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HEADER    TRANSFERASE/DNA                         11-JUL-11   3SUP              
TITLE     RB69 DNA POLYMERASE (Y567A) TERNARY COMPLEX WITH DCTP 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 3SUP    1       JRNL                                     
REVDAT   2   16-NOV-11 3SUP    1       JRNL                                     
REVDAT   1   09-NOV-11 3SUP    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.    2.32 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) : 2.32                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 88.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 48550                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2607                            
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) : 2.32                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.38                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3279                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.07                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2470                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 180                          
REMARK   3   BIN FREE R VALUE                    : 0.3010                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7367                                    
REMARK   3   NUCLEIC ACID ATOMS       : 591                                     
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 263                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.26                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.41000                                             
REMARK   3    B22 (A**2) : 0.77000                                              
REMARK   3    B33 (A**2) : -0.36000                                             
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): 0.347         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.255         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.177         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.066        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8256 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11287 ; 1.124 ; 2.056       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   906 ; 5.076 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   376 ;35.323 ;24.122       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1351 ;14.727 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    47 ;13.725 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1194 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6107 ; 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):  4512 ; 1.479 ; 4.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7316 ; 2.584 ; 6.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3744 ; 2.939 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3969 ; 4.291 ; 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   904        A   904                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.3220   2.5990  29.1810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0632 T22:   0.2117                                     
REMARK   3      T33:   0.1514 T12:   0.0374                                     
REMARK   3      T13:   0.0052 T23:  -0.0171                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4408 L22:   0.1202                                     
REMARK   3      L33:   0.0182 L12:   0.1772                                     
REMARK   3      L13:   0.0655 L23:   0.0293                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1142 S12:  -0.0667 S13:  -0.1130                       
REMARK   3      S21:  -0.0430 S22:   0.0863 S23:  -0.0572                       
REMARK   3      S31:  -0.0251 S32:  -0.0067 S33:   0.0280                       
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): -24.8750  -2.4110  31.9620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0812 T22:   0.0776                                     
REMARK   3      T33:   0.0808 T12:   0.0025                                     
REMARK   3      T13:   0.0109 T23:  -0.0227                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2229 L22:   1.0566                                     
REMARK   3      L33:   0.2796 L12:   0.1190                                     
REMARK   3      L13:   0.1231 L23:   0.4014                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0011 S12:  -0.0001 S13:  -0.0365                       
REMARK   3      S21:   0.0185 S22:  -0.0295 S23:   0.0666                       
REMARK   3      S31:   0.0199 S32:  -0.0450 S33:   0.0284                       
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): -10.3370  22.0420  50.5570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0808 T22:   0.0645                                     
REMARK   3      T33:   0.0317 T12:  -0.0023                                     
REMARK   3      T13:   0.0107 T23:   0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2863 L22:   0.9462                                     
REMARK   3      L33:   0.9023 L12:   0.2553                                     
REMARK   3      L13:  -0.0404 L23:   0.0100                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0382 S12:  -0.0138 S13:  -0.0265                       
REMARK   3      S21:   0.0835 S22:  -0.0693 S23:  -0.0077                       
REMARK   3      S31:  -0.0517 S32:   0.0342 S33:   0.0311                       
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):   3.6970   6.6220   5.0400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1208 T22:   0.1270                                     
REMARK   3      T33:   0.0102 T12:  -0.0269                                     
REMARK   3      T13:   0.0105 T23:  -0.0214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7464 L22:   0.8658                                     
REMARK   3      L33:   0.1772 L12:   0.6056                                     
REMARK   3      L13:   0.2084 L23:   0.0140                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0818 S12:   0.2029 S13:  -0.0596                       
REMARK   3      S21:  -0.1123 S22:   0.1164 S23:  -0.0183                       
REMARK   3      S31:  -0.0119 S32:   0.1094 S33:  -0.0347                       
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):  -9.4610  26.1480  18.3850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1512 T22:   0.0972                                     
REMARK   3      T33:   0.0629 T12:   0.0097                                     
REMARK   3      T13:  -0.0299 T23:   0.0113                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4292 L22:   3.8491                                     
REMARK   3      L33:   0.2964 L12:   0.0849                                     
REMARK   3      L13:   0.0874 L23:  -0.5587                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0804 S12:   0.1073 S13:   0.1088                       
REMARK   3      S21:   0.1956 S22:  -0.0274 S23:  -0.0329                       
REMARK   3      S31:  -0.0937 S32:  -0.0426 S33:   0.1078                       
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):   9.3740  22.7820  17.3940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1601 T22:   0.1063                                     
REMARK   3      T33:   0.0745 T12:  -0.0579                                     
REMARK   3      T13:  -0.0082 T23:   0.0085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4737 L22:   0.6171                                     
REMARK   3      L33:   1.5036 L12:  -0.2786                                     
REMARK   3      L13:   0.6508 L23:   0.0065                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0736 S12:  -0.0135 S13:   0.0617                       
REMARK   3      S21:  -0.0329 S22:   0.1265 S23:  -0.0712                       
REMARK   3      S31:  -0.0357 S32:   0.0052 S33:  -0.0529                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   738        A   901                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.3320  20.7140  37.4650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0653 T22:   0.1083                                     
REMARK   3      T33:   0.0308 T12:   0.0302                                     
REMARK   3      T13:  -0.0040 T23:  -0.0469                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4437 L22:   0.4979                                     
REMARK   3      L33:   1.0491 L12:  -0.1789                                     
REMARK   3      L13:  -0.1622 L23:  -0.3248                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1467 S12:  -0.2626 S13:   0.1031                       
REMARK   3      S21:   0.0083 S22:   0.1388 S23:  -0.0682                       
REMARK   3      S31:  -0.0357 S32:   0.0777 S33:   0.0079                       
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 3SUP 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 RCSB066674.                                      
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   : 48550                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.320                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 88.575                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.100                              
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) : 2.32                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.36                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
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   (%): 52.59                                     
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       37.37800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.41150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.17850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.41150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.37800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.17850            
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: 6850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 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. =   1.8 DEGREES          
REMARK 500     DC T   6   O4' -  C1' -  N1  ANGL. DEV. =   3.5 DEGREES          
REMARK 500     DG T  13   O4' -  C1' -  N9  ANGL. DEV. =  -5.6 DEGREES          
REMARK 500     DG T  15   O4' -  C1' -  N9  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DC T  16   O4' -  C1' -  N1  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DG P 104   O4' -  C1' -  N9  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DC P 105   O4' -  C1' -  N1  ANGL. DEV. =   3.9 DEGREES          
REMARK 500     DG P 112   O4' -  C1' -  N9  ANGL. DEV. =   2.6 DEGREES          
REMARK 500     DC P 113   O4' -  C1' -  N1  ANGL. DEV. =   2.2 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       55.92   -103.25                                   
REMARK 500    ASP A 121       39.21    -94.49                                   
REMARK 500    PHE A 221      -69.50   -123.93                                   
REMARK 500    ASN A 255     -153.02   -103.99                                   
REMARK 500    SER A 414       68.12     28.52                                   
REMARK 500    ASN A 424       52.12     71.99                                   
REMARK 500    PRO A 458        2.00    -64.46                                   
REMARK 500    ASP A 579      117.12   -161.37                                   
REMARK 500    THR A 622      -67.50     66.59                                   
REMARK 500    GLU A 686      -69.10   -108.86                                   
REMARK 500    GLU A 716       45.81     37.21                                   
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 A1135        DISTANCE =  7.57 ANGSTROMS                       
REMARK 525    HOH A1151        DISTANCE =  5.24 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 905  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 623   OD1                                                    
REMARK 620 2 DCP A 904   O1G 157.8                                              
REMARK 620 3 DCP A 904   O2B  84.1  77.8                                        
REMARK 620 4 LEU A 412   O    90.8 100.6  85.7                                  
REMARK 620 5 ASP A 411   OD1 124.5  76.8 147.1  78.7                            
REMARK 620 6 ASP A 411   OD2  80.7 113.9 161.0 105.6  51.7                      
REMARK 620 7 DCP A 904   O2A  75.8  88.1  79.3 160.7 120.3  86.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 907  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS A 531   O                                                      
REMARK 620 2 ASN A 507   OD1  77.2                                              
REMARK 620 3 ASN A 505   O   161.3  96.7                                        
REMARK 620 4 HOH A1060   O   100.3 121.0  67.4                                  
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 DCP A 904   O2A                                                    
REMARK 620 2 ASP A 623   OD2  80.9                                              
REMARK 620 3 ASP A 411   OD2  84.6  76.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 909  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 116   OE1                                                    
REMARK 620 2 GLU A 116   OE2  44.4                                              
REMARK 620 3 HOH A 998   O    76.6  79.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 908  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A1087   O                                                      
REMARK 620 2 HOH A1068   O    54.7                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCP A 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 905                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 906                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 907                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 908                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 909                  
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: 3SUO   RELATED DB: PDB                                   
REMARK 900 RB69 DNA POLYMERASE (Y567A) TERNARY COMPLEX WITH DTTP                
REMARK 900 OPPOSITE 2AP (GC RICH SEQUENCE)                                      
REMARK 900 RELATED ID: 3SUQ   RELATED DB: PDB                                   
REMARK 900 RB69 DNA POLYMERASE (Y567A) TERNARY COMPLEX WITH DCTP                
REMARK 900 OPPOSITE 2AP (AT RICH SEQUENCE)                                      
DBREF  3SUP A    1   903  UNP    Q38087   DPOL_BPR69       1    903             
DBREF  3SUP T    3    18  PDB    3SUP     3SUP             3     18             
DBREF  3SUP P  103   115  PDB    3SUP     3SUP           103    115             
SEQADV 3SUP ALA A  222  UNP  Q38087    ASP   222 ENGINEERED MUTATION            
SEQADV 3SUP ALA A  327  UNP  Q38087    ASP   327 ENGINEERED MUTATION            
SEQADV 3SUP ALA A  567  UNP  Q38087    TYR   567 ENGINEERED MUTATION            
SEQRES   1 A  903  MET LYS GLU PHE TYR LEU THR VAL GLU GLN ILE GLY ASP          
SEQRES   2 A  903  SER ILE PHE GLU ARG TYR ILE ASP SER ASN GLY ARG GLU          
SEQRES   3 A  903  ARG THR ARG GLU VAL GLU TYR LYS PRO SER LEU PHE ALA          
SEQRES   4 A  903  HIS CYS PRO GLU SER GLN ALA THR LYS TYR PHE ASP ILE          
SEQRES   5 A  903  TYR GLY LYS PRO CYS THR ARG LYS LEU PHE ALA ASN MET          
SEQRES   6 A  903  ARG ASP ALA SER GLN TRP ILE LYS ARG MET GLU ASP ILE          
SEQRES   7 A  903  GLY LEU GLU ALA LEU GLY MET ASP ASP PHE LYS LEU ALA          
SEQRES   8 A  903  TYR LEU SER ASP THR TYR ASN TYR GLU ILE LYS TYR ASP          
SEQRES   9 A  903  HIS THR LYS ILE ARG VAL ALA ASN PHE ASP ILE GLU VAL          
SEQRES  10 A  903  THR SER PRO ASP GLY PHE PRO GLU PRO SER GLN ALA LYS          
SEQRES  11 A  903  HIS PRO ILE ASP ALA ILE THR HIS TYR ASP SER ILE ASP          
SEQRES  12 A  903  ASP ARG PHE TYR VAL PHE ASP LEU LEU ASN SER PRO TYR          
SEQRES  13 A  903  GLY ASN VAL GLU GLU TRP SER ILE GLU ILE ALA ALA LYS          
SEQRES  14 A  903  LEU GLN GLU GLN GLY GLY ASP GLU VAL PRO SER GLU ILE          
SEQRES  15 A  903  ILE ASP LYS ILE ILE TYR MET PRO PHE ASP ASN GLU LYS          
SEQRES  16 A  903  GLU LEU LEU MET GLU TYR LEU ASN PHE TRP GLN GLN LYS          
SEQRES  17 A  903  THR PRO VAL ILE LEU THR GLY TRP ASN VAL GLU SER PHE          
SEQRES  18 A  903  ALA ILE PRO TYR VAL TYR ASN ARG ILE LYS ASN ILE PHE          
SEQRES  19 A  903  GLY GLU SER THR ALA LYS ARG LEU SER PRO HIS ARG LYS          
SEQRES  20 A  903  THR ARG VAL LYS VAL ILE GLU ASN MET TYR GLY SER ARG          
SEQRES  21 A  903  GLU ILE ILE THR LEU PHE GLY ILE SER VAL LEU ASP TYR          
SEQRES  22 A  903  ILE ASP LEU TYR LYS LYS PHE SER PHE THR ASN GLN PRO          
SEQRES  23 A  903  SER TYR SER LEU ASP TYR ILE SER GLU PHE GLU LEU ASN          
SEQRES  24 A  903  VAL GLY LYS LEU LYS TYR ASP GLY PRO ILE SER LYS LEU          
SEQRES  25 A  903  ARG GLU SER ASN HIS GLN ARG TYR ILE SER TYR ASN ILE          
SEQRES  26 A  903  ILE ALA VAL TYR ARG VAL LEU GLN ILE ASP ALA LYS ARG          
SEQRES  27 A  903  GLN PHE ILE ASN LEU SER LEU ASP MET GLY TYR TYR ALA          
SEQRES  28 A  903  LYS ILE GLN ILE GLN SER VAL PHE SER PRO ILE LYS THR          
SEQRES  29 A  903  TRP ASP ALA ILE ILE PHE ASN SER LEU LYS GLU GLN ASN          
SEQRES  30 A  903  LYS VAL ILE PRO GLN GLY ARG SER HIS PRO VAL GLN PRO          
SEQRES  31 A  903  TYR PRO GLY ALA PHE VAL LYS GLU PRO ILE PRO ASN ARG          
SEQRES  32 A  903  TYR LYS TYR VAL MET SER PHE ASP LEU THR SER LEU TYR          
SEQRES  33 A  903  PRO SER ILE ILE ARG GLN VAL ASN ILE SER PRO GLU THR          
SEQRES  34 A  903  ILE ALA GLY THR PHE LYS VAL ALA PRO LEU HIS ASP TYR          
SEQRES  35 A  903  ILE ASN ALA VAL ALA GLU ARG PRO SER ASP VAL TYR SER          
SEQRES  36 A  903  CYS SER PRO ASN GLY MET MET TYR TYR LYS ASP ARG ASP          
SEQRES  37 A  903  GLY VAL VAL PRO THR GLU ILE THR LYS VAL PHE ASN GLN          
SEQRES  38 A  903  ARG LYS GLU HIS LYS GLY TYR MET LEU ALA ALA GLN ARG          
SEQRES  39 A  903  ASN GLY GLU ILE ILE LYS GLU ALA LEU HIS ASN PRO ASN          
SEQRES  40 A  903  LEU SER VAL ASP GLU PRO LEU ASP VAL ASP TYR ARG PHE          
SEQRES  41 A  903  ASP PHE SER ASP GLU ILE LYS GLU LYS ILE LYS LYS LEU          
SEQRES  42 A  903  SER ALA LYS SER LEU ASN GLU MET LEU PHE ARG ALA GLN          
SEQRES  43 A  903  ARG THR GLU VAL ALA GLY MET THR ALA GLN ILE ASN ARG          
SEQRES  44 A  903  LYS LEU LEU ILE ASN SER LEU ALA GLY ALA LEU GLY ASN          
SEQRES  45 A  903  VAL TRP PHE ARG TYR TYR ASP LEU ARG ASN ALA THR ALA          
SEQRES  46 A  903  ILE THR THR PHE GLY GLN MET ALA LEU GLN TRP ILE GLU          
SEQRES  47 A  903  ARG LYS VAL ASN GLU TYR LEU ASN GLU VAL CYS GLY THR          
SEQRES  48 A  903  GLU GLY GLU ALA PHE VAL LEU TYR GLY ASP THR ASP SER          
SEQRES  49 A  903  ILE TYR VAL SER ALA ASP LYS ILE ILE ASP LYS VAL GLY          
SEQRES  50 A  903  GLU SER LYS PHE ARG ASP THR ASN HIS TRP VAL ASP PHE          
SEQRES  51 A  903  LEU ASP LYS PHE ALA ARG GLU ARG MET GLU PRO ALA ILE          
SEQRES  52 A  903  ASP ARG GLY PHE ARG GLU MET CYS GLU TYR MET ASN ASN          
SEQRES  53 A  903  LYS GLN HIS LEU MET PHE MET ASP ARG GLU ALA ILE ALA          
SEQRES  54 A  903  GLY PRO PRO LEU GLY SER LYS GLY ILE GLY GLY PHE TRP          
SEQRES  55 A  903  THR GLY LYS LYS ARG TYR ALA LEU ASN VAL TRP ASP MET          
SEQRES  56 A  903  GLU GLY THR ARG TYR ALA GLU PRO LYS LEU LYS ILE MET          
SEQRES  57 A  903  GLY LEU GLU THR GLN LYS SER SER THR PRO LYS ALA VAL          
SEQRES  58 A  903  GLN LYS ALA LEU LYS GLU CYS ILE ARG ARG MET LEU GLN          
SEQRES  59 A  903  GLU GLY GLU GLU SER LEU GLN GLU TYR PHE LYS GLU PHE          
SEQRES  60 A  903  GLU LYS GLU PHE ARG GLN LEU ASN TYR ILE SER ILE ALA          
SEQRES  61 A  903  SER VAL SER SER ALA ASN ASN ILE ALA LYS TYR ASP VAL          
SEQRES  62 A  903  GLY GLY PHE PRO GLY PRO LYS CYS PRO PHE HIS ILE ARG          
SEQRES  63 A  903  GLY ILE LEU THR TYR ASN ARG ALA ILE LYS GLY ASN ILE          
SEQRES  64 A  903  ASP ALA PRO GLN VAL VAL GLU GLY GLU LYS VAL TYR VAL          
SEQRES  65 A  903  LEU PRO LEU ARG GLU GLY ASN PRO PHE GLY ASP LYS CYS          
SEQRES  66 A  903  ILE ALA TRP PRO SER GLY THR GLU ILE THR ASP LEU ILE          
SEQRES  67 A  903  LYS ASP ASP VAL LEU HIS TRP MET ASP TYR THR VAL LEU          
SEQRES  68 A  903  LEU GLU LYS THR PHE ILE LYS PRO LEU GLU GLY PHE THR          
SEQRES  69 A  903  SER ALA ALA LYS LEU ASP TYR GLU LYS LYS ALA SER LEU          
SEQRES  70 A  903  PHE ASP MET PHE ASP PHE                                      
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 3SUP 2PR T    4   DG  2-AMINOPURINE-2'-DEOXYRIBO-5'-MONOPHOSPHA          
MODRES 3SUP 2DA P  115   DA  2',3'-DIDEOXYADENOSINE-5'-MONOPHOSPHATE            
HET    2PR  T   4      21                                                       
HET    2DA  P 115      20                                                       
HET    DCP  A 904      28                                                       
HET     CA  A 905       1                                                       
HET     CA  A 906       1                                                       
HET     CA  A 907       1                                                       
HET     CA  A 908       1                                                       
HET     CA  A 909       1                                                       
HETNAM     2PR 2-AMINO-9-[2-DEOXYRIBOFURANOSYL]-9H-PURINE-5'-                   
HETNAM   2 2PR  MONOPHOSPHATE                                                   
HETNAM     2DA 2',3'-DIDEOXYADENOSINE-5'-MONOPHOSPHATE                          
HETNAM     DCP 2'-DEOXYCYTIDINE-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  DCP    C9 H16 N3 O13 P3                                             
FORMUL   5   CA    5(CA 2+)                                                     
FORMUL  10  HOH   *263(H2 O)                                                    
HELIX    1   1 ASN A   64  GLY A   79  1                                  16    
HELIX    2   2 ASP A   87  TYR A   97  1                                  11    
HELIX    3   3 ASP A  104  ILE A  108  5                                   5    
HELIX    4   4 SER A  163  LYS A  169  1                                   7    
HELIX    5   5 LEU A  170  GLY A  174  5                                   5    
HELIX    6   6 PRO A  179  ASP A  184  1                                   6    
HELIX    7   7 ASN A  193  LYS A  208  1                                  16    
HELIX    8   8 PHE A  221  GLY A  235  1                                  15    
HELIX    9   9 GLY A  235  LYS A  240  1                                   6    
HELIX   10  10 ARG A  241  SER A  243  5                                   3    
HELIX   11  11 ASP A  272  SER A  281  1                                  10    
HELIX   12  12 SER A  289  ASN A  299  1                                  11    
HELIX   13  13 PRO A  308  ASN A  316  1                                   9    
HELIX   14  14 ASN A  316  GLN A  339  1                                  24    
HELIX   15  15 GLN A  339  LYS A  352  1                                  14    
HELIX   16  16 GLN A  354  PHE A  359  5                                   6    
HELIX   17  17 SER A  360  GLN A  376  1                                  17    
HELIX   18  18 SER A  414  ASN A  424  1                                  11    
HELIX   19  19 SER A  426  GLU A  428  5                                   3    
HELIX   20  20 PRO A  438  ASN A  444  1                                   7    
HELIX   21  21 GLY A  469  LEU A  503  1                                  35    
HELIX   22  22 SER A  523  LYS A  531  1                                   9    
HELIX   23  23 SER A  534  LEU A  570  1                                  37    
HELIX   24  24 ASP A  579  GLY A  610  1                                  32    
HELIX   25  25 ALA A  629  GLY A  637  1                                   9    
HELIX   26  26 GLU A  638  PHE A  641  5                                   4    
HELIX   27  27 ASP A  643  ARG A  658  1                                  16    
HELIX   28  28 ARG A  658  MET A  674  1                                  17    
HELIX   29  29 LEU A  730  LYS A  734  5                                   5    
HELIX   30  30 PRO A  738  GLU A  755  1                                  18    
HELIX   31  31 GLY A  756  PHE A  771  1                                  16    
HELIX   32  32 ARG A  772  LEU A  774  5                                   3    
HELIX   33  33 ASN A  775  ALA A  780  5                                   6    
HELIX   34  34 ILE A  788  LYS A  790  5                                   3    
HELIX   35  35 PRO A  802  ILE A  815  1                                  14    
HELIX   36  36 THR A  855  MET A  866  1                                  12    
HELIX   37  37 ASP A  867  PHE A  876  1                                  10    
HELIX   38  38 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  ILE A  20   N  PHE A   4           
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  THR A 214   N  ALA A 111           
SHEET    6   C 6 SER A 269  VAL A 270  1  O  SER A 269   N  LEU A 213           
SHEET    1   D 2 ASN A 153  SER A 154  0                                        
SHEET    2   D 2 GLY A 157  ASN A 158 -1  O  GLY A 157   N  SER A 154           
SHEET    1   E 2 THR A 248  VAL A 252  0                                        
SHEET    2   E 2 GLU A 261  LEU A 265 -1  O  THR A 264   N  ARG A 249           
SHEET    1   F 7 ASN A 402  ARG A 403  0                                        
SHEET    2   F 7 GLY A 700  GLY A 704 -1  O  TRP A 702   N  ASN A 402           
SHEET    3   F 7 ARG A 707  MET A 715 -1  O  ALA A 709   N  PHE A 701           
SHEET    4   F 7 MET A 683  ALA A 689 -1  N  ILE A 688   O  TRP A 713           
SHEET    5   F 7 VAL A 407  LEU A 412 -1  N  VAL A 407   O  ALA A 689           
SHEET    6   F 7 SER A 624  SER A 628 -1  O  VAL A 627   N  MET A 408           
SHEET    7   F 7 VAL A 617  ASP A 621 -1  N  LEU A 618   O  TYR A 626           
SHEET    1   G 4 ASN A 402  ARG A 403  0                                        
SHEET    2   G 4 GLY A 700  GLY A 704 -1  O  TRP A 702   N  ASN A 402           
SHEET    3   G 4 ARG A 707  MET A 715 -1  O  ALA A 709   N  PHE A 701           
SHEET    4   G 4 THR A 718  MET A 728 -1  O  MET A 728   N  TYR A 708           
SHEET    1   H 3 ILE A 430  THR A 433  0                                        
SHEET    2   H 3 MET A 461  TYR A 463 -1  O  MET A 462   N  ALA A 431           
SHEET    3   H 3 SER A 455  SER A 457 -1  N  SER A 455   O  TYR A 463           
SHEET    1   I 3 SER A 781  SER A 784  0                                        
SHEET    2   I 3 LYS A 829  PRO A 834 -1  O  VAL A 830   N  SER A 783           
SHEET    3   I 3 CYS A 845  PRO A 849 -1  O  TRP A 848   N  TYR A 831           
SHEET    1   J 2 ASP A 792  VAL A 793  0                                        
SHEET    2   J 2 PHE A 796  PRO A 797 -1  O  PHE A 796   N  VAL A 793           
LINK         O3'  DC T   3                 P   2PR T   4     1555   1555  1.60  
LINK         O3' 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 905     1555   1555  2.14  
LINK         O   LYS A 531                CA    CA A 907     1555   1555  2.30  
LINK         O1G DCP A 904                CA    CA A 905     1555   1555  2.31  
LINK         O2B DCP A 904                CA    CA A 905     1555   1555  2.31  
LINK         O   LEU A 412                CA    CA A 905     1555   1555  2.33  
LINK         OD1 ASN A 507                CA    CA A 907     1555   1555  2.39  
LINK         O   ASN A 505                CA    CA A 907     1555   1555  2.40  
LINK         O2A DCP A 904                CA    CA A 906     1555   1555  2.49  
LINK         OD1 ASP A 411                CA    CA A 905     1555   1555  2.50  
LINK         OD2 ASP A 411                CA    CA A 905     1555   1555  2.54  
LINK         O2A DCP A 904                CA    CA A 905     1555   1555  2.63  
LINK         OD2 ASP A 623                CA    CA A 906     1555   1555  2.74  
LINK         OD2 ASP A 411                CA    CA A 906     1555   1555  2.74  
LINK         OE1 GLU A 116                CA    CA A 909     1555   1555  2.75  
LINK         OE2 GLU A 116                CA    CA A 909     1555   1555  3.02  
LINK        CA    CA A 907                 O   HOH A1060     1555   1555  2.32  
LINK        CA    CA A 908                 O   HOH A1087     1555   1555  2.41  
LINK        CA    CA A 909                 O   HOH A 998     1555   1555  2.51  
LINK        CA    CA A 908                 O   HOH A1068     1555   1555  3.19  
CISPEP   1 ASP A  899    MET A  900          0        -4.06                     
SITE     1 AC1 17 ASP A 411  LEU A 412  SER A 414  LEU A 415                    
SITE     2 AC1 17 TYR A 416  ARG A 482  LYS A 560  ASN A 564                    
SITE     3 AC1 17 THR A 622  ASP A 623   CA A 905   CA A 906                    
SITE     4 AC1 17 HOH A 942  HOH A1124  HOH A1141  2DA P 115                    
SITE     5 AC1 17 2PR T   4                                                     
SITE     1 AC2  4 ASP A 411  LEU A 412  ASP A 623  DCP A 904                    
SITE     1 AC3  3 ASP A 411  ASP A 623  DCP A 904                               
SITE     1 AC4  4 ASN A 505  ASN A 507  LYS A 531  HOH A1060                    
SITE     1 AC5  2 GLU A 716  HOH A1087                                          
SITE     1 AC6  2 GLU A 116  HOH A 998                                          
CRYST1   74.756  120.357  130.823  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      0.013377  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008309  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007644        0.00000                         
ATOM      1  N   MET A   1     -37.787  18.139  29.749  1.00 57.30           N  
ANISOU    1  N   MET A   1     7030   6991   7750    395   -564   -634       N  
ATOM      2  CA  MET A   1     -36.467  17.646  29.266  1.00 58.16           C  
ANISOU    2  CA  MET A   1     7219   7119   7761    370   -536   -565       C  
ATOM      3  C   MET A   1     -36.353  16.128  29.419  1.00 55.53           C  
ANISOU    3  C   MET A   1     6863   6819   7418    341   -472   -558       C  
ATOM      4  O   MET A   1     -37.103  15.517  30.183  1.00 55.02           O  
ANISOU    4  O   MET A   1     6726   6769   7410    333   -428   -598       O  
ATOM      5  CB  MET A   1     -35.324  18.359  30.004  1.00 60.62           C  
ANISOU    5  CB  MET A   1     7564   7450   8018    356   -487   -525       C  
ATOM      6  CG  MET A   1     -35.144  17.967  31.487  1.00 66.99           C  
ANISOU    6  CG  MET A   1     8320   8298   8835    332   -391   -533       C  
ATOM      7  SD  MET A   1     -33.796  18.847  32.338  1.00 73.98           S  
ANISOU    7  SD  MET A   1     9247   9201   9660    319   -347   -490       S  
ATOM      8  CE  MET A   1     -32.385  18.433  31.310  1.00 73.43           C  
ANISOU    8  CE  MET A   1     9263   9134   9503    300   -349   -424       C  
ATOM      9  N   LYS A   2     -35.425  15.529  28.676  1.00 53.28           N  
ANISOU    9  N   LYS A   2     6642   6541   7062    324   -466   -509       N  
ATOM     10  CA  LYS A   2     -35.115  14.107  28.822  1.00 52.43           C  
ANISOU   10  CA  LYS A   2     6523   6464   6936    296   -405   -496       C  
ATOM     11  C   LYS A   2     -34.330  13.873  30.109  1.00 48.58           C  
ANISOU   11  C   LYS A   2     6022   6014   6424    270   -315   -475       C  
ATOM     12  O   LYS A   2     -33.380  14.599  30.405  1.00 47.86           O  
ANISOU   12  O   LYS A   2     5968   5928   6288    266   -300   -443       O  
ATOM     13  CB  LYS A   2     -34.323  13.580  27.614  1.00 53.79           C  
ANISOU   13  CB  LYS A   2     6768   6628   7040    287   -425   -454       C  
ATOM     14  CG  LYS A   2     -35.172  12.972  26.493  1.00 60.09           C  
ANISOU   14  CG  LYS A   2     7568   7401   7863    301   -489   -478       C  
ATOM     15  CD  LYS A   2     -35.791  11.633  26.916  1.00 64.37           C  
ANISOU   15  CD  LYS A   2     8044   7964   8451    286   -446   -505       C  
ATOM     16  CE  LYS A   2     -36.524  10.933  25.772  1.00 65.01           C  
ANISOU   16  CE  LYS A   2     8130   8020   8553    298   -508   -526       C  
ATOM     17  NZ  LYS A   2     -35.603  10.169  24.877  1.00 62.31           N  
ANISOU   17  NZ  LYS A   2     7856   7683   8136    281   -500   -484       N  
ATOM     18  N   GLU A   3     -34.741  12.861  30.867  1.00 44.02           N  
ANISOU   18  N   GLU A   3     5393   5457   5874    251   -257   -494       N  
ATOM     19  CA  GLU A   3     -34.080  12.499  32.118  1.00 41.56           C  
ANISOU   19  CA  GLU A   3     5076   5177   5538    225   -176   -476       C  
ATOM     20  C   GLU A   3     -32.640  12.012  31.919  1.00 38.56           C  
ANISOU   20  C   GLU A   3     4753   4812   5084    207   -151   -421       C  
ATOM     21  O   GLU A   3     -32.309  11.447  30.877  1.00 39.35           O  
ANISOU   21  O   GLU A   3     4885   4906   5159    205   -175   -402       O  
ATOM     22  CB  GLU A   3     -34.900  11.446  32.862  1.00 39.46           C  
ANISOU   22  CB  GLU A   3     4754   4923   5316    206   -122   -510       C  
ATOM     23  CG  GLU A   3     -36.317  11.900  33.116  1.00 45.51           C  
ANISOU   23  CG  GLU A   3     5453   5673   6166    221   -137   -573       C  
ATOM     24  CD  GLU A   3     -37.054  11.080  34.158  1.00 47.94           C  
ANISOU   24  CD  GLU A   3     5707   5993   6515    194    -63   -609       C  
ATOM     25  OE1 GLU A   3     -38.185  11.480  34.497  1.00 55.44           O  
ANISOU   25  OE1 GLU A   3     6595   6930   7540    201    -62   -668       O  
ATOM     26  OE2 GLU A   3     -36.528  10.056  34.643  1.00 46.02           O  
ANISOU   26  OE2 GLU A   3     5482   5769   6234    164     -5   -582       O  
ATOM     27  N   PHE A   4     -31.788  12.273  32.906  1.00 34.89           N  
ANISOU   27  N   PHE A   4     4302   4364   4589    195   -107   -399       N  
ATOM     28  CA  PHE A   4     -30.444  11.703  32.936  1.00 34.02           C  
ANISOU   28  CA  PHE A   4     4233   4269   4424    176    -77   -356       C  
ATOM     29  C   PHE A   4     -29.999  11.367  34.353  1.00 31.83           C  
ANISOU   29  C   PHE A   4     3949   4010   4134    158    -18   -349       C  
ATOM     30  O   PHE A   4     -30.424  11.996  35.316  1.00 32.71           O  
ANISOU   30  O   PHE A   4     4040   4123   4263    160     -1   -369       O  
ATOM     31  CB  PHE A   4     -29.419  12.586  32.209  1.00 33.47           C  
ANISOU   31  CB  PHE A   4     4214   4188   4313    184   -108   -325       C  
ATOM     32  CG  PHE A   4     -29.302  13.983  32.755  1.00 33.63           C  
ANISOU   32  CG  PHE A   4     4240   4203   4337    196   -119   -328       C  
ATOM     33  CD1 PHE A   4     -30.211  14.967  32.392  1.00 32.20           C  
ANISOU   33  CD1 PHE A   4     4047   3999   4188    220   -168   -354       C  
ATOM     34  CD2 PHE A   4     -28.258  14.322  33.606  1.00 30.22           C  
ANISOU   34  CD2 PHE A   4     3823   3782   3878    187    -87   -307       C  
ATOM     35  CE1 PHE A   4     -30.088  16.279  32.894  1.00 32.59           C  
ANISOU   35  CE1 PHE A   4     4101   4040   4241    232   -181   -357       C  
ATOM     36  CE2 PHE A   4     -28.133  15.619  34.103  1.00 30.31           C  
ANISOU   36  CE2 PHE A   4     3839   3785   3892    198    -99   -310       C  
ATOM     37  CZ  PHE A   4     -29.050  16.599  33.738  1.00 27.20           C  
ANISOU   37  CZ  PHE A   4     3434   3372   3530    220   -144   -335       C  
ATOM     38  N   TYR A   5     -29.166  10.341  34.467  1.00 32.91           N  
ANISOU   38  N   TYR A   5     4107   4158   4241    140     10   -323       N  
ATOM     39  CA  TYR A   5     -28.620   9.937  35.756  1.00 32.73           C  
ANISOU   39  CA  TYR A   5     4091   4146   4199    123     55   -312       C  
ATOM     40  C   TYR A   5     -27.553  10.910  36.219  1.00 30.69           C  
ANISOU   40  C   TYR A   5     3860   3887   3912    129     51   -292       C  
ATOM     41  O   TYR A   5     -26.952  11.620  35.417  1.00 29.20           O  
ANISOU   41  O   TYR A   5     3691   3692   3712    139     20   -278       O  
ATOM     42  CB  TYR A   5     -28.053   8.509  35.693  1.00 34.63           C  
ANISOU   42  CB  TYR A   5     4346   4392   4420    105     76   -293       C  
ATOM     43  CG  TYR A   5     -26.804   8.350  34.839  1.00 33.94           C  
ANISOU   43  CG  TYR A   5     4288   4302   4304    107     58   -264       C  
ATOM     44  CD1 TYR A   5     -26.900   8.114  33.470  1.00 33.57           C  
ANISOU   44  CD1 TYR A   5     4246   4250   4260    112     31   -263       C  
ATOM     45  CD2 TYR A   5     -25.526   8.425  35.408  1.00 33.33           C  
ANISOU   45  CD2 TYR A   5     4236   4226   4201    102     68   -241       C  
ATOM     46  CE1 TYR A   5     -25.750   7.962  32.681  1.00 35.99           C  
ANISOU   46  CE1 TYR A   5     4581   4553   4540    109     24   -241       C  
ATOM     47  CE2 TYR A   5     -24.372   8.276  34.627  1.00 32.47           C  
ANISOU   47  CE2 TYR A   5     4147   4113   4076    102     57   -222       C  
ATOM     48  CZ  TYR A   5     -24.497   8.049  33.264  1.00 33.44           C  
ANISOU   48  CZ  TYR A   5     4274   4232   4199    103     40   -223       C  
ATOM     49  OH  TYR A   5     -23.381   7.901  32.480  1.00 35.36           O  
ANISOU   49  OH  TYR A   5     4538   4470   4426     98     39   -209       O  
ATOM     50  N   LEU A   6     -27.341  10.947  37.528  1.00 32.39           N  
ANISOU   50  N   LEU A   6     4081   4108   4116    120     82   -292       N  
ATOM     51  CA  LEU A   6     -26.233  11.680  38.118  1.00 28.49           C  
ANISOU   51  CA  LEU A   6     3615   3614   3597    123     78   -273       C  
ATOM     52  C   LEU A   6     -25.196  10.682  38.624  1.00 28.70           C  
ANISOU   52  C   LEU A   6     3668   3641   3597    109     94   -250       C  
ATOM     53  O   LEU A   6     -24.032  10.734  38.221  1.00 26.93           O  
ANISOU   53  O   LEU A   6     3460   3413   3359    111     78   -230       O  
ATOM     54  CB  LEU A   6     -26.738  12.569  39.254  1.00 31.86           C  
ANISOU   54  CB  LEU A   6     4035   4040   4030    126     93   -293       C  
ATOM     55  CG  LEU A   6     -27.735  13.676  38.885  1.00 31.37           C  
ANISOU   55  CG  LEU A   6     3944   3972   4002    144     73   -322       C  
ATOM     56  CD1 LEU A   6     -28.375  14.224  40.132  1.00 34.85           C  
ANISOU   56  CD1 LEU A   6     4373   4414   4453    141    102   -350       C  
ATOM     57  CD2 LEU A   6     -27.042  14.792  38.118  1.00 32.21           C  
ANISOU   57  CD2 LEU A   6     4067   4069   4102    161     30   -306       C  
ATOM     58  N   THR A   7     -25.629   9.768  39.495  1.00 28.70           N  
ANISOU   58  N   THR A   7     3672   3643   3591     93    126   -255       N  
ATOM     59  CA  THR A   7     -24.769   8.715  40.047  1.00 28.10           C  
ANISOU   59  CA  THR A   7     3626   3562   3490     80    134   -235       C  
ATOM     60  C   THR A   7     -25.512   7.396  40.127  1.00 29.05           C  
ANISOU   60  C   THR A   7     3742   3680   3614     61    161   -241       C  
ATOM     61  O   THR A   7     -26.738   7.378  40.218  1.00 32.86           O  
ANISOU   61  O   THR A   7     4201   4167   4117     54    185   -265       O  
ATOM     62  CB  THR A   7     -24.303   9.038  41.480  1.00 28.93           C  
ANISOU   62  CB  THR A   7     3765   3660   3569     75    144   -231       C  
ATOM     63  OG1 THR A   7     -25.439   9.081  42.351  1.00 30.90           O  
ANISOU   63  OG1 THR A   7     4014   3910   3817     62    182   -253       O  
ATOM     64  CG2 THR A   7     -23.547  10.358  41.548  1.00 24.20           C  
ANISOU   64  CG2 THR A   7     3169   3058   2967     92    118   -227       C  
ATOM     65  N   VAL A   8     -24.776   6.289  40.116  1.00 30.02           N  
ANISOU   65  N   VAL A   8     3887   3797   3723     53    158   -222       N  
ATOM     66  CA  VAL A   8     -25.392   4.970  40.242  1.00 30.45           C  
ANISOU   66  CA  VAL A   8     3944   3846   3778     33    183   -224       C  
ATOM     67  C   VAL A   8     -24.501   4.039  41.061  1.00 33.23           C  
ANISOU   67  C   VAL A   8     4342   4182   4102     22    180   -203       C  
ATOM     68  O   VAL A   8     -23.278   4.054  40.921  1.00 34.08           O  
ANISOU   68  O   VAL A   8     4463   4283   4203     35    149   -187       O  
ATOM     69  CB  VAL A   8     -25.749   4.358  38.844  1.00 32.28           C  
ANISOU   69  CB  VAL A   8     4144   4085   4037     36    171   -229       C  
ATOM     70  CG1 VAL A   8     -24.506   3.876  38.089  1.00 31.77           C  
ANISOU   70  CG1 VAL A   8     4089   4015   3966     45    144   -209       C  
ATOM     71  CG2 VAL A   8     -26.753   3.240  38.981  1.00 28.18           C  
ANISOU   71  CG2 VAL A   8     3616   3561   3529     15    202   -241       C  
ATOM     72  N   GLU A   9     -25.118   3.246  41.932  1.00 33.21           N  
ANISOU   72  N   GLU A   9     4366   4169   4084     -1    213   -206       N  
ATOM     73  CA  GLU A   9     -24.379   2.299  42.755  1.00 35.32           C  
ANISOU   73  CA  GLU A   9     4688   4413   4320    -13    206   -185       C  
ATOM     74  C   GLU A   9     -25.161   1.014  42.936  1.00 36.79           C  
ANISOU   74  C   GLU A   9     4887   4587   4502    -40    239   -187       C  
ATOM     75  O   GLU A   9     -26.393   1.024  42.938  1.00 41.43           O  
ANISOU   75  O   GLU A   9     5452   5184   5106    -57    282   -209       O  
ATOM     76  CB  GLU A   9     -24.075   2.894  44.138  1.00 33.79           C  
ANISOU   76  CB  GLU A   9     4544   4205   4087    -17    209   -181       C  
ATOM     77  CG  GLU A   9     -23.386   4.258  44.115  1.00 34.81           C  
ANISOU   77  CG  GLU A   9     4661   4344   4220      8    180   -182       C  
ATOM     78  CD  GLU A   9     -21.887   4.194  43.818  1.00 33.31           C  
ANISOU   78  CD  GLU A   9     4478   4143   4036     29    128   -165       C  
ATOM     79  OE1 GLU A   9     -21.371   3.114  43.476  1.00 37.73           O  
ANISOU   79  OE1 GLU A   9     5043   4690   4601     28    111   -155       O  
ATOM     80  OE2 GLU A   9     -21.213   5.236  43.939  1.00 35.09           O  
ANISOU   80  OE2 GLU A   9     4699   4370   4263     46    104   -166       O  
ATOM     81  N   GLN A  10     -24.440  -0.088  43.088  1.00 36.18           N  
ANISOU   81  N   GLN A  10     4846   4489   4411    -45    219   -167       N  
ATOM     82  CA  GLN A  10     -25.046  -1.332  43.509  1.00 36.74           C  
ANISOU   82  CA  GLN A  10     4949   4541   4470    -75    249   -164       C  
ATOM     83  C   GLN A  10     -24.713  -1.560  44.975  1.00 38.92           C  
ANISOU   83  C   GLN A  10     5308   4787   4693    -92    253   -149       C  
ATOM     84  O   GLN A  10     -23.541  -1.579  45.364  1.00 40.21           O  
ANISOU   84  O   GLN A  10     5510   4931   4837    -75    204   -131       O  
ATOM     85  CB  GLN A  10     -24.557  -2.508  42.665  1.00 36.92           C  
ANISOU   85  CB  GLN A  10     4961   4555   4511    -70    221   -154       C  
ATOM     86  CG  GLN A  10     -25.225  -3.825  43.038  1.00 38.29           C  
ANISOU   86  CG  GLN A  10     5167   4707   4674   -102    252   -151       C  
ATOM     87  CD  GLN A  10     -24.520  -5.058  42.482  1.00 43.07           C  
ANISOU   87  CD  GLN A  10     5779   5294   5290    -96    217   -137       C  
ATOM     88  OE1 GLN A  10     -23.753  -4.987  41.512  1.00 42.12           O  
ANISOU   88  OE1 GLN A  10     5622   5184   5196    -69    179   -137       O  
ATOM     89  NE2 GLN A  10     -24.787  -6.203  43.102  1.00 40.75           N  
ANISOU   89  NE2 GLN A  10     5536   4970   4975   -123    232   -126       N  
ATOM     90  N   ILE A  11     -25.757  -1.710  45.780  1.00 40.14           N  
ANISOU   90  N   ILE A  11     5491   4933   4826   -126    311   -160       N  
ATOM     91  CA  ILE A  11     -25.627  -2.093  47.179  1.00 41.46           C  
ANISOU   91  CA  ILE A  11     5753   5066   4935   -152    325   -146       C  
ATOM     92  C   ILE A  11     -26.515  -3.315  47.413  1.00 41.53           C  
ANISOU   92  C   ILE A  11     5791   5055   4935   -194    376   -148       C  
ATOM     93  O   ILE A  11     -27.754  -3.217  47.453  1.00 39.44           O  
ANISOU   93  O   ILE A  11     5498   4802   4687   -222    444   -174       O  
ATOM     94  CB  ILE A  11     -26.007  -0.934  48.141  1.00 42.79           C  
ANISOU   94  CB  ILE A  11     5944   5239   5074   -161    358   -160       C  
ATOM     95  CG1 ILE A  11     -25.105   0.288  47.899  1.00 45.33           C  
ANISOU   95  CG1 ILE A  11     6237   5578   5407   -120    306   -159       C  
ATOM     96  CG2 ILE A  11     -25.896  -1.393  49.588  1.00 43.62           C  
ANISOU   96  CG2 ILE A  11     6162   5304   5109   -192    375   -145       C  
ATOM     97  CD1 ILE A  11     -25.567   1.573  48.587  1.00 47.18           C  
ANISOU   97  CD1 ILE A  11     6473   5825   5628   -122    337   -179       C  
ATOM     98  N   GLY A  12     -25.868  -4.468  47.554  1.00 43.02           N  
ANISOU   98  N   GLY A  12     6032   5210   5102   -199    342   -122       N  
ATOM     99  CA  GLY A  12     -26.576  -5.737  47.663  1.00 44.36           C  
ANISOU   99  CA  GLY A  12     6231   5358   5267   -237    383   -120       C  
ATOM    100  C   GLY A  12     -27.463  -5.965  46.454  1.00 43.36           C  
ANISOU  100  C   GLY A  12     6010   5260   5204   -238    411   -144       C  
ATOM    101  O   GLY A  12     -26.982  -6.022  45.324  1.00 45.44           O  
ANISOU  101  O   GLY A  12     6214   5543   5508   -206    366   -143       O  
ATOM    102  N   ASP A  13     -28.764  -6.071  46.696  1.00 42.18           N  
ANISOU  102  N   ASP A  13     5848   5114   5066   -277    488   -170       N  
ATOM    103  CA  ASP A  13     -29.719  -6.334  45.628  1.00 40.52           C  
ANISOU  103  CA  ASP A  13     5550   4926   4920   -281    513   -198       C  
ATOM    104  C   ASP A  13     -30.459  -5.078  45.193  1.00 38.86           C  
ANISOU  104  C   ASP A  13     5259   4752   4753   -266    534   -234       C  
ATOM    105  O   ASP A  13     -31.439  -5.147  44.459  1.00 35.88           O  
ANISOU  105  O   ASP A  13     4810   4389   4432   -271    559   -266       O  
ATOM    106  CB  ASP A  13     -30.697  -7.439  46.044  1.00 41.03           C  
ANISOU  106  CB  ASP A  13     5643   4965   4984   -334    580   -208       C  
ATOM    107  CG  ASP A  13     -30.046  -8.807  46.061  1.00 42.76           C  
ANISOU  107  CG  ASP A  13     5921   5148   5178   -342    547   -175       C  
ATOM    108  OD1 ASP A  13     -30.322  -9.589  46.994  1.00 47.73           O  
ANISOU  108  OD1 ASP A  13     6631   5739   5765   -386    588   -164       O  
ATOM    109  OD2 ASP A  13     -29.249  -9.096  45.142  1.00 39.29           O  
ANISOU  109  OD2 ASP A  13     5451   4717   4760   -304    481   -161       O  
ATOM    110  N   SER A  14     -29.966  -3.928  45.638  1.00 38.81           N  
ANISOU  110  N   SER A  14     5265   4757   4725   -245    517   -231       N  
ATOM    111  CA  SER A  14     -30.552  -2.664  45.245  1.00 40.10           C  
ANISOU  111  CA  SER A  14     5358   4951   4928   -226    526   -264       C  
ATOM    112  C   SER A  14     -29.613  -1.867  44.357  1.00 39.84           C  
ANISOU  112  C   SER A  14     5289   4941   4908   -176    454   -250       C  
ATOM    113  O   SER A  14     -28.390  -1.913  44.526  1.00 38.78           O  
ANISOU  113  O   SER A  14     5197   4797   4739   -158    406   -219       O  
ATOM    114  CB  SER A  14     -30.949  -1.854  46.482  1.00 40.30           C  
ANISOU  114  CB  SER A  14     5419   4970   4921   -248    577   -280       C  
ATOM    115  OG  SER A  14     -32.147  -2.371  47.044  1.00 42.69           O  
ANISOU  115  OG  SER A  14     5727   5260   5234   -297    660   -309       O  
ATOM    116  N   ILE A  15     -30.202  -1.169  43.391  1.00 39.78           N  
ANISOU  116  N   ILE A  15     5204   4959   4953   -156    446   -277       N  
ATOM    117  CA  ILE A  15     -29.512  -0.127  42.646  1.00 37.83           C  
ANISOU  117  CA  ILE A  15     4926   4731   4716   -114    391   -271       C  
ATOM    118  C   ILE A  15     -29.923   1.199  43.271  1.00 37.83           C  
ANISOU  118  C   ILE A  15     4917   4741   4717   -110    411   -292       C  
ATOM    119  O   ILE A  15     -31.116   1.502  43.383  1.00 37.70           O  
ANISOU  119  O   ILE A  15     4861   4729   4736   -124    453   -330       O  
ATOM    120  CB  ILE A  15     -29.889  -0.127  41.133  1.00 37.22           C  
ANISOU  120  CB  ILE A  15     4781   4670   4690    -93    361   -285       C  
ATOM    121  CG1 ILE A  15     -29.214  -1.285  40.366  1.00 33.98           C  
ANISOU  121  CG1 ILE A  15     4381   4253   4277    -89    330   -262       C  
ATOM    122  CG2 ILE A  15     -29.542   1.213  40.488  1.00 36.86           C  
ANISOU  122  CG2 ILE A  15     4706   4642   4656    -57    320   -288       C  
ATOM    123  CD1 ILE A  15     -27.681  -1.267  40.356  1.00 35.62           C  
ANISOU  123  CD1 ILE A  15     4627   4457   4451    -69    285   -228       C  
ATOM    124  N   PHE A  16     -28.938   1.983  43.691  1.00 37.33           N  
ANISOU  124  N   PHE A  16     4885   4678   4620    -91    381   -273       N  
ATOM    125  CA  PHE A  16     -29.212   3.327  44.186  1.00 35.37           C  
ANISOU  125  CA  PHE A  16     4626   4439   4374    -82    391   -292       C  
ATOM    126  C   PHE A  16     -28.829   4.335  43.113  1.00 34.77           C  
ANISOU  126  C   PHE A  16     4504   4381   4327    -43    339   -292       C  
ATOM    127  O   PHE A  16     -27.678   4.376  42.678  1.00 35.08           O  
ANISOU  127  O   PHE A  16     4558   4421   4350    -24    293   -264       O  
ATOM    128  CB  PHE A  16     -28.462   3.594  45.492  1.00 33.31           C  
ANISOU  128  CB  PHE A  16     4438   4163   4055    -89    395   -274       C  
ATOM    129  CG  PHE A  16     -29.070   2.918  46.692  1.00 37.07           C  
ANISOU  129  CG  PHE A  16     4968   4619   4498   -132    458   -281       C  
ATOM    130  CD1 PHE A  16     -29.998   3.590  47.493  1.00 41.23           C  
ANISOU  130  CD1 PHE A  16     5494   5147   5026   -152    516   -316       C  
ATOM    131  CD2 PHE A  16     -28.714   1.616  47.033  1.00 38.14           C  
ANISOU  131  CD2 PHE A  16     5162   4731   4600   -154    461   -256       C  
ATOM    132  CE1 PHE A  16     -30.564   2.968  48.615  1.00 42.14           C  
ANISOU  132  CE1 PHE A  16     5667   5240   5105   -198    584   -325       C  
ATOM    133  CE2 PHE A  16     -29.274   0.983  48.153  1.00 40.42           C  
ANISOU  133  CE2 PHE A  16     5513   4994   4849   -199    522   -261       C  
ATOM    134  CZ  PHE A  16     -30.199   1.660  48.945  1.00 42.20           C  
ANISOU  134  CZ  PHE A  16     5740   5221   5071   -223    588   -295       C  
ATOM    135  N   GLU A  17     -29.806   5.131  42.680  1.00 33.22           N  
ANISOU  135  N   GLU A  17     4252   4195   4173    -34    346   -326       N  
ATOM    136  CA  GLU A  17     -29.595   6.089  41.607  1.00 32.83           C  
ANISOU  136  CA  GLU A  17     4166   4157   4150     -1    296   -328       C  
ATOM    137  C   GLU A  17     -30.012   7.494  42.007  1.00 33.58           C  
ANISOU  137  C   GLU A  17     4243   4257   4260     12    298   -353       C  
ATOM    138  O   GLU A  17     -31.131   7.707  42.456  1.00 34.86           O  
ANISOU  138  O   GLU A  17     4377   4417   4451      0    337   -391       O  
ATOM    139  CB  GLU A  17     -30.371   5.688  40.347  1.00 31.76           C  
ANISOU  139  CB  GLU A  17     3981   4025   4061      6    280   -346       C  
ATOM    140  CG  GLU A  17     -29.936   6.479  39.119  1.00 33.65           C  
ANISOU  140  CG  GLU A  17     4204   4270   4312     38    221   -337       C  
ATOM    141  CD  GLU A  17     -30.929   6.463  37.965  1.00 36.61           C  
ANISOU  141  CD  GLU A  17     4531   4644   4735     50    197   -364       C  
ATOM    142  OE1 GLU A  17     -30.686   7.204  36.990  1.00 35.27           O  
ANISOU  142  OE1 GLU A  17     4357   4473   4570     74    149   -360       O  
ATOM    143  OE2 GLU A  17     -31.946   5.736  38.020  1.00 36.45           O  
ANISOU  143  OE2 GLU A  17     4481   4619   4749     34    224   -392       O  
ATOM    144  N   ARG A  18     -29.103   8.446  41.834  1.00 33.46           N  
ANISOU  144  N   ARG A  18     4241   4245   4228     36    259   -334       N  
ATOM    145  CA  ARG A  18     -29.463   9.852  41.860  1.00 34.05           C  
ANISOU  145  CA  ARG A  18     4292   4322   4324     55    245   -356       C  
ATOM    146  C   ARG A  18     -29.610  10.249  40.405  1.00 33.58           C  
ANISOU  146  C   ARG A  18     4199   4264   4297     79    196   -358       C  
ATOM    147  O   ARG A  18     -28.836   9.797  39.568  1.00 34.93           O  
ANISOU  147  O   ARG A  18     4383   4435   4452     85    168   -330       O  
ATOM    148  CB  ARG A  18     -28.380  10.689  42.547  1.00 32.86           C  
ANISOU  148  CB  ARG A  18     4180   4169   4135     64    230   -335       C  
ATOM    149  CG  ARG A  18     -28.128  10.306  44.002  1.00 35.64           C  
ANISOU  149  CG  ARG A  18     4581   4514   4445     41    269   -330       C  
ATOM    150  CD  ARG A  18     -26.859  10.973  44.532  1.00 35.89           C  
ANISOU  150  CD  ARG A  18     4654   4541   4442     54    239   -305       C  
ATOM    151  NE  ARG A  18     -27.038  12.408  44.727  1.00 31.57           N  
ANISOU  151  NE  ARG A  18     4091   3997   3908     71    230   -324       N  
ATOM    152  CZ  ARG A  18     -26.048  13.273  44.938  1.00 31.44           C  
ANISOU  152  CZ  ARG A  18     4095   3977   3875     87    197   -309       C  
ATOM    153  NH1 ARG A  18     -24.784  12.857  44.987  1.00 28.55           N  
ANISOU  153  NH1 ARG A  18     3762   3603   3483     89    170   -277       N  
ATOM    154  NH2 ARG A  18     -26.323  14.564  45.101  1.00 25.57           N  
ANISOU  154  NH2 ARG A  18     3336   3234   3147    102    189   -328       N  
ATOM    155  N   TYR A  19     -30.606  11.076  40.099  1.00 34.10           N  
ANISOU  155  N   TYR A  19     4223   4327   4407     94    185   -394       N  
ATOM    156  CA  TYR A  19     -30.903  11.422  38.714  1.00 32.92           C  
ANISOU  156  CA  TYR A  19     4049   4171   4287    116    132   -399       C  
ATOM    157  C   TYR A  19     -31.637  12.751  38.612  1.00 34.88           C  
ANISOU  157  C   TYR A  19     4267   4411   4576    139    106   -432       C  
ATOM    158  O   TYR A  19     -32.135  13.283  39.610  1.00 36.26           O  
ANISOU  158  O   TYR A  19     4426   4586   4765    135    137   -461       O  
ATOM    159  CB  TYR A  19     -31.713  10.304  38.036  1.00 34.24           C  
ANISOU  159  CB  TYR A  19     4188   4337   4486    108    136   -415       C  
ATOM    160  CG  TYR A  19     -33.128  10.127  38.564  1.00 32.74           C  
ANISOU  160  CG  TYR A  19     3947   4142   4349     96    173   -467       C  
ATOM    161  CD1 TYR A  19     -33.373   9.476  39.777  1.00 34.48           C  
ANISOU  161  CD1 TYR A  19     4174   4367   4560     65    242   -477       C  
ATOM    162  CD2 TYR A  19     -34.223  10.612  37.844  1.00 32.78           C  
ANISOU  162  CD2 TYR A  19     3902   4136   4418    116    138   -509       C  
ATOM    163  CE1 TYR A  19     -34.698   9.315  40.268  1.00 36.10           C  
ANISOU  163  CE1 TYR A  19     4330   4566   4819     48    287   -530       C  
ATOM    164  CE2 TYR A  19     -35.542  10.449  38.313  1.00 31.23           C  
ANISOU  164  CE2 TYR A  19     3649   3933   4284    105    174   -565       C  
ATOM    165  CZ  TYR A  19     -35.769   9.800  39.519  1.00 32.53           C  
ANISOU  165  CZ  TYR A  19     3816   4104   4440     69    254   -577       C  
ATOM    166  OH  TYR A  19     -37.062   9.653  39.976  1.00 34.29           O  
ANISOU  166  OH  TYR A  19     3982   4319   4729     53    299   -637       O  
ATOM    167  N   ILE A  20     -31.682  13.286  37.398  1.00 34.66           N  
ANISOU  167  N   ILE A  20     4236   4372   4562    163     46   -430       N  
ATOM    168  CA  ILE A  20     -32.455  14.479  37.104  1.00 35.80           C  
ANISOU  168  CA  ILE A  20     4353   4501   4750    188      6   -462       C  
ATOM    169  C   ILE A  20     -33.727  14.066  36.355  1.00 36.70           C  
ANISOU  169  C   ILE A  20     4419   4601   4923    197    -19   -503       C  
ATOM    170  O   ILE A  20     -33.658  13.491  35.262  1.00 33.60           O  
ANISOU  170  O   ILE A  20     4039   4203   4525    201    -53   -488       O  
ATOM    171  CB  ILE A  20     -31.632  15.507  36.266  1.00 34.87           C  
ANISOU  171  CB  ILE A  20     4274   4370   4604    209    -51   -432       C  
ATOM    172  CG1 ILE A  20     -30.411  16.026  37.052  1.00 34.04           C  
ANISOU  172  CG1 ILE A  20     4206   4274   4451    202    -29   -401       C  
ATOM    173  CG2 ILE A  20     -32.519  16.644  35.771  1.00 34.32           C  
ANISOU  173  CG2 ILE A  20     4182   4277   4582    238   -107   -466       C  
ATOM    174  CD1 ILE A  20     -30.720  16.764  38.358  1.00 34.85           C  
ANISOU  174  CD1 ILE A  20     4292   4380   4568    202      1   -426       C  
ATOM    175  N   ASP A  21     -34.883  14.361  36.947  1.00 37.90           N  
ANISOU  175  N   ASP A  21     4517   4747   5136    200      0   -557       N  
ATOM    176  CA  ASP A  21     -36.161  14.021  36.328  1.00 39.86           C  
ANISOU  176  CA  ASP A  21     4710   4980   5457    209    -26   -605       C  
ATOM    177  C   ASP A  21     -36.540  14.975  35.187  1.00 42.31           C  
ANISOU  177  C   ASP A  21     5016   5261   5798    248   -119   -619       C  
ATOM    178  O   ASP A  21     -35.834  15.952  34.910  1.00 41.12           O  
ANISOU  178  O   ASP A  21     4909   5103   5613    264   -158   -590       O  
ATOM    179  CB  ASP A  21     -37.271  13.936  37.382  1.00 40.01           C  
ANISOU  179  CB  ASP A  21     4665   4998   5537    194     35   -666       C  
ATOM    180  CG  ASP A  21     -37.638  15.292  37.984  1.00 40.53           C  
ANISOU  180  CG  ASP A  21     4707   5054   5637    213     28   -702       C  
ATOM    181  OD1 ASP A  21     -37.248  16.362  37.448  1.00 41.52           O  
ANISOU  181  OD1 ASP A  21     4857   5167   5751    243    -37   -686       O  
ATOM    182  OD2 ASP A  21     -38.338  15.275  39.018  1.00 36.81           O  
ANISOU  182  OD2 ASP A  21     4196   4587   5204    195     93   -748       O  
ATOM    183  N   SER A  22     -37.671  14.694  34.547  1.00 44.13           N  
ANISOU  183  N   SER A  22     5198   5471   6097    261   -156   -664       N  
ATOM    184  CA  SER A  22     -38.117  15.452  33.376  1.00 46.72           C  
ANISOU  184  CA  SER A  22     5530   5765   6457    299   -256   -679       C  
ATOM    185  C   SER A  22     -38.408  16.931  33.653  1.00 47.04           C  
ANISOU  185  C   SER A  22     5558   5785   6531    327   -295   -706       C  
ATOM    186  O   SER A  22     -38.712  17.687  32.732  1.00 47.94           O  
ANISOU  186  O   SER A  22     5685   5865   6666    360   -385   -715       O  
ATOM    187  CB  SER A  22     -39.332  14.775  32.737  1.00 46.62           C  
ANISOU  187  CB  SER A  22     5460   5732   6520    308   -291   -730       C  
ATOM    188  OG  SER A  22     -40.347  14.560  33.699  1.00 49.30           O  
ANISOU  188  OG  SER A  22     5719   6076   6938    296   -234   -794       O  
ATOM    189  N   ASN A  23     -38.284  17.342  34.910  1.00 46.97           N  
ANISOU  189  N   ASN A  23     5531   5794   6523    314   -229   -717       N  
ATOM    190  CA  ASN A  23     -38.525  18.733  35.300  1.00 48.34           C  
ANISOU  190  CA  ASN A  23     5690   5951   6728    338   -257   -745       C  
ATOM    191  C   ASN A  23     -37.257  19.435  35.771  1.00 48.00           C  
ANISOU  191  C   ASN A  23     5709   5921   6606    332   -239   -691       C  
ATOM    192  O   ASN A  23     -37.277  20.619  36.129  1.00 47.41           O  
ANISOU  192  O   ASN A  23     5633   5834   6546    350   -259   -705       O  
ATOM    193  CB  ASN A  23     -39.621  18.803  36.368  1.00 48.73           C  
ANISOU  193  CB  ASN A  23     5656   6001   6858    332   -202   -819       C  
ATOM    194  CG  ASN A  23     -40.967  18.343  35.841  1.00 50.17           C  
ANISOU  194  CG  ASN A  23     5765   6160   7139    344   -233   -884       C  
ATOM    195  OD1 ASN A  23     -41.447  18.848  34.829  1.00 51.37           O  
ANISOU  195  OD1 ASN A  23     5910   6276   7333    381   -331   -903       O  
ATOM    196  ND2 ASN A  23     -41.577  17.376  36.517  1.00 52.00           N  
ANISOU  196  ND2 ASN A  23     5944   6407   7407    313   -152   -921       N  
ATOM    197  N   GLY A  24     -36.152  18.698  35.753  1.00 46.63           N  
ANISOU  197  N   GLY A  24     5590   5773   6355    307   -203   -632       N  
ATOM    198  CA  GLY A  24     -34.874  19.240  36.173  1.00 45.70           C  
ANISOU  198  CA  GLY A  24     5528   5668   6168    298   -185   -582       C  
ATOM    199  C   GLY A  24     -34.696  19.176  37.676  1.00 44.55           C  
ANISOU  199  C   GLY A  24     5369   5546   6011    276   -104   -592       C  
ATOM    200  O   GLY A  24     -33.778  19.785  38.217  1.00 45.65           O  
ANISOU  200  O   GLY A  24     5546   5694   6107    273    -92   -563       O  
ATOM    201  N   ARG A  25     -35.576  18.439  38.349  1.00 43.43           N  
ANISOU  201  N   ARG A  25     5178   5414   5910    259    -49   -634       N  
ATOM    202  CA  ARG A  25     -35.418  18.176  39.776  1.00 43.62           C  
ANISOU  202  CA  ARG A  25     5202   5459   5913    231     35   -641       C  
ATOM    203  C   ARG A  25     -34.469  17.003  40.015  1.00 40.66           C  
ANISOU  203  C   ARG A  25     4875   5106   5469    200     77   -590       C  
ATOM    204  O   ARG A  25     -34.594  15.958  39.381  1.00 40.96           O  
ANISOU  204  O   ARG A  25     4909   5146   5508    191     76   -579       O  
ATOM    205  CB  ARG A  25     -36.766  17.872  40.441  1.00 43.49           C  
ANISOU  205  CB  ARG A  25     5119   5439   5967    218     87   -710       C  
ATOM    206  CG  ARG A  25     -37.526  19.080  40.989  1.00 45.15           C  
ANISOU  206  CG  ARG A  25     5284   5634   6236    237     85   -768       C  
ATOM    207  CD  ARG A  25     -38.455  19.691  39.954  1.00 43.59           C  
ANISOU  207  CD  ARG A  25     5035   5407   6120    275      4   -811       C  
ATOM    208  NE  ARG A  25     -39.368  20.671  40.549  1.00 44.32           N  
ANISOU  208  NE  ARG A  25     5070   5483   6288    290      9   -881       N  
ATOM    209  CZ  ARG A  25     -40.662  20.470  40.797  1.00 42.25           C  
ANISOU  209  CZ  ARG A  25     4728   5209   6118    287     38   -959       C  
ATOM    210  NH1 ARG A  25     -41.248  19.310  40.504  1.00 40.08           N  
ANISOU  210  NH1 ARG A  25     4419   4936   5873    268     63   -976       N  
ATOM    211  NH2 ARG A  25     -41.374  21.445  41.346  1.00 42.93           N  
ANISOU  211  NH2 ARG A  25     4763   5278   6271    303     42  -1023       N  
ATOM    212  N   GLU A  26     -33.528  17.191  40.932  1.00 37.74           N  
ANISOU  212  N   GLU A  26     4549   4748   5043    187    110   -560       N  
ATOM    213  CA  GLU A  26     -32.736  16.091  41.457  1.00 38.31           C  
ANISOU  213  CA  GLU A  26     4662   4835   5057    158    154   -523       C  
ATOM    214  C   GLU A  26     -33.606  15.161  42.304  1.00 39.74           C  
ANISOU  214  C   GLU A  26     4822   5021   5255    127    227   -557       C  
ATOM    215  O   GLU A  26     -34.363  15.613  43.178  1.00 37.98           O  
ANISOU  215  O   GLU A  26     4574   4795   5061    119    269   -602       O  
ATOM    216  CB  GLU A  26     -31.542  16.598  42.282  1.00 37.06           C  
ANISOU  216  CB  GLU A  26     4557   4683   4841    155    162   -489       C  
ATOM    217  CG  GLU A  26     -30.694  15.452  42.858  1.00 36.38           C  
ANISOU  217  CG  GLU A  26     4518   4606   4698    128    197   -452       C  
ATOM    218  CD  GLU A  26     -29.368  15.889  43.454  1.00 35.33           C  
ANISOU  218  CD  GLU A  26     4437   4474   4513    130    186   -417       C  
ATOM    219  OE1 GLU A  26     -28.885  16.999  43.140  1.00 36.47           O  
ANISOU  219  OE1 GLU A  26     4584   4614   4660    151    146   -409       O  
ATOM    220  OE2 GLU A  26     -28.798  15.104  44.235  1.00 36.18           O  
ANISOU  220  OE2 GLU A  26     4584   4584   4578    109    215   -397       O  
ATOM    221  N   ARG A  27     -33.488  13.862  42.031  1.00 39.37           N  
ANISOU  221  N   ARG A  27     4787   4980   5193    107    244   -536       N  
ATOM    222  CA  ARG A  27     -34.214  12.836  42.768  1.00 41.12           C  
ANISOU  222  CA  ARG A  27     4997   5203   5423     72    315   -561       C  
ATOM    223  C   ARG A  27     -33.297  11.660  43.062  1.00 40.23           C  
ANISOU  223  C   ARG A  27     4942   5096   5246     48    337   -513       C  
ATOM    224  O   ARG A  27     -32.203  11.551  42.498  1.00 40.74           O  
ANISOU  224  O   ARG A  27     5041   5165   5274     61    292   -466       O  
ATOM    225  CB  ARG A  27     -35.413  12.335  41.955  1.00 44.17           C  
ANISOU  225  CB  ARG A  27     5319   5582   5881     73    310   -602       C  
ATOM    226  CG  ARG A  27     -36.382  13.388  41.478  1.00 48.83           C  
ANISOU  226  CG  ARG A  27     5846   6159   6547    103    273   -655       C  
ATOM    227  CD  ARG A  27     -37.603  13.483  42.367  1.00 59.08           C  
ANISOU  227  CD  ARG A  27     7092   7451   7905     83    339   -724       C  
ATOM    228  NE  ARG A  27     -38.744  13.969  41.595  1.00 67.36           N  
ANISOU  228  NE  ARG A  27     8063   8482   9049    110    297   -782       N  
ATOM    229  CZ  ARG A  27     -39.616  13.186  40.961  1.00 71.78           C  
ANISOU  229  CZ  ARG A  27     8572   9033   9668    105    292   -814       C  
ATOM    230  NH1 ARG A  27     -39.500  11.865  41.019  1.00 73.35           N  
ANISOU  230  NH1 ARG A  27     8789   9240   9841     73    335   -793       N  
ATOM    231  NH2 ARG A  27     -40.613  13.724  40.271  1.00 74.88           N  
ANISOU  231  NH2 ARG A  27     8894   9404  10151    134    241   -870       N  
ATOM    232  N   THR A  28     -33.759  10.777  43.938  1.00 40.97           N  
ANISOU  232  N   THR A  28     5049   5188   5331     11    405   -527       N  
ATOM    233  CA  THR A  28     -33.058   9.546  44.274  1.00 41.57           C  
ANISOU  233  CA  THR A  28     5181   5263   5352    -15    426   -487       C  
ATOM    234  C   THR A  28     -34.090   8.434  44.314  1.00 42.27           C  
ANISOU  234  C   THR A  28     5243   5345   5473    -47    479   -515       C  
ATOM    235  O   THR A  28     -35.247   8.667  44.670  1.00 45.24           O  
ANISOU  235  O   THR A  28     5574   5717   5898    -61    526   -569       O  
ATOM    236  CB  THR A  28     -32.383   9.622  45.665  1.00 43.00           C  
ANISOU  236  CB  THR A  28     5434   5439   5467    -35    461   -468       C  
ATOM    237  OG1 THR A  28     -31.903  10.948  45.909  1.00 46.97           O  
ANISOU  237  OG1 THR A  28     5942   5945   5960    -10    431   -467       O  
ATOM    238  CG2 THR A  28     -31.220   8.637  45.766  1.00 42.11           C  
ANISOU  238  CG2 THR A  28     5385   5322   5294    -43    443   -414       C  
ATOM    239  N   ARG A  29     -33.675   7.228  43.951  1.00 40.14           N  
ANISOU  239  N   ARG A  29     4998   5073   5180    -59    474   -483       N  
ATOM    240  CA  ARG A  29     -34.554   6.069  44.006  1.00 40.77           C  
ANISOU  240  CA  ARG A  29     5059   5144   5285    -93    525   -505       C  
ATOM    241  C   ARG A  29     -33.749   4.796  44.230  1.00 42.97           C  
ANISOU  241  C   ARG A  29     5403   5416   5507   -115    531   -458       C  
ATOM    242  O   ARG A  29     -32.572   4.713  43.862  1.00 42.97           O  
ANISOU  242  O   ARG A  29     5438   5420   5468    -94    478   -413       O  
ATOM    243  CB  ARG A  29     -35.393   5.950  42.727  1.00 40.66           C  
ANISOU  243  CB  ARG A  29     4970   5133   5347    -75    492   -535       C  
ATOM    244  CG  ARG A  29     -34.580   5.794  41.441  1.00 37.12           C  
ANISOU  244  CG  ARG A  29     4525   4692   4888    -43    413   -496       C  
ATOM    245  CD  ARG A  29     -35.497   5.720  40.256  1.00 35.30           C  
ANISOU  245  CD  ARG A  29     4227   4458   4728    -26    379   -530       C  
ATOM    246  NE  ARG A  29     -34.789   5.933  39.005  1.00 36.14           N  
ANISOU  246  NE  ARG A  29     4341   4568   4822      8    302   -499       N  
ATOM    247  CZ  ARG A  29     -35.339   6.476  37.924  1.00 39.63           C  
ANISOU  247  CZ  ARG A  29     4740   5004   5311     37    246   -522       C  
ATOM    248  NH1 ARG A  29     -36.608   6.871  37.947  1.00 40.24           N  
ANISOU  248  NH1 ARG A  29     4756   5072   5460     40    253   -580       N  
ATOM    249  NH2 ARG A  29     -34.619   6.636  36.822  1.00 39.80           N  
ANISOU  249  NH2 ARG A  29     4784   5027   5310     61    184   -491       N  
ATOM    250  N   GLU A  30     -34.394   3.818  44.848  1.00 43.75           N  
ANISOU  250  N   GLU A  30     5517   5501   5604   -158    597   -473       N  
ATOM    251  CA  GLU A  30     -33.797   2.528  45.096  1.00 45.01           C  
ANISOU  251  CA  GLU A  30     5738   5648   5715   -181    605   -434       C  
ATOM    252  C   GLU A  30     -34.603   1.543  44.280  1.00 46.34           C  
ANISOU  252  C   GLU A  30     5857   5813   5937   -194    615   -454       C  
ATOM    253  O   GLU A  30     -35.832   1.500  44.383  1.00 47.82           O  
ANISOU  253  O   GLU A  30     5994   5996   6179   -216    668   -504       O  
ATOM    254  CB  GLU A  30     -33.872   2.194  46.583  1.00 46.64           C  
ANISOU  254  CB  GLU A  30     6020   5834   5867   -226    675   -433       C  
ATOM    255  CG  GLU A  30     -33.123   0.937  46.998  1.00 49.59           C  
ANISOU  255  CG  GLU A  30     6476   6187   6180   -249    674   -387       C  
ATOM    256  CD  GLU A  30     -33.517   0.440  48.387  1.00 51.56           C  
ANISOU  256  CD  GLU A  30     6802   6409   6380   -303    755   -394       C  
ATOM    257  OE1 GLU A  30     -33.998   1.256  49.210  1.00 53.25           O  
ANISOU  257  OE1 GLU A  30     7024   6623   6586   -318    805   -424       O  
ATOM    258  OE2 GLU A  30     -33.349  -0.772  48.654  1.00 48.42           O  
ANISOU  258  OE2 GLU A  30     6462   5988   5949   -333    770   -369       O  
ATOM    259  N   VAL A  31     -33.920   0.772  43.442  1.00 46.31           N  
ANISOU  259  N   VAL A  31     5862   5810   5923   -179    565   -419       N  
ATOM    260  CA  VAL A  31     -34.611  -0.157  42.557  1.00 45.41           C  
ANISOU  260  CA  VAL A  31     5701   5693   5859   -187    565   -436       C  
ATOM    261  C   VAL A  31     -34.070  -1.560  42.752  1.00 44.27           C  
ANISOU  261  C   VAL A  31     5615   5532   5675   -211    573   -400       C  
ATOM    262  O   VAL A  31     -32.857  -1.771  42.733  1.00 45.16           O  
ANISOU  262  O   VAL A  31     5778   5644   5739   -195    530   -355       O  
ATOM    263  CB  VAL A  31     -34.503   0.276  41.079  1.00 44.77           C  
ANISOU  263  CB  VAL A  31     5565   5627   5818   -142    490   -438       C  
ATOM    264  CG1 VAL A  31     -35.393  -0.574  40.207  1.00 46.24           C  
ANISOU  264  CG1 VAL A  31     5698   5808   6062   -150    490   -465       C  
ATOM    265  CG2 VAL A  31     -34.902   1.741  40.925  1.00 46.97           C  
ANISOU  265  CG2 VAL A  31     5799   5917   6130   -115    471   -468       C  
ATOM    266  N   GLU A  32     -34.976  -2.509  42.972  1.00 44.48           N  
ANISOU  266  N   GLU A  32     5631   5542   5726   -251    629   -423       N  
ATOM    267  CA  GLU A  32     -34.607  -3.917  43.069  1.00 46.81           C  
ANISOU  267  CA  GLU A  32     5977   5818   5992   -276    636   -393       C  
ATOM    268  C   GLU A  32     -34.445  -4.467  41.647  1.00 45.99           C  
ANISOU  268  C   GLU A  32     5828   5723   5925   -248    576   -387       C  
ATOM    269  O   GLU A  32     -35.300  -5.199  41.139  1.00 45.09           O  
ANISOU  269  O   GLU A  32     5671   5602   5860   -264    594   -413       O  
ATOM    270  CB  GLU A  32     -35.654  -4.708  43.856  1.00 48.24           C  
ANISOU  270  CB  GLU A  32     6169   5975   6185   -333    724   -421       C  
ATOM    271  CG  GLU A  32     -35.788  -4.309  45.320  1.00 54.61           C  
ANISOU  271  CG  GLU A  32     7039   6768   6944   -369    793   -426       C  
ATOM    272  CD  GLU A  32     -36.903  -5.068  46.031  1.00 59.17           C  
ANISOU  272  CD  GLU A  32     7625   7319   7538   -433    892   -460       C  
ATOM    273  OE1 GLU A  32     -36.730  -6.279  46.294  1.00 62.00           O  
ANISOU  273  OE1 GLU A  32     8043   7651   7864   -465    910   -434       O  
ATOM    274  OE2 GLU A  32     -37.950  -4.453  46.328  1.00 58.04           O  
ANISOU  274  OE2 GLU A  32     7430   7180   7443   -451    953   -515       O  
ATOM    275  N   TYR A  33     -33.342  -4.076  41.013  1.00 44.42           N  
ANISOU  275  N   TYR A  33     5638   5537   5702   -207    507   -355       N  
ATOM    276  CA  TYR A  33     -33.078  -4.370  39.608  1.00 41.50           C  
ANISOU  276  CA  TYR A  33     5232   5178   5360   -177    448   -350       C  
ATOM    277  C   TYR A  33     -32.998  -5.868  39.357  1.00 40.29           C  
ANISOU  277  C   TYR A  33     5097   5006   5205   -197    452   -336       C  
ATOM    278  O   TYR A  33     -32.386  -6.612  40.128  1.00 41.07           O  
ANISOU  278  O   TYR A  33     5260   5086   5260   -217    465   -307       O  
ATOM    279  CB  TYR A  33     -31.783  -3.672  39.167  1.00 39.73           C  
ANISOU  279  CB  TYR A  33     5027   4967   5102   -138    388   -318       C  
ATOM    280  CG  TYR A  33     -31.423  -3.829  37.699  1.00 37.37           C  
ANISOU  280  CG  TYR A  33     4699   4678   4823   -108    332   -314       C  
ATOM    281  CD1 TYR A  33     -32.306  -3.432  36.689  1.00 36.69           C  
ANISOU  281  CD1 TYR A  33     4554   4601   4786    -93    313   -346       C  
ATOM    282  CD2 TYR A  33     -30.194  -4.359  37.322  1.00 32.40           C  
ANISOU  282  CD2 TYR A  33     4102   4045   4163    -95    297   -281       C  
ATOM    283  CE1 TYR A  33     -31.972  -3.571  35.342  1.00 35.04           C  
ANISOU  283  CE1 TYR A  33     4331   4397   4586    -69    262   -342       C  
ATOM    284  CE2 TYR A  33     -29.849  -4.496  35.975  1.00 35.30           C  
ANISOU  284  CE2 TYR A  33     4448   4421   4545    -72    254   -280       C  
ATOM    285  CZ  TYR A  33     -30.741  -4.100  34.997  1.00 34.45           C  
ANISOU  285  CZ  TYR A  33     4292   4322   4476    -60    238   -308       C  
ATOM    286  OH  TYR A  33     -30.401  -4.243  33.676  1.00 32.63           O  
ANISOU  286  OH  TYR A  33     4052   4095   4250    -40    196   -307       O  
ATOM    287  N   LYS A  34     -33.643  -6.295  38.281  1.00 39.02           N  
ANISOU  287  N   LYS A  34     4882   4849   5095   -190    435   -360       N  
ATOM    288  CA  LYS A  34     -33.653  -7.691  37.884  1.00 40.14           C  
ANISOU  288  CA  LYS A  34     5033   4975   5245   -206    434   -352       C  
ATOM    289  C   LYS A  34     -32.779  -7.827  36.644  1.00 38.39           C  
ANISOU  289  C   LYS A  34     4805   4764   5019   -169    366   -333       C  
ATOM    290  O   LYS A  34     -33.214  -7.514  35.531  1.00 39.53           O  
ANISOU  290  O   LYS A  34     4901   4920   5200   -147    333   -356       O  
ATOM    291  CB  LYS A  34     -35.080  -8.159  37.591  1.00 42.18           C  
ANISOU  291  CB  LYS A  34     5233   5225   5569   -229    467   -398       C  
ATOM    292  CG  LYS A  34     -36.114  -7.702  38.612  1.00 46.99           C  
ANISOU  292  CG  LYS A  34     5825   5827   6200   -262    538   -433       C  
ATOM    293  CD  LYS A  34     -36.515  -8.803  39.569  1.00 52.13           C  
ANISOU  293  CD  LYS A  34     6515   6450   6840   -317    608   -433       C  
ATOM    294  CE  LYS A  34     -37.515  -9.747  38.918  1.00 55.08           C  
ANISOU  294  CE  LYS A  34     6836   6811   7281   -337    623   -468       C  
ATOM    295  NZ  LYS A  34     -38.662 -10.026  39.834  1.00 58.34           N  
ANISOU  295  NZ  LYS A  34     7237   7204   7727   -392    716   -508       N  
ATOM    296  N   PRO A  35     -31.534  -8.284  36.833  1.00 35.86           N  
ANISOU  296  N   PRO A  35     4537   4436   4652   -163    344   -295       N  
ATOM    297  CA  PRO A  35     -30.579  -8.339  35.742  1.00 32.81           C  
ANISOU  297  CA  PRO A  35     4148   4059   4260   -130    289   -280       C  
ATOM    298  C   PRO A  35     -30.784  -9.568  34.861  1.00 32.11           C  
ANISOU  298  C   PRO A  35     4044   3959   4195   -135    276   -287       C  
ATOM    299  O   PRO A  35     -31.383 -10.564  35.290  1.00 29.07           O  
ANISOU  299  O   PRO A  35     3667   3556   3824   -165    307   -293       O  
ATOM    300  CB  PRO A  35     -29.233  -8.430  36.465  1.00 32.05           C  
ANISOU  300  CB  PRO A  35     4109   3953   4116   -125    276   -244       C  
ATOM    301  CG  PRO A  35     -29.538  -9.021  37.806  1.00 35.29           C  
ANISOU  301  CG  PRO A  35     4564   4339   4505   -161    318   -235       C  
ATOM    302  CD  PRO A  35     -31.030  -8.969  38.036  1.00 36.30           C  
ANISOU  302  CD  PRO A  35     4659   4468   4666   -189    370   -268       C  
ATOM    303  N   SER A  36     -30.296  -9.489  33.630  1.00 30.43           N  
ANISOU  303  N   SER A  36     3816   3759   3989   -107    233   -288       N  
ATOM    304  CA  SER A  36     -30.285 -10.648  32.764  1.00 33.31           C  
ANISOU  304  CA  SER A  36     4174   4113   4370   -109    216   -293       C  
ATOM    305  C   SER A  36     -28.873 -11.016  32.381  1.00 34.27           C  
ANISOU  305  C   SER A  36     4325   4232   4465    -91    186   -269       C  
ATOM    306  O   SER A  36     -28.025 -10.142  32.150  1.00 36.15           O  
ANISOU  306  O   SER A  36     4570   4483   4683    -70    167   -260       O  
ATOM    307  CB  SER A  36     -31.106 -10.406  31.507  1.00 32.94           C  
ANISOU  307  CB  SER A  36     4082   4076   4358    -95    191   -323       C  
ATOM    308  OG  SER A  36     -32.462 -10.208  31.826  1.00 36.94           O  
ANISOU  308  OG  SER A  36     4551   4580   4904   -111    216   -353       O  
ATOM    309  N   LEU A  37     -28.622 -12.320  32.336  1.00 33.51           N  
ANISOU  309  N   LEU A  37     4244   4116   4374   -103    184   -264       N  
ATOM    310  CA  LEU A  37     -27.386 -12.850  31.772  1.00 31.81           C  
ANISOU  310  CA  LEU A  37     4045   3894   4148    -86    155   -252       C  
ATOM    311  C   LEU A  37     -27.767 -13.901  30.744  1.00 31.55           C  
ANISOU  311  C   LEU A  37     3994   3854   4141    -88    144   -270       C  
ATOM    312  O   LEU A  37     -28.954 -14.165  30.550  1.00 33.98           O  
ANISOU  312  O   LEU A  37     4277   4161   4475   -102    156   -289       O  
ATOM    313  CB  LEU A  37     -26.463 -13.393  32.862  1.00 29.99           C  
ANISOU  313  CB  LEU A  37     3858   3639   3897    -92    154   -227       C  
ATOM    314  CG  LEU A  37     -25.933 -12.326  33.809  1.00 32.44           C  
ANISOU  314  CG  LEU A  37     4191   3956   4180    -86    157   -211       C  
ATOM    315  CD1 LEU A  37     -25.183 -12.962  34.974  1.00 32.28           C  
ANISOU  315  CD1 LEU A  37     4222   3904   4139    -94    149   -188       C  
ATOM    316  CD2 LEU A  37     -25.055 -11.294  33.081  1.00 36.27           C  
ANISOU  316  CD2 LEU A  37     4658   4462   4660    -57    134   -214       C  
ATOM    317  N   PHE A  38     -26.785 -14.474  30.056  1.00 31.54           N  
ANISOU  317  N   PHE A  38     4000   3846   4137    -74    121   -268       N  
ATOM    318  CA  PHE A  38     -27.094 -15.285  28.882  1.00 32.71           C  
ANISOU  318  CA  PHE A  38     4131   3991   4306    -72    107   -289       C  
ATOM    319  C   PHE A  38     -26.289 -16.574  28.809  1.00 33.38           C  
ANISOU  319  C   PHE A  38     4232   4052   4398    -73     96   -285       C  
ATOM    320  O   PHE A  38     -25.158 -16.647  29.295  1.00 33.22           O  
ANISOU  320  O   PHE A  38     4234   4022   4368    -64     87   -271       O  
ATOM    321  CB  PHE A  38     -26.905 -14.466  27.595  1.00 33.17           C  
ANISOU  321  CB  PHE A  38     4176   4070   4355    -51     88   -304       C  
ATOM    322  CG  PHE A  38     -27.797 -13.243  27.510  1.00 37.50           C  
ANISOU  322  CG  PHE A  38     4709   4637   4903    -47     89   -311       C  
ATOM    323  CD1 PHE A  38     -27.487 -12.079  28.220  1.00 36.85           C  
ANISOU  323  CD1 PHE A  38     4634   4567   4802    -41     97   -297       C  
ATOM    324  CD2 PHE A  38     -28.942 -13.255  26.716  1.00 35.01           C  
ANISOU  324  CD2 PHE A  38     4370   4323   4608    -46     75   -336       C  
ATOM    325  CE1 PHE A  38     -28.312 -10.958  28.152  1.00 35.46           C  
ANISOU  325  CE1 PHE A  38     4441   4405   4628    -36     95   -307       C  
ATOM    326  CE2 PHE A  38     -29.763 -12.140  26.636  1.00 34.41           C  
ANISOU  326  CE2 PHE A  38     4277   4259   4539    -39     67   -347       C  
ATOM    327  CZ  PHE A  38     -29.446 -10.988  27.357  1.00 37.24           C  
ANISOU  327  CZ  PHE A  38     4642   4629   4878    -34     78   -332       C  
ATOM    328  N   ALA A  39     -26.899 -17.589  28.205  1.00 32.09           N  
ANISOU  328  N   ALA A  39     4058   3877   4258    -82     92   -301       N  
ATOM    329  CA  ALA A  39     -26.224 -18.835  27.918  1.00 31.75           C  
ANISOU  329  CA  ALA A  39     4025   3811   4227    -80     77   -303       C  
ATOM    330  C   ALA A  39     -26.456 -19.230  26.467  1.00 32.75           C  
ANISOU  330  C   ALA A  39     4132   3944   4367    -72     62   -330       C  
ATOM    331  O   ALA A  39     -27.559 -19.071  25.938  1.00 33.95           O  
ANISOU  331  O   ALA A  39     4264   4104   4529    -77     62   -347       O  
ATOM    332  CB  ALA A  39     -26.715 -19.923  28.856  1.00 31.27           C  
ANISOU  332  CB  ALA A  39     3982   3719   4179   -106     88   -292       C  
ATOM    333  N   HIS A  40     -25.409 -19.725  25.817  1.00 33.38           N  
ANISOU  333  N   HIS A  40     4219   4017   4448    -58     49   -339       N  
ATOM    334  CA  HIS A  40     -25.563 -20.371  24.525  1.00 37.39           C  
ANISOU  334  CA  HIS A  40     4717   4523   4966    -53     36   -366       C  
ATOM    335  C   HIS A  40     -26.675 -21.426  24.610  1.00 37.49           C  
ANISOU  335  C   HIS A  40     4721   4518   5008    -71     34   -373       C  
ATOM    336  O   HIS A  40     -26.816 -22.102  25.626  1.00 34.98           O  
ANISOU  336  O   HIS A  40     4412   4177   4702    -88     42   -357       O  
ATOM    337  CB  HIS A  40     -24.246 -21.014  24.097  1.00 36.77           C  
ANISOU  337  CB  HIS A  40     4646   4432   4895    -41     29   -376       C  
ATOM    338  CG  HIS A  40     -23.204 -20.025  23.675  1.00 38.30           C  
ANISOU  338  CG  HIS A  40     4843   4643   5068    -25     36   -381       C  
ATOM    339  ND1 HIS A  40     -21.908 -20.064  24.142  1.00 40.10           N  
ANISOU  339  ND1 HIS A  40     5072   4859   5305    -16     36   -379       N  
ATOM    340  CD2 HIS A  40     -23.268 -18.968  22.831  1.00 39.85           C  
ANISOU  340  CD2 HIS A  40     5042   4862   5237    -20     43   -390       C  
ATOM    341  CE1 HIS A  40     -21.217 -19.077  23.599  1.00 41.38           C  
ANISOU  341  CE1 HIS A  40     5234   5039   5450     -7     50   -388       C  
ATOM    342  NE2 HIS A  40     -22.020 -18.394  22.804  1.00 39.52           N  
ANISOU  342  NE2 HIS A  40     5003   4824   5188    -10     55   -392       N  
ATOM    343  N   CYS A  41     -27.485 -21.529  23.564  1.00 39.90           N  
ANISOU  343  N   CYS A  41     5011   4828   5321    -70     23   -397       N  
ATOM    344  CA  CYS A  41     -28.577 -22.501  23.536  1.00 45.94           C  
ANISOU  344  CA  CYS A  41     5761   5575   6119    -88     19   -410       C  
ATOM    345  C   CYS A  41     -28.582 -23.261  22.201  1.00 48.89           C  
ANISOU  345  C   CYS A  41     6131   5942   6502    -79     -4   -439       C  
ATOM    346  O   CYS A  41     -27.860 -22.873  21.283  1.00 47.72           O  
ANISOU  346  O   CYS A  41     5996   5805   6328    -61    -14   -450       O  
ATOM    347  CB  CYS A  41     -29.919 -21.809  23.814  1.00 45.92           C  
ANISOU  347  CB  CYS A  41     5734   5583   6131    -99     27   -416       C  
ATOM    348  SG  CYS A  41     -30.369 -20.523  22.632  1.00 49.43           S  
ANISOU  348  SG  CYS A  41     6168   6053   6559    -77      0   -437       S  
ATOM    349  N   PRO A  42     -29.373 -24.360  22.093  1.00 53.76           N  
ANISOU  349  N   PRO A  42     6736   6537   7154    -94    -11   -454       N  
ATOM    350  CA  PRO A  42     -29.395 -25.137  20.841  1.00 55.91           C  
ANISOU  350  CA  PRO A  42     7008   6801   7435    -86    -36   -483       C  
ATOM    351  C   PRO A  42     -29.852 -24.315  19.639  1.00 58.78           C  
ANISOU  351  C   PRO A  42     7372   7182   7779    -70    -60   -506       C  
ATOM    352  O   PRO A  42     -30.711 -23.431  19.767  1.00 57.27           O  
ANISOU  352  O   PRO A  42     7166   7003   7591    -70    -66   -507       O  
ATOM    353  CB  PRO A  42     -30.398 -26.260  21.132  1.00 56.20           C  
ANISOU  353  CB  PRO A  42     7026   6811   7517   -108    -37   -493       C  
ATOM    354  CG  PRO A  42     -30.390 -26.401  22.608  1.00 57.65           C  
ANISOU  354  CG  PRO A  42     7214   6982   7708   -130     -6   -463       C  
ATOM    355  CD  PRO A  42     -30.194 -25.000  23.140  1.00 55.02           C  
ANISOU  355  CD  PRO A  42     6885   6676   7345   -122      8   -444       C  
ATOM    356  N   GLU A  43     -29.263 -24.614  18.484  1.00 64.05           N  
ANISOU  356  N   GLU A  43     8061   7849   8428    -57    -75   -526       N  
ATOM    357  CA  GLU A  43     -29.546 -23.900  17.234  1.00 69.11           C  
ANISOU  357  CA  GLU A  43     8721   8500   9038    -43   -102   -547       C  
ATOM    358  C   GLU A  43     -31.030 -23.960  16.887  1.00 70.79           C  
ANISOU  358  C   GLU A  43     8911   8703   9281    -45   -137   -568       C  
ATOM    359  O   GLU A  43     -31.544 -23.085  16.191  1.00 70.61           O  
ANISOU  359  O   GLU A  43     8901   8688   9240    -33   -166   -580       O  
ATOM    360  CB  GLU A  43     -28.725 -24.484  16.072  1.00 71.58           C  
ANISOU  360  CB  GLU A  43     9065   8806   9328    -34   -107   -569       C  
ATOM    361  CG  GLU A  43     -27.257 -24.829  16.397  1.00 75.05           C  
ANISOU  361  CG  GLU A  43     9511   9244   9759    -33    -73   -560       C  
ATOM    362  CD  GLU A  43     -26.407 -23.608  16.738  1.00 79.05           C  
ANISOU  362  CD  GLU A  43    10031   9772  10233    -28    -49   -540       C  
ATOM    363  OE1 GLU A  43     -26.329 -22.670  15.907  1.00 78.65           O  
ANISOU  363  OE1 GLU A  43    10009   9733  10140    -21    -52   -548       O  
ATOM    364  OE2 GLU A  43     -25.810 -23.597  17.841  1.00 79.94           O  
ANISOU  364  OE2 GLU A  43    10129   9885  10361    -30    -29   -518       O  
ATOM    365  N   SER A  44     -31.703 -25.000  17.382  1.00 73.12           N  
ANISOU  365  N   SER A  44     9176   8980   9627    -61   -135   -575       N  
ATOM    366  CA  SER A  44     -33.118 -25.228  17.104  1.00 76.00           C  
ANISOU  366  CA  SER A  44     9509   9330  10036    -67   -165   -603       C  
ATOM    367  C   SER A  44     -34.017 -24.842  18.282  1.00 76.29           C  
ANISOU  367  C   SER A  44     9505   9369  10113    -84   -143   -594       C  
ATOM    368  O   SER A  44     -34.783 -25.669  18.793  1.00 76.75           O  
ANISOU  368  O   SER A  44     9531   9408  10224   -106   -131   -605       O  
ATOM    369  CB  SER A  44     -33.361 -26.686  16.681  1.00 77.44           C  
ANISOU  369  CB  SER A  44     9684   9487  10252    -76   -178   -625       C  
ATOM    370  OG  SER A  44     -33.084 -27.585  17.744  1.00 79.54           O  
ANISOU  370  OG  SER A  44     9938   9739  10545    -98   -141   -606       O  
ATOM    371  N   GLN A  45     -33.893 -23.588  18.720  1.00 75.26           N  
ANISOU  371  N   GLN A  45     9378   9260   9959    -77   -132   -577       N  
ATOM    372  CA  GLN A  45     -34.875 -22.972  19.619  1.00 73.87           C  
ANISOU  372  CA  GLN A  45     9162   9086   9820    -90   -117   -579       C  
ATOM    373  C   GLN A  45     -34.920 -21.456  19.433  1.00 72.66           C  
ANISOU  373  C   GLN A  45     9016   8954   9639    -69   -134   -576       C  
ATOM    374  O   GLN A  45     -33.882 -20.779  19.455  1.00 72.04           O  
ANISOU  374  O   GLN A  45     8973   8893   9507    -57   -123   -550       O  
ATOM    375  CB  GLN A  45     -34.684 -23.373  21.094  1.00 73.66           C  
ANISOU  375  CB  GLN A  45     9127   9054   9804   -118    -60   -552       C  
ATOM    376  CG  GLN A  45     -33.412 -22.893  21.774  1.00 73.60           C  
ANISOU  376  CG  GLN A  45     9155   9062   9746   -113    -32   -512       C  
ATOM    377  CD  GLN A  45     -33.663 -22.457  23.211  1.00 73.73           C  
ANISOU  377  CD  GLN A  45     9163   9082   9770   -134     12   -491       C  
ATOM    378  OE1 GLN A  45     -34.178 -21.362  23.455  1.00 71.78           O  
ANISOU  378  OE1 GLN A  45     8898   8850   9525   -130     15   -495       O  
ATOM    379  NE2 GLN A  45     -33.297 -23.308  24.169  1.00 71.87           N  
ANISOU  379  NE2 GLN A  45     8944   8828   9535   -157     44   -469       N  
ATOM    380  N   ALA A  46     -36.138 -20.948  19.245  1.00 70.73           N  
ANISOU  380  N   ALA A  46     8735   8703   9436    -65   -163   -606       N  
ATOM    381  CA  ALA A  46     -36.380 -19.556  18.866  1.00 67.58           C  
ANISOU  381  CA  ALA A  46     8343   8316   9020    -41   -197   -612       C  
ATOM    382  C   ALA A  46     -35.871 -18.550  19.892  1.00 64.46           C  
ANISOU  382  C   ALA A  46     7952   7942   8598    -44   -156   -580       C  
ATOM    383  O   ALA A  46     -36.193 -18.628  21.083  1.00 64.19           O  
ANISOU  383  O   ALA A  46     7886   7909   8594    -66   -110   -573       O  
ATOM    384  CB  ALA A  46     -37.872 -19.328  18.583  1.00 69.19           C  
ANISOU  384  CB  ALA A  46     8496   8501   9291    -36   -240   -658       C  
ATOM    385  N   THR A  47     -35.068 -17.608  19.409  1.00 59.59           N  
ANISOU  385  N   THR A  47     7379   7340   7922    -24   -171   -562       N  
ATOM    386  CA  THR A  47     -34.556 -16.526  20.236  1.00 56.22           C  
ANISOU  386  CA  THR A  47     6959   6933   7468    -22   -142   -534       C  
ATOM    387  C   THR A  47     -34.248 -15.293  19.386  1.00 52.64           C  
ANISOU  387  C   THR A  47     6545   6487   6968      3   -181   -531       C  
ATOM    388  O   THR A  47     -34.041 -15.393  18.173  1.00 51.99           O  
ANISOU  388  O   THR A  47     6502   6397   6856     16   -219   -541       O  
ATOM    389  CB  THR A  47     -33.294 -16.958  21.044  1.00 56.04           C  
ANISOU  389  CB  THR A  47     6959   6921   7413    -36    -89   -497       C  
ATOM    390  OG1 THR A  47     -32.882 -15.893  21.908  1.00 51.23           O  
ANISOU  390  OG1 THR A  47     6354   6329   6782    -34    -64   -472       O  
ATOM    391  CG2 THR A  47     -32.142 -17.325  20.115  1.00 56.15           C  
ANISOU  391  CG2 THR A  47     7019   6936   7380    -26    -98   -488       C  
ATOM    392  N   LYS A  48     -34.228 -14.132  20.031  1.00 48.28           N  
ANISOU  392  N   LYS A  48     5988   5948   6408      8   -170   -518       N  
ATOM    393  CA  LYS A  48     -33.811 -12.905  19.369  1.00 45.46           C  
ANISOU  393  CA  LYS A  48     5674   5597   6003     29   -199   -509       C  
ATOM    394  C   LYS A  48     -32.425 -12.454  19.851  1.00 42.33           C  
ANISOU  394  C   LYS A  48     5309   5219   5554     24   -155   -471       C  
ATOM    395  O   LYS A  48     -31.917 -11.412  19.426  1.00 41.18           O  
ANISOU  395  O   LYS A  48     5202   5079   5365     36   -167   -459       O  
ATOM    396  CB  LYS A  48     -34.866 -11.800  19.550  1.00 45.30           C  
ANISOU  396  CB  LYS A  48     5625   5571   6015     42   -234   -528       C  
ATOM    397  CG  LYS A  48     -34.988 -11.231  20.964  1.00 43.15           C  
ANISOU  397  CG  LYS A  48     5314   5314   5766     32   -187   -516       C  
ATOM    398  CD  LYS A  48     -36.053 -10.130  21.028  1.00 41.60           C  
ANISOU  398  CD  LYS A  48     5087   5110   5609     48   -225   -543       C  
ATOM    399  CE  LYS A  48     -36.199  -9.589  22.437  1.00 41.48           C  
ANISOU  399  CE  LYS A  48     5035   5109   5617     36   -173   -536       C  
ATOM    400  NZ  LYS A  48     -37.399  -8.715  22.595  1.00 39.82           N  
ANISOU  400  NZ  LYS A  48     4778   4889   5465     49   -204   -573       N  
ATOM    401  N   TYR A  49     -31.822 -13.240  20.740  1.00 41.27           N  
ANISOU  401  N   TYR A  49     5162   5092   5427      7   -106   -454       N  
ATOM    402  CA  TYR A  49     -30.516 -12.906  21.304  1.00 39.89           C  
ANISOU  402  CA  TYR A  49     5010   4932   5216      4    -69   -423       C  
ATOM    403  C   TYR A  49     -29.413 -13.768  20.711  1.00 39.26           C  
ANISOU  403  C   TYR A  49     4959   4848   5111      1    -56   -418       C  
ATOM    404  O   TYR A  49     -29.485 -14.997  20.738  1.00 38.80           O  
ANISOU  404  O   TYR A  49     4887   4778   5075     -9    -50   -426       O  
ATOM    405  CB  TYR A  49     -30.517 -13.026  22.829  1.00 39.11           C  
ANISOU  405  CB  TYR A  49     4883   4838   5139    -11    -28   -406       C  
ATOM    406  CG  TYR A  49     -31.639 -12.277  23.509  1.00 38.75           C  
ANISOU  406  CG  TYR A  49     4804   4796   5125    -12    -29   -416       C  
ATOM    407  CD1 TYR A  49     -32.763 -12.951  23.985  1.00 33.14           C  
ANISOU  407  CD1 TYR A  49     4052   4073   4466    -28    -20   -437       C  
ATOM    408  CD2 TYR A  49     -31.572 -10.896  23.689  1.00 37.52           C  
ANISOU  408  CD2 TYR A  49     4655   4651   4951      0    -36   -408       C  
ATOM    409  CE1 TYR A  49     -33.790 -12.272  24.611  1.00 35.11           C  
ANISOU  409  CE1 TYR A  49     4265   4323   4751    -31    -14   -453       C  
ATOM    410  CE2 TYR A  49     -32.601 -10.203  24.308  1.00 34.83           C  
ANISOU  410  CE2 TYR A  49     4279   4311   4644      0    -36   -423       C  
ATOM    411  CZ  TYR A  49     -33.707 -10.894  24.768  1.00 37.89           C  
ANISOU  411  CZ  TYR A  49     4623   4688   5087    -16    -23   -448       C  
ATOM    412  OH  TYR A  49     -34.730 -10.209  25.391  1.00 37.99           O  
ANISOU  412  OH  TYR A  49     4595   4700   5140    -18    -17   -470       O  
ATOM    413  N   PHE A  50     -28.390 -13.105  20.179  1.00 39.26           N  
ANISOU  413  N   PHE A  50     4997   4855   5066      7    -50   -409       N  
ATOM    414  CA  PHE A  50     -27.240 -13.787  19.596  1.00 40.26           C  
ANISOU  414  CA  PHE A  50     5148   4978   5172      4    -32   -411       C  
ATOM    415  C   PHE A  50     -25.933 -13.213  20.124  1.00 40.26           C  
ANISOU  415  C   PHE A  50     5157   4987   5153      2      3   -392       C  
ATOM    416  O   PHE A  50     -25.825 -12.005  20.354  1.00 39.34           O  
ANISOU  416  O   PHE A  50     5049   4880   5017      7      4   -380       O  
ATOM    417  CB  PHE A  50     -27.286 -13.692  18.068  1.00 40.61           C  
ANISOU  417  CB  PHE A  50     5235   5013   5181      9    -56   -431       C  
ATOM    418  CG  PHE A  50     -28.440 -14.432  17.457  1.00 42.23           C  
ANISOU  418  CG  PHE A  50     5432   5203   5409     12    -96   -454       C  
ATOM    419  CD1 PHE A  50     -29.686 -13.821  17.318  1.00 41.42           C  
ANISOU  419  CD1 PHE A  50     5322   5096   5321     21   -139   -464       C  
ATOM    420  CD2 PHE A  50     -28.291 -15.749  17.040  1.00 43.71           C  
ANISOU  420  CD2 PHE A  50     5617   5380   5610      6    -93   -470       C  
ATOM    421  CE1 PHE A  50     -30.762 -14.517  16.766  1.00 42.71           C  
ANISOU  421  CE1 PHE A  50     5472   5243   5514     25   -180   -491       C  
ATOM    422  CE2 PHE A  50     -29.369 -16.456  16.480  1.00 44.33           C  
ANISOU  422  CE2 PHE A  50     5687   5443   5714      8   -131   -494       C  
ATOM    423  CZ  PHE A  50     -30.599 -15.838  16.344  1.00 42.04           C  
ANISOU  423  CZ  PHE A  50     5386   5147   5440     17   -175   -505       C  
ATOM    424  N   ASP A  51     -24.937 -14.075  20.323  1.00 38.36           N  
ANISOU  424  N   ASP A  51     4911   4741   4923     -3     26   -393       N  
ATOM    425  CA  ASP A  51     -23.620 -13.573  20.687  1.00 36.67           C  
ANISOU  425  CA  ASP A  51     4702   4532   4699     -2     54   -384       C  
ATOM    426  C   ASP A  51     -22.995 -12.892  19.462  1.00 36.03           C  
ANISOU  426  C   ASP A  51     4659   4452   4577     -3     65   -397       C  
ATOM    427  O   ASP A  51     -23.615 -12.844  18.400  1.00 36.80           O  
ANISOU  427  O   ASP A  51     4786   4545   4650     -3     46   -410       O  
ATOM    428  CB  ASP A  51     -22.751 -14.669  21.324  1.00 36.46           C  
ANISOU  428  CB  ASP A  51     4656   4494   4704     -5     69   -385       C  
ATOM    429  CG  ASP A  51     -22.208 -15.684  20.322  1.00 38.09           C  
ANISOU  429  CG  ASP A  51     4870   4688   4916     -7     75   -412       C  
ATOM    430  OD1 ASP A  51     -22.387 -15.525  19.092  1.00 34.02           O  
ANISOU  430  OD1 ASP A  51     4381   4172   4372     -9     74   -430       O  
ATOM    431  OD2 ASP A  51     -21.574 -16.653  20.792  1.00 35.92           O  
ANISOU  431  OD2 ASP A  51     4577   4398   4672     -6     79   -417       O  
ATOM    432  N   ILE A  52     -21.794 -12.345  19.599  1.00 36.40           N  
ANISOU  432  N   ILE A  52     4712   4503   4618     -6     95   -395       N  
ATOM    433  CA  ILE A  52     -21.231 -11.523  18.524  1.00 34.42           C  
ANISOU  433  CA  ILE A  52     4502   4250   4324    -13    115   -405       C  
ATOM    434  C   ILE A  52     -20.834 -12.330  17.283  1.00 37.15           C  
ANISOU  434  C   ILE A  52     4875   4585   4657    -22    130   -435       C  
ATOM    435  O   ILE A  52     -20.678 -11.768  16.198  1.00 38.18           O  
ANISOU  435  O   ILE A  52     5055   4709   4741    -32    142   -445       O  
ATOM    436  CB  ILE A  52     -20.052 -10.644  19.010  1.00 34.92           C  
ANISOU  436  CB  ILE A  52     4561   4319   4389    -17    148   -399       C  
ATOM    437  CG1 ILE A  52     -18.935 -11.507  19.608  1.00 30.82           C  
ANISOU  437  CG1 ILE A  52     4003   3792   3915    -17    169   -412       C  
ATOM    438  CG2 ILE A  52     -20.556  -9.593  19.996  1.00 30.86           C  
ANISOU  438  CG2 ILE A  52     4035   3816   3873     -9    130   -371       C  
ATOM    439  CD1 ILE A  52     -17.591 -10.799  19.737  1.00 28.80           C  
ANISOU  439  CD1 ILE A  52     3741   3534   3668    -23    206   -421       C  
ATOM    440  N   TYR A  53     -20.696 -13.642  17.457  1.00 37.63           N  
ANISOU  440  N   TYR A  53     4906   4637   4753    -21    130   -449       N  
ATOM    441  CA  TYR A  53     -20.392 -14.574  16.372  1.00 37.74           C  
ANISOU  441  CA  TYR A  53     4939   4638   4762    -28    143   -480       C  
ATOM    442  C   TYR A  53     -21.651 -15.144  15.705  1.00 39.79           C  
ANISOU  442  C   TYR A  53     5218   4893   5009    -24    103   -485       C  
ATOM    443  O   TYR A  53     -21.553 -15.967  14.796  1.00 40.30           O  
ANISOU  443  O   TYR A  53     5300   4945   5066    -29    107   -512       O  
ATOM    444  CB  TYR A  53     -19.508 -15.706  16.900  1.00 38.05           C  
ANISOU  444  CB  TYR A  53     4936   4668   4855    -26    159   -496       C  
ATOM    445  CG  TYR A  53     -18.346 -15.195  17.715  1.00 42.04           C  
ANISOU  445  CG  TYR A  53     5414   5175   5386    -25    185   -492       C  
ATOM    446  CD1 TYR A  53     -18.352 -15.279  19.106  1.00 40.93           C  
ANISOU  446  CD1 TYR A  53     5237   5035   5281    -14    165   -469       C  
ATOM    447  CD2 TYR A  53     -17.256 -14.588  17.095  1.00 43.99           C  
ANISOU  447  CD2 TYR A  53     5675   5420   5620    -36    231   -514       C  
ATOM    448  CE1 TYR A  53     -17.292 -14.790  19.859  1.00 43.65           C  
ANISOU  448  CE1 TYR A  53     5558   5376   5649    -10    180   -468       C  
ATOM    449  CE2 TYR A  53     -16.190 -14.098  17.835  1.00 46.51           C  
ANISOU  449  CE2 TYR A  53     5963   5737   5971    -35    252   -516       C  
ATOM    450  CZ  TYR A  53     -16.213 -14.198  19.213  1.00 46.40           C  
ANISOU  450  CZ  TYR A  53     5912   5723   5993    -20    222   -493       C  
ATOM    451  OH  TYR A  53     -15.154 -13.704  19.936  1.00 44.66           O  
ANISOU  451  OH  TYR A  53     5665   5499   5806    -17    235   -496       O  
ATOM    452  N   GLY A  54     -22.828 -14.703  16.147  1.00 39.66           N  
ANISOU  452  N   GLY A  54     5195   4882   4993    -16     64   -465       N  
ATOM    453  CA  GLY A  54     -24.085 -15.160  15.555  1.00 40.14           C  
ANISOU  453  CA  GLY A  54     5266   4934   5050    -11     21   -475       C  
ATOM    454  C   GLY A  54     -24.643 -16.445  16.151  1.00 41.91           C  
ANISOU  454  C   GLY A  54     5446   5153   5326     -9      6   -478       C  
ATOM    455  O   GLY A  54     -25.534 -17.070  15.569  1.00 42.00           O  
ANISOU  455  O   GLY A  54     5462   5154   5344     -7    -26   -494       O  
ATOM    456  N   LYS A  55     -24.132 -16.834  17.317  1.00 41.76           N  
ANISOU  456  N   LYS A  55     5387   5137   5344    -10     26   -465       N  
ATOM    457  CA  LYS A  55     -24.621 -18.020  18.008  1.00 42.78           C  
ANISOU  457  CA  LYS A  55     5481   5256   5519    -12     15   -464       C  
ATOM    458  C   LYS A  55     -25.790 -17.685  18.936  1.00 41.42           C  
ANISOU  458  C   LYS A  55     5283   5088   5366    -13     -3   -446       C  
ATOM    459  O   LYS A  55     -25.707 -16.738  19.731  1.00 41.65           O  
ANISOU  459  O   LYS A  55     5307   5130   5389    -11      6   -425       O  
ATOM    460  CB  LYS A  55     -23.485 -18.739  18.748  1.00 45.03           C  
ANISOU  460  CB  LYS A  55     5746   5532   5832    -13     38   -461       C  
ATOM    461  CG  LYS A  55     -22.388 -19.260  17.804  1.00 50.61           C  
ANISOU  461  CG  LYS A  55     6467   6230   6534    -14     59   -490       C  
ATOM    462  CD  LYS A  55     -21.482 -20.311  18.451  1.00 57.05           C  
ANISOU  462  CD  LYS A  55     7256   7028   7393    -11     67   -496       C  
ATOM    463  CE  LYS A  55     -22.070 -21.728  18.352  1.00 62.41           C  
ANISOU  463  CE  LYS A  55     7924   7687   8102    -13     46   -507       C  
ATOM    464  NZ  LYS A  55     -22.317 -22.195  16.943  1.00 61.83           N  
ANISOU  464  NZ  LYS A  55     7872   7610   8011    -16     43   -539       N  
ATOM    465  N   PRO A  56     -26.893 -18.454  18.826  1.00 40.19           N  
ANISOU  465  N   PRO A  56     5111   4922   5237    -17    -27   -457       N  
ATOM    466  CA  PRO A  56     -28.126 -18.191  19.577  1.00 39.29           C  
ANISOU  466  CA  PRO A  56     4969   4809   5150    -21    -39   -450       C  
ATOM    467  C   PRO A  56     -27.927 -18.278  21.084  1.00 37.77           C  
ANISOU  467  C   PRO A  56     4756   4618   4978    -31    -11   -425       C  
ATOM    468  O   PRO A  56     -27.182 -19.133  21.564  1.00 37.26           O  
ANISOU  468  O   PRO A  56     4692   4542   4924    -36      3   -418       O  
ATOM    469  CB  PRO A  56     -29.069 -19.308  19.106  1.00 40.60           C  
ANISOU  469  CB  PRO A  56     5119   4957   5349    -27    -62   -474       C  
ATOM    470  CG  PRO A  56     -28.158 -20.414  18.679  1.00 38.53           C  
ANISOU  470  CG  PRO A  56     4871   4684   5086    -28    -52   -482       C  
ATOM    471  CD  PRO A  56     -26.980 -19.710  18.057  1.00 40.34           C  
ANISOU  471  CD  PRO A  56     5134   4924   5271    -19    -38   -481       C  
ATOM    472  N   CYS A  57     -28.593 -17.388  21.812  1.00 37.40           N  
ANISOU  472  N   CYS A  57     4695   4581   4935    -33     -8   -415       N  
ATOM    473  CA  CYS A  57     -28.488 -17.335  23.266  1.00 37.90           C  
ANISOU  473  CA  CYS A  57     4748   4644   5009    -45     19   -391       C  
ATOM    474  C   CYS A  57     -29.861 -17.294  23.912  1.00 37.66           C  
ANISOU  474  C   CYS A  57     4689   4610   5011    -59     24   -398       C  
ATOM    475  O   CYS A  57     -30.785 -16.675  23.393  1.00 39.44           O  
ANISOU  475  O   CYS A  57     4898   4841   5248    -52      5   -417       O  
ATOM    476  CB  CYS A  57     -27.673 -16.118  23.714  1.00 37.92           C  
ANISOU  476  CB  CYS A  57     4765   4664   4981    -35     31   -371       C  
ATOM    477  SG  CYS A  57     -25.889 -16.205  23.362  1.00 41.78           S  
ANISOU  477  SG  CYS A  57     5277   5151   5445    -25     39   -365       S  
ATOM    478  N   THR A  58     -29.988 -17.966  25.048  1.00 37.61           N  
ANISOU  478  N   THR A  58     4678   4590   5022    -80     51   -385       N  
ATOM    479  CA  THR A  58     -31.192 -17.864  25.857  1.00 38.60           C  
ANISOU  479  CA  THR A  58     4778   4711   5177   -100     72   -392       C  
ATOM    480  C   THR A  58     -30.945 -16.832  26.952  1.00 36.72           C  
ANISOU  480  C   THR A  58     4549   4485   4917   -102     96   -370       C  
ATOM    481  O   THR A  58     -29.866 -16.794  27.546  1.00 35.95           O  
ANISOU  481  O   THR A  58     4482   4387   4790    -99    105   -344       O  
ATOM    482  CB  THR A  58     -31.651 -19.248  26.437  1.00 39.41           C  
ANISOU  482  CB  THR A  58     4877   4786   5309   -129     93   -393       C  
ATOM    483  OG1 THR A  58     -32.645 -19.045  27.449  1.00 43.44           O  
ANISOU  483  OG1 THR A  58     5370   5291   5843   -155    130   -398       O  
ATOM    484  CG2 THR A  58     -30.487 -20.020  27.050  1.00 38.99           C  
ANISOU  484  CG2 THR A  58     4864   4718   5234   -133    101   -365       C  
ATOM    485  N   ARG A  59     -31.933 -15.969  27.183  1.00 39.07           N  
ANISOU  485  N   ARG A  59     4820   4792   5234   -105    104   -385       N  
ATOM    486  CA  ARG A  59     -31.868 -14.983  28.261  1.00 37.73           C  
ANISOU  486  CA  ARG A  59     4656   4633   5048   -109    130   -370       C  
ATOM    487  C   ARG A  59     -32.276 -15.618  29.588  1.00 39.69           C  
ANISOU  487  C   ARG A  59     4912   4863   5306   -144    177   -362       C  
ATOM    488  O   ARG A  59     -33.279 -16.329  29.662  1.00 39.68           O  
ANISOU  488  O   ARG A  59     4887   4847   5344   -167    195   -384       O  
ATOM    489  CB  ARG A  59     -32.770 -13.772  27.962  1.00 37.28           C  
ANISOU  489  CB  ARG A  59     4565   4590   5010    -97    118   -394       C  
ATOM    490  CG  ARG A  59     -32.985 -12.866  29.181  1.00 38.99           C  
ANISOU  490  CG  ARG A  59     4780   4814   5221   -107    153   -387       C  
ATOM    491  CD  ARG A  59     -33.337 -11.441  28.822  1.00 41.29           C  
ANISOU  491  CD  ARG A  59     5052   5122   5516    -84    130   -401       C  
ATOM    492  NE  ARG A  59     -34.771 -11.227  28.662  1.00 45.29           N  
ANISOU  492  NE  ARG A  59     5506   5622   6079    -88    128   -443       N  
ATOM    493  CZ  ARG A  59     -35.528 -10.485  29.466  1.00 45.75           C  
ANISOU  493  CZ  ARG A  59     5536   5682   6164    -98    155   -461       C  
ATOM    494  NH1 ARG A  59     -35.004  -9.870  30.519  1.00 42.34           N  
ANISOU  494  NH1 ARG A  59     5129   5260   5698   -104    189   -438       N  
ATOM    495  NH2 ARG A  59     -36.822 -10.357  29.207  1.00 46.41           N  
ANISOU  495  NH2 ARG A  59     5565   5757   6312    -99    148   -507       N  
ATOM    496  N   LYS A  60     -31.502 -15.349  30.634  1.00 41.21           N  
ANISOU  496  N   LYS A  60     5142   5055   5463   -149    197   -332       N  
ATOM    497  CA  LYS A  60     -31.878 -15.746  31.983  1.00 42.20           C  
ANISOU  497  CA  LYS A  60     5290   5161   5584   -184    243   -322       C  
ATOM    498  C   LYS A  60     -32.105 -14.528  32.870  1.00 42.79           C  
ANISOU  498  C   LYS A  60     5365   5248   5644   -187    270   -320       C  
ATOM    499  O   LYS A  60     -31.164 -13.789  33.183  1.00 40.53           O  
ANISOU  499  O   LYS A  60     5106   4973   5320   -169    256   -297       O  
ATOM    500  CB  LYS A  60     -30.836 -16.694  32.572  1.00 44.16           C  
ANISOU  500  CB  LYS A  60     5594   5385   5802   -192    240   -290       C  
ATOM    501  CG  LYS A  60     -30.962 -18.114  32.036  1.00 49.30           C  
ANISOU  501  CG  LYS A  60     6244   6013   6476   -202    230   -297       C  
ATOM    502  CD  LYS A  60     -29.623 -18.816  31.974  1.00 51.34           C  
ANISOU  502  CD  LYS A  60     6541   6255   6711   -187    197   -273       C  
ATOM    503  CE  LYS A  60     -29.748 -20.203  31.335  1.00 56.12           C  
ANISOU  503  CE  LYS A  60     7142   6837   7343   -194    184   -283       C  
ATOM    504  NZ  LYS A  60     -30.395 -21.221  32.226  1.00 54.61           N  
ANISOU  504  NZ  LYS A  60     6979   6611   7160   -235    217   -276       N  
ATOM    505  N   LEU A  61     -33.371 -14.321  33.238  1.00 44.20           N  
ANISOU  505  N   LEU A  61     5512   5426   5858   -211    308   -348       N  
ATOM    506  CA  LEU A  61     -33.801 -13.230  34.112  1.00 44.96           C  
ANISOU  506  CA  LEU A  61     5603   5532   5950   -219    342   -356       C  
ATOM    507  C   LEU A  61     -33.695 -13.664  35.574  1.00 44.48           C  
ANISOU  507  C   LEU A  61     5597   5448   5855   -257    395   -335       C  
ATOM    508  O   LEU A  61     -34.262 -14.686  35.970  1.00 43.64           O  
ANISOU  508  O   LEU A  61     5502   5316   5763   -294    432   -341       O  
ATOM    509  CB  LEU A  61     -35.244 -12.813  33.777  1.00 45.98           C  
ANISOU  509  CB  LEU A  61     5664   5666   6142   -226    358   -405       C  
ATOM    510  CG  LEU A  61     -35.925 -11.585  34.426  1.00 49.68           C  
ANISOU  510  CG  LEU A  61     6105   6146   6626   -229    389   -429       C  
ATOM    511  CD1 LEU A  61     -36.537 -11.911  35.784  1.00 54.38           C  
ANISOU  511  CD1 LEU A  61     6718   6722   7222   -278    468   -437       C  
ATOM    512  CD2 LEU A  61     -35.009 -10.360  34.529  1.00 42.99           C  
ANISOU  512  CD2 LEU A  61     5282   5320   5733   -197    361   -404       C  
ATOM    513  N   PHE A  62     -32.981 -12.875  36.373  1.00 40.86           N  
ANISOU  513  N   PHE A  62     5178   4995   5350   -249    397   -311       N  
ATOM    514  CA  PHE A  62     -32.731 -13.235  37.761  1.00 40.62           C  
ANISOU  514  CA  PHE A  62     5217   4940   5276   -282    437   -287       C  
ATOM    515  C   PHE A  62     -33.632 -12.493  38.757  1.00 41.48           C  
ANISOU  515  C   PHE A  62     5323   5050   5386   -311    501   -308       C  
ATOM    516  O   PHE A  62     -33.969 -11.318  38.558  1.00 42.59           O  
ANISOU  516  O   PHE A  62     5419   5216   5546   -292    499   -329       O  
ATOM    517  CB  PHE A  62     -31.234 -13.099  38.089  1.00 39.81           C  
ANISOU  517  CB  PHE A  62     5173   4834   5120   -257    394   -246       C  
ATOM    518  CG  PHE A  62     -30.364 -14.062  37.316  1.00 39.76           C  
ANISOU  518  CG  PHE A  62     5175   4817   5114   -238    344   -229       C  
ATOM    519  CD1 PHE A  62     -29.741 -13.669  36.134  1.00 40.31           C  
ANISOU  519  CD1 PHE A  62     5207   4911   5198   -198    295   -233       C  
ATOM    520  CD2 PHE A  62     -30.195 -15.373  37.754  1.00 38.93           C  
ANISOU  520  CD2 PHE A  62     5119   4675   4997   -263    349   -213       C  
ATOM    521  CE1 PHE A  62     -28.950 -14.566  35.400  1.00 40.22           C  
ANISOU  521  CE1 PHE A  62     5201   4889   5192   -182    255   -225       C  
ATOM    522  CE2 PHE A  62     -29.411 -16.279  37.028  1.00 44.75           C  
ANISOU  522  CE2 PHE A  62     5860   5401   5743   -244    302   -203       C  
ATOM    523  CZ  PHE A  62     -28.785 -15.873  35.848  1.00 40.45           C  
ANISOU  523  CZ  PHE A  62     5271   4882   5214   -204    257   -210       C  
ATOM    524  N   ALA A  63     -34.034 -13.198  39.812  1.00 39.76           N  
ANISOU  524  N   ALA A  63     5156   4801   5149   -360    559   -303       N  
ATOM    525  CA  ALA A  63     -34.866 -12.624  40.868  1.00 41.01           C  
ANISOU  525  CA  ALA A  63     5323   4955   5305   -396    633   -325       C  
ATOM    526  C   ALA A  63     -34.217 -11.398  41.504  1.00 40.23           C  
ANISOU  526  C   ALA A  63     5254   4872   5161   -375    621   -310       C  
ATOM    527  O   ALA A  63     -34.905 -10.466  41.902  1.00 41.51           O  
ANISOU  527  O   ALA A  63     5387   5047   5339   -383    662   -339       O  
ATOM    528  CB  ALA A  63     -35.183 -13.679  41.938  1.00 40.68           C  
ANISOU  528  CB  ALA A  63     5355   4870   5232   -455    697   -315       C  
ATOM    529  N   ASN A  64     -32.891 -11.420  41.600  1.00 41.18           N  
ANISOU  529  N   ASN A  64     5428   4989   5230   -347    565   -267       N  
ATOM    530  CA  ASN A  64     -32.106 -10.346  42.213  1.00 40.92           C  
ANISOU  530  CA  ASN A  64     5429   4966   5151   -325    545   -249       C  
ATOM    531  C   ASN A  64     -30.656 -10.414  41.725  1.00 39.71           C  
ANISOU  531  C   ASN A  64     5297   4816   4975   -282    465   -214       C  
ATOM    532  O   ASN A  64     -30.287 -11.361  41.032  1.00 40.55           O  
ANISOU  532  O   ASN A  64     5398   4913   5095   -274    432   -204       O  
ATOM    533  CB  ASN A  64     -32.189 -10.412  43.747  1.00 39.60           C  
ANISOU  533  CB  ASN A  64     5350   4770   4927   -367    599   -236       C  
ATOM    534  CG  ASN A  64     -31.824 -11.783  44.303  1.00 42.11           C  
ANISOU  534  CG  ASN A  64     5752   5042   5205   -398    600   -206       C  
ATOM    535  OD1 ASN A  64     -30.727 -12.290  44.067  1.00 42.67           O  
ANISOU  535  OD1 ASN A  64     5856   5100   5255   -371    534   -174       O  
ATOM    536  ND2 ASN A  64     -32.748 -12.386  45.058  1.00 41.01           N  
ANISOU  536  ND2 ASN A  64     5651   4875   5057   -455    677   -218       N  
ATOM    537  N   MET A  65     -29.838  -9.426  42.088  1.00 39.66           N  
ANISOU  537  N   MET A  65     5309   4820   4938   -256    436   -200       N  
ATOM    538  CA  MET A  65     -28.462  -9.347  41.585  1.00 39.08           C  
ANISOU  538  CA  MET A  65     5243   4751   4854   -215    365   -175       C  
ATOM    539  C   MET A  65     -27.502 -10.373  42.190  1.00 41.29           C  
ANISOU  539  C   MET A  65     5600   4992   5098   -220    333   -143       C  
ATOM    540  O   MET A  65     -26.563 -10.825  41.519  1.00 40.74           O  
ANISOU  540  O   MET A  65     5522   4918   5040   -193    279   -132       O  
ATOM    541  CB  MET A  65     -27.907  -7.934  41.732  1.00 36.70           C  
ANISOU  541  CB  MET A  65     4932   4473   4541   -186    343   -174       C  
ATOM    542  CG  MET A  65     -28.502  -6.964  40.730  1.00 34.84           C  
ANISOU  542  CG  MET A  65     4617   4274   4349   -166    345   -202       C  
ATOM    543  SD  MET A  65     -27.799  -5.319  40.828  1.00 36.52           S  
ANISOU  543  SD  MET A  65     4820   4509   4547   -132    317   -199       S  
ATOM    544  CE  MET A  65     -28.698  -4.624  42.218  1.00 34.50           C  
ANISOU  544  CE  MET A  65     4591   4249   4269   -162    378   -214       C  
ATOM    545  N   ARG A  66     -27.737 -10.745  43.445  1.00 44.22           N  
ANISOU  545  N   ARG A  66     6049   5330   5424   -256    366   -131       N  
ATOM    546  CA  ARG A  66     -26.911 -11.769  44.090  1.00 46.87           C  
ANISOU  546  CA  ARG A  66     6468   5618   5721   -263    330   -100       C  
ATOM    547  C   ARG A  66     -27.032 -13.114  43.366  1.00 43.90           C  
ANISOU  547  C   ARG A  66     6080   5226   5375   -270    320    -99       C  
ATOM    548  O   ARG A  66     -26.025 -13.751  43.079  1.00 41.79           O  
ANISOU  548  O   ARG A  66     5828   4939   5112   -246    259    -83       O  
ATOM    549  CB  ARG A  66     -27.213 -11.881  45.589  1.00 49.87           C  
ANISOU  549  CB  ARG A  66     6948   5960   6038   -304    369    -86       C  
ATOM    550  CG  ARG A  66     -26.575 -10.731  46.397  1.00 59.73           C  
ANISOU  550  CG  ARG A  66     8234   7213   7247   -286    349    -78       C  
ATOM    551  CD  ARG A  66     -27.108 -10.630  47.826  1.00 66.69           C  
ANISOU  551  CD  ARG A  66     9210   8065   8065   -331    404    -72       C  
ATOM    552  NE  ARG A  66     -26.549  -9.476  48.538  1.00 69.32           N  
ANISOU  552  NE  ARG A  66     9573   8404   8363   -312    383    -68       N  
ATOM    553  CZ  ARG A  66     -26.982  -9.028  49.718  1.00 75.38           C  
ANISOU  553  CZ  ARG A  66    10411   9155   9075   -345    432    -69       C  
ATOM    554  NH1 ARG A  66     -27.993  -9.627  50.344  1.00 75.64           N  
ANISOU  554  NH1 ARG A  66    10495   9164   9080   -402    511    -75       N  
ATOM    555  NH2 ARG A  66     -26.403  -7.969  50.278  1.00 76.71           N  
ANISOU  555  NH2 ARG A  66    10602   9329   9215   -323    405    -66       N  
ATOM    556  N   ASP A  67     -28.259 -13.505  43.034  1.00 42.83           N  
ANISOU  556  N   ASP A  67     5907   5097   5268   -301    377   -121       N  
ATOM    557  CA  ASP A  67     -28.505 -14.726  42.266  1.00 43.65           C  
ANISOU  557  CA  ASP A  67     5989   5189   5406   -309    371   -125       C  
ATOM    558  C   ASP A  67     -27.712 -14.731  40.959  1.00 41.44           C  
ANISOU  558  C   ASP A  67     5648   4933   5166   -262    309   -129       C  
ATOM    559  O   ASP A  67     -27.011 -15.693  40.669  1.00 41.95           O  
ANISOU  559  O   ASP A  67     5731   4973   5234   -251    267   -116       O  
ATOM    560  CB  ASP A  67     -30.005 -14.917  42.005  1.00 44.40           C  
ANISOU  560  CB  ASP A  67     6036   5294   5538   -346    442   -156       C  
ATOM    561  CG  ASP A  67     -30.754 -15.442  43.225  1.00 47.03           C  
ANISOU  561  CG  ASP A  67     6443   5590   5837   -405    511   -152       C  
ATOM    562  OD1 ASP A  67     -30.119 -15.752  44.258  1.00 50.61           O  
ANISOU  562  OD1 ASP A  67     6995   6004   6230   -418    499   -121       O  
ATOM    563  OD2 ASP A  67     -31.993 -15.548  43.151  1.00 51.44           O  
ANISOU  563  OD2 ASP A  67     6962   6154   6431   -440    577   -183       O  
ATOM    564  N   ALA A  68     -27.794 -13.633  40.207  1.00 39.54           N  
ANISOU  564  N   ALA A  68     5338   4736   4951   -234    304   -148       N  
ATOM    565  CA  ALA A  68     -27.036 -13.461  38.964  1.00 37.04           C  
ANISOU  565  CA  ALA A  68     4968   4442   4663   -192    254   -154       C  
ATOM    566  C   ALA A  68     -25.531 -13.721  39.133  1.00 39.36           C  
ANISOU  566  C   ALA A  68     5299   4715   4940   -166    195   -132       C  
ATOM    567  O   ALA A  68     -24.914 -14.420  38.309  1.00 38.55           O  
ANISOU  567  O   ALA A  68     5177   4606   4862   -147    160   -135       O  
ATOM    568  CB  ALA A  68     -27.271 -12.072  38.403  1.00 34.95           C  
ANISOU  568  CB  ALA A  68     4647   4220   4413   -171    258   -172       C  
ATOM    569  N   SER A  69     -24.957 -13.152  40.196  1.00 37.33           N  
ANISOU  569  N   SER A  69     5094   4445   4645   -163    184   -115       N  
ATOM    570  CA  SER A  69     -23.549 -13.334  40.532  1.00 38.91           C  
ANISOU  570  CA  SER A  69     5331   4619   4835   -137    123    -99       C  
ATOM    571  C   SER A  69     -23.217 -14.781  40.881  1.00 40.74           C  
ANISOU  571  C   SER A  69     5618   4802   5061   -149     96    -84       C  
ATOM    572  O   SER A  69     -22.185 -15.304  40.457  1.00 39.44           O  
ANISOU  572  O   SER A  69     5446   4620   4919   -122     42    -85       O  
ATOM    573  CB  SER A  69     -23.149 -12.419  41.695  1.00 38.87           C  
ANISOU  573  CB  SER A  69     5375   4606   4788   -135    116    -85       C  
ATOM    574  OG  SER A  69     -22.868 -11.114  41.231  1.00 39.77           O  
ANISOU  574  OG  SER A  69     5437   4759   4916   -110    113    -97       O  
ATOM    575  N   GLN A  70     -24.095 -15.418  41.653  1.00 42.70           N  
ANISOU  575  N   GLN A  70     5921   5024   5281   -190    135    -73       N  
ATOM    576  CA  GLN A  70     -23.895 -16.804  42.052  1.00 43.62           C  
ANISOU  576  CA  GLN A  70     6099   5087   5386   -206    112    -57       C  
ATOM    577  C   GLN A  70     -24.032 -17.764  40.870  1.00 42.06           C  
ANISOU  577  C   GLN A  70     5849   4894   5238   -200    105    -72       C  
ATOM    578  O   GLN A  70     -23.430 -18.843  40.876  1.00 41.11           O  
ANISOU  578  O   GLN A  70     5761   4733   5125   -194     61    -63       O  
ATOM    579  CB  GLN A  70     -24.844 -17.193  43.191  1.00 44.90           C  
ANISOU  579  CB  GLN A  70     6342   5218   5501   -258    166    -42       C  
ATOM    580  CG  GLN A  70     -24.655 -16.385  44.482  1.00 53.42           C  
ANISOU  580  CG  GLN A  70     7494   6283   6521   -267    171    -26       C  
ATOM    581  CD  GLN A  70     -23.188 -16.084  44.808  1.00 59.95           C  
ANISOU  581  CD  GLN A  70     8351   7090   7337   -225     86    -13       C  
ATOM    582  OE1 GLN A  70     -22.728 -14.942  44.666  1.00 61.85           O  
ANISOU  582  OE1 GLN A  70     8551   7363   7586   -196     72    -22       O  
ATOM    583  NE2 GLN A  70     -22.448 -17.108  45.234  1.00 61.65           N  
ANISOU  583  NE2 GLN A  70     8636   7247   7539   -220     26      6       N  
ATOM    584  N   TRP A  71     -24.814 -17.365  39.866  1.00 39.83           N  
ANISOU  584  N   TRP A  71     5488   4657   4990   -200    143    -96       N  
ATOM    585  CA  TRP A  71     -24.977 -18.159  38.645  1.00 40.92           C  
ANISOU  585  CA  TRP A  71     5571   4803   5173   -193    135   -113       C  
ATOM    586  C   TRP A  71     -23.697 -18.106  37.824  1.00 40.78           C  
ANISOU  586  C   TRP A  71     5520   4793   5182   -148     78   -121       C  
ATOM    587  O   TRP A  71     -23.287 -19.108  37.237  1.00 41.78           O  
ANISOU  587  O   TRP A  71     5638   4900   5334   -139     49   -127       O  
ATOM    588  CB  TRP A  71     -26.175 -17.676  37.810  1.00 39.24           C  
ANISOU  588  CB  TRP A  71     5289   4633   4988   -203    183   -139       C  
ATOM    589  CG  TRP A  71     -26.386 -18.466  36.525  1.00 37.76           C  
ANISOU  589  CG  TRP A  71     5050   4452   4844   -195    172   -159       C  
ATOM    590  CD1 TRP A  71     -26.950 -19.714  36.408  1.00 37.21           C  
ANISOU  590  CD1 TRP A  71     4991   4356   4791   -220    183   -162       C  
ATOM    591  CD2 TRP A  71     -26.039 -18.062  35.187  1.00 33.94           C  
ANISOU  591  CD2 TRP A  71     4504   4002   4389   -162    149   -180       C  
ATOM    592  NE1 TRP A  71     -26.969 -20.108  35.086  1.00 37.23           N  
ANISOU  592  NE1 TRP A  71     4938   4374   4832   -202    165   -184       N  
ATOM    593  CE2 TRP A  71     -26.416 -19.115  34.318  1.00 34.90           C  
ANISOU  593  CE2 TRP A  71     4602   4116   4542   -167    145   -195       C  
ATOM    594  CE3 TRP A  71     -25.441 -16.917  34.640  1.00 34.43           C  
ANISOU  594  CE3 TRP A  71     4534   4098   4451   -131    133   -187       C  
ATOM    595  CZ2 TRP A  71     -26.215 -19.054  32.933  1.00 34.16           C  
ANISOU  595  CZ2 TRP A  71     4458   4046   4475   -143    126   -217       C  
ATOM    596  CZ3 TRP A  71     -25.240 -16.862  33.256  1.00 32.97           C  
ANISOU  596  CZ3 TRP A  71     4301   3934   4290   -109    117   -208       C  
ATOM    597  CH2 TRP A  71     -25.628 -17.923  32.424  1.00 32.64           C  
ANISOU  597  CH2 TRP A  71     4241   3884   4275   -115    113   -223       C  
ATOM    598  N   ILE A  72     -23.070 -16.934  37.792  1.00 41.85           N  
ANISOU  598  N   ILE A  72     5635   4954   5312   -123     64   -124       N  
ATOM    599  CA  ILE A  72     -21.783 -16.763  37.116  1.00 43.14           C  
ANISOU  599  CA  ILE A  72     5768   5123   5503    -85     18   -135       C  
ATOM    600  C   ILE A  72     -20.750 -17.736  37.690  1.00 43.85           C  
ANISOU  600  C   ILE A  72     5905   5159   5596    -74    -38   -125       C  
ATOM    601  O   ILE A  72     -20.033 -18.402  36.939  1.00 42.35           O  
ANISOU  601  O   ILE A  72     5688   4959   5445    -54    -70   -141       O  
ATOM    602  CB  ILE A  72     -21.276 -15.312  37.213  1.00 42.57           C  
ANISOU  602  CB  ILE A  72     5676   5079   5421    -65     15   -137       C  
ATOM    603  CG1 ILE A  72     -22.118 -14.390  36.321  1.00 41.85           C  
ANISOU  603  CG1 ILE A  72     5528   5037   5336    -66     56   -153       C  
ATOM    604  CG2 ILE A  72     -19.781 -15.212  36.837  1.00 45.00           C  
ANISOU  604  CG2 ILE A  72     5963   5378   5757    -30    -34   -149       C  
ATOM    605  CD1 ILE A  72     -21.887 -12.880  36.590  1.00 36.86           C  
ANISOU  605  CD1 ILE A  72     4886   4432   4688    -54     62   -152       C  
ATOM    606  N   LYS A  73     -20.697 -17.817  39.019  1.00 45.71           N  
ANISOU  606  N   LYS A  73     6216   5360   5794    -87    -51   -101       N  
ATOM    607  CA  LYS A  73     -19.791 -18.732  39.716  1.00 48.24           C  
ANISOU  607  CA  LYS A  73     6597   5621   6113    -77   -114    -88       C  
ATOM    608  C   LYS A  73     -20.073 -20.192  39.375  1.00 48.24           C  
ANISOU  608  C   LYS A  73     6609   5588   6131    -91   -121    -89       C  
ATOM    609  O   LYS A  73     -19.145 -20.966  39.151  1.00 48.74           O  
ANISOU  609  O   LYS A  73     6673   5619   6228    -67   -178    -97       O  
ATOM    610  CB  LYS A  73     -19.847 -18.521  41.228  1.00 48.98           C  
ANISOU  610  CB  LYS A  73     6783   5679   6150    -95   -123    -60       C  
ATOM    611  CG  LYS A  73     -19.021 -17.336  41.717  1.00 56.84           C  
ANISOU  611  CG  LYS A  73     7778   6683   7135    -69   -152    -61       C  
ATOM    612  CD  LYS A  73     -19.267 -17.061  43.201  1.00 62.41           C  
ANISOU  612  CD  LYS A  73     8582   7357   7774    -91   -152    -33       C  
ATOM    613  CE  LYS A  73     -18.484 -15.842  43.685  1.00 64.93           C  
ANISOU  613  CE  LYS A  73     8900   7686   8085    -65   -182    -36       C  
ATOM    614  NZ  LYS A  73     -17.045 -16.152  43.963  1.00 64.41           N  
ANISOU  614  NZ  LYS A  73     8853   7573   8045    -27   -276    -40       N  
ATOM    615  N   ARG A  74     -21.349 -20.560  39.319  1.00 48.10           N  
ANISOU  615  N   ARG A  74     6597   5579   6098   -128    -64    -83       N  
ATOM    616  CA  ARG A  74     -21.718 -21.936  38.991  1.00 50.00           C  
ANISOU  616  CA  ARG A  74     6851   5790   6357   -145    -66    -84       C  
ATOM    617  C   ARG A  74     -21.323 -22.317  37.568  1.00 48.49           C  
ANISOU  617  C   ARG A  74     6580   5620   6222   -118    -82   -114       C  
ATOM    618  O   ARG A  74     -20.902 -23.446  37.334  1.00 49.54           O  
ANISOU  618  O   ARG A  74     6725   5717   6382   -111   -119   -118       O  
ATOM    619  CB  ARG A  74     -23.206 -22.198  39.241  1.00 50.82           C  
ANISOU  619  CB  ARG A  74     6972   5899   6439   -194      4    -77       C  
ATOM    620  CG  ARG A  74     -23.584 -22.214  40.714  1.00 54.95           C  
ANISOU  620  CG  ARG A  74     7593   6384   6903   -230     23    -48       C  
ATOM    621  CD  ARG A  74     -25.016 -22.690  40.904  1.00 60.74           C  
ANISOU  621  CD  ARG A  74     8340   7112   7625   -283     98    -47       C  
ATOM    622  NE  ARG A  74     -25.710 -21.902  41.922  1.00 64.35           N  
ANISOU  622  NE  ARG A  74     8841   7575   8035   -317    154    -38       N  
ATOM    623  CZ  ARG A  74     -26.701 -21.046  41.676  1.00 64.00           C  
ANISOU  623  CZ  ARG A  74     8739   7577   8002   -332    219    -58       C  
ATOM    624  NH1 ARG A  74     -27.147 -20.861  40.436  1.00 61.88           N  
ANISOU  624  NH1 ARG A  74     8371   7353   7786   -317    232    -87       N  
ATOM    625  NH2 ARG A  74     -27.256 -20.377  42.679  1.00 65.69           N  
ANISOU  625  NH2 ARG A  74     8996   7790   8173   -363    270    -52       N  
ATOM    626  N   MET A  75     -21.432 -21.365  36.639  1.00 47.60           N  
ANISOU  626  N   MET A  75     6395   5563   6127   -103    -56   -135       N  
ATOM    627  CA  MET A  75     -21.075 -21.594  35.236  1.00 46.47           C  
ANISOU  627  CA  MET A  75     6184   5443   6030    -80    -64   -165       C  
ATOM    628  C   MET A  75     -19.577 -21.794  35.079  1.00 48.95           C  
ANISOU  628  C   MET A  75     6489   5734   6375    -44   -121   -179       C  
ATOM    629  O   MET A  75     -19.130 -22.458  34.139  1.00 49.81           O  
ANISOU  629  O   MET A  75     6561   5840   6524    -29   -136   -204       O  
ATOM    630  CB  MET A  75     -21.548 -20.446  34.339  1.00 43.12           C  
ANISOU  630  CB  MET A  75     5699   5078   5607    -75    -25   -182       C  
ATOM    631  CG  MET A  75     -23.057 -20.318  34.221  1.00 41.64           C  
ANISOU  631  CG  MET A  75     5501   4912   5408   -106     27   -181       C  
ATOM    632  SD  MET A  75     -23.878 -21.793  33.553  1.00 41.05           S  
ANISOU  632  SD  MET A  75     5417   4818   5361   -126     36   -193       S  
ATOM    633  CE  MET A  75     -23.594 -21.568  31.798  1.00 25.73           C  
ANISOU  633  CE  MET A  75     3407   2916   3453    -98     28   -228       C  
ATOM    634  N   GLU A  76     -18.813 -21.202  35.996  1.00 50.89           N  
ANISOU  634  N   GLU A  76     6766   5963   6606    -30   -152   -167       N  
ATOM    635  CA  GLU A  76     -17.368 -21.409  36.078  1.00 52.40           C  
ANISOU  635  CA  GLU A  76     6952   6123   6834      4   -214   -183       C  
ATOM    636  C   GLU A  76     -17.077 -22.826  36.593  1.00 51.18           C  
ANISOU  636  C   GLU A  76     6851   5905   6693      4   -267   -175       C  
ATOM    637  O   GLU A  76     -16.296 -23.558  35.984  1.00 50.53           O  
ANISOU  637  O   GLU A  76     6737   5801   6662     26   -303   -202       O  
ATOM    638  CB  GLU A  76     -16.729 -20.346  36.978  1.00 54.03           C  
ANISOU  638  CB  GLU A  76     7180   6327   7021     17   -237   -172       C  
ATOM    639  CG  GLU A  76     -15.215 -20.214  36.839  1.00 60.89           C  
ANISOU  639  CG  GLU A  76     8017   7176   7941     56   -293   -201       C  
ATOM    640  CD  GLU A  76     -14.565 -19.420  37.976  1.00 65.33           C  
ANISOU  640  CD  GLU A  76     8617   7718   8486     69   -333   -188       C  
ATOM    641  OE1 GLU A  76     -13.320 -19.503  38.110  1.00 66.64           O  
ANISOU  641  OE1 GLU A  76     8769   7852   8699    100   -393   -211       O  
ATOM    642  OE2 GLU A  76     -15.283 -18.722  38.734  1.00 64.26           O  
ANISOU  642  OE2 GLU A  76     8525   7598   8294     49   -306   -159       O  
ATOM    643  N   ASP A  77     -17.725 -23.207  37.699  1.00 49.69           N  
ANISOU  643  N   ASP A  77     6742   5681   6455    -24   -268   -140       N  
ATOM    644  CA  ASP A  77     -17.651 -24.574  38.234  1.00 50.47           C  
ANISOU  644  CA  ASP A  77     6907   5715   6555    -32   -312   -127       C  
ATOM    645  C   ASP A  77     -18.021 -25.635  37.187  1.00 49.72           C  
ANISOU  645  C   ASP A  77     6771   5621   6498    -38   -298   -146       C  
ATOM    646  O   ASP A  77     -17.381 -26.681  37.112  1.00 51.68           O  
ANISOU  646  O   ASP A  77     7032   5821   6781    -21   -352   -156       O  
ATOM    647  CB  ASP A  77     -18.569 -24.746  39.455  1.00 51.01           C  
ANISOU  647  CB  ASP A  77     7071   5754   6556    -74   -290    -86       C  
ATOM    648  CG  ASP A  77     -18.167 -23.878  40.643  1.00 53.28           C  
ANISOU  648  CG  ASP A  77     7418   6027   6798    -70   -313    -65       C  
ATOM    649  OD1 ASP A  77     -16.988 -23.456  40.726  1.00 50.82           O  
ANISOU  649  OD1 ASP A  77     7090   5706   6514    -31   -373    -79       O  
ATOM    650  OD2 ASP A  77     -19.046 -23.627  41.505  1.00 51.89           O  
ANISOU  650  OD2 ASP A  77     7307   5848   6562   -108   -270    -37       O  
ATOM    651  N   ILE A  78     -19.061 -25.368  36.397  1.00 47.14           N  
ANISOU  651  N   ILE A  78     6399   5346   6167    -59   -230   -152       N  
ATOM    652  CA  ILE A  78     -19.470 -26.280  35.323  1.00 45.70           C  
ANISOU  652  CA  ILE A  78     6175   5168   6019    -64   -215   -174       C  
ATOM    653  C   ILE A  78     -18.513 -26.214  34.124  1.00 45.27           C  
ANISOU  653  C   ILE A  78     6046   5135   6020    -27   -234   -215       C  
ATOM    654  O   ILE A  78     -18.260 -27.225  33.483  1.00 46.48           O  
ANISOU  654  O   ILE A  78     6182   5267   6212    -18   -254   -236       O  
ATOM    655  CB  ILE A  78     -20.938 -26.037  34.873  1.00 45.33           C  
ANISOU  655  CB  ILE A  78     6105   5164   5953    -98   -142   -171       C  
ATOM    656  CG1 ILE A  78     -21.906 -26.291  36.034  1.00 45.23           C  
ANISOU  656  CG1 ILE A  78     6166   5124   5895   -141   -114   -138       C  
ATOM    657  CG2 ILE A  78     -21.307 -26.947  33.717  1.00 43.75           C  
ANISOU  657  CG2 ILE A  78     5862   4969   5791   -100   -134   -196       C  
ATOM    658  CD1 ILE A  78     -23.249 -25.605  35.894  1.00 40.93           C  
ANISOU  658  CD1 ILE A  78     5595   4624   5332   -172    -42   -138       C  
ATOM    659  N   GLY A  79     -17.981 -25.028  33.832  1.00 43.83           N  
ANISOU  659  N   GLY A  79     5822   4992   5840     -7   -223   -228       N  
ATOM    660  CA  GLY A  79     -17.031 -24.856  32.728  1.00 44.72           C  
ANISOU  660  CA  GLY A  79     5867   5123   6001     23   -230   -270       C  
ATOM    661  C   GLY A  79     -17.646 -24.332  31.440  1.00 44.86           C  
ANISOU  661  C   GLY A  79     5830   5197   6016     15   -174   -289       C  
ATOM    662  O   GLY A  79     -17.189 -24.659  30.338  1.00 44.60           O  
ANISOU  662  O   GLY A  79     5753   5172   6019     29   -170   -325       O  
ATOM    663  N   LEU A  80     -18.683 -23.511  31.585  1.00 43.53           N  
ANISOU  663  N   LEU A  80     5668   5065   5805     -6   -131   -269       N  
ATOM    664  CA  LEU A  80     -19.418 -22.960  30.451  1.00 43.01           C  
ANISOU  664  CA  LEU A  80     5561   5048   5732    -13    -86   -284       C  
ATOM    665  C   LEU A  80     -19.483 -21.442  30.541  1.00 42.39           C  
ANISOU  665  C   LEU A  80     5471   5010   5626    -11    -61   -276       C  
ATOM    666  O   LEU A  80     -19.498 -20.877  31.639  1.00 42.17           O  
ANISOU  666  O   LEU A  80     5472   4976   5573    -15    -66   -252       O  
ATOM    667  CB  LEU A  80     -20.838 -23.523  30.413  1.00 42.02           C  
ANISOU  667  CB  LEU A  80     5448   4925   5592    -42    -61   -272       C  
ATOM    668  CG  LEU A  80     -21.005 -24.998  30.060  1.00 43.76           C  
ANISOU  668  CG  LEU A  80     5675   5113   5841    -49    -77   -283       C  
ATOM    669  CD1 LEU A  80     -22.340 -25.503  30.569  1.00 39.62           C  
ANISOU  669  CD1 LEU A  80     5176   4577   5300    -83    -54   -263       C  
ATOM    670  CD2 LEU A  80     -20.870 -25.203  28.552  1.00 40.05           C  
ANISOU  670  CD2 LEU A  80     5158   4665   5396    -36    -69   -319       C  
