5344   5438   4732   -169   -252    434       C  
ATOM   7196  C   GLU A 881     -27.285 -17.731 -43.822  1.00 39.47           C  
ANISOU 7196  C   GLU A 881     5231   5249   4518   -175   -288    437       C  
ATOM   7197  O   GLU A 881     -27.632 -17.584 -44.992  1.00 41.87           O  
ANISOU 7197  O   GLU A 881     5539   5580   4788   -207   -318    433       O  
ATOM   7198  CB  GLU A 881     -29.059 -18.115 -42.061  1.00 44.58           C  
ANISOU 7198  CB  GLU A 881     5780   5952   5205   -101   -273    455       C  
ATOM   7199  CG  GLU A 881     -29.976 -17.122 -42.796  1.00 55.45           C  
ANISOU 7199  CG  GLU A 881     7157   7363   6550    -74   -335    459       C  
ATOM   7200  CD  GLU A 881     -31.122 -17.788 -43.558  1.00 63.63           C  
ANISOU 7200  CD  GLU A 881     8138   8456   7581   -112   -348    448       C  
ATOM   7201  OE1 GLU A 881     -31.806 -18.656 -42.967  1.00 68.72           O  
ANISOU 7201  OE1 GLU A 881     8720   9133   8256   -125   -318    446       O  
ATOM   7202  OE2 GLU A 881     -31.356 -17.426 -44.738  1.00 66.31           O  
ANISOU 7202  OE2 GLU A 881     8493   8817   7887   -132   -389    444       O  
ATOM   7203  N   GLY A 882     -26.303 -17.027 -43.259  1.00 38.15           N  
ANISOU 7203  N   GLY A 882     5103   5043   4350   -150   -284    446       N  
ATOM   7204  CA  GLY A 882     -25.493 -16.065 -44.005  1.00 36.38           C  
ANISOU 7204  CA  GLY A 882     4934   4794   4095   -169   -312    459       C  
ATOM   7205  C   GLY A 882     -24.748 -16.699 -45.169  1.00 34.35           C  
ANISOU 7205  C   GLY A 882     4690   4553   3809   -242   -293    443       C  
ATOM   7206  O   GLY A 882     -24.691 -16.124 -46.263  1.00 33.49           O  
ANISOU 7206  O   GLY A 882     4604   4464   3655   -272   -324    462       O  
ATOM   7207  N   PHE A 883     -24.183 -17.884 -44.939  1.00 31.98           N  
ANISOU 7207  N   PHE A 883     4370   4249   3532   -266   -243    408       N  
ATOM   7208  CA  PHE A 883     -23.449 -18.600 -45.987  1.00 33.17           C  
ANISOU 7208  CA  PHE A 883     4524   4422   3659   -325   -222    372       C  
ATOM   7209  C   PHE A 883     -24.404 -19.003 -47.092  1.00 33.47           C  
ANISOU 7209  C   PHE A 883     4538   4510   3671   -357   -245    351       C  
ATOM   7210  O   PHE A 883     -24.210 -18.640 -48.246  1.00 36.46           O  
ANISOU 7210  O   PHE A 883     4928   4934   3989   -392   -266    352       O  
ATOM   7211  CB  PHE A 883     -22.746 -19.874 -45.473  1.00 29.24           C  
ANISOU 7211  CB  PHE A 883     4006   3898   3204   -331   -169    331       C  
ATOM   7212  CG  PHE A 883     -21.769 -19.649 -44.351  1.00 30.77           C  
ANISOU 7212  CG  PHE A 883     4214   4058   3419   -295   -144    346       C  
ATOM   7213  CD1 PHE A 883     -21.333 -18.366 -44.003  1.00 28.21           C  
ANISOU 7213  CD1 PHE A 883     3920   3726   3072   -276   -167    376       C  
ATOM   7214  CD2 PHE A 883     -21.248 -20.740 -43.663  1.00 30.49           C  
ANISOU 7214  CD2 PHE A 883     4159   3997   3428   -282   -102    326       C  
ATOM   7215  CE1 PHE A 883     -20.428 -18.173 -42.970  1.00 25.70           C  
ANISOU 7215  CE1 PHE A 883     3606   3388   2769   -246   -147    377       C  
ATOM   7216  CE2 PHE A 883     -20.338 -20.557 -42.626  1.00 30.43           C  
ANISOU 7216  CE2 PHE A 883     4157   3974   3430   -245    -82    339       C  
ATOM   7217  CZ  PHE A 883     -19.929 -19.269 -42.276  1.00 29.66           C  
ANISOU 7217  CZ  PHE A 883     4084   3882   3303   -228   -104    359       C  
ATOM   7218  N   THR A 884     -25.438 -19.748 -46.707  1.00 34.17           N  
ANISOU 7218  N   THR A 884     4584   4598   3802   -349   -241    336       N  
ATOM   7219  CA  THR A 884     -26.354 -20.397 -47.636  1.00 33.73           C  
ANISOU 7219  CA  THR A 884     4491   4589   3735   -386   -258    299       C  
ATOM   7220  C   THR A 884     -27.165 -19.424 -48.488  1.00 35.37           C  
ANISOU 7220  C   THR A 884     4700   4859   3880   -380   -315    328       C  
ATOM   7221  O   THR A 884     -27.421 -19.698 -49.664  1.00 36.23           O  
ANISOU 7221  O   THR A 884     4793   5030   3943   -419   -334    295       O  
ATOM   7222  CB  THR A 884     -27.324 -21.336 -46.898  1.00 33.65           C  
ANISOU 7222  CB  THR A 884     4430   4562   3794   -384   -242    287       C  
ATOM   7223  OG1 THR A 884     -27.981 -20.607 -45.855  1.00 33.95           O  
ANISOU 7223  OG1 THR A 884     4459   4598   3843   -328   -253    342       O  
ATOM   7224  CG2 THR A 884     -26.571 -22.518 -46.296  1.00 30.50           C  
ANISOU 7224  CG2 THR A 884     4028   4100   3461   -398   -190    261       C  
ATOM   7225  N   SER A 885     -27.575 -18.302 -47.903  1.00 34.50           N  
ANISOU 7225  N   SER A 885     4606   4735   3768   -326   -345    385       N  
ATOM   7226  CA  SER A 885     -28.334 -17.312 -48.656  1.00 36.35           C  
ANISOU 7226  CA  SER A 885     4845   5016   3949   -307   -405    423       C  
ATOM   7227  C   SER A 885     -27.433 -16.665 -49.703  1.00 38.58           C  
ANISOU 7227  C   SER A 885     5175   5317   4167   -340   -420    451       C  
ATOM   7228  O   SER A 885     -27.858 -16.443 -50.837  1.00 37.90           O  
ANISOU 7228  O   SER A 885     5080   5301   4018   -359   -456    463       O  
ATOM   7229  CB  SER A 885     -28.976 -16.266 -47.740  1.00 38.06           C  
ANISOU 7229  CB  SER A 885     5067   5203   4189   -230   -437    469       C  
ATOM   7230  OG  SER A 885     -28.008 -15.553 -47.003  1.00 42.16           O  
ANISOU 7230  OG  SER A 885     5636   5654   4729   -205   -426    493       O  
ATOM   7231  N   ALA A 886     -26.177 -16.415 -49.331  1.00 37.53           N  
ANISOU 7231  N   ALA A 886     5082   5133   4044   -350   -391    462       N  
ATOM   7232  CA  ALA A 886     -25.186 -15.917 -50.278  1.00 38.02           C  
ANISOU 7232  CA  ALA A 886     5180   5222   4045   -395   -393    490       C  
ATOM   7233  C   ALA A 886     -24.956 -16.924 -51.402  1.00 36.84           C  
ANISOU 7233  C   ALA A 886     4999   5156   3841   -452   -373    430       C  
ATOM   7234  O   ALA A 886     -24.849 -16.536 -52.560  1.00 38.08           O  
ANISOU 7234  O   ALA A 886     5161   5388   3918   -484   -396    456       O  
ATOM   7235  CB  ALA A 886     -23.875 -15.581 -49.572  1.00 38.25           C  
ANISOU 7235  CB  ALA A 886     5244   5187   4100   -400   -361    500       C  
ATOM   7236  N   ALA A 887     -24.908 -18.210 -51.059  1.00 36.50           N  
ANISOU 7236  N   ALA A 887     4922   5103   3844   -463   -332    351       N  
ATOM   7237  CA  ALA A 887     -24.698 -19.275 -52.046  1.00 38.19           C  
ANISOU 7237  CA  ALA A 887     5102   5384   4023   -510   -314    269       C  
ATOM   7238  C   ALA A 887     -25.985 -19.715 -52.761  1.00 40.89           C  
ANISOU 7238  C   ALA A 887     5398   5793   4344   -521   -349    232       C  
ATOM   7239  O   ALA A 887     -25.940 -20.595 -53.634  1.00 40.16           O  
ANISOU 7239  O   ALA A 887     5273   5764   4223   -560   -342    149       O  
ATOM   7240  CB  ALA A 887     -24.010 -20.473 -51.399  1.00 37.01           C  
ANISOU 7240  CB  ALA A 887     4940   5178   3944   -515   -260    198       C  
ATOM   7241  N   LYS A 888     -27.112 -19.086 -52.409  1.00 41.27           N  
ANISOU 7241  N   LYS A 888     5439   5835   4405   -484   -389    284       N  
ATOM   7242  CA  LYS A 888     -28.442 -19.424 -52.956  1.00 44.72           C  
ANISOU 7242  CA  LYS A 888     5824   6342   4827   -489   -427    254       C  
ATOM   7243  C   LYS A 888     -28.814 -20.898 -52.732  1.00 44.27           C  
ANISOU 7243  C   LYS A 888     5716   6266   4840   -522   -398    157       C  
ATOM   7244  O   LYS A 888     -29.281 -21.582 -53.644  1.00 46.54           O  
ANISOU 7244  O   LYS A 888     5959   6624   5099   -561   -414     83       O  
ATOM   7245  CB  LYS A 888     -28.569 -19.070 -54.449  1.00 45.10           C  
ANISOU 7245  CB  LYS A 888     5861   6512   4762   -514   -467    255       C  
ATOM   7246  CG  LYS A 888     -27.793 -17.840 -54.919  1.00 50.44           C  
ANISOU 7246  CG  LYS A 888     6593   7208   5365   -509   -484    349       C  
ATOM   7247  CD  LYS A 888     -28.590 -16.563 -54.823  1.00 54.44           C  
ANISOU 7247  CD  LYS A 888     7120   7707   5856   -456   -542    452       C  
ATOM   7248  CE  LYS A 888     -28.256 -15.657 -56.000  1.00 56.93           C  
ANISOU 7248  CE  LYS A 888     7461   8105   6065   -472   -578    531       C  
ATOM   7249  NZ  LYS A 888     -28.507 -14.227 -55.686  1.00 59.01           N  
ANISOU 7249  NZ  LYS A 888     7775   8306   6341   -420   -626    652       N  
ATOM   7250  N   LEU A 889     -28.592 -21.368 -51.511  1.00 44.86           N  
ANISOU 7250  N   LEU A 889     5796   6243   5005   -507   -357    160       N  
ATOM   7251  CA  LEU A 889     -28.915 -22.728 -51.100  1.00 46.36           C  
ANISOU 7251  CA  LEU A 889     5946   6388   5283   -538   -328     93       C  
ATOM   7252  C   LEU A 889     -29.799 -22.651 -49.867  1.00 46.87           C  
ANISOU 7252  C   LEU A 889     5986   6410   5412   -506   -323    146       C  
ATOM   7253  O   LEU A 889     -29.818 -21.638 -49.159  1.00 46.48           O  
ANISOU 7253  O   LEU A 889     5962   6349   5350   -452   -331    219       O  
ATOM   7254  CB  LEU A 889     -27.632 -23.496 -50.736  1.00 48.02           C  
ANISOU 7254  CB  LEU A 889     6183   6523   5541   -548   -275     56       C  
ATOM   7255  CG  LEU A 889     -26.824 -24.369 -51.713  1.00 50.00           C  
ANISOU 7255  CG  LEU A 889     6430   6793   5777   -588   -260    -44       C  
ATOM   7256  CD1 LEU A 889     -26.491 -23.687 -53.009  1.00 53.40           C  
ANISOU 7256  CD1 LEU A 889     6867   7336   6086   -601   -288    -56       C  
ATOM   7257  CD2 LEU A 889     -25.537 -24.816 -51.060  1.00 51.45           C  
ANISOU 7257  CD2 LEU A 889     6643   6896   6008   -571   -212    -52       C  
ATOM   7258  N   ASP A 890     -30.522 -23.732 -49.602  1.00 46.50           N  
ANISOU 7258  N   ASP A 890     5887   6343   5437   -542   -311    105       N  
ATOM   7259  CA  ASP A 890     -31.279 -23.848 -48.372  1.00 45.44           C  
ANISOU 7259  CA  ASP A 890     5721   6178   5366   -522   -295    157       C  
ATOM   7260  C   ASP A 890     -30.651 -24.909 -47.466  1.00 43.63           C  
ANISOU 7260  C   ASP A 890     5498   5848   5230   -539   -240    157       C  
ATOM   7261  O   ASP A 890     -30.291 -25.996 -47.926  1.00 39.11           O  
ANISOU 7261  O   ASP A 890     4922   5232   4707   -589   -224     89       O  
ATOM   7262  CB  ASP A 890     -32.761 -24.127 -48.680  1.00 48.14           C  
ANISOU 7262  CB  ASP A 890     5987   6588   5716   -553   -326    136       C  
ATOM   7263  CG  ASP A 890     -33.509 -22.869 -49.158  1.00 51.34           C  
ANISOU 7263  CG  ASP A 890     6383   7091   6035   -505   -382    169       C  
ATOM   7264  OD1 ASP A 890     -33.555 -21.871 -48.397  1.00 49.39           O  
ANISOU 7264  OD1 ASP A 890     6155   6840   5769   -436   -388    238       O  
ATOM   7265  OD2 ASP A 890     -34.052 -22.875 -50.291  1.00 52.46           O  
ANISOU 7265  OD2 ASP A 890     6494   7313   6125   -532   -424    123       O  
ATOM   7266  N   TYR A 891     -30.482 -24.581 -46.184  1.00 43.85           N  
ANISOU 7266  N   TYR A 891     5537   5843   5280   -491   -213    230       N  
ATOM   7267  CA  TYR A 891     -29.913 -25.544 -45.242  1.00 43.70           C  
ANISOU 7267  CA  TYR A 891     5522   5739   5343   -498   -163    249       C  
ATOM   7268  C   TYR A 891     -30.982 -26.500 -44.720  1.00 44.76           C  
ANISOU 7268  C   TYR A 891     5591   5859   5556   -543   -148    267       C  
ATOM   7269  O   TYR A 891     -30.667 -27.544 -44.158  1.00 44.99           O  
ANISOU 7269  O   TYR A 891     5617   5808   5669   -568   -112    281       O  
ATOM   7270  CB  TYR A 891     -29.115 -24.867 -44.106  1.00 43.58           C  
ANISOU 7270  CB  TYR A 891     5543   5703   5310   -429   -138    316       C  
ATOM   7271  CG  TYR A 891     -29.888 -23.877 -43.268  1.00 44.11           C  
ANISOU 7271  CG  TYR A 891     5587   5830   5342   -374   -151    376       C  
ATOM   7272  CD1 TYR A 891     -29.946 -22.532 -43.623  1.00 46.74           C  
ANISOU 7272  CD1 TYR A 891     5946   6210   5602   -329   -192    379       C  
ATOM   7273  CD2 TYR A 891     -30.550 -24.282 -42.107  1.00 46.45           C  
ANISOU 7273  CD2 TYR A 891     5834   6137   5678   -363   -124    430       C  
ATOM   7274  CE1 TYR A 891     -30.659 -21.617 -42.854  1.00 48.14           C  
ANISOU 7274  CE1 TYR A 891     6101   6437   5754   -267   -209    420       C  
ATOM   7275  CE2 TYR A 891     -31.264 -23.372 -41.326  1.00 45.83           C  
ANISOU 7275  CE2 TYR A 891     5725   6129   5559   -304   -136    472       C  
ATOM   7276  CZ  TYR A 891     -31.312 -22.043 -41.705  1.00 46.39           C  
ANISOU 7276  CZ  TYR A 891     5823   6238   5564   -251   -180    458       C  
ATOM   7277  OH  TYR A 891     -32.015 -21.137 -40.949  1.00 43.34           O  
ANISOU 7277  OH  TYR A 891     5407   5916   5146   -182   -197    484       O  
ATOM   7278  N   GLU A 892     -32.241 -26.132 -44.928  1.00 45.83           N  
ANISOU 7278  N   GLU A 892     5672   6074   5666   -554   -178    270       N  
ATOM   7279  CA  GLU A 892     -33.379 -26.988 -44.629  1.00 49.77           C  
ANISOU 7279  CA  GLU A 892     6097   6582   6233   -613   -170    280       C  
ATOM   7280  C   GLU A 892     -34.157 -27.214 -45.914  1.00 51.53           C  
ANISOU 7280  C   GLU A 892     6280   6857   6444   -671   -214    196       C  
ATOM   7281  O   GLU A 892     -34.424 -26.267 -46.649  1.00 52.32           O  
ANISOU 7281  O   GLU A 892     6383   7040   6456   -639   -258    175       O  
ATOM   7282  CB  GLU A 892     -34.276 -26.340 -43.573  1.00 49.87           C  
ANISOU 7282  CB  GLU A 892     6059   6671   6220   -568   -165    359       C  
ATOM   7283  CG  GLU A 892     -33.618 -26.232 -42.207  1.00 53.84           C  
ANISOU 7283  CG  GLU A 892     6584   7140   6732   -513   -120    438       C  
ATOM   7284  CD  GLU A 892     -34.558 -25.740 -41.125  1.00 56.24           C  
ANISOU 7284  CD  GLU A 892     6824   7535   7009   -472   -110    507       C  
ATOM   7285  OE1 GLU A 892     -34.793 -26.499 -40.159  1.00 58.98           O  
ANISOU 7285  OE1 GLU A 892     7129   7873   7407   -497    -67    571       O  
ATOM   7286  OE2 GLU A 892     -35.057 -24.600 -41.235  1.00 56.29           O  
ANISOU 7286  OE2 GLU A 892     6819   7624   6943   -411   -146    498       O  
ATOM   7287  N   LYS A 893     -34.512 -28.465 -46.188  1.00 54.02           N  
ANISOU 7287  N   LYS A 893     6557   7120   6849   -756   -207    148       N  
ATOM   7288  CA  LYS A 893     -35.237 -28.798 -47.408  1.00 58.82           C  
ANISOU 7288  CA  LYS A 893     7119   7780   7450   -819   -251     51       C  
ATOM   7289  C   LYS A 893     -36.592 -28.095 -47.468  1.00 60.96           C  
ANISOU 7289  C   LYS A 893     7316   8182   7663   -811   -286     73       C  
ATOM   7290  O   LYS A 893     -37.408 -28.222 -46.557  1.00 62.15           O  
ANISOU 7290  O   LYS A 893     7409   8355   7851   -821   -267    137       O  
ATOM   7291  CB  LYS A 893     -35.420 -30.309 -47.538  1.00 61.03           C  
ANISOU 7291  CB  LYS A 893     7367   7965   7858   -916   -237     -7       C  
ATOM   7292  CG  LYS A 893     -35.932 -30.748 -48.903  1.00 64.93           C  
ANISOU 7292  CG  LYS A 893     7820   8505   8347   -982   -285   -137       C  
ATOM   7293  CD  LYS A 893     -36.296 -32.221 -48.899  1.00 71.09           C  
ANISOU 7293  CD  LYS A 893     8559   9181   9273  -1085   -276   -193       C  
ATOM   7294  CE  LYS A 893     -36.863 -32.652 -50.242  1.00 73.57           C  
ANISOU 7294  CE  LYS A 893     8822   9551   9580  -1152   -329   -340       C  
ATOM   7295  NZ  LYS A 893     -37.143 -34.110 -50.254  1.00 75.04           N  
ANISOU 7295  NZ  LYS A 893     8973   9613   9926  -1257   -324   -408       N  
ATOM   7296  N   LYS A 894     -36.807 -27.341 -48.542  1.00 63.55           N  
ANISOU 7296  N   LYS A 894     7645   8606   7896   -787   -338     24       N  
ATOM   7297  CA  LYS A 894     -38.090 -26.688 -48.801  1.00 66.75           C  
ANISOU 7297  CA  LYS A 894     7977   9143   8242   -772   -382     30       C  
ATOM   7298  C   LYS A 894     -39.117 -27.720 -49.268  1.00 68.30           C  
ANISOU 7298  C   LYS A 894     8082   9371   8500   -873   -399    -42       C  
ATOM   7299  O   LYS A 894     -38.750 -28.740 -49.862  1.00 68.44           O  
ANISOU 7299  O   LYS A 894     8105   9321   8577   -947   -396   -128       O  
ATOM   7300  CB  LYS A 894     -37.928 -25.586 -49.856  1.00 67.61           C  
ANISOU 7300  CB  LYS A 894     8119   9340   8229   -714   -436     10       C  
ATOM   7301  CG  LYS A 894     -37.112 -26.008 -51.079  1.00 71.02           C  
ANISOU 7301  CG  LYS A 894     8591   9758   8635   -752   -450    -80       C  
ATOM   7302  CD  LYS A 894     -37.593 -25.319 -52.349  1.00 75.89           C  
ANISOU 7302  CD  LYS A 894     9185  10511   9138   -735   -516   -117       C  
ATOM   7303  CE  LYS A 894     -36.914 -25.912 -53.581  1.00 78.12           C  
ANISOU 7303  CE  LYS A 894     9486  10807   9389   -783   -528   -223       C  
ATOM   7304  NZ  LYS A 894     -37.463 -25.365 -54.856  1.00 78.14           N  
ANISOU 7304  NZ  LYS A 894     9452  10963   9273   -774   -593   -261       N  
ATOM   7305  N   ALA A 895     -40.395 -27.456 -48.999  1.00 69.01           N  
ANISOU 7305  N   ALA A 895     8081   9563   8575   -876   -418    -17       N  
ATOM   7306  CA  ALA A 895     -41.475 -28.358 -49.404  1.00 70.84           C  
ANISOU 7306  CA  ALA A 895     8212   9842   8864   -978   -437    -83       C  
ATOM   7307  C   ALA A 895     -41.695 -28.325 -50.916  1.00 71.96           C  
ANISOU 7307  C   ALA A 895     8334  10069   8939  -1001   -500   -198       C  
ATOM   7308  O   ALA A 895     -41.597 -27.262 -51.546  1.00 72.21           O  
ANISOU 7308  O   ALA A 895     8393  10190   8853   -921   -542   -191       O  
ATOM   7309  CB  ALA A 895     -42.757 -28.018 -48.668  1.00 71.67           C  
ANISOU 7309  CB  ALA A 895     8216  10053   8960   -968   -438    -21       C  
ATOM   7310  N   SER A 896     -41.985 -29.491 -51.491  1.00 72.54           N  
ANISOU 7310  N   SER A 896     8359  10114   9090  -1110   -510   -300       N  
ATOM   7311  CA  SER A 896     -42.207 -29.612 -52.937  1.00 73.90           C  
ANISOU 7311  CA  SER A 896     8500  10378   9200  -1141   -571   -428       C  
ATOM   7312  C   SER A 896     -43.419 -30.482 -53.276  1.00 74.47           C  
ANISOU 7312  C   SER A 896     8452  10508   9337  -1251   -600   -515       C  
ATOM   7313  O   SER A 896     -43.933 -31.214 -52.424  1.00 74.48           O  
ANISOU 7313  O   SER A 896     8402  10443   9455  -1324   -565   -481       O  
ATOM   7314  CB  SER A 896     -40.954 -30.167 -53.634  1.00 74.71           C  
ANISOU 7314  CB  SER A 896     8684  10387   9317  -1156   -562   -516       C  
ATOM   7315  OG  SER A 896     -40.892 -31.584 -53.542  1.00 74.96           O  