ATOM    671  N   GLU A  81     -19.551 -20.793  29.384  1.00 39.31           N  
ANISOU  671  N   GLU A  81     5043   4657   5236     -5    -36   -298       N  
ATOM    672  CA  GLU A  81     -19.525 -19.342  29.325  1.00 37.68           C  
ANISOU  672  CA  GLU A  81     4824   4485   5006     -1    -15   -294       C  
ATOM    673  C   GLU A  81     -20.822 -18.702  29.844  1.00 36.88           C  
ANISOU  673  C   GLU A  81     4737   4405   4871    -21      9   -271       C  
ATOM    674  O   GLU A  81     -21.926 -19.067  29.424  1.00 36.76           O  
ANISOU  674  O   GLU A  81     4715   4397   4854    -36     25   -274       O  
ATOM    675  CB  GLU A  81     -19.215 -18.880  27.899  1.00 36.85           C  
ANISOU  675  CB  GLU A  81     4686   4408   4906      7      5   -323       C  
ATOM    676  CG  GLU A  81     -18.954 -17.390  27.781  1.00 36.31           C  
ANISOU  676  CG  GLU A  81     4609   4369   4817     13     22   -321       C  
ATOM    677  CD  GLU A  81     -18.659 -16.944  26.363  1.00 36.46           C  
ANISOU  677  CD  GLU A  81     4610   4410   4833     16     45   -349       C  
ATOM    678  OE1 GLU A  81     -18.555 -17.793  25.450  1.00 40.34           O  
ANISOU  678  OE1 GLU A  81     5094   4894   5341     16     47   -373       O  
ATOM    679  OE2 GLU A  81     -18.529 -15.728  26.161  1.00 36.75           O  
ANISOU  679  OE2 GLU A  81     4646   4469   4850     17     61   -346       O  
ATOM    680  N   ALA A  82     -20.664 -17.770  30.785  1.00 33.83           N  
ANISOU  680  N   ALA A  82     4366   4024   4464    -19     10   -252       N  
ATOM    681  CA  ALA A  82     -21.754 -16.926  31.257  1.00 31.59           C  
ANISOU  681  CA  ALA A  82     4089   3762   4152    -35     36   -236       C  
ATOM    682  C   ALA A  82     -21.620 -15.587  30.548  1.00 32.55           C  
ANISOU  682  C   ALA A  82     4183   3919   4263    -22     49   -246       C  
ATOM    683  O   ALA A  82     -20.700 -14.809  30.837  1.00 33.48           O  
ANISOU  683  O   ALA A  82     4302   4040   4378     -9     41   -244       O  
ATOM    684  CB  ALA A  82     -21.679 -16.752  32.764  1.00 29.66           C  
ANISOU  684  CB  ALA A  82     3886   3497   3886    -43     31   -210       C  
ATOM    685  N   LEU A  83     -22.521 -15.337  29.601  1.00 31.84           N  
ANISOU  685  N   LEU A  83     4073   3852   4172    -27     65   -259       N  
ATOM    686  CA  LEU A  83     -22.444 -14.165  28.734  1.00 31.05           C  
ANISOU  686  CA  LEU A  83     3957   3781   4060    -16     72   -269       C  
ATOM    687  C   LEU A  83     -23.287 -13.020  29.286  1.00 31.20           C  
ANISOU  687  C   LEU A  83     3975   3819   4060    -21     84   -258       C  
ATOM    688  O   LEU A  83     -24.162 -13.238  30.128  1.00 31.81           O  
ANISOU  688  O   LEU A  83     4059   3890   4138    -37     95   -249       O  
ATOM    689  CB  LEU A  83     -22.896 -14.520  27.311  1.00 30.89           C  
ANISOU  689  CB  LEU A  83     3922   3769   4045    -16     72   -292       C  
ATOM    690  CG  LEU A  83     -22.087 -15.583  26.561  1.00 32.93           C  
ANISOU  690  CG  LEU A  83     4179   4012   4323    -11     64   -310       C  
ATOM    691  CD1 LEU A  83     -22.743 -16.965  26.687  1.00 33.42           C  
ANISOU  691  CD1 LEU A  83     4240   4053   4404    -22     57   -312       C  
ATOM    692  CD2 LEU A  83     -21.938 -15.211  25.101  1.00 31.52           C  
ANISOU  692  CD2 LEU A  83     3997   3848   4133     -5     70   -332       C  
ATOM    693  N   GLY A  84     -23.021 -11.803  28.813  1.00 29.90           N  
ANISOU  693  N   GLY A  84     3805   3674   3881    -10     86   -261       N  
ATOM    694  CA  GLY A  84     -23.786 -10.629  29.228  1.00 29.86           C  
ANISOU  694  CA  GLY A  84     3797   3686   3863    -11     94   -254       C  
ATOM    695  C   GLY A  84     -23.018  -9.711  30.160  1.00 29.75           C  
ANISOU  695  C   GLY A  84     3794   3674   3834     -5     96   -239       C  
ATOM    696  O   GLY A  84     -21.934 -10.050  30.627  1.00 30.27           O  
ANISOU  696  O   GLY A  84     3871   3725   3905      0     87   -233       O  
ATOM    697  N   MET A  85     -23.592  -8.544  30.428  1.00 31.25           N  
ANISOU  697  N   MET A  85     3981   3880   4012     -4    102   -236       N  
ATOM    698  CA  MET A  85     -22.943  -7.518  31.232  1.00 30.83           C  
ANISOU  698  CA  MET A  85     3938   3830   3945      3    103   -223       C  
ATOM    699  C   MET A  85     -23.003  -7.852  32.711  1.00 31.97           C  
ANISOU  699  C   MET A  85     4103   3961   4084     -7    108   -208       C  
ATOM    700  O   MET A  85     -24.039  -7.702  33.358  1.00 32.79           O  
ANISOU  700  O   MET A  85     4209   4067   4184    -19    125   -207       O  
ATOM    701  CB  MET A  85     -23.547  -6.140  30.933  1.00 30.94           C  
ANISOU  701  CB  MET A  85     3943   3864   3949      9    105   -227       C  
ATOM    702  CG  MET A  85     -23.024  -4.999  31.810  1.00 32.85           C  
ANISOU  702  CG  MET A  85     4194   4110   4177     16    106   -216       C  
ATOM    703  SD  MET A  85     -21.230  -4.856  31.881  1.00 36.12           S  
ANISOU  703  SD  MET A  85     4617   4515   4592     26     96   -210       S  
ATOM    704  CE  MET A  85     -20.926  -4.039  30.313  1.00 29.88           C  
ANISOU  704  CE  MET A  85     3820   3737   3796     32     98   -223       C  
ATOM    705  N   ASP A  86     -21.870  -8.317  33.226  1.00 33.75           N  
ANISOU  705  N   ASP A  86     4347   4167   4311     -1     92   -200       N  
ATOM    706  CA  ASP A  86     -21.731  -8.732  34.614  1.00 34.97           C  
ANISOU  706  CA  ASP A  86     4536   4299   4454    -10     88   -183       C  
ATOM    707  C   ASP A  86     -21.570  -7.555  35.594  1.00 34.78           C  
ANISOU  707  C   ASP A  86     4528   4280   4408     -6     89   -173       C  
ATOM    708  O   ASP A  86     -21.635  -7.742  36.809  1.00 35.08           O  
ANISOU  708  O   ASP A  86     4604   4299   4426    -16     89   -159       O  
ATOM    709  CB  ASP A  86     -20.565  -9.723  34.748  1.00 37.93           C  
ANISOU  709  CB  ASP A  86     4925   4644   4844     -1     58   -182       C  
ATOM    710  CG  ASP A  86     -19.239  -9.161  34.213  1.00 42.72           C  
ANISOU  710  CG  ASP A  86     5510   5253   5468     20     39   -194       C  
ATOM    711  OD1 ASP A  86     -18.250  -9.176  34.973  1.00 44.80           O  
ANISOU  711  OD1 ASP A  86     5790   5494   5739     30     11   -190       O  
ATOM    712  OD2 ASP A  86     -19.180  -8.709  33.042  1.00 42.94           O  
ANISOU  712  OD2 ASP A  86     5508   5301   5504     25     52   -209       O  
ATOM    713  N   ASP A  87     -21.351  -6.348  35.077  1.00 33.79           N  
ANISOU  713  N   ASP A  87     4380   4176   4283      7     90   -180       N  
ATOM    714  CA  ASP A  87     -21.405  -5.152  35.929  1.00 34.15           C  
ANISOU  714  CA  ASP A  87     4437   4229   4310      9     94   -173       C  
ATOM    715  C   ASP A  87     -22.828  -4.599  35.844  1.00 32.68           C  
ANISOU  715  C   ASP A  87     4236   4062   4119     -1    122   -180       C  
ATOM    716  O   ASP A  87     -23.194  -3.903  34.889  1.00 33.14           O  
ANISOU  716  O   ASP A  87     4267   4140   4186      7    123   -191       O  
ATOM    717  CB  ASP A  87     -20.338  -4.106  35.544  1.00 34.48           C  
ANISOU  717  CB  ASP A  87     4464   4278   4357     28     79   -176       C  
ATOM    718  CG  ASP A  87     -20.326  -2.887  36.487  1.00 38.58           C  
ANISOU  718  CG  ASP A  87     4998   4803   4859     32     79   -169       C  
ATOM    719  OD1 ASP A  87     -21.267  -2.733  37.296  1.00 41.08           O  
ANISOU  719  OD1 ASP A  87     5330   5121   5157     20     97   -165       O  
ATOM    720  OD2 ASP A  87     -19.376  -2.071  36.412  1.00 38.28           O  
ANISOU  720  OD2 ASP A  87     4953   4765   4826     45     65   -172       O  
ATOM    721  N   PHE A  88     -23.622  -4.930  36.855  1.00 31.47           N  
ANISOU  721  N   PHE A  88     4105   3900   3953    -20    143   -176       N  
ATOM    722  CA  PHE A  88     -25.067  -4.770  36.791  1.00 32.35           C  
ANISOU  722  CA  PHE A  88     4194   4023   4073    -34    174   -191       C  
ATOM    723  C   PHE A  88     -25.528  -3.326  36.726  1.00 34.63           C  
ANISOU  723  C   PHE A  88     4461   4332   4364    -24    180   -202       C  
ATOM    724  O   PHE A  88     -26.546  -3.037  36.100  1.00 38.08           O  
ANISOU  724  O   PHE A  88     4864   4781   4822    -24    188   -221       O  
ATOM    725  CB  PHE A  88     -25.750  -5.519  37.936  1.00 31.86           C  
ANISOU  725  CB  PHE A  88     4164   3942   3998    -63    206   -187       C  
ATOM    726  CG  PHE A  88     -25.463  -6.990  37.942  1.00 33.99           C  
ANISOU  726  CG  PHE A  88     4458   4188   4269    -75    199   -177       C  
ATOM    727  CD1 PHE A  88     -25.658  -7.756  36.790  1.00 34.92           C  
ANISOU  727  CD1 PHE A  88     4545   4310   4415    -72    190   -187       C  
ATOM    728  CD2 PHE A  88     -25.005  -7.615  39.097  1.00 33.24           C  
ANISOU  728  CD2 PHE A  88     4422   4063   4145    -89    197   -158       C  
ATOM    729  CE1 PHE A  88     -25.396  -9.117  36.791  1.00 37.31           C  
ANISOU  729  CE1 PHE A  88     4868   4588   4720    -82    183   -179       C  
ATOM    730  CE2 PHE A  88     -24.741  -8.976  39.113  1.00 35.98           C  
ANISOU  730  CE2 PHE A  88     4795   4384   4494    -99    186   -148       C  
ATOM    731  CZ  PHE A  88     -24.928  -9.731  37.958  1.00 37.42           C  
ANISOU  731  CZ  PHE A  88     4939   4571   4708    -95    179   -159       C  
ATOM    732  N   LYS A  89     -24.777  -2.420  37.339  1.00 33.46           N  
ANISOU  732  N   LYS A  89     4332   4186   4198    -13    170   -192       N  
ATOM    733  CA  LYS A  89     -25.117  -1.007  37.241  1.00 36.59           C  
ANISOU  733  CA  LYS A  89     4708   4598   4596     -2    170   -202       C  
ATOM    734  C   LYS A  89     -24.986  -0.437  35.820  1.00 34.70           C  
ANISOU  734  C   LYS A  89     4440   4373   4373     17    147   -209       C  
ATOM    735  O   LYS A  89     -25.690   0.504  35.473  1.00 34.74           O  
ANISOU  735  O   LYS A  89     4424   4388   4387     24    145   -223       O  
ATOM    736  CB  LYS A  89     -24.382  -0.155  38.291  1.00 36.19           C  
ANISOU  736  CB  LYS A  89     4686   4544   4521      4    165   -190       C  
ATOM    737  CG  LYS A  89     -22.902   0.008  38.124  1.00 37.09           C  
ANISOU  737  CG  LYS A  89     4811   4651   4630     21    133   -177       C  
ATOM    738  CD  LYS A  89     -22.326   0.524  39.436  1.00 41.15           C  
ANISOU  738  CD  LYS A  89     5362   5154   5121     22    126   -167       C  
ATOM    739  CE  LYS A  89     -20.830   0.318  39.528  1.00 40.23           C  
ANISOU  739  CE  LYS A  89     5259   5020   5006     35     91   -157       C  
ATOM    740  NZ  LYS A  89     -20.479  -1.093  39.789  1.00 38.94           N  
ANISOU  740  NZ  LYS A  89     5120   4833   4842     28     79   -149       N  
ATOM    741  N   LEU A  90     -24.113  -1.025  35.003  1.00 34.39           N  
ANISOU  741  N   LEU A  90     4403   4329   4335     22    130   -202       N  
ATOM    742  CA  LEU A  90     -23.994  -0.623  33.605  1.00 33.44           C  
ANISOU  742  CA  LEU A  90     4267   4216   4221     34    114   -209       C  
ATOM    743  C   LEU A  90     -25.196  -1.096  32.788  1.00 32.89           C  
ANISOU  743  C   LEU A  90     4178   4151   4169     30    113   -226       C  
ATOM    744  O   LEU A  90     -25.669  -0.387  31.904  1.00 34.41           O  
ANISOU  744  O   LEU A  90     4360   4348   4366     40     98   -237       O  
ATOM    745  CB  LEU A  90     -22.692  -1.146  32.988  1.00 35.01           C  
ANISOU  745  CB  LEU A  90     4475   4409   4420     38    104   -203       C  
ATOM    746  CG  LEU A  90     -21.354  -0.601  33.497  1.00 35.80           C  
ANISOU  746  CG  LEU A  90     4586   4502   4514     45     97   -194       C  
ATOM    747  CD1 LEU A  90     -20.218  -1.173  32.665  1.00 35.18           C  
ANISOU  747  CD1 LEU A  90     4504   4415   4446     46     92   -199       C  
ATOM    748  CD2 LEU A  90     -21.309   0.930  33.493  1.00 37.94           C  
ANISOU  748  CD2 LEU A  90     4857   4782   4777     53     94   -194       C  
ATOM    749  N   ALA A  91     -25.684  -2.296  33.093  1.00 31.31           N  
ANISOU  749  N   ALA A  91     3975   3943   3980     16    127   -229       N  
ATOM    750  CA  ALA A  91     -26.883  -2.829  32.453  1.00 30.11           C  
ANISOU  750  CA  ALA A  91     3798   3791   3851     10    127   -249       C  
ATOM    751  C   ALA A  91     -28.127  -2.046  32.873  1.00 29.65           C  
ANISOU  751  C   ALA A  91     3716   3738   3813      9    137   -269       C  
ATOM    752  O   ALA A  91     -29.041  -1.845  32.069  1.00 29.03           O  
ANISOU  752  O   ALA A  91     3612   3659   3758     16    119   -291       O  
ATOM    753  CB  ALA A  91     -27.045  -4.313  32.768  1.00 28.79           C  
ANISOU  753  CB  ALA A  91     3635   3611   3692     -8    143   -248       C  
ATOM    754  N   TYR A  92     -28.152  -1.602  34.130  1.00 30.95           N  
ANISOU  754  N   TYR A  92     3889   3903   3968      1    161   -264       N  
ATOM    755  CA  TYR A  92     -29.232  -0.754  34.631  1.00 32.75           C  
ANISOU  755  CA  TYR A  92     4092   4134   4216      0    175   -287       C  
ATOM    756  C   TYR A  92     -29.296   0.565  33.870  1.00 32.66           C  
ANISOU  756  C   TYR A  92     4068   4130   4210     25    141   -295       C  
ATOM    757  O   TYR A  92     -30.365   0.972  33.406  1.00 34.29           O  
ANISOU  757  O   TYR A  92     4242   4335   4451     32    128   -323       O  
ATOM    758  CB  TYR A  92     -29.070  -0.468  36.126  1.00 33.62           C  
ANISOU  758  CB  TYR A  92     4225   4242   4306    -14    209   -279       C  
ATOM    759  CG  TYR A  92     -30.052   0.571  36.636  1.00 35.79           C  
ANISOU  759  CG  TYR A  92     4474   4522   4602    -14    227   -306       C  
ATOM    760  CD1 TYR A  92     -29.651   1.884  36.873  1.00 34.11           C  
ANISOU  760  CD1 TYR A  92     4268   4317   4377      4    212   -302       C  
ATOM    761  CD2 TYR A  92     -31.389   0.241  36.862  1.00 37.85           C  
ANISOU  761  CD2 TYR A  92     4700   4778   4903    -31    258   -340       C  
ATOM    762  CE1 TYR A  92     -30.555   2.836  37.342  1.00 38.11           C  
ANISOU  762  CE1 TYR A  92     4747   4825   4907      6    227   -331       C  
ATOM    763  CE2 TYR A  92     -32.300   1.187  37.322  1.00 36.78           C  
ANISOU  763  CE2 TYR A  92     4533   4644   4796    -30    276   -373       C  
ATOM    764  CZ  TYR A  92     -31.878   2.478  37.559  1.00 39.35           C  
ANISOU  764  CZ  TYR A  92     4867   4977   5106    -11    259   -368       C  
ATOM    765  OH  TYR A  92     -32.784   3.407  38.015  1.00 40.62           O  
ANISOU  765  OH  TYR A  92     4995   5138   5299     -9    275   -403       O  
ATOM    766  N   LEU A  93     -28.152   1.229  33.755  1.00 31.85           N  
ANISOU  766  N   LEU A  93     3992   4031   4078     37    125   -273       N  
ATOM    767  CA  LEU A  93     -28.075   2.506  33.054  1.00 32.46           C  
ANISOU  767  CA  LEU A  93     4069   4111   4153     57     93   -276       C  
ATOM    768  C   LEU A  93     -28.499   2.362  31.593  1.00 33.25           C  
ANISOU  768  C   LEU A  93     4163   4206   4264     68     59   -287       C  
ATOM    769  O   LEU A  93     -29.125   3.262  31.025  1.00 31.65           O  
ANISOU  769  O   LEU A  93     3952   3998   4074     83     29   -302       O  
ATOM    770  CB  LEU A  93     -26.664   3.096  33.143  1.00 29.46           C  
ANISOU  770  CB  LEU A  93     3719   3733   3741     63     88   -250       C  
ATOM    771  CG  LEU A  93     -26.249   3.823  34.423  1.00 29.18           C  
ANISOU  771  CG  LEU A  93     3694   3700   3693     63    104   -242       C  
ATOM    772  CD1 LEU A  93     -24.885   4.448  34.232  1.00 24.62           C  
ANISOU  772  CD1 LEU A  93     3139   3122   3095     71     91   -223       C  
ATOM    773  CD2 LEU A  93     -27.253   4.895  34.844  1.00 24.86           C  
ANISOU  773  CD2 LEU A  93     3127   3156   3164     70    104   -263       C  
ATOM    774  N   SER A  94     -28.166   1.216  31.008  1.00 34.12           N  
ANISOU  774  N   SER A  94     4281   4313   4369     60     60   -281       N  
ATOM    775  CA  SER A  94     -28.475   0.934  29.613  1.00 35.67           C  
ANISOU  775  CA  SER A  94     4482   4502   4569     67     28   -290       C  
ATOM    776  C   SER A  94     -29.976   0.676  29.402  1.00 36.48           C  
ANISOU  776  C   SER A  94     4549   4599   4715     69     13   -323       C  
ATOM    777  O   SER A  94     -30.545   1.091  28.394  1.00 35.91           O  
ANISOU  777  O   SER A  94     4476   4516   4651     84    -29   -338       O  
ATOM    778  CB  SER A  94     -27.646  -0.258  29.134  1.00 35.30           C  
ANISOU  778  CB  SER A  94     4452   4454   4506     57     38   -278       C  
ATOM    779  OG  SER A  94     -27.828  -0.465  27.750  1.00 36.64           O  
ANISOU  779  OG  SER A  94     4635   4615   4670     63      9   -286       O  
ATOM    780  N   ASP A  95     -30.604  -0.007  30.358  1.00 35.11           N  
ANISOU  780  N   ASP A  95     4345   4426   4567     53     47   -335       N  
ATOM    781  CA  ASP A  95     -32.048  -0.225  30.340  1.00 34.73           C  
ANISOU  781  CA  ASP A  95     4252   4370   4572     51     43   -372       C  
ATOM    782  C   ASP A  95     -32.833   1.042  30.640  1.00 36.27           C  
ANISOU  782  C   ASP A  95     4421   4563   4795     65     29   -397       C  
ATOM    783  O   ASP A  95     -33.878   1.292  30.026  1.00 35.07           O  
ANISOU  783  O   ASP A  95     4238   4399   4688     79     -7   -431       O  
ATOM    784  CB  ASP A  95     -32.436  -1.304  31.349  1.00 33.93           C  
ANISOU  784  CB  ASP A  95     4133   4269   4489     23     95   -378       C  
ATOM    785  CG  ASP A  95     -32.090  -2.691  30.867  1.00 31.11           C  
ANISOU  785  CG  ASP A  95     3789   3907   4124     11     98   -367       C  
ATOM    786  OD1 ASP A  95     -31.692  -3.532  31.698  1.00 29.03           O  
ANISOU  786  OD1 ASP A  95     3540   3643   3847    -10    136   -351       O  
ATOM    787  OD2 ASP A  95     -32.213  -2.934  29.653  1.00 29.68           O  
ANISOU  787  OD2 ASP A  95     3608   3721   3949     24     59   -375       O  
ATOM    788  N   THR A  96     -32.325   1.837  31.583  1.00 35.04           N  
ANISOU  788  N   THR A  96     4278   4416   4619     64     53   -382       N  
ATOM    789  CA  THR A  96     -33.037   3.025  32.051  1.00 33.47           C  
ANISOU  789  CA  THR A  96     4053   4215   4449     76     48   -408       C  
ATOM    790  C   THR A  96     -32.931   4.212  31.087  1.00 33.39           C  
ANISOU  790  C   THR A  96     4058   4197   4432    105    -13   -407       C  
ATOM    791  O   THR A  96     -33.853   5.024  31.000  1.00 34.41           O  
ANISOU  791  O   THR A  96     4156   4315   4602    122    -41   -440       O  
ATOM    792  CB  THR A  96     -32.588   3.412  33.474  1.00 32.88           C  
ANISOU  792  CB  THR A  96     3989   4151   4353     62     97   -395       C  
ATOM    793  OG1 THR A  96     -32.568   2.231  34.289  1.00 31.93           O  
ANISOU  793  OG1 THR A  96     3873   4033   4227     33    149   -390       O  
ATOM    794  CG2 THR A  96     -33.551   4.427  34.094  1.00 31.11           C  
ANISOU  794  CG2 THR A  96     3728   3924   4170     69    104   -432       C  
ATOM    795  N   TYR A  97     -31.821   4.290  30.362  1.00 32.34           N  
ANISOU  795  N   TYR A  97     3974   4066   4250    110    -33   -373       N  
ATOM    796  CA  TYR A  97     -31.564   5.383  29.420  1.00 34.51           C  
ANISOU  796  CA  TYR A  97     4279   4328   4504    132    -85   -366       C  
ATOM    797  C   TYR A  97     -31.263   4.779  28.050  1.00 37.19           C  
ANISOU  797  C   TYR A  97     4654   4658   4820    134   -116   -356       C  
ATOM    798  O   TYR A  97     -30.129   4.806  27.565  1.00 34.62           O  
ANISOU  798  O   TYR A  97     4374   4334   4446    129   -111   -326       O  
ATOM    799  CB  TYR A  97     -30.426   6.301  29.927  1.00 32.72           C  
ANISOU  799  CB  TYR A  97     4085   4110   4238    132    -69   -336       C  
ATOM    800  CG  TYR A  97     -30.720   6.855  31.305  1.00 33.05           C  
ANISOU  800  CG  TYR A  97     4098   4159   4298    129    -37   -347       C  
ATOM    801  CD1 TYR A  97     -30.255   6.211  32.450  1.00 33.83           C  
ANISOU  801  CD1 TYR A  97     4194   4273   4386    109     16   -335       C  
ATOM    802  CD2 TYR A  97     -31.509   7.994  31.467  1.00 33.47           C  
ANISOU  802  CD2 TYR A  97     4130   4203   4383    147    -62   -372       C  
ATOM    803  CE1 TYR A  97     -30.560   6.695  33.722  1.00 34.22           C  
ANISOU  803  CE1 TYR A  97     4227   4328   4448    104     48   -347       C  
ATOM    804  CE2 TYR A  97     -31.811   8.492  32.733  1.00 33.21           C  
ANISOU  804  CE2 TYR A  97     4071   4178   4368    143    -28   -387       C  
ATOM    805  CZ  TYR A  97     -31.338   7.834  33.855  1.00 35.51           C  
ANISOU  805  CZ  TYR A  97     4367   4485   4642    120     29   -374       C  
ATOM    806  OH  TYR A  97     -31.626   8.321  35.107  1.00 34.42           O  
ANISOU  806  OH  TYR A  97     4213   4352   4514    114     65   -389       O  
ATOM    807  N   ASN A  98     -32.303   4.208  27.449  1.00 39.11           N  
ANISOU  807  N   ASN A  98     4873   4889   5100    140   -146   -384       N  
ATOM    808  CA  ASN A  98     -32.189   3.541  26.169  1.00 44.21           C  
ANISOU  808  CA  ASN A  98     5551   5522   5725    141   -178   -381       C  
ATOM    809  C   ASN A  98     -32.284   4.554  25.023  1.00 45.50           C  
ANISOU  809  C   ASN A  98     5761   5661   5866    162   -245   -381       C  
ATOM    810  O   ASN A  98     -33.073   4.389  24.091  1.00 48.92           O  
ANISOU  810  O   ASN A  98     6200   6072   6317    176   -301   -403       O  
ATOM    811  CB  ASN A  98     -33.251   2.433  26.050  1.00 46.15           C  
ANISOU  811  CB  ASN A  98     5752   5763   6021    137   -184   -413       C  
ATOM    812  CG  ASN A  98     -32.940   1.435  24.940  1.00 53.97           C  
ANISOU  812  CG  ASN A  98     6774   6746   6985    132   -200   -406       C  
ATOM    813  OD1 ASN A  98     -31.895   1.520  24.277  1.00 57.99           O  
ANISOU  813  OD1 ASN A  98     7340   7255   7438    129   -201   -378       O  
ATOM    814  ND2 ASN A  98     -33.850   0.478  24.731  1.00 55.84           N  
ANISOU  814  ND2 ASN A  98     6975   6975   7267    130   -211   -434       N  
ATOM    815  N   TYR A  99     -31.464   5.599  25.119  1.00 43.45           N  
ANISOU  815  N   TYR A  99     5539   5401   5568    164   -241   -357       N  
ATOM    816  CA  TYR A  99     -31.437   6.709  24.172  1.00 42.48           C  
ANISOU  816  CA  TYR A  99     5472   5252   5417    180   -298   -351       C  
ATOM    817  C   TYR A  99     -30.136   7.485  24.379  1.00 42.61           C  
ANISOU  817  C   TYR A  99     5531   5276   5382    169   -265   -317       C  
ATOM    818  O   TYR A  99     -29.471   7.310  25.405  1.00 42.31           O  
ANISOU  818  O   TYR A  99     5467   5262   5345    156   -209   -304       O  
ATOM    819  CB  TYR A  99     -32.654   7.633  24.367  1.00 42.70           C  
ANISOU  819  CB  TYR A  99     5468   5261   5497    207   -353   -384       C  
ATOM    820  CG  TYR A  99     -32.914   8.113  25.803  1.00 42.19           C  
ANISOU  820  CG  TYR A  99     5342   5214   5473    207   -315   -396       C  
ATOM    821  CD1 TYR A  99     -33.827   7.448  26.628  1.00 41.84           C  
ANISOU  821  CD1 TYR A  99     5224   5181   5491    203   -288   -430       C  
ATOM    822  CD2 TYR A  99     -32.268   9.245  26.320  1.00 42.90           C  
ANISOU  822  CD2 TYR A  99     5452   5307   5540    209   -303   -377       C  
ATOM    823  CE1 TYR A  99     -34.082   7.885  27.938  1.00 42.33           C  
ANISOU  823  CE1 TYR A  99     5240   5258   5586    200   -247   -443       C  
ATOM    824  CE2 TYR A  99     -32.515   9.696  27.623  1.00 40.77           C  
ANISOU  824  CE2 TYR A  99     5132   5052   5305    210   -268   -390       C  
ATOM    825  CZ  TYR A  99     -33.423   9.008  28.427  1.00 45.92           C  
ANISOU  825  CZ  TYR A  99     5718   5717   6014    204   -239   -424       C  
ATOM    826  OH  TYR A  99     -33.679   9.439  29.713  1.00 44.95           O  
ANISOU  826  OH  TYR A  99     5553   5606   5919    201   -199   -439       O  
ATOM    827  N   GLU A 100     -29.764   8.315  23.403  1.00 41.99           N  
ANISOU  827  N   GLU A 100     5523   5173   5260    173   -301   -303       N  
ATOM    828  CA  GLU A 100     -28.606   9.199  23.534  1.00 43.93           C  
ANISOU  828  CA  GLU A 100     5809   5420   5464    161   -272   -274       C  
ATOM    829  C   GLU A 100     -28.879  10.217  24.639  1.00 44.31           C  
ANISOU  829  C   GLU A 100     5818   5473   5543    174   -273   -279       C  
ATOM    830  O   GLU A 100     -29.879  10.949  24.587  1.00 47.09           O  
ANISOU  830  O   GLU A 100     6161   5807   5926    197   -327   -300       O  
ATOM    831  CB  GLU A 100     -28.321   9.922  22.216  1.00 45.30           C  
ANISOU  831  CB  GLU A 100     6071   5558   5582    160   -313   -261       C  
ATOM    832  CG  GLU A 100     -27.015  10.727  22.196  1.00 52.44           C  
ANISOU  832  CG  GLU A 100     7023   6460   6441    140   -273   -233       C  
ATOM    833  CD  GLU A 100     -26.790  11.487  20.883  1.00 60.10           C  
ANISOU  833  CD  GLU A 100     8094   7390   7351    133   -309   -219       C  
ATOM    834  OE1 GLU A 100     -25.612  11.709  20.522  1.00 61.35           O  
ANISOU  834  OE1 GLU A 100     8301   7545   7464    106   -262   -199       O  
ATOM    835  OE2 GLU A 100     -27.781  11.862  20.211  1.00 62.86           O  
ANISOU  835  OE2 GLU A 100     8476   7708   7701    154   -384   -231       O  
ATOM    836  N   ILE A 101     -28.001  10.256  25.637  1.00 41.00           N  
ANISOU  836  N   ILE A 101     5377   5078   5121    161   -216   -264       N  
ATOM    837  CA  ILE A 101     -28.199  11.131  26.792  1.00 40.84           C  
ANISOU  837  CA  ILE A 101     5322   5067   5129    171   -209   -270       C  
ATOM    838  C   ILE A 101     -27.906  12.582  26.458  1.00 42.63           C  
ANISOU  838  C   ILE A 101     5593   5270   5333    179   -240   -259       C  
ATOM    839  O   ILE A 101     -26.815  12.920  25.999  1.00 44.92           O  
ANISOU  839  O   ILE A 101     5934   5554   5580    163   -222   -234       O  
ATOM    840  CB  ILE A 101     -27.357  10.678  28.011  1.00 38.31           C  
ANISOU  840  CB  ILE A 101     4970   4775   4810    155   -146   -259       C  
ATOM    841  CG1 ILE A 101     -27.937   9.390  28.590  1.00 37.08           C  
ANISOU  841  CG1 ILE A 101     4767   4638   4686    149   -121   -274       C  
ATOM    842  CG2 ILE A 101     -27.304  11.771  29.091  1.00 36.84           C  
ANISOU  842  CG2 ILE A 101     4767   4594   4639    163   -139   -260       C  
ATOM    843  CD1 ILE A 101     -26.965   8.604  29.423  1.00 38.49           C  
ANISOU  843  CD1 ILE A 101     4935   4837   4853    131    -67   -258       C  
ATOM    844  N   LYS A 102     -28.904  13.428  26.682  1.00 45.25           N  
ANISOU  844  N   LYS A 102     5906   5586   5699    203   -286   -281       N  
ATOM    845  CA  LYS A 102     -28.731  14.866  26.636  1.00 47.84           C  
ANISOU  845  CA  LYS A 102     6268   5892   6016    213   -316   -273       C  
ATOM    846  C   LYS A 102     -28.701  15.350  28.076  1.00 47.18           C  
ANISOU  846  C   LYS A 102     6132   5830   5964    217   -283   -282       C  
ATOM    847  O   LYS A 102     -29.687  15.214  28.808  1.00 47.45           O  
ANISOU  847  O   LYS A 102     6108   5873   6049    230   -285   -313       O  
ATOM    848  CB  LYS A 102     -29.884  15.527  25.868  1.00 52.35           C  
ANISOU  848  CB  LYS A 102     6856   6425   6608    240   -400   -296       C  
ATOM    849  CG  LYS A 102     -29.549  16.905  25.276  1.00 59.45           C  
ANISOU  849  CG  LYS A 102     7826   7288   7473    247   -443   -279       C  
ATOM    850  CD  LYS A 102     -28.519  16.788  24.136  1.00 66.88           C  
ANISOU  850  CD  LYS A 102     8856   8214   8341    221   -432   -244       C  
ATOM    851  CE  LYS A 102     -28.135  18.155  23.566  1.00 71.08           C  
ANISOU  851  CE  LYS A 102     9467   8706   8834    220   -467   -225       C  
ATOM    852  NZ  LYS A 102     -26.943  18.080  22.663  1.00 71.16           N  
ANISOU  852  NZ  LYS A 102     9560   8705   8773    185   -430   -192       N  
ATOM    853  N   TYR A 103     -27.560  15.887  28.498  1.00 45.53           N  
ANISOU  853  N   TYR A 103     5944   5628   5726    203   -248   -257       N  
ATOM    854  CA  TYR A 103     -27.412  16.309  29.882  1.00 42.06           C  
ANISOU  854  CA  TYR A 103     5463   5207   5309    205   -217   -264       C  
ATOM    855  C   TYR A 103     -27.380  17.820  29.989  1.00 41.09           C  
ANISOU  855  C   TYR A 103     5362   5064   5187    219   -248   -263       C  
ATOM    856  O   TYR A 103     -27.038  18.511  29.031  1.00 41.63           O  
ANISOU  856  O   TYR A 103     5488   5105   5226    218   -280   -247       O  
ATOM    857  CB  TYR A 103     -26.201  15.633  30.559  1.00 39.21           C  
ANISOU  857  CB  TYR A 103     5098   4873   4927    182   -156   -243       C  
ATOM    858  CG  TYR A 103     -24.829  16.130  30.135  1.00 36.76           C  
ANISOU  858  CG  TYR A 103     4833   4553   4579    166   -141   -215       C  
ATOM    859  CD1 TYR A 103     -24.125  15.530  29.076  1.00 33.67           C  
ANISOU  859  CD1 TYR A 103     4480   4156   4157    147   -129   -199       C  
ATOM    860  CD2 TYR A 103     -24.222  17.185  30.813  1.00 31.60           C  
ANISOU  860  CD2 TYR A 103     4184   3897   3926    167   -134   -209       C  
ATOM    861  CE1 TYR A 103     -22.842  15.994  28.698  1.00 32.15           C  
ANISOU  861  CE1 TYR A 103     4327   3954   3937    128   -105   -180       C  
ATOM    862  CE2 TYR A 103     -22.970  17.656  30.448  1.00 32.90           C  
ANISOU  862  CE2 TYR A 103     4385   4051   4063    149   -116   -188       C  
ATOM    863  CZ  TYR A 103     -22.278  17.063  29.402  1.00 33.65           C  
ANISOU  863  CZ  TYR A 103     4515   4139   4131    128    -99   -175       C  
ATOM    864  OH  TYR A 103     -21.033  17.564  29.090  1.00 32.43           O  
ANISOU  864  OH  TYR A 103     4392   3973   3958    107    -73   -161       O  
ATOM    865  N   ASP A 104     -27.786  18.327  31.149  1.00 38.28           N  
ANISOU  865  N   ASP A 104     4962   4717   4864    230   -239   -283       N  
ATOM    866  CA  ASP A 104     -27.748  19.752  31.417  1.00 36.10           C  
ANISOU  866  CA  ASP A 104     4699   4423   4594    244   -265   -285       C  
ATOM    867  C   ASP A 104     -26.822  19.992  32.589  1.00 34.54           C  
ANISOU  867  C   ASP A 104     4490   4246   4387    232   -217   -274       C  
ATOM    868  O   ASP A 104     -27.215  19.797  33.738  1.00 36.68           O  
ANISOU  868  O   ASP A 104     4716   4536   4683    235   -189   -294       O  
ATOM    869  CB  ASP A 104     -29.151  20.284  31.722  1.00 36.39           C  
ANISOU  869  CB  ASP A 104     4694   4447   4686    272   -305   -327       C  
ATOM    870  CG  ASP A 104     -29.167  21.784  31.986  1.00 40.97           C  
ANISOU  870  CG  ASP A 104     5287   5004   5277    289   -338   -333       C  
ATOM    871  OD1 ASP A 104     -28.090  22.418  32.038  1.00 40.82           O  
ANISOU  871  OD1 ASP A 104     5306   4981   5221    277   -325   -303       O  
ATOM    872  OD2 ASP A 104     -30.272  22.340  32.136  1.00 46.45           O  
ANISOU  872  OD2 ASP A 104     5948   5681   6020    314   -378   -370       O  
ATOM    873  N   HIS A 105     -25.600  20.431  32.298  1.00 34.39           N  
ANISOU  873  N   HIS A 105     4514   4220   4334    217   -206   -245       N  
ATOM    874  CA  HIS A 105     -24.575  20.619  33.325  1.00 35.31           C  
ANISOU  874  CA  HIS A 105     4621   4352   4442    205   -166   -234       C  
ATOM    875  C   HIS A 105     -25.002  21.545  34.468  1.00 34.99           C  
ANISOU  875  C   HIS A 105     4554   4312   4427    222   -172   -255       C  
ATOM    876  O   HIS A 105     -24.493  21.425  35.578  1.00 33.91           O  
ANISOU  876  O   HIS A 105     4401   4194   4291    216   -139   -255       O  
ATOM    877  CB  HIS A 105     -23.251  21.094  32.709  1.00 35.70           C  
ANISOU  877  CB  HIS A 105     4717   4386   4460    187   -158   -207       C  
ATOM    878  CG  HIS A 105     -23.276  22.506  32.214  1.00 38.25           C  
ANISOU  878  CG  HIS A 105     5078   4676   4778    194   -195   -202       C  
ATOM    879  ND1 HIS A 105     -22.880  23.575  32.993  1.00 41.38           N  
ANISOU  879  ND1 HIS A 105     5471   5067   5184    199   -196   -204       N  
ATOM    880  CD2 HIS A 105     -23.631  23.026  31.014  1.00 40.39           C  
ANISOU  880  CD2 HIS A 105     5399   4916   5033    196   -236   -195       C  
ATOM    881  CE1 HIS A 105     -22.997  24.693  32.295  1.00 44.09           C  
ANISOU  881  CE1 HIS A 105     5856   5376   5519    203   -234   -198       C  
ATOM    882  NE2 HIS A 105     -23.453  24.388  31.091  1.00 42.81           N  
ANISOU  882  NE2 HIS A 105     5731   5196   5339    202   -261   -191       N  
ATOM    883  N   THR A 106     -25.945  22.449  34.197  1.00 36.72           N  
ANISOU  883  N   THR A 106     4615   4850   4488    240   -384    -99       N  
ATOM    884  CA  THR A 106     -26.395  23.429  35.198  1.00 36.54           C  
ANISOU  884  CA  THR A 106     4545   4827   4513    290   -365    -97       C  
ATOM    885  C   THR A 106     -27.256  22.781  36.278  1.00 35.64           C  
ANISOU  885  C   THR A 106     4341   4744   4456    278   -331   -121       C  
ATOM    886  O   THR A 106     -27.528  23.391  37.310  1.00 34.65           O  
ANISOU  886  O   THR A 106     4179   4618   4369    309   -294   -126       O  
ATOM    887  CB  THR A 106     -27.173  24.615  34.562  1.00 37.16           C  
ANISOU  887  CB  THR A 106     4613   4902   4605    347   -432    -80       C  
ATOM    888  OG1 THR A 106     -28.434  24.151  34.052  1.00 38.09           O  
ANISOU  888  OG1 THR A 106     4661   5058   4753    344   -493    -88       O  
ATOM    889  CG2 THR A 106     -26.365  25.254  33.417  1.00 38.02           C  
ANISOU  889  CG2 THR A 106     4820   4976   4649    352   -467    -55       C  
ATOM    890  N   LYS A 107     -27.683  21.545  36.037  1.00 35.71           N  
ANISOU  890  N   LYS A 107     4322   4779   4468    228   -341   -138       N  
ATOM    891  CA  LYS A 107     -28.456  20.804  37.028  1.00 36.28           C  
ANISOU  891  CA  LYS A 107     4316   4880   4587    203   -305   -161       C  
ATOM    892  C   LYS A 107     -27.578  19.872  37.849  1.00 35.24           C  
ANISOU  892  C   LYS A 107     4219   4733   4437    159   -236   -170       C  
ATOM    893  O   LYS A 107     -28.025  19.300  38.845  1.00 36.75           O  
ANISOU  893  O   LYS A 107     4364   4940   4660    135   -193   -187       O  
ATOM    894  CB  LYS A 107     -29.596  20.026  36.365  1.00 38.41           C  
ANISOU  894  CB  LYS A 107     4528   5190   4877    171   -360   -174       C  
ATOM    895  CG  LYS A 107     -30.592  20.896  35.615  1.00 42.36           C  
ANISOU  895  CG  LYS A 107     4981   5711   5404    217   -437   -163       C  
ATOM    896  CD  LYS A 107     -31.195  21.971  36.511  1.00 48.10           C  
ANISOU  896  CD  LYS A 107     5642   6444   6189    280   -414   -164       C  
ATOM    897  CE  LYS A 107     -32.107  22.914  35.723  1.00 56.08           C  
ANISOU  897  CE  LYS A 107     6610   7469   7228    339   -496   -149       C  
ATOM    898  NZ  LYS A 107     -33.195  22.184  35.005  1.00 56.49           N  
ANISOU  898  NZ  LYS A 107     6592   7569   7302    306   -565   -157       N  
ATOM    899  N   ILE A 108     -26.328  19.721  37.427  1.00 34.63           N  
ANISOU  899  N   ILE A 108     4223   4625   4309    148   -225   -158       N  
ATOM    900  CA  ILE A 108     -25.380  18.864  38.128  1.00 33.09           C  
ANISOU  900  CA  ILE A 108     4063   4413   4097    114   -166   -162       C  
ATOM    901  C   ILE A 108     -24.619  19.682  39.169  1.00 33.91           C  
ANISOU  901  C   ILE A 108     4184   4496   4203    142   -119   -152       C  
ATOM    902  O   ILE A 108     -24.103  20.772  38.870  1.00 35.81           O  
ANISOU  902  O   ILE A 108     4458   4720   4428    177   -130   -135       O  
ATOM    903  CB  ILE A 108     -24.419  18.160  37.148  1.00 34.05           C  
ANISOU  903  CB  ILE A 108     4256   4513   4167     88   -175   -158       C  
ATOM    904  CG1 ILE A 108     -25.222  17.344  36.124  1.00 33.39           C  
ANISOU  904  CG1 ILE A 108     4165   4447   4075     54   -224   -171       C  
ATOM    905  CG2 ILE A 108     -23.434  17.278  37.908  1.00 31.97           C  
ANISOU  905  CG2 ILE A 108     4024   4231   3894     63   -117   -160       C  
ATOM    906  CD1 ILE A 108     -24.411  16.740  34.995  1.00 34.16           C  
ANISOU  906  CD1 ILE A 108     4340   4522   4118     31   -235   -170       C  
ATOM    907  N   ARG A 109     -24.579  19.163  40.395  1.00 29.40           N  
ANISOU  907  N   ARG A 109     3595   3926   3650    121    -67   -161       N  
ATOM    908  CA  ARG A 109     -23.927  19.847  41.498  1.00 28.06           C  
ANISOU  908  CA  ARG A 109     3443   3739   3481    138    -23   -153       C  
ATOM    909  C   ARG A 109     -22.460  19.471  41.531  1.00 28.80           C  
ANISOU  909  C   ARG A 109     3598   3807   3537    123     -3   -138       C  
ATOM    910  O   ARG A 109     -22.107  18.341  41.899  1.00 28.41           O  
ANISOU  910  O   ARG A 109     3560   3753   3482     89     20   -143       O  
ATOM    911  CB  ARG A 109     -24.603  19.499  42.838  1.00 29.00           C  
ANISOU  911  CB  ARG A 109     3518   3869   3631    121     22   -169       C  
ATOM    912  CG  ARG A 109     -24.251  20.449  43.981  1.00 28.79           C  
ANISOU  912  CG  ARG A 109     3505   3826   3606    142     62   -164       C  
ATOM    913  CD  ARG A 109     -25.030  20.129  45.256  1.00 25.91           C  
ANISOU  913  CD  ARG A 109     3102   3474   3269    122    111   -183       C  
ATOM    914  NE  ARG A 109     -26.464  20.296  45.049  1.00 29.92           N  
ANISOU  914  NE  ARG A 109     3534   4012   3821    137    100   -202       N  
ATOM    915  CZ  ARG A 109     -27.114  21.449  45.199  1.00 30.63           C  
ANISOU  915  CZ  ARG A 109     3591   4106   3940    185    102   -207       C  
ATOM    916  NH1 ARG A 109     -26.462  22.540  45.584  1.00 26.80           N  
ANISOU  916  NH1 ARG A 109     3152   3592   3439    218    116   -196       N  
ATOM    917  NH2 ARG A 109     -28.421  21.505  44.972  1.00 29.56           N  
ANISOU  917  NH2 ARG A 109     3377   4004   3852    200     89   -224       N  
ATOM    918  N   VAL A 110     -21.615  20.418  41.129  1.00 27.30           N  
ANISOU  918  N   VAL A 110     3449   3601   3325    147    -12   -121       N  
ATOM    919  CA  VAL A 110     -20.177  20.218  41.141  1.00 27.75           C  
ANISOU  919  CA  VAL A 110     3554   3639   3352    136      8   -107       C  
ATOM    920  C   VAL A 110     -19.633  20.920  42.375  1.00 30.02           C  
ANISOU  920  C   VAL A 110     3851   3915   3642    142     40    -98       C  
ATOM    921  O   VAL A 110     -19.847  22.121  42.573  1.00 29.44           O  
ANISOU  921  O   VAL A 110     3780   3835   3572    167     37    -94       O  
ATOM    922  CB  VAL A 110     -19.484  20.713  39.835  1.00 26.79           C  
ANISOU  922  CB  VAL A 110     3475   3507   3197    147    -18    -94       C  
ATOM    923  CG1 VAL A 110     -17.984  20.410  39.868  1.00 27.02           C  
ANISOU  923  CG1 VAL A 110     3542   3522   3202    133      9    -81       C  
ATOM    924  CG2 VAL A 110     -20.089  20.034  38.621  1.00 28.98           C  
ANISOU  924  CG2 VAL A 110     3752   3793   3464    137    -53   -104       C  
ATOM    925  N   ALA A 111     -18.963  20.146  43.222  1.00 29.57           N  
ANISOU  925  N   ALA A 111     3802   3851   3581    117     70    -95       N  
ATOM    926  CA  ALA A 111     -18.429  20.663  44.464  1.00 29.96           C  
ANISOU  926  CA  ALA A 111     3865   3891   3628    113     96    -86       C  
ATOM    927  C   ALA A 111     -16.915  20.647  44.417  1.00 28.60           C  
ANISOU  927  C   ALA A 111     3727   3708   3434    106    100    -66       C  
ATOM    928  O   ALA A 111     -16.300  19.665  43.999  1.00 26.34           O  
ANISOU  928  O   ALA A 111     3446   3420   3141     95    100    -62       O  
ATOM    929  CB  ALA A 111     -18.934  19.870  45.643  1.00 28.89           C  
ANISOU  929  CB  ALA A 111     3712   3757   3506     90    124    -96       C  
ATOM    930  N   ASN A 112     -16.340  21.756  44.861  1.00 29.18           N  
ANISOU  930  N   ASN A 112     3821   3772   3495    111    105    -54       N  
ATOM    931  CA  ASN A 112     -14.914  22.001  44.818  1.00 29.75           C  
ANISOU  931  CA  ASN A 112     3918   3838   3548    101    106    -34       C  
ATOM    932  C   ASN A 112     -14.518  22.463  46.202  1.00 28.36           C  
ANISOU  932  C   ASN A 112     3754   3654   3366     85    120    -26       C  
ATOM    933  O   ASN A 112     -14.924  23.543  46.629  1.00 27.34           O  
ANISOU  933  O   ASN A 112     3640   3516   3233     91    125    -30       O  
ATOM    934  CB  ASN A 112     -14.655  23.118  43.801  1.00 31.75           C  
ANISOU  934  CB  ASN A 112     4193   4086   3785    115     91    -27       C  
ATOM    935  CG  ASN A 112     -13.249  23.121  43.272  1.00 39.90           C  
ANISOU  935  CG  ASN A 112     5241   5119   4799    102     93    -11       C  
ATOM    936  OD1 ASN A 112     -12.275  23.349  44.013  1.00 42.94           O  
ANISOU  936  OD1 ASN A 112     5633   5505   5179     85    103      3       O  
ATOM    937  ND2 ASN A 112     -13.124  22.901  41.967  1.00 40.81           N  
ANISOU  937  ND2 ASN A 112     5364   5238   4904    109     86    -13       N  
ATOM    938  N   PHE A 113     -13.765  21.644  46.928  1.00 30.68           N  
ANISOU  938  N   PHE A 113     4049   3949   3659     65    127    -15       N  
ATOM    939  CA  PHE A 113     -13.372  22.028  48.285  1.00 32.06           C  
ANISOU  939  CA  PHE A 113     4243   4116   3822     43    134     -6       C  
ATOM    940  C   PHE A 113     -11.911  21.792  48.640  1.00 33.62           C  
ANISOU  940  C   PHE A 113     4448   4317   4011     25    124     19       C  
ATOM    941  O   PHE A 113     -11.223  20.988  48.012  1.00 33.45           O  
ANISOU  941  O   PHE A 113     4408   4302   3998     31    118     28       O  
ATOM    942  CB  PHE A 113     -14.326  21.442  49.356  1.00 30.71           C  
ANISOU  942  CB  PHE A 113     4070   3941   3657     31    153    -19       C  
ATOM    943  CG  PHE A 113     -13.982  20.046  49.823  1.00 28.71           C  
ANISOU  943  CG  PHE A 113     3814   3687   3407     15    153    -10       C  
ATOM    944  CD1 PHE A 113     -13.878  18.988  48.927  1.00 33.63           C  
ANISOU  944  CD1 PHE A 113     4419   4314   4044     26    146    -11       C  
ATOM    945  CD2 PHE A 113     -13.810  19.787  51.173  1.00 32.56           C  
ANISOU  945  CD2 PHE A 113     4325   4164   3880    -11    160     -1       C  
ATOM    946  CE1 PHE A 113     -13.573  17.693  49.374  1.00 33.41           C  
ANISOU  946  CE1 PHE A 113     4397   4278   4020     14    146     -2       C  
ATOM    947  CE2 PHE A 113     -13.518  18.495  51.633  1.00 32.84           C  
ANISOU  947  CE2 PHE A 113     4367   4194   3918    -25    156     10       C  
ATOM    948  CZ  PHE A 113     -13.399  17.448  50.727  1.00 30.74           C  
ANISOU  948  CZ  PHE A 113     4082   3929   3669    -10    150      9       C  
ATOM    949  N   ASP A 114     -11.470  22.510  49.668  1.00 34.88           N  
ANISOU  949  N   ASP A 114     4631   4469   4152      2    122     29       N  
ATOM    950  CA  ASP A 114     -10.142  22.369  50.243  1.00 36.52           C  
ANISOU  950  CA  ASP A 114     4842   4682   4351    -21    105     54       C  
ATOM    951  C   ASP A 114     -10.271  22.537  51.751  1.00 34.87           C  
ANISOU  951  C   ASP A 114     4665   4461   4121    -50    105     58       C  
ATOM    952  O   ASP A 114     -11.114  23.298  52.229  1.00 34.49           O  
ANISOU  952  O   ASP A 114     4644   4400   4061    -55    123     41       O  
ATOM    953  CB  ASP A 114      -9.205  23.434  49.670  1.00 37.96           C  
ANISOU  953  CB  ASP A 114     5029   4872   4524    -30     96     65       C  
ATOM    954  CG  ASP A 114      -7.753  23.198  50.037  1.00 46.82           C  
ANISOU  954  CG  ASP A 114     6135   6008   5646    -52     75     92       C  
ATOM    955  OD1 ASP A 114      -7.155  22.239  49.505  1.00 47.31           O  
ANISOU  955  OD1 ASP A 114     6162   6084   5730    -36     72    101       O  
ATOM    956  OD2 ASP A 114      -7.206  23.978  50.857  1.00 53.94           O  
ANISOU  956  OD2 ASP A 114     7059   6908   6527    -85     62    104       O  
ATOM    957  N   ILE A 115      -9.449  21.820  52.505  1.00 34.65           N  
ANISOU  957  N   ILE A 115     4638   4438   4091    -69     86     80       N  
ATOM    958  CA  ILE A 115      -9.478  21.940  53.960  1.00 33.79           C  
ANISOU  958  CA  ILE A 115     4570   4316   3954   -103     81     87       C  
ATOM    959  C   ILE A 115      -8.120  22.376  54.510  1.00 34.14           C  
ANISOU  959  C   ILE A 115     4622   4367   3981   -133     46    115       C  
ATOM    960  O   ILE A 115      -7.102  22.195  53.859  1.00 34.63           O  
ANISOU  960  O   ILE A 115     4647   4449   4062   -125     25    132       O  
ATOM    961  CB  ILE A 115      -9.938  20.625  54.644  1.00 33.27           C  
ANISOU  961  CB  ILE A 115     4511   4240   3889   -105     85     89       C  
ATOM    962  CG1 ILE A 115      -8.854  19.539  54.539  1.00 33.38           C  
ANISOU  962  CG1 ILE A 115     4501   4262   3921    -97     53    117       C  
ATOM    963  CG2 ILE A 115     -11.283  20.153  54.068  1.00 29.22           C  
ANISOU  963  CG2 ILE A 115     3983   3724   3396    -83    119     60       C  
ATOM    964  CD1 ILE A 115      -9.000  18.422  55.547  1.00 28.17           C  
ANISOU  964  CD1 ILE A 115     3868   3584   3249   -111     45    130       C  
ATOM    965  N   GLU A 116      -8.120  22.963  55.705  1.00 33.32           N  
ANISOU  965  N   GLU A 116     4568   4250   3841   -172     40    118       N  
ATOM    966  CA  GLU A 116      -6.886  23.310  56.383  1.00 31.82           C  
ANISOU  966  CA  GLU A 116     4390   4069   3631   -210     -1    146       C  
ATOM    967  C   GLU A 116      -6.807  22.558  57.705  1.00 32.39           C  
ANISOU  967  C   GLU A 116     4497   4130   3678   -236    -23    162       C  
ATOM    968  O   GLU A 116      -7.801  22.459  58.421  1.00 34.46           O  
ANISOU  968  O   GLU A 116     4805   4371   3919   -247      5    145       O  
ATOM    969  CB  GLU A 116      -6.795  24.820  56.619  1.00 32.97           C  
ANISOU  969  CB  GLU A 116     4578   4205   3745   -242      3    137       C  
ATOM    970  CG  GLU A 116      -6.863  25.707  55.362  1.00 35.60           C  
ANISOU  970  CG  GLU A 116     4891   4541   4093   -221     22    123       C  
ATOM    971  CD  GLU A 116      -5.739  25.463  54.353  1.00 42.52           C  
ANISOU  971  CD  GLU A 116     5708   5448   4999   -212      1    143       C  
ATOM    972  OE1 GLU A 116      -4.718  24.828  54.703  1.00 47.33           O  
ANISOU  972  OE1 GLU A 116     6288   6078   5618   -225    -34    169       O  
ATOM    973  OE2 GLU A 116      -5.876  25.914  53.192  1.00 43.82           O  
ANISOU  973  OE2 GLU A 116     5856   5615   5177   -190     20    132       O  
ATOM    974  N   VAL A 117      -5.635  21.997  57.995  1.00 32.90           N  
ANISOU  974  N   VAL A 117     4540   4211   3750   -246    -73    197       N  
ATOM    975  CA  VAL A 117      -5.360  21.306  59.254  1.00 32.84           C  
ANISOU  975  CA  VAL A 117     4570   4193   3717   -273   -108    221       C  
ATOM    976  C   VAL A 117      -3.997  21.754  59.788  1.00 33.02           C  
ANISOU  976  C   VAL A 117     4587   4233   3724   -311   -169    254       C  
ATOM    977  O   VAL A 117      -2.964  21.389  59.224  1.00 31.86           O  
ANISOU  977  O   VAL A 117     4375   4113   3615   -291   -202    277       O  
ATOM    978  CB  VAL A 117      -5.325  19.758  59.085  1.00 33.42           C  
ANISOU  978  CB  VAL A 117     4614   4263   3820   -236   -118    237       C  
ATOM    979  CG1 VAL A 117      -5.004  19.064  60.417  1.00 30.19           C  
ANISOU  979  CG1 VAL A 117     4253   3837   3379   -265   -161    267       C  
ATOM    980  CG2 VAL A 117      -6.631  19.218  58.499  1.00 35.44           C  
ANISOU  980  CG2 VAL A 117     4870   4504   4093   -205    -63    205       C  
ATOM    981  N   THR A 118      -3.998  22.530  60.873  1.00 33.51           N  
ANISOU  981  N   THR A 118     4718   4283   3734   -367   -183    255       N  
ATOM    982  CA  THR A 118      -2.759  22.919  61.565  1.00 37.27           C  
ANISOU  982  CA  THR A 118     5197   4775   4187   -414   -250    288       C  
ATOM    983  C   THR A 118      -2.112  21.691  62.231  1.00 41.81           C  
ANISOU  983  C   THR A 118     5762   5354   4768   -409   -309    329       C  
ATOM    984  O   THR A 118      -2.777  20.948  62.954  1.00 41.44           O  
ANISOU  984  O   THR A 118     5767   5280   4697   -410   -302    329       O  
ATOM    985  CB  THR A 118      -3.030  24.039  62.621  1.00 37.50           C  
ANISOU  985  CB  THR A 118     5319   4780   4147   -481   -248    276       C  
ATOM    986  OG1 THR A 118      -3.504  25.219  61.955  1.00 35.71           O  
ANISOU  986  OG1 THR A 118     5102   4547   3920   -480   -198    243       O  
ATOM    987  CG2 THR A 118      -1.763  24.384  63.429  1.00 31.95           C  
ANISOU  987  CG2 THR A 118     4628   4095   3416   -540   -326    312       C  
ATOM    988  N   SER A 119      -0.819  21.482  61.977  1.00 47.48           N  
ANISOU  988  N   SER A 119     6412   6107   5521   -402   -366    362       N  
ATOM    989  CA  SER A 119      -0.100  20.331  62.537  1.00 51.56           C  
ANISOU  989  CA  SER A 119     6909   6628   6052   -387   -430    404       C  
ATOM    990  C   SER A 119       1.360  20.633  62.897  1.00 54.67           C  
ANISOU  990  C   SER A 119     7259   7060   6455   -418   -512    444       C  
ATOM    991  O   SER A 119       2.199  20.787  62.007  1.00 55.25           O  
ANISOU  991  O   SER A 119     7242   7171   6581   -396   -518    450       O  
ATOM    992  CB  SER A 119      -0.172  19.131  61.587  1.00 51.39           C  
ANISOU  992  CB  SER A 119     6824   6608   6094   -310   -408    405       C  
ATOM    993  OG  SER A 119       0.707  18.103  62.016  1.00 53.82           O  
ANISOU  993  OG  SER A 119     7103   6921   6424   -287   -474    448       O  
ATOM    994  N   PRO A 120       1.666  20.699  64.209  1.00 58.27           N  
ANISOU  994  N   PRO A 120     7778   7506   6856   -473   -575    471       N  
ATOM    995  CA  PRO A 120       3.031  20.962  64.688  1.00 60.54           C  
ANISOU  995  CA  PRO A 120     8025   7830   7147   -510   -665    512       C  
ATOM    996  C   PRO A 120       3.997  19.783  64.506  1.00 61.49           C  
ANISOU  996  C   PRO A 120     8058   7974   7331   -453   -725    555       C  
ATOM    997  O   PRO A 120       5.187  19.999  64.269  1.00 63.46           O  
ANISOU  997  O   PRO A 120     8221   8270   7620   -457   -776    580       O  
ATOM    998  CB  PRO A 120       2.832  21.261  66.182  1.00 60.48           C  
ANISOU  998  CB  PRO A 120     8132   7794   7053   -584   -710    525       C  
ATOM    999  CG  PRO A 120       1.568  20.550  66.549  1.00 60.27           C  
ANISOU  999  CG  PRO A 120     8186   7718   6995   -563   -657    506       C  
ATOM   1000  CD  PRO A 120       0.701  20.574  65.321  1.00 59.38           C  
ANISOU 1000  CD  PRO A 120     8036   7601   6927   -508   -562    462       C  
ATOM   1001  N   ASP A 121       3.490  18.557  64.612  1.00 60.57           N  
ANISOU 1001  N   ASP A 121     7963   7825   7225   -400   -716    563       N  
ATOM   1002  CA  ASP A 121       4.342  17.369  64.558  1.00 62.17           C  
ANISOU 1002  CA  ASP A 121     8098   8039   7484   -340   -774    605       C  
ATOM   1003  C   ASP A 121       4.449  16.753  63.158  1.00 61.29           C  
ANISOU 1003  C   ASP A 121     7891   7941   7455   -256   -720    589       C  
ATOM   1004  O   ASP A 121       4.462  15.530  63.005  1.00 61.23           O  
ANISOU 1004  O   ASP A 121     7869   7912   7483   -191   -725    605       O  
ATOM   1005  CB  ASP A 121       3.874  16.324  65.585  1.00 64.43           C  
ANISOU 1005  CB  ASP A 121     8473   8276   7730   -334   -808    630       C  
ATOM   1006  CG  ASP A 121       2.377  16.050  65.507  1.00 66.00           C  
ANISOU 1006  CG  ASP A 121     8756   8427   7894   -330   -721    590       C  
ATOM   1007  OD1 ASP A 121       1.801  15.591  66.519  1.00 66.14           O  
ANISOU 1007  OD1 ASP A 121     8874   8404   7854   -358   -735    601       O  
ATOM   1008  OD2 ASP A 121       1.777  16.296  64.438  1.00 68.38           O  
ANISOU 1008  OD2 ASP A 121     9023   8733   8226   -302   -640    548       O  
ATOM   1009  N   GLY A 122       4.529  17.606  62.140  1.00 60.67           N  
ANISOU 1009  N   GLY A 122     7757   7893   7402   -260   -667    558       N  
ATOM   1010  CA  GLY A 122       4.728  17.144  60.769  1.00 59.31           C  
ANISOU 1010  CA  GLY A 122     7496   7736   7302   -189   -614    541       C  
ATOM   1011  C   GLY A 122       3.441  16.950  59.998  1.00 57.46           C  
ANISOU 1011  C   GLY A 122     7303   7467   7061   -161   -524    496       C  
ATOM   1012  O   GLY A 122       2.406  17.514  60.360  1.00 56.85           O  
ANISOU 1012  O   GLY A 122     7307   7364   6928   -202   -491    471       O  
ATOM   1013  N   PHE A 123       3.511  16.149  58.936  1.00 55.50           N  
ANISOU 1013  N   PHE A 123     6998   7219   6870    -91   -484    486       N  
ATOM   1014  CA  PHE A 123       2.377  15.958  58.027  1.00 54.12           C  
ANISOU 1014  CA  PHE A 123     6850   7018   6695    -64   -403    443       C  
ATOM   1015  C   PHE A 123       1.177  15.292  58.704  1.00 51.07           C  
ANISOU 1015  C   PHE A 123     6557   6580   6266    -68   -390    435       C  
ATOM   1016  O   PHE A 123       1.333  14.258  59.357  1.00 52.18           O  
ANISOU 1016  O   PHE A 123     6721   6697   6410    -46   -429    464       O  
ATOM   1017  CB  PHE A 123       2.790  15.156  56.789  1.00 55.21           C  
ANISOU 1017  CB  PHE A 123     6915   7164   6899      9   -367    435       C  
ATOM   1018  CG  PHE A 123       1.754  15.151  55.703  1.00 56.95           C  
ANISOU 1018  CG  PHE A 123     7155   7367   7118     27   -288    390       C  
ATOM   1019  CD1 PHE A 123       1.698  16.188  54.776  1.00 57.05           C  
ANISOU 1019  CD1 PHE A 123     7142   7404   7130      9   -245    363       C  
ATOM   1020  CD2 PHE A 123       0.823  14.116  55.613  1.00 58.32           C  
ANISOU 1020  CD2 PHE A 123     7376   7496   7286     59   -261    377       C  
ATOM   1021  CE1 PHE A 123       0.730  16.193  53.769  1.00 59.70           C  
ANISOU 1021  CE1 PHE A 123     7498   7724   7461     25   -181    324       C  
ATOM   1022  CE2 PHE A 123      -0.144  14.111  54.615  1.00 58.03           C  
ANISOU 1022  CE2 PHE A 123     7356   7447   7248     71   -196    337       C  
ATOM   1023  CZ  PHE A 123      -0.191  15.152  53.687  1.00 58.34           C  
ANISOU 1023  CZ  PHE A 123     7368   7513   7287     56   -158    311       C  
ATOM   1024  N   PRO A 124      -0.022  15.884  58.538  1.00 47.36           N  
ANISOU 1024  N   PRO A 124     6139   6094   5759    -95   -334    397       N  
ATOM   1025  CA  PRO A 124      -1.234  15.357  59.159  1.00 47.65           C  
ANISOU 1025  CA  PRO A 124     6259   6088   5757   -107   -312    384       C  
ATOM   1026  C   PRO A 124      -1.789  14.167  58.379  1.00 48.36           C  
ANISOU 1026  C   PRO A 124     6342   6153   5880    -53   -273    370       C  
ATOM   1027  O   PRO A 124      -2.475  14.351  57.370  1.00 50.57           O  
ANISOU 1027  O   PRO A 124     6607   6435   6173    -38   -216    334       O  
ATOM   1028  CB  PRO A 124      -2.201  16.544  59.106  1.00 45.73           C  
ANISOU 1028  CB  PRO A 124     6053   5845   5475   -150   -265    347       C  
ATOM   1029  CG  PRO A 124      -1.746  17.365  57.950  1.00 44.01           C  
ANISOU 1029  CG  PRO A 124     5770   5661   5289   -137   -242    331       C  
ATOM   1030  CD  PRO A 124      -0.285  17.098  57.740  1.00 44.94           C  
ANISOU 1030  CD  PRO A 124     5816   5810   5449   -116   -290    364       C  
ATOM   1031  N   GLU A 125      -1.481  12.959  58.841  1.00 48.92           N  
ANISOU 1031  N   GLU A 125     6428   6197   5961    -25   -307    399       N  
ATOM   1032  CA  GLU A 125      -1.912  11.739  58.159  1.00 48.20           C  
ANISOU 1032  CA  GLU A 125     6339   6075   5899     25   -274    387       C  
ATOM   1033  C   GLU A 125      -3.426  11.576  58.223  1.00 45.66           C  
ANISOU 1033  C   GLU A 125     6083   5725   5543     -2   -221    353       C  
ATOM   1034  O   GLU A 125      -4.002  11.546  59.313  1.00 44.94           O  
ANISOU 1034  O   GLU A 125     6060   5611   5403    -46   -230    360       O  
ATOM   1035  CB  GLU A 125      -1.201  10.500  58.723  1.00 50.39           C  
ANISOU 1035  CB  GLU A 125     6627   6325   6195     62   -327    429       C  
ATOM   1036  CG  GLU A 125       0.246  10.318  58.244  1.00 54.27           C  
ANISOU 1036  CG  GLU A 125     7030   6844   6746    116   -364    456       C  
ATOM   1037  CD  GLU A 125       0.359   9.958  56.760  1.00 59.09           C  
ANISOU 1037  CD  GLU A 125     7581   7460   7409    173   -308    428       C  
ATOM   1038  OE1 GLU A 125      -0.594   9.377  56.195  1.00 59.58           O  
ANISOU 1038  OE1 GLU A 125     7680   7490   7465    184   -256    398       O  
ATOM   1039  OE2 GLU A 125       1.413  10.250  56.156  1.00 60.17           O  
ANISOU 1039  OE2 GLU A 125     7635   7635   7592    203   -314    435       O  
ATOM   1040  N   PRO A 126      -4.076  11.485  57.048  1.00 44.19           N  
ANISOU 1040  N   PRO A 126     5873   5540   5379     20   -165    316       N  
ATOM   1041  CA  PRO A 126      -5.529  11.350  56.948  1.00 42.59           C  
ANISOU 1041  CA  PRO A 126     5715   5317   5152     -4   -114    282       C  
ATOM   1042  C   PRO A 126      -6.077  10.144  57.696  1.00 42.56           C  
ANISOU 1042  C   PRO A 126     5777   5266   5127    -13   -117    293       C  
ATOM   1043  O   PRO A 126      -7.147  10.245  58.283  1.00 43.71           O  
ANISOU 1043  O   PRO A 126     5973   5399   5236    -57    -90    276       O  
ATOM   1044  CB  PRO A 126      -5.765  11.189  55.447  1.00 41.46           C  
ANISOU 1044  CB  PRO A 126     5526   5183   5046     34    -72    251       C  
ATOM   1045  CG  PRO A 126      -4.618  11.874  54.819  1.00 42.56           C  
ANISOU 1045  CG  PRO A 126     5600   5358   5214     58    -88    260       C  
ATOM   1046  CD  PRO A 126      -3.451  11.605  55.717  1.00 44.00           C  
ANISOU 1046  CD  PRO A 126     5776   5541   5402     65   -146    305       C  
ATOM   1047  N   SER A 127      -5.354   9.025  57.694  1.00 42.59           N  
ANISOU 1047  N   SER A 127     5783   5244   5154     27   -147    321       N  
ATOM   1048  CA  SER A 127      -5.833   7.814  58.376  1.00 44.96           C  
ANISOU 1048  CA  SER A 127     6157   5492   5433     18   -152    334       C  
ATOM   1049  C   SER A 127      -5.835   7.959  59.899  1.00 44.75           C  
ANISOU 1049  C   SER A 127     6197   5452   5355    -31   -190    364       C  
ATOM   1050  O   SER A 127      -6.587   7.272  60.590  1.00 47.08           O  
ANISOU 1050  O   SER A 127     6567   5708   5615    -64   -178    366       O  
ATOM   1051  CB  SER A 127      -5.042   6.567  57.945  1.00 45.29           C  
ANISOU 1051  CB  SER A 127     6191   5502   5516     81   -174    357       C  
ATOM   1052  OG  SER A 127      -3.767   6.530  58.559  1.00 46.95           O  
ANISOU 1052  OG  SER A 127     6383   5718   5739    107   -240    403       O  
ATOM   1053  N   GLN A 128      -4.997   8.856  60.412  1.00 45.25           N  
ANISOU 1053  N   GLN A 128     6237   5546   5411    -42   -234    386       N  
ATOM   1054  CA  GLN A 128      -4.957   9.148  61.842  1.00 46.51           C  
ANISOU 1054  CA  GLN A 128     6464   5696   5514    -95   -272    412       C  
ATOM   1055  C   GLN A 128      -5.940  10.260  62.221  1.00 44.49           C  
ANISOU 1055  C   GLN A 128     6235   5456   5213   -156   -227    378       C  
ATOM   1056  O   GLN A 128      -6.684  10.129  63.192  1.00 43.15           O  
ANISOU 1056  O   GLN A 128     6145   5261   4991   -207   -212    376       O  
ATOM   1057  CB  GLN A 128      -3.532   9.503  62.294  1.00 49.54           C  
ANISOU 1057  CB  GLN A 128     6814   6102   5907    -82   -351    456       C  
ATOM   1058  CG  GLN A 128      -2.493   8.384  62.104  1.00 56.11           C  
ANISOU 1058  CG  GLN A 128     7618   6915   6784    -16   -404    496       C  
ATOM   1059  CD  GLN A 128      -2.896   7.068  62.778  1.00 62.47           C  
ANISOU 1059  CD  GLN A 128     8512   7658   7564    -15   -417    518       C  
ATOM   1060  OE1 GLN A 128      -3.151   6.065  62.104  1.00 61.63           O  
ANISOU 1060  OE1 GLN A 128     8408   7519   7488     28   -388    509       O  
ATOM   1061  NE2 GLN A 128      -2.958   7.072  64.112  1.00 62.85           N  
ANISOU 1061  NE2 GLN A 128     8643   7685   7551    -66   -459    548       N  
ATOM   1062  N   ALA A 129      -5.937  11.338  61.436  1.00 42.50           N  
ANISOU 1062  N   ALA A 129     5921   5245   4983   -150   -201    350       N  
ATOM   1063  CA  ALA A 129      -6.763  12.537  61.666  1.00 40.74           C  
ANISOU 1063  CA  ALA A 129     5715   5038   4727   -195   -158    317       C  
ATOM   1064  C   ALA A 129      -6.777  13.028  63.121  1.00 41.03           C  
ANISOU 1064  C   ALA A 129     5828   5063   4699   -256   -181    332       C  
ATOM   1065  O   ALA A 129      -7.838  13.279  63.698  1.00 40.67           O  
ANISOU 1065  O   ALA A 129     5837   5002   4612   -299   -133    307       O  
ATOM   1066  CB  ALA A 129      -8.187  12.343  61.117  1.00 37.22           C  
ANISOU 1066  CB  ALA A 129     5273   4583   4287   -199    -85    272       C  
ATOM   1067  N   LYS A 130      -5.592  13.173  63.705  1.00 41.95           N  
ANISOU 1067  N   LYS A 130     5947   5188   4805   -262   -253    373       N  
ATOM   1068  CA  LYS A 130      -5.498  13.518  65.124  1.00 43.65           C  
ANISOU 1068  CA  LYS A 130     6246   5388   4952   -323   -286    393       C  
ATOM   1069  C   LYS A 130      -5.479  15.015  65.396  1.00 42.00           C  
ANISOU 1069  C   LYS A 130     6043   5202   4712   -366   -276    374       C  
ATOM   1070  O   LYS A 130      -5.407  15.433  66.548  1.00 41.02           O  
ANISOU 1070  O   LYS A 130     5994   5066   4526   -422   -300    386       O  
ATOM   1071  CB  LYS A 130      -4.316  12.805  65.807  1.00 46.10           C  
ANISOU 1071  CB  LYS A 130     6571   5688   5256   -316   -378    451       C  
ATOM   1072  CG  LYS A 130      -2.962  12.954  65.129  1.00 52.23           C  
ANISOU 1072  CG  LYS A 130     7253   6501   6091   -270   -436    477       C  
ATOM   1073  CD  LYS A 130      -1.901  12.108  65.845  1.00 57.01           C  
ANISOU 1073  CD  LYS A 130     7871   7093   6696   -255   -529    536       C  
ATOM   1074  CE  LYS A 130      -0.486  12.488  65.407  1.00 60.04           C  
ANISOU 1074  CE  LYS A 130     8158   7524   7132   -224   -592    563       C  
ATOM   1075  NZ  LYS A 130       0.566  11.714  66.129  1.00 62.10           N  
ANISOU 1075  NZ  LYS A 130     8423   7775   7398   -206   -690    623       N  
ATOM   1076  N   HIS A 131      -5.564  15.819  64.337  1.00 40.63           N  
ANISOU 1076  N   HIS A 131     5802   5058   4578   -341   -241    344       N  
ATOM   1077  CA  HIS A 131      -5.573  17.272  64.484  1.00 39.56           C  
ANISOU 1077  CA  HIS A 131     5676   4939   4417   -377   -228    324       C  
ATOM   1078  C   HIS A 131      -6.877  17.912  63.994  1.00 38.50           C  
ANISOU 1078  C   HIS A 131     5543   4801   4284   -375   -142    272       C  
ATOM   1079  O   HIS A 131      -7.481  17.449  63.022  1.00 39.29           O  
ANISOU 1079  O   HIS A 131     5596   4904   4428   -332   -102    251       O  
ATOM   1080  CB  HIS A 131      -4.365  17.894  63.784  1.00 40.42           C  
ANISOU 1080  CB  HIS A 131     5709   5085   4563   -359   -272    340       C  
ATOM   1081  CG  HIS A 131      -3.056  17.320  64.223  1.00 41.83           C  
ANISOU 1081  CG  HIS A 131     5869   5275   4750   -357   -359    391       C  
ATOM   1082  ND1 HIS A 131      -2.264  16.559  63.393  1.00 42.23           N  
ANISOU 1082  ND1 HIS A 131     5837   5344   4864   -299   -386    412       N  
ATOM   1083  CD2 HIS A 131      -2.413  17.372  65.412  1.00 44.91           C  
ANISOU 1083  CD2 HIS A 131     6311   5659   5093   -403   -426    426       C  
ATOM   1084  CE1 HIS A 131      -1.182  16.179  64.047  1.00 42.89           C  
ANISOU 1084  CE1 HIS A 131     5915   5435   4947   -304   -467    459       C  
ATOM   1085  NE2 HIS A 131      -1.249  16.656  65.275  1.00 44.47           N  
ANISOU 1085  NE2 HIS A 131     6197   5621   5079   -369   -497    470       N  
ATOM   1086  N   PRO A 132      -7.323  18.970  64.685  1.00 38.02           N  
ANISOU 1086  N   PRO A 132     5540   4730   4174   -420   -115    250       N  
ATOM   1087  CA  PRO A 132      -8.552  19.665  64.331  1.00 36.78           C  
ANISOU 1087  CA  PRO A 132     5386   4568   4020   -414    -36    202       C  
ATOM   1088  C   PRO A 132      -8.558  20.159  62.895  1.00 35.62           C  
ANISOU 1088  C   PRO A 132     5158   4447   3931   -365    -19    183       C  
ATOM   1089  O   PRO A 132      -7.527  20.597  62.382  1.00 36.47           O  
ANISOU 1089  O   PRO A 132     5224   4575   4057   -356    -61    201       O  
ATOM   1090  CB  PRO A 132      -8.560  20.862  65.288  1.00 36.76           C  
ANISOU 1090  CB  PRO A 132     5457   4552   3957   -468    -29    191       C  
ATOM   1091  CG  PRO A 132      -7.826  20.371  66.481  1.00 38.96           C  
ANISOU 1091  CG  PRO A 132     5801   4819   4185   -516    -89    229       C  
ATOM   1092  CD  PRO A 132      -6.760  19.464  65.960  1.00 38.15           C  
ANISOU 1092  CD  PRO A 132     5633   4736   4126   -481   -158    271       C  
ATOM   1093  N   ILE A 133      -9.718  20.072  62.253  1.00 34.59           N  
ANISOU 1093  N   ILE A 133     5003   4314   3826   -336     41    149       N  
ATOM   1094  CA  ILE A 133      -9.928  20.738  60.979  1.00 33.66           C  
ANISOU 1094  CA  ILE A 133     4825   4215   3751   -296     63    127       C  
ATOM   1095  C   ILE A 133     -10.291  22.185  61.294  1.00 33.68           C  
ANISOU 1095  C   ILE A 133     4865   4207   3725   -316     92    102       C  
ATOM   1096  O   ILE A 133     -11.291  22.442  61.964  1.00 33.18           O  
ANISOU 1096  O   ILE A 133     4845   4124   3636   -332    141     76       O  
ATOM   1097  CB  ILE A 133     -11.046  20.071  60.153  1.00 31.93           C  
ANISOU 1097  CB  ILE A 133     4564   3997   3571   -258    107    101       C  
ATOM   1098  CG1 ILE A 133     -10.654  18.631  59.796  1.00 31.83           C  
ANISOU 1098  CG1 ILE A 133     4523   3987   3584   -239     80    123       C  
ATOM   1099  CG2 ILE A 133     -11.349  20.906  58.903  1.00 31.97           C  
ANISOU 1099  CG2 ILE A 133     4518   4017   3610   -220    126     78       C  
ATOM   1100  CD1 ILE A 133     -11.780  17.788  59.195  1.00 26.20           C  
ANISOU 1100  CD1 ILE A 133     3784   3271   2899   -217    121     99       C  
ATOM   1101  N   ASP A 134      -9.481  23.128  60.819  1.00 33.26           N  
ANISOU 1101  N   ASP A 134     4797   4165   3675   -315     66    110       N  
ATOM   1102  CA  ASP A 134      -9.686  24.534  61.191  1.00 34.19           C  
ANISOU 1102  CA  ASP A 134     4964   4266   3760   -339     88     90       C  
ATOM   1103  C   ASP A 134     -10.175  25.450  60.063  1.00 33.44           C  
ANISOU 1103  C   ASP A 134     4838   4173   3696   -299    118     64       C  
ATOM   1104  O   ASP A 134     -10.295  26.656  60.251  1.00 34.94           O  
ANISOU 1104  O   ASP A 134     5070   4343   3862   -312    135     49       O  
ATOM   1105  CB  ASP A 134      -8.441  25.106  61.886  1.00 31.15           C  
ANISOU 1105  CB  ASP A 134     4619   3881   3335   -390     34    117       C  
ATOM   1106  CG  ASP A 134      -7.160  24.854  61.113  1.00 32.01           C  
ANISOU 1106  CG  ASP A 134     4662   4022   3477   -380    -22    150       C  
ATOM   1107  OD1 ASP A 134      -7.167  24.965  59.869  1.00 37.68           O  
ANISOU 1107  OD1 ASP A 134     5323   4757   4239   -339    -11    142       O  
ATOM   1108  OD2 ASP A 134      -6.132  24.561  61.754  1.00 28.81           O  
ANISOU 1108  OD2 ASP A 134     4266   3628   3054   -415    -79    183       O  
ATOM   1109  N   ALA A 135     -10.446  24.876  58.894  1.00 31.34           N  
ANISOU 1109  N   ALA A 135     4503   3925   3478   -251    123     62       N  
ATOM   1110  CA  ALA A 135     -11.010  25.629  57.776  1.00 29.55           C  
ANISOU 1110  CA  ALA A 135     4249   3699   3280   -211    147     40       C  
ATOM   1111  C   ALA A 135     -11.499  24.712  56.664  1.00 29.48           C  
ANISOU 1111  C   ALA A 135     4175   3709   3318   -166    153     35       C  
ATOM   1112  O   ALA A 135     -10.821  23.760  56.281  1.00 29.18           O  
ANISOU 1112  O   ALA A 135     4101   3688   3297   -161    124     56       O  
ATOM   1113  CB  ALA A 135     -10.003  26.634  57.219  1.00 28.50           C  
ANISOU 1113  CB  ALA A 135     4119   3570   3141   -221    119     53       C  
ATOM   1114  N   ILE A 136     -12.687  25.007  56.153  1.00 29.03           N  
ANISOU 1114  N   ILE A 136     4102   3647   3281   -132    189      7       N  
ATOM   1115  CA  ILE A 136     -13.173  24.363  54.948  1.00 28.20           C  
ANISOU 1115  CA  ILE A 136     3939   3560   3217    -92    190      0       C  
ATOM   1116  C   ILE A 136     -13.753  25.443  54.068  1.00 30.30           C  
ANISOU 1116  C   ILE A 136     4197   3820   3497    -58    201    -17       C  
ATOM   1117  O   ILE A 136     -14.620  26.204  54.512  1.00 30.81           O  
ANISOU 1117  O   ILE A 136     4284   3867   3557    -49    232    -40       O  
ATOM   1118  CB  ILE A 136     -14.290  23.326  55.231  1.00 27.28           C  
ANISOU 1118  CB  ILE A 136     3803   3446   3117    -87    218    -17       C  
ATOM   1119  CG1 ILE A 136     -13.812  22.250  56.213  1.00 27.77           C  
ANISOU 1119  CG1 ILE A 136     3887   3505   3160   -123    208      1       C  
ATOM   1120  CG2 ILE A 136     -14.793  22.718  53.921  1.00 23.84           C  
ANISOU 1120  CG2 ILE A 136     3310   3027   2719    -51    213    -25       C  
ATOM   1121  CD1 ILE A 136     -14.916  21.329  56.715  1.00 27.35           C  
ANISOU 1121  CD1 ILE A 136     3830   3448   3112   -132    243    -16       C  
ATOM   1122  N   THR A 137     -13.255  25.523  52.833  1.00 30.24           N  
ANISOU 1122  N   THR A 137     4161   3824   3504    -37    177     -7       N  
ATOM   1123  CA  THR A 137     -13.915  26.284  51.784  1.00 27.44           C  
ANISOU 1123  CA  THR A 137     3796   3465   3166      1    181    -21       C  
ATOM   1124  C   THR A 137     -14.476  25.275  50.800  1.00 27.76           C  
ANISOU 1124  C   THR A 137     3785   3526   3238     27    175    -27       C  
ATOM   1125  O   THR A 137     -13.734  24.462  50.243  1.00 25.46           O  
ANISOU 1125  O   THR A 137     3473   3249   2951     22    157    -12       O  
ATOM   1126  CB  THR A 137     -12.960  27.264  51.065  1.00 26.92           C  
ANISOU 1126  CB  THR A 137     3751   3393   3085     -3    160     -5       C  
ATOM   1127  OG1 THR A 137     -12.463  28.217  52.008  1.00 28.36           O  
ANISOU 1127  OG1 THR A 137     3986   3554   3235    -35    164     -1       O  
ATOM   1128  CG2 THR A 137     -13.690  28.010  49.939  1.00 25.13           C  
ANISOU 1128  CG2 THR A 137     3520   3157   2870     38    159    -16       C  
ATOM   1129  N   HIS A 138     -15.791  25.350  50.606  1.00 26.85           N  
ANISOU 1129  N   HIS A 138     3648   3410   3143     55    192    -49       N  
ATOM   1130  CA  HIS A 138     -16.547  24.452  49.750  1.00 27.76           C  
ANISOU 1130  CA  HIS A 138     3716   3545   3287     75    186    -59       C  
ATOM   1131  C   HIS A 138     -17.288  25.312  48.724  1.00 28.11           C  
ANISOU 1131  C   HIS A 138     3747   3586   3346    116    174    -69       C  
ATOM   1132  O   HIS A 138     -18.208  26.033  49.091  1.00 28.16           O  
ANISOU 1132  O   HIS A 138     3752   3584   3365    137    192    -85       O  
ATOM   1133  CB  HIS A 138     -17.533  23.668  50.639  1.00 29.63           C  
ANISOU 1133  CB  HIS A 138     3932   3787   3538     63    216    -77       C  
ATOM   1134  CG  HIS A 138     -18.386  22.670  49.913  1.00 29.98           C  
ANISOU 1134  CG  HIS A 138     3929   3851   3610     72    211    -90       C  
ATOM   1135  ND1 HIS A 138     -18.275  21.311  50.117  1.00 29.31           N  
ANISOU 1135  ND1 HIS A 138     3835   3773   3527     45    213    -87       N  
ATOM   1136  CD2 HIS A 138     -19.389  22.834  49.015  1.00 31.35           C  
ANISOU 1136  CD2 HIS A 138     4064   4038   3811    101    201   -104       C  
ATOM   1137  CE1 HIS A 138     -19.158  20.680  49.361  1.00 27.17           C  
ANISOU 1137  CE1 HIS A 138     3525   3519   3280     53    207   -101       C  
ATOM   1138  NE2 HIS A 138     -19.854  21.583  48.692  1.00 27.47           N  
ANISOU 1138  NE2 HIS A 138     3540   3563   3334     86    197   -112       N  
ATOM   1139  N   TYR A 139     -16.867  25.273  47.454  1.00 27.82           N  
ANISOU 1139  N   TYR A 139     3707   3556   3308    127    145    -58       N  
ATOM   1140  CA  TYR A 139     -17.602  25.970  46.394  1.00 26.83           C  
ANISOU 1140  CA  TYR A 139     3573   3428   3193    165    124    -63       C  
ATOM   1141  C   TYR A 139     -18.666  25.060  45.787  1.00 29.45           C  
ANISOU 1141  C   TYR A 139     3855   3783   3553    178    113    -78       C  
ATOM   1142  O   TYR A 139     -18.395  23.907  45.443  1.00 32.45           O  
ANISOU 1142  O   TYR A 139     4219   4177   3933    158    107    -76       O  
ATOM   1143  CB  TYR A 139     -16.671  26.511  45.301  1.00 24.10           C  
ANISOU 1143  CB  TYR A 139     3259   3074   2823    166     99    -44       C  
ATOM   1144  CG  TYR A 139     -17.405  27.041  44.075  1.00 25.81           C  
ANISOU 1144  CG  TYR A 139     3473   3287   3045    202     70    -46       C  
ATOM   1145  CD1 TYR A 139     -17.655  26.218  42.971  1.00 30.02           C  
ANISOU 1145  CD1 TYR A 139     3985   3839   3583    205     46    -47       C  
ATOM   1146  CD2 TYR A 139     -17.847  28.359  44.015  1.00 26.08           C  
ANISOU 1146  CD2 TYR A 139     3535   3297   3078    233     63    -46       C  
ATOM   1147  CE1 TYR A 139     -18.324  26.700  41.838  1.00 24.32           C  
ANISOU 1147  CE1 TYR A 139     3266   3113   2860    235     10    -46       C  
ATOM   1148  CE2 TYR A 139     -18.510  28.849  42.895  1.00 27.29           C  
ANISOU 1148  CE2 TYR A 139     3691   3444   3235    269     28    -43       C  
ATOM   1149  CZ  TYR A 139     -18.754  28.015  41.812  1.00 30.80           C  
ANISOU 1149  CZ  TYR A 139     4111   3910   3681    269     -1    -42       C  
ATOM   1150  OH  TYR A 139     -19.422  28.509  40.699  1.00 29.63           O  
ANISOU 1150  OH  TYR A 139     3970   3756   3532    302    -44    -37       O  
ATOM   1151  N   ASP A 140     -19.873  25.597  45.650  1.00 29.71           N  
ANISOU 1151  N   ASP A 140     3861   3817   3611    212    109    -92       N  
ATOM   1152  CA  ASP A 140     -20.998  24.879  45.072  1.00 29.56           C  
ANISOU 1152  CA  ASP A 140     3787   3822   3621    223     93   -107       C  
ATOM   1153  C   ASP A 140     -21.346  25.511  43.721  1.00 31.66           C  
ANISOU 1153  C   ASP A 140     4054   4086   3888    258     46   -100       C  
ATOM   1154  O   ASP A 140     -21.569  26.719  43.643  1.00 30.93           O  
ANISOU 1154  O   ASP A 140     3980   3974   3797    294     38    -96       O  
ATOM   1155  CB  ASP A 140     -22.185  24.950  46.033  1.00 28.08           C  
ANISOU 1155  CB  ASP A 140     3556   3643   3468    233    125   -129       C  
ATOM   1156  CG  ASP A 140     -23.387  24.200  45.528  1.00 31.85           C  
ANISOU 1156  CG  ASP A 140     3968   4153   3982    237    109   -145       C  
ATOM   1157  OD1 ASP A 140     -24.122  24.752  44.675  1.00 32.74           O  
ANISOU 1157  OD1 ASP A 140     4054   4272   4114    276     73   -147       O  
ATOM   1158  OD2 ASP A 140     -23.607  23.066  46.002  1.00 34.89           O  
ANISOU 1158  OD2 ASP A 140     4330   4554   4374    200    130   -156       O  
ATOM   1159  N   SER A 141     -21.389  24.691  42.669  1.00 31.13           N  
ANISOU 1159  N   SER A 141     3976   4036   3816    246     14    -98       N  
ATOM   1160  CA  SER A 141     -21.541  25.183  41.296  1.00 33.27           C  
ANISOU 1160  CA  SER A 141     4263   4304   4075    270    -35    -87       C  
ATOM   1161  C   SER A 141     -22.952  25.673  40.989  1.00 35.03           C  
ANISOU 1161  C   SER A 141     4439   4538   4333    311    -66    -96       C  
ATOM   1162  O   SER A 141     -23.142  26.529  40.124  1.00 34.57           O  
ANISOU 1162  O   SER A 141     4403   4467   4267    345   -108    -84       O  
ATOM   1163  CB  SER A 141     -21.131  24.110  40.280  1.00 33.32           C  
ANISOU 1163  CB  SER A 141     4279   4322   4059    240    -56    -85       C  
ATOM   1164  OG  SER A 141     -22.079  23.048  40.240  1.00 34.72           O  
ANISOU 1164  OG  SER A 141     4405   4526   4262    225    -64   -102       O  
ATOM   1165  N   ILE A 142     -23.935  25.119  41.694  1.00 36.09           N  
ANISOU 1165  N   ILE A 142     4509   4696   4508    309    -48   -117       N  
ATOM   1166  CA  ILE A 142     -25.331  25.507  41.509  1.00 36.46           C  
ANISOU 1166  CA  ILE A 142     4494   4761   4600    348    -74   -128       C  
ATOM   1167  C   ILE A 142     -25.685  26.841  42.201  1.00 37.99           C  
ANISOU 1167  C   ILE A 142     4688   4932   4815    401    -52   -130       C  
ATOM   1168  O   ILE A 142     -26.367  27.688  41.614  1.00 38.43           O  
ANISOU 1168  O   ILE A 142     4729   4981   4890    453    -92   -124       O  
ATOM   1169  CB  ILE A 142     -26.292  24.348  41.896  1.00 37.07           C  
ANISOU 1169  CB  ILE A 142     4495   4877   4714    319    -60   -151       C  
ATOM   1170  CG1 ILE A 142     -26.218  23.247  40.827  1.00 32.66           C  
ANISOU 1170  CG1 ILE A 142     3938   4337   4135    281   -102   -148       C  
ATOM   1171  CG2 ILE A 142     -27.752  24.847  42.068  1.00 35.64           C  
ANISOU 1171  CG2 ILE A 142     4231   4718   4590    362    -69   -166       C  
ATOM   1172  CD1 ILE A 142     -26.988  21.990  41.154  1.00 35.95           C  
ANISOU 1172  CD1 ILE A 142     4295   4786   4577    238    -89   -169       C  
ATOM   1173  N   ASP A 143     -25.215  27.029  43.433  1.00 37.55           N  
ANISOU 1173  N   ASP A 143     4655   4859   4754    387      7   -137       N  
ATOM   1174  CA  ASP A 143     -25.385  28.309  44.135  1.00 38.65           C  
ANISOU 1174  CA  ASP A 143     4815   4968   4904    431     35   -141       C  
ATOM   1175  C   ASP A 143     -24.408  29.356  43.625  1.00 38.12           C  
ANISOU 1175  C   ASP A 143     4831   4858   4794    445     13   -117       C  
ATOM   1176  O   ASP A 143     -24.671  30.562  43.731  1.00 38.70           O  
ANISOU 1176  O   ASP A 143     4930   4900   4875    493     14   -115       O  
ATOM   1177  CB  ASP A 143     -25.163  28.147  45.643  1.00 39.89           C  
ANISOU 1177  CB  ASP A 143     4980   5119   5059    402    106   -157       C  
ATOM   1178  CG  ASP A 143     -26.221  27.298  46.307  1.00 40.85           C  
ANISOU 1178  CG  ASP A 143     5023   5276   5222    389    140   -183       C  
ATOM   1179  OD1 ASP A 143     -27.298  27.076  45.710  1.00 45.18           O  
ANISOU 1179  OD1 ASP A 143     5500   5854   5813    413    112   -192       O  
ATOM   1180  OD2 ASP A 143     -25.968  26.859  47.443  1.00 39.80           O  
ANISOU 1180  OD2 ASP A 143     4903   5141   5078    350    194   -194       O  
ATOM   1181  N   ASP A 144     -23.278  28.887  43.085  1.00 37.49           N  
ANISOU 1181  N   ASP A 144     4797   4778   4671    402     -1    -99       N  
ATOM   1182  CA  ASP A 144     -22.176  29.756  42.650  1.00 35.97           C  
ANISOU 1182  CA  ASP A 144     4685   4549   4433    399    -13    -77       C  
ATOM   1183  C   ASP A 144     -21.630  30.536  43.845  1.00 34.50           C  
ANISOU 1183  C   ASP A 144     4543   4333   4234    392     34    -80       C  
ATOM   1184  O   ASP A 144     -21.425  31.751  43.778  1.00 36.93           O  
ANISOU 1184  O   ASP A 144     4906   4601   4526    417     30    -71       O  
ATOM   1185  CB  ASP A 144     -22.637  30.694  41.518  1.00 38.23           C  
ANISOU 1185  CB  ASP A 144     4993   4815   4717    448    -66    -62       C  
ATOM   1186  CG  ASP A 144     -21.493  31.475  40.886  1.00 39.88           C  
ANISOU 1186  CG  ASP A 144     5290   4990   4874    434    -80    -37       C  
ATOM   1187  OD1 ASP A 144     -20.328  31.021  40.938  1.00 42.46           O  
ANISOU 1187  OD1 ASP A 144     5645   5320   5167    382    -60    -30       O  
ATOM   1188  OD2 ASP A 144     -21.775  32.549  40.326  1.00 42.29           O  
ANISOU 1188  OD2 ASP A 144     5634   5261   5172    475   -111    -24       O  
ATOM   1189  N   ARG A 145     -21.407  29.825  44.945  1.00 32.08           N  
ANISOU 1189  N   ARG A 145     4219   4039   3929    355     77    -92       N  
ATOM   1190  CA  ARG A 145     -20.962  30.452  46.188  1.00 33.54           C  
ANISOU 1190  CA  ARG A 145     4447   4198   4099    341    122    -98       C  
ATOM   1191  C   ARG A 145     -19.837  29.665  46.834  1.00 32.45           C  
ANISOU 1191  C   ARG A 145     4326   4070   3932    280    141    -91       C  
ATOM   1192  O   ARG A 145     -19.783  28.435  46.725  1.00 31.41           O  
ANISOU 1192  O   ARG A 145     4157   3970   3808    255    138    -91       O  
ATOM   1193  CB  ARG A 145     -22.120  30.582  47.184  1.00 33.08           C  
ANISOU 1193  CB  ARG A 145     4350   4141   4078    368    163   -125       C  
ATOM   1194  CG  ARG A 145     -23.296  31.443  46.704  1.00 36.04           C  
ANISOU 1194  CG  ARG A 145     4698   4504   4491    439    148   -134       C  
ATOM   1195  CD  ARG A 145     -22.985  32.930  46.798  1.00 35.59           C  
ANISOU 1195  CD  ARG A 145     4717   4392   4413    471    151   -127       C  
ATOM   1196  NE  ARG A 145     -24.111  33.764  46.385  1.00 38.09           N  
ANISOU 1196  NE  ARG A 145     5009   4692   4770    548    136   -134       N  
ATOM   1197  CZ  ARG A 145     -24.316  34.210  45.148  1.00 40.94           C  
ANISOU 1197  CZ  ARG A 145     5376   5044   5135    587     77   -115       C  
ATOM   1198  NH1 ARG A 145     -23.477  33.908  44.166  1.00 40.71           N  
ANISOU 1198  NH1 ARG A 145     5378   5021   5067    553     33    -90       N  
ATOM   1199  NH2 ARG A 145     -25.373  34.968  44.892  1.00 42.81           N  
ANISOU 1199  NH2 ARG A 145     5589   5265   5413    663     62   -121       N  
ATOM   1200  N   PHE A 146     -18.942  30.391  47.496  1.00 31.37           N  
ANISOU 1200  N   PHE A 146     4250   3906   3763    256    157    -83       N  
ATOM   1201  CA  PHE A 146     -17.860  29.808  48.281  1.00 30.33           C  
ANISOU 1201  CA  PHE A 146     4137   3782   3605    200    172    -74       C  
ATOM   1202  C   PHE A 146     -18.306  29.800  49.740  1.00 30.22           C  
ANISOU 1202  C   PHE A 146     4129   3760   3593    188    216    -93       C  
ATOM   1203  O   PHE A 146     -18.402  30.854  50.377  1.00 30.27           O  
ANISOU 1203  O   PHE A 146     4182   3734   3586    196    238   -101       O  
ATOM   1204  CB  PHE A 146     -16.574  30.640  48.143  1.00 28.83           C  
ANISOU 1204  CB  PHE A 146     4009   3570   3376    173    160    -53       C  
ATOM   1205  CG  PHE A 146     -16.003  30.671  46.752  1.00 30.25           C  
ANISOU 1205  CG  PHE A 146     4192   3755   3546    176    125    -34       C  
ATOM   1206  CD1 PHE A 146     -16.489  31.570  45.806  1.00 27.85           C  
ANISOU 1206  CD1 PHE A 146     3910   3430   3243    215    105    -31       C  
ATOM   1207  CD2 PHE A 146     -14.964  29.809  46.392  1.00 29.47           C  
ANISOU 1207  CD2 PHE A 146     4078   3682   3436    140    115    -19       C  
ATOM   1208  CE1 PHE A 146     -15.969  31.600  44.510  1.00 30.29           C  
ANISOU 1208  CE1 PHE A 146     4230   3742   3535    212     76    -14       C  
ATOM   1209  CE2 PHE A 146     -14.424  29.834  45.094  1.00 31.24           C  
ANISOU 1209  CE2 PHE A 146     4309   3911   3648    140     93     -5       C  
ATOM   1210  CZ  PHE A 146     -14.930  30.724  44.151  1.00 30.32           C  
ANISOU 1210  CZ  PHE A 146     4220   3773   3526    172     73     -2       C  
ATOM   1211  N   TYR A 147     -18.600  28.617  50.265  1.00 29.41           N  
ANISOU 1211  N   TYR A 147     3987   3683   3503    167    231   -101       N  
ATOM   1212  CA  TYR A 147     -18.977  28.500  51.668  1.00 28.09           C  
ANISOU 1212  CA  TYR A 147     3833   3510   3331    147    276   -118       C  
ATOM   1213  C   TYR A 147     -17.731  28.230  52.488  1.00 27.72           C  
ANISOU 1213  C   TYR A 147     3832   3457   3243     92    274   -100       C  
ATOM   1214  O   TYR A 147     -17.034  27.237  52.274  1.00 27.34           O  
ANISOU 1214  O   TYR A 147     3767   3429   3191     66    251    -83       O  
ATOM   1215  CB  TYR A 147     -20.015  27.401  51.864  1.00 29.13           C  
ANISOU 1215  CB  TYR A 147     3904   3669   3495    148    297   -136       C  
ATOM   1216  CG  TYR A 147     -21.325  27.648  51.140  1.00 29.20           C  
ANISOU 1216  CG  TYR A 147     3855   3689   3549    200    296   -154       C  
ATOM   1217  CD1 TYR A 147     -21.540  27.168  49.844  1.00 30.34           C  
ANISOU 1217  CD1 TYR A 147     3955   3857   3715    219    253   -146       C  
ATOM   1218  CD2 TYR A 147     -22.349  28.344  51.754  1.00 29.67           C  
ANISOU 1218  CD2 TYR A 147     3905   3737   3630    231    338   -180       C  
ATOM   1219  CE1 TYR A 147     -22.757  27.386  49.185  1.00 27.16           C  
ANISOU 1219  CE1 TYR A 147     3497   3468   3355    265    243   -161       C  
ATOM   1220  CE2 TYR A 147     -23.566  28.563  51.111  1.00 31.71           C  
ANISOU 1220  CE2 TYR A 147     4100   4010   3938    283    334   -196       C  
ATOM   1221  CZ  TYR A 147     -23.760  28.091  49.831  1.00 31.00           C  
ANISOU 1221  CZ  TYR A 147     3965   3946   3869    299    282   -184       C  
ATOM   1222  OH  TYR A 147     -24.971  28.322  49.219  1.00 30.52           O  
ANISOU 1222  OH  TYR A 147     3838   3901   3856    350    269   -197       O  
ATOM   1223  N   VAL A 148     -17.452  29.137  53.417  1.00 29.41           N  
ANISOU 1223  N   VAL A 148     4106   3641   3426     74    295   -104       N  
ATOM   1224  CA  VAL A 148     -16.232  29.117  54.211  1.00 28.64           C  
ANISOU 1224  CA  VAL A 148     4059   3536   3286     20    284    -86       C  
ATOM   1225  C   VAL A 148     -16.598  28.749  55.652  1.00 31.98           C  
ANISOU 1225  C   VAL A 148     4509   3952   3690    -12    322   -100       C  
ATOM   1226  O   VAL A 148     -17.414  29.425  56.289  1.00 31.92           O  
ANISOU 1226  O   VAL A 148     4527   3921   3679      1    367   -126       O  
ATOM   1227  CB  VAL A 148     -15.507  30.499  54.158  1.00 29.53           C  
ANISOU 1227  CB  VAL A 148     4235   3618   3369     11    273    -78       C  
ATOM   1228  CG1 VAL A 148     -14.118  30.431  54.790  1.00 27.82           C  
ANISOU 1228  CG1 VAL A 148     4056   3402   3112    -50    248    -54       C  
ATOM   1229  CG2 VAL A 148     -15.402  31.006  52.712  1.00 30.37           C  
ANISOU 1229  CG2 VAL A 148     4323   3724   3492     47    244    -68       C  
ATOM   1230  N   PHE A 149     -16.014  27.661  56.147  1.00 30.71           N  
ANISOU 1230  N   PHE A 149     4344   3809   3516    -52    308    -83       N  
ATOM   1231  CA  PHE A 149     -16.224  27.218  57.516  1.00 31.98           C  
ANISOU 1231  CA  PHE A 149     4541   3961   3650    -91    338    -91       C  
ATOM   1232  C   PHE A 149     -14.919  27.454  58.250  1.00 32.65           C  
ANISOU 1232  C   PHE A 149     4685   4035   3686   -142    307    -66       C  
ATOM   1233  O   PHE A 149     -13.913  26.816  57.959  1.00 35.56           O  
ANISOU 1233  O   PHE A 149     5035   4421   4054   -159    261    -37       O  
ATOM   1234  CB  PHE A 149     -16.619  25.732  57.561  1.00 31.93           C  
ANISOU 1234  CB  PHE A 149     4491   3979   3662    -99    342    -89       C  
ATOM   1235  CG  PHE A 149     -17.886  25.405  56.800  1.00 31.92           C  
ANISOU 1235  CG  PHE A 149     4424   3995   3710    -57    366   -112       C  
ATOM   1236  CD1 PHE A 149     -17.909  25.416  55.406  1.00 33.74           C  
ANISOU 1236  CD1 PHE A 149     4603   4241   3975    -17    334   -107       C  
ATOM   1237  CD2 PHE A 149     -19.052  25.069  57.479  1.00 33.14           C  
ANISOU 1237  CD2 PHE A 149     4567   4151   3875    -61    419   -139       C  
ATOM   1238  CE1 PHE A 149     -19.076  25.108  54.706  1.00 32.95           C  
ANISOU 1238  CE1 PHE A 149     4442   4160   3918     17    347   -127       C  
ATOM   1239  CE2 PHE A 149     -20.225  24.760  56.785  1.00 28.87           C  
ANISOU 1239  CE2 PHE A 149     3956   3631   3382    -27    437   -160       C  
ATOM   1240  CZ  PHE A 149     -20.232  24.779  55.398  1.00 32.74           C  
ANISOU 1240  CZ  PHE A 149     4395   4137   3905     12    397   -153       C  
ATOM   1241  N   ASP A 150     -14.939  28.385  59.194  1.00 33.41           N  
ANISOU 1241  N   ASP A 150     4851   4100   3742   -167    332    -79       N  
ATOM   1242  CA  ASP A 150     -13.726  28.844  59.851  1.00 33.69           C  
ANISOU 1242  CA  ASP A 150     4949   4124   3730   -220    297    -57       C  
ATOM   1243  C   ASP A 150     -13.777  28.560  61.351  1.00 32.92           C  
ANISOU 1243  C   ASP A 150     4917   4009   3582   -272    317    -61       C  
ATOM   1244  O   ASP A 150     -14.730  28.955  62.021  1.00 30.91           O  
ANISOU 1244  O   ASP A 150     4700   3731   3314   -270    376    -93       O  
ATOM   1245  CB  ASP A 150     -13.548  30.349  59.597  1.00 33.52           C  
ANISOU 1245  CB  ASP A 150     4972   4072   3693   -214    302    -67       C  
ATOM   1246  CG  ASP A 150     -12.283  30.913  60.230  1.00 38.24           C  
ANISOU 1246  CG  ASP A 150     5633   4658   4238   -276    264    -45       C  
ATOM   1247  OD1 ASP A 150     -11.411  30.131  60.686  1.00 36.55           O  
ANISOU 1247  OD1 ASP A 150     5414   4465   4008   -318    222    -17       O  
ATOM   1248  OD2 ASP A 150     -12.161  32.157  60.256  1.00 38.87           O  
ANISOU 1248  OD2 ASP A 150     5769   4706   4295   -284    272    -56       O  
ATOM   1249  N   LEU A 151     -12.747  27.883  61.865  1.00 31.37           N  
ANISOU 1249  N   LEU A 151     4735   3825   3358   -318    268    -28       N  
ATOM   1250  CA  LEU A 151     -12.669  27.557  63.286  1.00 31.33           C  
ANISOU 1250  CA  LEU A 151     4801   3804   3298   -374    274    -25       C  
ATOM   1251  C   LEU A 151     -11.907  28.645  64.036  1.00 34.27           C  
ANISOU 1251  C   LEU A 151     5257   4150   3612   -426    255    -21       C  
ATOM   1252  O   LEU A 151     -10.755  28.956  63.708  1.00 34.92           O  
ANISOU 1252  O   LEU A 151     5332   4245   3690   -445    196      7       O  
ATOM   1253  CB  LEU A 151     -12.006  26.192  63.495  1.00 29.55           C  
ANISOU 1253  CB  LEU A 151     4553   3602   3074   -394    225     11       C  
ATOM   1254  CG  LEU A 151     -11.841  25.656  64.923  1.00 29.35           C  
ANISOU 1254  CG  LEU A 151     4602   3560   2988   -453    218     23       C  
ATOM   1255  CD1 LEU A 151     -13.194  25.491  65.606  1.00 26.12           C  
ANISOU 1255  CD1 LEU A 151     4229   3131   2565   -457    298    -14       C  
ATOM   1256  CD2 LEU A 151     -11.082  24.334  64.948  1.00 32.65           C  
ANISOU 1256  CD2 LEU A 151     4991   3998   3416   -461    159     64       C  
ATOM   1257  N   LEU A 152     -12.546  29.220  65.047  1.00 37.68           N  
ANISOU 1257  N   LEU A 152     5771   4547   3999   -451    308    -50       N  
ATOM   1258  CA  LEU A 152     -11.934  30.336  65.795  1.00 39.42           C  
ANISOU 1258  CA  LEU A 152     6085   4735   4156   -504    297    -52       C  
ATOM   1259  C   LEU A 152     -11.189  29.878  67.028  1.00 37.52           C  
ANISOU 1259  C   LEU A 152     5915   4492   3851   -580    255    -27       C  
ATOM   1260  O   LEU A 152     -10.261  30.553  67.474  1.00 39.05           O  
ANISOU 1260  O   LEU A 152     6167   4674   3998   -634    211    -13       O  
ATOM   1261  CB  LEU A 152     -12.967  31.412  66.177  1.00 37.81           C  
ANISOU 1261  CB  LEU A 152     5945   4487   3935   -490    378   -100       C  
ATOM   1262  CG  LEU A 152     -13.719  32.138  65.055  1.00 39.99           C  
ANISOU 1262  CG  LEU A 152     6169   4756   4269   -414    416   -125       C  
ATOM   1263  CD1 LEU A 152     -14.402  33.371  65.638  1.00 42.61           C  
ANISOU 1263  CD1 LEU A 152     6586   5034   4569   -410    484   -167       C  
ATOM   1264  CD2 LEU A 152     -12.814  32.535  63.880  1.00 36.53           C  
ANISOU 1264  CD2 LEU A 152     5684   4336   3860   -398    355    -99       C  
ATOM   1265  N   ASN A 153     -11.604  28.743  67.578  1.00 36.93           N  
ANISOU 1265  N   ASN A 153     5838   4425   3770   -588    267    -22       N  
ATOM   1266  CA  ASN A 153     -10.992  28.209  68.793  1.00 41.12           C  
ANISOU 1266  CA  ASN A 153     6442   4948   4234   -658    226      4       C  
ATOM   1267  C   ASN A 153     -10.505  26.783  68.611  1.00 42.38           C  
ANISOU 1267  C   ASN A 153     6542   5140   4420   -650    169     45       C  
ATOM   1268  O   ASN A 153     -11.272  25.897  68.211  1.00 41.19           O  
ANISOU 1268  O   ASN A 153     6338   5000   4311   -610    204     37       O  
ATOM   1269  CB  ASN A 153     -11.957  28.286  69.980  1.00 43.15           C  
ANISOU 1269  CB  ASN A 153     6794   5168   4432   -692    302    -30       C  
ATOM   1270  CG  ASN A 153     -12.418  29.707  70.279  1.00 47.08           C  
ANISOU 1270  CG  ASN A 153     7364   5626   4899   -699    363    -73       C  
ATOM   1271  OD1 ASN A 153     -11.707  30.682  70.022  1.00 50.66           O  
ANISOU 1271  OD1 ASN A 153     7837   6071   5342   -711    328    -68       O  
ATOM   1272  ND2 ASN A 153     -13.618  29.825  70.830  1.00 51.77           N  
ANISOU 1272  ND2 ASN A 153     7999   6193   5478   -691    458   -116       N  
ATOM   1273  N   SER A 154      -9.227  26.573  68.926  1.00 44.29           N  
ANISOU 1273  N   SER A 154     6794   5395   4637   -691     80     89       N  
ATOM   1274  CA  SER A 154      -8.542  25.301  68.707  1.00 43.22           C  
ANISOU 1274  CA  SER A 154     6601   5288   4531   -678     14    133       C  
ATOM   1275  C   SER A 154      -7.470  25.113  69.775  1.00 43.33           C  
ANISOU 1275  C   SER A 154     6680   5299   4484   -745    -68    175       C  
ATOM   1276  O   SER A 154      -6.978  26.098  70.312  1.00 45.88           O  
ANISOU 1276  O   SER A 154     7065   5611   4757   -797    -90    173       O  
ATOM   1277  CB  SER A 154      -7.898  25.315  67.318  1.00 42.34           C  
ANISOU 1277  CB  SER A 154     6379   5213   4494   -625    -21    148       C  
ATOM   1278  OG  SER A 154      -6.874  24.343  67.207  1.00 45.63           O  
ANISOU 1278  OG  SER A 154     6747   5657   4933   -621    -98    195       O  
ATOM   1279  N   PRO A 155      -7.098  23.853  70.086  1.00 43.59           N  
ANISOU 1279  N   PRO A 155     6702   5341   4519   -745   -118    213       N  
ATOM   1280  CA  PRO A 155      -5.949  23.621  70.968  1.00 44.47           C  
ANISOU 1280  CA  PRO A 155     6858   5455   4582   -799   -215    261       C  
ATOM   1281  C   PRO A 155      -4.639  24.227  70.443  1.00 45.61           C  
ANISOU 1281  C   PRO A 155     6940   5634   4754   -804   -292    287       C  
ATOM   1282  O   PRO A 155      -3.681  24.366  71.207  1.00 45.78           O  
ANISOU 1282  O   PRO A 155     7003   5661   4732   -860   -373    321       O  
ATOM   1283  CB  PRO A 155      -5.844  22.089  71.029  1.00 43.18           C  
ANISOU 1283  CB  PRO A 155     6669   5296   4442   -772   -250    296       C  
ATOM   1284  CG  PRO A 155      -6.685  21.587  69.888  1.00 44.08           C  
ANISOU 1284  CG  PRO A 155     6699   5420   4630   -699   -183    270       C  
ATOM   1285  CD  PRO A 155      -7.778  22.589  69.743  1.00 43.42           C  
ANISOU 1285  CD  PRO A 155     6639   5320   4537   -699    -89    214       C  
ATOM   1286  N   TYR A 156      -4.605  24.600  69.163  1.00 45.69           N  
ANISOU 1286  N   TYR A 156     6857   5670   4834   -751   -267    272       N  
ATOM   1287  CA  TYR A 156      -3.405  25.197  68.574  1.00 46.48           C  
ANISOU 1287  CA  TYR A 156     6893   5803   4963   -758   -328    294       C  
ATOM   1288  C   TYR A 156      -3.479  26.723  68.443  1.00 46.84           C  
ANISOU 1288  C   TYR A 156     6977   5838   4983   -792   -296    262       C  
ATOM   1289  O   TYR A 156      -2.549  27.354  67.931  1.00 46.86           O  
ANISOU 1289  O   TYR A 156     6933   5866   5005   -807   -337    275       O  
ATOM   1290  CB  TYR A 156      -3.040  24.513  67.246  1.00 46.46           C  
ANISOU 1290  CB  TYR A 156     6762   5838   5051   -684   -336    307       C  
ATOM   1291  CG  TYR A 156      -2.813  23.022  67.399  1.00 49.18           C  
ANISOU 1291  CG  TYR A 156     7075   6190   5420   -652   -376    342       C  
ATOM   1292  CD1 TYR A 156      -2.083  22.515  68.480  1.00 53.24           C  
ANISOU 1292  CD1 TYR A 156     7634   6702   5894   -694   -456    384       C  
ATOM   1293  CD2 TYR A 156      -3.329  22.117  66.474  1.00 48.42           C  
ANISOU 1293  CD2 TYR A 156     6914   6099   5386   -581   -337    333       C  
ATOM   1294  CE1 TYR A 156      -1.880  21.147  68.637  1.00 53.84           C  
ANISOU 1294  CE1 TYR A 156     7689   6777   5991   -660   -495    419       C  
ATOM   1295  CE2 TYR A 156      -3.125  20.745  66.619  1.00 49.37           C  
ANISOU 1295  CE2 TYR A 156     7015   6218   5527   -551   -371    365       C  
ATOM   1296  CZ  TYR A 156      -2.402  20.270  67.701  1.00 53.32           C  
ANISOU 1296  CZ  TYR A 156     7560   6712   5988   -588   -450    408       C  
ATOM   1297  OH  TYR A 156      -2.196  18.918  67.854  1.00 56.25           O  
ANISOU 1297  OH  TYR A 156     7920   7075   6378   -554   -486    441       O  
ATOM   1298  N   GLY A 157      -4.578  27.304  68.923  1.00 46.02           N  
ANISOU 1298  N   GLY A 157     6959   5692   4835   -805   -220    219       N  
ATOM   1299  CA  GLY A 157      -4.702  28.756  69.031  1.00 45.53           C  
ANISOU 1299  CA  GLY A 157     6960   5604   4734   -842   -189    188       C  
ATOM   1300  C   GLY A 157      -6.119  29.276  68.868  1.00 45.45           C  
ANISOU 1300  C   GLY A 157     6988   5558   4725   -806    -82    134       C  
ATOM   1301  O   GLY A 157      -6.902  28.728  68.087  1.00 45.01           O  
ANISOU 1301  O   GLY A 157     6865   5510   4726   -738    -35    120       O  
ATOM   1302  N   ASN A 158      -6.446  30.327  69.621  1.00 43.54           N  
ANISOU 1302  N   ASN A 158     6853   5274   4418   -854    -47    105       N  
ATOM   1303  CA  ASN A 158      -7.711  31.041  69.474  1.00 44.18           C  
ANISOU 1303  CA  ASN A 158     6970   5316   4499   -818     54     52       C  
ATOM   1304  C   ASN A 158      -7.502  32.304  68.632  1.00 44.67           C  
ANISOU 1304  C   ASN A 158     7022   5368   4582   -804     65     36       C  
ATOM   1305  O   ASN A 158      -6.582  33.088  68.890  1.00 44.26           O  
ANISOU 1305  O   ASN A 158     7017   5310   4491   -865     17     48       O  
ATOM   1306  CB  ASN A 158      -8.311  31.402  70.840  1.00 46.39           C  
ANISOU 1306  CB  ASN A 158     7383   5547   4694   -872    102     24       C  
ATOM   1307  CG  ASN A 158      -8.597  30.179  71.709  1.00 48.70           C  
ANISOU 1307  CG  ASN A 158     7701   5844   4959   -891    100     38       C  
ATOM   1308  OD1 ASN A 158      -8.887  29.088  71.216  1.00 50.95           O  
ANISOU 1308  OD1 ASN A 158     7904   6156   5298   -843    100     52       O  
ATOM   1309  ND2 ASN A 158      -8.520  30.366  73.014  1.00 52.58           N  
ANISOU 1309  ND2 ASN A 158     8314   6302   5360   -966     97     35       N  
ATOM   1310  N   VAL A 159      -8.349  32.487  67.622  1.00 43.41           N  
ANISOU 1310  N   VAL A 159     6804   5206   4482   -728    123     10       N  
ATOM   1311  CA  VAL A 159      -8.164  33.561  66.648  1.00 44.35           C  
ANISOU 1311  CA  VAL A 159     6906   5317   4628   -705    128      0       C  
ATOM   1312  C   VAL A 159      -9.397  34.449  66.500  1.00 45.34           C  
ANISOU 1312  C   VAL A 159     7074   5395   4757   -658    217    -49       C  
ATOM   1313  O   VAL A 159     -10.487  34.093  66.949  1.00 46.77           O  
ANISOU 1313  O   VAL A 159     7270   5561   4940   -630    281    -77       O  
ATOM   1314  CB  VAL A 159      -7.751  33.004  65.254  1.00 44.11           C  
ANISOU 1314  CB  VAL A 159     6749   5335   4675   -652     95     25       C  
ATOM   1315  CG1 VAL A 159      -6.375  32.345  65.319  1.00 42.84           C  
ANISOU 1315  CG1 VAL A 159     6543   5220   4515   -696      6     73       C  
ATOM   1316  CG2 VAL A 159      -8.791  32.036  64.715  1.00 41.17           C  
ANISOU 1316  CG2 VAL A 159     6305   4979   4359   -577    138     13       C  
ATOM   1317  N   GLU A 160      -9.207  35.608  65.874  1.00 46.29           N  
ANISOU 1317  N   GLU A 160     7215   5491   4882   -651    222    -59       N  
ATOM   1318  CA  GLU A 160     -10.300  36.521  65.542  1.00 45.43           C  
ANISOU 1318  CA  GLU A 160     7139   5336   4788   -594    297   -101       C  
ATOM   1319  C   GLU A 160     -10.958  36.133  64.211  1.00 42.09           C  
ANISOU 1319  C   GLU A 160     6606   4939   4447   -503    313   -102       C  
ATOM   1320  O   GLU A 160     -10.377  35.389  63.424  1.00 39.19           O  
ANISOU 1320  O   GLU A 160     6151   4621   4120   -492    264    -70       O  
ATOM   1321  CB  GLU A 160      -9.788  37.968  65.495  1.00 46.79           C  
ANISOU 1321  CB  GLU A 160     7397   5461   4920   -630    292   -109       C  
ATOM   1322  CG  GLU A 160      -9.339  38.527  66.859  1.00 56.16           C  
ANISOU 1322  CG  GLU A 160     8712   6609   6016   -721    287   -118       C  
ATOM   1323  CD  GLU A 160     -10.466  38.560  67.889  1.00 62.63           C  
ANISOU 1323  CD  GLU A 160     9607   7386   6802   -709    369   -160       C  
ATOM   1324  OE1 GLU A 160     -11.544  39.112  67.576  1.00 66.10           O  
ANISOU 1324  OE1 GLU A 160    10055   7789   7271   -638    443   -197       O  
ATOM   1325  OE2 GLU A 160     -10.278  38.036  69.011  1.00 65.04           O  
ANISOU 1325  OE2 GLU A 160     9964   7695   7054   -769    359   -156       O  
ATOM   1326  N   GLU A 161     -12.165  36.643  63.966  1.00 41.73           N  
ANISOU 1326  N   GLU A 161     6568   4861   4428   -437    382   -139       N  
ATOM   1327  CA  GLU A 161     -12.878  36.387  62.714  1.00 42.27           C  
ANISOU 1327  CA  GLU A 161     6540   4950   4570   -351    394   -142       C  
ATOM   1328  C   GLU A 161     -12.116  36.927  61.517  1.00 41.41           C  
ANISOU 1328  C   GLU A 161     6404   4848   4481   -343    346   -118       C  
ATOM   1329  O   GLU A 161     -11.414  37.931  61.614  1.00 41.48           O  
ANISOU 1329  O   GLU A 161     6485   4825   4450   -386    329   -113       O  
ATOM   1330  CB  GLU A 161     -14.277  37.007  62.738  1.00 43.17           C  
ANISOU 1330  CB  GLU A 161     6673   5024   4707   -283    472   -185       C  
ATOM   1331  CG  GLU A 161     -15.334  36.151  63.418  1.00 41.68           C  
ANISOU 1331  CG  GLU A 161     6455   4849   4533   -263    529   -209       C  
ATOM   1332  CD  GLU A 161     -16.734  36.753  63.367  1.00 44.44           C  
ANISOU 1332  CD  GLU A 161     6803   5166   4917   -188    608   -253       C  
ATOM   1333  OE1 GLU A 161     -17.092  37.423  62.372  1.00 43.69           O  
ANISOU 1333  OE1 GLU A 161     6679   5056   4863   -123    606   -257       O  
ATOM   1334  OE2 GLU A 161     -17.494  36.535  64.332  1.00 51.11           O  
ANISOU 1334  OE2 GLU A 161     7675   5999   5747   -193    673   -283       O  
ATOM   1335  N   TRP A 162     -12.259  36.234  60.396  1.00 41.14           N  
ANISOU 1335  N   TRP A 162     6271   4855   4505   -293    326   -103       N  
ATOM   1336  CA  TRP A 162     -11.703  36.663  59.117  1.00 40.16           C  
ANISOU 1336  CA  TRP A 162     6116   4740   4404   -276    290    -82       C  
ATOM   1337  C   TRP A 162     -12.437  37.904  58.628  1.00 39.79           C  
ANISOU 1337  C   TRP A 162     6116   4638   4363   -226    325   -106       C  
ATOM   1338  O   TRP A 162     -13.634  38.061  58.858  1.00 38.20           O  
ANISOU 1338  O   TRP A 162     5919   4413   4182   -170    376   -136       O  
ATOM   1339  CB  TRP A 162     -11.832  35.514  58.123  1.00 39.35           C  
ANISOU 1339  CB  TRP A 162     5902   4690   4357   -234    269    -66       C  
ATOM   1340  CG  TRP A 162     -11.545  35.814  56.688  1.00 37.12           C  
ANISOU 1340  CG  TRP A 162     5582   4417   4104   -203    243    -50       C  
ATOM   1341  CD1 TRP A 162     -10.320  35.870  56.090  1.00 37.38           C  
ANISOU 1341  CD1 TRP A 162     5601   4472   4128   -243    199    -21       C  
ATOM   1342  CD2 TRP A 162     -12.509  36.042  55.656  1.00 34.35           C  
ANISOU 1342  CD2 TRP A 162     5199   4057   3794   -128    260    -62       C  
ATOM   1343  NE1 TRP A 162     -10.461  36.126  54.746  1.00 37.16           N  
ANISOU 1343  NE1 TRP A 162     5543   4446   4129   -201    192    -15       N  
ATOM   1344  CE2 TRP A 162     -11.796  36.244  54.455  1.00 35.34           C  
ANISOU 1344  CE2 TRP A 162     5304   4195   3927   -130    224    -39       C  
ATOM   1345  CE3 TRP A 162     -13.909  36.108  55.632  1.00 33.40           C  
ANISOU 1345  CE3 TRP A 162     5064   3921   3706    -61    300    -91       C  
ATOM   1346  CZ2 TRP A 162     -12.435  36.508  53.237  1.00 34.27           C  
ANISOU 1346  CZ2 TRP A 162     5144   4053   3823    -68    223    -41       C  
ATOM   1347  CZ3 TRP A 162     -14.546  36.361  54.424  1.00 34.81           C  
ANISOU 1347  CZ3 TRP A 162     5207   4096   3922      4    294    -91       C  
ATOM   1348  CH2 TRP A 162     -13.806  36.559  53.240  1.00 35.98           C  
ANISOU 1348  CH2 TRP A 162     5347   4254   4071     -1    253    -66       C  
ATOM   1349  N   SER A 163     -11.704  38.794  57.973  1.00 40.84           N  
ANISOU 1349  N   SER A 163     6285   4751   4480   -245    297    -90       N  
ATOM   1350  CA  SER A 163     -12.274  40.048  57.503  1.00 41.95           C  
ANISOU 1350  CA  SER A 163     6486   4832   4621   -201    323   -108       C  
ATOM   1351  C   SER A 163     -12.263  40.107  55.990  1.00 41.96           C  
ANISOU 1351  C   SER A 163     6435   4848   4661   -155    296    -89       C  
ATOM   1352  O   SER A 163     -11.197  40.159  55.366  1.00 43.31           O  
ANISOU 1352  O   SER A 163     6598   5038   4819   -200    255    -61       O  
ATOM   1353  CB  SER A 163     -11.525  41.241  58.090  1.00 40.78           C  
ANISOU 1353  CB  SER A 163     6454   4631   4409   -268    321   -110       C  
ATOM   1354  OG  SER A 163     -11.802  42.412  57.344  1.00 45.98           O  
ANISOU 1354  OG  SER A 163     7169   5234   5069   -230    331   -115       O  
ATOM   1355  N   ILE A 164     -13.461  40.097  55.417  1.00 41.97           N  
ANISOU 1355  N   ILE A 164     6400   4840   4707    -68    319   -104       N  
ATOM   1356  CA  ILE A 164     -13.660  40.173  53.971  1.00 41.44           C  
ANISOU 1356  CA  ILE A 164     6289   4781   4674    -17    293    -89       C  
ATOM   1357  C   ILE A 164     -13.145  41.501  53.405  1.00 43.46           C  
ANISOU 1357  C   ILE A 164     6633   4982   4898    -30    279    -78       C  
ATOM   1358  O   ILE A 164     -12.683  41.557  52.260  1.00 45.52           O  
ANISOU 1358  O   ILE A 164     6877   5256   5163    -31    246    -54       O  
ATOM   1359  CB  ILE A 164     -15.161  39.919  53.588  1.00 40.77           C  
ANISOU 1359  CB  ILE A 164     6148   4698   4646     80    316   -109       C  
ATOM   1360  CG1 ILE A 164     -15.342  39.786  52.066  1.00 40.33           C  
ANISOU 1360  CG1 ILE A 164     6041   4660   4623    127    279    -90       C  
ATOM   1361  CG2 ILE A 164     -16.089  41.002  54.183  1.00 41.17           C  
ANISOU 1361  CG2 ILE A 164     6267   4681   4694    128    364   -140       C  
ATOM   1362  CD1 ILE A 164     -16.635  39.061  51.642  1.00 36.06           C  
ANISOU 1362  CD1 ILE A 164     5410   4149   4141    203    285   -103       C  
ATOM   1363  N   GLU A 165     -13.205  42.562  54.211  1.00 43.83           N  
ANISOU 1363  N   GLU A 165     6781   4965   4907    -46    308    -96       N  
ATOM   1364  CA  GLU A 165     -12.740  43.880  53.776  1.00 43.00           C  
ANISOU 1364  CA  GLU A 165     6775   4798   4765    -65    299    -88       C  
ATOM   1365  C   GLU A 165     -11.236  43.860  53.570  1.00 39.53           C  
ANISOU 1365  C   GLU A 165     6347   4386   4288   -163    260    -58       C  
ATOM   1366  O   GLU A 165     -10.738  44.395  52.580  1.00 39.95           O  
ANISOU 1366  O   GLU A 165     6424   4425   4331   -175    237    -37       O  
ATOM   1367  CB  GLU A 165     -13.119  44.988  54.778  1.00 47.45           C  
ANISOU 1367  CB  GLU A 165     7453   5281   5293    -65    342   -117       C  
ATOM   1368  CG  GLU A 165     -14.621  45.149  55.044  1.00 54.25           C  
ANISOU 1368  CG  GLU A 165     8307   6111   6196     37    391   -151       C  
ATOM   1369  CD  GLU A 165     -15.157  44.151  56.073  1.00 59.92           C  
ANISOU 1369  CD  GLU A 165     8965   6871   6932     38    426   -174       C  
ATOM   1370  OE1 GLU A 165     -14.379  43.295  56.557  1.00 59.98           O  
ANISOU 1370  OE1 GLU A 165     8939   6931   6919    -34    406   -161       O  
ATOM   1371  OE2 GLU A 165     -16.365  44.220  56.399  1.00 63.35           O  
ANISOU 1371  OE2 GLU A 165     9384   7285   7400    113    473   -204       O  
ATOM   1372  N   ILE A 166     -10.515  43.250  54.507  1.00 38.84           N  
ANISOU 1372  N   ILE A 166     6242   4336   4179   -234    253    -56       N  
ATOM   1373  CA  ILE A 166      -9.055  43.157  54.404  1.00 37.74           C  
ANISOU 1373  CA  ILE A 166     6098   4231   4010   -329    214    -28       C  
ATOM   1374  C   ILE A 166      -8.660  42.186  53.296  1.00 35.29           C  
ANISOU 1374  C   ILE A 166     5680   3989   3740   -315    184     -2       C  
ATOM   1375  O   ILE A 166      -7.702  42.427  52.576  1.00 36.22           O  
ANISOU 1375  O   ILE A 166     5797   4121   3845   -362    161     21       O  
ATOM   1376  CB  ILE A 166      -8.380  42.760  55.750  1.00 37.73           C  
ANISOU 1376  CB  ILE A 166     6108   4253   3976   -407    206    -30       C  
ATOM   1377  CG1 ILE A 166      -8.625  43.836  56.812  1.00 37.50           C  
ANISOU 1377  CG1 ILE A 166     6203   4150   3894   -435    235    -56       C  
ATOM   1378  CG2 ILE A 166      -6.872  42.546  55.563  1.00 36.71           C  
ANISOU 1378  CG2 ILE A 166     5947   4171   3829   -497    159      2       C  
ATOM   1379  CD1 ILE A 166      -8.108  43.482  58.208  1.00 37.93           C  
ANISOU 1379  CD1 ILE A 166     6282   4220   3908   -511    227    -60       C  
ATOM   1380  N   ALA A 167      -9.421  41.105  53.163  1.00 34.32           N  
ANISOU 1380  N   ALA A 167     5472   3906   3664   -253    191     -8       N  
ATOM   1381  CA  ALA A 167      -9.186  40.090  52.146  1.00 35.02           C  
ANISOU 1381  CA  ALA A 167     5462   4054   3790   -233    168     11       C  
ATOM   1382  C   ALA A 167      -9.315  40.647  50.725  1.00 37.31           C  
ANISOU 1382  C   ALA A 167     5764   4325   4087   -199    160     22       C  
ATOM   1383  O   ALA A 167      -8.594  40.215  49.819  1.00 36.42           O  
ANISOU 1383  O   ALA A 167     5605   4251   3982   -219    140     43       O  
ATOM   1384  CB  ALA A 167     -10.137  38.916  52.346  1.00 32.61           C  
ANISOU 1384  CB  ALA A 167     5079   3783   3529   -175    180     -2       C  
ATOM   1385  N   ALA A 168     -10.231  41.598  50.538  1.00 39.08           N  
ANISOU 1385  N   ALA A 168     6053   4488   4308   -146    177      8       N  
ATOM   1386  CA  ALA A 168     -10.418  42.245  49.238  1.00 41.91           C  
ANISOU 1386  CA  ALA A 168     6441   4817   4667   -112    164     20       C  
ATOM   1387  C   ALA A 168      -9.282  43.198  48.880  1.00 44.06           C  
ANISOU 1387  C   ALA A 168     6789   5062   4890   -187    153     40       C  
ATOM   1388  O   ALA A 168      -9.014  43.416  47.698  1.00 45.22           O  
ANISOU 1388  O   ALA A 168     6943   5207   5032   -186    139     58       O  
ATOM   1389  CB  ALA A 168     -11.749  42.979  49.185  1.00 42.94           C  
ANISOU 1389  CB  ALA A 168     6616   4887   4812    -26    180      2       C  
ATOM   1390  N   LYS A 169      -8.620  43.759  49.893  1.00 45.23           N  
ANISOU 1390  N   LYS A 169     6997   5188   5000   -257    161     35       N  
ATOM   1391  CA  LYS A 169      -7.587  44.784  49.671  1.00 46.02           C  
ANISOU 1391  CA  LYS A 169     7178   5255   5050   -337    153     50       C  
ATOM   1392  C   LYS A 169      -6.338  44.227  48.992  1.00 45.58           C  
ANISOU 1392  C   LYS A 169     7059   5264   4994   -404    133     76       C  
ATOM   1393  O   LYS A 169      -6.019  43.042  49.132  1.00 44.90           O  
ANISOU 1393  O   LYS A 169     6873   5249   4939   -408    124     81       O  
ATOM   1394  CB  LYS A 169      -7.194  45.471  50.985  1.00 45.82           C  
ANISOU 1394  CB  LYS A 169     7233   5193   4982   -403    163     37       C  
ATOM   1395  CG  LYS A 169      -8.272  46.333  51.610  1.00 48.53           C  
ANISOU 1395  CG  LYS A 169     7669   5456   5315   -348    193      9       C  
ATOM   1396  CD  LYS A 169      -7.682  47.243  52.685  1.00 54.46           C  
ANISOU 1396  CD  LYS A 169     8526   6158   6007   -431    202     -2       C  
ATOM   1397  CE  LYS A 169      -8.765  47.899  53.545  1.00 59.37           C  
ANISOU 1397  CE  LYS A 169     9233   6706   6621   -376    242    -37       C  
ATOM   1398  NZ  LYS A 169      -9.700  48.752  52.751  1.00 59.25           N  
ANISOU 1398  NZ  LYS A 169     9275   6619   6619   -287    258    -42       N  
ATOM   1399  N   LEU A 170      -5.629  45.097  48.272  1.00 46.36           N  
ANISOU 1399  N   LEU A 170     7220   5337   5059   -456    129     93       N  
ATOM   1400  CA  LEU A 170      -4.366  44.732  47.621  1.00 46.69           C  
ANISOU 1400  CA  LEU A 170     7208   5435   5096   -529    118    116       C  
ATOM   1401  C   LEU A 170      -3.324  44.329  48.654  1.00 46.34           C  
ANISOU 1401  C   LEU A 170     7119   5441   5048   -611    106    119       C  
ATOM   1402  O   LEU A 170      -3.360  44.799  49.792  1.00 47.27           O  
ANISOU 1402  O   LEU A 170     7292   5527   5140   -642    105    107       O  
ATOM   1403  CB  LEU A 170      -3.821  45.912  46.820  1.00 48.02           C  
ANISOU 1403  CB  LEU A 170     7470   5556   5219   -582    122    131       C  
ATOM   1404  CG  LEU A 170      -4.756  46.736  45.930  1.00 51.67           C  
ANISOU 1404  CG  LEU A 170     8021   5945   5668   -516    127    132       C  
ATOM   1405  CD1 LEU A 170      -4.036  48.005  45.472  1.00 55.44           C  
ANISOU 1405  CD1 LEU A 170     8610   6366   6088   -594    132    146       C  
ATOM   1406  CD2 LEU A 170      -5.256  45.931  44.737  1.00 49.61           C  
ANISOU 1406  CD2 LEU A 170     7691   5718   5440   -446    121    140       C  
ATOM   1407  N   GLN A 171      -2.387  43.476  48.259  1.00 46.29           N  
ANISOU 1407  N   GLN A 171     7015   5509   5064   -647     97    136       N  
ATOM   1408  CA  GLN A 171      -1.307  43.076  49.159  1.00 49.22           C  
ANISOU 1408  CA  GLN A 171     7334   5932   5436   -724     77    144       C  
ATOM   1409  C   GLN A 171      -0.477  44.275  49.642  1.00 49.45           C  
ANISOU 1409  C   GLN A 171     7449   5928   5412   -828     70    149       C  
ATOM   1410  O   GLN A 171       0.107  44.242  50.722  1.00 48.68           O  
ANISOU 1410  O   GLN A 171     7346   5849   5302   -891     48    150       O  
ATOM   1411  CB  GLN A 171      -0.424  41.994  48.524  1.00 51.36           C  
ANISOU 1411  CB  GLN A 171     7482   6287   5747   -736     72    162       C  
ATOM   1412  CG  GLN A 171      -1.167  40.672  48.290  1.00 58.00           C  
ANISOU 1412  CG  GLN A 171     8238   7162   6637   -643     74    155       C  
ATOM   1413  CD  GLN A 171      -0.280  39.434  48.377  1.00 65.14           C  
ANISOU 1413  CD  GLN A 171     9021   8147   7582   -657     61    169       C  
ATOM   1414  OE1 GLN A 171       0.948  39.514  48.272  1.00 68.44           O  
ANISOU 1414  OE1 GLN A 171     9401   8605   8000   -728     54    185       O  
ATOM   1415  NE2 GLN A 171      -0.911  38.274  48.570  1.00 65.56           N  
ANISOU 1415  NE2 GLN A 171     9014   8224   7673   -588     58    162       N  
ATOM   1416  N   GLU A 172      -0.479  45.343  48.847  1.00 49.32           N  
ANISOU 1416  N   GLU A 172     7520   5858   5362   -848     86    152       N  
ATOM   1417  CA  GLU A 172       0.266  46.559  49.134  1.00 49.24           C  
ANISOU 1417  CA  GLU A 172     7605   5807   5298   -951     83    156       C  
ATOM   1418  C   GLU A 172      -0.472  47.434  50.145  1.00 50.59           C  
ANISOU 1418  C   GLU A 172     7896   5896   5430   -943     86    135       C  
ATOM   1419  O   GLU A 172       0.099  48.375  50.711  1.00 50.01           O  
ANISOU 1419  O   GLU A 172     7909   5785   5308  -1033     80    134       O  
ATOM   1420  CB  GLU A 172       0.521  47.330  47.833  1.00 51.45           C  
ANISOU 1420  CB  GLU A 172     7939   6056   5554   -974    102    169       C  
ATOM   1421  CG  GLU A 172       1.434  46.606  46.830  1.00 54.17           C  
ANISOU 1421  CG  GLU A 172     8176   6479   5927  -1002    109    189       C  
ATOM   1422  CD  GLU A 172       0.710  45.587  45.944  1.00 59.39           C  
ANISOU 1422  CD  GLU A 172     8763   7169   6632   -896    120    188       C  
ATOM   1423  OE1 GLU A 172       1.391  44.871  45.171  1.00 58.93           O  
ANISOU 1423  OE1 GLU A 172     8615   7175   6600   -909    130    200       O  
ATOM   1424  OE2 GLU A 172      -0.534  45.501  46.014  1.00 60.71           O  
ANISOU 1424  OE2 GLU A 172     8962   7296   6810   -803    120    174       O  
ATOM   1425  N   GLN A 173      -1.748  47.124  50.364  1.00 49.92           N  
ANISOU 1425  N   GLN A 173     7818   5782   5367   -838     98    116       N  
ATOM   1426  CA  GLN A 173      -2.538  47.785  51.397  1.00 49.14           C  
ANISOU 1426  CA  GLN A 173     7819   5612   5241   -818    110     91       C  
ATOM   1427  C   GLN A 173      -2.590  46.913  52.638  1.00 47.02           C  
ANISOU 1427  C   GLN A 173     7493   5386   4986   -819     98     80       C  
ATOM   1428  O   GLN A 173      -3.259  47.256  53.617  1.00 47.86           O  
ANISOU 1428  O   GLN A 173     7670   5443   5072   -801    112     57       O  
ATOM   1429  CB  GLN A 173      -3.963  48.043  50.913  1.00 50.93           C  
ANISOU 1429  CB  GLN A 173     8089   5778   5486   -699    135     76       C  
ATOM   1430  CG  GLN A 173      -4.124  49.187  49.949  1.00 53.00           C  
ANISOU 1430  CG  GLN A 173     8452   5966   5719   -692    145     83       C  
ATOM   1431  CD  GLN A 173      -5.560  49.341  49.514  1.00 57.27           C  
ANISOU 1431  CD  GLN A 173     9019   6455   6286   -565    161     70       C  
ATOM   1432  OE1 GLN A 173      -6.020  48.650  48.600  1.00 58.49           O  
ANISOU 1432  OE1 GLN A 173     9097   6645   6481   -497    154     80       O  
ATOM   1433  NE2 GLN A 173      -6.289  50.243  50.175  1.00 57.17           N  
ANISOU 1433  NE2 GLN A 173     9114   6357   6251   -533    181     48       N  
ATOM   1434  N   GLY A 174      -1.882  45.788  52.589  1.00 43.87           N  
ANISOU 1434  N   GLY A 174     6971   5076   4622   -840     74     98       N  
ATOM   1435  CA  GLY A 174      -1.847  44.848  53.703  1.00 42.30           C  
ANISOU 1435  CA  GLY A 174     6713   4923   4437   -843     56     94       C  
ATOM   1436  C   GLY A 174      -2.887  43.755  53.571  1.00 41.37           C  
ANISOU 1436  C   GLY A 174     6521   4829   4371   -735     70     84       C  
ATOM   1437  O   GLY A 174      -3.011  42.900  54.449  1.00 39.46           O  
ANISOU 1437  O   GLY A 174     6233   4620   4141   -728     60     80       O  
ATOM   1438  N   GLY A 175      -3.634  43.789  52.468  1.00 40.64           N  
ANISOU 1438  N   GLY A 175     6419   4719   4304   -657     92     81       N  
ATOM   1439  CA  GLY A 175      -4.703  42.828  52.221  1.00 39.83           C  
ANISOU 1439  CA  GLY A 175     6249   4636   4250   -557    105     71       C  
ATOM   1440  C   GLY A 175      -4.222  41.534  51.598  1.00 38.93           C  
ANISOU 1440  C   GLY A 175     6009   4601   4180   -545     88     89       C  
ATOM   1441  O   GLY A 175      -3.021  41.326  51.426  1.00 36.76           O  
ANISOU 1441  O   GLY A 175     5691   4373   3904   -611     68    110       O  
ATOM   1442  N   ASP A 176      -5.171  40.671  51.244  1.00 40.41           N  
ANISOU 1442  N   ASP A 176     6140   4806   4410   -460     99     81       N  
ATOM   1443  CA  ASP A 176      -4.862  39.323  50.751  1.00 41.40           C  
ANISOU 1443  CA  ASP A 176     6152   5000   4578   -440     88     94       C  
ATOM   1444  C   ASP A 176      -5.092  39.165  49.251  1.00 43.39           C  
ANISOU 1444  C   ASP A 176     6375   5260   4851   -394     95    100       C  
ATOM   1445  O   ASP A 176      -4.798  38.110  48.681  1.00 43.84           O  
ANISOU 1445  O   ASP A 176     6347   5369   4941   -378     90    109       O  
ATOM   1446  CB  ASP A 176      -5.682  38.284  51.514  1.00 39.99           C  
ANISOU 1446  CB  ASP A 176     5929   4840   4427   -390     92     80       C  
ATOM   1447  CG  ASP A 176      -5.496  38.384  53.027  1.00 40.16           C  
ANISOU 1447  CG  ASP A 176     5988   4852   4420   -437     86     74       C  
ATOM   1448  OD1 ASP A 176      -4.347  38.574  53.477  1.00 37.68           O  
ANISOU 1448  OD1 ASP A 176     5679   4556   4083   -515     60     90       O  
ATOM   1449  OD2 ASP A 176      -6.503  38.270  53.761  1.00 39.45           O  
ANISOU 1449  OD2 ASP A 176     5923   4737   4331   -400    106     52       O  
ATOM   1450  N   GLU A 177      -5.634  40.207  48.625  1.00 45.40           N  
ANISOU 1450  N   GLU A 177     6704   5459   5085   -371    106     95       N  
ATOM   1451  CA  GLU A 177      -5.815  40.249  47.174  1.00 48.77           C  
ANISOU 1451  CA  GLU A 177     7125   5885   5520   -337    108    104       C  
ATOM   1452  C   GLU A 177      -6.676  39.080  46.665  1.00 47.69           C  
ANISOU 1452  C   GLU A 177     6911   5780   5428   -260    107     97       C  
ATOM   1453  O   GLU A 177      -6.375  38.477  45.633  1.00 47.47           O  
ANISOU 1453  O   GLU A 177     6837   5787   5414   -253    105    107       O  
ATOM   1454  CB  GLU A 177      -4.445  40.267  46.487  1.00 51.30           C  
ANISOU 1454  CB  GLU A 177     7424   6241   5828   -408    105    125       C  
ATOM   1455  CG  GLU A 177      -4.337  41.143  45.256  1.00 57.38           C  
ANISOU 1455  CG  GLU A 177     8257   6976   6569   -417    112    136       C  
ATOM   1456  CD  GLU A 177      -2.889  41.371  44.852  1.00 62.52           C  
ANISOU 1456  CD  GLU A 177     8898   7656   7200   -507    117    154       C  
ATOM   1457  OE1 GLU A 177      -2.416  40.693  43.912  1.00 63.56           O  
ANISOU 1457  OE1 GLU A 177     8970   7833   7348   -508    126    163       O  
ATOM   1458  OE2 GLU A 177      -2.220  42.217  45.489  1.00 62.82           O  
ANISOU 1458  OE2 GLU A 177     8988   7675   7207   -580    115    158       O  
ATOM   1459  N   VAL A 178      -7.736  38.757  47.409  1.00 46.37           N  
ANISOU 1459  N   VAL A 178     6734   5603   5282   -208    112     78       N  
ATOM   1460  CA  VAL A 178      -8.753  37.808  46.946  1.00 44.19           C  
ANISOU 1460  CA  VAL A 178     6396   5348   5045   -136    112     68       C  
ATOM   1461  C   VAL A 178      -9.483  38.457  45.766  1.00 44.41           C  
ANISOU 1461  C   VAL A 178     6464   5341   5070    -86    106     70       C  
ATOM   1462  O   VAL A 178     -10.059  39.535  45.922  1.00 44.95           O  
ANISOU 1462  O   VAL A 178     6604   5352   5123    -63    109     63       O  
ATOM   1463  CB  VAL A 178      -9.758  37.442  48.067  1.00 42.17           C  
ANISOU 1463  CB  VAL A 178     6126   5086   4810    -98    125     46       C  
ATOM   1464  CG1 VAL A 178     -10.888  36.583  47.532  1.00 40.96           C  
ANISOU 1464  CG1 VAL A 178     5913   4953   4699    -28    124     35       C  
ATOM   1465  CG2 VAL A 178      -9.054  36.724  49.208  1.00 40.97           C  
ANISOU 1465  CG2 VAL A 178     5941   4968   4657   -148    125     47       C  
ATOM   1466  N   PRO A 179      -9.445  37.812  44.580  1.00 44.40           N  
ANISOU 1466  N   PRO A 179     6421   5369   5081    -68     95     79       N  
ATOM   1467  CA  PRO A 179      -9.997  38.384  43.346  1.00 43.13           C  
ANISOU 1467  CA  PRO A 179     6301   5177   4909    -30     80     86       C  
ATOM   1468  C   PRO A 179     -11.375  38.991  43.576  1.00 43.31           C  
ANISOU 1468  C   PRO A 179     6355   5154   4946     41     74     73       C  
ATOM   1469  O   PRO A 179     -12.248  38.337  44.153  1.00 44.70           O  
ANISOU 1469  O   PRO A 179     6477   5348   5159     84     79     55       O  
ATOM   1470  CB  PRO A 179     -10.099  37.172  42.425  1.00 43.31           C  
ANISOU 1470  CB  PRO A 179     6254   5248   4954     -9     71     88       C  
ATOM   1471  CG  PRO A 179      -8.982  36.298  42.854  1.00 44.48           C  
ANISOU 1471  CG  PRO A 179     6345   5447   5110    -62     86     92       C  
ATOM   1472  CD  PRO A 179      -8.899  36.460  44.353  1.00 43.54           C  
ANISOU 1472  CD  PRO A 179     6227   5321   4994    -82     95     83       C  
ATOM   1473  N   SER A 180     -11.555  40.238  43.152  1.00 41.19           N  
ANISOU 1473  N   SER A 180     6174   4826   4650     53     67     81       N  
ATOM   1474  CA  SER A 180     -12.791  40.964  43.413  1.00 43.15           C  
ANISOU 1474  CA  SER A 180     6458   5024   4914    125     63     68       C  
ATOM   1475  C   SER A 180     -14.031  40.274  42.840  1.00 43.08           C  
ANISOU 1475  C   SER A 180     6383   5037   4949    203     41     61       C  
ATOM   1476  O   SER A 180     -15.129  40.421  43.382  1.00 42.50           O  
ANISOU 1476  O   SER A 180     6292   4947   4909    264     46     43       O  
ATOM   1477  CB  SER A 180     -12.701  42.419  42.914  1.00 47.25           C  
ANISOU 1477  CB  SER A 180     7090   5469   5393    127     53     83       C  
ATOM   1478  OG  SER A 180     -12.272  42.505  41.562  1.00 46.10           O  
ANISOU 1478  OG  SER A 180     6971   5324   5221    110     30    107       O  
ATOM   1479  N   GLU A 181     -13.852  39.512  41.763  1.00 41.06           N  
ANISOU 1479  N   GLU A 181     6088   4820   4694    198     19     74       N  
ATOM   1480  CA  GLU A 181     -14.988  38.886  41.083  1.00 42.03           C  
ANISOU 1480  CA  GLU A 181     6155   4963   4851    263    -10     70       C  
ATOM   1481  C   GLU A 181     -15.665  37.759  41.878  1.00 39.76           C  
ANISOU 1481  C   GLU A 181     5772   4723   4614    284      4     46       C  
ATOM   1482  O   GLU A 181     -16.716  37.272  41.471  1.00 42.59           O  
ANISOU 1482  O   GLU A 181     6078   5099   5005    336    -18     39       O  
ATOM   1483  CB  GLU A 181     -14.606  38.420  39.665  1.00 43.04           C  
ANISOU 1483  CB  GLU A 181     6284   5114   4957    245    -38     88       C  
ATOM   1484  CG  GLU A 181     -13.697  37.198  39.597  1.00 45.38           C  
ANISOU 1484  CG  GLU A 181     6522   5469   5252    191    -19     86       C  
ATOM   1485  CD  GLU A 181     -12.211  37.542  39.610  1.00 48.21           C  
ANISOU 1485  CD  GLU A 181     6922   5826   5570    115      6    100       C  
ATOM   1486  OE1 GLU A 181     -11.854  38.716  39.844  1.00 45.47           O  
ANISOU 1486  OE1 GLU A 181     6649   5433   5194     95     12    108       O  
ATOM   1487  OE2 GLU A 181     -11.393  36.623  39.377  1.00 48.86           O  
ANISOU 1487  OE2 GLU A 181     6960   5953   5652     75     20    101       O  
ATOM   1488  N   ILE A 182     -15.064  37.345  42.995  1.00 35.50           N  
ANISOU 1488  N   ILE A 182     5210   4203   4075    240     39     35       N  
ATOM   1489  CA  ILE A 182     -15.665  36.332  43.862  1.00 34.94           C  
ANISOU 1489  CA  ILE A 182     5061   4169   4043    253     57     14       C  
ATOM   1490  C   ILE A 182     -16.037  36.838  45.266  1.00 34.65           C  
ANISOU 1490  C   ILE A 182     5043   4107   4015    260     92     -6       C  
ATOM   1491  O   ILE A 182     -16.720  36.141  46.007  1.00 37.20           O  
ANISOU 1491  O   ILE A 182     5310   4454   4371    276    112    -25       O  
ATOM   1492  CB  ILE A 182     -14.785  35.045  44.004  1.00 34.84           C  
ANISOU 1492  CB  ILE A 182     4997   4211   4031    199     66     17       C  
ATOM   1493  CG1 ILE A 182     -13.584  35.291  44.932  1.00 34.17           C  
ANISOU 1493  CG1 ILE A 182     4943   4122   3918    136     88     22       C  
ATOM   1494  CG2 ILE A 182     -14.375  34.484  42.625  1.00 34.58           C  
ANISOU 1494  CG2 ILE A 182     4950   4202   3987    190     40     32       C  
ATOM   1495  CD1 ILE A 182     -13.014  34.019  45.546  1.00 33.55           C  
ANISOU 1495  CD1 ILE A 182     4805   4090   3851    100     99     21       C  
ATOM   1496  N   ILE A 183     -15.591  38.038  45.623  1.00 34.79           N  
ANISOU 1496  N   ILE A 183     5143   4074   4000    244    103     -2       N  
ATOM   1497  CA  ILE A 183     -15.853  38.608  46.945  1.00 38.60           C  
ANISOU 1497  CA  ILE A 183     5660   4525   4481    245    140    -22       C  
ATOM   1498  C   ILE A 183     -17.339  38.556  47.328  1.00 40.97           C  
ANISOU 1498  C   ILE A 183     5919   4819   4828    319    157    -48       C  
ATOM   1499  O   ILE A 183     -17.692  38.202  48.461  1.00 41.47           O  
ANISOU 1499  O   ILE A 183     5959   4892   4905    314    195    -70       O  
ATOM   1500  CB  ILE A 183     -15.307  40.066  47.048  1.00 40.11           C  
ANISOU 1500  CB  ILE A 183     5962   4650   4629    225    144    -15       C  
ATOM   1501  CG1 ILE A 183     -13.773  40.064  47.161  1.00 40.80           C  
ANISOU 1501  CG1 ILE A 183     6081   4750   4672    133    141      3       C  
ATOM   1502  CG2 ILE A 183     -15.978  40.841  48.197  1.00 37.98           C  
ANISOU 1502  CG2 ILE A 183     5738   4331   4362    253    183    -41       C  
ATOM   1503  CD1 ILE A 183     -13.205  39.480  48.476  1.00 40.58           C  
ANISOU 1503  CD1 ILE A 183     6034   4750   4636     77    164     -7       C  
ATOM   1504  N   ASP A 184     -18.198  38.895  46.368  1.00 41.86           N  
ANISOU 1504  N   ASP A 184     6020   4919   4967    386    129    -43       N  
ATOM   1505  CA  ASP A 184     -19.640  38.909  46.574  1.00 41.58           C  
ANISOU 1505  CA  ASP A 184     5934   4882   4984    463    140    -65       C  
ATOM   1506  C   ASP A 184     -20.221  37.504  46.682  1.00 39.09           C  
ANISOU 1506  C   ASP A 184     5512   4633   4709    464    143    -77       C  
ATOM   1507  O   ASP A 184     -21.375  37.347  47.056  1.00 38.81           O  
ANISOU 1507  O   ASP A 184     5420   4607   4719    514    162   -100       O  
ATOM   1508  CB  ASP A 184     -20.333  39.684  45.441  1.00 44.95           C  
ANISOU 1508  CB  ASP A 184     6378   5276   5425    535     97    -51       C  
ATOM   1509  CG  ASP A 184     -20.234  41.207  45.611  1.00 51.23           C  
ANISOU 1509  CG  ASP A 184     7279   5989   6195    560    106    -48       C  
ATOM   1510  OD1 ASP A 184     -20.040  41.682  46.753  1.00 56.66           O  
ANISOU 1510  OD1 ASP A 184     8013   6646   6869    542    155    -67       O  
ATOM   1511  OD2 ASP A 184     -20.363  41.935  44.602  1.00 54.42           O  
ANISOU 1511  OD2 ASP A 184     7729   6357   6590    597     64    -27       O  
ATOM   1512  N   LYS A 185     -19.415  36.491  46.362  1.00 37.23           N  
ANISOU 1512  N   LYS A 185     5249   4442   4457    407    128    -64       N  
ATOM   1513  CA  LYS A 185     -19.877  35.097  46.323  1.00 35.30           C  
ANISOU 1513  CA  LYS A 185     4913   4255   4244    401    126    -73       C  
ATOM   1514  C   LYS A 185     -19.487  34.299  47.574  1.00 33.74           C  
ANISOU 1514  C   LYS A 185     4698   4080   4040    349    168    -86       C  
ATOM   1515  O   LYS A 185     -19.741  33.090  47.663  1.00 31.14           O  
ANISOU 1515  O   LYS A 185     4304   3795   3732    334    170    -93       O  
ATOM   1516  CB  LYS A 185     -19.365  34.398  45.056  1.00 33.52           C  
ANISOU 1516  CB  LYS A 185     4668   4060   4007    381     81    -51       C  
ATOM   1517  CG  LYS A 185     -19.741  35.135  43.776  1.00 36.67           C  
ANISOU 1517  CG  LYS A 185     5093   4436   4404    426     34    -35       C  
ATOM   1518  CD  LYS A 185     -19.363  34.370  42.530  1.00 33.54           C  
ANISOU 1518  CD  LYS A 185     4680   4070   3993    406     -6    -18       C  
ATOM   1519  CE  LYS A 185     -19.871  35.090  41.281  1.00 37.95           C  
ANISOU 1519  CE  LYS A 185     5268   4605   4546    452    -57     -2       C  
ATOM   1520  NZ  LYS A 185     -19.753  34.234  40.057  1.00 39.04           N  
ANISOU 1520  NZ  LYS A 185     5386   4776   4673    435    -96     10       N  
ATOM   1521  N   ILE A 186     -18.868  34.976  48.535  1.00 33.70           N  
ANISOU 1521  N   ILE A 186     4757   4043   4004    319    197    -89       N  
ATOM   1522  CA  ILE A 186     -18.404  34.311  49.754  1.00 34.83           C  
ANISOU 1522  CA  ILE A 186     4899   4202   4131    265    230    -98       C  
ATOM   1523  C   ILE A 186     -19.450  34.346  50.867  1.00 34.62           C  
ANISOU 1523  C   ILE A 186     4858   4168   4128    288    281   -129       C  
ATOM   1524  O   ILE A 186     -19.957  35.403  51.236  1.00 34.42           O  
ANISOU 1524  O   ILE A 186     4874   4100   4103    323    307   -145       O  
ATOM   1525  CB  ILE A 186     -17.030  34.859  50.236  1.00 33.67           C  
ANISOU 1525  CB  ILE A 186     4828   4033   3932    203    229    -82       C  
ATOM   1526  CG1 ILE A 186     -15.948  34.552  49.196  1.00 34.06           C  
ANISOU 1526  CG1 ILE A 186     4873   4104   3965    172    188    -53       C  
ATOM   1527  CG2 ILE A 186     -16.637  34.254  51.586  1.00 32.78           C  
ANISOU 1527  CG2 ILE A 186     4720   3933   3801    151    257    -90       C  
ATOM   1528  CD1 ILE A 186     -14.632  35.306  49.413  1.00 32.86           C  
ANISOU 1528  CD1 ILE A 186     4790   3929   3766    116    182    -36       C  