ANISOU 7315  OG  SER A 896     8695  10293   9495  -1261   -541   -596       O  
ATOM   7316  N   LEU A 897     -43.847 -30.402 -54.536  1.00 74.76           N  
ANISOU 7316  N   LEU A 897     8439  10673   9293  -1265   -664   -625       N  
ATOM   7317  CA  LEU A 897     -44.964 -31.191 -55.068  1.00 75.07           C  
ANISOU 7317  CA  LEU A 897     8357  10787   9378  -1372   -703   -734       C  
ATOM   7318  C   LEU A 897     -44.781 -32.703 -54.919  1.00 75.84           C  
ANISOU 7318  C   LEU A 897     8444  10722   9648  -1502   -676   -821       C  
ATOM   7319  O   LEU A 897     -45.757 -33.447 -54.855  1.00 77.01           O  
ANISOU 7319  O   LEU A 897     8491  10884   9885  -1608   -689   -870       O  
ATOM   7320  CB  LEU A 897     -45.193 -30.841 -56.542  1.00 75.75           C  
ANISOU 7320  CB  LEU A 897     8409  11040   9332  -1354   -779   -848       C  
ATOM   7321  CG  LEU A 897     -46.254 -29.813 -56.963  1.00 74.83           C  
ANISOU 7321  CG  LEU A 897     8212  11138   9081  -1290   -839   -817       C  
ATOM   7322  CD1 LEU A 897     -46.323 -28.585 -56.059  1.00 71.98           C  
ANISOU 7322  CD1 LEU A 897     7888  10797   8665  -1172   -820   -650       C  
ATOM   7323  CD2 LEU A 897     -46.012 -29.408 -58.415  1.00 73.94           C  
ANISOU 7323  CD2 LEU A 897     8107  11165   8822  -1251   -903   -905       C  
ATOM   7324  N   PHE A 898     -43.528 -33.145 -54.866  1.00 76.55           N  
ANISOU 7324  N   PHE A 898     8637  10657   9791  -1491   -641   -839       N  
ATOM   7325  CA  PHE A 898     -43.189 -34.557 -54.663  1.00 78.98           C  
ANISOU 7325  CA  PHE A 898     8954  10778  10275  -1596   -615   -911       C  
ATOM   7326  C   PHE A 898     -43.668 -35.151 -53.330  1.00 79.54           C  
ANISOU 7326  C   PHE A 898     8994  10732  10494  -1664   -563   -797       C  
ATOM   7327  O   PHE A 898     -43.777 -36.375 -53.196  1.00 79.87           O  
ANISOU 7327  O   PHE A 898     9013  10636  10699  -1776   -553   -852       O  
ATOM   7328  CB  PHE A 898     -41.677 -34.761 -54.826  1.00 79.49           C  
ANISOU 7328  CB  PHE A 898     9138  10715  10351  -1544   -587   -941       C  
ATOM   7329  CG  PHE A 898     -41.299 -35.586 -56.026  1.00 81.34           C  
ANISOU 7329  CG  PHE A 898     9368  10930  10608  -1592   -626  -1140       C  
ATOM   7330  CD1 PHE A 898     -40.388 -36.630 -55.900  1.00 82.56           C  
ANISOU 7330  CD1 PHE A 898     9582  10890  10899  -1623   -599  -1205       C  
ATOM   7331  CD2 PHE A 898     -41.864 -35.335 -57.274  1.00 82.56           C  
ANISOU 7331  CD2 PHE A 898     9454  11266  10647  -1602   -693  -1267       C  
ATOM   7332  CE1 PHE A 898     -40.036 -37.405 -57.000  1.00 85.05           C  
ANISOU 7332  CE1 PHE A 898     9888  11189  11237  -1659   -637  -1406       C  
ATOM   7333  CE2 PHE A 898     -41.523 -36.107 -58.379  1.00 84.17           C  
ANISOU 7333  CE2 PHE A 898     9646  11469  10864  -1643   -730  -1465       C  
ATOM   7334  CZ  PHE A 898     -40.606 -37.143 -58.241  1.00 85.74           C  
ANISOU 7334  CZ  PHE A 898     9904  11470  11202  -1671   -702  -1541       C  
ATOM   7335  N   ASP A 899     -43.957 -34.283 -52.358  1.00 78.50           N  
ANISOU 7335  N   ASP A 899     8859  10659  10307  -1597   -531   -638       N  
ATOM   7336  CA  ASP A 899     -44.440 -34.703 -51.041  1.00 79.26           C  
ANISOU 7336  CA  ASP A 899     8917  10684  10512  -1650   -478   -510       C  
ATOM   7337  C   ASP A 899     -45.895 -35.212 -51.071  1.00 81.75           C  
ANISOU 7337  C   ASP A 899     9089  11084  10886  -1770   -501   -540       C  
ATOM   7338  O   ASP A 899     -46.734 -34.749 -50.294  1.00 83.23           O  
ANISOU 7338  O   ASP A 899     9205  11374  11045  -1761   -482   -433       O  
ATOM   7339  CB  ASP A 899     -44.303 -33.552 -50.029  1.00 76.98           C  
ANISOU 7339  CB  ASP A 899     8662  10459  10129  -1531   -441   -349       C  
ATOM   7340  CG  ASP A 899     -42.858 -33.109 -49.820  1.00 75.84           C  
ANISOU 7340  CG  ASP A 899     8652  10219   9945  -1428   -412   -307       C  
ATOM   7341  OD1 ASP A 899     -41.962 -33.975 -49.715  1.00 75.43           O  
ANISOU 7341  OD1 ASP A 899     8665   9999   9995  -1462   -384   -330       O  
ATOM   7342  OD2 ASP A 899     -42.618 -31.884 -49.743  1.00 74.48           O  
ANISOU 7342  OD2 ASP A 899     8518  10138   9644  -1312   -418   -251       O  
ATOM   7343  N   MET A 900     -46.189 -36.162 -51.958  1.00 82.99           N  
ANISOU 7343  N   MET A 900     9200  11206  11126  -1881   -542   -692       N  
ATOM   7344  CA  MET A 900     -47.531 -36.755 -52.039  1.00 85.26           C  
ANISOU 7344  CA  MET A 900     9347  11563  11486  -2013   -566   -736       C  
ATOM   7345  C   MET A 900     -47.517 -38.279 -51.931  1.00 87.00           C  
ANISOU 7345  C   MET A 900     9553  11583  11921  -2169   -554   -794       C  
ATOM   7346  O   MET A 900     -46.608 -38.942 -52.428  1.00 87.61           O  
ANISOU 7346  O   MET A 900     9711  11507  12072  -2179   -563   -894       O  
ATOM   7347  CB  MET A 900     -48.252 -36.323 -53.320  1.00 85.59           C  
ANISOU 7347  CB  MET A 900     9307  11805  11408  -2008   -646   -879       C  
ATOM   7348  CG  MET A 900     -49.225 -35.160 -53.143  1.00 85.83           C  
ANISOU 7348  CG  MET A 900     9254  12064  11293  -1933   -665   -801       C  
ATOM   7349  SD  MET A 900     -48.457 -33.528 -53.058  1.00 84.82           S  
ANISOU 7349  SD  MET A 900     9233  12021  10973  -1723   -661   -699       S  
ATOM   7350  CE  MET A 900     -49.904 -32.470 -53.072  1.00 85.70           C  
ANISOU 7350  CE  MET A 900     9211  12399  10954  -1666   -704   -658       C  
TER    7351      MET A 900                                                      
ATOM   7352  P    DC T   3       4.529   0.702 -27.122  1.00 85.65           P  
ANISOU 7352  P    DC T   3    10256  11119  11168    865   -296   -862       P  
ATOM   7353  OP1  DC T   3       4.745   2.142 -26.834  1.00 84.22           O  
ANISOU 7353  OP1  DC T   3    10009  10877  11115    899   -376   -952       O  
ATOM   7354  OP2  DC T   3       5.397  -0.322 -26.484  1.00 85.52           O  
ANISOU 7354  OP2  DC T   3    10263  11172  11061    889   -253   -865       O  
ATOM   7355  O5'  DC T   3       4.543   0.449 -28.709  1.00 81.13           O  
ANISOU 7355  O5'  DC T   3     9730  10474  10622    766   -270   -744       O  
ATOM   7356  C5'  DC T   3       5.767   0.189 -29.414  1.00 72.72           C  
ANISOU 7356  C5'  DC T   3     8689   9366   9574    717   -255   -700       C  
ATOM   7357  C4'  DC T   3       5.626   0.527 -30.898  1.00 66.64           C  
ANISOU 7357  C4'  DC T   3     7930   8528   8863    635   -258   -609       C  
ATOM   7358  O4'  DC T   3       4.909   1.776 -31.100  1.00 68.65           O  
ANISOU 7358  O4'  DC T   3     8137   8725   9223    637   -316   -621       O  
ATOM   7359  C3'  DC T   3       6.921   0.687 -31.688  1.00 56.81           C  
ANISOU 7359  C3'  DC T   3     6686   7231   7668    586   -261   -568       C  
ATOM   7360  O3'  DC T   3       6.705   0.186 -33.011  1.00 39.33           O  
ANISOU 7360  O3'  DC T   3     4504   5017   5424    512   -225   -468       O  
ATOM   7361  C2'  DC T   3       7.175   2.200 -31.657  1.00 61.10           C  
ANISOU 7361  C2'  DC T   3     7163   7693   8359    598   -338   -602       C  
ATOM   7362  C1'  DC T   3       5.828   2.839 -31.284  1.00 67.00           C  
ANISOU 7362  C1'  DC T   3     7881   8438   9140    630   -372   -639       C  
ATOM   7363  N1   DC T   3       5.799   3.702 -30.025  1.00 71.69           N  
ANISOU 7363  N1   DC T   3     8415   9023   9799    711   -431   -765       N  
ATOM   7364  C2   DC T   3       4.580   4.037 -29.376  1.00 74.84           C  
ANISOU 7364  C2   DC T   3     8789   9453  10195    760   -453   -823       C  
ATOM   7365  O2   DC T   3       3.484   3.639 -29.805  1.00 74.45           O  
ANISOU 7365  O2   DC T   3     8768   9430  10091    736   -423   -767       O  
ATOM   7366  N3   DC T   3       4.622   4.812 -28.255  1.00 76.55           N  
ANISOU 7366  N3   DC T   3     8944   9673  10469    838   -510   -950       N  
ATOM   7367  C4   DC T   3       5.792   5.251 -27.772  1.00 77.04           C  
ANISOU 7367  C4   DC T   3     8970   9706  10594    867   -546  -1019       C  
ATOM   7368  N4   DC T   3       5.781   6.008 -26.666  1.00 76.59           N  
ANISOU 7368  N4   DC T   3     8846   9661  10593    948   -605  -1156       N  
ATOM   7369  C5   DC T   3       7.029   4.929 -28.409  1.00 74.97           C  
ANISOU 7369  C5   DC T   3     8737   9407  10341    816   -524   -954       C  
ATOM   7370  C6   DC T   3       6.980   4.168 -29.510  1.00 72.90           C  
ANISOU 7370  C6   DC T   3     8535   9146  10018    741   -467   -829       C  
HETATM 7371  P   2PR T   4       7.259  -1.232 -33.533  1.00 31.35           P  
ANISOU 7371  P   2PR T   4     3548   4054   4310    475   -157   -421       P  
HETATM 7372  OP1 2PR T   4       8.985  -0.834 -33.138  1.00 42.41           O  
ANISOU 7372  OP1 2PR T   4     4929   5421   5765    491   -181   -461       O  
HETATM 7373  OP2 2PR T   4       6.231  -2.336 -32.503  1.00 38.13           O  
ANISOU 7373  OP2 2PR T   4     4437   4989   5063    525   -115   -456       O  
HETATM 7374  O5' 2PR T   4       6.638  -0.882 -35.090  1.00 37.97           O  
ANISOU 7374  O5' 2PR T   4     4379   4872   5176    400   -158   -325       O  
HETATM 7375  C5' 2PR T   4       5.237  -0.879 -35.307  1.00 35.03           C  
ANISOU 7375  C5' 2PR T   4     4010   4513   4785    395   -155   -304       C  
HETATM 7376  C4' 2PR T   4       5.106  -0.351 -36.720  1.00 35.94           C  
ANISOU 7376  C4' 2PR T   4     4105   4609   4941    328   -166   -216       C  
HETATM 7377  O4' 2PR T   4       5.698  -1.268 -37.639  1.00 35.65           O  
ANISOU 7377  O4' 2PR T   4     4095   4615   4837    281   -121   -168       O  
HETATM 7378  C3' 2PR T   4       3.670  -0.209 -37.136  1.00 33.61           C  
ANISOU 7378  C3' 2PR T   4     3807   4323   4639    313   -168   -182       C  
HETATM 7379  O3' 2PR T   4       3.170   1.062 -36.716  1.00 34.05           O  
ANISOU 7379  O3' 2PR T   4     3817   4323   4798    339   -227   -203       O  
HETATM 7380  C2' 2PR T   4       3.781  -0.342 -38.639  1.00 36.52           C  
ANISOU 7380  C2' 2PR T   4     4171   4714   4990    242   -151    -90       C  
HETATM 7381  C1' 2PR T   4       4.887  -1.366 -38.802  1.00 33.41           C  
ANISOU 7381  C1' 2PR T   4     3808   4358   4527    230   -108    -98       C  
HETATM 7382  N9  2PR T   4       4.278  -2.720 -38.848  1.00 34.86           N  
ANISOU 7382  N9  2PR T   4     4037   4598   4609    229    -55   -112       N  
HETATM 7383  C8  2PR T   4       4.317  -3.664 -37.885  1.00 30.12           C  
ANISOU 7383  C8  2PR T   4     3471   4015   3958    269    -25   -169       C  
HETATM 7384  N7  2PR T   4       3.636  -4.749 -38.323  1.00 31.08           N  
ANISOU 7384  N7  2PR T   4     3619   4179   4012    250     16   -156       N  
HETATM 7385  C5  2PR T   4       3.169  -4.478 -39.569  1.00 30.55           C  
ANISOU 7385  C5  2PR T   4     3535   4128   3943    199     12    -99       C  
HETATM 7386  C6  2PR T   4       2.414  -5.193 -40.505  1.00 30.65           C  
ANISOU 7386  C6  2PR T   4     3556   4187   3904    163     39    -72       C  
HETATM 7387  N1  2PR T   4       2.092  -4.629 -41.689  1.00 27.58           N  
ANISOU 7387  N1  2PR T   4     3138   3820   3521    118     26    -11       N  
HETATM 7388  C2  2PR T   4       2.506  -3.367 -41.967  1.00 31.08           C  
ANISOU 7388  C2  2PR T   4     3543   4235   4031    105    -14     33       C  
HETATM 7389  N2  2PR T   4       2.176  -2.804 -43.152  1.00 34.15           N  
ANISOU 7389  N2  2PR T   4     3894   4655   4426     59    -27    108       N  
HETATM 7390  N3  2PR T   4       3.244  -2.649 -41.077  1.00 24.35           N  
ANISOU 7390  N3  2PR T   4     2680   3326   3244    138    -44      6       N  
HETATM 7391  C4  2PR T   4       3.571  -3.188 -39.883  1.00 29.76           C  
ANISOU 7391  C4  2PR T   4     3397   3995   3917    186    -31    -65       C  
ATOM   7392  P    DT T   5       1.602   1.219 -36.511  1.00 31.42           P  
ANISOU 7392  P    DT T   5     3483   3998   4457    356   -234   -210       P  
ATOM   7393  OP1  DT T   5       1.356   2.498 -35.807  1.00 38.96           O  
ANISOU 7393  OP1  DT T   5     4385   4893   5527    398   -300   -263       O  
ATOM   7394  OP2  DT T   5       1.041  -0.043 -35.976  1.00 35.24           O  
ANISOU 7394  OP2  DT T   5     4017   4546   4826    380   -182   -240       O  
ATOM   7395  O5'  DT T   5       1.065   1.312 -38.019  1.00 33.32           O  
ANISOU 7395  O5'  DT T   5     3716   4247   4697    284   -226   -104       O  
ATOM   7396  C5'  DT T   5       1.461   2.318 -38.953  1.00 35.43           C  
ANISOU 7396  C5'  DT T   5     3932   4473   5057    239   -263    -29       C  
ATOM   7397  C4'  DT T   5       0.751   2.062 -40.280  1.00 33.93           C  
ANISOU 7397  C4'  DT T   5     3743   4329   4821    179   -240     66       C  
ATOM   7398  O4'  DT T   5       1.139   0.756 -40.775  1.00 33.66           O  
ANISOU 7398  O4'  DT T   5     3754   4367   4666    155   -180     74       O  
ATOM   7399  C3'  DT T   5      -0.766   1.986 -40.180  1.00 32.19           C  
ANISOU 7399  C3'  DT T   5     3535   4120   4577    189   -237     60       C  
ATOM   7400  O3'  DT T   5      -1.373   3.272 -40.309  1.00 34.72           O  
ANISOU 7400  O3'  DT T   5     3799   4381   5014    186   -294     92       O  
ATOM   7401  C2'  DT T   5      -1.140   1.079 -41.345  1.00 31.24           C  
ANISOU 7401  C2'  DT T   5     3439   4074   4356    137   -189    123       C  
ATOM   7402  C1'  DT T   5       0.042   0.139 -41.429  1.00 29.18           C  
ANISOU 7402  C1'  DT T   5     3208   3853   4027    130   -150    104       C  
ATOM   7403  N1   DT T   5      -0.246  -1.203 -40.856  1.00 28.76           N  
ANISOU 7403  N1   DT T   5     3212   3839   3878    155   -101     42       N  
ATOM   7404  C2   DT T   5      -0.868  -2.111 -41.688  1.00 28.91           C  
ANISOU 7404  C2   DT T   5     3250   3918   3817    122    -63     68       C  
ATOM   7405  O2   DT T   5      -1.185  -1.850 -42.830  1.00 33.86           O  
ANISOU 7405  O2   DT T   5     3851   4576   4438     77    -66    134       O  
ATOM   7406  N3   DT T   5      -1.107  -3.339 -41.138  1.00 27.03           N  
ANISOU 7406  N3   DT T   5     3055   3704   3511    145    -23     16       N  
ATOM   7407  C4   DT T   5      -0.794  -3.747 -39.846  1.00 31.63           C  
ANISOU 7407  C4   DT T   5     3661   4268   4090    198    -14    -48       C  
ATOM   7408  O4   DT T   5      -1.065  -4.884 -39.453  1.00 33.21           O  
ANISOU 7408  O4   DT T   5     3891   4493   4236    213     23    -77       O  
ATOM   7409  C5   DT T   5      -0.147  -2.754 -39.007  1.00 28.39           C  
ANISOU 7409  C5   DT T   5     3230   3808   3748    233    -53    -77       C  
ATOM   7410  C7   DT T   5       0.228  -3.087 -37.582  1.00 22.32           C  
ANISOU 7410  C7   DT T   5     2477   3034   2970    295    -48   -149       C  
ATOM   7411  C6   DT T   5       0.094  -1.537 -39.547  1.00 25.79           C  
ANISOU 7411  C6   DT T   5     2859   3444   3496    211    -96    -36       C  
ATOM   7412  P    DC T   6      -2.948   3.414 -40.043  1.00 34.48           P  
ANISOU 7412  P    DC T   6     3773   4348   4980    204   -302     76       P  
ATOM   7413  OP1  DC T   6      -3.233   4.840 -39.830  1.00 33.11           O  
ANISOU 7413  OP1  DC T   6     3533   4093   4954    217   -372     78       O  
ATOM   7414  OP2  DC T   6      -3.351   2.409 -39.037  1.00 35.72           O  
ANISOU 7414  OP2  DC T   6     3985   4545   5043    252   -264     -9       O  
ATOM   7415  O5'  DC T   6      -3.659   2.896 -41.376  1.00 35.37           O  
ANISOU 7415  O5'  DC T   6     3897   4523   5019    143   -267    169       O  
ATOM   7416  C5'  DC T   6      -3.406   3.365 -42.706  1.00 35.41           C  
ANISOU 7416  C5'  DC T   6     3858   4544   5051     82   -278    279       C  
ATOM   7417  C4'  DC T   6      -4.254   2.536 -43.664  1.00 30.51           C  
ANISOU 7417  C4'  DC T   6     3263   4007   4324     44   -234    326       C  
ATOM   7418  O4'  DC T   6      -3.982   1.116 -43.483  1.00 33.52           O  
ANISOU 7418  O4'  DC T   6     3705   4446   4584     53   -177    270       O  
ATOM   7419  C3'  DC T   6      -5.763   2.658 -43.491  1.00 33.88           C  
ANISOU 7419  C3'  DC T   6     3696   4425   4752     55   -242    319       C  
ATOM   7420  O3'  DC T   6      -6.387   2.552 -44.771  1.00 33.29           O  
ANISOU 7420  O3'  DC T   6     3603   4410   4634      3   -229    406       O  
ATOM   7421  C2'  DC T   6      -6.119   1.474 -42.587  1.00 30.88           C  
ANISOU 7421  C2'  DC T   6     3382   4070   4280     96   -199    226       C  
ATOM   7422  C1'  DC T   6      -5.162   0.415 -43.125  1.00 30.00           C  
ANISOU 7422  C1'  DC T   6     3299   4021   4081     72   -153    230       C  
ATOM   7423  N1   DC T   6      -4.870  -0.681 -42.149  1.00 30.04           N  
ANISOU 7423  N1   DC T   6     3356   4036   4023    112   -116    145       N  
ATOM   7424  C2   DC T   6      -5.148  -2.021 -42.501  1.00 32.56           C  
ANISOU 7424  C2   DC T   6     3712   4413   4245     99    -66    132       C  
ATOM   7425  O2   DC T   6      -5.619  -2.296 -43.618  1.00 34.24           O  
ANISOU 7425  O2   DC T   6     3916   4676   4418     56    -53    179       O  
ATOM   7426  N3   DC T   6      -4.872  -3.006 -41.598  1.00 29.47           N  
ANISOU 7426  N3   DC T   6     3359   4026   3811    135    -36     67       N  
ATOM   7427  C4   DC T   6      -4.365  -2.705 -40.389  1.00 27.89           C  
ANISOU 7427  C4   DC T   6     3163   3788   3646    185    -50     16       C  
ATOM   7428  N4   DC T   6      -4.136  -3.719 -39.542  1.00 26.17           N  
ANISOU 7428  N4   DC T   6     2976   3585   3382    219    -18    -34       N  
ATOM   7429  C5   DC T   6      -4.083  -1.353 -40.005  1.00 24.53           C  
ANISOU 7429  C5   DC T   6     2701   3308   3310    202   -101     14       C  
ATOM   7430  C6   DC T   6      -4.344  -0.390 -40.912  1.00 27.67           C  
ANISOU 7430  C6   DC T   6     3060   3689   3765    164   -134     79       C  
ATOM   7431  P    DG T   7      -7.943   2.822 -44.999  1.00 36.44           P  
ANISOU 7431  P    DG T   7     3995   4810   5041     -3   -240    432       P  
ATOM   7432  OP1  DG T   7      -8.097   3.521 -46.293  1.00 40.08           O  
ANISOU 7432  OP1  DG T   7     4394   5301   5532    -58   -260    552       O  
ATOM   7433  OP2  DG T   7      -8.499   3.439 -43.776  1.00 38.09           O  
ANISOU 7433  OP2  DG T   7     4204   4938   5330     50   -275    364       O  
ATOM   7434  O5'  DG T   7      -8.528   1.349 -45.166  1.00 36.15           O  
ANISOU 7434  O5'  DG T   7     4018   4849   4868     -5   -181    392       O  
ATOM   7435  C5'  DG T   7      -8.007   0.490 -46.175  1.00 36.56           C  
ANISOU 7435  C5'  DG T   7     4076   4988   4828    -44   -143    419       C  
ATOM   7436  C4'  DG T   7      -8.949  -0.674 -46.414  1.00 36.45           C  
ANISOU 7436  C4'  DG T   7     4100   5029   4719    -47   -102    387       C  
ATOM   7437  O4'  DG T   7      -8.688  -1.742 -45.465  1.00 36.58           O  
ANISOU 7437  O4'  DG T   7     4171   5035   4694     -9    -70    297       O  
ATOM   7438  C3'  DG T   7     -10.426  -0.344 -46.250  1.00 39.98           C  
ANISOU 7438  C3'  DG T   7     4548   5454   5189    -39   -117    396       C  
ATOM   7439  O3'  DG T   7     -11.138  -1.127 -47.199  1.00 39.12           O  
ANISOU 7439  O3'  DG T   7     4442   5422   4999    -70    -89    413       O  
ATOM   7440  C2'  DG T   7     -10.728  -0.729 -44.792  1.00 38.98           C  
ANISOU 7440  C2'  DG T   7     4465   5273   5071     18   -110    308       C  
ATOM   7441  C1'  DG T   7      -9.783  -1.905 -44.568  1.00 36.56           C  
ANISOU 7441  C1'  DG T   7     4195   4997   4700     27    -69    256       C  
ATOM   7442  N9   DG T   7      -9.234  -2.036 -43.214  1.00 36.78           N  
ANISOU 7442  N9   DG T   7     4248   4979   4749     79    -68    188       N  
ATOM   7443  C8   DG T   7      -8.661  -1.056 -42.430  1.00 36.56           C  
ANISOU 7443  C8   DG T   7     4201   4894   4796    110   -104    170       C  
ATOM   7444  N7   DG T   7      -8.242  -1.489 -41.269  1.00 36.18           N  
ANISOU 7444  N7   DG T   7     4178   4832   4738    158    -93    103       N  
ATOM   7445  C5   DG T   7      -8.550  -2.842 -41.287  1.00 34.45           C  
ANISOU 7445  C5   DG T   7     3994   4656   4438    156    -45     85       C  
ATOM   7446  C6   DG T   7      -8.348  -3.836 -40.309  1.00 31.49           C  
ANISOU 7446  C6   DG T   7     3650   4291   4024    196    -14     32       C  
ATOM   7447  O6   DG T   7      -7.829  -3.686 -39.204  1.00 37.79           O  
ANISOU 7447  O6   DG T   7     4450   5071   4837    242    -21    -12       O  
ATOM   7448  N1   DG T   7      -8.810  -5.094 -40.705  1.00 32.67           N  
ANISOU 7448  N1   DG T   7     3820   4477   4115    178     26     35       N  
ATOM   7449  C2   DG T   7      -9.415  -5.339 -41.921  1.00 34.01           C  
ANISOU 7449  C2   DG T   7     3984   4677   4262    130     33     72       C  
ATOM   7450  N2   DG T   7      -9.820  -6.593 -42.193  1.00 33.39           N  
ANISOU 7450  N2   DG T   7     3920   4627   4140    120     68     60       N  
ATOM   7451  N3   DG T   7      -9.614  -4.404 -42.837  1.00 37.47           N  
ANISOU 7451  N3   DG T   7     4396   5120   4723     95      6    121       N  
ATOM   7452  C4   DG T   7      -9.163  -3.188 -42.465  1.00 34.22           C  
ANISOU 7452  C4   DG T   7     3962   4666   4374    109    -32    130       C  
ATOM   7453  P    DC T   8     -12.726  -1.063 -47.362  1.00 36.05           P  
ANISOU 7453  P    DC T   8     4055   5036   4607    -74    -94    430       P  
ATOM   7454  OP1  DC T   8     -12.973  -1.602 -48.721  1.00 38.61           O  
ANISOU 7454  OP1  DC T   8     4358   5458   4854   -118    -75    468       O  
ATOM   7455  OP2  DC T   8     -13.225   0.272 -46.970  1.00 34.86           O  
ANISOU 7455  OP2  DC T   8     3874   4816   4555    -63   -141    467       O  
ATOM   7456  O5'  DC T   8     -13.232  -2.085 -46.243  1.00 36.28           O  
ANISOU 7456  O5'  DC T   8     4140   5037   4607    -29    -66    341       O  
ATOM   7457  C5'  DC T   8     -13.087  -3.486 -46.423  1.00 32.53           C  
ANISOU 7457  C5'  DC T   8     3693   4608   4057    -32    -23    295       C  
ATOM   7458  C4'  DC T   8     -13.757  -4.183 -45.261  1.00 31.35           C  
ANISOU 7458  C4'  DC T   8     3582   4421   3907     11     -6    237       C  
ATOM   7459  O4'  DC T   8     -12.909  -4.054 -44.095  1.00 31.26           O  
ANISOU 7459  O4'  DC T   8     3587   4364   3925     53     -8    198       O  
ATOM   7460  C3'  DC T   8     -15.107  -3.579 -44.886  1.00 33.21           C  
ANISOU 7460  C3'  DC T   8     3814   4627   4176     27    -26    255       C  
ATOM   7461  O3'  DC T   8     -16.053  -4.637 -44.816  1.00 35.22           O  
ANISOU 7461  O3'  DC T   8     4089   4900   4392     31      2    232       O  
ATOM   7462  C2'  DC T   8     -14.871  -2.913 -43.532  1.00 31.84           C  
ANISOU 7462  C2'  DC T   8     3646   4394   4057     78    -46    222       C  
ATOM   7463  C1'  DC T   8     -13.743  -3.788 -42.992  1.00 32.58           C  
ANISOU 7463  C1'  DC T   8     3764   4493   4121     97    -18    176       C  
ATOM   7464  N1   DC T   8     -12.926  -3.261 -41.839  1.00 30.70           N  
ANISOU 7464  N1   DC T   8     3526   4215   3921    143    -35    137       N  
ATOM   7465  C2   DC T   8     -12.468  -4.197 -40.891  1.00 31.78           C  
ANISOU 7465  C2   DC T   8     3689   4359   4028    180     -5     89       C  
ATOM   7466  O2   DC T   8     -12.727  -5.403 -41.035  1.00 32.14           O  
ANISOU 7466  O2   DC T   8     3753   4431   4028    172     31     84       O  
ATOM   7467  N3   DC T   8     -11.733  -3.763 -39.841  1.00 29.63           N  
ANISOU 7467  N3   DC T   8     3413   4063   3781    224    -20     50       N  
ATOM   7468  C4   DC T   8     -11.465  -2.456 -39.702  1.00 36.30           C  
ANISOU 7468  C4   DC T   8     4230   4871   4691    233    -64     49       C  
ATOM   7469  N4   DC T   8     -10.726  -2.092 -38.643  1.00 33.37           N  
ANISOU 7469  N4   DC T   8     3852   4480   4345    281    -80     -2       N  
ATOM   7470  C5   DC T   8     -11.921  -1.480 -40.657  1.00 32.91           C  
ANISOU 7470  C5   DC T   8     3772   4423   4310    194    -97    102       C  
ATOM   7471  C6   DC T   8     -12.650  -1.925 -41.701  1.00 27.02           C  
ANISOU 7471  C6   DC T   8     3031   3709   3526    150    -79    149       C  
ATOM   7472  P    DC T   9     -17.610  -4.406 -45.112  1.00 32.37           P  
ANISOU 7472  P    DC T   9     3720   4543   4036     23     -8    261       P  
ATOM   7473  OP1  DC T   9     -17.848  -4.582 -46.561  1.00 35.93           O  
ANISOU 7473  OP1  DC T   9     4148   5053   4449    -29     -5    296       O  
ATOM   7474  OP2  DC T   9     -18.074  -3.157 -44.475  1.00 33.86           O  
ANISOU 7474  OP2  DC T   9     3896   4685   4286     47    -44    278       O  
ATOM   7475  O5'  DC T   9     -18.175  -5.680 -44.340  1.00 29.99           O  
ANISOU 7475  O5'  DC T   9     3447   4237   3712     52     26    216       O  
ATOM   7476  C5'  DC T   9     -17.730  -6.985 -44.724  1.00 30.76           C  
ANISOU 7476  C5'  DC T   9     3552   4363   3772     38     57    186       C  
ATOM   7477  C4'  DC T   9     -17.334  -7.791 -43.496  1.00 34.37           C  
ANISOU 7477  C4'  DC T   9     4030   4793   4236     81     80    149       C  
ATOM   7478  O4'  DC T   9     -16.266  -7.151 -42.765  1.00 35.51           O  
ANISOU 7478  O4'  DC T   9     4179   4916   4396    107     69    137       O  
ATOM   7479  C3'  DC T   9     -18.424  -7.878 -42.450  1.00 36.52           C  
ANISOU 7479  C3'  DC T   9     4308   5044   4524    121     83    153       C  
ATOM   7480  O3'  DC T   9     -19.365  -8.866 -42.857  1.00 36.94           O  
ANISOU 7480  O3'  DC T   9     4357   5109   4571    106    101    156       O  
ATOM   7481  C2'  DC T   9     -17.641  -8.257 -41.192  1.00 36.15           C  
ANISOU 7481  C2'  DC T   9     4270   4983   4481    167     98    128       C  
ATOM   7482  C1'  DC T   9     -16.303  -7.570 -41.404  1.00 35.61           C  
ANISOU 7482  C1'  DC T   9     4203   4911   4416    159     83    115       C  
ATOM   7483  N1   DC T   9     -16.010  -6.390 -40.492  1.00 35.17           N  
ANISOU 7483  N1   DC T   9     4143   4834   4387    198     55    106       N  
ATOM   7484  C2   DC T   9     -15.515  -6.586 -39.192  1.00 35.88           C  
ANISOU 7484  C2   DC T   9     4236   4922   4475    250     63     76       C  
ATOM   7485  O2   DC T   9     -15.336  -7.727 -38.753  1.00 41.17           O  
ANISOU 7485  O2   DC T   9     4913   5605   5124    264     95     70       O  
ATOM   7486  N3   DC T   9     -15.243  -5.502 -38.420  1.00 37.33           N  
ANISOU 7486  N3   DC T   9     4407   5092   4685    288     33     53       N  
ATOM   7487  C4   DC T   9     -15.435  -4.262 -38.890  1.00 36.68           C  
ANISOU 7487  C4   DC T   9     4308   4985   4644    273     -6     63       C  
ATOM   7488  N4   DC T   9     -15.144  -3.243 -38.076  1.00 40.21           N  
ANISOU 7488  N4   DC T   9     4734   5411   5131    314    -40     29       N  
ATOM   7489  C5   DC T   9     -15.937  -4.025 -40.203  1.00 34.93           C  
ANISOU 7489  C5   DC T   9     4081   4760   4429    217    -14    109       C  
ATOM   7490  C6   DC T   9     -16.202  -5.110 -40.956  1.00 36.62           C  
ANISOU 7490  C6   DC T   9     4310   5002   4602    182     18    126       C  
ATOM   7491  P    DG T  10     -20.827  -8.854 -42.225  1.00 39.86           P  
ANISOU 7491  P    DG T  10     4723   5467   4953    131    101    178       P  
ATOM   7492  OP1  DG T  10     -21.627  -9.888 -42.920  1.00 38.16           O  
ANISOU 7492  OP1  DG T  10     4499   5261   4738    104    116    179       O  
ATOM   7493  OP2  DG T  10     -21.298  -7.447 -42.161  1.00 42.42           O  
ANISOU 7493  OP2  DG T  10     5043   5785   5289    137     69    198       O  
ATOM   7494  O5'  DG T  10     -20.545  -9.328 -40.720  1.00 40.09           O  
ANISOU 7494  O5'  DG T  10     4756   5487   4989    186    119    169       O  
ATOM   7495  C5'  DG T  10     -20.140 -10.663 -40.433  1.00 38.31           C  
ANISOU 7495  C5'  DG T  10     4527   5259   4770    192    148    160       C  
ATOM   7496  C4'  DG T  10     -20.252 -10.893 -38.940  1.00 38.71           C  
ANISOU 7496  C4'  DG T  10     4570   5316   4822    250    162    174       C  
ATOM   7497  O4'  DG T  10     -19.373  -9.974 -38.249  1.00 40.86           O  
ANISOU 7497  O4'  DG T  10     4848   5595   5080    281    147    153       O  
ATOM   7498  C3'  DG T  10     -21.640 -10.656 -38.358  1.00 41.31           C  
ANISOU 7498  C3'  DG T  10     4886   5657   5152    277    159    205       C  
ATOM   7499  O3'  DG T  10     -21.881 -11.663 -37.373  1.00 42.31           O  
ANISOU 7499  O3'  DG T  10     4991   5797   5287    311    185    234       O  
ATOM   7500  C2'  DG T  10     -21.563  -9.239 -37.780  1.00 37.13           C  
ANISOU 7500  C2'  DG T  10     4359   5140   4609    309    131    189       C  
ATOM   7501  C1'  DG T  10     -20.092  -9.113 -37.396  1.00 36.77           C  
ANISOU 7501  C1'  DG T  10     4321   5094   4556    324    131    158       C  
ATOM   7502  N9   DG T  10     -19.561  -7.750 -37.518  1.00 35.84           N  
ANISOU 7502  N9   DG T  10     4207   4965   4446    326     97    130       N  
ATOM   7503  C8   DG T  10     -19.702  -6.896 -38.582  1.00 32.22           C  
ANISOU 7503  C8   DG T  10     3752   4485   4005    284     70    134       C  
ATOM   7504  N7   DG T  10     -19.127  -5.736 -38.394  1.00 36.38           N  
ANISOU 7504  N7   DG T  10     4273   4997   4554    297     38    113       N  
ATOM   7505  C5   DG T  10     -18.575  -5.816 -37.119  1.00 34.88           C  
ANISOU 7505  C5   DG T  10     4075   4824   4353    353     44     80       C  
ATOM   7506  C6   DG T  10     -17.835  -4.867 -36.361  1.00 36.10           C  
ANISOU 7506  C6   DG T  10     4216   4974   4527    394     15     37       C  
ATOM   7507  O6   DG T  10     -17.502  -3.719 -36.679  1.00 35.18           O  
ANISOU 7507  O6   DG T  10     4088   4825   4455    385    -23     21       O  
ATOM   7508  N1   DG T  10     -17.459  -5.353 -35.108  1.00 34.52           N  
ANISOU 7508  N1   DG T  10     4006   4813   4295    450     33     11       N  
ATOM   7509  C2   DG T  10     -17.774  -6.607 -34.638  1.00 36.55           C  
ANISOU 7509  C2   DG T  10     4266   5107   4515    464     73     40       C  
ATOM   7510  N2   DG T  10     -17.347  -6.923 -33.398  1.00 29.14           N  
ANISOU 7510  N2   DG T  10     3309   4217   3548    522     86     22       N  
ATOM   7511  N3   DG T  10     -18.473  -7.496 -35.344  1.00 36.48           N  
ANISOU 7511  N3   DG T  10     4267   5090   4503    425     98     84       N  
ATOM   7512  C4   DG T  10     -18.837  -7.048 -36.569  1.00 33.74           C  
ANISOU 7512  C4   DG T  10     3932   4708   4178    372     81     96       C  
ATOM   7513  P    DC T  11     -23.224 -11.728 -36.520  1.00 42.56           P  
ANISOU 7513  P    DC T  11     4998   5856   5317    349    191    278       P  
ATOM   7514  OP1  DC T  11     -23.488 -13.167 -36.294  1.00 46.30           O  
ANISOU 7514  OP1  DC T  11     5445   6323   5826    348    219    320       O  
ATOM   7515  OP2  DC T  11     -24.267 -10.885 -37.162  1.00 44.85           O  
ANISOU 7515  OP2  DC T  11     5295   6139   5605    329    168    276       O  
ATOM   7516  O5'  DC T  11     -22.805 -11.046 -35.134  1.00 41.91           O  
ANISOU 7516  O5'  DC T  11     4902   5822   5198    415    187    268       O  
ATOM   7517  C5'  DC T  11     -21.900 -11.717 -34.248  1.00 42.59           C  
ANISOU 7517  C5'  DC T  11     4974   5934   5276    448    208    277       C  
ATOM   7518  C4'  DC T  11     -21.846 -11.037 -32.891  1.00 46.14           C  
ANISOU 7518  C4'  DC T  11     5398   6451   5681    518    202    268       C  
ATOM   7519  O4'  DC T  11     -21.162  -9.767 -33.008  1.00 47.60           O  
ANISOU 7519  O4'  DC T  11     5603   6627   5855    524    170    202       O  
ATOM   7520  C3'  DC T  11     -23.201 -10.738 -32.252  1.00 47.98           C  
ANISOU 7520  C3'  DC T  11     5602   6735   5895    555    200    296       C  
ATOM   7521  O3'  DC T  11     -23.169 -11.225 -30.908  1.00 51.33           O  
ANISOU 7521  O3'  DC T  11     5980   7238   6283    617    221    332       O  
ATOM   7522  C2'  DC T  11     -23.356  -9.223 -32.366  1.00 45.71           C  
ANISOU 7522  C2'  DC T  11     5326   6444   5597    567    161    233       C  
ATOM   7523  C1'  DC T  11     -21.921  -8.710 -32.449  1.00 44.21           C  
ANISOU 7523  C1'  DC T  11     5156   6234   5409    564    145    178       C  
ATOM   7524  N1   DC T  11     -21.688  -7.480 -33.315  1.00 41.84           N  
ANISOU 7524  N1   DC T  11     4879   5879   5137    533    106    129       N  
ATOM   7525  C2   DC T  11     -21.014  -6.342 -32.813  1.00 42.16           C  
ANISOU 7525  C2   DC T  11     4911   5927   5183    568     73     67       C  
ATOM   7526  O2   DC T  11     -20.605  -6.311 -31.646  1.00 42.77           O  
ANISOU 7526  O2   DC T  11     4961   6062   5228    629     75     39       O  
ATOM   7527  N3   DC T  11     -20.816  -5.268 -33.628  1.00 42.50           N  
ANISOU 7527  N3   DC T  11     4965   5913   5269    536     35     38       N  
ATOM   7528  C4   DC T  11     -21.249  -5.286 -34.890  1.00 41.00           C  
ANISOU 7528  C4   DC T  11     4797   5676   5104    472     33     72       C  
ATOM   7529  N4   DC T  11     -21.022  -4.201 -35.640  1.00 39.78           N  
ANISOU 7529  N4   DC T  11     4644   5475   4994    443     -4     57       N  
ATOM   7530  C5   DC T  11     -21.933  -6.423 -35.425  1.00 39.25           C  
ANISOU 7530  C5   DC T  11     4588   5456   4867    438     67    125       C  
ATOM   7531  C6   DC T  11     -22.116  -7.481 -34.617  1.00 41.09           C  
ANISOU 7531  C6   DC T  11     4809   5732   5072    469    101    149       C  
ATOM   7532  P    DC T  12     -24.402 -11.143 -29.889  1.00 52.50           P  
ANISOU 7532  P    DC T  12     6078   7475   6395    674    227    373       P  
ATOM   7533  OP1  DC T  12     -24.101 -12.111 -28.808  1.00 52.50           O  
ANISOU 7533  OP1  DC T  12     6029   7548   6372    717    259    437       O  
ATOM   7534  OP2  DC T  12     -25.680 -11.187 -30.625  1.00 52.84           O  
ANISOU 7534  OP2  DC T  12     6129   7479   6468    639    224    401       O  
ATOM   7535  O5'  DC T  12     -24.280  -9.657 -29.308  1.00 51.88           O  
ANISOU 7535  O5'  DC T  12     5994   7444   6274    725    192    288       O  
ATOM   7536  C5'  DC T  12     -23.100  -9.263 -28.627  1.00 47.64           C  
ANISOU 7536  C5'  DC T  12     5449   6944   5708    764    183    235       C  
ATOM   7537  C4'  DC T  12     -23.207  -7.807 -28.227  1.00 48.41           C  
ANISOU 7537  C4'  DC T  12     5533   7071   5788    808    141    145       C  
ATOM   7538  O4'  DC T  12     -22.828  -6.969 -29.340  1.00 47.16           O  
ANISOU 7538  O4'  DC T  12     5422   6812   5686    755    108     94       O  
ATOM   7539  C3'  DC T  12     -24.611  -7.375 -27.816  1.00 47.67           C  
ANISOU 7539  C3'  DC T  12     5405   7034   5674    844    132    151       C  
ATOM   7540  O3'  DC T  12     -24.619  -7.233 -26.401  1.00 45.22           O  
ANISOU 7540  O3'  DC T  12     5032   6854   5295    930    134    130       O  
ATOM   7541  C2'  DC T  12     -24.845  -6.060 -28.553  1.00 47.63           C  
ANISOU 7541  C2'  DC T  12     5424   6957   5716    821     85     78       C  
ATOM   7542  C1'  DC T  12     -23.520  -5.745 -29.235  1.00 46.27           C  
ANISOU 7542  C1'  DC T  12     5292   6704   5584    781     69     37       C  
ATOM   7543  N1   DC T  12     -23.668  -5.164 -30.610  1.00 46.59           N  
ANISOU 7543  N1   DC T  12     5374   6638   5689    710     44     32       N  
ATOM   7544  C2   DC T  12     -23.174  -3.880 -30.889  1.00 47.00           C  
ANISOU 7544  C2   DC T  12     5427   6641   5788    708     -3    -38       C  
ATOM   7545  O2   DC T  12     -22.619  -3.236 -29.988  1.00 47.33           O  
ANISOU 7545  O2   DC T  12     5437   6723   5823    767    -27   -108       O  
ATOM   7546  N3   DC T  12     -23.316  -3.377 -32.149  1.00 45.50           N  
ANISOU 7546  N3   DC T  12     5267   6366   5656    644    -24    -25       N  
ATOM   7547  C4   DC T  12     -23.919  -4.099 -33.103  1.00 46.47           C  
ANISOU 7547  C4   DC T  12     5418   6459   5781    585      1     42       C  
ATOM   7548  N4   DC T  12     -24.037  -3.567 -34.328  1.00 47.18           N  
ANISOU 7548  N4   DC T  12     5528   6481   5917    525    -21     56       N  
ATOM   7549  C5   DC T  12     -24.434  -5.406 -32.840  1.00 47.28           C  
ANISOU 7549  C5   DC T  12     5522   6603   5841    587     46    100       C  
ATOM   7550  C6   DC T  12     -24.283  -5.891 -31.597  1.00 47.88           C  
ANISOU 7550  C6   DC T  12     5568   6756   5870    648     66     99       C  
ATOM   7551  P    DG T  13     -25.862  -6.692 -25.559  1.00 43.60           P  
ANISOU 7551  P    DG T  13     4769   6753   5044    996    123    115       P  
ATOM   7552  OP1  DG T  13     -25.651  -7.139 -24.160  1.00 44.65           O  
ANISOU 7552  OP1  DG T  13     4834   7039   5094   1075    145    134       O  
ATOM   7553  OP2  DG T  13     -27.126  -7.030 -26.258  1.00 44.80           O  
ANISOU 7553  OP2  DG T  13     4936   6860   5225    952    135    182       O  
ATOM   7554  O5'  DG T  13     -25.670  -5.105 -25.632  1.00 45.31           O  
ANISOU 7554  O5'  DG T  13     4986   6939   5291   1018     64    -16       O  
ATOM   7555  C5'  DG T  13     -24.579  -4.465 -24.953  1.00 44.31           C  