ATOM   1529  N   ILE A 187     -19.776  33.166  51.378  1.00 34.82           N  
ANISOU 1529  N   ILE A 187     4827   4232   4169    267    299   -139       N  
ATOM   1530  CA  ILE A 187     -20.653  33.044  52.522  1.00 33.60           C  
ANISOU 1530  CA  ILE A 187     4660   4076   4030    273    355   -169       C  
ATOM   1531  C   ILE A 187     -19.796  32.499  53.649  1.00 35.22           C  
ANISOU 1531  C   ILE A 187     4903   4285   4192    201    374   -165       C  
ATOM   1532  O   ILE A 187     -19.361  31.342  53.626  1.00 34.92           O  
ANISOU 1532  O   ILE A 187     4833   4282   4152    164    356   -152       O  
ATOM   1533  CB  ILE A 187     -21.896  32.167  52.209  1.00 35.30           C  
ANISOU 1533  CB  ILE A 187     4780   4332   4301    307    363   -185       C  
ATOM   1534  CG1 ILE A 187     -22.729  32.842  51.100  1.00 35.53           C  
ANISOU 1534  CG1 ILE A 187     4775   4355   4371    381    334   -186       C  
ATOM   1535  CG2 ILE A 187     -22.737  31.972  53.467  1.00 35.53           C  
ANISOU 1535  CG2 ILE A 187     4795   4362   4342    302    431   -218       C  
ATOM   1536  CD1 ILE A 187     -23.942  32.080  50.618  1.00 34.50           C  
ANISOU 1536  CD1 ILE A 187     4544   4268   4298    414    329   -199       C  
ATOM   1537  N   TYR A 188     -19.545  33.367  54.625  1.00 33.23           N  
ANISOU 1537  N   TYR A 188     4728   3992   3905    183    406   -176       N  
ATOM   1538  CA  TYR A 188     -18.562  33.129  55.654  1.00 31.96           C  
ANISOU 1538  CA  TYR A 188     4623   3827   3694    112    411   -167       C  
ATOM   1539  C   TYR A 188     -19.228  32.729  56.958  1.00 33.85           C  
ANISOU 1539  C   TYR A 188     4871   4065   3926     92    470   -194       C  
ATOM   1540  O   TYR A 188     -20.118  33.427  57.446  1.00 35.21           O  
ANISOU 1540  O   TYR A 188     5063   4209   4107    126    522   -224       O  
ATOM   1541  CB  TYR A 188     -17.722  34.396  55.867  1.00 32.64           C  
ANISOU 1541  CB  TYR A 188     4802   3867   3735     90    403   -160       C  
ATOM   1542  CG  TYR A 188     -16.764  34.300  57.032  1.00 31.81           C  
ANISOU 1542  CG  TYR A 188     4761   3754   3573     13    405   -152       C  
ATOM   1543  CD1 TYR A 188     -15.638  33.474  56.964  1.00 26.81           C  
ANISOU 1543  CD1 TYR A 188     4111   3154   2923    -39    359   -121       C  
ATOM   1544  CD2 TYR A 188     -16.991  35.019  58.210  1.00 35.56           C  
ANISOU 1544  CD2 TYR A 188     5314   4186   4011     -6    452   -176       C  
ATOM   1545  CE1 TYR A 188     -14.755  33.371  58.032  1.00 28.05           C  
ANISOU 1545  CE1 TYR A 188     4323   3306   3030   -108    351   -111       C  
ATOM   1546  CE2 TYR A 188     -16.105  34.930  59.299  1.00 33.33           C  
ANISOU 1546  CE2 TYR A 188     5097   3896   3671    -82    446   -168       C  
ATOM   1547  CZ  TYR A 188     -14.991  34.099  59.199  1.00 31.99           C  
ANISOU 1547  CZ  TYR A 188     4904   3764   3488   -133    391   -134       C  
ATOM   1548  OH  TYR A 188     -14.110  34.002  60.250  1.00 29.50           O  
ANISOU 1548  OH  TYR A 188     4648   3444   3117   -207    376   -122       O  
ATOM   1549  N   MET A 189     -18.778  31.618  57.529  1.00 33.12           N  
ANISOU 1549  N   MET A 189     4770   4000   3815     40    463   -182       N  
ATOM   1550  CA  MET A 189     -19.363  31.086  58.756  1.00 35.72           C  
ANISOU 1550  CA  MET A 189     5112   4329   4130     11    517   -204       C  
ATOM   1551  C   MET A 189     -18.258  30.726  59.735  1.00 35.43           C  
ANISOU 1551  C   MET A 189     5141   4287   4033    -64    500   -184       C  
ATOM   1552  O   MET A 189     -17.566  29.721  59.540  1.00 38.30           O  
ANISOU 1552  O   MET A 189     5478   4679   4394    -93    456   -156       O  
ATOM   1553  CB  MET A 189     -20.233  29.855  58.461  1.00 36.89           C  
ANISOU 1553  CB  MET A 189     5174   4519   4324     25    529   -211       C  
ATOM   1554  CG  MET A 189     -21.437  30.138  57.553  1.00 38.20           C  
ANISOU 1554  CG  MET A 189     5264   4697   4552     97    543   -231       C  
ATOM   1555  SD  MET A 189     -22.095  28.696  56.672  1.00 42.33           S  
ANISOU 1555  SD  MET A 189     5680   5276   5129    107    520   -227       S  
ATOM   1556  CE  MET A 189     -20.717  28.303  55.582  1.00 38.91           C  
ANISOU 1556  CE  MET A 189     5250   4854   4680     93    437   -184       C  
ATOM   1557  N   PRO A 190     -18.069  31.557  60.778  1.00 34.85           N  
ANISOU 1557  N   PRO A 190     5158   4174   3910    -95    530   -197       N  
ATOM   1558  CA  PRO A 190     -17.119  31.254  61.845  1.00 34.50           C  
ANISOU 1558  CA  PRO A 190     5183   4122   3803   -171    512   -180       C  
ATOM   1559  C   PRO A 190     -17.739  30.352  62.912  1.00 36.72           C  
ANISOU 1559  C   PRO A 190     5475   4411   4068   -203    559   -194       C  
ATOM   1560  O   PRO A 190     -18.951  30.394  63.122  1.00 37.60           O  
ANISOU 1560  O   PRO A 190     5565   4517   4203   -172    626   -229       O  
ATOM   1561  CB  PRO A 190     -16.786  32.636  62.419  1.00 36.73           C  
ANISOU 1561  CB  PRO A 190     5563   4355   4038   -190    528   -193       C  
ATOM   1562  CG  PRO A 190     -17.993  33.480  62.133  1.00 36.88           C  
ANISOU 1562  CG  PRO A 190     5572   4348   4093   -122    589   -231       C  
ATOM   1563  CD  PRO A 190     -18.723  32.869  60.961  1.00 35.05           C  
ANISOU 1563  CD  PRO A 190     5228   4155   3935    -58    579   -229       C  
ATOM   1564  N   PHE A 191     -16.916  29.550  63.583  1.00 36.33           N  
ANISOU 1564  N   PHE A 191     5457   4371   3976   -264    523   -167       N  
ATOM   1565  CA  PHE A 191     -17.409  28.588  64.573  1.00 36.23           C  
ANISOU 1565  CA  PHE A 191     5463   4362   3941   -301    560   -175       C  
ATOM   1566  C   PHE A 191     -16.608  28.625  65.874  1.00 38.45           C  
ANISOU 1566  C   PHE A 191     5849   4620   4141   -377    545   -161       C  
ATOM   1567  O   PHE A 191     -15.379  28.742  65.856  1.00 37.26           O  
ANISOU 1567  O   PHE A 191     5723   4470   3963   -409    475   -127       O  
ATOM   1568  CB  PHE A 191     -17.395  27.168  63.983  1.00 35.82           C  
ANISOU 1568  CB  PHE A 191     5333   4350   3927   -294    527   -152       C  
ATOM   1569  CG  PHE A 191     -18.421  26.953  62.903  1.00 36.09           C  
ANISOU 1569  CG  PHE A 191     5270   4408   4033   -231    551   -171       C  
ATOM   1570  CD1 PHE A 191     -18.112  27.207  61.568  1.00 33.44           C  
ANISOU 1570  CD1 PHE A 191     4875   4089   3742   -184    505   -158       C  
ATOM   1571  CD2 PHE A 191     -19.711  26.524  63.224  1.00 36.48           C  
ANISOU 1571  CD2 PHE A 191     5291   4465   4105   -223    620   -203       C  
ATOM   1572  CE1 PHE A 191     -19.065  27.027  60.567  1.00 35.90           C  
ANISOU 1572  CE1 PHE A 191     5103   4423   4115   -129    519   -174       C  
ATOM   1573  CE2 PHE A 191     -20.676  26.344  62.227  1.00 36.00           C  
ANISOU 1573  CE2 PHE A 191     5135   4430   4112   -168    635   -220       C  
ATOM   1574  CZ  PHE A 191     -20.348  26.594  60.894  1.00 35.26           C  
ANISOU 1574  CZ  PHE A 191     4987   4352   4059   -121    581   -205       C  
ATOM   1575  N   ASP A 192     -17.310  28.524  66.999  1.00 42.77           N  
ANISOU 1575  N   ASP A 192     6455   5145   4648   -410    612   -187       N  
ATOM   1576  CA  ASP A 192     -16.672  28.505  68.321  1.00 46.33           C  
ANISOU 1576  CA  ASP A 192     7018   5571   5014   -488    601   -175       C  
ATOM   1577  C   ASP A 192     -15.858  27.235  68.571  1.00 43.70           C  
ANISOU 1577  C   ASP A 192     6682   5260   4662   -530    532   -129       C  
ATOM   1578  O   ASP A 192     -14.845  27.270  69.271  1.00 44.13           O  
ANISOU 1578  O   ASP A 192     6807   5303   4656   -587    476   -101       O  
ATOM   1579  CB  ASP A 192     -17.718  28.656  69.433  1.00 51.06           C  
ANISOU 1579  CB  ASP A 192     7684   6141   5574   -513    700   -218       C  
ATOM   1580  CG  ASP A 192     -18.334  30.045  69.475  1.00 60.23           C  
ANISOU 1580  CG  ASP A 192     8879   7268   6738   -479    768   -263       C  
ATOM   1581  OD1 ASP A 192     -17.574  31.039  69.549  1.00 63.29           O  
ANISOU 1581  OD1 ASP A 192     9329   7628   7090   -494    735   -257       O  
ATOM   1582  OD2 ASP A 192     -19.584  30.141  69.444  1.00 64.56           O  
ANISOU 1582  OD2 ASP A 192     9391   7816   7325   -438    855   -304       O  
ATOM   1583  N   ASN A 193     -16.318  26.115  68.016  1.00 40.34           N  
ANISOU 1583  N   ASN A 193     6178   4864   4287   -503    533   -122       N  
ATOM   1584  CA  ASN A 193     -15.663  24.823  68.234  1.00 39.35           C  
ANISOU 1584  CA  ASN A 193     6051   4753   4148   -534    474    -80       C  
ATOM   1585  C   ASN A 193     -15.765  23.888  67.026  1.00 37.01           C  
ANISOU 1585  C   ASN A 193     5647   4491   3925   -484    448    -66       C  
ATOM   1586  O   ASN A 193     -16.675  24.010  66.209  1.00 35.78           O  
ANISOU 1586  O   ASN A 193     5420   4350   3826   -434    491    -94       O  
ATOM   1587  CB  ASN A 193     -16.210  24.147  69.500  1.00 40.40           C  
ANISOU 1587  CB  ASN A 193     6261   4865   4223   -591    522    -88       C  
ATOM   1588  CG  ASN A 193     -17.687  23.808  69.387  1.00 44.13           C  
ANISOU 1588  CG  ASN A 193     6690   5345   4733   -569    616   -130       C  
ATOM   1589  OD1 ASN A 193     -18.050  22.705  68.977  1.00 43.60           O  
ANISOU 1589  OD1 ASN A 193     6567   5298   4701   -559    614   -121       O  
ATOM   1590  ND2 ASN A 193     -18.548  24.768  69.721  1.00 47.92           N  
ANISOU 1590  ND2 ASN A 193     7193   5807   5207   -560    699   -176       N  
ATOM   1591  N   GLU A 194     -14.821  22.954  66.929  1.00 38.32           N  
ANISOU 1591  N   GLU A 194     5803   4669   4089   -496    375    -22       N  
ATOM   1592  CA  GLU A 194     -14.734  22.020  65.811  1.00 36.01           C  
ANISOU 1592  CA  GLU A 194     5421   4404   3859   -453    344     -6       C  
ATOM   1593  C   GLU A 194     -15.977  21.146  65.642  1.00 37.21           C  
ANISOU 1593  C   GLU A 194     5537   4562   4041   -442    403    -30       C  
ATOM   1594  O   GLU A 194     -16.386  20.855  64.512  1.00 36.13           O  
ANISOU 1594  O   GLU A 194     5317   4447   3965   -395    406    -39       O  
ATOM   1595  CB  GLU A 194     -13.487  21.137  65.944  1.00 35.95           C  
ANISOU 1595  CB  GLU A 194     5421   4399   3837   -470    260     45       C  
ATOM   1596  CG  GLU A 194     -13.164  20.335  64.674  1.00 34.21           C  
ANISOU 1596  CG  GLU A 194     5111   4204   3682   -419    224     62       C  
ATOM   1597  CD  GLU A 194     -12.076  19.297  64.872  1.00 38.15           C  
ANISOU 1597  CD  GLU A 194     5618   4703   4174   -428    152    110       C  
ATOM   1598  OE1 GLU A 194     -11.733  18.609  63.882  1.00 39.69           O  
ANISOU 1598  OE1 GLU A 194     5747   4914   4419   -386    125    123       O  
ATOM   1599  OE2 GLU A 194     -11.556  19.167  66.003  1.00 41.64           O  
ANISOU 1599  OE2 GLU A 194     6134   5127   4561   -475    121    134       O  
ATOM   1600  N   LYS A 195     -16.567  20.716  66.755  1.00 38.86           N  
ANISOU 1600  N   LYS A 195     5811   4751   4205   -490    449    -40       N  
ATOM   1601  CA  LYS A 195     -17.730  19.833  66.697  1.00 39.87           C  
ANISOU 1601  CA  LYS A 195     5907   4885   4356   -493    508    -62       C  
ATOM   1602  C   LYS A 195     -18.873  20.495  65.944  1.00 38.97           C  
ANISOU 1602  C   LYS A 195     5717   4790   4298   -447    570   -107       C  
ATOM   1603  O   LYS A 195     -19.415  19.910  65.002  1.00 37.44           O  
ANISOU 1603  O   LYS A 195     5444   4620   4161   -415    572   -114       O  
ATOM   1604  CB  LYS A 195     -18.179  19.391  68.087  1.00 42.24           C  
ANISOU 1604  CB  LYS A 195     6299   5159   4591   -560    556    -68       C  
ATOM   1605  CG  LYS A 195     -17.304  18.311  68.706  1.00 48.34           C  
ANISOU 1605  CG  LYS A 195     7135   5912   5318   -602    494    -20       C  
ATOM   1606  CD  LYS A 195     -17.948  17.732  69.961  1.00 51.14           C  
ANISOU 1606  CD  LYS A 195     7579   6241   5611   -670    550    -28       C  
ATOM   1607  CE  LYS A 195     -16.994  16.804  70.694  1.00 55.79           C  
ANISOU 1607  CE  LYS A 195     8250   6804   6144   -712    479     24       C  
ATOM   1608  NZ  LYS A 195     -15.931  17.567  71.408  1.00 58.84           N  
ANISOU 1608  NZ  LYS A 195     8709   7175   6472   -736    422     49       N  
ATOM   1609  N   GLU A 196     -19.217  21.719  66.339  1.00 39.37           N  
ANISOU 1609  N   GLU A 196     5795   4829   4334   -442    615   -136       N  
ATOM   1610  CA  GLU A 196     -20.298  22.440  65.673  1.00 41.25           C  
ANISOU 1610  CA  GLU A 196     5963   5083   4628   -391    671   -177       C  
ATOM   1611  C   GLU A 196     -19.959  22.739  64.205  1.00 38.19           C  
ANISOU 1611  C   GLU A 196     5493   4718   4300   -328    616   -167       C  
ATOM   1612  O   GLU A 196     -20.839  22.652  63.344  1.00 39.92           O  
ANISOU 1612  O   GLU A 196     5630   4961   4578   -286    637   -187       O  
ATOM   1613  CB  GLU A 196     -20.774  23.676  66.469  1.00 43.11           C  
ANISOU 1613  CB  GLU A 196     6253   5293   4833   -395    738   -213       C  
ATOM   1614  CG  GLU A 196     -19.895  24.920  66.394  1.00 52.44           C  
ANISOU 1614  CG  GLU A 196     7479   6454   5992   -381    700   -205       C  
ATOM   1615  CD  GLU A 196     -20.507  26.147  67.104  1.00 58.35           C  
ANISOU 1615  CD  GLU A 196     8283   7172   6716   -378    777   -247       C  
ATOM   1616  OE1 GLU A 196     -20.275  27.292  66.633  1.00 55.67           O  
ANISOU 1616  OE1 GLU A 196     7944   6819   6389   -339    765   -254       O  
ATOM   1617  OE2 GLU A 196     -21.206  25.969  68.132  1.00 60.67           O  
ANISOU 1617  OE2 GLU A 196     8624   7452   6977   -415    852   -273       O  
ATOM   1618  N   LEU A 197     -18.689  23.045  63.925  1.00 33.26           N  
ANISOU 1618  N   LEU A 197     4891   4088   3659   -325    544   -134       N  
ATOM   1619  CA  LEU A 197     -18.219  23.245  62.554  1.00 33.56           C  
ANISOU 1619  CA  LEU A 197     4861   4146   3744   -275    491   -119       C  
ATOM   1620  C   LEU A 197     -18.517  22.008  61.687  1.00 32.77           C  
ANISOU 1620  C   LEU A 197     4691   4072   3690   -258    473   -111       C  
ATOM   1621  O   LEU A 197     -19.085  22.122  60.599  1.00 31.00           O  
ANISOU 1621  O   LEU A 197     4394   3867   3516   -212    475   -125       O  
ATOM   1622  CB  LEU A 197     -16.713  23.602  62.518  1.00 31.58           C  
ANISOU 1622  CB  LEU A 197     4646   3888   3464   -288    420    -83       C  
ATOM   1623  CG  LEU A 197     -16.041  23.925  61.168  1.00 32.05           C  
ANISOU 1623  CG  LEU A 197     4649   3966   3563   -244    368    -67       C  
ATOM   1624  CD1 LEU A 197     -14.769  24.739  61.344  1.00 29.40           C  
ANISOU 1624  CD1 LEU A 197     4357   3620   3194   -264    321    -43       C  
ATOM   1625  CD2 LEU A 197     -15.717  22.673  60.365  1.00 30.52           C  
ANISOU 1625  CD2 LEU A 197     4400   3795   3403   -230    330    -44       C  
ATOM   1626  N   LEU A 198     -18.142  20.833  62.181  1.00 32.27           N  
ANISOU 1626  N   LEU A 198     4653   4004   3603   -295    455    -88       N  
ATOM   1627  CA  LEU A 198     -18.318  19.611  61.419  1.00 33.63           C  
ANISOU 1627  CA  LEU A 198     4773   4193   3811   -285    436    -79       C  
ATOM   1628  C   LEU A 198     -19.790  19.209  61.331  1.00 35.36           C  
ANISOU 1628  C   LEU A 198     4949   4425   4060   -286    498   -115       C  
ATOM   1629  O   LEU A 198     -20.226  18.693  60.305  1.00 36.71           O  
ANISOU 1629  O   LEU A 198     5054   4618   4277   -261    489   -121       O  
ATOM   1630  CB  LEU A 198     -17.435  18.483  61.972  1.00 32.85           C  
ANISOU 1630  CB  LEU A 198     4721   4080   3680   -320    395    -42       C  
ATOM   1631  CG  LEU A 198     -15.914  18.703  61.870  1.00 31.13           C  
ANISOU 1631  CG  LEU A 198     4523   3858   3447   -313    323     -4       C  
ATOM   1632  CD1 LEU A 198     -15.146  17.645  62.651  1.00 25.39           C  
ANISOU 1632  CD1 LEU A 198     3849   3113   2685   -347    285     33       C  
ATOM   1633  CD2 LEU A 198     -15.436  18.727  60.415  1.00 29.14           C  
ANISOU 1633  CD2 LEU A 198     4200   3628   3244   -262    285      4       C  
ATOM   1634  N   MET A 199     -20.555  19.469  62.388  1.00 37.13           N  
ANISOU 1634  N   MET A 199     5209   4639   4258   -318    563   -139       N  
ATOM   1635  CA  MET A 199     -21.983  19.150  62.392  1.00 39.30           C  
ANISOU 1635  CA  MET A 199     5437   4931   4565   -324    630   -175       C  
ATOM   1636  C   MET A 199     -22.734  20.019  61.389  1.00 38.81           C  
ANISOU 1636  C   MET A 199     5291   4894   4563   -264    642   -202       C  
ATOM   1637  O   MET A 199     -23.563  19.524  60.618  1.00 38.90           O  
ANISOU 1637  O   MET A 199     5227   4932   4623   -249    649   -217       O  
ATOM   1638  CB  MET A 199     -22.586  19.287  63.799  1.00 41.75           C  
ANISOU 1638  CB  MET A 199     5808   5223   4831   -374    705   -197       C  
ATOM   1639  CG  MET A 199     -22.212  18.142  64.742  1.00 43.50           C  
ANISOU 1639  CG  MET A 199     6106   5423   4999   -441    702   -173       C  
ATOM   1640  SD  MET A 199     -23.047  18.176  66.341  1.00 51.04           S  
ANISOU 1640  SD  MET A 199     7137   6357   5897   -509    800   -201       S  
ATOM   1641  CE  MET A 199     -22.217  19.534  67.171  1.00 47.34           C  
ANISOU 1641  CE  MET A 199     6759   5860   5370   -510    793   -197       C  
ATOM   1642  N   GLU A 200     -22.418  21.311  61.385  1.00 38.50           N  
ANISOU 1642  N   GLU A 200     5269   4843   4517   -231    639   -207       N  
ATOM   1643  CA  GLU A 200     -23.006  22.231  60.421  1.00 40.08           C  
ANISOU 1643  CA  GLU A 200     5401   5058   4769   -168    640   -227       C  
ATOM   1644  C   GLU A 200     -22.576  21.888  58.986  1.00 38.17           C  
ANISOU 1644  C   GLU A 200     5103   4835   4562   -133    570   -206       C  
ATOM   1645  O   GLU A 200     -23.391  21.966  58.064  1.00 38.97           O  
ANISOU 1645  O   GLU A 200     5131   4961   4715    -95    569   -222       O  
ATOM   1646  CB  GLU A 200     -22.685  23.688  60.777  1.00 41.26           C  
ANISOU 1646  CB  GLU A 200     5598   5181   4897   -144    652   -235       C  
ATOM   1647  CG  GLU A 200     -23.324  24.733  59.852  1.00 47.57           C  
ANISOU 1647  CG  GLU A 200     6339   5988   5748    -74    654   -255       C  
ATOM   1648  CD  GLU A 200     -24.838  24.553  59.666  1.00 56.77           C  
ANISOU 1648  CD  GLU A 200     7420   7180   6969    -49    707   -290       C  
ATOM   1649  OE1 GLU A 200     -25.560  24.342  60.678  1.00 55.43           O  
ANISOU 1649  OE1 GLU A 200     7261   7009   6790    -80    780   -315       O  
ATOM   1650  OE2 GLU A 200     -25.298  24.634  58.497  1.00 57.87           O  
ANISOU 1650  OE2 GLU A 200     7483   7344   7162     -1    676   -291       O  
ATOM   1651  N   TYR A 201     -21.318  21.489  58.807  1.00 34.44           N  
ANISOU 1651  N   TYR A 201     4668   4354   4063   -147    513   -171       N  
ATOM   1652  CA  TYR A 201     -20.832  21.088  57.481  1.00 34.30           C  
ANISOU 1652  CA  TYR A 201     4606   4353   4073   -119    454   -152       C  
ATOM   1653  C   TYR A 201     -21.579  19.862  56.951  1.00 34.56           C  
ANISOU 1653  C   TYR A 201     4587   4408   4138   -128    457   -160       C  
ATOM   1654  O   TYR A 201     -21.976  19.822  55.781  1.00 32.78           O  
ANISOU 1654  O   TYR A 201     4302   4202   3950    -95    434   -166       O  
ATOM   1655  CB  TYR A 201     -19.319  20.843  57.488  1.00 33.04           C  
ANISOU 1655  CB  TYR A 201     4491   4180   3881   -133    401   -114       C  
ATOM   1656  CG  TYR A 201     -18.753  20.551  56.117  1.00 32.69           C  
ANISOU 1656  CG  TYR A 201     4408   4150   3864   -101    349    -98       C  
ATOM   1657  CD1 TYR A 201     -18.816  21.508  55.099  1.00 32.65           C  
ANISOU 1657  CD1 TYR A 201     4373   4153   3881    -58    333   -104       C  
ATOM   1658  CD2 TYR A 201     -18.156  19.315  55.828  1.00 32.61           C  
ANISOU 1658  CD2 TYR A 201     4395   4141   3852   -115    320    -77       C  
ATOM   1659  CE1 TYR A 201     -18.306  21.243  53.816  1.00 29.41           C  
ANISOU 1659  CE1 TYR A 201     3933   3755   3488    -34    291    -90       C  
ATOM   1660  CE2 TYR A 201     -17.636  19.045  54.544  1.00 31.46           C  
ANISOU 1660  CE2 TYR A 201     4218   4007   3729    -86    281    -66       C  
ATOM   1661  CZ  TYR A 201     -17.717  20.024  53.549  1.00 29.16           C  
ANISOU 1661  CZ  TYR A 201     3898   3725   3455    -48    268    -73       C  
ATOM   1662  OH  TYR A 201     -17.220  19.786  52.290  1.00 27.10           O  
ANISOU 1662  OH  TYR A 201     3613   3473   3209    -25    235    -63       O  
ATOM   1663  N   LEU A 202     -21.786  18.874  57.821  1.00 33.92           N  
ANISOU 1663  N   LEU A 202     4534   4320   4036   -177    484   -159       N  
ATOM   1664  CA  LEU A 202     -22.532  17.681  57.444  1.00 33.99           C  
ANISOU 1664  CA  LEU A 202     4502   4344   4069   -198    493   -169       C  
ATOM   1665  C   LEU A 202     -23.971  18.011  57.048  1.00 34.50           C  
ANISOU 1665  C   LEU A 202     4490   4437   4180   -181    530   -205       C  
ATOM   1666  O   LEU A 202     -24.479  17.481  56.052  1.00 33.82           O  
ANISOU 1666  O   LEU A 202     4346   4374   4130   -171    509   -211       O  
ATOM   1667  CB  LEU A 202     -22.514  16.649  58.563  1.00 34.53           C  
ANISOU 1667  CB  LEU A 202     4627   4393   4101   -259    520   -161       C  
ATOM   1668  CG  LEU A 202     -21.260  15.792  58.724  1.00 35.69           C  
ANISOU 1668  CG  LEU A 202     4833   4515   4214   -276    472   -122       C  
ATOM   1669  CD1 LEU A 202     -21.427  14.920  59.947  1.00 31.19           C  
ANISOU 1669  CD1 LEU A 202     4326   3922   3604   -337    504   -117       C  
ATOM   1670  CD2 LEU A 202     -20.964  14.929  57.483  1.00 31.72           C  
ANISOU 1670  CD2 LEU A 202     4295   4019   3740   -256    426   -111       C  
ATOM   1671  N   ASN A 203     -24.614  18.886  57.824  1.00 34.69           N  
ANISOU 1671  N   ASN A 203     4515   4462   4205   -177    585   -228       N  
ATOM   1672  CA  ASN A 203     -25.968  19.348  57.518  1.00 36.56           C  
ANISOU 1672  CA  ASN A 203     4671   4726   4492   -151    623   -263       C  
ATOM   1673  C   ASN A 203     -26.021  20.110  56.201  1.00 35.62           C  
ANISOU 1673  C   ASN A 203     4497   4623   4414    -85    574   -262       C  
ATOM   1674  O   ASN A 203     -26.969  19.980  55.433  1.00 36.27           O  
ANISOU 1674  O   ASN A 203     4499   4737   4545    -66    568   -278       O  
ATOM   1675  CB  ASN A 203     -26.525  20.209  58.654  1.00 37.14           C  
ANISOU 1675  CB  ASN A 203     4764   4790   4556   -153    697   -289       C  
ATOM   1676  CG  ASN A 203     -26.931  19.381  59.865  1.00 39.27           C  
ANISOU 1676  CG  ASN A 203     5070   5054   4796   -222    761   -301       C  
ATOM   1677  OD1 ASN A 203     -26.844  19.840  61.005  1.00 43.91           O  
ANISOU 1677  OD1 ASN A 203     5721   5619   5345   -244    812   -309       O  
ATOM   1678  ND2 ASN A 203     -27.386  18.162  59.624  1.00 34.78           N  
ANISOU 1678  ND2 ASN A 203     4469   4504   4242   -262    761   -301       N  
ATOM   1679  N   PHE A 204     -24.978  20.892  55.953  1.00 34.90           N  
ANISOU 1679  N   PHE A 204     4451   4510   4299    -56    535   -240       N  
ATOM   1680  CA  PHE A 204     -24.822  21.637  54.715  1.00 33.79           C  
ANISOU 1680  CA  PHE A 204     4279   4376   4184      1    484   -233       C  
ATOM   1681  C   PHE A 204     -24.702  20.646  53.561  1.00 32.18           C  
ANISOU 1681  C   PHE A 204     4040   4191   3995     -4    433   -220       C  
ATOM   1682  O   PHE A 204     -25.422  20.756  52.570  1.00 32.20           O  
ANISOU 1682  O   PHE A 204     3981   4217   4036     26    409   -230       O  
ATOM   1683  CB  PHE A 204     -23.596  22.563  54.841  1.00 31.58           C  
ANISOU 1683  CB  PHE A 204     4068   4065   3867     16    460   -211       C  
ATOM   1684  CG  PHE A 204     -23.035  23.034  53.535  1.00 32.78           C  
ANISOU 1684  CG  PHE A 204     4210   4218   4028     56    400   -193       C  
ATOM   1685  CD1 PHE A 204     -23.498  24.208  52.947  1.00 31.74           C  
ANISOU 1685  CD1 PHE A 204     4056   4083   3920    110    393   -203       C  
ATOM   1686  CD2 PHE A 204     -22.012  22.327  52.907  1.00 30.74           C  
ANISOU 1686  CD2 PHE A 204     3968   3960   3751     40    354   -167       C  
ATOM   1687  CE1 PHE A 204     -22.967  24.657  51.750  1.00 32.36           C  
ANISOU 1687  CE1 PHE A 204     4136   4159   3999    142    338   -184       C  
ATOM   1688  CE2 PHE A 204     -21.480  22.769  51.705  1.00 30.39           C  
ANISOU 1688  CE2 PHE A 204     3920   3917   3711     72    306   -152       C  
ATOM   1689  CZ  PHE A 204     -21.966  23.930  51.118  1.00 28.42           C  
ANISOU 1689  CZ  PHE A 204     3654   3664   3480    120    297   -160       C  
ATOM   1690  N   TRP A 205     -23.813  19.667  53.727  1.00 31.73           N  
ANISOU 1690  N   TRP A 205     4028   4123   3907    -43    415   -199       N  
ATOM   1691  CA  TRP A 205     -23.551  18.620  52.744  1.00 32.48           C  
ANISOU 1691  CA  TRP A 205     4108   4226   4007    -52    373   -187       C  
ATOM   1692  C   TRP A 205     -24.830  17.882  52.394  1.00 36.28           C  
ANISOU 1692  C   TRP A 205     4525   4735   4524    -70    385   -210       C  
ATOM   1693  O   TRP A 205     -25.075  17.590  51.223  1.00 37.59           O  
ANISOU 1693  O   TRP A 205     4653   4917   4710    -57    346   -211       O  
ATOM   1694  CB  TRP A 205     -22.515  17.641  53.304  1.00 31.22           C  
ANISOU 1694  CB  TRP A 205     4009   4043   3810    -91    366   -164       C  
ATOM   1695  CG  TRP A 205     -21.952  16.576  52.360  1.00 30.84           C  
ANISOU 1695  CG  TRP A 205     3963   3993   3762    -96    325   -149       C  
ATOM   1696  CD1 TRP A 205     -22.539  15.382  52.009  1.00 32.03           C  
ANISOU 1696  CD1 TRP A 205     4096   4150   3924   -125    326   -158       C  
ATOM   1697  CD2 TRP A 205     -20.657  16.575  51.739  1.00 29.90           C  
ANISOU 1697  CD2 TRP A 205     3873   3861   3627    -75    285   -123       C  
ATOM   1698  NE1 TRP A 205     -21.696  14.654  51.186  1.00 28.08           N  
ANISOU 1698  NE1 TRP A 205     3616   3637   3415   -119    289   -141       N  
ATOM   1699  CE2 TRP A 205     -20.538  15.363  51.007  1.00 29.49           C  
ANISOU 1699  CE2 TRP A 205     3819   3806   3580    -87    265   -120       C  
ATOM   1700  CE3 TRP A 205     -19.589  17.488  51.713  1.00 30.35           C  
ANISOU 1700  CE3 TRP A 205     3955   3909   3668    -51    265   -104       C  
ATOM   1701  CZ2 TRP A 205     -19.394  15.045  50.260  1.00 29.86           C  
ANISOU 1701  CZ2 TRP A 205     3887   3841   3617    -68    233   -100       C  
ATOM   1702  CZ3 TRP A 205     -18.444  17.165  50.962  1.00 30.33           C  
ANISOU 1702  CZ3 TRP A 205     3967   3899   3658    -37    231    -83       C  
ATOM   1703  CH2 TRP A 205     -18.360  15.952  50.256  1.00 27.88           C  
ANISOU 1703  CH2 TRP A 205     3652   3586   3355    -43    217    -82       C  
ATOM   1704  N   GLN A 206     -25.641  17.594  53.411  1.00 38.42           N  
ANISOU 1704  N   GLN A 206     4785   5012   4799   -105    441   -230       N  
ATOM   1705  CA  GLN A 206     -26.930  16.944  53.216  1.00 41.91           C  
ANISOU 1705  CA  GLN A 206     5161   5486   5279   -130    461   -254       C  
ATOM   1706  C   GLN A 206     -27.849  17.761  52.312  1.00 41.88           C  
ANISOU 1706  C   GLN A 206     5073   5514   5324    -81    442   -271       C  
ATOM   1707  O   GLN A 206     -28.447  17.209  51.385  1.00 41.64           O  
ANISOU 1707  O   GLN A 206     4990   5509   5321    -87    409   -278       O  
ATOM   1708  CB  GLN A 206     -27.613  16.656  54.553  1.00 44.48           C  
ANISOU 1708  CB  GLN A 206     5491   5812   5598   -178    535   -274       C  
ATOM   1709  CG  GLN A 206     -28.832  15.744  54.428  1.00 52.19           C  
ANISOU 1709  CG  GLN A 206     6403   6821   6607   -222    559   -297       C  
ATOM   1710  CD  GLN A 206     -29.443  15.362  55.772  1.00 58.86           C  
ANISOU 1710  CD  GLN A 206     7261   7663   7439   -279    640   -316       C  
ATOM   1711  OE1 GLN A 206     -29.750  14.193  56.008  1.00 60.64           O  
ANISOU 1711  OE1 GLN A 206     7496   7889   7654   -343    657   -318       O  
ATOM   1712  NE2 GLN A 206     -29.625  16.347  56.655  1.00 62.10           N  
ANISOU 1712  NE2 GLN A 206     7680   8069   7846   -260    692   -329       N  
ATOM   1713  N   GLN A 207     -27.952  19.064  52.572  1.00 42.86           N  
ANISOU 1713  N   GLN A 207     5191   5634   5459    -32    458   -277       N  
ATOM   1714  CA  GLN A 207     -28.768  19.949  51.732  1.00 45.98           C  
ANISOU 1714  CA  GLN A 207     5514   6054   5903     26    434   -289       C  
ATOM   1715  C   GLN A 207     -28.194  20.105  50.332  1.00 43.96           C  
ANISOU 1715  C   GLN A 207     5264   5795   5643     59    355   -268       C  
ATOM   1716  O   GLN A 207     -28.941  20.228  49.365  1.00 46.60           O  
ANISOU 1716  O   GLN A 207     5536   6158   6014     85    317   -273       O  
ATOM   1717  CB  GLN A 207     -28.947  21.333  52.361  1.00 47.03           C  
ANISOU 1717  CB  GLN A 207     5652   6172   6045     76    471   -300       C  
ATOM   1718  CG  GLN A 207     -30.238  21.512  53.161  1.00 60.54           C  
ANISOU 1718  CG  GLN A 207     7298   7905   7797     75    542   -335       C  
ATOM   1719  CD  GLN A 207     -31.493  21.633  52.287  1.00 68.10           C  
ANISOU 1719  CD  GLN A 207     8144   8908   8824    111    518   -351       C  
ATOM   1720  OE1 GLN A 207     -32.043  22.724  52.124  1.00 70.60           O  
ANISOU 1720  OE1 GLN A 207     8419   9227   9178    177    521   -362       O  
ATOM   1721  NE2 GLN A 207     -31.949  20.508  51.728  1.00 71.17           N  
ANISOU 1721  NE2 GLN A 207     8484   9330   9228     66    491   -353       N  
ATOM   1722  N   LYS A 208     -26.869  20.105  50.233  1.00 40.39           N  
ANISOU 1722  N   LYS A 208     4888   5312   5145     56    332   -242       N  
ATOM   1723  CA  LYS A 208     -26.195  20.398  48.976  1.00 37.37           C  
ANISOU 1723  CA  LYS A 208     4522   4923   4752     86    269   -222       C  
ATOM   1724  C   LYS A 208     -25.188  19.295  48.665  1.00 35.99           C  
ANISOU 1724  C   LYS A 208     4396   4736   4543     48    248   -204       C  
ATOM   1725  O   LYS A 208     -23.974  19.531  48.627  1.00 34.49           O  
ANISOU 1725  O   LYS A 208     4263   4522   4320     54    235   -182       O  
ATOM   1726  CB  LYS A 208     -25.514  21.767  49.058  1.00 37.17           C  
ANISOU 1726  CB  LYS A 208     4540   4871   4710    131    265   -209       C  
ATOM   1727  CG  LYS A 208     -26.479  22.937  49.197  1.00 39.94           C  
ANISOU 1727  CG  LYS A 208     4850   5227   5097    182    281   -226       C  
ATOM   1728  CD  LYS A 208     -25.742  24.240  49.480  1.00 42.17           C  
ANISOU 1728  CD  LYS A 208     5194   5474   5357    216    286   -215       C  
ATOM   1729  CE  LYS A 208     -26.671  25.286  50.091  1.00 43.34           C  
ANISOU 1729  CE  LYS A 208     5315   5616   5536    260    326   -238       C  
ATOM   1730  NZ  LYS A 208     -27.720  25.730  49.128  1.00 40.76           N  
ANISOU 1730  NZ  LYS A 208     4918   5310   5260    315    291   -244       N  
ATOM   1731  N   THR A 209     -25.715  18.088  48.460  1.00 33.16           N  
ANISOU 1731  N   THR A 209     4011   4393   4193      8    246   -213       N  
ATOM   1732  CA  THR A 209     -24.913  16.892  48.272  1.00 33.97           C  
ANISOU 1732  CA  THR A 209     4159   4480   4268    -29    235   -201       C  
ATOM   1733  C   THR A 209     -24.198  16.931  46.929  1.00 32.65           C  
ANISOU 1733  C   THR A 209     4012   4307   4086     -5    182   -186       C  
ATOM   1734  O   THR A 209     -24.833  17.032  45.885  1.00 32.89           O  
ANISOU 1734  O   THR A 209     4006   4357   4133      8    147   -194       O  
ATOM   1735  CB  THR A 209     -25.761  15.605  48.404  1.00 34.82           C  
ANISOU 1735  CB  THR A 209     4241   4602   4388    -82    250   -217       C  
ATOM   1736  OG1 THR A 209     -26.451  15.623  49.658  1.00 39.00           O  
ANISOU 1736  OG1 THR A 209     4753   5138   4928   -108    306   -232       O  
ATOM   1737  CG2 THR A 209     -24.879  14.350  48.338  1.00 33.17           C  
ANISOU 1737  CG2 THR A 209     4091   4365   4147   -117    243   -204       C  
ATOM   1738  N   PRO A 210     -22.861  16.861  46.961  1.00 32.55           N  
ANISOU 1738  N   PRO A 210     4057   4269   4043     -1    178   -165       N  
ATOM   1739  CA  PRO A 210     -22.091  16.908  45.720  1.00 31.86           C  
ANISOU 1739  CA  PRO A 210     3992   4175   3939     19    139   -152       C  
ATOM   1740  C   PRO A 210     -22.452  15.726  44.834  1.00 32.49           C  
ANISOU 1740  C   PRO A 210     4066   4259   4019     -7    119   -162       C  
ATOM   1741  O   PRO A 210     -22.700  14.626  45.340  1.00 32.91           O  
ANISOU 1741  O   PRO A 210     4125   4307   4074    -45    139   -169       O  
ATOM   1742  CB  PRO A 210     -20.645  16.777  46.199  1.00 31.35           C  
ANISOU 1742  CB  PRO A 210     3979   4084   3848     18    150   -130       C  
ATOM   1743  CG  PRO A 210     -20.671  17.245  47.641  1.00 32.90           C  
ANISOU 1743  CG  PRO A 210     4182   4275   4043     10    184   -128       C  
ATOM   1744  CD  PRO A 210     -22.004  16.827  48.164  1.00 30.41           C  
ANISOU 1744  CD  PRO A 210     3830   3976   3751    -14    208   -151       C  
ATOM   1745  N   VAL A 211     -22.509  15.965  43.530  1.00 29.17           N  
ANISOU 1745  N   VAL A 211     3644   3846   3594     11     80   -162       N  
ATOM   1746  CA  VAL A 211     -22.632  14.885  42.563  1.00 29.72           C  
ANISOU 1746  CA  VAL A 211     3726   3914   3652    -15     58   -171       C  
ATOM   1747  C   VAL A 211     -21.227  14.586  42.058  1.00 31.04           C  
ANISOU 1747  C   VAL A 211     3950   4053   3788     -5     60   -156       C  
ATOM   1748  O   VAL A 211     -20.739  13.460  42.182  1.00 31.39           O  
ANISOU 1748  O   VAL A 211     4026   4077   3823    -27     76   -157       O  
ATOM   1749  CB  VAL A 211     -23.549  15.289  41.398  1.00 30.15           C  
ANISOU 1749  CB  VAL A 211     3749   3992   3714     -6     11   -181       C  
ATOM   1750  CG1 VAL A 211     -23.388  14.330  40.214  1.00 27.65           C  
ANISOU 1750  CG1 VAL A 211     3467   3667   3373    -31    -15   -187       C  
ATOM   1751  CG2 VAL A 211     -24.995  15.351  41.878  1.00 28.78           C  
ANISOU 1751  CG2 VAL A 211     3505   3850   3580    -19     11   -198       C  
ATOM   1752  N   ILE A 212     -20.590  15.613  41.496  1.00 30.00           N  
ANISOU 1752  N   ILE A 212     3833   3921   3644     29     45   -143       N  
ATOM   1753  CA  ILE A 212     -19.179  15.571  41.153  1.00 29.49           C  
ANISOU 1753  CA  ILE A 212     3813   3836   3555     41     55   -128       C  
ATOM   1754  C   ILE A 212     -18.419  16.254  42.274  1.00 30.25           C  
ANISOU 1754  C   ILE A 212     3912   3927   3656     54     79   -110       C  
ATOM   1755  O   ILE A 212     -18.715  17.395  42.633  1.00 31.56           O  
ANISOU 1755  O   ILE A 212     4062   4102   3829     71     75   -107       O  
ATOM   1756  CB  ILE A 212     -18.875  16.305  39.819  1.00 27.98           C  
ANISOU 1756  CB  ILE A 212     3642   3647   3342     61     28   -123       C  
ATOM   1757  CG1 ILE A 212     -19.731  15.763  38.667  1.00 27.75           C  
ANISOU 1757  CG1 ILE A 212     3615   3625   3303     44     -5   -140       C  
ATOM   1758  CG2 ILE A 212     -17.382  16.240  39.504  1.00 23.83           C  
ANISOU 1758  CG2 ILE A 212     3156   3104   2795     70     48   -110       C  
ATOM   1759  CD1 ILE A 212     -19.546  14.264  38.313  1.00 27.50           C  
ANISOU 1759  CD1 ILE A 212     3612   3577   3259     15      7   -153       C  
ATOM   1760  N   LEU A 213     -17.445  15.550  42.835  1.00 31.11           N  
ANISOU 1760  N   LEU A 213     4042   4019   3760     47    100   -100       N  
ATOM   1761  CA  LEU A 213     -16.652  16.100  43.913  1.00 31.22           C  
ANISOU 1761  CA  LEU A 213     4061   4028   3775     53    116    -82       C  
ATOM   1762  C   LEU A 213     -15.223  16.237  43.435  1.00 31.47           C  
ANISOU 1762  C   LEU A 213     4112   4051   3792     68    117    -65       C  
ATOM   1763  O   LEU A 213     -14.604  15.263  43.014  1.00 33.37           O  
ANISOU 1763  O   LEU A 213     4368   4280   4030     68    124    -64       O  
ATOM   1764  CB  LEU A 213     -16.747  15.220  45.169  1.00 31.88           C  
ANISOU 1764  CB  LEU A 213     4148   4100   3865     30    135    -80       C  
ATOM   1765  CG  LEU A 213     -16.109  15.784  46.450  1.00 32.51           C  
ANISOU 1765  CG  LEU A 213     4237   4175   3940     29    146    -62       C  
ATOM   1766  CD1 LEU A 213     -16.590  17.209  46.752  1.00 26.36           C  
ANISOU 1766  CD1 LEU A 213     3445   3409   3162     38    147    -65       C  
ATOM   1767  CD2 LEU A 213     -16.353  14.860  47.638  1.00 26.97           C  
ANISOU 1767  CD2 LEU A 213     3548   3460   3239      1    163    -60       C  
ATOM   1768  N   THR A 214     -14.706  17.458  43.467  1.00 30.84           N  
ANISOU 1768  N   THR A 214     4035   3978   3706     80    114    -53       N  
ATOM   1769  CA  THR A 214     -13.364  17.699  42.977  1.00 31.09           C  
ANISOU 1769  CA  THR A 214     4079   4008   3726     88    118    -37       C  
ATOM   1770  C   THR A 214     -12.602  18.652  43.891  1.00 31.02           C  
ANISOU 1770  C   THR A 214     4070   4001   3714     85    120    -18       C  
ATOM   1771  O   THR A 214     -13.105  19.049  44.941  1.00 28.77           O  
ANISOU 1771  O   THR A 214     3784   3716   3433     76    121    -18       O  
ATOM   1772  CB  THR A 214     -13.356  18.164  41.477  1.00 32.94           C  
ANISOU 1772  CB  THR A 214     4327   4246   3943     98    109    -44       C  
ATOM   1773  OG1 THR A 214     -12.002  18.283  41.017  1.00 32.00           O  
ANISOU 1773  OG1 THR A 214     4217   4126   3814    102    123    -31       O  
ATOM   1774  CG2 THR A 214     -14.074  19.495  41.297  1.00 28.79           C  
ANISOU 1774  CG2 THR A 214     3804   3726   3410    105     90    -44       C  
ATOM   1775  N   GLY A 215     -11.381  18.995  43.483  1.00 31.71           N  
ANISOU 1775  N   GLY A 215     4161   4093   3795     87    125     -4       N  
ATOM   1776  CA  GLY A 215     -10.482  19.832  44.272  1.00 32.63           C  
ANISOU 1776  CA  GLY A 215     4278   4214   3907     76    124     15       C  
ATOM   1777  C   GLY A 215      -9.068  19.379  43.994  1.00 34.15           C  
ANISOU 1777  C   GLY A 215     4456   4414   4106     78    132     30       C  
ATOM   1778  O   GLY A 215      -8.843  18.595  43.072  1.00 38.62           O  
ANISOU 1778  O   GLY A 215     5019   4978   4676     92    145     22       O  
ATOM   1779  N   TRP A 216      -8.113  19.857  44.781  1.00 31.54           N  
ANISOU 1779  N   TRP A 216     4116   4090   3776     64    127     50       N  
ATOM   1780  CA  TRP A 216      -6.722  19.493  44.571  1.00 32.01           C  
ANISOU 1780  CA  TRP A 216     4150   4164   3850     67    134     65       C  
ATOM   1781  C   TRP A 216      -6.235  18.522  45.651  1.00 32.90           C  
ANISOU 1781  C   TRP A 216     4245   4274   3984     71    122     81       C  
ATOM   1782  O   TRP A 216      -6.109  18.892  46.818  1.00 30.85           O  
ANISOU 1782  O   TRP A 216     3989   4015   3719     52    102     96       O  
ATOM   1783  CB  TRP A 216      -5.837  20.743  44.499  1.00 31.81           C  
ANISOU 1783  CB  TRP A 216     4121   4154   3813     44    133     79       C  
ATOM   1784  CG  TRP A 216      -4.515  20.458  43.846  1.00 36.03           C  
ANISOU 1784  CG  TRP A 216     4621   4706   4362     48    150     88       C  
ATOM   1785  CD1 TRP A 216      -3.334  20.187  44.473  1.00 35.23           C  
ANISOU 1785  CD1 TRP A 216     4479   4622   4284     43    142    109       C  
ATOM   1786  CD2 TRP A 216      -4.247  20.385  42.435  1.00 34.42           C  
ANISOU 1786  CD2 TRP A 216     4419   4506   4154     58    180     76       C  
ATOM   1787  NE1 TRP A 216      -2.347  19.959  43.546  1.00 37.47           N  
ANISOU 1787  NE1 TRP A 216     4731   4923   4584     53    170    109       N  
ATOM   1788  CE2 TRP A 216      -2.876  20.073  42.288  1.00 35.32           C  
ANISOU 1788  CE2 TRP A 216     4487   4641   4291     60    197     88       C  
ATOM   1789  CE3 TRP A 216      -5.028  20.559  41.286  1.00 37.13           C  
ANISOU 1789  CE3 TRP A 216     4797   4837   4473     63    193     57       C  
ATOM   1790  CZ2 TRP A 216      -2.263  19.931  41.032  1.00 35.04           C  
ANISOU 1790  CZ2 TRP A 216     4444   4614   4256     67    237     78       C  
ATOM   1791  CZ3 TRP A 216      -4.415  20.416  40.027  1.00 38.10           C  
ANISOU 1791  CZ3 TRP A 216     4921   4966   4590     67    226     49       C  
ATOM   1792  CH2 TRP A 216      -3.045  20.107  39.918  1.00 34.37           C  
ANISOU 1792  CH2 TRP A 216     4405   4514   4140     68    252     58       C  
ATOM   1793  N   ASN A 217      -5.972  17.278  45.244  1.00 34.83           N  
ANISOU 1793  N   ASN A 217     4477   4511   4248     97    133     78       N  
ATOM   1794  CA  ASN A 217      -5.615  16.183  46.160  1.00 35.53           C  
ANISOU 1794  CA  ASN A 217     4556   4587   4355    109    120     94       C  
ATOM   1795  C   ASN A 217      -6.731  15.748  47.114  1.00 33.68           C  
ANISOU 1795  C   ASN A 217     4354   4333   4111     97    108     89       C  
ATOM   1796  O   ASN A 217      -6.465  15.138  48.145  1.00 34.44           O  
ANISOU 1796  O   ASN A 217     4454   4418   4212     95     90    107       O  
ATOM   1797  CB  ASN A 217      -4.348  16.510  46.966  1.00 38.21           C  
ANISOU 1797  CB  ASN A 217     4865   4945   4707    101     98    124       C  
ATOM   1798  CG  ASN A 217      -3.087  16.104  46.257  1.00 43.20           C  
ANISOU 1798  CG  ASN A 217     5452   5592   5369    128    113    132       C  
ATOM   1799  OD1 ASN A 217      -2.980  14.985  45.734  1.00 43.10           O  
ANISOU 1799  OD1 ASN A 217     5436   5564   5376    163    131    124       O  
ATOM   1800  ND2 ASN A 217      -2.108  17.009  46.238  1.00 42.08           N  
ANISOU 1800  ND2 ASN A 217     5278   5481   5232    109    108    146       N  
ATOM   1801  N   VAL A 218      -7.977  16.035  46.769  1.00 32.82           N  
ANISOU 1801  N   VAL A 218     4266   4218   3986     87    118     66       N  
ATOM   1802  CA  VAL A 218      -9.095  15.671  47.651  1.00 34.89           C  
ANISOU 1802  CA  VAL A 218     4552   4465   4240     71    114     59       C  
ATOM   1803  C   VAL A 218      -9.235  14.175  47.905  1.00 36.35           C  
ANISOU 1803  C   VAL A 218     4750   4626   4435     79    117     60       C  
ATOM   1804  O   VAL A 218      -9.626  13.776  49.001  1.00 35.87           O  
ANISOU 1804  O   VAL A 218     4710   4551   4368     62    110     67       O  
ATOM   1805  CB  VAL A 218     -10.434  16.250  47.172  1.00 34.17           C  
ANISOU 1805  CB  VAL A 218     4468   4376   4137     63    124     33       C  
ATOM   1806  CG1 VAL A 218     -10.377  17.770  47.221  1.00 33.77           C  
ANISOU 1806  CG1 VAL A 218     4417   4340   4074     55    120     35       C  
ATOM   1807  CG2 VAL A 218     -10.786  15.744  45.759  1.00 29.29           C  
ANISOU 1807  CG2 VAL A 218     3847   3757   3524     79    134     13       C  
ATOM   1808  N   GLU A 219      -8.900  13.356  46.903  1.00 38.96           N  
ANISOU 1808  N   GLU A 219     5076   4948   4780    104    129     52       N  
ATOM   1809  CA  GLU A 219      -8.993  11.902  47.026  1.00 41.94           C  
ANISOU 1809  CA  GLU A 219     5474   5294   5166    115    133     51       C  
ATOM   1810  C   GLU A 219      -7.962  11.353  48.005  1.00 42.82           C  
ANISOU 1810  C   GLU A 219     5585   5393   5290    128    115     83       C  
ATOM   1811  O   GLU A 219      -8.265  10.451  48.789  1.00 44.51           O  
ANISOU 1811  O   GLU A 219     5830   5580   5502    122    107     91       O  
ATOM   1812  CB  GLU A 219      -8.848  11.200  45.670  1.00 43.58           C  
ANISOU 1812  CB  GLU A 219     5685   5491   5382    139    155     33       C  
ATOM   1813  CG  GLU A 219      -9.168   9.697  45.740  1.00 48.80           C  
ANISOU 1813  CG  GLU A 219     6382   6113   6049    145    162     26       C  
ATOM   1814  CD  GLU A 219      -8.978   8.960  44.424  1.00 53.64           C  
ANISOU 1814  CD  GLU A 219     7008   6709   6665    167    186      6       C  
ATOM   1815  OE1 GLU A 219      -9.904   8.217  44.030  1.00 50.69           O  
ANISOU 1815  OE1 GLU A 219     6668   6313   6280    150    194    -16       O  
ATOM   1816  OE2 GLU A 219      -7.909   9.113  43.789  1.00 56.85           O  
ANISOU 1816  OE2 GLU A 219     7394   7124   7085    199    200     10       O  
ATOM   1817  N   SER A 220      -6.749  11.895  47.959  1.00 40.68           N  
ANISOU 1817  N   SER A 220     5279   5143   5033    145    105    102       N  
ATOM   1818  CA  SER A 220      -5.678  11.391  48.808  1.00 39.95           C  
ANISOU 1818  CA  SER A 220     5177   5045   4959    163     79    135       C  
ATOM   1819  C   SER A 220      -5.609  12.086  50.167  1.00 38.43           C  
ANISOU 1819  C   SER A 220     4992   4863   4748    130     45    158       C  
ATOM   1820  O   SER A 220      -5.083  11.514  51.123  1.00 39.97           O  
ANISOU 1820  O   SER A 220     5196   5043   4946    134     15    187       O  
ATOM   1821  CB  SER A 220      -4.321  11.434  48.083  1.00 39.97           C  
ANISOU 1821  CB  SER A 220     5129   5065   4992    199     85    145       C  
ATOM   1822  OG  SER A 220      -4.057  12.707  47.524  1.00 40.03           O  
ANISOU 1822  OG  SER A 220     5108   5109   4993    183     94    138       O  
ATOM   1823  N   PHE A 221      -6.138  13.305  50.261  1.00 33.08           N  
ANISOU 1823  N   PHE A 221     4316   4206   4047     97     49    147       N  
ATOM   1824  CA  PHE A 221      -6.055  14.039  51.514  1.00 32.63           C  
ANISOU 1824  CA  PHE A 221     4274   4156   3968     63     22    165       C  
ATOM   1825  C   PHE A 221      -7.380  14.514  52.115  1.00 33.60           C  
ANISOU 1825  C   PHE A 221     4436   4270   4059     27     36    146       C  
ATOM   1826  O   PHE A 221      -7.787  14.018  53.169  1.00 35.13           O  
ANISOU 1826  O   PHE A 221     4668   4445   4236      7     28    155       O  
ATOM   1827  CB  PHE A 221      -5.056  15.204  51.438  1.00 33.40           C  
ANISOU 1827  CB  PHE A 221     4337   4286   4067     53      7    179       C  
ATOM   1828  CG  PHE A 221      -4.959  15.972  52.721  1.00 33.17           C  
ANISOU 1828  CG  PHE A 221     4332   4261   4009     12    -22    196       C  
ATOM   1829  CD1 PHE A 221      -5.579  17.205  52.857  1.00 31.66           C  
ANISOU 1829  CD1 PHE A 221     4162   4077   3790    -19     -9    179       C  
ATOM   1830  CD2 PHE A 221      -4.292  15.430  53.822  1.00 33.30           C  
ANISOU 1830  CD2 PHE A 221     4359   4271   4023      5    -63    228       C  
ATOM   1831  CE1 PHE A 221      -5.526  17.896  54.060  1.00 31.14           C  
ANISOU 1831  CE1 PHE A 221     4131   4010   3693    -60    -31    191       C  
ATOM   1832  CE2 PHE A 221      -4.226  16.126  55.032  1.00 28.18           C  
ANISOU 1832  CE2 PHE A 221     3744   3624   3340    -39    -92    243       C  
ATOM   1833  CZ  PHE A 221      -4.842  17.352  55.149  1.00 30.93           C  
ANISOU 1833  CZ  PHE A 221     4117   3977   3659    -73    -73    222       C  
ATOM   1834  N   ALA A 222      -8.026  15.486  51.471  1.00 31.76           N  
ANISOU 1834  N   ALA A 222     4196   4052   3819     20     58    122       N  
ATOM   1835  CA  ALA A 222      -9.221  16.129  52.036  1.00 32.88           C  
ANISOU 1835  CA  ALA A 222     4366   4190   3937     -8     74    103       C  
ATOM   1836  C   ALA A 222     -10.343  15.150  52.398  1.00 32.29           C  
ANISOU 1836  C   ALA A 222     4316   4094   3859    -18     92     89       C  
ATOM   1837  O   ALA A 222     -10.899  15.208  53.494  1.00 31.35           O  
ANISOU 1837  O   ALA A 222     4229   3965   3719    -47     98     89       O  
ATOM   1838  CB  ALA A 222      -9.749  17.213  51.091  1.00 30.60           C  
ANISOU 1838  CB  ALA A 222     4061   3916   3649     -2     92     80       C  
ATOM   1839  N   ILE A 223     -10.687  14.267  51.471  1.00 32.28           N  
ANISOU 1839  N   ILE A 223     4303   4086   3877      2    104     75       N  
ATOM   1840  CA  ILE A 223     -11.812  13.365  51.692  1.00 32.87           C  
ANISOU 1840  CA  ILE A 223     4399   4143   3949    -14    123     59       C  
ATOM   1841  C   ILE A 223     -11.539  12.421  52.867  1.00 34.18           C  
ANISOU 1841  C   ILE A 223     4604   4281   4101    -31    112     82       C  
ATOM   1842  O   ILE A 223     -12.345  12.375  53.802  1.00 36.21           O  
ANISOU 1842  O   ILE A 223     4892   4530   4338    -66    126     76       O  
ATOM   1843  CB  ILE A 223     -12.245  12.626  50.404  1.00 31.66           C  
ANISOU 1843  CB  ILE A 223     4231   3985   3813      4    135     38       C  
ATOM   1844  CG1 ILE A 223     -12.949  13.610  49.459  1.00 30.71           C  
ANISOU 1844  CG1 ILE A 223     4082   3889   3695      9    144     14       C  
ATOM   1845  CG2 ILE A 223     -13.163  11.437  50.734  1.00 31.95           C  
ANISOU 1845  CG2 ILE A 223     4295   3998   3846    -20    150     27       C  
ATOM   1846  CD1 ILE A 223     -12.876  13.230  47.988  1.00 27.00           C  
ANISOU 1846  CD1 ILE A 223     3599   3421   3237     31    146      0       C  
ATOM   1847  N   PRO A 224     -10.398  11.694  52.843  1.00 33.75           N  
ANISOU 1847  N   PRO A 224     4553   4214   4059     -6     87    108       N  
ATOM   1848  CA  PRO A 224     -10.118  10.818  53.979  1.00 34.13           C  
ANISOU 1848  CA  PRO A 224     4644   4231   4092    -20     69    134       C  
ATOM   1849  C   PRO A 224      -9.867  11.538  55.303  1.00 34.86           C  
ANISOU 1849  C   PRO A 224     4763   4329   4155    -51     49    154       C  
ATOM   1850  O   PRO A 224     -10.193  10.986  56.359  1.00 33.88           O  
ANISOU 1850  O   PRO A 224     4690   4180   4004    -81     46    166       O  
ATOM   1851  CB  PRO A 224      -8.867  10.035  53.543  1.00 35.80           C  
ANISOU 1851  CB  PRO A 224     4841   4430   4330     26     43    158       C  
ATOM   1852  CG  PRO A 224      -8.327  10.753  52.354  1.00 34.89           C  
ANISOU 1852  CG  PRO A 224     4671   4346   4239     55     50    147       C  
ATOM   1853  CD  PRO A 224      -9.468  11.457  51.721  1.00 32.97           C  
ANISOU 1853  CD  PRO A 224     4420   4121   3988     36     81    112       C  
ATOM   1854  N   TYR A 225      -9.303  12.746  55.267  1.00 32.67           N  
ANISOU 1854  N   TYR A 225     4458   4080   3876    -51     36    158       N  
ATOM   1855  CA  TYR A 225      -9.103  13.473  56.520  1.00 33.88           C  
ANISOU 1855  CA  TYR A 225     4644   4235   3994    -87     18    174       C  
ATOM   1856  C   TYR A 225     -10.437  13.842  57.156  1.00 32.36           C  
ANISOU 1856  C   TYR A 225     4488   4036   3772   -126     58    148       C  
ATOM   1857  O   TYR A 225     -10.641  13.621  58.352  1.00 32.65           O  
ANISOU 1857  O   TYR A 225     4579   4054   3774   -163     55    159       O  
ATOM   1858  CB  TYR A 225      -8.203  14.716  56.391  1.00 32.60           C  
ANISOU 1858  CB  TYR A 225     4452   4101   3832    -86     -4    184       C  
ATOM   1859  CG  TYR A 225      -7.623  15.078  57.739  1.00 32.08           C  
ANISOU 1859  CG  TYR A 225     4427   4032   3732   -122    -41    211       C  
ATOM   1860  CD1 TYR A 225      -8.388  15.759  58.687  1.00 33.40           C  
ANISOU 1860  CD1 TYR A 225     4644   4190   3856   -167    -21    198       C  
ATOM   1861  CD2 TYR A 225      -6.327  14.694  58.094  1.00 32.27           C  
ANISOU 1861  CD2 TYR A 225     4439   4059   3763   -112    -95    251       C  
ATOM   1862  CE1 TYR A 225      -7.879  16.056  59.951  1.00 30.25           C  
ANISOU 1862  CE1 TYR A 225     4295   3784   3415   -206    -55    223       C  
ATOM   1863  CE2 TYR A 225      -5.805  14.993  59.356  1.00 31.18           C  
ANISOU 1863  CE2 TYR A 225     4342   3916   3588   -150   -138    278       C  
ATOM   1864  CZ  TYR A 225      -6.589  15.676  60.274  1.00 33.29           C  
ANISOU 1864  CZ  TYR A 225     4671   4173   3806   -200   -117    264       C  
ATOM   1865  OH  TYR A 225      -6.097  15.980  61.526  1.00 36.50           O  
ANISOU 1865  OH  TYR A 225     5129   4573   4167   -244   -159    289       O  
ATOM   1866  N   VAL A 226     -11.329  14.408  56.350  1.00 30.54           N  
ANISOU 1866  N   VAL A 226     4227   3820   3555   -119     94    114       N  
ATOM   1867  CA  VAL A 226     -12.656  14.782  56.810  1.00 30.49           C  
ANISOU 1867  CA  VAL A 226     4239   3812   3533   -148    137     85       C  
ATOM   1868  C   VAL A 226     -13.409  13.555  57.331  1.00 31.05           C  
ANISOU 1868  C   VAL A 226     4343   3859   3594   -173    157     81       C  
ATOM   1869  O   VAL A 226     -13.961  13.594  58.427  1.00 32.14           O  
ANISOU 1869  O   VAL A 226     4526   3985   3700   -213    179     78       O  
ATOM   1870  CB  VAL A 226     -13.449  15.511  55.698  1.00 29.08           C  
ANISOU 1870  CB  VAL A 226     4013   3656   3380   -125    163     52       C  
ATOM   1871  CG1 VAL A 226     -14.941  15.518  55.982  1.00 28.67           C  
ANISOU 1871  CG1 VAL A 226     3963   3604   3327   -146    209     20       C  
ATOM   1872  CG2 VAL A 226     -12.942  16.927  55.540  1.00 27.67           C  
ANISOU 1872  CG2 VAL A 226     3824   3493   3197   -116    153     53       C  
ATOM   1873  N   TYR A 227     -13.398  12.470  56.555  1.00 31.00           N  
ANISOU 1873  N   TYR A 227     4323   3844   3612   -153    152     82       N  
ATOM   1874  CA  TYR A 227     -14.085  11.233  56.928  1.00 31.45           C  
ANISOU 1874  CA  TYR A 227     4415   3873   3660   -179    171     79       C  
ATOM   1875  C   TYR A 227     -13.576  10.636  58.246  1.00 33.90           C  
ANISOU 1875  C   TYR A 227     4794   4152   3935   -207    150    112       C  
ATOM   1876  O   TYR A 227     -14.369  10.227  59.093  1.00 33.64           O  
ANISOU 1876  O   TYR A 227     4807   4102   3874   -252    179    105       O  
ATOM   1877  CB  TYR A 227     -13.954  10.194  55.817  1.00 30.80           C  
ANISOU 1877  CB  TYR A 227     4315   3780   3608   -151    163     76       C  
ATOM   1878  CG  TYR A 227     -14.666   8.896  56.116  1.00 33.43           C  
ANISOU 1878  CG  TYR A 227     4689   4081   3931   -182    182     72       C  
ATOM   1879  CD1 TYR A 227     -16.006   8.722  55.775  1.00 31.95           C  
ANISOU 1879  CD1 TYR A 227     4485   3903   3750   -211    221     37       C  
ATOM   1880  CD2 TYR A 227     -13.996   7.836  56.735  1.00 34.54           C  
ANISOU 1880  CD2 TYR A 227     4886   4180   4057   -184    158    104       C  
ATOM   1881  CE1 TYR A 227     -16.659   7.533  56.039  1.00 36.79           C  
ANISOU 1881  CE1 TYR A 227     5139   4486   4353   -249    241     32       C  
ATOM   1882  CE2 TYR A 227     -14.641   6.640  57.006  1.00 35.59           C  
ANISOU 1882  CE2 TYR A 227     5068   4277   4177   -216    176    101       C  
ATOM   1883  CZ  TYR A 227     -15.972   6.498  56.653  1.00 36.65           C  
ANISOU 1883  CZ  TYR A 227     5187   4423   4316   -253    219     64       C  
ATOM   1884  OH  TYR A 227     -16.621   5.330  56.913  1.00 37.85           O  
ANISOU 1884  OH  TYR A 227     5388   4540   4455   -294    239     60       O  
ATOM   1885  N   ASN A 228     -12.255  10.585  58.397  1.00 35.83           N  
ANISOU 1885  N   ASN A 228     5044   4390   4179   -182    101    147       N  
ATOM   1886  CA  ASN A 228     -11.615  10.014  59.578  1.00 35.14           C  
ANISOU 1886  CA  ASN A 228     5020   4273   4059   -201     66    185       C  
ATOM   1887  C   ASN A 228     -11.715  10.887  60.816  1.00 36.49           C  
ANISOU 1887  C   ASN A 228     5235   4448   4183   -247     67    190       C  
ATOM   1888  O   ASN A 228     -11.827  10.371  61.932  1.00 35.63           O  
ANISOU 1888  O   ASN A 228     5196   4309   4031   -286     62    208       O  
ATOM   1889  CB  ASN A 228     -10.158   9.673  59.288  1.00 34.65           C  
ANISOU 1889  CB  ASN A 228     4937   4207   4020   -154      8    222       C  
ATOM   1890  CG  ASN A 228     -10.011   8.383  58.502  1.00 36.06           C  
ANISOU 1890  CG  ASN A 228     5110   4359   4230   -117      6    226       C  
ATOM   1891  OD1 ASN A 228     -10.362   7.313  58.982  1.00 41.70           O  
ANISOU 1891  OD1 ASN A 228     5882   5033   4928   -134      9    235       O  
ATOM   1892  ND2 ASN A 228      -9.492   8.482  57.288  1.00 36.48           N  
ANISOU 1892  ND2 ASN A 228     5103   4432   4327    -68      4    217       N  
ATOM   1893  N   ARG A 229     -11.679  12.203  60.614  1.00 36.16           N  
ANISOU 1893  N   ARG A 229     5158   4438   4144   -244     75    174       N  
ATOM   1894  CA  ARG A 229     -11.801  13.154  61.716  1.00 35.26           C  
ANISOU 1894  CA  ARG A 229     5089   4325   3984   -287     82    172       C  
ATOM   1895  C   ARG A 229     -13.205  13.102  62.296  1.00 35.80           C  
ANISOU 1895  C   ARG A 229     5193   4382   4026   -330    148    141       C  
ATOM   1896  O   ARG A 229     -13.380  13.118  63.516  1.00 35.68           O  
ANISOU 1896  O   ARG A 229     5249   4348   3960   -378    157    148       O  
ATOM   1897  CB  ARG A 229     -11.466  14.580  61.254  1.00 34.28           C  
ANISOU 1897  CB  ARG A 229     4922   4232   3871   -272     80    160       C  
ATOM   1898  CG  ARG A 229     -11.502  15.628  62.355  1.00 33.93           C  
ANISOU 1898  CG  ARG A 229     4930   4185   3777   -315     86    157       C  
ATOM   1899  CD  ARG A 229     -10.328  15.474  63.325  1.00 35.64           C  
ANISOU 1899  CD  ARG A 229     5196   4390   3957   -340     21    201       C  
ATOM   1900  NE  ARG A 229     -10.447  16.352  64.490  1.00 34.36           N  
ANISOU 1900  NE  ARG A 229     5103   4218   3735   -392     30    197       N  
ATOM   1901  CZ  ARG A 229      -9.690  16.257  65.584  1.00 38.81           C  
ANISOU 1901  CZ  ARG A 229     5731   4767   4250   -431    -21    232       C  
ATOM   1902  NH1 ARG A 229      -8.754  15.312  65.675  1.00 32.31           N  
ANISOU 1902  NH1 ARG A 229     4904   3937   3435   -416    -88    275       N  
ATOM   1903  NH2 ARG A 229      -9.876  17.102  66.599  1.00 37.06           N  
ANISOU 1903  NH2 ARG A 229     5579   4534   3969   -483     -7    222       N  
ATOM   1904  N   ILE A 230     -14.202  13.043  61.414  1.00 36.20           N  
ANISOU 1904  N   ILE A 230     5193   4447   4112   -315    194    105       N  
ATOM   1905  CA  ILE A 230     -15.597  12.917  61.842  1.00 34.66           C  
ANISOU 1905  CA  ILE A 230     5014   4249   3905   -353    260     72       C  
ATOM   1906  C   ILE A 230     -15.807  11.561  62.510  1.00 34.66           C  
ANISOU 1906  C   ILE A 230     5075   4215   3879   -391    264     88       C  
ATOM   1907  O   ILE A 230     -16.430  11.487  63.580  1.00 36.52           O  
ANISOU 1907  O   ILE A 230     5370   4434   4071   -444    303     81       O  
ATOM   1908  CB  ILE A 230     -16.599  13.180  60.686  1.00 33.36           C  
ANISOU 1908  CB  ILE A 230     4772   4113   3789   -327    298     32       C  
ATOM   1909  CG1 ILE A 230     -16.537  14.656  60.263  1.00 29.77           C  
ANISOU 1909  CG1 ILE A 230     4277   3685   3350   -297    301     16       C  
ATOM   1910  CG2 ILE A 230     -18.019  12.815  61.102  1.00 34.50           C  
ANISOU 1910  CG2 ILE A 230     4923   4257   3929   -368    364      1       C  
ATOM   1911  CD1 ILE A 230     -17.303  14.983  58.982  1.00 31.19           C  
ANISOU 1911  CD1 ILE A 230     4379   3891   3578   -261    319    -14       C  
ATOM   1912  N   LYS A 231     -15.252  10.510  61.903  1.00 34.39           N  
ANISOU 1912  N   LYS A 231     5034   4165   3867   -364    226    110       N  
ATOM   1913  CA  LYS A 231     -15.271   9.168  62.485  1.00 36.49           C  
ANISOU 1913  CA  LYS A 231     5367   4389   4108   -394    219    132       C  
ATOM   1914  C   LYS A 231     -14.664   9.129  63.893  1.00 37.57           C  
ANISOU 1914  C   LYS A 231     5593   4498   4185   -430    191    168       C  
ATOM   1915  O   LYS A 231     -15.259   8.566  64.809  1.00 38.86           O  
ANISOU 1915  O   LYS A 231     5828   4633   4305   -484    220    169       O  
ATOM   1916  CB  LYS A 231     -14.570   8.155  61.574  1.00 37.00           C  
ANISOU 1916  CB  LYS A 231     5413   4436   4208   -347    178    153       C  
ATOM   1917  CG  LYS A 231     -14.725   6.698  62.050  1.00 40.68           C  
ANISOU 1917  CG  LYS A 231     5952   4851   4651   -375    176    172       C  
ATOM   1918  CD  LYS A 231     -14.053   5.688  61.122  1.00 42.88           C  
ANISOU 1918  CD  LYS A 231     6218   5107   4967   -324    140    188       C  
ATOM   1919  CE  LYS A 231     -12.580   5.488  61.470  1.00 50.53           C  
ANISOU 1919  CE  LYS A 231     7209   6056   5934   -282     69    238       C  
ATOM   1920  NZ  LYS A 231     -11.979   4.349  60.718  1.00 51.76           N  
ANISOU 1920  NZ  LYS A 231     7364   6178   6122   -232     43    254       N  
ATOM   1921  N   ASN A 232     -13.488   9.733  64.057  1.00 37.83           N  
ANISOU 1921  N   ASN A 232     5622   4539   4213   -404    133    197       N  
ATOM   1922  CA  ASN A 232     -12.814   9.784  65.355  1.00 41.21           C  
ANISOU 1922  CA  ASN A 232     6131   4943   4583   -438     92    233       C  
ATOM   1923  C   ASN A 232     -13.573  10.569  66.430  1.00 41.90           C  
ANISOU 1923  C   ASN A 232     6275   5031   4614   -500    142    211       C  
ATOM   1924  O   ASN A 232     -13.499  10.232  67.609  1.00 45.16           O  
ANISOU 1924  O   ASN A 232     6781   5413   4966   -550    133    234       O  
ATOM   1925  CB  ASN A 232     -11.396  10.343  65.206  1.00 41.37           C  
ANISOU 1925  CB  ASN A 232     6121   4981   4618   -399     17    266       C  
ATOM   1926  CG  ASN A 232     -10.435   9.363  64.538  1.00 43.66           C  
ANISOU 1926  CG  ASN A 232     6380   5258   4949   -342    -40    300       C  
ATOM   1927  OD1 ASN A 232     -10.736   8.177  64.361  1.00 45.48           O  
ANISOU 1927  OD1 ASN A 232     6634   5457   5188   -336    -32    305       O  
ATOM   1928  ND2 ASN A 232      -9.265   9.861  64.168  1.00 43.76           N  
ANISOU 1928  ND2 ASN A 232     6340   5295   4989   -303    -95    322       N  
ATOM   1929  N   ILE A 233     -14.302  11.607  66.017  1.00 41.57           N  
ANISOU 1929  N   ILE A 233     6181   5021   4591   -497    197    168       N  
ATOM   1930  CA  ILE A 233     -15.046  12.467  66.943  1.00 38.99           C  
ANISOU 1930  CA  ILE A 233     5900   4695   4218   -547    255    140       C  
ATOM   1931  C   ILE A 233     -16.463  11.959  67.234  1.00 40.14           C  
ANISOU 1931  C   ILE A 233     6064   4833   4355   -589    339    106       C  
ATOM   1932  O   ILE A 233     -16.915  12.003  68.379  1.00 41.73           O  
ANISOU 1932  O   ILE A 233     6344   5014   4497   -648    380    100       O  
ATOM   1933  CB  ILE A 233     -15.101  13.937  66.446  1.00 38.09           C  
ANISOU 1933  CB  ILE A 233     5728   4615   4129   -519    272    111       C  
ATOM   1934  CG1 ILE A 233     -13.702  14.568  66.464  1.00 38.46           C  
ANISOU 1934  CG1 ILE A 233     5776   4669   4168   -499    195    144       C  
ATOM   1935  CG2 ILE A 233     -16.045  14.781  67.305  1.00 35.91           C  
ANISOU 1935  CG2 ILE A 233     5495   4337   3813   -562    347     74       C  
ATOM   1936  CD1 ILE A 233     -13.596  15.864  65.674  1.00 37.23           C  
ANISOU 1936  CD1 ILE A 233     5555   4544   4047   -463    201    121       C  
ATOM   1937  N   PHE A 234     -17.150  11.468  66.205  1.00 39.37           N  
ANISOU 1937  N   PHE A 234     5893   4751   4313   -563    367     83       N  
ATOM   1938  CA  PHE A 234     -18.574  11.154  66.320  1.00 38.74           C  
ANISOU 1938  CA  PHE A 234     5805   4676   4237   -602    450     43       C  
ATOM   1939  C   PHE A 234     -18.883   9.674  66.164  1.00 38.48           C  
ANISOU 1939  C   PHE A 234     5794   4618   4208   -625    452     55       C  
ATOM   1940  O   PHE A 234     -19.904   9.207  66.653  1.00 37.00           O  
ANISOU 1940  O   PHE A 234     5633   4423   4002   -680    516     33       O  
ATOM   1941  CB  PHE A 234     -19.380  11.946  65.283  1.00 37.38           C  
ANISOU 1941  CB  PHE A 234     5528   4548   4128   -563    490     -1       C  
ATOM   1942  CG  PHE A 234     -19.316  13.440  65.463  1.00 36.99           C  
ANISOU 1942  CG  PHE A 234     5464   4517   4074   -544    505    -19       C  
ATOM   1943  CD1 PHE A 234     -18.529  14.223  64.619  1.00 35.21           C  
ANISOU 1943  CD1 PHE A 234     5188   4310   3881   -486    454    -10       C  
ATOM   1944  CD2 PHE A 234     -20.048  14.070  66.475  1.00 36.77           C  
ANISOU 1944  CD2 PHE A 234     5478   4485   4009   -585    574    -46       C  
ATOM   1945  CE1 PHE A 234     -18.472  15.619  64.777  1.00 36.32           C  
ANISOU 1945  CE1 PHE A 234     5323   4461   4015   -471    468    -27       C  
ATOM   1946  CE2 PHE A 234     -20.001  15.460  66.637  1.00 35.89           C  
ANISOU 1946  CE2 PHE A 234     5361   4383   3892   -566    591    -65       C  
ATOM   1947  CZ  PHE A 234     -19.215  16.234  65.788  1.00 34.93           C  
ANISOU 1947  CZ  PHE A 234     5193   4277   3802   -509    535    -55       C  
ATOM   1948  N   GLY A 235     -18.002   8.946  65.481  1.00 39.78           N  
ANISOU 1948  N   GLY A 235     5948   4769   4396   -584    384     87       N  
ATOM   1949  CA  GLY A 235     -18.243   7.541  65.158  1.00 40.89           C  
ANISOU 1949  CA  GLY A 235     6108   4882   4546   -597    382     96       C  
ATOM   1950  C   GLY A 235     -18.500   7.349  63.679  1.00 41.30           C  
ANISOU 1950  C   GLY A 235     6068   4959   4666   -551    379     74       C  
ATOM   1951  O   GLY A 235     -18.676   8.321  62.946  1.00 42.23           O  
ANISOU 1951  O   GLY A 235     6105   5118   4822   -514    387     49       O  
ATOM   1952  N   GLU A 236     -18.531   6.092  63.246  1.00 43.62           N  
ANISOU 1952  N   GLU A 236     6381   5223   4970   -555    367     84       N  
ATOM   1953  CA  GLU A 236     -18.677   5.747  61.832  1.00 46.75           C  
ANISOU 1953  CA  GLU A 236     6706   5634   5422   -515    358     67       C  
ATOM   1954  C   GLU A 236     -19.970   6.254  61.173  1.00 47.45           C  
ANISOU 1954  C   GLU A 236     6714   5770   5546   -529    413     16       C  
ATOM   1955  O   GLU A 236     -19.927   6.784  60.059  1.00 48.35           O  
ANISOU 1955  O   GLU A 236     6750   5917   5705   -481    398      0       O  
ATOM   1956  CB  GLU A 236     -18.522   4.237  61.622  1.00 50.09           C  
ANISOU 1956  CB  GLU A 236     7184   6007   5841   -525    341     85       C  
ATOM   1957  CG  GLU A 236     -17.092   3.805  61.294  1.00 57.77           C  
ANISOU 1957  CG  GLU A 236     8176   6950   6824   -461    270    126       C  
ATOM   1958  CD  GLU A 236     -16.959   2.312  60.980  1.00 64.75           C  
ANISOU 1958  CD  GLU A 236     9116   7779   7709   -461    256    141       C  
ATOM   1959  OE1 GLU A 236     -17.814   1.761  60.245  1.00 64.44           O  
ANISOU 1959  OE1 GLU A 236     9056   7739   7687   -484    289    110       O  
ATOM   1960  OE2 GLU A 236     -15.982   1.690  61.463  1.00 68.28           O  
ANISOU 1960  OE2 GLU A 236     9627   8180   8138   -438    209    184       O  
ATOM   1961  N   SER A 237     -21.107   6.087  61.854  1.00 46.32           N  
ANISOU 1961  N   SER A 237     6586   5629   5383   -596    476     -7       N  
ATOM   1962  CA  SER A 237     -22.422   6.431  61.285  1.00 44.63           C  
ANISOU 1962  CA  SER A 237     6289   5460   5207   -613    529    -54       C  
ATOM   1963  C   SER A 237     -22.513   7.897  60.869  1.00 42.46           C  
ANISOU 1963  C   SER A 237     5934   5234   4964   -564    531    -75       C  
ATOM   1964  O   SER A 237     -23.148   8.239  59.866  1.00 40.69           O  
ANISOU 1964  O   SER A 237     5625   5048   4788   -541    537   -103       O  
ATOM   1965  CB  SER A 237     -23.545   6.112  62.275  1.00 45.54           C  
ANISOU 1965  CB  SER A 237     6435   5573   5294   -695    603    -75       C  
ATOM   1966  OG  SER A 237     -23.700   7.149  63.237  1.00 47.25           O  
ANISOU 1966  OG  SER A 237     6662   5804   5486   -705    641    -84       O  
ATOM   1967  N   THR A 238     -21.882   8.760  61.657  1.00 38.34           N  
ANISOU 1967  N   THR A 238     5445   4707   4413   -551    525    -60       N  
ATOM   1968  CA  THR A 238     -21.860  10.174  61.351  1.00 35.13           C  
ANISOU 1968  CA  THR A 238     4980   4336   4030   -505    526    -76       C  
ATOM   1969  C   THR A 238     -20.943  10.436  60.142  1.00 34.20           C  
ANISOU 1969  C   THR A 238     4820   4229   3947   -437    461    -61       C  
ATOM   1970  O   THR A 238     -21.323  11.169  59.234  1.00 35.78           O  
ANISOU 1970  O   THR A 238     4946   4463   4187   -400    462    -83       O  
ATOM   1971  CB  THR A 238     -21.450  11.000  62.590  1.00 35.49           C  
ANISOU 1971  CB  THR A 238     5086   4370   4027   -520    540    -66       C  
ATOM   1972  OG1 THR A 238     -22.262  10.617  63.710  1.00 37.30           O  
ANISOU 1972  OG1 THR A 238     5368   4585   4218   -589    604    -80       O  
ATOM   1973  CG2 THR A 238     -21.633  12.483  62.345  1.00 33.23           C  
ANISOU 1973  CG2 THR A 238     4747   4115   3764   -480    555    -90       C  
ATOM   1974  N   ALA A 239     -19.761   9.821  60.122  1.00 31.99           N  
ANISOU 1974  N   ALA A 239     4586   3919   3650   -421    407    -23       N  
ATOM   1975  CA  ALA A 239     -18.839   9.955  58.985  1.00 35.12           C  
ANISOU 1975  CA  ALA A 239     4944   4323   4077   -360    353    -10       C  
ATOM   1976  C   ALA A 239     -19.487   9.525  57.675  1.00 35.02           C  
ANISOU 1976  C   ALA A 239     4871   4328   4107   -344    356    -34       C  
ATOM   1977  O   ALA A 239     -19.281  10.155  56.637  1.00 34.24           O  
ANISOU 1977  O   ALA A 239     4717   4254   4039   -299    336    -42       O  
ATOM   1978  CB  ALA A 239     -17.553   9.163  59.221  1.00 32.77           C  
ANISOU 1978  CB  ALA A 239     4701   3988   3761   -346    301     33       C  
ATOM   1979  N   LYS A 240     -20.282   8.459  57.742  1.00 36.44           N  
ANISOU 1979  N   LYS A 240     5068   4494   4285   -389    382    -45       N  
ATOM   1980  CA  LYS A 240     -20.940   7.896  56.564  1.00 38.31           C  
ANISOU 1980  CA  LYS A 240     5257   4743   4555   -387    383    -68       C  
ATOM   1981  C   LYS A 240     -22.053   8.784  55.990  1.00 38.29           C  
ANISOU 1981  C   LYS A 240     5171   4790   4587   -383    408   -105       C  
ATOM   1982  O   LYS A 240     -22.615   8.475  54.938  1.00 41.35           O  
ANISOU 1982  O   LYS A 240     5514   5195   5003   -381    400   -124       O  
ATOM   1983  CB  LYS A 240     -21.459   6.493  56.869  1.00 39.76           C  
ANISOU 1983  CB  LYS A 240     5490   4893   4723   -445    402    -69       C  
ATOM   1984  CG  LYS A 240     -20.351   5.487  57.139  1.00 42.62           C  
ANISOU 1984  CG  LYS A 240     5933   5201   5060   -435    368    -32       C  
ATOM   1985  CD  LYS A 240     -20.909   4.124  57.505  1.00 45.76           C  
ANISOU 1985  CD  LYS A 240     6391   5558   5437   -496    390    -32       C  
ATOM   1986  CE  LYS A 240     -19.842   3.054  57.389  1.00 47.80           C  
ANISOU 1986  CE  LYS A 240     6720   5759   5683   -470    349      1       C  
ATOM   1987  NZ  LYS A 240     -20.443   1.695  57.484  1.00 49.39           N  
ANISOU 1987  NZ  LYS A 240     6981   5916   5867   -528    369     -3       N  
ATOM   1988  N   ARG A 241     -22.352   9.891  56.661  1.00 36.17           N  
ANISOU 1988  N   ARG A 241     4885   4543   4316   -380    435   -115       N  
ATOM   1989  CA  ARG A 241     -23.311  10.866  56.136  1.00 35.30           C  
ANISOU 1989  CA  ARG A 241     4694   4477   4242   -361    455   -147       C  
ATOM   1990  C   ARG A 241     -22.757  11.623  54.919  1.00 33.65           C  
ANISOU 1990  C   ARG A 241     4443   4285   4058   -297    407   -142       C  
ATOM   1991  O   ARG A 241     -23.498  12.305  54.212  1.00 34.77           O  
ANISOU 1991  O   ARG A 241     4518   4459   4232   -274    408   -165       O  
ATOM   1992  CB  ARG A 241     -23.766  11.834  57.233  1.00 34.12           C  
ANISOU 1992  CB  ARG A 241     4546   4337   4081   -372    503   -160       C  
ATOM   1993  CG  ARG A 241     -24.757  11.207  58.229  1.00 36.56           C  
ANISOU 1993  CG  ARG A 241     4872   4644   4376   -441    567   -177       C  
ATOM   1994  CD  ARG A 241     -25.063  12.151  59.383  1.00 33.90           C  
ANISOU 1994  CD  ARG A 241     4552   4310   4019   -451    621   -190       C  
ATOM   1995  NE  ARG A 241     -25.651  13.406  58.921  1.00 38.56           N  
ANISOU 1995  NE  ARG A 241     5066   4936   4650   -403    634   -216       N  
ATOM   1996  CZ  ARG A 241     -25.604  14.563  59.580  1.00 37.59           C  
ANISOU 1996  CZ  ARG A 241     4956   4811   4515   -383    663   -224       C  
ATOM   1997  NH1 ARG A 241     -24.992  14.653  60.754  1.00 38.67           N  
ANISOU 1997  NH1 ARG A 241     5179   4916   4597   -412    680   -209       N  
ATOM   1998  NH2 ARG A 241     -26.172  15.636  59.055  1.00 32.11           N  
ANISOU 1998  NH2 ARG A 241     4193   4144   3863   -334    672   -247       N  
ATOM   1999  N   LEU A 242     -21.455  11.495  54.689  1.00 32.06           N  
ANISOU 1999  N   LEU A 242     4281   4061   3841   -269    366   -113       N  
ATOM   2000  CA  LEU A 242     -20.816  12.001  53.470  1.00 32.63           C  
ANISOU 2000  CA  LEU A 242     4323   4144   3931   -216    324   -107       C  
ATOM   2001  C   LEU A 242     -21.262  11.238  52.221  1.00 31.80           C  
ANISOU 2001  C   LEU A 242     4189   4047   3848   -216    307   -121       C  
ATOM   2002  O   LEU A 242     -21.113  11.731  51.110  1.00 31.87           O  
ANISOU 2002  O   LEU A 242     4166   4072   3873   -180    280   -125       O  
ATOM   2003  CB  LEU A 242     -19.287  11.965  53.604  1.00 30.95           C  
ANISOU 2003  CB  LEU A 242     4155   3906   3697   -191    291    -73       C  
ATOM   2004  CG  LEU A 242     -18.718  12.920  54.660  1.00 31.17           C  
ANISOU 2004  CG  LEU A 242     4210   3932   3703   -190    295    -59       C  
ATOM   2005  CD1 LEU A 242     -17.260  12.589  54.963  1.00 32.53           C  
ANISOU 2005  CD1 LEU A 242     4425   4080   3855   -178    259    -22       C  
ATOM   2006  CD2 LEU A 242     -18.861  14.370  54.205  1.00 32.86           C  
ANISOU 2006  CD2 LEU A 242     4385   4171   3931   -156    294    -71       C  
ATOM   2007  N   SER A 243     -21.810  10.042  52.409  1.00 32.33           N  
ANISOU 2007  N   SER A 243     4274   4099   3910   -262    323   -129       N  
ATOM   2008  CA  SER A 243     -22.437   9.312  51.317  1.00 34.64           C  
ANISOU 2008  CA  SER A 243     4542   4399   4220   -275    310   -147       C  
ATOM   2009  C   SER A 243     -23.951   9.445  51.390  1.00 36.70           C  
ANISOU 2009  C   SER A 243     4744   4694   4504   -312    338   -178       C  
ATOM   2010  O   SER A 243     -24.543   9.127  52.431  1.00 39.82           O  
ANISOU 2010  O   SER A 243     5151   5087   4892   -358    380   -184       O  
ATOM   2011  CB  SER A 243     -22.053   7.833  51.357  1.00 33.02           C  
ANISOU 2011  CB  SER A 243     4399   4151   3996   -304    307   -136       C  
ATOM   2012  OG  SER A 243     -23.003   7.046  50.664  1.00 30.27           O  
ANISOU 2012  OG  SER A 243     4032   3809   3658   -343    309   -160       O  
ATOM   2013  N   PRO A 244     -24.589   9.878  50.279  1.00 35.63           N  
ANISOU 2013  N   PRO A 244     4547   4593   4396   -293    315   -196       N  
ATOM   2014  CA  PRO A 244     -26.046  10.056  50.250  1.00 36.52           C  
ANISOU 2014  CA  PRO A 244     4588   4746   4540   -322    334   -225       C  
ATOM   2015  C   PRO A 244     -26.820   8.766  50.515  1.00 37.26           C  
ANISOU 2015  C   PRO A 244     4692   4835   4632   -396    358   -239       C  
ATOM   2016  O   PRO A 244     -28.010   8.824  50.810  1.00 38.68           O  
ANISOU 2016  O   PRO A 244     4813   5048   4836   -431    387   -263       O  
ATOM   2017  CB  PRO A 244     -26.324  10.554  48.828  1.00 35.13           C  
ANISOU 2017  CB  PRO A 244     4362   4599   4388   -286    286   -234       C  
ATOM   2018  CG  PRO A 244     -25.099  10.201  48.037  1.00 36.90           C  
ANISOU 2018  CG  PRO A 244     4644   4791   4586   -260    249   -214       C  
ATOM   2019  CD  PRO A 244     -23.964  10.263  49.003  1.00 35.75           C  
ANISOU 2019  CD  PRO A 244     4557   4612   4416   -245    268   -190       C  
ATOM   2020  N   HIS A 245     -26.150   7.623  50.410  1.00 36.97           N  
ANISOU 2020  N   HIS A 245     4726   4754   4566   -418    347   -226       N  
ATOM   2021  CA  HIS A 245     -26.768   6.331  50.704  1.00 36.46           C  
ANISOU 2021  CA  HIS A 245     4689   4673   4492   -493    370   -236       C  
ATOM   2022  C   HIS A 245     -26.223   5.738  52.002  1.00 38.24           C  
ANISOU 2022  C   HIS A 245     4995   4853   4682   -521    405   -216       C  
ATOM   2023  O   HIS A 245     -26.531   4.598  52.344  1.00 38.30           O  
ANISOU 2023  O   HIS A 245     5048   4832   4672   -582    424   -219       O  
ATOM   2024  CB  HIS A 245     -26.532   5.353  49.555  1.00 34.49           C  
ANISOU 2024  CB  HIS A 245     4472   4400   4233   -504    332   -238       C  
ATOM   2025  CG  HIS A 245     -26.727   5.951  48.198  1.00 31.66           C  
ANISOU 2025  CG  HIS A 245     4058   4075   3896   -468    287   -250       C  
ATOM   2026  ND1 HIS A 245     -27.884   6.602  47.829  1.00 32.16           N  
ANISOU 2026  ND1 HIS A 245     4031   4194   3993   -475    280   -272       N  
ATOM   2027  CD2 HIS A 245     -25.915   5.983  47.115  1.00 31.07           C  
ANISOU 2027  CD2 HIS A 245     4010   3985   3811   -424    247   -242       C  
ATOM   2028  CE1 HIS A 245     -27.773   7.017  46.580  1.00 32.97           C  
ANISOU 2028  CE1 HIS A 245     4112   4312   4103   -439    230   -274       C  
ATOM   2029  NE2 HIS A 245     -26.588   6.654  46.123  1.00 31.62           N  
ANISOU 2029  NE2 HIS A 245     4012   4098   3902   -410    213   -258       N  
ATOM   2030  N   ARG A 246     -25.405   6.516  52.710  1.00 39.05           N  
ANISOU 2030  N   ARG A 246     5119   4946   4771   -478    409   -195       N  
ATOM   2031  CA  ARG A 246     -24.793   6.095  53.984  1.00 41.29           C  
ANISOU 2031  CA  ARG A 246     5483   5188   5018   -499    432   -172       C  
ATOM   2032  C   ARG A 246     -23.942   4.821  53.869  1.00 41.30           C  
ANISOU 2032  C   ARG A 246     5569   5131   4992   -506    409   -148       C  
ATOM   2033  O   ARG A 246     -23.877   4.013  54.802  1.00 38.62           O  
ANISOU 2033  O   ARG A 246     5299   4752   4622   -550    430   -135       O  
ATOM   2034  CB  ARG A 246     -25.847   5.943  55.101  1.00 42.58           C  
ANISOU 2034  CB  ARG A 246     5644   5361   5173   -568    493   -188       C  
ATOM   2035  CG  ARG A 246     -26.852   7.094  55.226  1.00 48.06           C  
ANISOU 2035  CG  ARG A 246     6248   6113   5900   -562    526   -217       C  
ATOM   2036  CD  ARG A 246     -26.188   8.409  55.651  1.00 53.99           C  
ANISOU 2036  CD  ARG A 246     6997   6870   6647   -502    522   -205       C  
ATOM   2037  NE  ARG A 246     -27.184   9.439  55.951  1.00 60.97           N  
ANISOU 2037  NE  ARG A 246     7808   7798   7560   -498    565   -233       N  
ATOM   2038  CZ  ARG A 246     -27.626  10.348  55.081  1.00 63.58           C  
ANISOU 2038  CZ  ARG A 246     8055   8169   7934   -450    546   -250       C  
ATOM   2039  NH1 ARG A 246     -27.161  10.383  53.837  1.00 63.32           N  
ANISOU 2039  NH1 ARG A 246     8005   8139   7914   -408    485   -241       N  
ATOM   2040  NH2 ARG A 246     -28.540  11.231  55.463  1.00 66.44           N  
ANISOU 2040  NH2 ARG A 246     8355   8566   8324   -442    589   -275       N  
ATOM   2041  N   LYS A 247     -23.293   4.636  52.724  1.00 41.74           N  
ANISOU 2041  N   LYS A 247     5623   5177   5058   -463    367   -144       N  
ATOM   2042  CA  LYS A 247     -22.359   3.525  52.579  1.00 44.54           C  
ANISOU 2042  CA  LYS A 247     6056   5473   5392   -453    346   -122       C  
ATOM   2043  C   LYS A 247     -20.982   3.996  52.109  1.00 44.74           C  
ANISOU 2043  C   LYS A 247     6087   5491   5423   -375    309    -98       C  
ATOM   2044  O   LYS A 247     -20.864   4.748  51.139  1.00 43.59           O  
ANISOU 2044  O   LYS A 247     5888   5377   5298   -335    290   -109       O  
ATOM   2045  CB  LYS A 247     -22.909   2.426  51.663  1.00 44.81           C  
ANISOU 2045  CB  LYS A 247     6106   5489   5429   -490    342   -142       C  
ATOM   2046  CG  LYS A 247     -22.177   1.098  51.860  1.00 50.07           C  
ANISOU 2046  CG  LYS A 247     6870   6083   6070   -496    337   -121       C  
ATOM   2047  CD  LYS A 247     -22.379   0.119  50.709  1.00 53.11           C  
ANISOU 2047  CD  LYS A 247     7280   6442   6456   -512    325   -140       C  
ATOM   2048  CE  LYS A 247     -21.375  -1.037  50.769  1.00 53.22           C  
ANISOU 2048  CE  LYS A 247     7392   6378   6450   -489    315   -116       C  
ATOM   2049  NZ  LYS A 247     -21.287  -1.688  52.112  1.00 53.59           N  
ANISOU 2049  NZ  LYS A 247     7513   6380   6470   -524    333    -91       N  
ATOM   2050  N   THR A 248     -19.948   3.570  52.829  1.00 45.43           N  
ANISOU 2050  N   THR A 248     6237   5535   5490   -356    299    -65       N  
ATOM   2051  CA  THR A 248     -18.576   3.856  52.437  1.00 48.71           C  
ANISOU 2051  CA  THR A 248     6655   5941   5913   -286    265    -42       C  
ATOM   2052  C   THR A 248     -17.745   2.582  52.440  1.00 53.14           C  
ANISOU 2052  C   THR A 248     7288   6440   6465   -270    251    -20       C  
ATOM   2053  O   THR A 248     -18.116   1.584  53.067  1.00 54.78           O  
ANISOU 2053  O   THR A 248     7558   6605   6651   -314    264    -14       O  
ATOM   2054  CB  THR A 248     -17.896   4.913  53.343  1.00 47.26           C  
ANISOU 2054  CB  THR A 248     6460   5775   5723   -262    256    -18       C  
ATOM   2055  OG1 THR A 248     -17.607   4.342  54.623  1.00 44.19           O  
ANISOU 2055  OG1 THR A 248     6138   5348   5304   -287    257      9       O  
ATOM   2056  CG2 THR A 248     -18.771   6.155  53.509  1.00 46.18           C  
ANISOU 2056  CG2 THR A 248     6263   5690   5592   -277    277    -40       C  
ATOM   2057  N   ARG A 249     -16.622   2.628  51.734  1.00 57.80           N  
ANISOU 2057  N   ARG A 249     7871   7021   7070   -206    227     -7       N  
ATOM   2058  CA  ARG A 249     -15.684   1.519  51.688  1.00 63.02           C  
ANISOU 2058  CA  ARG A 249     8592   7623   7730   -173    213     15       C  
ATOM   2059  C   ARG A 249     -14.278   2.063  51.891  1.00 65.55           C  
ANISOU 2059  C   ARG A 249     8893   7950   8064   -108    184     47       C  
ATOM   2060  O   ARG A 249     -13.853   2.989  51.193  1.00 64.43           O  
ANISOU 2060  O   ARG A 249     8691   7849   7941    -72    178     40       O  
ATOM   2061  CB  ARG A 249     -15.792   0.792  50.343  1.00 64.35           C  
ANISOU 2061  CB  ARG A 249     8769   7771   7908   -162    220    -11       C  
ATOM   2062  CG  ARG A 249     -15.266  -0.644  50.336  1.00 71.22           C  
ANISOU 2062  CG  ARG A 249     9721   8567   8773   -147    219      2       C  
ATOM   2063  CD  ARG A 249     -16.193  -1.612  51.095  1.00 78.34           C  
ANISOU 2063  CD  ARG A 249    10692   9427   9647   -219    235      0       C  
ATOM   2064  NE  ARG A 249     -17.516  -1.754  50.475  1.00 81.47           N  
ANISOU 2064  NE  ARG A 249    11075   9844  10037   -284    257    -40       N  
ATOM   2065  CZ  ARG A 249     -17.875  -2.749  49.664  1.00 83.55           C  
ANISOU 2065  CZ  ARG A 249    11383  10068  10293   -307    266    -62       C  
ATOM   2066  NH1 ARG A 249     -17.015  -3.715  49.356  1.00 84.27           N  
ANISOU 2066  NH1 ARG A 249    11542  10093  10385   -264    262    -51       N  
ATOM   2067  NH2 ARG A 249     -19.101  -2.782  49.157  1.00 83.34           N  
ANISOU 2067  NH2 ARG A 249    11336  10068  10263   -373    280    -97       N  
ATOM   2068  N   VAL A 250     -13.569   1.500  52.864  1.00 70.49           N  
ANISOU 2068  N   VAL A 250     9569   8536   8680    -96    164     84       N  
ATOM   2069  CA  VAL A 250     -12.176   1.858  53.109  1.00 75.28           C  
ANISOU 2069  CA  VAL A 250    10156   9145   9302    -35    130    118       C  
ATOM   2070  C   VAL A 250     -11.300   0.830  52.394  1.00 80.53           C  
ANISOU 2070  C   VAL A 250    10844   9764   9990     24    123    126       C  
ATOM   2071  O   VAL A 250     -11.185  -0.319  52.833  1.00 80.83           O  
ANISOU 2071  O   VAL A 250    10952   9740  10019     25    117    143       O  
ATOM   2072  CB  VAL A 250     -11.853   1.935  54.627  1.00 74.96           C  
ANISOU 2072  CB  VAL A 250    10154   9092   9237    -52    104    156       C  
ATOM   2073  CG1 VAL A 250     -10.458   2.499  54.855  1.00 74.69           C  
ANISOU 2073  CG1 VAL A 250    10083   9075   9221      4     62    190       C  
ATOM   2074  CG2 VAL A 250     -12.884   2.788  55.357  1.00 73.87           C  
ANISOU 2074  CG2 VAL A 250    10007   8989   9070   -117    124    142       C  
ATOM   2075  N   LYS A 251     -10.698   1.249  51.282  1.00 86.90           N  
ANISOU 2075  N   LYS A 251    11596  10596  10825     72    128    112       N  
ATOM   2076  CA  LYS A 251     -10.012   0.326  50.377  1.00 94.14           C  
ANISOU 2076  CA  LYS A 251    12531  11472  11765    126    137    108       C  
ATOM   2077  C   LYS A 251      -8.693   0.876  49.820  1.00 97.95           C  
ANISOU 2077  C   LYS A 251    12950  11982  12284    196    128    119       C  
ATOM   2078  O   LYS A 251      -8.626   2.021  49.363  1.00 97.53           O  
ANISOU 2078  O   LYS A 251    12834  11986  12236    194    132    107       O  
ATOM   2079  CB  LYS A 251     -10.944  -0.071  49.224  1.00 95.01           C  
ANISOU 2079  CB  LYS A 251    12658  11574  11867     98    171     63       C  
ATOM   2080  CG  LYS A 251     -10.456  -1.258  48.404  1.00 96.95           C  
ANISOU 2080  CG  LYS A 251    12951  11761  12125    140    188     53       C  
ATOM   2081  CD  LYS A 251     -10.733  -1.054  46.925  1.00 97.75           C  
ANISOU 2081  CD  LYS A 251    13031  11882  12228    141    216     12       C  
ATOM   2082  CE  LYS A 251      -9.903  -2.011  46.085  1.00 99.24           C  
ANISOU 2082  CE  LYS A 251    13256  12017  12433    200    237      4       C  
ATOM   2083  NZ  LYS A 251      -9.959  -1.667  44.640  1.00100.00           N  
ANISOU 2083  NZ  LYS A 251    13331  12137  12528    206    265    -34       N  
ATOM   2084  N   VAL A 252      -7.660   0.032  49.860  1.00103.60           N  
ANISOU 2084  N   VAL A 252    13685  12655  13025    257    117    142       N  
ATOM   2085  CA  VAL A 252      -6.320   0.358  49.351  1.00108.08           C  
ANISOU 2085  CA  VAL A 252    14188  13243  13632    328    113    154       C  
ATOM   2086  C   VAL A 252      -6.195   0.225  47.832  1.00110.95           C  
ANISOU 2086  C   VAL A 252    14536  13608  14010    356    158    115       C  
ATOM   2087  O   VAL A 252      -6.921  -0.551  47.200  1.00111.04           O  
ANISOU 2087  O   VAL A 252    14605  13580  14006    338    186     86       O  
ATOM   2088  CB  VAL A 252      -5.200  -0.516  50.013  1.00109.03           C  
ANISOU 2088  CB  VAL A 252    14326  13318  13782    392     82    195       C  
ATOM   2089  CG1 VAL A 252      -4.423   0.273  51.061  1.00108.96           C  
ANISOU 2089  CG1 VAL A 252    14268  13350  13783    399     30    238       C  
ATOM   2090  CG2 VAL A 252      -5.762  -1.820  50.589  1.00110.44           C  
ANISOU 2090  CG2 VAL A 252    14605  13419  13938    378     76    204       C  
ATOM   2091  N   ILE A 253      -5.267   0.995  47.263  1.00114.63           N  
ANISOU 2091  N   ILE A 253    14930  14119  14505    395    165    116       N  
ATOM   2092  CA  ILE A 253      -4.871   0.864  45.859  1.00118.32           C  
ANISOU 2092  CA  ILE A 253    15383  14586  14989    430    210     85       C  
ATOM   2093  C   ILE A 253      -3.672  -0.087  45.783  1.00121.18           C  
ANISOU 2093  C   ILE A 253    15744  14905  15394    512    219    101       C  
ATOM   2094  O   ILE A 253      -2.665   0.116  46.471  1.00121.65           O  
ANISOU 2094  O   ILE A 253    15754  14982  15487    553    188    138       O  
ATOM   2095  CB  ILE A 253      -4.506   2.248  45.220  1.00118.13           C  
ANISOU 2095  CB  ILE A 253    15282  14634  14969    424    221     75       C  
ATOM   2096  CG1 ILE A 253      -5.668   3.254  45.337  1.00117.80           C  
ANISOU 2096  CG1 ILE A 253    15238  14632  14889    352    210     62       C  
ATOM   2097  CG2 ILE A 253      -4.034   2.091  43.763  1.00118.24           C  
ANISOU 2097  CG2 ILE A 253    15286  14644  14993    458    274     43       C  
ATOM   2098  CD1 ILE A 253      -6.886   2.973  44.444  1.00117.97           C  
ANISOU 2098  CD1 ILE A 253    15307  14638  14878    311    235     21       C  
ATOM   2099  N   GLU A 254      -3.797  -1.128  44.958  1.00124.08           N  
ANISOU 2099  N   GLU A 254    16168  15216  15760    536    258     73       N  
ATOM   2100  CA  GLU A 254      -2.734  -2.124  44.777  1.00127.05           C  
ANISOU 2100  CA  GLU A 254    16552  15541  16179    622    276     83       C  
ATOM   2101  C   GLU A 254      -1.666  -1.647  43.784  1.00128.58           C  
ANISOU 2101  C   GLU A 254    16672  15773  16410    675    317     68       C  
ATOM   2102  O   GLU A 254      -1.784  -1.869  42.573  1.00128.93           O  
ANISOU 2102  O   GLU A 254    16742  15803  16444    679    373     27       O  
ATOM   2103  CB  GLU A 254      -3.315  -3.474  44.325  1.00127.70           C  
ANISOU 2103  CB  GLU A 254    16739  15539  16242    624    306     57       C  
ATOM   2104  CG  GLU A 254      -4.105  -4.235  45.391  1.00127.68           C  
ANISOU 2104  CG  GLU A 254    16817  15484  16213    586    269     77       C  
ATOM   2105  CD  GLU A 254      -4.647  -5.572  44.893  1.00128.16           C  
ANISOU 2105  CD  GLU A 254    16986  15457  16253    583    301     50       C  
ATOM   2106  OE1 GLU A 254      -4.826  -5.740  43.667  1.00127.88           O  
ANISOU 2106  OE1 GLU A 254    16971  15411  16206    582    350      6       O  
ATOM   2107  OE2 GLU A 254      -4.903  -6.458  45.736  1.00128.37           O  
ANISOU 2107  OE2 GLU A 254    17084  15421  16269    578    277     73       O  
ATOM   2108  N   ASN A 255      -0.630  -0.990  44.306  1.00130.06           N  
ANISOU 2108  N   ASN A 255    16771  16008  16637    709    291    102       N  
ATOM   2109  CA  ASN A 255       0.503  -0.531  43.493  1.00131.53           C  
ANISOU 2109  CA  ASN A 255    16876  16234  16865    758    331     93       C  
ATOM   2110  C   ASN A 255       1.753  -1.410  43.670  1.00132.60           C  
ANISOU 2110  C   ASN A 255    16980  16336  17066    857    336    114       C  
ATOM   2111  O   ASN A 255       1.638  -2.599  43.985  1.00133.22           O  
ANISOU 2111  O   ASN A 255    17127  16340  17151    894    329    121       O  
ATOM   2112  CB  ASN A 255       0.796   0.969  43.726  1.00131.75           C  
ANISOU 2112  CB  ASN A 255    16816  16349  16893    719    306    108       C  
ATOM   2113  CG  ASN A 255       1.277   1.278  45.146  1.00132.67           C  
ANISOU 2113  CG  ASN A 255    16888  16489  17030    722    234    160       C  
ATOM   2114  OD1 ASN A 255       2.408   1.727  45.341  1.00133.02           O  
ANISOU 2114  OD1 ASN A 255    16846  16576  17120    757    220    184       O  
ATOM   2115  ND2 ASN A 255       0.414   1.057  46.136  1.00132.44           N  
ANISOU 2115  ND2 ASN A 255    16921  16434  16967    680    187    178       N  
ATOM   2116  N   MET A 256       2.935  -0.832  43.460  1.00133.00           N  
ANISOU 2116  N   MET A 256    16927  16439  17166    899    348    125       N  
ATOM   2117  CA  MET A 256       4.190  -1.581  43.554  1.00134.01           C  
ANISOU 2117  CA  MET A 256    17005  16545  17366   1000    356    144       C  
ATOM   2118  C   MET A 256       5.261  -0.831  44.368  1.00133.66           C  
ANISOU 2118  C   MET A 256    16844  16569  17372   1019    302    191       C  
ATOM   2119  O   MET A 256       6.448  -1.170  44.318  1.00134.67           O  
ANISOU 2119  O   MET A 256    16896  16702  17569   1101    311    206       O  
ATOM   2120  CB  MET A 256       4.696  -1.930  42.147  1.00134.83           C  
ANISOU 2120  CB  MET A 256    17101  16635  17492   1049    450     99       C  
ATOM   2121  CG  MET A 256       5.479  -3.238  42.054  1.00136.48           C  
ANISOU 2121  CG  MET A 256    17321  16776  17759   1157    478    101       C  
ATOM   2122  SD  MET A 256       5.554  -3.922  40.382  1.00137.49           S  
ANISOU 2122  SD  MET A 256    17503  16855  17882   1196    599     34       S  
ATOM   2123  CE  MET A 256       6.497  -2.668  39.512  1.00137.22           C  
ANISOU 2123  CE  MET A 256    17341  16920  17875   1189    657     16       C  
ATOM   2124  N   TYR A 257       4.827   0.177  45.125  1.00132.04           N  
ANISOU 2124  N   TYR A 257    16623  16414  17132    944    245    212       N  
ATOM   2125  CA  TYR A 257       5.734   0.998  45.934  1.00131.06           C  
ANISOU 2125  CA  TYR A 257    16397  16356  17042    943    187    255       C  
ATOM   2126  C   TYR A 257       5.272   1.131  47.394  1.00129.16           C  
ANISOU 2126  C   TYR A 257    16193  16111  16772    900     95    299       C  
ATOM   2127  O   TYR A 257       5.942   1.774  48.209  1.00129.36           O  
ANISOU 2127  O   TYR A 257    16149  16185  16817    891     35    338       O  
ATOM   2128  CB  TYR A 257       5.916   2.389  45.301  1.00131.34           C  
ANISOU 2128  CB  TYR A 257    16365  16473  17067    887    217    236       C  
ATOM   2129  CG  TYR A 257       6.230   2.384  43.814  1.00132.49           C  
ANISOU 2129  CG  TYR A 257    16489  16624  17225    911    313    189       C  
ATOM   2130  CD1 TYR A 257       5.347   2.955  42.893  1.00132.50           C  
ANISOU 2130  CD1 TYR A 257    16542  16633  17168    849    361    147       C  
ATOM   2131  CD2 TYR A 257       7.408   1.810  43.326  1.00133.86           C  
ANISOU 2131  CD2 TYR A 257    16595  16797  17470    998    356    186       C  
ATOM   2132  CE1 TYR A 257       5.629   2.954  41.525  1.00132.57           C  
ANISOU 2132  CE1 TYR A 257    16543  16646  17180    865    448    104       C  
ATOM   2133  CE2 TYR A 257       7.698   1.802  41.962  1.00133.89           C  
ANISOU 2133  CE2 TYR A 257    16586  16804  17480   1016    452    141       C  
ATOM   2134  CZ  TYR A 257       6.806   2.375  41.069  1.00133.25           C  
ANISOU 2134  CZ  TYR A 257    16567  16729  17333    946    497    100       C  
ATOM   2135  OH  TYR A 257       7.092   2.368  39.723  1.00133.04           O  
ANISOU 2135  OH  TYR A 257    16540  16705  17306    960    590     56       O  
ATOM   2136  N   GLY A 258       4.133   0.517  47.713  1.00126.71           N  
ANISOU 2136  N   GLY A 258    15993  15740  16411    869     87    292       N  
ATOM   2137  CA  GLY A 258       3.556   0.569  49.058  1.00123.62           C  
ANISOU 2137  CA  GLY A 258    15654  15336  15981    822     13    328       C  
ATOM   2138  C   GLY A 258       2.047   0.399  49.034  1.00120.73           C  
ANISOU 2138  C   GLY A 258    15393  14932  15546    753     31    300       C  
ATOM   2139  O   GLY A 258       1.522  -0.412  48.266  1.00121.04           O  
ANISOU 2139  O   GLY A 258    15493  14919  15575    768     82    267       O  
ATOM   2140  N   SER A 259       1.353   1.161  49.883  1.00117.29           N  
ANISOU 2140  N   SER A 259    14978  14523  15063    677     -8    312       N  
ATOM   2141  CA  SER A 259      -0.116   1.159  49.930  1.00113.24           C  
ANISOU 2141  CA  SER A 259    14549  13987  14489    606      9    286       C  
ATOM   2142  C   SER A 259      -0.686   2.440  50.541  1.00109.79           C  
ANISOU 2142  C   SER A 259    14099  13605  14011    527    -16    289       C  
ATOM   2143  O   SER A 259      -0.198   2.922  51.568  1.00109.88           O  
ANISOU 2143  O   SER A 259    14085  13641  14022    515    -71    327       O  
ATOM   2144  CB  SER A 259      -0.645  -0.066  50.693  1.00113.76           C  
ANISOU 2144  CB  SER A 259    14713  13976  14534    608    -14    304       C  
ATOM   2145  OG  SER A 259      -0.295  -0.021  52.067  1.00113.46           O  
ANISOU 2145  OG  SER A 259    14682  13937  14490    602    -85    354       O  
ATOM   2146  N   ARG A 260      -1.714   2.987  49.895  1.00105.45           N  
ANISOU 2146  N   ARG A 260    13568  13072  13427    475     25    249       N  
ATOM   2147  CA  ARG A 260      -2.481   4.110  50.446  1.00100.98           C  
ANISOU 2147  CA  ARG A 260    13003  12546  12819    402     10    246       C  
ATOM   2148  C   ARG A 260      -3.986   3.826  50.389  1.00 96.48           C  
ANISOU 2148  C   ARG A 260    12504  11948  12206    349     35    217       C  
ATOM   2149  O   ARG A 260      -4.481   3.261  49.409  1.00 96.30           O  
ANISOU 2149  O   ARG A 260    12506  11902  12182    356     76    184       O  
ATOM   2150  CB  ARG A 260      -2.129   5.440  49.751  1.00101.65           C  
ANISOU 2150  CB  ARG A 260    13016  12695  12911    389     27    231       C  
ATOM   2151  CG  ARG A 260      -2.487   5.544  48.263  1.00102.15           C  
ANISOU 2151  CG  ARG A 260    13073  12766  12976    394     86    187       C  
ATOM   2152  CD  ARG A 260      -2.241   6.957  47.742  1.00102.66           C  
ANISOU 2152  CD  ARG A 260    13079  12890  13036    370     97    176       C  
ATOM   2153  NE  ARG A 260      -2.669   7.133  46.353  1.00103.41           N  
ANISOU 2153  NE  ARG A 260    13180  12991  13122    367    148    136       N  
ATOM   2154  CZ  ARG A 260      -3.773   7.774  45.970  1.00103.19           C  
ANISOU 2154  CZ  ARG A 260    13176  12974  13057    321    160    111       C  
ATOM   2155  NH1 ARG A 260      -4.587   8.316  46.867  1.00102.53           N  
ANISOU 2155  NH1 ARG A 260    13112  12899  12947    276    132    118       N  
ATOM   2156  NH2 ARG A 260      -4.066   7.878  44.680  1.00102.36           N  
ANISOU 2156  NH2 ARG A 260    13078  12872  12942    321    199     78       N  
ATOM   2157  N   GLU A 261      -4.699   4.205  51.450  1.00 90.56           N  
ANISOU 2157  N   GLU A 261    11787  11203  11419    294     11    228       N  
ATOM   2158  CA  GLU A 261      -6.142   3.963  51.543  1.00 84.20           C  
ANISOU 2158  CA  GLU A 261    11040  10377  10576    239     34    202       C  
ATOM   2159  C   GLU A 261      -7.001   5.192  51.246  1.00 77.47           C  
ANISOU 2159  C   GLU A 261    10159   9573   9702    190     54    174       C  
ATOM   2160  O   GLU A 261      -6.867   6.242  51.884  1.00 76.11           O  
ANISOU 2160  O   GLU A 261     9963   9437   9519    167     35    186       O  
ATOM   2161  CB  GLU A 261      -6.518   3.325  52.889  1.00 86.36           C  
ANISOU 2161  CB  GLU A 261    11382  10611  10821    208      6    229       C  
ATOM   2162  CG  GLU A 261      -7.068   1.896  52.752  1.00 87.95           C  
ANISOU 2162  CG  GLU A 261    11656  10746  11015    209     24    221       C  
ATOM   2163  CD  GLU A 261      -6.586   0.935  53.835  1.00 89.69           C  
ANISOU 2163  CD  GLU A 261    11937  10912  11229    226    -15    264       C  
ATOM   2164  OE1 GLU A 261      -6.234   1.389  54.946  1.00 90.16           O  
ANISOU 2164  OE1 GLU A 261    11998  10984  11273    211    -57    298       O  
ATOM   2165  OE2 GLU A 261      -6.565  -0.287  53.569  1.00 89.34           O  
ANISOU 2165  OE2 GLU A 261    11946  10807  11193    253     -6    264       O  
ATOM   2166  N   ILE A 262      -7.868   5.042  50.249  1.00 69.79           N  
ANISOU 2166  N   ILE A 262     9195   8598   8724    177     91    136       N  
ATOM   2167  CA  ILE A 262      -8.840   6.069  49.888  1.00 61.43           C  
ANISOU 2167  CA  ILE A 262     8115   7579   7648    135    108    107       C  
ATOM   2168  C   ILE A 262     -10.233   5.653  50.368  1.00 55.87           C  
ANISOU 2168  C   ILE A 262     7456   6856   6917     82    121     91       C  
ATOM   2169  O   ILE A 262     -10.489   4.468  50.625  1.00 54.20           O  
ANISOU 2169  O   ILE A 262     7297   6599   6700     75    125     94       O  
ATOM   2170  CB  ILE A 262      -8.845   6.368  48.354  1.00 62.03           C  
ANISOU 2170  CB  ILE A 262     8159   7673   7734    155    135     77       C  
ATOM   2171  CG1 ILE A 262      -9.421   5.193  47.552  1.00 63.72           C  
ANISOU 2171  CG1 ILE A 262     8416   7847   7946    155    159     51       C  
ATOM   2172  CG2 ILE A 262      -7.439   6.713  47.863  1.00 62.06           C  
ANISOU 2172  CG2 ILE A 262     8118   7695   7766    204    132     91       C  
ATOM   2173  CD1 ILE A 262     -10.072   5.600  46.228  1.00 62.02           C  
ANISOU 2173  CD1 ILE A 262     8188   7654   7723    143    180     15       C  
ATOM   2174  N   ILE A 263     -11.126   6.629  50.494  1.00 49.28           N  
ANISOU 2174  N   ILE A 263     6600   6056   6067     44    130     74       N  
ATOM   2175  CA  ILE A 263     -12.484   6.360  50.947  1.00 44.74           C  
ANISOU 2175  CA  ILE A 263     6054   5474   5472     -9    147     55       C  
ATOM   2176  C   ILE A 263     -13.455   6.488  49.783  1.00 42.88           C  
ANISOU 2176  C   ILE A 263     5795   5256   5240    -23    168     17       C  
ATOM   2177  O   ILE A 263     -13.545   7.540  49.144  1.00 43.31           O  
ANISOU 2177  O   ILE A 263     5805   5349   5301    -13    168      5       O  
ATOM   2178  CB  ILE A 263     -12.918   7.291  52.117  1.00 42.82           C  
ANISOU 2178  CB  ILE A 263     5806   5254   5209    -45    146     63       C  
ATOM   2179  CG1 ILE A 263     -11.847   7.353  53.220  1.00 43.61           C  
ANISOU 2179  CG1 ILE A 263     5928   5342   5300    -33    116    102       C  
ATOM   2180  CG2 ILE A 263     -14.282   6.874  52.675  1.00 42.81           C  
ANISOU 2180  CG2 ILE A 263     5833   5243   5189   -101    172     44       C  
ATOM   2181  CD1 ILE A 263     -11.475   6.017  53.859  1.00 40.30           C  
ANISOU 2181  CD1 ILE A 263     5568   4872   4874    -31    101    128       C  
ATOM   2182  N   THR A 264     -14.178   5.407  49.512  1.00 39.16           N  
ANISOU 2182  N   THR A 264     5359   4755   4764    -48    182      1       N  
ATOM   2183  CA  THR A 264     -15.159   5.396  48.452  1.00 35.85           C  
ANISOU 2183  CA  THR A 264     4923   4352   4346    -69    194    -34       C  
ATOM   2184  C   THR A 264     -16.511   5.792  49.034  1.00 36.26           C  
ANISOU 2184  C   THR A 264     4958   4430   4391   -122    207    -51       C  
ATOM   2185  O   THR A 264     -17.037   5.120  49.927  1.00 36.04           O  
ANISOU 2185  O   THR A 264     4964   4379   4350   -163    219    -48       O  
ATOM   2186  CB  THR A 264     -15.237   4.020  47.772  1.00 36.05           C  
ANISOU 2186  CB  THR A 264     4997   4332   4369    -73    202    -47       C  
ATOM   2187  OG1 THR A 264     -13.996   3.751  47.103  1.00 34.69           O  
ANISOU 2187  OG1 THR A 264     4833   4141   4208    -17    198    -37       O  
ATOM   2188  CG2 THR A 264     -16.384   3.984  46.766  1.00 31.57           C  
ANISOU 2188  CG2 THR A 264     4414   3783   3797   -109    208    -83       C  
ATOM   2189  N   LEU A 265     -17.046   6.901  48.531  1.00 33.12           N  
ANISOU 2189  N   LEU A 265     4506   4076   4001   -120    205    -68       N  
ATOM   2190  CA  LEU A 265     -18.316   7.430  48.988  1.00 31.51           C  
ANISOU 2190  CA  LEU A 265     4271   3903   3799   -159    219    -85       C  
ATOM   2191  C   LEU A 265     -19.378   7.041  47.973  1.00 30.54           C  
ANISOU 2191  C   LEU A 265     4128   3792   3683   -185    218   -116       C  
ATOM   2192  O   LEU A 265     -19.451   7.615  46.894  1.00 28.05           O  
ANISOU 2192  O   LEU A 265     3782   3500   3376   -163    201   -128       O  
ATOM   2193  CB  LEU A 265     -18.244   8.955  49.143  1.00 28.96           C  
ANISOU 2193  CB  LEU A 265     3904   3618   3483   -135    214    -83       C  
ATOM   2194  CG  LEU A 265     -17.116   9.552  49.992  1.00 30.21           C  
ANISOU 2194  CG  LEU A 265     4077   3770   3633   -110    207    -53       C  
ATOM   2195  CD1 LEU A 265     -16.976  11.035  49.710  1.00 26.00           C  
ANISOU 2195  CD1 LEU A 265     3504   3270   3105    -84    199    -55       C  
ATOM   2196  CD2 LEU A 265     -17.326   9.317  51.489  1.00 25.72           C  
ANISOU 2196  CD2 LEU A 265     3540   3186   3046   -145    224    -42       C  
ATOM   2197  N   PHE A 266     -20.181   6.043  48.316  1.00 31.60           N  
ANISOU 2197  N   PHE A 266     4285   3908   3812   -237    234   -128       N  
ATOM   2198  CA  PHE A 266     -21.262   5.600  47.448  1.00 34.28           C  
ANISOU 2198  CA  PHE A 266     4606   4262   4157   -274    231   -157       C  
ATOM   2199  C   PHE A 266     -22.245   6.735  47.173  1.00 33.96           C  
ANISOU 2199  C   PHE A 266     4489   4278   4138   -276    225   -175       C  
ATOM   2200  O   PHE A 266     -22.642   7.456  48.084  1.00 30.50           O  
ANISOU 2200  O   PHE A 266     4019   3861   3708   -280    244   -173       O  
ATOM   2201  CB  PHE A 266     -21.953   4.378  48.044  1.00 36.09           C  
ANISOU 2201  CB  PHE A 266     4875   4463   4377   -339    253   -165       C  
ATOM   2202  CG  PHE A 266     -21.186   3.090  47.830  1.00 40.78           C  
ANISOU 2202  CG  PHE A 266     5547   4995   4951   -337    251   -155       C  
ATOM   2203  CD1 PHE A 266     -20.015   2.827  48.542  1.00 36.89           C  
ANISOU 2203  CD1 PHE A 266     5105   4463   4449   -302    252   -124       C  
ATOM   2204  CD2 PHE A 266     -21.635   2.144  46.907  1.00 44.16           C  
ANISOU 2204  CD2 PHE A 266     6003   5403   5372   -370    245   -177       C  
ATOM   2205  CE1 PHE A 266     -19.298   1.644  48.335  1.00 42.88           C  
ANISOU 2205  CE1 PHE A 266     5935   5162   5197   -290    250   -114       C  
ATOM   2206  CE2 PHE A 266     -20.925   0.946  46.691  1.00 46.05           C  
ANISOU 2206  CE2 PHE A 266     6323   5578   5594   -363    247   -170       C  
ATOM   2207  CZ  PHE A 266     -19.754   0.699  47.404  1.00 44.25           C  
ANISOU 2207  CZ  PHE A 266     6140   5310   5362   -319    251   -138       C  
ATOM   2208  N   GLY A 267     -22.597   6.911  45.901  1.00 34.49           N  
ANISOU 2208  N   GLY A 267     4529   4365   4211   -268    197   -191       N  
ATOM   2209  CA  GLY A 267     -23.508   7.984  45.496  1.00 33.77           C  
ANISOU 2209  CA  GLY A 267     4366   4325   4142   -261    181   -206       C  
ATOM   2210  C   GLY A 267     -22.826   9.317  45.222  1.00 34.24           C  
ANISOU 2210  C   GLY A 267     4406   4400   4205   -200    166   -192       C  
ATOM   2211  O   GLY A 267     -23.487  10.340  45.016  1.00 37.24           O  
ANISOU 2211  O   GLY A 267     4731   4816   4603   -183    154   -199       O  
ATOM   2212  N   ILE A 268     -21.501   9.319  45.221  1.00 32.15           N  
ANISOU 2212  N   ILE A 268     4185   4108   3924   -165    166   -171       N  
ATOM   2213  CA  ILE A 268     -20.749  10.495  44.791  1.00 29.52           C  
ANISOU 2213  CA  ILE A 268     3841   3786   3589   -115    151   -158       C  
ATOM   2214  C   ILE A 268     -19.703  10.076  43.763  1.00 30.35           C  
ANISOU 2214  C   ILE A 268     3987   3869   3677    -92    139   -152       C  
ATOM   2215  O   ILE A 268     -19.166   8.967  43.831  1.00 30.83           O  
ANISOU 2215  O   ILE A 268     4090   3895   3728   -101    150   -148       O  
ATOM   2216  CB  ILE A 268     -20.128  11.227  45.991  1.00 29.55           C  
ANISOU 2216  CB  ILE A 268     3847   3788   3593    -96    170   -138       C  
ATOM   2217  CG1 ILE A 268     -21.254  11.773  46.885  1.00 26.94           C  
ANISOU 2217  CG1 ILE A 268     3476   3481   3278   -116    188   -150       C  
ATOM   2218  CG2 ILE A 268     -19.184  12.361  45.534  1.00 24.48           C  
ANISOU 2218  CG2 ILE A 268     3203   3152   2946    -51    155   -123       C  
ATOM   2219  CD1 ILE A 268     -20.829  12.197  48.227  1.00 28.40           C  
ANISOU 2219  CD1 ILE A 268     3678   3656   3455   -116    213   -135       C  
ATOM   2220  N   SER A 269     -19.457  10.954  42.792  1.00 28.63           N  
ANISOU 2220  N   SER A 269     3758   3667   3455    -62    118   -151       N  
ATOM   2221  CA  SER A 269     -18.422  10.746  41.800  1.00 29.54           C  
ANISOU 2221  CA  SER A 269     3909   3764   3551    -39    114   -146       C  
ATOM   2222  C   SER A 269     -17.266  11.698  42.043  1.00 29.94           C  
ANISOU 2222  C   SER A 269     3957   3817   3601     -1    120   -124       C  
ATOM   2223  O   SER A 269     -17.335  12.890  41.730  1.00 31.07           O  
ANISOU 2223  O   SER A 269     4080   3982   3742     16    107   -120       O  
ATOM   2224  CB  SER A 269     -18.977  10.914  40.390  1.00 30.10           C  
ANISOU 2224  CB  SER A 269     3981   3848   3609    -44     86   -163       C  
ATOM   2225  OG  SER A 269     -19.711   9.759  40.024  1.00 31.93           O  
ANISOU 2225  OG  SER A 269     4229   4068   3834    -83     81   -183       O  
ATOM   2226  N   VAL A 270     -16.197  11.150  42.601  1.00 30.04           N  
ANISOU 2226  N   VAL A 270     3992   3807   3614     10    139   -108       N  
ATOM   2227  CA  VAL A 270     -15.027  11.922  42.963  1.00 27.56           C  
ANISOU 2227  CA  VAL A 270     3673   3498   3302     39    144    -86       C  
ATOM   2228  C   VAL A 270     -14.113  12.037  41.744  1.00 28.28           C  
ANISOU 2228  C   VAL A 270     3777   3586   3382     62    148    -86       C  
ATOM   2229  O   VAL A 270     -13.663  11.033  41.208  1.00 28.21           O  
ANISOU 2229  O   VAL A 270     3794   3553   3369     68    161    -92       O  
ATOM   2230  CB  VAL A 270     -14.293  11.268  44.159  1.00 27.39           C  
ANISOU 2230  CB  VAL A 270     3663   3455   3289     40    156    -66       C  
ATOM   2231  CG1 VAL A 270     -12.999  12.010  44.488  1.00 23.57           C  
ANISOU 2231  CG1 VAL A 270     3168   2979   2809     66    156    -42       C  
ATOM   2232  CG2 VAL A 270     -15.207  11.224  45.363  1.00 23.87           C  
ANISOU 2232  CG2 VAL A 270     3212   3011   2847     11    158    -67       C  
ATOM   2233  N   LEU A 271     -13.890  13.266  41.285  1.00 30.36           N  
ANISOU 2233  N   LEU A 271     4028   3870   3638     74    139    -81       N  
ATOM   2234  CA  LEU A 271     -12.929  13.532  40.222  1.00 31.64           C  
ANISOU 2234  CA  LEU A 271     4203   4031   3786     91    149    -79       C  
ATOM   2235  C   LEU A 271     -11.869  14.459  40.767  1.00 30.01           C  
ANISOU 2235  C   LEU A 271     3979   3837   3586    105    155    -55       C  
ATOM   2236  O   LEU A 271     -11.955  15.671  40.569  1.00 29.42           O  
ANISOU 2236  O   LEU A 271     3899   3777   3500    104    144    -50       O  
ATOM   2237  CB  LEU A 271     -13.584  14.187  38.999  1.00 32.49           C  
ANISOU 2237  CB  LEU A 271     4323   4150   3870     86    131    -92       C  
ATOM   2238  CG  LEU A 271     -14.745  13.529  38.236  1.00 36.92           C  
ANISOU 2238  CG  LEU A 271     4901   4708   4420     66    112   -115       C  
ATOM   2239  CD1 LEU A 271     -15.249  14.487  37.161  1.00 31.07           C  
ANISOU 2239  CD1 LEU A 271     4169   3980   3655     66     84   -119       C  
ATOM   2240  CD2 LEU A 271     -14.343  12.199  37.607  1.00 37.58           C  
ANISOU 2240  CD2 LEU A 271     5021   4764   4493     62    133   -130       C  
ATOM   2241  N   ASP A 272     -10.875  13.895  41.455  1.00 29.18           N  
ANISOU 2241  N   ASP A 272     3867   3724   3498    116    169    -40       N  
ATOM   2242  CA  ASP A 272      -9.771  14.696  42.001  1.00 31.74           C  
ANISOU 2242  CA  ASP A 272     4169   4062   3829    123    170    -17       C  
ATOM   2243  C   ASP A 272      -9.121  15.431  40.830  1.00 30.31           C  
ANISOU 2243  C   ASP A 272     3991   3893   3633    128    183    -19       C  
ATOM   2244  O   ASP A 272      -8.735  14.794  39.844  1.00 29.42           O  
ANISOU 2244  O   ASP A 272     3892   3772   3516    139    205    -31       O  
ATOM   2245  CB  ASP A 272      -8.760  13.787  42.716  1.00 32.65           C  
ANISOU 2245  CB  ASP A 272     4273   4165   3966    139    178      0       C  
ATOM   2246  CG  ASP A 272      -7.721  14.560  43.537  1.00 35.45           C  
ANISOU 2246  CG  ASP A 272     4600   4538   4331    138    169     27       C  
ATOM   2247  OD1 ASP A 272      -7.346  15.702  43.176  1.00 38.36           O  
ANISOU 2247  OD1 ASP A 272     4958   4927   4689    130    170     31       O  
ATOM   2248  OD2 ASP A 272      -7.254  13.993  44.552  1.00 36.52           O  
ANISOU 2248  OD2 ASP A 272     4727   4666   4483    144    158     45       O  
ATOM   2249  N   TYR A 273      -9.014  16.758  40.917  1.00 29.89           N  
ANISOU 2249  N   TYR A 273     3932   3856   3568    118    174     -9       N  
ATOM   2250  CA  TYR A 273      -8.502  17.526  39.778  1.00 30.03           C  
ANISOU 2250  CA  TYR A 273     3962   3882   3565    115    186    -11       C  
ATOM   2251  C   TYR A 273      -7.054  17.192  39.421  1.00 32.32           C  
ANISOU 2251  C   TYR A 273     4234   4179   3867    125    218     -3       C  
ATOM   2252  O   TYR A 273      -6.679  17.271  38.245  1.00 31.93           O  
ANISOU 2252  O   TYR A 273     4203   4131   3800    125    242    -13       O  
ATOM   2253  CB  TYR A 273      -8.707  19.037  39.925  1.00 30.90           C  
ANISOU 2253  CB  TYR A 273     4079   4001   3659    101    170     -1       C  
ATOM   2254  CG  TYR A 273      -9.018  19.676  38.593  1.00 30.31           C  
ANISOU 2254  CG  TYR A 273     4038   3924   3553     97    169    -10       C  
ATOM   2255  CD1 TYR A 273      -7.996  20.087  37.730  1.00 30.24           C  
ANISOU 2255  CD1 TYR A 273     4041   3921   3526     89    194     -5       C  
ATOM   2256  CD2 TYR A 273     -10.341  19.837  38.175  1.00 31.26           C  
ANISOU 2256  CD2 TYR A 273     4179   4037   3660    100    143    -23       C  
ATOM   2257  CE1 TYR A 273      -8.288  20.650  36.497  1.00 31.02           C  
ANISOU 2257  CE1 TYR A 273     4183   4015   3590     81    193    -12       C  
ATOM   2258  CE2 TYR A 273     -10.643  20.400  36.953  1.00 30.28           C  
ANISOU 2258  CE2 TYR A 273     4091   3909   3503     97    133    -28       C  
ATOM   2259  CZ  TYR A 273      -9.613  20.801  36.115  1.00 32.69           C  
ANISOU 2259  CZ  TYR A 273     4420   4216   3786     87    159    -22       C  
ATOM   2260  OH  TYR A 273      -9.915  21.353  34.898  1.00 33.24           O  
ANISOU 2260  OH  TYR A 273     4537   4278   3816     80    149    -25       O  
ATOM   2261  N   ILE A 274      -6.246  16.800  40.411  1.00 31.70           N  
ANISOU 2261  N   ILE A 274     4121   4105   3817    133    218     14       N  
ATOM   2262  CA  ILE A 274      -4.862  16.396  40.117  1.00 32.80           C  
ANISOU 2262  CA  ILE A 274     4231   4254   3977    148    248     21       C  
ATOM   2263  C   ILE A 274      -4.829  15.198  39.153  1.00 33.45           C  
ANISOU 2263  C   ILE A 274     4331   4318   4062    173    280      0       C  
ATOM   2264  O   ILE A 274      -4.050  15.182  38.196  1.00 36.84           O  
ANISOU 2264  O   ILE A 274     4758   4752   4489    180    318     -8       O  
ATOM   2265  CB  ILE A 274      -4.015  16.143  41.402  1.00 33.92           C  
ANISOU 2265  CB  ILE A 274     4329   4405   4152    156    232     47       C  
ATOM   2266  CG1 ILE A 274      -2.519  16.177  41.077  1.00 34.96           C  
ANISOU 2266  CG1 ILE A 274     4415   4559   4308    166    258     58       C  
ATOM   2267  CG2 ILE A 274      -4.403  14.823  42.090  1.00 32.68           C  
ANISOU 2267  CG2 ILE A 274     4179   4224   4015    178    220     47       C  
ATOM   2268  CD1 ILE A 274      -1.615  16.135  42.313  1.00 40.45           C  
ANISOU 2268  CD1 ILE A 274     5061   5271   5036    169    231     88       C  
ATOM   2269  N   ASP A 275      -5.711  14.229  39.382  1.00 33.12           N  
ANISOU 2269  N   ASP A 275     4312   4250   4022    181    268    -11       N  
ATOM   2270  CA  ASP A 275      -5.804  13.041  38.539  1.00 33.83           C  
ANISOU 2270  CA  ASP A 275     4431   4313   4109    200    296    -34       C  
ATOM   2271  C   ASP A 275      -6.377  13.370  37.168  1.00 32.41           C  
ANISOU 2271  C   ASP A 275     4295   4131   3889    183    308    -57       C  
ATOM   2272  O   ASP A 275      -5.940  12.800  36.166  1.00 32.87           O  
ANISOU 2272  O   ASP A 275     4375   4176   3937    195    346    -75       O  
ATOM   2273  CB  ASP A 275      -6.632  11.933  39.210  1.00 35.42           C  
ANISOU 2273  CB  ASP A 275     4652   4486   4320    204    278    -39       C  
ATOM   2274  CG  ASP A 275      -6.033  11.457  40.522  1.00 37.14           C  
ANISOU 2274  CG  ASP A 275     4840   4700   4572    222    264    -14       C  
ATOM   2275  OD1 ASP A 275      -4.799  11.485  40.677  1.00 40.44           O  
ANISOU 2275  OD1 ASP A 275     5221   5129   5016    246    277      3       O  
ATOM   2276  OD2 ASP A 275      -6.807  11.046  41.409  1.00 48.19           O  
ANISOU 2276  OD2 ASP A 275     6252   6085   5972    211    239     -9       O  
ATOM   2277  N   LEU A 276      -7.364  14.268  37.127  1.00 30.49           N  
ANISOU 2277  N   LEU A 276     4066   3898   3622    158    275    -58       N  
ATOM   2278  CA  LEU A 276      -7.867  14.795  35.853  1.00 29.45           C  
ANISOU 2278  CA  LEU A 276     3976   3766   3448    141    275    -73       C  
ATOM   2279  C   LEU A 276      -6.739  15.485  35.085  1.00 29.33           C  
ANISOU 2279  C   LEU A 276     3961   3765   3419    138    311    -69       C  
ATOM   2280  O   LEU A 276      -6.542  15.238  33.893  1.00 28.25           O  
ANISOU 2280  O   LEU A 276     3862   3618   3254    135    341    -87       O  
ATOM   2281  CB  LEU A 276      -9.012  15.788  36.073  1.00 27.41           C  
ANISOU 2281  CB  LEU A 276     3723   3517   3174    122    230    -69       C  
ATOM   2282  CG  LEU A 276     -10.395  15.318  36.529  1.00 29.94           C  
ANISOU 2282  CG  LEU A 276     4045   3830   3499    115    195    -78       C  
ATOM   2283  CD1 LEU A 276     -11.269  16.529  36.732  1.00 21.22           C  
ANISOU 2283  CD1 LEU A 276     2935   2739   2386    106    158    -71       C  
ATOM   2284  CD2 LEU A 276     -11.076  14.325  35.553  1.00 25.96           C  
ANISOU 2284  CD2 LEU A 276     3580   3308   2974    107    194   -104       C  
ATOM   2285  N   TYR A 277      -6.004  16.353  35.776  1.00 29.70           N  
ANISOU 2285  N   TYR A 277     3969   3833   3483    135    310    -46       N  
ATOM   2286  CA  TYR A 277      -4.891  17.075  35.166  1.00 30.31           C  
ANISOU 2286  CA  TYR A 277     4039   3927   3550    124    345    -40       C  
ATOM   2287  C   TYR A 277      -3.842  16.107  34.615  1.00 31.63           C  
ANISOU 2287  C   TYR A 277     4193   4091   3735    146    402    -52       C  
ATOM   2288  O   TYR A 277      -3.383  16.262  33.483  1.00 33.77           O  
ANISOU 2288  O   TYR A 277     4491   4363   3979    137    443    -65       O  
ATOM   2289  CB  TYR A 277      -4.269  18.058  36.165  1.00 30.84           C  
ANISOU 2289  CB  TYR A 277     4063   4018   3637    112    330    -14       C  
ATOM   2290  CG  TYR A 277      -3.271  19.011  35.554  1.00 31.46           C  
ANISOU 2290  CG  TYR A 277     4138   4116   3700     88    362     -6       C  
ATOM   2291  CD1 TYR A 277      -3.664  20.282  35.127  1.00 30.39           C  
ANISOU 2291  CD1 TYR A 277     4044   3979   3525     57    346     -1       C  
ATOM   2292  CD2 TYR A 277      -1.934  18.642  35.397  1.00 29.10           C  
ANISOU 2292  CD2 TYR A 277     3795   3834   3428     95    409     -4       C  
ATOM   2293  CE1 TYR A 277      -2.758  21.153  34.554  1.00 29.42           C  
ANISOU 2293  CE1 TYR A 277     3925   3870   3382     28    377      6       C  
ATOM   2294  CE2 TYR A 277      -1.014  19.510  34.831  1.00 29.85           C  
ANISOU 2294  CE2 TYR A 277     3883   3950   3509     66    443      1       C  
ATOM   2295  CZ  TYR A 277      -1.431  20.760  34.414  1.00 31.95           C  
ANISOU 2295  CZ  TYR A 277     4198   4213   3730     29    428      7       C  
ATOM   2296  OH  TYR A 277      -0.520  21.617  33.861  1.00 27.54           O  
ANISOU 2296  OH  TYR A 277     3639   3671   3153     -7    464     13       O  
ATOM   2297  N   LYS A 278      -3.478  15.097  35.399  1.00 32.37           N  
ANISOU 2297  N   LYS A 278     4250   4179   3872    177    405    -48       N  
ATOM   2298  CA  LYS A 278      -2.429  14.155  34.983  1.00 31.57           C  
ANISOU 2298  CA  LYS A 278     4128   4071   3796    209    459    -59       C  
ATOM   2299  C   LYS A 278      -2.829  13.291  33.783  1.00 32.65           C  
ANISOU 2299  C   LYS A 278     4327   4177   3903    216    494    -92       C  
ATOM   2300  O   LYS A 278      -1.975  12.901  32.987  1.00 33.30           O  
ANISOU 2300  O   LYS A 278     4411   4256   3987    232    554   -107       O  
ATOM   2301  CB  LYS A 278      -1.977  13.263  36.145  1.00 29.90           C  
ANISOU 2301  CB  LYS A 278     3868   3855   3639    245    447    -43       C  
ATOM   2302  CG  LYS A 278      -1.003  13.929  37.112  1.00 34.43           C  
ANISOU 2302  CG  LYS A 278     4371   4464   4249    244    431    -12       C  
ATOM   2303  CD  LYS A 278      -0.755  13.040  38.337  1.00 33.88           C  
ANISOU 2303  CD  LYS A 278     4265   4384   4225    277    403      7       C  
ATOM   2304  CE  LYS A 278       0.109  13.722  39.374  1.00 36.59           C  
ANISOU 2304  CE  LYS A 278     4542   4761   4597    269    374     40       C  
ATOM   2305  NZ  LYS A 278       0.391  12.815  40.533  1.00 39.53           N  
ANISOU 2305  NZ  LYS A 278     4887   5122   5011    303    342     61       N  
ATOM   2306  N   LYS A 279      -4.114  12.978  33.652  1.00 33.75           N  
ANISOU 2306  N   LYS A 279     4516   4292   4013    203    459   -104       N  
ATOM   2307  CA  LYS A 279      -4.537  12.130  32.545  1.00 34.93           C  
ANISOU 2307  CA  LYS A 279     4732   4411   4130    202    485   -136       C  
ATOM   2308  C   LYS A 279      -4.842  12.911  31.268  1.00 34.70           C  
ANISOU 2308  C   LYS A 279     4758   4386   4041    167    493   -149       C  
ATOM   2309  O   LYS A 279      -4.663  12.386  30.163  1.00 36.90           O  
ANISOU 2309  O   LYS A 279     5089   4644   4288    165    536   -175       O  
ATOM   2310  CB  LYS A 279      -5.724  11.242  32.931  1.00 36.68           C  
ANISOU 2310  CB  LYS A 279     4983   4604   4349    200    445   -145       C  
ATOM   2311  CG  LYS A 279      -5.962  10.093  31.935  1.00 38.94           C  
ANISOU 2311  CG  LYS A 279     5336   4851   4609    202    477   -179       C  
ATOM   2312  CD  LYS A 279      -7.311   9.417  32.144  1.00 42.23           C  
ANISOU 2312  CD  LYS A 279     5790   5245   5012    182    432   -190       C  
ATOM   2313  CE  LYS A 279      -7.549   8.311  31.116  1.00 45.11           C  
ANISOU 2313  CE  LYS A 279     6229   5567   5342    175    461   -225       C  
ATOM   2314  NZ  LYS A 279      -6.492   7.242  31.150  1.00 48.94           N  
ANISOU 2314  NZ  LYS A 279     6716   6019   5858    221    522   -236       N  
ATOM   2315  N   PHE A 280      -5.276  14.161  31.407  1.00 31.48           N  
ANISOU 2315  N   PHE A 280     4347   4000   3614    141    452   -131       N  
ATOM   2316  CA  PHE A 280      -5.787  14.897  30.251  1.00 31.65           C  
ANISOU 2316  CA  PHE A 280     4432   4020   3575    108    444   -139       C  
ATOM   2317  C   PHE A 280      -5.001  16.135  29.817  1.00 31.01           C  
ANISOU 2317  C   PHE A 280     4350   3959   3472     87    467   -125       C  
ATOM   2318  O   PHE A 280      -5.290  16.695  28.756  1.00 33.48           O  
ANISOU 2318  O   PHE A 280     4726   4266   3728     59    467   -131       O  
ATOM   2319  CB  PHE A 280      -7.257  15.276  30.470  1.00 32.06           C  
ANISOU 2319  CB  PHE A 280     4503   4070   3610     91    370   -134       C  
ATOM   2320  CG  PHE A 280      -8.170  14.101  30.708  1.00 34.23           C  
ANISOU 2320  CG  PHE A 280     4789   4324   3895     97    346   -151       C  
ATOM   2321  CD1 PHE A 280      -9.027  14.083  31.806  1.00 30.51           C  
ANISOU 2321  CD1 PHE A 280     4280   3860   3454    101    298   -140       C  
ATOM   2322  CD2 PHE A 280      -8.194  13.020  29.826  1.00 33.69           C  
ANISOU 2322  CD2 PHE A 280     4772   4227   3801     95    375   -179       C  
ATOM   2323  CE1 PHE A 280      -9.884  13.007  32.021  1.00 28.86           C  
ANISOU 2323  CE1 PHE A 280     4082   3632   3252     98    278   -155       C  
ATOM   2324  CE2 PHE A 280      -9.046  11.945  30.040  1.00 32.21           C  
ANISOU 2324  CE2 PHE A 280     4600   4018   3619     93    353   -195       C  
ATOM   2325  CZ  PHE A 280      -9.888  11.939  31.139  1.00 31.46           C  
ANISOU 2325  CZ  PHE A 280     4464   3933   3557     92    304   -182       C  
ATOM   2326  N   SER A 281      -4.035  16.579  30.619  1.00 28.92           N  
ANISOU 2326  N   SER A 281     4019   3719   3248     95    485   -105       N  
ATOM   2327  CA  SER A 281      -3.281  17.805  30.287  1.00 31.41           C  
ANISOU 2327  CA  SER A 281     4334   4056   3546     67    506    -91       C  
ATOM   2328  C   SER A 281      -2.164  17.620  29.260  1.00 31.75           C  
ANISOU 2328  C   SER A 281     4388   4102   3571     59    587   -107       C  
ATOM   2329  O   SER A 281      -1.758  18.584  28.610  1.00 32.43           O  
ANISOU 2329  O   SER A 281     4503   4198   3621     24    609   -101       O  
ATOM   2330  CB  SER A 281      -2.708  18.483  31.540  1.00 29.74           C  
ANISOU 2330  CB  SER A 281     4050   3872   3379     67    488    -63       C  
ATOM   2331  OG  SER A 281      -1.568  17.787  32.021  1.00 34.07           O  
ANISOU 2331  OG  SER A 281     4531   4436   3980     92    530    -62       O  
ATOM   2332  N   PHE A 282      -1.664  16.394  29.127  1.00 33.14           N  
ANISOU 2332  N   PHE A 282     4548   4269   3776     91    635   -127       N  
ATOM   2333  CA  PHE A 282      -0.497  16.110  28.280  1.00 34.96           C  
ANISOU 2333  CA  PHE A 282     4775   4504   4003     93    723   -145       C  
ATOM   2334  C   PHE A 282       0.702  16.971  28.685  1.00 35.91           C  
ANISOU 2334  C   PHE A 282     4824   4666   4156     79    753   -124       C  
ATOM   2335  O   PHE A 282       1.356  17.626  27.864  1.00 34.31           O  
ANISOU 2335  O   PHE A 282     4640   4476   3922     45    805   -128       O  
ATOM   2336  CB  PHE A 282      -0.837  16.213  26.790  1.00 35.42           C  
ANISOU 2336  CB  PHE A 282     4934   4540   3983     61    754   -169       C  
ATOM   2337  CG  PHE A 282      -1.670  15.069  26.299  1.00 39.14           C  
ANISOU 2337  CG  PHE A 282     5467   4972   4431     77    746   -196       C  
ATOM   2338  CD1 PHE A 282      -1.084  14.015  25.605  1.00 41.55           C  
ANISOU 2338  CD1 PHE A 282     5795   5256   4734     98    823   -229       C  
ATOM   2339  CD2 PHE A 282      -3.036  15.024  26.563  1.00 36.90           C  
ANISOU 2339  CD2 PHE A 282     5218   4673   4129     70    665   -192       C  
ATOM   2340  CE1 PHE A 282      -1.847  12.949  25.174  1.00 42.12           C  
ANISOU 2340  CE1 PHE A 282     5932   5289   4782    107    815   -255       C  
ATOM   2341  CE2 PHE A 282      -3.804  13.960  26.136  1.00 36.68           C  
ANISOU 2341  CE2 PHE A 282     5245   4612   4080     77    654   -217       C  
ATOM   2342  CZ  PHE A 282      -3.210  12.921  25.443  1.00 40.66           C  
ANISOU 2342  CZ  PHE A 282     5780   5091   4577     93    728   -249       C  
ATOM   2343  N   THR A 283       0.952  16.967  29.988  1.00 35.88           N  
ANISOU 2343  N   THR A 283     4739   4681   4212    100    716   -101       N  
ATOM   2344  CA  THR A 283       2.139  17.559  30.558  1.00 36.62           C  
ANISOU 2344  CA  THR A 283     4750   4816   4348     90    736    -80       C  
ATOM   2345  C   THR A 283       2.815  16.497  31.412  1.00 38.98           C  
ANISOU 2345  C   THR A 283     4965   5123   4723    145    744    -76       C  
ATOM   2346  O   THR A 283       2.212  15.460  31.721  1.00 38.63           O  
ANISOU 2346  O   THR A 283     4936   5050   4693    185    722    -85       O  
ATOM   2347  CB  THR A 283       1.795  18.787  31.423  1.00 37.11           C  
ANISOU 2347  CB  THR A 283     4802   4894   4404     55    669    -50       C  
ATOM   2348  OG1 THR A 283       1.008  18.382  32.555  1.00 34.35           O  
ANISOU 2348  OG1 THR A 283     4437   4532   4081     82    602    -38       O  
ATOM   2349  CG2 THR A 283       1.038  19.841  30.599  1.00 31.94           C  
ANISOU 2349  CG2 THR A 283     4237   4223   3675      9    654    -50       C  
ATOM   2350  N   ASN A 284       4.084  16.725  31.732  1.00 40.75           N  
ANISOU 2350  N   ASN A 284     5103   5387   4995    146    777    -64       N  
ATOM   2351  CA  ASN A 284       4.727  16.069  32.866  1.00 40.96           C  
ANISOU 2351  CA  ASN A 284     5037   5430   5097    191    756    -46       C  
ATOM   2352  C   ASN A 284       5.412  17.205  33.599  1.00 39.52           C  
ANISOU 2352  C   ASN A 284     4790   5294   4933    149    728    -15       C  
ATOM   2353  O   ASN A 284       6.282  17.873  33.043  1.00 40.98           O  
ANISOU 2353  O   ASN A 284     4945   5510   5115    115    779    -17       O  
ATOM   2354  CB  ASN A 284       5.724  14.968  32.444  1.00 43.06           C  
ANISOU 2354  CB  ASN A 284     5251   5697   5413    247    829    -64       C  
ATOM   2355  CG  ASN A 284       6.092  13.998  33.610  1.00 45.33           C  
ANISOU 2355  CG  ASN A 284     5466   5983   5775    309    793    -45       C  
ATOM   2356  OD1 ASN A 284       5.473  14.014  34.677  1.00 45.86           O  
ANISOU 2356  OD1 ASN A 284     5536   6042   5847    310    715    -22       O  
ATOM   2357  ND2 ASN A 284       7.093  13.151  33.386  1.00 42.30           N  
ANISOU 2357  ND2 ASN A 284     5021   5605   5448    364    851    -56       N  
ATOM   2358  N   GLN A 285       4.982  17.443  34.832  1.00 36.44           N  
ANISOU 2358  N   GLN A 285     4384   4905   4556    146    650     11       N  
ATOM   2359  CA  GLN A 285       5.414  18.607  35.580  1.00 34.80           C  
ANISOU 2359  CA  GLN A 285     4138   4733   4353     97    613     39       C  
ATOM   2360  C   GLN A 285       6.529  18.288  36.566  1.00 35.27           C  
ANISOU 2360  C   GLN A 285     4088   4830   4484    118    596     63       C  
ATOM   2361  O   GLN A 285       6.558  17.195  37.136  1.00 34.87           O  
ANISOU 2361  O   GLN A 285     4007   4766   4476    175    577     67       O  
ATOM   2362  CB  GLN A 285       4.227  19.216  36.328  1.00 32.91           C  
ANISOU 2362  CB  GLN A 285     3957   4471   4076     74    539     52       C  
ATOM   2363  CG  GLN A 285       3.145  19.775  35.429  1.00 36.22           C  
ANISOU 2363  CG  GLN A 285     4476   4860   4428     48    542     34       C  
ATOM   2364  CD  GLN A 285       3.585  20.997  34.638  1.00 39.02           C  
ANISOU 2364  CD  GLN A 285     4853   5229   4742    -10    576     35       C  
ATOM   2365  OE1 GLN A 285       4.755  21.389  34.668  1.00 41.12           O  
ANISOU 2365  OE1 GLN A 285     5058   5533   5033    -35    607     44       O  
ATOM   2366  NE2 GLN A 285       2.642  21.606  33.919  1.00 37.03           N  
ANISOU 2366  NE2 GLN A 285     4691   4949   4428    -33    568     26       N  
ATOM   2367  N   PRO A 286       7.445  19.250  36.783  1.00 33.57           N  
ANISOU 2367  N   PRO A 286     3816   4659   4280     68    598     80       N  
ATOM   2368  CA  PRO A 286       8.429  19.117  37.855  1.00 33.70           C  
ANISOU 2368  CA  PRO A 286     3729   4715   4360     77    562    108       C  
ATOM   2369  C   PRO A 286       7.775  19.060  39.239  1.00 35.32           C  
ANISOU 2369  C   PRO A 286     3951   4904   4565     82    471    133       C  
ATOM   2370  O   PRO A 286       8.340  18.482  40.168  1.00 35.87           O  
ANISOU 2370  O   PRO A 286     3952   4991   4688    113    432    155       O  
ATOM   2371  CB  PRO A 286       9.261  20.391  37.724  1.00 33.46           C  
ANISOU 2371  CB  PRO A 286     3661   4731   4321      1    577    119       C  
ATOM   2372  CG  PRO A 286       9.097  20.808  36.305  1.00 32.50           C  
ANISOU 2372  CG  PRO A 286     3601   4597   4150    -26    653     91       C  
ATOM   2373  CD  PRO A 286       7.697  20.438  35.948  1.00 32.64           C  
ANISOU 2373  CD  PRO A 286     3726   4557   4117      1    639     74       C  
ATOM   2374  N   SER A 287       6.590  19.647  39.367  1.00 34.62           N  
ANISOU 2374  N   SER A 287     3953   4783   4418     53    439    129       N  
ATOM   2375  CA  SER A 287       5.890  19.693  40.639  1.00 34.86           C  
ANISOU 2375  CA  SER A 287     4008   4796   4440     51    362    148       C  
ATOM   2376  C   SER A 287       4.380  19.690  40.443  1.00 34.39           C  
ANISOU 2376  C   SER A 287     4048   4689   4330     56    350    131       C  
ATOM   2377  O   SER A 287       3.868  20.222  39.456  1.00 35.59           O  
ANISOU 2377  O   SER A 287     4257   4827   4439     36    382    112       O  
ATOM   2378  CB  SER A 287       6.318  20.932  41.434  1.00 35.09           C  
ANISOU 2378  CB  SER A 287     4021   4854   4458    -15    321    172       C  
ATOM   2379  OG  SER A 287       5.494  21.114  42.574  1.00 37.40           O  
ANISOU 2379  OG  SER A 287     4359   5123   4729    -24    256    185       O  
ATOM   2380  N   TYR A 288       3.675  19.096  41.397  1.00 34.69           N  
ANISOU 2380  N   TYR A 288     4106   4703   4373     81    302    139       N  
ATOM   2381  CA  TYR A 288       2.215  19.054  41.365  1.00 36.11           C  
ANISOU 2381  CA  TYR A 288     4366   4842   4512     85    287    124       C  
ATOM   2382  C   TYR A 288       1.526  19.742  42.540  1.00 35.35           C  
ANISOU 2382  C   TYR A 288     4302   4738   4393     54    230    138       C  
ATOM   2383  O   TYR A 288       0.359  19.473  42.823  1.00 35.85           O  
ANISOU 2383  O   TYR A 288     4415   4771   4437     65    212    129       O  
ATOM   2384  CB  TYR A 288       1.713  17.622  41.172  1.00 33.54           C  
ANISOU 2384  CB  TYR A 288     4054   4486   4203    140    298    109       C  
ATOM   2385  CG  TYR A 288       1.937  17.152  39.758  1.00 36.61           C  
ANISOU 2385  CG  TYR A 288     4450   4869   4590    162    361     84       C  
ATOM   2386  CD1 TYR A 288       3.040  16.367  39.430  1.00 34.57           C  
ANISOU 2386  CD1 TYR A 288     4133   4625   4378    199    400     83       C  
ATOM   2387  CD2 TYR A 288       1.064  17.525  38.736  1.00 32.68           C  
ANISOU 2387  CD2 TYR A 288     4020   4353   4045    145    382     60       C  
ATOM   2388  CE1 TYR A 288       3.257  15.946  38.127  1.00 32.06           C  
ANISOU 2388  CE1 TYR A 288     3828   4298   4054    217    466     55       C  
ATOM   2389  CE2 TYR A 288       1.277  17.115  37.434  1.00 34.47           C  
ANISOU 2389  CE2 TYR A 288     4263   4572   4260    159    440     36       C  
ATOM   2390  CZ  TYR A 288       2.371  16.324  37.135  1.00 34.89           C  
ANISOU 2390  CZ  TYR A 288     4263   4636   4356    193    486     32       C  
ATOM   2391  OH  TYR A 288       2.578  15.921  35.838  1.00 35.38           O  
ANISOU 2391  OH  TYR A 288     4351   4689   4405    205    551      4       O  
ATOM   2392  N   SER A 289       2.243  20.642  43.207  1.00 37.49           N  
ANISOU 2392  N   SER A 289     4545   5035   4665     12    206    159       N  
ATOM   2393  CA  SER A 289       1.619  21.537  44.174  1.00 38.99           C  
ANISOU 2393  CA  SER A 289     4779   5214   4823    -26    163    168       C  
ATOM   2394  C   SER A 289       0.697  22.481  43.403  1.00 39.97           C  
ANISOU 2394  C   SER A 289     4969   5316   4900    -46    182    149       C  
ATOM   2395  O   SER A 289       0.924  22.741  42.216  1.00 42.72           O  
ANISOU 2395  O   SER A 289     5324   5670   5239    -50    221    137       O  
ATOM   2396  CB  SER A 289       2.679  22.331  44.933  1.00 38.17           C  
ANISOU 2396  CB  SER A 289     4635   5143   4726    -74    135    193       C  
ATOM   2397  OG  SER A 289       3.330  23.248  44.071  1.00 43.63           O  
ANISOU 2397  OG  SER A 289     5316   5855   5406   -112    168    190       O  
ATOM   2398  N   LEU A 290      -0.333  22.994  44.067  1.00 39.33           N  
ANISOU 2398  N   LEU A 290     4942   5211   4792    -57    154    147       N  
ATOM   2399  CA  LEU A 290      -1.307  23.863  43.408  1.00 37.09           C  
ANISOU 2399  CA  LEU A 290     4721   4902   4468    -67    164    130       C  
ATOM   2400  C   LEU A 290      -0.705  25.204  42.979  1.00 37.40           C  
ANISOU 2400  C   LEU A 290     4779   4951   4483   -114    175    137       C  
ATOM   2401  O   LEU A 290      -1.082  25.741  41.937  1.00 39.14           O  
ANISOU 2401  O   LEU A 290     5039   5156   4675   -117    196    125       O  
ATOM   2402  CB  LEU A 290      -2.540  24.065  44.295  1.00 36.86           C  
ANISOU 2402  CB  LEU A 290     4736   4846   4422    -62    136    125       C  
ATOM   2403  CG  LEU A 290      -3.754  24.766  43.673  1.00 37.58           C  
ANISOU 2403  CG  LEU A 290     4885   4910   4484    -55    141    108       C  
ATOM   2404  CD1 LEU A 290      -4.211  24.068  42.398  1.00 30.87           C  
ANISOU 2404  CD1 LEU A 290     4039   4056   3636    -23    163     91       C  
ATOM   2405  CD2 LEU A 290      -4.889  24.836  44.684  1.00 35.26           C  
ANISOU 2405  CD2 LEU A 290     4619   4595   4184    -46    120    101       C  
ATOM   2406  N   ASP A 291       0.219  25.731  43.784  1.00 36.45           N  
ANISOU 2406  N   ASP A 291     4631   4850   4367   -155    156    156       N  
ATOM   2407  CA  ASP A 291       0.998  26.928  43.450  1.00 38.67           C  
ANISOU 2407  CA  ASP A 291     4922   5143   4627   -211    167    164       C  
ATOM   2408  C   ASP A 291       1.660  26.781  42.097  1.00 36.18           C  
ANISOU 2408  C   ASP A 291     4583   4846   4317   -211    215    157       C  
ATOM   2409  O   ASP A 291       1.556  27.653  41.241  1.00 35.96           O  
ANISOU 2409  O   ASP A 291     4604   4805   4254   -237    238    152       O  
ATOM   2410  CB  ASP A 291       2.124  27.139  44.466  1.00 43.04           C  
ANISOU 2410  CB  ASP A 291     5427   5729   5199   -253    140    186       C  
ATOM   2411  CG  ASP A 291       1.772  28.128  45.554  1.00 51.67           C  
ANISOU 2411  CG  ASP A 291     6572   6800   6258   -295    103    193       C  
ATOM   2412  OD1 ASP A 291       0.761  28.859  45.419  1.00 55.74           O  
ANISOU 2412  OD1 ASP A 291     7164   7277   6738   -293    106    180       O  
ATOM   2413  OD2 ASP A 291       2.530  28.171  46.552  1.00 55.97           O  
ANISOU 2413  OD2 ASP A 291     7084   7367   6813   -328     69    212       O  
ATOM   2414  N   TYR A 292       2.354  25.661  41.929  1.00 34.43           N  
ANISOU 2414  N   TYR A 292     4291   4653   4139   -181    232    158       N  
ATOM   2415  CA  TYR A 292       3.169  25.425  40.760  1.00 32.32           C  
ANISOU 2415  CA  TYR A 292     3990   4408   3883   -181    286    151       C  
ATOM   2416  C   TYR A 292       2.298  25.258  39.516  1.00 31.97           C  
ANISOU 2416  C   TYR A 292     4006   4334   3807   -155    319    128       C  
ATOM   2417  O   TYR A 292       2.567  25.886  38.498  1.00 28.71           O  
ANISOU 2417  O   TYR A 292     3622   3920   3365   -185    356    122       O  
ATOM   2418  CB  TYR A 292       4.080  24.211  40.969  1.00 32.39           C  
ANISOU 2418  CB  TYR A 292     3907   4448   3950   -145    296    157       C  
ATOM   2419  CG  TYR A 292       5.122  24.087  39.896  1.00 30.93           C  
ANISOU 2419  CG  TYR A 292     3675   4294   3783   -152    358    149       C  
ATOM   2420  CD1 TYR A 292       4.826  23.469  38.685  1.00 29.53           C  
ANISOU 2420  CD1 TYR A 292     3522   4101   3597   -118    410    125       C  
ATOM   2421  CD2 TYR A 292       6.402  24.610  40.079  1.00 30.55           C  
ANISOU 2421  CD2 TYR A 292     3559   4291   3758   -198    367    165       C  
ATOM   2422  CE1 TYR A 292       5.784  23.356  37.685  1.00 33.81           C  
ANISOU 2422  CE1 TYR A 292     4025   4668   4151   -126    477    116       C  
ATOM   2423  CE2 TYR A 292       7.373  24.510  39.075  1.00 32.85           C  
ANISOU 2423  CE2 TYR A 292     3801   4613   4068   -207    434    156       C  
ATOM   2424  CZ  TYR A 292       7.051  23.878  37.884  1.00 33.57           C  
ANISOU 2424  CZ  TYR A 292     3922   4685   4148   -170    491    130       C  
ATOM   2425  OH  TYR A 292       7.986  23.766  36.885  1.00 36.83           O  
ANISOU 2425  OH  TYR A 292     4293   5126   4576   -179    566    118       O  
ATOM   2426  N   ILE A 293       1.250  24.434  39.613  1.00 30.08           N  
ANISOU 2426  N   ILE A 293     3790   4068   3570   -106    302    116       N  
ATOM   2427  CA  ILE A 293       0.346  24.200  38.484  1.00 29.38           C  
ANISOU 2427  CA  ILE A 293     3759   3953   3452    -83    323     95       C  
ATOM   2428  C   ILE A 293      -0.445  25.470  38.134  1.00 30.12           C  
ANISOU 2428  C   ILE A 293     3931   4020   3495   -111    307     95       C  
ATOM   2429  O   ILE A 293      -0.621  25.788  36.951  1.00 30.32           O  
ANISOU 2429  O   ILE A 293     4003   4032   3485   -120    333     86       O  
ATOM   2430  CB  ILE A 293      -0.609  23.005  38.750  1.00 29.14           C  
ANISOU 2430  CB  ILE A 293     3731   3902   3438    -31    305     83       C  
ATOM   2431  CG1 ILE A 293       0.183  21.724  39.040  1.00 31.05           C  
ANISOU 2431  CG1 ILE A 293     3906   4163   3730      2    321     84       C  
ATOM   2432  CG2 ILE A 293      -1.581  22.799  37.594  1.00 29.56           C  
ANISOU 2432  CG2 ILE A 293     3843   3929   3458    -14    318     62       C  
ATOM   2433  CD1 ILE A 293       0.896  21.112  37.842  1.00 27.79           C  
ANISOU 2433  CD1 ILE A 293     3476   3758   3324     17    380     69       C  
ATOM   2434  N   SER A 294      -0.901  26.194  39.156  1.00 29.18           N  
ANISOU 2434  N   SER A 294     3830   3889   3369   -125    267    106       N  
ATOM   2435  CA  SER A 294      -1.565  27.486  38.949  1.00 31.56           C  
ANISOU 2435  CA  SER A 294     4204   4160   3626   -148    251    108       C  
ATOM   2436  C   SER A 294      -0.704  28.486  38.195  1.00 32.68           C  
ANISOU 2436  C   SER A 294     4371   4307   3738   -200    279    116       C  
ATOM   2437  O   SER A 294      -1.196  29.170  37.304  1.00 32.13           O  
ANISOU 2437  O   SER A 294     4370   4211   3627   -207    284    112       O  
ATOM   2438  CB  SER A 294      -1.994  28.125  40.274  1.00 30.22           C  
ANISOU 2438  CB  SER A 294     4048   3977   3456   -158    211    116       C  
ATOM   2439  OG  SER A 294      -3.041  27.396  40.851  1.00 33.32           O  
ANISOU 2439  OG  SER A 294     4437   4358   3866   -115    189    107       O  
ATOM   2440  N   GLU A 295       0.567  28.599  38.579  1.00 35.16           N  
ANISOU 2440  N   GLU A 295     4632   4656   4073   -238    295    127       N  
ATOM   2441  CA  GLU A 295       1.461  29.560  37.932  1.00 38.35           C  
ANISOU 2441  CA  GLU A 295     5054   5068   4449   -298    327    135       C  
ATOM   2442  C   GLU A 295       1.705  29.164  36.473  1.00 37.26           C  
ANISOU 2442  C   GLU A 295     4926   4934   4295   -293    379    122       C  
ATOM   2443  O   GLU A 295       1.767  30.021  35.590  1.00 37.63           O  
ANISOU 2443  O   GLU A 295     5037   4964   4296   -330    401    124       O  
ATOM   2444  CB  GLU A 295       2.765  29.742  38.738  1.00 41.66           C  
ANISOU 2444  CB  GLU A 295     5401   5528   4898   -345    327    151       C  
ATOM   2445  CG  GLU A 295       4.060  29.965  37.921  1.00 54.92           C  
ANISOU 2445  CG  GLU A 295     7044   7242   6579   -394    382    153       C  
ATOM   2446  CD  GLU A 295       4.289  31.401  37.464  1.00 63.16           C  
ANISOU 2446  CD  GLU A 295     8159   8268   7571   -465    395    161       C  
ATOM   2447  OE1 GLU A 295       3.359  32.024  36.904  1.00 67.21           O  
ANISOU 2447  OE1 GLU A 295     8768   8733   8035   -460    388    157       O  
ATOM   2448  OE2 GLU A 295       5.423  31.902  37.646  1.00 65.69           O  
ANISOU 2448  OE2 GLU A 295     8437   8621   7899   -529    411    172       O  
ATOM   2449  N   PHE A 296       1.806  27.862  36.226  1.00 35.17           N  
ANISOU 2449  N   PHE A 296     4610   4687   4065   -247    400    110       N  
ATOM   2450  CA  PHE A 296       1.994  27.358  34.874  1.00 35.54           C  
ANISOU 2450  CA  PHE A 296     4672   4735   4095   -239    453     93       C  
ATOM   2451  C   PHE A 296       0.751  27.619  34.017  1.00 33.72           C  
ANISOU 2451  C   PHE A 296     4538   4461   3813   -223    437     84       C  
ATOM   2452  O   PHE A 296       0.847  28.149  32.914  1.00 34.18           O  
ANISOU 2452  O   PHE A 296     4656   4506   3823   -252    467     81       O  
ATOM   2453  CB  PHE A 296       2.327  25.862  34.912  1.00 35.88           C  
ANISOU 2453  CB  PHE A 296     4644   4800   4189   -189    476     81       C  
ATOM   2454  CG  PHE A 296       2.529  25.242  33.552  1.00 36.79           C  
ANISOU 2454  CG  PHE A 296     4779   4914   4288   -177    537     59       C  
ATOM   2455  CD1 PHE A 296       3.785  25.267  32.939  1.00 36.34           C  
ANISOU 2455  CD1 PHE A 296     4680   4887   4239   -206    604     56       C  
ATOM   2456  CD2 PHE A 296       1.471  24.615  32.893  1.00 32.99           C  
ANISOU 2456  CD2 PHE A 296     4355   4400   3781   -140    529     41       C  
ATOM   2457  CE1 PHE A 296       3.984  24.693  31.679  1.00 36.52           C  
ANISOU 2457  CE1 PHE A 296     4728   4906   4242   -197    669     33       C  
ATOM   2458  CE2 PHE A 296       1.660  24.025  31.635  1.00 37.10           C  
ANISOU 2458  CE2 PHE A 296     4904   4916   4279   -134    586     20       C  
ATOM   2459  CZ  PHE A 296       2.919  24.068  31.024  1.00 34.48           C  
ANISOU 2459  CZ  PHE A 296     4538   4611   3952   -162    659     15       C  
ATOM   2460  N   GLU A 297      -0.413  27.258  34.539  1.00 32.35           N  
ANISOU 2460  N   GLU A 297     4379   4266   3647   -180    388     80       N  
ATOM   2461  CA  GLU A 297      -1.647  27.314  33.772  1.00 33.12           C  
ANISOU 2461  CA  GLU A 297     4551   4329   3706   -157    366     71       C  
ATOM   2462  C   GLU A 297      -2.199  28.726  33.613  1.00 33.75           C  
ANISOU 2462  C   GLU A 297     4709   4376   3739   -181    336     84       C  
ATOM   2463  O   GLU A 297      -2.741  29.059  32.562  1.00 33.62           O  
ANISOU 2463  O   GLU A 297     4764   4334   3677   -183    333     81       O  
ATOM   2464  CB  GLU A 297      -2.710  26.421  34.414  1.00 32.07           C  
ANISOU 2464  CB  GLU A 297     4396   4186   3601   -105    326     61       C  
ATOM   2465  CG  GLU A 297      -2.445  24.928  34.275  1.00 34.13           C  
ANISOU 2465  CG  GLU A 297     4608   4464   3895    -73    353     45       C  
ATOM   2466  CD  GLU A 297      -2.399  24.450  32.827  1.00 35.72           C  
ANISOU 2466  CD  GLU A 297     4850   4658   4064    -72    392     28       C  
ATOM   2467  OE1 GLU A 297      -3.216  24.909  31.992  1.00 37.12           O  
ANISOU 2467  OE1 GLU A 297     5101   4811   4194    -78    373     25       O  
ATOM   2468  OE2 GLU A 297      -1.546  23.594  32.530  1.00 37.12           O  
ANISOU 2468  OE2 GLU A 297     4988   4852   4262    -65    441     17       O  
ATOM   2469  N   LEU A 298      -2.051  29.544  34.653  1.00 33.25           N  
ANISOU 2469  N   LEU A 298     4637   4311   3687   -201    313     98       N  
ATOM   2470  CA  LEU A 298      -2.767  30.813  34.756  1.00 33.24           C  
ANISOU 2470  CA  LEU A 298     4710   4270   3650   -210    277    109       C  
ATOM   2471  C   LEU A 298      -1.871  32.044  34.780  1.00 36.91           C  
ANISOU 2471  C   LEU A 298     5209   4729   4087   -274    294    125       C  
ATOM   2472  O   LEU A 298      -2.354  33.156  34.562  1.00 34.98           O  
ANISOU 2472  O   LEU A 298     5043   4443   3802   -286    274    135       O  
ATOM   2473  CB  LEU A 298      -3.629  30.824  36.017  1.00 31.77           C  
ANISOU 2473  CB  LEU A 298     4505   4072   3492   -177    233    109       C  
ATOM   2474  CG  LEU A 298      -4.569  29.643  36.255  1.00 27.02           C  
ANISOU 2474  CG  LEU A 298     3866   3477   2923   -121    213     94       C  
ATOM   2475  CD1 LEU A 298      -5.057  29.643  37.686  1.00 21.94           C  
ANISOU 2475  CD1 LEU A 298     3193   2831   2310   -104    185     94       C  
ATOM   2476  CD2 LEU A 298      -5.734  29.683  35.270  1.00 27.51           C  
ANISOU 2476  CD2 LEU A 298     3983   3513   2958    -90    190     87       C  
ATOM   2477  N   ASN A 299      -0.578  31.850  35.047  1.00 40.15           N  
ANISOU 2477  N   ASN A 299     5558   5179   4520   -315    330    129       N  
ATOM   2478  CA  ASN A 299       0.342  32.969  35.259  1.00 44.12           C  
ANISOU 2478  CA  ASN A 299     6078   5682   5002   -385    345    144       C  
ATOM   2479  C   ASN A 299       0.030  33.827  36.487  1.00 45.33           C  
ANISOU 2479  C   ASN A 299     6253   5813   5156   -397    302    154       C  
ATOM   2480  O   ASN A 299       0.186  35.056  36.454  1.00 46.76           O  
ANISOU 2480  O   ASN A 299     6502   5964   5299   -444    299    165       O  
ATOM   2481  CB  ASN A 299       0.430  33.858  34.019  1.00 47.21           C  
ANISOU 2481  CB  ASN A 299     6561   6045   5333   -424    369    149       C  
ATOM   2482  CG  ASN A 299       1.801  33.880  33.438  1.00 54.00           C  
ANISOU 2482  CG  ASN A 299     7389   6941   6188   -486    431    151       C  
ATOM   2483  OD1 ASN A 299       2.603  34.758  33.765  1.00 58.83           O  
ANISOU 2483  OD1 ASN A 299     8005   7558   6789   -552    442    163       O  
ATOM   2484  ND2 ASN A 299       2.106  32.897  32.595  1.00 56.94           N  
ANISOU 2484  ND2 ASN A 299     7727   7339   6569   -468    474    137       N  
ATOM   2485  N   VAL A 300      -0.408  33.183  37.563  1.00 44.16           N  
ANISOU 2485  N   VAL A 300     6054   5675   5048   -357    271    149       N  
ATOM   2486  CA  VAL A 300      -0.624  33.880  38.827  1.00 46.81           C  
ANISOU 2486  CA  VAL A 300     6407   5993   5386   -371    237    156       C  
ATOM   2487  C   VAL A 300       0.543  33.587  39.761  1.00 48.87           C  
ANISOU 2487  C   VAL A 300     6589   6298   5679   -412    239    164       C  
ATOM   2488  O   VAL A 300       1.069  32.473  39.767  1.00 49.44           O  
ANISOU 2488  O   VAL A 300     6579   6414   5792   -393    252    162       O  
ATOM   2489  CB  VAL A 300      -1.974  33.507  39.502  1.00 45.96           C  
ANISOU 2489  CB  VAL A 300     6308   5861   5294   -305    201    146       C  
ATOM   2490  CG1 VAL A 300      -3.138  34.029  38.681  1.00 44.95           C  
ANISOU 2490  CG1 VAL A 300     6257   5687   5134   -269    189    141       C  
ATOM   2491  CG2 VAL A 300      -2.095  31.995  39.727  1.00 46.39           C  
ANISOU 2491  CG2 VAL A 300     6281   5951   5394   -260    202    136       C  
ATOM   2492  N   GLY A 301       0.958  34.590  40.528  1.00 49.90           N  
ANISOU 2492  N   GLY A 301     6749   6418   5792   -467    224    175       N  
ATOM   2493  CA  GLY A 301       2.076  34.429  41.457  1.00 53.43           C  
ANISOU 2493  CA  GLY A 301     7125   6909   6266   -515    215    185       C  
ATOM   2494  C   GLY A 301       1.731  33.492  42.599  1.00 55.06           C  
ANISOU 2494  C   GLY A 301     7279   7130   6510   -472    182    183       C  
ATOM   2495  O   GLY A 301       0.561  33.374  42.974  1.00 54.22           O  
ANISOU 2495  O   GLY A 301     7211   6990   6399   -423    163    173       O  
ATOM   2496  N   LYS A 302       2.747  32.822  43.144  1.00 58.65           N  
ANISOU 2496  N   LYS A 302     7645   7636   7003   -490    176    194       N  
ATOM   2497  CA  LYS A 302       2.580  31.937  44.309  1.00 62.07           C  
ANISOU 2497  CA  LYS A 302     8032   8084   7469   -458    140    197       C  
ATOM   2498  C   LYS A 302       1.916  32.660  45.495  1.00 63.90           C  
ANISOU 2498  C   LYS A 302     8330   8278   7672   -475    103    197       C  
ATOM   2499  O   LYS A 302       2.000  33.891  45.615  1.00 64.64           O  
ANISOU 2499  O   LYS A 302     8490   8345   7726   -528    100    199       O  
ATOM   2500  CB  LYS A 302       3.931  31.347  44.747  1.00 62.44           C  
ANISOU 2500  CB  LYS A 302     7978   8189   7558   -485    130    214       C  
ATOM   2501  CG  LYS A 302       4.931  32.388  45.276  1.00 66.68           C  
ANISOU 2501  CG  LYS A 302     8515   8743   8078   -575    112    230       C  
ATOM   2502  CD  LYS A 302       5.744  31.871  46.465  1.00 69.02           C  
ANISOU 2502  CD  LYS A 302     8737   9081   8408   -595     65    249       C  
ATOM   2503  CE  LYS A 302       7.114  31.342  46.039  1.00 71.04           C  
ANISOU 2503  CE  LYS A 302     8878   9402   8713   -610     80    262       C  
ATOM   2504  NZ  LYS A 302       7.921  30.886  47.209  1.00 67.40           N  
ANISOU 2504  NZ  LYS A 302     8342   8981   8285   -628     24    284       N  
ATOM   2505  N   LEU A 303       1.252  31.898  46.360  1.00 65.15           N  
ANISOU 2505  N   LEU A 303     8478   8430   7845   -432     79    193       N  
ATOM   2506  CA  LEU A 303       0.731  32.459  47.604  1.00 67.94           C  
ANISOU 2506  CA  LEU A 303     8889   8753   8172   -451     50    192       C  
ATOM   2507  C   LEU A 303       1.878  32.611  48.601  1.00 69.82           C  
ANISOU 2507  C   LEU A 303     9094   9022   8412   -516     15    212       C  
ATOM   2508  O   LEU A 303       2.449  31.614  49.058  1.00 70.66           O  
ANISOU 2508  O   LEU A 303     9126   9167   8553   -504     -6    225       O  
ATOM   2509  CB  LEU A 303      -0.396  31.597  48.191  1.00 67.36           C  
ANISOU 2509  CB  LEU A 303     8820   8663   8112   -389     41    180       C  
ATOM   2510  CG  LEU A 303      -1.794  31.554  47.550  1.00 66.59           C  
ANISOU 2510  CG  LEU A 303     8763   8529   8009   -328     64    159       C  
ATOM   2511  CD1 LEU A 303      -2.111  32.782  46.695  1.00 65.20           C  
ANISOU 2511  CD1 LEU A 303     8655   8319   7801   -339     82    152       C  
ATOM   2512  CD2 LEU A 303      -2.000  30.263  46.767  1.00 68.02           C  
ANISOU 2512  CD2 LEU A 303     8886   8733   8227   -273     78    154       C  
ATOM   2513  N   LYS A 304       2.213  33.861  48.920  1.00 71.45           N  
ANISOU 2513  N   LYS A 304     9359   9210   8579   -584      7    215       N  
ATOM   2514  CA  LYS A 304       3.384  34.168  49.737  1.00 73.28           C  
ANISOU 2514  CA  LYS A 304     9562   9473   8806   -661    -29    234       C  
ATOM   2515  C   LYS A 304       3.007  34.392  51.198  1.00 72.56           C  
ANISOU 2515  C   LYS A 304     9527   9357   8686   -683    -68    234       C  
ATOM   2516  O   LYS A 304       2.060  35.119  51.497  1.00 72.81           O  
ANISOU 2516  O   LYS A 304     9653   9333   8679   -678    -57    217       O  
ATOM   2517  CB  LYS A 304       4.104  35.404  49.190  1.00 75.09           C  
ANISOU 2517  CB  LYS A 304     9825   9699   9007   -738    -15    238       C  
ATOM   2518  CG  LYS A 304       5.612  35.234  49.064  1.00 79.67           C  
ANISOU 2518  CG  LYS A 304    10310  10345   9617   -796    -26    259       C  
ATOM   2519  CD  LYS A 304       6.349  36.566  49.217  1.00 84.27           C  
ANISOU 2519  CD  LYS A 304    10939  10921  10159   -901    -34    265       C  
ATOM   2520  CE  LYS A 304       7.081  36.673  50.562  1.00 85.96           C  
ANISOU 2520  CE  LYS A 304    11134  11160  10367   -968    -95    282       C  
ATOM   2521  NZ  LYS A 304       6.186  36.599  51.756  1.00 87.29           N  
ANISOU 2521  NZ  LYS A 304    11374  11287  10507   -945   -127    275       N  
ATOM   2522  N   TYR A 305       3.754  33.756  52.098  1.00 71.97           N  
ANISOU 2522  N   TYR A 305     9395   9321   8629   -706   -113    254       N  
ATOM   2523  CA  TYR A 305       3.587  33.950  53.539  1.00 71.15           C  
ANISOU 2523  CA  TYR A 305     9345   9198   8491   -741   -155    257       C  
ATOM   2524  C   TYR A 305       4.893  33.688  54.290  1.00 70.48           C  
ANISOU 2524  C   TYR A 305     9195   9166   8419   -802   -214    286       C  
ATOM   2525  O   TYR A 305       5.813  33.072  53.748  1.00 69.73           O  
ANISOU 2525  O   TYR A 305     8996   9126   8374   -795   -220    304       O  
ATOM   2526  CB  TYR A 305       2.455  33.071  54.086  1.00 72.17           C  
ANISOU 2526  CB  TYR A 305     9495   9303   8625   -671   -151    246       C  
ATOM   2527  CG  TYR A 305       2.631  31.581  53.860  1.00 73.97           C  
ANISOU 2527  CG  TYR A 305     9628   9570   8907   -610   -159    258       C  
ATOM   2528  CD1 TYR A 305       3.322  30.794  54.781  1.00 75.14           C  
ANISOU 2528  CD1 TYR A 305     9728   9750   9071   -623   -211    283       C  
ATOM   2529  CD2 TYR A 305       2.091  30.956  52.736  1.00 74.58           C  
ANISOU 2529  CD2 TYR A 305     9672   9648   9019   -539   -116    245       C  
ATOM   2530  CE1 TYR A 305       3.485  29.428  54.586  1.00 75.93           C  
ANISOU 2530  CE1 TYR A 305     9749   9878   9221   -563   -218    295       C  
ATOM   2531  CE2 TYR A 305       2.247  29.584  52.530  1.00 76.57           C  
ANISOU 2531  CE2 TYR A 305     9846   9928   9318   -484   -120    254       C  
ATOM   2532  CZ  TYR A 305       2.946  28.828  53.462  1.00 77.45           C  
ANISOU 2532  CZ  TYR A 305     9913  10067   9446   -493   -170    279       C  
ATOM   2533  OH  TYR A 305       3.107  27.473  53.276  1.00 79.01           O  
ANISOU 2533  OH  TYR A 305    10042  10286   9692   -435   -174    289       O  
ATOM   2534  N   ASP A 306       4.962  34.161  55.535  1.00 69.99           N  
ANISOU 2534  N   ASP A 306     9194   9086   8311   -861   -257    292       N  
ATOM   2535  CA  ASP A 306       6.151  34.005  56.382  1.00 70.27           C  
ANISOU 2535  CA  ASP A 306     9180   9169   8351   -927   -325    321       C  
ATOM   2536  C   ASP A 306       5.996  32.854  57.377  1.00 68.69           C  
ANISOU 2536  C   ASP A 306     8958   8979   8162   -890   -371    337       C  
ATOM   2537  O   ASP A 306       4.909  32.630  57.920  1.00 67.23           O  
ANISOU 2537  O   ASP A 306     8846   8749   7949   -854   -356    321       O  
ATOM   2538  CB  ASP A 306       6.449  35.299  57.151  1.00 71.83           C  
ANISOU 2538  CB  ASP A 306     9467   9341   8483  -1030   -353    320       C  
ATOM   2539  CG  ASP A 306       6.618  36.513  56.241  1.00 74.14           C  
ANISOU 2539  CG  ASP A 306     9798   9616   8758  -1076   -310    306       C  
ATOM   2540  OD1 ASP A 306       6.691  37.637  56.781  1.00 75.67           O  
ANISOU 2540  OD1 ASP A 306    10085   9775   8893  -1155   -322    299       O  
ATOM   2541  OD2 ASP A 306       6.679  36.357  54.999  1.00 74.05           O  
ANISOU 2541  OD2 ASP A 306     9732   9621   8784  -1036   -265    302       O  
ATOM   2542  N   GLY A 307       7.093  32.139  57.618  1.00 67.57           N  
ANISOU 2542  N   GLY A 307     8716   8896   8061   -901   -425    369       N  
ATOM   2543  CA  GLY A 307       7.101  31.001  58.540  1.00 64.71           C  
ANISOU 2543  CA  GLY A 307     8330   8545   7712   -867   -478    391       C  
ATOM   2544  C   GLY A 307       6.428  29.764  57.967  1.00 63.08           C  
ANISOU 2544  C   GLY A 307     8083   8333   7552   -761   -440    385       C  
ATOM   2545  O   GLY A 307       5.849  29.817  56.873  1.00 62.01           O  
ANISOU 2545  O   GLY A 307     7944   8183   7435   -714   -373    360       O  
ATOM   2546  N   PRO A 308       6.499  28.633  58.696  1.00 61.97           N  
ANISOU 2546  N   PRO A 308     7917   8201   7429   -726   -486    407       N  
ATOM   2547  CA  PRO A 308       5.876  27.400  58.211  1.00 60.42           C  
ANISOU 2547  CA  PRO A 308     7688   7994   7273   -630   -453    402       C  
ATOM   2548  C   PRO A 308       4.351  27.471  58.281  1.00 58.91           C  
ANISOU 2548  C   PRO A 308     7595   7744   7043   -600   -399    368       C  
ATOM   2549  O   PRO A 308       3.803  28.158  59.146  1.00 57.44           O  
ANISOU 2549  O   PRO A 308     7505   7522   6796   -646   -405    358       O  
ATOM   2550  CB  PRO A 308       6.403  26.337  59.180  1.00 61.73           C  
ANISOU 2550  CB  PRO A 308     7821   8178   7455   -617   -526    438       C  
ATOM   2551  CG  PRO A 308       6.683  27.085  60.444  1.00 61.43           C  
ANISOU 2551  CG  PRO A 308     7851   8134   7355   -705   -589    453       C  
ATOM   2552  CD  PRO A 308       7.140  28.451  60.014  1.00 62.40           C  
ANISOU 2552  CD  PRO A 308     7979   8270   7459   -776   -573    440       C  
ATOM   2553  N   ILE A 309       3.687  26.757  57.375  1.00 58.07           N  
ANISOU 2553  N   ILE A 309     7463   7628   6973   -525   -347    351       N  
ATOM   2554  CA  ILE A 309       2.224  26.682  57.334  1.00 57.14           C  
ANISOU 2554  CA  ILE A 309     7419   7462   6831   -488   -296    320       C  
ATOM   2555  C   ILE A 309       1.645  26.212  58.680  1.00 55.61           C  
ANISOU 2555  C   ILE A 309     7292   7239   6598   -498   -324    326       C  
ATOM   2556  O   ILE A 309       0.507  26.536  59.027  1.00 54.10           O  
ANISOU 2556  O   ILE A 309     7180   7008   6369   -498   -288    300       O  
ATOM   2557  CB  ILE A 309       1.744  25.786  56.138  1.00 57.69           C  
ANISOU 2557  CB  ILE A 309     7437   7533   6949   -408   -247    306       C  
ATOM   2558  CG1 ILE A 309       0.395  26.274  55.568  1.00 60.68           C  
ANISOU 2558  CG1 ILE A 309     7875   7873   7308   -384   -186    268       C  
ATOM   2559  CG2 ILE A 309       1.784  24.297  56.491  1.00 57.09           C  
ANISOU 2559  CG2 ILE A 309     7327   7461   6905   -359   -270    324       C  
ATOM   2560  CD1 ILE A 309      -0.862  25.650  56.177  1.00 62.96           C  
ANISOU 2560  CD1 ILE A 309     8216   8126   7579   -355   -169    253       C  
ATOM   2561  N   SER A 310       2.455  25.474  59.440  1.00 53.90           N  
ANISOU 2561  N   SER A 310     7044   7045   6391   -508   -388    361       N  
ATOM   2562  CA  SER A 310       2.069  24.985  60.760  1.00 53.01           C  
ANISOU 2562  CA  SER A 310     6999   6905   6236   -525   -423    374       C  
ATOM   2563  C   SER A 310       1.982  26.097  61.810  1.00 52.01           C  
ANISOU 2563  C   SER A 310     6966   6758   6036   -607   -443    368       C  
ATOM   2564  O   SER A 310       1.528  25.862  62.931  1.00 52.17           O  
ANISOU 2564  O   SER A 310     7063   6750   6009   -630   -461    372       O  
ATOM   2565  CB  SER A 310       3.031  23.883  61.218  1.00 55.32           C  
ANISOU 2565  CB  SER A 310     7233   7226   6561   -509   -494    417       C  
ATOM   2566  OG  SER A 310       4.385  24.303  61.145  1.00 59.18           O  
ANISOU 2566  OG  SER A 310     7652   7763   7072   -545   -548    444       O  
ATOM   2567  N   LYS A 311       2.407  27.303  61.441  1.00 50.25           N  
ANISOU 2567  N   LYS A 311     6746   6545   5802   -653   -437    359       N  
ATOM   2568  CA  LYS A 311       2.304  28.466  62.322  1.00 50.43           C  
ANISOU 2568  CA  LYS A 311     6866   6540   5753   -732   -447    348       C  
ATOM   2569  C   LYS A 311       1.515  29.612  61.689  1.00 49.55           C  
ANISOU 2569  C   LYS A 311     6808   6396   5623   -733   -376    308       C  
ATOM   2570  O   LYS A 311       1.328  30.659  62.313  1.00 49.68           O  
ANISOU 2570  O   LYS A 311     6914   6381   5581   -792   -372    293       O  
ATOM   2571  CB  LYS A 311       3.694  28.955  62.741  1.00 51.77           C  
ANISOU 2571  CB  LYS A 311     7007   6749   5914   -807   -524    380       C  
ATOM   2572  CG  LYS A 311       4.415  28.023  63.702  1.00 55.76           C  
ANISOU 2572  CG  LYS A 311     7487   7278   6419   -819   -609    423       C  
ATOM   2573  CD  LYS A 311       5.704  28.648  64.218  1.00 62.95           C  
ANISOU 2573  CD  LYS A 311     8377   8226   7314   -904   -690    452       C  
ATOM   2574  CE  LYS A 311       6.501  27.665  65.082  1.00 66.75           C  
ANISOU 2574  CE  LYS A 311     8820   8737   7805   -908   -786    500       C  
ATOM   2575  NZ  LYS A 311       7.775  28.264  65.594  1.00 69.61           N  
ANISOU 2575  NZ  LYS A 311     9153   9141   8154   -995   -873    531       N  
ATOM   2576  N   LEU A 312       1.039  29.402  60.463  1.00 46.11           N  
ANISOU 2576  N   LEU A 312     6323   5963   5235   -667   -322    290       N  
ATOM   2577  CA  LEU A 312       0.335  30.443  59.717  1.00 44.96           C  
ANISOU 2577  CA  LEU A 312     6217   5786   5078   -659   -261    257       C  
ATOM   2578  C   LEU A 312      -1.013  30.829  60.321  1.00 43.19           C  
ANISOU 2578  C   LEU A 312     6092   5507   4811   -650   -215    224       C  
ATOM   2579  O   LEU A 312      -1.353  32.007  60.363  1.00 42.14           O  
ANISOU 2579  O   LEU A 312     6030   5339   4641   -678   -188    202       O  
ATOM   2580  CB  LEU A 312       0.163  30.049  58.245  1.00 43.41           C  
ANISOU 2580  CB  LEU A 312     5946   5608   4941   -592   -221    249       C  
ATOM   2581  CG  LEU A 312      -0.377  31.132  57.305  1.00 46.62           C  
ANISOU 2581  CG  LEU A 312     6385   5987   5339   -583   -169    221       C  
ATOM   2582  CD1 LEU A 312       0.544  32.353  57.262  1.00 46.67           C  
ANISOU 2582  CD1 LEU A 312     6416   5999   5319   -658   -188    229       C  
ATOM   2583  CD2 LEU A 312      -0.593  30.576  55.896  1.00 43.29           C  
ANISOU 2583  CD2 LEU A 312     5895   5583   4969   -517   -135    215       C  
ATOM   2584  N   ARG A 313      -1.779  29.844  60.778  1.00 41.20           N  
ANISOU 2584  N   ARG A 313     5845   5246   4563   -610   -202    219       N  
ATOM   2585  CA  ARG A 313      -3.081  30.137  61.364  1.00 40.67           C  
ANISOU 2585  CA  ARG A 313     5861   5130   4460   -600   -151    186       C  
ATOM   2586  C   ARG A 313      -2.951  31.059  62.577  1.00 40.12           C  
ANISOU 2586  C   ARG A 313     5896   5030   4319   -675   -165    181       C  
ATOM   2587  O   ARG A 313      -3.659  32.063  62.666  1.00 39.72           O  
ANISOU 2587  O   ARG A 313     5916   4937   4237   -681   -118    149       O  
ATOM   2588  CB  ARG A 313      -3.846  28.857  61.728  1.00 40.21           C  
ANISOU 2588  CB  ARG A 313     5791   5070   4416   -558   -137    185       C  
ATOM   2589  CG  ARG A 313      -5.214  29.120  62.351  1.00 39.29           C  
ANISOU 2589  CG  ARG A 313     5752   4910   4267   -549    -77    149       C  
ATOM   2590  CD  ARG A 313      -5.947  27.826  62.722  1.00 39.94           C  
ANISOU 2590  CD  ARG A 313     5823   4993   4362   -517    -60    149       C  
ATOM   2591  NE  ARG A 313      -7.134  28.110  63.529  1.00 39.00           N  
ANISOU 2591  NE  ARG A 313     5780   4834   4204   -524     -3    115       N  
ATOM   2592  CZ  ARG A 313      -7.148  28.162  64.861  1.00 37.03           C  
ANISOU 2592  CZ  ARG A 313     5615   4561   3892   -579     -9    117       C  
ATOM   2593  NH1 ARG A 313      -6.042  27.939  65.554  1.00 35.07           N  
ANISOU 2593  NH1 ARG A 313     5385   4327   3614   -632    -80    153       N  
ATOM   2594  NH2 ARG A 313      -8.275  28.440  65.503  1.00 36.05           N  
ANISOU 2594  NH2 ARG A 313     5557   4403   3738   -581     56     82       N  
ATOM   2595  N   GLU A 314      -2.042  30.733  63.492  1.00 40.10           N  
ANISOU 2595  N   GLU A 314     5903   5046   4289   -731   -231    212       N  
ATOM   2596  CA  GLU A 314      -1.902  31.517  64.724  1.00 43.76           C  
ANISOU 2596  CA  GLU A 314     6473   5478   4675   -810   -250    207       C  
ATOM   2597  C   GLU A 314      -1.179  32.841  64.514  1.00 42.03           C  
ANISOU 2597  C   GLU A 314     6283   5254   4432   -870   -266    205       C  
ATOM   2598  O   GLU A 314      -1.467  33.815  65.212  1.00 42.39           O  
ANISOU 2598  O   GLU A 314     6435   5255   4416   -920   -248    183       O  
ATOM   2599  CB  GLU A 314      -1.257  30.699  65.861  1.00 47.89           C  
ANISOU 2599  CB  GLU A 314     7010   6019   5169   -854   -321    242       C  
ATOM   2600  CG  GLU A 314       0.277  30.713  65.921  1.00 54.05           C  
ANISOU 2600  CG  GLU A 314     7735   6845   5956   -907   -412    285       C  
ATOM   2601  CD  GLU A 314       0.844  29.510  66.668  1.00 60.53           C  
ANISOU 2601  CD  GLU A 314     8528   7692   6778   -911   -485    327       C  
ATOM   2602  OE1 GLU A 314       1.129  29.635  67.885  1.00 59.47           O  
ANISOU 2602  OE1 GLU A 314     8473   7545   6578   -980   -535    341       O  
ATOM   2603  OE2 GLU A 314       0.990  28.436  66.033  1.00 61.91           O  
ANISOU 2603  OE2 GLU A 314     8609   7897   7019   -846   -492    345       O  
ATOM   2604  N   SER A 315      -0.250  32.877  63.562  1.00 40.36           N  
ANISOU 2604  N   SER A 315     5982   5086   4268   -868   -295    226       N  
ATOM   2605  CA  SER A 315       0.486  34.103  63.277  1.00 41.58           C  
ANISOU 2605  CA  SER A 315     6159   5238   4402   -931   -308    226       C  
ATOM   2606  C   SER A 315      -0.287  35.049  62.356  1.00 41.70           C  
ANISOU 2606  C   SER A 315     6208   5214   4423   -896   -237    192       C  
ATOM   2607  O   SER A 315      -0.222  36.270  62.528  1.00 43.32           O  
ANISOU 2607  O   SER A 315     6495   5382   4583   -948   -226    176       O  
ATOM   2608  CB  SER A 315       1.879  33.807  62.711  1.00 40.94           C  
ANISOU 2608  CB  SER A 315     5969   5222   4365   -954   -368    263       C  
ATOM   2609  OG  SER A 315       1.811  33.159  61.456  1.00 42.83           O  
ANISOU 2609  OG  SER A 315     6107   5490   4676   -878   -339    266       O  
ATOM   2610  N   ASN A 316      -1.014  34.488  61.388  1.00 39.36           N  
ANISOU 2610  N   ASN A 316     5852   4922   4180   -808   -192    181       N  
ATOM   2611  CA  ASN A 316      -1.812  35.291  60.455  1.00 36.24           C  
ANISOU 2611  CA  ASN A 316     5483   4491   3795   -765   -130    151       C  
ATOM   2612  C   ASN A 316      -3.051  34.544  59.993  1.00 34.19           C  
ANISOU 2612  C   ASN A 316     5193   4223   3574   -672    -81    132       C  
ATOM   2613  O   ASN A 316      -3.092  34.017  58.883  1.00 35.75           O  
ANISOU 2613  O   ASN A 316     5311   4447   3823   -619    -71    137       O  
ATOM   2614  CB  ASN A 316      -0.964  35.724  59.251  1.00 35.78           C  
ANISOU 2614  CB  ASN A 316     5368   4461   3767   -776   -140    166       C  
ATOM   2615  CG  ASN A 316      -1.561  36.924  58.494  1.00 39.25           C  
ANISOU 2615  CG  ASN A 316     5869   4850   4193   -760    -91    140       C  
ATOM   2616  OD1 ASN A 316      -2.764  37.200  58.556  1.00 38.17           O  
ANISOU 2616  OD1 ASN A 316     5787   4666   4048   -710    -44    112       O  
ATOM   2617  ND2 ASN A 316      -0.708  37.627  57.758  1.00 39.28           N  
ANISOU 2617  ND2 ASN A 316     5862   4864   4197   -803   -102    152       N  
ATOM   2618  N   HIS A 317      -4.070  34.515  60.844  1.00 33.22           N  
ANISOU 2618  N   HIS A 317     5135   4063   3423   -658    -47    108       N  
ATOM   2619  CA  HIS A 317      -5.310  33.812  60.542  1.00 30.82           C  
ANISOU 2619  CA  HIS A 317     4803   3753   3154   -579      0     87       C  
ATOM   2620  C   HIS A 317      -6.053  34.414  59.350  1.00 32.72           C  
ANISOU 2620  C   HIS A 317     5033   3974   3426   -519     45     66       C  
ATOM   2621  O   HIS A 317      -6.730  33.693  58.598  1.00 32.75           O  
ANISOU 2621  O   HIS A 317     4974   3994   3477   -452     65     61       O  
ATOM   2622  CB  HIS A 317      -6.224  33.779  61.765  1.00 29.50           C  
ANISOU 2622  CB  HIS A 317     4712   3549   2946   -586     34     63       C  
ATOM   2623  CG  HIS A 317      -7.571  33.194  61.487  1.00 30.28           C  
ANISOU 2623  CG  HIS A 317     4784   3641   3081   -511     90     38       C  
ATOM   2624  ND1 HIS A 317      -8.706  33.967  61.372  1.00 29.51           N  
ANISOU 2624  ND1 HIS A 317     4728   3500   2982   -472    151      2       N  
ATOM   2625  CD2 HIS A 317      -7.959  31.916  61.260  1.00 27.34           C  
ANISOU 2625  CD2 HIS A 317     4342   3299   2749   -470     92     45       C  
ATOM   2626  CE1 HIS A 317      -9.740  33.189  61.113  1.00 26.14           C  
ANISOU 2626  CE1 HIS A 317     4253   3084   2596   -412    187    -13       C  
ATOM   2627  NE2 HIS A 317      -9.313  31.940  61.034  1.00 28.43           N  
ANISOU 2627  NE2 HIS A 317     4478   3415   2907   -414    152     12       N  
ATOM   2628  N   GLN A 318      -5.917  35.726  59.183  1.00 32.51           N  
ANISOU 2628  N   GLN A 318     5072   3911   3371   -544     55     56       N  
ATOM   2629  CA  GLN A 318      -6.553  36.453  58.092  1.00 35.22           C  
ANISOU 2629  CA  GLN A 318     5420   4227   3736   -491     89     40       C  
ATOM   2630  C   GLN A 318      -6.115  35.878  56.739  1.00 36.51           C  
ANISOU 2630  C   GLN A 318     5490   4435   3949   -460     71     60       C  
ATOM   2631  O   GLN A 318      -6.945  35.479  55.930  1.00 39.64           O  
ANISOU 2631  O   GLN A 318     5844   4834   4383   -391     94     50       O  
ATOM   2632  CB  GLN A 318      -6.222  37.955  58.193  1.00 34.60           C  
ANISOU 2632  CB  GLN A 318     5437   4099   3611   -538     94     32       C  
ATOM   2633  CG  GLN A 318      -6.636  38.787  56.970  1.00 34.48           C  
ANISOU 2633  CG  GLN A 318     5433   4053   3613   -491    117     24       C  
ATOM   2634  CD  GLN A 318      -8.143  38.852  56.757  1.00 34.39           C  
ANISOU 2634  CD  GLN A 318     5431   4009   3628   -403    165     -5       C  
ATOM   2635  OE1 GLN A 318      -8.916  38.880  57.709  1.00 33.53           O  
ANISOU 2635  OE1 GLN A 318     5363   3872   3504   -391    198    -30       O  
ATOM   2636  NE2 GLN A 318      -8.563  38.878  55.498  1.00 36.89           N  
ANISOU 2636  NE2 GLN A 318     5706   4328   3982   -343    171     -3       N  
ATOM   2637  N   ARG A 319      -4.803  35.821  56.528  1.00 37.81           N  
ANISOU 2637  N   ARG A 319     5621   4634   4110   -514     30     88       N  
ATOM   2638  CA  ARG A 319      -4.203  35.244  55.335  1.00 38.00           C  
ANISOU 2638  CA  ARG A 319     5558   4703   4177   -494     16    107       C  
ATOM   2639  C   ARG A 319      -4.491  33.750  55.179  1.00 36.10           C  
ANISOU 2639  C   ARG A 319     5234   4501   3981   -443     13    113       C  
ATOM   2640  O   ARG A 319      -4.753  33.276  54.069  1.00 34.04           O  
ANISOU 2640  O   ARG A 319     4920   4257   3758   -393     26    112       O  
ATOM   2641  CB  ARG A 319      -2.695  35.489  55.357  1.00 39.99           C  
ANISOU 2641  CB  ARG A 319     5789   4988   4418   -569    -24    135       C  
ATOM   2642  CG  ARG A 319      -1.972  34.997  54.125  1.00 42.77           C  
ANISOU 2642  CG  ARG A 319     6054   5385   4812   -555    -30    152       C  
ATOM   2643  CD  ARG A 319      -0.901  35.970  53.713  1.00 47.92           C  
ANISOU 2643  CD  ARG A 319     6720   6043   5444   -624    -41    165       C  
ATOM   2644  NE  ARG A 319      -1.475  37.250  53.302  1.00 48.94           N  
ANISOU 2644  NE  ARG A 319     6939   6114   5540   -626    -12    148       N  
ATOM   2645  CZ  ARG A 319      -0.754  38.300  52.931  1.00 50.93           C  
ANISOU 2645  CZ  ARG A 319     7232   6354   5766   -688    -14    155       C  
ATOM   2646  NH1 ARG A 319       0.569  38.226  52.912  1.00 50.82           N  
ANISOU 2646  NH1 ARG A 319     7166   6388   5757   -756    -42    177       N  
ATOM   2647  NH2 ARG A 319      -1.359  39.423  52.579  1.00 52.86           N  
ANISOU 2647  NH2 ARG A 319     7567   6538   5980   -682     12    140       N  
ATOM   2648  N   TYR A 320      -4.436  33.024  56.294  1.00 34.85           N  
ANISOU 2648  N   TYR A 320     5074   4354   3814   -460     -5    119       N  
ATOM   2649  CA  TYR A 320      -4.698  31.582  56.333  1.00 33.22           C  
ANISOU 2649  CA  TYR A 320     4803   4177   3643   -419     -9    125       C  
ATOM   2650  C   TYR A 320      -6.025  31.249  55.686  1.00 29.74           C  
ANISOU 2650  C   TYR A 320     4350   3721   3230   -348     33    101       C  
ATOM   2651  O   TYR A 320      -6.097  30.382  54.820  1.00 30.90           O  
ANISOU 2651  O   TYR A 320     4431   3893   3415   -306     35    105       O  
ATOM   2652  CB  TYR A 320      -4.712  31.122  57.783  1.00 35.84           C  
ANISOU 2652  CB  TYR A 320     5169   4503   3945   -451    -28    130       C  
ATOM   2653  CG  TYR A 320      -4.711  29.628  58.036  1.00 35.66           C  
ANISOU 2653  CG  TYR A 320     5092   4508   3950   -426    -44    145       C  
ATOM   2654  CD1 TYR A 320      -3.551  28.876  57.876  1.00 34.54           C  
ANISOU 2654  CD1 TYR A 320     4884   4407   3833   -436    -90    177       C  
ATOM   2655  CD2 TYR A 320      -5.851  28.987  58.523  1.00 36.68           C  
ANISOU 2655  CD2 TYR A 320     5239   4618   4078   -395    -14    127       C  
ATOM   2656  CE1 TYR A 320      -3.531  27.517  58.157  1.00 34.13           C  
ANISOU 2656  CE1 TYR A 320     4793   4372   3805   -411   -108    192       C  
ATOM   2657  CE2 TYR A 320      -5.843  27.627  58.807  1.00 36.49           C  
ANISOU 2657  CE2 TYR A 320     5179   4613   4074   -378    -29    141       C  
ATOM   2658  CZ  TYR A 320      -4.676  26.899  58.621  1.00 36.49           C  
ANISOU 2658  CZ  TYR A 320     5121   4647   4097   -384    -78    175       C  
ATOM   2659  OH  TYR A 320      -4.652  25.555  58.904  1.00 32.87           O  
ANISOU 2659  OH  TYR A 320     4633   4200   3658   -363    -95    191       O  
ATOM   2660  N   ILE A 321      -7.070  31.956  56.100  1.00 30.92           N  
ANISOU 2660  N   ILE A 321     4561   3829   3358   -335     68     74       N  
ATOM   2661  CA  ILE A 321      -8.404  31.764  55.536  1.00 28.63           C  
ANISOU 2661  CA  ILE A 321     4256   3525   3095   -268    106     49       C  
ATOM   2662  C   ILE A 321      -8.454  32.214  54.073  1.00 30.49           C  
ANISOU 2662  C   ILE A 321     4468   3763   3355   -233    109     49       C  
ATOM   2663  O   ILE A 321      -8.987  31.496  53.225  1.00 29.70           O  
ANISOU 2663  O   ILE A 321     4315   3680   3291   -185    116     45       O  
ATOM   2664  CB  ILE A 321      -9.505  32.462  56.374  1.00 28.50           C  
ANISOU 2664  CB  ILE A 321     4307   3465   3056   -259    147     19       C  
ATOM   2665  CG1 ILE A 321      -9.589  31.859  57.786  1.00 29.75           C  
ANISOU 2665  CG1 ILE A 321     4492   3622   3188   -293    150     17       C  
ATOM   2666  CG2 ILE A 321     -10.884  32.385  55.672  1.00 27.05           C  
ANISOU 2666  CG2 ILE A 321     4096   3272   2909   -187    183     -5       C  
ATOM   2667  CD1 ILE A 321      -9.832  30.328  57.849  1.00 31.02           C  
ANISOU 2667  CD1 ILE A 321     4591   3817   3379   -274    145     25       C  
ATOM   2668  N   SER A 322      -7.881  33.381  53.777  1.00 29.14           N  
ANISOU 2668  N   SER A 322     4341   3571   3158   -262    103     54       N  
ATOM   2669  CA  SER A 322      -7.904  33.912  52.414  1.00 32.30           C  
ANISOU 2669  CA  SER A 322     4735   3966   3571   -235    106     56       C  
ATOM   2670  C   SER A 322      -7.218  32.984  51.414  1.00 33.44           C  
ANISOU 2670  C   SER A 322     4803   4157   3746   -228     89     75       C  
ATOM   2671  O   SER A 322      -7.712  32.785  50.308  1.00 34.92           O  
ANISOU 2671  O   SER A 322     4966   4348   3955   -183     97     70       O  
ATOM   2672  CB  SER A 322      -7.270  35.308  52.356  1.00 33.58           C  
ANISOU 2672  CB  SER A 322     4967   4096   3695   -281    102     61       C  
ATOM   2673  OG  SER A 322      -8.127  36.288  52.919  1.00 32.52           O  
ANISOU 2673  OG  SER A 322     4910   3907   3538   -267    126     39       O  
ATOM   2674  N   TYR A 323      -6.086  32.409  51.815  1.00 36.53           N  
ANISOU 2674  N   TYR A 323     5160   4583   4138   -271     66     95       N  
ATOM   2675  CA  TYR A 323      -5.349  31.496  50.952  1.00 36.96           C  
ANISOU 2675  CA  TYR A 323     5141   4680   4224   -262     55    111       C  
ATOM   2676  C   TYR A 323      -6.117  30.205  50.749  1.00 35.25           C  
ANISOU 2676  C   TYR A 323     4875   4477   4040   -208     63    103       C  
ATOM   2677  O   TYR A 323      -6.006  29.584  49.696  1.00 37.67           O  
ANISOU 2677  O   TYR A 323     5137   4803   4371   -181     68    105       O  
ATOM   2678  CB  TYR A 323      -3.934  31.249  51.490  1.00 38.29           C  
ANISOU 2678  CB  TYR A 323     5277   4881   4390   -317     26    136       C  
ATOM   2679  CG  TYR A 323      -2.963  32.382  51.170  1.00 43.73           C  
ANISOU 2679  CG  TYR A 323     5991   5570   5056   -373     19    147       C  
ATOM   2680  CD1 TYR A 323      -1.614  32.299  51.528  1.00 43.18           C  
ANISOU 2680  CD1 TYR A 323     5882   5535   4987   -429    -10    170       C  
ATOM   2681  CD2 TYR A 323      -3.392  33.533  50.489  1.00 46.28           C  
ANISOU 2681  CD2 TYR A 323     6373   5856   5356   -372     40    136       C  
ATOM   2682  CE1 TYR A 323      -0.722  33.334  51.229  1.00 44.56           C  
ANISOU 2682  CE1 TYR A 323     6076   5713   5141   -489    -14    180       C  
ATOM   2683  CE2 TYR A 323      -2.510  34.571  50.185  1.00 46.58           C  
ANISOU 2683  CE2 TYR A 323     6440   5889   5368   -431     36    146       C  
ATOM   2684  CZ  TYR A 323      -1.179  34.463  50.555  1.00 48.49           C  
ANISOU 2684  CZ  TYR A 323     6641   6170   5611   -492     11    167       C  
ATOM   2685  OH  TYR A 323      -0.308  35.488  50.256  1.00 53.94           O  
ANISOU 2685  OH  TYR A 323     7359   6859   6277   -558     10    176       O  
ATOM   2686  N   ASN A 324      -6.907  29.819  51.749  1.00 34.02           N  
ANISOU 2686  N   ASN A 324     4736   4309   3882   -198     69     91       N  
ATOM   2687  CA  ASN A 324      -7.773  28.646  51.642  1.00 32.59           C  
ANISOU 2687  CA  ASN A 324     4518   4137   3730   -154     80     81       C  
ATOM   2688  C   ASN A 324      -8.881  28.890  50.622  1.00 31.42           C  
ANISOU 2688  C   ASN A 324     4368   3974   3595   -106    100     61       C  
ATOM   2689  O   ASN A 324      -9.172  28.016  49.818  1.00 31.61           O  
ANISOU 2689  O   ASN A 324     4350   4016   3645    -74    102     58       O  
ATOM   2690  CB  ASN A 324      -8.358  28.252  53.009  1.00 32.58           C  
ANISOU 2690  CB  ASN A 324     4540   4124   3717   -164     86     73       C  
ATOM   2691  CG  ASN A 324      -9.281  27.033  52.933  1.00 34.89           C  
ANISOU 2691  CG  ASN A 324     4798   4424   4037   -127    100     61       C  
ATOM   2692  OD1 ASN A 324     -10.462  27.121  53.261  1.00 36.99           O  
ANISOU 2692  OD1 ASN A 324     5079   4673   4303   -109    126     39       O  
ATOM   2693  ND2 ASN A 324      -8.744  25.895  52.495  1.00 34.91           N  
ANISOU 2693  ND2 ASN A 324     4752   4451   4063   -117     85     76       N  
ATOM   2694  N   ILE A 325      -9.484  30.081  50.650  1.00 30.24           N  
ANISOU 2694  N   ILE A 325     4269   3794   3429    -99    113     48       N  
ATOM   2695  CA  ILE A 325     -10.492  30.452  49.655  1.00 31.40           C  
ANISOU 2695  CA  ILE A 325     4416   3925   3588    -51    123     33       C  
ATOM   2696  C   ILE A 325      -9.872  30.508  48.246  1.00 32.14           C  
ANISOU 2696  C   ILE A 325     4495   4032   3685    -47    111     46       C  
ATOM   2697  O   ILE A 325     -10.444  29.984  47.287  1.00 31.65           O  
ANISOU 2697  O   ILE A 325     4404   3980   3642    -11    109     40       O  
ATOM   2698  CB  ILE A 325     -11.172  31.806  49.988  1.00 31.87           C  
ANISOU 2698  CB  ILE A 325     4538   3941   3629    -40    138     18       C  
ATOM   2699  CG1 ILE A 325     -11.891  31.742  51.342  1.00 30.64           C  
ANISOU 2699  CG1 ILE A 325     4400   3772   3470    -42    161      0       C  
ATOM   2700  CG2 ILE A 325     -12.141  32.221  48.878  1.00 28.45           C  
ANISOU 2700  CG2 ILE A 325     4103   3494   3212     14    138      9       C  
ATOM   2701  CD1 ILE A 325     -12.234  33.123  51.936  1.00 23.00           C  
ANISOU 2701  CD1 ILE A 325     3507   2756   2476    -44    180    -13       C  
ATOM   2702  N   ILE A 326      -8.697  31.131  48.137  1.00 32.30           N  
ANISOU 2702  N   ILE A 326     4536   4054   3683    -90    103     63       N  
ATOM   2703  CA  ILE A 326      -8.025  31.309  46.846  1.00 31.30           C  
ANISOU 2703  CA  ILE A 326     4402   3937   3552    -95     99     75       C  
ATOM   2704  C   ILE A 326      -7.629  29.978  46.202  1.00 31.35           C  
ANISOU 2704  C   ILE A 326     4346   3982   3585    -83     99     79       C  
ATOM   2705  O   ILE A 326      -7.765  29.808  44.983  1.00 32.10           O  
ANISOU 2705  O   ILE A 326     4434   4081   3683    -62    102     78       O  
ATOM   2706  CB  ILE A 326      -6.805  32.256  46.969  1.00 32.99           C  
ANISOU 2706  CB  ILE A 326     4649   4147   3738   -154     95     91       C  
ATOM   2707  CG1 ILE A 326      -7.289  33.691  47.234  1.00 31.25           C  
ANISOU 2707  CG1 ILE A 326     4509   3878   3488   -159     98     84       C  
ATOM   2708  CG2 ILE A 326      -5.933  32.204  45.696  1.00 32.03           C  
ANISOU 2708  CG2 ILE A 326     4509   4047   3616   -168     99    104       C  
ATOM   2709  CD1 ILE A 326      -6.209  34.658  47.685  1.00 30.41           C  
ANISOU 2709  CD1 ILE A 326     4445   3761   3348   -227     94     97       C  
ATOM   2710  N   ALA A 327      -7.159  29.036  47.022  1.00 29.44           N  
ANISOU 2710  N   ALA A 327     4064   3763   3359    -95     94     85       N  
ATOM   2711  CA  ALA A 327      -6.823  27.698  46.544  1.00 29.49           C  
ANISOU 2711  CA  ALA A 327     4014   3797   3392    -78     96     88       C  
ATOM   2712  C   ALA A 327      -8.006  27.042  45.827  1.00 29.53           C  
ANISOU 2712  C   ALA A 327     4011   3797   3412    -32    102     70       C  
ATOM   2713  O   ALA A 327      -7.842  26.429  44.767  1.00 29.91           O  
ANISOU 2713  O   ALA A 327     4037   3857   3468    -17    108     69       O  
ATOM   2714  CB  ALA A 327      -6.336  26.824  47.690  1.00 28.91           C  
ANISOU 2714  CB  ALA A 327     3911   3740   3333    -91     84     99       C  
ATOM   2715  N   VAL A 328      -9.198  27.193  46.389  1.00 29.76           N  
ANISOU 2715  N   VAL A 328     4056   3808   3443    -13    103     56       N  
ATOM   2716  CA  VAL A 328     -10.396  26.615  45.784  1.00 30.88           C  
ANISOU 2716  CA  VAL A 328     4184   3949   3601     26    105     38       C  
ATOM   2717  C   VAL A 328     -10.674  27.271  44.436  1.00 30.41           C  
ANISOU 2717  C   VAL A 328     4144   3880   3529     43     99     36       C  
ATOM   2718  O   VAL A 328     -10.866  26.589  43.439  1.00 28.07           O  
ANISOU 2718  O   VAL A 328     3831   3594   3239     59     96     31       O  
ATOM   2719  CB  VAL A 328     -11.620  26.709  46.728  1.00 32.23           C  
ANISOU 2719  CB  VAL A 328     4360   4106   3780     40    111     22       C  
ATOM   2720  CG1 VAL A 328     -12.900  26.288  46.015  1.00 30.46           C  
ANISOU 2720  CG1 VAL A 328     4115   3884   3575     77    109      4       C  
ATOM   2721  CG2 VAL A 328     -11.395  25.826  47.952  1.00 33.48           C  
ANISOU 2721  CG2 VAL A 328     4504   4273   3945     20    117     24       C  
ATOM   2722  N   TYR A 329     -10.666  28.599  44.417  1.00 31.03           N  
ANISOU 2722  N   TYR A 329     4267   3936   3587     38     96     40       N  
ATOM   2723  CA  TYR A 329     -10.905  29.356  43.196  1.00 31.06           C  
ANISOU 2723  CA  TYR A 329     4303   3923   3573     53     87     42       C  
ATOM   2724  C   TYR A 329      -9.914  29.004  42.092  1.00 32.12           C  
ANISOU 2724  C   TYR A 329     4433   4075   3695     34     91     53       C  
ATOM   2725  O   TYR A 329     -10.278  28.955  40.919  1.00 34.48           O  
ANISOU 2725  O   TYR A 329     4746   4371   3985     51     83     50       O  
ATOM   2726  CB  TYR A 329     -10.852  30.857  43.487  1.00 30.69           C  
ANISOU 2726  CB  TYR A 329     4315   3843   3503     43     85     48       C  
ATOM   2727  CG  TYR A 329     -11.228  31.728  42.309  1.00 30.39           C  
ANISOU 2727  CG  TYR A 329     4323   3780   3444     63     71     52       C  
ATOM   2728  CD1 TYR A 329     -12.301  31.396  41.477  1.00 29.94           C  
ANISOU 2728  CD1 TYR A 329     4254   3723   3400    107     52     44       C  
ATOM   2729  CD2 TYR A 329     -10.520  32.890  42.035  1.00 32.26           C  
ANISOU 2729  CD2 TYR A 329     4620   3991   3648     34     73     66       C  
ATOM   2730  CE1 TYR A 329     -12.651  32.203  40.396  1.00 32.65           C  
ANISOU 2730  CE1 TYR A 329     4644   4040   3720    126     31     52       C  
ATOM   2731  CE2 TYR A 329     -10.860  33.703  40.958  1.00 36.24           C  
ANISOU 2731  CE2 TYR A 329     5175   4466   4127     51     57     74       C  
ATOM   2732  CZ  TYR A 329     -11.926  33.357  40.147  1.00 32.20           C  
ANISOU 2732  CZ  TYR A 329     4653   3954   3628     99     34     67       C  
ATOM   2733  OH  TYR A 329     -12.251  34.166  39.081  1.00 35.44           O  
ANISOU 2733  OH  TYR A 329     5121   4333   4011    116     11     78       O  
ATOM   2734  N   ARG A 330      -8.665  28.757  42.468  1.00 32.10           N  
ANISOU 2734  N   ARG A 330     4412   4091   3692     -2    104     64       N  
ATOM   2735  CA  ARG A 330      -7.637  28.456  41.483  1.00 32.61           C  
ANISOU 2735  CA  ARG A 330     4467   4173   3749    -21    119     72       C  
ATOM   2736  C   ARG A 330      -7.916  27.189  40.686  1.00 31.48           C  
ANISOU 2736  C   ARG A 330     4295   4046   3621      5    124     61       C  
ATOM   2737  O   ARG A 330      -7.705  27.161  39.477  1.00 33.74           O  
ANISOU 2737  O   ARG A 330     4597   4333   3889      4    133     60       O  
ATOM   2738  CB  ARG A 330      -6.244  28.483  42.116  1.00 33.53           C  
ANISOU 2738  CB  ARG A 330     4559   4311   3870    -62    130     87       C  
ATOM   2739  CG  ARG A 330      -5.772  29.912  42.306  1.00 38.76           C  
ANISOU 2739  CG  ARG A 330     5268   4955   4503   -101    128     98       C  
ATOM   2740  CD  ARG A 330      -4.408  30.003  42.931  1.00 48.37           C  
ANISOU 2740  CD  ARG A 330     6456   6197   5724   -150    133    113       C  
ATOM   2741  NE  ARG A 330      -3.956  31.394  42.968  1.00 53.70           N  
ANISOU 2741  NE  ARG A 330     7185   6853   6367   -196    133    123       N  
ATOM   2742  CZ  ARG A 330      -2.708  31.778  43.230  1.00 56.82           C  
ANISOU 2742  CZ  ARG A 330     7564   7268   6757   -251    137    137       C  
ATOM   2743  NH1 ARG A 330      -1.756  30.878  43.468  1.00 54.16           N  
ANISOU 2743  NH1 ARG A 330     7154   6974   6451   -262    141    145       N  
ATOM   2744  NH2 ARG A 330      -2.408  33.072  43.236  1.00 56.90           N  
ANISOU 2744  NH2 ARG A 330     7633   7255   6733   -297    137    144       N  
ATOM   2745  N   VAL A 331      -8.438  26.161  41.346  1.00 29.72           N  
ANISOU 2745  N   VAL A 331     4036   3831   3425     25    120     52       N  
ATOM   2746  CA  VAL A 331      -8.883  24.958  40.643  1.00 29.86           C  
ANISOU 2746  CA  VAL A 331     4034   3856   3454     48    123     39       C  
ATOM   2747  C   VAL A 331     -10.020  25.271  39.657  1.00 30.39           C  
ANISOU 2747  C   VAL A 331     4131   3909   3505     68    105     28       C  
ATOM   2748  O   VAL A 331     -10.011  24.791  38.527  1.00 31.65           O  
ANISOU 2748  O   VAL A 331     4302   4071   3653     72    108     22       O  
ATOM   2749  CB  VAL A 331      -9.319  23.842  41.614  1.00 31.22           C  
ANISOU 2749  CB  VAL A 331     4170   4034   3656     59    121     32       C  
ATOM   2750  CG1 VAL A 331      -9.510  22.546  40.864  1.00 29.64           C  
ANISOU 2750  CG1 VAL A 331     3956   3840   3466     75    128     19       C  
ATOM   2751  CG2 VAL A 331      -8.290  23.656  42.723  1.00 32.20           C  
ANISOU 2751  CG2 VAL A 331     4270   4169   3793     40    127     47       C  
ATOM   2752  N   LEU A 332     -10.987  26.082  40.081  1.00 30.58           N  
ANISOU 2752  N   LEU A 332     4171   3917   3530     83     85     26       N  
ATOM   2753  CA  LEU A 332     -12.079  26.497  39.200  1.00 29.83           C  
ANISOU 2753  CA  LEU A 332     4101   3810   3424    107     59     20       C  
ATOM   2754  C   LEU A 332     -11.550  27.236  37.975  1.00 32.05           C  
ANISOU 2754  C   LEU A 332     4432   4078   3666     96     56     31       C  
ATOM   2755  O   LEU A 332     -12.057  27.046  36.871  1.00 34.61           O  
ANISOU 2755  O   LEU A 332     4776   4400   3974    107     38     27       O  
ATOM   2756  CB  LEU A 332     -13.063  27.400  39.946  1.00 29.07           C  
ANISOU 2756  CB  LEU A 332     4012   3696   3339    129     43     17       C  
ATOM   2757  CG  LEU A 332     -13.915  26.786  41.056  1.00 31.97           C  
ANISOU 2757  CG  LEU A 332     4334   4072   3739    142     47      2       C  
ATOM   2758  CD1 LEU A 332     -14.640  27.893  41.810  1.00 31.07           C  
ANISOU 2758  CD1 LEU A 332     4235   3937   3632    162     44     -1       C  
ATOM   2759  CD2 LEU A 332     -14.903  25.754  40.487  1.00 30.00           C  
ANISOU 2759  CD2 LEU A 332     4052   3837   3507    159     31    -13       C  
ATOM   2760  N   GLN A 333     -10.531  28.074  38.184  1.00 30.68           N  
ANISOU 2760  N   GLN A 333     4284   3899   3476     68     73     45       N  
ATOM   2761  CA  GLN A 333      -9.917  28.853  37.113  1.00 32.08           C  
ANISOU 2761  CA  GLN A 333     4514   4063   3612     47     78     57       C  
ATOM   2762  C   GLN A 333      -9.150  27.958  36.141  1.00 32.24           C  
ANISOU 2762  C   GLN A 333     4527   4103   3621     31    104     53       C  
ATOM   2763  O   GLN A 333      -9.200  28.156  34.928  1.00 34.05           O  
ANISOU 2763  O   GLN A 333     4801   4321   3815     26    101     55       O  
ATOM   2764  CB  GLN A 333      -8.974  29.903  37.691  1.00 31.54           C  
ANISOU 2764  CB  GLN A 333     4468   3984   3530     13     94     72       C  
ATOM   2765  CG  GLN A 333      -9.663  31.094  38.305  1.00 32.49           C  
ANISOU 2765  CG  GLN A 333     4626   4072   3646     27     73     76       C  
ATOM   2766  CD  GLN A 333      -8.670  32.086  38.891  1.00 38.11           C  
ANISOU 2766  CD  GLN A 333     5367   4772   4340    -17     89     89       C  
ATOM   2767  OE1 GLN A 333      -8.570  33.221  38.427  1.00 38.22           O  
ANISOU 2767  OE1 GLN A 333     5447   4754   4320    -31     84    100       O  
ATOM   2768  NE2 GLN A 333      -7.925  31.658  39.910  1.00 36.65           N  
ANISOU 2768  NE2 GLN A 333     5139   4612   4176    -42    105     89       N  
ATOM   2769  N   ILE A 334      -8.438  26.977  36.682  1.00 30.98           N  
ANISOU 2769  N   ILE A 334     4314   3968   3489     23    130     48       N  
ATOM   2770  CA  ILE A 334      -7.780  25.976  35.857  1.00 32.88           C  
ANISOU 2770  CA  ILE A 334     4542   4224   3726     17    160     40       C  
ATOM   2771  C   ILE A 334      -8.826  25.236  35.012  1.00 33.92           C  
ANISOU 2771  C   ILE A 334     4690   4349   3850     40    140     24       C  
ATOM   2772  O   ILE A 334      -8.632  25.039  33.812  1.00 33.50           O  
ANISOU 2772  O   ILE A 334     4673   4293   3765     31    153     19       O  
ATOM   2773  CB  ILE A 334      -6.924  25.007  36.717  1.00 31.72           C  
ANISOU 2773  CB  ILE A 334     4332   4102   3620     15    185     39       C  
ATOM   2774  CG1 ILE A 334      -5.727  25.762  37.324  1.00 28.79           C  
ANISOU 2774  CG1 ILE A 334     3946   3743   3252    -18    202     56       C  
ATOM   2775  CG2 ILE A 334      -6.474  23.796  35.897  1.00 29.29           C  
ANISOU 2775  CG2 ILE A 334     4011   3804   3315     22    216     26       C  
ATOM   2776  CD1 ILE A 334      -4.992  24.992  38.419  1.00 27.72           C  
ANISOU 2776  CD1 ILE A 334     3746   3629   3157    -17    210     61       C  
ATOM   2777  N   ASP A 335      -9.941  24.854  35.635  1.00 34.21           N  
ANISOU 2777  N   ASP A 335     4703   4384   3911     65    110     16       N  
ATOM   2778  CA  ASP A 335     -11.022  24.215  34.897  1.00 34.15           C  
ANISOU 2778  CA  ASP A 335     4706   4372   3896     82     84      2       C  
ATOM   2779  C   ASP A 335     -11.696  25.104  33.847  1.00 33.32           C  
ANISOU 2779  C   ASP A 335     4657   4250   3752     86     49      7       C  
ATOM   2780  O   ASP A 335     -11.996  24.635  32.755  1.00 33.13           O  
ANISOU 2780  O   ASP A 335     4664   4224   3702     82     38     -1       O  
ATOM   2781  CB  ASP A 335     -12.085  23.605  35.807  1.00 33.06           C  
ANISOU 2781  CB  ASP A 335     4524   4240   3796    102     62     -9       C  
ATOM   2782  CG  ASP A 335     -12.937  22.583  35.063  1.00 36.77           C  
ANISOU 2782  CG  ASP A 335     4996   4714   4263    107     44    -27       C  
ATOM   2783  OD1 ASP A 335     -12.355  21.606  34.534  1.00 35.64           O  
ANISOU 2783  OD1 ASP A 335     4859   4572   4112     96     70    -37       O  
ATOM   2784  OD2 ASP A 335     -14.167  22.771  34.964  1.00 34.31           O  
ANISOU 2784  OD2 ASP A 335     4679   4401   3957    122      4    -32       O  
ATOM   2785  N   ALA A 336     -11.943  26.369  34.178  1.00 30.23           N  
ANISOU 2785  N   ALA A 336     4286   3843   3356     93     29     22       N  
ATOM   2786  CA  ALA A 336     -12.487  27.324  33.206  1.00 30.62           C  
ANISOU 2786  CA  ALA A 336     4397   3870   3367    100     -8     33       C  
ATOM   2787  C   ALA A 336     -11.681  27.316  31.911  1.00 31.15           C  
ANISOU 2787  C   ALA A 336     4522   3931   3383     69     13     37       C  
ATOM   2788  O   ALA A 336     -12.233  27.489  30.823  1.00 30.49           O  
ANISOU 2788  O   ALA A 336     4489   3833   3261     72    -20     39       O  
ATOM   2789  CB  ALA A 336     -12.517  28.723  33.793  1.00 31.66           C  
ANISOU 2789  CB  ALA A 336     4553   3979   3499    108    -18     49       C  
ATOM   2790  N   LYS A 337     -10.375  27.095  32.051  1.00 32.17           N  
ANISOU 2790  N   LYS A 337     4641   4072   3511     40     67     37       N  
ATOM   2791  CA  LYS A 337      -9.440  27.066  30.938  1.00 29.91           C  
ANISOU 2791  CA  LYS A 337     4401   3784   3179      7    104     38       C  
ATOM   2792  C   LYS A 337      -9.359  25.688  30.260  1.00 31.52           C  
ANISOU 2792  C   LYS A 337     4596   4001   3380      6    126     16       C  
ATOM   2793  O   LYS A 337      -9.528  25.580  29.034  1.00 31.24           O  
ANISOU 2793  O   LYS A 337     4620   3954   3296     -7    121     12       O  
ATOM   2794  CB  LYS A 337      -8.058  27.512  31.427  1.00 29.31           C  
ANISOU 2794  CB  LYS A 337     4308   3718   3110    -25    155     47       C  
ATOM   2795  CG  LYS A 337      -6.968  27.391  30.389  1.00 30.70           C  
ANISOU 2795  CG  LYS A 337     4516   3899   3248    -62    208     45       C  
ATOM   2796  CD  LYS A 337      -5.601  27.698  30.974  1.00 35.38           C  
ANISOU 2796  CD  LYS A 337     5070   4512   3859    -93    257     52       C  
ATOM   2797  CE  LYS A 337      -4.535  27.632  29.873  1.00 39.31           C  
ANISOU 2797  CE  LYS A 337     5599   5017   4321   -132    318     48       C  
ATOM   2798  NZ  LYS A 337      -3.163  27.370  30.413  1.00 42.60           N  
ANISOU 2798  NZ  LYS A 337     5944   5467   4774   -153    374     48       N  
ATOM   2799  N   ARG A 338      -9.096  24.645  31.053  1.00 28.52           N  
ANISOU 2799  N   ARG A 338     4149   3640   3046     17    150      3       N  
ATOM   2800  CA  ARG A 338      -8.839  23.309  30.525  1.00 26.82           C  
ANISOU 2800  CA  ARG A 338     3926   3432   2831     17    181    -18       C  
ATOM   2801  C   ARG A 338     -10.102  22.536  30.194  1.00 28.74           C  
ANISOU 2801  C   ARG A 338     4178   3669   3072     32    138    -33       C  
ATOM   2802  O   ARG A 338     -10.108  21.722  29.256  1.00 30.73           O  
ANISOU 2802  O   ARG A 338     4464   3915   3296     23    151    -50       O  
ATOM   2803  CB  ARG A 338      -7.969  22.486  31.488  1.00 27.42           C  
ANISOU 2803  CB  ARG A 338     3934   3527   2958     25    222    -23       C  
ATOM   2804  CG  ARG A 338      -6.493  22.899  31.559  1.00 25.66           C  
ANISOU 2804  CG  ARG A 338     3694   3318   2739      4    276    -13       C  
ATOM   2805  CD  ARG A 338      -5.722  22.624  30.256  1.00 24.64           C  
ANISOU 2805  CD  ARG A 338     3605   3186   2570    -17    329    -25       C  
ATOM   2806  NE  ARG A 338      -4.281  22.669  30.491  1.00 26.51           N  
ANISOU 2806  NE  ARG A 338     3798   3444   2829    -31    387    -20       N  
ATOM   2807  CZ  ARG A 338      -3.366  21.973  29.816  1.00 28.53           C  
ANISOU 2807  CZ  ARG A 338     4049   3708   3084    -34    451    -36       C  
ATOM   2808  NH1 ARG A 338      -3.714  21.146  28.834  1.00 27.39           N  
ANISOU 2808  NH1 ARG A 338     3950   3547   2910    -27    468    -59       N  
ATOM   2809  NH2 ARG A 338      -2.083  22.095  30.142  1.00 29.16           N  
ANISOU 2809  NH2 ARG A 338     4074   3813   3193    -45    499    -29       N  
ATOM   2810  N   GLN A 339     -11.153  22.774  30.972  1.00 27.48           N  
ANISOU 2810  N   GLN A 339     3989   3512   2942     53     89    -29       N  
ATOM   2811  CA  GLN A 339     -12.478  22.162  30.763  1.00 28.94           C  
ANISOU 2811  CA  GLN A 339     4169   3695   3130     65     41    -41       C  
ATOM   2812  C   GLN A 339     -12.507  20.624  30.915  1.00 29.87           C  
ANISOU 2812  C   GLN A 339     4260   3819   3269     63     62    -64       C  
ATOM   2813  O   GLN A 339     -13.208  19.930  30.176  1.00 30.54           O  
ANISOU 2813  O   GLN A 339     4370   3900   3335     55     39    -80       O  
ATOM   2814  CB  GLN A 339     -13.081  22.642  29.431  1.00 27.52           C  
ANISOU 2814  CB  GLN A 339     4058   3502   2896     55     -1    -38       C  
ATOM   2815  CG  GLN A 339     -13.028  24.175  29.314  1.00 32.62           C  
ANISOU 2815  CG  GLN A 339     4740   4135   3520     59    -22    -13       C  
ATOM   2816  CD  GLN A 339     -13.673  24.764  28.057  1.00 36.94           C  
ANISOU 2816  CD  GLN A 339     5360   4663   4011     54    -74     -4       C  
ATOM   2817  OE1 GLN A 339     -13.530  25.958  27.794  1.00 41.91           O  
ANISOU 2817  OE1 GLN A 339     6036   5275   4614     54    -88     18       O  
ATOM   2818  NE2 GLN A 339     -14.384  23.947  27.293  1.00 36.97           N  
ANISOU 2818  NE2 GLN A 339     5382   4670   3996     47   -106    -18       N  
ATOM   2819  N   PHE A 340     -11.771  20.108  31.904  1.00 31.09           N  
ANISOU 2819  N   PHE A 340     4126   3753   3935     -5    131   -194       N  
ATOM   2820  CA  PHE A 340     -11.702  18.661  32.136  1.00 30.33           C  
ANISOU 2820  CA  PHE A 340     3996   3675   3852      3    135   -203       C  
ATOM   2821  C   PHE A 340     -12.982  18.077  32.736  1.00 32.35           C  
ANISOU 2821  C   PHE A 340     4248   3956   4086     33     99   -191       C  
ATOM   2822  O   PHE A 340     -13.320  16.916  32.460  1.00 34.74           O  
ANISOU 2822  O   PHE A 340     4544   4272   4382     35    103   -191       O  
ATOM   2823  CB  PHE A 340     -10.473  18.254  32.978  1.00 30.06           C  
ANISOU 2823  CB  PHE A 340     3911   3637   3872      4    140   -226       C  
ATOM   2824  CG  PHE A 340      -9.134  18.566  32.333  1.00 30.07           C  
ANISOU 2824  CG  PHE A 340     3902   3613   3909    -29    185   -248       C  
ATOM   2825  CD1 PHE A 340      -8.975  18.565  30.946  1.00 28.96           C  
ANISOU 2825  CD1 PHE A 340     3795   3460   3747    -62    233   -249       C  
ATOM   2826  CD2 PHE A 340      -8.026  18.844  33.124  1.00 31.62           C  
ANISOU 2826  CD2 PHE A 340     4057   3796   4162    -28    181   -272       C  
ATOM   2827  CE1 PHE A 340      -7.744  18.864  30.367  1.00 29.85           C  
ANISOU 2827  CE1 PHE A 340     3899   3548   3895    -97    285   -273       C  
ATOM   2828  CE2 PHE A 340      -6.784  19.142  32.556  1.00 30.29           C  
ANISOU 2828  CE2 PHE A 340     3870   3601   4037    -60    227   -300       C  
ATOM   2829  CZ  PHE A 340      -6.641  19.141  31.172  1.00 31.86           C  
ANISOU 2829  CZ  PHE A 340     4102   3789   4216    -97    285   -301       C  
ATOM   2830  N   ILE A 341     -13.682  18.853  33.563  1.00 30.49           N  
ANISOU 2830  N   ILE A 341     4014   3725   3844     53     66   -185       N  
ATOM   2831  CA  ILE A 341     -14.977  18.405  34.098  1.00 31.62           C  
ANISOU 2831  CA  ILE A 341     4154   3889   3971     77     40   -179       C  
ATOM   2832  C   ILE A 341     -15.973  18.190  32.941  1.00 30.23           C  
ANISOU 2832  C   ILE A 341     4007   3715   3766     74     38   -170       C  
ATOM   2833  O   ILE A 341     -16.619  17.144  32.850  1.00 29.98           O  
ANISOU 2833  O   ILE A 341     3966   3697   3727     80     36   -170       O  
ATOM   2834  CB  ILE A 341     -15.585  19.394  35.143  1.00 31.57           C  
ANISOU 2834  CB  ILE A 341     4146   3885   3965     97     12   -179       C  
ATOM   2835  CG1 ILE A 341     -14.577  19.779  36.241  1.00 34.19           C  
ANISOU 2835  CG1 ILE A 341     4458   4210   4322    100      7   -189       C  
ATOM   2836  CG2 ILE A 341     -16.856  18.822  35.748  1.00 31.62           C  
ANISOU 2836  CG2 ILE A 341     4142   3911   3960    116     -3   -181       C  
ATOM   2837  CD1 ILE A 341     -14.008  18.638  37.032  1.00 34.29           C  
ANISOU 2837  CD1 ILE A 341     4446   4231   4351    104      7   -196       C  
ATOM   2838  N   ASN A 342     -16.078  19.194  32.073  1.00 29.59           N  
ANISOU 2838  N   ASN A 342     3964   3612   3666     65     34   -162       N  
ATOM   2839  CA  ASN A 342     -16.848  19.125  30.822  1.00 31.85           C  
ANISOU 2839  CA  ASN A 342     4291   3889   3920     60     25   -154       C  
ATOM   2840  C   ASN A 342     -16.512  17.887  29.987  1.00 29.39           C  
ANISOU 2840  C   ASN A 342     3983   3583   3600     43     54   -156       C  
ATOM   2841  O   ASN A 342     -17.396  17.145  29.580  1.00 30.00           O  
ANISOU 2841  O   ASN A 342     4065   3669   3665     51     40   -155       O  
ATOM   2842  CB  ASN A 342     -16.603  20.402  30.003  1.00 32.97           C  
ANISOU 2842  CB  ASN A 342     4486   3999   4042     45     22   -145       C  
ATOM   2843  CG  ASN A 342     -17.386  20.431  28.695  1.00 37.54           C  
ANISOU 2843  CG  ASN A 342     5122   4560   4582     40      3   -135       C  
ATOM   2844  OD1 ASN A 342     -18.595  20.683  28.687  1.00 36.05           O  
ANISOU 2844  OD1 ASN A 342     4940   4370   4388     65    -43   -135       O  
ATOM   2845  ND2 ASN A 342     -16.688  20.199  27.577  1.00 32.82           N  
ANISOU 2845  ND2 ASN A 342     4567   3945   3959      9     38   -131       N  
ATOM   2846  N   LEU A 343     -15.222  17.666  29.755  1.00 29.84           N  
ANISOU 2846  N   LEU A 343     4035   3632   3670     19     95   -163       N  
ATOM   2847  CA  LEU A 343     -14.756  16.493  29.035  1.00 28.60           C  
ANISOU 2847  CA  LEU A 343     3876   3479   3512      1    127   -170       C  
ATOM   2848  C   LEU A 343     -15.238  15.203  29.691  1.00 29.33           C  
ANISOU 2848  C   LEU A 343     3927   3597   3620     21    115   -175       C  
ATOM   2849  O   LEU A 343     -15.769  14.316  29.016  1.00 32.66           O  
ANISOU 2849  O   LEU A 343     4359   4025   4025     20    115   -175       O  
ATOM   2850  CB  LEU A 343     -13.235  16.503  28.938  1.00 27.08           C  
ANISOU 2850  CB  LEU A 343     3668   3274   3349    -25    174   -186       C  
ATOM   2851  CG  LEU A 343     -12.591  15.205  28.426  1.00 26.69           C  
ANISOU 2851  CG  LEU A 343     3600   3229   3314    -40    210   -203       C  
ATOM   2852  CD1 LEU A 343     -12.865  14.952  26.911  1.00 23.36           C  
ANISOU 2852  CD1 LEU A 343     3233   2794   2847    -64    234   -199       C  
ATOM   2853  CD2 LEU A 343     -11.112  15.254  28.739  1.00 21.27           C  
ANISOU 2853  CD2 LEU A 343     2875   2529   2676    -58    245   -227       C  
ATOM   2854  N   SER A 344     -15.060  15.120  31.004  1.00 28.88           N  
ANISOU 2854  N   SER A 344     3831   3552   3591     37    102   -179       N  
ATOM   2855  CA  SER A 344     -15.460  13.960  31.794  1.00 29.48           C  
ANISOU 2855  CA  SER A 344     3874   3647   3678     53     91   -183       C  
ATOM   2856  C   SER A 344     -16.940  13.675  31.674  1.00 28.59           C  
ANISOU 2856  C   SER A 344     3771   3548   3545     67     68   -176       C  
ATOM   2857  O   SER A 344     -17.336  12.536  31.435  1.00 29.41           O  
ANISOU 2857  O   SER A 344     3867   3661   3647     68     71   -178       O  
ATOM   2858  CB  SER A 344     -15.101  14.164  33.273  1.00 28.55           C  
ANISOU 2858  CB  SER A 344     3730   3534   3584     67     75   -186       C  
ATOM   2859  OG  SER A 344     -13.699  14.235  33.441  1.00 25.56           O  
ANISOU 2859  OG  SER A 344     3334   3142   3237     57     90   -199       O  
ATOM   2860  N   LEU A 345     -17.760  14.709  31.837  1.00 28.43           N  
ANISOU 2860  N   LEU A 345     3764   3525   3515     79     44   -171       N  
ATOM   2861  CA  LEU A 345     -19.207  14.547  31.731  1.00 28.53           C  
ANISOU 2861  CA  LEU A 345     3777   3545   3519     94     20   -173       C  
ATOM   2862  C   LEU A 345     -19.615  14.110  30.314  1.00 31.06           C  
ANISOU 2862  C   LEU A 345     4126   3857   3819     86     16   -171       C  
ATOM   2863  O   LEU A 345     -20.453  13.219  30.159  1.00 32.11           O  
ANISOU 2863  O   LEU A 345     4248   4000   3954     92      8   -176       O  
ATOM   2864  CB  LEU A 345     -19.932  15.824  32.173  1.00 29.93           C  
ANISOU 2864  CB  LEU A 345     3958   3716   3698    110     -8   -174       C  
ATOM   2865  CG  LEU A 345     -19.812  16.196  33.657  1.00 30.57           C  
ANISOU 2865  CG  LEU A 345     4014   3807   3795    121     -7   -180       C  
ATOM   2866  CD1 LEU A 345     -20.068  17.700  33.890  1.00 28.16           C  
ANISOU 2866  CD1 LEU A 345     3719   3488   3491    132    -29   -181       C  
ATOM   2867  CD2 LEU A 345     -20.733  15.343  34.515  1.00 23.70           C  
ANISOU 2867  CD2 LEU A 345     3117   2955   2934    130     -5   -190       C  
ATOM   2868  N   ASP A 346     -18.993  14.707  29.293  1.00 31.18           N  
ANISOU 2868  N   ASP A 346     4182   3852   3812     69     25   -164       N  
ATOM   2869  CA  ASP A 346     -19.211  14.305  27.896  1.00 35.06           C  
ANISOU 2869  CA  ASP A 346     4715   4331   4276     57     24   -162       C  
ATOM   2870  C   ASP A 346     -18.913  12.826  27.645  1.00 34.50           C  
ANISOU 2870  C   ASP A 346     4625   4273   4210     48     50   -169       C  
ATOM   2871  O   ASP A 346     -19.735  12.133  27.065  1.00 36.45           O  
ANISOU 2871  O   ASP A 346     4880   4522   4447     53     33   -172       O  
ATOM   2872  CB  ASP A 346     -18.365  15.153  26.929  1.00 38.04           C  
ANISOU 2872  CB  ASP A 346     5148   4681   4626     33     43   -154       C  
ATOM   2873  CG  ASP A 346     -18.990  16.502  26.616  1.00 42.64           C  
ANISOU 2873  CG  ASP A 346     5773   5239   5187     41      4   -145       C  
ATOM   2874  OD1 ASP A 346     -20.186  16.710  26.920  1.00 43.68           O  
ANISOU 2874  OD1 ASP A 346     5895   5375   5328     68    -42   -148       O  
ATOM   2875  OD2 ASP A 346     -18.279  17.358  26.046  1.00 44.79           O  
ANISOU 2875  OD2 ASP A 346     6093   5488   5439     19     21   -137       O  
ATOM   2876  N   MET A 347     -17.729  12.361  28.055  1.00 34.84           N  
ANISOU 2876  N   MET A 347     4643   4321   4273     35     86   -174       N  
ATOM   2877  CA  MET A 347     -17.329  10.959  27.877  1.00 33.95           C  
ANISOU 2877  CA  MET A 347     4510   4218   4172     28    109   -183       C  
ATOM   2878  C   MET A 347     -18.207  10.046  28.718  1.00 30.28           C  
ANISOU 2878  C   MET A 347     4009   3772   3722     47     89   -184       C  
ATOM   2879  O   MET A 347     -18.654   9.004  28.250  1.00 30.16           O  
ANISOU 2879  O   MET A 347     3992   3762   3704     46     88   -188       O  
ATOM   2880  CB  MET A 347     -15.872  10.727  28.296  1.00 36.18           C  
ANISOU 2880  CB  MET A 347     4765   4498   4484     15    143   -194       C  
ATOM   2881  CG  MET A 347     -14.784  11.180  27.328  1.00 46.44           C  
ANISOU 2881  CG  MET A 347     6091   5777   5777    -14    184   -202       C  
ATOM   2882  SD  MET A 347     -13.094  10.860  27.986  1.00 57.89           S  
ANISOU 2882  SD  MET A 347     7491   7222   7285    -25    218   -226       S  
ATOM   2883  CE  MET A 347     -13.198   9.134  28.475  1.00 48.50           C  
ANISOU 2883  CE  MET A 347     6259   6046   6120     -9    207   -235       C  
ATOM   2884  N   GLY A 348     -18.429  10.444  29.966  1.00 28.26           N  
ANISOU 2884  N   GLY A 348     3729   3525   3483     62     75   -182       N  
ATOM   2885  CA  GLY A 348     -19.217   9.671  30.916  1.00 25.32           C  
ANISOU 2885  CA  GLY A 348     3328   3168   3123     75     64   -184       C  
ATOM   2886  C   GLY A 348     -20.620   9.394  30.436  1.00 26.74           C  
ANISOU 2886  C   GLY A 348     3512   3353   3297     82     45   -187       C  
ATOM   2887  O   GLY A 348     -21.059   8.242  30.425  1.00 29.37           O  
ANISOU 2887  O   GLY A 348     3831   3693   3637     81     48   -192       O  
ATOM   2888  N   TYR A 349     -21.328  10.442  30.022  1.00 26.72           N  
ANISOU 2888  N   TYR A 349     3527   3341   3284     91     21   -188       N  
ATOM   2889  CA  TYR A 349     -22.691  10.263  29.550  1.00 28.89           C  
ANISOU 2889  CA  TYR A 349     3800   3615   3561    101     -7   -197       C  
ATOM   2890  C   TYR A 349     -22.750   9.530  28.210  1.00 29.23           C  
ANISOU 2890  C   TYR A 349     3869   3650   3587     93    -11   -198       C  
ATOM   2891  O   TYR A 349     -23.683   8.764  27.961  1.00 29.70           O  
ANISOU 2891  O   TYR A 349     3915   3712   3657     99    -26   -209       O  
ATOM   2892  CB  TYR A 349     -23.458  11.583  29.511  1.00 26.20           C  
ANISOU 2892  CB  TYR A 349     3469   3262   3222    117    -41   -202       C  
ATOM   2893  CG  TYR A 349     -23.842  12.058  30.884  1.00 29.33           C  
ANISOU 2893  CG  TYR A 349     3833   3670   3642    128    -38   -209       C  
ATOM   2894  CD1 TYR A 349     -24.647  11.278  31.704  1.00 28.74           C  
ANISOU 2894  CD1 TYR A 349     3721   3610   3590    131    -28   -223       C  
ATOM   2895  CD2 TYR A 349     -23.388  13.281  31.375  1.00 28.19           C  
ANISOU 2895  CD2 TYR A 349     3696   3519   3494    132    -42   -204       C  
ATOM   2896  CE1 TYR A 349     -24.983  11.694  32.971  1.00 27.78           C  
ANISOU 2896  CE1 TYR A 349     3575   3495   3484    136    -17   -232       C  
ATOM   2897  CE2 TYR A 349     -23.736  13.714  32.641  1.00 29.08           C  
ANISOU 2897  CE2 TYR A 349     3783   3642   3626    141    -37   -213       C  
ATOM   2898  CZ  TYR A 349     -24.530  12.911  33.432  1.00 28.82           C  
ANISOU 2898  CZ  TYR A 349     3717   3621   3610    142    -23   -228       C  
ATOM   2899  OH  TYR A 349     -24.883  13.329  34.685  1.00 27.58           O  
ANISOU 2899  OH  TYR A 349     3540   3471   3466    148    -12   -239       O  
ATOM   2900  N   TYR A 350     -21.745   9.749  27.368  1.00 29.16           N  
ANISOU 2900  N   TYR A 350     3897   3629   3553     77      5   -190       N  
ATOM   2901  CA  TYR A 350     -21.672   9.085  26.068  1.00 30.23           C  
ANISOU 2901  CA  TYR A 350     4067   3755   3666     65      7   -192       C  
ATOM   2902  C   TYR A 350     -21.560   7.566  26.256  1.00 31.10           C  
ANISOU 2902  C   TYR A 350     4144   3879   3792     61     28   -199       C  
ATOM   2903  O   TYR A 350     -22.288   6.805  25.626  1.00 29.05           O  
ANISOU 2903  O   TYR A 350     3890   3619   3531     63     12   -207       O  
ATOM   2904  CB  TYR A 350     -20.503   9.641  25.236  1.00 31.88           C  
ANISOU 2904  CB  TYR A 350     4322   3946   3845     43     34   -185       C  
ATOM   2905  CG  TYR A 350     -20.401   9.047  23.844  1.00 32.43           C  
ANISOU 2905  CG  TYR A 350     4438   4001   3881     27     42   -189       C  
ATOM   2906  CD1 TYR A 350     -21.127   9.583  22.779  1.00 31.18           C  
ANISOU 2906  CD1 TYR A 350     4341   3820   3686     29      5   -186       C  
ATOM   2907  CD2 TYR A 350     -19.592   7.941  23.598  1.00 31.05           C  
ANISOU 2907  CD2 TYR A 350     4251   3834   3713     11     83   -198       C  
ATOM   2908  CE1 TYR A 350     -21.047   9.024  21.495  1.00 36.63           C  
ANISOU 2908  CE1 TYR A 350     5083   4494   4339     13     11   -190       C  
ATOM   2909  CE2 TYR A 350     -19.497   7.379  22.328  1.00 34.60           C  
ANISOU 2909  CE2 TYR A 350     4745   4270   4131     -5     94   -205       C  
ATOM   2910  CZ  TYR A 350     -20.221   7.925  21.278  1.00 37.22           C  
ANISOU 2910  CZ  TYR A 350     5143   4580   4419     -5     59   -200       C  
ATOM   2911  OH  TYR A 350     -20.127   7.362  20.023  1.00 39.43           O  
ANISOU 2911  OH  TYR A 350     5477   4844   4661    -22     69   -207       O  
ATOM   2912  N   ALA A 351     -20.667   7.143  27.150  1.00 32.22           N  
ANISOU 2912  N   ALA A 351     4256   4032   3955     56     57   -198       N  
ATOM   2913  CA  ALA A 351     -20.434   5.724  27.423  1.00 32.86           C  
ANISOU 2913  CA  ALA A 351     4309   4122   4054     52     74   -204       C  
ATOM   2914  C   ALA A 351     -21.521   5.097  28.297  1.00 33.02           C  
ANISOU 2914  C   ALA A 351     4298   4154   4094     64     59   -207       C  
ATOM   2915  O   ALA A 351     -21.723   3.875  28.271  1.00 31.35           O  
ANISOU 2915  O   ALA A 351     4073   3947   3893     60     64   -212       O  
ATOM   2916  CB  ALA A 351     -19.059   5.533  28.068  1.00 32.56           C  
ANISOU 2916  CB  ALA A 351     4253   4084   4033     44    102   -204       C  
ATOM   2917  N   LYS A 352     -22.212   5.951  29.057  1.00 33.35           N  
ANISOU 2917  N   LYS A 352     4330   4200   4142     75     44   -205       N  
ATOM   2918  CA  LYS A 352     -23.210   5.547  30.058  1.00 33.01           C  
ANISOU 2918  CA  LYS A 352     4257   4166   4120     81     41   -212       C  
ATOM   2919  C   LYS A 352     -22.552   4.784  31.204  1.00 31.40           C  
ANISOU 2919  C   LYS A 352     4038   3968   3925     75     63   -206       C  
ATOM   2920  O   LYS A 352     -22.892   3.642  31.505  1.00 32.96           O  
ANISOU 2920  O   LYS A 352     4224   4167   4132     69     71   -209       O  
ATOM   2921  CB  LYS A 352     -24.365   4.761  29.423  1.00 36.02           C  
ANISOU 2921  CB  LYS A 352     4628   4546   4511     83     26   -225       C  
ATOM   2922  CG  LYS A 352     -25.181   5.573  28.437  1.00 35.82           C  
ANISOU 2922  CG  LYS A 352     4619   4511   4481     94    -10   -234       C  
ATOM   2923  CD  LYS A 352     -26.282   4.745  27.785  1.00 39.96           C  
ANISOU 2923  CD  LYS A 352     5132   5031   5022     97    -30   -252       C  
ATOM   2924  CE  LYS A 352     -27.011   5.580  26.738  1.00 40.97           C  
ANISOU 2924  CE  LYS A 352     5283   5140   5143    111    -79   -262       C  
ATOM   2925  NZ  LYS A 352     -27.941   4.780  25.899  1.00 38.71           N  
ANISOU 2925  NZ  LYS A 352     4993   4844   4870    115   -108   -280       N  
ATOM   2926  N   ILE A 353     -21.582   5.435  31.825  1.00 29.85           N  
ANISOU 2926  N   ILE A 353     3848   3770   3725     76     69   -198       N  
ATOM   2927  CA  ILE A 353     -20.820   4.854  32.914  1.00 30.00           C  
ANISOU 2927  CA  ILE A 353     3861   3786   3751     73     79   -192       C  
ATOM   2928  C   ILE A 353     -20.903   5.817  34.083  1.00 29.65           C  
ANISOU 2928  C   ILE A 353     3817   3743   3703     79     75   -189       C  
ATOM   2929  O   ILE A 353     -21.400   6.943  33.929  1.00 29.86           O  
ANISOU 2929  O   ILE A 353     3845   3773   3726     86     68   -192       O  
ATOM   2930  CB  ILE A 353     -19.330   4.654  32.516  1.00 28.80           C  
ANISOU 2930  CB  ILE A 353     3712   3625   3605     69     85   -192       C  
ATOM   2931  CG1 ILE A 353     -18.677   6.002  32.131  1.00 29.36           C  
ANISOU 2931  CG1 ILE A 353     3793   3692   3672     69     85   -191       C  
ATOM   2932  CG2 ILE A 353     -19.219   3.644  31.392  1.00 23.98           C  
ANISOU 2932  CG2 ILE A 353     3102   3012   2997     61     93   -199       C  
ATOM   2933  CD1 ILE A 353     -17.272   5.892  31.569  1.00 21.50           C  
ANISOU 2933  CD1 ILE A 353     2796   2685   2690     60    100   -199       C  
ATOM   2934  N   GLN A 354     -20.425   5.378  35.245  1.00 28.39           N  
ANISOU 2934  N   GLN A 354     3663   3579   3545     78     78   -185       N  
ATOM   2935  CA  GLN A 354     -20.193   6.295  36.359  1.00 30.29           C  
ANISOU 2935  CA  GLN A 354     3912   3818   3780     84     73   -182       C  
ATOM   2936  C   GLN A 354     -19.191   7.334  35.860  1.00 29.55           C  
ANISOU 2936  C   GLN A 354     3817   3719   3691     89     64   -181       C  
ATOM   2937  O   GLN A 354     -18.234   6.982  35.168  1.00 29.44           O  
ANISOU 2937  O   GLN A 354     3800   3698   3688     85     66   -183       O  
ATOM   2938  CB  GLN A 354     -19.619   5.559  37.568  1.00 29.72           C  
ANISOU 2938  CB  GLN A 354     3856   3733   3703     82     68   -176       C  
ATOM   2939  CG  GLN A 354     -20.504   4.454  38.154  1.00 32.54           C  
ANISOU 2939  CG  GLN A 354     4224   4090   4051     71     81   -175       C  
ATOM   2940  CD  GLN A 354     -19.905   3.850  39.428  1.00 36.62           C  
ANISOU 2940  CD  GLN A 354     4773   4587   4554     68     71   -166       C  
ATOM   2941  OE1 GLN A 354     -20.540   3.827  40.484  1.00 37.11           O  
ANISOU 2941  OE1 GLN A 354     4860   4645   4595     59     83   -165       O  
ATOM   2942  NE2 GLN A 354     -18.673   3.380  39.332  1.00 34.67           N  
ANISOU 2942  NE2 GLN A 354     4528   4324   4320     74     47   -163       N  
ATOM   2943  N   ILE A 355     -19.405   8.605  36.186  1.00 30.31           N  
ANISOU 2943  N   ILE A 355     3917   3817   3782     96     59   -182       N  
ATOM   2944  CA  ILE A 355     -18.514   9.658  35.666  1.00 30.41           C  
ANISOU 2944  CA  ILE A 355     3932   3823   3801     97     54   -182       C  
ATOM   2945  C   ILE A 355     -17.050   9.393  36.024  1.00 29.37           C  
ANISOU 2945  C   ILE A 355     3796   3678   3686     95     50   -184       C  
ATOM   2946  O   ILE A 355     -16.170   9.589  35.192  1.00 29.92           O  
ANISOU 2946  O   ILE A 355     3861   3740   3768     88     59   -188       O  
ATOM   2947  CB  ILE A 355     -18.952  11.109  36.064  1.00 29.93           C  
ANISOU 2947  CB  ILE A 355     3875   3762   3733    106     44   -183       C  
ATOM   2948  CG1 ILE A 355     -20.440  11.349  35.757  1.00 27.91           C  
ANISOU 2948  CG1 ILE A 355     3616   3516   3472    111     42   -189       C  
ATOM   2949  CG2 ILE A 355     -18.092  12.162  35.341  1.00 27.05           C  
ANISOU 2949  CG2 ILE A 355     3517   3387   3373    103     42   -182       C  
ATOM   2950  CD1 ILE A 355     -20.833  11.129  34.292  1.00 32.71           C  
ANISOU 2950  CD1 ILE A 355     4229   4122   4078    108     38   -189       C  
ATOM   2951  N   GLN A 356     -16.787   8.918  37.238  1.00 30.60           N  
ANISOU 2951  N   GLN A 356     3956   3828   3843    100     38   -183       N  
ATOM   2952  CA  GLN A 356     -15.400   8.661  37.651  1.00 29.86           C  
ANISOU 2952  CA  GLN A 356     3857   3716   3774    103     23   -189       C  
ATOM   2953  C   GLN A 356     -14.707   7.551  36.839  1.00 29.13           C  
ANISOU 2953  C   GLN A 356     3749   3615   3703     96     30   -197       C  
ATOM   2954  O   GLN A 356     -13.491   7.416  36.895  1.00 29.75           O  
ANISOU 2954  O   GLN A 356     3813   3677   3815     98     20   -210       O  
ATOM   2955  CB  GLN A 356     -15.287   8.421  39.168  1.00 30.13           C  
ANISOU 2955  CB  GLN A 356     3911   3738   3798    111     -1   -186       C  
ATOM   2956  CG  GLN A 356     -15.935   7.125  39.715  1.00 27.68           C  
ANISOU 2956  CG  GLN A 356     3620   3427   3470    108     -1   -178       C  
ATOM   2957  CD  GLN A 356     -17.423   7.270  40.015  1.00 31.58           C  
ANISOU 2957  CD  GLN A 356     4127   3938   3934    102     21   -173       C  
ATOM   2958  OE1 GLN A 356     -18.095   8.172  39.501  1.00 31.38           O  
ANISOU 2958  OE1 GLN A 356     4089   3927   3906    102     34   -176       O  
ATOM   2959  NE2 GLN A 356     -17.948   6.369  40.841  1.00 29.59           N  
ANISOU 2959  NE2 GLN A 356     3901   3679   3661     95     24   -167       N  
ATOM   2960  N   SER A 357     -15.472   6.780  36.068  1.00 29.69           N  
ANISOU 2960  N   SER A 357     3820   3698   3763     90     46   -193       N  
ATOM   2961  CA  SER A 357     -14.877   5.734  35.220  1.00 29.16           C  
ANISOU 2961  CA  SER A 357     3739   3624   3717     83     55   -203       C  
ATOM   2962  C   SER A 357     -14.174   6.265  33.972  1.00 29.89           C  
ANISOU 2962  C   SER A 357     3821   3714   3823     72     79   -215       C  
ATOM   2963  O   SER A 357     -13.511   5.491  33.258  1.00 30.82           O  
ANISOU 2963  O   SER A 357     3925   3823   3962     64     92   -230       O  
ATOM   2964  CB  SER A 357     -15.912   4.690  34.808  1.00 28.07           C  
ANISOU 2964  CB  SER A 357     3607   3497   3562     78     63   -197       C  
ATOM   2965  OG  SER A 357     -16.368   3.965  35.923  1.00 28.76           O  
ANISOU 2965  OG  SER A 357     3707   3580   3640     82     49   -189       O  
ATOM   2966  N   VAL A 358     -14.304   7.563  33.702  1.00 28.74           N  
ANISOU 2966  N   VAL A 358     3685   3572   3665     69     86   -211       N  
ATOM   2967  CA  VAL A 358     -13.537   8.201  32.604  1.00 29.82           C  
ANISOU 2967  CA  VAL A 358     3821   3700   3810     53    113   -223       C  
ATOM   2968  C   VAL A 358     -12.026   7.966  32.735  1.00 29.49           C  
ANISOU 2968  C   VAL A 358     3750   3638   3816     48    121   -246       C  
ATOM   2969  O   VAL A 358     -11.322   7.987  31.736  1.00 31.06           O  
ANISOU 2969  O   VAL A 358     3943   3829   4030     30    154   -263       O  
ATOM   2970  CB  VAL A 358     -13.817   9.723  32.461  1.00 30.62           C  
ANISOU 2970  CB  VAL A 358     3941   3802   3892     51    115   -214       C  
ATOM   2971  CG1 VAL A 358     -15.297   9.962  32.168  1.00 32.35           C  
ANISOU 2971  CG1 VAL A 358     4184   4034   4073     57    104   -198       C  
ATOM   2972  CG2 VAL A 358     -13.349  10.513  33.722  1.00 24.62           C  
ANISOU 2972  CG2 VAL A 358     3171   3036   3149     62     93   -214       C  
ATOM   2973  N   PHE A 359     -11.541   7.738  33.958  1.00 27.50           N  
ANISOU 2973  N   PHE A 359     3482   3377   3589     64     89   -250       N  
ATOM   2974  CA  PHE A 359     -10.126   7.394  34.185  1.00 31.05           C  
ANISOU 2974  CA  PHE A 359     3898   3804   4096     65     84   -279       C  
ATOM   2975  C   PHE A 359      -9.740   6.033  33.614  1.00 30.57           C  
ANISOU 2975  C   PHE A 359     3819   3736   4061     61     93   -296       C  
ATOM   2976  O   PHE A 359      -8.552   5.695  33.531  1.00 31.19           O  
ANISOU 2976  O   PHE A 359     3862   3793   4195     59     95   -328       O  
ATOM   2977  CB  PHE A 359      -9.777   7.412  35.674  1.00 30.00           C  
ANISOU 2977  CB  PHE A 359     3761   3656   3980     86     35   -279       C  
ATOM   2978  CG  PHE A 359      -9.764   8.786  36.272  1.00 30.81           C  
ANISOU 2978  CG  PHE A 359     3873   3759   4074     89     25   -272       C  
ATOM   2979  CD1 PHE A 359      -8.854   9.744  35.822  1.00 27.25           C  
ANISOU 2979  CD1 PHE A 359     3402   3297   3656     77     45   -291       C  
ATOM   2980  CD2 PHE A 359     -10.659   9.128  37.287  1.00 31.33           C  
ANISOU 2980  CD2 PHE A 359     3968   3835   4100    102     -1   -249       C  
ATOM   2981  CE1 PHE A 359      -8.831  11.018  36.362  1.00 22.32           C  
ANISOU 2981  CE1 PHE A 359     2785   2670   3026     81     34   -286       C  
ATOM   2982  CE2 PHE A 359     -10.650  10.410  37.846  1.00 27.68           C  
ANISOU 2982  CE2 PHE A 359     3514   3372   3631    106    -10   -246       C  
ATOM   2983  CZ  PHE A 359      -9.734  11.359  37.375  1.00 27.55           C  
ANISOU 2983  CZ  PHE A 359     3477   3344   3648     97      4   -263       C  
ATOM   2984  N   SER A 360     -10.749   5.267  33.220  1.00 28.09           N  
ANISOU 2984  N   SER A 360     3524   3437   3711     60     98   -280       N  
ATOM   2985  CA  SER A 360     -10.549   3.921  32.731  1.00 27.07           C  
ANISOU 2985  CA  SER A 360     3382   3303   3601     58    104   -294       C  
ATOM   2986  C   SER A 360     -11.127   3.765  31.314  1.00 27.89           C  
ANISOU 2986  C   SER A 360     3501   3421   3675     40    144   -292       C  
ATOM   2987  O   SER A 360     -12.337   3.590  31.132  1.00 26.90           O  
ANISOU 2987  O   SER A 360     3401   3312   3507     41    140   -270       O  
ATOM   2988  CB  SER A 360     -11.161   2.926  33.712  1.00 23.17           C  
ANISOU 2988  CB  SER A 360     2900   2807   3095     75     65   -278       C  
ATOM   2989  OG  SER A 360     -11.363   1.680  33.097  1.00 25.69           O  
ANISOU 2989  OG  SER A 360     3216   3126   3418     71     73   -283       O  
ATOM   2990  N   PRO A 361     -10.257   3.866  30.300  1.00 30.20           N  
ANISOU 2990  N   PRO A 361     3780   3703   3991     21    184   -319       N  
ATOM   2991  CA  PRO A 361     -10.685   3.670  28.909  1.00 29.94           C  
ANISOU 2991  CA  PRO A 361     3771   3678   3926      2    223   -320       C  
ATOM   2992  C   PRO A 361     -11.224   2.254  28.667  1.00 29.76           C  
ANISOU 2992  C   PRO A 361     3748   3660   3899      8    213   -320       C  
ATOM   2993  O   PRO A 361     -12.164   2.084  27.884  1.00 30.81           O  
ANISOU 2993  O   PRO A 361     3912   3806   3990      1    222   -307       O  
ATOM   2994  CB  PRO A 361      -9.408   3.938  28.100  1.00 29.88           C  
ANISOU 2994  CB  PRO A 361     3746   3653   3955    -22    272   -356       C  
ATOM   2995  CG  PRO A 361      -8.269   3.748  29.091  1.00 32.36           C  
ANISOU 2995  CG  PRO A 361     4009   3947   4339     -9    251   -382       C  
ATOM   2996  CD  PRO A 361      -8.836   4.260  30.392  1.00 31.01           C  
ANISOU 2996  CD  PRO A 361     3848   3784   4151     15    199   -351       C  
ATOM   2997  N   ILE A 362     -10.664   1.259  29.357  1.00 28.96           N  
ANISOU 2997  N   ILE A 362     3615   3546   3841     21    190   -334       N  
ATOM   2998  CA  ILE A 362     -11.200  -0.114  29.307  1.00 29.57           C  
ANISOU 2998  CA  ILE A 362     3693   3625   3916     29    174   -332       C  
ATOM   2999  C   ILE A 362     -12.686  -0.158  29.741  1.00 29.61           C  
ANISOU 2999  C   ILE A 362     3729   3649   3872     37    150   -296       C  
ATOM   3000  O   ILE A 362     -13.519  -0.774  29.081  1.00 30.21           O  
ANISOU 3000  O   ILE A 362     3820   3735   3924     32    156   -290       O  
ATOM   3001  CB  ILE A 362     -10.298  -1.138  30.110  1.00 27.25           C  
ANISOU 3001  CB  ILE A 362     3366   3308   3682     45    142   -353       C  
ATOM   3002  CG1 ILE A 362      -9.057  -1.523  29.290  1.00 24.40           C  
ANISOU 3002  CG1 ILE A 362     2969   2928   3375     34    175   -399       C  
ATOM   3003  CG2 ILE A 362     -11.082  -2.397  30.535  1.00 24.83           C  
ANISOU 3003  CG2 ILE A 362     3073   3001   3363     56    111   -336       C  
ATOM   3004  CD1 ILE A 362      -7.998  -2.344  30.055  1.00 19.76           C  
ANISOU 3004  CD1 ILE A 362     2340   2309   2859     53    137   -428       C  
ATOM   3005  N   LYS A 363     -13.009   0.508  30.843  1.00 31.10           N  
ANISOU 3005  N   LYS A 363     3924   3841   4050     48    124   -276       N  
ATOM   3006  CA  LYS A 363     -14.388   0.553  31.324  1.00 30.66           C  
ANISOU 3006  CA  LYS A 363     3892   3802   3955     53    109   -249       C  
ATOM   3007  C   LYS A 363     -15.246   1.387  30.377  1.00 29.25           C  
ANISOU 3007  C   LYS A 363     3734   3640   3741     44    128   -241       C  
ATOM   3008  O   LYS A 363     -16.419   1.069  30.130  1.00 28.06           O  
ANISOU 3008  O   LYS A 363     3595   3500   3567     44    123   -231       O  
ATOM   3009  CB  LYS A 363     -14.449   1.112  32.756  1.00 28.59           C  
ANISOU 3009  CB  LYS A 363     3637   3537   3691     64     82   -235       C  
ATOM   3010  CG  LYS A 363     -15.852   1.187  33.372  1.00 31.41           C  
ANISOU 3010  CG  LYS A 363     4014   3909   4013     66     75   -213       C  
ATOM   3011  CD  LYS A 363     -16.558  -0.177  33.490  1.00 34.50           C  
ANISOU 3011  CD  LYS A 363     4410   4297   4399     63     70   -209       C  
ATOM   3012  CE  LYS A 363     -15.902  -1.098  34.501  1.00 36.85           C  
ANISOU 3012  CE  LYS A 363     4714   4572   4715     70     45   -208       C  
ATOM   3013  NZ  LYS A 363     -16.886  -2.081  35.062  1.00 40.03           N  
ANISOU 3013  NZ  LYS A 363     5137   4971   5100     64     42   -195       N  
ATOM   3014  N   THR A 364     -14.648   2.452  29.851  1.00 26.68           N  
ANISOU 3014  N   THR A 364     3413   3312   3414     36    146   -247       N  
ATOM   3015  CA  THR A 364     -15.338   3.351  28.935  1.00 25.76           C  
ANISOU 3015  CA  THR A 364     3325   3204   3261     28    157   -239       C  
ATOM   3016  C   THR A 364     -15.738   2.612  27.664  1.00 27.43           C  
ANISOU 3016  C   THR A 364     3553   3415   3454     17    171   -247       C  
ATOM   3017  O   THR A 364     -16.889   2.677  27.254  1.00 29.22           O  
ANISOU 3017  O   THR A 364     3800   3650   3652     20    157   -236       O  
ATOM   3018  CB  THR A 364     -14.477   4.607  28.632  1.00 26.00           C  
ANISOU 3018  CB  THR A 364     3363   3224   3292     17    177   -245       C  
ATOM   3019  OG1 THR A 364     -14.186   5.278  29.866  1.00 27.48           O  
ANISOU 3019  OG1 THR A 364     3535   3411   3496     29    158   -239       O  
ATOM   3020  CG2 THR A 364     -15.206   5.594  27.696  1.00 22.24           C  
ANISOU 3020  CG2 THR A 364     2928   2749   2772      8    181   -234       C  
ATOM   3021  N   TRP A 365     -14.794   1.892  27.062  1.00 28.38           N  
ANISOU 3021  N   TRP A 365     3662   3525   3594      6    196   -268       N  
ATOM   3022  CA  TRP A 365     -15.054   1.169  25.830  1.00 27.93           C  
ANISOU 3022  CA  TRP A 365     3626   3467   3520     -5    213   -279       C  
ATOM   3023  C   TRP A 365     -15.914  -0.062  26.048  1.00 30.78           C  
ANISOU 3023  C   TRP A 365     3976   3834   3884      6    189   -274       C  
ATOM   3024  O   TRP A 365     -16.745  -0.404  25.194  1.00 30.85           O  
ANISOU 3024  O   TRP A 365     4008   3847   3867      2    185   -273       O  
ATOM   3025  CB  TRP A 365     -13.756   0.818  25.113  1.00 26.80           C  
ANISOU 3025  CB  TRP A 365     3473   3309   3401    -23    255   -309       C  
ATOM   3026  CG  TRP A 365     -13.184   1.993  24.371  1.00 30.93           C  
ANISOU 3026  CG  TRP A 365     4025   3823   3905    -45    291   -315       C  
ATOM   3027  CD1 TRP A 365     -12.030   2.667  24.663  1.00 27.35           C  
ANISOU 3027  CD1 TRP A 365     3550   3358   3483    -55    317   -330       C  
ATOM   3028  CD2 TRP A 365     -13.754   2.646  23.226  1.00 25.89           C  
ANISOU 3028  CD2 TRP A 365     3447   3182   3210    -61    303   -306       C  
ATOM   3029  NE1 TRP A 365     -11.843   3.682  23.763  1.00 30.43           N  
ANISOU 3029  NE1 TRP A 365     3985   3739   3839    -79    352   -330       N  
ATOM   3030  CE2 TRP A 365     -12.886   3.699  22.874  1.00 28.72           C  
ANISOU 3030  CE2 TRP A 365     3822   3525   3564    -83    342   -314       C  
ATOM   3031  CE3 TRP A 365     -14.910   2.434  22.459  1.00 27.06           C  
ANISOU 3031  CE3 TRP A 365     3637   3332   3311    -58    282   -293       C  
ATOM   3032  CZ2 TRP A 365     -13.133   4.548  21.782  1.00 27.88           C  
ANISOU 3032  CZ2 TRP A 365     3784   3407   3402   -105    360   -306       C  
ATOM   3033  CZ3 TRP A 365     -15.162   3.281  21.376  1.00 25.28           C  
ANISOU 3033  CZ3 TRP A 365     3478   3095   3033    -76    292   -287       C  
ATOM   3034  CH2 TRP A 365     -14.273   4.321  21.048  1.00 26.78           C  
ANISOU 3034  CH2 TRP A 365     3693   3269   3213   -100    332   -292       C  
ATOM   3035  N   ASP A 366     -15.738  -0.719  27.193  1.00 30.78           N  
ANISOU 3035  N   ASP A 366     3946   3833   3915     18    171   -272       N  
ATOM   3036  CA  ASP A 366     -16.598  -1.841  27.523  1.00 32.69           C  
ANISOU 3036  CA  ASP A 366     4183   4079   4159     25    151   -265       C  
ATOM   3037  C   ASP A 366     -18.076  -1.424  27.509  1.00 32.35           C  
ANISOU 3037  C   ASP A 366     4156   4049   4086     29    134   -249       C  
ATOM   3038  O   ASP A 366     -18.915  -2.127  26.945  1.00 32.39           O  
ANISOU 3038  O   ASP A 366     4167   4056   4083     27    128   -251       O  
ATOM   3039  CB  ASP A 366     -16.217  -2.449  28.874  1.00 35.67           C  
ANISOU 3039  CB  ASP A 366     4540   4447   4566     35    131   -261       C  
ATOM   3040  CG  ASP A 366     -16.779  -3.834  29.058  1.00 34.96           C  
ANISOU 3040  CG  ASP A 366     4447   4353   4483     37    118   -259       C  
ATOM   3041  OD1 ASP A 366     -16.647  -4.655  28.136  1.00 37.71           O  
ANISOU 3041  OD1 ASP A 366     4792   4697   4839     32    129   -275       O  
ATOM   3042  OD2 ASP A 366     -17.366  -4.098  30.115  1.00 36.77           O  
ANISOU 3042  OD2 ASP A 366     4680   4582   4710     41    101   -244       O  
ATOM   3043  N   ALA A 367     -18.386  -0.274  28.109  1.00 30.65           N  
ANISOU 3043  N   ALA A 367     3946   3840   3860     34    126   -236       N  
ATOM   3044  CA  ALA A 367     -19.760   0.230  28.134  1.00 31.02           C  
ANISOU 3044  CA  ALA A 367     4000   3896   3888     39    109   -227       C  
ATOM   3045  C   ALA A 367     -20.260   0.737  26.778  1.00 32.76           C  
ANISOU 3045  C   ALA A 367     4249   4115   4083     36    104   -232       C  
ATOM   3046  O   ALA A 367     -21.409   0.501  26.422  1.00 34.80           O  
ANISOU 3046  O   ALA A 367     4510   4375   4336     40     85   -234       O  
ATOM   3047  CB  ALA A 367     -19.912   1.294  29.171  1.00 31.04           C  
ANISOU 3047  CB  ALA A 367     3999   3903   3890     47    101   -216       C  
ATOM   3048  N   ILE A 368     -19.413   1.442  26.032  1.00 32.65           N  
ANISOU 3048  N   ILE A 368     4258   4093   4052     27    120   -234       N  
ATOM   3049  CA  ILE A 368     -19.773   1.868  24.679  1.00 33.58           C  
ANISOU 3049  CA  ILE A 368     4419   4203   4136     20    116   -238       C  
ATOM   3050  C   ILE A 368     -20.150   0.657  23.793  1.00 34.63           C  
ANISOU 3050  C   ILE A 368     4561   4333   4265     16    114   -250       C  
ATOM   3051  O   ILE A 368     -21.215   0.632  23.172  1.00 37.30           O  
ANISOU 3051  O   ILE A 368     4918   4668   4587     22     85   -252       O  
ATOM   3052  CB  ILE A 368     -18.642   2.699  24.017  1.00 33.24           C  
ANISOU 3052  CB  ILE A 368     4407   4148   4075      3    146   -241       C  
ATOM   3053  CG1 ILE A 368     -18.399   3.986  24.811  1.00 31.41           C  
ANISOU 3053  CG1 ILE A 368     4171   3918   3847      8    142   -229       C  
ATOM   3054  CG2 ILE A 368     -18.989   3.012  22.552  1.00 28.53           C  
ANISOU 3054  CG2 ILE A 368     3870   3536   3432     -8    143   -243       C  
ATOM   3055  CD1 ILE A 368     -17.150   4.789  24.396  1.00 32.25           C  
ANISOU 3055  CD1 ILE A 368     4297   4010   3946    -11    179   -234       C  
ATOM   3056  N   ILE A 369     -19.281  -0.348  23.776  1.00 32.55           N  
ANISOU 3056  N   ILE A 369     4279   4068   4021      8    140   -262       N  
ATOM   3057  CA  ILE A 369     -19.462  -1.527  22.947  1.00 30.45           C  
ANISOU 3057  CA  ILE A 369     4020   3798   3753      3    142   -276       C  
ATOM   3058  C   ILE A 369     -20.684  -2.340  23.389  1.00 31.90           C  
ANISOU 3058  C   ILE A 369     4181   3988   3953     15    111   -273       C  
ATOM   3059  O   ILE A 369     -21.469  -2.801  22.546  1.00 30.87           O  
ANISOU 3059  O   ILE A 369     4068   3853   3809     15     93   -281       O  
ATOM   3060  CB  ILE A 369     -18.146  -2.363  22.877  1.00 29.64           C  
ANISOU 3060  CB  ILE A 369     3899   3689   3675     -8    178   -294       C  
ATOM   3061  CG1 ILE A 369     -17.070  -1.559  22.127  1.00 27.30           C  
ANISOU 3061  CG1 ILE A 369     3630   3383   3362    -26    217   -305       C  
ATOM   3062  CG2 ILE A 369     -18.379  -3.722  22.202  1.00 26.83           C  
ANISOU 3062  CG2 ILE A 369     3541   3328   3323    -11    178   -310       C  
ATOM   3063  CD1 ILE A 369     -15.631  -1.998  22.369  1.00 23.86           C  
ANISOU 3063  CD1 ILE A 369     3159   2938   2966    -35    254   -327       C  
ATOM   3064  N   PHE A 370     -20.861  -2.477  24.703  1.00 31.61           N  
ANISOU 3064  N   PHE A 370     4109   3959   3943     23    106   -263       N  
ATOM   3065  CA  PHE A 370     -22.034  -3.156  25.266  1.00 30.92           C  
ANISOU 3065  CA  PHE A 370     3999   3876   3872     29     86   -262       C  
ATOM   3066  C   PHE A 370     -23.356  -2.483  24.911  1.00 31.19           C  
ANISOU 3066  C   PHE A 370     4041   3911   3897     37     57   -264       C  
ATOM   3067  O   PHE A 370     -24.311  -3.174  24.567  1.00 31.84           O  
ANISOU 3067  O   PHE A 370     4116   3991   3990     38     40   -274       O  
ATOM   3068  CB  PHE A 370     -21.916  -3.328  26.788  1.00 29.62           C  
ANISOU 3068  CB  PHE A 370     3809   3715   3730     31     91   -251       C  
ATOM   3069  CG  PHE A 370     -23.240  -3.555  27.485  1.00 29.41           C  
ANISOU 3069  CG  PHE A 370     3765   3692   3716     33     80   -249       C  
ATOM   3070  CD1 PHE A 370     -23.746  -2.604  28.368  1.00 31.25           C  
ANISOU 3070  CD1 PHE A 370     3991   3932   3950     37     78   -242       C  
ATOM   3071  CD2 PHE A 370     -23.982  -4.712  27.253  1.00 28.41           C  
ANISOU 3071  CD2 PHE A 370     3628   3562   3605     28     75   -259       C  
ATOM   3072  CE1 PHE A 370     -24.963  -2.808  29.007  1.00 31.81           C  
ANISOU 3072  CE1 PHE A 370     4043   4005   4037     35     76   -247       C  
ATOM   3073  CE2 PHE A 370     -25.197  -4.926  27.886  1.00 27.69           C  
ANISOU 3073  CE2 PHE A 370     3517   3471   3532     25     73   -262       C  
ATOM   3074  CZ  PHE A 370     -25.689  -3.979  28.767  1.00 30.35           C  
ANISOU 3074  CZ  PHE A 370     3846   3815   3870     27     76   -258       C  
ATOM   3075  N   ASN A 371     -23.420  -1.154  25.014  1.00 29.84           N  
ANISOU 3075  N   ASN A 371     3884   3742   3712     42     49   -256       N  
ATOM   3076  CA  ASN A 371     -24.624  -0.411  24.606  1.00 31.54           C  
ANISOU 3076  CA  ASN A 371     4108   3953   3923     53     13   -262       C  
ATOM   3077  C   ASN A 371     -24.890  -0.515  23.100  1.00 30.97           C  
ANISOU 3077  C   ASN A 371     4076   3866   3824     53    -11   -272       C  
ATOM   3078  O   ASN A 371     -26.028  -0.657  22.671  1.00 33.48           O  
ANISOU 3078  O   ASN A 371     4392   4178   4152     62    -48   -285       O  
ATOM   3079  CB  ASN A 371     -24.567   1.063  25.040  1.00 30.43           C  
ANISOU 3079  CB  ASN A 371     3976   3814   3774     60      6   -252       C  
ATOM   3080  CG  ASN A 371     -24.847   1.248  26.522  1.00 36.68           C  
ANISOU 3080  CG  ASN A 371     4728   4617   4591     64     17   -248       C  
ATOM   3081  OD1 ASN A 371     -26.005   1.262  26.951  1.00 37.66           O  
ANISOU 3081  OD1 ASN A 371     4827   4743   4739     71      2   -259       O  
ATOM   3082  ND2 ASN A 371     -23.789   1.394  27.314  1.00 33.06           N  
ANISOU 3082  ND2 ASN A 371     4266   4164   4130     59     43   -235       N  
ATOM   3083  N   SER A 372     -23.836  -0.458  22.301  1.00 31.47           N  
ANISOU 3083  N   SER A 372     4179   3924   3856     41     11   -269       N  
ATOM   3084  CA  SER A 372     -23.978  -0.577  20.854  1.00 32.18           C  
ANISOU 3084  CA  SER A 372     4321   3997   3911     36     -6   -279       C  
ATOM   3085  C   SER A 372     -24.513  -1.965  20.463  1.00 32.53           C  
ANISOU 3085  C   SER A 372     4349   4039   3971     36    -16   -295       C  
ATOM   3086  O   SER A 372     -25.388  -2.079  19.611  1.00 33.42           O  
ANISOU 3086  O   SER A 372     4487   4139   4073     43    -57   -306       O  
ATOM   3087  CB  SER A 372     -22.643  -0.295  20.172  1.00 31.72           C  
ANISOU 3087  CB  SER A 372     4305   3930   3816     16     34   -277       C  
ATOM   3088  OG  SER A 372     -22.740  -0.426  18.759  1.00 37.35           O  
ANISOU 3088  OG  SER A 372     5080   4624   4486      7     24   -286       O  
ATOM   3089  N   LEU A 373     -24.003  -3.006  21.113  1.00 32.79           N  
ANISOU 3089  N   LEU A 373     4343   4083   4032     30     15   -296       N  
ATOM   3090  CA  LEU A 373     -24.403  -4.379  20.808  1.00 32.60           C  
ANISOU 3090  CA  LEU A 373     4304   4057   4027     28     10   -311       C  
ATOM   3091  C   LEU A 373     -25.813  -4.694  21.324  1.00 32.95           C  
ANISOU 3091  C   LEU A 373     4311   4103   4106     39    -23   -317       C  
ATOM   3092  O   LEU A 373     -26.611  -5.306  20.616  1.00 32.54           O  
ANISOU 3092  O   LEU A 373     4262   4041   4059     42    -52   -334       O  
ATOM   3093  CB  LEU A 373     -23.365  -5.380  21.343  1.00 28.95           C  
ANISOU 3093  CB  LEU A 373     3815   3600   3585     19     49   -311       C  
ATOM   3094  CG  LEU A 373     -22.028  -5.452  20.589  1.00 30.01           C  
ANISOU 3094  CG  LEU A 373     3977   3727   3697      6     85   -319       C  
ATOM   3095  CD1 LEU A 373     -21.069  -6.430  21.273  1.00 28.97           C  
ANISOU 3095  CD1 LEU A 373     3808   3597   3600      2    113   -324       C  
ATOM   3096  CD2 LEU A 373     -22.203  -5.821  19.087  1.00 27.12           C  
ANISOU 3096  CD2 LEU A 373     3658   3348   3297     -2     78   -336       C  
ATOM   3097  N   LYS A 374     -26.112  -4.258  22.546  1.00 33.66           N  
ANISOU 3097  N   LYS A 374     4365   4203   4221     43    -17   -308       N  
ATOM   3098  CA  LYS A 374     -27.447  -4.393  23.128  1.00 35.94           C  
ANISOU 3098  CA  LYS A 374     4615   4493   4548     49    -38   -319       C  
ATOM   3099  C   LYS A 374     -28.555  -3.825  22.224  1.00 38.43           C  
ANISOU 3099  C   LYS A 374     4943   4794   4864     63    -90   -337       C  
ATOM   3100  O   LYS A 374     -29.620  -4.435  22.085  1.00 41.02           O  
ANISOU 3100  O   LYS A 374     5245   5114   5226     67   -114   -358       O  
ATOM   3101  CB  LYS A 374     -27.486  -3.762  24.522  1.00 35.41           C  
ANISOU 3101  CB  LYS A 374     4519   4436   4497     50    -18   -308       C  
ATOM   3102  CG  LYS A 374     -28.866  -3.740  25.163  1.00 38.26           C  
ANISOU 3102  CG  LYS A 374     4839   4797   4900     52    -29   -324       C  
ATOM   3103  CD  LYS A 374     -28.798  -3.559  26.675  1.00 35.26           C  
ANISOU 3103  CD  LYS A 374     4435   4427   4534     44      6   -314       C  
ATOM   3104  CE  LYS A 374     -30.091  -2.948  27.178  1.00 33.47           C  
ANISOU 3104  CE  LYS A 374     4175   4200   4344     49     -3   -335       C  
ATOM   3105  NZ  LYS A 374     -30.128  -1.498  26.854  1.00 35.95           N  
ANISOU 3105  NZ  LYS A 374     4502   4513   4645     67    -32   -335       N  
ATOM   3106  N   GLU A 375     -28.295  -2.680  21.602  1.00 40.42           N  
ANISOU 3106  N   GLU A 375     5239   5039   5081     71   -111   -331       N  
ATOM   3107  CA  GLU A 375     -29.210  -2.093  20.608  1.00 45.09           C  
ANISOU 3107  CA  GLU A 375     5859   5609   5665     86   -172   -346       C  
ATOM   3108  C   GLU A 375     -29.639  -3.066  19.489  1.00 43.74           C  
ANISOU 3108  C   GLU A 375     5708   5422   5489     87   -202   -365       C  
ATOM   3109  O   GLU A 375     -30.760  -2.982  18.978  1.00 42.19           O  
ANISOU 3109  O   GLU A 375     5510   5208   5314    102   -259   -388       O  
ATOM   3110  CB  GLU A 375     -28.592  -0.827  19.997  1.00 47.09           C  
ANISOU 3110  CB  GLU A 375     6175   5852   5867     89   -184   -331       C  
ATOM   3111  CG  GLU A 375     -29.089   0.480  20.623  1.00 58.58           C  
ANISOU 3111  CG  GLU A 375     7616   7304   7337    104   -207   -329       C  
ATOM   3112  CD  GLU A 375     -30.423   0.955  20.025  1.00 68.28           C  
ANISOU 3112  CD  GLU A 375     8849   8507   8586    126   -283   -353       C  
ATOM   3113  OE1 GLU A 375     -30.528   1.058  18.778  1.00 68.64           O  
ANISOU 3113  OE1 GLU A 375     8958   8527   8594    131   -327   -357       O  
ATOM   3114  OE2 GLU A 375     -31.368   1.231  20.802  1.00 71.40           O  
ANISOU 3114  OE2 GLU A 375     9187   8905   9036    139   -299   -370       O  
ATOM   3115  N   GLN A 376     -28.750  -3.982  19.115  1.00 41.60           N  
ANISOU 3115  N   GLN A 376     5455   5155   5195     71   -167   -360       N  
ATOM   3116  CA  GLN A 376     -29.055  -4.954  18.065  1.00 42.61           C  
ANISOU 3116  CA  GLN A 376     5606   5269   5316     70   -191   -378       C  
ATOM   3117  C   GLN A 376     -29.465  -6.317  18.638  1.00 40.59           C  
ANISOU 3117  C   GLN A 376     5291   5021   5110     64   -174   -390       C  
ATOM   3118  O   GLN A 376     -29.515  -7.309  17.912  1.00 40.90           O  
ANISOU 3118  O   GLN A 376     5343   5052   5147     60   -182   -404       O  
ATOM   3119  CB  GLN A 376     -27.859  -5.109  17.120  1.00 45.11           C  
ANISOU 3119  CB  GLN A 376     5986   5580   5574     55   -162   -371       C  
ATOM   3120  CG  GLN A 376     -27.387  -3.807  16.463  1.00 50.31           C  
ANISOU 3120  CG  GLN A 376     6715   6225   6175     54   -170   -358       C  
ATOM   3121  CD  GLN A 376     -25.927  -3.870  16.042  1.00 54.51           C  
ANISOU 3121  CD  GLN A 376     7288   6761   6663     31   -110   -350       C  
ATOM   3122  OE1 GLN A 376     -25.056  -3.317  16.715  1.00 57.34           O  
ANISOU 3122  OE1 GLN A 376     7633   7132   7023     23    -67   -334       O  
ATOM   3123  NE2 GLN A 376     -25.649  -4.564  14.936  1.00 56.40           N  
ANISOU 3123  NE2 GLN A 376     7575   6986   6868     20   -105   -363       N  
ATOM   3124  N   ASN A 377     -29.754  -6.351  19.942  1.00 38.06           N  
ANISOU 3124  N   ASN A 377     4912   4715   4833     62   -150   -386       N  
ATOM   3125  CA  ASN A 377     -30.079  -7.584  20.671  1.00 36.37           C  
ANISOU 3125  CA  ASN A 377     4648   4506   4664     51   -126   -393       C  
ATOM   3126  C   ASN A 377     -28.929  -8.608  20.718  1.00 36.67           C  
ANISOU 3126  C   ASN A 377     4697   4550   4687     37    -84   -381       C  
ATOM   3127  O   ASN A 377     -29.142  -9.819  20.880  1.00 36.93           O  
ANISOU 3127  O   ASN A 377     4706   4579   4747     28    -75   -390       O  
ATOM   3128  CB  ASN A 377     -31.387  -8.205  20.158  1.00 36.28           C  
ANISOU 3128  CB  ASN A 377     4613   4478   4692     57   -169   -424       C  
ATOM   3129  CG  ASN A 377     -32.622  -7.397  20.561  1.00 37.56           C  
ANISOU 3129  CG  ASN A 377     4738   4634   4898     69   -201   -443       C  
ATOM   3130  OD1 ASN A 377     -32.698  -6.854  21.664  1.00 34.21           O  
ANISOU 3130  OD1 ASN A 377     4283   4222   4492     66   -172   -435       O  
ATOM   3131  ND2 ASN A 377     -33.603  -7.332  19.667  1.00 32.88           N  
ANISOU 3131  ND2 ASN A 377     4147   4020   4325     84   -262   -473       N  
ATOM   3132  N   LYS A 378     -27.704  -8.106  20.604  1.00 35.22           N  
ANISOU 3132  N   LYS A 378     4545   4372   4464     34    -59   -364       N  
ATOM   3133  CA  LYS A 378     -26.533  -8.955  20.660  1.00 35.26           C  
ANISOU 3133  CA  LYS A 378     4554   4380   4463     23    -22   -358       C  
ATOM   3134  C   LYS A 378     -25.985  -9.031  22.076  1.00 35.43           C  
ANISOU 3134  C   LYS A 378     4545   4411   4505     18     10   -340       C  
ATOM   3135  O   LYS A 378     -26.196  -8.124  22.889  1.00 35.87           O  
ANISOU 3135  O   LYS A 378     4589   4475   4564     22     12   -328       O  
ATOM   3136  CB  LYS A 378     -25.471  -8.472  19.674  1.00 38.58           C  
ANISOU 3136  CB  LYS A 378     5025   4797   4837     20     -9   -358       C  
ATOM   3137  CG  LYS A 378     -25.950  -8.446  18.229  1.00 37.41           C  
ANISOU 3137  CG  LYS A 378     4924   4634   4657     22    -42   -375       C  
ATOM   3138  CD  LYS A 378     -24.836  -8.027  17.289  1.00 42.09           C  
ANISOU 3138  CD  LYS A 378     5573   5220   5199     12    -15   -376       C  
ATOM   3139  CE  LYS A 378     -25.231  -8.232  15.823  1.00 45.07           C  
ANISOU 3139  CE  LYS A 378     6010   5578   5536     10    -44   -394       C  
ATOM   3140  NZ  LYS A 378     -24.033  -8.186  14.926  1.00 44.13           N  
ANISOU 3140  NZ  LYS A 378     5945   5452   5371     -8     -1   -402       N  
ATOM   3141  N   VAL A 379     -25.293 -10.127  22.368  1.00 34.26           N  
ANISOU 3141  N   VAL A 379     4387   4259   4372     11     31   -340       N  
ATOM   3142  CA  VAL A 379     -24.823 -10.416  23.714  1.00 34.73           C  
ANISOU 3142  CA  VAL A 379     4425   4320   4451      6     52   -324       C  
ATOM   3143  C   VAL A 379     -23.300 -10.435  23.773  1.00 34.47           C  
ANISOU 3143  C   VAL A 379     4401   4285   4411      7     73   -320       C  
ATOM   3144  O   VAL A 379     -22.655 -11.093  22.954  1.00 35.06           O  
ANISOU 3144  O   VAL A 379     4484   4351   4484      5     79   -335       O  
ATOM   3145  CB  VAL A 379     -25.402 -11.754  24.226  1.00 36.10           C  
ANISOU 3145  CB  VAL A 379     4577   4482   4656     -3     52   -328       C  
ATOM   3146  CG1 VAL A 379     -24.885 -12.065  25.611  1.00 36.40           C  
ANISOU 3146  CG1 VAL A 379     4609   4515   4707     -9     68   -309       C  
ATOM   3147  CG2 VAL A 379     -26.923 -11.698  24.239  1.00 37.41           C  
ANISOU 3147  CG2 VAL A 379     4725   4649   4841     -5     36   -338       C  
ATOM   3148  N   ILE A 380     -22.737  -9.710  24.744  1.00 32.63           N  
ANISOU 3148  N   ILE A 380     4164   4057   4177      9     83   -304       N  
ATOM   3149  CA  ILE A 380     -21.284  -9.607  24.899  1.00 31.65           C  
ANISOU 3149  CA  ILE A 380     4042   3928   4056     11     99   -305       C  
ATOM   3150  C   ILE A 380     -20.694 -10.890  25.486  1.00 31.71           C  
ANISOU 3150  C   ILE A 380     4036   3919   4094     10     97   -308       C  
ATOM   3151  O   ILE A 380     -21.336 -11.545  26.302  1.00 31.82           O  
ANISOU 3151  O   ILE A 380     4044   3925   4120      7     88   -297       O  
ATOM   3152  CB  ILE A 380     -20.872  -8.378  25.775  1.00 30.78           C  
ANISOU 3152  CB  ILE A 380     3932   3826   3939     15    103   -288       C  
ATOM   3153  CG1 ILE A 380     -21.217  -8.597  27.249  1.00 27.43           C  
ANISOU 3153  CG1 ILE A 380     3497   3397   3527     15     96   -271       C  
ATOM   3154  CG2 ILE A 380     -21.514  -7.079  25.240  1.00 34.67           C  
ANISOU 3154  CG2 ILE A 380     4440   4332   4403     17     99   -285       C  
ATOM   3155  CD1 ILE A 380     -21.012  -7.372  28.114  1.00 26.43           C  
ANISOU 3155  CD1 ILE A 380     3373   3278   3389     20     98   -256       C  
ATOM   3156  N   PRO A 381     -19.464 -11.252  25.081  1.00 32.84           N  
ANISOU 3156  N   PRO A 381     4174   4051   4252     12    108   -325       N  
ATOM   3157  CA  PRO A 381     -18.855 -12.458  25.670  1.00 33.63           C  
ANISOU 3157  CA  PRO A 381     4261   4129   4386     15     97   -330       C  
ATOM   3158  C   PRO A 381     -18.399 -12.214  27.103  1.00 33.75           C  
ANISOU 3158  C   PRO A 381     4275   4135   4414     21     83   -311       C  
ATOM   3159  O   PRO A 381     -18.195 -11.060  27.497  1.00 35.32           O  
ANISOU 3159  O   PRO A 381     4476   4344   4599     24     88   -301       O  
ATOM   3160  CB  PRO A 381     -17.647 -12.721  24.766  1.00 31.83           C  
ANISOU 3160  CB  PRO A 381     4025   3893   4178     16    114   -361       C  
ATOM   3161  CG  PRO A 381     -17.260 -11.375  24.239  1.00 33.38           C  
ANISOU 3161  CG  PRO A 381     4229   4103   4349     13    138   -364       C  
ATOM   3162  CD  PRO A 381     -18.523 -10.519  24.213  1.00 32.68           C  
ANISOU 3162  CD  PRO A 381     4160   4034   4222     10    131   -341       C  
ATOM   3163  N   GLN A 382     -18.255 -13.287  27.876  1.00 34.62           N  
ANISOU 3163  N   GLN A 382     4387   4221   4547     23     63   -307       N  
ATOM   3164  CA  GLN A 382     -17.684 -13.202  29.220  1.00 36.68           C  
ANISOU 3164  CA  GLN A 382     4656   4463   4816     30     41   -291       C  
ATOM   3165  C   GLN A 382     -16.221 -12.816  29.138  1.00 37.89           C  
ANISOU 3165  C   GLN A 382     4791   4607   4999     43     36   -312       C  
ATOM   3166  O   GLN A 382     -15.510 -13.242  28.226  1.00 40.39           O  
ANISOU 3166  O   GLN A 382     5087   4917   5342     46     46   -341       O  
ATOM   3167  CB  GLN A 382     -17.809 -14.550  29.931  1.00 39.59           C  
ANISOU 3167  CB  GLN A 382     5041   4800   5201     28     15   -283       C  
ATOM   3168  CG  GLN A 382     -17.329 -14.582  31.384  1.00 38.93           C  
ANISOU 3168  CG  GLN A 382     4984   4690   5119     34    -15   -265       C  
ATOM   3169  CD  GLN A 382     -17.635 -15.902  32.079  1.00 42.10           C  
ANISOU 3169  CD  GLN A 382     5416   5057   5525     27    -40   -252       C  
ATOM   3170  OE1 GLN A 382     -17.509 -16.980  31.489  1.00 41.48           O  
ANISOU 3170  OE1 GLN A 382     5328   4962   5472     28    -48   -268       O  
ATOM   3171  NE2 GLN A 382     -18.040 -15.822  33.346  1.00 44.74           N  
ANISOU 3171  NE2 GLN A 382     5792   5376   5832     18    -50   -224       N  
ATOM   3172  N   GLY A 383     -15.767 -12.020  30.096  1.00 38.47           N  
ANISOU 3172  N   GLY A 383     4871   4676   5070     50     23   -299       N  
ATOM   3173  CA  GLY A 383     -14.343 -11.742  30.238  1.00 39.21           C  
ANISOU 3173  CA  GLY A 383     4943   4753   5202     64     11   -321       C  
ATOM   3174  C   GLY A 383     -13.584 -12.994  30.649  1.00 41.26           C  
ANISOU 3174  C   GLY A 383     5197   4972   5506     76    -28   -337       C  
ATOM   3175  O   GLY A 383     -14.036 -13.751  31.513  1.00 40.05           O  
ANISOU 3175  O   GLY A 383     5075   4799   5345     77    -58   -315       O  
ATOM   3176  N   ARG A 384     -12.433 -13.209  30.016  1.00 42.44           N  
ANISOU 3176  N   ARG A 384     5310   5109   5707     85    -25   -376       N  
ATOM   3177  CA  ARG A 384     -11.594 -14.374  30.269  1.00 44.67           C  
ANISOU 3177  CA  ARG A 384     5578   5349   6044    101    -65   -401       C  
ATOM   3178  C   ARG A 384     -10.240 -13.980  30.864  1.00 44.33           C  
ANISOU 3178  C   ARG A 384     5509   5278   6055    120    -97   -426       C  
ATOM   3179  O   ARG A 384      -9.847 -12.808  30.830  1.00 43.17           O  
ANISOU 3179  O   ARG A 384     5347   5148   5907    118    -76   -431       O  
ATOM   3180  CB  ARG A 384     -11.393 -15.166  28.980  1.00 46.40           C  
ANISOU 3180  CB  ARG A 384     5770   5569   6291     96    -37   -437       C  
ATOM   3181  CG  ARG A 384     -12.514 -16.133  28.672  1.00 54.09           C  
ANISOU 3181  CG  ARG A 384     6769   6548   7236     85    -35   -419       C  
ATOM   3182  CD  ARG A 384     -12.382 -16.704  27.260  1.00 63.52           C  
ANISOU 3182  CD  ARG A 384     7939   7749   8447     79      1   -455       C  
ATOM   3183  NE  ARG A 384     -13.141 -17.948  27.073  1.00 71.85           N  
ANISOU 3183  NE  ARG A 384     9010   8793   9497     75    -13   -448       N  
ATOM   3184  CZ  ARG A 384     -14.465 -18.026  26.913  1.00 74.83           C  
ANISOU 3184  CZ  ARG A 384     9415   9191   9827     60     -1   -420       C  
ATOM   3185  NH1 ARG A 384     -15.220 -16.930  26.927  1.00 75.50           N  
ANISOU 3185  NH1 ARG A 384     9514   9309   9865     50     21   -395       N  
ATOM   3186  NH2 ARG A 384     -15.043 -19.210  26.748  1.00 75.39           N  
ANISOU 3186  NH2 ARG A 384     9496   9248   9903     56    -14   -419       N  
ATOM   3187  N   SER A 385      -9.540 -14.970  31.411  1.00 43.04           N  
ANISOU 3187  N   SER A 385     5342   5070   5943    139   -152   -443       N  
ATOM   3188  CA  SER A 385      -8.229 -14.761  32.008  1.00 43.32           C  
ANISOU 3188  CA  SER A 385     5348   5069   6042    161   -197   -474       C  
ATOM   3189  C   SER A 385      -7.138 -14.942  30.953  1.00 40.53           C  
ANISOU 3189  C   SER A 385     4927   4708   5764    165   -169   -537       C  
ATOM   3190  O   SER A 385      -7.186 -15.880  30.157  1.00 37.36           O  
ANISOU 3190  O   SER A 385     4510   4302   5382    162   -153   -560       O  
ATOM   3191  CB  SER A 385      -8.021 -15.742  33.171  1.00 44.32           C  
ANISOU 3191  CB  SER A 385     5510   5141   6186    182   -281   -462       C  
ATOM   3192  OG  SER A 385      -7.123 -15.208  34.132  1.00 46.89           O  
ANISOU 3192  OG  SER A 385     5834   5436   6545    203   -335   -471       O  
ATOM   3193  N   HIS A 386      -6.154 -14.046  30.941  1.00 41.00           N  
ANISOU 3193  N   HIS A 386     4945   4765   5868    170   -159   -569       N  
ATOM   3194  CA  HIS A 386      -5.048 -14.173  29.984  1.00 40.44           C  
ANISOU 3194  CA  HIS A 386     4806   4683   5877    170   -124   -637       C  
ATOM   3195  C   HIS A 386      -3.711 -13.890  30.634  1.00 40.74           C  
ANISOU 3195  C   HIS A 386     4796   4680   6002    193   -171   -681       C  
ATOM   3196  O   HIS A 386      -3.607 -12.977  31.459  1.00 41.75           O  
ANISOU 3196  O   HIS A 386     4938   4808   6116    199   -195   -660       O  
ATOM   3197  CB  HIS A 386      -5.227 -13.251  28.769  1.00 39.02           C  
ANISOU 3197  CB  HIS A 386     4613   4548   5664    139    -30   -647       C  
ATOM   3198  CG  HIS A 386      -6.576 -13.340  28.131  1.00 37.13           C  
ANISOU 3198  CG  HIS A 386     4422   4348   5338    118      9   -605       C  
ATOM   3199  ND1 HIS A 386      -6.959 -14.405  27.345  1.00 39.88           N  
ANISOU 3199  ND1 HIS A 386     4773   4696   5682    113     24   -616       N  
ATOM   3200  CD2 HIS A 386      -7.636 -12.498  28.168  1.00 37.15           C  
ANISOU 3200  CD2 HIS A 386     4469   4389   5259    103     31   -555       C  
ATOM   3201  CE1 HIS A 386      -8.198 -14.217  26.926  1.00 40.50           C  
ANISOU 3201  CE1 HIS A 386     4896   4810   5683     95     52   -575       C  
ATOM   3202  NE2 HIS A 386      -8.632 -13.067  27.411  1.00 39.76           N  
ANISOU 3202  NE2 HIS A 386     4825   4739   5542     90     56   -539       N  
ATOM   3203  N   PRO A 387      -2.679 -14.678  30.265  1.00 40.57           N  
ANISOU 3203  N   PRO A 387     4717   4621   6077    207   -185   -746       N  
ATOM   3204  CA  PRO A 387      -1.314 -14.335  30.643  1.00 39.14           C  
ANISOU 3204  CA  PRO A 387     4473   4401   5997    227   -217   -803       C  
ATOM   3205  C   PRO A 387      -0.864 -13.112  29.849  1.00 39.32           C  
ANISOU 3205  C   PRO A 387     4454   4456   6030    199   -128   -833       C  
ATOM   3206  O   PRO A 387      -1.182 -12.998  28.665  1.00 36.98           O  
ANISOU 3206  O   PRO A 387     4155   4194   5703    169    -40   -841       O  
ATOM   3207  CB  PRO A 387      -0.506 -15.575  30.234  1.00 38.98           C  
ANISOU 3207  CB  PRO A 387     4398   4337   6075    245   -240   -869       C  
ATOM   3208  CG  PRO A 387      -1.313 -16.230  29.162  1.00 38.33           C  
ANISOU 3208  CG  PRO A 387     4336   4286   5941    222   -177   -858       C  
ATOM   3209  CD  PRO A 387      -2.750 -15.949  29.517  1.00 40.45           C  
ANISOU 3209  CD  PRO A 387     4688   4593   6087    208   -175   -772       C  
ATOM   3210  N   VAL A 388      -0.154 -12.207  30.518  1.00 40.09           N  
ANISOU 3210  N   VAL A 388     4527   4538   6168    209   -153   -847       N  
ATOM   3211  CA  VAL A 388       0.419 -11.019  29.893  1.00 40.77           C  
ANISOU 3211  CA  VAL A 388     4571   4645   6276    183    -75   -879       C  
ATOM   3212  C   VAL A 388       1.524 -11.459  28.942  1.00 43.60           C  
ANISOU 3212  C   VAL A 388     4847   4980   6740    175    -24   -968       C  
ATOM   3213  O   VAL A 388       2.412 -12.217  29.331  1.00 47.14           O  
ANISOU 3213  O   VAL A 388     5242   5378   7292    204    -86  -1022       O  
ATOM   3214  CB  VAL A 388       0.965 -10.026  30.967  1.00 40.13           C  
ANISOU 3214  CB  VAL A 388     4479   4545   6222    199   -127   -877       C  
ATOM   3215  CG1 VAL A 388       1.815  -8.917  30.334  1.00 39.14           C  
ANISOU 3215  CG1 VAL A 388     4295   4428   6148    173    -50   -927       C  
ATOM   3216  CG2 VAL A 388      -0.187  -9.421  31.773  1.00 36.00           C  
ANISOU 3216  CG2 VAL A 388     4040   4053   5586    199   -154   -791       C  
ATOM   3217  N   GLN A 389       1.441 -11.006  27.693  1.00 44.25           N  
ANISOU 3217  N   GLN A 389     4922   5095   6795    134     86   -985       N  
ATOM   3218  CA  GLN A 389       2.402 -11.378  26.643  1.00 45.24           C  
ANISOU 3218  CA  GLN A 389     4977   5204   7009    116    157  -1072       C  
ATOM   3219  C   GLN A 389       2.878 -10.145  25.861  1.00 43.11           C  
ANISOU 3219  C   GLN A 389     4686   4953   6741     73    263  -1101       C  
ATOM   3220  O   GLN A 389       2.062  -9.310  25.464  1.00 40.17           O  
ANISOU 3220  O   GLN A 389     4377   4622   6264     45    314  -1047       O  
ATOM   3221  CB  GLN A 389       1.769 -12.368  25.661  1.00 46.41           C  
ANISOU 3221  CB  GLN A 389     5152   5368   7113    103    199  -1069       C  
ATOM   3222  CG  GLN A 389       1.668 -13.810  26.132  1.00 53.60           C  
ANISOU 3222  CG  GLN A 389     6059   6246   8060    140    113  -1072       C  
ATOM   3223  CD  GLN A 389       1.220 -14.755  25.011  1.00 59.46           C  
ANISOU 3223  CD  GLN A 389     6815   7001   8774    123    167  -1085       C  
ATOM   3224  OE1 GLN A 389       0.084 -14.672  24.512  1.00 57.42           O  
ANISOU 3224  OE1 GLN A 389     6625   6784   8406    103    201  -1028       O  
ATOM   3225  NE2 GLN A 389       2.118 -15.657  24.606  1.00 58.34           N  
ANISOU 3225  NE2 GLN A 389     6607   6823   8738    133    171  -1164       N  
ATOM   3226  N   PRO A 390       4.197 -10.030  25.622  1.00 39.90           N  
ANISOU 3226  N   PRO A 390     5507   4661   4993   -234   -650    190       N  
ATOM   3227  CA  PRO A 390       4.677  -8.883  24.843  1.00 38.97           C  
ANISOU 3227  CA  PRO A 390     5371   4586   4850   -199   -582    141       C  
ATOM   3228  C   PRO A 390       4.271  -8.998  23.378  1.00 36.51           C  
ANISOU 3228  C   PRO A 390     5015   4292   4567   -135   -525     73       C  
ATOM   3229  O   PRO A 390       4.030 -10.097  22.891  1.00 38.62           O  
ANISOU 3229  O   PRO A 390     5247   4527   4900   -107   -552     57       O  
ATOM   3230  CB  PRO A 390       6.206  -8.969  24.981  1.00 39.02           C  
ANISOU 3230  CB  PRO A 390     5336   4565   4924   -194   -643    149       C  
ATOM   3231  CG  PRO A 390       6.456  -9.907  26.127  1.00 41.60           C  
ANISOU 3231  CG  PRO A 390     5679   4839   5289   -244   -744    218       C  
ATOM   3232  CD  PRO A 390       5.310 -10.874  26.094  1.00 40.05           C  
ANISOU 3232  CD  PRO A 390     5493   4624   5101   -245   -751    225       C  
ATOM   3233  N   TYR A 391       4.182  -7.870  22.687  1.00 35.50           N  
ANISOU 3233  N   TYR A 391     4889   4213   4387   -116   -451     36       N  
ATOM   3234  CA  TYR A 391       3.882  -7.870  21.253  1.00 33.86           C  
ANISOU 3234  CA  TYR A 391     4643   4027   4197    -64   -399    -25       C  
ATOM   3235  C   TYR A 391       4.480  -6.634  20.579  1.00 34.21           C  
ANISOU 3235  C   TYR A 391     4676   4116   4205    -50   -344    -58       C  
ATOM   3236  O   TYR A 391       4.728  -5.643  21.255  1.00 33.15           O  
ANISOU 3236  O   TYR A 391     4576   4001   4018    -80   -333    -32       O  
ATOM   3237  CB  TYR A 391       2.373  -7.992  20.997  1.00 31.71           C  
ANISOU 3237  CB  TYR A 391     4397   3765   3885    -64   -361    -27       C  
ATOM   3238  CG  TYR A 391       1.516  -6.809  21.408  1.00 32.28           C  
ANISOU 3238  CG  TYR A 391     4521   3872   3870    -93   -304     -9       C  
ATOM   3239  CD1 TYR A 391       1.119  -6.631  22.736  1.00 34.17           C  
ANISOU 3239  CD1 TYR A 391     4813   4105   4065   -145   -315     39       C  
ATOM   3240  CD2 TYR A 391       1.073  -5.884  20.457  1.00 29.90           C  
ANISOU 3240  CD2 TYR A 391     4216   3610   3535    -72   -240    -43       C  
ATOM   3241  CE1 TYR A 391       0.310  -5.555  23.107  1.00 33.44           C  
ANISOU 3241  CE1 TYR A 391     4763   4041   3903   -171   -256     45       C  
ATOM   3242  CE2 TYR A 391       0.273  -4.815  20.816  1.00 28.18           C  
ANISOU 3242  CE2 TYR A 391     4037   3415   3254    -95   -190    -30       C  
ATOM   3243  CZ  TYR A 391      -0.113  -4.657  22.140  1.00 30.30           C  
ANISOU 3243  CZ  TYR A 391     4353   3674   3487   -142   -194     10       C  