ANISOU 7555  C5'  DG T  13     4837   6851   5149   1068     38   -109       C  
ATOM   7556  C4'  DG T  13     -24.748  -2.951 -24.899  1.00 43.83           C  
ANISOU 7556  C4'  DG T  13     4754   6768   5131   1099    -23   -231       C  
ATOM   7557  O4'  DG T  13     -24.624  -2.416 -26.239  1.00 43.85           O  
ANISOU 7557  O4'  DG T  13     4815   6618   5229   1020    -48   -234       O  
ATOM   7558  C3'  DG T  13     -26.079  -2.427 -24.356  1.00 45.99           C  
ANISOU 7558  C3'  DG T  13     4975   7119   5379   1151    -39   -259       C  
ATOM   7559  O3'  DG T  13     -25.840  -1.275 -23.535  1.00 47.31           O  
ANISOU 7559  O3'  DG T  13     5083   7345   5548   1228    -90   -395       O  
ATOM   7560  C2'  DG T  13     -26.900  -2.117 -25.611  1.00 45.77           C  
ANISOU 7560  C2'  DG T  13     4994   6966   5429   1077    -52   -225       C  
ATOM   7561  C1'  DG T  13     -25.815  -1.754 -26.623  1.00 44.32           C  
ANISOU 7561  C1'  DG T  13     4867   6648   5326   1011    -73   -244       C  
ATOM   7562  N9   DG T  13     -26.035  -2.132 -28.017  1.00 45.03           N  
ANISOU 7562  N9   DG T  13     5020   6623   5467    917    -59   -165       N  
ATOM   7563  C8   DG T  13     -26.498  -3.323 -28.531  1.00 44.25           C  
ANISOU 7563  C8   DG T  13     4954   6515   5345    869    -11    -61       C  
ATOM   7564  N7   DG T  13     -26.560  -3.348 -29.839  1.00 41.14           N  
ANISOU 7564  N7   DG T  13     4609   6017   5006    790    -13    -23       N  
ATOM   7565  C5   DG T  13     -26.100  -2.092 -30.212  1.00 43.10           C  
ANISOU 7565  C5   DG T  13     4856   6201   5318    783    -64    -94       C  
ATOM   7566  C6   DG T  13     -25.935  -1.518 -31.493  1.00 40.59           C  
ANISOU 7566  C6   DG T  13     4571   5777   5073    713    -89    -83       C  
ATOM   7567  O6   DG T  13     -26.175  -2.035 -32.580  1.00 41.76           O  
ANISOU 7567  O6   DG T  13     4758   5876   5233    645    -70    -17       O  
ATOM   7568  N1   DG T  13     -25.454  -0.209 -31.441  1.00 43.37           N  
ANISOU 7568  N1   DG T  13     4899   6087   5493    730   -144   -159       N  
ATOM   7569  C2   DG T  13     -25.156   0.470 -30.276  1.00 44.79           C  
ANISOU 7569  C2   DG T  13     5029   6320   5672    809   -175   -252       C  
ATOM   7570  N2   DG T  13     -24.693   1.722 -30.400  1.00 44.24           N  
ANISOU 7570  N2   DG T  13     4932   6186   5690    815   -233   -322       N  
ATOM   7571  N3   DG T  13     -25.298  -0.053 -29.066  1.00 44.25           N  
ANISOU 7571  N3   DG T  13     4929   6362   5521    878   -151   -274       N  
ATOM   7572  C4   DG T  13     -25.775  -1.330 -29.107  1.00 44.92           C  
ANISOU 7572  C4   DG T  13     5037   6491   5539    859    -94   -184       C  
ATOM   7573  P    DC T  14     -27.029  -0.490 -22.792  1.00 46.80           P  
ANISOU 7573  P    DC T  14     4945   7376   5459   1302   -120   -468       P  
ATOM   7574  OP1  DC T  14     -26.469   0.212 -21.620  1.00 48.82           O  
ANISOU 7574  OP1  DC T  14     5126   7744   5679   1398   -157   -601       O  
ATOM   7575  OP2  DC T  14     -28.172  -1.411 -22.610  1.00 48.15           O  
ANISOU 7575  OP2  DC T  14     5107   7627   5562   1303    -72   -359       O  
ATOM   7576  O5'  DC T  14     -27.450   0.598 -23.881  1.00 49.11           O  
ANISOU 7576  O5'  DC T  14     5270   7514   5876   1248   -171   -512       O  
ATOM   7577  C5'  DC T  14     -26.546   1.562 -24.393  1.00 46.57           C  
ANISOU 7577  C5'  DC T  14     4962   7076   5656   1224   -223   -592       C  
ATOM   7578  C4'  DC T  14     -27.179   2.257 -25.587  1.00 50.28           C  
ANISOU 7578  C4'  DC T  14     5464   7404   6235   1156   -254   -574       C  
ATOM   7579  O4'  DC T  14     -27.353   1.315 -26.672  1.00 49.62           O  
ANISOU 7579  O4'  DC T  14     5455   7250   6146   1066   -207   -440       O  
ATOM   7580  C3'  DC T  14     -28.574   2.844 -25.360  1.00 52.49           C  
ANISOU 7580  C3'  DC T  14     5701   7718   6526   1190   -278   -607       C  
ATOM   7581  O3'  DC T  14     -28.490   4.254 -25.484  1.00 56.57           O  
ANISOU 7581  O3'  DC T  14     6178   8157   7159   1206   -352   -718       O  
ATOM   7582  C2'  DC T  14     -29.437   2.252 -26.477  1.00 51.15           C  
ANISOU 7582  C2'  DC T  14     5592   7475   6368   1106   -244   -480       C  
ATOM   7583  C1'  DC T  14     -28.388   1.817 -27.493  1.00 50.12           C  
ANISOU 7583  C1'  DC T  14     5531   7240   6274   1024   -227   -415       C  
ATOM   7584  N1   DC T  14     -28.766   0.731 -28.477  1.00 49.34           N  
ANISOU 7584  N1   DC T  14     5497   7097   6152    944   -175   -284       N  
ATOM   7585  C2   DC T  14     -28.617   0.935 -29.862  1.00 47.43           C  
ANISOU 7585  C2   DC T  14     5305   6731   5986    857   -185   -236       C  
ATOM   7586  O2   DC T  14     -28.193   2.015 -30.293  1.00 48.37           O  
ANISOU 7586  O2   DC T  14     5414   6770   6195    842   -236   -285       O  
ATOM   7587  N3   DC T  14     -28.942  -0.077 -30.709  1.00 46.83           N  
ANISOU 7587  N3   DC T  14     5279   6629   5884    791   -141   -133       N  
ATOM   7588  C4   DC T  14     -29.396  -1.244 -30.231  1.00 49.03           C  
ANISOU 7588  C4   DC T  14     5560   6985   6085    807    -90    -75       C  
ATOM   7589  N4   DC T  14     -29.713  -2.210 -31.104  1.00 46.70           N  
ANISOU 7589  N4   DC T  14     5307   6653   5783    742    -53     15       N  
ATOM   7590  C5   DC T  14     -29.552  -1.474 -28.830  1.00 48.49           C  
ANISOU 7590  C5   DC T  14     5440   7040   5944    891    -77   -106       C  
ATOM   7591  C6   DC T  14     -29.223  -0.473 -28.007  1.00 49.96           C  
ANISOU 7591  C6   DC T  14     5577   7265   6139    958   -119   -211       C  
ATOM   7592  P    DG T  15     -29.488   5.242 -24.723  1.00 59.74           P  
ANISOU 7592  P    DG T  15     6495   8620   7583   1286   -403   -834       P  
ATOM   7593  OP1  DG T  15     -28.648   6.267 -24.061  1.00 56.96           O  
ANISOU 7593  OP1  DG T  15     6078   8269   7297   1349   -467   -987       O  
ATOM   7594  OP2  DG T  15     -30.493   4.458 -23.968  1.00 57.18           O  
ANISOU 7594  OP2  DG T  15     6147   8448   7130   1333   -356   -794       O  
ATOM   7595  O5'  DG T  15     -30.272   5.940 -25.914  1.00 58.64           O  
ANISOU 7595  O5'  DG T  15     6380   8336   7566   1215   -435   -795       O  
ATOM   7596  C5'  DG T  15     -29.609   6.460 -27.056  1.00 57.63           C  
ANISOU 7596  C5'  DG T  15     6289   8047   7559   1137   -464   -764       C  
ATOM   7597  C4'  DG T  15     -30.590   6.428 -28.210  1.00 57.15           C  
ANISOU 7597  C4'  DG T  15     6271   7903   7541   1060   -455   -661       C  
ATOM   7598  O4'  DG T  15     -30.549   5.102 -28.794  1.00 55.95           O  
ANISOU 7598  O4'  DG T  15     6196   7765   7299    998   -382   -529       O  
ATOM   7599  C3'  DG T  15     -32.051   6.695 -27.817  1.00 56.85           C  
ANISOU 7599  C3'  DG T  15     6191   7920   7487   1100   -464   -686       C  
ATOM   7600  O3'  DG T  15     -32.610   7.711 -28.653  1.00 54.48           O  
ANISOU 7600  O3'  DG T  15     5878   7500   7322   1060   -517   -686       O  
ATOM   7601  C2'  DG T  15     -32.733   5.339 -28.005  1.00 55.31           C  
ANISOU 7601  C2'  DG T  15     6051   7792   7171   1069   -387   -561       C  
ATOM   7602  C1'  DG T  15     -31.872   4.752 -29.124  1.00 55.85           C  
ANISOU 7602  C1'  DG T  15     6196   7767   7256    977   -359   -462       C  
ATOM   7603  N9   DG T  15     -32.004   3.307 -29.319  1.00 53.14           N  
ANISOU 7603  N9   DG T  15     5908   7474   6809    943   -285   -352       N  
ATOM   7604  C8   DG T  15     -32.237   2.338 -28.367  1.00 53.55           C  
ANISOU 7604  C8   DG T  15     5947   7654   6746    993   -238   -332       C  
ATOM   7605  N7   DG T  15     -32.324   1.130 -28.857  1.00 50.09           N  
ANISOU 7605  N7   DG T  15     5559   7216   6257    942   -182   -222       N  
ATOM   7606  C5   DG T  15     -32.148   1.312 -30.221  1.00 47.84           C  
ANISOU 7606  C5   DG T  15     5326   6806   6046    855   -192   -175       C  
ATOM   7607  C6   DG T  15     -32.147   0.364 -31.271  1.00 48.24           C  
ANISOU 7607  C6   DG T  15     5435   6807   6087    776   -152    -73       C  
ATOM   7608  O6   DG T  15     -32.306  -0.861 -31.171  1.00 49.76           O  
ANISOU 7608  O6   DG T  15     5647   7044   6215    767   -101     -5       O  
ATOM   7609  N1   DG T  15     -31.938   0.960 -32.522  1.00 47.23           N  
ANISOU 7609  N1   DG T  15     5336   6571   6039    707   -180    -54       N  
ATOM   7610  C2   DG T  15     -31.748   2.315 -32.721  1.00 48.01           C  
ANISOU 7610  C2   DG T  15     5406   6606   6229    710   -240   -114       C  
ATOM   7611  N2   DG T  15     -31.556   2.738 -33.982  1.00 46.06           N  
ANISOU 7611  N2   DG T  15     5183   6267   6052    638   -260    -69       N  
ATOM   7612  N3   DG T  15     -31.753   3.208 -31.737  1.00 48.25           N  
ANISOU 7612  N3   DG T  15     5380   6667   6287    783   -281   -213       N  
ATOM   7613  C4   DG T  15     -31.953   2.642 -30.521  1.00 49.18           C  
ANISOU 7613  C4   DG T  15     5472   6900   6314    854   -254   -244       C  
ATOM   7614  P    DC T  16     -33.975   8.476 -28.301  1.00 55.10           P  
ANISOU 7614  P    DC T  16     5895   7599   7442   1106   -556   -749       P  
ATOM   7615  OP1  DC T  16     -34.022   9.666 -29.183  1.00 57.87           O  
ANISOU 7615  OP1  DC T  16     6223   7797   7966   1061   -622   -757       O  
ATOM   7616  OP2  DC T  16     -34.130   8.656 -26.836  1.00 55.19           O  
ANISOU 7616  OP2  DC T  16     5831   7748   7390   1218   -570   -881       O  
ATOM   7617  O5'  DC T  16     -35.099   7.421 -28.761  1.00 55.24           O  
ANISOU 7617  O5'  DC T  16     5969   7659   7360   1062   -489   -619       O  
ATOM   7618  C5'  DC T  16     -35.748   7.533 -30.020  1.00 51.20           C  
ANISOU 7618  C5'  DC T  16     5497   7044   6912    979   -490   -521       C  
ATOM   7619  C4'  DC T  16     -34.872   7.006 -31.146  1.00 52.29           C  
ANISOU 7619  C4'  DC T  16     5706   7101   7059    888   -463   -417       C  
ATOM   7620  O4'  DC T  16     -34.441   5.651 -30.852  1.00 51.59           O  
ANISOU 7620  O4'  DC T  16     5666   7096   6841    887   -394   -363       O  
ATOM   7621  C3'  DC T  16     -35.553   6.945 -32.507  1.00 53.95           C  
ANISOU 7621  C3'  DC T  16     5958   7229   7310    800   -455   -304       C  
ATOM   7622  O3'  DC T  16     -34.677   7.436 -33.497  1.00 55.22           O  
ANISOU 7622  O3'  DC T  16     6133   7285   7563    736   -482   -266       O  
ATOM   7623  C2'  DC T  16     -35.836   5.460 -32.721  1.00 52.03           C  
ANISOU 7623  C2'  DC T  16     5779   7051   6941    768   -378   -207       C  
ATOM   7624  C1'  DC T  16     -34.691   4.812 -31.957  1.00 48.35           C  
ANISOU 7624  C1'  DC T  16     5321   6647   6403    804   -350   -239       C  
ATOM   7625  N1   DC T  16     -35.008   3.440 -31.456  1.00 45.50           N  
ANISOU 7625  N1   DC T  16     4986   6387   5916    819   -283   -187       N  
ATOM   7626  C2   DC T  16     -35.020   2.357 -32.351  1.00 43.21           C  
ANISOU 7626  C2   DC T  16     4756   6073   5587    748   -234    -79       C  
ATOM   7627  O2   DC T  16     -34.768   2.543 -33.551  1.00 39.21           O  
ANISOU 7627  O2   DC T  16     4284   5479   5136    675   -244    -32       O  
ATOM   7628  N3   DC T  16     -35.311   1.115 -31.878  1.00 45.19           N  
ANISOU 7628  N3   DC T  16     5020   6404   5744    763   -178    -29       N  
ATOM   7629  C4   DC T  16     -35.573   0.928 -30.582  1.00 47.11           C  
ANISOU 7629  C4   DC T  16     5219   6759   5923    843   -166    -68       C  
ATOM   7630  N4   DC T  16     -35.850  -0.321 -30.175  1.00 46.14           N  
ANISOU 7630  N4   DC T  16     5101   6710   5719    851   -111      2       N  
ATOM   7631  C5   DC T  16     -35.568   2.020 -29.656  1.00 46.27           C  
ANISOU 7631  C5   DC T  16     5050   6694   5837    919   -213   -181       C  
ATOM   7632  C6   DC T  16     -35.287   3.242 -30.130  1.00 45.10           C  
ANISOU 7632  C6   DC T  16     4890   6455   5792    905   -272   -242       C  
ATOM   7633  P    DG T  17     -35.273   8.211 -34.758  1.00 55.75           P  
ANISOU 7633  P    DG T  17     6194   7247   7740    667   -518   -195       P  
ATOM   7634  OP1  DG T  17     -34.139   8.430 -35.686  1.00 58.63           O  
ANISOU 7634  OP1  DG T  17     6575   7537   8166    604   -530   -140       O  
ATOM   7635  OP2  DG T  17     -36.055   9.360 -34.254  1.00 56.92           O  
ANISOU 7635  OP2  DG T  17     6270   7370   7987    716   -579   -276       O  
ATOM   7636  O5'  DG T  17     -36.324   7.195 -35.411  1.00 56.43           O  
ANISOU 7636  O5'  DG T  17     6335   7373   7734    619   -461    -92       O  
ATOM   7637  C5'  DG T  17     -36.066   6.503 -36.631  1.00 53.59           C  
ANISOU 7637  C5'  DG T  17     6031   6989   7343    536   -426     17       C  
ATOM   7638  C4'  DG T  17     -37.129   5.444 -36.905  1.00 50.76           C  
ANISOU 7638  C4'  DG T  17     5713   6684   6891    515   -373     82       C  
ATOM   7639  O4'  DG T  17     -37.153   4.446 -35.854  1.00 50.97           O  
ANISOU 7639  O4'  DG T  17     5752   6800   6812    568   -327     52       O  
ATOM   7640  C3'  DG T  17     -38.555   5.955 -37.000  1.00 49.53           C  
ANISOU 7640  C3'  DG T  17     5531   6518   6771    520   -395     90       C  
ATOM   7641  O3'  DG T  17     -38.757   6.367 -38.353  1.00 48.69           O  
ANISOU 7641  O3'  DG T  17     5430   6344   6726    444   -413    171       O  
ATOM   7642  C2'  DG T  17     -39.393   4.731 -36.621  1.00 50.37           C  
ANISOU 7642  C2'  DG T  17     5667   6706   6764    534   -336    119       C  
ATOM   7643  C1'  DG T  17     -38.457   3.897 -35.747  1.00 49.80           C  
ANISOU 7643  C1'  DG T  17     5610   6697   6613    574   -300     86       C  
ATOM   7644  N9   DG T  17     -38.769   3.879 -34.318  1.00 49.52           N  
ANISOU 7644  N9   DG T  17     5536   6746   6532    662   -296     12       N  
ATOM   7645  C8   DG T  17     -39.144   4.938 -33.520  1.00 49.47           C  
ANISOU 7645  C8   DG T  17     5469   6752   6576    726   -344    -79       C  
ATOM   7646  N7   DG T  17     -39.332   4.609 -32.268  1.00 50.00           N  
ANISOU 7646  N7   DG T  17     5505   6924   6568    803   -327   -133       N  
ATOM   7647  C5   DG T  17     -39.060   3.249 -32.229  1.00 46.94           C  
ANISOU 7647  C5   DG T  17     5160   6589   6086    786   -263    -62       C  
ATOM   7648  C6   DG T  17     -39.095   2.338 -31.140  1.00 49.62           C  
ANISOU 7648  C6   DG T  17     5484   7047   6323    843   -220    -61       C  
ATOM   7649  O6   DG T  17     -39.381   2.555 -29.949  1.00 48.48           O  
ANISOU 7649  O6   DG T  17     5283   7003   6134    926   -226   -126       O  
ATOM   7650  N1   DG T  17     -38.750   1.048 -31.543  1.00 49.01           N  
ANISOU 7650  N1   DG T  17     5455   6972   6192    798   -166     29       N  
ATOM   7651  C2   DG T  17     -38.408   0.689 -32.824  1.00 47.15           C  
ANISOU 7651  C2   DG T  17     5277   6648   5991    712   -156     94       C  
ATOM   7652  N2   DG T  17     -38.100  -0.604 -33.007  1.00 50.93           N  
ANISOU 7652  N2   DG T  17     5789   7143   6419    683   -105    163       N  
ATOM   7653  N3   DG T  17     -38.368   1.533 -33.848  1.00 42.32           N  
ANISOU 7653  N3   DG T  17     4678   5941   5459    661   -194     93       N  
ATOM   7654  C4   DG T  17     -38.705   2.788 -33.480  1.00 45.92           C  
ANISOU 7654  C4   DG T  17     5088   6383   5976    700   -246     20       C  
ATOM   7655  P    DG T  18     -40.161   6.872 -38.904  1.00 44.90           P  
ANISOU 7655  P    DG T  18     4930   5837   6292    422   -435    213       P  
ATOM   7656  OP1  DG T  18     -41.008   5.689 -39.125  1.00 49.24           O  
ANISOU 7656  OP1  DG T  18     5524   6444   6740    404   -380    265       O  
ATOM   7657  OP2  DG T  18     -39.894   7.780 -40.041  1.00 49.61           O  
ANISOU 7657  OP2  DG T  18     5503   6354   6992    362   -478    273       O  
ATOM   7658  O5'  DG T  18     -40.744   7.741 -37.690  1.00 43.43           O  
ANISOU 7658  O5'  DG T  18     4685   5657   6160    505   -477    108       O  
ATOM   7659  C5'  DG T  18     -42.137   8.046 -37.598  1.00 38.62           C  
ANISOU 7659  C5'  DG T  18     4052   5053   5568    519   -490    108       C  
ATOM   7660  C4'  DG T  18     -42.637   7.741 -36.190  1.00 38.71           C  
ANISOU 7660  C4'  DG T  18     4044   5153   5511    606   -474     22       C  
ATOM   7661  O4'  DG T  18     -43.974   8.262 -36.016  1.00 37.32           O  
ANISOU 7661  O4'  DG T  18     3832   4979   5370    629   -497      5       O  
ATOM   7662  C3'  DG T  18     -42.731   6.263 -35.806  1.00 37.57           C  
ANISOU 7662  C3'  DG T  18     3948   5103   5225    614   -401     57       C  
ATOM   7663  O3'  DG T  18     -42.348   6.113 -34.440  1.00 37.00           O  
ANISOU 7663  O3'  DG T  18     3847   5112   5099    697   -393    -30       O  
ATOM   7664  C2'  DG T  18     -44.205   5.927 -36.031  1.00 36.74           C  
ANISOU 7664  C2'  DG T  18     3848   5021   5090    603   -382    107       C  
ATOM   7665  C1'  DG T  18     -44.855   7.235 -35.591  1.00 35.75           C  
ANISOU 7665  C1'  DG T  18     3657   4869   5057    649   -443     31       C  
ATOM   7666  N9   DG T  18     -46.168   7.560 -36.140  1.00 34.76           N  
ANISOU 7666  N9   DG T  18     3522   4715   4968    624   -457     73       N  
ATOM   7667  C8   DG T  18     -47.286   7.855 -35.402  1.00 32.46           C  
ANISOU 7667  C8   DG T  18     3190   4471   4674    680   -468     25       C  
ATOM   7668  N7   DG T  18     -48.320   8.152 -36.135  1.00 35.83           N  
ANISOU 7668  N7   DG T  18     3616   4854   5145    641   -481     77       N  
ATOM   7669  C5   DG T  18     -47.871   8.053 -37.446  1.00 36.73           C  
ANISOU 7669  C5   DG T  18     3771   4896   5290    555   -479    168       C  
ATOM   7670  C6   DG T  18     -48.554   8.262 -38.681  1.00 35.79           C  
ANISOU 7670  C6   DG T  18     3663   4718   5216    484   -489    257       C  
ATOM   7671  O6   DG T  18     -49.733   8.576 -38.870  1.00 34.52           O  
ANISOU 7671  O6   DG T  18     3484   4547   5083    481   -503    275       O  
ATOM   7672  N1   DG T  18     -47.732   8.070 -39.791  1.00 36.99           N  
ANISOU 7672  N1   DG T  18     3848   4829   5377    412   -483    331       N  
ATOM   7673  C2   DG T  18     -46.406   7.713 -39.712  1.00 36.86           C  
ANISOU 7673  C2   DG T  18     3854   4819   5333    408   -467    319       C  
ATOM   7674  N2   DG T  18     -45.771   7.568 -40.886  1.00 42.78           N  
ANISOU 7674  N2   DG T  18     4628   5536   6090    336   -462    397       N  