ATOM   3244  OH  TYR A 391      -0.905  -3.588  22.497  1.00 31.37           O  
ANISOU 3244  OH  TYR A 391     4521   3829   3570   -165   -138     13       O  
ATOM   3245  N   PRO A 392       4.718  -6.697  19.250  1.00 34.55           N  
ANISOU 3245  N   PRO A 392     4674   4177   4275    -10   -311   -116       N  
ATOM   3246  CA  PRO A 392       5.417  -5.614  18.556  1.00 34.33           C  
ANISOU 3246  CA  PRO A 392     4631   4193   4221     -1   -266   -147       C  
ATOM   3247  C   PRO A 392       4.553  -4.388  18.273  1.00 33.47           C  
ANISOU 3247  C   PRO A 392     4562   4129   4028    -13   -206   -143       C  
ATOM   3248  O   PRO A 392       3.340  -4.511  18.092  1.00 32.05           O  
ANISOU 3248  O   PRO A 392     4403   3950   3823    -13   -186   -139       O  
ATOM   3249  CB  PRO A 392       5.852  -6.266  17.241  1.00 33.91           C  
ANISOU 3249  CB  PRO A 392     4519   4143   4224     36   -252   -212       C  
ATOM   3250  CG  PRO A 392       4.816  -7.296  16.982  1.00 34.52           C  
ANISOU 3250  CG  PRO A 392     4598   4196   4321     48   -262   -220       C  
ATOM   3251  CD  PRO A 392       4.385  -7.808  18.338  1.00 34.94           C  
ANISOU 3251  CD  PRO A 392     4686   4209   4382     23   -316   -158       C  
ATOM   3252  N   GLY A 393       5.202  -3.223  18.225  1.00 33.01           N  
ANISOU 3252  N   GLY A 393     4508   4101   3933    -22   -181   -143       N  
ATOM   3253  CA  GLY A 393       4.530  -1.956  17.970  1.00 30.83           C  
ANISOU 3253  CA  GLY A 393     4264   3861   3589    -34   -129   -138       C  
ATOM   3254  C   GLY A 393       4.953  -1.290  16.673  1.00 30.69           C  
ANISOU 3254  C   GLY A 393     4218   3884   3558    -20    -91   -176       C  
ATOM   3255  O   GLY A 393       5.030  -1.933  15.624  1.00 29.43           O  
ANISOU 3255  O   GLY A 393     4023   3732   3425      0    -84   -217       O  
ATOM   3256  N   ALA A 394       5.238   0.006  16.751  1.00 30.54           N  
ANISOU 3256  N   ALA A 394     4216   3893   3496    -37    -67   -164       N  
ATOM   3257  CA  ALA A 394       5.474   0.811  15.562  1.00 31.49           C  
ANISOU 3257  CA  ALA A 394     4319   4054   3590    -34    -30   -190       C  
ATOM   3258  C   ALA A 394       6.885   0.655  15.003  1.00 32.76           C  
ANISOU 3258  C   ALA A 394     4435   4233   3781    -26    -32   -224       C  
ATOM   3259  O   ALA A 394       7.780   0.116  15.668  1.00 32.98           O  
ANISOU 3259  O   ALA A 394     4442   4235   3853    -22    -65   -222       O  
ATOM   3260  CB  ALA A 394       5.181   2.276  15.855  1.00 31.48           C  
ANISOU 3260  CB  ALA A 394     4352   4071   3538    -56     -6   -162       C  
ATOM   3261  N   PHE A 395       7.064   1.130  13.773  1.00 31.76           N  
ANISOU 3261  N   PHE A 395     4290   4148   3630    -29      2   -255       N  
ATOM   3262  CA  PHE A 395       8.370   1.190  13.148  1.00 33.88           C  
ANISOU 3262  CA  PHE A 395     4514   4441   3917    -28     14   -292       C  
ATOM   3263  C   PHE A 395       8.962   2.578  13.316  1.00 34.33           C  
ANISOU 3263  C   PHE A 395     4584   4525   3933    -51     27   -268       C  
ATOM   3264  O   PHE A 395       8.266   3.587  13.131  1.00 32.90           O  
ANISOU 3264  O   PHE A 395     4437   4364   3701    -68     44   -243       O  
ATOM   3265  CB  PHE A 395       8.290   0.848  11.657  1.00 33.64           C  
ANISOU 3265  CB  PHE A 395     4458   4446   3878    -29     48   -346       C  
ATOM   3266  CG  PHE A 395       9.605   0.967  10.943  1.00 34.28           C  
ANISOU 3266  CG  PHE A 395     4492   4559   3973    -35     73   -391       C  
ATOM   3267  CD1 PHE A 395      10.564  -0.034  11.058  1.00 34.88           C  
ANISOU 3267  CD1 PHE A 395     4516   4610   4127    -14     62   -432       C  
ATOM   3268  CD2 PHE A 395       9.890   2.088  10.163  1.00 38.06           C  
ANISOU 3268  CD2 PHE A 395     4977   5090   4393    -65    107   -393       C  
ATOM   3269  CE1 PHE A 395      11.792   0.077  10.405  1.00 36.21           C  
ANISOU 3269  CE1 PHE A 395     4634   4806   4317    -20     92   -480       C  
ATOM   3270  CE2 PHE A 395      11.117   2.211   9.504  1.00 36.56           C  
ANISOU 3270  CE2 PHE A 395     4742   4933   4214    -76    135   -437       C  
ATOM   3271  CZ  PHE A 395      12.070   1.203   9.630  1.00 35.23           C  
ANISOU 3271  CZ  PHE A 395     4519   4741   4127    -53    131   -483       C  
ATOM   3272  N   VAL A 396      10.248   2.610  13.668  1.00 33.43           N  
ANISOU 3272  N   VAL A 396     4440   4409   3853    -50     15   -275       N  
ATOM   3273  CA  VAL A 396      11.025   3.850  13.742  1.00 33.30           C  
ANISOU 3273  CA  VAL A 396     4426   4419   3806    -72     25   -258       C  
ATOM   3274  C   VAL A 396      12.288   3.713  12.870  1.00 35.46           C  
ANISOU 3274  C   VAL A 396     4643   4723   4109    -72     46   -305       C  
ATOM   3275  O   VAL A 396      13.070   2.761  13.026  1.00 35.03           O  
ANISOU 3275  O   VAL A 396     4542   4644   4125    -53     30   -333       O  
ATOM   3276  CB  VAL A 396      11.406   4.224  15.208  1.00 33.27           C  
ANISOU 3276  CB  VAL A 396     4449   4383   3811    -80    -13   -211       C  
ATOM   3277  CG1 VAL A 396      11.979   5.637  15.275  1.00 29.39           C  
ANISOU 3277  CG1 VAL A 396     3971   3919   3279   -105      0   -190       C  
ATOM   3278  CG2 VAL A 396      10.192   4.110  16.142  1.00 32.11           C  
ANISOU 3278  CG2 VAL A 396     4354   4204   3643    -84    -29   -174       C  
ATOM   3279  N   LYS A 397      12.464   4.656  11.945  1.00 34.41           N  
ANISOU 3279  N   LYS A 397     4509   4640   3925    -95     83   -315       N  
ATOM   3280  CA  LYS A 397      13.613   4.656  11.041  1.00 34.09           C  
ANISOU 3280  CA  LYS A 397     4416   4637   3900   -105    114   -363       C  
ATOM   3281  C   LYS A 397      14.814   5.284  11.740  1.00 33.70           C  
ANISOU 3281  C   LYS A 397     4348   4582   3874   -112     98   -342       C  
ATOM   3282  O   LYS A 397      14.674   6.298  12.422  1.00 33.76           O  
ANISOU 3282  O   LYS A 397     4396   4587   3845   -127     81   -291       O  
ATOM   3283  CB  LYS A 397      13.287   5.428   9.758  1.00 33.63           C  
ANISOU 3283  CB  LYS A 397     4371   4638   3769   -139    157   -375       C  
ATOM   3284  CG  LYS A 397      14.420   5.459   8.729  1.00 37.19           C  
ANISOU 3284  CG  LYS A 397     4771   5136   4222   -161    199   -430       C  
ATOM   3285  CD  LYS A 397      14.070   6.320   7.513  1.00 36.03           C  
ANISOU 3285  CD  LYS A 397     4647   5051   3991   -208    234   -430       C  
ATOM   3286  CE  LYS A 397      15.267   6.490   6.574  1.00 37.20           C  
ANISOU 3286  CE  LYS A 397     4749   5254   4133   -240    281   -481       C  
ATOM   3287  NZ  LYS A 397      15.647   5.218   5.905  1.00 40.60           N  
ANISOU 3287  NZ  LYS A 397     5129   5689   4608   -230    317   -565       N  
ATOM   3288  N   GLU A 398      15.979   4.667  11.568  1.00 31.24           N  
ANISOU 3288  N   GLU A 398     3973   4266   3629   -102    102   -384       N  
ATOM   3289  CA  GLU A 398      17.243   5.213  12.043  1.00 34.64           C  
ANISOU 3289  CA  GLU A 398     4373   4696   4091   -110     89   -371       C  
ATOM   3290  C   GLU A 398      17.670   6.401  11.166  1.00 33.38           C  
ANISOU 3290  C   GLU A 398     4213   4599   3870   -147    133   -376       C  
ATOM   3291  O   GLU A 398      18.021   6.222   9.996  1.00 36.68           O  
ANISOU 3291  O   GLU A 398     4594   5060   4282   -160    182   -431       O  
ATOM   3292  CB  GLU A 398      18.329   4.119  12.050  1.00 34.17           C  
ANISOU 3292  CB  GLU A 398     4235   4607   4139    -87     82   -419       C  
ATOM   3293  CG  GLU A 398      19.605   4.481  12.835  1.00 37.64           C  
ANISOU 3293  CG  GLU A 398     4641   5026   4635    -91     47   -394       C  
ATOM   3294  CD  GLU A 398      19.417   4.462  14.359  1.00 40.15           C  
ANISOU 3294  CD  GLU A 398     5000   5288   4968    -86    -27   -324       C  
ATOM   3295  OE1 GLU A 398      19.188   3.371  14.933  1.00 39.44           O  
ANISOU 3295  OE1 GLU A 398     4901   5146   4939    -64    -69   -321       O  
ATOM   3296  OE2 GLU A 398      19.513   5.541  14.988  1.00 40.33           O  
ANISOU 3296  OE2 GLU A 398     5066   5319   4941   -111    -44   -273       O  
ATOM   3297  N   PRO A 399      17.639   7.623  11.716  1.00 32.29           N  
ANISOU 3297  N   PRO A 399     4118   4467   3683   -168    116   -320       N  
ATOM   3298  CA  PRO A 399      18.089   8.734  10.868  1.00 32.17           C  
ANISOU 3298  CA  PRO A 399     4100   4510   3615   -205    151   -321       C  
ATOM   3299  C   PRO A 399      19.619   8.842  10.827  1.00 35.51           C  
ANISOU 3299  C   PRO A 399     4461   4944   4087   -213    159   -343       C  
ATOM   3300  O   PRO A 399      20.296   8.441  11.775  1.00 35.50           O  
ANISOU 3300  O   PRO A 399     4435   4899   4156   -193    121   -331       O  
ATOM   3301  CB  PRO A 399      17.511   9.952  11.574  1.00 31.07           C  
ANISOU 3301  CB  PRO A 399     4023   4361   3421   -221    125   -254       C  
ATOM   3302  CG  PRO A 399      17.530   9.559  13.037  1.00 27.47           C  
ANISOU 3302  CG  PRO A 399     3583   3845   3009   -197     74   -223       C  
ATOM   3303  CD  PRO A 399      17.293   8.066  13.082  1.00 29.65           C  
ANISOU 3303  CD  PRO A 399     3833   4091   3342   -164     66   -258       C  
ATOM   3304  N   ILE A 400      20.151   9.364   9.725  1.00 37.47           N  
ANISOU 3304  N   ILE A 400     4683   5251   4301   -247    208   -372       N  
ATOM   3305  CA  ILE A 400      21.555   9.733   9.642  1.00 37.20           C  
ANISOU 3305  CA  ILE A 400     4595   5236   4304   -263    221   -386       C  
ATOM   3306  C   ILE A 400      21.722  11.051  10.403  1.00 38.22           C  
ANISOU 3306  C   ILE A 400     4765   5361   4396   -282    185   -316       C  
ATOM   3307  O   ILE A 400      21.188  12.084   9.976  1.00 38.03           O  
ANISOU 3307  O   ILE A 400     4786   5370   4293   -315    194   -285       O  
ATOM   3308  CB  ILE A 400      22.011   9.904   8.167  1.00 38.06           C  
ANISOU 3308  CB  ILE A 400     4668   5417   4377   -303    291   -442       C  
ATOM   3309  CG1 ILE A 400      21.908   8.574   7.417  1.00 37.84           C  
ANISOU 3309  CG1 ILE A 400     4597   5392   4387   -287    332   -523       C  
ATOM   3310  CG2 ILE A 400      23.446  10.456   8.092  1.00 33.57           C  
ANISOU 3310  CG2 ILE A 400     4044   4871   3839   -326    307   -451       C  
ATOM   3311  CD1 ILE A 400      21.950   8.721   5.906  1.00 44.37           C  
ANISOU 3311  CD1 ILE A 400     5415   6295   5150   -337    403   -577       C  
ATOM   3312  N   PRO A 401      22.438  11.020  11.547  1.00 38.60           N  
ANISOU 3312  N   PRO A 401     4798   5363   4503   -266    138   -288       N  
ATOM   3313  CA  PRO A 401      22.650  12.264  12.299  1.00 37.70           C  
ANISOU 3313  CA  PRO A 401     4724   5243   4356   -288    104   -225       C  
ATOM   3314  C   PRO A 401      23.272  13.321  11.398  1.00 37.58           C  
ANISOU 3314  C   PRO A 401     4694   5288   4297   -331    141   -227       C  
ATOM   3315  O   PRO A 401      24.306  13.078  10.766  1.00 38.27           O  
ANISOU 3315  O   PRO A 401     4714   5404   4422   -341    174   -269       O  
ATOM   3316  CB  PRO A 401      23.629  11.859  13.406  1.00 37.19           C  
ANISOU 3316  CB  PRO A 401     4626   5129   4374   -272     54   -210       C  
ATOM   3317  CG  PRO A 401      23.491  10.381  13.534  1.00 40.36           C  
ANISOU 3317  CG  PRO A 401     4993   5494   4848   -234     45   -246       C  
ATOM   3318  CD  PRO A 401      23.109   9.867  12.174  1.00 39.87           C  
ANISOU 3318  CD  PRO A 401     4905   5474   4769   -232    109   -310       C  
ATOM   3319  N   ASN A 402      22.626  14.479  11.335  1.00 37.19           N  
ANISOU 3319  N   ASN A 402     4703   5255   4171   -357    135   -183       N  
ATOM   3320  CA  ASN A 402      23.039  15.557  10.455  1.00 37.93           C  
ANISOU 3320  CA  ASN A 402     4793   5405   4214   -405    163   -174       C  
ATOM   3321  C   ASN A 402      22.169  16.780  10.668  1.00 36.22           C  
ANISOU 3321  C   ASN A 402     4646   5183   3933   -426    139   -117       C  
ATOM   3322  O   ASN A 402      21.125  16.697  11.308  1.00 35.50           O  
ANISOU 3322  O   ASN A 402     4603   5052   3834   -403    115    -95       O  
ATOM   3323  CB  ASN A 402      22.924  15.119   8.989  1.00 39.10           C  
ANISOU 3323  CB  ASN A 402     4913   5611   4332   -427    222   -227       C  
ATOM   3324  CG  ASN A 402      23.988  15.749   8.100  1.00 42.82           C  
ANISOU 3324  CG  ASN A 402     5344   6143   4784   -476    261   -243       C  
ATOM   3325  OD1 ASN A 402      24.573  16.786   8.432  1.00 42.97           O  
ANISOU 3325  OD1 ASN A 402     5369   6167   4793   -500    240   -201       O  
ATOM   3326  ND2 ASN A 402      24.237  15.123   6.953  1.00 42.00           N  
ANISOU 3326  ND2 ASN A 402     5199   6088   4672   -497    320   -306       N  
ATOM   3327  N   ARG A 403      22.619  17.913  10.143  1.00 36.20           N  
ANISOU 3327  N   ARG A 403     4645   5219   3891   -470    147    -93       N  
ATOM   3328  CA  ARG A 403      21.744  19.043   9.891  1.00 37.65           C  
ANISOU 3328  CA  ARG A 403     4883   5407   4014   -498    133    -47       C  
ATOM   3329  C   ARG A 403      20.893  18.726   8.661  1.00 37.88           C  
ANISOU 3329  C   ARG A 403     4919   5474   3998   -517    163    -66       C  
ATOM   3330  O   ARG A 403      21.323  17.973   7.780  1.00 38.65           O  
ANISOU 3330  O   ARG A 403     4976   5614   4094   -528    205   -116       O  
ATOM   3331  CB  ARG A 403      22.555  20.321   9.651  1.00 37.49           C  
ANISOU 3331  CB  ARG A 403     4858   5416   3971   -545    126    -13       C  
ATOM   3332  CG  ARG A 403      23.486  20.268   8.437  1.00 39.22           C  
ANISOU 3332  CG  ARG A 403     5025   5704   4171   -588    171    -44       C  
ATOM   3333  CD  ARG A 403      24.223  21.579   8.249  1.00 41.12           C  
ANISOU 3333  CD  ARG A 403     5266   5972   4387   -638    160     -3       C  
ATOM   3334  NE  ARG A 403      25.340  21.727   9.174  1.00 42.32           N  
ANISOU 3334  NE  ARG A 403     5389   6099   4591   -624    140      4       N  
ATOM   3335  CZ  ARG A 403      26.189  22.755   9.171  1.00 45.61           C  
ANISOU 3335  CZ  ARG A 403     5797   6534   5001   -662    128     36       C  
ATOM   3336  NH1 ARG A 403      26.049  23.743   8.294  1.00 44.26           N  
ANISOU 3336  NH1 ARG A 403     5643   6404   4771   -717    133     66       N  
ATOM   3337  NH2 ARG A 403      27.183  22.799  10.048  1.00 42.96           N  
ANISOU 3337  NH2 ARG A 403     5434   6172   4718   -648    106     42       N  
ATOM   3338  N   TYR A 404      19.687  19.292   8.620  1.00 37.24           N  
ANISOU 3338  N   TYR A 404     4890   5374   3885   -522    142    -30       N  
ATOM   3339  CA  TYR A 404      18.795  19.178   7.464  1.00 34.89           C  
ANISOU 3339  CA  TYR A 404     4607   5108   3541   -549    158    -33       C  
ATOM   3340  C   TYR A 404      18.128  20.532   7.221  1.00 35.98           C  
ANISOU 3340  C   TYR A 404     4785   5240   3644   -586    125     28       C  
ATOM   3341  O   TYR A 404      17.360  21.019   8.067  1.00 32.53           O  
ANISOU 3341  O   TYR A 404     4383   4748   3229   -561     93     61       O  
ATOM   3342  CB  TYR A 404      17.756  18.070   7.681  1.00 32.78           C  
ANISOU 3342  CB  TYR A 404     4353   4810   3293   -504    160    -58       C  
ATOM   3343  CG  TYR A 404      18.361  16.680   7.736  1.00 32.43           C  
ANISOU 3343  CG  TYR A 404     4264   4770   3288   -472    189   -121       C  
ATOM   3344  CD1 TYR A 404      18.588  15.949   6.561  1.00 30.57           C  
ANISOU 3344  CD1 TYR A 404     3997   4586   3032   -495    232   -172       C  
ATOM   3345  CD2 TYR A 404      18.719  16.100   8.961  1.00 25.66           C  
ANISOU 3345  CD2 TYR A 404     3395   3863   2490   -425    171   -129       C  
ATOM   3346  CE1 TYR A 404      19.141  14.672   6.604  1.00 29.61           C  
ANISOU 3346  CE1 TYR A 404     3830   4462   2960   -463    260   -235       C  
ATOM   3347  CE2 TYR A 404      19.284  14.826   9.016  1.00 28.62           C  
ANISOU 3347  CE2 TYR A 404     3724   4234   2915   -395    190   -182       C  
ATOM   3348  CZ  TYR A 404      19.491  14.120   7.832  1.00 31.36           C  
ANISOU 3348  CZ  TYR A 404     4035   4628   3252   -412    236   -238       C  
ATOM   3349  OH  TYR A 404      20.047  12.867   7.872  1.00 30.65           O  
ANISOU 3349  OH  TYR A 404     3894   4528   3224   -381    255   -296       O  
ATOM   3350  N   LYS A 405      18.437  21.130   6.067  1.00 35.67           N  
ANISOU 3350  N   LYS A 405     4741   5259   3555   -648    134     42       N  
ATOM   3351  CA  LYS A 405      18.100  22.525   5.782  1.00 37.18           C  
ANISOU 3351  CA  LYS A 405     4961   5446   3719   -694     97    106       C  
ATOM   3352  C   LYS A 405      16.607  22.747   5.536  1.00 38.68           C  
ANISOU 3352  C   LYS A 405     5189   5603   3905   -694     66    140       C  
ATOM   3353  O   LYS A 405      15.964  23.510   6.264  1.00 39.50           O  
ANISOU 3353  O   LYS A 405     5318   5649   4041   -675     29    179       O  
ATOM   3354  CB  LYS A 405      18.926  23.039   4.603  1.00 37.45           C  
ANISOU 3354  CB  LYS A 405     4977   5554   3697   -769    114    114       C  
ATOM   3355  CG  LYS A 405      18.941  24.553   4.440  1.00 40.13           C  
ANISOU 3355  CG  LYS A 405     5339   5890   4020   -819     70    184       C  
ATOM   3356  CD  LYS A 405      19.907  24.947   3.321  1.00 45.55           C  
ANISOU 3356  CD  LYS A 405     6005   6657   4647   -899     92    187       C  
ATOM   3357  CE  LYS A 405      19.899  26.448   3.024  1.00 48.92           C  
ANISOU 3357  CE  LYS A 405     6454   7082   5052   -959     43    263       C  
ATOM   3358  NZ  LYS A 405      20.690  26.789   1.787  1.00 49.64           N  
ANISOU 3358  NZ  LYS A 405     6531   7258   5071  -1050     64    271       N  
ATOM   3359  N   TYR A 406      16.071  22.070   4.522  1.00 38.02           N  
ANISOU 3359  N   TYR A 406     5107   5555   3785   -717     81    123       N  
ATOM   3360  CA  TYR A 406      14.682  22.198   4.129  1.00 39.20           C  
ANISOU 3360  CA  TYR A 406     5287   5678   3931   -724     49    156       C  
ATOM   3361  C   TYR A 406      13.971  20.873   4.374  1.00 39.58           C  
ANISOU 3361  C   TYR A 406     5334   5705   4000   -672     69    110       C  
ATOM   3362  O   TYR A 406      14.366  19.839   3.834  1.00 40.04           O  
ANISOU 3362  O   TYR A 406     5373   5807   4035   -675    109     57       O  
ATOM   3363  CB  TYR A 406      14.573  22.618   2.649  1.00 39.96           C  
ANISOU 3363  CB  TYR A 406     5393   5832   3958   -810     37    185       C  
ATOM   3364  CG  TYR A 406      15.006  24.047   2.389  1.00 43.09           C  
ANISOU 3364  CG  TYR A 406     5796   6238   4337   -867      1    247       C  
ATOM   3365  CD1 TYR A 406      16.233  24.326   1.788  1.00 46.67           C  
ANISOU 3365  CD1 TYR A 406     6231   6760   4742   -923     27    238       C  
ATOM   3366  CD2 TYR A 406      14.196  25.126   2.760  1.00 42.76           C  
ANISOU 3366  CD2 TYR A 406     5776   6134   4336   -865    -58    311       C  
ATOM   3367  CE1 TYR A 406      16.643  25.638   1.549  1.00 44.92           C  
ANISOU 3367  CE1 TYR A 406     6016   6547   4504   -979     -9    298       C  
ATOM   3368  CE2 TYR A 406      14.598  26.444   2.531  1.00 42.14           C  
ANISOU 3368  CE2 TYR A 406     5702   6058   4249   -918    -96    369       C  
ATOM   3369  CZ  TYR A 406      15.823  26.689   1.925  1.00 45.88           C  
ANISOU 3369  CZ  TYR A 406     6162   6603   4667   -976    -73    365       C  
ATOM   3370  OH  TYR A 406      16.235  27.983   1.694  1.00 47.62           O  
ANISOU 3370  OH  TYR A 406     6387   6827   4879  -1031   -114    425       O  
ATOM   3371  N   VAL A 407      12.929  20.899   5.201  1.00 38.09           N  
ANISOU 3371  N   VAL A 407     5164   5449   3859   -625     45    127       N  
ATOM   3372  CA  VAL A 407      12.227  19.669   5.565  1.00 37.01           C  
ANISOU 3372  CA  VAL A 407     5028   5287   3748   -574     61     89       C  
ATOM   3373  C   VAL A 407      10.716  19.828   5.459  1.00 37.75           C  
ANISOU 3373  C   VAL A 407     5145   5336   3861   -568     28    123       C  
ATOM   3374  O   VAL A 407      10.142  20.755   6.030  1.00 38.05           O  
ANISOU 3374  O   VAL A 407     5197   5323   3937   -560     -2    163       O  
ATOM   3375  CB  VAL A 407      12.607  19.191   6.998  1.00 34.71           C  
ANISOU 3375  CB  VAL A 407     4729   4954   3505   -511     74     60       C  
ATOM   3376  CG1 VAL A 407      11.809  17.948   7.404  1.00 29.74           C  
ANISOU 3376  CG1 VAL A 407     4103   4295   2903   -462     85     28       C  
ATOM   3377  CG2 VAL A 407      14.092  18.913   7.098  1.00 32.49           C  
ANISOU 3377  CG2 VAL A 407     4417   4711   3218   -514    101     27       C  
ATOM   3378  N   MET A 408      10.085  18.916   4.722  1.00 37.80           N  
ANISOU 3378  N   MET A 408     5153   5361   3848   -573     36    103       N  
ATOM   3379  CA  MET A 408       8.630  18.778   4.737  1.00 38.14           C  
ANISOU 3379  CA  MET A 408     5212   5357   3921   -557      9    126       C  
ATOM   3380  C   MET A 408       8.245  17.463   5.387  1.00 35.80           C  
ANISOU 3380  C   MET A 408     4911   5037   3654   -498     34     78       C  
ATOM   3381  O   MET A 408       8.706  16.395   4.961  1.00 34.79           O  
ANISOU 3381  O   MET A 408     4770   4947   3500   -496     64     30       O  
ATOM   3382  CB  MET A 408       8.052  18.772   3.329  1.00 39.32           C  
ANISOU 3382  CB  MET A 408     5373   5542   4025   -617    -14    150       C  
ATOM   3383  CG  MET A 408       8.629  19.788   2.384  1.00 49.19           C  
ANISOU 3383  CG  MET A 408     6628   6838   5224   -693    -35    190       C  
ATOM   3384  SD  MET A 408       7.545  19.906   0.964  1.00 58.59           S  
ANISOU 3384  SD  MET A 408     7841   8046   6376   -765    -84    239       S  
ATOM   3385  CE  MET A 408       6.172  20.738   1.763  1.00 54.16           C  
ANISOU 3385  CE  MET A 408     7284   7383   5913   -725   -141    299       C  
ATOM   3386  N   SER A 409       7.379  17.528   6.391  1.00 33.00           N  
ANISOU 3386  N   SER A 409     4566   4618   3355   -454     23     90       N  
ATOM   3387  CA  SER A 409       6.871  16.308   7.008  1.00 33.26           C  
ANISOU 3387  CA  SER A 409     4598   4626   3415   -404     42     53       C  
ATOM   3388  C   SER A 409       5.462  15.985   6.516  1.00 36.18           C  
ANISOU 3388  C   SER A 409     4976   4971   3800   -404     22     70       C  
ATOM   3389  O   SER A 409       4.694  16.888   6.148  1.00 38.31           O  
ANISOU 3389  O   SER A 409     5252   5217   4085   -429    -12    117       O  
ATOM   3390  CB  SER A 409       6.914  16.394   8.539  1.00 29.09           C  
ANISOU 3390  CB  SER A 409     4075   4047   2930   -359     51     46       C  
ATOM   3391  OG  SER A 409       5.958  17.315   9.032  1.00 25.55           O  
ANISOU 3391  OG  SER A 409     3640   3546   2523   -355     32     81       O  
ATOM   3392  N   PHE A 410       5.150  14.689   6.492  1.00 33.90           N  
ANISOU 3392  N   PHE A 410     4683   4685   3513   -379     38     33       N  
ATOM   3393  CA  PHE A 410       3.816  14.207   6.185  1.00 32.87           C  
ANISOU 3393  CA  PHE A 410     4559   4527   3403   -372     21     44       C  
ATOM   3394  C   PHE A 410       3.328  13.259   7.286  1.00 33.31           C  
ANISOU 3394  C   PHE A 410     4614   4540   3502   -316     38     17       C  
ATOM   3395  O   PHE A 410       4.109  12.536   7.907  1.00 32.71           O  
ANISOU 3395  O   PHE A 410     4532   4473   3425   -289     61    -20       O  
ATOM   3396  CB  PHE A 410       3.788  13.527   4.820  1.00 31.03           C  
ANISOU 3396  CB  PHE A 410     4326   4344   3120   -410     18     30       C  
ATOM   3397  CG  PHE A 410       4.039  14.465   3.664  1.00 31.99           C  
ANISOU 3397  CG  PHE A 410     4456   4507   3193   -479     -6     66       C  
ATOM   3398  CD1 PHE A 410       5.333  14.858   3.332  1.00 31.04           C  
ANISOU 3398  CD1 PHE A 410     4328   4439   3026   -510     14     52       C  
ATOM   3399  CD2 PHE A 410       2.979  14.940   2.897  1.00 30.80           C  
ANISOU 3399  CD2 PHE A 410     4317   4343   3045   -517    -52    117       C  
ATOM   3400  CE1 PHE A 410       5.563  15.713   2.261  1.00 34.88           C  
ANISOU 3400  CE1 PHE A 410     4825   4967   3462   -582     -9     88       C  
ATOM   3401  CE2 PHE A 410       3.195  15.795   1.835  1.00 32.69           C  
ANISOU 3401  CE2 PHE A 410     4566   4619   3236   -589    -82    158       C  
ATOM   3402  CZ  PHE A 410       4.493  16.185   1.511  1.00 36.11           C  
ANISOU 3402  CZ  PHE A 410     4997   5109   3616   -624    -59    143       C  
ATOM   3403  N   ASP A 411       2.027  13.275   7.524  1.00 32.36           N  
ANISOU 3403  N   ASP A 411     4499   4373   3424   -302     22     39       N  
ATOM   3404  CA  ASP A 411       1.455  12.566   8.647  1.00 33.58           C  
ANISOU 3404  CA  ASP A 411     4655   4484   3619   -257     39     21       C  
ATOM   3405  C   ASP A 411       0.106  11.933   8.290  1.00 32.63           C  
ANISOU 3405  C   ASP A 411     4533   4338   3526   -249     24     29       C  
ATOM   3406  O   ASP A 411      -0.709  12.546   7.606  1.00 33.31           O  
ANISOU 3406  O   ASP A 411     4617   4410   3628   -273     -4     66       O  
ATOM   3407  CB  ASP A 411       1.278  13.537   9.816  1.00 33.78           C  
ANISOU 3407  CB  ASP A 411     4688   4464   3684   -243     46     37       C  
ATOM   3408  CG  ASP A 411       0.639  12.891  11.003  1.00 37.62           C  
ANISOU 3408  CG  ASP A 411     5180   4908   4205   -208     66     19       C  
ATOM   3409  OD1 ASP A 411      -0.576  13.096  11.211  1.00 41.26           O  
ANISOU 3409  OD1 ASP A 411     5639   5326   4712   -201     64     34       O  
ATOM   3410  OD2 ASP A 411       1.336  12.132  11.708  1.00 45.98           O  
ANISOU 3410  OD2 ASP A 411     6245   5976   5249   -191     82     -8       O  
ATOM   3411  N   LEU A 412      -0.120  10.718   8.781  1.00 32.79           N  
ANISOU 3411  N   LEU A 412     4554   4348   3558   -218     39     -1       N  
ATOM   3412  CA  LEU A 412      -1.390  10.023   8.605  1.00 33.58           C  
ANISOU 3412  CA  LEU A 412     4652   4420   3688   -207     28      5       C  
ATOM   3413  C   LEU A 412      -2.387  10.411   9.695  1.00 33.33           C  
ANISOU 3413  C   LEU A 412     4621   4329   3715   -185     37     20       C  
ATOM   3414  O   LEU A 412      -2.049  10.430  10.881  1.00 36.27           O  
ANISOU 3414  O   LEU A 412     5000   4685   4097   -166     62      5       O  
ATOM   3415  CB  LEU A 412      -1.166   8.506   8.610  1.00 33.51           C  
ANISOU 3415  CB  LEU A 412     4641   4425   3666   -186     38    -36       C  
ATOM   3416  CG  LEU A 412      -0.627   7.905   7.306  1.00 34.54           C  
ANISOU 3416  CG  LEU A 412     4767   4607   3750   -211     32    -60       C  
ATOM   3417  CD1 LEU A 412       0.313   6.738   7.552  1.00 31.03           C  
ANISOU 3417  CD1 LEU A 412     4313   4181   3296   -189     53   -112       C  
ATOM   3418  CD2 LEU A 412      -1.790   7.486   6.406  1.00 31.66           C  
ANISOU 3418  CD2 LEU A 412     4404   4235   3389   -227      7    -45       C  
ATOM   3419  N   THR A 413      -3.607  10.729   9.277  1.00 30.56           N  
ANISOU 3419  N   THR A 413     4260   3946   3406   -193     16     50       N  
ATOM   3420  CA  THR A 413      -4.698  11.087  10.170  1.00 31.37           C  
ANISOU 3420  CA  THR A 413     4355   3990   3576   -175     29     61       C  
ATOM   3421  C   THR A 413      -5.143   9.876  10.995  1.00 32.18           C  
ANISOU 3421  C   THR A 413     4461   4076   3689   -147     53     34       C  
ATOM   3422  O   THR A 413      -5.406   8.802  10.441  1.00 29.45           O  
ANISOU 3422  O   THR A 413     4115   3744   3332   -143     39     26       O  
ATOM   3423  CB  THR A 413      -5.893  11.602   9.349  1.00 32.41           C  
ANISOU 3423  CB  THR A 413     4466   4089   3758   -192     -7    101       C  
ATOM   3424  OG1 THR A 413      -5.446  12.660   8.492  1.00 36.57           O  
ANISOU 3424  OG1 THR A 413     4992   4634   4270   -226    -39    133       O  
ATOM   3425  CG2 THR A 413      -7.010  12.113  10.255  1.00 28.62           C  
ANISOU 3425  CG2 THR A 413     3968   3542   3363   -174     12    107       C  
ATOM   3426  N   SER A 414      -5.238  10.063  12.313  1.00 33.16           N  
ANISOU 3426  N   SER A 414     4593   4172   3836   -132     87     19       N  
ATOM   3427  CA  SER A 414      -5.599   8.982  13.248  1.00 32.79           C  
ANISOU 3427  CA  SER A 414     4554   4109   3794   -114    110     -2       C  
ATOM   3428  C   SER A 414      -5.188   7.601  12.752  1.00 29.72           C  
ANISOU 3428  C   SER A 414     4169   3752   3370   -106     92    -17       C  
ATOM   3429  O   SER A 414      -6.046   6.772  12.433  1.00 31.99           O  
ANISOU 3429  O   SER A 414     4450   4028   3679    -98     81    -15       O  
ATOM   3430  CB  SER A 414      -7.102   8.988  13.537  1.00 32.35           C  
ANISOU 3430  CB  SER A 414     4482   4005   3804   -108    121      7       C  
ATOM   3431  OG  SER A 414      -7.411   9.868  14.600  1.00 43.68           O  
ANISOU 3431  OG  SER A 414     5917   5405   5273   -111    159     -1       O  
ATOM   3432  N   LEU A 415      -3.886   7.346  12.692  1.00 27.61           N  
ANISOU 3432  N   LEU A 415     3911   3522   3057   -106     89    -34       N  
ATOM   3433  CA  LEU A 415      -3.404   6.112  12.067  1.00 27.58           C  
ANISOU 3433  CA  LEU A 415     3903   3546   3030    -99     73    -55       C  
ATOM   3434  C   LEU A 415      -4.055   4.830  12.592  1.00 26.24           C  
ANISOU 3434  C   LEU A 415     3735   3353   2882    -81     72    -65       C  
ATOM   3435  O   LEU A 415      -4.712   4.121  11.831  1.00 25.44           O  
ANISOU 3435  O   LEU A 415     3625   3251   2791    -79     55    -67       O  
ATOM   3436  CB  LEU A 415      -1.879   5.990  12.109  1.00 27.69           C  
ANISOU 3436  CB  LEU A 415     3919   3595   3008    -99     74    -77       C  
ATOM   3437  CG  LEU A 415      -1.458   4.700  11.395  1.00 26.85           C  
ANISOU 3437  CG  LEU A 415     3800   3510   2890    -91     61   -108       C  
ATOM   3438  CD1 LEU A 415      -1.857   4.736   9.911  1.00 23.83           C  
ANISOU 3438  CD1 LEU A 415     3410   3153   2492   -109     49   -107       C  
ATOM   3439  CD2 LEU A 415       0.012   4.383  11.567  1.00 27.80           C  
ANISOU 3439  CD2 LEU A 415     3913   3655   2995    -86     64   -135       C  
ATOM   3440  N   TYR A 416      -3.876   4.525  13.875  1.00 26.20           N  
ANISOU 3440  N   TYR A 416     3744   3330   2881    -75     86    -70       N  
ATOM   3441  CA  TYR A 416      -4.352   3.241  14.382  1.00 25.92           C  
ANISOU 3441  CA  TYR A 416     3711   3274   2862    -64     79    -77       C  
ATOM   3442  C   TYR A 416      -5.863   3.065  14.254  1.00 26.60           C  
ANISOU 3442  C   TYR A 416     3791   3332   2985    -62     83    -62       C  
ATOM   3443  O   TYR A 416      -6.299   2.006  13.829  1.00 29.28           O  
ANISOU 3443  O   TYR A 416     4123   3667   3336    -53     64    -67       O  
ATOM   3444  CB  TYR A 416      -3.865   2.966  15.807  1.00 24.54           C  
ANISOU 3444  CB  TYR A 416     3558   3087   2680    -68     87    -78       C  
ATOM   3445  CG  TYR A 416      -2.442   2.451  15.883  1.00 24.98           C  
ANISOU 3445  CG  TYR A 416     3612   3163   2717    -64     67    -92       C  
ATOM   3446  CD1 TYR A 416      -1.545   2.642  14.823  1.00 22.47           C  
ANISOU 3446  CD1 TYR A 416     3275   2877   2385    -58     58   -109       C  
ATOM   3447  CD2 TYR A 416      -1.981   1.792  17.022  1.00 25.59           C  
ANISOU 3447  CD2 TYR A 416     3704   3225   2793    -70     54    -89       C  
ATOM   3448  CE1 TYR A 416      -0.234   2.190  14.892  1.00 22.85           C  
ANISOU 3448  CE1 TYR A 416     3313   2940   2429    -53     43   -127       C  
ATOM   3449  CE2 TYR A 416      -0.656   1.341  17.102  1.00 29.39           C  
ANISOU 3449  CE2 TYR A 416     4177   3717   3273    -65     29    -99       C  
ATOM   3450  CZ  TYR A 416       0.208   1.548  16.033  1.00 28.07           C  
ANISOU 3450  CZ  TYR A 416     3985   3580   3102    -54     26   -121       C  
ATOM   3451  OH  TYR A 416       1.510   1.101  16.101  1.00 29.26           O  
ANISOU 3451  OH  TYR A 416     4118   3736   3262    -48      5   -135       O  
ATOM   3452  N   PRO A 417      -6.661   4.102  14.605  1.00 29.26           N  
ANISOU 3452  N   PRO A 417     4125   3645   3345    -71    106    -47       N  
ATOM   3453  CA  PRO A 417      -8.104   3.974  14.430  1.00 29.10           C  
ANISOU 3453  CA  PRO A 417     4091   3594   3373    -69    109    -33       C  
ATOM   3454  C   PRO A 417      -8.509   3.867  12.960  1.00 30.09           C  
ANISOU 3454  C   PRO A 417     4197   3728   3507    -69     74    -21       C  
ATOM   3455  O   PRO A 417      -9.487   3.181  12.651  1.00 31.23           O  
ANISOU 3455  O   PRO A 417     4331   3854   3681    -65     61    -13       O  
ATOM   3456  CB  PRO A 417      -8.651   5.269  15.052  1.00 31.95           C  
ANISOU 3456  CB  PRO A 417     4447   3927   3766    -79    143    -25       C  
ATOM   3457  CG  PRO A 417      -7.590   5.692  16.026  1.00 30.96           C  
ANISOU 3457  CG  PRO A 417     4347   3815   3602    -88    164    -39       C  
ATOM   3458  CD  PRO A 417      -6.317   5.339  15.341  1.00 30.26           C  
ANISOU 3458  CD  PRO A 417     4263   3767   3468    -83    134    -45       C  
ATOM   3459  N   SER A 418      -7.769   4.537  12.072  1.00 28.96           N  
ANISOU 3459  N   SER A 418     4053   3615   3336    -79     59    -18       N  
ATOM   3460  CA  SER A 418      -7.997   4.429  10.627  1.00 27.61           C  
ANISOU 3460  CA  SER A 418     3872   3462   3156    -92     24     -7       C  
ATOM   3461  C   SER A 418      -7.665   3.045  10.089  1.00 27.96           C  
ANISOU 3461  C   SER A 418     3921   3529   3173    -85      7    -33       C  
ATOM   3462  O   SER A 418      -8.305   2.585   9.148  1.00 26.58           O  
ANISOU 3462  O   SER A 418     3741   3355   3003    -95    -19    -26       O  
ATOM   3463  CB  SER A 418      -7.196   5.477   9.855  1.00 28.14           C  
ANISOU 3463  CB  SER A 418     3940   3560   3190   -113     13      1       C  
ATOM   3464  OG  SER A 418      -7.542   6.779  10.299  1.00 32.56           O  
ANISOU 3464  OG  SER A 418     4494   4093   3785   -119     24     25       O  
ATOM   3465  N   ILE A 419      -6.661   2.389  10.680  1.00 28.91           N  
ANISOU 3465  N   ILE A 419     4050   3665   3271    -72     19    -62       N  
ATOM   3466  CA  ILE A 419      -6.313   1.016  10.309  1.00 28.61           C  
ANISOU 3466  CA  ILE A 419     4010   3638   3223    -61      5    -93       C  
ATOM   3467  C   ILE A 419      -7.446   0.074  10.745  1.00 29.67           C  
ANISOU 3467  C   ILE A 419     4142   3735   3395    -49     -3    -84       C  
ATOM   3468  O   ILE A 419      -7.875  -0.789   9.980  1.00 28.80           O  
ANISOU 3468  O   ILE A 419     4027   3624   3290    -50    -25    -93       O  
ATOM   3469  CB  ILE A 419      -4.955   0.565  10.915  1.00 29.00           C  
ANISOU 3469  CB  ILE A 419     4062   3702   3256    -49     14   -122       C  
ATOM   3470  CG1 ILE A 419      -3.798   1.381  10.334  1.00 27.81           C  
ANISOU 3470  CG1 ILE A 419     3908   3592   3067    -62     22   -134       C  
ATOM   3471  CG2 ILE A 419      -4.707  -0.915  10.654  1.00 26.97           C  
ANISOU 3471  CG2 ILE A 419     3796   3443   3009    -35     -3   -155       C  
ATOM   3472  CD1 ILE A 419      -2.455   1.165  11.054  1.00 27.66           C  
ANISOU 3472  CD1 ILE A 419     3886   3581   3042    -51     30   -156       C  
ATOM   3473  N   ILE A 420      -7.956   0.272  11.957  1.00 28.86           N  
ANISOU 3473  N   ILE A 420     4045   3602   3319    -44     16    -67       N  
ATOM   3474  CA  ILE A 420      -9.100  -0.517  12.435  1.00 29.33           C  
ANISOU 3474  CA  ILE A 420     4102   3628   3417    -38     13    -56       C  
ATOM   3475  C   ILE A 420     -10.284  -0.429  11.461  1.00 30.58           C  
ANISOU 3475  C   ILE A 420     4244   3772   3602    -45     -6    -37       C  
ATOM   3476  O   ILE A 420     -10.974  -1.425  11.217  1.00 30.60           O  
ANISOU 3476  O   ILE A 420     4242   3760   3625    -41    -25    -36       O  
ATOM   3477  CB  ILE A 420      -9.534  -0.102  13.867  1.00 27.31           C  
ANISOU 3477  CB  ILE A 420     3854   3345   3179    -42     46    -43       C  
ATOM   3478  CG1 ILE A 420      -8.438  -0.484  14.876  1.00 26.34           C  
ANISOU 3478  CG1 ILE A 420     3751   3231   3027    -42     52    -56       C  
ATOM   3479  CG2 ILE A 420     -10.883  -0.751  14.246  1.00 24.71           C  
ANISOU 3479  CG2 ILE A 420     3517   2981   2892    -43     49    -29       C  
ATOM   3480  CD1 ILE A 420      -8.691  -0.050  16.339  1.00 24.83           C  
ANISOU 3480  CD1 ILE A 420     3578   3021   2836    -59     86    -47       C  
ATOM   3481  N   ARG A 421     -10.490   0.760  10.899  1.00 30.27           N  
ANISOU 3481  N   ARG A 421     4197   3736   3566    -58     -6    -18       N  
ATOM   3482  CA  ARG A 421     -11.610   1.023   9.999  1.00 30.69           C  
ANISOU 3482  CA  ARG A 421     4234   3773   3654    -71    -32     10       C  
ATOM   3483  C   ARG A 421     -11.325   0.492   8.591  1.00 31.71           C  
ANISOU 3483  C   ARG A 421     4369   3933   3745    -87    -70      2       C  
ATOM   3484  O   ARG A 421     -12.169  -0.178   7.999  1.00 33.09           O  
ANISOU 3484  O   ARG A 421     4539   4096   3939    -93    -98     11       O  
ATOM   3485  CB  ARG A 421     -11.927   2.518   9.964  1.00 29.65           C  
ANISOU 3485  CB  ARG A 421     4090   3626   3550    -83    -26     38       C  
ATOM   3486  CG  ARG A 421     -12.424   3.105  11.298  1.00 32.60           C  
ANISOU 3486  CG  ARG A 421     4454   3963   3971    -73     18     41       C  
ATOM   3487  CD  ARG A 421     -12.554   4.629  11.230  1.00 33.71           C  
ANISOU 3487  CD  ARG A 421     4578   4086   4143    -83     24     60       C  
ATOM   3488  NE  ARG A 421     -13.396   5.030  10.108  1.00 35.00           N  
ANISOU 3488  NE  ARG A 421     4719   4231   4348    -99    -20     96       N  
ATOM   3489  CZ  ARG A 421     -13.267   6.162   9.418  1.00 35.08           C  
ANISOU 3489  CZ  ARG A 421     4720   4240   4369   -118    -45    123       C  
ATOM   3490  NH1 ARG A 421     -12.320   7.047   9.722  1.00 32.61           N  
ANISOU 3490  NH1 ARG A 421     4419   3945   4028   -121    -26    114       N  
ATOM   3491  NH2 ARG A 421     -14.088   6.398   8.405  1.00 27.18           N  
ANISOU 3491  NH2 ARG A 421     3700   3220   3408   -137    -96    162       N  
ATOM   3492  N   GLN A 422     -10.133   0.789   8.074  1.00 29.96           N  
ANISOU 3492  N   GLN A 422     4159   3754   3469    -97    -68    -18       N  
ATOM   3493  CA  GLN A 422      -9.683   0.308   6.769  1.00 29.78           C  
ANISOU 3493  CA  GLN A 422     4145   3770   3399   -120    -92    -39       C  
ATOM   3494  C   GLN A 422      -9.681  -1.226   6.678  1.00 29.80           C  
ANISOU 3494  C   GLN A 422     4150   3771   3402   -105    -98    -74       C  
ATOM   3495  O   GLN A 422     -10.194  -1.798   5.718  1.00 31.33           O  
ANISOU 3495  O   GLN A 422     4348   3970   3588   -124   -126    -77       O  
ATOM   3496  CB  GLN A 422      -8.288   0.864   6.451  1.00 27.52           C  
ANISOU 3496  CB  GLN A 422     3867   3530   3059   -132    -76    -62       C  
ATOM   3497  CG  GLN A 422      -7.586   0.166   5.288  1.00 28.15           C  
ANISOU 3497  CG  GLN A 422     3955   3655   3087   -154    -83   -103       C  
ATOM   3498  CD  GLN A 422      -6.768   1.115   4.429  1.00 30.18           C  
ANISOU 3498  CD  GLN A 422     4220   3960   3289   -193    -80   -103       C  
ATOM   3499  OE1 GLN A 422      -6.919   2.333   4.506  1.00 35.38           O  
ANISOU 3499  OE1 GLN A 422     4878   4613   3951   -207    -87    -62       O  
ATOM   3500  NE2 GLN A 422      -5.899   0.556   3.600  1.00 31.66           N  
ANISOU 3500  NE2 GLN A 422     4412   4191   3427   -212    -70   -152       N  
ATOM   3501  N   VAL A 423      -9.116  -1.880   7.685  1.00 28.38           N  
ANISOU 3501  N   VAL A 423     3969   3582   3233    -76    -78    -99       N  
ATOM   3502  CA  VAL A 423      -8.976  -3.340   7.673  1.00 29.51           C  
ANISOU 3502  CA  VAL A 423     4110   3717   3384    -60    -88   -134       C  
ATOM   3503  C   VAL A 423     -10.244  -4.061   8.154  1.00 28.96           C  
ANISOU 3503  C   VAL A 423     4037   3605   3363    -50   -103   -110       C  
ATOM   3504  O   VAL A 423     -10.476  -5.201   7.777  1.00 30.47           O  
ANISOU 3504  O   VAL A 423     4227   3787   3564    -46   -123   -131       O  
ATOM   3505  CB  VAL A 423      -7.754  -3.810   8.513  1.00 27.34           C  
ANISOU 3505  CB  VAL A 423     3833   3446   3109    -37    -71   -166       C  
ATOM   3506  CG1 VAL A 423      -7.569  -5.318   8.390  1.00 29.48           C  
ANISOU 3506  CG1 VAL A 423     4097   3704   3401    -22    -87   -204       C  
ATOM   3507  CG2 VAL A 423      -6.496  -3.084   8.065  1.00 25.52           C  
ANISOU 3507  CG2 VAL A 423     3601   3257   2837    -48    -53   -189       C  
ATOM   3508  N   ASN A 424     -11.049  -3.382   8.974  1.00 27.43           N  
ANISOU 3508  N   ASN A 424     3838   3383   3201    -47    -91    -72       N  
ATOM   3509  CA  ASN A 424     -12.224  -3.961   9.620  1.00 28.95           C  
ANISOU 3509  CA  ASN A 424     4024   3534   3441    -39    -96    -49       C  
ATOM   3510  C   ASN A 424     -11.846  -4.947  10.737  1.00 29.98           C  
ANISOU 3510  C   ASN A 424     4160   3649   3581    -21    -88    -64       C  
ATOM   3511  O   ASN A 424     -12.321  -6.085  10.786  1.00 29.61           O  
ANISOU 3511  O   ASN A 424     4111   3582   3557    -15   -109    -67       O  
ATOM   3512  CB  ASN A 424     -13.197  -4.577   8.606  1.00 27.94           C  
ANISOU 3512  CB  ASN A 424     3890   3395   3330    -50   -132    -40       C  
ATOM   3513  CG  ASN A 424     -14.617  -4.692   9.152  1.00 33.80           C  
ANISOU 3513  CG  ASN A 424     4617   4094   4131    -48   -134     -5       C  
ATOM   3514  OD1 ASN A 424     -15.045  -3.894  10.002  1.00 29.97           O  
ANISOU 3514  OD1 ASN A 424     4122   3590   3675    -47   -105     17       O  
ATOM   3515  ND2 ASN A 424     -15.355  -5.695   8.671  1.00 31.16           N  
ANISOU 3515  ND2 ASN A 424     4280   3744   3818    -51   -165     -2       N  
ATOM   3516  N   ILE A 425     -10.996  -4.470  11.639  1.00 30.86           N  
ANISOU 3516  N   ILE A 425     4280   3769   3676    -17    -63    -69       N  
ATOM   3517  CA  ILE A 425     -10.499  -5.253  12.770  1.00 31.33           C  
ANISOU 3517  CA  ILE A 425     4348   3816   3740    -10    -63    -75       C  
ATOM   3518  C   ILE A 425     -11.455  -5.115  13.943  1.00 30.15           C  
ANISOU 3518  C   ILE A 425     4204   3638   3614    -20    -41    -46       C  
ATOM   3519  O   ILE A 425     -11.638  -4.029  14.480  1.00 27.63           O  
ANISOU 3519  O   ILE A 425     3889   3319   3291    -30     -7    -33       O  
ATOM   3520  CB  ILE A 425      -9.077  -4.787  13.194  1.00 30.44           C  
ANISOU 3520  CB  ILE A 425     4244   3726   3596     -7    -51    -91       C  
ATOM   3521  CG1 ILE A 425      -8.077  -5.052  12.069  1.00 32.23           C  
ANISOU 3521  CG1 ILE A 425     4461   3981   3804      1    -66   -129       C  
ATOM   3522  CG2 ILE A 425      -8.625  -5.483  14.473  1.00 28.09           C  
ANISOU 3522  CG2 ILE A 425     3959   3410   3306     -8    -58    -86       C  
ATOM   3523  CD1 ILE A 425      -6.800  -4.253  12.181  1.00 32.26           C  
ANISOU 3523  CD1 ILE A 425     4467   4013   3779     -1    -50   -142       C  
ATOM   3524  N   SER A 426     -12.054  -6.234  14.329  1.00 30.66           N  
ANISOU 3524  N   SER A 426     4269   3678   3703    -20    -58    -38       N  
ATOM   3525  CA  SER A 426     -13.016  -6.293  15.418  1.00 30.89           C  
ANISOU 3525  CA  SER A 426     4302   3681   3752    -36    -36    -13       C  
ATOM   3526  C   SER A 426     -12.980  -7.734  15.900  1.00 31.16           C  
ANISOU 3526  C   SER A 426     4344   3697   3798    -38    -69     -9       C  
ATOM   3527  O   SER A 426     -12.505  -8.607  15.175  1.00 32.75           O  
ANISOU 3527  O   SER A 426     4538   3899   4006    -22   -108    -27       O  
ATOM   3528  CB  SER A 426     -14.421  -5.933  14.912  1.00 30.16           C  
ANISOU 3528  CB  SER A 426     4189   3572   3700    -39    -26      4       C  
ATOM   3529  OG  SER A 426     -15.270  -5.497  15.971  1.00 31.57           O  
ANISOU 3529  OG  SER A 426     4366   3731   3898    -58     17     20       O  
ATOM   3530  N   PRO A 427     -13.457  -8.001  17.125  1.00 32.47           N  
ANISOU 3530  N   PRO A 427     4523   3847   3967    -62    -54     12       N  
ATOM   3531  CA  PRO A 427     -13.437  -9.390  17.570  1.00 32.06           C  
ANISOU 3531  CA  PRO A 427     4479   3775   3929    -68    -94     23       C  
ATOM   3532  C   PRO A 427     -14.295 -10.312  16.706  1.00 34.18           C  
ANISOU 3532  C   PRO A 427     4727   4023   4237    -55   -126     24       C  
ATOM   3533  O   PRO A 427     -13.918 -11.464  16.487  1.00 36.17           O  
ANISOU 3533  O   PRO A 427     4977   4261   4505    -45   -172     17       O  
ATOM   3534  CB  PRO A 427     -14.003  -9.314  18.991  1.00 34.20           C  
ANISOU 3534  CB  PRO A 427     4770   4037   4189   -108    -64     49       C  
ATOM   3535  CG  PRO A 427     -14.710  -7.988  19.063  1.00 34.85           C  
ANISOU 3535  CG  PRO A 427     4845   4127   4271   -116     -2     46       C  
ATOM   3536  CD  PRO A 427     -13.904  -7.090  18.192  1.00 32.98           C  
ANISOU 3536  CD  PRO A 427     4599   3911   4019    -89      0     24       C  
ATOM   3537  N   GLU A 428     -15.427  -9.814  16.207  1.00 33.47           N  
ANISOU 3537  N   GLU A 428     4620   3928   4168    -54   -104     32       N  
ATOM   3538  CA  GLU A 428     -16.381 -10.673  15.489  1.00 34.05           C  
ANISOU 3538  CA  GLU A 428     4677   3981   4281    -48   -135     39       C  
ATOM   3539  C   GLU A 428     -16.219 -10.665  13.962  1.00 34.56           C  
ANISOU 3539  C   GLU A 428     4728   4056   4347    -27   -163     16       C  
ATOM   3540  O   GLU A 428     -16.975 -11.336  13.248  1.00 35.36           O  
ANISOU 3540  O   GLU A 428     4818   4141   4477    -25   -192     20       O  
ATOM   3541  CB  GLU A 428     -17.827 -10.355  15.910  1.00 33.72           C  
ANISOU 3541  CB  GLU A 428     4620   3920   4273    -66   -103     66       C  
ATOM   3542  CG  GLU A 428     -18.492  -9.159  15.224  1.00 33.28           C  
ANISOU 3542  CG  GLU A 428     4541   3866   4238    -61    -76     68       C  
ATOM   3543  CD  GLU A 428     -17.905  -7.821  15.627  1.00 35.25           C  
ANISOU 3543  CD  GLU A 428     4797   4135   4461    -64    -32     58       C  
ATOM   3544  OE1 GLU A 428     -16.775  -7.785  16.153  1.00 32.94           O  
ANISOU 3544  OE1 GLU A 428     4529   3862   4125    -65    -28     45       O  
ATOM   3545  OE2 GLU A 428     -18.575  -6.793  15.397  1.00 41.88           O  
ANISOU 3545  OE2 GLU A 428     5615   4968   5331    -66     -4     65       O  
ATOM   3546  N   THR A 429     -15.230  -9.917  13.470  1.00 33.70           N  
ANISOU 3546  N   THR A 429     4624   3975   4205    -18   -154     -7       N  
ATOM   3547  CA  THR A 429     -14.937  -9.872  12.034  1.00 34.21           C  
ANISOU 3547  CA  THR A 429     4682   4058   4258     -8   -176    -32       C  
ATOM   3548  C   THR A 429     -13.779 -10.767  11.596  1.00 33.25           C  
ANISOU 3548  C   THR A 429     4564   3946   4123      6   -203    -73       C  
ATOM   3549  O   THR A 429     -13.457 -10.807  10.416  1.00 35.23           O  
ANISOU 3549  O   THR A 429     4813   4216   4359      7   -215   -103       O  
ATOM   3550  CB  THR A 429     -14.676  -8.435  11.518  1.00 33.89           C  
ANISOU 3550  CB  THR A 429     4640   4045   4190    -13   -150    -32       C  
ATOM   3551  OG1 THR A 429     -13.733  -7.780  12.374  1.00 33.40           O  
ANISOU 3551  OG1 THR A 429     4589   3999   4102    -11   -120    -37       O  
ATOM   3552  CG2 THR A 429     -15.965  -7.646  11.459  1.00 32.02           C  
ANISOU 3552  CG2 THR A 429     4389   3792   3986    -25   -137      3       C  
ATOM   3553  N   ILE A 430     -13.160 -11.480  12.534  1.00 36.15           N  
ANISOU 3553  N   ILE A 430     4937   4299   4501     11   -213    -76       N  
ATOM   3554  CA  ILE A 430     -12.069 -12.404  12.212  1.00 34.24           C  
ANISOU 3554  CA  ILE A 430     4689   4053   4267     27   -241   -116       C  
ATOM   3555  C   ILE A 430     -12.566 -13.489  11.262  1.00 36.90           C  
ANISOU 3555  C   ILE A 430     5016   4372   4632     32   -275   -138       C  
ATOM   3556  O   ILE A 430     -13.545 -14.188  11.564  1.00 40.36           O  
ANISOU 3556  O   ILE A 430     5454   4780   5100     27   -296   -112       O  
ATOM   3557  CB  ILE A 430     -11.469 -13.046  13.484  1.00 34.26           C  
ANISOU 3557  CB  ILE A 430     4696   4031   4289     27   -259   -102       C  
ATOM   3558  CG1 ILE A 430     -10.724 -11.995  14.314  1.00 35.29           C  
ANISOU 3558  CG1 ILE A 430     4840   4184   4387     18   -229    -89       C  
ATOM   3559  CG2 ILE A 430     -10.521 -14.196  13.122  1.00 33.40           C  
ANISOU 3559  CG2 ILE A 430     4570   3903   4216     46   -298   -142       C  
ATOM   3560  CD1 ILE A 430     -10.344 -12.464  15.717  1.00 34.33           C  
ANISOU 3560  CD1 ILE A 430     4731   4039   4275      3   -248    -60       C  
ATOM   3561  N   ALA A 431     -11.897 -13.624  10.117  1.00 35.39           N  
ANISOU 3561  N   ALA A 431     4819   4201   4428     39   -278   -189       N  
ATOM   3562  CA  ALA A 431     -12.309 -14.586   9.093  1.00 35.15           C  
ANISOU 3562  CA  ALA A 431     4783   4158   4415     39   -306   -220       C  
ATOM   3563  C   ALA A 431     -11.360 -15.773   8.977  1.00 35.62           C  
ANISOU 3563  C   ALA A 431     4826   4195   4512     57   -329   -274       C  
ATOM   3564  O   ALA A 431     -11.758 -16.844   8.526  1.00 37.00           O  
ANISOU 3564  O   ALA A 431     4996   4343   4721     59   -359   -295       O  
ATOM   3565  CB  ALA A 431     -12.461 -13.896   7.738  1.00 36.10           C  
ANISOU 3565  CB  ALA A 431     4909   4316   4489     20   -292   -242       C  
ATOM   3566  N   GLY A 432     -10.106 -15.577   9.372  1.00 34.83           N  
ANISOU 3566  N   GLY A 432     4716   4104   4414     70   -316   -296       N  
ATOM   3567  CA  GLY A 432      -9.094 -16.619   9.258  1.00 34.17           C  
ANISOU 3567  CA  GLY A 432     4607   3995   4381     89   -337   -351       C  
ATOM   3568  C   GLY A 432      -7.696 -16.047   9.168  1.00 35.07           C  
ANISOU 3568  C   GLY A 432     4707   4136   4483     98   -309   -389       C  
ATOM   3569  O   GLY A 432      -7.451 -14.922   9.608  1.00 35.08           O  
ANISOU 3569  O   GLY A 432     4720   4166   4442     91   -283   -358       O  
ATOM   3570  N   THR A 433      -6.781 -16.827   8.595  1.00 34.23           N  
ANISOU 3570  N   THR A 433     4571   4016   4419    113   -313   -459       N  
ATOM   3571  CA  THR A 433      -5.381 -16.424   8.453  1.00 33.63           C  
ANISOU 3571  CA  THR A 433     4471   3961   4345    122   -286   -504       C  
ATOM   3572  C   THR A 433      -4.818 -16.818   7.096  1.00 35.54           C  
ANISOU 3572  C   THR A 433     4693   4221   4591    120   -259   -597       C  
ATOM   3573  O   THR A 433      -5.338 -17.711   6.429  1.00 33.26           O  
ANISOU 3573  O   THR A 433     4402   3913   4323    118   -272   -633       O  
ATOM   3574  CB  THR A 433      -4.468 -17.078   9.532  1.00 34.31           C  
ANISOU 3574  CB  THR A 433     4529   3998   4511    145   -323   -497       C  
ATOM   3575  OG1 THR A 433      -4.501 -18.509   9.397  1.00 29.99           O  
ANISOU 3575  OG1 THR A 433     3954   3394   4046    161   -363   -531       O  
ATOM   3576  CG2 THR A 433      -4.897 -16.673  10.943  1.00 34.07           C  
ANISOU 3576  CG2 THR A 433     4522   3953   4468    136   -347   -408       C  
ATOM   3577  N   PHE A 434      -3.739 -16.155   6.704  1.00 35.68           N  
ANISOU 3577  N   PHE A 434     4695   4276   4585    118   -218   -639       N  
ATOM   3578  CA  PHE A 434      -2.996 -16.553   5.519  1.00 39.76           C  
ANISOU 3578  CA  PHE A 434     5186   4811   5110    113   -184   -737       C  
ATOM   3579  C   PHE A 434      -1.535 -16.776   5.895  1.00 39.52           C  
ANISOU 3579  C   PHE A 434     5105   4760   5149    138   -175   -782       C  
ATOM   3580  O   PHE A 434      -1.103 -16.409   6.986  1.00 40.18           O  
ANISOU 3580  O   PHE A 434     5183   4828   5256    153   -196   -729       O  
ATOM   3581  CB  PHE A 434      -3.138 -15.519   4.385  1.00 38.48           C  
ANISOU 3581  CB  PHE A 434     5053   4722   4845     72   -135   -755       C  
ATOM   3582  CG  PHE A 434      -2.604 -14.160   4.731  1.00 37.99           C  
ANISOU 3582  CG  PHE A 434     5000   4704   4731     64   -109   -717       C  
ATOM   3583  CD1 PHE A 434      -3.410 -13.225   5.381  1.00 34.87           C  
ANISOU 3583  CD1 PHE A 434     4639   4318   4291     56   -122   -628       C  
ATOM   3584  CD2 PHE A 434      -1.296 -13.810   4.409  1.00 35.32           C  
ANISOU 3584  CD2 PHE A 434     4633   4394   4394     62    -68   -772       C  
ATOM   3585  CE1 PHE A 434      -2.921 -11.963   5.704  1.00 31.54           C  
ANISOU 3585  CE1 PHE A 434     4225   3932   3825     47    -99   -595       C  
ATOM   3586  CE2 PHE A 434      -0.797 -12.555   4.739  1.00 33.62           C  
ANISOU 3586  CE2 PHE A 434     4426   4217   4131     53    -47   -735       C  
ATOM   3587  CZ  PHE A 434      -1.615 -11.625   5.380  1.00 32.69           C  
ANISOU 3587  CZ  PHE A 434     4345   4107   3967     46    -64   -645       C  
ATOM   3588  N   LYS A 435      -0.791 -17.392   4.985  1.00 42.31           N  
ANISOU 3588  N   LYS A 435     5422   5114   5540    140   -145   -882       N  
ATOM   3589  CA  LYS A 435       0.621 -17.669   5.182  1.00 43.23           C  
ANISOU 3589  CA  LYS A 435     5480   5207   5738    164   -133   -938       C  
ATOM   3590  C   LYS A 435       1.393 -16.374   4.989  1.00 43.17           C  
ANISOU 3590  C   LYS A 435     5475   5264   5662    145    -83   -937       C  
ATOM   3591  O   LYS A 435       1.440 -15.834   3.877  1.00 42.32           O  
ANISOU 3591  O   LYS A 435     5384   5219   5478    111    -28   -984       O  
ATOM   3592  CB  LYS A 435       1.074 -18.731   4.181  1.00 45.02           C  
ANISOU 3592  CB  LYS A 435     5664   5414   6028    167   -106  -1055       C  
ATOM   3593  CG  LYS A 435       2.351 -19.466   4.553  1.00 49.38           C  
ANISOU 3593  CG  LYS A 435     6140   5908   6713    204   -114  -1113       C  
ATOM   3594  CD  LYS A 435       2.357 -20.893   3.975  1.00 52.97           C  
ANISOU 3594  CD  LYS A 435     6555   6306   7266    219   -120  -1205       C  
ATOM   3595  CE  LYS A 435       2.684 -20.922   2.479  1.00 50.88           C  
ANISOU 3595  CE  LYS A 435     6281   6091   6959    188    -37  -1327       C  
ATOM   3596  NZ  LYS A 435       2.670 -22.299   1.929  1.00 45.08           N  
ANISOU 3596  NZ  LYS A 435     5508   5298   6321    201    -40  -1423       N  
ATOM   3597  N   VAL A 436       1.975 -15.871   6.078  1.00 42.15           N  
ANISOU 3597  N   VAL A 436     5336   5121   5559    162   -105   -880       N  
ATOM   3598  CA  VAL A 436       2.724 -14.617   6.045  1.00 41.95           C  
ANISOU 3598  CA  VAL A 436     5314   5151   5475    147    -65   -870       C  
ATOM   3599  C   VAL A 436       4.098 -14.768   5.405  1.00 42.73           C  
ANISOU 3599  C   VAL A 436     5354   5261   5623    151    -18   -966       C  
ATOM   3600  O   VAL A 436       4.827 -15.727   5.668  1.00 41.55           O  
ANISOU 3600  O   VAL A 436     5145   5052   5589    181    -37  -1012       O  
ATOM   3601  CB  VAL A 436       2.890 -13.968   7.453  1.00 41.85           C  
ANISOU 3601  CB  VAL A 436     5313   5121   5466    158   -104   -777       C  
ATOM   3602  CG1 VAL A 436       1.550 -13.685   8.060  1.00 43.21           C  
ANISOU 3602  CG1 VAL A 436     5542   5290   5584    148   -136   -690       C  
ATOM   3603  CG2 VAL A 436       3.711 -14.855   8.391  1.00 45.26           C  
ANISOU 3603  CG2 VAL A 436     5695   5481   6021    191   -155   -777       C  
ATOM   3604  N   ALA A 437       4.425 -13.808   4.551  1.00 42.18           N  
ANISOU 3604  N   ALA A 437     5297   5264   5467    117     43   -995       N  
ATOM   3605  CA  ALA A 437       5.766 -13.640   4.032  1.00 41.37           C  
ANISOU 3605  CA  ALA A 437     5142   5184   5393    112     96  -1074       C  
ATOM   3606  C   ALA A 437       6.475 -12.635   4.953  1.00 42.18           C  
ANISOU 3606  C   ALA A 437     5240   5295   5490    120     84  -1009       C  
ATOM   3607  O   ALA A 437       5.813 -11.952   5.734  1.00 39.94           O  
ANISOU 3607  O   ALA A 437     5004   5015   5155    117     49   -913       O  
ATOM   3608  CB  ALA A 437       5.701 -13.122   2.613  1.00 39.47           C  
ANISOU 3608  CB  ALA A 437     4925   5022   5050     61    166  -1134       C  
ATOM   3609  N   PRO A 438       7.820 -12.558   4.889  1.00 43.68           N  
ANISOU 3609  N   PRO A 438     5372   5487   5739    128    114  -1062       N  
ATOM   3610  CA  PRO A 438       8.539 -11.537   5.654  1.00 43.94           C  
ANISOU 3610  CA  PRO A 438     5401   5534   5759    129    106  -1004       C  
ATOM   3611  C   PRO A 438       8.042 -10.141   5.314  1.00 43.01           C  
ANISOU 3611  C   PRO A 438     5347   5492   5503     88    134   -954       C  
ATOM   3612  O   PRO A 438       7.729  -9.872   4.156  1.00 44.29           O  
ANISOU 3612  O   PRO A 438     5530   5710   5586     51    183   -996       O  
ATOM   3613  CB  PRO A 438       9.980 -11.704   5.182  1.00 44.82           C  
ANISOU 3613  CB  PRO A 438     5437   5649   5945    133    153  -1094       C  
ATOM   3614  CG  PRO A 438      10.077 -13.142   4.830  1.00 45.34           C  
ANISOU 3614  CG  PRO A 438     5450   5657   6119    158    151  -1178       C  
ATOM   3615  CD  PRO A 438       8.745 -13.504   4.239  1.00 44.43           C  
ANISOU 3615  CD  PRO A 438     5392   5557   5933    141    151  -1178       C  
ATOM   3616  N   LEU A 439       7.981  -9.271   6.319  1.00 42.20           N  
ANISOU 3616  N   LEU A 439     5273   5389   5373     91    100   -864       N  
ATOM   3617  CA  LEU A 439       7.357  -7.954   6.186  1.00 41.94           C  
ANISOU 3617  CA  LEU A 439     5300   5412   5222     57    114   -803       C  
ATOM   3618  C   LEU A 439       7.863  -7.122   5.004  1.00 42.16           C  
ANISOU 3618  C   LEU A 439     5329   5516   5175     15    179   -849       C  
ATOM   3619  O   LEU A 439       7.058  -6.499   4.302  1.00 43.45           O  
ANISOU 3619  O   LEU A 439     5540   5725   5245    -22    194   -830       O  
ATOM   3620  CB  LEU A 439       7.476  -7.157   7.494  1.00 40.88           C  
ANISOU 3620  CB  LEU A 439     5187   5261   5085     67     75   -716       C  
ATOM   3621  CG  LEU A 439       6.744  -5.810   7.562  1.00 40.74           C  
ANISOU 3621  CG  LEU A 439     5228   5285   4964     38     81   -647       C  
ATOM   3622  CD1 LEU A 439       5.222  -5.984   7.694  1.00 37.37           C  
ANISOU 3622  CD1 LEU A 439     4851   4844   4504     37     56   -602       C  
ATOM   3623  CD2 LEU A 439       7.283  -4.971   8.706  1.00 41.54           C  
ANISOU 3623  CD2 LEU A 439     5338   5378   5069     43     59   -587       C  
ATOM   3624  N   HIS A 440       9.179  -7.112   4.781  1.00 42.33           N  
ANISOU 3624  N   HIS A 440     5295   5548   5241     16    214   -907       N  
ATOM   3625  CA AHIS A 440       9.752  -6.320   3.692  0.50 42.63           C  
ANISOU 3625  CA AHIS A 440     5331   5661   5207    -31    278   -952       C  
ATOM   3626  CA BHIS A 440       9.767  -6.330   3.689  0.50 42.83           C  
ANISOU 3626  CA BHIS A 440     5355   5686   5233    -31    279   -953       C  
ATOM   3627  C   HIS A 440       9.233  -6.758   2.318  1.00 42.75           C  
ANISOU 3627  C   HIS A 440     5362   5716   5166    -70    322  -1021       C  
ATOM   3628  O   HIS A 440       9.238  -5.973   1.366  1.00 43.65           O  
ANISOU 3628  O   HIS A 440     5501   5899   5183   -126    364  -1033       O  
ATOM   3629  CB AHIS A 440      11.290  -6.289   3.748  0.50 43.69           C  
ANISOU 3629  CB AHIS A 440     5395   5796   5409    -23    311  -1006       C  
ATOM   3630  CB BHIS A 440      11.305  -6.369   3.730  0.50 43.95           C  
ANISOU 3630  CB BHIS A 440     5425   5826   5447    -22    311  -1011       C  
ATOM   3631  CG AHIS A 440      11.948  -7.566   3.330  0.50 45.54           C  
ANISOU 3631  CG AHIS A 440     5559   5996   5748     -2    338  -1110       C  
ATOM   3632  CG BHIS A 440      11.916  -5.251   4.523  0.50 45.85           C  
ANISOU 3632  CG BHIS A 440     5669   6077   5674    -21    294   -943       C  
ATOM   3633  ND1AHIS A 440      12.280  -8.560   4.226  0.50 47.36           N  
ANISOU 3633  ND1AHIS A 440     5740   6143   6110     52    290  -1113       N  
ATOM   3634  ND1BHIS A 440      12.153  -4.002   3.988  0.50 45.09           N  
ANISOU 3634  ND1BHIS A 440     5598   6050   5484    -67    330   -926       N  
ATOM   3635  CD2AHIS A 440      12.356  -8.003   2.115  0.50 47.11           C  
ANISOU 3635  CD2AHIS A 440     5726   6230   5943    -30    409  -1218       C  
ATOM   3636  CD2BHIS A 440      12.330  -5.192   5.812  0.50 46.35           C  
ANISOU 3636  CD2BHIS A 440     5718   6089   5804     14    242   -887       C  
ATOM   3637  CE1AHIS A 440      12.852  -9.560   3.578  0.50 49.01           C  
ANISOU 3637  CE1AHIS A 440     5886   6333   6403     61    329  -1220       C  
ATOM   3638  CE1BHIS A 440      12.685  -3.222   4.913  0.50 45.92           C  
ANISOU 3638  CE1BHIS A 440     5701   6144   5601    -56    303   -866       C  
ATOM   3639  NE2AHIS A 440      12.908  -9.248   2.295  0.50 47.85           N  
ANISOU 3639  NE2AHIS A 440     5748   6258   6173     12    406  -1290       N  
ATOM   3640  NE2BHIS A 440      12.804  -3.920   6.028  0.50 45.91           N  
ANISOU 3640  NE2BHIS A 440     5677   6072   5694     -9    249   -841       N  
ATOM   3641  N   ASP A 441       8.765  -8.005   2.229  1.00 40.83           N  
ANISOU 3641  N   ASP A 441     5105   5427   4981    -47    308  -1063       N  
ATOM   3642  CA  ASP A 441       8.167  -8.523   0.996  1.00 40.85           C  
ANISOU 3642  CA  ASP A 441     5128   5461   4932    -85    342  -1127       C  
ATOM   3643  C   ASP A 441       6.817  -7.869   0.700  1.00 39.10           C  
ANISOU 3643  C   ASP A 441     4984   5270   4602   -120    316  -1052       C  
ATOM   3644  O   ASP A 441       6.476  -7.635  -0.462  1.00 41.07           O  
ANISOU 3644  O   ASP A 441     5266   5577   4764   -178    349  -1081       O  
ATOM   3645  CB  ASP A 441       8.054 -10.051   1.028  1.00 40.27           C  
ANISOU 3645  CB  ASP A 441     5016   5323   4960    -47    330  -1192       C  
ATOM   3646  CG  ASP A 441       9.416 -10.745   0.908  1.00 44.16           C  
ANISOU 3646  CG  ASP A 441     5424   5792   5563    -26    372  -1294       C  
ATOM   3647  OD1 ASP A 441      10.445 -10.057   0.700  1.00 44.07           O  
ANISOU 3647  OD1 ASP A 441     5383   5820   5541    -44    418  -1320       O  
ATOM   3648  OD2 ASP A 441       9.459 -11.984   1.026  1.00 42.19           O  
ANISOU 3648  OD2 ASP A 441     5133   5480   5418     10    358  -1349       O  
ATOM   3649  N   TYR A 442       6.062  -7.564   1.751  1.00 36.11           N  
ANISOU 3649  N   TYR A 442     4634   4854   4232    -89    256   -955       N  
ATOM   3650  CA  TYR A 442       4.850  -6.780   1.596  1.00 34.60           C  
ANISOU 3650  CA  TYR A 442     4507   4686   3952   -119    230   -877       C  
ATOM   3651  C   TYR A 442       5.220  -5.328   1.338  1.00 35.95           C  
ANISOU 3651  C   TYR A 442     4700   4917   4045   -160    250   -838       C  
ATOM   3652  O   TYR A 442       4.672  -4.700   0.438  1.00 36.65           O  
ANISOU 3652  O   TYR A 442     4828   5054   4045   -214    258   -822       O  
ATOM   3653  CB  TYR A 442       3.925  -6.937   2.805  1.00 33.63           C  
ANISOU 3653  CB  TYR A 442     4404   4504   3870    -76    168   -795       C  
ATOM   3654  CG  TYR A 442       3.446  -8.358   2.987  1.00 32.13           C  
ANISOU 3654  CG  TYR A 442     4199   4258   3752    -44    143   -826       C  
ATOM   3655  CD1 TYR A 442       2.583  -8.952   2.059  1.00 33.20           C  
ANISOU 3655  CD1 TYR A 442     4356   4401   3856    -69    144   -856       C  
ATOM   3656  CD2 TYR A 442       3.873  -9.119   4.070  1.00 34.60           C  
ANISOU 3656  CD2 TYR A 442     4476   4508   4164      7    112   -823       C  
ATOM   3657  CE1 TYR A 442       2.148 -10.262   2.218  1.00 33.69           C  
ANISOU 3657  CE1 TYR A 442     4404   4410   3987    -39    119   -884       C  
ATOM   3658  CE2 TYR A 442       3.448 -10.437   4.238  1.00 35.26           C  
ANISOU 3658  CE2 TYR A 442     4543   4535   4318     35     83   -848       C  
ATOM   3659  CZ  TYR A 442       2.589 -10.998   3.310  1.00 36.15           C  
ANISOU 3659  CZ  TYR A 442     4677   4657   4400     13     89   -880       C  
ATOM   3660  OH  TYR A 442       2.184 -12.299   3.477  1.00 38.60           O  
ANISOU 3660  OH  TYR A 442     4972   4911   4785     40     58   -905       O  
ATOM   3661  N   ILE A 443       6.187  -4.811   2.097  1.00 38.38           N  
ANISOU 3661  N   ILE A 443     4979   5218   4386   -137    254   -824       N  
ATOM   3662  CA  ILE A 443       6.663  -3.443   1.897  1.00 38.67           C  
ANISOU 3662  CA  ILE A 443     5030   5308   4357   -174    273   -790       C  
ATOM   3663  C   ILE A 443       7.067  -3.222   0.437  1.00 40.35           C  
ANISOU 3663  C   ILE A 443     5245   5592   4494   -240    328   -853       C  
ATOM   3664  O   ILE A 443       6.701  -2.216  -0.170  1.00 39.77           O  
ANISOU 3664  O   ILE A 443     5213   5568   4332   -294    329   -811       O  
ATOM   3665  CB  ILE A 443       7.820  -3.084   2.871  1.00 38.84           C  
ANISOU 3665  CB  ILE A 443     5012   5311   4435   -141    273   -780       C  
ATOM   3666  CG1 ILE A 443       7.307  -3.063   4.320  1.00 39.82           C  
ANISOU 3666  CG1 ILE A 443     5151   5374   4607    -94    216   -703       C  
ATOM   3667  CG2 ILE A 443       8.455  -1.742   2.500  1.00 35.18           C  
ANISOU 3667  CG2 ILE A 443     4558   4906   3904   -184    300   -759       C  
ATOM   3668  CD1 ILE A 443       8.397  -3.125   5.380  1.00 42.21           C  
ANISOU 3668  CD1 ILE A 443     5412   5642   4984    -58    204   -699       C  
ATOM   3669  N   ASN A 444       7.792  -4.180  -0.132  1.00 44.34           N  
ANISOU 3669  N   ASN A 444     5707   6102   5038   -241    374   -953       N  
ATOM   3670  CA  ASN A 444       8.316  -4.029  -1.491  1.00 47.26           C  
ANISOU 3670  CA  ASN A 444     6076   6544   5337   -310    438  -1027       C  
ATOM   3671  C   ASN A 444       7.445  -4.613  -2.593  1.00 48.21           C  
ANISOU 3671  C   ASN A 444     6233   6688   5397   -358    447  -1065       C  
ATOM   3672  O   ASN A 444       7.857  -4.681  -3.753  1.00 51.17           O  
ANISOU 3672  O   ASN A 444     6608   7121   5711   -422    504  -1139       O  
ATOM   3673  CB  ASN A 444       9.760  -4.529  -1.563  1.00 49.91           C  
ANISOU 3673  CB  ASN A 444     6338   6881   5744   -296    496  -1123       C  
ATOM   3674  CG  ASN A 444      10.690  -3.697  -0.695  1.00 53.15           C  
ANISOU 3674  CG  ASN A 444     6719   7286   6189   -271    489  -1080       C  
ATOM   3675  OD1 ASN A 444      10.898  -2.511  -0.959  1.00 55.09           O  
ANISOU 3675  OD1 ASN A 444     6990   7584   6357   -315    500  -1038       O  
ATOM   3676  ND2 ASN A 444      11.224  -4.301   0.365  1.00 50.87           N  
ANISOU 3676  ND2 ASN A 444     6380   6930   6018   -203    465  -1084       N  
ATOM   3677  N   ALA A 445       6.236  -5.028  -2.219  1.00 47.79           N  
ANISOU 3677  N   ALA A 445     6211   6590   5357   -331    391  -1014       N  
ATOM   3678  CA  ALA A 445       5.224  -5.503  -3.165  1.00 48.32           C  
ANISOU 3678  CA  ALA A 445     6321   6673   5366   -376    383  -1030       C  
ATOM   3679  C   ALA A 445       5.656  -6.721  -3.988  1.00 50.30           C  
ANISOU 3679  C   ALA A 445     6543   6930   5639   -391    437  -1155       C  
ATOM   3680  O   ALA A 445       5.270  -6.857  -5.154  1.00 51.20           O  
ANISOU 3680  O   ALA A 445     6692   7090   5670   -461    459  -1194       O  
ATOM   3681  CB  ALA A 445       4.759  -4.355  -4.084  1.00 47.86           C  
ANISOU 3681  CB  ALA A 445     6320   6683   5181   -461    379   -979       C  
ATOM   3682  N   VAL A 446       6.448  -7.605  -3.382  1.00 50.89           N  
ANISOU 3682  N   VAL A 446     6554   6955   5829   -329    455  -1218       N  
ATOM   3683  CA  VAL A 446       6.869  -8.842  -4.054  1.00 51.69           C  
ANISOU 3683  CA  VAL A 446     6617   7046   5976   -333    505  -1344       C  
ATOM   3684  C   VAL A 446       6.218 -10.094  -3.464  1.00 50.99           C  
ANISOU 3684  C   VAL A 446     6513   6875   5985   -271    459  -1351       C  
ATOM   3685  O   VAL A 446       6.216 -11.160  -4.087  1.00 51.93           O  
ANISOU 3685  O   VAL A 446     6615   6982   6136   -278    487  -1445       O  
ATOM   3686  CB  VAL A 446       8.414  -9.001  -4.117  1.00 52.97           C  
ANISOU 3686  CB  VAL A 446     6705   7218   6205   -323    575  -1440       C  
ATOM   3687  CG1 VAL A 446       9.025  -7.908  -4.994  1.00 52.88           C  
ANISOU 3687  CG1 VAL A 446     6711   7299   6081   -403    634  -1454       C  
ATOM   3688  CG2 VAL A 446       9.037  -9.010  -2.719  1.00 52.97           C  
ANISOU 3688  CG2 VAL A 446     6650   7151   6323   -241    537  -1396       C  
ATOM   3689  N   ALA A 447       5.667  -9.963  -2.264  1.00 49.50           N  
ANISOU 3689  N   ALA A 447     6332   6632   5844   -214    389  -1252       N  
ATOM   3690  CA  ALA A 447       4.896 -11.046  -1.671  1.00 48.56           C  
ANISOU 3690  CA  ALA A 447     6209   6439   5803   -163    336  -1239       C  
ATOM   3691  C   ALA A 447       3.599 -11.267  -2.452  1.00 47.53           C  
ANISOU 3691  C   ALA A 447     6138   6325   5596   -206    316  -1225       C  
ATOM   3692  O   ALA A 447       3.064 -10.337  -3.077  1.00 44.09           O  
ANISOU 3692  O   ALA A 447     5756   5947   5049   -264    316  -1179       O  
ATOM   3693  CB  ALA A 447       4.604 -10.753  -0.216  1.00 47.94           C  
ANISOU 3693  CB  ALA A 447     6131   6307   5777   -106    271  -1134       C  
ATOM   3694  N   GLU A 448       3.112 -12.505  -2.434  1.00 47.76           N  
ANISOU 3694  N   GLU A 448     6157   6301   5690   -179    295  -1264       N  
ATOM   3695  CA  GLU A 448       1.853 -12.818  -3.090  1.00 47.96           C  
ANISOU 3695  CA  GLU A 448     6235   6332   5655   -216    268  -1247       C  
ATOM   3696  C   GLU A 448       0.700 -12.159  -2.340  1.00 44.57           C  
ANISOU 3696  C   GLU A 448     5849   5886   5199   -201    200  -1116       C  
ATOM   3697  O   GLU A 448       0.791 -11.897  -1.132  1.00 42.51           O  
ANISOU 3697  O   GLU A 448     5571   5587   4995   -149    168  -1050       O  
ATOM   3698  CB  GLU A 448       1.648 -14.334  -3.254  1.00 50.94           C  
ANISOU 3698  CB  GLU A 448     6588   6654   6114   -191    262  -1325       C  
ATOM   3699  CG  GLU A 448       1.270 -15.112  -1.995  1.00 55.40           C  
ANISOU 3699  CG  GLU A 448     7126   7129   6793   -114    198  -1276       C  
ATOM   3700  CD  GLU A 448       1.093 -16.618  -2.258  1.00 62.55           C  
ANISOU 3700  CD  GLU A 448     8006   7979   7782    -95    191  -1357       C  
ATOM   3701  OE1 GLU A 448       0.846 -17.016  -3.427  1.00 63.43           O  
ANISOU 3701  OE1 GLU A 448     8138   8120   7841   -145    224  -1432       O  
ATOM   3702  OE2 GLU A 448       1.197 -17.402  -1.286  1.00 61.31           O  
ANISOU 3702  OE2 GLU A 448     7809   7746   7742    -33    149  -1343       O  
ATOM   3703  N   ARG A 449      -0.369 -11.874  -3.072  1.00 41.77           N  
ANISOU 3703  N   ARG A 449     5550   5561   4760   -253    179  -1079       N  
ATOM   3704  CA  ARG A 449      -1.537 -11.219  -2.510  1.00 41.38           C  
ANISOU 3704  CA  ARG A 449     5538   5496   4688   -247    119   -962       C  
ATOM   3705  C   ARG A 449      -2.175 -12.109  -1.433  1.00 39.39           C  
ANISOU 3705  C   ARG A 449     5269   5165   4533   -181     70   -927       C  
ATOM   3706  O   ARG A 449      -2.460 -13.286  -1.687  1.00 38.39           O  
ANISOU 3706  O   ARG A 449     5133   5004   4448   -172     61   -978       O  
ATOM   3707  CB  ARG A 449      -2.527 -10.864  -3.622  1.00 42.69           C  
ANISOU 3707  CB  ARG A 449     5760   5704   4757   -321    102   -937       C  
ATOM   3708  CG  ARG A 449      -3.525  -9.806  -3.230  1.00 44.69           C  
ANISOU 3708  CG  ARG A 449     6047   5956   4979   -328     52   -817       C  
ATOM   3709  CD  ARG A 449      -4.079  -9.069  -4.443  1.00 48.22           C  
ANISOU 3709  CD  ARG A 449     6543   6459   5319   -415     41   -791       C  
ATOM   3710  NE  ARG A 449      -5.151  -8.162  -4.038  1.00 47.35           N  
ANISOU 3710  NE  ARG A 449     6455   6332   5203   -416    -15   -676       N  
ATOM   3711  CZ  ARG A 449      -6.447  -8.382  -4.246  1.00 44.81           C  
ANISOU 3711  CZ  ARG A 449     6159   5985   4884   -431    -69   -625       C  
ATOM   3712  NH1 ARG A 449      -6.849  -9.471  -4.890  1.00 47.07           N  
ANISOU 3712  NH1 ARG A 449     6457   6262   5166   -451    -76   -676       N  
ATOM   3713  NH2 ARG A 449      -7.342  -7.500  -3.829  1.00 40.54           N  
ANISOU 3713  NH2 ARG A 449     5628   5423   4351   -429   -114   -526       N  
ATOM   3714  N   PRO A 450      -2.361 -11.558  -0.216  1.00 35.98           N  
ANISOU 3714  N   PRO A 450     4833   4704   4135   -140     40   -843       N  
ATOM   3715  CA  PRO A 450      -2.882 -12.323   0.922  1.00 35.15           C  
ANISOU 3715  CA  PRO A 450     4713   4528   4115    -84     -5   -804       C  
ATOM   3716  C   PRO A 450      -4.237 -12.978   0.668  1.00 34.89           C  
ANISOU 3716  C   PRO A 450     4706   4467   4082    -93    -46   -779       C  
ATOM   3717  O   PRO A 450      -4.383 -14.167   0.919  1.00 35.58           O  
ANISOU 3717  O   PRO A 450     4775   4506   4239    -64    -66   -809       O  
ATOM   3718  CB  PRO A 450      -2.994 -11.269   2.029  1.00 34.05           C  
ANISOU 3718  CB  PRO A 450     4581   4384   3973    -64    -21   -714       C  
ATOM   3719  CG  PRO A 450      -1.945 -10.288   1.704  1.00 34.41           C  
ANISOU 3719  CG  PRO A 450     4620   4482   3972    -85     21   -733       C  
ATOM   3720  CD  PRO A 450      -1.890 -10.224   0.199  1.00 34.25           C  
ANISOU 3720  CD  PRO A 450     4617   4517   3879   -144     52   -791       C  
ATOM   3721  N   SER A 451      -5.216 -12.212   0.182  1.00 36.75           N  
ANISOU 3721  N   SER A 451     4982   4731   4249   -133    -63   -721       N  
ATOM   3722  CA  SER A 451      -6.565 -12.744  -0.047  1.00 35.58           C  
ANISOU 3722  CA  SER A 451     4858   4557   4105   -144   -106   -688       C  
ATOM   3723  C   SER A 451      -7.288 -12.071  -1.200  1.00 36.67           C  
ANISOU 3723  C   SER A 451     5037   4739   4156   -211   -115   -665       C  
ATOM   3724  O   SER A 451      -7.148 -10.866  -1.424  1.00 35.23           O  
ANISOU 3724  O   SER A 451     4870   4599   3918   -241   -106   -627       O  
ATOM   3725  CB  SER A 451      -7.434 -12.650   1.216  1.00 32.82           C  
ANISOU 3725  CB  SER A 451     4506   4157   3807   -104   -145   -601       C  
ATOM   3726  OG  SER A 451      -8.734 -13.180   0.967  1.00 30.35           O  
ANISOU 3726  OG  SER A 451     4211   3818   3503   -116   -186   -570       O  
ATOM   3727  N   ASP A 452      -8.068 -12.875  -1.916  1.00 37.88           N  
ANISOU 3727  N   ASP A 452     5208   4881   4302   -236   -140   -684       N  
ATOM   3728  CA  ASP A 452      -8.964 -12.381  -2.954  1.00 40.04           C  
ANISOU 3728  CA  ASP A 452     5524   5187   4504   -303   -167   -649       C  
ATOM   3729  C   ASP A 452     -10.396 -12.230  -2.437  1.00 37.21           C  
ANISOU 3729  C   ASP A 452     5173   4785   4179   -291   -225   -554       C  
ATOM   3730  O   ASP A 452     -11.290 -11.833  -3.180  1.00 36.29           O  
ANISOU 3730  O   ASP A 452     5087   4682   4021   -342   -260   -509       O  
ATOM   3731  CB  ASP A 452      -8.926 -13.314  -4.162  1.00 43.45           C  
ANISOU 3731  CB  ASP A 452     5975   5638   4898   -351   -159   -733       C  
ATOM   3732  CG  ASP A 452      -7.998 -12.818  -5.247  1.00 53.14           C  
ANISOU 3732  CG  ASP A 452     7220   6937   6036   -415   -110   -795       C  
ATOM   3733  OD1 ASP A 452      -8.318 -11.775  -5.871  1.00 59.12           O  
ANISOU 3733  OD1 ASP A 452     8010   7738   6714   -476   -125   -743       O  
ATOM   3734  OD2 ASP A 452      -6.957 -13.472  -5.481  1.00 55.11           O  
ANISOU 3734  OD2 ASP A 452     7446   7196   6296   -408    -58   -897       O  
ATOM   3735  N   VAL A 453     -10.599 -12.540  -1.158  1.00 35.89           N  
ANISOU 3735  N   VAL A 453     4979   4566   4091   -227   -234   -521       N  
ATOM   3736  CA  VAL A 453     -11.935 -12.558  -0.554  1.00 36.78           C  
ANISOU 3736  CA  VAL A 453     5092   4634   4249   -212   -279   -442       C  
ATOM   3737  C   VAL A 453     -12.053 -11.611   0.638  1.00 36.04           C  
ANISOU 3737  C   VAL A 453     4984   4525   4186   -177   -273   -373       C  
ATOM   3738  O   VAL A 453     -13.028 -10.868   0.754  1.00 38.83           O  
ANISOU 3738  O   VAL A 453     5342   4868   4544   -190   -298   -301       O  
ATOM   3739  CB  VAL A 453     -12.332 -13.990  -0.102  1.00 35.89           C  
ANISOU 3739  CB  VAL A 453     4965   4467   4204   -176   -301   -465       C  
ATOM   3740  CG1 VAL A 453     -13.645 -13.981   0.678  1.00 35.36           C  
ANISOU 3740  CG1 VAL A 453     4893   4355   4188   -158   -340   -382       C  
ATOM   3741  CG2 VAL A 453     -12.439 -14.908  -1.300  1.00 37.32           C  
ANISOU 3741  CG2 VAL A 453     5164   4657   4358   -214   -311   -529       C  
ATOM   3742  N   TYR A 454     -11.052 -11.642   1.511  1.00 34.43           N  
ANISOU 3742  N   TYR A 454     4758   4317   4006   -137   -241   -397       N  
ATOM   3743  CA  TYR A 454     -11.121 -10.965   2.797  1.00 31.85           C  
ANISOU 3743  CA  TYR A 454     4419   3970   3713   -104   -234   -342       C  
ATOM   3744  C   TYR A 454     -10.139  -9.800   2.884  1.00 31.13           C  
ANISOU 3744  C   TYR A 454     4328   3919   3583   -109   -199   -342       C  
ATOM   3745  O   TYR A 454      -9.253  -9.666   2.047  1.00 32.12           O  
ANISOU 3745  O   TYR A 454     4456   4085   3661   -132   -177   -393       O  
ATOM   3746  CB  TYR A 454     -10.844 -11.966   3.917  1.00 31.84           C  
ANISOU 3746  CB  TYR A 454     4397   3925   3776    -57   -236   -355       C  
ATOM   3747  CG  TYR A 454     -11.795 -13.146   3.961  1.00 28.73           C  
ANISOU 3747  CG  TYR A 454     4002   3487   3428    -50   -272   -350       C  
ATOM   3748  CD1 TYR A 454     -13.162 -12.967   4.216  1.00 32.16           C  
ANISOU 3748  CD1 TYR A 454     4442   3897   3881    -57   -298   -285       C  
ATOM   3749  CD2 TYR A 454     -11.329 -14.442   3.767  1.00 29.66           C  
ANISOU 3749  CD2 TYR A 454     4108   3584   3577    -36   -281   -411       C  
ATOM   3750  CE1 TYR A 454     -14.040 -14.056   4.264  1.00 32.47           C  
ANISOU 3750  CE1 TYR A 454     4479   3897   3963    -52   -333   -278       C  
ATOM   3751  CE2 TYR A 454     -12.195 -15.536   3.815  1.00 32.03           C  
ANISOU 3751  CE2 TYR A 454     4407   3841   3921    -30   -318   -405       C  
ATOM   3752  CZ  TYR A 454     -13.544 -15.336   4.069  1.00 34.72           C  
ANISOU 3752  CZ  TYR A 454     4757   4163   4273    -39   -344   -337       C  
ATOM   3753  OH  TYR A 454     -14.392 -16.423   4.123  1.00 43.40           O  
ANISOU 3753  OH  TYR A 454     5854   5221   5417    -36   -381   -329       O  
ATOM   3754  N   SER A 455     -10.320  -8.960   3.900  1.00 29.27           N  
ANISOU 3754  N   SER A 455     4086   3669   3366    -90   -192   -289       N  
ATOM   3755  CA  SER A 455      -9.463  -7.809   4.149  1.00 30.44           C  
ANISOU 3755  CA  SER A 455     4233   3848   3485    -92   -163   -282       C  
ATOM   3756  C   SER A 455      -8.315  -8.186   5.092  1.00 29.22           C  
ANISOU 3756  C   SER A 455     4062   3685   3355    -56   -140   -314       C  
ATOM   3757  O   SER A 455      -8.545  -8.755   6.160  1.00 30.94           O  
ANISOU 3757  O   SER A 455     4271   3863   3620    -27   -150   -297       O  
ATOM   3758  CB  SER A 455     -10.301  -6.669   4.740  1.00 29.43           C  
ANISOU 3758  CB  SER A 455     4108   3706   3369    -94   -167   -210       C  
ATOM   3759  OG  SER A 455      -9.482  -5.717   5.385  1.00 31.81           O  
ANISOU 3759  OG  SER A 455     4406   4022   3659    -85   -139   -203       O  
ATOM   3760  N   CYS A 456      -7.085  -7.851   4.715  1.00 28.88           N  
ANISOU 3760  N   CYS A 456     4013   3679   3281    -63   -113   -356       N  
ATOM   3761  CA  CYS A 456      -5.921  -8.380   5.432  1.00 29.79           C  
ANISOU 3761  CA  CYS A 456     4106   3783   3429    -31    -99   -393       C  
ATOM   3762  C   CYS A 456      -4.969  -7.382   6.080  1.00 28.60           C  
ANISOU 3762  C   CYS A 456     3950   3650   3265    -25    -75   -380       C  
ATOM   3763  O   CYS A 456      -4.887  -6.214   5.686  1.00 30.20           O  
ANISOU 3763  O   CYS A 456     4165   3889   3421    -49    -60   -360       O  
ATOM   3764  CB  CYS A 456      -5.116  -9.302   4.516  1.00 30.86           C  
ANISOU 3764  CB  CYS A 456     4225   3933   3566    -36    -87   -476       C  
ATOM   3765  SG  CYS A 456      -6.138 -10.459   3.608  1.00 36.32           S  
ANISOU 3765  SG  CYS A 456     4927   4608   4266    -50   -113   -502       S  
ATOM   3766  N   SER A 457      -4.245  -7.874   7.080  1.00 28.97           N  
ANISOU 3766  N   SER A 457     3980   3671   3357      6    -78   -389       N  
ATOM   3767  CA  SER A 457      -3.076  -7.191   7.621  1.00 28.84           C  
ANISOU 3767  CA  SER A 457     3953   3671   3336     12    -59   -391       C  
ATOM   3768  C   SER A 457      -1.891  -8.132   7.480  1.00 29.41           C  
ANISOU 3768  C   SER A 457     3990   3734   3449     30    -56   -456       C  
ATOM   3769  O   SER A 457      -2.065  -9.347   7.603  1.00 29.29           O  
ANISOU 3769  O   SER A 457     3961   3681   3486     48    -79   -478       O  
ATOM   3770  CB  SER A 457      -3.292  -6.826   9.087  1.00 28.28           C  
ANISOU 3770  CB  SER A 457     3892   3569   3284     26    -71   -335       C  
ATOM   3771  OG  SER A 457      -2.049  -6.673   9.758  1.00 33.55           O  
ANISOU 3771  OG  SER A 457     4544   4236   3966     37    -67   -345       O  
ATOM   3772  N   PRO A 458      -0.681  -7.581   7.227  1.00 30.95           N  
ANISOU 3772  N   PRO A 458     4168   3961   3629     24    -28   -487       N  
ATOM   3773  CA  PRO A 458       0.529  -8.384   6.994  1.00 30.10           C  
ANISOU 3773  CA  PRO A 458     4017   3847   3571     40    -19   -557       C  
ATOM   3774  C   PRO A 458       1.000  -9.226   8.188  1.00 32.95           C  
ANISOU 3774  C   PRO A 458     4354   4150   4016     75    -55   -547       C  
ATOM   3775  O   PRO A 458       2.025  -9.901   8.086  1.00 35.62           O  
ANISOU 3775  O   PRO A 458     4649   4472   4414     91    -53   -601       O  
ATOM   3776  CB  PRO A 458       1.586  -7.329   6.636  1.00 32.43           C  
ANISOU 3776  CB  PRO A 458     4304   4192   3827     22     19   -573       C  
ATOM   3777  CG  PRO A 458       1.078  -6.062   7.261  1.00 33.11           C  
ANISOU 3777  CG  PRO A 458     4425   4290   3865     10     13   -497       C  
ATOM   3778  CD  PRO A 458      -0.404  -6.140   7.060  1.00 31.02           C  
ANISOU 3778  CD  PRO A 458     4192   4015   3578      1     -4   -461       C  
ATOM   3779  N   ASN A 459       0.270  -9.196   9.301  1.00 31.44           N  
ANISOU 3779  N   ASN A 459     4187   3927   3832     81    -88   -479       N  
ATOM   3780  CA  ASN A 459       0.557 -10.107  10.407  1.00 30.87           C  
ANISOU 3780  CA  ASN A 459     4099   3798   3834    103   -133   -462       C  
ATOM   3781  C   ASN A 459      -0.058 -11.479  10.165  1.00 31.30           C  
ANISOU 3781  C   ASN A 459     4141   3810   3941    117   -162   -485       C  
ATOM   3782  O   ASN A 459       0.187 -12.414  10.923  1.00 31.09           O  
ANISOU 3782  O   ASN A 459     4095   3731   3986    133   -205   -476       O  
ATOM   3783  CB  ASN A 459       0.073  -9.535  11.759  1.00 31.20           C  
ANISOU 3783  CB  ASN A 459     4175   3825   3855     95   -154   -382       C  
ATOM   3784  CG  ASN A 459      -1.421  -9.648  11.940  1.00 28.30           C  
ANISOU 3784  CG  ASN A 459     3842   3447   3465     85   -162   -342       C  
ATOM   3785  OD1 ASN A 459      -2.186  -9.505  10.989  1.00 36.24           O  
ANISOU 3785  OD1 ASN A 459     4857   4475   4440     78   -142   -356       O  
ATOM   3786  ND2 ASN A 459      -1.850  -9.906  13.167  1.00 29.51           N  
ANISOU 3786  ND2 ASN A 459     4014   3566   3634     81   -192   -289       N  
ATOM   3787  N   GLY A 460      -0.867 -11.589   9.112  1.00 29.97           N  
ANISOU 3787  N   GLY A 460     3986   3664   3738    106   -143   -510       N  
ATOM   3788  CA  GLY A 460      -1.505 -12.852   8.763  1.00 27.63           C  
ANISOU 3788  CA  GLY A 460     3681   3330   3486    115   -168   -535       C  
ATOM   3789  C   GLY A 460      -2.999 -12.929   8.985  1.00 27.94           C  
ANISOU 3789  C   GLY A 460     3757   3359   3501    105   -188   -481       C  
ATOM   3790  O   GLY A 460      -3.599 -13.956   8.726  1.00 28.58           O  
ANISOU 3790  O   GLY A 460     3834   3409   3618    111   -212   -496       O  
ATOM   3791  N   MET A 461      -3.613 -11.852   9.458  1.00 29.77           N  
ANISOU 3791  N   MET A 461     4021   3613   3679     90   -177   -420       N  
ATOM   3792  CA  MET A 461      -5.035 -11.905   9.790  1.00 29.55           C  
ANISOU 3792  CA  MET A 461     4020   3568   3639     81   -193   -367       C  
ATOM   3793  C   MET A 461      -5.918 -11.481   8.621  1.00 31.58           C  
ANISOU 3793  C   MET A 461     4294   3857   3849     60   -175   -374       C  
ATOM   3794  O   MET A 461      -5.550 -10.605   7.824  1.00 30.71           O  
ANISOU 3794  O   MET A 461     4187   3791   3689     44   -146   -392       O  
ATOM   3795  CB  MET A 461      -5.341 -11.071  11.037  1.00 30.09           C  
ANISOU 3795  CB  MET A 461     4111   3633   3688     73   -191   -301       C  
ATOM   3796  CG  MET A 461      -4.770 -11.641  12.348  1.00 29.51           C  
ANISOU 3796  CG  MET A 461     4031   3521   3658     81   -222   -277       C  
ATOM   3797  SD  MET A 461      -5.414 -13.267  12.836  1.00 35.84           S  
ANISOU 3797  SD  MET A 461     4827   4263   4527     88   -277   -264       S  
ATOM   3798  CE  MET A 461      -7.096 -12.852  13.286  1.00 32.22           C  
ANISOU 3798  CE  MET A 461     4403   3806   4034     66   -266   -204       C  
ATOM   3799  N   MET A 462      -7.077 -12.123   8.518  1.00 30.36           N  
ANISOU 3799  N   MET A 462     4148   3677   3710     57   -199   -355       N  
ATOM   3800  CA  MET A 462      -8.061 -11.793   7.499  1.00 31.65           C  
ANISOU 3800  CA  MET A 462     4327   3861   3836     34   -195   -349       C  
ATOM   3801  C   MET A 462      -9.357 -11.409   8.182  1.00 31.23           C  
ANISOU 3801  C   MET A 462     4290   3789   3788     28   -205   -280       C  
ATOM   3802  O   MET A 462      -9.702 -11.964   9.224  1.00 30.79           O  
ANISOU 3802  O   MET A 462     4233   3697   3770     40   -222   -251       O  
ATOM   3803  CB  MET A 462      -8.297 -12.981   6.562  1.00 34.50           C  
ANISOU 3803  CB  MET A 462     4682   4210   4218     32   -215   -399       C  
ATOM   3804  CG  MET A 462      -7.039 -13.478   5.866  1.00 36.48           C  
ANISOU 3804  CG  MET A 462     4912   4475   4476     37   -197   -481       C  
ATOM   3805  SD  MET A 462      -7.342 -14.716   4.601  1.00 39.04           S  
ANISOU 3805  SD  MET A 462     5232   4790   4813     25   -209   -551       S  
ATOM   3806  CE  MET A 462      -8.218 -15.988   5.521  1.00 43.96           C  
ANISOU 3806  CE  MET A 462     5847   5340   5514     51   -262   -516       C  
ATOM   3807  N   TYR A 463     -10.073 -10.455   7.597  1.00 31.38           N  
ANISOU 3807  N   TYR A 463     4321   3830   3770      6   -195   -253       N  
ATOM   3808  CA  TYR A 463     -11.332  -9.995   8.177  1.00 32.20           C  
ANISOU 3808  CA  TYR A 463     4431   3914   3890      0   -199   -193       C  
ATOM   3809  C   TYR A 463     -12.462  -9.949   7.156  1.00 32.64           C  
ANISOU 3809  C   TYR A 463     4492   3970   3941    -22   -220   -177       C  
ATOM   3810  O   TYR A 463     -12.214  -9.814   5.952  1.00 31.72           O  
ANISOU 3810  O   TYR A 463     4382   3883   3788    -43   -224   -204       O  
ATOM   3811  CB  TYR A 463     -11.135  -8.631   8.844  1.00 30.97           C  
ANISOU 3811  CB  TYR A 463     4280   3773   3715     -3   -169   -161       C  
ATOM   3812  CG  TYR A 463     -10.051  -8.645   9.902  1.00 31.82           C  
ANISOU 3812  CG  TYR A 463     4387   3880   3824     12   -154   -171       C  
ATOM   3813  CD1 TYR A 463      -8.716  -8.405   9.563  1.00 31.21           C  
ANISOU 3813  CD1 TYR A 463     4305   3831   3722     16   -142   -209       C  
ATOM   3814  CD2 TYR A 463     -10.355  -8.922  11.229  1.00 28.55           C  
ANISOU 3814  CD2 TYR A 463     3976   3435   3436     18   -155   -141       C  
ATOM   3815  CE1 TYR A 463      -7.717  -8.424  10.518  1.00 32.49           C  
ANISOU 3815  CE1 TYR A 463     4464   3989   3891     28   -136   -213       C  
ATOM   3816  CE2 TYR A 463      -9.365  -8.936  12.202  1.00 31.87           C  
ANISOU 3816  CE2 TYR A 463     4401   3854   3855     24   -150   -143       C  
ATOM   3817  CZ  TYR A 463      -8.045  -8.686  11.838  1.00 33.97           C  
ANISOU 3817  CZ  TYR A 463     4659   4144   4102     31   -144   -178       C  
ATOM   3818  OH  TYR A 463      -7.059  -8.695  12.792  1.00 28.64           O  
ANISOU 3818  OH  TYR A 463     3985   3465   3432     35   -146   -176       O  
ATOM   3819  N   TYR A 464     -13.701 -10.069   7.638  1.00 32.83           N  
ANISOU 3819  N   TYR A 464     4512   3961   4002    -23   -232   -133       N  
ATOM   3820  CA  TYR A 464     -14.875  -9.997   6.758  1.00 32.90           C  
ANISOU 3820  CA  TYR A 464     4520   3962   4017    -45   -259   -108       C  
ATOM   3821  C   TYR A 464     -14.964  -8.630   6.096  1.00 32.75           C  
ANISOU 3821  C   TYR A 464     4505   3970   3969    -69   -252    -85       C  
ATOM   3822  O   TYR A 464     -14.510  -7.626   6.653  1.00 32.43           O  
ANISOU 3822  O   TYR A 464     4463   3941   3920    -64   -223    -73       O  
ATOM   3823  CB  TYR A 464     -16.175 -10.272   7.523  1.00 31.78           C  
ANISOU 3823  CB  TYR A 464     4367   3777   3931    -41   -268    -62       C  
ATOM   3824  CG  TYR A 464     -16.262 -11.643   8.145  1.00 33.78           C  
ANISOU 3824  CG  TYR A 464     4618   4000   4215    -25   -283    -73       C  
ATOM   3825  CD1 TYR A 464     -16.704 -11.806   9.453  1.00 32.08           C  
ANISOU 3825  CD1 TYR A 464     4397   3758   4034    -16   -270    -43       C  
ATOM   3826  CD2 TYR A 464     -15.895 -12.784   7.425  1.00 37.13           C  
ANISOU 3826  CD2 TYR A 464     5047   4423   4637    -22   -312   -116       C  
ATOM   3827  CE1 TYR A 464     -16.779 -13.081  10.036  1.00 38.84           C  
ANISOU 3827  CE1 TYR A 464     5253   4586   4920     -8   -291    -46       C  
ATOM   3828  CE2 TYR A 464     -15.965 -14.055   7.992  1.00 38.89           C  
ANISOU 3828  CE2 TYR A 464     5265   4612   4898     -8   -333   -124       C  
ATOM   3829  CZ  TYR A 464     -16.405 -14.200   9.297  1.00 40.93           C  
ANISOU 3829  CZ  TYR A 464     5519   4843   5188     -2   -327    -85       C  
ATOM   3830  OH  TYR A 464     -16.474 -15.465   9.851  1.00 44.13           O  
ANISOU 3830  OH  TYR A 464     5922   5215   5632      6   -355    -86       O  
ATOM   3831  N   LYS A 465     -15.554  -8.597   4.912  1.00 33.53           N  
ANISOU 3831  N   LYS A 465     4609   4076   4053   -100   -284    -76       N  
ATOM   3832  CA  LYS A 465     -15.749  -7.345   4.195  1.00 34.54           C  
ANISOU 3832  CA  LYS A 465     4741   4223   4158   -131   -292    -45       C  
ATOM   3833  C   LYS A 465     -17.224  -6.996   3.986  1.00 35.76           C  
ANISOU 3833  C   LYS A 465     4881   4343   4363   -148   -327     15       C  
ATOM   3834  O   LYS A 465     -17.543  -5.922   3.457  1.00 36.32           O  
ANISOU 3834  O   LYS A 465     4949   4419   4433   -175   -344     52       O  
ATOM   3835  CB  LYS A 465     -15.026  -7.388   2.851  1.00 32.51           C  
ANISOU 3835  CB  LYS A 465     4506   4013   3832   -168   -305    -82       C  
ATOM   3836  CG  LYS A 465     -13.516  -7.354   2.958  1.00 31.98           C  
ANISOU 3836  CG  LYS A 465     4446   3985   3721   -156   -265   -137       C  
ATOM   3837  CD  LYS A 465     -12.853  -7.332   1.570  1.00 34.32           C  
ANISOU 3837  CD  LYS A 465     4764   4331   3944   -202   -269   -177       C  
ATOM   3838  CE  LYS A 465     -12.797  -5.918   0.992  1.00 32.36           C  
ANISOU 3838  CE  LYS A 465     4525   4113   3656   -242   -276   -138       C  
ATOM   3839  NZ  LYS A 465     -11.939  -5.861  -0.228  1.00 33.57           N  
ANISOU 3839  NZ  LYS A 465     4702   4324   3729   -292   -269   -183       N  
ATOM   3840  N   ASP A 466     -18.121  -7.888   4.397  1.00 37.37           N  
ANISOU 3840  N   ASP A 466     5074   4509   4618   -134   -341     26       N  
ATOM   3841  CA  ASP A 466     -19.542  -7.699   4.100  1.00 41.72           C  
ANISOU 3841  CA  ASP A 466     5606   5024   5223   -152   -379     80       C  
ATOM   3842  C   ASP A 466     -20.198  -6.628   4.974  1.00 43.79           C  
ANISOU 3842  C   ASP A 466     5836   5254   5548   -139   -355    124       C  
ATOM   3843  O   ASP A 466     -21.096  -5.915   4.520  1.00 46.01           O  
ANISOU 3843  O   ASP A 466     6097   5512   5872   -160   -385    171       O  
ATOM   3844  CB  ASP A 466     -20.305  -9.022   4.194  1.00 41.65           C  
ANISOU 3844  CB  ASP A 466     5592   4984   5248   -144   -403     77       C  
ATOM   3845  CG  ASP A 466     -20.367  -9.568   5.612  1.00 45.92           C  
ANISOU 3845  CG  ASP A 466     6120   5500   5829   -107   -366     72       C  
ATOM   3846  OD1 ASP A 466     -19.300  -9.752   6.239  1.00 44.10           O  
ANISOU 3846  OD1 ASP A 466     5900   5288   5568    -87   -333     35       O  
ATOM   3847  OD2 ASP A 466     -21.492  -9.817   6.094  1.00 47.85           O  
ANISOU 3847  OD2 ASP A 466     6341   5705   6136   -104   -373    105       O  
ATOM   3848  N   ARG A 467     -19.732  -6.517   6.216  1.00 44.53           N  
ANISOU 3848  N   ARG A 467     5925   5345   5649   -108   -302    107       N  
ATOM   3849  CA  ARG A 467     -20.310  -5.614   7.205  1.00 46.62           C  
ANISOU 3849  CA  ARG A 467     6160   5580   5972    -97   -266    135       C  
ATOM   3850  C   ARG A 467     -19.241  -5.119   8.174  1.00 45.11           C  
ANISOU 3850  C   ARG A 467     5980   5410   5748    -79   -212    107       C  
ATOM   3851  O   ARG A 467     -18.254  -5.818   8.427  1.00 44.85           O  
ANISOU 3851  O   ARG A 467     5971   5403   5666    -67   -202     71       O  
ATOM   3852  CB  ARG A 467     -21.433  -6.319   7.985  1.00 48.68           C  
ANISOU 3852  CB  ARG A 467     6397   5798   6299    -87   -258    151       C  
ATOM   3853  CG  ARG A 467     -21.015  -7.630   8.659  1.00 55.82           C  
ANISOU 3853  CG  ARG A 467     7321   6708   7179    -71   -247    120       C  
ATOM   3854  CD  ARG A 467     -22.177  -8.304   9.391  1.00 66.05           C  
ANISOU 3854  CD  ARG A 467     8594   7964   8538    -69   -241    142       C  
ATOM   3855  NE  ARG A 467     -22.036  -9.765   9.415  1.00 71.73           N  
ANISOU 3855  NE  ARG A 467     9331   8683   9241    -65   -266    125       N  
ATOM   3856  CZ  ARG A 467     -21.472 -10.469  10.397  1.00 74.97           C  
ANISOU 3856  CZ  ARG A 467     9756   9096   9633    -54   -245    106       C  
ATOM   3857  NH1 ARG A 467     -20.982  -9.866  11.476  1.00 74.14           N  
ANISOU 3857  NH1 ARG A 467     9656   9000   9514    -50   -196    100       N  
ATOM   3858  NH2 ARG A 467     -21.400 -11.792  10.298  1.00 76.29           N  
ANISOU 3858  NH2 ARG A 467     9935   9255   9797    -51   -278     94       N  
ATOM   3859  N   ASP A 468     -19.453  -3.921   8.718  1.00 43.55           N  
ANISOU 3859  N   ASP A 468     5765   5199   5585    -77   -181    125       N  
ATOM   3860  CA  ASP A 468     -18.554  -3.329   9.713  1.00 41.60           C  
ANISOU 3860  CA  ASP A 468     5527   4967   5310    -65   -129    102       C  
ATOM   3861  C   ASP A 468     -18.685  -4.003  11.069  1.00 37.69           C  
ANISOU 3861  C   ASP A 468     5036   4459   4827    -53    -89     89       C  
ATOM   3862  O   ASP A 468     -19.789  -4.270  11.535  1.00 39.80           O  
ANISOU 3862  O   ASP A 468     5280   4691   5150    -55    -79    106       O  
ATOM   3863  CB  ASP A 468     -18.830  -1.831   9.868  1.00 43.01           C  
ANISOU 3863  CB  ASP A 468     5683   5129   5528    -70   -108    122       C  
ATOM   3864  CG  ASP A 468     -18.273  -1.003   8.719  1.00 48.28           C  
ANISOU 3864  CG  ASP A 468     6359   5822   6165    -87   -143    134       C  
ATOM   3865  OD1 ASP A 468     -17.222  -1.374   8.156  1.00 50.20           O  
ANISOU 3865  OD1 ASP A 468     6632   6108   6334    -92   -157    111       O  
ATOM   3866  OD2 ASP A 468     -18.875   0.043   8.390  1.00 53.82           O  
ANISOU 3866  OD2 ASP A 468     7034   6497   6919    -99   -156    166       O  
ATOM   3867  N   GLY A 469     -17.547  -4.281  11.694  1.00 40.30           N  
ANISOU 3867  N   GLY A 469     5626   4944   4742   -331   -232   -596       N  
ATOM   3868  CA  GLY A 469     -17.520  -4.731  13.083  1.00 35.59           C  
ANISOU 3868  CA  GLY A 469     4897   4372   4252   -311   -115   -581       C  
ATOM   3869  C   GLY A 469     -17.872  -3.608  14.043  1.00 33.90           C  
ANISOU 3869  C   GLY A 469     4566   4192   4124   -285    -66   -533       C  
ATOM   3870  O   GLY A 469     -17.812  -2.422  13.683  1.00 32.51           O  
ANISOU 3870  O   GLY A 469     4406   4040   3906   -275    -97   -513       O  
ATOM   3871  N   VAL A 470     -18.238  -3.984  15.267  1.00 32.60           N  
ANISOU 3871  N   VAL A 470     4299   4019   4069   -275     20   -513       N  
ATOM   3872  CA  VAL A 470     -18.628  -3.033  16.310  1.00 29.39           C  
ANISOU 3872  CA  VAL A 470     3806   3622   3740   -248     95   -470       C  
ATOM   3873  C   VAL A 470     -17.455  -2.151  16.769  1.00 30.30           C  
ANISOU 3873  C   VAL A 470     3979   3799   3736   -212    175   -462       C  
ATOM   3874  O   VAL A 470     -17.648  -0.996  17.145  1.00 32.81           O  
ANISOU 3874  O   VAL A 470     4268   4128   4069   -192    195   -433       O  
ATOM   3875  CB  VAL A 470     -19.322  -3.761  17.504  1.00 30.84           C  
ANISOU 3875  CB  VAL A 470     3902   3757   4059   -247    190   -451       C  
ATOM   3876  CG1 VAL A 470     -18.343  -4.622  18.295  1.00 28.79           C  
ANISOU 3876  CG1 VAL A 470     3703   3518   3719   -235    290   -468       C  
ATOM   3877  CG2 VAL A 470     -20.052  -2.779  18.415  1.00 30.63           C  
ANISOU 3877  CG2 VAL A 470     3797   3706   4136   -221    272   -406       C  
ATOM   3878  N   VAL A 471     -16.239  -2.680  16.722  1.00 29.90           N  
ANISOU 3878  N   VAL A 471     4003   3776   3582   -205    215   -485       N  
ATOM   3879  CA  VAL A 471     -15.067  -1.854  17.024  1.00 30.85           C  
ANISOU 3879  CA  VAL A 471     4167   3937   3618   -177    264   -470       C  
ATOM   3880  C   VAL A 471     -14.887  -0.733  15.984  1.00 28.81           C  
ANISOU 3880  C   VAL A 471     3944   3705   3296   -175    206   -465       C  
ATOM   3881  O   VAL A 471     -14.874   0.430  16.361  1.00 29.93           O  
ANISOU 3881  O   VAL A 471     4067   3866   3438   -156    214   -436       O  
ATOM   3882  CB  VAL A 471     -13.782  -2.694  17.260  1.00 31.61           C  
ANISOU 3882  CB  VAL A 471     4309   4035   3667   -170    320   -484       C  
ATOM   3883  CG1 VAL A 471     -12.534  -1.813  17.247  1.00 29.31           C  
ANISOU 3883  CG1 VAL A 471     4048   3768   3319   -147    344   -463       C  
ATOM   3884  CG2 VAL A 471     -13.887  -3.442  18.589  1.00 31.75           C  
ANISOU 3884  CG2 VAL A 471     4304   4023   3736   -167    376   -474       C  
ATOM   3885  N   PRO A 472     -14.790  -1.068  14.679  1.00 28.60           N  
ANISOU 3885  N   PRO A 472     3989   3670   3207   -194    149   -492       N  
ATOM   3886  CA  PRO A 472     -14.762   0.007  13.678  1.00 28.16           C  
ANISOU 3886  CA  PRO A 472     3989   3626   3085   -195     89   -482       C  
ATOM   3887  C   PRO A 472     -15.957   0.969  13.749  1.00 31.41           C  
ANISOU 3887  C   PRO A 472     4331   4029   3574   -200      6   -453       C  
ATOM   3888  O   PRO A 472     -15.779   2.190  13.658  1.00 32.88           O  
ANISOU 3888  O   PRO A 472     4519   4240   3734   -185     -1   -427       O  
ATOM   3889  CB  PRO A 472     -14.770  -0.749  12.340  1.00 29.49           C  
ANISOU 3889  CB  PRO A 472     4277   3756   3172   -222     31   -519       C  
ATOM   3890  CG  PRO A 472     -14.130  -2.062  12.644  1.00 26.64           C  
ANISOU 3890  CG  PRO A 472     3931   3382   2809   -219    112   -549       C  
ATOM   3891  CD  PRO A 472     -14.469  -2.383  14.083  1.00 27.62           C  
ANISOU 3891  CD  PRO A 472     3930   3518   3047   -211    153   -532       C  
ATOM   3892  N   THR A 473     -17.158   0.432  13.924  1.00 31.86           N  
ANISOU 3892  N   THR A 473     4315   4043   3749   -221    -52   -453       N  
ATOM   3893  CA  THR A 473     -18.358   1.264  13.960  1.00 33.06           C  
ANISOU 3893  CA  THR A 473     4376   4163   4022   -226   -127   -419       C  
ATOM   3894  C   THR A 473     -18.257   2.316  15.063  1.00 32.90           C  
ANISOU 3894  C   THR A 473     4291   4170   4038   -188    -27   -386       C  
ATOM   3895  O   THR A 473     -18.462   3.512  14.818  1.00 32.53           O  
ANISOU 3895  O   THR A 473     4233   4130   3998   -177    -66   -361       O  
ATOM   3896  CB  THR A 473     -19.625   0.402  14.126  1.00 33.00           C  
ANISOU 3896  CB  THR A 473     4270   4083   4184   -253   -183   -415       C  
ATOM   3897  OG1 THR A 473     -19.776  -0.430  12.971  1.00 36.64           O  
ANISOU 3897  OG1 THR A 473     4816   4504   4602   -294   -315   -445       O  
ATOM   3898  CG2 THR A 473     -20.868   1.267  14.262  1.00 37.76           C  
ANISOU 3898  CG2 THR A 473     4747   4634   4965   -253   -241   -369       C  
ATOM   3899  N   GLU A 474     -17.903   1.862  16.261  1.00 30.42           N  
ANISOU 3899  N   GLU A 474     3959   3863   3736   -168     96   -388       N  
ATOM   3900  CA  GLU A 474     -17.886   2.720  17.430  1.00 31.59           C  
ANISOU 3900  CA  GLU A 474     4081   4012   3908   -134    193   -360       C  
ATOM   3901  C   GLU A 474     -16.692   3.649  17.484  1.00 31.18           C  
ANISOU 3901  C   GLU A 474     4102   4010   3734   -113    209   -354       C  
ATOM   3902  O   GLU A 474     -16.812   4.760  17.980  1.00 28.65           O  
ANISOU 3902  O   GLU A 474     3772   3687   3426    -90    235   -330       O  
ATOM   3903  CB  GLU A 474     -17.975   1.890  18.711  1.00 31.14           C  
ANISOU 3903  CB  GLU A 474     4016   3923   3892   -125    309   -360       C  
ATOM   3904  CG  GLU A 474     -19.323   1.180  18.870  1.00 32.78           C  
ANISOU 3904  CG  GLU A 474     4124   4062   4267   -140    323   -351       C  
ATOM   3905  CD  GLU A 474     -20.502   2.142  18.794  1.00 36.11           C  
ANISOU 3905  CD  GLU A 474     4445   4435   4838   -131    310   -315       C  
ATOM   3906  OE1 GLU A 474     -21.516   1.772  18.167  1.00 36.18           O  
ANISOU 3906  OE1 GLU A 474     4358   4392   4997   -157    227   -305       O  
ATOM   3907  OE2 GLU A 474     -20.414   3.264  19.354  1.00 35.41           O  
ANISOU 3907  OE2 GLU A 474     4374   4350   4732    -99    374   -295       O  
ATOM   3908  N   ILE A 475     -15.548   3.193  16.976  1.00 31.55           N  
ANISOU 3908  N   ILE A 475     4218   4090   3682   -120    201   -374       N  
ATOM   3909  CA  ILE A 475     -14.347   4.018  16.959  1.00 29.93           C  
ANISOU 3909  CA  ILE A 475     4062   3916   3394   -102    215   -360       C  
ATOM   3910  C   ILE A 475     -14.516   5.192  15.979  1.00 31.69           C  
ANISOU 3910  C   ILE A 475     4294   4157   3589   -103    149   -344       C  
ATOM   3911  O   ILE A 475     -13.957   6.264  16.206  1.00 32.02           O  
ANISOU 3911  O   ILE A 475     4348   4215   3605    -85    159   -320       O  
ATOM   3912  CB  ILE A 475     -13.061   3.172  16.670  1.00 30.85           C  
ANISOU 3912  CB  ILE A 475     4227   4040   3453   -106    245   -376       C  
ATOM   3913  CG1 ILE A 475     -11.840   3.799  17.334  1.00 28.83           C  
ANISOU 3913  CG1 ILE A 475     3988   3786   3179    -86    276   -348       C  
ATOM   3914  CG2 ILE A 475     -12.850   2.951  15.162  1.00 29.38           C  
ANISOU 3914  CG2 ILE A 475     4096   3861   3207   -122    211   -395       C  
ATOM   3915  CD1 ILE A 475     -10.587   2.941  17.277  1.00 26.14           C  
ANISOU 3915  CD1 ILE A 475     3663   3430   2838    -87    312   -351       C  
ATOM   3916  N   THR A 476     -15.301   4.974  14.917  1.00 31.07           N  
ANISOU 3916  N   THR A 476     4219   4065   3521   -127     67   -355       N  
ATOM   3917  CA  THR A 476     -15.600   5.979  13.886  1.00 32.62           C  
ANISOU 3917  CA  THR A 476     4444   4263   3687   -134    -20   -339       C  
ATOM   3918  C   THR A 476     -16.414   7.158  14.434  1.00 34.43           C  
ANISOU 3918  C   THR A 476     4593   4481   4006   -117    -39   -305       C  
ATOM   3919  O   THR A 476     -16.157   8.312  14.080  1.00 35.66           O  
ANISOU 3919  O   THR A 476     4771   4652   4125   -107    -66   -282       O  
ATOM   3920  CB  THR A 476     -16.385   5.340  12.694  1.00 34.31           C  
ANISOU 3920  CB  THR A 476     4702   4438   3898   -171   -138   -357       C  
ATOM   3921  OG1 THR A 476     -15.595   4.315  12.079  1.00 31.84           O  
ANISOU 3921  OG1 THR A 476     4491   4123   3483   -184   -109   -391       O  
ATOM   3922  CG2 THR A 476     -16.770   6.382  11.632  1.00 33.13           C  
ANISOU 3922  CG2 THR A 476     4602   4271   3713   -184   -256   -334       C  
ATOM   3923  N   LYS A 477     -17.400   6.857  15.282  1.00 34.57           N  
ANISOU 3923  N   LYS A 477     4521   4462   4151   -112    -10   -301       N  
ATOM   3924  CA  LYS A 477     -18.275   7.876  15.869  1.00 35.17           C  
ANISOU 3924  CA  LYS A 477     4517   4506   4340    -91      5   -269       C  
ATOM   3925  C   LYS A 477     -17.478   8.876  16.695  1.00 35.09           C  
ANISOU 3925  C   LYS A 477     4546   4521   4265    -57     85   -256       C  
ATOM   3926  O   LYS A 477     -17.643  10.081  16.534  1.00 36.96           O  
ANISOU 3926  O   LYS A 477     4771   4756   4515    -43     56   -232       O  
ATOM   3927  CB  LYS A 477     -19.375   7.235  16.725  1.00 35.47           C  
ANISOU 3927  CB  LYS A 477     4459   4482   4537    -87     71   -263       C  
ATOM   3928  CG  LYS A 477     -20.472   6.525  15.928  1.00 36.24           C  
ANISOU 3928  CG  LYS A 477     4479   4525   4765   -121    -39   -260       C  
ATOM   3929  CD  LYS A 477     -21.404   5.764  16.852  1.00 37.95           C  
ANISOU 3929  CD  LYS A 477     4595   4674   5152   -117     56   -250       C  
ATOM   3930  CE  LYS A 477     -22.288   4.800  16.096  1.00 46.66           C  
ANISOU 3930  CE  LYS A 477     5627   5718   6384   -159    -66   -249       C  
ATOM   3931  NZ  LYS A 477     -23.280   4.145  17.011  1.00 50.03           N  
ANISOU 3931  NZ  LYS A 477     5929   6062   7018   -153     42   -228       N  
ATOM   3932  N   VAL A 478     -16.606   8.366  17.562  1.00 33.72           N  
ANISOU 3932  N   VAL A 478     4426   4361   4026    -47    168   -270       N  
ATOM   3933  CA  VAL A 478     -15.769   9.209  18.416  1.00 32.94           C  
ANISOU 3933  CA  VAL A 478     4384   4267   3866    -22    216   -257       C  
ATOM   3934  C   VAL A 478     -14.683   9.894  17.601  1.00 33.74           C  
ANISOU 3934  C   VAL A 478     4525   4412   3882    -26    158   -246       C  
ATOM   3935  O   VAL A 478     -14.391  11.067  17.840  1.00 36.77           O  
ANISOU 3935  O   VAL A 478     4925   4794   4251     -9    151   -224       O  
ATOM   3936  CB  VAL A 478     -15.129   8.421  19.589  1.00 32.71           C  
ANISOU 3936  CB  VAL A 478     4414   4217   3798    -16    290   -268       C  
ATOM   3937  CG1 VAL A 478     -14.234   9.334  20.424  1.00 31.73           C  
ANISOU 3937  CG1 VAL A 478     4369   4078   3611      3    298   -251       C  
ATOM   3938  CG2 VAL A 478     -16.198   7.788  20.462  1.00 27.86           C  
ANISOU 3938  CG2 VAL A 478     3777   3547   3262     -9    376   -273       C  
ATOM   3939  N   PHE A 479     -14.094   9.174  16.642  1.00 33.82           N  
ANISOU 3939  N   PHE A 479     4558   4449   3842    -47    129   -260       N  
ATOM   3940  CA  PHE A 479     -13.194   9.796  15.664  1.00 33.70           C  
ANISOU 3940  CA  PHE A 479     4584   4459   3760    -51     99   -245       C  
ATOM   3941  C   PHE A 479     -13.815  11.024  14.982  1.00 34.20           C  
ANISOU 3941  C   PHE A 479     4640   4526   3829    -50     33   -222       C  
ATOM   3942  O   PHE A 479     -13.155  12.057  14.850  1.00 35.07           O  
ANISOU 3942  O   PHE A 479     4770   4646   3909    -39     29   -196       O  
ATOM   3943  CB  PHE A 479     -12.720   8.815  14.582  1.00 33.68           C  
ANISOU 3943  CB  PHE A 479     4631   4465   3702    -72     99   -266       C  
ATOM   3944  CG  PHE A 479     -12.057   9.502  13.416  1.00 38.97           C  
ANISOU 3944  CG  PHE A 479     5364   5143   4301    -76     88   -247       C  
ATOM   3945  CD1 PHE A 479     -10.723   9.920  13.501  1.00 41.78           C  
ANISOU 3945  CD1 PHE A 479     5730   5498   4645    -62    148   -222       C  
ATOM   3946  CD2 PHE A 479     -12.777   9.795  12.259  1.00 36.37           C  
ANISOU 3946  CD2 PHE A 479     5087   4805   3926    -94     11   -248       C  
ATOM   3947  CE1 PHE A 479     -10.113  10.590  12.430  1.00 44.04           C  
ANISOU 3947  CE1 PHE A 479     6077   5780   4877    -63    165   -197       C  
ATOM   3948  CE2 PHE A 479     -12.177  10.465  11.187  1.00 37.40           C  
ANISOU 3948  CE2 PHE A 479     5307   4931   3974    -97     12   -227       C  
ATOM   3949  CZ  PHE A 479     -10.845  10.862  11.273  1.00 39.02           C  
ANISOU 3949  CZ  PHE A 479     5519   5140   4168    -80    106   -202       C  
ATOM   3950  N   ASN A 480     -15.059  10.893  14.525  1.00 34.44           N  
ANISOU 3950  N   ASN A 480     4635   4537   3913    -63    -30   -227       N  
ATOM   3951  CA  ASN A 480     -15.770  12.004  13.873  1.00 37.39           C  
ANISOU 3951  CA  ASN A 480     4992   4897   4316    -64   -116   -200       C  
ATOM   3952  C   ASN A 480     -15.980  13.207  14.798  1.00 37.97           C  
ANISOU 3952  C   ASN A 480     5017   4959   4450    -33    -81   -175       C  
ATOM   3953  O   ASN A 480     -15.820  14.351  14.373  1.00 40.33           O  
ANISOU 3953  O   ASN A 480     5331   5264   4729    -27   -123   -148       O  
ATOM   3954  CB  ASN A 480     -17.106  11.537  13.274  1.00 36.80           C  
ANISOU 3954  CB  ASN A 480     4874   4779   4329    -88   -214   -202       C  
ATOM   3955  CG  ASN A 480     -16.937  10.788  11.949  1.00 38.41           C  
ANISOU 3955  CG  ASN A 480     5179   4977   4438   -124   -299   -220       C  
ATOM   3956  OD1 ASN A 480     -15.955  10.978  11.227  1.00 41.04           O  
ANISOU 3956  OD1 ASN A 480     5621   5333   4639   -128   -284   -220       O  
ATOM   3957  ND2 ASN A 480     -17.916   9.951  11.615  1.00 34.96           N  
ANISOU 3957  ND2 ASN A 480     4715   4493   4074   -152   -385   -232       N  
ATOM   3958  N   GLN A 481     -16.339  12.941  16.056  1.00 39.09           N  
ANISOU 3958  N   GLN A 481     5120   5076   4657    -13      2   -184       N  
ATOM   3959  CA  GLN A 481     -16.421  13.976  17.091  1.00 39.27           C  
ANISOU 3959  CA  GLN A 481     5138   5071   4711     20     61   -168       C  
ATOM   3960  C   GLN A 481     -15.073  14.678  17.262  1.00 38.06           C  
ANISOU 3960  C   GLN A 481     5059   4945   4458     27     61   -157       C  
ATOM   3961  O   GLN A 481     -15.006  15.902  17.351  1.00 38.50           O  
ANISOU 3961  O   GLN A 481     5121   4991   4516     43     44   -135       O  
ATOM   3962  CB  GLN A 481     -16.807  13.368  18.441  1.00 40.50           C  
ANISOU 3962  CB  GLN A 481     5296   5181   4910     38    173   -183       C  
ATOM   3963  CG  GLN A 481     -18.191  12.750  18.528  1.00 44.15           C  
ANISOU 3963  CG  GLN A 481     5667   5594   5515     37    206   -184       C  
ATOM   3964  CD  GLN A 481     -18.456  12.089  19.885  1.00 48.86           C  
ANISOU 3964  CD  GLN A 481     6292   6137   6137     56    346   -196       C  
ATOM   3965  OE1 GLN A 481     -17.686  12.246  20.841  1.00 46.70           O  
ANISOU 3965  OE1 GLN A 481     6125   5853   5764     71    406   -203       O  
ATOM   3966  NE2 GLN A 481     -19.548  11.339  19.966  1.00 53.54           N  
ANISOU 3966  NE2 GLN A 481     6796   6680   6866     52    391   -193       N  
ATOM   3967  N   ARG A 482     -14.004  13.890  17.325  1.00 36.75           N  
ANISOU 3967  N   ARG A 482     4936   4801   4225     15     77   -169       N  
ATOM   3968  CA  ARG A 482     -12.662  14.426  17.494  1.00 37.57           C  
ANISOU 3968  CA  ARG A 482     5087   4912   4278     18     69   -151       C  
ATOM   3969  C   ARG A 482     -12.365  15.432  16.376  1.00 39.50           C  
ANISOU 3969  C   ARG A 482     5328   5180   4501     13     17   -122       C  
ATOM   3970  O   ARG A 482     -11.911  16.547  16.640  1.00 39.23           O  
ANISOU 3970  O   ARG A 482     5306   5132   4467     25      0    -96       O  
ATOM   3971  CB  ARG A 482     -11.638  13.284  17.525  1.00 35.85           C  
ANISOU 3971  CB  ARG A 482     4888   4701   4033      3     92   -161       C  
ATOM   3972  CG  ARG A 482     -10.214  13.686  17.871  1.00 34.66           C  
ANISOU 3972  CG  ARG A 482     4760   4529   3878      4     79   -133       C  
ATOM   3973  CD  ARG A 482      -9.349  13.781  16.633  1.00 37.17           C  
ANISOU 3973  CD  ARG A 482     5064   4869   4190     -6     83   -111       C  
ATOM   3974  NE  ARG A 482      -8.032  14.368  16.887  1.00 31.22           N  
ANISOU 3974  NE  ARG A 482     4304   4080   3480     -5     69    -70       N  
ATOM   3975  CZ  ARG A 482      -6.947  14.080  16.172  1.00 35.95           C  
ANISOU 3975  CZ  ARG A 482     4880   4666   4113    -12    109    -45       C  
ATOM   3976  NH1 ARG A 482      -7.021  13.188  15.182  1.00 37.33           N  
ANISOU 3976  NH1 ARG A 482     5067   4863   4255    -19    173    -66       N  
ATOM   3977  NH2 ARG A 482      -5.778  14.659  16.453  1.00 28.33           N  
ANISOU 3977  NH2 ARG A 482     3883   3651   3229    -11     90      2       N  
ATOM   3978  N   LYS A 483     -12.668  15.040  15.143  1.00 39.04           N  
ANISOU 3978  N   LYS A 483     5270   5144   4420     -6    -12   -127       N  
ATOM   3979  CA  LYS A 483     -12.408  15.864  13.967  1.00 42.83           C  
ANISOU 3979  CA  LYS A 483     5781   5635   4857    -15    -56    -98       C  
ATOM   3980  C   LYS A 483     -13.113  17.226  14.025  1.00 42.86           C  
ANISOU 3980  C   LYS A 483     5758   5627   4901     -1   -110    -73       C  
ATOM   3981  O   LYS A 483     -12.520  18.250  13.667  1.00 42.67           O  
ANISOU 3981  O   LYS A 483     5755   5604   4852      2   -125    -40       O  
ATOM   3982  CB  LYS A 483     -12.766  15.095  12.678  1.00 45.10           C  
ANISOU 3982  CB  LYS A 483     6118   5928   5091    -41    -90   -113       C  
ATOM   3983  CG  LYS A 483     -12.254  15.750  11.397  1.00 50.41           C  
ANISOU 3983  CG  LYS A 483     6875   6598   5682    -52   -110    -84       C  
ATOM   3984  CD  LYS A 483     -12.379  14.833  10.183  1.00 56.18           C  
ANISOU 3984  CD  LYS A 483     7709   7313   6323    -79   -128   -104       C  
ATOM   3985  CE  LYS A 483     -12.187  15.628   8.891  1.00 59.87           C  
ANISOU 3985  CE  LYS A 483     8296   7758   6695    -91   -162    -72       C  
ATOM   3986  NZ  LYS A 483     -12.358  14.795   7.668  1.00 63.61           N  
ANISOU 3986  NZ  LYS A 483     8923   8194   7051   -119   -189    -92       N  
ATOM   3987  N   GLU A 484     -14.361  17.245  14.491  1.00 43.51           N  
ANISOU 3987  N   GLU A 484     5785   5685   5060      8   -127    -83       N  
ATOM   3988  CA  GLU A 484     -15.091  18.505  14.652  1.00 43.96           C  
ANISOU 3988  CA  GLU A 484     5804   5715   5183     27   -162    -59       C  
ATOM   3989  C   GLU A 484     -14.333  19.468  15.570  1.00 42.97           C  
ANISOU 3989  C   GLU A 484     5703   5579   5044     51   -120    -46       C  
ATOM   3990  O   GLU A 484     -14.112  20.632  15.218  1.00 44.40           O  
ANISOU 3990  O   GLU A 484     5893   5758   5220     57   -161    -15       O  
ATOM   3991  CB  GLU A 484     -16.508  18.266  15.189  1.00 46.30           C  
ANISOU 3991  CB  GLU A 484     6020   5966   5606     40   -150    -68       C  
ATOM   3992  CG  GLU A 484     -17.388  19.529  15.177  1.00 52.41           C  
ANISOU 3992  CG  GLU A 484     6737   6695   6482     60   -186    -37       C  
ATOM   3993  CD  GLU A 484     -18.666  19.407  16.015  1.00 59.09           C  
ANISOU 3993  CD  GLU A 484     7492   7471   7489     85   -119    -40       C  
ATOM   3994  OE1 GLU A 484     -18.791  18.451  16.810  1.00 61.96           O  
ANISOU 3994  OE1 GLU A 484     7854   7821   7868     91    -26    -66       O  
ATOM   3995  OE2 GLU A 484     -19.552  20.281  15.884  1.00 60.14           O  
ANISOU 3995  OE2 GLU A 484     7553   7551   7748    101   -149    -11       O  
ATOM   3996  N   HIS A 485     -13.924  18.967  16.737  1.00 40.01           N  
ANISOU 3996  N   HIS A 485     5354   5188   4660     62    -53    -67       N  
ATOM   3997  CA  HIS A 485     -13.251  19.785  17.742  1.00 36.74           C  
ANISOU 3997  CA  HIS A 485     4991   4740   4228     81    -36    -57       C  
ATOM   3998  C   HIS A 485     -11.860  20.211  17.323  1.00 35.57           C  
ANISOU 3998  C   HIS A 485     4868   4609   4039     66    -78    -29       C  
ATOM   3999  O   HIS A 485     -11.420  21.305  17.673  1.00 38.85           O  
ANISOU 3999  O   HIS A 485     5308   4995   4458     76   -107     -5       O  
ATOM   4000  CB  HIS A 485     -13.197  19.066  19.085  1.00 34.40           C  
ANISOU 4000  CB  HIS A 485     4749   4403   3919     91     28    -84       C  
ATOM   4001  CG  HIS A 485     -14.531  18.938  19.743  1.00 37.10           C  
ANISOU 4001  CG  HIS A 485     5077   4699   4320    114    105   -103       C  
ATOM   4002  ND1 HIS A 485     -15.160  19.999  20.356  1.00 38.81           N  
ANISOU 4002  ND1 HIS A 485     5316   4856   4575    146    145    -97       N  
ATOM   4003  CD2 HIS A 485     -15.359  17.876  19.883  1.00 37.81           C  
ANISOU 4003  CD2 HIS A 485     5128   4781   4458    113    165   -123       C  
ATOM   4004  CE1 HIS A 485     -16.324  19.599  20.837  1.00 39.08           C  
ANISOU 4004  CE1 HIS A 485     5321   4842   4687    165    242   -109       C  
ATOM   4005  NE2 HIS A 485     -16.466  18.314  20.569  1.00 40.75           N  
ANISOU 4005  NE2 HIS A 485     5489   5084   4910    144    250   -124       N  
ATOM   4006  N   LYS A 486     -11.167  19.352  16.584  1.00 35.30           N  
ANISOU 4006  N   LYS A 486     4827   4609   3978     44    -72    -27       N  
ATOM   4007  CA  LYS A 486      -9.856  19.710  16.054  1.00 35.11           C  
ANISOU 4007  CA  LYS A 486     4808   4585   3948     33    -83      9       C  
ATOM   4008  C   LYS A 486      -9.986  20.849  15.045  1.00 33.72           C  
ANISOU 4008  C   LYS A 486     4629   4421   3762     32   -116     43       C  
ATOM   4009  O   LYS A 486      -9.145  21.745  15.016  1.00 35.62           O  
ANISOU 4009  O   LYS A 486     4870   4640   4024     32   -132     82       O  
ATOM   4010  CB  LYS A 486      -9.134  18.503  15.445  1.00 33.83           C  
ANISOU 4010  CB  LYS A 486     4642   4439   3771     15    -36      3       C  
ATOM   4011  CG  LYS A 486      -7.675  18.784  15.127  1.00 36.31           C  
ANISOU 4011  CG  LYS A 486     4944   4727   4125      8    -17     48       C  
ATOM   4012  CD  LYS A 486      -6.954  17.611  14.460  1.00 40.24           C  
ANISOU 4012  CD  LYS A 486     5438   5225   4626     -3     59     45       C  
ATOM   4013  CE  LYS A 486      -5.574  18.075  13.963  1.00 44.37           C  
ANISOU 4013  CE  LYS A 486     5932   5704   5222     -5    106    104       C  
ATOM   4014  NZ  LYS A 486      -4.574  16.991  13.698  1.00 45.11           N  
ANISOU 4014  NZ  LYS A 486     5998   5764   5377     -9    195    113       N  
ATOM   4015  N   GLY A 487     -11.046  20.812  14.235  1.00 32.86           N  
ANISOU 4015  N   GLY A 487     4518   4334   3632     27   -139     34       N  
ATOM   4016  CA  GLY A 487     -11.354  21.895  13.295  1.00 31.98           C  
ANISOU 4016  CA  GLY A 487     4420   4223   3508     25   -191     68       C  
ATOM   4017  C   GLY A 487     -11.523  23.211  14.040  1.00 33.44           C  
ANISOU 4017  C   GLY A 487     4582   4380   3742     46   -222     86       C  
ATOM   4018  O   GLY A 487     -10.943  24.231  13.658  1.00 34.87           O  
ANISOU 4018  O   GLY A 487     4776   4552   3922     45   -244    126       O  
ATOM   4019  N   TYR A 488     -12.291  23.182  15.126  1.00 32.34           N  
ANISOU 4019  N   TYR A 488     4422   4216   3649     68   -209     58       N  
ATOM   4020  CA  TYR A 488     -12.413  24.346  15.995  1.00 32.26           C  
ANISOU 4020  CA  TYR A 488     4419   4162   3675     93   -217     67       C  
ATOM   4021  C   TYR A 488     -11.061  24.795  16.539  1.00 31.78           C  
ANISOU 4021  C   TYR A 488     4400   4078   3599     89   -227     87       C  
ATOM   4022  O   TYR A 488     -10.772  25.988  16.547  1.00 32.00           O  
ANISOU 4022  O   TYR A 488     4436   4079   3642     95   -267    117       O  
ATOM   4023  CB  TYR A 488     -13.388  24.106  17.150  1.00 33.59           C  
ANISOU 4023  CB  TYR A 488     4589   4288   3886    119   -162     32       C  
ATOM   4024  CG  TYR A 488     -14.797  23.701  16.752  1.00 34.99           C  
ANISOU 4024  CG  TYR A 488     4697   4463   4136    125   -152     21       C  
ATOM   4025  CD1 TYR A 488     -15.407  24.213  15.604  1.00 36.62           C  
ANISOU 4025  CD1 TYR A 488     4853   4679   4382    115   -230     50       C  
ATOM   4026  CD2 TYR A 488     -15.529  22.814  17.548  1.00 38.94           C  
ANISOU 4026  CD2 TYR A 488     5183   4935   4678    137    -74    -11       C  
ATOM   4027  CE1 TYR A 488     -16.705  23.836  15.246  1.00 38.60           C  
ANISOU 4027  CE1 TYR A 488     5027   4906   4732    115   -252     49       C  
ATOM   4028  CE2 TYR A 488     -16.825  22.435  17.207  1.00 40.28           C  
ANISOU 4028  CE2 TYR A 488     5266   5084   4955    140    -70    -12       C  
ATOM   4029  CZ  TYR A 488     -17.408  22.952  16.059  1.00 40.08           C  
ANISOU 4029  CZ  TYR A 488     5178   5063   4988    128   -170     19       C  
ATOM   4030  OH  TYR A 488     -18.688  22.572  15.727  1.00 42.12           O  
ANISOU 4030  OH  TYR A 488     5339   5280   5384    126   -196     26       O  
ATOM   4031  N   MET A 489     -10.226  23.848  16.969  1.00 32.95           N  
ANISOU 4031  N   MET A 489     4565   4224   3731     76   -205     76       N  
ATOM   4032  CA  MET A 489      -8.930  24.199  17.564  1.00 32.93           C  
ANISOU 4032  CA  MET A 489     4588   4175   3749     68   -242    103       C  
ATOM   4033  C   MET A 489      -7.968  24.836  16.571  1.00 32.02           C  
ANISOU 4033  C   MET A 489     4434   4066   3667     52   -261    158       C  
ATOM   4034  O   MET A 489      -7.309  25.821  16.893  1.00 33.35           O  
ANISOU 4034  O   MET A 489     4609   4186   3878     51   -314    192       O  
ATOM   4035  CB  MET A 489      -8.260  22.994  18.230  1.00 34.26           C  
ANISOU 4035  CB  MET A 489     4773   4325   3919     56   -229     86       C  
ATOM   4036  CG  MET A 489      -6.839  23.285  18.727  1.00 34.04           C  
ANISOU 4036  CG  MET A 489     4751   4230   3950     41   -297    126       C  
ATOM   4037  SD  MET A 489      -5.820  21.827  19.014  1.00 46.95           S  
ANISOU 4037  SD  MET A 489     6364   5844   5633     21   -291    129       S  
ATOM   4038  CE  MET A 489      -5.381  21.360  17.337  1.00 40.14           C  
ANISOU 4038  CE  MET A 489     5408   5042   4802     11   -196    155       C  
ATOM   4039  N   LEU A 490      -7.872  24.266  15.376  1.00 33.52           N  
ANISOU 4039  N   LEU A 490     4598   4302   3836     39   -212    167       N  
ATOM   4040  CA  LEU A 490      -6.970  24.800  14.360  1.00 34.76           C  
ANISOU 4040  CA  LEU A 490     4738   4453   4018     26   -192    223       C  
ATOM   4041  C   LEU A 490      -7.384  26.193  13.886  1.00 34.25           C  
ANISOU 4041  C   LEU A 490     4683   4385   3945     32   -236    254       C  
ATOM   4042  O   LEU A 490      -6.529  27.073  13.709  1.00 33.89           O  
ANISOU 4042  O   LEU A 490     4620   4302   3953     27   -248    306       O  
ATOM   4043  CB  LEU A 490      -6.833  23.835  13.177  1.00 35.56           C  
ANISOU 4043  CB  LEU A 490     4854   4586   4072     14   -110    221       C  
ATOM   4044  CG  LEU A 490      -6.001  22.566  13.416  1.00 38.44           C  
ANISOU 4044  CG  LEU A 490     5195   4937   4474      7    -47    211       C  
ATOM   4045  CD1 LEU A 490      -5.959  21.711  12.157  1.00 38.82           C  
ANISOU 4045  CD1 LEU A 490     5288   5006   4458     -2     47    206       C  
ATOM   4046  CD2 LEU A 490      -4.577  22.892  13.886  1.00 38.71           C  
ANISOU 4046  CD2 LEU A 490     5169   4902   4637      2    -47    264       C  
ATOM   4047  N   ALA A 491      -8.688  26.390  13.689  1.00 33.31           N  
ANISOU 4047  N   ALA A 491     4581   4295   3781     43   -264    227       N  
ATOM   4048  CA  ALA A 491      -9.219  27.702  13.291  1.00 32.66           C  
ANISOU 4048  CA  ALA A 491     4504   4203   3704     50   -318    255       C  
ATOM   4049  C   ALA A 491      -8.927  28.770  14.348  1.00 33.45           C  
ANISOU 4049  C   ALA A 491     4598   4252   3861     66   -362    266       C  
ATOM   4050  O   ALA A 491      -8.566  29.895  14.005  1.00 34.10           O  
ANISOU 4050  O   ALA A 491     4677   4311   3968     64   -395    310       O  
ATOM   4051  CB  ALA A 491     -10.709  27.618  13.014  1.00 33.22           C  
ANISOU 4051  CB  ALA A 491     4572   4292   3757     59   -352    227       C  
ATOM   4052  N   ALA A 492      -9.055  28.409  15.630  1.00 31.32           N  
ANISOU 4052  N   ALA A 492     4344   3954   3601     79   -363    226       N  
ATOM   4053  CA  ALA A 492      -8.718  29.326  16.723  1.00 33.11           C  
ANISOU 4053  CA  ALA A 492     4609   4111   3859     91   -413    230       C  
ATOM   4054  C   ALA A 492      -7.225  29.678  16.733  1.00 32.34           C  
ANISOU 4054  C   ALA A 492     4498   3971   3819     68   -457    281       C  
ATOM   4055  O   ALA A 492      -6.818  30.776  17.133  1.00 33.74           O  
ANISOU 4055  O   ALA A 492     4694   4088   4037     69   -523    308       O  
ATOM   4056  CB  ALA A 492      -9.147  28.732  18.067  1.00 31.54           C  
ANISOU 4056  CB  ALA A 492     4474   3875   3635    107   -395    176       C  
ATOM   4057  N   GLN A 493      -6.422  28.729  16.282  1.00 31.47           N  
ANISOU 4057  N   GLN A 493     4348   3879   3731     48   -417    296       N  
ATOM   4058  CA  GLN A 493      -4.985  28.878  16.203  1.00 34.02           C  
ANISOU 4058  CA  GLN A 493     4625   4148   4153     27   -439    354       C  
ATOM   4059  C   GLN A 493      -4.647  29.821  15.044  1.00 35.20           C  
ANISOU 4059  C   GLN A 493     4737   4302   4336     20   -413    415       C  
ATOM   4060  O   GLN A 493      -3.920  30.798  15.223  1.00 33.96           O  
ANISOU 4060  O   GLN A 493     4557   4080   4266     12   -471    465       O  
ATOM   4061  CB  GLN A 493      -4.383  27.489  15.997  1.00 34.67           C  
ANISOU 4061  CB  GLN A 493     4670   4243   4259     14   -373    350       C  
ATOM   4062  CG  GLN A 493      -2.879  27.365  16.030  1.00 37.84           C  
ANISOU 4062  CG  GLN A 493     5000   4570   4809     -6   -383    411       C  
ATOM   4063  CD  GLN A 493      -2.455  25.918  15.854  1.00 41.58           C  
ANISOU 4063  CD  GLN A 493     5438   5054   5306    -13   -305    400       C  
ATOM   4064  OE1 GLN A 493      -2.145  25.485  14.743  1.00 43.10           O  
ANISOU 4064  OE1 GLN A 493     5597   5270   5509    -14   -185    422       O  
ATOM   4065  NE2 GLN A 493      -2.491  25.150  16.940  1.00 39.19           N  
ANISOU 4065  NE2 GLN A 493     5164   4727   4998    -15   -366    363       N  
ATOM   4066  N   ARG A 494      -5.204  29.537  13.866  1.00 36.82           N  
ANISOU 4066  N   ARG A 494     4952   4571   4466     21   -336    412       N  
ATOM   4067  CA  ARG A 494      -5.008  30.387  12.690  1.00 38.76           C  
ANISOU 4067  CA  ARG A 494     5200   4816   4711     14   -303    469       C  
ATOM   4068  C   ARG A 494      -5.457  31.821  12.959  1.00 39.58           C  
ANISOU 4068  C   ARG A 494     5314   4897   4826     24   -391    485       C  
ATOM   4069  O   ARG A 494      -4.794  32.766  12.532  1.00 38.81           O  
ANISOU 4069  O   ARG A 494     5197   4760   4790     15   -396    547       O  
ATOM   4070  CB  ARG A 494      -5.749  29.830  11.473  1.00 37.35           C  
ANISOU 4070  CB  ARG A 494     5079   4697   4416     12   -240    455       C  
ATOM   4071  CG  ARG A 494      -5.155  28.563  10.894  1.00 35.61           C  
ANISOU 4071  CG  ARG A 494     4869   4484   4178      1   -128    452       C  
ATOM   4072  CD  ARG A 494      -5.802  28.260   9.542  1.00 38.38           C  
ANISOU 4072  CD  ARG A 494     5320   4866   4395     -6    -82    448       C  
ATOM   4073  NE  ARG A 494      -7.232  27.991   9.682  1.00 35.15           N  
ANISOU 4073  NE  ARG A 494     4940   4504   3911     -1   -170    391       N  
ATOM   4074  CZ  ARG A 494      -7.746  26.792   9.934  1.00 34.32           C  
ANISOU 4074  CZ  ARG A 494     4839   4430   3771     -1   -164    335       C  
ATOM   4075  NH1 ARG A 494      -6.953  25.738  10.063  1.00 38.58           N  
ANISOU 4075  NH1 ARG A 494     5365   4965   4328     -5    -76    323       N  
ATOM   4076  NH2 ARG A 494      -9.056  26.646  10.052  1.00 33.26           N  
ANISOU 4076  NH2 ARG A 494     4711   4322   3606      3   -243    295       N  
ATOM   4077  N   ASN A 495      -6.576  31.963  13.674  1.00 39.26           N  
ANISOU 4077  N   ASN A 495     5303   4874   4741     44   -447    430       N  
ATOM   4078  CA  ASN A 495      -7.101  33.266  14.083  1.00 39.96           C  
ANISOU 4078  CA  ASN A 495     5407   4930   4846     61   -520    435       C  
ATOM   4079  C   ASN A 495      -6.163  33.992  15.027  1.00 41.61           C  
ANISOU 4079  C   ASN A 495     5616   5057   5137     56   -587    458       C  
ATOM   4080  O   ASN A 495      -6.071  35.224  14.992  1.00 43.89           O  
ANISOU 4080  O   ASN A 495     5907   5305   5464     58   -641    492       O  
ATOM   4081  CB  ASN A 495      -8.487  33.127  14.728  1.00 39.15           C  
ANISOU 4081  CB  ASN A 495     5331   4841   4703     89   -530    372       C  
ATOM   4082  CG  ASN A 495      -9.582  32.843  13.706  1.00 40.94           C  
ANISOU 4082  CG  ASN A 495     5547   5123   4886     91   -513    365       C  
ATOM   4083  OD1 ASN A 495      -9.453  33.187  12.533  1.00 43.48           O  
ANISOU 4083  OD1 ASN A 495     5874   5461   5186     75   -520    410       O  
ATOM   4084  ND2 ASN A 495     -10.667  32.214  14.151  1.00 40.96           N  
ANISOU 4084  ND2 ASN A 495     5544   5137   4881    109   -497    314       N  
ATOM   4085  N   GLY A 496      -5.472  33.221  15.866  1.00 41.84           N  
ANISOU 4085  N   GLY A 496     5648   5052   5198     46   -601    443       N  
ATOM   4086  CA  GLY A 496      -4.494  33.765  16.805  1.00 40.65           C  
ANISOU 4086  CA  GLY A 496     5509   4802   5136     33   -701    469       C  
ATOM   4087  C   GLY A 496      -3.338  34.436  16.092  1.00 42.00           C  
ANISOU 4087  C   GLY A 496     5599   4929   5431      9   -712    555       C  
ATOM   4088  O   GLY A 496      -2.881  35.498  16.517  1.00 44.70           O  
ANISOU 4088  O   GLY A 496     5947   5190   5846      1   -808    589       O  
ATOM   4089  N   GLU A 497      -2.880  33.824  14.999  1.00 42.37           N  
ANISOU 4089  N   GLU A 497     5580   5016   5504     -2   -603    592       N  
ATOM   4090  CA  GLU A 497      -1.757  34.348  14.217  1.00 43.37           C  
ANISOU 4090  CA  GLU A 497     5627   5090   5763    -23   -565    682       C  
ATOM   4091  C   GLU A 497      -2.122  35.642  13.491  1.00 43.76           C  
ANISOU 4091  C   GLU A 497     5693   5146   5788    -18   -567    719       C  
ATOM   4092  O   GLU A 497      -1.267  36.501  13.279  1.00 42.29           O  
ANISOU 4092  O   GLU A 497     5453   4887   5728    -33   -586    792       O  
ATOM   4093  CB  GLU A 497      -1.241  33.303  13.221  1.00 43.43           C  
ANISOU 4093  CB  GLU A 497     5589   5125   5787    -30   -411    707       C  
ATOM   4094  CG  GLU A 497      -0.688  32.019  13.858  1.00 44.08           C  
ANISOU 4094  CG  GLU A 497     5633   5185   5930    -36   -403    685       C  
ATOM   4095  CD  GLU A 497       0.380  32.270  14.928  1.00 44.42           C  
ANISOU 4095  CD  GLU A 497     5609   5108   6159    -56   -535    725       C  
ATOM   4096  OE1 GLU A 497       1.394  32.939  14.638  1.00 46.64           O  
ANISOU 4096  OE1 GLU A 497     5801   5301   6619    -72   -539    810       O  
ATOM   4097  OE2 GLU A 497       0.208  31.774  16.060  1.00 44.86           O  
ANISOU 4097  OE2 GLU A 497     5711   5145   6189    -57   -641    676       O  
ATOM   4098  N   ILE A 498      -3.397  35.769  13.121  1.00 43.78           N  
ANISOU 4098  N   ILE A 498     5764   5226   5646      2   -555    672       N  
ATOM   4099  CA  ILE A 498      -3.909  36.983  12.489  1.00 45.62           C  
ANISOU 4099  CA  ILE A 498     6022   5463   5850      8   -577    702       C  
ATOM   4100  C   ILE A 498      -3.875  38.146  13.480  1.00 46.91           C  
ANISOU 4100  C   ILE A 498     6190   5556   6077     14   -702    703       C  
ATOM   4101  O   ILE A 498      -3.546  39.278  13.111  1.00 48.83           O  
ANISOU 4101  O   ILE A 498     6417   5756   6381      6   -732    761       O  
ATOM   4102  CB  ILE A 498      -5.343  36.777  11.940  1.00 45.07           C  
ANISOU 4102  CB  ILE A 498     6012   5472   5640     26   -563    655       C  
ATOM   4103  CG1 ILE A 498      -5.319  35.818  10.749  1.00 44.19           C  
ANISOU 4103  CG1 ILE A 498     5928   5410   5451     13   -456    665       C  
ATOM   4104  CG2 ILE A 498      -5.965  38.104  11.519  1.00 43.68           C  
ANISOU 4104  CG2 ILE A 498     5858   5284   5453     34   -621    683       C  
ATOM   4105  CD1 ILE A 498      -6.651  35.170  10.455  1.00 45.88           C  
ANISOU 4105  CD1 ILE A 498     6194   5689   5550     24   -468    607       C  
ATOM   4106  N   ILE A 499      -4.211  37.854  14.735  1.00 45.99           N  
ANISOU 4106  N   ILE A 499     6115   5418   5940     27   -769    640       N  
ATOM   4107  CA  ILE A 499      -4.167  38.842  15.800  1.00 46.15           C  
ANISOU 4107  CA  ILE A 499     6184   5353   5998     33   -887    630       C  
ATOM   4108  C   ILE A 499      -2.723  39.230  16.122  1.00 47.92           C  
ANISOU 4108  C   ILE A 499     6360   5473   6374      0   -970    695       C  
ATOM   4109  O   ILE A 499      -2.426  40.411  16.305  1.00 48.98           O  
ANISOU 4109  O   ILE A 499     6500   5534   6576     -6  -1057    732       O  
ATOM   4110  CB  ILE A 499      -4.914  38.354  17.059  1.00 46.52           C  
ANISOU 4110  CB  ILE A 499     6328   5386   5961     57   -915    544       C  
ATOM   4111  CG1 ILE A 499      -6.402  38.151  16.739  1.00 44.27           C  
ANISOU 4111  CG1 ILE A 499     6064   5180   5576     90   -835    491       C  
ATOM   4112  CG2 ILE A 499      -4.735  39.344  18.211  1.00 43.86           C  
ANISOU 4112  CG2 ILE A 499     6086   4934   5646     61  -1036    532       C  
ATOM   4113  CD1 ILE A 499      -7.146  37.299  17.746  1.00 42.76           C  
ANISOU 4113  CD1 ILE A 499     5947   4989   5312    113   -802    414       C  
ATOM   4114  N   LYS A 500      -1.833  38.240  16.176  1.00 48.92           N  
ANISOU 4114  N   LYS A 500     6428   5583   6575    -21   -949    716       N  
ATOM   4115  CA  LYS A 500      -0.399  38.499  16.370  1.00 50.06           C  
ANISOU 4115  CA  LYS A 500     6490   5613   6918    -56  -1026    794       C  
ATOM   4116  C   LYS A 500       0.175  39.418  15.281  1.00 51.93           C  
ANISOU 4116  C   LYS A 500     6637   5828   7267    -69   -970    886       C  
ATOM   4117  O   LYS A 500       0.904  40.362  15.584  1.00 52.31           O  
ANISOU 4117  O   LYS A 500     6647   5768   7458    -89  -1078    944       O  
ATOM   4118  CB  LYS A 500       0.396  37.193  16.427  1.00 48.14           C  
ANISOU 4118  CB  LYS A 500     6175   5356   6758    -72   -984    807       C  
ATOM   4119  CG  LYS A 500       0.173  36.380  17.679  1.00 46.56           C  
ANISOU 4119  CG  LYS A 500     6065   5134   6493    -70  -1078    737       C  
ATOM   4120  CD  LYS A 500       0.974  35.098  17.651  1.00 45.28           C  
ANISOU 4120  CD  LYS A 500     5819   4956   6430    -87  -1037    758       C  
ATOM   4121  CE  LYS A 500       0.403  34.083  18.627  1.00 44.25           C  
ANISOU 4121  CE  LYS A 500     5796   4847   6170    -77  -1075    674       C  
ATOM   4122  NZ  LYS A 500       1.138  32.784  18.580  1.00 44.07           N  
ANISOU 4122  NZ  LYS A 500     5690   4811   6245    -92  -1035    692       N  
ATOM   4123  N   GLU A 501      -0.170  39.140  14.024  1.00 53.28           N  
ANISOU 4123  N   GLU A 501     6789   6089   7367    -59   -808    901       N  
ATOM   4124  CA  GLU A 501       0.253  39.974  12.895  1.00 56.32           C  
ANISOU 4124  CA  GLU A 501     7124   6454   7820    -68   -727    987       C  
ATOM   4125  C   GLU A 501      -0.204  41.421  13.050  1.00 56.88           C  
ANISOU 4125  C   GLU A 501     7237   6498   7875    -63   -831    996       C  
ATOM   4126  O   GLU A 501       0.576  42.344  12.831  1.00 57.41           O  
ANISOU 4126  O   GLU A 501     7244   6481   8088    -82   -858   1077       O  
ATOM   4127  CB  GLU A 501      -0.245  39.400  11.562  1.00 57.11           C  
ANISOU 4127  CB  GLU A 501     7263   6648   7787    -58   -550    987       C  
ATOM   4128  CG  GLU A 501       0.635  38.286  10.963  1.00 62.00           C  
ANISOU 4128  CG  GLU A 501     7825   7254   8480    -68   -392   1024       C  
ATOM   4129  CD  GLU A 501       1.950  38.791  10.355  1.00 67.67           C  
ANISOU 4129  CD  GLU A 501     8441   7862   9410    -88   -298   1141       C  
ATOM   4130  OE1 GLU A 501       2.171  40.026  10.296  1.00 68.72           O  
ANISOU 4130  OE1 GLU A 501     8551   7938   9623    -97   -357   1197       O  
ATOM   4131  OE2 GLU A 501       2.766  37.942   9.931  1.00 69.37           O  
ANISOU 4131  OE2 GLU A 501     8593   8038   9725    -93   -152   1179       O  
ATOM   4132  N   ALA A 502      -1.460  41.604  13.449  1.00 57.04           N  
ANISOU 4132  N   ALA A 502     7354   6581   7739    -36   -882    916       N  
ATOM   4133  CA  ALA A 502      -2.030  42.931  13.647  1.00 59.00           C  
ANISOU 4133  CA  ALA A 502     7648   6801   7967    -23   -972    915       C  
ATOM   4134  C   ALA A 502      -1.386  43.695  14.808  1.00 61.84           C  
ANISOU 4134  C   ALA A 502     8016   7037   8442    -36  -1131    923       C  
ATOM   4135  O   ALA A 502      -1.358  44.928  14.803  1.00 63.79           O  
ANISOU 4135  O   ALA A 502     8272   7227   8738    -38  -1202    957       O  
ATOM   4136  CB  ALA A 502      -3.529  42.837  13.841  1.00 57.88           C  
ANISOU 4136  CB  ALA A 502     7591   6735   7665     13   -970    830       C  
ATOM   4137  N   LEU A 503      -0.859  42.965  15.790  1.00 63.30           N  
ANISOU 4137  N   LEU A 503     8212   7170   8670    -49  -1201    896       N  
ATOM   4138  CA  LEU A 503      -0.221  43.582  16.957  1.00 64.64           C  
ANISOU 4138  CA  LEU A 503     8423   7200   8937    -68  -1386    902       C  
ATOM   4139  C   LEU A 503       1.080  44.323  16.640  1.00 67.49           C  
ANISOU 4139  C   LEU A 503     8666   7448   9529   -107  -1452   1012       C  
ATOM   4140  O   LEU A 503       1.553  45.120  17.457  1.00 68.72           O  
ANISOU 4140  O   LEU A 503     8859   7474   9776   -127  -1629   1028       O  
ATOM   4141  CB  LEU A 503       0.013  42.546  18.060  1.00 62.74           C  
ANISOU 4141  CB  LEU A 503     8244   6918   8676    -75  -1460    850       C  
ATOM   4142  CG  LEU A 503      -1.146  42.333  19.032  1.00 60.07           C  
ANISOU 4142  CG  LEU A 503     8081   6603   8141    -41  -1477    741       C  
ATOM   4143  CD1 LEU A 503      -1.066  40.954  19.667  1.00 59.85           C  
ANISOU 4143  CD1 LEU A 503     8092   6585   8062    -44  -1470    695       C  
ATOM   4144  CD2 LEU A 503      -1.170  43.426  20.096  1.00 60.24           C  
ANISOU 4144  CD2 LEU A 503     8247   6492   8151    -41  -1641    720       C  
ATOM   4145  N   HIS A 504       1.648  44.063  15.463  1.00 69.08           N  
ANISOU 4145  N   HIS A 504     8737   7683   9827   -119  -1307   1089       N  
ATOM   4146  CA  HIS A 504       2.856  44.755  15.020  1.00 72.00           C  
ANISOU 4146  CA  HIS A 504     8975   7941  10442   -153  -1324   1206       C  
ATOM   4147  C   HIS A 504       2.544  46.177  14.577  1.00 73.18           C  
ANISOU 4147  C   HIS A 504     9146   8075  10583   -149  -1345   1241       C  
ATOM   4148  O   HIS A 504       3.428  47.036  14.561  1.00 75.21           O  
ANISOU 4148  O   HIS A 504     9321   8213  11043   -178  -1420   1327       O  
ATOM   4149  CB  HIS A 504       3.557  43.984  13.902  1.00 72.93           C  
ANISOU 4149  CB  HIS A 504     8965   8082  10664   -162  -1120   1279       C  
ATOM   4150  CG  HIS A 504       3.913  42.577  14.272  1.00 74.89           C  
ANISOU 4150  CG  HIS A 504     9178   8338  10941   -165  -1090   1251       C  
ATOM   4151  ND1 HIS A 504       4.388  42.233  15.520  1.00 76.23           N  
ANISOU 4151  ND1 HIS A 504     9349   8412  11204   -184  -1278   1231       N  
ATOM   4152  CD2 HIS A 504       3.874  41.430  13.555  1.00 74.98           C  
ANISOU 4152  CD2 HIS A 504     9163   8428  10896   -152   -901   1242       C  
ATOM   4153  CE1 HIS A 504       4.615  40.932  15.559  1.00 76.90           C  
ANISOU 4153  CE1 HIS A 504     9396   8524  11298   -183  -1206   1213       C  
ATOM   4154  NE2 HIS A 504       4.313  40.422  14.379  1.00 76.29           N  
ANISOU 4154  NE2 HIS A 504     9298   8554  11134   -162   -972   1217       N  
ATOM   4155  N   ASN A 505       1.281  46.415  14.228  1.00 72.76           N  
ANISOU 4155  N   ASN A 505     9194   8135  10316   -114  -1286   1178       N  
ATOM   4156  CA  ASN A 505       0.794  47.749  13.877  1.00 73.47           C  
ANISOU 4156  CA  ASN A 505     9321   8217  10378   -104  -1317   1198       C  
ATOM   4157  C   ASN A 505      -0.489  48.117  14.630  1.00 72.07           C  
ANISOU 4157  C   ASN A 505     9282   8076  10027    -67  -1396   1096       C  
ATOM   4158  O   ASN A 505      -1.550  48.257  14.010  1.00 70.76           O  
ANISOU 4158  O   ASN A 505     9158   8003   9727    -38  -1317   1067       O  
ATOM   4159  CB  ASN A 505       0.570  47.862  12.361  1.00 74.56           C  
ANISOU 4159  CB  ASN A 505     9431   8433  10466    -99  -1142   1255       C  
ATOM   4160  CG  ASN A 505       1.864  47.806  11.570  1.00 78.06           C  
ANISOU 4160  CG  ASN A 505     9751   8807  11102   -132  -1033   1372       C  
ATOM   4161  OD1 ASN A 505       2.066  46.905  10.752  1.00 79.29           O  
ANISOU 4161  OD1 ASN A 505     9885   9012  11230   -131   -862   1393       O  
ATOM   4162  ND2 ASN A 505       2.752  48.768  11.813  1.00 79.50           N  
ANISOU 4162  ND2 ASN A 505     9854   8859  11492   -159  -1125   1451       N  
ATOM   4163  N   PRO A 506      -0.400  48.283  15.968  1.00 71.87           N  
ANISOU 4163  N   PRO A 506     9338   7959  10011    -69  -1550   1045       N  
ATOM   4164  CA  PRO A 506      -1.603  48.613  16.728  1.00 71.80           C  
ANISOU 4164  CA  PRO A 506     9475   7963   9845    -28  -1587    948       C  
ATOM   4165  C   PRO A 506      -2.018  50.061  16.513  1.00 72.86           C  
ANISOU 4165  C   PRO A 506     9635   8057   9991    -14  -1631    969       C  
ATOM   4166  O   PRO A 506      -1.166  50.929  16.323  1.00 74.95           O  
ANISOU 4166  O   PRO A 506     9844   8234  10401    -45  -1710   1046       O  
ATOM   4167  CB  PRO A 506      -1.174  48.391  18.180  1.00 71.49           C  
ANISOU 4167  CB  PRO A 506     9544   7807   9813    -40  -1738    900       C  
ATOM   4168  CG  PRO A 506       0.286  48.657  18.185  1.00 72.74           C  
ANISOU 4168  CG  PRO A 506     9604   7848  10185    -93  -1857    994       C  
ATOM   4169  CD  PRO A 506       0.800  48.246  16.827  1.00 73.11           C  
ANISOU 4169  CD  PRO A 506     9472   7976  10333   -108  -1704   1079       C  
ATOM   4170  N   ASN A 507      -3.321  50.310  16.527  1.00 73.82           N  
ANISOU 4170  N   ASN A 507     9830   8234   9985     32  -1577    905       N  
ATOM   4171  CA  ASN A 507      -3.840  51.665  16.408  1.00 75.88           C  
ANISOU 4171  CA  ASN A 507    10122   8450  10259     51  -1618    916       C  
ATOM   4172  C   ASN A 507      -3.907  52.333  17.773  1.00 78.50           C  
ANISOU 4172  C   ASN A 507    10601   8648  10576     65  -1740    857       C  
ATOM   4173  O   ASN A 507      -3.901  51.656  18.804  1.00 79.24           O  
ANISOU 4173  O   ASN A 507    10803   8702  10603     70  -1768    791       O  
ATOM   4174  CB  ASN A 507      -5.208  51.661  15.727  1.00 74.63           C  
ANISOU 4174  CB  ASN A 507     9957   8392  10006     94  -1510    887       C  
ATOM   4175  CG  ASN A 507      -5.160  51.058  14.336  1.00 73.00           C  
ANISOU 4175  CG  ASN A 507     9651   8298   9788     76  -1410    945       C  
ATOM   4176  OD1 ASN A 507      -4.718  49.920  14.148  1.00 69.14           O  
ANISOU 4176  OD1 ASN A 507     9127   7864   9280     58  -1350    945       O  
ATOM   4177  ND2 ASN A 507      -5.617  51.820  13.350  1.00 72.31           N  
ANISOU 4177  ND2 ASN A 507     9534   8234   9705     81  -1394    995       N  
ATOM   4178  N   LEU A 508      -3.948  53.662  17.780  1.00 80.89           N  
ANISOU 4178  N   LEU A 508    10930   8871  10933     70  -1812    883       N  
ATOM   4179  CA  LEU A 508      -3.926  54.413  19.031  1.00 83.18           C  
ANISOU 4179  CA  LEU A 508    11387   9010  11207     80  -1936    832       C  
ATOM   4180  C   LEU A 508      -5.307  54.986  19.316  1.00 83.65           C  
ANISOU 4180  C   LEU A 508    11545   9064  11174    144  -1857    761       C  
ATOM   4181  O   LEU A 508      -5.633  56.098  18.895  1.00 85.36           O  
ANISOU 4181  O   LEU A 508    11738   9255  11442    159  -1869    791       O  
ATOM   4182  CB  LEU A 508      -2.842  55.501  18.998  1.00 84.60           C  
ANISOU 4182  CB  LEU A 508    11537   9068  11539     35  -2096    911       C  
ATOM   4183  CG  LEU A 508      -1.395  55.023  18.792  1.00 86.50           C  
ANISOU 4183  CG  LEU A 508    11659   9275  11931    -29  -2179    995       C  
ATOM   4184  CD1 LEU A 508      -0.480  56.175  18.386  1.00 88.67           C  
ANISOU 4184  CD1 LEU A 508    11846   9449  12395    -70  -2291   1096       C  
ATOM   4185  CD2 LEU A 508      -0.844  54.308  20.032  1.00 88.08           C  
ANISOU 4185  CD2 LEU A 508    11981   9375  12109    -51  -2306    946       C  
ATOM   4186  N   SER A 509      -6.118  54.201  20.023  1.00 83.38           N  
ANISOU 4186  N   SER A 509    11615   9047  11020    184  -1765    671       N  
ATOM   4187  CA  SER A 509      -7.517  54.538  20.271  1.00 83.85           C  
ANISOU 4187  CA  SER A 509    11741   9098  11019    251  -1646    607       C  
ATOM   4188  C   SER A 509      -8.086  53.823  21.497  1.00 84.31           C  
ANISOU 4188  C   SER A 509    11980   9100  10952    288  -1569    506       C  
ATOM   4189  O   SER A 509      -7.428  52.970  22.100  1.00 84.57           O  
ANISOU 4189  O   SER A 509    12089   9116  10928    258  -1618    486       O  
ATOM   4190  CB  SER A 509      -8.368  54.201  19.041  1.00 83.07           C  
ANISOU 4190  CB  SER A 509    11467   9147  10949    270  -1527    638       C  
ATOM   4191  OG  SER A 509      -8.348  52.808  18.779  1.00 83.43           O  
ANISOU 4191  OG  SER A 509    11452   9303  10944    256  -1457    627       O  
ATOM   4192  N   VAL A 510      -9.312  54.195  21.861  1.00 84.64           N  
ANISOU 4192  N   VAL A 510    12094   9099  10966    353  -1443    450       N  
ATOM   4193  CA  VAL A 510     -10.076  53.491  22.883  1.00 84.32           C  
ANISOU 4193  CA  VAL A 510    12212   9009  10819    399  -1308    360       C  
ATOM   4194  C   VAL A 510     -11.215  52.747  22.190  1.00 82.95           C  
ANISOU 4194  C   VAL A 510    11874   8960  10683    435  -1139    356       C  
ATOM   4195  O   VAL A 510     -12.073  53.359  21.542  1.00 83.23           O  
ANISOU 4195  O   VAL A 510    11793   9014  10815    470  -1079    379       O  
ATOM   4196  CB  VAL A 510     -10.615  54.448  23.981  1.00 85.97           C  
ANISOU 4196  CB  VAL A 510    12656   9032  10977    453  -1262    294       C  
ATOM   4197  CG1 VAL A 510     -11.570  53.717  24.927  1.00 87.05           C  
ANISOU 4197  CG1 VAL A 510    12949   9112  11015    510  -1065    208       C  
ATOM   4198  CG2 VAL A 510      -9.462  55.064  24.765  1.00 86.60           C  
ANISOU 4198  CG2 VAL A 510    12935   8968  11002    410  -1460    292       C  
ATOM   4199  N   ASP A 511     -11.197  51.423  22.317  1.00 80.64           N  
ANISOU 4199  N   ASP A 511    11569   8742  10327    423  -1082    332       N  
ATOM   4200  CA  ASP A 511     -12.169  50.559  21.655  1.00 78.06           C  
ANISOU 4200  CA  ASP A 511    11086   8532  10041    446   -949    332       C  
ATOM   4201  C   ASP A 511     -12.379  49.269  22.443  1.00 76.55           C  
ANISOU 4201  C   ASP A 511    10986   8345   9753    456   -847    271       C  
ATOM   4202  O   ASP A 511     -11.743  49.047  23.477  1.00 76.37           O  
ANISOU 4202  O   ASP A 511    11159   8236   9622    443   -887    231       O  
ATOM   4203  CB  ASP A 511     -11.718  50.247  20.222  1.00 76.62           C  
ANISOU 4203  CB  ASP A 511    10692   8500   9918    397  -1026    411       C  
ATOM   4204  CG  ASP A 511     -10.234  49.918  20.131  1.00 74.65           C  
ANISOU 4204  CG  ASP A 511    10452   8279   9634    332  -1156    448       C  
ATOM   4205  OD1 ASP A 511      -9.701  49.252  21.042  1.00 73.02           O  
ANISOU 4205  OD1 ASP A 511    10366   8029   9348    318  -1174    408       O  
ATOM   4206  OD2 ASP A 511      -9.598  50.331  19.141  1.00 75.00           O  
ANISOU 4206  OD2 ASP A 511    10380   8375   9741    294  -1237    524       O  
ATOM   4207  N   GLU A 512     -13.283  48.430  21.946  1.00 74.50           N  
ANISOU 4207  N   GLU A 512    10593   8174   9538    476   -728    267       N  
ATOM   4208  CA  GLU A 512     -13.566  47.135  22.551  1.00 72.08           C  
ANISOU 4208  CA  GLU A 512    10344   7886   9159    484   -620    217       C  
ATOM   4209  C   GLU A 512     -13.082  46.002  21.641  1.00 69.07           C  
ANISOU 4209  C   GLU A 512     9809   7661   8773    433   -674    253       C  
ATOM   4210  O   GLU A 512     -12.945  46.200  20.431  1.00 68.05           O  
ANISOU 4210  O   GLU A 512     9517   7625   8713    407   -744    314       O  
ATOM   4211  CB  GLU A 512     -15.070  46.987  22.827  1.00 73.06           C  
ANISOU 4211  CB  GLU A 512    10440   7962   9358    552   -418    182       C  
ATOM   4212  CG  GLU A 512     -15.639  47.942  23.886  1.00 76.43           C  
ANISOU 4212  CG  GLU A 512    11051   8208   9782    614   -303    134       C  
ATOM   4213  CD  GLU A 512     -15.154  47.647  25.309  1.00 78.67           C  
ANISOU 4213  CD  GLU A 512    11634   8370   9888    619   -265     68       C  
ATOM   4214  OE1 GLU A 512     -15.205  48.571  26.149  1.00 78.89           O  
ANISOU 4214  OE1 GLU A 512    11870   8240   9866    652   -231     33       O  
ATOM   4215  OE2 GLU A 512     -14.727  46.504  25.592  1.00 76.92           O  
ANISOU 4215  OE2 GLU A 512    11458   8199   9569    588   -274     50       O  
ATOM   4216  N   PRO A 513     -12.796  44.818  22.223  1.00 67.45           N  
ANISOU 4216  N   PRO A 513     9677   7475   8479    419   -639    216       N  
ATOM   4217  CA  PRO A 513     -12.559  43.624  21.416  1.00 65.35           C  
ANISOU 4217  CA  PRO A 513     9270   7346   8213    382   -650    240       C  
ATOM   4218  C   PRO A 513     -13.820  43.218  20.648  1.00 65.54           C  
ANISOU 4218  C   PRO A 513     9137   7439   8327    409   -549    246       C  
ATOM   4219  O   PRO A 513     -14.936  43.430  21.134  1.00 66.78           O  
ANISOU 4219  O   PRO A 513     9311   7522   8540    462   -425    215       O  
ATOM   4220  CB  PRO A 513     -12.209  42.560  22.461  1.00 64.55           C  
ANISOU 4220  CB  PRO A 513     9310   7212   8002    375   -614    189       C  
ATOM   4221  CG  PRO A 513     -12.741  43.082  23.742  1.00 65.88           C  
ANISOU 4221  CG  PRO A 513     9687   7228   8116    423   -526    131       C  
ATOM   4222  CD  PRO A 513     -12.572  44.553  23.654  1.00 66.97           C  
ANISOU 4222  CD  PRO A 513     9854   7293   8297    432   -603    154       C  
ATOM   4223  N   LEU A 514     -13.635  42.657  19.456  1.00 63.87           N  
ANISOU 4223  N   LEU A 514     8780   7349   8139    372   -603    290       N  
ATOM   4224  CA  LEU A 514     -14.744  42.215  18.614  1.00 63.49           C  
ANISOU 4224  CA  LEU A 514     8589   7357   8177    385   -557    305       C  
ATOM   4225  C   LEU A 514     -15.421  40.985  19.201  1.00 62.08           C  
ANISOU 4225  C   LEU A 514     8417   7182   7990    403   -436    255       C  
ATOM   4226  O   LEU A 514     -14.753  40.031  19.581  1.00 61.64           O  
ANISOU 4226  O   LEU A 514     8420   7161   7839    379   -429    230       O  
ATOM   4227  CB  LEU A 514     -14.239  41.890  17.204  1.00 63.70           C  
ANISOU 4227  CB  LEU A 514     8514   7498   8193    334   -655    362       C  
ATOM   4228  CG  LEU A 514     -14.291  42.901  16.052  1.00 64.97           C  
ANISOU 4228  CG  LEU A 514     8604   7672   8411    321   -750    429       C  
ATOM   4229  CD1 LEU A 514     -13.977  44.341  16.461  1.00 66.55           C  
ANISOU 4229  CD1 LEU A 514     8857   7788   8641    337   -791    445       C  
ATOM   4230  CD2 LEU A 514     -13.346  42.439  14.957  1.00 65.73           C  
ANISOU 4230  CD2 LEU A 514     8676   7858   8438    267   -815    477       C  
ATOM   4231  N   ASP A 515     -16.748  41.011  19.270  1.00 62.07           N  
ANISOU 4231  N   ASP A 515     8343   7131   8108    447   -339    245       N  
ATOM   4232  CA  ASP A 515     -17.507  39.852  19.717  1.00 62.27           C  
ANISOU 4232  CA  ASP A 515     8346   7151   8161    465   -214    209       C  
ATOM   4233  C   ASP A 515     -17.584  38.840  18.579  1.00 59.84           C  
ANISOU 4233  C   ASP A 515     7908   6959   7869    422   -288    237       C  
ATOM   4234  O   ASP A 515     -18.454  38.929  17.706  1.00 60.61           O  
ANISOU 4234  O   ASP A 515     7870   7064   8095    424   -330    273       O  
ATOM   4235  CB  ASP A 515     -18.906  40.265  20.185  1.00 66.14           C  
ANISOU 4235  CB  ASP A 515     8787   7525   8818    528    -71    199       C  
ATOM   4236  CG  ASP A 515     -19.721  39.092  20.713  1.00 69.91           C  
ANISOU 4236  CG  ASP A 515     9237   7977   9350    550     82    167       C  
ATOM   4237  OD1 ASP A 515     -20.954  39.095  20.505  1.00 72.39           O  
ANISOU 4237  OD1 ASP A 515     9408   8232   9864    583    157    187       O  
ATOM   4238  OD2 ASP A 515     -19.136  38.173  21.333  1.00 69.82           O  
ANISOU 4238  OD2 ASP A 515     9337   7994   9199    533    122    129       O  
ATOM   4239  N   VAL A 516     -16.652  37.889  18.594  1.00 55.45           N  
ANISOU 4239  N   VAL A 516     7405   6480   7184    383   -315    221       N  
ATOM   4240  CA  VAL A 516     -16.502  36.912  17.522  1.00 50.73           C  
ANISOU 4240  CA  VAL A 516     6722   5987   6564    340   -383    243       C  
ATOM   4241  C   VAL A 516     -16.457  35.474  18.047  1.00 49.67           C  
ANISOU 4241  C   VAL A 516     6614   5882   6375    332   -305    200       C  
ATOM   4242  O   VAL A 516     -16.130  35.230  19.214  1.00 47.72           O  
ANISOU 4242  O   VAL A 516     6479   5589   6063    347   -227    158       O  
ATOM   4243  CB  VAL A 516     -15.219  37.182  16.680  1.00 51.00           C  
ANISOU 4243  CB  VAL A 516     6780   6093   6506    292   -499    283       C  
ATOM   4244  CG1 VAL A 516     -15.371  38.442  15.836  1.00 51.66           C  
ANISOU 4244  CG1 VAL A 516     6820   6161   6646    291   -588    337       C  
ATOM   4245  CG2 VAL A 516     -13.985  37.282  17.572  1.00 48.38           C  
ANISOU 4245  CG2 VAL A 516     6561   5739   6080    283   -498    264       C  
ATOM   4246  N   ASP A 517     -16.781  34.524  17.174  1.00 47.79           N  
ANISOU 4246  N   ASP A 517     6290   5712   6155    305   -338    211       N  
ATOM   4247  CA  ASP A 517     -16.637  33.115  17.499  1.00 45.34           C  
ANISOU 4247  CA  ASP A 517     5996   5441   5789    290   -282    175       C  
ATOM   4248  C   ASP A 517     -15.273  32.627  16.993  1.00 43.82           C  
ANISOU 4248  C   ASP A 517     5850   5330   5470    245   -350    185       C  
ATOM   4249  O   ASP A 517     -15.083  32.383  15.798  1.00 43.53           O  
ANISOU 4249  O   ASP A 517     5771   5355   5414    212   -422    216       O  
ATOM   4250  CB  ASP A 517     -17.796  32.297  16.911  1.00 44.30           C  
ANISOU 4250  CB  ASP A 517     5749   5317   5765    288   -277    179       C  
ATOM   4251  CG  ASP A 517     -17.826  30.859  17.424  1.00 42.36           C  
ANISOU 4251  CG  ASP A 517     5518   5095   5484    280   -197    139       C  
ATOM   4252  OD1 ASP A 517     -18.928  30.279  17.488  1.00 43.45           O  
ANISOU 4252  OD1 ASP A 517     5570   5196   5742    294   -145    133       O  
ATOM   4253  OD2 ASP A 517     -16.757  30.301  17.759  1.00 36.80           O  
ANISOU 4253  OD2 ASP A 517     4900   4434   4649    260   -190    118       O  
ATOM   4254  N   TYR A 518     -14.329  32.481  17.917  1.00 40.15           N  
ANISOU 4254  N   TYR A 518     5481   4848   4925    242   -324    162       N  
ATOM   4255  CA  TYR A 518     -12.959  32.105  17.568  1.00 39.71           C  
ANISOU 4255  CA  TYR A 518     5452   4843   4794    203   -379    180       C  
ATOM   4256  C   TYR A 518     -12.794  30.694  16.975  1.00 38.49           C  
ANISOU 4256  C   TYR A 518     5260   4760   4604    176   -363    171       C  
ATOM   4257  O   TYR A 518     -11.722  30.366  16.471  1.00 37.70           O  
ANISOU 4257  O   TYR A 518     5163   4697   4463    146   -391    193       O  
ATOM   4258  CB  TYR A 518     -12.033  32.297  18.770  1.00 38.38           C  
ANISOU 4258  CB  TYR A 518     5393   4612   4578    205   -386    164       C  
ATOM   4259  CG  TYR A 518     -11.953  33.724  19.250  1.00 37.73           C  
ANISOU 4259  CG  TYR A 518     5369   4452   4513    224   -424    176       C  
ATOM   4260  CD1 TYR A 518     -12.793  34.185  20.255  1.00 39.32           C  
ANISOU 4260  CD1 TYR A 518     5651   4568   4723    266   -355    140       C  
ATOM   4261  CD2 TYR A 518     -11.039  34.616  18.694  1.00 38.15           C  
ANISOU 4261  CD2 TYR A 518     5406   4507   4583    202   -515    226       C  
ATOM   4262  CE1 TYR A 518     -12.730  35.505  20.696  1.00 41.32           C  
ANISOU 4262  CE1 TYR A 518     5975   4739   4987    286   -385    147       C  
ATOM   4263  CE2 TYR A 518     -10.962  35.932  19.131  1.00 36.23           C  
ANISOU 4263  CE2 TYR A 518     5219   4188   4361    218   -559    237       C  
ATOM   4264  CZ  TYR A 518     -11.810  36.370  20.130  1.00 38.72           C  
ANISOU 4264  CZ  TYR A 518     5623   4419   4670    260   -499    194       C  
ATOM   4265  OH  TYR A 518     -11.748  37.678  20.568  1.00 44.38           O  
ANISOU 4265  OH  TYR A 518     6412   5050   5402    278   -538    201       O  
ATOM   4266  N   ARG A 519     -13.854  29.886  17.016  1.00 37.35           N  
ANISOU 4266  N   ARG A 519     5076   4624   4492    187   -312    142       N  
ATOM   4267  CA  ARG A 519     -13.838  28.533  16.451  1.00 39.64           C  
ANISOU 4267  CA  ARG A 519     5336   4972   4752    161   -301    129       C  
ATOM   4268  C   ARG A 519     -13.927  28.521  14.923  1.00 40.59           C  
ANISOU 4268  C   ARG A 519     5419   5141   4862    134   -371    164       C  
ATOM   4269  O   ARG A 519     -13.755  27.471  14.298  1.00 42.57           O  
ANISOU 4269  O   ARG A 519     5671   5434   5068    109   -370    156       O  
ATOM   4270  CB  ARG A 519     -14.982  27.685  17.027  1.00 40.97           C  
ANISOU 4270  CB  ARG A 519     5473   5118   4976    180   -228     92       C  
ATOM   4271  CG  ARG A 519     -15.002  27.549  18.556  1.00 42.08           C  
ANISOU 4271  CG  ARG A 519     5691   5195   5104    208   -133     55       C  
ATOM   4272  CD  ARG A 519     -16.235  26.777  19.022  1.00 44.96           C  
ANISOU 4272  CD  ARG A 519     6013   5523   5546    230    -34     28       C  
ATOM   4273  NE  ARG A 519     -17.476  27.517  18.778  1.00 45.41           N  
ANISOU 4273  NE  ARG A 519     5981   5529   5743    257    -17     47       N  
ATOM   4274  CZ  ARG A 519     -18.702  26.994  18.821  1.00 46.02           C  
ANISOU 4274  CZ  ARG A 519     5966   5565   5954    272     47     44       C  
ATOM   4275  NH1 ARG A 519     -18.885  25.704  19.095  1.00 38.45           N  
ANISOU 4275  NH1 ARG A 519     5000   4619   4992    262    104     20       N  
ATOM   4276  NH2 ARG A 519     -19.751  27.770  18.582  1.00 43.30           N  
ANISOU 4276  NH2 ARG A 519     5525   5157   5769    298     49     72       N  
ATOM   4277  N   PHE A 520     -14.212  29.677  14.327  1.00 40.71           N  
ANISOU 4277  N   PHE A 520     5418   5139   4910    138   -434    202       N  
ATOM   4278  CA  PHE A 520     -14.367  29.784  12.875  1.00 42.56           C  
ANISOU 4278  CA  PHE A 520     5654   5398   5119    110   -515    239       C  
ATOM   4279  C   PHE A 520     -13.420  30.827  12.310  1.00 42.40           C  
ANISOU 4279  C   PHE A 520     5677   5379   5054     99   -546    288       C  
ATOM   4280  O   PHE A 520     -13.176  31.859  12.940  1.00 42.43           O  
ANISOU 4280  O   PHE A 520     5676   5350   5097    119   -546    299       O  
ATOM   4281  CB  PHE A 520     -15.822  30.090  12.501  1.00 43.40           C  
ANISOU 4281  CB  PHE A 520     5696   5465   5330    120   -584    251       C  
ATOM   4282  CG  PHE A 520     -16.798  29.053  13.001  1.00 46.83           C  
ANISOU 4282  CG  PHE A 520     6068   5882   5842    129   -546    213       C  
ATOM   4283  CD1 PHE A 520     -17.051  27.897  12.257  1.00 46.18           C  
ANISOU 4283  CD1 PHE A 520     5991   5825   5729     98   -588    204       C  
ATOM   4284  CD2 PHE A 520     -17.435  29.210  14.232  1.00 43.38           C  
ANISOU 4284  CD2 PHE A 520     5581   5393   5509    170   -456    188       C  
ATOM   4285  CE1 PHE A 520     -17.938  26.924  12.726  1.00 46.56           C  
ANISOU 4285  CE1 PHE A 520     5971   5851   5867    104   -555    174       C  
ATOM   4286  CE2 PHE A 520     -18.322  28.243  14.708  1.00 43.15           C  
ANISOU 4286  CE2 PHE A 520     5491   5338   5568    179   -398    160       C  
ATOM   4287  CZ  PHE A 520     -18.575  27.099  13.954  1.00 43.43           C  
ANISOU 4287  CZ  PHE A 520     5508   5403   5590    145   -454    155       C  
ATOM   4288  N   ASP A 521     -12.866  30.537  11.136  1.00 42.16           N  
ANISOU 4288  N   ASP A 521     5702   5376   4942     68   -563    316       N  
ATOM   4289  CA  ASP A 521     -11.919  31.436  10.477  1.00 42.14           C  
ANISOU 4289  CA  ASP A 521     5746   5366   4900     55   -567    371       C  
ATOM   4290  C   ASP A 521     -12.511  32.831  10.343  1.00 41.57           C  
ANISOU 4290  C   ASP A 521     5655   5256   4884     68   -647    406       C  
ATOM   4291  O   ASP A 521     -13.671  32.987   9.958  1.00 43.63           O  
ANISOU 4291  O   ASP A 521     5897   5498   5182     71   -726    409       O  
ATOM   4292  CB  ASP A 521     -11.498  30.864   9.118  1.00 43.99           C  
ANISOU 4292  CB  ASP A 521     6072   5616   5028     22   -553    396       C  
ATOM   4293  CG  ASP A 521     -10.487  29.730   9.260  1.00 46.67           C  
ANISOU 4293  CG  ASP A 521     6427   5978   5329     13   -445    375       C  
ATOM   4294  OD1 ASP A 521      -9.289  30.028   9.461  1.00 49.22           O  
ANISOU 4294  OD1 ASP A 521     6738   6287   5677     13   -377    404       O  
ATOM   4295  OD2 ASP A 521     -10.885  28.547   9.190  1.00 45.41           O  
ANISOU 4295  OD2 ASP A 521     6280   5839   5133      6   -431    334       O  
ATOM   4296  N   PHE A 522     -11.738  33.845  10.708  1.00 40.02           N  
ANISOU 4296  N   PHE A 522     5455   5037   4714     76   -636    435       N  
ATOM   4297  CA  PHE A 522     -12.247  35.207  10.626  1.00 41.20           C  
ANISOU 4297  CA  PHE A 522     5587   5146   4920     90   -707    468       C  
ATOM   4298  C   PHE A 522     -12.621  35.545   9.193  1.00 42.49           C  
ANISOU 4298  C   PHE A 522     5806   5305   5035     66   -783    518       C  
ATOM   4299  O   PHE A 522     -11.904  35.193   8.256  1.00 42.61           O  
ANISOU 4299  O   PHE A 522     5902   5335   4954     37   -753    548       O  
ATOM   4300  CB  PHE A 522     -11.233  36.230  11.142  1.00 39.46           C  
ANISOU 4300  CB  PHE A 522     5367   4896   4732     95   -694    497       C  
ATOM   4301  CG  PHE A 522     -11.005  36.173  12.626  1.00 39.73           C  
ANISOU 4301  CG  PHE A 522     5381   4903   4811    118   -662    451       C  
ATOM   4302  CD1 PHE A 522     -11.998  35.713  13.488  1.00 38.72           C  
ANISOU 4302  CD1 PHE A 522     5236   4765   4712    146   -639    394       C  
ATOM   4303  CD2 PHE A 522      -9.803  36.612  13.167  1.00 35.68           C  
ANISOU 4303  CD2 PHE A 522     4880   4357   4319    111   -659    471       C  
ATOM   4304  CE1 PHE A 522     -11.774  35.663  14.863  1.00 39.99           C  
ANISOU 4304  CE1 PHE A 522     5424   4884   4885    167   -603    353       C  
ATOM   4305  CE2 PHE A 522      -9.577  36.577  14.538  1.00 36.62           C  
ANISOU 4305  CE2 PHE A 522     5021   4432   4462    127   -658    431       C  
ATOM   4306  CZ  PHE A 522     -10.558  36.101  15.388  1.00 36.66           C  
ANISOU 4306  CZ  PHE A 522     5042   4427   4459    155   -625    369       C  
ATOM   4307  N   SER A 523     -13.756  36.217   9.039  1.00 43.82           N  
ANISOU 4307  N   SER A 523     5940   5437   5275     79   -878    531       N  
ATOM   4308  CA  SER A 523     -14.165  36.776   7.760  1.00 45.82           C  
ANISOU 4308  CA  SER A 523     6256   5662   5492     55   -987    588       C  
ATOM   4309  C   SER A 523     -13.255  37.954   7.377  1.00 46.95           C  
ANISOU 4309  C   SER A 523     6448   5787   5605     48   -978    647       C  
ATOM   4310  O   SER A 523     -12.442  38.414   8.179  1.00 47.55           O  
ANISOU 4310  O   SER A 523     6485   5864   5718     64   -908    643       O  
ATOM   4311  CB  SER A 523     -15.618  37.251   7.851  1.00 44.97           C  
ANISOU 4311  CB  SER A 523     6067   5500   5518     74  -1100    592       C  
ATOM   4312  OG  SER A 523     -15.713  38.362   8.726  1.00 45.16           O  
ANISOU 4312  OG  SER A 523     6017   5489   5652    111  -1080    594       O  
ATOM   4313  N   ASP A 524     -13.407  38.445   6.155  1.00 50.52           N  
ANISOU 4313  N   ASP A 524     6994   6209   5993     23  -1060    705       N  
ATOM   4314  CA  ASP A 524     -12.685  39.634   5.718  1.00 52.59           C  
ANISOU 4314  CA  ASP A 524     7303   6442   6237     16  -1057    770       C  
ATOM   4315  C   ASP A 524     -13.101  40.887   6.502  1.00 53.21           C  
ANISOU 4315  C   ASP A 524     7279   6485   6455     48  -1110    777       C  
ATOM   4316  O   ASP A 524     -12.256  41.726   6.828  1.00 52.41           O  
ANISOU 4316  O   ASP A 524     7164   6370   6379     53  -1065    804       O  
ATOM   4317  CB  ASP A 524     -12.861  39.835   4.212  1.00 54.49           C  
ANISOU 4317  CB  ASP A 524     7700   6645   6359    -20  -1137    832       C  
ATOM   4318  CG  ASP A 524     -12.178  38.745   3.394  1.00 56.66           C  
ANISOU 4318  CG  ASP A 524     8120   6936   6472    -50  -1044    830       C  
ATOM   4319  OD1 ASP A 524     -11.377  37.967   3.957  1.00 57.40           O  
ANISOU 4319  OD1 ASP A 524     8171   7073   6564    -43   -906    793       O  
ATOM   4320  OD2 ASP A 524     -12.442  38.665   2.179  1.00 61.64           O  
ANISOU 4320  OD2 ASP A 524     8922   7525   6975    -82  -1112    868       O  
ATOM   4321  N   GLU A 525     -14.392  40.994   6.818  1.00 54.36           N  
ANISOU 4321  N   GLU A 525     7348   6602   6704     70  -1199    755       N  
ATOM   4322  CA  GLU A 525     -14.917  42.114   7.609  1.00 56.93           C  
ANISOU 4322  CA  GLU A 525     7578   6878   7174    108  -1229    756       C  
ATOM   4323  C   GLU A 525     -14.274  42.167   8.995  1.00 55.99           C  
ANISOU 4323  C   GLU A 525     7411   6770   7091    138  -1113    705       C  
ATOM   4324  O   GLU A 525     -13.905  43.246   9.476  1.00 55.81           O  
ANISOU 4324  O   GLU A 525     7377   6711   7119    155  -1110    720       O  
ATOM   4325  CB  GLU A 525     -16.437  42.019   7.742  1.00 59.22           C  
ANISOU 4325  CB  GLU A 525     7778   7120   7602    130  -1314    741       C  
ATOM   4326  CG  GLU A 525     -17.079  43.211   8.442  1.00 66.04           C  
ANISOU 4326  CG  GLU A 525     8549   7913   8631    174  -1331    747       C  
ATOM   4327  CD  GLU A 525     -18.568  43.024   8.710  1.00 72.06           C  
ANISOU 4327  CD  GLU A 525     9191   8609   9578    203  -1376    734       C  
ATOM   4328  OE1 GLU A 525     -19.058  41.871   8.712  1.00 72.62           O  
ANISOU 4328  OE1 GLU A 525     9233   8698   9662    195  -1369    704       O  
ATOM   4329  OE2 GLU A 525     -19.253  44.046   8.929  1.00 76.01           O  
ANISOU 4329  OE2 GLU A 525     9617   9030  10234    235  -1415    758       O  
ATOM   4330  N   ILE A 526     -14.149  40.999   9.625  1.00 54.25           N  
ANISOU 4330  N   ILE A 526     7179   6591   6844    142  -1032    646       N  
ATOM   4331  CA  ILE A 526     -13.501  40.881  10.927  1.00 52.90           C  
ANISOU 4331  CA  ILE A 526     6996   6420   6685    162   -940    599       C  
ATOM   4332  C   ILE A 526     -12.009  41.210  10.817  1.00 52.90           C  
ANISOU 4332  C   ILE A 526     7041   6429   6629    137   -914    634       C  
ATOM   4333  O   ILE A 526     -11.467  41.951  11.643  1.00 52.03           O  
ANISOU 4333  O   ILE A 526     6930   6276   6562    150   -910    631       O  
ATOM   4334  CB  ILE A 526     -13.717  39.478  11.539  1.00 52.54           C  
ANISOU 4334  CB  ILE A 526     6936   6410   6616    168   -868    535       C  
ATOM   4335  CG1 ILE A 526     -15.192  39.293  11.913  1.00 51.56           C  
ANISOU 4335  CG1 ILE A 526     6743   6249   6597    200   -873    503       C  
ATOM   4336  CG2 ILE A 526     -12.814  39.268  12.759  1.00 50.22           C  
ANISOU 4336  CG2 ILE A 526     6668   6110   6304    177   -794    495       C  
ATOM   4337  CD1 ILE A 526     -15.620  37.843  12.079  1.00 51.33           C  
ANISOU 4337  CD1 ILE A 526     6693   6255   6553    195   -825    458       C  
ATOM   4338  N   LYS A 527     -11.363  40.672   9.784  1.00 53.02           N  
ANISOU 4338  N   LYS A 527     7102   6484   6561    101   -895    670       N  
ATOM   4339  CA  LYS A 527      -9.947  40.931   9.535  1.00 55.18           C  
ANISOU 4339  CA  LYS A 527     7400   6749   6815     77   -847    717       C  
ATOM   4340  C   LYS A 527      -9.617  42.423   9.405  1.00 57.75           C  
ANISOU 4340  C   LYS A 527     7724   7021   7199     78   -897    775       C  
ATOM   4341  O   LYS A 527      -8.629  42.889   9.976  1.00 58.04           O  
ANISOU 4341  O   LYS A 527     7738   7021   7292     74   -882    793       O  
ATOM   4342  CB  LYS A 527      -9.465  40.159   8.304  1.00 55.56           C  
ANISOU 4342  CB  LYS A 527     7517   6830   6765     44   -790    751       C  
ATOM   4343  CG  LYS A 527      -8.876  38.797   8.636  1.00 55.24           C  
ANISOU 4343  CG  LYS A 527     7468   6825   6694     37   -699    711       C  
ATOM   4344  CD  LYS A 527      -8.369  38.065   7.398  1.00 54.58           C  
ANISOU 4344  CD  LYS A 527     7473   6756   6510      9   -618    744       C  
ATOM   4345  CE  LYS A 527      -9.374  37.031   6.923  1.00 53.83           C  
ANISOU 4345  CE  LYS A 527     7432   6697   6322      4   -647    700       C  
ATOM   4346  NZ  LYS A 527      -8.753  36.069   5.980  1.00 53.62           N  
ANISOU 4346  NZ  LYS A 527     7508   6677   6189    -20   -545    712       N  
ATOM   4347  N   GLU A 528     -10.447  43.162   8.669  1.00 59.80           N  
ANISOU 4347  N   GLU A 528     8004   7263   7455     80   -972    809       N  
ATOM   4348  CA  GLU A 528     -10.237  44.598   8.467  1.00 61.82           C  
ANISOU 4348  CA  GLU A 528     8260   7464   7765     81  -1025    867       C  
ATOM   4349  C   GLU A 528     -10.397  45.384   9.763  1.00 60.95           C  
ANISOU 4349  C   GLU A 528     8097   7306   7755    115  -1055    831       C  
ATOM   4350  O   GLU A 528      -9.609  46.290  10.038  1.00 61.04           O  
ANISOU 4350  O   GLU A 528     8105   7270   7818    110  -1069    865       O  
ATOM   4351  CB  GLU A 528     -11.179  45.159   7.391  1.00 64.13           C  
ANISOU 4351  CB  GLU A 528     8593   7738   8033     75  -1118    912       C  
ATOM   4352  CG  GLU A 528     -11.027  44.523   6.009  1.00 67.50           C  
ANISOU 4352  CG  GLU A 528     9130   8186   8329     38  -1105    954       C  
ATOM   4353  CD  GLU A 528      -9.648  44.729   5.410  1.00 70.13           C  
ANISOU 4353  CD  GLU A 528     9527   8507   8614      9  -1005   1018       C  
ATOM   4354  OE1 GLU A 528      -8.831  43.782   5.470  1.00 70.33           O  
ANISOU 4354  OE1 GLU A 528     9559   8560   8603     -2   -891   1003       O  
ATOM   4355  OE2 GLU A 528      -9.384  45.837   4.889  1.00 69.11           O  
ANISOU 4355  OE2 GLU A 528     9431   8330   8499      0  -1033   1087       O  
ATOM   4356  N   LYS A 529     -11.415  45.031  10.549  1.00 59.96           N  
ANISOU 4356  N   LYS A 529     7941   7178   7662    149  -1057    763       N  
ATOM   4357  CA  LYS A 529     -11.676  45.685  11.829  1.00 59.53           C  
ANISOU 4357  CA  LYS A 529     7875   7062   7683    187  -1059    719       C  
ATOM   4358  C   LYS A 529     -10.530  45.483  12.813  1.00 58.06           C  
ANISOU 4358  C   LYS A 529     7720   6856   7485    179  -1028    695       C  
ATOM   4359  O   LYS A 529     -10.181  46.399  13.552  1.00 58.16           O  
ANISOU 4359  O   LYS A 529     7758   6796   7543    190  -1062    693       O  
ATOM   4360  CB  LYS A 529     -12.986  45.188  12.440  1.00 60.22           C  
ANISOU 4360  CB  LYS A 529     7930   7138   7811    227  -1027    656       C  
ATOM   4361  CG  LYS A 529     -14.222  45.925  11.964  1.00 62.09           C  
ANISOU 4361  CG  LYS A 529     8117   7333   8143    251  -1084    680       C  
ATOM   4362  CD  LYS A 529     -15.484  45.282  12.528  1.00 63.83           C  
ANISOU 4362  CD  LYS A 529     8280   7530   8441    289  -1032    627       C  
ATOM   4363  CE  LYS A 529     -16.730  45.715  11.768  1.00 63.12           C  
ANISOU 4363  CE  LYS A 529     8110   7399   8474    301  -1113    667       C  
ATOM   4364  NZ  LYS A 529     -17.876  44.782  11.985  1.00 63.49           N  
ANISOU 4364  NZ  LYS A 529     8079   7433   8612    322  -1075    634       N  
ATOM   4365  N   ILE A 530      -9.955  44.281  12.806  1.00 58.38           N  
ANISOU 4365  N   ILE A 530     7762   6949   7470    157   -976    678       N  
ATOM   4366  CA  ILE A 530      -8.791  43.936  13.628  1.00 59.59           C  
ANISOU 4366  CA  ILE A 530     7936   7076   7630    141   -968    666       C  
ATOM   4367  C   ILE A 530      -7.609  44.875  13.357  1.00 61.00           C  
ANISOU 4367  C   ILE A 530     8102   7203   7871    112  -1016    739       C  
ATOM   4368  O   ILE A 530      -6.929  45.320  14.289  1.00 60.30           O  
ANISOU 4368  O   ILE A 530     8038   7038   7834    109  -1071    733       O  
ATOM   4369  CB  ILE A 530      -8.381  42.453  13.413  1.00 59.58           C  
ANISOU 4369  CB  ILE A 530     7923   7141   7576    120   -902    650       C  
ATOM   4370  CG1 ILE A 530      -9.289  41.523  14.218  1.00 58.61           C  
ANISOU 4370  CG1 ILE A 530     7819   7038   7412    147   -862    568       C  
ATOM   4371  CG2 ILE A 530      -6.930  42.200  13.815  1.00 60.26           C  
ANISOU 4371  CG2 ILE A 530     7999   7191   7705     91   -908    675       C  
ATOM   4372  CD1 ILE A 530      -9.225  40.077  13.764  1.00 59.14           C  
ANISOU 4372  CD1 ILE A 530     7868   7180   7423    130   -799    552       C  
ATOM   4373  N   LYS A 531      -7.396  45.184  12.078  1.00 62.91           N  
ANISOU 4373  N   LYS A 531     8320   7472   8110     91  -1000    809       N  
ATOM   4374  CA  LYS A 531      -6.324  46.075  11.634  1.00 65.88           C  
ANISOU 4374  CA  LYS A 531     8676   7796   8562     63  -1020    892       C  
ATOM   4375  C   LYS A 531      -6.525  47.532  12.072  1.00 66.28           C  
ANISOU 4375  C   LYS A 531     8736   7770   8677     78  -1112    906       C  
ATOM   4376  O   LYS A 531      -5.654  48.378  11.841  1.00 67.47           O  
ANISOU 4376  O   LYS A 531     8864   7862   8908     56  -1143    974       O  
ATOM   4377  CB  LYS A 531      -6.174  46.002  10.109  1.00 67.64           C  
ANISOU 4377  CB  LYS A 531     8906   8057   8739     40   -955    963       C  
ATOM   4378  CG  LYS A 531      -5.829  44.615   9.583  1.00 70.53           C  
ANISOU 4378  CG  LYS A 531     9279   8479   9039     24   -851    956       C  
ATOM   4379  CD  LYS A 531      -5.479  44.659   8.109  1.00 73.55           C  
ANISOU 4379  CD  LYS A 531     9711   8867   9369      0   -770   1033       C  
ATOM   4380  CE  LYS A 531      -4.722  43.408   7.693  1.00 75.69           C  
ANISOU 4380  CE  LYS A 531     9989   9160   9611    -17   -638   1039       C  
ATOM   4381  NZ  LYS A 531      -4.163  43.526   6.312  1.00 78.93           N  
ANISOU 4381  NZ  LYS A 531    10472   9544   9975    -40   -523   1123       N  
ATOM   4382  N   LYS A 532      -7.658  47.816  12.709  1.00 65.03           N  
ANISOU 4382  N   LYS A 532     8610   7602   8498    117  -1143    843       N  
ATOM   4383  CA  LYS A 532      -7.964  49.164  13.189  1.00 65.08           C  
ANISOU 4383  CA  LYS A 532     8639   7527   8563    139  -1216    845       C  
ATOM   4384  C   LYS A 532      -8.085  49.214  14.712  1.00 64.81           C  
ANISOU 4384  C   LYS A 532     8674   7420   8531    166  -1241    768       C  
ATOM   4385  O   LYS A 532      -8.562  50.207  15.269  1.00 65.40           O  
ANISOU 4385  O   LYS A 532     8795   7418   8636    195  -1280    748       O  
ATOM   4386  CB  LYS A 532      -9.242  49.702  12.520  1.00 65.37           C  
ANISOU 4386  CB  LYS A 532     8662   7581   8596    166  -1224    852       C  
ATOM   4387  CG  LYS A 532      -9.090  49.955  11.021  1.00 67.84           C  
ANISOU 4387  CG  LYS A 532     8955   7931   8892    136  -1231    939       C  
ATOM   4388  CD  LYS A 532     -10.374  50.458  10.367  1.00 69.18           C  
ANISOU 4388  CD  LYS A 532     9116   8100   9068    158  -1276    951       C  
ATOM   4389  CE  LYS A 532     -10.186  50.593   8.856  1.00 71.59           C  
ANISOU 4389  CE  LYS A 532     9448   8431   9322    121  -1293   1037       C  
ATOM   4390  NZ  LYS A 532     -11.369  51.186   8.160  1.00 72.59           N  
ANISOU 4390  NZ  LYS A 532     9576   8536   9468    135  -1378   1064       N  
ATOM   4391  N   LEU A 533      -7.636  48.152  15.382  1.00 64.18           N  
ANISOU 4391  N   LEU A 533     8621   7352   8414    156  -1217    727       N  
ATOM   4392  CA  LEU A 533      -7.800  48.030  16.835  1.00 63.55           C  
ANISOU 4392  CA  LEU A 533     8650   7195   8302    180  -1233    649       C  
ATOM   4393  C   LEU A 533      -6.539  48.331  17.647  1.00 62.76           C  
ANISOU 4393  C   LEU A 533     8609   6993   8242    148  -1343    664       C  
ATOM   4394  O   LEU A 533      -5.415  48.147  17.174  1.00 62.72           O  
ANISOU 4394  O   LEU A 533     8530   6994   8307    104  -1383    729       O  
ATOM   4395  CB  LEU A 533      -8.363  46.648  17.212  1.00 63.11           C  
ANISOU 4395  CB  LEU A 533     8612   7199   8168    196  -1144    584       C  
ATOM   4396  CG  LEU A 533      -9.834  46.367  16.870  1.00 64.50           C  
ANISOU 4396  CG  LEU A 533     8754   7429   8325    237  -1052    550       C  
ATOM   4397  CD1 LEU A 533     -10.159  44.894  17.046  1.00 63.21           C  
ANISOU 4397  CD1 LEU A 533     8584   7332   8102    238   -972    503       C  
ATOM   4398  CD2 LEU A 533     -10.801  47.236  17.687  1.00 66.09           C  
ANISOU 4398  CD2 LEU A 533     9027   7536   8548    289  -1027    505       C  
ATOM   4399  N   SER A 534      -6.760  48.800  18.874  1.00 62.21           N  
ANISOU 4399  N   SER A 534     8684   6814   8139    171  -1391    606       N  
ATOM   4400  CA  SER A 534      -5.701  49.093  19.835  1.00 61.33           C  
ANISOU 4400  CA  SER A 534     8675   6575   8054    141  -1532    609       C  
ATOM   4401  C   SER A 534      -5.002  47.824  20.306  1.00 61.71           C  
ANISOU 4401  C   SER A 534     8739   6630   8079    111  -1553    595       C  
ATOM   4402  O   SER A 534      -5.518  46.718  20.128  1.00 61.54           O  
ANISOU 4402  O   SER A 534     8686   6705   7991    125  -1441    561       O  
ATOM   4403  CB  SER A 534      -6.289  49.816  21.045  1.00 62.18           C  
ANISOU 4403  CB  SER A 534     8984   6552   8089    178  -1560    538       C  
ATOM   4404  OG  SER A 534      -7.240  49.001  21.710  1.00 59.54           O  
ANISOU 4404  OG  SER A 534     8749   6232   7640    220  -1437    455       O  
ATOM   4405  N   ALA A 535      -3.833  47.994  20.919  1.00 60.91           N  
ANISOU 4405  N   ALA A 535     8685   6413   8045     69  -1712    625       N  
ATOM   4406  CA  ALA A 535      -3.099  46.878  21.503  1.00 60.10           C  
ANISOU 4406  CA  ALA A 535     8609   6283   7942     38  -1770    617       C  
ATOM   4407  C   ALA A 535      -3.882  46.207  22.630  1.00 59.45           C  
ANISOU 4407  C   ALA A 535     8725   6172   7691     71  -1726    517       C  
ATOM   4408  O   ALA A 535      -3.868  44.983  22.751  1.00 59.50           O  
ANISOU 4408  O   ALA A 535     8719   6234   7653     66  -1672    495       O  
ATOM   4409  CB  ALA A 535      -1.728  47.331  21.994  1.00 61.00           C  
ANISOU 4409  CB  ALA A 535     8737   6246   8193    -17  -1985    676       C  
ATOM   4410  N   LYS A 536      -4.570  47.010  23.441  1.00 59.21           N  
ANISOU 4410  N   LYS A 536     8884   6045   7567    106  -1732    459       N  
ATOM   4411  CA  LYS A 536      -5.323  46.499  24.585  1.00 58.82           C  
ANISOU 4411  CA  LYS A 536     9060   5936   7353    142  -1666    367       C  
ATOM   4412  C   LYS A 536      -6.414  45.527  24.142  1.00 56.81           C  
ANISOU 4412  C   LYS A 536     8719   5826   7042    182  -1450    329       C  
ATOM   4413  O   LYS A 536      -6.561  44.447  24.714  1.00 56.28           O  
ANISOU 4413  O   LYS A 536     8731   5764   6888    185  -1400    286       O  
ATOM   4414  CB  LYS A 536      -5.931  47.649  25.395  1.00 60.22           C  
ANISOU 4414  CB  LYS A 536     9455   5974   7452    181  -1669    317       C  
ATOM   4415  CG  LYS A 536      -6.600  47.200  26.691  1.00 63.12           C  
ANISOU 4415  CG  LYS A 536    10105   6237   7639    217  -1590    225       C  
ATOM   4416  CD  LYS A 536      -7.377  48.320  27.362  1.00 65.31           C  
ANISOU 4416  CD  LYS A 536    10593   6381   7841    269  -1527    171       C  
ATOM   4417  CE  LYS A 536      -8.177  47.780  28.537  1.00 66.89           C  
ANISOU 4417  CE  LYS A 536    11071   6482   7862    315  -1380     82       C  
ATOM   4418  NZ  LYS A 536      -9.009  48.831  29.180  1.00 72.55           N  
ANISOU 4418  NZ  LYS A 536    12001   7056   8511    376  -1270     28       N  
ATOM   4419  N   SER A 537      -7.167  45.925  23.118  1.00 55.70           N  
ANISOU 4419  N   SER A 537     8417   5789   6956    210  -1339    349       N  
ATOM   4420  CA  SER A 537      -8.237  45.108  22.562  1.00 53.23           C  
ANISOU 4420  CA  SER A 537     8000   5602   6622    244  -1162    324       C  
ATOM   4421  C   SER A 537      -7.710  43.893  21.802  1.00 50.81           C  
ANISOU 4421  C   SER A 537     7542   5421   6343    207  -1152    358       C  
ATOM   4422  O   SER A 537      -8.280  42.803  21.901  1.00 49.19           O  
ANISOU 4422  O   SER A 537     7331   5277   6083    222  -1047    318       O  
ATOM   4423  CB  SER A 537      -9.135  45.949  21.655  1.00 53.09           C  
ANISOU 4423  CB  SER A 537     7861   5637   6674    276  -1090    347       C  
ATOM   4424  OG  SER A 537      -9.836  46.917  22.411  1.00 56.21           O  
ANISOU 4424  OG  SER A 537     8395   5914   7048    322  -1054    305       O  
ATOM   4425  N   LEU A 538      -6.630  44.083  21.046  1.00 50.13           N  
ANISOU 4425  N   LEU A 538     7335   5362   6350    161  -1248    432       N  
ATOM   4426  CA  LEU A 538      -6.027  42.990  20.283  1.00 49.13           C  
ANISOU 4426  CA  LEU A 538     7073   5335   6261    128  -1222    469       C  
ATOM   4427  C   LEU A 538      -5.487  41.929  21.220  1.00 48.65           C  
ANISOU 4427  C   LEU A 538     7098   5230   6157    110  -1263    436       C  
ATOM   4428  O   LEU A 538      -5.696  40.739  20.991  1.00 47.35           O  
ANISOU 4428  O   LEU A 538     6883   5150   5958    110  -1177    417       O  
ATOM   4429  CB  LEU A 538      -4.927  43.493  19.344  1.00 49.25           C  
ANISOU 4429  CB  LEU A 538     6953   5356   6403     86  -1290    562       C  
ATOM   4430  CG  LEU A 538      -5.368  44.343  18.144  1.00 51.00           C  
ANISOU 4430  CG  LEU A 538     7078   5638   6660     96  -1239    609       C  
ATOM   4431  CD1 LEU A 538      -4.175  45.058  17.538  1.00 52.11           C  
ANISOU 4431  CD1 LEU A 538     7131   5735   6932     56  -1313    702       C  
ATOM   4432  CD2 LEU A 538      -6.100  43.526  17.085  1.00 50.12           C  
ANISOU 4432  CD2 LEU A 538     6882   5660   6499    107  -1112    606       C  
ATOM   4433  N   ASN A 539      -4.822  42.365  22.287  1.00 48.23           N  
ANISOU 4433  N   ASN A 539     7188   5034   6103     92  -1406    431       N  
ATOM   4434  CA  ASN A 539      -4.322  41.450  23.308  1.00 48.90           C  
ANISOU 4434  CA  ASN A 539     7394   5047   6138     72  -1479    401       C  
ATOM   4435  C   ASN A 539      -5.423  40.652  23.983  1.00 48.27           C  
ANISOU 4435  C   ASN A 539     7445   4989   5905    113  -1345    317       C  
ATOM   4436  O   ASN A 539      -5.259  39.456  24.222  1.00 46.37           O  
ANISOU 4436  O   ASN A 539     7209   4777   5631    101  -1323    300       O  
ATOM   4437  CB  ASN A 539      -3.496  42.183  24.364  1.00 50.34           C  
ANISOU 4437  CB  ASN A 539     7747   5044   6336     43  -1688    410       C  
ATOM   4438  CG  ASN A 539      -2.086  42.465  23.902  1.00 52.34           C  
ANISOU 4438  CG  ASN A 539     7853   5249   6783    -13  -1848    505       C  
ATOM   4439  OD1 ASN A 539      -1.571  43.570  24.086  1.00 54.88           O  
ANISOU 4439  OD1 ASN A 539     8209   5460   7181    -32  -1990    542       O  
ATOM   4440  ND2 ASN A 539      -1.456  41.472  23.281  1.00 51.64           N  
ANISOU 4440  ND2 ASN A 539     7592   5234   6794    -38  -1815    550       N  
ATOM   4441  N   GLU A 540      -6.538  41.316  24.284  1.00 48.45           N  
ANISOU 4441  N   GLU A 540     7568   4988   5853    162  -1247    268       N  
ATOM   4442  CA  GLU A 540      -7.668  40.650  24.925  1.00 49.47           C  
ANISOU 4442  CA  GLU A 540     7813   5119   5865    207  -1087    194       C  
ATOM   4443  C   GLU A 540      -8.287  39.632  23.974  1.00 47.03           C  
ANISOU 4443  C   GLU A 540     7310   4972   5589    216   -947    197       C  
ATOM   4444  O   GLU A 540      -8.700  38.549  24.398  1.00 47.19           O  
ANISOU 4444  O   GLU A 540     7376   5012   5543    227   -858    156       O  
ATOM   4445  CB  GLU A 540      -8.709  41.662  25.427  1.00 50.09           C  
ANISOU 4445  CB  GLU A 540     8024   5113   5895    262   -992    150       C  
ATOM   4446  CG  GLU A 540     -10.000  41.042  26.001  1.00 56.67           C  
ANISOU 4446  CG  GLU A 540     8948   5935   6648    316   -781     84       C  
ATOM   4447  CD  GLU A 540      -9.769  40.087  27.184  1.00 62.69           C  
ANISOU 4447  CD  GLU A 540     9932   6612   7275    308   -778     38       C  
ATOM   4448  OE1 GLU A 540      -8.815  40.302  27.963  1.00 67.84           O  
ANISOU 4448  OE1 GLU A 540    10771   7144   7860    274   -947     39       O  
ATOM   4449  OE2 GLU A 540     -10.555  39.122  27.341  1.00 60.83           O  
ANISOU 4449  OE2 GLU A 540     9690   6418   7004    334   -615      4       O  
ATOM   4450  N   MET A 541      -8.326  39.983  22.689  1.00 44.65           N  
ANISOU 4450  N   MET A 541     6809   4775   5383    210   -936    247       N  
ATOM   4451  CA  MET A 541      -8.798  39.077  21.643  1.00 42.28           C  
ANISOU 4451  CA  MET A 541     6339   4616   5110    209   -839    257       C  
ATOM   4452  C   MET A 541      -7.878  37.869  21.504  1.00 40.65           C  
ANISOU 4452  C   MET A 541     6084   4457   4905    169   -873    273       C  
ATOM   4453  O   MET A 541      -8.348  36.747  21.315  1.00 40.70           O  
ANISOU 4453  O   MET A 541     6047   4537   4880    175   -782    248       O  
ATOM   4454  CB  MET A 541      -8.941  39.808  20.303  1.00 41.90           C  
ANISOU 4454  CB  MET A 541     6136   4642   5142    206   -843    313       C  
ATOM   4455  CG  MET A 541     -10.154  40.735  20.226  1.00 40.11           C  
ANISOU 4455  CG  MET A 541     5911   4392   4937    251   -783    298       C  
ATOM   4456  SD  MET A 541     -10.486  41.392  18.575  1.00 44.20           S  
ANISOU 4456  SD  MET A 541     6260   4997   5537    244   -798    364       S  
ATOM   4457  CE  MET A 541     -10.829  39.898  17.633  1.00 38.40           C  
ANISOU 4457  CE  MET A 541     5419   4389   4781    227   -733    364       C  
ATOM   4458  N   LEU A 542      -6.572  38.109  21.614  1.00 39.38           N  
ANISOU 4458  N   LEU A 542     5922   4240   4799    129  -1005    319       N  
ATOM   4459  CA  LEU A 542      -5.573  37.056  21.508  1.00 38.54           C  
ANISOU 4459  CA  LEU A 542     5756   4153   4735     91  -1045    345       C  
ATOM   4460  C   LEU A 542      -5.743  36.088  22.668  1.00 39.91           C  
ANISOU 4460  C   LEU A 542     6072   4277   4814     96  -1042    287       C  
ATOM   4461  O   LEU A 542      -5.702  34.869  22.477  1.00 36.57           O  
ANISOU 4461  O   LEU A 542     5594   3920   4382     88   -984    277       O  
ATOM   4462  CB  LEU A 542      -4.150  37.636  21.479  1.00 36.64           C  
ANISOU 4462  CB  LEU A 542     5473   3828   4620     48  -1198    417       C  
ATOM   4463  CG  LEU A 542      -2.978  36.639  21.434  1.00 37.43           C  
ANISOU 4463  CG  LEU A 542     5492   3913   4815      8  -1251    457       C  
ATOM   4464  CD1 LEU A 542      -3.062  35.707  20.230  1.00 35.52           C  
ANISOU 4464  CD1 LEU A 542     5095   3805   4596      9  -1104    474       C  
ATOM   4465  CD2 LEU A 542      -1.625  37.354  21.460  1.00 36.82           C  
ANISOU 4465  CD2 LEU A 542     5357   3722   4910    -33  -1409    538       C  
ATOM   4466  N   PHE A 543      -5.950  36.649  23.860  1.00 40.67           N  
ANISOU 4466  N   PHE A 543     6370   4249   4832    110  -1098    249       N  
ATOM   4467  CA  PHE A 543      -6.203  35.865  25.057  1.00 41.37           C  
ANISOU 4467  CA  PHE A 543     6649   4266   4803    118  -1085    193       C  
ATOM   4468  C   PHE A 543      -7.395  34.936  24.850  1.00 41.71           C  
ANISOU 4468  C   PHE A 543     6653   4409   4787    154   -889    145       C  
ATOM   4469  O   PHE A 543      -7.347  33.767  25.232  1.00 42.95           O  
ANISOU 4469  O   PHE A 543     6843   4577   4898    145   -860    123       O  
ATOM   4470  CB  PHE A 543      -6.440  36.775  26.272  1.00 42.15           C  
ANISOU 4470  CB  PHE A 543     7010   4204   4801    136  -1139    154       C  
ATOM   4471  CG  PHE A 543      -6.800  36.023  27.535  1.00 44.46           C  
ANISOU 4471  CG  PHE A 543     7548   4403   4942    149  -1100     94       C  
ATOM   4472  CD1 PHE A 543      -5.810  35.429  28.316  1.00 47.90           C  
ANISOU 4472  CD1 PHE A 543     8113   4739   5347    105  -1267    105       C  
ATOM   4473  CD2 PHE A 543      -8.130  35.897  27.935  1.00 45.61           C  
ANISOU 4473  CD2 PHE A 543     7793   4546   4990    204   -892     34       C  
ATOM   4474  CE1 PHE A 543      -6.140  34.718  29.480  1.00 49.60           C  
ANISOU 4474  CE1 PHE A 543     8583   4858   5403    114  -1233     53       C  
ATOM   4475  CE2 PHE A 543      -8.473  35.192  29.095  1.00 45.18           C  
ANISOU 4475  CE2 PHE A 543     7981   4395   4791    217   -827    -18       C  
ATOM   4476  CZ  PHE A 543      -7.475  34.604  29.868  1.00 48.68           C  
ANISOU 4476  CZ  PHE A 543     8582   4744   5172    171  -1000    -10       C  
ATOM   4477  N   ARG A 544      -8.456  35.464  24.246  1.00 41.86           N  
ANISOU 4477  N   ARG A 544     6592   4489   4823    191   -767    134       N  
ATOM   4478  CA  ARG A 544      -9.682  34.706  24.005  1.00 42.10           C  
ANISOU 4478  CA  ARG A 544     6564   4595   4837    225   -594     98       C  
ATOM   4479  C   ARG A 544      -9.503  33.693  22.883  1.00 41.89           C  
ANISOU 4479  C   ARG A 544     6346   4706   4865    200   -575    123       C  
ATOM   4480  O   ARG A 544     -10.055  32.594  22.942  1.00 41.21           O  
ANISOU 4480  O   ARG A 544     6240   4664   4752    207   -482     94       O  
ATOM   4481  CB  ARG A 544     -10.840  35.648  23.681  1.00 41.57           C  
ANISOU 4481  CB  ARG A 544     6457   4527   4812    270   -497     90       C  
ATOM   4482  CG  ARG A 544     -11.308  36.486  24.862  1.00 43.13           C  
ANISOU 4482  CG  ARG A 544     6865   4578   4946    309   -451     50       C  
ATOM   4483  CD  ARG A 544     -12.307  37.524  24.417  1.00 45.14           C  
ANISOU 4483  CD  ARG A 544     7045   4824   5281    351   -370     55       C  
ATOM   4484  NE  ARG A 544     -12.544  38.521  25.454  1.00 49.08           N  
ANISOU 4484  NE  ARG A 544     7753   5170   5726    387   -338     24       N  
ATOM   4485  CZ  ARG A 544     -13.440  39.502  25.369  1.00 50.35           C  
ANISOU 4485  CZ  ARG A 544     7895   5281   5956    433   -249     20       C  
ATOM   4486  NH1 ARG A 544     -14.204  39.630  24.290  1.00 46.80           N  
ANISOU 4486  NH1 ARG A 544     7220   4922   5641    447   -204     51       N  
ATOM   4487  NH2 ARG A 544     -13.574  40.355  26.371  1.00 49.97           N  
ANISOU 4487  NH2 ARG A 544     8066   5078   5841    466   -211    -13       N  
ATOM   4488  N   ALA A 545      -8.743  34.079  21.858  1.00 40.75           N  
ANISOU 4488  N   ALA A 545     6071   4617   4794    171   -653    180       N  
ATOM   4489  CA  ALA A 545      -8.400  33.166  20.780  1.00 39.08           C  
ANISOU 4489  CA  ALA A 545     5714   4514   4621    146   -631    207       C  
ATOM   4490  C   ALA A 545      -7.680  31.960  21.382  1.00 37.15           C  
ANISOU 4490  C   ALA A 545     5509   4252   4353    123   -653    194       C  
ATOM   4491  O   ALA A 545      -8.079  30.817  21.157  1.00 37.63           O  
ANISOU 4491  O   ALA A 545     5529   4378   4391    124   -574    169       O  
ATOM   4492  CB  ALA A 545      -7.529  33.863  19.727  1.00 36.80           C  
ANISOU 4492  CB  ALA A 545     5320   4251   4412    120   -695    275       C  
ATOM   4493  N   GLN A 546      -6.651  32.234  22.179  1.00 36.07           N  
ANISOU 4493  N   GLN A 546     5458   4015   4231    100   -775    212       N  
ATOM   4494  CA  GLN A 546      -5.836  31.186  22.800  1.00 38.98           C  
ANISOU 4494  CA  GLN A 546     5867   4343   4601     73   -833    211       C  
ATOM   4495  C   GLN A 546      -6.623  30.304  23.769  1.00 37.42           C  
ANISOU 4495  C   GLN A 546     5806   4124   4289     93   -761    147       C  
ATOM   4496  O   GLN A 546      -6.351  29.112  23.861  1.00 38.47           O  
ANISOU 4496  O   GLN A 546     5919   4280   4418     78   -747    140       O  
ATOM   4497  CB  GLN A 546      -4.597  31.782  23.478  1.00 40.48           C  
ANISOU 4497  CB  GLN A 546     6125   4401   4854     40  -1017    253       C  
ATOM   4498  CG  GLN A 546      -3.528  32.254  22.481  1.00 43.30           C  
ANISOU 4498  CG  GLN A 546     6308   4772   5373     12  -1076    333       C  
ATOM   4499  CD  GLN A 546      -2.430  33.113  23.106  1.00 48.66           C  
ANISOU 4499  CD  GLN A 546     7036   5304   6149    -20  -1272    382       C  
ATOM   4500  OE1 GLN A 546      -1.369  33.297  22.509  1.00 52.72           O  
ANISOU 4500  OE1 GLN A 546     7406   5794   6831    -50  -1329    456       O  
ATOM   4501  NE2 GLN A 546      -2.687  33.656  24.297  1.00 45.62           N  
ANISOU 4501  NE2 GLN A 546     6863   4805   5667    -15  -1370    345       N  
ATOM   4502  N   ARG A 547      -7.595  30.887  24.476  1.00 36.57           N  
ANISOU 4502  N   ARG A 547     5837   3962   4097    129   -700    104       N  
ATOM   4503  CA  ARG A 547      -8.513  30.114  25.318  1.00 37.10           C  
ANISOU 4503  CA  ARG A 547     6030   4002   4063    155   -582     46       C  
ATOM   4504  C   ARG A 547      -9.447  29.209  24.508  1.00 36.91           C  
ANISOU 4504  C   ARG A 547     5853   4102   4068    171   -434     30       C  
ATOM   4505  O   ARG A 547      -9.651  28.046  24.867  1.00 37.67           O  
ANISOU 4505  O   ARG A 547     5977   4210   4126    169   -375      5       O  
ATOM   4506  CB  ARG A 547      -9.316  31.019  26.262  1.00 38.06           C  
ANISOU 4506  CB  ARG A 547     6345   4012   4103    195   -520      8       C  
ATOM   4507  CG  ARG A 547      -8.528  31.510  27.494  1.00 40.58           C  
ANISOU 4507  CG  ARG A 547     6919   4167   4333    178   -662      4       C  
ATOM   4508  CD  ARG A 547      -8.109  30.344  28.406  1.00 42.04           C  
ANISOU 4508  CD  ARG A 547     7255   4288   4431    156   -703    -14       C  
ATOM   4509  NE  ARG A 547      -7.384  30.771  29.605  1.00 45.07           N  
ANISOU 4509  NE  ARG A 547     7916   4492   4717    134   -868    -16       N  
ATOM   4510  CZ  ARG A 547      -7.965  31.179  30.733  1.00 49.47           C  
ANISOU 4510  CZ  ARG A 547     8769   4906   5120    163   -806    -63       C  
ATOM   4511  NH1 ARG A 547      -9.293  31.230  30.833  1.00 49.16           N  
ANISOU 4511  NH1 ARG A 547     8761   4882   5035    220   -560   -106       N  
ATOM   4512  NH2 ARG A 547      -7.217  31.535  31.770  1.00 50.31           N  
ANISOU 4512  NH2 ARG A 547     9151   4837   5127    135   -991    -62       N  
ATOM   4513  N   THR A 548     -10.006  29.733  23.420  1.00 35.58           N  
ANISOU 4513  N   THR A 548     5532   4015   3969    184   -390     47       N  
ATOM   4514  CA  THR A 548     -10.817  28.919  22.513  1.00 36.73           C  
ANISOU 4514  CA  THR A 548     5533   4268   4155    190   -294     40       C  
ATOM   4515  C   THR A 548      -9.989  27.744  21.994  1.00 35.80           C  
ANISOU 4515  C   THR A 548     5340   4218   4046    153   -330     54       C  
ATOM   4516  O   THR A 548     -10.456  26.603  21.981  1.00 37.09           O  
ANISOU 4516  O   THR A 548     5477   4419   4194    154   -258     28       O  
ATOM   4517  CB  THR A 548     -11.375  29.743  21.328  1.00 35.40           C  
ANISOU 4517  CB  THR A 548     5232   4160   4059    199   -292     68       C  
ATOM   4518  OG1 THR A 548     -12.237  30.767  21.828  1.00 37.12           O  
ANISOU 4518  OG1 THR A 548     5505   4306   4292    238   -243     55       O  
ATOM   4519  CG2 THR A 548     -12.168  28.861  20.388  1.00 34.06           C  
ANISOU 4519  CG2 THR A 548     4937   4079   3927    196   -232     64       C  
ATOM   4520  N   GLU A 549      -8.758  28.034  21.591  1.00 35.71           N  
ANISOU 4520  N   GLU A 549     5289   4207   4071    123   -431     98       N  
ATOM   4521  CA  GLU A 549      -7.822  27.004  21.160  1.00 37.46           C  
ANISOU 4521  CA  GLU A 549     5442   4467   4325     92   -454    118       C  
ATOM   4522  C   GLU A 549      -7.589  25.924  22.218  1.00 36.61           C  
ANISOU 4522  C   GLU A 549     5426   4310   4174     84   -461     89       C  
ATOM   4523  O   GLU A 549      -7.659  24.739  21.900  1.00 36.88           O  
ANISOU 4523  O   GLU A 549     5406   4400   4208     77   -406     75       O  
ATOM   4524  CB  GLU A 549      -6.487  27.617  20.714  1.00 39.71           C  
ANISOU 4524  CB  GLU A 549     5668   4724   4695     65   -550    180       C  
ATOM   4525  CG  GLU A 549      -5.510  26.578  20.151  1.00 42.70           C  
ANISOU 4525  CG  GLU A 549     5954   5130   5141     38   -543    209       C  
ATOM   4526  CD  GLU A 549      -4.141  27.139  19.811  1.00 45.52           C  
ANISOU 4526  CD  GLU A 549     6238   5431   5625     13   -619    280       C  
ATOM   4527  OE1 GLU A 549      -3.990  28.381  19.728  1.00 47.85           O  
ANISOU 4527  OE1 GLU A 549     6538   5691   5953     13   -674    311       O  
ATOM   4528  OE2 GLU A 549      -3.213  26.320  19.617  1.00 44.59           O  
ANISOU 4528  OE2 GLU A 549     6051   5296   5595     -7   -617    309       O  
ATOM   4529  N   VAL A 550      -7.316  26.323  23.464  1.00 35.48           N  
ANISOU 4529  N   VAL A 550     5441   4053   3985     85   -535     80       N  
ATOM   4530  CA  VAL A 550      -7.089  25.341  24.534  1.00 34.53           C  
ANISOU 4530  CA  VAL A 550     5446   3866   3806     75   -558     56       C  
ATOM   4531  C   VAL A 550      -8.315  24.453  24.755  1.00 34.21           C  
ANISOU 4531  C   VAL A 550     5434   3867   3698    101   -405      5       C  
ATOM   4532  O   VAL A 550      -8.174  23.249  24.984  1.00 34.76           O  
ANISOU 4532  O   VAL A 550     5507   3946   3753     88   -386     -7       O  
ATOM   4533  CB  VAL A 550      -6.626  25.978  25.872  1.00 35.17           C  
ANISOU 4533  CB  VAL A 550     5746   3794   3825     68   -682     55       C  
ATOM   4534  CG1 VAL A 550      -6.642  24.932  27.002  1.00 30.33           C  
ANISOU 4534  CG1 VAL A 550     5302   3104   3117     61   -687     26       C  
ATOM   4535  CG2 VAL A 550      -5.219  26.589  25.737  1.00 32.82           C  
ANISOU 4535  CG2 VAL A 550     5403   3433   3634     31   -869    117       C  
ATOM   4536  N   ALA A 551      -9.505  25.048  24.674  1.00 33.38           N  
ANISOU 4536  N   ALA A 551     5333   3775   3575    136   -296    -19       N  
ATOM   4537  CA  ALA A 551     -10.762  24.306  24.810  1.00 34.35           C  
ANISOU 4537  CA  ALA A 551     5449   3922   3679    162   -141    -57       C  
ATOM   4538  C   ALA A 551     -10.889  23.238  23.719  1.00 33.73           C  
ANISOU 4538  C   ALA A 551     5194   3961   3659    146   -109    -54       C  
ATOM   4539  O   ALA A 551     -11.248  22.082  23.998  1.00 34.72           O  
ANISOU 4539  O   ALA A 551     5328   4096   3768    144    -42    -77       O  
ATOM   4540  CB  ALA A 551     -11.972  25.270  24.785  1.00 32.52           C  
ANISOU 4540  CB  ALA A 551     5214   3669   3473    204    -38    -70       C  
ATOM   4541  N   GLY A 552     -10.580  23.630  22.485  1.00 30.66           N  
ANISOU 4541  N   GLY A 552     4667   3651   3332    133   -157    -23       N  
ATOM   4542  CA  GLY A 552     -10.585  22.708  21.351  1.00 30.69           C  
ANISOU 4542  CA  GLY A 552     4540   3751   3372    114   -138    -19       C  
ATOM   4543  C   GLY A 552      -9.530  21.621  21.500  1.00 30.69           C  
ANISOU 4543  C   GLY A 552     4543   3752   3366     87   -173    -14       C  
ATOM   4544  O   GLY A 552      -9.778  20.454  21.174  1.00 29.83           O  
ANISOU 4544  O   GLY A 552     4388   3688   3257     79   -123    -33       O  
ATOM   4545  N   MET A 553      -8.358  22.010  21.995  1.00 27.48           N  
ANISOU 4545  N   MET A 553     4187   3283   2970     72   -269     14       N  
ATOM   4546  CA  MET A 553      -7.288  21.059  22.304  1.00 30.82           C  
ANISOU 4546  CA  MET A 553     4614   3678   3420     46   -322     28       C  
ATOM   4547  C   MET A 553      -7.739  20.016  23.322  1.00 30.31           C  
ANISOU 4547  C   MET A 553     4650   3577   3290     50   -284    -11       C  
ATOM   4548  O   MET A 553      -7.514  18.828  23.119  1.00 32.57           O  
ANISOU 4548  O   MET A 553     4888   3893   3594     37   -259    -18       O  
ATOM   4549  CB  MET A 553      -6.012  21.770  22.796  1.00 31.67           C  
ANISOU 4549  CB  MET A 553     4758   3691   3583     26   -461     74       C  
ATOM   4550  CG  MET A 553      -4.864  20.811  23.199  1.00 36.29           C  
ANISOU 4550  CG  MET A 553     5335   4220   4236     -2   -540     99       C  
ATOM   4551  SD  MET A 553      -4.220  19.839  21.811  1.00 49.80           S  
ANISOU 4551  SD  MET A 553     6855   6012   6056    -13   -461    124       S  
ATOM   4552  CE  MET A 553      -2.711  20.724  21.408  1.00 44.39           C  
ANISOU 4552  CE  MET A 553     6071   5252   5544    -34   -558    208       C  
ATOM   4553  N   THR A 554      -8.375  20.444  24.409  1.00 29.77           N  
ANISOU 4553  N   THR A 554     4733   3434   3143     68   -267    -36       N  
ATOM   4554  CA  THR A 554      -8.836  19.471  25.404  1.00 32.10           C  
ANISOU 4554  CA  THR A 554     5149   3680   3366     73   -210    -69       C  
ATOM   4555  C   THR A 554      -9.802  18.478  24.760  1.00 31.16           C  
ANISOU 4555  C   THR A 554     4918   3651   3269     82    -79    -95       C  
ATOM   4556  O   THR A 554      -9.601  17.262  24.847  1.00 32.59           O  
ANISOU 4556  O   THR A 554     5087   3846   3451     67    -67   -104       O  
ATOM   4557  CB  THR A 554      -9.514  20.134  26.602  1.00 31.81           C  
ANISOU 4557  CB  THR A 554     5316   3537   3231     99   -165    -92       C  
ATOM   4558  OG1 THR A 554      -8.569  20.948  27.305  1.00 33.93           O  
ANISOU 4558  OG1 THR A 554     5727   3701   3465     84   -314    -70       O  
ATOM   4559  CG2 THR A 554     -10.060  19.091  27.535  1.00 33.19           C  
ANISOU 4559  CG2 THR A 554     5622   3660   3330    106    -72   -122       C  
ATOM   4560  N   ALA A 555     -10.819  19.011  24.089  1.00 30.30           N  
ANISOU 4560  N   ALA A 555     4724   3594   3193    104     -1   -104       N  
ATOM   4561  CA  ALA A 555     -11.864  18.192  23.485  1.00 32.50           C  
ANISOU 4561  CA  ALA A 555     4898   3936   3514    110     99   -125       C  
ATOM   4562  C   ALA A 555     -11.348  17.246  22.400  1.00 32.50           C  
ANISOU 4562  C   ALA A 555     4777   4021   3549     83     65   -119       C  
ATOM   4563  O   ALA A 555     -11.799  16.105  22.310  1.00 36.06           O  
ANISOU 4563  O   ALA A 555     5195   4495   4010     77    119   -140       O  
ATOM   4564  CB  ALA A 555     -12.997  19.068  22.947  1.00 31.50           C  
ANISOU 4564  CB  ALA A 555     4697   3826   3444    135    153   -124       C  
ATOM   4565  N   GLN A 556     -10.396  17.707  21.595  1.00 31.32           N  
ANISOU 4565  N   GLN A 556     4572   3906   3421     67    -12    -90       N  
ATOM   4566  CA  GLN A 556      -9.909  16.902  20.477  1.00 29.57           C  
ANISOU 4566  CA  GLN A 556     4258   3750   3228     47    -16    -84       C  
ATOM   4567  C   GLN A 556      -8.833  15.901  20.882  1.00 31.66           C  
ANISOU 4567  C   GLN A 556     4539   3987   3503     28    -40    -79       C  
ATOM   4568  O   GLN A 556      -8.893  14.746  20.480  1.00 33.17           O  
ANISOU 4568  O   GLN A 556     4690   4211   3700     19      0    -97       O  
ATOM   4569  CB  GLN A 556      -9.462  17.780  19.293  1.00 27.14           C  
ANISOU 4569  CB  GLN A 556     3888   3480   2943     41    -50    -51       C  
ATOM   4570  CG  GLN A 556      -8.097  18.469  19.434  1.00 25.73           C  
ANISOU 4570  CG  GLN A 556     3716   3259   2802     32   -116     -7       C  
ATOM   4571  CD  GLN A 556      -6.916  17.564  19.074  1.00 26.72           C  
ANISOU 4571  CD  GLN A 556     3795   3379   2980     13   -112     13       C  
ATOM   4572  OE1 GLN A 556      -7.078  16.515  18.446  1.00 28.58           O  
ANISOU 4572  OE1 GLN A 556     3998   3655   3206      7    -52     -8       O  
ATOM   4573  NE2 GLN A 556      -5.729  17.966  19.485  1.00 24.90           N  
ANISOU 4573  NE2 GLN A 556     3557   3081   2821      3   -180     55       N  
ATOM   4574  N   ILE A 557      -7.854  16.328  21.682  1.00 33.93           N  
ANISOU 4574  N   ILE A 557     4885   4203   3804     22   -120    -52       N  
ATOM   4575  CA  ILE A 557      -6.740  15.436  22.003  1.00 33.13           C  
ANISOU 4575  CA  ILE A 557     4779   4059   3750      2   -167    -34       C  
ATOM   4576  C   ILE A 557      -7.143  14.274  22.908  1.00 33.76           C  
ANISOU 4576  C   ILE A 557     4934   4111   3783      0   -142    -66       C  
ATOM   4577  O   ILE A 557      -6.609  13.170  22.783  1.00 35.06           O  
ANISOU 4577  O   ILE A 557     5057   4275   3988    -14   -139    -64       O  
ATOM   4578  CB  ILE A 557      -5.482  16.179  22.541  1.00 33.97           C  
ANISOU 4578  CB  ILE A 557     4910   4074   3921    -12   -295     16       C  
ATOM   4579  CG1 ILE A 557      -4.220  15.359  22.200  1.00 28.52           C  
ANISOU 4579  CG1 ILE A 557     4126   3355   3354    -31   -325     53       C  
ATOM   4580  CG2 ILE A 557      -5.618  16.528  24.036  1.00 30.27           C  
ANISOU 4580  CG2 ILE A 557     4616   3506   3381    -11   -377      8       C  
ATOM   4581  CD1 ILE A 557      -2.911  15.986  22.636  1.00 32.64           C  
ANISOU 4581  CD1 ILE A 557     4635   3770   3997    -50   -465    116       C  
ATOM   4582  N   ASN A 558      -8.104  14.515  23.793  1.00 32.19           N  
ANISOU 4582  N   ASN A 558     4847   3881   3505     16   -106    -92       N  
ATOM   4583  CA  ASN A 558      -8.555  13.473  24.710  1.00 31.62           C  
ANISOU 4583  CA  ASN A 558     4867   3768   3380     15    -61   -118       C  
ATOM   4584  C   ASN A 558      -9.538  12.520  24.051  1.00 31.21           C  
ANISOU 4584  C   ASN A 558     4723   3792   3342     20     53   -150       C  
ATOM   4585  O   ASN A 558      -9.709  11.386  24.500  1.00 33.18           O  
ANISOU 4585  O   ASN A 558     5003   4025   3578     13     89   -167       O  
ATOM   4586  CB  ASN A 558      -9.121  14.087  25.984  1.00 30.34           C  
ANISOU 4586  CB  ASN A 558     4890   3514   3126     32    -44   -130       C  
ATOM   4587  CG  ASN A 558      -8.048  14.770  26.804  1.00 32.30           C  
ANISOU 4587  CG  ASN A 558     5270   3657   3347     18   -193    -99       C  
ATOM   4588  OD1 ASN A 558      -7.060  14.141  27.180  1.00 30.31           O  
ANISOU 4588  OD1 ASN A 558     5046   3350   3120     -8   -301    -77       O  
ATOM   4589  ND2 ASN A 558      -8.219  16.067  27.062  1.00 31.19           N  
ANISOU 4589  ND2 ASN A 558     5205   3476   3171     32   -215    -95       N  
ATOM   4590  N   ARG A 559     -10.163  12.968  22.968  1.00 30.21           N  
ANISOU 4590  N   ARG A 559     4490   3739   3248     28     92   -156       N  
ATOM   4591  CA  ARG A 559     -10.962  12.051  22.164  1.00 32.39           C  
ANISOU 4591  CA  ARG A 559     4676   4078   3553     24    157   -181       C  
ATOM   4592  C   ARG A 559     -10.035  11.146  21.355  1.00 31.64           C  
ANISOU 4592  C   ARG A 559     4517   4020   3485      3    130   -177       C  
ATOM   4593  O   ARG A 559     -10.305   9.956  21.210  1.00 32.45           O  
ANISOU 4593  O   ARG A 559     4596   4137   3595     -6    169   -200       O  
ATOM   4594  CB  ARG A 559     -11.979  12.795  21.294  1.00 31.30           C  
ANISOU 4594  CB  ARG A 559     4464   3984   3445     35    180   -183       C  
ATOM   4595  CG  ARG A 559     -13.249  13.116  22.063  1.00 31.34           C  
ANISOU 4595  CG  ARG A 559     4499   3942   3468     59    259   -194       C  
ATOM   4596  CD  ARG A 559     -14.185  14.015  21.284  1.00 31.15           C  
ANISOU 4596  CD  ARG A 559     4391   3938   3505     71    259   -185       C  
ATOM   4597  NE  ARG A 559     -15.395  14.314  22.053  1.00 35.33           N  
ANISOU 4597  NE  ARG A 559     4931   4403   4091     99    358   -189       N  
ATOM   4598  CZ  ARG A 559     -15.473  15.229  23.018  1.00 31.72           C  
ANISOU 4598  CZ  ARG A 559     4571   3876   3604    126    408   -183       C  
ATOM   4599  NH1 ARG A 559     -14.408  15.941  23.350  1.00 25.30           N  
ANISOU 4599  NH1 ARG A 559     3853   3052   2707    124    338   -174       N  
ATOM   4600  NH2 ARG A 559     -16.623  15.432  23.653  1.00 31.70           N  
ANISOU 4600  NH2 ARG A 559     4575   3801   3668    156    534   -185       N  
ATOM   4601  N   LYS A 560      -8.926  11.719  20.884  1.00 31.15           N  
ANISOU 4601  N   LYS A 560     4429   3958   3447     -2     75   -146       N  
ATOM   4602  CA  LYS A 560      -7.836  10.967  20.248  1.00 30.73           C  
ANISOU 4602  CA  LYS A 560     4322   3910   3443    -17     71   -133       C  
ATOM   4603  C   LYS A 560      -7.225   9.957  21.223  1.00 29.08           C  
ANISOU 4603  C   LYS A 560     4149   3642   3258    -26     46   -131       C  
ATOM   4604  O   LYS A 560      -6.980   8.805  20.863  1.00 28.57           O  
ANISOU 4604  O   LYS A 560     4046   3587   3221    -34     82   -144       O  
ATOM   4605  CB  LYS A 560      -6.767  11.934  19.708  1.00 29.38           C  
ANISOU 4605  CB  LYS A 560     4112   3725   3325    -17     33    -87       C  
ATOM   4606  CG  LYS A 560      -5.414  11.313  19.363  1.00 33.40           C  
ANISOU 4606  CG  LYS A 560     4562   4197   3931    -27     38    -56       C  
ATOM   4607  CD  LYS A 560      -4.393  12.390  18.952  1.00 34.90           C  
ANISOU 4607  CD  LYS A 560     4704   4353   4204    -27      9      0       C  
ATOM   4608  CE  LYS A 560      -2.960  11.866  19.067  1.00 43.33           C  
ANISOU 4608  CE  LYS A 560     5701   5339   5425    -36     -7     47       C  
ATOM   4609  NZ  LYS A 560      -1.928  12.756  18.429  1.00 43.48           N  
ANISOU 4609  NZ  LYS A 560     5642   5314   5564    -35      3    110       N  
ATOM   4610  N   LEU A 561      -6.990  10.392  22.459  1.00 28.69           N  
ANISOU 4610  N   LEU A 561     4190   3520   3191    -26    -24   -115       N  
ATOM   4611  CA  LEU A 561      -6.472   9.491  23.487  1.00 30.85           C  
ANISOU 4611  CA  LEU A 561     4530   3719   3472    -39    -73   -108       C  
ATOM   4612  C   LEU A 561      -7.400   8.290  23.684  1.00 29.60           C  
ANISOU 4612  C   LEU A 561     4393   3585   3268    -38     12   -149       C  
ATOM   4613  O   LEU A 561      -6.937   7.155  23.752  1.00 29.87           O  
ANISOU 4613  O   LEU A 561     4407   3603   3341    -50      8   -150       O  
ATOM   4614  CB  LEU A 561      -6.260  10.226  24.820  1.00 30.59           C  
ANISOU 4614  CB  LEU A 561     4647   3587   3390    -41   -171    -89       C  
ATOM   4615  CG  LEU A 561      -5.778   9.373  26.002  1.00 35.78           C  
ANISOU 4615  CG  LEU A 561     5420   4142   4030    -58   -249    -78       C  
ATOM   4616  CD1 LEU A 561      -4.453   8.646  25.688  1.00 34.58           C  
ANISOU 4616  CD1 LEU A 561     5164   3956   4020    -78   -331    -39       C  
ATOM   4617  CD2 LEU A 561      -5.635  10.221  27.272  1.00 38.64           C  
ANISOU 4617  CD2 LEU A 561     5979   4389   4311    -63   -357    -61       C  
ATOM   4618  N   LEU A 562      -8.701   8.559  23.765  1.00 26.96           N  
ANISOU 4618  N   LEU A 562     4087   3282   2874    -24     90   -178       N  
ATOM   4619  CA  LEU A 562      -9.703   7.519  23.935  1.00 29.71           C  
ANISOU 4619  CA  LEU A 562     4439   3643   3205    -23    178   -211       C  
ATOM   4620  C   LEU A 562      -9.688   6.477  22.807  1.00 30.18           C  
ANISOU 4620  C   LEU A 562     4385   3768   3315    -35    208   -230       C  
ATOM   4621  O   LEU A 562      -9.699   5.274  23.075  1.00 32.26           O  
ANISOU 4621  O   LEU A 562     4654   4016   3588    -45    231   -243       O  
ATOM   4622  CB  LEU A 562     -11.106   8.137  24.082  1.00 29.66           C  
ANISOU 4622  CB  LEU A 562     4448   3645   3178     -4    263   -227       C  
ATOM   4623  CG  LEU A 562     -12.228   7.146  24.415  1.00 30.37           C  
ANISOU 4623  CG  LEU A 562     4536   3722   3281     -2    365   -250       C  
ATOM   4624  CD1 LEU A 562     -12.010   6.477  25.799  1.00 29.26           C  
ANISOU 4624  CD1 LEU A 562     4545   3492   3081     -5    387   -246       C  
ATOM   4625  CD2 LEU A 562     -13.591   7.832  24.351  1.00 30.86           C  
ANISOU 4625  CD2 LEU A 562     4564   3780   3381     19    452   -255       C  
ATOM   4626  N   ILE A 563      -9.653   6.931  21.555  1.00 29.04           N  
ANISOU 4626  N   ILE A 563     4158   3684   3193    -35    207   -231       N  
ATOM   4627  CA  ILE A 563      -9.705   5.997  20.423  1.00 27.34           C  
ANISOU 4627  CA  ILE A 563     3877   3514   2999    -46    238   -254       C  
ATOM   4628  C   ILE A 563      -8.391   5.237  20.246  1.00 28.70           C  
ANISOU 4628  C   ILE A 563     4029   3662   3215    -53    229   -241       C  
ATOM   4629  O   ILE A 563      -8.390   4.074  19.849  1.00 29.06           O  
ANISOU 4629  O   ILE A 563     4054   3713   3275    -62    265   -265       O  
ATOM   4630  CB  ILE A 563     -10.200   6.657  19.090  1.00 27.96           C  
ANISOU 4630  CB  ILE A 563     3914   3647   3065    -45    239   -260       C  
ATOM   4631  CG1 ILE A 563      -9.313   7.819  18.653  1.00 24.24           C  
ANISOU 4631  CG1 ILE A 563     3437   3179   2594    -38    210   -226       C  
ATOM   4632  CG2 ILE A 563     -11.665   7.125  19.226  1.00 26.44           C  
ANISOU 4632  CG2 ILE A 563     3711   3463   2873    -40    246   -271       C  
ATOM   4633  CD1 ILE A 563      -9.771   8.470  17.366  1.00 27.72           C  
ANISOU 4633  CD1 ILE A 563     3866   3662   3007    -40    207   -228       C  
ATOM   4634  N   ASN A 564      -7.280   5.895  20.564  1.00 27.33           N  
ANISOU 4634  N   ASN A 564     3855   3447   3081    -50    178   -201       N  
ATOM   4635  CA  ASN A 564      -5.987   5.234  20.572  1.00 29.00           C  
ANISOU 4635  CA  ASN A 564     4029   3607   3381    -56    163   -175       C  
ATOM   4636  C   ASN A 564      -5.869   4.245  21.737  1.00 30.51           C  
ANISOU 4636  C   ASN A 564     4266   3740   3585    -65    125   -176       C  
ATOM   4637  O   ASN A 564      -5.160   3.250  21.631  1.00 29.89           O  
ANISOU 4637  O   ASN A 564     4148   3629   3581    -71    133   -170       O  
ATOM   4638  CB  ASN A 564      -4.856   6.264  20.601  1.00 29.22           C  
ANISOU 4638  CB  ASN A 564     4026   3589   3488    -53    104   -121       C  
ATOM   4639  CG  ASN A 564      -4.609   6.901  19.235  1.00 29.29           C  
ANISOU 4639  CG  ASN A 564     3977   3638   3512    -45    170   -111       C  
ATOM   4640  OD1 ASN A 564      -5.173   6.482  18.231  1.00 29.60           O  
ANISOU 4640  OD1 ASN A 564     4018   3731   3496    -43    251   -146       O  
ATOM   4641  ND2 ASN A 564      -3.748   7.906  19.198  1.00 29.93           N  
ANISOU 4641  ND2 ASN A 564     4024   3680   3669    -42    131    -61       N  
ATOM   4642  N   SER A 565      -6.580   4.518  22.834  1.00 29.40           N  
ANISOU 4642  N   SER A 565     4223   3577   3369    -66     94   -182       N  
ATOM   4643  CA  SER A 565      -6.632   3.597  23.969  1.00 28.48           C  
ANISOU 4643  CA  SER A 565     4189   3397   3234    -76     68   -183       C  
ATOM   4644  C   SER A 565      -7.435   2.328  23.669  1.00 27.95           C  
ANISOU 4644  C   SER A 565     4096   3370   3154    -80    157   -224       C  
ATOM   4645  O   SER A 565      -7.175   1.285  24.266  1.00 28.55           O  
ANISOU 4645  O   SER A 565     4203   3397   3247    -90    143   -222       O  
ATOM   4646  CB  SER A 565      -7.188   4.291  25.209  1.00 29.12           C  
ANISOU 4646  CB  SER A 565     4418   3425   3221    -73     39   -178       C  
ATOM   4647  OG  SER A 565      -6.389   5.409  25.551  1.00 31.56           O  
ANISOU 4647  OG  SER A 565     4767   3682   3542    -74    -66   -140       O  
ATOM   4648  N   LEU A 566      -8.395   2.414  22.747  1.00 26.32           N  
ANISOU 4648  N   LEU A 566     3836   3239   2926    -74    231   -257       N  
ATOM   4649  CA  LEU A 566      -9.139   1.235  22.302  1.00 28.36           C  
ANISOU 4649  CA  LEU A 566     4059   3526   3190    -82    294   -294       C  
ATOM   4650  C   LEU A 566      -8.199   0.244  21.623  1.00 29.31           C  
ANISOU 4650  C   LEU A 566     4126   3641   3369    -89    298   -299       C  
ATOM   4651  O   LEU A 566      -8.189  -0.937  21.973  1.00 28.11           O  
ANISOU 4651  O   LEU A 566     3980   3461   3238    -98    311   -311       O  
ATOM   4652  CB  LEU A 566     -10.295   1.619  21.365  1.00 28.54           C  
ANISOU 4652  CB  LEU A 566     4036   3611   3196    -80    333   -321       C  
ATOM   4653  CG  LEU A 566     -11.166   0.491  20.790  1.00 31.22           C  
ANISOU 4653  CG  LEU A 566     4338   3968   3556    -94    371   -357       C  
ATOM   4654  CD1 LEU A 566     -11.674  -0.484  21.867  1.00 28.96           C  
ANISOU 4654  CD1 LEU A 566     4083   3636   3283   -101    409   -361       C  
ATOM   4655  CD2 LEU A 566     -12.334   1.049  19.999  1.00 28.71           C  
ANISOU 4655  CD2 LEU A 566     3981   3686   3244    -96    368   -370       C  
ATOM   4656  N   ALA A 567      -7.408   0.743  20.666  1.00 28.75           N  
ANISOU 4656  N   ALA A 567     4006   3587   3331    -82    299   -287       N  
ATOM   4657  CA  ALA A 567      -6.360  -0.038  20.005  1.00 29.60           C  
ANISOU 4657  CA  ALA A 567     4064   3667   3514    -81    332   -283       C  
ATOM   4658  C   ALA A 567      -5.393  -0.634  21.029  1.00 30.54           C  
ANISOU 4658  C   ALA A 567     4179   3705   3720    -85    277   -248       C  
ATOM   4659  O   ALA A 567      -5.015  -1.807  20.933  1.00 29.27           O  
ANISOU 4659  O   ALA A 567     3992   3512   3617    -88    305   -257       O  
ATOM   4660  CB  ALA A 567      -5.601   0.833  19.010  1.00 30.71           C  
ANISOU 4660  CB  ALA A 567     4168   3816   3687    -69    360   -261       C  
ATOM   4661  N   GLY A 568      -5.003   0.175  22.014  1.00 28.18           N  
ANISOU 4661  N   GLY A 568     3916   3360   3432    -87    185   -207       N  
ATOM   4662  CA  GLY A 568      -4.152  -0.299  23.106  1.00 29.91           C  
ANISOU 4662  CA  GLY A 568     4159   3479   3725    -98     88   -166       C  
ATOM   4663  C   GLY A 568      -4.819  -1.362  23.968  1.00 31.05           C  
ANISOU 4663  C   GLY A 568     4383   3604   3809   -110     86   -188       C  
ATOM   4664  O   GLY A 568      -4.204  -2.372  24.298  1.00 32.34           O  
ANISOU 4664  O   GLY A 568     4532   3705   4050   -118     55   -174       O  
ATOM   4665  N   ALA A 569      -6.082  -1.135  24.322  1.00 30.60           N  
ANISOU 4665  N   ALA A 569     4405   3591   3632   -109    129   -219       N  
ATOM   4666  CA  ALA A 569      -6.831  -2.040  25.187  1.00 31.82           C  
ANISOU 4666  CA  ALA A 569     4644   3718   3730   -119    153   -235       C  
ATOM   4667  C   ALA A 569      -6.890  -3.451  24.612  1.00 34.00           C  
ANISOU 4667  C   ALA A 569     4849   4010   4058   -125    211   -263       C  
ATOM   4668  O   ALA A 569      -6.886  -4.431  25.359  1.00 37.92           O  
ANISOU 4668  O   ALA A 569     5396   4452   4558   -137    197   -258       O  
ATOM   4669  CB  ALA A 569      -8.222  -1.505  25.427  1.00 29.34           C  
ANISOU 4669  CB  ALA A 569     4387   3441   3319   -112    229   -259       C  
ATOM   4670  N   LEU A 570      -6.914  -3.546  23.284  1.00 33.82           N  
ANISOU 4670  N   LEU A 570     4729   4053   4070   -118    271   -292       N  
ATOM   4671  CA  LEU A 570      -6.839  -4.829  22.576  1.00 30.88           C  
ANISOU 4671  CA  LEU A 570     4302   3686   3746   -122    325   -322       C  
ATOM   4672  C   LEU A 570      -5.601  -5.633  22.969  1.00 29.64           C  
ANISOU 4672  C   LEU A 570     4119   3445   3696   -124    282   -290       C  
ATOM   4673  O   LEU A 570      -5.579  -6.858  22.820  1.00 26.83           O  
ANISOU 4673  O   LEU A 570     3744   3071   3380   -129    315   -310       O  
ATOM   4674  CB  LEU A 570      -6.878  -4.616  21.053  1.00 30.54           C  
ANISOU 4674  CB  LEU A 570     4201   3700   3702   -113    389   -354       C  
ATOM   4675  CG  LEU A 570      -8.179  -4.077  20.451  1.00 28.93           C  
ANISOU 4675  CG  LEU A 570     4012   3566   3415   -117    414   -387       C  
ATOM   4676  CD1 LEU A 570      -8.022  -3.781  18.967  1.00 29.62           C  
ANISOU 4676  CD1 LEU A 570     4083   3688   3484   -111    452   -410       C  
ATOM   4677  CD2 LEU A 570      -9.338  -5.043  20.672  1.00 32.95           C  
ANISOU 4677  CD2 LEU A 570     4533   4079   3908   -133    434   -419       C  
ATOM   4678  N   GLY A 571      -4.577  -4.932  23.458  1.00 29.54           N  
ANISOU 4678  N   GLY A 571     4102   3374   3749   -121    196   -237       N  
ATOM   4679  CA  GLY A 571      -3.384  -5.574  24.017  1.00 32.82           C  
ANISOU 4679  CA  GLY A 571     4487   3683   4298   -126    116   -191       C  
ATOM   4680  C   GLY A 571      -3.284  -5.590  25.545  1.00 32.87           C  
ANISOU 4680  C   GLY A 571     4613   3603   4273   -146    -20   -150       C  
ATOM   4681  O   GLY A 571      -2.204  -5.805  26.079  1.00 31.49           O  
ANISOU 4681  O   GLY A 571     4422   3322   4222   -155   -137    -96       O  
ATOM   4682  N   ASN A 572      -4.399  -5.348  26.245  1.00 34.55           N  
ANISOU 4682  N   ASN A 572     4955   3844   4330   -153     -6   -172       N  
ATOM   4683  CA  ASN A 572      -4.459  -5.489  27.714  1.00 32.25           C  
ANISOU 4683  CA  ASN A 572     4831   3457   3966   -171   -105   -140       C  
ATOM   4684  C   ASN A 572      -5.393  -6.611  28.165  1.00 31.54           C  
ANISOU 4684  C   ASN A 572     4813   3369   3803   -180    -26   -168       C  
ATOM   4685  O   ASN A 572      -6.570  -6.635  27.786  1.00 29.79           O  
ANISOU 4685  O   ASN A 572     4581   3227   3511   -173    102   -212       O  
ATOM   4686  CB  ASN A 572      -4.849  -4.172  28.397  1.00 32.92           C  
ANISOU 4686  CB  ASN A 572     5051   3529   3929   -170   -145   -128       C  
ATOM   4687  CG  ASN A 572      -4.967  -4.317  29.914  1.00 38.52           C  
ANISOU 4687  CG  ASN A 572     5987   4121   4528   -189   -230   -100       C  
ATOM   4688  OD1 ASN A 572      -5.852  -5.012  30.414  1.00 38.71           O  
ANISOU 4688  OD1 ASN A 572     6106   4140   4462   -192   -141   -120       O  
ATOM   4689  ND2 ASN A 572      -4.063  -3.669  30.649  1.00 36.64           N  
ANISOU 4689  ND2 ASN A 572     5849   3774   4299   -203   -408    -49       N  
ATOM   4690  N   VAL A 573      -4.858  -7.521  28.989  1.00 32.53           N  
ANISOU 4690  N   VAL A 573     5007   3392   3960   -198   -114   -136       N  
ATOM   4691  CA  VAL A 573      -5.539  -8.773  29.381  1.00 31.79           C  
ANISOU 4691  CA  VAL A 573     4967   3285   3828   -208    -46   -154       C  
ATOM   4692  C   VAL A 573      -6.889  -8.584  30.083  1.00 33.59           C  
ANISOU 4692  C   VAL A 573     5343   3522   3898   -209     60   -172       C  
ATOM   4693  O   VAL A 573      -7.734  -9.476  30.046  1.00 33.80           O  
ANISOU 4693  O   VAL A 573     5359   3569   3912   -213    169   -198       O  
ATOM   4694  CB  VAL A 573      -4.626  -9.717  30.247  1.00 33.69           C  
ANISOU 4694  CB  VAL A 573     5275   3394   4131   -230   -184   -105       C  
ATOM   4695  CG1 VAL A 573      -3.386 -10.165  29.453  1.00 34.00           C  
ANISOU 4695  CG1 VAL A 573     5126   3412   4378   -224   -245    -87       C  
ATOM   4696  CG2 VAL A 573      -4.221  -9.065  31.576  1.00 26.97           C  
ANISOU 4696  CG2 VAL A 573     4641   2416   3191   -248   -344    -51       C  
ATOM   4697  N   TRP A 574      -7.085  -7.424  30.707  1.00 34.32           N  
ANISOU 4697  N   TRP A 574     5568   3586   3885   -205     37   -157       N  
ATOM   4698  CA  TRP A 574      -8.339  -7.103  31.394  1.00 37.46           C  
ANISOU 4698  CA  TRP A 574     6112   3972   4148   -198    166   -169       C  
ATOM   4699  C   TRP A 574      -9.462  -6.587  30.477  1.00 35.90           C  
ANISOU 4699  C   TRP A 574     5782   3891   3967   -178    319   -212       C  
ATOM   4700  O   TRP A 574     -10.609  -6.474  30.900  1.00 36.15           O  
ANISOU 4700  O   TRP A 574     5884   3910   3941   -170    456   -220       O  
ATOM   4701  CB  TRP A 574      -8.065  -6.129  32.548  1.00 40.30           C  
ANISOU 4701  CB  TRP A 574     6710   4224   4377   -201     81   -133       C  
ATOM   4702  CG  TRP A 574      -7.141  -6.739  33.552  1.00 48.92           C  
ANISOU 4702  CG  TRP A 574     7968   5176   5443   -228    -85    -86       C  
ATOM   4703  CD1 TRP A 574      -5.793  -6.524  33.670  1.00 50.80           C  
ANISOU 4703  CD1 TRP A 574     8202   5344   5757   -245   -306    -44       C  
ATOM   4704  CD2 TRP A 574      -7.484  -7.702  34.557  1.00 49.97           C  
ANISOU 4704  CD2 TRP A 574     8290   5208   5488   -245    -55    -69       C  
ATOM   4705  NE1 TRP A 574      -5.284  -7.280  34.698  1.00 52.46           N  
ANISOU 4705  NE1 TRP A 574     8590   5411   5930   -273   -437     -1       N  
ATOM   4706  CE2 TRP A 574      -6.299  -8.011  35.260  1.00 52.12           C  
ANISOU 4706  CE2 TRP A 574     8682   5351   5772   -273   -283    -17       C  
ATOM   4707  CE3 TRP A 574      -8.683  -8.322  34.942  1.00 53.29           C  
ANISOU 4707  CE3 TRP A 574     8790   5623   5834   -239    142    -85       C  
ATOM   4708  CZ2 TRP A 574      -6.274  -8.922  36.328  1.00 56.87           C  
ANISOU 4708  CZ2 TRP A 574     9501   5820   6286   -297   -329     16       C  
ATOM   4709  CZ3 TRP A 574      -8.661  -9.229  36.010  1.00 55.89           C  
ANISOU 4709  CZ3 TRP A 574     9334   5825   6079   -261    123    -53       C  
ATOM   4710  CH2 TRP A 574      -7.461  -9.521  36.685  1.00 55.76           C  
ANISOU 4710  CH2 TRP A 574     9454   5684   6050   -290   -116     -5       C  
ATOM   4711  N   PHE A 575      -9.136  -6.287  29.221  1.00 35.47           N  
ANISOU 4711  N   PHE A 575     5541   3933   4003   -170    299   -235       N  
ATOM   4712  CA  PHE A 575     -10.149  -5.891  28.239  1.00 32.27           C  
ANISOU 4712  CA  PHE A 575     5010   3627   3623   -156    407   -273       C  
ATOM   4713  C   PHE A 575     -10.956  -7.096  27.783  1.00 32.68           C  
ANISOU 4713  C   PHE A 575     4976   3707   3734   -166    495   -301       C  
ATOM   4714  O   PHE A 575     -10.386  -8.105  27.375  1.00 35.64           O  
ANISOU 4714  O   PHE A 575     5289   4085   4170   -177    458   -311       O  
ATOM   4715  CB  PHE A 575      -9.489  -5.233  27.037  1.00 30.80           C  
ANISOU 4715  CB  PHE A 575     4690   3517   3495   -148    352   -284       C  
ATOM   4716  CG  PHE A 575     -10.442  -4.512  26.132  1.00 27.94           C  
ANISOU 4716  CG  PHE A 575     4240   3238   3136   -136    423   -313       C  
ATOM   4717  CD1 PHE A 575     -11.489  -3.759  26.647  1.00 29.26           C  
ANISOU 4717  CD1 PHE A 575     4465   3395   3256   -125    496   -310       C  
ATOM   4718  CD2 PHE A 575     -10.269  -4.557  24.760  1.00 30.34           C  
ANISOU 4718  CD2 PHE A 575     4417   3615   3494   -135    417   -340       C  
ATOM   4719  CE1 PHE A 575     -12.366  -3.076  25.803  1.00 26.36           C  
ANISOU 4719  CE1 PHE A 575     4004   3092   2921   -116    542   -329       C  
ATOM   4720  CE2 PHE A 575     -11.126  -3.860  23.911  1.00 28.78           C  
ANISOU 4720  CE2 PHE A 575     4158   3480   3297   -129    452   -361       C  
ATOM   4721  CZ  PHE A 575     -12.177  -3.131  24.434  1.00 27.29           C  
ANISOU 4721  CZ  PHE A 575     4001   3282   3085   -121    504   -353       C  
ATOM   4722  N   ARG A 576     -12.280  -6.984  27.856  1.00 31.18           N  
ANISOU 4722  N   ARG A 576     4652   3723   3470   -477    111    123       N  
ATOM   4723  CA  ARG A 576     -13.198  -8.041  27.418  1.00 30.03           C  
ANISOU 4723  CA  ARG A 576     4480   3558   3373   -462     89    139       C  
ATOM   4724  C   ARG A 576     -12.844  -8.547  26.006  1.00 30.72           C  
ANISOU 4724  C   ARG A 576     4523   3630   3520   -383     31    134       C  
ATOM   4725  O   ARG A 576     -12.939  -9.750  25.709  1.00 30.44           O  
ANISOU 4725  O   ARG A 576     4476   3574   3517   -371    -28    156       O  
ATOM   4726  CB  ARG A 576     -14.640  -7.512  27.453  1.00 29.41           C  
ANISOU 4726  CB  ARG A 576     4381   3479   3315   -471    174    114       C  
ATOM   4727  CG  ARG A 576     -15.733  -8.568  27.286  1.00 29.93           C  
ANISOU 4727  CG  ARG A 576     4427   3525   3420   -474    161    134       C  
ATOM   4728  CD  ARG A 576     -17.128  -7.959  27.344  1.00 29.57           C  
ANISOU 4728  CD  ARG A 576     4354   3477   3406   -484    249    108       C  
ATOM   4729  NE  ARG A 576     -17.401  -7.307  28.625  1.00 30.90           N  
ANISOU 4729  NE  ARG A 576     4557   3663   3520   -558    326     91       N  
ATOM   4730  CZ  ARG A 576     -17.920  -7.902  29.695  1.00 34.51           C  
ANISOU 4730  CZ  ARG A 576     5047   4127   3938   -635    346    109       C  
ATOM   4731  NH1 ARG A 576     -18.252  -9.189  29.663  1.00 32.41           N  
ANISOU 4731  NH1 ARG A 576     4780   3848   3685   -646    289    149       N  
ATOM   4732  NH2 ARG A 576     -18.110  -7.198  30.809  1.00 33.15           N  
ANISOU 4732  NH2 ARG A 576     4909   3976   3711   -706    426     84       N  
ATOM   4733  N   TYR A 577     -12.401  -7.628  25.155  1.00 29.01           N  
ANISOU 4733  N   TYR A 577     4283   3423   3316   -334     48    104       N  
ATOM   4734  CA  TYR A 577     -12.101  -7.940  23.757  1.00 28.47           C  
ANISOU 4734  CA  TYR A 577     4174   3347   3295   -267      8     91       C  
ATOM   4735  C   TYR A 577     -10.604  -8.021  23.464  1.00 26.92           C  
ANISOU 4735  C   TYR A 577     3981   3157   3091   -244    -44     88       C  
ATOM   4736  O   TYR A 577     -10.177  -7.878  22.317  1.00 27.87           O  
ANISOU 4736  O   TYR A 577     4071   3282   3237   -194    -58     65       O  
ATOM   4737  CB  TYR A 577     -12.814  -6.942  22.837  1.00 28.61           C  
ANISOU 4737  CB  TYR A 577     4160   3370   3341   -231     58     64       C  
ATOM   4738  CG  TYR A 577     -14.274  -6.815  23.175  1.00 28.23           C  
ANISOU 4738  CG  TYR A 577     4102   3310   3313   -253    111     65       C  
ATOM   4739  CD1 TYR A 577     -14.741  -5.752  23.945  1.00 28.01           C  
ANISOU 4739  CD1 TYR A 577     4085   3290   3269   -286    185     50       C  
ATOM   4740  CD2 TYR A 577     -15.189  -7.783  22.756  1.00 30.62           C  
ANISOU 4740  CD2 TYR A 577     4383   3592   3657   -244     88     79       C  
ATOM   4741  CE1 TYR A 577     -16.084  -5.651  24.281  1.00 26.47           C  
ANISOU 4741  CE1 TYR A 577     3873   3080   3102   -308    240     45       C  
ATOM   4742  CE2 TYR A 577     -16.535  -7.686  23.083  1.00 27.64           C  
ANISOU 4742  CE2 TYR A 577     3992   3204   3307   -266    137     80       C  
ATOM   4743  CZ  TYR A 577     -16.972  -6.623  23.844  1.00 25.31           C  
ANISOU 4743  CZ  TYR A 577     3702   2915   2999   -297    215     63       C  
ATOM   4744  OH  TYR A 577     -18.305  -6.526  24.150  1.00 27.55           O  
ANISOU 4744  OH  TYR A 577     3965   3184   3320   -318    269     58       O  
ATOM   4745  N   TYR A 578      -9.819  -8.241  24.514  1.00 27.67           N  
ANISOU 4745  N   TYR A 578     4109   3252   3150   -286    -71    111       N  
ATOM   4746  CA  TYR A 578      -8.402  -8.541  24.379  1.00 29.03           C  
ANISOU 4746  CA  TYR A 578     4280   3422   3329   -270   -131    115       C  
ATOM   4747  C   TYR A 578      -8.165  -9.631  23.349  1.00 30.05           C  
ANISOU 4747  C   TYR A 578     4370   3529   3520   -221   -188    106       C  
ATOM   4748  O   TYR A 578      -8.711 -10.731  23.455  1.00 29.05           O  
ANISOU 4748  O   TYR A 578     4239   3377   3421   -229   -223    125       O  
ATOM   4749  CB  TYR A 578      -7.862  -9.035  25.714  1.00 30.67           C  
ANISOU 4749  CB  TYR A 578     4529   3621   3505   -333   -174    156       C  
ATOM   4750  CG  TYR A 578      -6.444  -9.563  25.682  1.00 31.78           C  
ANISOU 4750  CG  TYR A 578     4660   3745   3670   -320   -250    168       C  
ATOM   4751  CD1 TYR A 578      -6.194 -10.931  25.660  1.00 30.52           C  
ANISOU 4751  CD1 TYR A 578     4485   3550   3562   -317   -328    192       C  
ATOM   4752  CD2 TYR A 578      -5.348  -8.691  25.704  1.00 33.16           C  
ANISOU 4752  CD2 TYR A 578     4837   3937   3824   -314   -246    156       C  
ATOM   4753  CE1 TYR A 578      -4.887 -11.429  25.655  1.00 29.48           C  
ANISOU 4753  CE1 TYR A 578     4336   3395   3469   -305   -401    202       C  
ATOM   4754  CE2 TYR A 578      -4.037  -9.174  25.698  1.00 31.18           C  
ANISOU 4754  CE2 TYR A 578     4572   3668   3607   -304   -317    168       C  
ATOM   4755  CZ  TYR A 578      -3.818 -10.544  25.674  1.00 34.13           C  
ANISOU 4755  CZ  TYR A 578     4925   4002   4039   -298   -393    190       C  
ATOM   4756  OH  TYR A 578      -2.534 -11.036  25.682  1.00 36.96           O  
ANISOU 4756  OH  TYR A 578     5261   4335   4447   -287   -464    199       O  
ATOM   4757  N   ASP A 579      -7.327  -9.317  22.371  1.00 31.35           N  
ANISOU 4757  N   ASP A 579     4506   3703   3703   -175   -195     75       N  
ATOM   4758  CA  ASP A 579      -6.888 -10.285  21.389  1.00 32.16           C  
ANISOU 4758  CA  ASP A 579     4570   3786   3862   -131   -243     55       C  
ATOM   4759  C   ASP A 579      -5.620  -9.766  20.716  1.00 32.26           C  
ANISOU 4759  C   ASP A 579     4561   3816   3880   -100   -246     22       C  
ATOM   4760  O   ASP A 579      -5.643  -8.721  20.053  1.00 32.31           O  
ANISOU 4760  O   ASP A 579     4562   3853   3863    -83   -198     -3       O  
ATOM   4761  CB  ASP A 579      -7.996 -10.542  20.362  1.00 30.99           C  
ANISOU 4761  CB  ASP A 579     4400   3637   3738   -103   -223     35       C  
ATOM   4762  CG  ASP A 579      -7.729 -11.762  19.510  1.00 34.44           C  
ANISOU 4762  CG  ASP A 579     4805   4048   4232    -69   -274     14       C  
ATOM   4763  OD1 ASP A 579      -8.714 -12.404  19.080  1.00 34.60           O  
ANISOU 4763  OD1 ASP A 579     4816   4054   4276    -62   -280     15       O  
ATOM   4764  OD2 ASP A 579      -6.537 -12.082  19.271  1.00 35.60           O  
ANISOU 4764  OD2 ASP A 579     4933   4188   4406    -50   -308     -5       O  
ATOM   4765  N   LEU A 580      -4.523 -10.505  20.894  1.00 32.15           N  
ANISOU 4765  N   LEU A 580     4532   3779   3904    -94   -303     25       N  
ATOM   4766  CA  LEU A 580      -3.208 -10.115  20.370  1.00 31.36           C  
ANISOU 4766  CA  LEU A 580     4407   3691   3819    -68   -309     -6       C  
ATOM   4767  C   LEU A 580      -3.096 -10.213  18.844  1.00 31.36           C  
ANISOU 4767  C   LEU A 580     4365   3703   3846    -21   -290    -61       C  
ATOM   4768  O   LEU A 580      -2.288  -9.508  18.229  1.00 27.64           O  
ANISOU 4768  O   LEU A 580     3878   3259   3366     -4   -267    -92       O  
ATOM   4769  CB  LEU A 580      -2.102 -10.923  21.048  1.00 32.80           C  
ANISOU 4769  CB  LEU A 580     4578   3838   4047    -78   -380     15       C  
ATOM   4770  CG  LEU A 580      -1.164 -10.309  22.103  1.00 35.58           C  
ANISOU 4770  CG  LEU A 580     4953   4193   4371   -114   -398     47       C  
ATOM   4771  CD1 LEU A 580      -1.521  -8.895  22.591  1.00 29.19           C  
ANISOU 4771  CD1 LEU A 580     4187   3425   3478   -144   -336     57       C  
ATOM   4772  CD2 LEU A 580      -1.005 -11.249  23.274  1.00 36.85           C  
ANISOU 4772  CD2 LEU A 580     5133   4313   4556   -156   -473    102       C  
ATOM   4773  N   ARG A 581      -3.913 -11.075  18.241  1.00 31.17           N  
ANISOU 4773  N   ARG A 581     4328   3662   3852     -5   -300    -74       N  
ATOM   4774  CA  ARG A 581      -4.040 -11.135  16.782  1.00 30.07           C  
ANISOU 4774  CA  ARG A 581     4161   3540   3726     28   -278   -126       C  
ATOM   4775  C   ARG A 581      -4.532  -9.784  16.240  1.00 29.89           C  
ANISOU 4775  C   ARG A 581     4152   3561   3643     24   -218   -131       C  
ATOM   4776  O   ARG A 581      -4.009  -9.285  15.249  1.00 30.86           O  
ANISOU 4776  O   ARG A 581     4259   3713   3755     39   -195   -169       O  
ATOM   4777  CB  ARG A 581      -5.007 -12.251  16.356  1.00 30.77           C  
ANISOU 4777  CB  ARG A 581     4241   3600   3849     36   -300   -130       C  
ATOM   4778  CG  ARG A 581      -4.679 -13.655  16.877  1.00 29.37           C  
ANISOU 4778  CG  ARG A 581     4048   3370   3740     38   -365   -120       C  
ATOM   4779  CD  ARG A 581      -5.798 -14.655  16.574  1.00 29.82           C  
ANISOU 4779  CD  ARG A 581     4104   3401   3826     41   -386   -117       C  
ATOM   4780  NE  ARG A 581      -6.999 -14.433  17.393  1.00 33.82           N  
ANISOU 4780  NE  ARG A 581     4645   3908   4295      9   -374    -63       N  
ATOM   4781  CZ  ARG A 581      -8.147 -15.092  17.237  1.00 35.46           C  
ANISOU 4781  CZ  ARG A 581     4857   4099   4519      5   -384    -51       C  
ATOM   4782  NH1 ARG A 581      -8.263 -16.018  16.295  1.00 34.87           N  
ANISOU 4782  NH1 ARG A 581     4755   4002   4490     30   -408    -86       N  
ATOM   4783  NH2 ARG A 581      -9.184 -14.825  18.016  1.00 33.18           N  
ANISOU 4783  NH2 ARG A 581     4595   3813   4199    -27   -365     -6       N  
ATOM   4784  N   ASN A 582      -5.526  -9.196  16.906  1.00 29.33           N  
ANISOU 4784  N   ASN A 582     4111   3494   3539      0   -194    -94       N  
ATOM   4785  CA  ASN A 582      -6.057  -7.882  16.528  1.00 29.85           C  
ANISOU 4785  CA  ASN A 582     4188   3592   3563     -5   -143    -93       C  
ATOM   4786  C   ASN A 582      -5.111  -6.708  16.819  1.00 28.19           C  
ANISOU 4786  C   ASN A 582     3985   3408   3318    -12   -120    -94       C  
ATOM   4787  O   ASN A 582      -4.923  -5.841  15.957  1.00 31.06           O  
ANISOU 4787  O   ASN A 582     4340   3800   3661     -4    -93   -114       O  
ATOM   4788  CB  ASN A 582      -7.446  -7.641  17.153  1.00 31.53           C  
ANISOU 4788  CB  ASN A 582     4420   3793   3766    -26   -120    -60       C  
ATOM   4789  CG  ASN A 582      -8.544  -8.472  16.490  1.00 33.91           C  
ANISOU 4789  CG  ASN A 582     4708   4077   4098    -17   -133    -61       C  
ATOM   4790  OD1 ASN A 582      -8.352  -9.038  15.412  1.00 33.67           O  
ANISOU 4790  OD1 ASN A 582     4658   4049   4087      5   -153    -91       O  
ATOM   4791  ND2 ASN A 582      -9.700  -8.549  17.140  1.00 33.11           N  
ANISOU 4791  ND2 ASN A 582     4619   3959   4001    -36   -120    -32       N  
ATOM   4792  N   ALA A 583      -4.502  -6.686  18.007  1.00 26.02           N  
ANISOU 4792  N   ALA A 583     3729   3123   3034    -32   -133    -72       N  
ATOM   4793  CA  ALA A 583      -3.534  -5.631  18.353  1.00 27.41           C  
ANISOU 4793  CA  ALA A 583     3914   3321   3180    -42   -117    -71       C  
ATOM   4794  C   ALA A 583      -2.352  -5.634  17.374  1.00 30.05           C  
ANISOU 4794  C   ALA A 583     4216   3673   3530    -16   -126   -109       C  
ATOM   4795  O   ALA A 583      -1.973  -4.587  16.833  1.00 31.24           O  
ANISOU 4795  O   ALA A 583     4363   3855   3653    -13    -96   -123       O  
ATOM   4796  CB  ALA A 583      -3.053  -5.770  19.809  1.00 23.36           C  
ANISOU 4796  CB  ALA A 583     3430   2792   2656    -75   -141    -38       C  
ATOM   4797  N   THR A 584      -1.810  -6.826  17.125  1.00 28.90           N  
ANISOU 4797  N   THR A 584     4044   3505   3433      2   -167   -127       N  
ATOM   4798  CA  THR A 584      -0.679  -7.003  16.221  1.00 30.53           C  
ANISOU 4798  CA  THR A 584     4211   3723   3665     25   -172   -172       C  
ATOM   4799  C   THR A 584      -1.060  -6.726  14.772  1.00 30.95           C  
ANISOU 4799  C   THR A 584     4250   3807   3702     39   -138   -211       C  
ATOM   4800  O   THR A 584      -0.251  -6.188  14.011  1.00 32.18           O  
ANISOU 4800  O   THR A 584     4388   3994   3845     44   -116   -243       O  
ATOM   4801  CB  THR A 584      -0.074  -8.415  16.365  1.00 30.29           C  
ANISOU 4801  CB  THR A 584     4150   3651   3707     41   -224   -185       C  
ATOM   4802  OG1 THR A 584       0.232  -8.638  17.747  1.00 33.47           O  
ANISOU 4802  OG1 THR A 584     4572   4025   4121     18   -265   -138       O  
ATOM   4803  CG2 THR A 584       1.213  -8.536  15.582  1.00 35.02           C  
ANISOU 4803  CG2 THR A 584     4704   4259   4342     62   -223   -237       C  
ATOM   4804  N   ALA A 585      -2.288  -7.077  14.394  1.00 28.42           N  
ANISOU 4804  N   ALA A 585     3939   3480   3379     39   -134   -205       N  
ATOM   4805  CA  ALA A 585      -2.783  -6.757  13.056  1.00 28.35           C  
ANISOU 4805  CA  ALA A 585     3924   3500   3347     42   -108   -232       C  
ATOM   4806  C   ALA A 585      -2.731  -5.244  12.801  1.00 28.52           C  
ANISOU 4806  C   ALA A 585     3960   3560   3318     27    -73   -220       C  
ATOM   4807  O   ALA A 585      -2.319  -4.814  11.727  1.00 30.91           O  
ANISOU 4807  O   ALA A 585     4251   3896   3598     23    -55   -249       O  
ATOM   4808  CB  ALA A 585      -4.201  -7.301  12.854  1.00 23.83           C  
ANISOU 4808  CB  ALA A 585     3362   2909   2784     40   -117   -217       C  
ATOM   4809  N   ILE A 586      -3.125  -4.452  13.800  1.00 26.53           N  
ANISOU 4809  N   ILE A 586     3731   3300   3047     13    -62   -179       N  
ATOM   4810  CA  ILE A 586      -3.020  -2.990  13.731  1.00 28.05           C  
ANISOU 4810  CA  ILE A 586     3936   3520   3202     -1    -31   -166       C  
ATOM   4811  C   ILE A 586      -1.574  -2.520  13.598  1.00 29.82           C  
ANISOU 4811  C   ILE A 586     4148   3770   3413      0    -27   -186       C  
ATOM   4812  O   ILE A 586      -1.262  -1.733  12.697  1.00 33.13           O  
ANISOU 4812  O   ILE A 586     4560   4222   3804     -7     -8   -199       O  
ATOM   4813  CB  ILE A 586      -3.641  -2.295  14.982  1.00 29.11           C  
ANISOU 4813  CB  ILE A 586     4097   3636   3326    -17    -16   -127       C  
ATOM   4814  CG1 ILE A 586      -5.138  -2.617  15.105  1.00 28.34           C  
ANISOU 4814  CG1 ILE A 586     4007   3516   3247    -20    -12   -108       C  
ATOM   4815  CG2 ILE A 586      -3.416  -0.793  14.934  1.00 22.36           C  
ANISOU 4815  CG2 ILE A 586     3250   2804   2442    -29     13   -118       C  
ATOM   4816  CD1 ILE A 586      -5.692  -2.319  16.472  1.00 30.20           C  
ANISOU 4816  CD1 ILE A 586     4267   3730   3480    -39      5    -80       C  
ATOM   4817  N   THR A 587      -0.704  -2.984  14.496  1.00 29.68           N  
ANISOU 4817  N   THR A 587     4127   3735   3414      3    -47   -184       N  
ATOM   4818  CA  THR A 587       0.664  -2.445  14.590  1.00 31.32           C  
ANISOU 4818  CA  THR A 587     4323   3962   3616      1    -45   -195       C  
ATOM   4819  C   THR A 587       1.563  -2.902  13.429  1.00 30.45           C  
ANISOU 4819  C   THR A 587     4174   3872   3523     15    -42   -246       C  
ATOM   4820  O   THR A 587       2.414  -2.136  12.943  1.00 28.23           O  
ANISOU 4820  O   THR A 587     3882   3625   3221      9    -23   -262       O  
ATOM   4821  CB  THR A 587       1.346  -2.750  15.962  1.00 31.99           C  
ANISOU 4821  CB  THR A 587     4416   4018   3719     -5    -75   -171       C  
ATOM   4822  OG1 THR A 587       1.605  -4.151  16.088  1.00 33.23           O  
ANISOU 4822  OG1 THR A 587     4551   4143   3931      9   -114   -183       O  
ATOM   4823  CG2 THR A 587       0.469  -2.293  17.135  1.00 34.17           C  
ANISOU 4823  CG2 THR A 587     4735   4279   3970    -29    -69   -128       C  
ATOM   4824  N   THR A 588       1.356  -4.134  12.977  1.00 27.97           N  
ANISOU 4824  N   THR A 588     3840   3540   3248     31    -59   -275       N  
ATOM   4825  CA  THR A 588       2.103  -4.651  11.837  1.00 28.42           C  
ANISOU 4825  CA  THR A 588     3859   3615   3323     41    -48   -335       C  
ATOM   4826  C   THR A 588       1.698  -3.902  10.564  1.00 29.90           C  
ANISOU 4826  C   THR A 588     4055   3850   3455     22    -13   -352       C  
ATOM   4827  O   THR A 588       2.571  -3.473   9.807  1.00 30.90           O  
ANISOU 4827  O   THR A 588     4163   4014   3563     12     12   -386       O  
ATOM   4828  CB  THR A 588       1.930  -6.166  11.694  1.00 29.62           C  
ANISOU 4828  CB  THR A 588     3989   3731   3536     61    -75   -365       C  
ATOM   4829  OG1 THR A 588       2.154  -6.774  12.972  1.00 30.84           O  
ANISOU 4829  OG1 THR A 588     4142   3837   3737     69   -117   -333       O  
ATOM   4830  CG2 THR A 588       2.922  -6.741  10.685  1.00 30.12           C  
ANISOU 4830  CG2 THR A 588     4006   3807   3632     71    -59   -438       C  
ATOM   4831  N   PHE A 589       0.389  -3.722  10.353  1.00 29.38           N  
ANISOU 4831  N   PHE A 589     4017   3783   3365     13    -13   -324       N  
ATOM   4832  CA  PHE A 589      -0.132  -2.911   9.232  1.00 30.12           C  
ANISOU 4832  CA  PHE A 589     4122   3914   3406    -12      7   -323       C  
ATOM   4833  C   PHE A 589       0.556  -1.553   9.220  1.00 30.26           C  
ANISOU 4833  C   PHE A 589     4145   3965   3385    -30     28   -308       C  
ATOM   4834  O   PHE A 589       1.040  -1.102   8.183  1.00 31.82           O  
ANISOU 4834  O   PHE A 589     4336   4206   3548    -52     47   -332       O  
ATOM   4835  CB  PHE A 589      -1.663  -2.724   9.340  1.00 29.01           C  
ANISOU 4835  CB  PHE A 589     4008   3755   3260    -18     -4   -279       C  
ATOM   4836  CG  PHE A 589      -2.326  -2.207   8.068  1.00 26.99           C  
ANISOU 4836  CG  PHE A 589     3762   3530   2965    -47      1   -277       C  
ATOM   4837  CD1 PHE A 589      -2.395  -0.838   7.797  1.00 26.47           C  
ANISOU 4837  CD1 PHE A 589     3708   3488   2863    -71     11   -246       C  
ATOM   4838  CD2 PHE A 589      -2.904  -3.093   7.155  1.00 27.87           C  
ANISOU 4838  CD2 PHE A 589     3871   3641   3077    -53    -10   -302       C  
ATOM   4839  CE1 PHE A 589      -3.015  -0.361   6.625  1.00 24.73           C  
ANISOU 4839  CE1 PHE A 589     3498   3292   2608   -104      4   -234       C  
ATOM   4840  CE2 PHE A 589      -3.519  -2.629   5.976  1.00 27.39           C  
ANISOU 4840  CE2 PHE A 589     3824   3609   2976    -88    -13   -294       C  
ATOM   4841  CZ  PHE A 589      -3.576  -1.261   5.713  1.00 26.03           C  
ANISOU 4841  CZ  PHE A 589     3663   3459   2767   -115     -9   -257       C  
ATOM   4842  N   GLY A 590       0.603  -0.915  10.387  1.00 30.46           N  
ANISOU 4842  N   GLY A 590     4185   3972   3415    -25     23   -268       N  
ATOM   4843  CA  GLY A 590       1.238   0.392  10.546  1.00 30.49           C  
ANISOU 4843  CA  GLY A 590     4196   4001   3389    -41     39   -250       C  
ATOM   4844  C   GLY A 590       2.687   0.400  10.094  1.00 31.52           C  
ANISOU 4844  C   GLY A 590     4298   4162   3516    -44     51   -289       C  
ATOM   4845  O   GLY A 590       3.118   1.327   9.398  1.00 31.06           O  
ANISOU 4845  O   GLY A 590     4240   4143   3419    -67     70   -291       O  
ATOM   4846  N   GLN A 591       3.427  -0.646  10.466  1.00 30.61           N  
ANISOU 4846  N   GLN A 591     4157   4027   3447    -22     40   -320       N  
ATOM   4847  CA  GLN A 591       4.841  -0.767  10.102  1.00 32.00           C  
ANISOU 4847  CA  GLN A 591     4296   4224   3639    -21     53   -363       C  
ATOM   4848  C   GLN A 591       4.987  -0.886   8.600  1.00 32.27           C  
ANISOU 4848  C   GLN A 591     4314   4302   3645    -40     83   -414       C  
ATOM   4849  O   GLN A 591       5.922  -0.332   8.021  1.00 32.10           O  
ANISOU 4849  O   GLN A 591     4275   4320   3602    -59    109   -439       O  
ATOM   4850  CB  GLN A 591       5.504  -1.975  10.779  1.00 32.40           C  
ANISOU 4850  CB  GLN A 591     4315   4233   3764      7     27   -385       C  
ATOM   4851  CG  GLN A 591       5.729  -1.830  12.285  1.00 33.80           C  
ANISOU 4851  CG  GLN A 591     4507   4373   3964     13     -7   -336       C  
ATOM   4852  CD  GLN A 591       6.853  -2.728  12.814  1.00 40.27           C  
ANISOU 4852  CD  GLN A 591     5285   5159   4858     31    -37   -356       C  
ATOM   4853  OE1 GLN A 591       7.418  -3.541  12.077  1.00 39.36           O  
ANISOU 4853  OE1 GLN A 591     5124   5042   4790     46    -29   -413       O  
ATOM   4854  NE2 GLN A 591       7.185  -2.573  14.100  1.00 39.97           N  
ANISOU 4854  NE2 GLN A 591     5261   5092   4835     27    -72   -311       N  
ATOM   4855  N   MET A 592       4.055  -1.618   7.987  1.00 32.23           N  
ANISOU 4855  N   MET A 592     4317   4290   3638    -40     80   -429       N  
ATOM   4856  CA  MET A 592       4.018  -1.816   6.547  1.00 31.74           C  
ANISOU 4856  CA  MET A 592     4248   4269   3541    -67    106   -478       C  
ATOM   4857  C   MET A 592       3.690  -0.513   5.844  1.00 32.91           C  
ANISOU 4857  C   MET A 592     4425   4463   3615   -110    118   -445       C  
ATOM   4858  O   MET A 592       4.354  -0.148   4.879  1.00 34.51           O  
ANISOU 4858  O   MET A 592     4619   4715   3777   -144    147   -478       O  
ATOM   4859  CB  MET A 592       2.979  -2.881   6.158  1.00 31.53           C  
ANISOU 4859  CB  MET A 592     4230   4220   3529    -60     91   -493       C  
ATOM   4860  CG  MET A 592       2.873  -3.104   4.645  1.00 32.04           C  
ANISOU 4860  CG  MET A 592     4297   4329   3549    -97    117   -544       C  
ATOM   4861  SD  MET A 592       1.465  -4.073   4.067  1.00 36.17           S  
ANISOU 4861  SD  MET A 592     4840   4831   4071   -102     94   -549       S  
ATOM   4862  CE  MET A 592       0.088  -3.144   4.741  1.00 39.22           C  
ANISOU 4862  CE  MET A 592     5267   5196   4440   -103     59   -451       C  
ATOM   4863  N   ALA A 593       2.666   0.177   6.339  1.00 32.85           N  
ANISOU 4863  N   ALA A 593     4450   4436   3594   -111     96   -381       N  
ATOM   4864  CA  ALA A 593       2.135   1.370   5.689  1.00 33.81           C  
ANISOU 4864  CA  ALA A 593     4598   4589   3661   -150     95   -341       C  
ATOM   4865  C   ALA A 593       3.169   2.484   5.629  1.00 35.35           C  
ANISOU 4865  C   ALA A 593     4788   4819   3826   -172    112   -334       C  
ATOM   4866  O   ALA A 593       3.295   3.167   4.607  1.00 36.15           O  
ANISOU 4866  O   ALA A 593     4897   4965   3873   -217    122   -332       O  
ATOM   4867  CB  ALA A 593       0.886   1.848   6.409  1.00 30.61           C  
ANISOU 4867  CB  ALA A 593     4216   4143   3270   -140     69   -279       C  
ATOM   4868  N   LEU A 594       3.900   2.654   6.732  1.00 34.51           N  
ANISOU 4868  N   LEU A 594     4669   4691   3752   -144    113   -327       N  
ATOM   4869  CA  LEU A 594       4.942   3.667   6.844  1.00 34.31           C  
ANISOU 4869  CA  LEU A 594     4637   4693   3707   -160    126   -319       C  
ATOM   4870  C   LEU A 594       6.098   3.396   5.875  1.00 34.93           C  
ANISOU 4870  C   LEU A 594     4685   4821   3768   -182    159   -378       C  
ATOM   4871  O   LEU A 594       6.557   4.298   5.170  1.00 33.88           O  
ANISOU 4871  O   LEU A 594     4555   4733   3586   -223    174   -374       O  
ATOM   4872  CB  LEU A 594       5.467   3.727   8.285  1.00 34.23           C  
ANISOU 4872  CB  LEU A 594     4622   4646   3739   -128    115   -301       C  
ATOM   4873  CG  LEU A 594       6.593   4.726   8.556  1.00 36.55           C  
ANISOU 4873  CG  LEU A 594     4907   4961   4020   -141    124   -291       C  
ATOM   4874  CD1 LEU A 594       6.090   6.145   8.333  1.00 38.10           C  
ANISOU 4874  CD1 LEU A 594     5132   5172   4173   -171    121   -243       C  
ATOM   4875  CD2 LEU A 594       7.142   4.557   9.953  1.00 34.98           C  
ANISOU 4875  CD2 LEU A 594     4703   4723   3864   -113    107   -278       C  
ATOM   4876  N   GLN A 595       6.557   2.148   5.850  1.00 34.34           N  
ANISOU 4876  N   GLN A 595     4579   4733   3736   -158    169   -435       N  
ATOM   4877  CA  GLN A 595       7.695   1.765   5.032  1.00 36.50           C  
ANISOU 4877  CA  GLN A 595     4814   5045   4009   -174    208   -505       C  
ATOM   4878  C   GLN A 595       7.324   1.660   3.556  1.00 36.54           C  
ANISOU 4878  C   GLN A 595     4832   5100   3953   -223    233   -539       C  
ATOM   4879  O   GLN A 595       8.139   1.992   2.698  1.00 39.14           O  
ANISOU 4879  O   GLN A 595     5146   5482   4243   -263    271   -577       O  
ATOM   4880  CB  GLN A 595       8.347   0.491   5.573  1.00 35.62           C  
ANISOU 4880  CB  GLN A 595     4658   4894   3982   -130    207   -555       C  
ATOM   4881  CG  GLN A 595       9.203   0.778   6.793  1.00 38.56           C  
ANISOU 4881  CG  GLN A 595     5012   5236   4404   -103    188   -529       C  
ATOM   4882  CD  GLN A 595       9.589  -0.457   7.570  1.00 37.90           C  
ANISOU 4882  CD  GLN A 595     4891   5097   4413    -59    165   -553       C  
ATOM   4883  OE1 GLN A 595      10.701  -0.963   7.429  1.00 38.12           O  
ANISOU 4883  OE1 GLN A 595     4865   5121   4496    -49    181   -606       O  
ATOM   4884  NE2 GLN A 595       8.677  -0.946   8.405  1.00 37.21           N  
ANISOU 4884  NE2 GLN A 595     4829   4961   4347    -34    125   -514       N  
ATOM   4885  N   TRP A 596       6.095   1.221   3.278  1.00 34.24           N  
ANISOU 4885  N   TRP A 596     4568   4792   3649   -225    212   -525       N  
ATOM   4886  CA  TRP A 596       5.518   1.241   1.926  1.00 34.42           C  
ANISOU 4886  CA  TRP A 596     4615   4859   3604   -280    222   -540       C  
ATOM   4887  C   TRP A 596       5.570   2.638   1.309  1.00 35.87           C  
ANISOU 4887  C   TRP A 596     4825   5092   3713   -338    222   -495       C  
ATOM   4888  O   TRP A 596       6.046   2.809   0.183  1.00 35.66           O  
ANISOU 4888  O   TRP A 596     4800   5123   3626   -397    253   -531       O  
ATOM   4889  CB  TRP A 596       4.068   0.733   1.955  1.00 32.14           C  
ANISOU 4889  CB  TRP A 596     4355   4534   3322   -269    185   -509       C  
ATOM   4890  CG  TRP A 596       3.316   0.831   0.658  1.00 31.48           C  
ANISOU 4890  CG  TRP A 596     4304   4489   3170   -330    180   -508       C  
ATOM   4891  CD1 TRP A 596       2.736   1.948   0.135  1.00 33.27           C  
ANISOU 4891  CD1 TRP A 596     4563   4739   3338   -379    156   -446       C  
ATOM   4892  CD2 TRP A 596       3.040  -0.232  -0.271  1.00 34.78           C  
ANISOU 4892  CD2 TRP A 596     4724   4921   3571   -352    194   -568       C  
ATOM   4893  NE1 TRP A 596       2.125   1.658  -1.062  1.00 33.17           N  
ANISOU 4893  NE1 TRP A 596     4576   4757   3270   -435    150   -458       N  
ATOM   4894  CE2 TRP A 596       2.297   0.328  -1.339  1.00 36.02           C  
ANISOU 4894  CE2 TRP A 596     4921   5114   3651   -421    175   -536       C  
ATOM   4895  CE3 TRP A 596       3.357  -1.599  -0.312  1.00 34.83           C  
ANISOU 4895  CE3 TRP A 596     4701   4908   3624   -323    217   -647       C  
ATOM   4896  CZ2 TRP A 596       1.861  -0.434  -2.440  1.00 34.58           C  
ANISOU 4896  CZ2 TRP A 596     4756   4956   3426   -465    181   -580       C  
ATOM   4897  CZ3 TRP A 596       2.926  -2.357  -1.408  1.00 34.26           C  
ANISOU 4897  CZ3 TRP A 596     4644   4858   3516   -362    227   -697       C  
ATOM   4898  CH2 TRP A 596       2.181  -1.770  -2.453  1.00 35.01           C  
ANISOU 4898  CH2 TRP A 596     4785   4994   3523   -435    210   -663       C  
ATOM   4899  N   ILE A 597       5.072   3.630   2.047  1.00 36.15           N  
ANISOU 4899  N   ILE A 597     4881   5101   3753   -327    188   -418       N  
ATOM   4900  CA  ILE A 597       4.983   4.992   1.529  1.00 36.19           C  
ANISOU 4900  CA  ILE A 597     4910   5140   3700   -380    176   -365       C  
ATOM   4901  C   ILE A 597       6.345   5.695   1.466  1.00 39.18           C  
ANISOU 4901  C   ILE A 597     5269   5560   4058   -401    206   -381       C  
ATOM   4902  O   ILE A 597       6.533   6.621   0.670  1.00 39.82           O  
ANISOU 4902  O   ILE A 597     5366   5688   4078   -462    207   -358       O  
ATOM   4903  CB  ILE A 597       3.935   5.835   2.290  1.00 34.45           C  
ANISOU 4903  CB  ILE A 597     4713   4872   3502   -362    130   -283       C  
ATOM   4904  CG1 ILE A 597       3.272   6.837   1.341  1.00 34.03           C  
ANISOU 4904  CG1 ILE A 597     4689   4844   3395   -426    101   -229       C  
ATOM   4905  CG2 ILE A 597       4.535   6.513   3.536  1.00 34.80           C  
ANISOU 4905  CG2 ILE A 597     4747   4890   3586   -325    131   -258       C  
ATOM   4906  CD1 ILE A 597       2.427   6.185   0.266  1.00 32.06           C  
ANISOU 4906  CD1 ILE A 597     4459   4610   3111   -464     87   -239       C  
ATOM   4907  N   GLU A 598       7.281   5.245   2.300  1.00 39.04           N  
ANISOU 4907  N   GLU A 598     5216   5523   4096   -354    227   -416       N  
ATOM   4908  CA  GLU A 598       8.668   5.701   2.240  1.00 39.85           C  
ANISOU 4908  CA  GLU A 598     5289   5661   4191   -370    260   -442       C  
ATOM   4909  C   GLU A 598       9.217   5.312   0.878  1.00 39.29           C  
ANISOU 4909  C   GLU A 598     5205   5654   4069   -425    307   -510       C  
ATOM   4910  O   GLU A 598       9.777   6.147   0.169  1.00 42.45           O  
ANISOU 4910  O   GLU A 598     5610   6109   4410   -483    326   -505       O  
ATOM   4911  CB  GLU A 598       9.503   5.069   3.370  1.00 38.72           C  
ANISOU 4911  CB  GLU A 598     5105   5477   4129   -308    265   -470       C  
ATOM   4912  CG  GLU A 598      10.994   5.419   3.333  1.00 41.31           C  
ANISOU 4912  CG  GLU A 598     5394   5837   4466   -320    299   -502       C  
ATOM   4913  CD  GLU A 598      11.843   4.632   4.332  1.00 42.93           C  
ANISOU 4913  CD  GLU A 598     5552   5997   4761   -264    298   -534       C  
ATOM   4914  OE1 GLU A 598      11.345   3.657   4.939  1.00 44.64           O  
ANISOU 4914  OE1 GLU A 598     5766   6164   5032   -219    276   -541       O  
ATOM   4915  OE2 GLU A 598      13.026   4.996   4.509  1.00 44.48           O  
ANISOU 4915  OE2 GLU A 598     5715   6209   4978   -268    315   -548       O  
ATOM   4916  N   ARG A 599       9.030   4.043   0.519  1.00 39.16           N  
ANISOU 4916  N   ARG A 599     5175   5630   4074   -411    325   -574       N  
ATOM   4917  CA  ARG A 599       9.440   3.517  -0.779  1.00 39.54           C  
ANISOU 4917  CA  ARG A 599     5213   5736   4075   -466    376   -651       C  
ATOM   4918  C   ARG A 599       8.789   4.285  -1.936  1.00 40.04           C  
ANISOU 4918  C   ARG A 599     5326   5853   4033   -551    366   -615       C  
ATOM   4919  O   ARG A 599       9.465   4.634  -2.900  1.00 40.97           O  
ANISOU 4919  O   ARG A 599     5443   6037   4085   -620    407   -648       O  
ATOM   4920  CB  ARG A 599       9.143   2.014  -0.884  1.00 38.08           C  
ANISOU 4920  CB  ARG A 599     5009   5521   3938   -432    389   -721       C  
ATOM   4921  CG  ARG A 599       9.595   1.405  -2.215  1.00 40.63           C  
ANISOU 4921  CG  ARG A 599     5320   5901   4215   -491    451   -816       C  
ATOM   4922  CD  ARG A 599       9.228  -0.058  -2.360  1.00 38.39           C  
ANISOU 4922  CD  ARG A 599     5021   5585   3981   -460    461   -886       C  
ATOM   4923  NE  ARG A 599       7.798  -0.330  -2.194  1.00 38.91           N  
ANISOU 4923  NE  ARG A 599     5131   5613   4041   -446    405   -831       N  
ATOM   4924  CZ  ARG A 599       6.895  -0.323  -3.172  1.00 39.42           C  
ANISOU 4924  CZ  ARG A 599     5243   5708   4028   -504    394   -822       C  
ATOM   4925  NH1 ARG A 599       7.241  -0.038  -4.420  1.00 38.85           N  
ANISOU 4925  NH1 ARG A 599     5187   5710   3866   -590    435   -862       N  
ATOM   4926  NH2 ARG A 599       5.632  -0.608  -2.897  1.00 41.05           N  
ANISOU 4926  NH2 ARG A 599     5479   5872   4246   -482    340   -771       N  
ATOM   4927  N   LYS A 600       7.487   4.558  -1.823  1.00 38.65           N  
ANISOU 4927  N   LYS A 600     5193   5648   3845   -550    310   -544       N  
ATOM   4928  CA  LYS A 600       6.758   5.292  -2.865  1.00 38.16           C  
ANISOU 4928  CA  LYS A 600     5179   5627   3695   -631    283   -496       C  
ATOM   4929  C   LYS A 600       7.205   6.739  -3.001  1.00 37.08           C  
ANISOU 4929  C   LYS A 600     5054   5523   3513   -678    271   -436       C  
ATOM   4930  O   LYS A 600       7.406   7.218  -4.114  1.00 40.34           O  
ANISOU 4930  O   LYS A 600     5489   5999   3840   -765    281   -435       O  
ATOM   4931  CB  LYS A 600       5.236   5.221  -2.647  1.00 37.14           C  
ANISOU 4931  CB  LYS A 600     5083   5447   3583   -613    221   -432       C  
ATOM   4932  CG  LYS A 600       4.622   3.840  -2.867  1.00 36.68           C  
ANISOU 4932  CG  LYS A 600     5024   5367   3545   -592    226   -484       C  
ATOM   4933  CD  LYS A 600       4.595   3.429  -4.336  1.00 36.05           C  
ANISOU 4933  CD  LYS A 600     4967   5349   3380   -676    250   -534       C  
ATOM   4934  CE  LYS A 600       3.695   2.212  -4.547  1.00 37.67           C  
ANISOU 4934  CE  LYS A 600     5182   5526   3606   -659    237   -566       C  
ATOM   4935  NZ  LYS A 600       3.485   1.898  -6.002  1.00 40.19           N  
ANISOU 4935  NZ  LYS A 600     5536   5904   3832   -753    251   -604       N  
ATOM   4936  N   VAL A 601       7.357   7.426  -1.870  1.00 38.29           N  
ANISOU 4936  N   VAL A 601     5194   5633   3720   -625    248   -387       N  
ATOM   4937  CA  VAL A 601       7.767   8.830  -1.857  1.00 38.40           C  
ANISOU 4937  CA  VAL A 601     5218   5667   3704   -662    232   -327       C  
ATOM   4938  C   VAL A 601       9.155   8.977  -2.463  1.00 40.49           C  
ANISOU 4938  C   VAL A 601     5459   6000   3926   -709    289   -381       C  
ATOM   4939  O   VAL A 601       9.374   9.846  -3.305  1.00 42.31           O  
ANISOU 4939  O   VAL A 601     5711   6284   4083   -788    286   -352       O  
ATOM   4940  CB  VAL A 601       7.679   9.459  -0.435  1.00 37.74           C  
ANISOU 4940  CB  VAL A 601     5126   5521   3694   -593    201   -274       C  
ATOM   4941  CG1 VAL A 601       8.470  10.759  -0.342  1.00 35.91           C  
ANISOU 4941  CG1 VAL A 601     4891   5312   3440   -623    198   -235       C  
ATOM   4942  CG2 VAL A 601       6.227   9.726  -0.075  1.00 35.77           C  
ANISOU 4942  CG2 VAL A 601     4904   5215   3470   -574    144   -207       C  
ATOM   4943  N   ASN A 602      10.077   8.111  -2.054  1.00 42.26           N  
ANISOU 4943  N   ASN A 602     5637   6220   4199   -663    339   -458       N  
ATOM   4944  CA  ASN A 602      11.410   8.079  -2.654  1.00 43.13           C  
ANISOU 4944  CA  ASN A 602     5714   6392   4281   -704    404   -525       C  
ATOM   4945  C   ASN A 602      11.356   7.864  -4.154  1.00 45.15           C  
ANISOU 4945  C   ASN A 602     5992   6720   4442   -798    438   -568       C  
ATOM   4946  O   ASN A 602      11.950   8.631  -4.912  1.00 48.55           O  
ANISOU 4946  O   ASN A 602     6431   7216   4800   -877    460   -562       O  
ATOM   4947  CB  ASN A 602      12.305   7.030  -1.983  1.00 41.07           C  
ANISOU 4947  CB  ASN A 602     5393   6103   4109   -635    447   -606       C  
ATOM   4948  CG  ASN A 602      12.909   7.533  -0.677  1.00 41.68           C  
ANISOU 4948  CG  ASN A 602     5444   6135   4258   -574    425   -568       C  
ATOM   4949  OD1 ASN A 602      12.969   8.746  -0.433  1.00 39.39           O  
ANISOU 4949  OD1 ASN A 602     5174   5851   3942   -594    397   -499       O  
ATOM   4950  ND2 ASN A 602      13.360   6.605   0.168  1.00 33.26           N  
ANISOU 4950  ND2 ASN A 602     4334   5021   3283   -503    434   -611       N  
ATOM   4951  N   GLU A 603      10.625   6.835  -4.576  1.00 45.75           N  
ANISOU 4951  N   GLU A 603     6082   6788   4515   -796    442   -609       N  
ATOM   4952  CA  GLU A 603      10.466   6.517  -5.997  1.00 45.59           C  
ANISOU 4952  CA  GLU A 603     6089   6834   4398   -890    473   -654       C  
ATOM   4953  C   GLU A 603       9.924   7.712  -6.782  1.00 45.28           C  
ANISOU 4953  C   GLU A 603     6107   6838   4259   -985    426   -566       C  
ATOM   4954  O   GLU A 603      10.394   7.997  -7.883  1.00 46.97           O  
ANISOU 4954  O   GLU A 603     6338   7129   4379  -1084    461   -592       O  
ATOM   4955  CB  GLU A 603       9.546   5.305  -6.186  1.00 44.27           C  
ANISOU 4955  CB  GLU A 603     5935   6637   4250   -866    465   -693       C  
ATOM   4956  CG  GLU A 603      10.164   3.963  -5.790  1.00 47.69           C  
ANISOU 4956  CG  GLU A 603     6312   7042   4768   -798    521   -799       C  
ATOM   4957  CD  GLU A 603       9.215   2.774  -5.986  1.00 49.50           C  
ANISOU 4957  CD  GLU A 603     6556   7238   5016   -777    508   -834       C  
ATOM   4958  OE1 GLU A 603       8.084   2.970  -6.486  1.00 48.79           O  
ANISOU 4958  OE1 GLU A 603     6520   7152   4868   -819    460   -779       O  
ATOM   4959  OE2 GLU A 603       9.609   1.636  -5.643  1.00 49.24           O  