ATOM   7675  N3   DG T  18     -45.753   7.519 -38.565  1.00 37.57           N  
ANISOU 7675  N3   DG T  18     3937   4953   5386    472   -458    237       N  
ATOM   7676  C4   DG T  18     -46.538   7.696 -37.467  1.00 35.66           C  
ANISOU 7676  C4   DG T  18     3660   4759   5130    544   -464    165       C  
TER    7677       DG T  18                                                      
ATOM   7678  O5'  DC P 103     -35.366 -12.864 -36.074  1.00133.88           O  
ANISOU 7678  O5'  DC P 103    16389  17487  16993    378    205    633       O  
ATOM   7679  C5'  DC P 103     -35.724 -11.926 -35.062  1.00134.86           C  
ANISOU 7679  C5'  DC P 103    16500  17678  17062    434    200    635       C  
ATOM   7680  C4'  DC P 103     -36.273 -10.636 -35.655  1.00134.91           C  
ANISOU 7680  C4'  DC P 103    16536  17674  17050    421    168    588       C  
ATOM   7681  O4'  DC P 103     -36.817  -9.790 -34.603  1.00136.32           O  
ANISOU 7681  O4'  DC P 103    16690  17921  17186    482    161    585       O  
ATOM   7682  C3'  DC P 103     -35.250  -9.779 -36.399  1.00134.05           C  
ANISOU 7682  C3'  DC P 103    16469  17531  16933    393    144    520       C  
ATOM   7683  O3'  DC P 103     -35.806  -9.360 -37.640  1.00132.04           O  
ANISOU 7683  O3'  DC P 103    16237  17232  16699    341    123    507       O  
ATOM   7684  C2'  DC P 103     -35.022  -8.599 -35.458  1.00135.23           C  
ANISOU 7684  C2'  DC P 103    16610  17729  17044    449    126    482       C  
ATOM   7685  C1'  DC P 103     -36.406  -8.456 -34.836  1.00136.84           C  
ANISOU 7685  C1'  DC P 103    16781  17977  17236    484    128    516       C  
ATOM   7686  N1   DC P 103     -36.469  -7.627 -33.569  1.00138.65           N  
ANISOU 7686  N1   DC P 103    16977  18283  17421    559    118    486       N  
ATOM   7687  C2   DC P 103     -37.696  -7.067 -33.149  1.00139.70           C  
ANISOU 7687  C2   DC P 103    17082  18456  17542    592    107    490       C  
ATOM   7688  O2   DC P 103     -38.730  -7.261 -33.807  1.00139.07           O  
ANISOU 7688  O2   DC P 103    17008  18344  17488    557    108    526       O  
ATOM   7689  N3   DC P 103     -37.720  -6.318 -32.010  1.00140.14           N  
ANISOU 7689  N3   DC P 103    17100  18592  17556    664     95    448       N  
ATOM   7690  C4   DC P 103     -36.600  -6.112 -31.307  1.00139.70           C  
ANISOU 7690  C4   DC P 103    17034  18573  17471    703     93    404       C  
ATOM   7691  N4   DC P 103     -36.686  -5.369 -30.198  1.00139.15           N  
ANISOU 7691  N4   DC P 103    16920  18592  17361    778     78    351       N  
ATOM   7692  C5   DC P 103     -35.344  -6.666 -31.712  1.00139.15           C  
ANISOU 7692  C5   DC P 103    16996  18458  17415    668    105    405       C  
ATOM   7693  C6   DC P 103     -35.329  -7.405 -32.833  1.00138.89           C  
ANISOU 7693  C6   DC P 103    17001  18349  17424    597    117    446       C  
ATOM   7694  P    DG P 104     -34.907  -8.748 -38.818  1.00130.62           P  
ANISOU 7694  P    DG P 104    16093  17015  16523    291    100    462       P  
ATOM   7695  OP1  DG P 104     -34.596  -9.850 -39.758  1.00130.76           O  
ANISOU 7695  OP1  DG P 104    16116  17003  16563    242    114    464       O  
ATOM   7696  OP2  DG P 104     -33.813  -7.942 -38.231  1.00131.19           O  
ANISOU 7696  OP2  DG P 104    16172  17100  16575    321     88    423       O  
ATOM   7697  O5'  DG P 104     -35.915  -7.722 -39.523  1.00128.15           O  
ANISOU 7697  O5'  DG P 104    15784  16689  16217    269     71    462       O  
ATOM   7698  C5'  DG P 104     -36.784  -6.925 -38.717  1.00124.57           C  
ANISOU 7698  C5'  DG P 104    15313  16261  15758    313     58    466       C  
ATOM   7699  C4'  DG P 104     -36.843  -5.472 -39.167  1.00121.41           C  
ANISOU 7699  C4'  DG P 104    14918  15842  15371    303     18    439       C  
ATOM   7700  O4'  DG P 104     -37.627  -4.742 -38.184  1.00121.17           O  
ANISOU 7700  O4'  DG P 104    14861  15839  15338    358      4    429       O  
ATOM   7701  C3'  DG P 104     -35.507  -4.737 -39.263  1.00118.97           C  
ANISOU 7701  C3'  DG P 104    14619  15516  15067    301     -2    400       C  
ATOM   7702  O3'  DG P 104     -34.997  -4.791 -40.599  1.00115.33           O  
ANISOU 7702  O3'  DG P 104    14178  15028  14616    238     -9    409       O  
ATOM   7703  C2'  DG P 104     -35.893  -3.314 -38.873  1.00119.25           C  
ANISOU 7703  C2'  DG P 104    14635  15546  15128    331    -42    373       C  
ATOM   7704  C1'  DG P 104     -36.965  -3.546 -37.816  1.00119.17           C  
ANISOU 7704  C1'  DG P 104    14600  15580  15098    384    -29    379       C  
ATOM   7705  N9   DG P 104     -36.432  -3.654 -36.454  1.00117.24           N  
ANISOU 7705  N9   DG P 104    14336  15387  14823    451    -17    346       N  
ATOM   7706  C8   DG P 104     -36.270  -4.791 -35.697  1.00116.20           C  
ANISOU 7706  C8   DG P 104    14195  15302  14652    479     22    371       C  
ATOM   7707  N7   DG P 104     -35.768  -4.563 -34.516  1.00115.63           N  
ANISOU 7707  N7   DG P 104    14098  15285  14552    542     22    336       N  
ATOM   7708  C5   DG P 104     -35.582  -3.188 -34.480  1.00115.30           C  
ANISOU 7708  C5   DG P 104    14046  15224  14537    559    -22    272       C  
ATOM   7709  C6   DG P 104     -35.066  -2.354 -33.454  1.00114.17           C  
ANISOU 7709  C6   DG P 104    13871  15120  14388    624    -47    200       C  
ATOM   7710  O6   DG P 104     -34.659  -2.688 -32.333  1.00114.26           O  
ANISOU 7710  O6   DG P 104    13855  15206  14351    683    -31    180       O  
ATOM   7711  N1   DG P 104     -35.046  -1.009 -33.826  1.00113.23           N  
ANISOU 7711  N1   DG P 104    13743  14949  14329    619    -98    148       N  
ATOM   7712  C2   DG P 104     -35.474  -0.531 -35.045  1.00113.63           C  
ANISOU 7712  C2   DG P 104    13814  14925  14435    556   -120    177       C  
ATOM   7713  N2   DG P 104     -35.387   0.789 -35.244  1.00112.90           N  
ANISOU 7713  N2   DG P 104    13700  14785  14413    558   -172    131       N  
ATOM   7714  N3   DG P 104     -35.960  -1.300 -36.013  1.00115.16           N  
ANISOU 7714  N3   DG P 104    14039  15096  14622    496    -95    246       N  
ATOM   7715  C4   DG P 104     -35.985  -2.614 -35.667  1.00116.19           C  
ANISOU 7715  C4   DG P 104    14179  15270  14699    502    -47    284       C  
ATOM   7716  P    DC P 105     -33.430  -4.645 -40.925  1.00111.58           P  
ANISOU 7716  P    DC P 105    13715  14541  14138    220    -13    384       P  
ATOM   7717  OP1  DC P 105     -33.261  -4.843 -42.383  1.00111.24           O  
ANISOU 7717  OP1  DC P 105    13681  14492  14094    156    -16    403       O  
ATOM   7718  OP2  DC P 105     -32.668  -5.483 -39.972  1.00111.26           O  
ANISOU 7718  OP2  DC P 105    13678  14520  14076    257     16    366       O  
ATOM   7719  O5'  DC P 105     -33.103  -3.123 -40.570  1.00108.56           O  
ANISOU 7719  O5'  DC P 105    13317  14140  13789    244    -54    359       O  
ATOM   7720  C5'  DC P 105     -33.684  -2.057 -41.317  1.00104.19           C  
ANISOU 7720  C5'  DC P 105    12751  13562  13276    217    -91    379       C  
ATOM   7721  C4'  DC P 105     -33.258  -0.724 -40.734  1.00 99.89           C  
ANISOU 7721  C4'  DC P 105    12181  12990  12782    250   -132    345       C  
ATOM   7722  O4'  DC P 105     -33.803  -0.554 -39.400  1.00 98.12           O  
ANISOU 7722  O4'  DC P 105    11940  12787  12555    318   -134    303       O  
ATOM   7723  C3'  DC P 105     -31.758  -0.580 -40.543  1.00 97.02           C  
ANISOU 7723  C3'  DC P 105    11822  12617  12424    256   -136    316       C  
ATOM   7724  O3'  DC P 105     -31.158  -0.304 -41.811  1.00 94.04           O  
ANISOU 7724  O3'  DC P 105    11446  12221  12064    195   -148    355       O  
ATOM   7725  C2'  DC P 105     -31.726   0.569 -39.538  1.00 97.02           C  
ANISOU 7725  C2'  DC P 105    11788  12598  12476    312   -175    263       C  
ATOM   7726  C1'  DC P 105     -32.883   0.186 -38.614  1.00 96.78           C  
ANISOU 7726  C1'  DC P 105    11751  12608  12413    361   -159    247       C  
ATOM   7727  N1   DC P 105     -32.471  -0.604 -37.383  1.00 94.79           N  
ANISOU 7727  N1   DC P 105    11501  12410  12105    418   -127    211       N  
ATOM   7728  C2   DC P 105     -32.048   0.075 -36.220  1.00 92.12           C  
ANISOU 7728  C2   DC P 105    11132  12091  11778    485   -150    140       C  
ATOM   7729  O2   DC P 105     -32.009   1.312 -36.203  1.00 89.42           O  
ANISOU 7729  O2   DC P 105    10759  11710  11505    497   -200    101       O  
ATOM   7730  N3   DC P 105     -31.687  -0.653 -35.129  1.00 91.40           N  
ANISOU 7730  N3   DC P 105    11036  12065  11628    536   -120    116       N  
ATOM   7731  C4   DC P 105     -31.732  -1.990 -35.159  1.00 91.04           C  
ANISOU 7731  C4   DC P 105    11014  12051  11527    522    -71    166       C  
ATOM   7732  N4   DC P 105     -31.368  -2.655 -34.059  1.00 89.50           N  
ANISOU 7732  N4   DC P 105    10806  11921  11280    574    -44    154       N  
ATOM   7733  C5   DC P 105     -32.156  -2.702 -36.323  1.00 91.66           C  
ANISOU 7733  C5   DC P 105    11123  12097  11606    454    -50    230       C  
ATOM   7734  C6   DC P 105     -32.511  -1.978 -37.394  1.00 92.88           C  
ANISOU 7734  C6   DC P 105    11284  12201  11805    406    -78    246       C  
ATOM   7735  P    DG P 106     -29.633   0.151 -41.980  1.00 90.58           P  
ANISOU 7735  P    DG P 106    11003  11763  11650    185   -163    343       P  
ATOM   7736  OP1  DG P 106     -29.276   0.054 -43.415  1.00 90.51           O  
ANISOU 7736  OP1  DG P 106    10994  11764  11631    118   -161    399       O  
ATOM   7737  OP2  DG P 106     -28.807  -0.555 -40.973  1.00 91.76           O  
ANISOU 7737  OP2  DG P 106    11170  11931  11763    227   -137    293       O  
ATOM   7738  O5'  DG P 106     -29.741   1.693 -41.578  1.00 88.19           O  
ANISOU 7738  O5'  DG P 106    10658  11410  11439    211   -220    326       O  
ATOM   7739  C5'  DG P 106     -28.662   2.565 -41.810  1.00 84.78           C  
ANISOU 7739  C5'  DG P 106    10202  10941  11070    200   -253    327       C  
ATOM   7740  C4'  DG P 106     -28.383   3.417 -40.586  1.00 81.95           C  
ANISOU 7740  C4'  DG P 106     9814  10549  10775    264   -289    252       C  
ATOM   7741  O4'  DG P 106     -28.930   2.829 -39.374  1.00 79.36           O  
ANISOU 7741  O4'  DG P 106     9498  10263  10393    325   -266    192       O  
ATOM   7742  C3'  DG P 106     -26.898   3.619 -40.336  1.00 81.51           C  
ANISOU 7742  C3'  DG P 106     9753  10476  10742    272   -299    223       C  
ATOM   7743  O3'  DG P 106     -26.687   5.014 -40.156  1.00 82.93           O  
ANISOU 7743  O3'  DG P 106     9879  10591  11041    288   -361    202       O  
ATOM   7744  C2'  DG P 106     -26.602   2.780 -39.090  1.00 78.26           C  
ANISOU 7744  C2'  DG P 106     9366  10110  10260    332   -265    152       C  
ATOM   7745  C1'  DG P 106     -27.941   2.791 -38.362  1.00 75.14           C  
ANISOU 7745  C1'  DG P 106     8960   9739   9851    375   -266    125       C  
ATOM   7746  N9   DG P 106     -28.199   1.632 -37.500  1.00 70.08           N  
ANISOU 7746  N9   DG P 106     8344   9165   9116    414   -217    103       N  
ATOM   7747  C8   DG P 106     -28.469   0.341 -37.897  1.00 67.07           C  
ANISOU 7747  C8   DG P 106     8001   8821   8661    385   -166    151       C  
ATOM   7748  N7   DG P 106     -28.670  -0.485 -36.906  1.00 64.44           N  
ANISOU 7748  N7   DG P 106     7673   8542   8268    431   -133    130       N  
ATOM   7749  C5   DG P 106     -28.526   0.307 -35.770  1.00 65.04           C  
ANISOU 7749  C5   DG P 106     7712   8633   8366    499   -163     59       C  
ATOM   7750  C6   DG P 106     -28.631  -0.029 -34.393  1.00 62.18           C  
ANISOU 7750  C6   DG P 106     7330   8343   7953    573   -148     13       C  
ATOM   7751  O6   DG P 106     -28.880  -1.134 -33.899  1.00 58.95           O  
ANISOU 7751  O6   DG P 106     6930   7994   7475    590   -103     41       O  
ATOM   7752  N1   DG P 106     -28.417   1.064 -33.551  1.00 62.94           N  
ANISOU 7752  N1   DG P 106     7380   8444   8090    632   -193    -71       N  
ATOM   7753  C2   DG P 106     -28.130   2.338 -33.993  1.00 65.15           C  
ANISOU 7753  C2   DG P 106     7636   8650   8468    618   -249   -104       C  
ATOM   7754  N2   DG P 106     -27.950   3.274 -33.047  1.00 63.19           N  
ANISOU 7754  N2   DG P 106     7336   8411   8262    685   -293   -198       N  
ATOM   7755  N3   DG P 106     -28.029   2.668 -35.281  1.00 66.14           N  
ANISOU 7755  N3   DG P 106     7780   8702   8650    546   -263    -45       N  
ATOM   7756  C4   DG P 106     -28.238   1.613 -36.117  1.00 66.94           C  
ANISOU 7756  C4   DG P 106     7926   8813   8694    490   -217     34       C  
ATOM   7757  P    DC P 107     -25.215   5.628 -40.105  1.00 83.73           P  
ANISOU 7757  P    DC P 107     9955  10650  11210    288   -390    184       P  
ATOM   7758  OP1  DC P 107     -25.281   7.029 -40.590  1.00 82.60           O  
ANISOU 7758  OP1  DC P 107     9748  10429  11207    269   -455    217       O  
ATOM   7759  OP2  DC P 107     -24.280   4.656 -40.725  1.00 82.51           O  
ANISOU 7759  OP2  DC P 107     9842  10533  10973    248   -344    225       O  
ATOM   7760  O5'  DC P 107     -24.945   5.611 -38.529  1.00 81.09           O  
ANISOU 7760  O5'  DC P 107     9614  10330  10865    372   -396     67       O  
ATOM   7761  C5'  DC P 107     -25.430   6.637 -37.675  1.00 76.92           C  
ANISOU 7761  C5'  DC P 107     9032   9769  10424    429   -448    -10       C  
ATOM   7762  C4'  DC P 107     -24.693   6.553 -36.351  1.00 74.85           C  
ANISOU 7762  C4'  DC P 107     8760   9537  10141    502   -451   -117       C  
ATOM   7763  O4'  DC P 107     -25.115   5.363 -35.636  1.00 70.99           O  
ANISOU 7763  O4'  DC P 107     8313   9141   9520    537   -394   -137       O  
ATOM   7764  C3'  DC P 107     -23.174   6.463 -36.473  1.00 74.17           C  
ANISOU 7764  C3'  DC P 107     8683   9432  10065    488   -449   -118       C  
ATOM   7765  O3'  DC P 107     -22.593   7.397 -35.571  1.00 76.15           O  
ANISOU 7765  O3'  DC P 107     8878   9648  10406    546   -504   -218       O  
ATOM   7766  C2'  DC P 107     -22.846   5.006 -36.126  1.00 70.50           C  
ANISOU 7766  C2'  DC P 107     8280   9051   9457    495   -379   -114       C  
ATOM   7767  C1'  DC P 107     -23.985   4.647 -35.175  1.00 66.60           C  
ANISOU 7767  C1'  DC P 107     7783   8622   8901    553   -363   -160       C  
ATOM   7768  N1   DC P 107     -24.370   3.190 -35.114  1.00 59.46           N  
ANISOU 7768  N1   DC P 107     6931   7792   7869    545   -293   -117       N  
ATOM   7769  C2   DC P 107     -24.630   2.593 -33.862  1.00 53.17           C  
ANISOU 7769  C2   DC P 107     6129   7078   6995    614   -268   -169       C  
ATOM   7770  O2   DC P 107     -24.530   3.266 -32.822  1.00 49.08           O  
ANISOU 7770  O2   DC P 107     5565   6582   6501    683   -302   -259       O  
ATOM   7771  N3   DC P 107     -24.987   1.280 -33.830  1.00 47.75           N  
ANISOU 7771  N3   DC P 107     5480   6450   6212    604   -209   -118       N  
ATOM   7772  C4   DC P 107     -25.092   0.577 -34.965  1.00 49.20           C  
ANISOU 7772  C4   DC P 107     5706   6610   6378    533   -178    -37       C  
ATOM   7773  N4   DC P 107     -25.446  -0.710 -34.870  1.00 45.99           N  
ANISOU 7773  N4   DC P 107     5327   6253   5895    528   -126      5       N  
ATOM   7774  C5   DC P 107     -24.833   1.161 -36.246  1.00 48.33           C  
ANISOU 7774  C5   DC P 107     5602   6430   6331    466   -202      7       C  
ATOM   7775  C6   DC P 107     -24.486   2.456 -36.271  1.00 53.74           C  
ANISOU 7775  C6   DC P 107     6249   7060   7109    474   -258    -28       C  
ATOM   7776  P    DG P 108     -21.009   7.649 -35.536  1.00 79.37           P  
ANISOU 7776  P    DG P 108     9276  10019  10863    543   -521   -239       P  
ATOM   7777  OP1  DG P 108     -20.800   9.093 -35.270  1.00 78.34           O  
ANISOU 7777  OP1  DG P 108     9065   9803  10899    570   -603   -300       O  
ATOM   7778  OP2  DG P 108     -20.372   6.997 -36.708  1.00 78.11           O  
ANISOU 7778  OP2  DG P 108     9163   9858  10658    465   -481   -129       O  
ATOM   7779  O5'  DG P 108     -20.578   6.815 -34.244  1.00 75.12           O  
ANISOU 7779  O5'  DG P 108     8760   9569  10213    612   -485   -328       O  
ATOM   7780  C5'  DG P 108     -20.970   7.246 -32.944  1.00 71.82           C  
ANISOU 7780  C5'  DG P 108     8295   9190   9804    700   -515   -448       C  
ATOM   7781  C4'  DG P 108     -20.469   6.247 -31.923  1.00 69.22           C  
ANISOU 7781  C4'  DG P 108     7991   8962   9345    752   -468   -496       C  
ATOM   7782  O4'  DG P 108     -21.140   4.981 -32.153  1.00 64.75           O  
ANISOU 7782  O4'  DG P 108     7485   8464   8653    727   -398   -417       O  
ATOM   7783  C3'  DG P 108     -18.967   5.977 -32.012  1.00 68.84           C  
ANISOU 7783  C3'  DG P 108     7964   8898   9295    736   -458   -493       C  
ATOM   7784  O3'  DG P 108     -18.378   6.117 -30.713  1.00 71.17           O  
ANISOU 7784  O3'  DG P 108     8222   9247   9572    818   -475   -608       O  
ATOM   7785  C2'  DG P 108     -18.876   4.566 -32.605  1.00 64.51           C  
ANISOU 7785  C2'  DG P 108     7491   8393   8626    683   -381   -393       C  
ATOM   7786  C1'  DG P 108     -20.190   3.939 -32.153  1.00 61.33           C  
ANISOU 7786  C1'  DG P 108     7098   8068   8138    711   -348   -385       C  
ATOM   7787  N9   DG P 108     -20.681   2.863 -33.010  1.00 57.21           N  
ANISOU 7787  N9   DG P 108     6633   7560   7544    650   -291   -281       N  
ATOM   7788  C8   DG P 108     -20.759   2.847 -34.385  1.00 56.26           C  
ANISOU 7788  C8   DG P 108     6540   7381   7454    569   -286   -194       C  
ATOM   7789  N7   DG P 108     -21.244   1.735 -34.872  1.00 52.20           N  
ANISOU 7789  N7   DG P 108     6070   6902   6862    534   -234   -127       N  
ATOM   7790  C5   DG P 108     -21.506   0.957 -33.748  1.00 51.43           C  
ANISOU 7790  C5   DG P 108     5974   6883   6684    591   -201   -160       C  
ATOM   7791  C6   DG P 108     -22.050  -0.353 -33.639  1.00 46.68           C  
ANISOU 7791  C6   DG P 108     5402   6339   5994    587   -145   -112       C  
ATOM   7792  O6   DG P 108     -22.413  -1.119 -34.543  1.00 43.31           O  
ANISOU 7792  O6   DG P 108     5010   5902   5544    531   -114    -42       O  
ATOM   7793  N1   DG P 108     -22.150  -0.771 -32.316  1.00 46.80           N  
ANISOU 7793  N1   DG P 108     5396   6436   5949    659   -128   -152       N  
ATOM   7794  C2   DG P 108     -21.777  -0.011 -31.228  1.00 52.04           C  
ANISOU 7794  C2   DG P 108     6015   7133   6626    730   -162   -240       C  
ATOM   7795  N2   DG P 108     -21.945  -0.576 -30.023  1.00 51.08           N  