ANISOU 4959  OE2 GLU A 603     6477   7172   5062   -719    544   -915       O  
ATOM   4960  N   TYR A 604       8.939   8.403  -6.206  1.00 43.84           N  
ANISOU 4960  N   TYR A 604     5952   6603   4103   -957    346   -465       N  
ATOM   4961  CA  TYR A 604       8.337   9.575  -6.835  1.00 43.03           C  
ANISOU 4961  CA  TYR A 604     5898   6523   3929  -1038    285   -369       C  
ATOM   4962  C   TYR A 604       9.330  10.717  -7.022  1.00 43.86           C  
ANISOU 4962  C   TYR A 604     5997   6676   3992  -1091    299   -343       C  
ATOM   4963  O   TYR A 604       9.466  11.246  -8.127  1.00 45.63           O  
ANISOU 4963  O   TYR A 604     6254   6968   4117  -1201    298   -326       O  
ATOM   4964  CB  TYR A 604       7.119  10.067  -6.039  1.00 42.83           C  
ANISOU 4964  CB  TYR A 604     5890   6418   3966   -984    202   -274       C  
ATOM   4965  CG  TYR A 604       6.481  11.314  -6.628  1.00 44.07           C  
ANISOU 4965  CG  TYR A 604     6088   6585   4072  -1062    130   -170       C  
ATOM   4966  CD1 TYR A 604       6.539  12.539  -5.957  1.00 44.37           C  
ANISOU 4966  CD1 TYR A 604     6121   6590   4150  -1043     88    -93       C  
ATOM   4967  CD2 TYR A 604       5.836  11.270  -7.867  1.00 45.64           C  
ANISOU 4967  CD2 TYR A 604     6331   6824   4185  -1161     99   -148       C  
ATOM   4968  CE1 TYR A 604       5.963  13.686  -6.503  1.00 45.40           C  
ANISOU 4968  CE1 TYR A 604     6284   6722   4246  -1115     16      3       C  
ATOM   4969  CE2 TYR A 604       5.259  12.406  -8.419  1.00 47.70           C  
ANISOU 4969  CE2 TYR A 604     6628   7088   4406  -1238     22    -47       C  
ATOM   4970  CZ  TYR A 604       5.326  13.610  -7.736  1.00 47.84           C  
ANISOU 4970  CZ  TYR A 604     6634   7068   4475  -1213    -20     29       C  
ATOM   4971  OH  TYR A 604       4.752  14.730  -8.293  1.00 49.89           O  
ANISOU 4971  OH  TYR A 604     6925   7324   4708  -1289   -102    132       O  
ATOM   4972  N   LEU A 605      10.019  11.096  -5.946  1.00 43.24           N  
ANISOU 4972  N   LEU A 605     5880   6563   3985  -1020    308   -337       N  
ATOM   4973  CA  LEU A 605      10.925  12.245  -5.990  1.00 45.45           C  
ANISOU 4973  CA  LEU A 605     6152   6879   4236  -1062    313   -303       C  
ATOM   4974  C   LEU A 605      12.185  11.985  -6.822  1.00 46.65           C  
ANISOU 4974  C   LEU A 605     6282   7116   4327  -1128    397   -387       C  
ATOM   4975  O   LEU A 605      12.663  12.885  -7.519  1.00 45.50           O  
ANISOU 4975  O   LEU A 605     6153   7030   4106  -1218    399   -356       O  
ATOM   4976  CB  LEU A 605      11.272  12.747  -4.577  1.00 42.83           C  
ANISOU 4976  CB  LEU A 605     5791   6485   3999   -971    295   -270       C  
ATOM   4977  CG  LEU A 605      10.153  13.461  -3.803  1.00 44.77           C  
ANISOU 4977  CG  LEU A 605     6060   6656   4295   -928    215   -176       C  
ATOM   4978  CD1 LEU A 605      10.563  13.723  -2.369  1.00 43.92           C  
ANISOU 4978  CD1 LEU A 605     5922   6489   4275   -838    212   -166       C  
ATOM   4979  CD2 LEU A 605       9.700  14.768  -4.461  1.00 45.24           C  
ANISOU 4979  CD2 LEU A 605     6158   6732   4299  -1010    154    -82       C  
ATOM   4980  N   ASN A 606      12.712  10.761  -6.741  1.00 47.85           N  
ANISOU 4980  N   ASN A 606     6394   7271   4517  -1086    466   -493       N  
ATOM   4981  CA  ASN A 606      13.816  10.326  -7.598  1.00 51.05           C  
ANISOU 4981  CA  ASN A 606     6772   7753   4873  -1148    557   -591       C  
ATOM   4982  C   ASN A 606      13.467  10.510  -9.077  1.00 55.35           C  
ANISOU 4982  C   ASN A 606     7371   8377   5284  -1281    564   -590       C  
ATOM   4983  O   ASN A 606      14.292  10.988  -9.862  1.00 56.49           O  
ANISOU 4983  O   ASN A 606     7515   8599   5350  -1373    611   -613       O  
ATOM   4984  CB  ASN A 606      14.179   8.859  -7.324  1.00 49.37           C  
ANISOU 4984  CB  ASN A 606     6508   7515   4734  -1079    620   -706       C  
ATOM   4985  CG  ASN A 606      15.245   8.704  -6.250  1.00 49.18           C  
ANISOU 4985  CG  ASN A 606     6414   7452   4819   -992    649   -740       C  
ATOM   4986  OD1 ASN A 606      16.407   9.051  -6.467  1.00 49.76           O  
ANISOU 4986  OD1 ASN A 606     6450   7571   4885  -1025    703   -776       O  
ATOM   4987  ND2 ASN A 606      14.859   8.159  -5.090  1.00 41.66           N  
ANISOU 4987  ND2 ASN A 606     5442   6415   3970   -885    612   -727       N  
ATOM   4988  N   GLU A 607      12.241  10.135  -9.442  1.00 57.96           N  
ANISOU 4988  N   GLU A 607     7747   8688   5586  -1295    516   -562       N  
ATOM   4989  CA  GLU A 607      11.735  10.307 -10.806  1.00 61.85           C  
ANISOU 4989  CA  GLU A 607     8301   9248   5950  -1426    504   -546       C  
ATOM   4990  C   GLU A 607      11.623  11.790 -11.162  1.00 61.62           C  
ANISOU 4990  C   GLU A 607     8312   9248   5854  -1510    439   -432       C  
ATOM   4991  O   GLU A 607      12.049  12.206 -12.244  1.00 63.17           O  
ANISOU 4991  O   GLU A 607     8536   9528   5937  -1635    463   -437       O  
ATOM   4992  CB  GLU A 607      10.382   9.598 -10.968  1.00 63.54           C  
ANISOU 4992  CB  GLU A 607     8552   9421   6167  -1412    452   -530       C  
ATOM   4993  CG  GLU A 607       9.515  10.083 -12.136  1.00 70.99           C  
ANISOU 4993  CG  GLU A 607     9570  10409   6994  -1538    393   -461       C  
ATOM   4994  CD  GLU A 607       8.019   9.965 -11.847  1.00 77.33           C  
ANISOU 4994  CD  GLU A 607    10404  11140   7839  -1499    298   -383       C  
ATOM   4995  OE1 GLU A 607       7.330  11.012 -11.831  1.00 79.03           O  
ANISOU 4995  OE1 GLU A 607    10649  11330   8048  -1527    207   -265       O  
ATOM   4996  OE2 GLU A 607       7.532   8.831 -11.625  1.00 78.93           O  
ANISOU 4996  OE2 GLU A 607    10597  11305   8087  -1439    313   -440       O  
ATOM   4997  N   VAL A 608      11.053  12.572 -10.246  1.00 59.94           N  
ANISOU 4997  N   VAL A 608     8101   8963   5713  -1444    357   -331       N  
ATOM   4998  CA  VAL A 608      10.882  14.019 -10.417  1.00 61.28           C  
ANISOU 4998  CA  VAL A 608     8301   9138   5845  -1507    284   -216       C  
ATOM   4999  C   VAL A 608      12.218  14.759 -10.579  1.00 62.40           C  
ANISOU 4999  C   VAL A 608     8419   9340   5949  -1556    332   -229       C  
ATOM   5000  O   VAL A 608      12.311  15.723 -11.350  1.00 62.90           O  
ANISOU 5000  O   VAL A 608     8518   9454   5926  -1666    299   -164       O  
ATOM   5001  CB  VAL A 608      10.044  14.621  -9.249  1.00 60.63           C  
ANISOU 5001  CB  VAL A 608     8213   8954   5869  -1410    199   -124       C  
ATOM   5002  CG1 VAL A 608      10.433  16.063  -8.946  1.00 59.75           C  
ANISOU 5002  CG1 VAL A 608     8100   8836   5766  -1430    155    -38       C  
ATOM   5003  CG2 VAL A 608       8.559  14.523  -9.564  1.00 62.98           C  
ANISOU 5003  CG2 VAL A 608     8553   9212   6165  -1426    118    -60       C  
ATOM   5004  N   CYS A 609      13.243  14.290  -9.865  1.00 61.63           N  
ANISOU 5004  N   CYS A 609     8262   9236   5918  -1479    407   -309       N  
ATOM   5005  CA  CYS A 609      14.568  14.910  -9.898  1.00 62.18           C  
ANISOU 5005  CA  CYS A 609     8300   9357   5971  -1512    458   -328       C  
ATOM   5006  C   CYS A 609      15.525  14.283 -10.928  1.00 62.97           C  
ANISOU 5006  C   CYS A 609     8385   9552   5991  -1597    564   -439       C  
ATOM   5007  O   CYS A 609      16.640  14.764 -11.125  1.00 62.41           O  
ANISOU 5007  O   CYS A 609     8286   9533   5893  -1642    615   -462       O  
ATOM   5008  CB  CYS A 609      15.182  14.902  -8.496  1.00 60.79           C  
ANISOU 5008  CB  CYS A 609     8065   9115   5919  -1386    469   -342       C  
ATOM   5009  SG  CYS A 609      14.276  15.945  -7.314  1.00 59.03           S  
ANISOU 5009  SG  CYS A 609     7860   8793   5775  -1310    356   -213       S  
ATOM   5010  N   GLY A 610      15.074  13.222 -11.587  1.00 64.15           N  
ANISOU 5010  N   GLY A 610     8550   9721   6101  -1622    599   -511       N  
ATOM   5011  CA  GLY A 610      15.883  12.503 -12.573  1.00 66.66           C  
ANISOU 5011  CA  GLY A 610     8854  10126   6349  -1702    708   -632       C  
ATOM   5012  C   GLY A 610      17.080  11.763 -11.993  1.00 67.70           C  
ANISOU 5012  C   GLY A 610     8900  10249   6575  -1622    805   -747       C  
ATOM   5013  O   GLY A 610      18.143  11.718 -12.619  1.00 67.50           O  
ANISOU 5013  O   GLY A 610     8845  10297   6505  -1690    896   -826       O  
ATOM   5014  N   THR A 611      16.907  11.182 -10.803  1.00 66.51           N  
ANISOU 5014  N   THR A 611     8707  10006   6556  -1482    785   -757       N  
ATOM   5015  CA  THR A 611      17.979  10.440 -10.130  1.00 67.05           C  
ANISOU 5015  CA  THR A 611     8690  10050   6735  -1396    860   -855       C  
ATOM   5016  C   THR A 611      17.611   8.970  -9.886  1.00 68.41           C  
ANISOU 5016  C   THR A 611     8835  10172   6984  -1319    887   -944       C  
ATOM   5017  O   THR A 611      16.595   8.488 -10.395  1.00 67.92           O  
ANISOU 5017  O   THR A 611     8823  10109   6873  -1345    862   -942       O  
ATOM   5018  CB  THR A 611      18.383  11.105  -8.794  1.00 65.61           C  
ANISOU 5018  CB  THR A 611     8472   9802   6656  -1300    812   -788       C  
ATOM   5019  OG1 THR A 611      17.220  11.320  -7.988  1.00 63.92           O  
ANISOU 5019  OG1 THR A 611     8295   9509   6481  -1231    713   -693       O  
ATOM   5020  CG2 THR A 611      19.083  12.437  -9.035  1.00 67.68           C  
ANISOU 5020  CG2 THR A 611     8740  10116   6859  -1374    806   -727       C  
ATOM   5021  N   GLU A 612      18.452   8.270  -9.119  1.00 70.05           N  
ANISOU 5021  N   GLU A 612     8964  10337   7314  -1228    933  -1018       N  
ATOM   5022  CA  GLU A 612      18.234   6.861  -8.753  1.00 71.00           C  
ANISOU 5022  CA  GLU A 612     9048  10399   7531  -1144    955  -1102       C  
ATOM   5023  C   GLU A 612      18.916   6.515  -7.419  1.00 69.47           C  
ANISOU 5023  C   GLU A 612     8778  10126   7492  -1022    946  -1112       C  
ATOM   5024  O   GLU A 612      20.116   6.762  -7.239  1.00 68.64           O  
ANISOU 5024  O   GLU A 612     8613  10036   7432  -1020    994  -1148       O  
ATOM   5025  CB  GLU A 612      18.738   5.926  -9.865  1.00 73.57           C  
ANISOU 5025  CB  GLU A 612     9347  10784   7821  -1210   1063  -1244       C  
ATOM   5026  CG  GLU A 612      18.571   4.430  -9.568  1.00 77.84           C  
ANISOU 5026  CG  GLU A 612     9845  11264   8468  -1128   1089  -1340       C  
ATOM   5027  CD  GLU A 612      19.434   3.534 -10.457  1.00 83.30           C  
ANISOU 5027  CD  GLU A 612    10482  12003   9166  -1176   1212  -1500       C  
ATOM   5028  OE1 GLU A 612      20.366   4.045 -11.123  1.00 84.95           O  
ANISOU 5028  OE1 GLU A 612    10670  12287   9319  -1257   1286  -1544       O  
ATOM   5029  OE2 GLU A 612      19.178   2.308 -10.482  1.00 84.33           O  
ANISOU 5029  OE2 GLU A 612    10588  12093   9361  -1132   1236  -1585       O  
ATOM   5030  N   GLY A 613      18.143   5.946  -6.494  1.00 66.63           N  
ANISOU 5030  N   GLY A 613     8424   9681   7212   -927    884  -1079       N  
ATOM   5031  CA  GLY A 613      18.677   5.486  -5.212  1.00 64.53           C  
ANISOU 5031  CA  GLY A 613     8093   9334   7090   -817    866  -1086       C  
ATOM   5032  C   GLY A 613      18.786   6.537  -4.114  1.00 62.12           C  
ANISOU 5032  C   GLY A 613     7796   8992   6814   -775    796   -977       C  
ATOM   5033  O   GLY A 613      19.092   6.201  -2.964  1.00 61.84           O  
ANISOU 5033  O   GLY A 613     7720   8886   6890   -688    767   -967       O  
ATOM   5034  N   GLU A 614      18.545   7.803  -4.462  1.00 59.29           N  
ANISOU 5034  N   GLU A 614     7490   8679   6357   -840    768   -896       N  
ATOM   5035  CA  GLU A 614      18.568   8.902  -3.487  1.00 57.15           C  
ANISOU 5035  CA  GLU A 614     7234   8374   6106   -809    702   -792       C  
ATOM   5036  C   GLU A 614      17.507   8.705  -2.407  1.00 52.99           C  
ANISOU 5036  C   GLU A 614     6737   7763   5632   -727    623   -726       C  
ATOM   5037  O   GLU A 614      16.351   8.396  -2.705  1.00 49.98           O  
ANISOU 5037  O   GLU A 614     6403   7372   5215   -733    595   -708       O  
ATOM   5038  CB  GLU A 614      18.341  10.251  -4.172  1.00 57.66           C  
ANISOU 5038  CB  GLU A 614     7354   8498   6055   -900    680   -716       C  
ATOM   5039  CG  GLU A 614      19.278  10.536  -5.337  1.00 65.30           C  
ANISOU 5039  CG  GLU A 614     8305   9559   6948   -999    756   -772       C  
ATOM   5040  CD  GLU A 614      20.607  11.140  -4.911  1.00 68.38           C  
ANISOU 5040  CD  GLU A 614     8640   9960   7381   -994    782   -775       C  
ATOM   5041  OE1 GLU A 614      20.611  12.021  -4.016  1.00 70.63           O  
ANISOU 5041  OE1 GLU A 614     8936  10207   7696   -959    720   -689       O  
ATOM   5042  OE2 GLU A 614      21.645  10.740  -5.484  1.00 68.74           O  
ANISOU 5042  OE2 GLU A 614     8630  10053   7434  -1029    867   -868       O  
ATOM   5043  N   ALA A 615      17.918   8.873  -1.158  1.00 49.85           N  
ANISOU 5043  N   ALA A 615     6312   7307   5320   -657    590   -693       N  
ATOM   5044  CA  ALA A 615      17.002   8.786  -0.032  1.00 48.60           C  
ANISOU 5044  CA  ALA A 615     6183   7073   5210   -586    520   -630       C  
ATOM   5045  C   ALA A 615      16.483  10.181   0.295  1.00 46.43           C  
ANISOU 5045  C   ALA A 615     5961   6796   4886   -607    464   -526       C  
ATOM   5046  O   ALA A 615      17.191  10.983   0.892  1.00 48.61           O  
ANISOU 5046  O   ALA A 615     6223   7065   5181   -601    452   -491       O  
ATOM   5047  CB  ALA A 615      17.699   8.172   1.179  1.00 48.07           C  
ANISOU 5047  CB  ALA A 615     6064   6943   5259   -507    510   -649       C  
ATOM   5048  N   PHE A 616      15.256  10.471  -0.122  1.00 43.15           N  
ANISOU 5048  N   PHE A 616     5601   6380   4412   -633    430   -479       N  
ATOM   5049  CA  PHE A 616      14.625  11.748   0.183  1.00 39.60           C  
ANISOU 5049  CA  PHE A 616     5198   5916   3933   -649    372   -382       C  
ATOM   5050  C   PHE A 616      14.002  11.729   1.560  1.00 38.20           C  
ANISOU 5050  C   PHE A 616     5032   5659   3825   -572    324   -338       C  
ATOM   5051  O   PHE A 616      13.988  12.752   2.244  1.00 37.84           O  
ANISOU 5051  O   PHE A 616     5001   5588   3788   -565    288   -276       O  
ATOM   5052  CB  PHE A 616      13.545  12.080  -0.839  1.00 41.54           C  
ANISOU 5052  CB  PHE A 616     5493   6189   4099   -713    349   -345       C  
ATOM   5053  CG  PHE A 616      14.074  12.564  -2.152  1.00 41.08           C  
ANISOU 5053  CG  PHE A 616     5443   6215   3951   -812    381   -358       C  
ATOM   5054  CD1 PHE A 616      14.255  13.923  -2.385  1.00 42.00           C  
ANISOU 5054  CD1 PHE A 616     5581   6357   4021   -868    352   -288       C  
ATOM   5055  CD2 PHE A 616      14.378  11.661  -3.168  1.00 43.04           C  
ANISOU 5055  CD2 PHE A 616     5678   6518   4158   -855    440   -441       C  
ATOM   5056  CE1 PHE A 616      14.739  14.382  -3.621  1.00 43.10           C  
ANISOU 5056  CE1 PHE A 616     5731   6578   4068   -971    379   -295       C  
ATOM   5057  CE2 PHE A 616      14.861  12.109  -4.399  1.00 44.74           C  
ANISOU 5057  CE2 PHE A 616     5904   6816   4278   -958    475   -455       C  
ATOM   5058  CZ  PHE A 616      15.039  13.473  -4.624  1.00 39.55           C  
ANISOU 5058  CZ  PHE A 616     5270   6186   3569  -1019    442   -379       C  
ATOM   5059  N   VAL A 617      13.470  10.570   1.953  1.00 36.50           N  
ANISOU 5059  N   VAL A 617     4810   5403   3657   -519    323   -372       N  
ATOM   5060  CA  VAL A 617      12.898  10.397   3.279  1.00 35.87           C  
ANISOU 5060  CA  VAL A 617     4739   5249   3639   -450    283   -338       C  
ATOM   5061  C   VAL A 617      14.044  10.132   4.251  1.00 36.67           C  
ANISOU 5061  C   VAL A 617     4798   5327   3808   -408    292   -361       C  
ATOM   5062  O   VAL A 617      14.762   9.136   4.126  1.00 38.62           O  
ANISOU 5062  O   VAL A 617     5000   5578   4095   -390    324   -427       O  
ATOM   5063  CB  VAL A 617      11.837   9.267   3.325  1.00 34.72           C  
ANISOU 5063  CB  VAL A 617     4605   5069   3517   -416    273   -357       C  
ATOM   5064  CG1 VAL A 617      11.224   9.157   4.724  1.00 31.62           C  
ANISOU 5064  CG1 VAL A 617     4226   4605   3182   -355    234   -319       C  
ATOM   5065  CG2 VAL A 617      10.743   9.529   2.315  1.00 31.55           C  
ANISOU 5065  CG2 VAL A 617     4243   4692   3053   -464    259   -332       C  
ATOM   5066  N   LEU A 618      14.221  11.047   5.200  1.00 32.77           N  
ANISOU 5066  N   LEU A 618     4317   4805   3328   -394    261   -307       N  
ATOM   5067  CA  LEU A 618      15.365  11.007   6.105  1.00 33.34           C  
ANISOU 5067  CA  LEU A 618     4355   4858   3457   -366    260   -316       C  
ATOM   5068  C   LEU A 618      14.999  10.311   7.409  1.00 33.20           C  
ANISOU 5068  C   LEU A 618     4342   4772   3502   -307    227   -306       C  
ATOM   5069  O   LEU A 618      15.846   9.748   8.094  1.00 29.46           O  
ANISOU 5069  O   LEU A 618     3832   4273   3087   -278    223   -327       O  
ATOM   5070  CB  LEU A 618      15.869  12.426   6.384  1.00 33.68           C  
ANISOU 5070  CB  LEU A 618     4411   4912   3475   -394    244   -265       C  
ATOM   5071  CG  LEU A 618      14.944  13.407   7.127  1.00 34.10           C  
ANISOU 5071  CG  LEU A 618     4515   4926   3515   -389    201   -194       C  
ATOM   5072  CD1 LEU A 618      15.378  13.527   8.548  1.00 34.66           C  
ANISOU 5072  CD1 LEU A 618     4586   4948   3635   -353    176   -175       C  
ATOM   5073  CD2 LEU A 618      14.947  14.794   6.481  1.00 38.92           C  
ANISOU 5073  CD2 LEU A 618     5147   5571   4071   -444    194   -150       C  
ATOM   5074  N   TYR A 619      13.718  10.360   7.745  1.00 33.97           N  
ANISOU 5074  N   TYR A 619     4483   4837   3586   -294    202   -271       N  
ATOM   5075  CA  TYR A 619      13.265   9.842   9.009  1.00 32.31           C  
ANISOU 5075  CA  TYR A 619     4287   4566   3423   -249    172   -254       C  
ATOM   5076  C   TYR A 619      11.805   9.501   8.923  1.00 32.99           C  
ANISOU 5076  C   TYR A 619     4408   4631   3497   -238    161   -241       C  
ATOM   5077  O   TYR A 619      11.072  10.034   8.076  1.00 30.60           O  
ANISOU 5077  O   TYR A 619     4126   4351   3148   -267    166   -225       O  
ATOM   5078  CB  TYR A 619      13.483  10.897  10.095  1.00 31.98           C  
ANISOU 5078  CB  TYR A 619     4269   4499   3382   -250    145   -204       C  
ATOM   5079  CG  TYR A 619      13.112  10.458  11.493  1.00 28.88           C  
ANISOU 5079  CG  TYR A 619     3897   4048   3027   -217    115   -184       C  
ATOM   5080  CD1 TYR A 619      12.073  11.085  12.192  1.00 21.98           C  
ANISOU 5080  CD1 TYR A 619     3071   3144   2137   -216     99   -144       C  
ATOM   5081  CD2 TYR A 619      13.804   9.422  12.120  1.00 25.56           C  
ANISOU 5081  CD2 TYR A 619     3448   3604   2662   -191    102   -207       C  
ATOM   5082  CE1 TYR A 619      11.744  10.687  13.482  1.00 25.19           C  
ANISOU 5082  CE1 TYR A 619     3501   3503   2569   -196     77   -129       C  
ATOM   5083  CE2 TYR A 619      13.484   9.027  13.406  1.00 25.21           C  
ANISOU 5083  CE2 TYR A 619     3427   3509   2644   -171     69   -184       C  
ATOM   5084  CZ  TYR A 619      12.461   9.653  14.078  1.00 22.52           C  
ANISOU 5084  CZ  TYR A 619     3137   3144   2273   -177     60   -146       C  
ATOM   5085  OH  TYR A 619      12.168   9.246  15.351  1.00 30.39           O  
ANISOU 5085  OH  TYR A 619     4161   4098   3289   -167     33   -127       O  
ATOM   5086  N   GLY A 620      11.395   8.621   9.830  1.00 33.13           N  
ANISOU 5086  N   GLY A 620     4429   4601   3557   -200    143   -243       N  
ATOM   5087  CA  GLY A 620      10.011   8.235   9.992  1.00 32.37           C  
ANISOU 5087  CA  GLY A 620     4364   4476   3460   -186    131   -228       C  
ATOM   5088  C   GLY A 620       9.808   7.588  11.347  1.00 33.45           C  
ANISOU 5088  C   GLY A 620     4511   4559   3641   -153    106   -216       C  
ATOM   5089  O   GLY A 620      10.669   6.843  11.834  1.00 32.61           O  
ANISOU 5089  O   GLY A 620     4376   4438   3577   -136     96   -236       O  
ATOM   5090  N   ASP A 621       8.662   7.881  11.953  1.00 32.66           N  
ANISOU 5090  N   ASP A 621     4449   4429   3533   -149     95   -182       N  
ATOM   5091  CA  ASP A 621       8.287   7.298  13.221  1.00 33.02           C  
ANISOU 5091  CA  ASP A 621     4511   4427   3607   -128     74   -168       C  
ATOM   5092  C   ASP A 621       6.785   7.007  13.237  1.00 33.25           C  
ANISOU 5092  C   ASP A 621     4566   4434   3635   -121     75   -157       C  
ATOM   5093  O   ASP A 621       5.973   7.927  13.193  1.00 32.82           O  
ANISOU 5093  O   ASP A 621     4534   4375   3561   -133     83   -131       O  
ATOM   5094  CB  ASP A 621       8.680   8.240  14.360  1.00 34.60           C  
ANISOU 5094  CB  ASP A 621     4736   4610   3800   -141     64   -136       C  
ATOM   5095  CG  ASP A 621       8.349   7.677  15.743  1.00 36.07           C  
ANISOU 5095  CG  ASP A 621     4949   4753   4005   -133     42   -120       C  
ATOM   5096  OD1 ASP A 621       7.600   6.678  15.852  1.00 34.96           O  
ANISOU 5096  OD1 ASP A 621     4810   4591   3882   -118     36   -127       O  
ATOM   5097  OD2 ASP A 621       8.840   8.260  16.727  1.00 33.45           O  
ANISOU 5097  OD2 ASP A 621     4636   4407   3665   -148     30    -98       O  
ATOM   5098  N   THR A 622       6.436   5.720  13.294  1.00 32.90           N  
ANISOU 5098  N   THR A 622     4511   4370   3619   -100     66   -176       N  
ATOM   5099  CA  THR A 622       5.039   5.247  13.375  1.00 32.48           C  
ANISOU 5099  CA  THR A 622     4478   4293   3572    -91     64   -166       C  
ATOM   5100  C   THR A 622       4.189   5.522  12.130  1.00 34.87           C  
ANISOU 5100  C   THR A 622     4779   4616   3853   -101     77   -168       C  
ATOM   5101  O   THR A 622       3.804   4.581  11.428  1.00 35.39           O  
ANISOU 5101  O   THR A 622     4833   4687   3928    -93     75   -192       O  
ATOM   5102  CB  THR A 622       4.294   5.796  14.621  1.00 30.48           C  
ANISOU 5102  CB  THR A 622     4261   4005   3316    -97     63   -131       C  
ATOM   5103  OG1 THR A 622       5.085   5.576  15.800  1.00 35.74           O  
ANISOU 5103  OG1 THR A 622     4935   4653   3992    -99     46   -124       O  
ATOM   5104  CG2 THR A 622       2.958   5.106  14.781  1.00 31.09           C  
ANISOU 5104  CG2 THR A 622     4350   4055   3409    -87     62   -126       C  
ATOM   5105  N   ASP A 623       3.913   6.804  11.869  1.00 34.26           N  
ANISOU 5105  N   ASP A 623     4715   4550   3751   -122     84   -142       N  
ATOM   5106  CA  ASP A 623       2.902   7.216  10.903  1.00 35.25           C  
ANISOU 5106  CA  ASP A 623     4847   4684   3864   -137     84   -128       C  
ATOM   5107  C   ASP A 623       3.276   8.495  10.158  1.00 36.69           C  
ANISOU 5107  C   ASP A 623     5028   4896   4014   -169     86   -110       C  
ATOM   5108  O   ASP A 623       2.459   9.055   9.425  1.00 35.26           O  
ANISOU 5108  O   ASP A 623     4853   4718   3826   -189     77    -86       O  
ATOM   5109  CB  ASP A 623       1.574   7.451  11.623  1.00 35.28           C  
ANISOU 5109  CB  ASP A 623     4870   4643   3893   -129     82   -100       C  
ATOM   5110  CG  ASP A 623       1.543   8.760  12.395  1.00 35.41           C  
ANISOU 5110  CG  ASP A 623     4901   4641   3912   -139     89    -73       C  
ATOM   5111  OD1 ASP A 623       0.448   9.339  12.522  1.00 38.86           O  
ANISOU 5111  OD1 ASP A 623     5345   5049   4371   -142     92    -51       O  
ATOM   5112  OD2 ASP A 623       2.595   9.222  12.883  1.00 38.73           O  
ANISOU 5112  OD2 ASP A 623     5325   5073   4319   -144     93    -75       O  
ATOM   5113  N   SER A 624       4.496   8.971  10.374  1.00 35.92           N  
ANISOU 5113  N   SER A 624     4923   4820   3903   -176     93   -116       N  
ATOM   5114  CA  SER A 624       4.933  10.211   9.761  1.00 36.67           C  
ANISOU 5114  CA  SER A 624     5019   4944   3970   -209     93    -95       C  
ATOM   5115  C   SER A 624       6.269  10.015   9.069  1.00 36.32           C  
ANISOU 5115  C   SER A 624     4952   4950   3899   -225    106   -126       C  
ATOM   5116  O   SER A 624       7.120   9.274   9.563  1.00 38.09           O  
ANISOU 5116  O   SER A 624     5158   5173   4141   -205    113   -157       O  
ATOM   5117  CB  SER A 624       5.075  11.289  10.828  1.00 37.23           C  
ANISOU 5117  CB  SER A 624     5106   4987   4052   -209     90    -68       C  
ATOM   5118  OG  SER A 624       6.177  10.980  11.660  1.00 41.50           O  
ANISOU 5118  OG  SER A 624     5641   5529   4597   -196     95    -85       O  
ATOM   5119  N   ILE A 625       6.446  10.683   7.934  1.00 33.01           N  
ANISOU 5119  N   ILE A 625     4531   4572   3441   -266    107   -118       N  
ATOM   5120  CA  ILE A 625       7.724  10.691   7.230  1.00 32.36           C  
ANISOU 5120  CA  ILE A 625     4425   4542   3328   -291    127   -148       C  
ATOM   5121  C   ILE A 625       8.293  12.116   7.151  1.00 31.90           C  
ANISOU 5121  C   ILE A 625     4373   4503   3246   -324    121   -112       C  
ATOM   5122  O   ILE A 625       7.546  13.095   7.146  1.00 31.41           O  
ANISOU 5122  O   ILE A 625     4332   4422   3180   -340     99    -65       O  
ATOM   5123  CB  ILE A 625       7.626  10.061   5.804  1.00 33.00           C  
ANISOU 5123  CB  ILE A 625     4498   4670   3371   -323    141   -180       C  
ATOM   5124  CG1 ILE A 625       6.498  10.697   4.984  1.00 31.37           C  
ANISOU 5124  CG1 ILE A 625     4319   4468   3134   -361    117   -137       C  
ATOM   5125  CG2 ILE A 625       7.440   8.547   5.884  1.00 34.49           C  
ANISOU 5125  CG2 ILE A 625     4672   4844   3590   -288    152   -230       C  
ATOM   5126  CD1 ILE A 625       6.680  10.549   3.481  1.00 29.21           C  
ANISOU 5126  CD1 ILE A 625     4045   4255   2799   -419    128   -157       C  
ATOM   5127  N   TYR A 626       9.617  12.225   7.095  1.00 32.44           N  
ANISOU 5127  N   TYR A 626     4418   4603   3304   -335    139   -135       N  
ATOM   5128  CA  TYR A 626      10.278  13.520   6.971  1.00 31.55           C  
ANISOU 5128  CA  TYR A 626     4307   4512   3167   -370    134   -103       C  
ATOM   5129  C   TYR A 626      11.101  13.554   5.702  1.00 32.73           C  
ANISOU 5129  C   TYR A 626     4437   4729   3269   -419    158   -128       C  
ATOM   5130  O   TYR A 626      11.989  12.721   5.508  1.00 31.85           O  
ANISOU 5130  O   TYR A 626     4293   4644   3165   -412    189   -182       O  
ATOM   5131  CB  TYR A 626      11.138  13.813   8.203  1.00 32.22           C  
ANISOU 5131  CB  TYR A 626     4386   4572   3286   -344    131    -99       C  
ATOM   5132  CG  TYR A 626      10.292  14.038   9.417  1.00 29.76           C  
ANISOU 5132  CG  TYR A 626     4102   4200   3006   -313    110    -71       C  
ATOM   5133  CD1 TYR A 626       9.711  12.964  10.080  1.00 29.25           C  
ANISOU 5133  CD1 TYR A 626     4041   4100   2973   -274    110    -90       C  
ATOM   5134  CD2 TYR A 626      10.037  15.324   9.891  1.00 31.84           C  
ANISOU 5134  CD2 TYR A 626     4388   4439   3271   -326     93    -29       C  
ATOM   5135  CE1 TYR A 626       8.905  13.155  11.184  1.00 26.84           C  
ANISOU 5135  CE1 TYR A 626     3763   3743   2692   -253     98    -68       C  
ATOM   5136  CE2 TYR A 626       9.232  15.525  11.006  1.00 30.03           C  
ANISOU 5136  CE2 TYR A 626     4184   4155   3072   -301     84    -13       C  
ATOM   5137  CZ  TYR A 626       8.669  14.426  11.645  1.00 30.92           C  
ANISOU 5137  CZ  TYR A 626     4301   4239   3208   -267     89    -33       C  
ATOM   5138  OH  TYR A 626       7.859  14.581  12.749  1.00 36.41           O  
ANISOU 5138  OH  TYR A 626     5022   4884   3928   -250     86    -22       O  
ATOM   5139  N   VAL A 627      10.771  14.511   4.833  1.00 33.10           N  
ANISOU 5139  N   VAL A 627     4502   4803   3270   -473    143    -89       N  
ATOM   5140  CA  VAL A 627      11.332  14.587   3.492  1.00 33.98           C  
ANISOU 5140  CA  VAL A 627     4605   4984   3320   -536    165   -107       C  
ATOM   5141  C   VAL A 627      12.266  15.784   3.341  1.00 35.13           C  
ANISOU 5141  C   VAL A 627     4746   5161   3440   -579    163    -78       C  
ATOM   5142  O   VAL A 627      11.906  16.922   3.651  1.00 37.46           O  
ANISOU 5142  O   VAL A 627     5062   5430   3740   -590    126    -18       O  
ATOM   5143  CB  VAL A 627      10.218  14.660   2.412  1.00 36.81           C  
ANISOU 5143  CB  VAL A 627     4992   5359   3635   -582    143    -81       C  
ATOM   5144  CG1 VAL A 627      10.811  14.581   1.005  1.00 37.84           C  
ANISOU 5144  CG1 VAL A 627     5119   5568   3690   -658    171   -108       C  
ATOM   5145  CG2 VAL A 627       9.211  13.536   2.597  1.00 36.62           C  
ANISOU 5145  CG2 VAL A 627     4974   5299   3640   -540    140   -104       C  
ATOM   5146  N   SER A 628      13.473  15.504   2.870  1.00 35.86           N  
ANISOU 5146  N   SER A 628     4807   5307   3512   -603    205   -124       N  
ATOM   5147  CA  SER A 628      14.434  16.530   2.491  1.00 36.94           C  
ANISOU 5147  CA  SER A 628     4936   5487   3614   -655    210   -103       C  
ATOM   5148  C   SER A 628      13.944  17.262   1.251  1.00 36.42           C  
ANISOU 5148  C   SER A 628     4899   5464   3474   -737    191    -62       C  
ATOM   5149  O   SER A 628      13.636  16.640   0.235  1.00 37.56           O  
ANISOU 5149  O   SER A 628     5050   5649   3571   -776    210    -91       O  
ATOM   5150  CB  SER A 628      15.791  15.888   2.210  1.00 37.97           C  
ANISOU 5150  CB  SER A 628     5018   5663   3745   -662    267   -173       C  
ATOM   5151  OG  SER A 628      16.802  16.868   2.076  1.00 41.61           O  
ANISOU 5151  OG  SER A 628     5465   6158   4185   -704    273   -152       O  
ATOM   5152  N   ALA A 629      13.877  18.584   1.344  1.00 36.99           N  
ANISOU 5152  N   ALA A 629     4990   5526   3538   -767    150      7       N  
ATOM   5153  CA  ALA A 629      13.322  19.421   0.279  1.00 38.07           C  
ANISOU 5153  CA  ALA A 629     5158   5691   3616   -847    113     64       C  
ATOM   5154  C   ALA A 629      14.401  20.305  -0.349  1.00 37.74           C  
ANISOU 5154  C   ALA A 629     5109   5710   3522   -921    123     82       C  
ATOM   5155  O   ALA A 629      14.118  21.135  -1.223  1.00 37.03           O  
ANISOU 5155  O   ALA A 629     5043   5647   3378   -999     87    138       O  
ATOM   5156  CB  ALA A 629      12.169  20.269   0.820  1.00 37.41           C  
ANISOU 5156  CB  ALA A 629     5101   5535   3577   -826     47    137       C  
ATOM   5157  N   ASP A 630      15.638  20.103   0.099  1.00 38.27           N  
ANISOU 5157  N   ASP A 630     5139   5797   3606   -899    168     36       N  
ATOM   5158  CA  ASP A 630      16.804  20.789  -0.439  1.00 39.63           C  
ANISOU 5158  CA  ASP A 630     5294   6029   3734   -964    190     40       C  
ATOM   5159  C   ASP A 630      16.783  20.839  -1.964  1.00 42.50           C  
ANISOU 5159  C   ASP A 630     5674   6472   4000  -1068    205     40       C  
ATOM   5160  O   ASP A 630      16.812  21.923  -2.558  1.00 43.43           O  
ANISOU 5160  O   ASP A 630     5815   6616   4070  -1144    169    104       O  
ATOM   5161  CB  ASP A 630      18.082  20.091   0.036  1.00 40.37           C  
ANISOU 5161  CB  ASP A 630     5336   6140   3863   -926    251    -34       C  
ATOM   5162  CG  ASP A 630      18.424  20.402   1.484  1.00 43.89           C  
ANISOU 5162  CG  ASP A 630     5768   6520   4388   -852    228    -17       C  
ATOM   5163  OD1 ASP A 630      17.520  20.791   2.264  1.00 36.15           O  
ANISOU 5163  OD1 ASP A 630     4818   5475   3444   -811    178     29       O  
ATOM   5164  OD2 ASP A 630      19.615  20.259   1.840  1.00 48.86           O  
ANISOU 5164  OD2 ASP A 630     6355   7164   5044   -839    260    -52       O  
ATOM   5165  N   LYS A 631      16.722  19.663  -2.588  1.00 42.02           N  
ANISOU 5165  N   LYS A 631     5606   6448   3912  -1075    255    -32       N  
ATOM   5166  CA  LYS A 631      16.757  19.561  -4.044  1.00 45.49           C  
ANISOU 5166  CA  LYS A 631     6063   6970   4251  -1181    281    -46       C  
ATOM   5167  C   LYS A 631      15.593  20.289  -4.710  1.00 45.52           C  
ANISOU 5167  C   LYS A 631     6124   6968   4205  -1245    205     41       C  
ATOM   5168  O   LYS A 631      15.761  20.862  -5.785  1.00 47.47           O  
ANISOU 5168  O   LYS A 631     6394   7279   4365  -1353    198     72       O  
ATOM   5169  CB  LYS A 631      16.828  18.101  -4.505  1.00 45.21           C  
ANISOU 5169  CB  LYS A 631     6009   6965   4203  -1170    350   -147       C  
ATOM   5170  CG  LYS A 631      18.195  17.458  -4.295  1.00 46.08           C  
ANISOU 5170  CG  LYS A 631     6057   7105   4347  -1144    432   -239       C  
ATOM   5171  CD  LYS A 631      18.121  15.941  -4.447  1.00 51.02           C  
ANISOU 5171  CD  LYS A 631     6657   7730   4997  -1106    490   -338       C  
ATOM   5172  CE  LYS A 631      19.506  15.302  -4.462  1.00 54.86           C  
ANISOU 5172  CE  LYS A 631     7075   8250   5519  -1096    576   -436       C  
ATOM   5173  NZ  LYS A 631      20.264  15.572  -3.204  1.00 56.38           N  
ANISOU 5173  NZ  LYS A 631     7224   8390   5808  -1018    562   -421       N  
ATOM   5174  N   ILE A 632      14.432  20.291  -4.057  1.00 45.10           N  
ANISOU 5174  N   ILE A 632     6089   6836   4211  -1182    148     83       N  
ATOM   5175  CA  ILE A 632      13.242  20.958  -4.602  1.00 45.60           C  
ANISOU 5175  CA  ILE A 632     6197   6878   4251  -1233     68    169       C  
ATOM   5176  C   ILE A 632      13.447  22.467  -4.624  1.00 46.22           C  
ANISOU 5176  C   ILE A 632     6287   6949   4325  -1283     10    258       C  
ATOM   5177  O   ILE A 632      13.218  23.114  -5.650  1.00 47.87           O  
ANISOU 5177  O   ILE A 632     6527   7197   4466  -1385    -33    317       O  
ATOM   5178  CB  ILE A 632      11.948  20.586  -3.824  1.00 44.39           C  
ANISOU 5178  CB  ILE A 632     6051   6636   4177  -1148     26    187       C  
ATOM   5179  CG1 ILE A 632      11.772  19.063  -3.750  1.00 42.57           C  
ANISOU 5179  CG1 ILE A 632     5809   6410   3956  -1097     81    101       C  
ATOM   5180  CG2 ILE A 632      10.715  21.274  -4.433  1.00 42.93           C  
ANISOU 5180  CG2 ILE A 632     5905   6425   3981  -1203    -60    277       C  
ATOM   5181  CD1 ILE A 632      11.804  18.344  -5.097  1.00 47.62           C  
ANISOU 5181  CD1 ILE A 632     6465   7127   4501  -1180    114     58       C  
ATOM   5182  N   ILE A 633      13.894  23.012  -3.493  1.00 45.42           N  
ANISOU 5182  N   ILE A 633     6162   6798   4297  -1215      5    268       N  
ATOM   5183  CA  ILE A 633      14.267  24.417  -3.402  1.00 46.15           C  
ANISOU 5183  CA  ILE A 633     6259   6882   4394  -1255    -42    341       C  
ATOM   5184  C   ILE A 633      15.364  24.766  -4.418  1.00 48.40           C  
ANISOU 5184  C   ILE A 633     6542   7262   4585  -1360    -11    338       C  
ATOM   5185  O   ILE A 633      15.289  25.800  -5.078  1.00 48.98           O  
ANISOU 5185  O   ILE A 633     6639   7353   4617  -1446    -66    414       O  
ATOM   5186  CB  ILE A 633      14.717  24.799  -1.963  1.00 44.43           C  
ANISOU 5186  CB  ILE A 633     6016   6601   4266  -1164    -39    335       C  
ATOM   5187  CG1 ILE A 633      13.523  24.813  -0.994  1.00 42.86           C  
ANISOU 5187  CG1 ILE A 633     5825   6304   4155  -1081    -81    358       C  
ATOM   5188  CG2 ILE A 633      15.462  26.143  -1.944  1.00 43.83           C  
ANISOU 5188  CG2 ILE A 633     5938   6533   4184  -1212    -69    393       C  
ATOM   5189  CD1 ILE A 633      12.442  25.830  -1.329  1.00 43.33           C  
ANISOU 5189  CD1 ILE A 633     5911   6316   4236  -1120   -167    448       C  
ATOM   5190  N   ASP A 634      16.361  23.892  -4.549  1.00 49.13           N  
ANISOU 5190  N   ASP A 634     6605   7414   4649  -1355     77    248       N  
ATOM   5191  CA  ASP A 634      17.510  24.151  -5.415  1.00 51.53           C  
ANISOU 5191  CA  ASP A 634     6897   7810   4871  -1449    123    230       C  
ATOM   5192  C   ASP A 634      17.165  24.163  -6.903  1.00 53.49           C  
ANISOU 5192  C   ASP A 634     7185   8133   5006  -1576    115    250       C  
ATOM   5193  O   ASP A 634      17.789  24.894  -7.674  1.00 55.07           O  
ANISOU 5193  O   ASP A 634     7395   8397   5131  -1679    115    282       O  
ATOM   5194  CB  ASP A 634      18.643  23.154  -5.140  1.00 51.57           C  
ANISOU 5194  CB  ASP A 634     6850   7850   4892  -1406    222    121       C  
ATOM   5195  CG  ASP A 634      19.416  23.470  -3.858  1.00 52.93           C  
ANISOU 5195  CG  ASP A 634     6984   7974   5154  -1321    226    116       C  
ATOM   5196  OD1 ASP A 634      19.143  24.502  -3.207  1.00 51.89           O  
ANISOU 5196  OD1 ASP A 634     6866   7785   5062  -1301    160    191       O  
ATOM   5197  OD2 ASP A 634      20.306  22.674  -3.498  1.00 54.88           O  
ANISOU 5197  OD2 ASP A 634     7183   8234   5435  -1277    295     35       O  
ATOM   5198  N   LYS A 635      16.175  23.360  -7.294  1.00 52.83           N  
ANISOU 5198  N   LYS A 635     7126   8040   4906  -1572    107    233       N  
ATOM   5199  CA  LYS A 635      15.751  23.258  -8.690  1.00 55.15           C  
ANISOU 5199  CA  LYS A 635     7464   8402   5088  -1695     96    250       C  
ATOM   5200  C   LYS A 635      15.233  24.580  -9.255  1.00 54.98           C  
ANISOU 5200  C   LYS A 635     7484   8375   5028  -1789     -5    374       C  
ATOM   5201  O   LYS A 635      15.290  24.804 -10.459  1.00 54.39           O  
ANISOU 5201  O   LYS A 635     7445   8375   4844  -1920    -15    400       O  
ATOM   5202  CB  LYS A 635      14.701  22.154  -8.869  1.00 56.31           C  
ANISOU 5202  CB  LYS A 635     7629   8527   5239  -1662     97    213       C  
ATOM   5203  CG  LYS A 635      15.272  20.825  -9.343  1.00 61.88           C  
ANISOU 5203  CG  LYS A 635     8316   9298   5899  -1669    202     90       C  
ATOM   5204  CD  LYS A 635      14.179  19.770  -9.518  1.00 66.14           C  
ANISOU 5204  CD  LYS A 635     8876   9811   6444  -1639    194     60       C  
ATOM   5205  CE  LYS A 635      14.641  18.623 -10.414  1.00 71.34           C  
ANISOU 5205  CE  LYS A 635     9531  10549   7025  -1692    288    -50       C  
ATOM   5206  NZ  LYS A 635      14.678  18.990 -11.871  1.00 73.15           N  
ANISOU 5206  NZ  LYS A 635     9810  10871   7113  -1855    285    -27       N  
ATOM   5207  N   VAL A 636      14.725  25.448  -8.385  1.00 55.20           N  
ANISOU 5207  N   VAL A 636     7510   8314   5150  -1727    -83    450       N  
ATOM   5208  CA  VAL A 636      14.303  26.778  -8.810  1.00 56.37           C  
ANISOU 5208  CA  VAL A 636     7688   8443   5286  -1808   -185    571       C  
ATOM   5209  C   VAL A 636      15.384  27.803  -8.458  1.00 57.23           C  
ANISOU 5209  C   VAL A 636     7775   8563   5406  -1823   -183    598       C  
ATOM   5210  O   VAL A 636      15.533  28.822  -9.143  1.00 58.07           O  
ANISOU 5210  O   VAL A 636     7905   8698   5462  -1928   -240    680       O  
ATOM   5211  CB  VAL A 636      12.906  27.185  -8.242  1.00 56.24           C  
ANISOU 5211  CB  VAL A 636     7682   8315   5370  -1746   -283    645       C  
ATOM   5212  CG1 VAL A 636      12.095  25.964  -7.820  1.00 54.45           C  
ANISOU 5212  CG1 VAL A 636     7449   8050   5188  -1656   -253    582       C  
ATOM   5213  CG2 VAL A 636      13.028  28.171  -7.108  1.00 55.31           C  
ANISOU 5213  CG2 VAL A 636     7539   8116   5360  -1672   -321    687       C  
ATOM   5214  N   GLY A 637      16.147  27.507  -7.408  1.00 54.83           N  
ANISOU 5214  N   GLY A 637     7428   8238   5167  -1722   -120    531       N  
ATOM   5215  CA  GLY A 637      17.221  28.381  -6.956  1.00 56.56           C  
ANISOU 5215  CA  GLY A 637     7621   8463   5404  -1724   -112    548       C  
ATOM   5216  C   GLY A 637      16.721  29.354  -5.912  1.00 56.33           C  
ANISOU 5216  C   GLY A 637     7589   8329   5483  -1654   -190    617       C  
ATOM   5217  O   GLY A 637      15.660  29.952  -6.080  1.00 56.54           O  
ANISOU 5217  O   GLY A 637     7643   8302   5538  -1673   -278    697       O  
ATOM   5218  N   GLU A 638      17.485  29.510  -4.834  1.00 56.39           N  
ANISOU 5218  N   GLU A 638     7564   8307   5556  -1576   -158    585       N  
ATOM   5219  CA  GLU A 638      17.098  30.390  -3.728  1.00 58.14           C  
ANISOU 5219  CA  GLU A 638     7781   8429   5882  -1505   -219    635       C  
ATOM   5220  C   GLU A 638      16.907  31.841  -4.173  1.00 59.09           C  
ANISOU 5220  C   GLU A 638     7922   8530   6000  -1586   -311    743       C  
ATOM   5221  O   GLU A 638      15.968  32.510  -3.737  1.00 59.29           O  
ANISOU 5221  O   GLU A 638     7957   8467   6104  -1555   -386    801       O  
ATOM   5222  CB  GLU A 638      18.102  30.298  -2.567  1.00 58.01           C  
ANISOU 5222  CB  GLU A 638     7729   8395   5919  -1424   -168    580       C  
ATOM   5223  CG  GLU A 638      17.924  29.051  -1.685  1.00 59.89           C  
ANISOU 5223  CG  GLU A 638     7948   8602   6206  -1315   -111    496       C  
ATOM   5224  CD  GLU A 638      18.881  28.996  -0.495  1.00 63.14           C  
ANISOU 5224  CD  GLU A 638     8327   8990   6674  -1241    -74    453       C  
ATOM   5225  OE1 GLU A 638      18.601  28.248   0.470  1.00 60.86           O  
ANISOU 5225  OE1 GLU A 638     8029   8653   6444  -1149    -52    405       O  
ATOM   5226  OE2 GLU A 638      19.915  29.696  -0.520  1.00 68.01           O  
ANISOU 5226  OE2 GLU A 638     8928   9636   7276  -1280    -70    469       O  
ATOM   5227  N   SER A 639      17.786  32.298  -5.064  1.00 60.60           N  
ANISOU 5227  N   SER A 639     8117   8802   6104  -1692   -304    767       N  
ATOM   5228  CA  SER A 639      17.809  33.678  -5.562  1.00 60.85           C  
ANISOU 5228  CA  SER A 639     8167   8827   6125  -1784   -390    872       C  
ATOM   5229  C   SER A 639      16.509  34.125  -6.222  1.00 60.55           C  
ANISOU 5229  C   SER A 639     8164   8748   6095  -1837   -490    960       C  
ATOM   5230  O   SER A 639      16.297  35.323  -6.433  1.00 60.55           O  
ANISOU 5230  O   SER A 639     8175   8710   6120  -1893   -581   1056       O  
ATOM   5231  CB  SER A 639      18.957  33.855  -6.566  1.00 62.69           C  
ANISOU 5231  CB  SER A 639     8401   9174   6242  -1903   -352    873       C  
ATOM   5232  OG  SER A 639      20.185  33.406  -6.027  1.00 63.72           O  
ANISOU 5232  OG  SER A 639     8493   9345   6373  -1858   -259    791       O  
ATOM   5233  N   LYS A 640      15.653  33.167  -6.562  1.00 59.95           N  
ANISOU 5233  N   LYS A 640     8102   8675   6002  -1823   -478    930       N  
ATOM   5234  CA  LYS A 640      14.379  33.469  -7.216  1.00 60.84           C  
ANISOU 5234  CA  LYS A 640     8244   8746   6124  -1874   -574   1011       C  
ATOM   5235  C   LYS A 640      13.258  33.809  -6.227  1.00 59.42           C  
ANISOU 5235  C   LYS A 640     8051   8436   6088  -1771   -634   1038       C  
ATOM   5236  O   LYS A 640      12.187  34.266  -6.638  1.00 59.64           O  
ANISOU 5236  O   LYS A 640     8093   8409   6156  -1806   -728   1117       O  
ATOM   5237  CB  LYS A 640      13.964  32.325  -8.157  1.00 62.68           C  
ANISOU 5237  CB  LYS A 640     8503   9048   6265  -1922   -539    972       C  
ATOM   5238  CG  LYS A 640      14.211  32.573  -9.657  1.00 67.30           C  
ANISOU 5238  CG  LYS A 640     9127   9729   6715  -2089   -567   1025       C  
ATOM   5239  CD  LYS A 640      15.652  33.012  -9.987  1.00 72.48           C  
ANISOU 5239  CD  LYS A 640     9776  10474   7290  -2164   -516   1013       C  
ATOM   5240  CE  LYS A 640      16.595  31.829 -10.226  1.00 74.28           C  
ANISOU 5240  CE  LYS A 640     9989  10801   7431  -2163   -381    891       C  
ATOM   5241  NZ  LYS A 640      16.395  31.183 -11.561  1.00 74.78           N  
ANISOU 5241  NZ  LYS A 640    10092  10956   7363  -2283   -361    878       N  
ATOM   5242  N   PHE A 641      13.511  33.596  -4.933  1.00 56.93           N  
ANISOU 5242  N   PHE A 641     7707   8072   5853  -1651   -581    974       N  
ATOM   5243  CA  PHE A 641      12.516  33.876  -3.886  1.00 54.00           C  
ANISOU 5243  CA  PHE A 641     7321   7580   5616  -1551   -620    983       C  
ATOM   5244  C   PHE A 641      12.639  35.278  -3.315  1.00 53.80           C  
ANISOU 5244  C   PHE A 641     7284   7481   5677  -1546   -684   1044       C  
ATOM   5245  O   PHE A 641      13.740  35.768  -3.067  1.00 54.05           O  
ANISOU 5245  O   PHE A 641     7308   7544   5686  -1560   -660   1038       O  
ATOM   5246  CB  PHE A 641      12.576  32.837  -2.758  1.00 51.20           C  
ANISOU 5246  CB  PHE A 641     6947   7206   5301  -1428   -532    881       C  
ATOM   5247  CG  PHE A 641      12.265  31.444  -3.211  1.00 48.07           C  
ANISOU 5247  CG  PHE A 641     6559   6861   4845  -1420   -478    820       C  
ATOM   5248  CD1 PHE A 641      13.281  30.507  -3.361  1.00 45.04           C  
ANISOU 5248  CD1 PHE A 641     6168   6563   4381  -1420   -387    741       C  
ATOM   5249  CD2 PHE A 641      10.957  31.076  -3.525  1.00 47.07           C  
ANISOU 5249  CD2 PHE A 641     6444   6692   4748  -1414   -521    843       C  
ATOM   5250  CE1 PHE A 641      13.003  29.220  -3.806  1.00 43.64           C  
ANISOU 5250  CE1 PHE A 641     5997   6430   4154  -1414   -337    681       C  
ATOM   5251  CE2 PHE A 641      10.665  29.784  -3.970  1.00 44.17           C  
ANISOU 5251  CE2 PHE A 641     6086   6372   4324  -1409   -473    788       C  
ATOM   5252  CZ  PHE A 641      11.691  28.853  -4.105  1.00 41.94           C  
ANISOU 5252  CZ  PHE A 641     5798   6175   3962  -1409   -380    705       C  
ATOM   5253  N   ARG A 642      11.492  35.914  -3.117  1.00 54.48           N  
ANISOU 5253  N   ARG A 642     7366   7467   5868  -1527   -765   1101       N  
ATOM   5254  CA  ARG A 642      11.427  37.269  -2.589  1.00 55.69           C  
ANISOU 5254  CA  ARG A 642     7504   7534   6122  -1520   -833   1159       C  
ATOM   5255  C   ARG A 642      11.759  37.295  -1.105  1.00 53.86           C  
ANISOU 5255  C   ARG A 642     7251   7248   5964  -1409   -773   1087       C  
ATOM   5256  O   ARG A 642      12.537  38.139  -0.653  1.00 54.70           O  
ANISOU 5256  O   ARG A 642     7350   7341   6090  -1412   -780   1098       O  
ATOM   5257  CB  ARG A 642      10.037  37.862  -2.835  1.00 58.59           C  
ANISOU 5257  CB  ARG A 642     7865   7803   6594  -1531   -936   1234       C  
ATOM   5258  CG  ARG A 642       9.761  38.186  -4.299  1.00 65.11           C  
ANISOU 5258  CG  ARG A 642     8714   8669   7356  -1661  -1025   1332       C  
ATOM   5259  CD  ARG A 642       8.317  38.617  -4.537  1.00 68.99           C  
ANISOU 5259  CD  ARG A 642     9194   9058   7961  -1666  -1129   1406       C  
ATOM   5260  NE  ARG A 642       7.391  37.485  -4.584  1.00 71.12           N  
ANISOU 5260  NE  ARG A 642     9466   9324   8233  -1621  -1100   1363       N  
ATOM   5261  CZ  ARG A 642       6.481  37.211  -3.652  1.00 71.03           C  
ANISOU 5261  CZ  ARG A 642     9426   9221   8340  -1515  -1081   1319       C  
ATOM   5262  NH1 ARG A 642       6.362  37.984  -2.578  1.00 72.58           N  
ANISOU 5262  NH1 ARG A 642     9591   9322   8663  -1442  -1084   1306       N  
ATOM   5263  NH2 ARG A 642       5.682  36.161  -3.795  1.00 67.75           N  
ANISOU 5263  NH2 ARG A 642     9014   8811   7916  -1485  -1057   1286       N  
ATOM   5264  N   ASP A 643      11.164  36.361  -0.361  1.00 50.71           N  
ANISOU 5264  N   ASP A 643     6846   6820   5604  -1317   -718   1015       N  
ATOM   5265  CA  ASP A 643      11.363  36.228   1.078  1.00 47.84           C  
ANISOU 5265  CA  ASP A 643     6468   6406   5302  -1214   -659    943       C  
ATOM   5266  C   ASP A 643      11.041  34.797   1.545  1.00 46.64           C  
ANISOU 5266  C   ASP A 643     6317   6273   5132  -1141   -581    859       C  
ATOM   5267  O   ASP A 643      10.690  33.937   0.736  1.00 46.26           O  
ANISOU 5267  O   ASP A 643     6277   6274   5024  -1167   -572    855       O  
ATOM   5268  CB  ASP A 643      10.508  37.254   1.834  1.00 47.25           C  
ANISOU 5268  CB  ASP A 643     6377   6208   5369  -1174   -713    971       C  
ATOM   5269  CG  ASP A 643       9.054  37.265   1.378  1.00 49.58           C  
ANISOU 5269  CG  ASP A 643     6664   6438   5737  -1177   -775   1014       C  
ATOM   5270  OD1 ASP A 643       8.557  36.247   0.843  1.00 50.94           O  
ANISOU 5270  OD1 ASP A 643     6844   6649   5861  -1180   -756    999       O  
ATOM   5271  OD2 ASP A 643       8.394  38.305   1.561  1.00 52.06           O  
ANISOU 5271  OD2 ASP A 643     6959   6656   6164  -1177   -843   1062       O  
ATOM   5272  N   THR A 644      11.150  34.557   2.850  1.00 43.97           N  
ANISOU 5272  N   THR A 644     5970   5893   4842  -1054   -528    795       N  
ATOM   5273  CA  THR A 644      10.875  33.245   3.424  1.00 41.80           C  
ANISOU 5273  CA  THR A 644     5696   5628   4557   -984   -459    718       C  
ATOM   5274  C   THR A 644       9.479  32.773   3.024  1.00 43.02           C  
ANISOU 5274  C   THR A 644     5851   5746   4751   -973   -484    732       C  
ATOM   5275  O   THR A 644       9.322  31.684   2.454  1.00 41.83           O  
ANISOU 5275  O   THR A 644     5706   5649   4538   -979   -456    707       O  
ATOM   5276  CB  THR A 644      11.022  33.257   4.971  1.00 41.26           C  
ANISOU 5276  CB  THR A 644     5624   5504   4549   -902   -414    660       C  
ATOM   5277  OG1 THR A 644      12.319  33.753   5.335  1.00 35.73           O  
ANISOU 5277  OG1 THR A 644     4924   4834   3817   -916   -399    654       O  
ATOM   5278  CG2 THR A 644      10.840  31.858   5.551  1.00 38.40           C  
ANISOU 5278  CG2 THR A 644     5265   5159   4169   -837   -347    586       C  
ATOM   5279  N   ASN A 645       8.478  33.611   3.289  1.00 42.38           N  
ANISOU 5279  N   ASN A 645     5757   5569   4774   -960   -540    770       N  
ATOM   5280  CA  ASN A 645       7.088  33.272   3.010  1.00 44.28           C  
ANISOU 5280  CA  ASN A 645     5991   5761   5074   -946   -570    786       C  
ATOM   5281  C   ASN A 645       6.858  32.766   1.583  1.00 44.16           C  
ANISOU 5281  C   ASN A 645     5988   5810   4981  -1019   -605    830       C  
ATOM   5282  O   ASN A 645       5.963  31.951   1.352  1.00 45.39           O  
ANISOU 5282  O   ASN A 645     6144   5958   5146  -1001   -602    818       O  
ATOM   5283  CB  ASN A 645       6.168  34.458   3.314  1.00 46.48           C  
ANISOU 5283  CB  ASN A 645     6247   5927   5488   -939   -636    833       C  
ATOM   5284  CG  ASN A 645       4.771  34.020   3.730  1.00 50.64           C  
ANISOU 5284  CG  ASN A 645     6754   6379   6109   -882   -633    812       C  
ATOM   5285  OD1 ASN A 645       4.610  33.181   4.618  1.00 49.47           O  
ANISOU 5285  OD1 ASN A 645     6607   6226   5962   -813   -561    738       O  
ATOM   5286  ND2 ASN A 645       3.753  34.587   3.085  1.00 50.08           N  
ANISOU 5286  ND2 ASN A 645     6663   6245   6118   -913   -715    880       N  
ATOM   5287  N   HIS A 646       7.682  33.240   0.645  1.00 43.33           N  
ANISOU 5287  N   HIS A 646     5896   5770   4797  -1105   -637    878       N  
ATOM   5288  CA  HIS A 646       7.621  32.827  -0.760  1.00 41.71           C  
ANISOU 5288  CA  HIS A 646     5711   5639   4499  -1193   -667    918       C  
ATOM   5289  C   HIS A 646       8.009  31.358  -0.971  1.00 39.50           C  
ANISOU 5289  C   HIS A 646     5443   5444   4120  -1178   -584    843       C  
ATOM   5290  O   HIS A 646       7.223  30.590  -1.542  1.00 38.27           O  
ANISOU 5290  O   HIS A 646     5296   5298   3946  -1188   -593    842       O  
ATOM   5291  CB  HIS A 646       8.459  33.772  -1.631  1.00 44.94           C  
ANISOU 5291  CB  HIS A 646     6132   6097   4845  -1296   -716    987       C  
ATOM   5292  CG  HIS A 646       8.277  33.578  -3.107  1.00 47.55           C  
ANISOU 5292  CG  HIS A 646     6488   6495   5085  -1405   -764   1043       C  
ATOM   5293  ND1 HIS A 646       9.099  34.181  -4.038  1.00 50.67           N  
ANISOU 5293  ND1 HIS A 646     6902   6959   5392  -1514   -795   1097       N  
ATOM   5294  CD2 HIS A 646       7.385  32.843  -3.815  1.00 45.76           C  
ANISOU 5294  CD2 HIS A 646     6274   6277   4835  -1429   -785   1054       C  
ATOM   5295  CE1 HIS A 646       8.717  33.834  -5.253  1.00 46.99           C  
ANISOU 5295  CE1 HIS A 646     6461   6545   4848  -1604   -832   1137       C  
ATOM   5296  NE2 HIS A 646       7.682  33.019  -5.145  1.00 52.10           N  
ANISOU 5296  NE2 HIS A 646     7106   7156   5533  -1554   -828   1112       N  
ATOM   5297  N   TRP A 647       9.190  30.950  -0.506  1.00 38.93           N  
ANISOU 5297  N   TRP A 647     5370   5428   3994  -1153   -508    779       N  
ATOM   5298  CA  TRP A 647       9.545  29.520  -0.586  1.00 39.25           C  
ANISOU 5298  CA  TRP A 647     5413   5536   3963  -1127   -429    700       C  
ATOM   5299  C   TRP A 647       8.624  28.618   0.251  1.00 39.29           C  
ANISOU 5299  C   TRP A 647     5411   5486   4033  -1034   -399    649       C  
ATOM   5300  O   TRP A 647       8.365  27.472  -0.127  1.00 39.99           O  
ANISOU 5300  O   TRP A 647     5505   5610   4078  -1027   -365    609       O  
ATOM   5301  CB  TRP A 647      11.045  29.229  -0.352  1.00 40.91           C  
ANISOU 5301  CB  TRP A 647     5616   5818   4110  -1125   -357    644       C  
ATOM   5302  CG  TRP A 647      11.615  29.405   1.063  1.00 40.01           C  
ANISOU 5302  CG  TRP A 647     5485   5661   4056  -1043   -320    602       C  
ATOM   5303  CD1 TRP A 647      12.424  30.425   1.496  1.00 41.65           C  
ANISOU 5303  CD1 TRP A 647     5686   5858   4280  -1054   -333    625       C  
ATOM   5304  CD2 TRP A 647      11.477  28.508   2.182  1.00 38.00           C  
ANISOU 5304  CD2 TRP A 647     5222   5375   3843   -950   -267    533       C  
ATOM   5305  NE1 TRP A 647      12.770  30.236   2.818  1.00 39.05           N  
ANISOU 5305  NE1 TRP A 647     5348   5491   3999   -975   -293    574       N  
ATOM   5306  CE2 TRP A 647      12.201  29.072   3.264  1.00 38.35           C  
ANISOU 5306  CE2 TRP A 647     5258   5389   3925   -912   -253    519       C  
ATOM   5307  CE3 TRP A 647      10.798  27.298   2.383  1.00 35.83           C  
ANISOU 5307  CE3 TRP A 647     4948   5092   3576   -898   -234    484       C  
ATOM   5308  CZ2 TRP A 647      12.262  28.466   4.525  1.00 39.07           C  
ANISOU 5308  CZ2 TRP A 647     5343   5445   4056   -831   -209    461       C  
ATOM   5309  CZ3 TRP A 647      10.855  26.695   3.638  1.00 35.24           C  
ANISOU 5309  CZ3 TRP A 647     4864   4980   3544   -815   -190    428       C  
ATOM   5310  CH2 TRP A 647      11.585  27.278   4.692  1.00 38.94           C  
ANISOU 5310  CH2 TRP A 647     5328   5423   4045   -785   -179    418       C  
ATOM   5311  N   VAL A 648       8.109  29.146   1.362  1.00 38.88           N  
ANISOU 5311  N   VAL A 648     5345   5344   4083   -967   -410    650       N  
ATOM   5312  CA  VAL A 648       7.138  28.412   2.171  1.00 37.89           C  
ANISOU 5312  CA  VAL A 648     5213   5161   4023   -887   -385    608       C  
ATOM   5313  C   VAL A 648       5.830  28.168   1.397  1.00 39.54           C  
ANISOU 5313  C   VAL A 648     5423   5343   4256   -910   -436    648       C  
ATOM   5314  O   VAL A 648       5.271  27.077   1.467  1.00 41.96           O  
ANISOU 5314  O   VAL A 648     5731   5653   4558   -874   -405    608       O  
ATOM   5315  CB  VAL A 648       6.886  29.091   3.536  1.00 36.07           C  
ANISOU 5315  CB  VAL A 648     4969   4842   3892   -821   -380    595       C  
ATOM   5316  CG1 VAL A 648       5.829  28.330   4.323  1.00 33.99           C  
ANISOU 5316  CG1 VAL A 648     4699   4523   3692   -749   -351    553       C  
ATOM   5317  CG2 VAL A 648       8.184  29.166   4.341  1.00 33.91           C  
ANISOU 5317  CG2 VAL A 648     4698   4598   3589   -799   -329    552       C  
ATOM   5318  N   ASP A 649       5.357  29.172   0.658  1.00 41.77           N  
ANISOU 5318  N   ASP A 649     5705   5596   4567   -973   -518    730       N  
ATOM   5319  CA  ASP A 649       4.219  28.997  -0.258  1.00 43.43           C  
ANISOU 5319  CA  ASP A 649     5920   5789   4792  -1014   -580    781       C  
ATOM   5320  C   ASP A 649       4.581  28.031  -1.367  1.00 42.43           C  
ANISOU 5320  C   ASP A 649     5819   5762   4540  -1075   -561    768       C  
ATOM   5321  O   ASP A 649       3.770  27.191  -1.764  1.00 42.38           O  
ANISOU 5321  O   ASP A 649     5818   5756   4527  -1072   -566    760       O  
ATOM   5322  CB  ASP A 649       3.781  30.333  -0.885  1.00 46.85           C  
ANISOU 5322  CB  ASP A 649     6347   6173   5280  -1082   -684    882       C  
ATOM   5323  CG  ASP A 649       2.981  31.202   0.071  1.00 50.05           C  
ANISOU 5323  CG  ASP A 649     6719   6459   5839  -1022   -714    897       C  
ATOM   5324  OD1 ASP A 649       2.220  30.662   0.903  1.00 54.96           O  
ANISOU 5324  OD1 ASP A 649     7323   7027   6531   -943   -676    848       O  
ATOM   5325  OD2 ASP A 649       3.109  32.435  -0.017  1.00 56.69           O  
ANISOU 5325  OD2 ASP A 649     7550   7258   6731  -1057   -775    956       O  
ATOM   5326  N   PHE A 650       5.806  28.151  -1.867  1.00 42.46           N  
ANISOU 5326  N   PHE A 650     5837   5850   4446  -1131   -537    761       N  
ATOM   5327  CA  PHE A 650       6.271  27.256  -2.911  1.00 42.40           C  
ANISOU 5327  CA  PHE A 650     5852   5941   4315  -1194   -505    735       C  
ATOM   5328  C   PHE A 650       6.191  25.793  -2.468  1.00 41.79           C  
ANISOU 5328  C   PHE A 650     5771   5882   4225  -1122   -427    644       C  
ATOM   5329  O   PHE A 650       5.647  24.960  -3.195  1.00 42.39           O  
ANISOU 5329  O   PHE A 650     5862   5986   4258  -1149   -429    635       O  
ATOM   5330  CB  PHE A 650       7.685  27.616  -3.375  1.00 42.02           C  
ANISOU 5330  CB  PHE A 650     5812   5978   4173  -1259   -476    729       C  
ATOM   5331  CG  PHE A 650       8.273  26.612  -4.309  1.00 44.06           C  
ANISOU 5331  CG  PHE A 650     6089   6340   4311  -1315   -421    679       C  
ATOM   5332  CD1 PHE A 650       7.746  26.442  -5.587  1.00 45.29           C  
ANISOU 5332  CD1 PHE A 650     6275   6538   4396  -1411   -466    720       C  
ATOM   5333  CD2 PHE A 650       9.336  25.810  -3.906  1.00 45.22           C  
ANISOU 5333  CD2 PHE A 650     6222   6541   4420  -1274   -326    588       C  
ATOM   5334  CE1 PHE A 650       8.278  25.496  -6.459  1.00 48.97           C  
ANISOU 5334  CE1 PHE A 650     6759   7100   4747  -1467   -408    664       C  
ATOM   5335  CE2 PHE A 650       9.877  24.860  -4.772  1.00 49.00           C  
ANISOU 5335  CE2 PHE A 650     6711   7111   4797  -1324   -269    532       C  
ATOM   5336  CZ  PHE A 650       9.341  24.702  -6.052  1.00 48.97           C  
ANISOU 5336  CZ  PHE A 650     6740   7151   4716  -1422   -306    566       C  
ATOM   5337  N   LEU A 651       6.698  25.492  -1.272  1.00 40.35           N  
ANISOU 5337  N   LEU A 651     5570   5680   4082  -1034   -365    581       N  
ATOM   5338  CA  LEU A 651       6.686  24.121  -0.751  1.00 40.40           C  
ANISOU 5338  CA  LEU A 651     5570   5697   4083   -965   -295    498       C  
ATOM   5339  C   LEU A 651       5.282  23.637  -0.383  1.00 41.13           C  
ANISOU 5339  C   LEU A 651     5659   5720   4250   -913   -317    501       C  
ATOM   5340  O   LEU A 651       4.928  22.486  -0.650  1.00 40.05           O  
ANISOU 5340  O   LEU A 651     5527   5604   4085   -899   -290    461       O  
ATOM   5341  CB  LEU A 651       7.660  23.959   0.429  1.00 39.70           C  
ANISOU 5341  CB  LEU A 651     5464   5606   4016   -896   -232    438       C  
ATOM   5342  CG  LEU A 651       9.161  24.049   0.108  1.00 41.20           C  
ANISOU 5342  CG  LEU A 651     5649   5874   4132   -936   -192    413       C  
ATOM   5343  CD1 LEU A 651       9.999  23.880   1.366  1.00 38.12           C  
ANISOU 5343  CD1 LEU A 651     5240   5467   3779   -864   -142    362       C  
ATOM   5344  CD2 LEU A 651       9.583  23.032  -0.964  1.00 40.44           C  
ANISOU 5344  CD2 LEU A 651     5559   5864   3944   -985   -151    368       C  
ATOM   5345  N   ASP A 652       4.493  24.526   0.220  1.00 42.34           N  
ANISOU 5345  N   ASP A 652     5800   5787   4500   -885   -363    547       N  
ATOM   5346  CA  ASP A 652       3.081  24.271   0.518  1.00 44.19           C  
ANISOU 5346  CA  ASP A 652     6025   5948   4818   -844   -390    560       C  
ATOM   5347  C   ASP A 652       2.320  23.804  -0.734  1.00 44.97           C  
ANISOU 5347  C   ASP A 652     6139   6070   4876   -905   -437    596       C  
ATOM   5348  O   ASP A 652       1.556  22.835  -0.685  1.00 43.50           O  
ANISOU 5348  O   ASP A 652     5952   5871   4705   -872   -424    568       O  
ATOM   5349  CB  ASP A 652       2.446  25.539   1.111  1.00 44.77           C  
ANISOU 5349  CB  ASP A 652     6079   5929   5004   -826   -441    611       C  
ATOM   5350  CG  ASP A 652       0.958  25.386   1.396  1.00 50.24           C  
ANISOU 5350  CG  ASP A 652     6754   6539   5798   -787   -469    626       C  
ATOM   5351  OD1 ASP A 652       0.571  24.478   2.167  1.00 48.11           O  
ANISOU 5351  OD1 ASP A 652     6477   6250   5551   -720   -417    568       O  
ATOM   5352  OD2 ASP A 652       0.171  26.190   0.845  1.00 53.74           O  
ANISOU 5352  OD2 ASP A 652     7185   6932   6302   -827   -548    698       O  
ATOM   5353  N   LYS A 653       2.563  24.487  -1.852  1.00 47.37           N  
ANISOU 5353  N   LYS A 653     6459   6412   5126  -1001   -493    658       N  
ATOM   5354  CA  LYS A 653       1.939  24.161  -3.137  1.00 49.54           C  
ANISOU 5354  CA  LYS A 653     6757   6719   5349  -1080   -547    701       C  
ATOM   5355  C   LYS A 653       2.506  22.866  -3.732  1.00 49.32           C  
ANISOU 5355  C   LYS A 653     6752   6783   5206  -1102   -483    632       C  
ATOM   5356  O   LYS A 653       1.759  22.045  -4.257  1.00 48.45           O  
ANISOU 5356  O   LYS A 653     6653   6678   5078  -1115   -494    627       O  
ATOM   5357  CB  LYS A 653       2.098  25.334  -4.113  1.00 51.68           C  
ANISOU 5357  CB  LYS A 653     7043   7004   5589  -1186   -629    793       C  
ATOM   5358  CG  LYS A 653       1.166  25.302  -5.314  1.00 57.92           C  
ANISOU 5358  CG  LYS A 653     7854   7796   6357  -1273   -715    864       C  
ATOM   5359  CD  LYS A 653       1.137  26.650  -6.045  1.00 61.39           C  
ANISOU 5359  CD  LYS A 653     8301   8220   6803  -1368   -816    972       C  
ATOM   5360  CE  LYS A 653       0.193  26.607  -7.247  1.00 64.41           C  
ANISOU 5360  CE  LYS A 653     8708   8603   7164  -1463   -912   1051       C  
ATOM   5361  NZ  LYS A 653      -0.161  27.963  -7.770  1.00 65.34           N  
ANISOU 5361  NZ  LYS A 653     8822   8670   7333  -1541  -1032   1170       N  
ATOM   5362  N   PHE A 654       3.820  22.677  -3.645  1.00 49.14           N  
ANISOU 5362  N   PHE A 654     6730   6827   5112  -1105   -415    577       N  
ATOM   5363  CA  PHE A 654       4.422  21.426  -4.106  1.00 49.53           C  
ANISOU 5363  CA  PHE A 654     6791   6957   5071  -1116   -344    498       C  
ATOM   5364  C   PHE A 654       3.905  20.212  -3.315  1.00 48.40           C  
ANISOU 5364  C   PHE A 654     6634   6779   4978  -1020   -298    432       C  
ATOM   5365  O   PHE A 654       3.582  19.174  -3.902  1.00 46.93           O  
ANISOU 5365  O   PHE A 654     6460   6624   4748  -1036   -282    397       O  
ATOM   5366  CB  PHE A 654       5.952  21.491  -4.062  1.00 49.48           C  
ANISOU 5366  CB  PHE A 654     6779   7021   5002  -1130   -278    449       C  
ATOM   5367  CG  PHE A 654       6.623  20.315  -4.717  1.00 50.02           C  
ANISOU 5367  CG  PHE A 654     6853   7172   4979  -1157   -208    368       C  
ATOM   5368  CD1 PHE A 654       7.079  19.242  -3.955  1.00 48.60           C  
ANISOU 5368  CD1 PHE A 654     6650   6993   4824  -1074   -132    279       C  
ATOM   5369  CD2 PHE A 654       6.788  20.273  -6.096  1.00 50.21           C  
ANISOU 5369  CD2 PHE A 654     6908   7273   4897  -1271   -217    381       C  
ATOM   5370  CE1 PHE A 654       7.692  18.152  -4.555  1.00 47.61           C  
ANISOU 5370  CE1 PHE A 654     6523   6936   4629  -1096    -66    199       C  
ATOM   5371  CE2 PHE A 654       7.400  19.185  -6.707  1.00 49.82           C  
ANISOU 5371  CE2 PHE A 654     6862   7300   4767  -1298   -144    295       C  
ATOM   5372  CZ  PHE A 654       7.850  18.121  -5.934  1.00 49.24           C  
ANISOU 5372  CZ  PHE A 654     6758   7219   4731  -1207    -68    202       C  
ATOM   5373  N   ALA A 655       3.817  20.355  -1.994  1.00 46.77           N  
ANISOU 5373  N   ALA A 655     6403   6508   4861   -928   -279    415       N  
ATOM   5374  CA  ALA A 655       3.336  19.272  -1.138  1.00 46.67           C  
ANISOU 5374  CA  ALA A 655     6376   6458   4897   -841   -238    358       C  
ATOM   5375  C   ALA A 655       1.880  18.919  -1.408  1.00 46.29           C  
ANISOU 5375  C   ALA A 655     6333   6362   4892   -838   -285    390       C  
ATOM   5376  O   ALA A 655       1.523  17.746  -1.415  1.00 46.35           O  
ANISOU 5376  O   ALA A 655     6342   6376   4892   -809   -257    344       O  
ATOM   5377  CB  ALA A 655       3.518  19.622   0.319  1.00 45.13           C  
ANISOU 5377  CB  ALA A 655     6160   6205   4782   -759   -213    342       C  
ATOM   5378  N   ARG A 656       1.055  19.935  -1.641  1.00 48.14           N  
ANISOU 5378  N   ARG A 656     6567   6545   5180   -868   -360    470       N  
ATOM   5379  CA  ARG A 656      -0.385  19.751  -1.810  1.00 49.53           C  
ANISOU 5379  CA  ARG A 656     6738   6662   5419   -862   -412    509       C  
ATOM   5380  C   ARG A 656      -0.792  19.368  -3.237  1.00 49.78           C  
ANISOU 5380  C   ARG A 656     6798   6740   5377   -950   -460    541       C  
ATOM   5381  O   ARG A 656      -1.753  18.625  -3.432  1.00 50.48           O  
ANISOU 5381  O   ARG A 656     6889   6806   5488   -940   -477    540       O  
ATOM   5382  CB  ARG A 656      -1.126  21.015  -1.363  1.00 52.11           C  
ANISOU 5382  CB  ARG A 656     7042   6901   5856   -851   -473    578       C  
ATOM   5383  CG  ARG A 656      -2.614  20.832  -1.071  1.00 57.94           C  
ANISOU 5383  CG  ARG A 656     7759   7557   6699   -813   -510    602       C  
ATOM   5384  CD  ARG A 656      -3.285  22.146  -0.657  1.00 63.96           C  
ANISOU 5384  CD  ARG A 656     8491   8229   7583   -804   -567    664       C  
ATOM   5385  NE  ARG A 656      -3.041  23.225  -1.620  1.00 69.57           N  
ANISOU 5385  NE  ARG A 656     9211   8950   8271   -892   -644    744       N  
ATOM   5386  CZ  ARG A 656      -2.280  24.291  -1.380  1.00 69.89           C  
ANISOU 5386  CZ  ARG A 656     9248   8989   8318   -905   -650    763       C  
ATOM   5387  NH1 ARG A 656      -1.691  24.445  -0.201  1.00 70.63           N  
ANISOU 5387  NH1 ARG A 656     9330   9068   8440   -836   -583    707       N  
ATOM   5388  NH2 ARG A 656      -2.110  25.209  -2.318  1.00 70.31           N  
ANISOU 5388  NH2 ARG A 656     9312   9054   8349   -993   -727    841       N  
ATOM   5389  N   GLU A 657      -0.068  19.863  -4.235  1.00 49.15           N  
ANISOU 5389  N   GLU A 657     6742   6726   5206  -1043   -480    569       N  
ATOM   5390  CA  GLU A 657      -0.468  19.630  -5.623  1.00 50.17           C  
ANISOU 5390  CA  GLU A 657     6905   6899   5257  -1144   -532    608       C  
ATOM   5391  C   GLU A 657       0.292  18.494  -6.313  1.00 50.23           C  
ANISOU 5391  C   GLU A 657     6939   7003   5142  -1181   -465    530       C  
ATOM   5392  O   GLU A 657      -0.185  17.945  -7.307  1.00 50.99           O  
ANISOU 5392  O   GLU A 657     7064   7132   5177  -1248   -492    539       O  
ATOM   5393  CB  GLU A 657      -0.389  20.923  -6.442  1.00 51.73           C  
ANISOU 5393  CB  GLU A 657     7119   7106   5432  -1245   -615    703       C  
ATOM   5394  CG  GLU A 657      -1.442  21.966  -6.061  1.00 54.94           C  
ANISOU 5394  CG  GLU A 657     7498   7406   5970  -1226   -704    791       C  
ATOM   5395  CD  GLU A 657      -1.345  23.263  -6.870  1.00 60.28           C  
ANISOU 5395  CD  GLU A 657     8188   8084   6633  -1328   -796    891       C  
ATOM   5396  OE1 GLU A 657      -0.490  23.358  -7.782  1.00 59.44           O  
ANISOU 5396  OE1 GLU A 657     8117   8067   6402  -1423   -792    897       O  
ATOM   5397  OE2 GLU A 657      -2.134  24.193  -6.586  1.00 60.00           O  
ANISOU 5397  OE2 GLU A 657     8125   7958   6716  -1315   -873    964       O  
ATOM   5398  N   ARG A 658       1.456  18.135  -5.777  1.00 49.68           N  
ANISOU 5398  N   ARG A 658     6857   6975   5044  -1138   -378    452       N  
ATOM   5399  CA  ARG A 658       2.314  17.121  -6.402  1.00 50.25           C  
ANISOU 5399  CA  ARG A 658     6944   7135   5013  -1172   -306    368       C  
ATOM   5400  C   ARG A 658       2.560  15.890  -5.529  1.00 48.72           C  
ANISOU 5400  C   ARG A 658     6725   6930   4855  -1071   -227    272       C  
ATOM   5401  O   ARG A 658       2.492  14.759  -6.008  1.00 49.06           O  
ANISOU 5401  O   ARG A 658     6780   7007   4855  -1080   -194    214       O  
ATOM   5402  CB  ARG A 658       3.661  17.728  -6.815  1.00 48.63           C  
ANISOU 5402  CB  ARG A 658     6745   7004   4730  -1234   -271    357       C  
ATOM   5403  CG  ARG A 658       3.567  18.782  -7.898  1.00 55.27           C  
ANISOU 5403  CG  ARG A 658     7617   7877   5507  -1356   -345    445       C  
ATOM   5404  CD  ARG A 658       3.536  18.165  -9.290  1.00 59.67           C  
ANISOU 5404  CD  ARG A 658     8217   8514   5942  -1468   -343    429       C  
ATOM   5405  NE  ARG A 658       3.145  19.150 -10.294  1.00 66.89           N  
ANISOU 5405  NE  ARG A 658     9167   9444   6806  -1589   -436    533       N  
ATOM   5406  CZ  ARG A 658       1.912  19.289 -10.777  1.00 70.10           C  
ANISOU 5406  CZ  ARG A 658     9595   9807   7234  -1630   -530    610       C  
ATOM   5407  NH1 ARG A 658       0.930  18.498 -10.362  1.00 70.42           N  
ANISOU 5407  NH1 ARG A 658     9623   9789   7344  -1557   -538    593       N  
ATOM   5408  NH2 ARG A 658       1.661  20.220 -11.687  1.00 72.23           N  
ANISOU 5408  NH2 ARG A 658     9895  10090   7457  -1747   -621    709       N  
ATOM   5409  N   MET A 659       2.871  16.109  -4.258  1.00 46.19           N  
ANISOU 5409  N   MET A 659     6374   6563   4613   -981   -200    257       N  
ATOM   5410  CA  MET A 659       3.251  14.999  -3.386  1.00 45.65           C  
ANISOU 5410  CA  MET A 659     6283   6485   4577   -893   -131    172       C  
ATOM   5411  C   MET A 659       2.065  14.209  -2.830  1.00 44.90           C  
ANISOU 5411  C   MET A 659     6182   6325   4551   -828   -145    167       C  
ATOM   5412  O   MET A 659       2.067  12.972  -2.855  1.00 44.59           O  
ANISOU 5412  O   MET A 659     6140   6300   4503   -801   -106    103       O  
ATOM   5413  CB  MET A 659       4.166  15.484  -2.270  1.00 44.29           C  
ANISOU 5413  CB  MET A 659     6085   6296   4449   -834    -95    155       C  
ATOM   5414  CG  MET A 659       5.505  15.954  -2.788  1.00 47.04           C  
ANISOU 5414  CG  MET A 659     6432   6716   4727   -891    -63    138       C  
ATOM   5415  SD  MET A 659       6.712  16.203  -1.495  1.00 51.16           S  
ANISOU 5415  SD  MET A 659     6920   7223   5296   -819    -14    102       S  
ATOM   5416  CE  MET A 659       7.029  14.502  -1.016  1.00 52.49           C  
ANISOU 5416  CE  MET A 659     7065   7394   5485   -749     52      2       C  
ATOM   5417  N   GLU A 660       1.056  14.927  -2.345  1.00 44.00           N  
ANISOU 5417  N   GLU A 660     6064   6141   4514   -804   -201    234       N  
ATOM   5418  CA  GLU A 660      -0.124  14.298  -1.771  1.00 43.73           C  
ANISOU 5418  CA  GLU A 660     6020   6041   4553   -745   -215    235       C  
ATOM   5419  C   GLU A 660      -0.898  13.432  -2.775  1.00 45.30           C  
ANISOU 5419  C   GLU A 660     6240   6259   4714   -788   -240    234       C  
ATOM   5420  O   GLU A 660      -1.328  12.336  -2.411  1.00 44.80           O  
ANISOU 5420  O   GLU A 660     6170   6177   4676   -738   -216    190       O  
ATOM   5421  CB  GLU A 660      -1.020  15.328  -1.072  1.00 44.75           C  
ANISOU 5421  CB  GLU A 660     6134   6089   4780   -716   -264    302       C  
ATOM   5422  CG  GLU A 660      -0.456  15.801   0.274  1.00 43.61           C  
ANISOU 5422  CG  GLU A 660     5969   5911   4689   -649   -225    282       C  
ATOM   5423  CD  GLU A 660      -1.298  16.876   0.959  1.00 49.63           C  
ANISOU 5423  CD  GLU A 660     6714   6593   5550   -624   -264    338       C  
ATOM   5424  OE1 GLU A 660      -2.522  16.959   0.714  1.00 54.32           O  
ANISOU 5424  OE1 GLU A 660     7302   7138   6200   -630   -312    380       O  
ATOM   5425  OE2 GLU A 660      -0.729  17.639   1.767  1.00 52.64           O  
ANISOU 5425  OE2 GLU A 660     7086   6956   5959   -599   -246    336       O  
ATOM   5426  N   PRO A 661      -1.060  13.891  -4.040  1.00 45.73           N  
ANISOU 5426  N   PRO A 661     6320   6351   4702   -885   -290    281       N  
ATOM   5427  CA  PRO A 661      -1.707  12.989  -4.998  1.00 46.26           C  
ANISOU 5427  CA  PRO A 661     6412   6442   4722   -932   -309    272       C  
ATOM   5428  C   PRO A 661      -0.909  11.713  -5.263  1.00 46.53           C  
ANISOU 5428  C   PRO A 661     6453   6538   4690   -927   -234    172       C  
ATOM   5429  O   PRO A 661      -1.503  10.645  -5.449  1.00 47.67           O  
ANISOU 5429  O   PRO A 661     6603   6674   4835   -914   -229    139       O  
ATOM   5430  CB  PRO A 661      -1.808  13.838  -6.271  1.00 47.55           C  
ANISOU 5430  CB  PRO A 661     6608   6643   4816  -1050   -376    343       C  
ATOM   5431  CG  PRO A 661      -1.851  15.238  -5.771  1.00 47.26           C  
ANISOU 5431  CG  PRO A 661     6554   6560   4844  -1042   -419    416       C  
ATOM   5432  CD  PRO A 661      -0.912  15.248  -4.600  1.00 46.52           C  
ANISOU 5432  CD  PRO A 661     6432   6461   4783   -958   -345    358       C  
ATOM   5433  N   ALA A 662       0.419  11.819  -5.279  1.00 45.03           N  
ANISOU 5433  N   ALA A 662     6257   6403   4448   -938   -175    122       N  
ATOM   5434  CA  ALA A 662       1.267  10.639  -5.450  1.00 43.06           C  
ANISOU 5434  CA  ALA A 662     6001   6204   4154   -927    -98     20       C  
ATOM   5435  C   ALA A 662       1.201   9.729  -4.223  1.00 41.99           C  
ANISOU 5435  C   ALA A 662     5834   6016   4105   -815    -60    -32       C  
ATOM   5436  O   ALA A 662       1.189   8.501  -4.356  1.00 41.66           O  
ANISOU 5436  O   ALA A 662     5788   5982   4057   -795    -27    -99       O  
ATOM   5437  CB  ALA A 662       2.706  11.039  -5.755  1.00 42.54           C  
ANISOU 5437  CB  ALA A 662     5931   6208   4026   -967    -45    -18       C  
ATOM   5438  N   ILE A 663       1.159  10.343  -3.038  1.00 40.19           N  
ANISOU 5438  N   ILE A 663     5584   5733   3953   -748    -68      1       N  
ATOM   5439  CA  ILE A 663       1.063   9.617  -1.772  1.00 36.81           C  
ANISOU 5439  CA  ILE A 663     5130   5252   3604   -650    -40    -35       C  
ATOM   5440  C   ILE A 663      -0.276   8.876  -1.699  1.00 37.03           C  
ANISOU 5440  C   ILE A 663     5164   5232   3675   -624    -72    -22       C  
ATOM   5441  O   ILE A 663      -0.321   7.707  -1.312  1.00 38.08           O  
ANISOU 5441  O   ILE A 663     5286   5352   3832   -576    -43    -76       O  
ATOM   5442  CB  ILE A 663       1.266  10.576  -0.561  1.00 36.68           C  
ANISOU 5442  CB  ILE A 663     5096   5190   3650   -599    -44      1       C  
ATOM   5443  CG1 ILE A 663       2.758  10.866  -0.362  1.00 35.94           C  
ANISOU 5443  CG1 ILE A 663     4989   5140   3528   -601      2    -36       C  
ATOM   5444  CG2 ILE A 663       0.641  10.015   0.720  1.00 31.61           C  
ANISOU 5444  CG2 ILE A 663     4438   4480   3091   -514    -39     -7       C  
ATOM   5445  CD1 ILE A 663       3.042  12.036   0.552  1.00 32.09           C  
ANISOU 5445  CD1 ILE A 663     4492   4619   3080   -577     -9      7       C  
ATOM   5446  N   ASP A 664      -1.355   9.559  -2.088  1.00 38.05           N  
ANISOU 5446  N   ASP A 664     5307   5332   3817   -659   -135     53       N  
ATOM   5447  CA  ASP A 664      -2.685   8.948  -2.187  1.00 40.65           C  
ANISOU 5447  CA  ASP A 664     5641   5619   4186   -647   -173     74       C  
ATOM   5448  C   ASP A 664      -2.674   7.719  -3.107  1.00 40.13           C  
ANISOU 5448  C   ASP A 664     5593   5595   4058   -681   -157     18       C  
ATOM   5449  O   ASP A 664      -3.177   6.662  -2.724  1.00 40.98           O  
ANISOU 5449  O   ASP A 664     5693   5673   4204   -633   -147    -15       O  
ATOM   5450  CB  ASP A 664      -3.735   9.962  -2.673  1.00 42.21           C  
ANISOU 5450  CB  ASP A 664     5849   5784   4407   -694   -250    166       C  
ATOM   5451  CG  ASP A 664      -3.978  11.096  -1.678  1.00 48.07           C  
ANISOU 5451  CG  ASP A 664     6567   6466   5232   -652   -266    216       C  
ATOM   5452  OD1 ASP A 664      -4.634  12.085  -2.071  1.00 54.98           O  
ANISOU 5452  OD1 ASP A 664     7443   7313   6134   -693   -329    291       O  
ATOM   5453  OD2 ASP A 664      -3.529  11.019  -0.511  1.00 49.39           O  
ANISOU 5453  OD2 ASP A 664     6714   6611   5440   -583   -219    182       O  
ATOM   5454  N   ARG A 665      -2.085   7.858  -4.298  1.00 37.87           N  
ANISOU 5454  N   ARG A 665     5332   5379   3678   -766   -154      5       N  
ATOM   5455  CA  ARG A 665      -2.010   6.750  -5.262  1.00 38.49           C  
ANISOU 5455  CA  ARG A 665     5431   5505   3690   -810   -133    -57       C  
ATOM   5456  C   ARG A 665      -1.278   5.546  -4.672  1.00 35.31           C  
ANISOU 5456  C   ARG A 665     5002   5103   3310   -742    -61   -154       C  
ATOM   5457  O   ARG A 665      -1.751   4.410  -4.779  1.00 35.26           O  
ANISOU 5457  O   ARG A 665     4997   5083   3317   -723    -56   -195       O  
ATOM   5458  CB  ARG A 665      -1.352   7.183  -6.584  1.00 39.20           C  
ANISOU 5458  CB  ARG A 665     5553   5677   3666   -921   -129    -62       C  
ATOM   5459  CG  ARG A 665      -2.205   8.125  -7.425  1.00 46.14           C  
ANISOU 5459  CG  ARG A 665     6465   6555   4512  -1007   -214     36       C  
ATOM   5460  CD  ARG A 665      -1.648   8.338  -8.841  1.00 51.26           C  
ANISOU 5460  CD  ARG A 665     7153   7291   5030  -1133   -211     27       C  
ATOM   5461  NE  ARG A 665      -0.305   8.925  -8.854  1.00 56.37           N  
ANISOU 5461  NE  ARG A 665     7793   7994   5632  -1154   -157     -3       N  
ATOM   5462  CZ  ARG A 665      -0.045  10.235  -8.851  1.00 59.17           C  
ANISOU 5462  CZ  ARG A 665     8149   8353   5981  -1189   -192     69       C  
ATOM   5463  NH1 ARG A 665      -1.036  11.126  -8.828  1.00 58.47           N  
ANISOU 5463  NH1 ARG A 665     8068   8212   5936  -1205   -283    175       N  
ATOM   5464  NH2 ARG A 665       1.216  10.658  -8.868  1.00 55.20           N  
ANISOU 5464  NH2 ARG A 665     7636   7902   5435  -1208   -138     34       N  
ATOM   5465  N   GLY A 666      -0.138   5.807  -4.040  1.00 31.88           N  
ANISOU 5465  N   GLY A 666     4543   4683   2888   -707    -13   -187       N  
ATOM   5466  CA  GLY A 666       0.623   4.777  -3.342  1.00 32.60           C  
ANISOU 5466  CA  GLY A 666     4601   4765   3019   -639     45   -270       C  
ATOM   5467  C   GLY A 666      -0.173   4.038  -2.275  1.00 32.87           C  
ANISOU 5467  C   GLY A 666     4620   4727   3142   -556     30   -265       C  
ATOM   5468  O   GLY A 666      -0.056   2.814  -2.138  1.00 34.48           O  
ANISOU 5468  O   GLY A 666     4810   4921   3370   -521     56   -329       O  
ATOM   5469  N   PHE A 667      -0.996   4.759  -1.521  1.00 32.66           N  
ANISOU 5469  N   PHE A 667     4594   4648   3166   -526    -11   -191       N  
ATOM   5470  CA  PHE A 667      -1.792   4.100  -0.475  1.00 33.35           C  
ANISOU 5470  CA  PHE A 667     4668   4669   3334   -454    -22   -184       C  
ATOM   5471  C   PHE A 667      -3.020   3.386  -1.037  1.00 34.56           C  
ANISOU 5471  C   PHE A 667     4837   4803   3492   -469    -58   -172       C  
ATOM   5472  O   PHE A 667      -3.401   2.322  -0.516  1.00 32.69           O  
ANISOU 5472  O   PHE A 667     4589   4531   3300   -421    -51   -201       O  
ATOM   5473  CB  PHE A 667      -2.175   5.058   0.653  1.00 30.83           C  
ANISOU 5473  CB  PHE A 667     4339   4300   3074   -414    -40   -124       C  
ATOM   5474  CG  PHE A 667      -1.130   5.182   1.735  1.00 31.98           C  
ANISOU 5474  CG  PHE A 667     4465   4441   3246   -366     -2   -150       C  
ATOM   5475  CD1 PHE A 667      -0.633   4.051   2.384  1.00 30.35           C  
ANISOU 5475  CD1 PHE A 667     4241   4222   3069   -317     28   -207       C  
ATOM   5476  CD2 PHE A 667      -0.670   6.437   2.133  1.00 32.53           C  
ANISOU 5476  CD2 PHE A 667     4533   4512   3314   -372     -2   -114       C  
ATOM   5477  CE1 PHE A 667       0.325   4.166   3.391  1.00 31.06           C  
ANISOU 5477  CE1 PHE A 667     4313   4304   3186   -279     54   -223       C  
ATOM   5478  CE2 PHE A 667       0.275   6.560   3.154  1.00 29.75           C  
ANISOU 5478  CE2 PHE A 667     4165   4153   2985   -332     28   -134       C  
ATOM   5479  CZ  PHE A 667       0.775   5.426   3.776  1.00 28.34           C  
ANISOU 5479  CZ  PHE A 667     3970   3964   2834   -288     54   -187       C  
ATOM   5480  N   ARG A 668      -3.625   3.964  -2.088  1.00 33.40           N  
ANISOU 5480  N   ARG A 668     4716   4676   3299   -540   -100   -126       N  
ATOM   5481  CA AARG A 668      -4.740   3.308  -2.764  0.50 34.40           C  
ANISOU 5481  CA AARG A 668     4860   4789   3422   -566   -140   -113       C  
ATOM   5482  CA BARG A 668      -4.732   3.326  -2.816  0.50 35.52           C  
ANISOU 5482  CA BARG A 668     5002   4933   3560   -570   -141   -112       C  
ATOM   5483  C   ARG A 668      -4.307   1.941  -3.281  1.00 34.62           C  
ANISOU 5483  C   ARG A 668     4892   4848   3415   -571   -103   -200       C  
ATOM   5484  O   ARG A 668      -5.054   0.982  -3.178  1.00 35.75           O  
ANISOU 5484  O   ARG A 668     5034   4957   3592   -546   -116   -213       O  
ATOM   5485  CB AARG A 668      -5.307   4.171  -3.894  0.50 34.68           C  
ANISOU 5485  CB AARG A 668     4925   4847   3407   -654   -197    -47       C  
ATOM   5486  CB BARG A 668      -5.145   4.163  -4.037  0.50 37.31           C  
ANISOU 5486  CB BARG A 668     5260   5191   3724   -664   -193    -55       C  
ATOM   5487  CG AARG A 668      -6.349   5.174  -3.433  0.50 32.26           C  
ANISOU 5487  CG AARG A 668     4607   4480   3169   -642   -256     46       C  
ATOM   5488  CG BARG A 668      -6.027   5.367  -3.742  0.50 38.21           C  
ANISOU 5488  CG BARG A 668     5369   5257   3892   -667   -253     43       C  
ATOM   5489  CD AARG A 668      -7.163   5.726  -4.598  0.50 32.28           C  
ANISOU 5489  CD AARG A 668     4637   4490   3139   -729   -330    115       C  
ATOM   5490  CD BARG A 668      -5.739   6.527  -4.706  0.50 42.79           C  
ANISOU 5490  CD BARG A 668     5971   5879   4407   -756   -289     94       C  
ATOM   5491  NE AARG A 668      -8.438   6.277  -4.147  0.50 34.72           N  
ANISOU 5491  NE AARG A 668     4926   4724   3542   -706   -389    193       N  
ATOM   5492  NE BARG A 668      -6.576   6.534  -5.903  0.50 44.08           N  
ANISOU 5492  NE BARG A 668     6167   6054   4528   -841   -355    141       N  
ATOM   5493  CZ AARG A 668      -8.594   7.506  -3.660  0.50 39.25           C  
ANISOU 5493  CZ AARG A 668     5480   5261   4171   -695   -413    252       C  
ATOM   5494  CZ BARG A 668      -6.154   6.238  -7.131  0.50 44.12           C  
ANISOU 5494  CZ BARG A 668     6210   6129   4426   -929   -354    114       C  
ATOM   5495  NH1AARG A 668      -7.552   8.329  -3.563  0.50 38.33           N  
ANISOU 5495  NH1AARG A 668     5365   5178   4020   -707   -387    248       N  
ATOM   5496  NH1BARG A 668      -4.894   5.892  -7.351  0.50 42.17           N  
ANISOU 5496  NH1BARG A 668     5968   5946   4108   -942   -282     34       N  
ATOM   5497  NH2AARG A 668      -9.796   7.915  -3.269  0.50 37.43           N  
ANISOU 5497  NH2AARG A 668     5225   4958   4039   -673   -461    314       N  
ATOM   5498  NH2BARG A 668      -7.003   6.288  -8.146  0.50 45.02           N  
ANISOU 5498  NH2BARG A 668     6355   6246   4503  -1010   -424    167       N  
ATOM   5499  N   GLU A 669      -3.090   1.860  -3.809  1.00 36.85           N  
ANISOU 5499  N   GLU A 669     5175   5189   3636   -603    -54   -262       N  
ATOM   5500  CA  GLU A 669      -2.522   0.593  -4.284  1.00 39.94           C  
ANISOU 5500  CA  GLU A 669     5563   5608   4004   -606     -8   -359       C  
ATOM   5501  C   GLU A 669      -2.314  -0.396  -3.129  1.00 38.45           C  
ANISOU 5501  C   GLU A 669     5338   5369   3902   -512     18   -404       C  
ATOM   5502  O   GLU A 669      -2.574  -1.593  -3.275  1.00 38.31           O  
ANISOU 5502  O   GLU A 669     5317   5336   3904   -497     24   -454       O  
ATOM   5503  CB  GLU A 669      -1.203   0.837  -5.039  1.00 40.06           C  
ANISOU 5503  CB  GLU A 669     5579   5696   3944   -661     46   -419       C  
ATOM   5504  CG  GLU A 669      -0.633  -0.390  -5.761  1.00 46.84           C  
ANISOU 5504  CG  GLU A 669     6434   6589   4773   -681     99   -528       C  
ATOM   5505  CD  GLU A 669       0.743  -0.136  -6.376  1.00 51.34           C  
ANISOU 5505  CD  GLU A 669     6994   7229   5282   -730    164   -595       C  
ATOM   5506  OE1 GLU A 669       0.823   0.568  -7.407  1.00 56.16           O  
ANISOU 5506  OE1 GLU A 669     7640   7900   5798   -824    160   -577       O  
ATOM   5507  OE2 GLU A 669       1.745  -0.650  -5.836  1.00 54.11           O  
ANISOU 5507  OE2 GLU A 669     7302   7573   5682   -677    218   -665       O  
ATOM   5508  N   MET A 670      -1.848   0.112  -1.989  1.00 36.70           N  
ANISOU 5508  N   MET A 670     5091   5121   3732   -456     29   -382       N  
ATOM   5509  CA  MET A 670      -1.621  -0.721  -0.812  1.00 37.62           C  
ANISOU 5509  CA  MET A 670     5177   5189   3928   -376     44   -411       C  
ATOM   5510  C   MET A 670      -2.935  -1.317  -0.299  1.00 37.13           C  
ANISOU 5510  C   MET A 670     5120   5068   3920   -341      4   -375       C  
ATOM   5511  O   MET A 670      -2.974  -2.480   0.109  1.00 36.13           O  
ANISOU 5511  O   MET A 670     4978   4912   3840   -300     11   -416       O  
ATOM   5512  CB  MET A 670      -0.929   0.081   0.296  1.00 37.90           C  
ANISOU 5512  CB  MET A 670     5193   5211   3997   -336     57   -385       C  
ATOM   5513  CG  MET A 670      -0.451  -0.754   1.469  1.00 37.23           C  
ANISOU 5513  CG  MET A 670     5078   5083   3985   -266     72   -417       C  
ATOM   5514  SD  MET A 670       0.189   0.269   2.793  1.00 36.01           S  
ANISOU 5514  SD  MET A 670     4911   4910   3861   -230     77   -374       S  
ATOM   5515  CE  MET A 670      -1.330   0.738   3.622  1.00 30.89           C  
ANISOU 5515  CE  MET A 670     4282   4207   3248   -209     35   -293       C  
ATOM   5516  N   CYS A 671      -4.002  -0.516  -0.334  1.00 38.25           N  
ANISOU 5516  N   CYS A 671     5280   5192   4061   -359    -38   -298       N  
ATOM   5517  CA  CYS A 671      -5.335  -0.963   0.086  1.00 38.02           C  
ANISOU 5517  CA  CYS A 671     5253   5108   4085   -333    -76   -259       C  
ATOM   5518  C   CYS A 671      -5.829  -2.130  -0.766  1.00 38.03           C  
ANISOU 5518  C   CYS A 671     5266   5114   4070   -356    -88   -298       C  
ATOM   5519  O   CYS A 671      -6.395  -3.087  -0.237  1.00 38.71           O  
ANISOU 5519  O   CYS A 671     5342   5157   4209   -315    -98   -307       O  
ATOM   5520  CB  CYS A 671      -6.349   0.186   0.039  1.00 37.29           C  
ANISOU 5520  CB  CYS A 671     5171   4996   4002   -357   -120   -173       C  
ATOM   5521  SG  CYS A 671      -8.063  -0.313   0.425  1.00 40.86           S  
ANISOU 5521  SG  CYS A 671     5619   5381   4524   -332   -165   -124       S  
ATOM   5522  N   GLU A 672      -5.618  -2.044  -2.076  1.00 37.72           N  
ANISOU 5522  N   GLU A 672     5251   5127   3956   -425    -89   -320       N  
ATOM   5523  CA  GLU A 672      -6.017  -3.109  -2.997  1.00 39.05           C  
ANISOU 5523  CA  GLU A 672     5436   5306   4097   -458    -97   -364       C  
ATOM   5524  C   GLU A 672      -5.167  -4.360  -2.788  1.00 37.95           C  
ANISOU 5524  C   GLU A 672     5274   5165   3982   -420    -50   -460       C  
ATOM   5525  O   GLU A 672      -5.669  -5.485  -2.801  1.00 37.25           O  
ANISOU 5525  O   GLU A 672     5182   5046   3924   -401    -61   -489       O  
ATOM   5526  CB  GLU A 672      -5.898  -2.638  -4.445  1.00 42.36           C  
ANISOU 5526  CB  GLU A 672     5891   5787   4416   -555   -105   -367       C  
ATOM   5527  CG  GLU A 672      -6.985  -1.666  -4.879  1.00 51.31           C  
ANISOU 5527  CG  GLU A 672     7050   6913   5534   -604   -172   -269       C  
ATOM   5528  CD  GLU A 672      -6.982  -1.416  -6.381  1.00 60.39           C  
ANISOU 5528  CD  GLU A 672     8242   8123   6581   -712   -191   -270       C  
ATOM   5529  OE1 GLU A 672      -7.808  -0.603  -6.857  1.00 62.74           O  
ANISOU 5529  OE1 GLU A 672     8561   8415   6862   -764   -255   -186       O  
ATOM   5530  OE2 GLU A 672      -6.157  -2.037  -7.088  1.00 63.62           O  
ANISOU 5530  OE2 GLU A 672     8663   8584   6927   -748   -144   -355       O  
ATOM   5531  N   TYR A 673      -3.872  -4.145  -2.594  1.00 36.61           N  
ANISOU 5531  N   TYR A 673     5084   5024   3804   -409     -1   -506       N  
ATOM   5532  CA  TYR A 673      -2.934  -5.219  -2.320  1.00 35.13           C  
ANISOU 5532  CA  TYR A 673     4864   4829   3657   -369     42   -595       C  
ATOM   5533  C   TYR A 673      -3.376  -6.013  -1.088  1.00 35.29           C  
ANISOU 5533  C   TYR A 673     4861   4778   3771   -292     21   -580       C  
ATOM   5534  O   TYR A 673      -3.447  -7.245  -1.135  1.00 34.89           O  
ANISOU 5534  O   TYR A 673     4798   4701   3759   -271     22   -633       O  
ATOM   5535  CB  TYR A 673      -1.543  -4.620  -2.146  1.00 34.62           C  
ANISOU 5535  CB  TYR A 673     4775   4798   3579   -366     90   -627       C  
ATOM   5536  CG  TYR A 673      -0.405  -5.600  -1.985  1.00 37.74           C  
ANISOU 5536  CG  TYR A 673     5129   5189   4022   -332    137   -723       C  
ATOM   5537  CD1 TYR A 673      -0.385  -6.825  -2.675  1.00 36.69           C  
ANISOU 5537  CD1 TYR A 673     4989   5054   3897   -343    156   -806       C  
ATOM   5538  CD2 TYR A 673       0.684  -5.284  -1.164  1.00 32.63           C  
ANISOU 5538  CD2 TYR A 673     4446   4535   3417   -293    162   -732       C  
ATOM   5539  CE1 TYR A 673       0.684  -7.721  -2.520  1.00 38.86           C  
ANISOU 5539  CE1 TYR A 673     5217   5316   4233   -309    199   -899       C  
ATOM   5540  CE2 TYR A 673       1.756  -6.163  -1.013  1.00 36.88           C  
ANISOU 5540  CE2 TYR A 673     4938   5063   4013   -262    200   -817       C  
ATOM   5541  CZ  TYR A 673       1.752  -7.375  -1.692  1.00 38.85           C  
ANISOU 5541  CZ  TYR A 673     5176   5306   4281   -269    220   -901       C  
ATOM   5542  OH  TYR A 673       2.818  -8.229  -1.529  1.00 41.38           O  
ANISOU 5542  OH  TYR A 673     5442   5606   4674   -235    256   -988       O  
ATOM   5543  N   MET A 674      -3.699  -5.305  -0.005  1.00 32.34           N  
ANISOU 5543  N   MET A 674     4483   4373   3433   -255      0   -508       N  
ATOM   5544  CA  MET A 674      -4.210  -5.937   1.213  1.00 32.28           C  
ANISOU 5544  CA  MET A 674     4459   4301   3503   -194    -22   -483       C  
ATOM   5545  C   MET A 674      -5.696  -6.294   1.116  1.00 31.75           C  
ANISOU 5545  C   MET A 674     4411   4201   3451   -199    -65   -438       C  
ATOM   5546  O   MET A 674      -6.240  -6.931   2.022  1.00 30.07           O  
ANISOU 5546  O   MET A 674     4187   3938   3299   -156    -83   -420       O  
ATOM   5547  CB  MET A 674      -3.965  -5.053   2.451  1.00 33.04           C  
ANISOU 5547  CB  MET A 674     4546   4379   3627   -160    -20   -430       C  
ATOM   5548  CG  MET A 674      -2.512  -4.990   2.945  1.00 34.92           C  
ANISOU 5548  CG  MET A 674     4758   4629   3880   -138     13   -470       C  
ATOM   5549  SD  MET A 674      -1.751  -6.583   3.372  1.00 37.43           S  
ANISOU 5549  SD  MET A 674     5039   4912   4272    -93     21   -544       S  
ATOM   5550  CE  MET A 674      -0.613  -6.810   2.008  1.00 34.30           C  
ANISOU 5550  CE  MET A 674     4625   4570   3835   -130     69   -640       C  
ATOM   5551  N   ASN A 675      -6.345  -5.890   0.018  1.00 33.20           N  
ANISOU 5551  N   ASN A 675     4622   4413   3580   -255    -84   -419       N  
ATOM   5552  CA  ASN A 675      -7.788  -6.126  -0.192  1.00 31.99           C  
ANISOU 5552  CA  ASN A 675     4484   4229   3441   -267   -131   -370       C  
ATOM   5553  C   ASN A 675      -8.662  -5.544   0.929  1.00 32.25           C  
ANISOU 5553  C   ASN A 675     4509   4216   3531   -232   -153   -293       C  
ATOM   5554  O   ASN A 675      -9.630  -6.163   1.349  1.00 33.66           O  
ANISOU 5554  O   ASN A 675     4682   4349   3757   -210   -179   -270       O  
ATOM   5555  CB  ASN A 675      -8.084  -7.633  -0.381  1.00 30.52           C  
ANISOU 5555  CB  ASN A 675     4294   4017   3284   -253   -139   -422       C  
ATOM   5556  CG  ASN A 675      -9.466  -7.892  -0.988  1.00 29.34           C  
ANISOU 5556  CG  ASN A 675     4166   3850   3131   -284   -188   -382       C  
ATOM   5557  OD1 ASN A 675      -9.911  -7.174  -1.883  1.00 28.35           O  
ANISOU 5557  OD1 ASN A 675     4066   3753   2953   -342   -211   -348       O  
ATOM   5558  ND2 ASN A 675     -10.152  -8.913  -0.488  1.00 31.47           N  
ANISOU 5558  ND2 ASN A 675     4426   4071   3460   -250   -209   -382       N  
ATOM   5559  N   ASN A 676      -8.318  -4.356   1.416  1.00 32.36           N  
ANISOU 5559  N   ASN A 676     4518   4237   3539   -228   -141   -256       N  
ATOM   5560  CA  ASN A 676      -9.019  -3.794   2.569  1.00 33.67           C  
ANISOU 5560  CA  ASN A 676     4673   4359   3760   -194   -149   -197       C  
ATOM   5561  C   ASN A 676     -10.434  -3.325   2.252  1.00 34.93           C  
ANISOU 5561  C   ASN A 676     4837   4493   3941   -217   -191   -132       C  
ATOM   5562  O   ASN A 676     -10.801  -3.166   1.086  1.00 34.55           O  
ANISOU 5562  O   ASN A 676     4806   4467   3856   -267   -221   -121       O  
ATOM   5563  CB  ASN A 676      -8.219  -2.658   3.195  1.00 33.64           C  
ANISOU 5563  CB  ASN A 676     4663   4370   3749   -185   -123   -182       C  
ATOM   5564  CG  ASN A 676      -6.882  -3.108   3.729  1.00 30.97           C  
ANISOU 5564  CG  ASN A 676     4313   4045   3407   -157    -87   -236       C  
ATOM   5565  OD1 ASN A 676      -5.894  -2.402   3.578  1.00 32.48           O  
ANISOU 5565  OD1 ASN A 676     4505   4272   3565   -169    -65   -249       O  
ATOM   5566  ND2 ASN A 676      -6.844  -4.281   4.377  1.00 29.79           N  
ANISOU 5566  ND2 ASN A 676     4152   3866   3300   -120    -86   -264       N  
ATOM   5567  N   LYS A 677     -11.221  -3.114   3.301  1.00 34.96           N  
ANISOU 5567  N   LYS A 677     4826   4450   4008   -184   -193    -91       N  
ATOM   5568  CA  LYS A 677     -12.635  -2.805   3.145  1.00 34.99           C  
ANISOU 5568  CA  LYS A 677     4822   4417   4055   -198   -230    -34       C  
ATOM   5569  C   LYS A 677     -12.851  -1.381   2.632  1.00 35.35           C  
ANISOU 5569  C   LYS A 677     4869   4470   4093   -233   -250     16       C  
ATOM   5570  O   LYS A 677     -13.753  -1.133   1.839  1.00 35.75           O  
ANISOU 5570  O   LYS A 677     4920   4509   4154   -269   -297     58       O  
ATOM   5571  CB  LYS A 677     -13.377  -3.045   4.463  1.00 35.69           C  
ANISOU 5571  CB  LYS A 677     4891   4455   4216   -155   -216    -14       C  
ATOM   5572  CG  LYS A 677     -14.873  -2.754   4.408  1.00 38.39           C  
ANISOU 5572  CG  LYS A 677     5216   4752   4620   -164   -248     41       C  
ATOM   5573  CD  LYS A 677     -15.600  -3.279   5.636  1.00 38.46           C  
ANISOU 5573  CD  LYS A 677     5205   4715   4692   -127   -228     48       C  
ATOM   5574  CE  LYS A 677     -17.101  -3.106   5.495  1.00 38.85           C  
ANISOU 5574  CE  LYS A 677     5232   4720   4811   -137   -259     97       C  
ATOM   5575  NZ  LYS A 677     -17.483  -1.667   5.539  1.00 41.79           N  
ANISOU 5575  NZ  LYS A 677     5583   5073   5222   -148   -259    138       N  
ATOM   5576  N   GLN A 678     -12.006  -0.459   3.079  1.00 37.35           N  
ANISOU 5576  N   GLN A 678     5120   4741   4332   -226   -221     14       N  
ATOM   5577  CA  GLN A 678     -12.147   0.965   2.766  1.00 38.35           C  
ANISOU 5577  CA  GLN A 678     5242   4866   4461   -255   -240     63       C  
ATOM   5578  C   GLN A 678     -10.762   1.615   2.806  1.00 38.19           C  
ANISOU 5578  C   GLN A 678     5232   4891   4386   -260   -207     38       C  
ATOM   5579  O   GLN A 678      -9.966   1.335   3.702  1.00 36.02           O  
ANISOU 5579  O   GLN A 678     4955   4622   4111   -223   -165      1       O  
ATOM   5580  CB  GLN A 678     -13.071   1.608   3.805  1.00 36.99           C  
ANISOU 5580  CB  GLN A 678     5042   4635   4377   -225   -234    103       C  
ATOM   5581  CG  GLN A 678     -13.654   2.966   3.462  1.00 42.24           C  
ANISOU 5581  CG  GLN A 678     5692   5277   5082   -252   -267    163       C  
ATOM   5582  CD  GLN A 678     -14.499   3.519   4.609  1.00 43.90           C  
ANISOU 5582  CD  GLN A 678     5868   5425   5388   -217   -247    185       C  
ATOM   5583  OE1 GLN A 678     -14.797   2.815   5.575  1.00 45.78           O  
ANISOU 5583  OE1 GLN A 678     6098   5642   5656   -180   -212    161       O  
ATOM   5584  NE2 GLN A 678     -14.877   4.778   4.509  1.00 44.23           N  
ANISOU 5584  NE2 GLN A 678     5889   5438   5479   -232   -267    228       N  
ATOM   5585  N   HIS A 679     -10.467   2.469   1.832  1.00 38.64           N  
ANISOU 5585  N   HIS A 679     5302   4981   4399   -312   -232     61       N  
ATOM   5586  CA  HIS A 679      -9.207   3.209   1.830  1.00 36.90           C  
ANISOU 5586  CA  HIS A 679     5088   4802   4130   -322   -204     44       C  
ATOM   5587  C   HIS A 679      -9.282   4.392   2.798  1.00 36.26           C  
ANISOU 5587  C   HIS A 679     4989   4685   4101   -298   -193     79       C  
ATOM   5588  O   HIS A 679     -10.060   5.330   2.603  1.00 36.49           O  
ANISOU 5588  O   HIS A 679     5009   4685   4173   -317   -229    136       O  
ATOM   5589  CB  HIS A 679      -8.829   3.657   0.410  1.00 37.18           C  
ANISOU 5589  CB  HIS A 679     5147   4889   4090   -395   -233     56       C  
ATOM   5590  CG  HIS A 679      -7.856   4.793   0.374  1.00 33.85           C  
ANISOU 5590  CG  HIS A 679     4728   4499   3635   -415   -219     65       C  
ATOM   5591  ND1 HIS A 679      -6.613   4.726   0.963  1.00 34.19           N  
ANISOU 5591  ND1 HIS A 679     4768   4569   3655   -387   -167     16       N  
ATOM   5592  CD2 HIS A 679      -7.946   6.028  -0.176  1.00 36.01           C  
ANISOU 5592  CD2 HIS A 679     5006   4777   3898   -463   -256    121       C  
ATOM   5593  CE1 HIS A 679      -5.979   5.871   0.780  1.00 34.36           C  
ANISOU 5593  CE1 HIS A 679     4792   4614   3650   -416   -168     40       C  
ATOM   5594  NE2 HIS A 679      -6.763   6.678   0.089  1.00 32.46           N  
ANISOU 5594  NE2 HIS A 679     4557   4361   3415   -462   -222    103       N  
ATOM   5595  N   LEU A 680      -8.481   4.330   3.855  1.00 34.08           N  
ANISOU 5595  N   LEU A 680     4709   4411   3830   -256   -146     46       N  
ATOM   5596  CA  LEU A 680      -8.505   5.368   4.884  1.00 32.95           C  
ANISOU 5596  CA  LEU A 680     4552   4235   3732   -233   -128     68       C  
ATOM   5597  C   LEU A 680      -7.108   5.815   5.311  1.00 30.75           C  
ANISOU 5597  C   LEU A 680     4280   3990   3412   -227    -94     41       C  
ATOM   5598  O   LEU A 680      -6.953   6.501   6.311  1.00 29.21           O  
ANISOU 5598  O   LEU A 680     4079   3772   3248   -205    -71     47       O  
ATOM   5599  CB  LEU A 680      -9.343   4.922   6.085  1.00 32.38           C  
ANISOU 5599  CB  LEU A 680     4465   4110   3728   -189   -108     66       C  
ATOM   5600  CG  LEU A 680     -10.858   4.840   5.832  1.00 34.93           C  
ANISOU 5600  CG  LEU A 680     4771   4387   4115   -194   -141    104       C  
ATOM   5601  CD1 LEU A 680     -11.539   4.056   6.944  1.00 32.09           C  
ANISOU 5601  CD1 LEU A 680     4400   3988   3805   -155   -114     89       C  
ATOM   5602  CD2 LEU A 680     -11.498   6.241   5.663  1.00 28.69           C  
ANISOU 5602  CD2 LEU A 680     3961   3561   3378   -213   -167    157       C  
ATOM   5603  N   MET A 681      -6.100   5.439   4.532  1.00 30.01           N  
ANISOU 5603  N   MET A 681     4198   3952   3251   -250    -88      8       N  
ATOM   5604  CA  MET A 681      -4.750   5.940   4.759  1.00 31.82           C  
ANISOU 5604  CA  MET A 681     4430   4216   3443   -251    -60    -14       C  
ATOM   5605  C   MET A 681      -4.600   7.331   4.148  1.00 32.12           C  
ANISOU 5605  C   MET A 681     4472   4269   3462   -295    -82     29       C  
ATOM   5606  O   MET A 681      -4.226   7.471   2.982  1.00 33.86           O  
ANISOU 5606  O   MET A 681     4703   4535   3625   -345    -98     31       O  
ATOM   5607  CB  MET A 681      -3.702   4.963   4.202  1.00 30.04           C  
ANISOU 5607  CB  MET A 681     4208   4041   3166   -258    -39    -73       C  
ATOM   5608  CG  MET A 681      -3.711   3.583   4.859  1.00 28.38           C  
ANISOU 5608  CG  MET A 681     3990   3810   2983   -214    -22   -115       C  
ATOM   5609  SD  MET A 681      -3.342   3.611   6.635  1.00 32.41           S  
ANISOU 5609  SD  MET A 681     4492   4282   3540   -161      3   -117       S  
ATOM   5610  CE  MET A 681      -4.980   3.548   7.376  1.00 28.24           C  
ANISOU 5610  CE  MET A 681     3965   3693   3073   -141    -12    -77       C  
ATOM   5611  N   PHE A 682      -4.906   8.359   4.939  1.00 34.05           N  
ANISOU 5611  N   PHE A 682     4708   4474   3755   -280    -83     63       N  
ATOM   5612  CA  PHE A 682      -4.835   9.742   4.462  1.00 34.66           C  
ANISOU 5612  CA  PHE A 682     4785   4554   3830   -318   -110    109       C  
ATOM   5613  C   PHE A 682      -3.605  10.461   5.016  1.00 35.18           C  
ANISOU 5613  C   PHE A 682     4853   4641   3873   -313    -81     95       C  
ATOM   5614  O   PHE A 682      -3.592  10.903   6.171  1.00 31.33           O  
ANISOU 5614  O   PHE A 682     4358   4117   3427   -279    -59     93       O  
ATOM   5615  CB  PHE A 682      -6.110  10.528   4.816  1.00 35.93           C  
ANISOU 5615  CB  PHE A 682     4928   4647   4075   -311   -137    158       C  
ATOM   5616  CG  PHE A 682      -7.383   9.905   4.312  1.00 36.83           C  
ANISOU 5616  CG  PHE A 682     5036   4734   4223   -316   -171    179       C  
ATOM   5617  CD1 PHE A 682      -7.483   9.437   3.002  1.00 38.53           C  
ANISOU 5617  CD1 PHE A 682     5267   4987   4387   -363   -208    189       C  
ATOM   5618  CD2 PHE A 682      -8.497   9.812   5.144  1.00 36.96           C  
ANISOU 5618  CD2 PHE A 682     5031   4687   4325   -280   -165    187       C  
ATOM   5619  CE1 PHE A 682      -8.667   8.866   2.532  1.00 39.48           C  
ANISOU 5619  CE1 PHE A 682     5382   5079   4540   -372   -244    211       C  
ATOM   5620  CE2 PHE A 682      -9.688   9.243   4.688  1.00 36.83           C  
ANISOU 5620  CE2 PHE A 682     5005   4643   4347   -285   -198    209       C  
ATOM   5621  CZ  PHE A 682      -9.776   8.773   3.375  1.00 39.38           C  
ANISOU 5621  CZ  PHE A 682     5344   5001   4619   -330   -241    224       C  
ATOM   5622  N   MET A 683      -2.571  10.584   4.185  1.00 36.76           N  
ANISOU 5622  N   MET A 683     5062   4900   4004   -351    -79     83       N  
ATOM   5623  CA  MET A 683      -1.347  11.271   4.600  1.00 35.68           C  
ANISOU 5623  CA  MET A 683     4925   4788   3844   -351    -55     72       C  
ATOM   5624  C   MET A 683      -1.242  12.678   4.015  1.00 37.14           C  
ANISOU 5624  C   MET A 683     5112   4979   4019   -399    -88    123       C  
ATOM   5625  O   MET A 683      -0.988  12.865   2.820  1.00 38.29           O  
ANISOU 5625  O   MET A 683     5268   5170   4109   -457   -110    139       O  
ATOM   5626  CB  MET A 683      -0.118  10.423   4.271  1.00 35.23           C  
ANISOU 5626  CB  MET A 683     4868   4789   3728   -355    -21     15       C  
ATOM   5627  CG  MET A 683       1.205  11.039   4.669  1.00 31.79           C  
ANISOU 5627  CG  MET A 683     4428   4380   3272   -356      3      2       C  
ATOM   5628  SD  MET A 683       2.612   9.937   4.401  1.00 33.18           S  
ANISOU 5628  SD  MET A 683     4591   4612   3405   -352     46    -71       S  
ATOM   5629  CE  MET A 683       2.783   9.183   6.017  1.00 25.85           C  
ANISOU 5629  CE  MET A 683     3652   3636   2535   -281     66    -98       C  
ATOM   5630  N   ASP A 684      -1.433  13.665   4.880  1.00 37.10           N  
ANISOU 5630  N   ASP A 684     5100   4929   4068   -380    -90    149       N  
ATOM   5631  CA  ASP A 684      -1.338  15.068   4.501  1.00 41.13           C  
ANISOU 5631  CA  ASP A 684     5610   5433   4586   -419   -124    200       C  
ATOM   5632  C   ASP A 684      -0.002  15.648   4.948  1.00 41.45           C  
ANISOU 5632  C   ASP A 684     5653   5502   4594   -419    -97    183       C  
ATOM   5633  O   ASP A 684       0.651  15.110   5.855  1.00 42.37           O  
ANISOU 5633  O   ASP A 684     5769   5623   4707   -380    -55    138       O  
ATOM   5634  CB  ASP A 684      -2.471  15.882   5.149  1.00 42.56           C  
ANISOU 5634  CB  ASP A 684     5774   5534   4862   -398   -146    236       C  
ATOM   5635  CG  ASP A 684      -3.840  15.536   4.595  1.00 47.75           C  
ANISOU 5635  CG  ASP A 684     6423   6157   5563   -405   -184    266       C  
ATOM   5636  OD1 ASP A 684      -3.921  14.975   3.477  1.00 49.45           O  
ANISOU 5636  OD1 ASP A 684     6650   6412   5726   -445   -210    275       O  
ATOM   5637  OD2 ASP A 684      -4.840  15.839   5.279  1.00 51.27           O  
ANISOU 5637  OD2 ASP A 684     6848   6534   6096   -375   -187    278       O  
ATOM   5638  N   ARG A 685       0.387  16.754   4.318  1.00 40.00           N  
ANISOU 5638  N   ARG A 685     5472   5335   4393   -468   -127    224       N  
ATOM   5639  CA  ARG A 685       1.543  17.525   4.749  1.00 38.23           C  
ANISOU 5639  CA  ARG A 685     5248   5129   4149   -472   -110    219       C  
ATOM   5640  C   ARG A 685       1.281  18.079   6.142  1.00 37.44           C  
ANISOU 5640  C   ARG A 685     5141   4964   4119   -424    -94    215       C  
ATOM   5641  O   ARG A 685       0.177  18.548   6.429  1.00 37.23           O  
ANISOU 5641  O   ARG A 685     5106   4877   4165   -412   -115    242       O  
ATOM   5642  CB  ARG A 685       1.820  18.661   3.756  1.00 37.26           C  
ANISOU 5642  CB  ARG A 685     5130   5029   3999   -540   -155    274       C  
ATOM   5643  CG  ARG A 685       3.162  19.364   3.937  1.00 36.48           C  
ANISOU 5643  CG  ARG A 685     5031   4965   3863   -557   -138    269       C  
ATOM   5644  CD  ARG A 685       3.076  20.520   4.938  1.00 37.56           C  
ANISOU 5644  CD  ARG A 685     5161   5041   4068   -533   -147    291       C  
ATOM   5645  NE  ARG A 685       2.238  21.613   4.453  1.00 37.97           N  
ANISOU 5645  NE  ARG A 685     5208   5049   4170   -567   -207    357       N  
ATOM   5646  CZ  ARG A 685       1.906  22.683   5.166  1.00 37.74           C  
ANISOU 5646  CZ  ARG A 685     5168   4954   4217   -551   -223    380       C  
ATOM   5647  NH1 ARG A 685       2.324  22.821   6.428  1.00 38.23           N  
ANISOU 5647  NH1 ARG A 685     5230   4991   4304   -505   -181    341       N  
ATOM   5648  NH2 ARG A 685       1.142  23.610   4.620  1.00 31.85           N  
ANISOU 5648  NH2 ARG A 685     4412   4165   3526   -584   -284    441       N  
ATOM   5649  N   GLU A 686       2.293  18.005   7.000  1.00 36.94           N  
ANISOU 5649  N   GLU A 686     5081   4916   4040   -400    -57    180       N  
ATOM   5650  CA  GLU A 686       2.190  18.516   8.359  1.00 38.00           C  
ANISOU 5650  CA  GLU A 686     5216   4997   4226   -364    -37    171       C  
ATOM   5651  C   GLU A 686       3.037  19.781   8.510  1.00 37.85           C  
ANISOU 5651  C   GLU A 686     5199   4981   4202   -387    -47    192       C  
ATOM   5652  O   GLU A 686       2.486  20.877   8.637  1.00 39.04           O  
ANISOU 5652  O   GLU A 686     5344   5083   4405   -396    -71    225       O  
ATOM   5653  CB  GLU A 686       2.588  17.448   9.385  1.00 38.42           C  
ANISOU 5653  CB  GLU A 686     5276   5054   4268   -322      5    120       C  
ATOM   5654  CG  GLU A 686       2.054  17.736  10.786  1.00 47.88           C  
ANISOU 5654  CG  GLU A 686     6480   6192   5519   -290     27    108       C  
ATOM   5655  CD  GLU A 686       2.241  16.584  11.760  1.00 53.53           C  
ANISOU 5655  CD  GLU A 686     7207   6909   6224   -257     59     68       C  
ATOM   5656  OE1 GLU A 686       1.233  16.154  12.369  1.00 51.98           O  
ANISOU 5656  OE1 GLU A 686     7013   6673   6065   -235     73     57       O  
ATOM   5657  OE2 GLU A 686       3.395  16.114  11.921  1.00 58.93           O  
ANISOU 5657  OE2 GLU A 686     7894   7629   6866   -256     68     48       O  
ATOM   5658  N   ALA A 687       4.363  19.635   8.463  1.00 34.74           N  
ANISOU 5658  N   ALA A 687     4809   4640   3752   -398    -31    173       N  
ATOM   5659  CA  ALA A 687       5.271  20.762   8.699  1.00 34.35           C  
ANISOU 5659  CA  ALA A 687     4762   4595   3696   -419    -38    190       C  
ATOM   5660  C   ALA A 687       6.124  21.171   7.494  1.00 33.86           C  
ANISOU 5660  C   ALA A 687     4695   4594   3577   -474    -58    215       C  
ATOM   5661  O   ALA A 687       6.572  20.328   6.717  1.00 33.72           O  
ANISOU 5661  O   ALA A 687     4674   4633   3506   -490    -45    194       O  
ATOM   5662  CB  ALA A 687       6.163  20.474   9.898  1.00 35.18           C  
ANISOU 5662  CB  ALA A 687     4873   4699   3793   -389     -4    153       C  
ATOM   5663  N   ILE A 688       6.327  22.476   7.335  1.00 33.71           N  
ANISOU 5663  N   ILE A 688     4676   4562   3571   -507    -88    257       N  
ATOM   5664  CA  ILE A 688       7.342  22.983   6.413  1.00 35.04           C  
ANISOU 5664  CA  ILE A 688     4842   4790   3681   -563   -102    279       C  
ATOM   5665  C   ILE A 688       8.414  23.698   7.221  1.00 36.70           C  
ANISOU 5665  C   ILE A 688     5052   4997   3893   -558    -90    273       C  
ATOM   5666  O   ILE A 688       8.129  24.643   7.965  1.00 38.61           O  
ANISOU 5666  O   ILE A 688     5299   5183   4189   -546   -105    292       O  
ATOM   5667  CB  ILE A 688       6.763  23.906   5.331  1.00 36.89           C  
ANISOU 5667  CB  ILE A 688     5078   5019   3919   -621   -158    344       C  
ATOM   5668  CG1 ILE A 688       5.719  23.160   4.499  1.00 37.41           C  
ANISOU 5668  CG1 ILE A 688     5147   5089   3980   -632   -175    352       C  
ATOM   5669  CG2 ILE A 688       7.870  24.410   4.399  1.00 34.11           C  
ANISOU 5669  CG2 ILE A 688     4727   4736   3497   -688   -169    367       C  
ATOM   5670  CD1 ILE A 688       4.924  24.066   3.578  1.00 41.03           C  
ANISOU 5670  CD1 ILE A 688     5606   5524   4460   -687   -244    424       C  
ATOM   5671  N   ALA A 689       9.647  23.221   7.096  1.00 37.14           N  
ANISOU 5671  N   ALA A 689     5101   5112   3898   -566    -61    244       N  
ATOM   5672  CA  ALA A 689      10.731  23.716   7.928  1.00 38.01           C  
ANISOU 5672  CA  ALA A 689     5209   5222   4010   -558    -50    235       C  
ATOM   5673  C   ALA A 689      11.928  24.158   7.108  1.00 37.05           C  
ANISOU 5673  C   ALA A 689     5076   5165   3837   -611    -51    249       C  
ATOM   5674  O   ALA A 689      12.199  23.620   6.035  1.00 37.23           O  
ANISOU 5674  O   ALA A 689     5089   5247   3809   -646    -40    240       O  
ATOM   5675  CB  ALA A 689      11.135  22.662   8.961  1.00 36.46           C  
ANISOU 5675  CB  ALA A 689     5011   5020   3822   -507    -13    183       C  
ATOM   5676  N   GLY A 690      12.634  25.157   7.624  1.00 38.63           N  
ANISOU 5676  N   GLY A 690     5277   5352   4049   -622    -64    269       N  
ATOM   5677  CA  GLY A 690      13.831  25.677   6.977  1.00 37.57           C  
ANISOU 5677  CA  GLY A 690     5130   5275   3870   -674    -65    284       C  
ATOM   5678  C   GLY A 690      14.356  26.923   7.661  1.00 38.70           C  
ANISOU 5678  C   GLY A 690     5278   5386   4039   -683    -89    314       C  
ATOM   5679  O   GLY A 690      13.710  27.456   8.564  1.00 39.29           O  
ANISOU 5679  O   GLY A 690     5370   5393   4167   -653   -106    323       O  
ATOM   5680  N   PRO A 691      15.533  27.406   7.224  1.00 39.45           N  
ANISOU 5680  N   PRO A 691     5360   5531   4099   -727    -89    327       N  
ATOM   5681  CA  PRO A 691      16.121  28.605   7.806  1.00 38.23           C  
ANISOU 5681  CA  PRO A 691     5211   5349   3966   -740   -115    358       C  
ATOM   5682  C   PRO A 691      15.489  29.881   7.249  1.00 39.41           C  
ANISOU 5682  C   PRO A 691     5373   5471   4132   -785   -168    421       C  
ATOM   5683  O   PRO A 691      14.973  29.872   6.121  1.00 42.72           O  
ANISOU 5683  O   PRO A 691     5791   5916   4524   -826   -186    450       O  
ATOM   5684  CB  PRO A 691      17.585  28.508   7.378  1.00 38.65           C  
ANISOU 5684  CB  PRO A 691     5239   5473   3975   -775    -93    347       C  
ATOM   5685  CG  PRO A 691      17.569  27.738   6.094  1.00 40.31           C  
ANISOU 5685  CG  PRO A 691     5435   5752   4131   -810    -68    333       C  
ATOM   5686  CD  PRO A 691      16.302  26.918   6.060  1.00 38.91           C  
ANISOU 5686  CD  PRO A 691     5271   5547   3968   -774    -64    315       C  
ATOM   5687  N   PRO A 692      15.519  30.983   8.025  1.00 39.49           N  
ANISOU 5687  N   PRO A 692     5393   5424   4189   -780   -196    445       N  
ATOM   5688  CA  PRO A 692      15.089  32.253   7.428  1.00 40.75           C  
ANISOU 5688  CA  PRO A 692     5556   5555   4371   -828   -253    509       C  
ATOM   5689  C   PRO A 692      15.901  32.525   6.165  1.00 41.75           C  
ANISOU 5689  C   PRO A 692     5672   5760   4431   -904   -267    547       C  
ATOM   5690  O   PRO A 692      17.126  32.361   6.187  1.00 40.95           O  
ANISOU 5690  O   PRO A 692     5559   5712   4289   -918   -239    528       O  
ATOM   5691  CB  PRO A 692      15.431  33.288   8.514  1.00 39.44           C  
ANISOU 5691  CB  PRO A 692     5399   5330   4256   -813   -270    514       C  
ATOM   5692  CG  PRO A 692      15.405  32.506   9.803  1.00 38.37           C  
ANISOU 5692  CG  PRO A 692     5273   5168   4139   -748   -226    453       C  
ATOM   5693  CD  PRO A 692      15.935  31.141   9.432  1.00 38.27           C  
ANISOU 5693  CD  PRO A 692     5246   5225   4067   -738   -183    416       C  
ATOM   5694  N   LEU A 693      15.228  32.895   5.074  1.00 42.53           N  
ANISOU 5694  N   LEU A 693     5775   5866   4518   -956   -310    598       N  
ATOM   5695  CA  LEU A 693      15.912  33.199   3.809  1.00 44.96           C  
ANISOU 5695  CA  LEU A 693     6079   6251   4753  -1044   -325    639       C  
ATOM   5696  C   LEU A 693      16.950  34.300   4.020  1.00 44.82           C  
ANISOU 5696  C   LEU A 693     6056   6237   4737  -1079   -347    671       C  
ATOM   5697  O   LEU A 693      16.658  35.320   4.646  1.00 44.83           O  
ANISOU 5697  O   LEU A 693     6063   6165   4805  -1066   -390    702       O  
ATOM   5698  CB  LEU A 693      14.920  33.641   2.727  1.00 46.09           C  
ANISOU 5698  CB  LEU A 693     6233   6384   4894  -1103   -387    704       C  
ATOM   5699  CG  LEU A 693      15.162  33.268   1.250  1.00 47.70           C  
ANISOU 5699  CG  LEU A 693     6443   6681   5000  -1190   -387    726       C  
ATOM   5700  CD1 LEU A 693      14.837  34.446   0.339  1.00 47.64           C  
ANISOU 5700  CD1 LEU A 693     6447   6664   4990  -1279   -472    821       C  
ATOM   5701  CD2 LEU A 693      16.567  32.740   0.958  1.00 46.27           C  
ANISOU 5701  CD2 LEU A 693     6248   6595   4739  -1218   -321    681       C  
ATOM   5702  N   GLY A 694      18.157  34.067   3.512  1.00 45.44           N  
ANISOU 5702  N   GLY A 694     6121   6399   4746  -1122   -313    658       N  
ATOM   5703  CA  GLY A 694      19.265  35.010   3.637  1.00 47.69           C  
ANISOU 5703  CA  GLY A 694     6397   6699   5024  -1160   -327    687       C  
ATOM   5704  C   GLY A 694      20.053  34.885   4.925  1.00 49.77           C  
ANISOU 5704  C   GLY A 694     6650   6938   5323  -1098   -295    640       C  
ATOM   5705  O   GLY A 694      20.938  35.701   5.190  1.00 51.98           O  
ANISOU 5705  O   GLY A 694     6924   7220   5609  -1123   -311    663       O  
ATOM   5706  N   SER A 695      19.740  33.865   5.727  1.00 48.50           N  
ANISOU 5706  N   SER A 695     6488   6754   5185  -1023   -254    579       N  
ATOM   5707  CA  SER A 695      20.416  33.661   7.007  1.00 48.23           C  
ANISOU 5707  CA  SER A 695     6449   6692   5183   -968   -229    538       C  
ATOM   5708  C   SER A 695      21.430  32.520   6.937  1.00 47.80           C  
ANISOU 5708  C   SER A 695     6364   6704   5092   -957   -171    484       C  
ATOM   5709  O   SER A 695      21.555  31.853   5.912  1.00 47.72           O  
ANISOU 5709  O   SER A 695     6338   6760   5032   -988   -141    469       O  
ATOM   5710  CB  SER A 695      19.398  33.384   8.116  1.00 47.29           C  
ANISOU 5710  CB  SER A 695     6351   6493   5122   -896   -229    510       C  
ATOM   5711  OG  SER A 695      18.899  32.055   8.014  1.00 48.77           O  
ANISOU 5711  OG  SER A 695     6535   6700   5296   -858   -189    464       O  
ATOM   5712  N   LYS A 696      22.137  32.299   8.041  1.00 47.42           N  
ANISOU 5712  N   LYS A 696     6309   6635   5074   -915   -156    453       N  
ATOM   5713  CA  LYS A 696      23.095  31.200   8.142  1.00 47.04           C  
ANISOU 5713  CA  LYS A 696     6226   6632   5014   -895   -108    401       C  
ATOM   5714  C   LYS A 696      22.596  30.077   9.067  1.00 45.39           C  
ANISOU 5714  C   LYS A 696     6025   6385   4838   -823    -87    352       C  
ATOM   5715  O   LYS A 696      23.349  29.156   9.402  1.00 44.29           O  
ANISOU 5715  O   LYS A 696     5857   6264   4708   -797    -57    310       O  
ATOM   5716  CB  LYS A 696      24.455  31.721   8.621  1.00 47.33           C  
ANISOU 5716  CB  LYS A 696     6242   6680   5063   -912   -114    410       C  
ATOM   5717  CG  LYS A 696      25.077  32.779   7.723  1.00 48.19           C  
ANISOU 5717  CG  LYS A 696     6339   6832   5138   -988   -132    458       C  
ATOM   5718  CD  LYS A 696      26.216  33.484   8.450  1.00 52.60           C  
ANISOU 5718  CD  LYS A 696     6886   7379   5721   -997   -151    475       C  
ATOM   5719  CE  LYS A 696      27.029  34.367   7.519  1.00 53.47           C  
ANISOU 5719  CE  LYS A 696     6976   7544   5796  -1076   -160    517       C  
ATOM   5720  NZ  LYS A 696      27.960  35.217   8.313  1.00 59.32           N  
ANISOU 5720  NZ  LYS A 696     7713   8259   6567  -1084   -191    542       N  
ATOM   5721  N   GLY A 697      21.330  30.152   9.472  1.00 43.24           N  
ANISOU 5721  N   GLY A 697     5788   6056   4587   -792   -104    358       N  
ATOM   5722  CA  GLY A 697      20.707  29.075  10.255  1.00 41.62           C  
ANISOU 5722  CA  GLY A 697     5592   5817   4406   -731    -85    314       C  
ATOM   5723  C   GLY A 697      20.685  27.749   9.503  1.00 40.92           C  
ANISOU 5723  C   GLY A 697     5477   5778   4293   -721    -44    274       C  
ATOM   5724  O   GLY A 697      20.626  27.723   8.268  1.00 37.72           O  
ANISOU 5724  O   GLY A 697     5058   5424   3849   -762    -33    281       O  
ATOM   5725  N   ILE A 698      20.755  26.645  10.244  1.00 39.46           N  
ANISOU 5725  N   ILE A 698     5285   5577   4132   -671    -24    231       N  
ATOM   5726  CA  ILE A 698      20.826  25.323   9.615  1.00 37.81           C  
ANISOU 5726  CA  ILE A 698     5045   5409   3911   -657     15    185       C  
ATOM   5727  C   ILE A 698      19.456  24.703   9.320  1.00 37.64           C  
ANISOU 5727  C   ILE A 698     5046   5371   3886   -635     21    174       C  
ATOM   5728  O   ILE A 698      19.371  23.715   8.589  1.00 37.80           O  
ANISOU 5728  O   ILE A 698     5045   5428   3890   -632     52    139       O  
ATOM   5729  CB  ILE A 698      21.718  24.333  10.412  1.00 38.55           C  
ANISOU 5729  CB  ILE A 698     5109   5497   4042   -620     30    145       C  
ATOM   5730  CG1 ILE A 698      21.125  24.055  11.803  1.00 37.58           C  
ANISOU 5730  CG1 ILE A 698     5021   5306   3953   -573      8    143       C  
ATOM   5731  CG2 ILE A 698      23.147  24.854  10.477  1.00 34.71           C  
ANISOU 5731  CG2 ILE A 698     4590   5035   3562   -648     27    154       C  
ATOM   5732  CD1 ILE A 698      21.853  22.991  12.596  1.00 35.52           C  
ANISOU 5732  CD1 ILE A 698     4735   5032   3730   -539     11    112       C  
ATOM   5733  N   GLY A 699      18.396  25.283   9.888  1.00 36.43           N  
ANISOU 5733  N   GLY A 699     4931   5161   3750   -619     -6    200       N  
ATOM   5734  CA  GLY A 699      17.025  24.860   9.605  1.00 33.74           C  
ANISOU 5734  CA  GLY A 699     4609   4798   3412   -601     -6    198       C  
ATOM   5735  C   GLY A 699      16.536  23.744  10.511  1.00 33.87           C  
ANISOU 5735  C   GLY A 699     4632   4779   3457   -545      9    160       C  
ATOM   5736  O   GLY A 699      15.454  23.835  11.101  1.00 33.69           O  
ANISOU 5736  O   GLY A 699     4637   4705   3458   -520      0    165       O  
ATOM   5737  N   GLY A 700      17.324  22.679  10.604  1.00 32.68           N  
ANISOU 5737  N   GLY A 700     4454   4655   3308   -527     33    121       N  
ATOM   5738  CA  GLY A 700      17.011  21.574  11.494  1.00 31.75           C  
ANISOU 5738  CA  GLY A 700     4341   4504   3219   -478     40     89       C  
ATOM   5739  C   GLY A 700      18.156  20.596  11.658  1.00 31.47           C  
ANISOU 5739  C   GLY A 700     4266   4490   3200   -464     55     54       C  
ATOM   5740  O   GLY A 700      19.191  20.711  10.987  1.00 31.42           O  
ANISOU 5740  O   GLY A 700     4223   4530   3183   -490     69     46       O  
ATOM   5741  N   PHE A 701      17.966  19.638  12.563  1.00 29.59           N  
ANISOU 5741  N   PHE A 701     4033   4218   2992   -425     52     33       N  
ATOM   5742  CA  PHE A 701      18.900  18.534  12.744  1.00 31.33           C  
ANISOU 5742  CA  PHE A 701     4212   4447   3246   -406     58      0       C  
ATOM   5743  C   PHE A 701      18.254  17.369  13.476  1.00 32.99           C  
ANISOU 5743  C   PHE A 701     4433   4618   3485   -366     52    -19       C  
ATOM   5744  O   PHE A 701      17.287  17.544  14.217  1.00 35.32           O  
ANISOU 5744  O   PHE A 701     4774   4874   3774   -355     39     -2       O  
ATOM   5745  CB  PHE A 701      20.186  18.974  13.472  1.00 29.89           C  
ANISOU 5745  CB  PHE A 701     4013   4257   3086   -416     37     14       C  
ATOM   5746  CG  PHE A 701      19.973  19.389  14.911  1.00 28.38           C  
ANISOU 5746  CG  PHE A 701     3868   4013   2903   -410      2     42       C  
ATOM   5747  CD1 PHE A 701      19.662  20.713  15.227  1.00 24.68           C  
ANISOU 5747  CD1 PHE A 701     3440   3529   2408   -434    -11     76       C  
ATOM   5748  CD2 PHE A 701      20.106  18.464  15.948  1.00 25.80           C  
ANISOU 5748  CD2 PHE A 701     3545   3649   2609   -387    -20     34       C  
ATOM   5749  CE1 PHE A 701      19.480  21.110  16.564  1.00 25.86           C  
ANISOU 5749  CE1 PHE A 701     3634   3630   2560   -434    -37     93       C  
ATOM   5750  CE2 PHE A 701      19.914  18.849  17.285  1.00 27.61           C  
ANISOU 5750  CE2 PHE A 701     3823   3834   2834   -393    -51     59       C  
ATOM   5751  CZ  PHE A 701      19.593  20.175  17.592  1.00 23.19           C  
ANISOU 5751  CZ  PHE A 701     3305   3262   2244   -417    -55     85       C  
ATOM   5752  N   TRP A 702      18.804  16.183  13.241  1.00 34.03           N  
ANISOU 5752  N   TRP A 702     4520   4759   3650   -346     62    -56       N  
ATOM   5753  CA  TRP A 702      18.475  14.978  13.986  1.00 35.84           C  
ANISOU 5753  CA  TRP A 702     4750   4949   3918   -311     48    -72       C  
ATOM   5754  C   TRP A 702      19.753  14.517  14.664  1.00 34.55           C  
ANISOU 5754  C   TRP A 702     4549   4770   3809   -305     23    -76       C  
ATOM   5755  O   TRP A 702      20.823  14.637  14.073  1.00 34.98           O  
ANISOU 5755  O   TRP A 702     4554   4855   3881   -317     37    -92       O  
ATOM   5756  CB  TRP A 702      18.004  13.882  13.030  1.00 34.48           C  
ANISOU 5756  CB  TRP A 702     4552   4796   3754   -293     77   -115       C  
ATOM   5757  CG  TRP A 702      16.539  13.820  12.835  1.00 34.69           C  
ANISOU 5757  CG  TRP A 702     4619   4812   3749   -286     83   -108       C  
ATOM   5758  CD1 TRP A 702      15.680  12.891  13.363  1.00 35.73           C  
ANISOU 5758  CD1 TRP A 702     4769   4908   3901   -257     73   -115       C  
ATOM   5759  CD2 TRP A 702      15.738  14.708  12.047  1.00 35.35           C  
ANISOU 5759  CD2 TRP A 702     4729   4918   3784   -310     97    -90       C  
ATOM   5760  NE1 TRP A 702      14.390  13.151  12.952  1.00 37.57           N  
ANISOU 5760  NE1 TRP A 702     5034   5140   4100   -259     84   -104       N  
ATOM   5761  CE2 TRP A 702      14.396  14.260  12.146  1.00 35.41           C  
ANISOU 5761  CE2 TRP A 702     4765   4899   3788   -291     95    -88       C  
ATOM   5762  CE3 TRP A 702      16.021  15.839  11.268  1.00 34.85           C  
ANISOU 5762  CE3 TRP A 702     4665   4892   3683   -348    105    -71       C  
ATOM   5763  CZ2 TRP A 702      13.339  14.904  11.495  1.00 32.80           C  
ANISOU 5763  CZ2 TRP A 702     4460   4575   3426   -307    100    -68       C  
ATOM   5764  CZ3 TRP A 702      14.971  16.480  10.624  1.00 38.77           C  
ANISOU 5764  CZ3 TRP A 702     5190   5395   4145   -367    106    -48       C  
ATOM   5765  CH2 TRP A 702      13.640  16.006  10.744  1.00 34.93           C  
ANISOU 5765  CH2 TRP A 702     4729   4878   3664   -345    102    -47       C  
ATOM   5766  N   THR A 703      19.652  13.996  15.888  1.00 34.15           N  
ANISOU 5766  N   THR A 703     4520   4670   3785   -290    -16    -60       N  
ATOM   5767  CA  THR A 703      20.797  13.328  16.527  1.00 33.12           C  
ANISOU 5767  CA  THR A 703     4349   4516   3720   -283    -51    -60       C  
ATOM   5768  C   THR A 703      20.624  11.805  16.537  1.00 32.80           C  
ANISOU 5768  C   THR A 703     4277   4450   3735   -250    -59    -90       C  
ATOM   5769  O   THR A 703      21.582  11.056  16.721  1.00 36.74           O  
ANISOU 5769  O   THR A 703     4721   4930   4307   -239    -83   -103       O  
ATOM   5770  CB  THR A 703      21.078  13.829  17.981  1.00 32.18           C  
ANISOU 5770  CB  THR A 703     4274   4357   3597   -303   -104    -13       C  
ATOM   5771  OG1 THR A 703      20.282  13.097  18.918  1.00 34.14           O  
ANISOU 5771  OG1 THR A 703     4562   4563   3846   -293   -131     -1       O  
ATOM   5772  CG2 THR A 703      20.804  15.313  18.136  1.00 34.83           C  
ANISOU 5772  CG2 THR A 703     4659   4704   3870   -332    -95     15       C  
ATOM   5773  N   GLY A 704      19.395  11.352  16.344  1.00 33.99           N  
ANISOU 5773  N   GLY A 704     4459   4597   3860   -235    -43   -100       N  
ATOM   5774  CA  GLY A 704      19.079   9.924  16.400  1.00 33.94           C  
ANISOU 5774  CA  GLY A 704     4430   4563   3904   -205    -53   -125       C  
ATOM   5775  C   GLY A 704      17.583   9.718  16.394  1.00 32.62           C  
ANISOU 5775  C   GLY A 704     4313   4389   3693   -196    -40   -122       C  
ATOM   5776  O   GLY A 704      16.821  10.658  16.154  1.00 29.95           O  
ANISOU 5776  O   GLY A 704     4016   4069   3294   -211    -16   -108       O  
ATOM   5777  N   LYS A 705      17.153   8.487  16.643  1.00 33.15           N  
ANISOU 5777  N   LYS A 705     4372   4424   3798   -173    -57   -135       N  
ATOM   5778  CA  LYS A 705      15.722   8.205  16.726  1.00 33.16           C  
ANISOU 5778  CA  LYS A 705     4419   4415   3766   -164    -47   -130       C  
ATOM   5779  C   LYS A 705      15.105   9.072  17.804  1.00 31.42           C  
ANISOU 5779  C   LYS A 705     4266   4176   3496   -188    -61    -86       C  
ATOM   5780  O   LYS A 705      15.662   9.212  18.892  1.00 34.46           O  
ANISOU 5780  O   LYS A 705     4669   4536   3890   -205   -100    -56       O  
ATOM   5781  CB  LYS A 705      15.461   6.729  17.031  1.00 32.44           C  
ANISOU 5781  CB  LYS A 705     4310   4285   3728   -140    -73   -144       C  
ATOM   5782  CG  LYS A 705      15.685   5.806  15.848  1.00 32.18           C  
ANISOU 5782  CG  LYS A 705     4218   4269   3740   -115    -47   -200       C  
ATOM   5783  CD  LYS A 705      15.416   4.364  16.237  1.00 32.62           C  
ANISOU 5783  CD  LYS A 705     4258   4280   3858    -90    -80   -210       C  
ATOM   5784  CE  LYS A 705      15.669   3.412  15.075  1.00 34.03           C  
ANISOU 5784  CE  LYS A 705     4374   4470   4088    -66    -50   -275       C  
ATOM   5785  NZ  LYS A 705      15.472   2.003  15.495  1.00 28.09           N  
ANISOU 5785  NZ  LYS A 705     3602   3665   3407    -41    -89   -283       N  
ATOM   5786  N   LYS A 706      13.971   9.678  17.481  1.00 32.59           N  
ANISOU 5786  N   LYS A 706     4451   4336   3596   -191    -30    -83       N  
ATOM   5787  CA  LYS A 706      13.136  10.373  18.467  1.00 32.71           C  
ANISOU 5787  CA  LYS A 706     4527   4328   3572   -210    -32    -52       C  
ATOM   5788  C   LYS A 706      13.790  11.615  19.079  1.00 31.38           C  
ANISOU 5788  C   LYS A 706     4382   4161   3378   -240    -41    -28       C  
ATOM   5789  O   LYS A 706      13.373  12.090  20.135  1.00 32.67           O  
ANISOU 5789  O   LYS A 706     4596   4301   3517   -262    -48     -7       O  
ATOM   5790  CB  LYS A 706      12.660   9.385  19.551  1.00 33.48           C  
ANISOU 5790  CB  LYS A 706     4652   4386   3685   -209    -61    -41       C  
ATOM   5791  CG  LYS A 706      11.674   8.345  19.022  1.00 38.09           C  
ANISOU 5791  CG  LYS A 706     5225   4964   4284   -183    -48    -61       C  
ATOM   5792  CD  LYS A 706      11.026   7.541  20.122  1.00 39.04           C  
ANISOU 5792  CD  LYS A 706     5379   5047   4408   -190    -73    -43       C  
ATOM   5793  CE  LYS A 706       9.947   6.603  19.573  1.00 39.92           C  
ANISOU 5793  CE  LYS A 706     5482   5152   4533   -165    -59    -62       C  
ATOM   5794  NZ  LYS A 706       8.726   7.332  19.142  1.00 33.80           N  
ANISOU 5794  NZ  LYS A 706     4731   4388   3723   -165    -16    -66       N  
ATOM   5795  N   ARG A 707      14.801  12.146  18.396  1.00 33.71           N  
ANISOU 5795  N   ARG A 707     4933   4148   3727   -324   -251   -175       N  
ATOM   5796  CA  ARG A 707      15.565  13.286  18.880  1.00 30.45           C  
ANISOU 5796  CA  ARG A 707     4439   3779   3353   -314   -216   -207       C  
ATOM   5797  C   ARG A 707      15.866  14.246  17.729  1.00 31.51           C  
ANISOU 5797  C   ARG A 707     4516   3952   3504   -352   -165   -210       C  
ATOM   5798  O   ARG A 707      16.770  13.996  16.926  1.00 33.49           O  
ANISOU 5798  O   ARG A 707     4748   4237   3741   -328   -153   -254       O  
ATOM   5799  CB  ARG A 707      16.866  12.805  19.529  1.00 30.05           C  
ANISOU 5799  CB  ARG A 707     4376   3745   3297   -238   -240   -281       C  
ATOM   5800  CG  ARG A 707      16.666  12.075  20.856  1.00 28.79           C  
ANISOU 5800  CG  ARG A 707     4271   3547   3122   -199   -289   -279       C  
ATOM   5801  CD  ARG A 707      17.975  11.750  21.562  1.00 23.54           C  
ANISOU 5801  CD  ARG A 707     3588   2901   2455   -118   -316   -357       C  
ATOM   5802  NE  ARG A 707      18.801  12.930  21.826  1.00 31.56           N  
ANISOU 5802  NE  ARG A 707     4508   3968   3514   -118   -283   -393       N  
ATOM   5803  CZ  ARG A 707      18.832  13.612  22.972  1.00 31.05           C  
ANISOU 5803  CZ  ARG A 707     4419   3903   3476   -112   -288   -394       C  
ATOM   5804  NH1 ARG A 707      18.070  13.253  24.003  1.00 30.49           N  
ANISOU 5804  NH1 ARG A 707     4406   3790   3387   -101   -316   -360       N  
ATOM   5805  NH2 ARG A 707      19.635  14.661  23.090  1.00 29.33           N  
ANISOU 5805  NH2 ARG A 707     4120   3726   3297   -118   -268   -429       N  
ATOM   5806  N   TYR A 708      15.103  15.335  17.638  1.00 30.97           N  
ANISOU 5806  N   TYR A 708     4423   3883   3460   -408   -137   -163       N  
ATOM   5807  CA  TYR A 708      15.251  16.284  16.526  1.00 31.14           C  
ANISOU 5807  CA  TYR A 708     4407   3932   3495   -453    -94   -155       C  
ATOM   5808  C   TYR A 708      14.640  17.654  16.789  1.00 31.53           C  
ANISOU 5808  C   TYR A 708     4430   3975   3574   -498    -75   -117       C  
ATOM   5809  O   TYR A 708      13.767  17.814  17.648  1.00 32.01           O  
ANISOU 5809  O   TYR A 708     4508   4015   3641   -495    -92    -86       O  
ATOM   5810  CB  TYR A 708      14.677  15.707  15.219  1.00 30.67           C  
ANISOU 5810  CB  TYR A 708     4392   3860   3402   -475    -90   -128       C  
ATOM   5811  CG  TYR A 708      13.187  15.441  15.245  1.00 29.29           C  
ANISOU 5811  CG  TYR A 708     4268   3644   3218   -508   -112    -66       C  
ATOM   5812  CD1 TYR A 708      12.693  14.213  15.668  1.00 28.01           C  
ANISOU 5812  CD1 TYR A 708     4164   3447   3030   -490   -158    -53       C  
ATOM   5813  CD2 TYR A 708      12.271  16.418  14.847  1.00 25.57           C  
ANISOU 5813  CD2 TYR A 708     3785   3170   2759   -558    -91    -17       C  
ATOM   5814  CE1 TYR A 708      11.328  13.959  15.701  1.00 29.34           C  
ANISOU 5814  CE1 TYR A 708     4368   3590   3190   -531   -179     10       C  
ATOM   5815  CE2 TYR A 708      10.903  16.172  14.867  1.00 27.81           C  
ANISOU 5815  CE2 TYR A 708     4102   3432   3034   -586   -112     39       C  
ATOM   5816  CZ  TYR A 708      10.437  14.935  15.297  1.00 32.10           C  
ANISOU 5816  CZ  TYR A 708     4692   3950   3554   -577   -153     54       C  
ATOM   5817  OH  TYR A 708       9.080  14.666  15.330  1.00 33.18           O  