ANISOU 7795  N2   DG P 108     5869   7112   6427    796   -138   -263       N  
ATOM   7796  N3   DG P 108     -21.273   1.220 -31.311  1.00 52.75           N  
ANISOU 7796  N3   DG P 108     6076   7164   6801    737   -218   -302       N  
ATOM   7797  C4   DG P 108     -21.164   1.641 -32.596  1.00 53.67           C  
ANISOU 7797  C4   DG P 108     6214   7191   6987    664   -235   -252       C  
ATOM   7798  P    DG P 109     -16.892   5.614 -30.374  1.00 73.81           P  
ANISOU 7798  P    DG P 109     8577   9602   9867    826   -455   -627       P  
ATOM   7799  OP1  DG P 109     -16.419   6.404 -29.213  1.00 74.41           O  
ANISOU 7799  OP1  DG P 109     8584   9697   9991    910   -508   -766       O  
ATOM   7800  OP2  DG P 109     -16.098   5.585 -31.623  1.00 73.25           O  
ANISOU 7800  OP2  DG P 109     8540   9446   9844    741   -448   -535       O  
ATOM   7801  O5'  DG P 109     -17.115   4.094 -29.918  1.00 72.07           O  
ANISOU 7801  O5'  DG P 109     8407   9495   9480    838   -375   -584       O  
ATOM   7802  C5'  DG P 109     -17.919   3.800 -28.768  1.00 72.09           C  
ANISOU 7802  C5'  DG P 109     8382   9608   9401    914   -363   -639       C  
ATOM   7803  C4'  DG P 109     -17.599   2.438 -28.157  1.00 70.53           C  
ANISOU 7803  C4'  DG P 109     8215   9513   9069    934   -296   -604       C  
ATOM   7804  O4'  DG P 109     -18.251   1.367 -28.896  1.00 68.87           O  
ANISOU 7804  O4'  DG P 109     8061   9307   8800    875   -239   -488       O  
ATOM   7805  C3'  DG P 109     -16.123   2.063 -28.097  1.00 70.06           C  
ANISOU 7805  C3'  DG P 109     8176   9444   8998    925   -283   -608       C  
ATOM   7806  O3'  DG P 109     -15.887   1.379 -26.860  1.00 71.24           O  
ANISOU 7806  O3'  DG P 109     8305   9717   9045    995   -254   -643       O  
ATOM   7807  C2'  DG P 109     -15.918   1.185 -29.339  1.00 67.36           C  
ANISOU 7807  C2'  DG P 109     7905   9047   8641    833   -237   -489       C  
ATOM   7808  C1'  DG P 109     -17.289   0.533 -29.525  1.00 64.78           C  
ANISOU 7808  C1'  DG P 109     7595   8759   8260    820   -201   -424       C  
ATOM   7809  N9   DG P 109     -17.689   0.281 -30.920  1.00 60.65           N  
ANISOU 7809  N9   DG P 109     7116   8164   7763    734   -185   -333       N  
ATOM   7810  C8   DG P 109     -17.565   1.111 -32.019  1.00 59.00           C  
ANISOU 7810  C8   DG P 109     6911   7861   7645    677   -220   -312       C  
ATOM   7811  N7   DG P 109     -18.024   0.584 -33.130  1.00 57.97           N  
ANISOU 7811  N7   DG P 109     6818   7704   7503    609   -193   -227       N  
ATOM   7812  C5   DG P 109     -18.489  -0.675 -32.745  1.00 54.77           C  
ANISOU 7812  C5   DG P 109     6437   7368   7006    621   -139   -194       C  
ATOM   7813  C6   DG P 109     -19.094  -1.714 -33.507  1.00 53.71           C  
ANISOU 7813  C6   DG P 109     6340   7239   6829    570    -95   -116       C  
ATOM   7814  O6   DG P 109     -19.360  -1.731 -34.724  1.00 53.20           O  
ANISOU 7814  O6   DG P 109     6297   7130   6788    505    -94    -63       O  
ATOM   7815  N1   DG P 109     -19.407  -2.825 -32.721  1.00 51.28           N  
ANISOU 7815  N1   DG P 109     6035   7002   6448    604    -52   -100       N  
ATOM   7816  C2   DG P 109     -19.160  -2.921 -31.367  1.00 52.77           C  
ANISOU 7816  C2   DG P 109     6192   7261   6595    677    -48   -146       C  
ATOM   7817  N2   DG P 109     -19.526  -4.054 -30.761  1.00 50.52           N  
ANISOU 7817  N2   DG P 109     5905   7045   6245    700     -4   -105       N  
ATOM   7818  N3   DG P 109     -18.597  -1.964 -30.647  1.00 53.49           N  
ANISOU 7818  N3   DG P 109     6250   7361   6711    728    -87   -226       N  
ATOM   7819  C4   DG P 109     -18.285  -0.873 -31.394  1.00 55.84           C  
ANISOU 7819  C4   DG P 109     6547   7577   7094    695   -133   -250       C  
ATOM   7820  P    DC P 110     -14.433   0.840 -26.440  1.00 72.62           P  
ANISOU 7820  P    DC P 110     8492   9917   9183   1007   -235   -655       P  
ATOM   7821  OP1  DC P 110     -14.454   0.718 -24.963  1.00 72.85           O  
ANISOU 7821  OP1  DC P 110     8465  10085   9131   1104   -234   -729       O  
ATOM   7822  OP2  DC P 110     -13.395   1.647 -27.127  1.00 72.34           O  
ANISOU 7822  OP2  DC P 110     8463   9769   9253    968   -276   -683       O  
ATOM   7823  O5'  DC P 110     -14.383  -0.630 -27.076  1.00 68.61           O  
ANISOU 7823  O5'  DC P 110     8049   9412   8606    945   -163   -529       O  
ATOM   7824  C5'  DC P 110     -15.451  -1.541 -26.799  1.00 65.62           C  
ANISOU 7824  C5'  DC P 110     7674   9109   8150    954   -118   -464       C  
ATOM   7825  C4'  DC P 110     -15.364  -2.783 -27.665  1.00 60.18           C  
ANISOU 7825  C4'  DC P 110     7044   8385   7438    882    -64   -354       C  
ATOM   7826  O4'  DC P 110     -15.759  -2.528 -29.034  1.00 57.86           O  
ANISOU 7826  O4'  DC P 110     6788   7989   7206    804    -72   -310       O  
ATOM   7827  C3'  DC P 110     -13.967  -3.373 -27.754  1.00 56.78           C  
ANISOU 7827  C3'  DC P 110     6638   7936   6998    862    -43   -343       C  
ATOM   7828  O3'  DC P 110     -14.000  -4.485 -26.876  1.00 52.93           O  
ANISOU 7828  O3'  DC P 110     6136   7546   6429    900      2   -302       O  
ATOM   7829  C2'  DC P 110     -13.768  -3.716 -29.239  1.00 55.55           C  
ANISOU 7829  C2'  DC P 110     6539   7680   6886    769    -29   -277       C  
ATOM   7830  C1'  DC P 110     -15.164  -3.528 -29.830  1.00 53.82           C  
ANISOU 7830  C1'  DC P 110     6323   7441   6683    743    -33   -241       C  
ATOM   7831  N1   DC P 110     -15.302  -3.077 -31.263  1.00 51.90           N  
ANISOU 7831  N1   DC P 110     6110   7104   6504    667    -49   -210       N  
ATOM   7832  C2   DC P 110     -15.986  -3.887 -32.195  1.00 49.89           C  
ANISOU 7832  C2   DC P 110     5888   6832   6237    610    -17   -136       C  
ATOM   7833  O2   DC P 110     -16.448  -4.984 -31.842  1.00 47.38           O  
ANISOU 7833  O2   DC P 110     5573   6560   5868    619     23    -95       O  
ATOM   7834  N3   DC P 110     -16.119  -3.444 -33.476  1.00 48.22           N  
ANISOU 7834  N3   DC P 110     5695   6554   6073    545    -33   -108       N  
ATOM   7835  C4   DC P 110     -15.618  -2.259 -33.846  1.00 48.13           C  
ANISOU 7835  C4   DC P 110     5670   6490   6126    534    -79   -138       C  
ATOM   7836  N4   DC P 110     -15.780  -1.863 -35.120  1.00 44.02           N  
ANISOU 7836  N4   DC P 110     5160   5919   5648    471    -92    -95       N  
ATOM   7837  C5   DC P 110     -14.926  -1.425 -32.915  1.00 48.73           C  
ANISOU 7837  C5   DC P 110     5713   6569   6232    590   -114   -212       C  
ATOM   7838  C6   DC P 110     -14.804  -1.863 -31.652  1.00 51.15           C  
ANISOU 7838  C6   DC P 110     6003   6947   6483    656    -99   -253       C  
ATOM   7839  P    DG P 111     -12.690  -5.303 -26.485  1.00 50.50           P  
ANISOU 7839  P    DG P 111     5836   7263   6089    907     30   -289       P  
ATOM   7840  OP1  DG P 111     -13.009  -5.983 -25.212  1.00 48.54           O  
ANISOU 7840  OP1  DG P 111     5540   7145   5758    975     58   -266       O  
ATOM   7841  OP2  DG P 111     -11.492  -4.435 -26.618  1.00 51.41           O  
ANISOU 7841  OP2  DG P 111     5956   7325   6252    906     -8   -364       O  
ATOM   7842  O5'  DG P 111     -12.613  -6.380 -27.680  1.00 48.95           O  
ANISOU 7842  O5'  DG P 111     5696   6990   5915    821     70   -197       O  
ATOM   7843  C5'  DG P 111     -13.737  -7.226 -27.929  1.00 46.25           C  
ANISOU 7843  C5'  DG P 111     5356   6660   5556    799    102   -120       C  
ATOM   7844  C4'  DG P 111     -13.564  -8.059 -29.183  1.00 44.58           C  
ANISOU 7844  C4'  DG P 111     5192   6366   5380    718    127    -62       C  
ATOM   7845  O4'  DG P 111     -13.767  -7.263 -30.377  1.00 45.42           O  
ANISOU 7845  O4'  DG P 111     5329   6392   5537    664     99    -80       O  
ATOM   7846  C3'  DG P 111     -12.193  -8.682 -29.332  1.00 44.69           C  
ANISOU 7846  C3'  DG P 111     5226   6356   5400    698    144    -60       C  
ATOM   7847  O3'  DG P 111     -12.448 -10.039 -29.557  1.00 46.38           O  
ANISOU 7847  O3'  DG P 111     5442   6566   5613    671    185     13       O  
ATOM   7848  C2'  DG P 111     -11.570  -7.957 -30.530  1.00 41.38           C  
ANISOU 7848  C2'  DG P 111     4843   5849   5029    641    118    -93       C  
ATOM   7849  C1'  DG P 111     -12.805  -7.604 -31.347  1.00 40.58           C  
ANISOU 7849  C1'  DG P 111     4751   5716   4950    606    107    -72       C  
ATOM   7850  N9   DG P 111     -12.745  -6.447 -32.235  1.00 38.85           N  
ANISOU 7850  N9   DG P 111     4544   5438   4777    572     68   -101       N  
ATOM   7851  C8   DG P 111     -12.194  -5.213 -31.975  1.00 34.56           C  
ANISOU 7851  C8   DG P 111     3985   4878   4267    595     25   -160       C  
ATOM   7852  N7   DG P 111     -12.327  -4.379 -32.973  1.00 38.87           N  
ANISOU 7852  N7   DG P 111     4539   5366   4865    551     -4   -156       N  
ATOM   7853  C5   DG P 111     -13.020  -5.088 -33.958  1.00 36.62           C  
ANISOU 7853  C5   DG P 111     4278   5068   4570    496     22    -97       C  
ATOM   7854  C6   DG P 111     -13.463  -4.713 -35.261  1.00 38.87           C  
ANISOU 7854  C6   DG P 111     4573   5310   4885    436      9    -63       C  
ATOM   7855  O6   DG P 111     -13.337  -3.639 -35.877  1.00 41.18           O  
ANISOU 7855  O6   DG P 111     4855   5563   5228    412    -28    -65       O  
ATOM   7856  N1   DG P 111     -14.120  -5.752 -35.908  1.00 38.64           N  
ANISOU 7856  N1   DG P 111     4562   5291   4828    399     43    -18       N  
ATOM   7857  C2   DG P 111     -14.333  -6.997 -35.379  1.00 35.32           C  
ANISOU 7857  C2   DG P 111     4145   4903   4371    416     82     -1       C  
ATOM   7858  N2   DG P 111     -14.997  -7.858 -36.166  1.00 29.30           N  
ANISOU 7858  N2   DG P 111     3394   4136   3603    376    105     36       N  
ATOM   7859  N3   DG P 111     -13.933  -7.356 -34.165  1.00 34.67           N  
ANISOU 7859  N3   DG P 111     4051   4858   4265    471     95    -19       N  
ATOM   7860  C4   DG P 111     -13.282  -6.365 -33.511  1.00 36.44           C  
ANISOU 7860  C4   DG P 111     4260   5085   4499    509     65    -68       C  
ATOM   7861  P    DG P 112     -11.255 -11.088 -29.606  1.00 48.78           P  
ANISOU 7861  P    DG P 112     5755   6853   5926    653    212     34       P  
ATOM   7862  OP1  DG P 112     -11.812 -12.392 -29.172  1.00 48.39           O  
ANISOU 7862  OP1  DG P 112     5677   6835   5875    661    249    114       O  
ATOM   7863  OP2  DG P 112     -10.035 -10.516 -28.994  1.00 47.15           O  
ANISOU 7863  OP2  DG P 112     5546   6668   5702    687    197    -21       O  
ATOM   7864  O5'  DG P 112     -10.977 -11.156 -31.173  1.00 46.55           O  
ANISOU 7864  O5'  DG P 112     5517   6479   5690    573    208     26       O  
ATOM   7865  C5'  DG P 112     -11.990 -11.646 -32.055  1.00 46.32           C  
ANISOU 7865  C5'  DG P 112     5497   6418   5686    529    218     63       C  
ATOM   7866  C4'  DG P 112     -11.538 -11.410 -33.481  1.00 43.65           C  
ANISOU 7866  C4'  DG P 112     5193   6016   5374    464    206     37       C  
ATOM   7867  O4'  DG P 112     -11.608  -9.991 -33.767  1.00 38.73           O  
ANISOU 7867  O4'  DG P 112     4580   5383   4752    462    169      1       O  
ATOM   7868  C3'  DG P 112     -10.087 -11.813 -33.704  1.00 40.97           C  
ANISOU 7868  C3'  DG P 112     4867   5657   5043    447    215     15       C  
ATOM   7869  O3'  DG P 112     -10.021 -12.889 -34.636  1.00 45.24           O  
ANISOU 7869  O3'  DG P 112     5413   6164   5611    399    235     30       O  
ATOM   7870  C2'  DG P 112      -9.422 -10.540 -34.223  1.00 39.60           C  
ANISOU 7870  C2'  DG P 112     4711   5462   4872    432    182    -29       C  
ATOM   7871  C1'  DG P 112     -10.625  -9.751 -34.726  1.00 38.00           C  
ANISOU 7871  C1'  DG P 112     4508   5252   4676    418    160    -21       C  
ATOM   7872  N9   DG P 112     -10.385  -8.320 -34.929  1.00 35.86           N  
ANISOU 7872  N9   DG P 112     4239   4965   4421    418    121    -51       N  
ATOM   7873  C8   DG P 112      -9.722  -7.451 -34.100  1.00 36.42           C  
ANISOU 7873  C8   DG P 112     4297   5043   4498    462     96    -92       C  
ATOM   7874  N7   DG P 112      -9.650  -6.235 -34.571  1.00 39.27           N  
ANISOU 7874  N7   DG P 112     4653   5371   4895    448     58   -110       N  
ATOM   7875  C5   DG P 112     -10.301  -6.300 -35.801  1.00 38.25           C  
ANISOU 7875  C5   DG P 112     4535   5222   4776    391     60    -71       C  
ATOM   7876  C6   DG P 112     -10.540  -5.295 -36.779  1.00 37.17           C  
ANISOU 7876  C6   DG P 112     4392   5053   4677    352     28    -55       C  
ATOM   7877  O6   DG P 112     -10.219  -4.098 -36.766  1.00 37.92           O  
ANISOU 7877  O6   DG P 112     4468   5120   4820    358    -12    -71       O  
ATOM   7878  N1   DG P 112     -11.245  -5.788 -37.872  1.00 36.54           N  
ANISOU 7878  N1   DG P 112     4323   4978   4584    302     44    -14       N  
ATOM   7879  C2   DG P 112     -11.663  -7.089 -38.020  1.00 37.12           C  
ANISOU 7879  C2   DG P 112     4408   5072   4622    290     82      0       C  
ATOM   7880  N2   DG P 112     -12.315  -7.372 -39.157  1.00 32.50           N  
ANISOU 7880  N2   DG P 112     3826   4491   4032    243     88     29       N  
ATOM   7881  N3   DG P 112     -11.447  -8.040 -37.113  1.00 36.08           N  
ANISOU 7881  N3   DG P 112     4280   4958   4471    325    110    -11       N  
ATOM   7882  C4   DG P 112     -10.759  -7.582 -36.033  1.00 36.04           C  
ANISOU 7882  C4   DG P 112     4268   4960   4468    374     98    -42       C  
ATOM   7883  P    DC P 113      -8.729 -13.829 -34.662  1.00 43.22           P  
ANISOU 7883  P    DC P 113     5158   5893   5373    389    254     19       P  
ATOM   7884  OP1  DC P 113      -9.124 -15.211 -34.343  1.00 44.39           O  
ANISOU 7884  OP1  DC P 113     5277   6035   5554    393    281     62       O  
ATOM   7885  OP2  DC P 113      -7.653 -13.113 -33.964  1.00 52.55           O  
ANISOU 7885  OP2  DC P 113     6345   7091   6530    421    243     -9       O  
ATOM   7886  O5'  DC P 113      -8.278 -13.874 -36.171  1.00 48.13           O  
ANISOU 7886  O5'  DC P 113     5798   6482   6008    327    248    -13       O  
ATOM   7887  C5'  DC P 113      -8.301 -12.683 -36.853  1.00 49.40           C  
ANISOU 7887  C5'  DC P 113     5976   6643   6151    307    223    -31       C  
ATOM   7888  C4'  DC P 113      -9.276 -12.830 -37.987  1.00 45.44           C  
ANISOU 7888  C4'  DC P 113     5473   6136   5657    263    220    -23       C  
ATOM   7889  O4'  DC P 113      -9.879 -11.537 -38.211  1.00 48.88           O  
ANISOU 7889  O4'  DC P 113     5915   6578   6080    261    192    -16       O  
ATOM   7890  C3'  DC P 113      -8.578 -13.172 -39.283  1.00 42.92           C  
ANISOU 7890  C3'  DC P 113     5156   5815   5338    214    221    -51       C  
ATOM   7891  O3'  DC P 113      -9.498 -13.728 -40.217  1.00 37.80           O  
ANISOU 7891  O3'  DC P 113     4495   5169   4698    181    225    -51       O  
ATOM   7892  C2'  DC P 113      -8.060 -11.802 -39.702  1.00 42.28           C  
ANISOU 7892  C2'  DC P 113     5086   5743   5237    202    195    -55       C  
ATOM   7893  C1'  DC P 113      -9.146 -10.850 -39.205  1.00 43.94           C  
ANISOU 7893  C1'  DC P 113     5295   5952   5448    224    176    -30       C  
ATOM   7894  N1   DC P 113      -8.602  -9.545 -38.676  1.00 42.27           N  
ANISOU 7894  N1   DC P 113     5086   5733   5242    248    148    -36       N  
ATOM   7895  C2   DC P 113      -8.933  -8.366 -39.361  1.00 40.98           C  
ANISOU 7895  C2   DC P 113     4916   5564   5089    225    117    -20       C  
ATOM   7896  O2   DC P 113      -9.673  -8.429 -40.350  1.00 43.55           O  
ANISOU 7896  O2   DC P 113     5237   5902   5409    187    116      2       O  
ATOM   7897  N3   DC P 113      -8.448  -7.179 -38.916  1.00 37.35           N  
ANISOU 7897  N3   DC P 113     4449   5088   4656    246     86    -29       N  
ATOM   7898  C4   DC P 113      -7.659  -7.139 -37.845  1.00 35.22           C  
ANISOU 7898  C4   DC P 113     4181   4813   4390    289     86    -60       C  
ATOM   7899  N4   DC P 113      -7.215  -5.934 -37.462  1.00 31.35           N  
ANISOU 7899  N4   DC P 113     3676   4300   3935    310     49    -77       N  
ATOM   7900  C5   DC P 113      -7.294  -8.329 -37.129  1.00 37.53           C  
ANISOU 7900  C5   DC P 113     4482   5120   4656    314    119    -73       C  
ATOM   7901  C6   DC P 113      -7.784  -9.498 -37.575  1.00 39.88           C  
ANISOU 7901  C6   DC P 113     4784   5428   4939    291    149    -57       C  
ATOM   7902  P    DG P 114      -8.946 -14.369 -41.562  1.00 41.15           P  
ANISOU 7902  P    DG P 114     4907   5609   5121    135    229    -92       P  
ATOM   7903  OP1  DG P 114     -10.045 -15.189 -42.111  1.00 47.52           O  
ANISOU 7903  OP1  DG P 114     5693   6412   5950    118    233    -98       O  
ATOM   7904  OP2  DG P 114      -7.626 -14.984 -41.301  1.00 46.58           O  
ANISOU 7904  OP2  DG P 114     5593   6285   5819    142    242   -121       O  
ATOM   7905  O5'  DG P 114      -8.677 -13.127 -42.532  1.00 37.84           O  
ANISOU 7905  O5'  DG P 114     4493   5225   4660    105    207    -88       O  
ATOM   7906  C5'  DG P 114      -9.801 -12.481 -43.093  1.00 40.50           C  
ANISOU 7906  C5'  DG P 114     4825   5579   4984     88    191    -61       C  
ATOM   7907  C4'  DG P 114      -9.378 -11.636 -44.270  1.00 37.64           C  
ANISOU 7907  C4'  DG P 114     4452   5261   4588     51    174    -53       C  
ATOM   7908  O4'  DG P 114      -8.958 -10.343 -43.768  1.00 42.30           O  
ANISOU 7908  O4'  DG P 114     5052   5835   5184     65    153    -20       O  
ATOM   7909  C3'  DG P 114      -8.218 -12.195 -45.070  1.00 37.43           C  
ANISOU 7909  C3'  DG P 114     4411   5272   4541     28    184    -91       C  
ATOM   7910  O3'  DG P 114      -8.581 -12.081 -46.450  1.00 39.64           O  
ANISOU 7910  O3'  DG P 114     4661   5617   4782    -11    176    -91       O  
ATOM   7911  C2'  DG P 114      -7.014 -11.356 -44.626  1.00 38.92           C  
ANISOU 7911  C2'  DG P 114     4611   5449   4729     38    175    -76       C  
ATOM   7912  C1'  DG P 114      -7.640 -10.039 -44.168  1.00 36.30           C  
ANISOU 7912  C1'  DG P 114     4287   5094   4413     51    150    -26       C  
ATOM   7913  N9   DG P 114      -6.962  -9.383 -43.050  1.00 34.41           N  
ANISOU 7913  N9   DG P 114     4062   4811   4199     86    140    -23       N  
ATOM   7914  C8   DG P 114      -6.473  -9.973 -41.905  1.00 36.59           C  
ANISOU 7914  C8   DG P 114     4356   5059   4489    124    156    -51       C  
ATOM   7915  N7   DG P 114      -5.903  -9.134 -41.074  1.00 36.15           N  
ANISOU 7915  N7   DG P 114     4305   4978   4452    154    139    -50       N  
ATOM   7916  C5   DG P 114      -6.019  -7.900 -41.712  1.00 35.83           C  
ANISOU 7916  C5   DG P 114     4249   4939   4424    131    108    -17       C  
ATOM   7917  C6   DG P 114      -5.581  -6.610 -41.307  1.00 34.92           C  
ANISOU 7917  C6   DG P 114     4124   4795   4349    146     74     -5       C  
ATOM   7918  O6   DG P 114      -4.992  -6.293 -40.270  1.00 35.67           O  
ANISOU 7918  O6   DG P 114     4224   4863   4467    186     65    -32       O  
ATOM   7919  N1   DG P 114      -5.883  -5.624 -42.243  1.00 34.61           N  
ANISOU 7919  N1   DG P 114     4059   4763   4329    112     47     42       N  
ATOM   7920  C2   DG P 114      -6.531  -5.866 -43.433  1.00 34.33           C  
ANISOU 7920  C2   DG P 114     4010   4771   4262     69     54     75       C  
ATOM   7921  N2   DG P 114      -6.746  -4.800 -44.220  1.00 32.85           N  
ANISOU 7921  N2   DG P 114     3791   4592   4099     39     25    132       N  
ATOM   7922  N3   DG P 114      -6.948  -7.068 -43.819  1.00 32.44           N  
ANISOU 7922  N3   DG P 114     3782   4566   3977     57     86     53       N  
ATOM   7923  C4   DG P 114      -6.664  -8.038 -42.922  1.00 31.88           C  
ANISOU 7923  C4   DG P 114     3735   4476   3902     89    110      7       C  
HETATM 7924  P   2DA P 115      -7.621 -12.436 -47.678  1.00 40.28           P  
ANISOU 7924  P   2DA P 115     4710   5776   4820    -42    180   -127       P  
HETATM 7925  OP1 2DA P 115      -8.490 -12.493 -48.922  1.00 43.82           O  
ANISOU 7925  OP1 2DA P 115     5122   6298   5229    -72    173   -130       O  
HETATM 7926  OP2 2DA P 115      -6.712 -13.586 -47.334  1.00 41.68           O  
ANISOU 7926  OP2 2DA P 115     4889   5931   5017    -28    200   -191       O  
HETATM 7927  O5' 2DA P 115      -6.778 -11.078 -47.784  1.00 40.80           O  
ANISOU 7927  O5' 2DA P 115     4775   5859   4869    -50    164    -70       O  
HETATM 7928  C5' 2DA P 115      -5.374 -10.977 -47.953  1.00 39.83           C  
ANISOU 7928  C5' 2DA P 115     4645   5758   4732    -55    167    -78       C  
HETATM 7929  C4' 2DA P 115      -5.176  -9.476 -48.121  1.00 39.43           C  
ANISOU 7929  C4' 2DA P 115     4583   5715   4684    -67    142      1       C  
HETATM 7930  O4' 2DA P 115      -5.474  -8.807 -46.892  1.00 38.58           O  
ANISOU 7930  O4' 2DA P 115     4507   5520   4630    -37    129     23       O  
HETATM 7931  C3' 2DA P 115      -3.749  -9.133 -48.493  1.00 35.83           C  
ANISOU 7931  C3' 2DA P 115     4109   5294   4212    -79    141     13       C  
HETATM 7932  C2' 2DA P 115      -3.502  -7.830 -47.769  1.00 38.45           C  
ANISOU 7932  C2' 2DA P 115     4449   5562   4597    -67    115     71       C  
HETATM 7933  C1' 2DA P 115      -4.557  -7.740 -46.680  1.00 36.38           C  
ANISOU 7933  C1' 2DA P 115     4222   5223   4379    -35    109     63       C  
HETATM 7934  N9  2DA P 115      -3.922  -7.886 -45.348  1.00 35.99           N  
ANISOU 7934  N9  2DA P 115     4205   5103   4365      5    114     27       N  
HETATM 7935  C8  2DA P 115      -3.707  -9.036 -44.669  1.00 32.29           C  
ANISOU 7935  C8  2DA P 115     3762   4615   3893     30    140    -30       C  
HETATM 7936  N7  2DA P 115      -3.118  -8.748 -43.489  1.00 30.50           N  
ANISOU 7936  N7  2DA P 115     3555   4335   3699     67    135    -42       N  
HETATM 7937  C5  2DA P 115      -2.957  -7.402 -43.447  1.00 30.97           C  
ANISOU 7937  C5  2DA P 115     3601   4376   3791     66    102     -2       C  
HETATM 7938  C6  2DA P 115      -2.424  -6.527 -42.510  1.00 30.68           C  
ANISOU 7938  C6  2DA P 115     3567   4290   3801     97     79     -3       C  
HETATM 7939  N6  2DA P 115      -1.975  -7.002 -41.322  1.00 27.23           N  
ANISOU 7939  N6  2DA P 115     3152   3823   3370    140     90    -49       N  
HETATM 7940  N1  2DA P 115      -2.414  -5.188 -42.771  1.00 30.45           N  
ANISOU 7940  N1  2DA P 115     3510   4242   3819     86     41     42       N  
HETATM 7941  C2  2DA P 115      -2.917  -4.702 -43.919  1.00 31.56           C  
ANISOU 7941  C2  2DA P 115     3621   4417   3954     44     29     99       C  
HETATM 7942  N3  2DA P 115      -3.438  -5.532 -44.841  1.00 31.37           N  
ANISOU 7942  N3  2DA P 115     3596   4454   3870     15     54    103       N  
HETATM 7943  C4  2DA P 115      -3.466  -6.870 -44.622  1.00 30.35           C  
ANISOU 7943  C4  2DA P 115     3494   4340   3700     26     89     47       C  
TER    7944      2DA P 115                                                      
HETATM 7945  PA  TTP A 901      -0.090 -10.460 -49.097  1.00 48.39           P  
ANISOU 7945  PA  TTP A 901     5671   6970   5743    -86    180    -86       P  
HETATM 7946  O1A TTP A 901      -0.668 -11.336 -48.022  1.00 44.48           O  
ANISOU 7946  O1A TTP A 901     5219   6391   5291    -55    192   -140       O  
HETATM 7947  O2A TTP A 901      -0.461 -10.958 -50.471  1.00 46.57           O  
ANISOU 7947  O2A TTP A 901     5393   6855   5446   -113    185   -108       O  
HETATM 7948  O3A TTP A 901       1.515 -10.486 -48.960  1.00 52.70           O  
ANISOU 7948  O3A TTP A 901     6215   7520   6288    -83    187    -99       O  
HETATM 7949  PB  TTP A 901       2.645 -10.052 -50.029  1.00 49.78           P  
ANISOU 7949  PB  TTP A 901     5795   7251   5869   -110    185    -66       P  
HETATM 7950  O1B TTP A 901       3.395  -8.873 -49.463  1.00 49.18           O  
ANISOU 7950  O1B TTP A 901     5725   7120   5842   -106    165      4       O  
HETATM 7951  O2B TTP A 901       2.116  -9.734 -51.407  1.00 52.90           O  
ANISOU 7951  O2B TTP A 901     6131   7767   6200   -143    178    -23       O  
HETATM 7952  O3B TTP A 901       3.601 -11.332 -50.015  1.00 45.79           O  
ANISOU 7952  O3B TTP A 901     5292   6761   5345    -99    210   -161       O  
HETATM 7953  PG  TTP A 901       3.340 -12.639 -50.919  1.00 47.51           P  
ANISOU 7953  PG  TTP A 901     5476   7062   5513   -106    227   -253       P  
HETATM 7954  O1G TTP A 901       2.011 -12.527 -51.610  1.00 48.12           O  
ANISOU 7954  O1G TTP A 901     5530   7190   5562   -121    218   -237       O  
HETATM 7955  O2G TTP A 901       4.455 -12.704 -51.920  1.00 48.55           O  
ANISOU 7955  O2G TTP A 901     5556   7310   5582   -122    233   -265       O  
HETATM 7956  O3G TTP A 901       3.377 -13.885 -50.060  1.00 50.45           O  
ANISOU 7956  O3G TTP A 901     5882   7351   5937    -79    242   -340       O  
HETATM 7957  O5' TTP A 901      -0.467  -8.915 -48.829  1.00 46.26           O  
ANISOU 7957  O5' TTP A 901     5402   6665   5511    -90    150      9       O  
HETATM 7958  C5' TTP A 901      -0.408  -7.971 -49.894  1.00 46.42           C  
ANISOU 7958  C5' TTP A 901     5370   6761   5504   -123    132     88       C  
HETATM 7959  C4' TTP A 901      -0.006  -6.605 -49.368  1.00 47.97           C  
ANISOU 7959  C4' TTP A 901     5564   6895   5767   -120    103    163       C  
HETATM 7960  O4' TTP A 901      -0.822  -6.227 -48.253  1.00 52.33           O  
ANISOU 7960  O4' TTP A 901     6154   7345   6382    -92     88    158       O  
HETATM 7961  C3' TTP A 901       1.413  -6.593 -48.838  1.00 46.46           C  
ANISOU 7961  C3' TTP A 901     5384   6671   5600   -107    106    145       C  
HETATM 7962  O3' TTP A 901       2.386  -6.400 -49.866  1.00 48.26           O  
ANISOU 7962  O3' TTP A 901     5560   6989   5786   -136    108    185       O  
HETATM 7963  C2' TTP A 901       1.360  -5.430 -47.874  1.00 47.65           C  
ANISOU 7963  C2' TTP A 901     5545   6720   5838    -87     73    185       C  
HETATM 7964  C1' TTP A 901      -0.039  -5.539 -47.267  1.00 47.78           C  
ANISOU 7964  C1' TTP A 901     5593   6689   5873    -67     70    163       C  
HETATM 7965  N1  TTP A 901       0.136  -6.272 -45.997  1.00 44.99           N  
ANISOU 7965  N1  TTP A 901     5290   6269   5535    -25     86     86       N  
HETATM 7966  C2  TTP A 901       0.542  -5.528 -44.858  1.00 41.89           C  
ANISOU 7966  C2  TTP A 901     4912   5796   5209      9     63     81       C  
HETATM 7967  O2  TTP A 901       0.704  -4.290 -44.932  1.00 46.29           O  
ANISOU 7967  O2  TTP A 901     5438   6326   5824      2     27    135       O  
HETATM 7968  N3  TTP A 901       0.748  -6.118 -43.681  1.00 46.94           N  
ANISOU 7968  N3  TTP A 901     5589   6390   5857     50     76     19       N  
HETATM 7969  C4  TTP A 901       0.594  -7.434 -43.527  1.00 44.94           C  
ANISOU 7969  C4  TTP A 901     5361   6154   5561     59    111    -30       C  
HETATM 7970  O4  TTP A 901       0.802  -7.956 -42.409  1.00 51.60           O  
ANISOU 7970  O4  TTP A 901     6231   6959   6414     97    123    -73       O  
HETATM 7971  C5  TTP A 901       0.176  -8.249 -44.691  1.00 42.06           C  
ANISOU 7971  C5  TTP A 901     4982   5857   5142     23    132    -33       C  
HETATM 7972  C5M TTP A 901      -0.010  -9.741 -44.544  1.00 41.70           C  
ANISOU 7972  C5M TTP A 901     4953   5819   5070     33    165    -93       C  
HETATM 7973  C6  TTP A 901      -0.030  -7.609 -45.909  1.00 40.82           C  
ANISOU 7973  C6  TTP A 901     4787   5759   4965    -16    119     22       C  
HETATM 7974 CA    CA A 902       0.663 -10.941 -52.615  1.00 34.00          CA  
HETATM 7975 CA    CA A 903      -3.009 -11.459 -51.517  1.00 68.92          CA  
HETATM 7976 CA    CA A 904       3.384 -48.273 -52.697  1.00 65.60          CA  
HETATM 7977 CA    CA A 905       2.860 -16.225 -55.358  1.00 65.16          CA  
HETATM 7978 CA    CA A 906       3.414 -24.642 -12.792  1.00 68.88          CA  
HETATM 7979  O   HOH A 907      10.099 -11.005 -23.935  1.00 32.40           O  
HETATM 7980  O   HOH A 908     -19.026  -8.258 -10.446  1.00 33.26           O  
HETATM 7981  O   HOH A 909     -10.984 -22.305  -7.655  1.00 54.32           O  
HETATM 7982  O   HOH A 910     -28.333 -34.310 -26.445  1.00 42.79           O  
HETATM 7983  O   HOH A 911      10.141  -5.952  -1.385  1.00 38.00           O  
HETATM 7984  O   HOH A 912       8.555  15.891 -64.261  1.00 20.16           O  
HETATM 7985  O   HOH A 913      25.481  21.265 -44.578  1.00 24.34           O  
HETATM 7986  O   HOH A 914      29.108   7.023 -32.353  1.00 19.40           O  
HETATM 7987  O   HOH A 915      -9.673 -28.398 -45.718  1.00 19.45           O  
HETATM 7988  O   HOH A 916      -5.758 -17.379 -53.345  1.00 25.85           O  
HETATM 7989  O   HOH A 917      15.205 -21.804 -32.664  1.00 19.60           O  
HETATM 7990  O   HOH A 918      15.266  13.806 -51.451  1.00 31.36           O  
HETATM 7991  O   HOH A 919       5.616 -10.042 -21.820  1.00 55.03           O  
HETATM 7992  O   HOH A 920     -12.263 -20.727 -30.449  1.00 11.04           O  
HETATM 7993  O   HOH A 921       5.520 -33.660 -23.264  1.00 31.33           O  
HETATM 7994  O   HOH A 922       4.785  -2.463 -63.466  1.00 31.31           O  
HETATM 7995  O   HOH A 923     -32.546 -22.831 -45.496  1.00 51.59           O  
HETATM 7996  O   HOH A 924      21.677  -6.937 -25.700  1.00 23.34           O  
HETATM 7997  O   HOH A 925      29.316 -15.591 -15.945  1.00 39.26           O  
HETATM 7998  O   HOH A 926      16.370 -38.836  -8.348  1.00 27.21           O  
HETATM 7999  O   HOH A 927      10.103  -7.074 -53.510  1.00 21.89           O  
HETATM 8000  O   HOH A 928     -14.349 -29.417 -31.486  1.00 35.39           O  
HETATM 8001  O   HOH A 929      23.262 -22.962 -27.485  1.00 22.16           O  
HETATM 8002  O   HOH A 930     -21.515 -23.221 -58.317  1.00 23.03           O  
HETATM 8003  O   HOH A 931      22.946  -4.087 -39.907  1.00 23.06           O  
HETATM 8004  O   HOH A 932      22.100 -21.134 -18.077  1.00 19.42           O  
HETATM 8005  O   HOH A 933     -14.875 -23.027 -27.752  1.00 19.02           O  
HETATM 8006  O   HOH A 934      24.452 -11.426 -40.026  1.00 26.80           O  
HETATM 8007  O   HOH A 935      18.797  -5.093 -45.493  1.00 25.53           O  
HETATM 8008  O   HOH A 936      21.432  22.227 -39.606  1.00 28.91           O  
HETATM 8009  O   HOH A 937      10.703   8.566 -45.821  1.00 12.16           O  
HETATM 8010  O   HOH A 938     -12.894 -20.468  -3.127  1.00 44.44           O  
HETATM 8011  O   HOH A 939      -4.756   9.726 -57.801  1.00 25.15           O  
HETATM 8012  O   HOH A 940     -20.940  -7.631 -51.200  1.00 21.71           O  
HETATM 8013  O   HOH A 941     -12.959 -20.494 -13.088  1.00 26.97           O  
HETATM 8014  O   HOH A 942     -12.293 -22.166 -28.264  1.00 10.76           O  
HETATM 8015  O   HOH A 943     -14.618  -6.838 -62.470  1.00 22.47           O  
HETATM 8016  O   HOH A 944     -30.139 -16.732 -22.645  1.00 30.54           O  
HETATM 8017  O   HOH A 945      18.758  -2.789 -30.001  1.00 30.32           O  
HETATM 8018  O   HOH A 946     -20.089 -19.446 -61.167  1.00 25.49           O  
HETATM 8019  O   HOH A 947     -16.075  -0.039 -10.396  1.00 35.31           O  
HETATM 8020  O   HOH A 948       3.209 -23.845 -44.615  1.00 30.25           O  
HETATM 8021  O   HOH A 949     -19.030  -8.577  -7.100  1.00 52.22           O  
HETATM 8022  O   HOH A 950       6.690 -18.287 -15.939  1.00 19.60           O  
HETATM 8023  O   HOH A 951       4.706 -29.997 -38.664  1.00 27.64           O  
HETATM 8024  O   HOH A 952      20.488  12.457 -43.056  1.00 32.51           O  
HETATM 8025  O   HOH A 953       7.924  -4.777  -9.024  1.00 45.41           O  
HETATM 8026  O   HOH A 954      25.188 -20.765 -35.961  1.00 31.30           O  
HETATM 8027  O   HOH A 955       0.719 -21.851 -18.572  1.00 19.94           O  
HETATM 8028  O   HOH A 956      37.849  -8.128 -29.099  1.00 38.83           O  
HETATM 8029  O   HOH A 957       1.546 -26.824  -4.400  1.00 18.44           O  
HETATM 8030  O   HOH A 958     -16.273  -1.941 -55.645  1.00 18.00           O  
HETATM 8031  O   HOH A 959      19.180  22.140 -38.287  1.00 33.02           O  
HETATM 8032  O   HOH A 960      42.869 -14.519 -23.449  1.00 34.07           O  
HETATM 8033  O   HOH A 961      -0.674 -16.246 -31.217  1.00 21.85           O  
HETATM 8034  O   HOH A 962       6.412 -36.375  -0.391  1.00 24.12           O  
HETATM 8035  O   HOH A 963     -14.945 -30.526 -42.587  1.00 26.85           O  
HETATM 8036  O   HOH A 964     -16.892 -18.276 -61.227  1.00 26.85           O  
HETATM 8037  O   HOH A 965     -25.065  -3.787 -21.473  1.00 28.29           O  
HETATM 8038  O   HOH A 966      -5.669 -31.377 -56.318  1.00 16.76           O  
HETATM 8039  O   HOH A 967      18.083  -8.583 -56.584  1.00 26.90           O  
HETATM 8040  O   HOH A 968     -25.200 -24.230  -6.288  1.00 31.87           O  
HETATM 8041  O   HOH A 969      33.082  16.025 -24.748  1.00 37.52           O  
HETATM 8042  O   HOH A 970      25.885  -6.368 -21.934  1.00 27.44           O  
HETATM 8043  O   HOH A 971     -31.547 -29.758 -43.186  1.00 32.44           O  
HETATM 8044  O   HOH A 972     -10.801  -1.414 -62.407  1.00 19.69           O  
HETATM 8045  O   HOH A 973     -21.430 -17.394 -60.430  1.00 24.15           O  
HETATM 8046  O   HOH A 974      -4.370 -14.068 -35.056  1.00 31.81           O  
HETATM 8047  O   HOH A 975      20.060  -4.433 -52.397  1.00 28.28           O  
HETATM 8048  O   HOH A 976     -10.857 -20.352 -15.016  1.00 44.06           O  
HETATM 8049  O   HOH A 977       0.696   9.448 -38.576  1.00 26.15           O  
HETATM 8050  O   HOH A 978      -7.060 -14.606 -17.553  1.00 37.02           O  
HETATM 8051  O   HOH A 979      -2.195 -14.440 -51.477  1.00 49.14           O  
HETATM 8052  O   HOH A 980      19.525 -37.757 -15.023  1.00 39.00           O  
HETATM 8053  O   HOH A 981      -4.232 -34.524 -28.051  1.00 50.05           O  
HETATM 8054  O   HOH A 982       1.532 -14.930 -53.041  1.00 38.49           O  
HETATM 8055  O   HOH A 983      22.821  -4.452 -44.349  1.00 32.05           O  
HETATM 8056  O   HOH A 984      -4.790 -14.833 -22.717  1.00 30.20           O  
HETATM 8057  O   HOH A 985       2.398 -12.772 -13.225  1.00 34.25           O  
HETATM 8058  O   HOH A 986       5.471 -22.853 -13.209  1.00 34.56           O  
HETATM 8059  O   HOH A 987      -4.811  -4.195 -47.144  1.00 21.54           O  
HETATM 8060  O   HOH A 988      33.113   8.028 -32.654  1.00 23.18           O  
HETATM 8061  O   HOH A 989     -14.499 -21.866 -56.960  1.00 28.80           O  
HETATM 8062  O   HOH A 990       4.824  -7.829 -57.414  1.00 17.70           O  
HETATM 8063  O   HOH A 991      37.079  -4.688 -19.807  1.00 25.12           O  
HETATM 8064  O   HOH A 992     -13.426  -2.171 -59.070  1.00 47.54           O  
HETATM 8065  O   HOH A 993     -12.233 -26.186 -34.770  1.00 27.08           O  
HETATM 8066  O   HOH A 994      17.709 -39.470 -21.609  1.00 44.65           O  
HETATM 8067  O   HOH A 995      -4.876 -37.465 -56.616  1.00 44.41           O  
HETATM 8068  O   HOH A 996      27.750 -13.326 -13.857  1.00 46.06           O  
HETATM 8069  O   HOH A 997      21.066  -5.071  -0.506  1.00 22.95           O  
HETATM 8070  O   HOH A 998      16.607  15.746 -60.186  1.00 55.83           O  
HETATM 8071  O   HOH A 999     -10.159 -10.442 -48.706  1.00 22.27           O  
HETATM 8072  O   HOH A1000     -22.208 -13.945 -39.999  1.00 29.38           O  
HETATM 8073  O   HOH A1001       3.405  -9.223 -43.712  1.00 20.18           O  
HETATM 8074  O   HOH A1002      -5.270 -26.877 -27.882  1.00 40.44           O  
HETATM 8075  O   HOH A1003      12.910  18.486 -61.099  1.00 34.88           O  
HETATM 8076  O   HOH A1004      14.345 -38.018 -43.951  1.00 24.92           O  
HETATM 8077  O   HOH A1005      -7.253 -12.106 -51.373  1.00 27.05           O  
HETATM 8078  O   HOH A1006       0.683 -23.409 -51.567  1.00 31.49           O  
HETATM 8079  O   HOH A1007       3.400  -4.128 -11.683  1.00 39.31           O  
HETATM 8080  O   HOH A1008       5.425 -37.579  -3.767  1.00 27.81           O  
HETATM 8081  O   HOH A1009       6.580  11.726 -32.120  1.00 40.77           O  
HETATM 8082  O   HOH A1010      20.081 -11.010 -49.380  1.00 28.68           O  
HETATM 8083  O   HOH A1011      31.367   6.721 -41.275  1.00 26.25           O  
HETATM 8084  O   HOH A1012      16.701  -1.464  -9.551  1.00 46.94           O  
HETATM 8085  O   HOH A1013      10.054 -42.127 -19.849  1.00 25.89           O  
HETATM 8086  O   HOH A1014       5.914  -8.774 -48.785  1.00 28.37           O  
HETATM 8087  O   HOH A1015       4.514  13.228 -43.070  1.00 26.83           O  
HETATM 8088  O   HOH A1016      -3.627 -31.033  -5.779  1.00 21.53           O  
HETATM 8089  O   HOH A1017      27.128 -17.568 -24.413  1.00 23.63           O  
HETATM 8090  O   HOH A1018       4.324   1.819 -12.991  1.00 42.83           O  
HETATM 8091  O   HOH A1019      14.451 -22.687 -44.098  1.00 26.09           O  
HETATM 8092  O   HOH A1020       2.052   6.803 -35.683  1.00 19.31           O  
HETATM 8093  O   HOH A1021      12.574 -23.242   3.219  1.00 27.17           O  
HETATM 8094  O   HOH A1022       5.531 -21.536  -1.661  1.00 23.66           O  
HETATM 8095  O   HOH A1023     -36.042 -23.440 -46.536  1.00 37.30           O  
HETATM 8096  O   HOH A1024     -18.919  -6.480 -48.180  1.00 32.75           O  
HETATM 8097  O   HOH A1025      27.260 -17.620 -20.112  1.00 22.33           O  
HETATM 8098  O   HOH A1026      -4.355  14.365 -66.481  1.00 36.37           O  
HETATM 8099  O   HOH A1027     -14.243 -29.252 -24.915  1.00 27.20           O  
HETATM 8100  O   HOH A1028       3.581 -11.832 -43.141  1.00 20.11           O  
HETATM 8101  O   HOH A1029       6.297 -24.047  -0.779  1.00 23.84           O  
HETATM 8102  O   HOH A1030       0.158  12.542 -71.276  1.00 22.35           O  
HETATM 8103  O   HOH A1031      -4.551  13.151 -41.617  1.00 45.66           O  
HETATM 8104  O   HOH A1032      15.179   0.536 -10.565  1.00 43.68           O  
HETATM 8105  O   HOH A1033       9.498 -33.699 -57.436  1.00 17.08           O  
HETATM 8106  O   HOH A1034      11.118  11.211 -45.838  1.00 24.05           O  
HETATM 8107  O   HOH A1035      30.839 -12.547 -36.737  1.00 38.77           O  
HETATM 8108  O   HOH A1036       9.680 -41.370 -24.048  1.00 42.93           O  
HETATM 8109  O   HOH A1037      29.872 -19.173 -21.908  1.00 26.44           O  
HETATM 8110  O   HOH A1038      14.762 -21.575 -52.429  1.00 25.61           O  
HETATM 8111  O   HOH A1039      -5.004 -20.515  -3.642  1.00 39.05           O  
HETATM 8112  O   HOH A1040      17.732  19.423 -32.632  1.00 30.05           O  
HETATM 8113  O   HOH A1041      10.420 -12.338 -57.397  1.00 19.97           O  
HETATM 8114  O   HOH A1042     -18.778 -29.931 -34.025  1.00 27.27           O  
HETATM 8115  O   HOH A1043      12.655  13.019 -46.852  1.00 23.88           O  
HETATM 8116  O   HOH A1044      21.708  -9.196 -27.290  1.00 28.09           O  
HETATM 8117  O   HOH A1045       9.282 -28.761  -4.087  1.00 23.24           O  
HETATM 8118  O   HOH A1046      28.811  -2.135 -39.337  1.00 30.59           O  
HETATM 8119  O   HOH A1047      12.610  -8.193 -23.256  1.00 33.27           O  
HETATM 8120  O   HOH A1048      20.518 -35.916 -11.079  1.00 33.73           O  
HETATM 8121  O   HOH A1049      22.238   4.043 -49.932  1.00 29.70           O  
HETATM 8122  O   HOH A1050     -22.994 -39.347 -27.829  1.00 18.40           O  
HETATM 8123  O   HOH A1051       4.914   9.204 -65.583  1.00 26.27           O  
HETATM 8124  O   HOH A1052      34.543  15.979 -40.094  1.00 21.87           O  
HETATM 8125  O   HOH A1053      26.572 -30.644 -24.598  1.00 38.53           O  
HETATM 8126  O   HOH A1054     -16.408  -7.254 -10.645  1.00 40.24           O  
HETATM 8127  O   HOH A1055      -2.688  -0.710 -47.096  1.00 28.67           O  
HETATM 8128  O   HOH A1056      16.170  -8.448 -21.997  1.00 23.97           O  
HETATM 8129  O   HOH A1057      23.990  -1.272 -35.123  1.00 22.66           O  
HETATM 8130  O   HOH A1058       1.265  14.540 -53.652  1.00 34.57           O  
HETATM 8131  O   HOH A1059      -1.956  17.495 -56.937  1.00 29.16           O  
HETATM 8132  O   HOH A1060      -9.224  10.002 -56.405  1.00 33.88           O  
HETATM 8133  O   HOH A1061      17.650  11.051 -33.317  1.00 32.30           O  
HETATM 8134  O   HOH A1062     -16.377   2.245 -13.062  1.00 30.22           O  
HETATM 8135  O   HOH A1063       4.628 -10.472 -28.994  1.00 32.22           O  
HETATM 8136  O   HOH A1064      21.582   2.008 -57.562  1.00 36.81           O  
HETATM 8137  O   HOH A1065      -4.455   4.615 -50.834  1.00 40.68           O  
HETATM 8138  O   HOH A1066       3.258 -27.730  -0.176  1.00 31.36           O  
HETATM 8139  O   HOH A1067       8.403  15.707 -66.890  1.00 21.93           O  
HETATM 8140  O   HOH A1068     -27.731 -13.792 -25.721  1.00 33.68           O  
HETATM 8141  O   HOH A1069     -23.739  -6.693 -22.124  1.00 24.20           O  
HETATM 8142  O   HOH A1070      -4.878  18.633 -58.586  1.00 25.82           O  
HETATM 8143  O   HOH A1071     -15.356  -2.505 -62.811  1.00 50.53           O  
HETATM 8144  O   HOH A1072     -30.033 -14.188 -27.717  1.00 35.68           O  
HETATM 8145  O   HOH A1073     -11.801   1.057 -61.749  1.00 39.02           O  
HETATM 8146  O   HOH A1074       4.749 -15.132 -63.898  1.00 28.74           O  
HETATM 8147  O   HOH A1075     -31.738 -24.576 -23.919  1.00 21.74           O  
HETATM 8148  O   HOH A1076     -13.004  -3.718 -66.068  1.00 27.31           O  
HETATM 8149  O   HOH A1077      -2.810  -0.394 -51.813  1.00 20.77           O  
HETATM 8150  O   HOH A1078      -4.621  -1.982 -53.099  1.00 29.97           O  
HETATM 8151  O   HOH A1079      11.397   2.704 -67.480  1.00 27.15           O  
HETATM 8152  O   HOH A1080      12.414  -2.394 -65.739  1.00 32.55           O  
HETATM 8153  O   HOH A1081      26.777   7.968 -32.015  1.00 17.73           O  
HETATM 8154  O   HOH A1082       8.931 -14.588 -52.819  1.00 18.31           O  
HETATM 8155  O   HOH A1083      15.149 -22.013 -41.437  1.00 25.71           O  
HETATM 8156  O   HOH A1084      14.115 -19.410 -37.975  1.00 22.97           O  
HETATM 8157  O   HOH A1085      14.955 -17.714 -39.871  1.00 20.52           O  
HETATM 8158  O   HOH A1086      19.041 -21.428 -45.120  1.00 37.27           O  
HETATM 8159  O   HOH A1087      20.347 -10.009 -51.841  1.00 25.37           O  
HETATM 8160  O   HOH A1088      22.315 -12.910 -39.356  1.00 28.55           O  
HETATM 8161  O   HOH A1089      18.393 -12.645 -41.646  1.00 33.05           O  
HETATM 8162  O   HOH A1090      20.434 -15.066 -42.072  1.00 33.60           O  
HETATM 8163  O   HOH A1091       5.987  16.230 -63.830  1.00 13.88           O  
HETATM 8164  O   HOH A1092       5.612  18.079 -61.743  1.00 21.32           O  
HETATM 8165  O   HOH A1093      17.066 -32.158 -24.776  1.00 36.11           O  
HETATM 8166  O   HOH A1094      16.003 -30.510 -26.223  1.00 31.20           O  
HETATM 8167  O   HOH A1095      14.279 -30.731 -28.463  1.00 41.74           O  
HETATM 8168  O   HOH A1096      15.703 -33.628 -26.416  1.00 38.82           O  
HETATM 8169  O   HOH A1097      -8.938 -36.011 -60.619  1.00 28.15           O  
HETATM 8170  O   HOH A1098       4.029 -22.816 -39.572  1.00 19.33           O  
HETATM 8171  O   HOH A1099      -0.351 -22.783 -41.445  1.00 41.44           O  
HETATM 8172  O   HOH A1100       5.150 -18.672 -38.527  1.00 17.14           O  
HETATM 8173  O   HOH A1101       5.872 -21.363 -38.514  1.00 20.76           O  
HETATM 8174  O   HOH A1102      19.050  15.098 -42.218  1.00 26.90           O  
HETATM 8175  O   HOH A1103       9.552  14.511 -43.242  1.00 42.68           O  
HETATM 8176  O   HOH A1104      -9.343 -23.830 -36.158  1.00 38.56           O  
HETATM 8177  O   HOH A1105      -9.517 -28.672 -29.448  1.00 45.49           O  
HETATM 8178  O   HOH A1106      -3.673 -27.442 -35.524  1.00 29.28           O  
HETATM 8179  O   HOH A1107     -10.052   1.417 -49.878  1.00 25.83           O  
HETATM 8180  O   HOH A1108     -23.419  -9.147 -14.659  1.00 26.79           O  
HETATM 8181  O   HOH A1109      34.058 -19.574 -22.863  1.00 35.16           O  
HETATM 8182  O   HOH A1110       7.432  -7.949 -26.442  1.00 37.31           O  
HETATM 8183  O   HOH A1111      24.993  24.600 -42.085  1.00 31.65           O  
HETATM 8184  O   HOH A1112       3.306 -13.375  -3.739  1.00 30.36           O  
HETATM 8185  O   HOH A1113      -6.507  -4.676 -72.776  1.00 23.95           O  
HETATM 8186  O   HOH A1114      15.760  -2.019 -55.674  1.00 34.70           O  
HETATM 8187  O   HOH A1115      -7.731  -4.400 -46.975  1.00 39.64           O  
HETATM 8188  O   HOH A1116     -23.152 -12.762 -68.545  1.00 22.22           O  
HETATM 8189  O   HOH A1117      -0.672 -16.234 -50.233  1.00 51.96           O  
HETATM 8190  O   HOH A1118     -10.625 -23.717 -26.966  1.00 26.53           O  
HETATM 8191  O   HOH A1119      -7.166 -23.714 -31.146  1.00 40.16           O  
HETATM 8192  O   HOH A1120       6.168   1.242  -6.719  1.00 41.17           O  
HETATM 8193  O   HOH A1121      11.331  -4.776  -7.193  1.00 31.63           O  
HETATM 8194  O   HOH A1122       7.783  -4.739  -5.974  1.00 28.12           O  
HETATM 8195  O  AHOH A1123      11.691  -1.270  -3.797  0.50 16.29           O  
HETATM 8196  O  BHOH A1123      10.877   0.818  -4.466  0.50 11.36           O  
HETATM 8197  O   HOH A1124      -5.582   5.625 -40.814  1.00 25.38           O  
HETATM 8198  O   HOH A1125      -7.668   8.164 -44.823  1.00 45.27           O  
HETATM 8199  O   HOH A1126       4.059 -32.693 -55.094  1.00 24.85           O  
HETATM 8200  O   HOH A1127      23.718  -3.098  -5.576  1.00 46.06           O  
HETATM 8201  O   HOH A1128       2.410 -23.169 -14.715  1.00 39.69           O  
HETATM 8202  O   HOH A1129       0.078 -21.833 -14.496  1.00 39.31           O  
HETATM 8203  O   HOH A1130      15.743 -42.079  -4.661  1.00 35.85           O  
HETATM 8204  O   HOH A1131       6.520 -40.158  -4.656  1.00 35.07           O  
HETATM 8205  O   HOH A1132       3.908 -35.251  -1.647  1.00 19.78           O  
HETATM 8206  O   HOH A1133      20.705  -6.913 -23.449  1.00 22.57           O  
HETATM 8207  O   HOH A1134      13.523   4.771 -36.090  1.00 38.89           O  
HETATM 8208  O   HOH A1135     -24.992 -13.410 -46.264  1.00 28.94           O  
HETATM 8209  O   HOH A1136      15.974 -34.881 -54.559  1.00 36.03           O  
HETATM 8210  O   HOH A1137     -25.650 -32.741 -52.326  1.00 34.63           O  
HETATM 8211  O   HOH A1138     -15.807 -29.798 -61.843  1.00 26.68           O  
HETATM 8212  O   HOH A1139       5.056 -30.787 -45.988  1.00 22.13           O  
HETATM 8213  O   HOH A1140      20.164  12.115 -33.986  1.00 29.43           O  
HETATM 8214  O   HOH A1141      16.681 -41.427  -7.858  1.00 40.28           O  
HETATM 8215  O   HOH A1142      27.355  16.900 -18.910  1.00 41.14           O  
HETATM 8216  O   HOH A1143     -29.570 -40.388 -48.741  1.00 52.06           O  
HETATM 8217  O   HOH A1144       9.554 -30.750 -31.593  1.00 31.43           O  
HETATM 8218  O   HOH A1145      10.962  -9.702 -57.223  1.00 27.07           O  
HETATM 8219  O   HOH A1146       9.912 -12.441 -63.127  1.00 29.97           O  
HETATM 8220  O   HOH A1147      -5.269 -19.395 -77.708  1.00 33.57           O  
HETATM 8221  O   HOH T  19     -11.782  -0.289 -50.780  1.00 14.85           O  
HETATM 8222  O   HOH T 100      -5.056  -1.688 -46.344  1.00 25.32           O  
HETATM 8223  O   HOH T 110       2.828   4.001 -32.289  1.00 30.29           O  
HETATM 8224  O   HOH T 185       9.686   3.815 -30.950  1.00 33.45           O  
HETATM 8225  O   HOH T 215       7.310  -3.603 -30.754  1.00 32.83           O  
HETATM 8226  O   HOH T 253      -2.218   6.819 -38.770  1.00 22.18           O  
HETATM 8227  O   HOH T 254      -0.579   4.435 -35.942  1.00 28.96           O  
HETATM 8228  O   HOH P  67      -8.307 -17.463 -42.397  1.00 19.98           O  
HETATM 8229  O   HOH P 116     -34.140 -13.096 -38.652  1.00 40.52           O  
HETATM 8230  O   HOH P 122      -2.689 -10.668 -41.537  1.00 29.99           O  
HETATM 8231  O   HOH P 141     -19.081   6.255 -26.632  1.00 39.01           O  
HETATM 8232  O   HOH P 194     -20.129  -0.179 -38.464  1.00 43.84           O  
HETATM 8233  O   HOH P1124     -32.382 -13.417 -41.768  1.00 44.45           O  
CONECT  972 7978                                                                
CONECT  973 7978                                                                
CONECT 3414 7974                                                                
CONECT 3415 7974 7975                                                           
CONECT 3419 7974                                                                
CONECT 4156 7976                                                                
CONECT 4174 7976                                                                
CONECT 4374 7976                                                                
CONECT 5109 7974                                                                
CONECT 5110 7975                                                                
CONECT 7360 7371                                                                
CONECT 7371 7360 7372 7373 7374                                                 
CONECT 7372 7371                                                                
CONECT 7373 7371                                                                
CONECT 7374 7371 7375                                                           
CONECT 7375 7374 7376                                                           
CONECT 7376 7375 7377 7378                                                      
CONECT 7377 7376 7381                                                           
CONECT 7378 7376 7379 7380                                                      
CONECT 7379 7378 7392                                                           
CONECT 7380 7378 7381                                                           
CONECT 7381 7377 7380 7382                                                      
CONECT 7382 7381 7383 7391                                                      
CONECT 7383 7382 7384                                                           
CONECT 7384 7383 7385                                                           
CONECT 7385 7384 7386 7391                                                      
CONECT 7386 7385 7387                                                           
CONECT 7387 7386 7388                                                           
CONECT 7388 7387 7389 7390                                                      
CONECT 7389 7388                                                                
CONECT 7390 7388 7391                                                           
CONECT 7391 7382 7385 7390                                                      
CONECT 7392 7379                                                                
CONECT 7910 7924                                                                
CONECT 7924 7910 7925 7926 7927                                                 
CONECT 7925 7924                                                                
CONECT 7926 7924                                                                
CONECT 7927 7924 7928                                                           
CONECT 7928 7927 7929                                                           
CONECT 7929 7928 7930 7931                                                      
CONECT 7930 7929 7933                                                           
CONECT 7931 7929 7932                                                           
CONECT 7932 7931 7933                                                           
CONECT 7933 7930 7932 7934                                                      
CONECT 7934 7933 7935 7943                                                      
CONECT 7935 7934 7936                                                           
CONECT 7936 7935 7937                                                           
CONECT 7937 7936 7938 7943                                                      
CONECT 7938 7937 7939 7940                                                      
CONECT 7939 7938                                                                
CONECT 7940 7938 7941                                                           
CONECT 7941 7940 7942                                                           
CONECT 7942 7941 7943                                                           
CONECT 7943 7934 7937 7942                                                      
CONECT 7945 7946 7947 7948 7957                                                 
CONECT 7946 7945                                                                
CONECT 7947 7945 7974 7975                                                      
CONECT 7948 7945 7949                                                           
CONECT 7949 7948 7950 7951 7952                                                 
CONECT 7950 7949                                                                
CONECT 7951 7949 7974                                                           
CONECT 7952 7949 7953                                                           
CONECT 7953 7952 7954 7955 7956                                                 
CONECT 7954 7953 7974                                                           
CONECT 7955 7953                                                                
CONECT 7956 7953                                                                
CONECT 7957 7945 7958                                                           
CONECT 7958 7957 7959                                                           
CONECT 7959 7958 7960 7961                                                      
CONECT 7960 7959 7964                                                           
CONECT 7961 7959 7962 7963                                                      
CONECT 7962 7961                                                                
CONECT 7963 7961 7964                                                           
CONECT 7964 7960 7963 7965                                                      
CONECT 7965 7964 7966 7973                                                      
CONECT 7966 7965 7967 7968                                                      
CONECT 7967 7966                                                                
CONECT 7968 7966 7969                                                           
CONECT 7969 7968 7970 7971                                                      
CONECT 7970 7969                                                                
CONECT 7971 7969 7972 7973                                                      
CONECT 7972 7971                                                                
CONECT 7973 7965 7971                                                           
CONECT 7974 3414 3415 3419 5109                                                 
CONECT 7974 7947 7951 7954                                                      
CONECT 7975 3415 5110 7947 8051                                                 
CONECT 7976 4156 4174 4374                                                      
CONECT 7977 8054                                                                
CONECT 7978  972  973 8058 8201                                                 
CONECT 8051 7975                                                                
CONECT 8054 7977                                                                
CONECT 8058 7978                                                                
CONECT 8201 7978                                                                
MASTER      522    0    8   36   34    0   11    6 8216    3   93   73          
END

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Related entries of code: 3suo

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
3sq4	RCSB PDB PDBbind	13aa, >3SQ4_3\|Chain... *
3sup	RCSB PDB PDBbind	13aa, >3SUP_3\|Chain... at 100%
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
3sq4	RCSB PDB PDBbind	dTTP Opposite 2AP (GC rich sequence) DNA

Entry Information

PDB ID	3suo
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	RB69 DNA Polymerase (Y567A) mutant
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=15.1uM
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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