ANISOU 5817  OH  TYR A 708     4851   4075   3680   -616   -175    116       O  
ATOM   5818  N   ALA A 709      15.114  18.631  16.016  1.00 32.18           N  
ANISOU 5818  N   ALA A 709     4475   4080   3673   -537    -42   -120       N  
ATOM   5819  CA  ALA A 709      14.688  20.019  16.103  1.00 30.48           C  
ANISOU 5819  CA  ALA A 709     4246   3852   3483   -579    -31    -90       C  
ATOM   5820  C   ALA A 709      14.482  20.592  14.702  1.00 31.70           C  
ANISOU 5820  C   ALA A 709     4406   4010   3628   -634      0    -60       C  
ATOM   5821  O   ALA A 709      15.268  20.323  13.791  1.00 33.00           O  
ANISOU 5821  O   ALA A 709     4552   4208   3777   -645     26    -79       O  
ATOM   5822  CB  ALA A 709      15.724  20.836  16.870  1.00 30.24           C  
ANISOU 5822  CB  ALA A 709     4167   3836   3487   -576    -34   -128       C  
ATOM   5823  N   LEU A 710      13.424  21.379  14.536  1.00 31.83           N  
ANISOU 5823  N   LEU A 710     4448   3998   3647   -662     -4    -15       N  
ATOM   5824  CA  LEU A 710      13.089  21.974  13.248  1.00 32.18           C  
ANISOU 5824  CA  LEU A 710     4511   4036   3679   -712     19     17       C  
ATOM   5825  C   LEU A 710      12.600  23.402  13.413  1.00 33.04           C  
ANISOU 5825  C   LEU A 710     4631   4116   3807   -740      9     44       C  
ATOM   5826  O   LEU A 710      11.890  23.718  14.370  1.00 32.09           O  
ANISOU 5826  O   LEU A 710     4520   3977   3696   -710    -18     52       O  
ATOM   5827  CB  LEU A 710      12.013  21.154  12.535  1.00 31.75           C  
ANISOU 5827  CB  LEU A 710     4501   3970   3593   -709     11     49       C  
ATOM   5828  CG  LEU A 710      12.378  19.797  11.930  1.00 36.24           C  
ANISOU 5828  CG  LEU A 710     5084   4554   4131   -687     13     29       C  
ATOM   5829  CD1 LEU A 710      11.110  19.077  11.490  1.00 38.74           C  
ANISOU 5829  CD1 LEU A 710     5451   4844   4424   -690    -12     67       C  
ATOM   5830  CD2 LEU A 710      13.356  19.915  10.759  1.00 35.75           C  
ANISOU 5830  CD2 LEU A 710     5007   4526   4051   -706     51     11       C  
ATOM   5831  N   ASN A 711      12.989  24.263  12.478  1.00 34.46           N  
ANISOU 5831  N   ASN A 711     4814   4294   3986   -793     30     57       N  
ATOM   5832  CA  ASN A 711      12.463  25.618  12.432  1.00 35.24           C  
ANISOU 5832  CA  ASN A 711     4943   4352   4094   -822     12     86       C  
ATOM   5833  C   ASN A 711      11.245  25.672  11.505  1.00 34.67           C  
ANISOU 5833  C   ASN A 711     4921   4260   3993   -828     10    128       C  
ATOM   5834  O   ASN A 711      11.386  25.681  10.289  1.00 35.17           O  
ANISOU 5834  O   ASN A 711     5000   4329   4034   -867     35    145       O  
ATOM   5835  CB  ASN A 711      13.550  26.604  12.003  1.00 37.20           C  
ANISOU 5835  CB  ASN A 711     5178   4601   4357   -886     26     83       C  
ATOM   5836  CG  ASN A 711      13.117  28.046  12.151  1.00 38.29           C  
ANISOU 5836  CG  ASN A 711     5362   4682   4506   -912     -9    107       C  
ATOM   5837  OD1 ASN A 711      12.558  28.439  13.175  1.00 39.14           O  
ANISOU 5837  OD1 ASN A 711     5485   4759   4626   -866    -49     99       O  
ATOM   5838  ND2 ASN A 711      13.366  28.842  11.125  1.00 37.66           N  
ANISOU 5838  ND2 ASN A 711     5308   4585   4414   -982      4    137       N  
ATOM   5839  N   VAL A 712      10.053  25.700  12.100  1.00 34.45           N  
ANISOU 5839  N   VAL A 712     4911   4217   3962   -787    -20    143       N  
ATOM   5840  CA  VAL A 712       8.797  25.524  11.369  1.00 34.36           C  
ANISOU 5840  CA  VAL A 712     4932   4198   3923   -783    -28    179       C  
ATOM   5841  C   VAL A 712       8.117  26.853  11.068  1.00 36.28           C  
ANISOU 5841  C   VAL A 712     5218   4405   4161   -789    -51    203       C  
ATOM   5842  O   VAL A 712       8.005  27.717  11.941  1.00 38.08           O  
ANISOU 5842  O   VAL A 712     5451   4614   4402   -762    -80    194       O  
ATOM   5843  CB  VAL A 712       7.818  24.567  12.119  1.00 33.45           C  
ANISOU 5843  CB  VAL A 712     4803   4106   3802   -737    -46    187       C  
ATOM   5844  CG1 VAL A 712       6.496  24.438  11.389  1.00 29.92           C  
ANISOU 5844  CG1 VAL A 712     4380   3660   3330   -739    -59    226       C  
ATOM   5845  CG2 VAL A 712       8.438  23.185  12.300  1.00 28.79           C  
ANISOU 5845  CG2 VAL A 712     4191   3537   3209   -732    -33    166       C  
ATOM   5846  N   TRP A 713       7.677  26.994   9.817  1.00 36.70           N  
ANISOU 5846  N   TRP A 713     5309   4447   4190   -818    -45    231       N  
ATOM   5847  CA  TRP A 713       6.990  28.190   9.323  1.00 35.94           C  
ANISOU 5847  CA  TRP A 713     5265   4310   4079   -823    -72    255       C  
ATOM   5848  C   TRP A 713       5.495  27.952   9.170  1.00 35.34           C  
ANISOU 5848  C   TRP A 713     5200   4246   3982   -781    -98    277       C  
ATOM   5849  O   TRP A 713       4.682  28.888   9.255  1.00 34.62           O  
ANISOU 5849  O   TRP A 713     5140   4134   3879   -750   -134    287       O  
ATOM   5850  CB  TRP A 713       7.585  28.612   7.980  1.00 35.26           C  
ANISOU 5850  CB  TRP A 713     5218   4203   3975   -887    -49    273       C  
ATOM   5851  CG  TRP A 713       9.028  28.965   8.108  1.00 37.28           C  
ANISOU 5851  CG  TRP A 713     5454   4461   4251   -938    -24    257       C  
ATOM   5852  CD1 TRP A 713      10.095  28.149   7.866  1.00 36.29           C  
ANISOU 5852  CD1 TRP A 713     5281   4379   4127   -963     20    240       C  
ATOM   5853  CD2 TRP A 713       9.566  30.213   8.555  1.00 32.89           C  
ANISOU 5853  CD2 TRP A 713     4919   3863   3714   -966    -48    256       C  
ATOM   5854  NE1 TRP A 713      11.268  28.814   8.129  1.00 35.82           N  
ANISOU 5854  NE1 TRP A 713     5201   4320   4088  -1010     31    229       N  
ATOM   5855  CE2 TRP A 713      10.975  30.084   8.552  1.00 33.54           C  
ANISOU 5855  CE2 TRP A 713     4957   3975   3814  -1020    -13    241       C  
ATOM   5856  CE3 TRP A 713       8.996  31.429   8.956  1.00 35.49           C  
ANISOU 5856  CE3 TRP A 713     5305   4134   4045   -948   -103    263       C  
ATOM   5857  CZ2 TRP A 713      11.830  31.131   8.927  1.00 33.13           C  
ANISOU 5857  CZ2 TRP A 713     4911   3893   3785  -1071    -32    240       C  
ATOM   5858  CZ3 TRP A 713       9.847  32.476   9.327  1.00 38.64           C  
ANISOU 5858  CZ3 TRP A 713     5725   4491   4464   -993   -127    259       C  
ATOM   5859  CH2 TRP A 713      11.252  32.315   9.307  1.00 38.01           C  
ANISOU 5859  CH2 TRP A 713     5596   4440   4406  -1061    -91    250       C  
ATOM   5860  N   ASP A 714       5.142  26.693   8.940  1.00 32.95           N  
ANISOU 5860  N   ASP A 714     4872   3978   3671   -780    -85    284       N  
ATOM   5861  CA  ASP A 714       3.768  26.320   8.707  1.00 34.78           C  
ANISOU 5861  CA  ASP A 714     5103   4229   3883   -756   -110    309       C  
ATOM   5862  C   ASP A 714       3.528  24.906   9.202  1.00 35.89           C  
ANISOU 5862  C   ASP A 714     5201   4409   4027   -750   -106    310       C  
ATOM   5863  O   ASP A 714       4.263  23.981   8.849  1.00 33.91           O  
ANISOU 5863  O   ASP A 714     4950   4157   3776   -776    -86    299       O  
ATOM   5864  CB  ASP A 714       3.407  26.461   7.220  1.00 35.19           C  
ANISOU 5864  CB  ASP A 714     5204   4259   3908   -785   -113    331       C  
ATOM   5865  CG  ASP A 714       1.909  26.408   6.976  1.00 37.03           C  
ANISOU 5865  CG  ASP A 714     5438   4511   4122   -757   -149    356       C  
ATOM   5866  OD1 ASP A 714       1.282  25.375   7.299  1.00 38.00           O  
ANISOU 5866  OD1 ASP A 714     5521   4673   4246   -751   -157    367       O  
ATOM   5867  OD2 ASP A 714       1.358  27.398   6.456  1.00 40.06           O  
ANISOU 5867  OD2 ASP A 714     5863   4870   4488   -743   -174    367       O  
ATOM   5868  N   MET A 715       2.491  24.772  10.029  1.00 37.71           N  
ANISOU 5868  N   MET A 715     5398   4677   4255   -714   -128    325       N  
ATOM   5869  CA  MET A 715       2.121  23.522  10.668  1.00 39.78           C  
ANISOU 5869  CA  MET A 715     5620   4976   4516   -715   -131    337       C  
ATOM   5870  C   MET A 715       0.631  23.247  10.441  1.00 41.45           C  
ANISOU 5870  C   MET A 715     5812   5227   4709   -713   -160    376       C  
ATOM   5871  O   MET A 715      -0.232  23.967  10.956  1.00 40.50           O  
ANISOU 5871  O   MET A 715     5665   5143   4579   -672   -174    386       O  
ATOM   5872  CB  MET A 715       2.436  23.587  12.170  1.00 41.07           C  
ANISOU 5872  CB  MET A 715     5748   5164   4694   -678   -126    320       C  
ATOM   5873  CG  MET A 715       2.187  22.298  12.937  1.00 44.34           C  
ANISOU 5873  CG  MET A 715     6130   5613   5105   -684   -129    335       C  
ATOM   5874  SD  MET A 715       3.393  21.025  12.529  1.00 48.91           S  
ANISOU 5874  SD  MET A 715     6737   6155   5691   -721   -117    312       S  
ATOM   5875  CE  MET A 715       2.984  19.773  13.751  1.00 57.85           C  
ANISOU 5875  CE  MET A 715     7844   7321   6817   -718   -133    333       C  
ATOM   5876  N   GLU A 716       0.356  22.193   9.673  1.00 41.79           N  
ANISOU 5876  N   GLU A 716     5869   5266   4744   -755   -171    395       N  
ATOM   5877  CA  GLU A 716      -0.997  21.786   9.253  1.00 43.57           C  
ANISOU 5877  CA  GLU A 716     6077   5525   4953   -771   -204    435       C  
ATOM   5878  C   GLU A 716      -1.985  22.921   8.931  1.00 42.68           C  
ANISOU 5878  C   GLU A 716     5955   5436   4826   -736   -222    446       C  
ATOM   5879  O   GLU A 716      -3.153  22.891   9.344  1.00 42.10           O  
ANISOU 5879  O   GLU A 716     5829   5427   4741   -721   -243    474       O  
ATOM   5880  CB  GLU A 716      -1.601  20.724  10.195  1.00 43.74           C  
ANISOU 5880  CB  GLU A 716     6049   5597   4973   -789   -217    465       C  
ATOM   5881  CG  GLU A 716      -1.820  21.146  11.632  1.00 49.20           C  
ANISOU 5881  CG  GLU A 716     6685   6345   5666   -745   -203    467       C  
ATOM   5882  CD  GLU A 716      -1.912  19.967  12.606  1.00 49.83           C  
ANISOU 5882  CD  GLU A 716     6734   6457   5743   -772   -205    492       C  
ATOM   5883  OE1 GLU A 716      -1.479  20.148  13.764  1.00 48.93           O  
ANISOU 5883  OE1 GLU A 716     6599   6362   5632   -736   -185    477       O  
ATOM   5884  OE2 GLU A 716      -2.406  18.877  12.222  1.00 47.76           O  
ANISOU 5884  OE2 GLU A 716     6477   6195   5475   -829   -232    526       O  
ATOM   5885  N   GLY A 717      -1.505  23.900   8.169  1.00 39.02           N  
ANISOU 5885  N   GLY A 717     5543   4923   4359   -725   -216    426       N  
ATOM   5886  CA  GLY A 717      -2.356  24.975   7.676  1.00 39.36           C  
ANISOU 5886  CA  GLY A 717     5601   4971   4383   -689   -243    432       C  
ATOM   5887  C   GLY A 717      -2.171  26.294   8.393  1.00 38.79           C  
ANISOU 5887  C   GLY A 717     5536   4893   4311   -631   -243    410       C  
ATOM   5888  O   GLY A 717      -2.642  27.330   7.927  1.00 38.16           O  
ANISOU 5888  O   GLY A 717     5491   4796   4213   -596   -269    407       O  
ATOM   5889  N   THR A 718      -1.499  26.255   9.538  1.00 39.18           N  
ANISOU 5889  N   THR A 718     5559   4951   4378   -616   -221    392       N  
ATOM   5890  CA  THR A 718      -1.260  27.461  10.314  1.00 40.70           C  
ANISOU 5890  CA  THR A 718     5765   5131   4570   -558   -230    366       C  
ATOM   5891  C   THR A 718       0.045  28.102   9.876  1.00 39.82           C  
ANISOU 5891  C   THR A 718     5717   4939   4474   -591   -216    344       C  
ATOM   5892  O   THR A 718       1.109  27.518  10.035  1.00 41.30           O  
ANISOU 5892  O   THR A 718     5898   5111   4684   -631   -185    332       O  
ATOM   5893  CB  THR A 718      -1.217  27.161  11.819  1.00 40.46           C  
ANISOU 5893  CB  THR A 718     5676   5152   4546   -520   -219    357       C  
ATOM   5894  OG1 THR A 718      -2.323  26.319  12.162  1.00 42.17           O  
ANISOU 5894  OG1 THR A 718     5826   5452   4747   -515   -222    389       O  
ATOM   5895  CG2 THR A 718      -1.286  28.455  12.629  1.00 38.88           C  
ANISOU 5895  CG2 THR A 718     5492   4947   4334   -440   -242    330       C  
ATOM   5896  N   ARG A 719      -0.047  29.293   9.305  1.00 41.12           N  
ANISOU 5896  N   ARG A 719     5943   5056   4624   -575   -243    340       N  
ATOM   5897  CA  ARG A 719       1.139  30.051   8.931  1.00 42.48           C  
ANISOU 5897  CA  ARG A 719     6178   5156   4809   -615   -235    326       C  
ATOM   5898  C   ARG A 719       1.496  30.966  10.086  1.00 42.70           C  
ANISOU 5898  C   ARG A 719     6214   5165   4847   -569   -258    299       C  
ATOM   5899  O   ARG A 719       0.733  31.876  10.414  1.00 45.54           O  
ANISOU 5899  O   ARG A 719     6599   5519   5184   -501   -303    292       O  
ATOM   5900  CB  ARG A 719       0.889  30.870   7.655  1.00 42.97           C  
ANISOU 5900  CB  ARG A 719     6318   5164   4845   -633   -258    343       C  
ATOM   5901  CG  ARG A 719       2.136  31.578   7.100  1.00 42.02           C  
ANISOU 5901  CG  ARG A 719     6260   4973   4731   -698   -245    342       C  
ATOM   5902  CD  ARG A 719       3.186  30.573   6.603  1.00 40.63           C  
ANISOU 5902  CD  ARG A 719     6055   4812   4569   -770   -187    345       C  
ATOM   5903  NE  ARG A 719       2.626  29.635   5.637  1.00 39.71           N  
ANISOU 5903  NE  ARG A 719     5933   4722   4433   -783   -174    363       N  
ATOM   5904  CZ  ARG A 719       2.531  29.877   4.331  1.00 42.46           C  
ANISOU 5904  CZ  ARG A 719     6340   5041   4751   -814   -175    384       C  
ATOM   5905  NH1 ARG A 719       2.967  31.032   3.837  1.00 40.30           N  
ANISOU 5905  NH1 ARG A 719     6136   4711   4464   -842   -184    394       N  
ATOM   5906  NH2 ARG A 719       2.002  28.965   3.521  1.00 33.80           N  
ANISOU 5906  NH2 ARG A 719     5239   3966   3636   -819   -170    396       N  
ATOM   5907  N   TYR A 720       2.647  30.723  10.706  1.00 42.90           N  
ANISOU 5907  N   TYR A 720     6219   5179   4901   -600   -232    281       N  
ATOM   5908  CA  TYR A 720       3.032  31.464  11.905  1.00 43.69           C  
ANISOU 5908  CA  TYR A 720     6324   5263   5013   -555   -257    251       C  
ATOM   5909  C   TYR A 720       3.490  32.872  11.563  1.00 45.81           C  
ANISOU 5909  C   TYR A 720     6678   5448   5279   -570   -297    246       C  
ATOM   5910  O   TYR A 720       4.097  33.090  10.516  1.00 47.00           O  
ANISOU 5910  O   TYR A 720     6870   5556   5433   -646   -284    263       O  
ATOM   5911  CB  TYR A 720       4.144  30.739  12.664  1.00 43.25           C  
ANISOU 5911  CB  TYR A 720     6219   5222   4990   -583   -223    231       C  
ATOM   5912  CG  TYR A 720       3.758  29.388  13.202  1.00 43.77           C  
ANISOU 5912  CG  TYR A 720     6215   5359   5056   -566   -194    236       C  
ATOM   5913  CD1 TYR A 720       2.792  29.256  14.203  1.00 44.42           C  
ANISOU 5913  CD1 TYR A 720     6260   5496   5121   -492   -209    237       C  
ATOM   5914  CD2 TYR A 720       4.364  28.236  12.716  1.00 43.94           C  
ANISOU 5914  CD2 TYR A 720     6210   5394   5090   -622   -154    242       C  
ATOM   5915  CE1 TYR A 720       2.434  28.003  14.690  1.00 45.30           C  
ANISOU 5915  CE1 TYR A 720     6312   5670   5229   -490   -185    251       C  
ATOM   5916  CE2 TYR A 720       4.018  26.988  13.196  1.00 45.41           C  
ANISOU 5916  CE2 TYR A 720     6347   5631   5274   -612   -139    249       C  
ATOM   5917  CZ  TYR A 720       3.056  26.874  14.178  1.00 46.01           C  
ANISOU 5917  CZ  TYR A 720     6389   5757   5335   -554   -154    258       C  
ATOM   5918  OH  TYR A 720       2.728  25.621  14.645  1.00 49.68           O  
ANISOU 5918  OH  TYR A 720     6811   6270   5795   -558   -140    273       O  
ATOM   5919  N   ALA A 721       3.188  33.826  12.440  1.00 46.32           N  
ANISOU 5919  N   ALA A 721     6776   5491   5334   -498   -350    223       N  
ATOM   5920  CA  ALA A 721       3.723  35.180  12.298  1.00 48.82           C  
ANISOU 5920  CA  ALA A 721     7185   5713   5650   -515   -403    215       C  
ATOM   5921  C   ALA A 721       5.221  35.143  12.594  1.00 48.86           C  
ANISOU 5921  C   ALA A 721     7178   5689   5697   -595   -382    204       C  
ATOM   5922  O   ALA A 721       6.012  35.822  11.943  1.00 50.10           O  
ANISOU 5922  O   ALA A 721     7391   5781   5862   -675   -393    218       O  
ATOM   5923  CB  ALA A 721       3.004  36.151  13.236  1.00 48.84           C  
ANISOU 5923  CB  ALA A 721     7231   5700   5626   -402   -474    186       C  
ATOM   5924  N   GLU A 722       5.593  34.330  13.580  1.00 48.20           N  
ANISOU 5924  N   GLU A 722     7020   5659   5636   -574   -353    182       N  
ATOM   5925  CA  GLU A 722       6.989  34.100  13.928  1.00 49.33           C  
ANISOU 5925  CA  GLU A 722     7132   5792   5818   -639   -330    166       C  
ATOM   5926  C   GLU A 722       7.296  32.611  13.820  1.00 46.93           C  
ANISOU 5926  C   GLU A 722     6742   5561   5528   -665   -261    169       C  
ATOM   5927  O   GLU A 722       6.484  31.784  14.241  1.00 45.33           O  
ANISOU 5927  O   GLU A 722     6496   5415   5311   -608   -246    170       O  
ATOM   5928  CB  GLU A 722       7.281  34.584  15.354  1.00 51.54           C  
ANISOU 5928  CB  GLU A 722     7416   6056   6112   -579   -376    127       C  
ATOM   5929  CG  GLU A 722       7.004  36.067  15.608  1.00 58.10           C  
ANISOU 5929  CG  GLU A 722     8343   6805   6925   -539   -460    115       C  
ATOM   5930  CD  GLU A 722       7.965  36.994  14.880  1.00 66.45           C  
ANISOU 5930  CD  GLU A 722     9469   7777   8001   -645   -487    132       C  
ATOM   5931  OE1 GLU A 722       9.004  36.511  14.374  1.00 70.89           O  
ANISOU 5931  OE1 GLU A 722     9987   8355   8593   -746   -437    146       O  
ATOM   5932  OE2 GLU A 722       7.682  38.213  14.816  1.00 70.16           O  
ANISOU 5932  OE2 GLU A 722    10040   8166   8453   -626   -562    131       O  
ATOM   5933  N   PRO A 723       8.475  32.259  13.274  1.00 45.18           N  
ANISOU 5933  N   PRO A 723     6497   5341   5329   -750   -222    171       N  
ATOM   5934  CA  PRO A 723       8.830  30.841  13.154  1.00 42.97           C  
ANISOU 5934  CA  PRO A 723     6147   5124   5056   -763   -166    167       C  
ATOM   5935  C   PRO A 723       8.753  30.139  14.514  1.00 43.21           C  
ANISOU 5935  C   PRO A 723     6128   5193   5097   -696   -169    138       C  
ATOM   5936  O   PRO A 723       9.031  30.754  15.549  1.00 40.80           O  
ANISOU 5936  O   PRO A 723     5829   4866   4805   -662   -205    112       O  
ATOM   5937  CB  PRO A 723      10.276  30.881  12.654  1.00 41.63           C  
ANISOU 5937  CB  PRO A 723     5957   4952   4907   -848   -136    162       C  
ATOM   5938  CG  PRO A 723      10.785  32.230  13.083  1.00 46.89           C  
ANISOU 5938  CG  PRO A 723     6667   5558   5592   -873   -185    155       C  
ATOM   5939  CD  PRO A 723       9.604  33.140  12.934  1.00 45.96           C  
ANISOU 5939  CD  PRO A 723     6626   5389   5447   -831   -234    174       C  
ATOM   5940  N   LYS A 724       8.361  28.870  14.512  1.00 42.08           N  
ANISOU 5940  N   LYS A 724     5944   5100   4944   -678   -138    144       N  
ATOM   5941  CA  LYS A 724       8.180  28.145  15.758  1.00 43.65           C  
ANISOU 5941  CA  LYS A 724     6105   5337   5145   -619   -141    126       C  
ATOM   5942  C   LYS A 724       9.108  26.937  15.804  1.00 42.69           C  
ANISOU 5942  C   LYS A 724     5941   5243   5037   -643   -108    108       C  
ATOM   5943  O   LYS A 724       9.228  26.195  14.821  1.00 42.27           O  
ANISOU 5943  O   LYS A 724     5883   5203   4975   -681    -80    121       O  
ATOM   5944  CB  LYS A 724       6.710  27.742  15.930  1.00 44.32           C  
ANISOU 5944  CB  LYS A 724     6183   5457   5198   -570   -147    153       C  
ATOM   5945  CG  LYS A 724       6.344  27.142  17.293  1.00 51.14           C  
ANISOU 5945  CG  LYS A 724     7011   6365   6053   -508   -152    145       C  
ATOM   5946  CD  LYS A 724       4.825  27.168  17.526  1.00 56.19           C  
ANISOU 5946  CD  LYS A 724     7640   7051   6657   -457   -164    175       C  
ATOM   5947  CE  LYS A 724       4.356  26.076  18.494  1.00 59.24           C  
ANISOU 5947  CE  LYS A 724     7982   7499   7027   -428   -151    189       C  
ATOM   5948  NZ  LYS A 724       4.743  26.348  19.907  1.00 59.98           N  
ANISOU 5948  NZ  LYS A 724     8068   7602   7119   -367   -164    158       N  
ATOM   5949  N   LEU A 725       9.774  26.750  16.941  1.00 39.87           N  
ANISOU 5949  N   LEU A 725     5558   4893   4696   -612   -118     74       N  
ATOM   5950  CA  LEU A 725      10.649  25.597  17.114  1.00 38.53           C  
ANISOU 5950  CA  LEU A 725     5354   4751   4536   -617    -96     50       C  
ATOM   5951  C   LEU A 725       9.856  24.332  17.417  1.00 37.32           C  
ANISOU 5951  C   LEU A 725     5194   4628   4358   -586    -90     67       C  
ATOM   5952  O   LEU A 725       9.131  24.264  18.407  1.00 38.53           O  
ANISOU 5952  O   LEU A 725     5345   4795   4498   -538   -107     76       O  
ATOM   5953  CB  LEU A 725      11.688  25.851  18.210  1.00 38.52           C  
ANISOU 5953  CB  LEU A 725     5331   4745   4561   -595   -114      5       C  
ATOM   5954  CG  LEU A 725      12.700  26.985  18.004  1.00 37.36           C  
ANISOU 5954  CG  LEU A 725     5183   4570   4443   -641   -126    -14       C  
ATOM   5955  CD1 LEU A 725      13.644  27.072  19.183  1.00 36.95           C  
ANISOU 5955  CD1 LEU A 725     5106   4519   4417   -613   -152    -60       C  
ATOM   5956  CD2 LEU A 725      13.484  26.821  16.715  1.00 38.65           C  
ANISOU 5956  CD2 LEU A 725     5327   4748   4609   -713    -89     -7       C  
ATOM   5957  N   LYS A 726       9.967  23.343  16.539  1.00 35.50           N  
ANISOU 5957  N   LYS A 726     4964   4408   4117   -615    -69     76       N  
ATOM   5958  CA  LYS A 726       9.459  22.022  16.841  1.00 35.02           C  
ANISOU 5958  CA  LYS A 726     4905   4366   4036   -597    -73     89       C  
ATOM   5959  C   LYS A 726      10.628  21.171  17.325  1.00 35.17           C  
ANISOU 5959  C   LYS A 726     4911   4390   4062   -578    -73     46       C  
ATOM   5960  O   LYS A 726      11.495  20.788  16.536  1.00 36.36           O  
ANISOU 5960  O   LYS A 726     5058   4544   4214   -597    -58     23       O  
ATOM   5961  CB  LYS A 726       8.788  21.384  15.626  1.00 34.86           C  
ANISOU 5961  CB  LYS A 726     4908   4345   3994   -632    -66    123       C  
ATOM   5962  CG  LYS A 726       8.088  20.053  15.957  1.00 37.57           C  
ANISOU 5962  CG  LYS A 726     5263   4698   4315   -625    -83    147       C  
ATOM   5963  CD  LYS A 726       7.495  19.389  14.718  1.00 41.09           C  
ANISOU 5963  CD  LYS A 726     5737   5136   4741   -663    -87    176       C  
ATOM   5964  CE  LYS A 726       7.065  17.937  14.981  1.00 45.04           C  
ANISOU 5964  CE  LYS A 726     6261   5633   5221   -667   -114    195       C  
ATOM   5965  NZ  LYS A 726       5.999  17.815  16.027  1.00 45.73           N  
ANISOU 5965  NZ  LYS A 726     6331   5747   5299   -663   -129    236       N  
ATOM   5966  N   ILE A 727      10.661  20.904  18.627  1.00 33.44           N  
ANISOU 5966  N   ILE A 727     4686   4178   3844   -534    -91     33       N  
ATOM   5967  CA  ILE A 727      11.719  20.100  19.219  1.00 32.46           C  
ANISOU 5967  CA  ILE A 727     4553   4056   3723   -505   -100    -11       C  
ATOM   5968  C   ILE A 727      11.140  18.846  19.845  1.00 34.02           C  
ANISOU 5968  C   ILE A 727     4778   4255   3892   -483   -119      9       C  
ATOM   5969  O   ILE A 727      10.271  18.928  20.713  1.00 36.28           O  
ANISOU 5969  O   ILE A 727     5068   4552   4165   -465   -128     39       O  
ATOM   5970  CB  ILE A 727      12.498  20.881  20.289  1.00 32.59           C  
ANISOU 5970  CB  ILE A 727     4545   4072   3764   -472   -113    -51       C  
ATOM   5971  CG1 ILE A 727      13.038  22.194  19.703  1.00 30.08           C  
ANISOU 5971  CG1 ILE A 727     4208   3745   3475   -509   -103    -63       C  
ATOM   5972  CG2 ILE A 727      13.628  20.011  20.866  1.00 29.25           C  
ANISOU 5972  CG2 ILE A 727     4113   3657   3344   -436   -126   -101       C  
ATOM   5973  CD1 ILE A 727      13.460  23.200  20.739  1.00 27.76           C  
ANISOU 5973  CD1 ILE A 727     3903   3439   3204   -483   -129    -91       C  
ATOM   5974  N   MET A 728      11.619  17.686  19.409  1.00 31.60           N  
ANISOU 5974  N   MET A 728     4495   3941   3572   -482   -127     -7       N  
ATOM   5975  CA  MET A 728      11.157  16.438  19.991  1.00 31.57           C  
ANISOU 5975  CA  MET A 728     4531   3925   3538   -469   -156     14       C  
ATOM   5976  C   MET A 728      12.292  15.683  20.665  1.00 31.41           C  
ANISOU 5976  C   MET A 728     4523   3897   3515   -418   -179    -41       C  
ATOM   5977  O   MET A 728      13.375  15.540  20.095  1.00 31.82           O  
ANISOU 5977  O   MET A 728     4564   3953   3574   -403   -175    -91       O  
ATOM   5978  CB  MET A 728      10.470  15.552  18.938  1.00 33.18           C  
ANISOU 5978  CB  MET A 728     4776   4113   3719   -509   -166     50       C  
ATOM   5979  CG  MET A 728       9.246  16.183  18.222  1.00 38.46           C  
ANISOU 5979  CG  MET A 728     5434   4792   4388   -557   -151    105       C  
ATOM   5980  SD  MET A 728       8.023  17.066  19.247  1.00 47.78           S  
ANISOU 5980  SD  MET A 728     6580   6008   5567   -554   -143    153       S  
ATOM   5981  CE  MET A 728       7.448  15.782  20.343  1.00 37.15           C  
ANISOU 5981  CE  MET A 728     5261   4665   4187   -553   -173    191       C  
ATOM   5982  N   GLY A 729      12.047  15.216  21.886  1.00 29.48           N  
ANISOU 5982  N   GLY A 729     4300   3646   3253   -389   -203    -31       N  
ATOM   5983  CA  GLY A 729      12.945  14.259  22.530  1.00 28.74           C  
ANISOU 5983  CA  GLY A 729     4239   3536   3146   -339   -236    -75       C  
ATOM   5984  C   GLY A 729      14.174  14.834  23.200  1.00 28.88           C  
ANISOU 5984  C   GLY A 729     4215   3568   3188   -287   -237   -142       C  
ATOM   5985  O   GLY A 729      14.675  14.262  24.157  1.00 30.46           O  
ANISOU 5985  O   GLY A 729     4439   3758   3376   -236   -268   -171       O  
ATOM   5986  N   LEU A 730      14.649  15.970  22.705  1.00 29.33           N  
ANISOU 5986  N   LEU A 730     4216   3648   3281   -303   -208   -165       N  
ATOM   5987  CA  LEU A 730      15.840  16.613  23.239  1.00 28.60           C  
ANISOU 5987  CA  LEU A 730     4077   3573   3218   -269   -212   -226       C  
ATOM   5988  C   LEU A 730      15.581  17.187  24.612  1.00 31.26           C  
ANISOU 5988  C   LEU A 730     4413   3904   3559   -236   -229   -223       C  
ATOM   5989  O   LEU A 730      14.423  17.350  25.039  1.00 30.15           O  
ANISOU 5989  O   LEU A 730     4295   3759   3400   -245   -225   -170       O  
ATOM   5990  CB  LEU A 730      16.337  17.722  22.304  1.00 29.36           C  
ANISOU 5990  CB  LEU A 730     4116   3691   3348   -313   -179   -238       C  
ATOM   5991  CG  LEU A 730      16.477  17.402  20.815  1.00 26.09           C  
ANISOU 5991  CG  LEU A 730     3698   3292   2925   -350   -152   -232       C  
ATOM   5992  CD1 LEU A 730      17.102  18.601  20.110  1.00 23.88           C  
ANISOU 5992  CD1 LEU A 730     3359   3037   2676   -396   -121   -243       C  
ATOM   5993  CD2 LEU A 730      17.303  16.141  20.599  1.00 25.75           C  
ANISOU 5993  CD2 LEU A 730     3668   3259   2856   -302   -170   -279       C  
ATOM   5994  N   GLU A 731      16.678  17.518  25.288  1.00 30.04           N  
ANISOU 5994  N   GLU A 731     4229   3757   3426   -196   -248   -283       N  
ATOM   5995  CA  GLU A 731      16.656  17.827  26.702  1.00 30.36           C  
ANISOU 5995  CA  GLU A 731     4281   3790   3464   -146   -276   -295       C  
ATOM   5996  C   GLU A 731      15.765  19.018  27.082  1.00 31.20           C  
ANISOU 5996  C   GLU A 731     4383   3895   3577   -158   -266   -259       C  
ATOM   5997  O   GLU A 731      15.347  19.139  28.232  1.00 31.56           O  
ANISOU 5997  O   GLU A 731     4451   3938   3601   -112   -284   -252       O  
ATOM   5998  CB  GLU A 731      18.087  17.981  27.212  1.00 31.85           C  
ANISOU 5998  CB  GLU A 731     4434   3989   3680   -104   -304   -371       C  
ATOM   5999  CG  GLU A 731      18.740  16.631  27.555  1.00 34.72           C  
ANISOU 5999  CG  GLU A 731     4826   4350   4016    -47   -334   -410       C  
ATOM   6000  CD  GLU A 731      19.274  15.856  26.343  1.00 37.80           C  
ANISOU 6000  CD  GLU A 731     5205   4757   4400    -61   -322   -429       C  
ATOM   6001  OE1 GLU A 731      19.189  16.345  25.189  1.00 33.45           O  
ANISOU 6001  OE1 GLU A 731     4619   4224   3865   -119   -284   -411       O  
ATOM   6002  OE2 GLU A 731      19.801  14.741  26.558  1.00 39.60           O  
ANISOU 6002  OE2 GLU A 731     5466   4979   4600     -6   -354   -464       O  
ATOM   6003  N   THR A 732      15.454  19.869  26.107  1.00 29.32           N  
ANISOU 6003  N   THR A 732     4122   3659   3360   -214   -240   -237       N  
ATOM   6004  CA  THR A 732      14.569  21.005  26.318  1.00 29.47           C  
ANISOU 6004  CA  THR A 732     4145   3673   3379   -219   -237   -205       C  
ATOM   6005  C   THR A 732      13.136  20.572  26.569  1.00 30.76           C  
ANISOU 6005  C   THR A 732     4338   3851   3499   -210   -224   -143       C  
ATOM   6006  O   THR A 732      12.336  21.359  27.061  1.00 33.27           O  
ANISOU 6006  O   THR A 732     4661   4178   3803   -187   -226   -121       O  
ATOM   6007  CB  THR A 732      14.555  21.950  25.091  1.00 30.22           C  
ANISOU 6007  CB  THR A 732     4220   3762   3503   -284   -216   -192       C  
ATOM   6008  OG1 THR A 732      14.170  21.214  23.925  1.00 33.22           O  
ANISOU 6008  OG1 THR A 732     4602   4149   3869   -328   -185   -159       O  
ATOM   6009  CG2 THR A 732      15.912  22.549  24.860  1.00 29.08           C  
ANISOU 6009  CG2 THR A 732     4036   3612   3399   -307   -227   -242       C  
ATOM   6010  N   GLN A 733      12.807  19.330  26.215  1.00 31.75           N  
ANISOU 6010  N   GLN A 733     4483   3981   3600   -229   -214   -115       N  
ATOM   6011  CA  GLN A 733      11.432  18.831  26.315  1.00 32.43           C  
ANISOU 6011  CA  GLN A 733     4589   4087   3645   -241   -202    -47       C  
ATOM   6012  C   GLN A 733      11.201  17.959  27.542  1.00 33.70           C  
ANISOU 6012  C   GLN A 733     4780   4258   3765   -201   -220    -33       C  
ATOM   6013  O   GLN A 733      10.070  17.562  27.812  1.00 35.70           O  
ANISOU 6013  O   GLN A 733     5044   4540   3981   -214   -210     28       O  
ATOM   6014  CB  GLN A 733      11.046  18.045  25.052  1.00 34.15           C  
ANISOU 6014  CB  GLN A 733     4818   4299   3859   -303   -188    -13       C  
ATOM   6015  CG  GLN A 733      11.364  18.754  23.739  1.00 34.53           C  
ANISOU 6015  CG  GLN A 733     4843   4337   3939   -346   -169    -26       C  
ATOM   6016  CD  GLN A 733      10.831  20.170  23.707  1.00 37.44           C  
ANISOU 6016  CD  GLN A 733     5191   4714   4320   -346   -160    -14       C  
ATOM   6017  OE1 GLN A 733      11.587  21.130  23.868  1.00 36.71           O  
ANISOU 6017  OE1 GLN A 733     5083   4609   4257   -334   -167    -54       O  
ATOM   6018  NE2 GLN A 733       9.519  20.309  23.524  1.00 35.40           N  
ANISOU 6018  NE2 GLN A 733     4934   4478   4038   -360   -149     41       N  
ATOM   6019  N   LYS A 734      12.272  17.673  28.278  1.00 35.96           N  
ANISOU 6019  N   LYS A 734     5079   4526   4057   -154   -246    -87       N  
ATOM   6020  CA  LYS A 734      12.231  16.763  29.422  1.00 36.95           C  
ANISOU 6020  CA  LYS A 734     5246   4652   4142   -113   -269    -79       C  
ATOM   6021  C   LYS A 734      11.993  17.516  30.722  1.00 36.47           C  
ANISOU 6021  C   LYS A 734     5181   4615   4061    -50   -275    -84       C  
ATOM   6022  O   LYS A 734      12.641  18.526  30.985  1.00 38.79           O  
ANISOU 6022  O   LYS A 734     5453   4901   4386    -14   -287   -136       O  
ATOM   6023  CB  LYS A 734      13.542  15.979  29.523  1.00 38.45           C  
ANISOU 6023  CB  LYS A 734     5458   4808   4343    -83   -302   -140       C  
ATOM   6024  CG  LYS A 734      13.807  15.033  28.360  1.00 41.84           C  
ANISOU 6024  CG  LYS A 734     5905   5216   4776   -125   -304   -141       C  
ATOM   6025  CD  LYS A 734      15.273  14.582  28.325  1.00 48.17           C  
ANISOU 6025  CD  LYS A 734     6708   6000   5594    -80   -334   -220       C  
ATOM   6026  CE  LYS A 734      15.516  13.292  29.099  1.00 50.48           C  
ANISOU 6026  CE  LYS A 734     7072   6264   5845    -35   -378   -228       C  
ATOM   6027  NZ  LYS A 734      15.029  12.104  28.339  1.00 52.26           N  
ANISOU 6027  NZ  LYS A 734     7357   6461   6040    -75   -391   -189       N  
ATOM   6028  N   SER A 735      11.073  17.013  31.542  1.00 35.44           N  
ANISOU 6028  N   SER A 735     5075   4516   3876    -37   -269    -29       N  
ATOM   6029  CA  SER A 735      10.768  17.634  32.829  1.00 34.21           C  
ANISOU 6029  CA  SER A 735     4920   4393   3686     34   -273    -31       C  
ATOM   6030  C   SER A 735      11.917  17.473  33.828  1.00 35.19           C  
ANISOU 6030  C   SER A 735     5074   4486   3812    103   -313    -96       C  
ATOM   6031  O   SER A 735      12.004  18.206  34.810  1.00 33.12           O  
ANISOU 6031  O   SER A 735     4812   4237   3534    172   -327   -122       O  
ATOM   6032  CB  SER A 735       9.475  17.060  33.403  1.00 35.41           C  
ANISOU 6032  CB  SER A 735     5082   4603   3771     23   -250     53       C  
ATOM   6033  OG  SER A 735       9.596  15.671  33.634  1.00 33.30           O  
ANISOU 6033  OG  SER A 735     4864   4313   3474     -5   -266     80       O  
ATOM   6034  N   SER A 736      12.792  16.509  33.558  1.00 34.38           N  
ANISOU 6034  N   SER A 736     4998   4342   3722     90   -337   -125       N  
ATOM   6035  CA  SER A 736      13.981  16.247  34.369  1.00 32.59           C  
ANISOU 6035  CA  SER A 736     4797   4085   3500    155   -381   -193       C  
ATOM   6036  C   SER A 736      15.105  17.276  34.187  1.00 31.87           C  
ANISOU 6036  C   SER A 736     4662   3978   3470    179   -401   -274       C  
ATOM   6037  O   SER A 736      15.991  17.386  35.027  1.00 28.77           O  
ANISOU 6037  O   SER A 736     4278   3570   3082    242   -441   -333       O  
ATOM   6038  CB  SER A 736      14.525  14.871  34.015  1.00 33.76           C  
ANISOU 6038  CB  SER A 736     4989   4198   3640    139   -405   -201       C  
ATOM   6039  OG  SER A 736      14.614  14.746  32.609  1.00 34.69           O  
ANISOU 6039  OG  SER A 736     5080   4306   3794     76   -387   -199       O  
ATOM   6040  N   THR A 737      15.084  18.004  33.077  1.00 31.12           N  
ANISOU 6040  N   THR A 737     4520   3885   3421    124   -377   -274       N  
ATOM   6041  CA  THR A 737      16.107  18.995  32.797  1.00 30.04           C  
ANISOU 6041  CA  THR A 737     4339   3735   3342    125   -395   -338       C  
ATOM   6042  C   THR A 737      15.796  20.284  33.548  1.00 32.05           C  
ANISOU 6042  C   THR A 737     4591   3991   3596    164   -410   -347       C  
ATOM   6043  O   THR A 737      14.646  20.737  33.532  1.00 32.44           O  
ANISOU 6043  O   THR A 737     4646   4060   3618    160   -385   -296       O  
ATOM   6044  CB  THR A 737      16.169  19.272  31.295  1.00 30.31           C  
ANISOU 6044  CB  THR A 737     4332   3769   3415     46   -364   -327       C  
ATOM   6045  OG1 THR A 737      16.408  18.040  30.606  1.00 28.58           O  
ANISOU 6045  OG1 THR A 737     4124   3548   3187     21   -355   -322       O  
ATOM   6046  CG2 THR A 737      17.285  20.258  30.952  1.00 30.18           C  
ANISOU 6046  CG2 THR A 737     4266   3744   3456     29   -382   -385       C  
ATOM   6047  N   PRO A 738      16.813  20.879  34.214  1.00 26.48           N  
ANISOU 6047  N   PRO A 738     3452   3588   3019    163    -24   -269       N  
ATOM   6048  CA  PRO A 738      16.624  22.138  34.943  1.00 26.70           C  
ANISOU 6048  CA  PRO A 738     3458   3628   3058    210    -51   -314       C  
ATOM   6049  C   PRO A 738      15.937  23.194  34.086  1.00 28.62           C  
ANISOU 6049  C   PRO A 738     3715   3823   3337    180    -67   -302       C  
ATOM   6050  O   PRO A 738      16.158  23.254  32.870  1.00 28.37           O  
ANISOU 6050  O   PRO A 738     3708   3744   3328    116    -63   -280       O  
ATOM   6051  CB  PRO A 738      18.052  22.576  35.268  1.00 26.37           C  
ANISOU 6051  CB  PRO A 738     3406   3580   3033    215    -60   -382       C  
ATOM   6052  CG  PRO A 738      18.825  21.324  35.350  1.00 27.10           C  
ANISOU 6052  CG  PRO A 738     3497   3697   3101    213    -34   -364       C  
ATOM   6053  CD  PRO A 738      18.185  20.362  34.367  1.00 25.04           C  
ANISOU 6053  CD  PRO A 738     3268   3408   2836    166     -9   -298       C  
ATOM   6054  N   LYS A 739      15.099  24.010  34.713  1.00 31.34           N  
ANISOU 6054  N   LYS A 739     4041   4182   3683    230    -82   -313       N  
ATOM   6055  CA  LYS A 739      14.362  25.045  33.985  1.00 35.27           C  
ANISOU 6055  CA  LYS A 739     4549   4635   4219    216    -94   -292       C  
ATOM   6056  C   LYS A 739      15.270  25.991  33.206  1.00 34.30           C  
ANISOU 6056  C   LYS A 739     4444   4435   4153    173   -104   -323       C  
ATOM   6057  O   LYS A 739      15.035  26.237  32.030  1.00 33.86           O  
ANISOU 6057  O   LYS A 739     4405   4342   4120    122   -103   -275       O  
ATOM   6058  CB  LYS A 739      13.423  25.824  34.916  1.00 36.69           C  
ANISOU 6058  CB  LYS A 739     4706   4841   4394    294   -104   -308       C  
ATOM   6059  CG  LYS A 739      12.069  25.155  35.100  1.00 46.16           C  
ANISOU 6059  CG  LYS A 739     5883   6104   5551    318    -93   -236       C  
ATOM   6060  CD  LYS A 739      11.306  25.058  33.767  1.00 51.54           C  
ANISOU 6060  CD  LYS A 739     6574   6762   6246    256    -94   -157       C  
ATOM   6061  CE  LYS A 739      10.302  23.900  33.756  1.00 55.95           C  
ANISOU 6061  CE  LYS A 739     7113   7385   6760    241    -83    -84       C  
ATOM   6062  NZ  LYS A 739       9.042  24.219  34.506  1.00 60.89           N  
ANISOU 6062  NZ  LYS A 739     7697   8070   7366    310    -82    -51       N  
ATOM   6063  N   ALA A 740      16.308  26.504  33.863  1.00 34.98           N  
ANISOU 6063  N   ALA A 740     4524   4507   4261    189   -115   -399       N  
ATOM   6064  CA  ALA A 740      17.235  27.435  33.228  1.00 37.03           C  
ANISOU 6064  CA  ALA A 740     4794   4694   4583    143   -125   -428       C  
ATOM   6065  C   ALA A 740      18.000  26.782  32.083  1.00 35.40           C  
ANISOU 6065  C   ALA A 740     4601   4473   4376     71   -107   -389       C  
ATOM   6066  O   ALA A 740      18.291  27.427  31.086  1.00 39.33           O  
ANISOU 6066  O   ALA A 740     5110   4916   4917     23   -106   -366       O  
ATOM   6067  CB  ALA A 740      18.197  28.031  34.258  1.00 38.98           C  
ANISOU 6067  CB  ALA A 740     5023   4938   4849    170   -144   -524       C  
ATOM   6068  N   VAL A 741      18.303  25.499  32.233  1.00 34.70           N  
ANISOU 6068  N   VAL A 741     4512   4436   4237     70    -89   -378       N  
ATOM   6069  CA  VAL A 741      18.979  24.720  31.202  1.00 32.60           C  
ANISOU 6069  CA  VAL A 741     4262   4163   3961     12    -66   -347       C  
ATOM   6070  C   VAL A 741      18.079  24.474  29.983  1.00 32.74           C  
ANISOU 6070  C   VAL A 741     4304   4169   3966    -31    -56   -277       C  
ATOM   6071  O   VAL A 741      18.547  24.583  28.855  1.00 32.17           O  
ANISOU 6071  O   VAL A 741     4247   4072   3905    -84    -46   -255       O  
ATOM   6072  CB  VAL A 741      19.529  23.386  31.767  1.00 33.15           C  
ANISOU 6072  CB  VAL A 741     4326   4283   3987     33    -45   -355       C  
ATOM   6073  CG1 VAL A 741      20.161  22.571  30.681  1.00 31.03           C  
ANISOU 6073  CG1 VAL A 741     4080   4002   3709    -18    -16   -328       C  
ATOM   6074  CG2 VAL A 741      20.551  23.660  32.865  1.00 34.06           C  
ANISOU 6074  CG2 VAL A 741     4409   4424   4108     71    -58   -420       C  
ATOM   6075  N   GLN A 742      16.798  24.162  30.208  1.00 31.35           N  
ANISOU 6075  N   GLN A 742     4127   4021   3762    -10    -61   -242       N  
ATOM   6076  CA  GLN A 742      15.846  23.999  29.107  1.00 32.37           C  
ANISOU 6076  CA  GLN A 742     4272   4152   3876    -53    -61   -178       C  
ATOM   6077  C   GLN A 742      15.806  25.287  28.301  1.00 33.82           C  
ANISOU 6077  C   GLN A 742     4456   4292   4103    -73    -73   -156       C  
ATOM   6078  O   GLN A 742      15.816  25.261  27.070  1.00 33.82           O  
ANISOU 6078  O   GLN A 742     4470   4285   4093   -127    -67   -114       O  
ATOM   6079  CB  GLN A 742      14.420  23.706  29.593  1.00 32.06           C  
ANISOU 6079  CB  GLN A 742     4218   4155   3810    -22    -69   -140       C  
ATOM   6080  CG  GLN A 742      14.217  22.525  30.535  1.00 32.14           C  
ANISOU 6080  CG  GLN A 742     4218   4209   3783      6    -57   -145       C  
ATOM   6081  CD  GLN A 742      12.761  22.404  30.995  1.00 33.88           C  
ANISOU 6081  CD  GLN A 742     4415   4477   3983     35    -65    -98       C  
ATOM   6082  OE1 GLN A 742      12.030  23.391  31.055  1.00 32.75           O  
ANISOU 6082  OE1 GLN A 742     4253   4335   3855     64    -81    -83       O  
ATOM   6083  NE2 GLN A 742      12.340  21.190  31.313  1.00 34.82           N  
ANISOU 6083  NE2 GLN A 742     4530   4631   4071     28    -52    -71       N  
ATOM   6084  N   LYS A 743      15.759  26.411  29.015  1.00 34.76           N  
ANISOU 6084  N   LYS A 743     4560   4381   4268    -28    -89   -185       N  
ATOM   6085  CA  LYS A 743      15.672  27.736  28.403  1.00 35.85           C  
ANISOU 6085  CA  LYS A 743     4698   4462   4463    -37    -98   -162       C  
ATOM   6086  C   LYS A 743      16.925  28.028  27.578  1.00 35.73           C  
ANISOU 6086  C   LYS A 743     4691   4406   4479    -94    -88   -165       C  
ATOM   6087  O   LYS A 743      16.830  28.420  26.407  1.00 35.84           O  
ANISOU 6087  O   LYS A 743     4712   4403   4503   -135    -83   -105       O  
ATOM   6088  CB  LYS A 743      15.453  28.797  29.488  1.00 37.17           C  
ANISOU 6088  CB  LYS A 743     4852   4594   4678     28   -114   -211       C  
ATOM   6089  CG  LYS A 743      15.126  30.206  28.993  1.00 41.94           C  
ANISOU 6089  CG  LYS A 743     5458   5126   5352     33   -121   -181       C  
ATOM   6090  CD  LYS A 743      14.424  30.994  30.099  1.00 48.48           C  
ANISOU 6090  CD  LYS A 743     6277   5937   6208    114   -133   -224       C  
ATOM   6091  CE  LYS A 743      14.968  32.416  30.245  1.00 52.45           C  
ANISOU 6091  CE  LYS A 743     6787   6337   6804    122   -141   -268       C  
ATOM   6092  NZ  LYS A 743      14.629  33.299  29.085  1.00 51.58           N  
ANISOU 6092  NZ  LYS A 743     6684   6162   6753     98   -135   -184       N  
ATOM   6093  N   ALA A 744      18.091  27.807  28.183  1.00 33.41           N  
ANISOU 6093  N   ALA A 744     4392   4108   4194    -94    -84   -229       N  
ATOM   6094  CA  ALA A 744      19.366  28.068  27.513  1.00 34.27           C  
ANISOU 6094  CA  ALA A 744     4499   4188   4334   -145    -72   -234       C  
ATOM   6095  C   ALA A 744      19.640  27.134  26.326  1.00 32.24           C  
ANISOU 6095  C   ALA A 744     4257   3965   4026   -195    -46   -187       C  
ATOM   6096  O   ALA A 744      20.082  27.595  25.267  1.00 32.22           O  
ANISOU 6096  O   ALA A 744     4257   3944   4043   -240    -34   -147       O  
ATOM   6097  CB  ALA A 744      20.510  28.023  28.506  1.00 32.90           C  
ANISOU 6097  CB  ALA A 744     4306   4017   4178   -130    -77   -312       C  
ATOM   6098  N   LEU A 745      19.389  25.837  26.501  1.00 30.61           N  
ANISOU 6098  N   LEU A 745     4063   3810   3758   -186    -34   -194       N  
ATOM   6099  CA  LEU A 745      19.504  24.878  25.394  1.00 30.44           C  
ANISOU 6099  CA  LEU A 745     4065   3818   3684   -230     -9   -162       C  
ATOM   6100  C   LEU A 745      18.578  25.262  24.234  1.00 31.46           C  
ANISOU 6100  C   LEU A 745     4205   3953   3797   -265    -15    -94       C  
ATOM   6101  O   LEU A 745      18.993  25.246  23.071  1.00 32.73           O  
ANISOU 6101  O   LEU A 745     4375   4124   3939   -310      2    -62       O  
ATOM   6102  CB  LEU A 745      19.228  23.439  25.861  1.00 29.40           C  
ANISOU 6102  CB  LEU A 745     3948   3723   3500   -213      4   -181       C  
ATOM   6103  CG  LEU A 745      20.277  22.696  26.705  1.00 29.18           C  
ANISOU 6103  CG  LEU A 745     3912   3705   3469   -183     22   -231       C  
ATOM   6104  CD1 LEU A 745      19.716  21.372  27.204  1.00 21.39           C  
ANISOU 6104  CD1 LEU A 745     2941   2745   2442   -162     33   -232       C  
ATOM   6105  CD2 LEU A 745      21.617  22.478  25.955  1.00 25.63           C  
ANISOU 6105  CD2 LEU A 745     3464   3253   3020   -213     52   -240       C  
ATOM   6106  N   LYS A 746      17.337  25.626  24.562  1.00 31.01           N  
ANISOU 6106  N   LYS A 746     4140   3899   3742   -240    -39    -67       N  
ATOM   6107  CA  LYS A 746      16.383  26.140  23.577  1.00 34.60           C  
ANISOU 6107  CA  LYS A 746     4593   4367   4185   -263    -50      5       C  
ATOM   6108  C   LYS A 746      16.895  27.343  22.773  1.00 36.58           C  
ANISOU 6108  C   LYS A 746     4836   4579   4484   -284    -47     48       C  
ATOM   6109  O   LYS A 746      16.703  27.409  21.547  1.00 38.65           O  
ANISOU 6109  O   LYS A 746     5102   4870   4714   -324    -41    109       O  
ATOM   6110  CB  LYS A 746      15.043  26.493  24.229  1.00 35.71           C  
ANISOU 6110  CB  LYS A 746     4717   4517   4334   -218    -74     28       C  
ATOM   6111  CG  LYS A 746      13.962  26.836  23.214  1.00 38.27           C  
ANISOU 6111  CG  LYS A 746     5033   4874   4634   -239    -88    111       C  
ATOM   6112  CD  LYS A 746      12.571  26.760  23.798  1.00 41.45           C  
ANISOU 6112  CD  LYS A 746     5414   5312   5023   -201   -107    137       C  
ATOM   6113  CE  LYS A 746      11.534  27.058  22.724  1.00 42.12           C  
ANISOU 6113  CE  LYS A 746     5481   5443   5077   -225   -123    226       C  
ATOM   6114  NZ  LYS A 746      10.145  26.848  23.217  1.00 48.18           N  
ANISOU 6114  NZ  LYS A 746     6220   6262   5824   -194   -141    258       N  
ATOM   6115  N   GLU A 747      17.530  28.293  23.452  1.00 34.57           N  
ANISOU 6115  N   GLU A 747     4569   4263   4305   -260    -51     17       N  
ATOM   6116  CA  GLU A 747      18.058  29.465  22.759  1.00 35.85           C  
ANISOU 6116  CA  GLU A 747     4721   4374   4528   -284    -45     60       C  
ATOM   6117  C   GLU A 747      19.228  29.069  21.848  1.00 35.92           C  
ANISOU 6117  C   GLU A 747     4731   4403   4512   -338    -17     70       C  
ATOM   6118  O   GLU A 747      19.354  29.584  20.742  1.00 33.93           O  
ANISOU 6118  O   GLU A 747     4474   4153   4264   -372     -6    140       O  
ATOM   6119  CB  GLU A 747      18.420  30.591  23.742  1.00 33.76           C  
ANISOU 6119  CB  GLU A 747     4443   4027   4358   -251    -59     16       C  
ATOM   6120  CG  GLU A 747      18.994  31.872  23.116  1.00 34.27           C  
ANISOU 6120  CG  GLU A 747     4496   4018   4506   -281    -52     61       C  
ATOM   6121  CD  GLU A 747      18.106  32.537  22.066  1.00 36.57           C  
ANISOU 6121  CD  GLU A 747     4786   4305   4804   -285    -51    170       C  
ATOM   6122  OE1 GLU A 747      18.616  33.436  21.362  1.00 39.63           O  
ANISOU 6122  OE1 GLU A 747     5163   4643   5252   -315    -39    228       O  
ATOM   6123  OE2 GLU A 747      16.915  32.184  21.930  1.00 37.55           O  
ANISOU 6123  OE2 GLU A 747     4913   4479   4876   -259    -61    206       O  
ATOM   6124  N   CYS A 748      20.056  28.138  22.314  1.00 36.33           N  
ANISOU 6124  N   CYS A 748     4789   4478   4538   -339     -4      5       N  
ATOM   6125  CA  CYS A 748      21.132  27.579  21.498  1.00 36.97           C  
ANISOU 6125  CA  CYS A 748     4872   4591   4586   -379     29      8       C  
ATOM   6126  C   CYS A 748      20.590  26.955  20.211  1.00 36.44           C  
ANISOU 6126  C   CYS A 748     4826   4585   4437   -411     43     61       C  
ATOM   6127  O   CYS A 748      21.090  27.226  19.123  1.00 37.93           O  
ANISOU 6127  O   CYS A 748     5008   4792   4610   -447     64    109       O  
ATOM   6128  CB  CYS A 748      21.905  26.525  22.289  1.00 36.89           C  
ANISOU 6128  CB  CYS A 748     4864   4600   4553   -360     42    -67       C  
ATOM   6129  SG  CYS A 748      22.919  27.203  23.604  1.00 36.58           S  
ANISOU 6129  SG  CYS A 748     4791   4515   4594   -335     27   -132       S  
ATOM   6130  N   ILE A 749      19.561  26.126  20.349  1.00 35.22           N  
ANISOU 6130  N   ILE A 749     4691   4464   4226   -401     30     51       N  
ATOM   6131  CA  ILE A 749      18.883  25.524  19.208  1.00 31.78           C  
ANISOU 6131  CA  ILE A 749     4275   4091   3710   -436     33     90       C  
ATOM   6132  C   ILE A 749      18.253  26.585  18.297  1.00 32.64           C  
ANISOU 6132  C   ILE A 749     4366   4213   3824   -452     19    181       C  
ATOM   6133  O   ILE A 749      18.425  26.533  17.072  1.00 34.20           O  
ANISOU 6133  O   ILE A 749     4566   4460   3967   -490     34    225       O  
ATOM   6134  CB  ILE A 749      17.834  24.492  19.669  1.00 31.40           C  
ANISOU 6134  CB  ILE A 749     4246   4071   3616   -427     16     61       C  
ATOM   6135  CG1 ILE A 749      18.521  23.285  20.313  1.00 28.91           C  
ANISOU 6135  CG1 ILE A 749     3951   3748   3286   -415     38    -14       C  
ATOM   6136  CG2 ILE A 749      16.969  24.041  18.507  1.00 33.92           C  
ANISOU 6136  CG2 ILE A 749     4578   4456   3856   -471      7    101       C  
ATOM   6137  CD1 ILE A 749      17.560  22.354  21.067  1.00 28.77           C  
ANISOU 6137  CD1 ILE A 749     3945   3739   3247   -400     23    -38       C  
ATOM   6138  N   ARG A 750      17.546  27.549  18.888  1.00 32.48           N  
ANISOU 6138  N   ARG A 750     4327   4150   3865   -419     -7    210       N  
ATOM   6139  CA  ARG A 750      17.007  28.680  18.126  1.00 34.57           C  
ANISOU 6139  CA  ARG A 750     4571   4412   4153   -423    -16    306       C  
ATOM   6140  C   ARG A 750      18.111  29.321  17.301  1.00 34.93           C  
ANISOU 6140  C   ARG A 750     4605   4442   4223   -454     12    348       C  
ATOM   6141  O   ARG A 750      17.963  29.507  16.088  1.00 36.14           O  
ANISOU 6141  O   ARG A 750     4752   4651   4330   -483     21    426       O  
ATOM   6142  CB  ARG A 750      16.359  29.735  19.037  1.00 35.10           C  
ANISOU 6142  CB  ARG A 750     4621   4411   4306   -371    -38    319       C  
ATOM   6143  CG  ARG A 750      15.434  30.694  18.275  1.00 37.18           C  
ANISOU 6143  CG  ARG A 750     4863   4683   4582   -362    -50    428       C  
ATOM   6144  CD  ARG A 750      15.088  31.960  19.058  1.00 35.92           C  
ANISOU 6144  CD  ARG A 750     4689   4430   4528   -307    -60    442       C  
ATOM   6145  NE  ARG A 750      16.277  32.764  19.346  1.00 39.77           N  
ANISOU 6145  NE  ARG A 750     5178   4824   5109   -315    -44    416       N  
ATOM   6146  CZ  ARG A 750      16.929  33.517  18.459  1.00 40.87           C  
ANISOU 6146  CZ  ARG A 750     5306   4935   5288   -348    -25    487       C  
ATOM   6147  NH1 ARG A 750      16.527  33.594  17.188  1.00 34.71           N  
ANISOU 6147  NH1 ARG A 750     4514   4221   4454   -371    -18    593       N  
ATOM   6148  NH2 ARG A 750      18.002  34.195  18.851  1.00 41.03           N  
ANISOU 6148  NH2 ARG A 750     5322   4868   5399   -362    -14    454       N  
ATOM   6149  N   ARG A 751      19.231  29.623  17.950  1.00 34.78           N  
ANISOU 6149  N   ARG A 751     4580   4361   4274   -450     26    299       N  
ATOM   6150  CA  ARG A 751      20.365  30.252  17.272  1.00 36.26           C  
ANISOU 6150  CA  ARG A 751     4748   4530   4497   -483     54    341       C  
ATOM   6151  C   ARG A 751      20.989  29.394  16.170  1.00 37.93           C  
ANISOU 6151  C   ARG A 751     4968   4829   4616   -521     87    352       C  
ATOM   6152  O   ARG A 751      21.352  29.920  15.110  1.00 40.05           O  
ANISOU 6152  O   ARG A 751     5219   5124   4875   -549    109    432       O  
ATOM   6153  CB  ARG A 751      21.409  30.713  18.283  1.00 36.21           C  
ANISOU 6153  CB  ARG A 751     4728   4446   4585   -476     56    278       C  
ATOM   6154  CG  ARG A 751      20.978  31.965  19.020  1.00 35.91           C  
ANISOU 6154  CG  ARG A 751     4679   4312   4653   -449     31    287       C  
ATOM   6155  CD  ARG A 751      21.757  32.173  20.288  1.00 35.54           C  
ANISOU 6155  CD  ARG A 751     4624   4202   4678   -436     20    192       C  
ATOM   6156  NE  ARG A 751      21.425  33.460  20.902  1.00 35.73           N  
ANISOU 6156  NE  ARG A 751     4643   4125   4810   -415     -1    192       N  
ATOM   6157  CZ  ARG A 751      22.113  34.584  20.715  1.00 37.29           C  
ANISOU 6157  CZ  ARG A 751     4821   4242   5107   -446      5    223       C  
ATOM   6158  NH1 ARG A 751      23.194  34.596  19.938  1.00 40.02           N  
ANISOU 6158  NH1 ARG A 751     5143   4606   5458   -501     32    264       N  
ATOM   6159  NH2 ARG A 751      21.727  35.700  21.316  1.00 32.93           N  
ANISOU 6159  NH2 ARG A 751     4271   3587   4655   -421    -14    212       N  
ATOM   6160  N   MET A 752      21.098  28.085  16.411  1.00 35.36           N  
ANISOU 6160  N   MET A 752     4669   4546   4221   -518     95    275       N  
ATOM   6161  CA  MET A 752      21.610  27.145  15.403  1.00 34.45           C  
ANISOU 6161  CA  MET A 752     4570   4510   4011   -546    128    268       C  
ATOM   6162  C   MET A 752      20.731  27.104  14.160  1.00 33.62           C  
ANISOU 6162  C   MET A 752     4472   4484   3819   -571    122    336       C  
ATOM   6163  O   MET A 752      21.229  27.184  13.045  1.00 34.94           O  
ANISOU 6163  O   MET A 752     4631   4710   3935   -596    151    384       O  
ATOM   6164  CB  MET A 752      21.711  25.728  15.975  1.00 34.54           C  
ANISOU 6164  CB  MET A 752     4614   4535   3974   -531    135    171       C  
ATOM   6165  CG  MET A 752      22.856  25.520  16.945  1.00 37.61           C  
ANISOU 6165  CG  MET A 752     4992   4879   4419   -508    153    107       C  
ATOM   6166  SD  MET A 752      22.609  24.041  17.930  1.00 40.74           S  
ANISOU 6166  SD  MET A 752     5423   5273   4784   -476    151     12       S  
ATOM   6167  CE  MET A 752      23.004  22.762  16.737  1.00 36.09           C  
ANISOU 6167  CE  MET A 752     4871   4750   4090   -498    195    -11       C  
ATOM   6168  N   LEU A 753      19.423  26.971  14.366  1.00 32.86           N  
ANISOU 6168  N   LEU A 753     4385   4399   3702   -562     85    343       N  
ATOM   6169  CA  LEU A 753      18.487  26.780  13.274  1.00 32.97           C  
ANISOU 6169  CA  LEU A 753     4402   4502   3622   -588     70    397       C  
ATOM   6170  C   LEU A 753      18.157  28.069  12.520  1.00 35.25           C  
ANISOU 6170  C   LEU A 753     4654   4807   3933   -590     64    521       C  
ATOM   6171  O   LEU A 753      17.864  28.025  11.318  1.00 37.61           O  
ANISOU 6171  O   LEU A 753     4947   5200   4143   -616     66    581       O  
ATOM   6172  CB  LEU A 753      17.194  26.109  13.767  1.00 32.02           C  
ANISOU 6172  CB  LEU A 753     4297   4399   3471   -583     31    363       C  
ATOM   6173  CG  LEU A 753      17.235  24.910  14.733  1.00 31.67           C  
ANISOU 6173  CG  LEU A 753     4283   4324   3424   -573     31    257       C  
ATOM   6174  CD1 LEU A 753      15.853  24.255  14.870  1.00 25.37           C  
ANISOU 6174  CD1 LEU A 753     3493   3565   2580   -585     -7    248       C  
ATOM   6175  CD2 LEU A 753      18.292  23.872  14.371  1.00 25.86           C  
ANISOU 6175  CD2 LEU A 753     3581   3606   2640   -591     71    186       C  
ATOM   6176  N   GLN A 754      18.205  29.204  13.213  1.00 34.33           N  
ANISOU 6176  N   GLN A 754     4514   4598   3930   -561     56    558       N  
ATOM   6177  CA  GLN A 754      17.763  30.478  12.637  1.00 37.14           C  
ANISOU 6177  CA  GLN A 754     4837   4947   4327   -553     50    682       C  
ATOM   6178  C   GLN A 754      18.894  31.424  12.264  1.00 40.64           C  
ANISOU 6178  C   GLN A 754     5257   5344   4841   -566     85    742       C  
ATOM   6179  O   GLN A 754      18.739  32.250  11.358  1.00 42.94           O  
ANISOU 6179  O   GLN A 754     5521   5660   5134   -573     93    861       O  
ATOM   6180  CB  GLN A 754      16.791  31.202  13.580  1.00 38.03           C  
ANISOU 6180  CB  GLN A 754     4940   4986   4525   -506     17    695       C  
ATOM   6181  CG  GLN A 754      15.449  30.487  13.756  1.00 39.66           C  
ANISOU 6181  CG  GLN A 754     5153   5255   4662   -495    -19    677       C  
ATOM   6182  CD  GLN A 754      14.504  31.180  14.723  1.00 40.01           C  
ANISOU 6182  CD  GLN A 754     5183   5234   4786   -439    -45    690       C  
ATOM   6183  OE1 GLN A 754      14.820  32.209  15.322  1.00 40.88           O  
ANISOU 6183  OE1 GLN A 754     5285   5241   5006   -406    -39    701       O  
ATOM   6184  NE2 GLN A 754      13.331  30.603  14.884  1.00 43.70           N  
ANISOU 6184  NE2 GLN A 754     5646   5762   5196   -430    -75    685       N  
ATOM   6185  N   GLU A 755      20.027  31.312  12.954  1.00 41.09           N  
ANISOU 6185  N   GLU A 755     5318   5336   4958   -571    105    668       N  
ATOM   6186  CA  GLU A 755      21.081  32.320  12.832  1.00 43.23           C  
ANISOU 6186  CA  GLU A 755     5559   5543   5323   -587    132    720       C  
ATOM   6187  C   GLU A 755      22.448  31.754  12.445  1.00 43.40           C  
ANISOU 6187  C   GLU A 755     5575   5607   5310   -619    174    688       C  
ATOM   6188  O   GLU A 755      23.184  32.376  11.686  1.00 46.95           O  
ANISOU 6188  O   GLU A 755     5993   6068   5779   -645    205    771       O  
ATOM   6189  CB  GLU A 755      21.154  33.176  14.105  1.00 41.76           C  
ANISOU 6189  CB  GLU A 755     5368   5221   5277   -563    112    681       C  
ATOM   6190  CG  GLU A 755      19.957  34.120  14.269  1.00 42.08           C  
ANISOU 6190  CG  GLU A 755     5405   5208   5375   -527     84    747       C  
ATOM   6191  CD  GLU A 755      19.855  34.756  15.647  1.00 44.63           C  
ANISOU 6191  CD  GLU A 755     5734   5406   5817   -492     61    678       C  
ATOM   6192  OE1 GLU A 755      18.808  35.377  15.931  1.00 45.36           O  
ANISOU 6192  OE1 GLU A 755     5829   5457   5950   -449     40    712       O  
ATOM   6193  OE2 GLU A 755      20.811  34.642  16.449  1.00 44.77           O  
ANISOU 6193  OE2 GLU A 755     5753   5374   5884   -503     64    588       O  
ATOM   6194  N   GLY A 756      22.790  30.581  12.959  1.00 42.81           N  
ANISOU 6194  N   GLY A 756     5525   5557   5184   -612    177    577       N  
ATOM   6195  CA  GLY A 756      23.992  29.898  12.499  1.00 43.26           C  
ANISOU 6195  CA  GLY A 756     5578   5670   5191   -632    221    548       C  
ATOM   6196  C   GLY A 756      25.008  29.648  13.582  1.00 44.83           C  
ANISOU 6196  C   GLY A 756     5768   5809   5456   -623    228    459       C  
ATOM   6197  O   GLY A 756      24.729  29.868  14.763  1.00 44.96           O  
ANISOU 6197  O   GLY A 756     5789   5747   5545   -601    195    404       O  
ATOM   6198  N   GLU A 757      26.194  29.202  13.166  1.00 45.91           N  
ANISOU 6198  N   GLU A 757     5888   5994   5563   -636    273    448       N  
ATOM   6199  CA  GLU A 757      27.273  28.829  14.078  1.00 45.10           C  
ANISOU 6199  CA  GLU A 757     5768   5860   5506   -626    284    369       C  
ATOM   6200  C   GLU A 757      27.791  29.988  14.938  1.00 46.10           C  
ANISOU 6200  C   GLU A 757     5855   5892   5771   -641    263    377       C  
ATOM   6201  O   GLU A 757      27.980  29.824  16.147  1.00 45.75           O  
ANISOU 6201  O   GLU A 757     5810   5799   5775   -621    238    294       O  
ATOM   6202  CB  GLU A 757      28.425  28.185  13.299  1.00 46.13           C  
ANISOU 6202  CB  GLU A 757     5882   6073   5572   -634    341    373       C  
ATOM   6203  CG  GLU A 757      29.577  27.666  14.168  1.00 47.07           C  
ANISOU 6203  CG  GLU A 757     5977   6180   5726   -616    358    297       C  
ATOM   6204  CD  GLU A 757      30.566  26.808  13.398  1.00 48.39           C  
ANISOU 6204  CD  GLU A 757     6136   6438   5814   -607    419    292       C  
ATOM   6205  OE1 GLU A 757      30.950  27.193  12.274  1.00 52.42           O  
ANISOU 6205  OE1 GLU A 757     6620   7006   6290   -632    456    372       O  
ATOM   6206  OE2 GLU A 757      30.967  25.748  13.926  1.00 48.01           O  
ANISOU 6206  OE2 GLU A 757     6103   6402   5735   -570    434    211       O  
ATOM   6207  N   GLU A 758      28.020  31.147  14.320  1.00 46.12           N  
ANISOU 6207  N   GLU A 758     5821   5868   5834   -676    272    476       N  
ATOM   6208  CA  GLU A 758      28.639  32.272  15.025  1.00 48.27           C  
ANISOU 6208  CA  GLU A 758     6052   6042   6244   -703    256    482       C  
ATOM   6209  C   GLU A 758      27.755  32.817  16.146  1.00 45.85           C  
ANISOU 6209  C   GLU A 758     5771   5637   6015   -678    203    430       C  
ATOM   6210  O   GLU A 758      28.255  33.166  17.218  1.00 45.92           O  
ANISOU 6210  O   GLU A 758     5763   5579   6107   -682    179    362       O  
ATOM   6211  CB  GLU A 758      29.044  33.393  14.060  1.00 51.45           C  
ANISOU 6211  CB  GLU A 758     6413   6430   6705   -749    282    611       C  
ATOM   6212  CG  GLU A 758      30.252  34.199  14.542  1.00 60.67           C  
ANISOU 6212  CG  GLU A 758     7524   7532   7996   -795    286    612       C  
ATOM   6213  CD  GLU A 758      30.589  35.379  13.636  1.00 68.63           C  
ANISOU 6213  CD  GLU A 758     8489   8509   9079   -846    311    751       C  
ATOM   6214  OE1 GLU A 758      29.840  36.379  13.654  1.00 71.08           O  
ANISOU 6214  OE1 GLU A 758     8811   8726   9469   -849    289    805       O  
ATOM   6215  OE2 GLU A 758      31.615  35.313  12.918  1.00 71.18           O  
ANISOU 6215  OE2 GLU A 758     8764   8899   9384   -879    357    810       O  
ATOM   6216  N   SER A 759      26.448  32.875  15.898  1.00 43.39           N  
ANISOU 6216  N   SER A 759     5495   5323   5668   -652    184    462       N  
ATOM   6217  CA  SER A 759      25.499  33.361  16.895  1.00 42.56           C  
ANISOU 6217  CA  SER A 759     5412   5134   5623   -619    139    419       C  
ATOM   6218  C   SER A 759      25.399  32.406  18.079  1.00 39.90           C  
ANISOU 6218  C   SER A 759     5098   4810   5253   -581    117    295       C  
ATOM   6219  O   SER A 759      25.243  32.829  19.230  1.00 37.60           O  
ANISOU 6219  O   SER A 759     4808   4448   5031   -559     84    229       O  
ATOM   6220  CB  SER A 759      24.125  33.554  16.277  1.00 42.26           C  
ANISOU 6220  CB  SER A 759     5398   5113   5545   -596    128    492       C  
ATOM   6221  OG  SER A 759      23.196  33.946  17.272  1.00 46.33           O  
ANISOU 6221  OG  SER A 759     5933   5558   6112   -554     89    448       O  
ATOM   6222  N   LEU A 760      25.495  31.120  17.772  1.00 38.91           N  
ANISOU 6222  N   LEU A 760     4989   4775   5020   -571    136    265       N  
ATOM   6223  CA  LEU A 760      25.482  30.056  18.767  1.00 39.57           C  
ANISOU 6223  CA  LEU A 760     5092   4879   5064   -535    124    163       C  
ATOM   6224  C   LEU A 760      26.662  30.191  19.737  1.00 39.45           C  
ANISOU 6224  C   LEU A 760     5043   4834   5112   -538    121     96       C  
ATOM   6225  O   LEU A 760      26.475  30.134  20.947  1.00 40.84           O  
ANISOU 6225  O   LEU A 760     5223   4979   5316   -506     90     21       O  
ATOM   6226  CB  LEU A 760      25.468  28.695  18.057  1.00 36.88           C  
ANISOU 6226  CB  LEU A 760     4778   4630   4606   -531    155    155       C  
ATOM   6227  CG  LEU A 760      25.364  27.328  18.756  1.00 38.77           C  
ANISOU 6227  CG  LEU A 760     5045   4901   4784   -495    155     70       C  
ATOM   6228  CD1 LEU A 760      26.687  26.610  18.778  1.00 37.52           C  
ANISOU 6228  CD1 LEU A 760     4869   4778   4608   -493    192     33       C  
ATOM   6229  CD2 LEU A 760      24.736  27.352  20.139  1.00 38.64           C  
ANISOU 6229  CD2 LEU A 760     5036   4839   4806   -456    115     10       C  
ATOM   6230  N   GLN A 761      27.862  30.400  19.198  1.00 39.82           N  
ANISOU 6230  N   GLN A 761     5051   4898   5180   -576    151    126       N  
ATOM   6231  CA  GLN A 761      29.073  30.554  20.005  1.00 39.01           C  
ANISOU 6231  CA  GLN A 761     4903   4781   5136   -588    147     72       C  
ATOM   6232  C   GLN A 761      29.055  31.801  20.891  1.00 41.93           C  
ANISOU 6232  C   GLN A 761     5254   5054   5623   -604    105     44       C  
ATOM   6233  O   GLN A 761      29.569  31.765  22.016  1.00 41.70           O  
ANISOU 6233  O   GLN A 761     5204   5014   5626   -593     79    -39       O  
ATOM   6234  CB  GLN A 761      30.316  30.551  19.117  1.00 40.71           C  
ANISOU 6234  CB  GLN A 761     5073   5045   5348   -629    192    126       C  
ATOM   6235  CG  GLN A 761      30.414  29.345  18.182  1.00 37.19           C  
ANISOU 6235  CG  GLN A 761     4649   4696   4785   -610    240    145       C  
ATOM   6236  CD  GLN A 761      31.483  29.508  17.114  1.00 39.25           C  
ANISOU 6236  CD  GLN A 761     4865   5011   5037   -647    290    217       C  
ATOM   6237  OE1 GLN A 761      31.907  28.532  16.490  1.00 41.93           O  
ANISOU 6237  OE1 GLN A 761     5210   5431   5289   -629    335    216       O  
ATOM   6238  NE2 GLN A 761      31.927  30.736  16.900  1.00 33.61           N  
ANISOU 6238  NE2 GLN A 761     4105   4249   4415   -698    287    280       N  
ATOM   6239  N   GLU A 762      28.466  32.890  20.390  1.00 41.22           N  
ANISOU 6239  N   GLU A 762     5172   4895   5595   -626     97    112       N  
ATOM   6240  CA  GLU A 762      28.213  34.087  21.204  1.00 45.22           C  
ANISOU 6240  CA  GLU A 762     5675   5291   6215   -631     58     80       C  
ATOM   6241  C   GLU A 762      27.393  33.780  22.455  1.00 43.71           C  
ANISOU 6241  C   GLU A 762     5516   5086   6005   -571     20    -17       C  
ATOM   6242  O   GLU A 762      27.733  34.223  23.558  1.00 44.85           O  
ANISOU 6242  O   GLU A 762     5646   5185   6210   -568    -13   -101       O  
ATOM   6243  CB  GLU A 762      27.459  35.148  20.399  1.00 48.39           C  
ANISOU 6243  CB  GLU A 762     6090   5622   6672   -646     63    180       C  
ATOM   6244  CG  GLU A 762      28.309  36.214  19.734  1.00 56.27           C  
ANISOU 6244  CG  GLU A 762     7047   6563   7771   -713     82    259       C  
ATOM   6245  CD  GLU A 762      27.481  37.444  19.350  1.00 65.42           C  
ANISOU 6245  CD  GLU A 762     8222   7618   9018   -714     76    340       C  
ATOM   6246  OE1 GLU A 762      26.338  37.586  19.856  1.00 65.51           O  
ANISOU 6246  OE1 GLU A 762     8273   7591   9029   -660     51    311       O  
ATOM   6247  OE2 GLU A 762      27.970  38.270  18.543  1.00 68.55           O  
ANISOU 6247  OE2 GLU A 762     8588   7972   9486   -766    101    440       O  
ATOM   6248  N   TYR A 763      26.311  33.027  22.279  1.00 41.72           N  
ANISOU 6248  N   TYR A 763     5304   4881   5667   -525     23     -4       N  
ATOM   6249  CA  TYR A 763      25.396  32.763  23.373  1.00 41.00           C  
ANISOU 6249  CA  TYR A 763     5239   4783   5555   -466     -9    -76       C  
ATOM   6250  C   TYR A 763      25.992  31.830  24.413  1.00 41.13           C  
ANISOU 6250  C   TYR A 763     5245   4856   5528   -440    -18   -170       C  
ATOM   6251  O   TYR A 763      25.878  32.089  25.611  1.00 40.80           O  
ANISOU 6251  O   TYR A 763     5200   4789   5513   -409    -50   -250       O  
ATOM   6252  CB  TYR A 763      24.065  32.210  22.870  1.00 40.23           C  
ANISOU 6252  CB  TYR A 763     5178   4725   5382   -432     -4    -28       C  
ATOM   6253  CG  TYR A 763      22.991  32.250  23.934  1.00 41.86           C  
ANISOU 6253  CG  TYR A 763     5406   4913   5587   -371    -34    -81       C  
ATOM   6254  CD1 TYR A 763      22.572  31.086  24.587  1.00 41.09           C  
ANISOU 6254  CD1 TYR A 763     5321   4881   5408   -330    -39   -130       C  
ATOM   6255  CD2 TYR A 763      22.419  33.461  24.313  1.00 41.07           C  
ANISOU 6255  CD2 TYR A 763     5309   4725   5570   -352    -55    -81       C  
ATOM   6256  CE1 TYR A 763      21.586  31.136  25.584  1.00 41.96           C  
ANISOU 6256  CE1 TYR A 763     5444   4985   5515   -273    -63   -172       C  
ATOM   6257  CE2 TYR A 763      21.450  33.521  25.300  1.00 42.70           C  
ANISOU 6257  CE2 TYR A 763     5531   4922   5772   -289    -79   -131       C  
ATOM   6258  CZ  TYR A 763      21.030  32.364  25.930  1.00 42.92           C  
ANISOU 6258  CZ  TYR A 763     5567   5029   5712   -250    -83   -174       C  
ATOM   6259  OH  TYR A 763      20.056  32.458  26.901  1.00 45.01           O  
ANISOU 6259  OH  TYR A 763     5841   5292   5969   -186   -102   -214       O  
ATOM   6260  N   PHE A 764      26.613  30.748  23.946  1.00 40.65           N  
ANISOU 6260  N   PHE A 764     5177   4872   5396   -448     13   -158       N  
ATOM   6261  CA  PHE A 764      27.256  29.778  24.820  1.00 40.70           C  
ANISOU 6261  CA  PHE A 764     5168   4937   5359   -419     12   -229       C  
ATOM   6262  C   PHE A 764      28.286  30.458  25.712  1.00 41.46           C  
ANISOU 6262  C   PHE A 764     5218   5010   5526   -437    -14   -292       C  
ATOM   6263  O   PHE A 764      28.284  30.264  26.925  1.00 38.65           O  
ANISOU 6263  O   PHE A 764     4854   4670   5162   -399    -42   -369       O  
ATOM   6264  CB  PHE A 764      27.920  28.666  23.999  1.00 41.35           C  
ANISOU 6264  CB  PHE A 764     5248   5093   5371   -427     57   -198       C  
ATOM   6265  CG  PHE A 764      28.856  27.792  24.797  1.00 40.68           C  
ANISOU 6265  CG  PHE A 764     5135   5064   5258   -400     64   -256       C  
ATOM   6266  CD1 PHE A 764      28.381  26.659  25.455  1.00 41.62           C  
ANISOU 6266  CD1 PHE A 764     5279   5222   5312   -344     65   -292       C  
ATOM   6267  CD2 PHE A 764      30.214  28.099  24.884  1.00 40.47           C  
ANISOU 6267  CD2 PHE A 764     5051   5053   5271   -430     69   -266       C  
ATOM   6268  CE1 PHE A 764      29.244  25.847  26.197  1.00 40.71           C  
ANISOU 6268  CE1 PHE A 764     5135   5160   5173   -311     73   -333       C  
ATOM   6269  CE2 PHE A 764      31.085  27.297  25.619  1.00 38.30           C  
ANISOU 6269  CE2 PHE A 764     4744   4840   4969   -399     75   -311       C  
ATOM   6270  CZ  PHE A 764      30.596  26.168  26.277  1.00 42.41           C  
ANISOU 6270  CZ  PHE A 764     5292   5398   5424   -335     78   -342       C  
ATOM   6271  N   LYS A 765      29.165  31.248  25.099  1.00 43.29           N  
ANISOU 6271  N   LYS A 765     5414   5210   5824   -498     -4   -256       N  
ATOM   6272  CA  LYS A 765      30.212  31.934  25.831  1.00 45.89           C  
ANISOU 6272  CA  LYS A 765     5692   5517   6227   -533    -31   -312       C  
ATOM   6273  C   LYS A 765      29.591  32.743  26.974  1.00 46.72           C  
ANISOU 6273  C   LYS A 765     5812   5555   6385   -510    -81   -392       C  
ATOM   6274  O   LYS A 765      30.020  32.628  28.126  1.00 46.21           O  
ANISOU 6274  O   LYS A 765     5722   5519   6316   -492   -112   -481       O  
ATOM   6275  CB  LYS A 765      31.035  32.824  24.894  1.00 49.13           C  
ANISOU 6275  CB  LYS A 765     6065   5886   6716   -610    -13   -245       C  
ATOM   6276  CG  LYS A 765      32.342  33.344  25.493  1.00 54.58           C  
ANISOU 6276  CG  LYS A 765     6688   6573   7476   -661    -35   -294       C  
ATOM   6277  CD  LYS A 765      32.841  34.580  24.745  1.00 62.73           C  
ANISOU 6277  CD  LYS A 765     7691   7525   8620   -743    -28   -230       C  
ATOM   6278  CE  LYS A 765      33.388  34.244  23.354  1.00 65.96           C  
ANISOU 6278  CE  LYS A 765     8076   7988   8998   -774     30   -116       C  
ATOM   6279  NZ  LYS A 765      33.190  35.368  22.386  1.00 67.18           N  
ANISOU 6279  NZ  LYS A 765     8233   8057   9237   -829     46    -18       N  
ATOM   6280  N   GLU A 766      28.557  33.520  26.660  1.00 45.78           N  
ANISOU 6280  N   GLU A 766     5731   5355   6307   -505    -86   -360       N  
ATOM   6281  CA  GLU A 766      27.901  34.344  27.668  1.00 47.85           C  
ANISOU 6281  CA  GLU A 766     6013   5546   6621   -476   -127   -434       C  
ATOM   6282  C   GLU A 766      27.192  33.518  28.734  1.00 47.04           C  
ANISOU 6282  C   GLU A 766     5931   5509   6434   -397   -144   -502       C  
ATOM   6283  O   GLU A 766      27.252  33.861  29.913  1.00 47.11           O  
ANISOU 6283  O   GLU A 766     5931   5509   6459   -373   -180   -599       O  
ATOM   6284  CB  GLU A 766      26.927  35.337  27.039  1.00 49.36           C  
ANISOU 6284  CB  GLU A 766     6239   5638   6877   -477   -122   -372       C  
ATOM   6285  CG  GLU A 766      26.707  36.571  27.904  1.00 53.83           C  
ANISOU 6285  CG  GLU A 766     6815   6097   7543   -472   -159   -449       C  
ATOM   6286  CD  GLU A 766      27.963  37.411  28.048  1.00 57.33           C  
ANISOU 6286  CD  GLU A 766     7216   6479   8087   -551   -176   -488       C  
ATOM   6287  OE1 GLU A 766      28.457  37.919  27.017  1.00 59.05           O  
ANISOU 6287  OE1 GLU A 766     7416   6652   8370   -615   -152   -399       O  
ATOM   6288  OE2 GLU A 766      28.453  37.571  29.191  1.00 59.25           O  
ANISOU 6288  OE2 GLU A 766     7440   6727   8345   -550   -214   -605       O  
ATOM   6289  N   PHE A 767      26.541  32.429  28.322  1.00 45.05           N  
ANISOU 6289  N   PHE A 767     5703   5322   6091   -360   -118   -452       N  
ATOM   6290  CA  PHE A 767      25.853  31.548  29.266  1.00 44.34           C  
ANISOU 6290  CA  PHE A 767     5629   5297   5922   -288   -127   -499       C  
ATOM   6291  C   PHE A 767      26.806  30.858  30.242  1.00 44.95           C  
ANISOU 6291  C   PHE A 767     5668   5451   5959   -272   -139   -569       C  
ATOM   6292  O   PHE A 767      26.497  30.748  31.425  1.00 44.93           O  
ANISOU 6292  O   PHE A 767     5663   5479   5928   -220   -165   -639       O  
ATOM   6293  CB  PHE A 767      24.958  30.512  28.561  1.00 42.87           C  
ANISOU 6293  CB  PHE A 767     5476   5158   5656   -264    -97   -427       C  
ATOM   6294  CG  PHE A 767      24.132  29.692  29.518  1.00 40.26           C  
ANISOU 6294  CG  PHE A 767     5159   4882   5256   -195   -106   -462       C  
ATOM   6295  CD1 PHE A 767      24.577  28.444  29.949  1.00 39.57           C  
ANISOU 6295  CD1 PHE A 767     5061   4875   5101   -171    -93   -478       C  
ATOM   6296  CD2 PHE A 767      22.936  30.194  30.032  1.00 38.88           C  
ANISOU 6296  CD2 PHE A 767     5004   4680   5088   -150   -124   -474       C  
ATOM   6297  CE1 PHE A 767      23.835  27.688  30.856  1.00 39.37           C  
ANISOU 6297  CE1 PHE A 767     5043   4900   5016   -108    -98   -499       C  
ATOM   6298  CE2 PHE A 767      22.186  29.453  30.946  1.00 42.54           C  
ANISOU 6298  CE2 PHE A 767     5473   5204   5488    -86   -129   -498       C  
ATOM   6299  CZ  PHE A 767      22.639  28.192  31.358  1.00 43.96           C  
ANISOU 6299  CZ  PHE A 767     5641   5461   5600    -68   -116   -508       C  
ATOM   6300  N   GLU A 768      27.953  30.398  29.741  1.00 46.72           N  
ANISOU 6300  N   GLU A 768     5861   5715   6177   -311   -118   -545       N  
ATOM   6301  CA  GLU A 768      29.013  29.818  30.576  1.00 46.18           C  
ANISOU 6301  CA  GLU A 768     5744   5723   6078   -298   -129   -600       C  
ATOM   6302  C   GLU A 768      29.540  30.832  31.600  1.00 46.52           C  
ANISOU 6302  C   GLU A 768     5752   5744   6180   -316   -179   -692       C  
ATOM   6303  O   GLU A 768      29.900  30.459  32.714  1.00 46.93           O  
ANISOU 6303  O   GLU A 768     5774   5867   6191   -279   -204   -760       O  
ATOM   6304  CB  GLU A 768      30.159  29.297  29.694  1.00 47.79           C  
ANISOU 6304  CB  GLU A 768     5915   5967   6276   -339    -92   -547       C  
ATOM   6305  CG  GLU A 768      31.195  28.390  30.389  1.00 49.05           C  
ANISOU 6305  CG  GLU A 768     6024   6224   6387   -311    -89   -579       C  
ATOM   6306  CD  GLU A 768      32.284  27.876  29.431  1.00 52.08           C  
ANISOU 6306  CD  GLU A 768     6376   6647   6765   -343    -45   -521       C  
ATOM   6307  OE1 GLU A 768      32.441  26.645  29.304  1.00 53.90           O  
ANISOU 6307  OE1 GLU A 768     6613   6939   6929   -298     -8   -496       O  
ATOM   6308  OE2 GLU A 768      32.985  28.696  28.801  1.00 50.03           O  
ANISOU 6308  OE2 GLU A 768     6084   6356   6570   -410    -43   -498       O  
ATOM   6309  N   LYS A 769      29.580  32.106  31.219  1.00 46.35           N  
ANISOU 6309  N   LYS A 769     5733   5625   6254   -372   -194   -696       N  
ATOM   6310  CA  LYS A 769      30.068  33.168  32.102  1.00 48.49           C  
ANISOU 6310  CA  LYS A 769     5976   5854   6594   -400   -243   -792       C  
ATOM   6311  C   LYS A 769      29.118  33.443  33.265  1.00 49.01           C  
ANISOU 6311  C   LYS A 769     6071   5912   6637   -334   -276   -878       C  
ATOM   6312  O   LYS A 769      29.559  33.609  34.402  1.00 49.66           O  
ANISOU 6312  O   LYS A 769     6124   6037   6708   -322   -317   -979       O  
ATOM   6313  CB  LYS A 769      30.262  34.475  31.327  1.00 49.89           C  
ANISOU 6313  CB  LYS A 769     6155   5907   6892   -478   -244   -764       C  
ATOM   6314  CG  LYS A 769      31.629  34.700  30.730  1.00 54.53           C  
ANISOU 6314  CG  LYS A 769     6684   6500   7534   -564   -236   -732       C  
ATOM   6315  CD  LYS A 769      31.773  36.171  30.318  1.00 61.61           C  
ANISOU 6315  CD  LYS A 769     7581   7260   8568   -640   -249   -726       C  
ATOM   6316  CE  LYS A 769      33.116  36.467  29.649  1.00 62.26           C  
ANISOU 6316  CE  LYS A 769     7597   7345   8713   -734   -238   -678       C  
ATOM   6317  NZ  LYS A 769      33.180  35.932  28.258  1.00 59.45           N  
ANISOU 6317  NZ  LYS A 769     7243   7020   8327   -744   -178   -543       N  
ATOM   6318  N   GLU A 770      27.818  33.501  32.972  1.00 47.40           N  
ANISOU 6318  N   GLU A 770     5922   5664   6424   -290   -259   -838       N  
ATOM   6319  CA  GLU A 770      26.843  34.045  33.922  1.00 47.29           C  
ANISOU 6319  CA  GLU A 770     5938   5620   6409   -230   -286   -912       C  
ATOM   6320  C   GLU A 770      26.088  32.960  34.690  1.00 45.27           C  
ANISOU 6320  C   GLU A 770     5692   5470   6040   -141   -280   -920       C  
ATOM   6321  O   GLU A 770      25.398  33.239  35.674  1.00 43.86           O  
ANISOU 6321  O   GLU A 770     5526   5301   5838    -81   -301   -989       O  
ATOM   6322  CB  GLU A 770      25.868  35.007  33.217  1.00 48.60           C  
ANISOU 6322  CB  GLU A 770     6150   5665   6650   -232   -273   -866       C  
ATOM   6323  CG  GLU A 770      26.512  35.995  32.209  1.00 49.77           C  
ANISOU 6323  CG  GLU A 770     6292   5704   6915   -321   -267   -819       C  
ATOM   6324  CD  GLU A 770      27.456  37.030  32.827  1.00 53.35           C  
ANISOU 6324  CD  GLU A 770     6717   6093   7460   -377   -306   -920       C  
ATOM   6325  OE1 GLU A 770      28.291  37.588  32.075  1.00 54.72           O  
ANISOU 6325  OE1 GLU A 770     6868   6206   7719   -461   -300   -879       O  
ATOM   6326  OE2 GLU A 770      27.372  37.302  34.044  1.00 53.41           O  
ANISOU 6326  OE2 GLU A 770     6726   6113   7456   -341   -344  -1040       O  
ATOM   6327  N   PHE A 771      26.269  31.723  34.242  1.00 42.89           N  
ANISOU 6327  N   PHE A 771     5382   5245   5670   -135   -249   -849       N  
ATOM   6328  CA  PHE A 771      25.611  30.533  34.780  1.00 43.26           C  
ANISOU 6328  CA  PHE A 771     5436   5384   5616    -63   -234   -830       C  
ATOM   6329  C   PHE A 771      25.503  30.456  36.314  1.00 43.00           C  
ANISOU 6329  C   PHE A 771     5383   5427   5529      4   -266   -921       C  
ATOM   6330  O   PHE A 771      24.446  30.108  36.837  1.00 44.11           O  
ANISOU 6330  O   PHE A 771     5543   5601   5617     71   -260   -915       O  
ATOM   6331  CB  PHE A 771      26.303  29.286  34.197  1.00 44.23           C  
ANISOU 6331  CB  PHE A 771     5542   5572   5691    -78   -201   -765       C  
ATOM   6332  CG  PHE A 771      25.980  28.009  34.903  1.00 44.46           C  
ANISOU 6332  CG  PHE A 771     5567   5697   5628    -10   -187   -753       C  
ATOM   6333  CD1 PHE A 771      26.944  27.378  35.678  1.00 47.78           C  
ANISOU 6333  CD1 PHE A 771     5942   6206   6006     11   -195   -785       C  
ATOM   6334  CD2 PHE A 771      24.725  27.420  34.773  1.00 48.33           C  
ANISOU 6334  CD2 PHE A 771     6095   6192   6077     30   -166   -702       C  
ATOM   6335  CE1 PHE A 771      26.663  26.192  36.335  1.00 48.58           C  
ANISOU 6335  CE1 PHE A 771     6038   6392   6029     77   -178   -762       C  
ATOM   6336  CE2 PHE A 771      24.427  26.223  35.422  1.00 51.82           C  
ANISOU 6336  CE2 PHE A 771     6532   6715   6444     88   -151   -682       C  
ATOM   6337  CZ  PHE A 771      25.401  25.607  36.208  1.00 52.22           C  
ANISOU 6337  CZ  PHE A 771     6540   6847   6456    114   -155   -710       C  
ATOM   6338  N   ARG A 772      26.578  30.799  37.020  1.00 43.75           N  
ANISOU 6338  N   ARG A 772     5434   5554   5634    -16   -300  -1003       N  
ATOM   6339  CA  ARG A 772      26.629  30.674  38.487  1.00 45.20           C  
ANISOU 6339  CA  ARG A 772     5590   5832   5750     46   -333  -1092       C  
ATOM   6340  C   ARG A 772      25.708  31.620  39.255  1.00 43.71           C  
ANISOU 6340  C   ARG A 772     5429   5606   5573     91   -358  -1174       C  
ATOM   6341  O   ARG A 772      25.468  31.419  40.440  1.00 45.74           O  
ANISOU 6341  O   ARG A 772     5670   5953   5756    158   -377  -1237       O  
ATOM   6342  CB  ARG A 772      28.071  30.765  39.001  1.00 45.70           C  
ANISOU 6342  CB  ARG A 772     5591   5956   5815      7   -367  -1157       C  
ATOM   6343  CG  ARG A 772      28.867  29.520  38.684  1.00 50.25           C  
ANISOU 6343  CG  ARG A 772     6132   6617   6343      6   -338  -1082       C  
ATOM   6344  CD  ARG A 772      30.365  29.762  38.600  1.00 56.28           C  
ANISOU 6344  CD  ARG A 772     6835   7407   7144    -60   -360  -1110       C  
ATOM   6345  NE  ARG A 772      30.994  28.709  37.801  1.00 62.66           N  
ANISOU 6345  NE  ARG A 772     7624   8252   7933    -69   -315  -1013       N  
ATOM   6346  CZ  ARG A 772      31.485  27.571  38.292  1.00 65.44           C  
ANISOU 6346  CZ  ARG A 772     7936   8718   8208    -17   -302   -984       C  
ATOM   6347  NH1 ARG A 772      31.449  27.328  39.603  1.00 65.34           N  
ANISOU 6347  NH1 ARG A 772     7894   8808   8124     46   -332  -1039       N  
ATOM   6348  NH2 ARG A 772      32.021  26.675  37.467  1.00 62.10           N  
ANISOU 6348  NH2 ARG A 772     7505   8310   7779    -24   -255   -899       N  
ATOM   6349  N   GLN A 773      25.178  32.630  38.573  1.00 43.17           N  
ANISOU 6349  N   GLN A 773     5400   5410   5592     61   -354  -1169       N  
ATOM   6350  CA  GLN A 773      24.230  33.570  39.179  1.00 43.93           C  
ANISOU 6350  CA  GLN A 773     5528   5453   5709    111   -369  -1240       C  
ATOM   6351  C   GLN A 773      22.804  33.022  39.241  1.00 41.22           C  
ANISOU 6351  C   GLN A 773     5213   5143   5304    192   -338  -1175       C  
ATOM   6352  O   GLN A 773      21.949  33.588  39.932  1.00 39.06           O  
ANISOU 6352  O   GLN A 773     4958   4861   5022    257   -345  -1231       O  
ATOM   6353  CB  GLN A 773      24.207  34.887  38.404  1.00 46.11           C  
ANISOU 6353  CB  GLN A 773     5836   5571   6114     52   -373  -1247       C  
ATOM   6354  CG  GLN A 773      25.505  35.662  38.419  1.00 51.86           C  
ANISOU 6354  CG  GLN A 773     6537   6246   6922    -34   -408  -1322       C  
ATOM   6355  CD  GLN A 773      25.655  36.573  37.207  1.00 56.40           C  
ANISOU 6355  CD  GLN A 773     7132   6671   7625   -112   -394  -1264       C  
ATOM   6356  OE1 GLN A 773      26.649  36.492  36.482  1.00 57.50           O  
ANISOU 6356  OE1 GLN A 773     7243   6799   7806   -193   -390  -1218       O  
ATOM   6357  NE2 GLN A 773      24.665  37.435  36.978  1.00 55.08           N  
ANISOU 6357  NE2 GLN A 773     7013   6394   7521    -83   -383  -1257       N  
ATOM   6358  N   LEU A 774      22.547  31.944  38.503  1.00 38.20           N  
ANISOU 6358  N   LEU A 774     4833   4799   4884    187   -302  -1060       N  
ATOM   6359  CA  LEU A 774      21.202  31.370  38.413  1.00 39.63           C  
ANISOU 6359  CA  LEU A 774     5034   5008   5014    247   -273   -985       C  
ATOM   6360  C   LEU A 774      20.688  30.853  39.756  1.00 41.23           C  
ANISOU 6360  C   LEU A 774     5217   5325   5121    337   -278  -1027       C  
ATOM   6361  O   LEU A 774      21.437  30.252  40.538  1.00 43.74           O  
ANISOU 6361  O   LEU A 774     5501   5739   5379    352   -291  -1063       O  
ATOM   6362  CB  LEU A 774      21.142  30.258  37.354  1.00 37.10           C  
ANISOU 6362  CB  LEU A 774     4720   4704   4672    211   -238   -866       C  
ATOM   6363  CG  LEU A 774      21.256  30.712  35.888  1.00 37.49           C  
ANISOU 6363  CG  LEU A 774     4792   4653   4799    136   -223   -799       C  
ATOM   6364  CD1 LEU A 774      21.535  29.550  34.951  1.00 36.62           C  
ANISOU 6364  CD1 LEU A 774     4683   4575   4656     97   -193   -710       C  
ATOM   6365  CD2 LEU A 774      20.030  31.485  35.439  1.00 35.27           C  
ANISOU 6365  CD2 LEU A 774     4541   4300   4558    157   -217   -763       C  
ATOM   6366  N   ASN A 775      19.408  31.109  40.009  1.00 40.31           N  
ANISOU 6366  N   ASN A 775     5120   5208   4990    401   -266  -1013       N  
ATOM   6367  CA  ASN A 775      18.712  30.597  41.178  1.00 40.08           C  
ANISOU 6367  CA  ASN A 775     5071   5292   4866    493   -262  -1029       C  
ATOM   6368  C   ASN A 775      18.800  29.068  41.247  1.00 38.21           C  
ANISOU 6368  C   ASN A 775     4809   5157   4552    499   -239   -944       C  
ATOM   6369  O   ASN A 775      18.583  28.365  40.241  1.00 35.04           O  
ANISOU 6369  O   ASN A 775     4421   4728   4165    456   -213   -844       O  
ATOM   6370  CB  ASN A 775      17.252  31.060  41.150  1.00 41.63           C  
ANISOU 6370  CB  ASN A 775     5287   5463   5069    552   -243   -999       C  
ATOM   6371  CG  ASN A 775      16.425  30.475  42.286  1.00 46.43           C  
ANISOU 6371  CG  ASN A 775     5868   6197   5575    649   -231   -997       C  
ATOM   6372  OD1 ASN A 775      15.550  29.637  42.061  1.00 49.71           O  
ANISOU 6372  OD1 ASN A 775     6276   6660   5952    668   -202   -894       O  
ATOM   6373  ND2 ASN A 775      16.701  30.910  43.509  1.00 45.98           N  
ANISOU 6373  ND2 ASN A 775     5796   6201   5472    707   -253  -1109       N  
ATOM   6374  N   TYR A 776      19.121  28.564  42.436  1.00 35.45           N  
ANISOU 6374  N   TYR A 776     4424   4925   4121    554   -248   -985       N  
ATOM   6375  CA  TYR A 776      19.349  27.126  42.640  1.00 36.15           C  
ANISOU 6375  CA  TYR A 776     4486   5108   4142    566   -226   -907       C  
ATOM   6376  C   TYR A 776      18.197  26.213  42.178  1.00 32.74           C  
ANISOU 6376  C   TYR A 776     4065   4684   3690    579   -186   -787       C  
ATOM   6377  O   TYR A 776      18.438  25.110  41.707  1.00 33.04           O  
ANISOU 6377  O   TYR A 776     4102   4734   3719    550   -162   -707       O  
ATOM   6378  CB  TYR A 776      19.730  26.836  44.098  1.00 37.59           C  
ANISOU 6378  CB  TYR A 776     4624   5427   4232    638   -242   -964       C  
ATOM   6379  CG  TYR A 776      18.565  26.824  45.065  1.00 40.34           C  
ANISOU 6379  CG  TYR A 776     4960   5858   4509    732   -231   -963       C  
ATOM   6380  CD1 TYR A 776      18.124  25.625  45.636  1.00 39.37           C  
ANISOU 6380  CD1 TYR A 776     4807   5845   4306    785   -201   -875       C  
ATOM   6381  CD2 TYR A 776      17.903  28.008  45.413  1.00 42.51           C  
ANISOU 6381  CD2 TYR A 776     5252   6102   4798    771   -245  -1046       C  
ATOM   6382  CE1 TYR A 776      17.054  25.604  46.528  1.00 42.39           C  
ANISOU 6382  CE1 TYR A 776     5170   6315   4619    873   -186   -864       C  
ATOM   6383  CE2 TYR A 776      16.829  27.997  46.306  1.00 43.43           C  
ANISOU 6383  CE2 TYR A 776     5353   6305   4843    865   -229  -1043       C  
ATOM   6384  CZ  TYR A 776      16.417  26.793  46.857  1.00 43.16           C  
ANISOU 6384  CZ  TYR A 776     5284   6391   4725    914   -200   -950       C  
ATOM   6385  OH  TYR A 776      15.366  26.772  47.728  1.00 46.87           O  
ANISOU 6385  OH  TYR A 776     5732   6956   5123   1007   -181   -938       O  
ATOM   6386  N   ILE A 777      16.956  26.673  42.302  1.00 35.24           N  
ANISOU 6386  N   ILE A 777     4391   4994   4003    622   -178   -774       N  
ATOM   6387  CA  ILE A 777      15.805  25.897  41.823  1.00 34.26           C  
ANISOU 6387  CA  ILE A 777     4271   4879   3867    625   -145   -661       C  
ATOM   6388  C   ILE A 777      15.795  25.817  40.285  1.00 34.08           C  
ANISOU 6388  C   ILE A 777     4283   4752   3914    536   -136   -599       C  
ATOM   6389  O   ILE A 777      15.499  24.769  39.708  1.00 33.67           O  
ANISOU 6389  O   ILE A 777     4236   4707   3852    503   -112   -511       O  
ATOM   6390  CB  ILE A 777      14.482  26.446  42.397  1.00 36.59           C  
ANISOU 6390  CB  ILE A 777     4558   5209   4137    700   -138   -661       C  
ATOM   6391  CG1 ILE A 777      14.418  26.164  43.898  1.00 37.78           C  
ANISOU 6391  CG1 ILE A 777     4667   5491   4195    791   -137   -697       C  
ATOM   6392  CG2 ILE A 777      13.255  25.844  41.692  1.00 37.45           C  
ANISOU 6392  CG2 ILE A 777     4668   5313   4251    685   -110   -543       C  
ATOM   6393  CD1 ILE A 777      13.564  27.150  44.673  1.00 45.33           C  
ANISOU 6393  CD1 ILE A 777     5618   6478   5129    877   -140   -759       C  
ATOM   6394  N   SER A 778      16.178  26.910  39.634  1.00 34.10           N  
ANISOU 6394  N   SER A 778     4310   4660   3986    495   -154   -647       N  
ATOM   6395  CA  SER A 778      16.184  26.977  38.176  1.00 33.20           C  
ANISOU 6395  CA  SER A 778     4226   4458   3932    416   -147   -589       C  
ATOM   6396  C   SER A 778      17.246  26.053  37.560  1.00 33.33           C  
ANISOU 6396  C   SER A 778     4245   4470   3948    353   -136   -562       C  
ATOM   6397  O   SER A 778      17.221  25.790  36.361  1.00 33.94           O  
ANISOU 6397  O   SER A 778     4345   4497   4053    291   -124   -505       O  
ATOM   6398  CB  SER A 778      16.372  28.423  37.707  1.00 32.98           C  
ANISOU 6398  CB  SER A 778     4217   4330   3983    394   -166   -640       C  
ATOM   6399  OG  SER A 778      17.742  28.785  37.719  1.00 34.96           O  
ANISOU 6399  OG  SER A 778     4467   4549   4268    352   -185   -708       O  
ATOM   6400  N   ILE A 779      18.158  25.546  38.388  1.00 32.66           N  
ANISOU 6400  N   ILE A 779     4137   4446   3826    375   -140   -602       N  
ATOM   6401  CA  ILE A 779      19.241  24.681  37.909  1.00 33.33           C  
ANISOU 6401  CA  ILE A 779     4220   4533   3910    329   -127   -580       C  
ATOM   6402  C   ILE A 779      19.287  23.281  38.574  1.00 32.82           C  
ANISOU 6402  C   ILE A 779     4136   4553   3782    369   -103   -535       C  
ATOM   6403  O   ILE A 779      20.184  22.485  38.295  1.00 30.76           O  
ANISOU 6403  O   ILE A 779     3872   4297   3517    346    -87   -515       O  
ATOM   6404  CB  ILE A 779      20.627  25.387  37.999  1.00 34.57           C  
ANISOU 6404  CB  ILE A 779     4363   4671   4103    301   -151   -657       C  
ATOM   6405  CG1 ILE A 779      20.900  25.884  39.422  1.00 36.96           C  
ANISOU 6405  CG1 ILE A 779     4631   5041   4370    362   -181   -746       C  
ATOM   6406  CG2 ILE A 779      20.699  26.549  37.018  1.00 34.77           C  
ANISOU 6406  CG2 ILE A 779     4413   4592   4207    242   -163   -673       C  
ATOM   6407  CD1 ILE A 779      22.196  26.692  39.563  1.00 40.34           C  
ANISOU 6407  CD1 ILE A 779     5040   5451   4837    325   -214   -832       C  
ATOM   6408  N   ALA A 780      18.329  22.991  39.451  1.00 31.35           N  
ANISOU 6408  N   ALA A 780     3933   4432   3546    432    -98   -513       N  
ATOM   6409  CA  ALA A 780      18.201  21.648  40.011  1.00 32.80           C  
ANISOU 6409  CA  ALA A 780     4099   4686   3678    467    -71   -449       C  
ATOM   6410  C   ALA A 780      17.566  20.718  38.993  1.00 32.56           C  
ANISOU 6410  C   ALA A 780     4098   4607   3666    416    -40   -361       C  
ATOM   6411  O   ALA A 780      16.629  21.112  38.293  1.00 32.91           O  
ANISOU 6411  O   ALA A 780     4163   4607   3735    386    -43   -337       O  
ATOM   6412  CB  ALA A 780      17.367  21.669  41.281  1.00 30.35           C  
ANISOU 6412  CB  ALA A 780     3755   4469   3308    550    -72   -447       C  
ATOM   6413  N   SER A 781      18.070  19.487  38.919  1.00 30.20           N  
ANISOU 6413  N   SER A 781     3801   4317   3357    409    -12   -315       N  
ATOM   6414  CA  SER A 781      17.446  18.461  38.084  1.00 31.21           C  
ANISOU 6414  CA  SER A 781     3959   4400   3499    363     17   -239       C  
ATOM   6415  C   SER A 781      16.158  18.001  38.753  1.00 31.95           C  
ANISOU 6415  C   SER A 781     4033   4545   3562    398     28   -178       C  
ATOM   6416  O   SER A 781      15.920  18.323  39.925  1.00 29.56           O  
ANISOU 6416  O   SER A 781     3691   4322   3218    470     19   -190       O  
ATOM   6417  CB  SER A 781      18.379  17.266  37.888  1.00 29.69           C  
ANISOU 6417  CB  SER A 781     3776   4193   3310    353     49   -212       C  
ATOM   6418  OG  SER A 781      19.443  17.599  37.022  1.00 38.49           O  
ANISOU 6418  OG  SER A 781     4911   5257   4457    310     47   -255       O  
ATOM   6419  N   VAL A 782      15.328  17.262  38.014  1.00 31.19           N  
ANISOU 6419  N   VAL A 782     3958   4410   3482    347     46   -114       N  
ATOM   6420  CA  VAL A 782      14.119  16.675  38.599  1.00 31.33           C  
ANISOU 6420  CA  VAL A 782     3950   4475   3477    371     59    -41       C  
ATOM   6421  C   VAL A 782      14.053  15.186  38.322  1.00 33.54           C  
ANISOU 6421  C   VAL A 782     4248   4724   3772    335     94     28       C  
ATOM   6422  O   VAL A 782      14.422  14.734  37.240  1.00 32.95           O  
ANISOU 6422  O   VAL A 782     4217   4572   3730    268    103     21       O  
ATOM   6423  CB  VAL A 782      12.830  17.351  38.100  1.00 31.71           C  
ANISOU 6423  CB  VAL A 782     3997   4519   3533    344     41    -23       C  
ATOM   6424  CG1 VAL A 782      11.597  16.738  38.779  1.00 33.17           C  
ANISOU 6424  CG1 VAL A 782     4143   4767   3693    369     57     58       C  
ATOM   6425  CG2 VAL A 782      12.877  18.849  38.361  1.00 24.96           C  
ANISOU 6425  CG2 VAL A 782     3130   3678   2675    384     11    -92       C  
ATOM   6426  N   SER A 783      13.596  14.432  39.319  1.00 35.77           N  
ANISOU 6426  N   SER A 783     4496   5066   4030    382    116     94       N  
ATOM   6427  CA  SER A 783      13.356  13.006  39.171  1.00 39.07           C  
ANISOU 6427  CA  SER A 783     4926   5447   4472    350    152    170       C  
ATOM   6428  C   SER A 783      12.173  12.543  40.028  1.00 42.39           C  
ANISOU 6428  C   SER A 783     5300   5935   4872    378    166    259       C  
ATOM   6429  O   SER A 783      11.686  13.288  40.883  1.00 42.94           O  
ANISOU 6429  O   SER A 783     5323   6094   4897    442    153    258       O  
ATOM   6430  CB  SER A 783      14.616  12.225  39.530  1.00 38.07           C  
ANISOU 6430  CB  SER A 783     4807   5308   4349    386    180    172       C  
ATOM   6431  OG  SER A 783      14.498  10.888  39.092  1.00 40.39           O  
ANISOU 6431  OG  SER A 783     5131   5530   4684    341    217    231       O  
ATOM   6432  N   SER A 784      11.703  11.319  39.782  1.00 44.78           N  
ANISOU 6432  N   SER A 784     5614   6192   5209    330    195    334       N  
ATOM   6433  CA  SER A 784      10.655  10.710  40.606  1.00 45.86           C  
ANISOU 6433  CA  SER A 784     5701   6388   5336    351    216    435       C  
ATOM   6434  C   SER A 784      11.263   9.831  41.688  1.00 47.04           C  
ANISOU 6434  C   SER A 784     5825   6575   5472    423    255    496       C  
ATOM   6435  O   SER A 784      12.199   9.075  41.427  1.00 48.60           O  
ANISOU 6435  O   SER A 784     6060   6704   5703    415    278    493       O  
ATOM   6436  CB  SER A 784       9.703   9.878  39.751  1.00 45.99           C  
ANISOU 6436  CB  SER A 784     5737   6333   5403    248    223    490       C  
ATOM   6437  OG  SER A 784       8.922  10.703  38.912  1.00 46.12           O  
ANISOU 6437  OG  SER A 784     5758   6347   5419    192    186    456       O  
ATOM   6438  N   ALA A 785      10.709   9.916  42.893  1.00 47.98           N  
ANISOU 6438  N   ALA A 785     5880   6809   5542    498    265    558       N  
ATOM   6439  CA  ALA A 785      11.228   9.180  44.051  1.00 49.70           C  
ANISOU 6439  CA  ALA A 785     6062   7091   5733    580    300    627       C  
ATOM   6440  C   ALA A 785      10.635   7.775  44.202  1.00 49.63           C  
ANISOU 6440  C   ALA A 785     6043   7043   5773    548    346    757       C  
ATOM   6441  O   ALA A 785       9.820   7.532  45.093  1.00 49.96           O  
ANISOU 6441  O   ALA A 785     6024   7173   5786    588    365    851       O  
ATOM   6442  CB  ALA A 785      11.009   9.990  45.328  1.00 49.79           C  
ANISOU 6442  CB  ALA A 785     6005   7259   5654    685    290    626       C  
ATOM   6443  N   ASN A 786      11.062   6.851  43.345  1.00 50.60           N  
ANISOU 6443  N   ASN A 786     6224   7031   5971    479    366    761       N  
ATOM   6444  CA  ASN A 786      10.579   5.469  43.413  1.00 52.27           C  
ANISOU 6444  CA  ASN A 786     6437   7177   6246    439    411    876       C  
ATOM   6445  C   ASN A 786      11.514   4.512  44.138  1.00 53.54           C  
ANISOU 6445  C   ASN A 786     6592   7329   6420    511    458    945       C  
ATOM   6446  O   ASN A 786      12.737   4.572  43.977  1.00 54.25           O  
ANISOU 6446  O   ASN A 786     6713   7392   6507    547    459    884       O  
ATOM   6447  CB  ASN A 786      10.249   4.935  42.021  1.00 52.82           C  
ANISOU 6447  CB  ASN A 786     6575   7097   6397    310    406    845       C  
ATOM   6448  CG  ASN A 786       9.139   5.721  41.346  1.00 51.38           C  
ANISOU 6448  CG  ASN A 786     6385   6934   6204    236    362    808       C  
ATOM   6449  OD1 ASN A 786       8.150   6.085  41.978  1.00 51.21           O  
ANISOU 6449  OD1 ASN A 786     6299   7012   6147    258    355    866       O  
ATOM   6450  ND2 ASN A 786       9.304   5.989  40.059  1.00 49.46           N  
ANISOU 6450  ND2 ASN A 786     6202   6604   5986    155    335    716       N  
ATOM   6451  N   ASN A 787      10.912   3.637  44.941  1.00 54.99           N  
ANISOU 6451  N   ASN A 787     6731   7542   6620    532    499   1081       N  
ATOM   6452  CA  ASN A 787      11.605   2.573  45.675  1.00 55.69           C  
ANISOU 6452  CA  ASN A 787     6808   7620   6732    600    552   1180       C  
ATOM   6453  C   ASN A 787      12.751   3.041  46.565  1.00 54.61           C  
ANISOU 6453  C   ASN A 787     6636   7600   6513    725    549   1158       C  
ATOM   6454  O   ASN A 787      13.859   2.496  46.510  1.00 54.39           O  
ANISOU 6454  O   ASN A 787     6635   7520   6512    761    573   1158       O  
ATOM   6455  CB  ASN A 787      12.075   1.469  44.719  1.00 57.35           C  
ANISOU 6455  CB  ASN A 787     7098   7640   7051    529    584   1178       C  
ATOM   6456  CG  ASN A 787      10.928   0.650  44.171  1.00 62.33           C  
ANISOU 6456  CG  ASN A 787     7748   8164   7769    415    600   1239       C  
ATOM   6457  OD1 ASN A 787      10.050   0.202  44.917  1.00 65.44           O  
ANISOU 6457  OD1 ASN A 787     8086   8609   8171    419    623   1364       O  
ATOM   6458  ND2 ASN A 787      10.931   0.440  42.860  1.00 60.95           N  
ANISOU 6458  ND2 ASN A 787     7653   7847   7659    309    587   1153       N  
ATOM   6459  N   ILE A 788      12.477   4.050  47.387  1.00 52.83           N  
ANISOU 6459  N   ILE A 788     6348   7537   6186    791    519   1137       N  
ATOM   6460  CA  ILE A 788      13.476   4.561  48.319  1.00 52.36           C  
ANISOU 6460  CA  ILE A 788     6248   7610   6037    906    508   1109       C  
ATOM   6461  C   ILE A 788      13.894   3.465  49.295  1.00 54.07           C  
ANISOU 6461  C   ILE A 788     6421   7872   6250    989    562   1252       C  
ATOM   6462  O   ILE A 788      15.083   3.214  49.470  1.00 55.13           O  
ANISOU 6462  O   ILE A 788     6559   8011   6378   1046    572   1243       O  
ATOM   6463  CB  ILE A 788      12.974   5.789  49.106  1.00 52.63           C  
ANISOU 6463  CB  ILE A 788     6223   7813   5961    964    469   1060       C  
ATOM   6464  CG1 ILE A 788      12.341   6.816  48.166  1.00 48.68           C  
ANISOU 6464  CG1 ILE A 788     5759   7262   5474    884    423    946       C  
ATOM   6465  CG2 ILE A 788      14.120   6.411  49.921  1.00 51.88           C  
ANISOU 6465  CG2 ILE A 788     6093   7845   5774   1066    447    998       C  
ATOM   6466  CD1 ILE A 788      11.547   7.889  48.893  1.00 51.85           C  
ANISOU 6466  CD1 ILE A 788     6106   7808   5786    936    397    918       C  
ATOM   6467  N   ALA A 789      12.913   2.802  49.905  1.00 55.51           N  
ANISOU 6467  N   ALA A 789     6559   8090   6442    995    600   1391       N  
ATOM   6468  CA  ALA A 789      13.182   1.751  50.893  1.00 57.47           C  
ANISOU 6468  CA  ALA A 789     6758   8389   6689   1076    656   1551       C  
ATOM   6469  C   ALA A 789      14.053   0.621  50.341  1.00 57.27           C  
ANISOU 6469  C   ALA A 789     6790   8202   6769   1060    698   1591       C  
ATOM   6470  O   ALA A 789      14.867   0.056  51.067  1.00 59.02           O  
ANISOU 6470  O   ALA A 789     6980   8475   6972   1154    732   1674       O  
ATOM   6471  CB  ALA A 789      11.873   1.198  51.461  1.00 57.61           C  
ANISOU 6471  CB  ALA A 789     6723   8448   6719   1063    692   1701       C  
ATOM   6472  N   LYS A 790      13.881   0.307  49.058  1.00 56.39           N  
ANISOU 6472  N   LYS A 790     6761   7901   6762    945    698   1530       N  
ATOM   6473  CA  LYS A 790      14.646  -0.749  48.391  1.00 56.92           C  
ANISOU 6473  CA  LYS A 790     6895   7796   6937    922    740   1548       C  
ATOM   6474  C   LYS A 790      16.157  -0.504  48.446  1.00 55.86           C  
ANISOU 6474  C   LYS A 790     6767   7694   6764   1005    733   1482       C  
ATOM   6475  O   LYS A 790      16.945  -1.446  48.567  1.00 55.36           O  
ANISOU 6475  O   LYS A 790     6715   7567   6753   1056    783   1554       O  
ATOM   6476  CB  LYS A 790      14.186  -0.890  46.935  1.00 57.12           C  
ANISOU 6476  CB  LYS A 790     7009   7635   7057    781    727   1457       C  
ATOM   6477  CG  LYS A 790      14.999  -1.863  46.089  1.00 58.13           C  
ANISOU 6477  CG  LYS A 790     7219   7577   7291    754    767   1440       C  
ATOM   6478  CD  LYS A 790      14.376  -2.062  44.719  1.00 60.31           C  
ANISOU 6478  CD  LYS A 790     7579   7687   7652    610    754   1357       C  
ATOM   6479  CE  LYS A 790      15.181  -3.037  43.879  1.00 62.12           C  
ANISOU 6479  CE  LYS A 790     7893   7730   7980    589    798   1329       C  
ATOM   6480  NZ  LYS A 790      14.513  -3.308  42.578  1.00 64.56           N  
ANISOU 6480  NZ  LYS A 790     8282   7883   8366    446    785   1248       N  
ATOM   6481  N   TYR A 791      16.546   0.765  48.363  1.00 53.94           N  
ANISOU 6481  N   TYR A 791     6514   7548   6435   1017    673   1348       N  
ATOM   6482  CA  TYR A 791      17.954   1.141  48.319  1.00 53.08           C  
ANISOU 6482  CA  TYR A 791     6406   7474   6289   1078    658   1270       C  
ATOM   6483  C   TYR A 791      18.432   1.810  49.611  1.00 54.54           C  
ANISOU 6483  C   TYR A 791     6500   7877   6346   1193    632   1282       C  
ATOM   6484  O   TYR A 791      19.538   2.356  49.657  1.00 53.34           O  
ANISOU 6484  O   TYR A 791     6335   7785   6146   1237    604   1202       O  
ATOM   6485  CB  TYR A 791      18.218   2.051  47.114  1.00 51.16           C  
ANISOU 6485  CB  TYR A 791     6224   7158   6057    995    609   1099       C  
ATOM   6486  CG  TYR A 791      18.014   1.391  45.769  1.00 47.83           C  
ANISOU 6486  CG  TYR A 791     5894   6532   5748    890    633   1068       C  
ATOM   6487  CD1 TYR A 791      16.848   1.607  45.037  1.00 45.66           C  
ANISOU 6487  CD1 TYR A 791     5656   6187   5507    782    612   1033       C  
ATOM   6488  CD2 TYR A 791      18.997   0.562  45.218  1.00 49.35           C  
ANISOU 6488  CD2 TYR A 791     6135   6608   6010    903    675   1070       C  
ATOM   6489  CE1 TYR A 791      16.658   1.014  43.789  1.00 45.94           C  
ANISOU 6489  CE1 TYR A 791     5774   6046   5635    681    628    994       C  
ATOM   6490  CE2 TYR A 791      18.821  -0.040  43.970  1.00 48.09           C  
ANISOU 6490  CE2 TYR A 791     6063   6263   5946    809    697   1028       C  
ATOM   6491  CZ  TYR A 791      17.648   0.190  43.263  1.00 47.71           C  
ANISOU 6491  CZ  TYR A 791     6050   6153   5923    695    671    987       C  
ATOM   6492  OH  TYR A 791      17.461  -0.403  42.035  1.00 46.67           O  
ANISOU 6492  OH  TYR A 791     6004   5851   5877    599    687    937       O  
ATOM   6493  N   ASP A 792      17.596   1.769  50.649  1.00 57.61           N  
ANISOU 6493  N   ASP A 792     6824   8390   6676   1239    640   1381       N  
ATOM   6494  CA  ASP A 792      17.955   2.306  51.960  1.00 60.75           C  
ANISOU 6494  CA  ASP A 792     7132   9009   6941   1353    620   1401       C  
ATOM   6495  C   ASP A 792      18.577   1.207  52.827  1.00 63.48           C  
ANISOU 6495  C   ASP A 792     7429   9408   7284   1455    675   1561       C  
ATOM   6496  O   ASP A 792      17.877   0.317  53.325  1.00 64.95           O  
ANISOU 6496  O   ASP A 792     7589   9589   7500   1473    727   1718       O  
ATOM   6497  CB  ASP A 792      16.726   2.916  52.655  1.00 62.04           C  
ANISOU 6497  CB  ASP A 792     7246   9298   7027   1360    602   1419       C  
ATOM   6498  CG  ASP A 792      17.083   3.744  53.899  1.00 64.58           C  
ANISOU 6498  CG  ASP A 792     7486   9856   7196   1469    567   1390       C  
ATOM   6499  OD1 ASP A 792      18.054   3.413  54.618  1.00 66.54           O  
ANISOU 6499  OD1 ASP A 792     7687  10204   7393   1561    577   1440       O  
ATOM   6500  OD2 ASP A 792      16.373   4.739  54.162  1.00 65.04           O  
ANISOU 6500  OD2 ASP A 792     7525  10005   7183   1466    529   1314       O  
ATOM   6501  N   VAL A 793      19.896   1.271  52.993  1.00 64.14           N  
ANISOU 6501  N   VAL A 793     7492   9543   7334   1521    665   1529       N  
ATOM   6502  CA  VAL A 793      20.606   0.368  53.893  1.00 64.80           C  
ANISOU 6502  CA  VAL A 793     7516   9709   7396   1635    711   1678       C  
ATOM   6503  C   VAL A 793      21.087   1.171  55.107  1.00 66.42           C  
ANISOU 6503  C   VAL A 793     7625  10172   7438   1738    665   1655       C  
ATOM   6504  O   VAL A 793      22.171   1.761  55.089  1.00 67.32           O  
ANISOU 6504  O   VAL A 793     7723  10354   7502   1766    623   1555       O  
ATOM   6505  CB  VAL A 793      21.772  -0.383  53.176  1.00 64.91           C  
ANISOU 6505  CB  VAL A 793     7575   9584   7504   1644    745   1685       C  
ATOM   6506  CG1 VAL A 793      22.522  -1.299  54.144  1.00 66.08           C  
ANISOU 6506  CG1 VAL A 793     7653   9825   7629   1774    794   1850       C  
ATOM   6507  CG2 VAL A 793      21.244  -1.203  52.008  1.00 64.44           C  
ANISOU 6507  CG2 VAL A 793     7614   9271   7600   1543    791   1698       C  
ATOM   6508  N   GLY A 794      20.251   1.206  56.145  1.00 67.00           N  
ANISOU 6508  N   GLY A 794     7635  10395   7427   1789    672   1745       N  
ATOM   6509  CA  GLY A 794      20.531   1.944  57.381  1.00 67.29           C  
ANISOU 6509  CA  GLY A 794     7579  10694   7296   1888    631   1724       C  
ATOM   6510  C   GLY A 794      20.876   3.415  57.203  1.00 66.05           C  
ANISOU 6510  C   GLY A 794     7429  10607   7060   1858    547   1509       C  
ATOM   6511  O   GLY A 794      21.808   3.917  57.833  1.00 67.49           O  
ANISOU 6511  O   GLY A 794     7555  10949   7140   1926    505   1453       O  
ATOM   6512  N   GLY A 795      20.130   4.102  56.339  1.00 63.61           N  
ANISOU 6512  N   GLY A 795     7187  10179   6803   1755    521   1391       N  
ATOM   6513  CA  GLY A 795      20.342   5.530  56.078  1.00 60.86           C  
ANISOU 6513  CA  GLY A 795     6854   9868   6400   1716    445   1190       C  
ATOM   6514  C   GLY A 795      21.361   5.836  54.991  1.00 58.49           C  
ANISOU 6514  C   GLY A 795     6612   9436   6176   1650    417   1070       C  
ATOM   6515  O   GLY A 795      21.585   6.999  54.652  1.00 56.74           O  
ANISOU 6515  O   GLY A 795     6409   9220   5930   1606    357    907       O  
ATOM   6516  N   PHE A 796      21.977   4.790  54.443  1.00 57.96           N  
ANISOU 6516  N   PHE A 796     6571   9247   6203   1645    464   1153       N  
ATOM   6517  CA  PHE A 796      23.020   4.938  53.431  1.00 56.06           C  
ANISOU 6517  CA  PHE A 796     6378   8890   6031   1594    449   1059       C  
ATOM   6518  C   PHE A 796      22.701   4.141  52.161  1.00 53.50           C  
ANISOU 6518  C   PHE A 796     6145   8329   5855   1509    498   1089       C  
ATOM   6519  O   PHE A 796      21.964   3.152  52.226  1.00 54.87           O  
ANISOU 6519  O   PHE A 796     6332   8431   6083   1510    554   1219       O  
ATOM   6520  CB  PHE A 796      24.383   4.545  54.013  1.00 57.60           C  
ANISOU 6520  CB  PHE A 796     6509   9194   6183   1687    453   1106       C  
ATOM   6521  CG  PHE A 796      24.910   5.523  55.035  1.00 59.51           C  
ANISOU 6521  CG  PHE A 796     6667   9662   6280   1748    387   1027       C  
ATOM   6522  CD1 PHE A 796      25.564   6.686  54.633  1.00 59.82           C  
ANISOU 6522  CD1 PHE A 796     6714   9715   6299   1697    319    853       C  
ATOM   6523  CD2 PHE A 796      24.754   5.281  56.396  1.00 62.55           C  
ANISOU 6523  CD2 PHE A 796     6967  10249   6550   1853    392   1126       C  
ATOM   6524  CE1 PHE A 796      26.054   7.597  55.574  1.00 61.71           C  
ANISOU 6524  CE1 PHE A 796     6879  10157   6409   1744    254    767       C  
ATOM   6525  CE2 PHE A 796      25.240   6.186  57.347  1.00 64.57           C  
ANISOU 6525  CE2 PHE A 796     7147  10722   6664   1908    327   1041       C  
ATOM   6526  CZ  PHE A 796      25.891   7.346  56.933  1.00 64.12           C  
ANISOU 6526  CZ  PHE A 796     7102  10668   6593   1850    256    855       C  
ATOM   6527  N   PRO A 797      23.246   4.571  51.001  1.00 50.73           N  
ANISOU 6527  N   PRO A 797     5855   7855   5566   1432    477    969       N  
ATOM   6528  CA  PRO A 797      22.903   3.944  49.717  1.00 48.41           C  
ANISOU 6528  CA  PRO A 797     5652   7343   5398   1343    516    971       C  
ATOM   6529  C   PRO A 797      23.275   2.467  49.640  1.00 48.82           C  
ANISOU 6529  C   PRO A 797     5719   7299   5529   1384    591   1107       C  
ATOM   6530  O   PRO A 797      24.420   2.108  49.915  1.00 48.37           O  
ANISOU 6530  O   PRO A 797     5627   7289   5462   1459    607   1140       O  
ATOM   6531  CB  PRO A 797      23.736   4.738  48.703  1.00 46.51           C  
ANISOU 6531  CB  PRO A 797     5451   7041   5180   1283    477    823       C  
ATOM   6532  CG  PRO A 797      24.069   6.011  49.376  1.00 47.66           C  
ANISOU 6532  CG  PRO A 797     5537   7349   5221   1309    409    725       C  
ATOM   6533  CD  PRO A 797      24.189   5.693  50.821  1.00 49.00           C  
ANISOU 6533  CD  PRO A 797     5619   7698   5299   1421    414    823       C  
ATOM   6534  N   GLY A 798      22.307   1.630  49.269  1.00 48.24           N  
ANISOU 6534  N   GLY A 798     5695   7093   5539   1335    637   1184       N  
ATOM   6535  CA  GLY A 798      22.558   0.214  48.999  1.00 48.86           C  
ANISOU 6535  CA  GLY A 798     5809   7035   5720   1355    713   1299       C  
ATOM   6536  C   GLY A 798      23.211  -0.008  47.640  1.00 48.63           C  
ANISOU 6536  C   GLY A 798     5864   6834   5781   1295    728   1210       C  
ATOM   6537  O   GLY A 798      23.521   0.957  46.947  1.00 47.12           O  
ANISOU 6537  O   GLY A 798     5695   6643   5566   1240    680   1069       O  
ATOM   6538  N   PRO A 799      23.434  -1.284  47.251  1.00 50.19           N  
ANISOU 6538  N   PRO A 799     6108   6881   6081   1306    800   1292       N  
ATOM   6539  CA  PRO A 799      24.009  -1.605  45.935  1.00 50.73           C  
ANISOU 6539  CA  PRO A 799     6261   6779   6234   1254    824   1208       C  
ATOM   6540  C   PRO A 799      23.118  -1.133  44.772  1.00 50.90           C  
ANISOU 6540  C   PRO A 799     6362   6686   6291   1115    792   1091       C  
ATOM   6541  O   PRO A 799      21.889  -1.207  44.863  1.00 51.04           O  
ANISOU 6541  O   PRO A 799     6390   6678   6324   1053    785   1123       O  
ATOM   6542  CB  PRO A 799      24.099  -3.139  45.949  1.00 51.05           C  
ANISOU 6542  CB  PRO A 799     6336   6679   6382   1296    910   1337       C  
ATOM   6543  CG  PRO A 799      24.080  -3.519  47.396  1.00 52.42           C  
ANISOU 6543  CG  PRO A 799     6420   6991   6508   1405    930   1496       C  
ATOM   6544  CD  PRO A 799      23.206  -2.499  48.061  1.00 52.72           C  
ANISOU 6544  CD  PRO A 799     6403   7186   6445   1378    865   1472       C  
ATOM   6545  N   LYS A 800      23.744  -0.651  43.699  1.00 49.83           N  
ANISOU 6545  N   LYS A 800     6274   6494   6165   1068    775    964       N  
ATOM   6546  CA  LYS A 800      23.039  -0.138  42.510  1.00 49.68           C  
ANISOU 6546  CA  LYS A 800     6327   6380   6170    941    743    848       C  
ATOM   6547  C   LYS A 800      22.140   1.080  42.788  1.00 47.58           C  
ANISOU 6547  C   LYS A 800     6026   6224   5830    891    672    798       C  
ATOM   6548  O   LYS A 800      21.222   1.362  42.013  1.00 46.83           O  
ANISOU 6548  O   LYS A 800     5978   6058   5756    789    649    742       O  
ATOM   6549  CB  LYS A 800      22.223  -1.247  41.822  1.00 51.18           C  
ANISOU 6549  CB  LYS A 800     6597   6387   6463    868    790    881       C  
ATOM   6550  CG  LYS A 800      23.026  -2.478  41.434  1.00 57.47           C  
ANISOU 6550  CG  LYS A 800     7443   7046   7345    913    865    918       C  
ATOM   6551  CD  LYS A 800      22.130  -3.582  40.890  1.00 62.54           C  
ANISOU 6551  CD  LYS A 800     8163   7505   8093    836    908    951       C  
ATOM   6552  CE  LYS A 800      22.964  -4.755  40.390  1.00 68.18           C  
ANISOU 6552  CE  LYS A 800     8939   8066   8899    880    986    966       C  
ATOM   6553  NZ  LYS A 800      22.148  -5.988  40.184  1.00 71.48           N  
ANISOU 6553  NZ  LYS A 800     9421   8306   9430    825   1036   1027       N  
ATOM   6554  N   CYS A 801      22.409   1.801  43.878  1.00 45.65           N  
ANISOU 6554  N   CYS A 801     5697   6150   5497    964    637    815       N  
ATOM   6555  CA  CYS A 801      21.559   2.921  44.288  1.00 44.01           C  
ANISOU 6555  CA  CYS A 801     5454   6049   5218    935    577    772       C  
ATOM   6556  C   CYS A 801      21.532   4.045  43.249  1.00 42.65           C  
ANISOU 6556  C   CYS A 801     5321   5847   5038    849    526    630       C  
ATOM   6557  O   CYS A 801      22.576   4.623  42.939  1.00 42.02           O  
ANISOU 6557  O   CYS A 801     5235   5793   4937    863    506    553       O  
ATOM   6558  CB  CYS A 801      21.986   3.478  45.643  1.00 43.00           C  
ANISOU 6558  CB  CYS A 801     5232   6113   4991   1035    550    800       C  
ATOM   6559  SG  CYS A 801      20.895   4.792  46.250  1.00 43.99           S  
ANISOU 6559  SG  CYS A 801     5316   6369   5030   1015    485    748       S  
ATOM   6560  N   PRO A 802      20.332   4.359  42.713  1.00 40.56           N  
ANISOU 6560  N   PRO A 802     5089   5532   4788    761    504    603       N  
ATOM   6561  CA  PRO A 802      20.243   5.429  41.713  1.00 38.45           C  
ANISOU 6561  CA  PRO A 802     4858   5238   4515    683    458    482       C  
ATOM   6562  C   PRO A 802      20.650   6.788  42.282  1.00 36.10           C  
ANISOU 6562  C   PRO A 802     4505   5071   4139    720    402    412       C  
ATOM   6563  O   PRO A 802      20.501   7.044  43.492  1.00 35.60           O  
ANISOU 6563  O   PRO A 802     4377   5133   4015    791    389    450       O  
ATOM   6564  CB  PRO A 802      18.766   5.412  41.290  1.00 34.42           C  
ANISOU 6564  CB  PRO A 802     4375   4676   4028    598    447    495       C  
ATOM   6565  CG  PRO A 802      18.298   4.040  41.623  1.00 40.38           C  
ANISOU 6565  CG  PRO A 802     5138   5370   4836    606    500    609       C  
ATOM   6566  CD  PRO A 802      19.029   3.698  42.910  1.00 39.87           C  
ANISOU 6566  CD  PRO A 802     5009   5405   4733    725    524    689       C  
ATOM   6567  N   PHE A 803      21.182   7.629  41.405  1.00 33.47           N  
ANISOU 6567  N   PHE A 803     4198   4709   3809    673    373    309       N  
ATOM   6568  CA  PHE A 803      21.724   8.927  41.779  1.00 34.59           C  
ANISOU 6568  CA  PHE A 803     4297   4949   3896    696    321    229       C  
ATOM   6569  C   PHE A 803      20.728   9.787  42.545  1.00 35.55           C  
ANISOU 6569  C   PHE A 803     4382   5159   3965    707    281    219       C  
ATOM   6570  O   PHE A 803      21.086  10.402  43.549  1.00 37.28           O  
ANISOU 6570  O   PHE A 803     4545   5498   4122    770    253    198       O  
ATOM   6571  CB  PHE A 803      22.206   9.656  40.532  1.00 34.79           C  
ANISOU 6571  CB  PHE A 803     4365   4905   3950    623    300    134       C  
ATOM   6572  CG  PHE A 803      22.967  10.923  40.813  1.00 35.10           C  
ANISOU 6572  CG  PHE A 803     4363   5024   3950    638    252     51       C  
ATOM   6573  CD1 PHE A 803      24.320  10.882  41.127  1.00 34.83           C  
ANISOU 6573  CD1 PHE A 803     4290   5042   3902    686    255     38       C  
ATOM   6574  CD2 PHE A 803      22.338  12.161  40.717  1.00 30.76           C  
ANISOU 6574  CD2 PHE A 803     3813   4490   3384    600    203    -13       C  
ATOM   6575  CE1 PHE A 803      25.038  12.064  41.364  1.00 34.28           C  
ANISOU 6575  CE1 PHE A 803     4179   5042   3803    686    206    -43       C  
ATOM   6576  CE2 PHE A 803      23.039  13.345  40.954  1.00 32.99           C  
ANISOU 6576  CE2 PHE A 803     4062   4829   3643    605    159    -95       C  
ATOM   6577  CZ  PHE A 803      24.394  13.294  41.277  1.00 33.99           C  
ANISOU 6577  CZ  PHE A 803     4148   5008   3757    643    158   -113       C  
ATOM   6578  N   HIS A 804      19.479   9.824  42.088  1.00 34.73           N  
ANISOU 6578  N   HIS A 804     4309   5003   3882    648    278    233       N  
ATOM   6579  CA  HIS A 804      18.473  10.664  42.745  1.00 34.34           C  
ANISOU 6579  CA  HIS A 804     4227   5036   3787    663    245    225       C  
ATOM   6580  C   HIS A 804      18.022  10.093  44.093  1.00 36.21           C  
ANISOU 6580  C   HIS A 804     4406   5376   3975    744    266    318       C  
ATOM   6581  O   HIS A 804      17.665  10.847  45.006  1.00 35.87           O  
ANISOU 6581  O   HIS A 804     4315   5446   3866    796    240    299       O  
ATOM   6582  CB  HIS A 804      17.290  10.958  41.815  1.00 33.43           C  
ANISOU 6582  CB  HIS A 804     4150   4845   3705    578    234    214       C  
ATOM   6583  CG  HIS A 804      16.512   9.745  41.414  1.00 33.87           C  
ANISOU 6583  CG  HIS A 804     4234   4825   3809    532    272    301       C  
ATOM   6584  ND1 HIS A 804      17.021   8.772  40.579  1.00 35.89           N  
ANISOU 6584  ND1 HIS A 804     4541   4972   4122    490    306    313       N  
ATOM   6585  CD2 HIS A 804      15.260   9.347  41.734  1.00 33.19           C  
ANISOU 6585  CD2 HIS A 804     4131   4755   3725    520    283    376       C  
ATOM   6586  CE1 HIS A 804      16.117   7.825  40.407  1.00 34.55           C  
ANISOU 6586  CE1 HIS A 804     4389   4747   3992    448    333    386       C  
ATOM   6587  NE2 HIS A 804      15.040   8.149  41.098  1.00 37.20           N  
ANISOU 6587  NE2 HIS A 804     4680   5159   4296    462    319    431       N  
ATOM   6588  N   ILE A 805      18.077   8.768  44.218  1.00 36.13           N  
ANISOU 6588  N   ILE A 805     4401   5329   3999    758    316    417       N  
ATOM   6589  CA  ILE A 805      17.724   8.074  45.460  1.00 37.56           C  
ANISOU 6589  CA  ILE A 805     4526   5603   4141    836    345    528       C  
ATOM   6590  C   ILE A 805      18.798   8.296  46.531  1.00 38.51           C  
ANISOU 6590  C   ILE A 805     4587   5856   4190    936    335    521       C  
ATOM   6591  O   ILE A 805      18.494   8.435  47.715  1.00 41.10           O  
ANISOU 6591  O   ILE A 805     4853   6320   4443   1011    331    563       O  
ATOM   6592  CB  ILE A 805      17.470   6.559  45.203  1.00 37.49           C  
ANISOU 6592  CB  ILE A 805     4544   5493   4206    814    405    643       C  
ATOM   6593  CG1 ILE A 805      16.320   6.368  44.202  1.00 37.18           C  
ANISOU 6593  CG1 ILE A 805     4556   5340   4230    707    406    645       C  
ATOM   6594  CG2 ILE A 805      17.142   5.837  46.493  1.00 38.40           C  
ANISOU 6594  CG2 ILE A 805     4598   5707   4286    896    439    774       C  
ATOM   6595  CD1 ILE A 805      14.954   6.930  44.683  1.00 32.94           C  
ANISOU 6595  CD1 ILE A 805     3979   4883   3653    700    385    672       C  
ATOM   6596  N   ARG A 806      20.052   8.337  46.096  1.00 39.30           N  
ANISOU 6596  N   ARG A 806     4702   5924   4308    937    330    467       N  
ATOM   6597  CA  ARG A 806      21.177   8.725  46.938  1.00 39.13           C  
ANISOU 6597  CA  ARG A 806     4622   6028   4218   1015    308    436       C  
ATOM   6598  C   ARG A 806      20.946  10.122  47.531  1.00 40.27           C  
ANISOU 6598  C   ARG A 806     4731   6285   4285   1031    248    338       C  
ATOM   6599  O   ARG A 806      21.184  10.356  48.720  1.00 39.80           O  
ANISOU 6599  O   ARG A 806     4606   6377   4140   1112    232    345       O  
ATOM   6600  CB  ARG A 806      22.461   8.715  46.101  1.00 38.94           C  
ANISOU 6600  CB  ARG A 806     4624   5935   4238    990    308    378       C  
ATOM   6601  CG  ARG A 806      23.727   9.106  46.858  1.00 40.90           C  
ANISOU 6601  CG  ARG A 806     4807   6311   4424   1060    282    344       C  
ATOM   6602  CD  ARG A 806      24.957   9.026  45.961  1.00 41.40           C  
ANISOU 6602  CD  ARG A 806     4890   6303   4536   1032    289    300       C  
ATOM   6603  NE  ARG A 806      25.250   7.652  45.552  1.00 42.62           N  
ANISOU 6603  NE  ARG A 806     5074   6367   4754   1050    356    396       N  
ATOM   6604  CZ  ARG A 806      26.076   6.827  46.194  1.00 43.95           C  
ANISOU 6604  CZ  ARG A 806     5196   6595   4909   1137    389    480       C  
ATOM   6605  NH1 ARG A 806      26.715   7.229  47.293  1.00 43.02           N  
ANISOU 6605  NH1 ARG A 806     4994   6646   4706   1212    356    480       N  
ATOM   6606  NH2 ARG A 806      26.261   5.593  45.738  1.00 36.62           N  
ANISOU 6606  NH2 ARG A 806     4304   5559   4050   1152    454    562       N  
ATOM   6607  N   GLY A 807      20.479  11.041  46.687  1.00 39.22           N  
ANISOU 6607  N   GLY A 807     4642   6077   4183    954    217    247       N  
ATOM   6608  CA  GLY A 807      20.205  12.412  47.094  1.00 38.47           C  
ANISOU 6608  CA  GLY A 807     4526   6056   4034    962    164    145       C  
ATOM   6609  C   GLY A 807      19.126  12.494  48.149  1.00 39.71           C  
ANISOU 6609  C   GLY A 807     4643   6323   4124   1021    166    191       C  
ATOM   6610  O   GLY A 807      19.195  13.329  49.054  1.00 41.32           O  
ANISOU 6610  O   GLY A 807     4804   6647   4248   1077    132    127       O  
ATOM   6611  N   ILE A 808      18.133  11.616  48.035  1.00 40.17           N  
ANISOU 6611  N   ILE A 808     4712   6340   4211   1008    209    299       N  
ATOM   6612  CA  ILE A 808      17.043  11.561  49.000  1.00 40.89           C  
ANISOU 6612  CA  ILE A 808     4758   6536   4241   1064    221    365       C  
ATOM   6613  C   ILE A 808      17.556  11.036  50.335  1.00 42.85           C  
ANISOU 6613  C   ILE A 808     4937   6937   4406   1169    237    433       C  
ATOM   6614  O   ILE A 808      17.178  11.545  51.391  1.00 45.33           O  
ANISOU 6614  O   ILE A 808     5199   7397   4627   1241    222    422       O  
ATOM   6615  CB  ILE A 808      15.877  10.683  48.491  1.00 41.39           C  
ANISOU 6615  CB  ILE A 808     4845   6514   4368   1012    263    474       C  
ATOM   6616  CG1 ILE A 808      15.116  11.399  47.374  1.00 38.02           C  
ANISOU 6616  CG1 ILE A 808     4468   5982   3994    922    239    408       C  
ATOM   6617  CG2 ILE A 808      14.922  10.309  49.639  1.00 39.50           C  
ANISOU 6617  CG2 ILE A 808     4543   6400   4065   1082    290    581       C  
ATOM   6618  CD1 ILE A 808      14.334  10.472  46.497  1.00 33.32           C  
ANISOU 6618  CD1 ILE A 808     3911   5270   3481    841    271    490       C  
ATOM   6619  N   LEU A 809      18.413  10.019  50.284  1.00 42.91           N  
ANISOU 6619  N   LEU A 809     4943   6917   4445   1183    268    505       N  
ATOM   6620  CA  LEU A 809      18.977   9.445  51.499  1.00 44.13           C  
ANISOU 6620  CA  LEU A 809     5028   7217   4523   1286    285    585       C  
ATOM   6621  C   LEU A 809      19.896  10.442  52.197  1.00 45.27           C  
ANISOU 6621  C   LEU A 809     5128   7499   4574   1339    230    471       C  
ATOM   6622  O   LEU A 809      19.880  10.544  53.428  1.00 49.29           O  
ANISOU 6622  O   LEU A 809     5570   8182   4976   1429    222    495       O  
ATOM   6623  CB  LEU A 809      19.709   8.140  51.197  1.00 44.10           C  
ANISOU 6623  CB  LEU A 809     5036   7137   4585   1291    334    690       C  
ATOM   6624  CG  LEU A 809      18.826   6.979  50.739  1.00 44.36           C  
ANISOU 6624  CG  LEU A 809     5104   7047   4705   1250    393    817       C  
ATOM   6625  CD1 LEU A 809      19.677   5.893  50.117  1.00 45.34           C  
ANISOU 6625  CD1 LEU A 809     5263   7049   4916   1237    436    874       C  
ATOM   6626  CD2 LEU A 809      18.015   6.429  51.898  1.00 44.73           C  
ANISOU 6626  CD2 LEU A 809     5088   7214   4695   1322    427    953       C  
ATOM   6627  N   THR A 810      20.668  11.190  51.406  1.00 43.04           N  
ANISOU 6627  N   THR A 810     4881   7141   4330   1280    190    346       N  
ATOM   6628  CA  THR A 810      21.477  12.290  51.918  1.00 42.86           C  
ANISOU 6628  CA  THR A 810     4824   7225   4237   1305    130    216       C  
ATOM   6629  C   THR A 810      20.553  13.261  52.644  1.00 44.68           C  
ANISOU 6629  C   THR A 810     5036   7552   4390   1336    100    149       C  
ATOM   6630  O   THR A 810      20.793  13.610  53.797  1.00 45.08           O  
ANISOU 6630  O   THR A 810     5026   7772   4331   1414     75    119       O  
ATOM   6631  CB  THR A 810      22.235  13.020  50.785  1.00 43.32           C  
ANISOU 6631  CB  THR A 810     4931   7160   4369   1217     96     97       C  
ATOM   6632  OG1 THR A 810      23.058  12.088  50.068  1.00 40.80           O  
ANISOU 6632  OG1 THR A 810     4630   6752   4120   1194    130    160       O  
ATOM   6633  CG2 THR A 810      23.111  14.145  51.339  1.00 40.11           C  
ANISOU 6633  CG2 THR A 810     4484   6859   3899   1233     31    -37       C  
ATOM   6634  N   TYR A 811      19.482  13.664  51.963  1.00 45.41           N  
ANISOU 6634  N   TYR A 811     5179   7540   4535   1280    105    128       N  
ATOM   6635  CA  TYR A 811      18.453  14.512  52.548  1.00 44.82           C  
ANISOU 6635  CA  TYR A 811     5091   7539   4399   1313     88     79       C  
ATOM   6636  C   TYR A 811      17.903  13.939  53.851  1.00 46.14           C  
ANISOU 6636  C   TYR A 811     5191   7877   4463   1415    118    180       C  
ATOM   6637  O   TYR A 811      17.842  14.647  54.854  1.00 46.38           O  
ANISOU 6637  O   TYR A 811     5179   8056   4388   1486     90    112       O  
ATOM   6638  CB  TYR A 811      17.313  14.739  51.551  1.00 41.99           C  
ANISOU 6638  CB  TYR A 811     4789   7042   4123   1240    102     85       C  
ATOM   6639  CG  TYR A 811      16.241  15.677  52.047  1.00 40.21           C  
ANISOU 6639  CG  TYR A 811     4552   6882   3845   1277     88     32       C  
ATOM   6640  CD1 TYR A 811      16.419  17.054  52.001  1.00 39.52           C  
ANISOU 6640  CD1 TYR A 811     4483   6786   3746   1270     39   -123       C  
ATOM   6641  CD2 TYR A 811      15.041  15.183  52.564  1.00 41.62           C  
ANISOU 6641  CD2 TYR A 811     4699   7126   3988   1320    128    139       C  
ATOM   6642  CE1 TYR A 811      15.431  17.920  52.466  1.00 43.52           C  
ANISOU 6642  CE1 TYR A 811     4981   7347   4207   1315     31   -175       C  
ATOM   6643  CE2 TYR A 811      14.053  16.032  53.023  1.00 41.95           C  
ANISOU 6643  CE2 TYR A 811     4726   7234   3978   1364    121     94       C  
ATOM   6644  CZ  TYR A 811      14.252  17.401  52.978  1.00 45.51           C  
ANISOU 6644  CZ  TYR A 811     5200   7674   4418   1365     74    -66       C  
ATOM   6645  OH  TYR A 811      13.265  18.250  53.443  1.00 48.29           O  
ANISOU 6645  OH  TYR A 811     5540   8087   4722   1419     72   -114       O  
ATOM   6646  N   ASN A 812      17.501  12.667  53.831  1.00 48.37           N  
ANISOU 6646  N   ASN A 812     5464   8138   4777   1422    175    342       N  
ATOM   6647  CA  ASN A 812      16.902  12.022  55.010  1.00 51.84           C  
ANISOU 6647  CA  ASN A 812     5836   8732   5129   1514    212    466       C  
ATOM   6648  C   ASN A 812      17.817  12.041  56.229  1.00 54.66           C  
ANISOU 6648  C   ASN A 812     6123   9281   5364   1614    193    457       C  
ATOM   6649  O   ASN A 812      17.348  12.217  57.352  1.00 58.61           O  
ANISOU 6649  O   ASN A 812     6565   9955   5749   1701    196    477       O  
ATOM   6650  CB  ASN A 812      16.478  10.579  54.710  1.00 51.87           C  
ANISOU 6650  CB  ASN A 812     5844   8657   5207   1494    277    647       C  
ATOM   6651  CG  ASN A 812      15.240  10.492  53.833  1.00 49.33           C  
ANISOU 6651  CG  ASN A 812     5568   8201   4972   1412    298    680       C  
ATOM   6652  OD1 ASN A 812      14.560  11.483  53.582  1.00 48.64           O  
ANISOU 6652  OD1 ASN A 812     5500   8104   4878   1388    271    588       O  
ATOM   6653  ND2 ASN A 812      14.946   9.291  53.359  1.00 50.51           N  
ANISOU 6653  ND2 ASN A 812     5736   8247   5208   1369    348    812       N  
ATOM   6654  N   ARG A 813      19.118  11.865  56.002  1.00 56.07           N  
ANISOU 6654  N   ARG A 813     6302   9439   5563   1602    173    426       N  
ATOM   6655  CA  ARG A 813      20.105  11.934  57.080  1.00 56.66           C  
ANISOU 6655  CA  ARG A 813     6305   9701   5522   1688    146    408       C  
ATOM   6656  C   ARG A 813      20.274  13.343  57.636  1.00 56.89           C  
ANISOU 6656  C   ARG A 813     6318   9840   5457   1708     78    226       C  
ATOM   6657  O   ARG A 813      20.553  13.517  58.828  1.00 59.62           O  
ANISOU 6657  O   ARG A 813     6594  10388   5669   1797     57    211       O  
ATOM   6658  CB  ARG A 813      21.457  11.416  56.609  1.00 56.12           C  
ANISOU 6658  CB  ARG A 813     6237   9577   5508   1666    141    421       C  
ATOM   6659  CG  ARG A 813      21.546   9.908  56.509  1.00 57.27           C  
ANISOU 6659  CG  ARG A 813     6375   9675   5709   1689    210    611       C  
ATOM   6660  CD  ARG A 813      22.994   9.447  56.425  1.00 54.45           C  
ANISOU 6660  CD  ARG A 813     5992   9330   5365   1708    205    628       C  
ATOM   6661  NE  ARG A 813      23.786  10.243  55.485  1.00 53.28           N  
ANISOU 6661  NE  ARG A 813     5887   9078   5278   1626    158    479       N  
ATOM   6662  CZ  ARG A 813      23.792  10.077  54.163  1.00 50.88           C  
ANISOU 6662  CZ  ARG A 813     5660   8569   5102   1534    177    462       C  
ATOM   6663  NH1 ARG A 813      23.042   9.138  53.594  1.00 49.48           N  
ANISOU 6663  NH1 ARG A 813     5530   8259   5011   1507    238    575       N  
ATOM   6664  NH2 ARG A 813      24.552  10.857  53.406  1.00 48.77           N  
ANISOU 6664  NH2 ARG A 813     5421   8232   4876   1467    135    333       N  
ATOM   6665  N   ALA A 814      20.109  14.341  56.772  1.00 53.87           N  
ANISOU 6665  N   ALA A 814     5999   9323   5145   1625     44     89       N  
ATOM   6666  CA  ALA A 814      20.340  15.731  57.149  1.00 55.03           C  
ANISOU 6666  CA  ALA A 814     6144   9534   5230   1630    -22    -98       C  
ATOM   6667  C   ALA A 814      19.170  16.318  57.939  1.00 56.00           C  
ANISOU 6667  C   ALA A 814     6252   9760   5265   1694    -17   -130       C  
ATOM   6668  O   ALA A 814      19.363  17.206  58.773  1.00 55.95           O  
ANISOU 6668  O   ALA A 814     6217   9884   5156   1744    -62   -257       O  
ATOM   6669  CB  ALA A 814      20.642  16.577  55.909  1.00 52.62           C  
ANISOU 6669  CB  ALA A 814     5911   9039   5043   1519    -55   -221       C  
ATOM   6670  N   ILE A 815      17.965  15.816  57.675  1.00 55.90           N  
ANISOU 6670  N   ILE A 815     6256   9692   5291   1693     36    -17       N  
ATOM   6671  CA  ILE A 815      16.773  16.249  58.405  1.00 59.15           C  
ANISOU 6671  CA  ILE A 815     6645  10207   5620   1762     52    -21       C  
ATOM   6672  C   ILE A 815      16.340  15.259  59.491  1.00 62.98           C  
ANISOU 6672  C   ILE A 815     7055  10871   6003   1861    102    141       C  
ATOM   6673  O   ILE A 815      15.299  15.456  60.127  1.00 63.50           O  
ANISOU 6673  O   ILE A 815     7093  11037   5996   1925    126    166       O  
ATOM   6674  CB  ILE A 815      15.561  16.495  57.464  1.00 56.96           C  
ANISOU 6674  CB  ILE A 815     6425   9774   5444   1700     77     -5       C  
ATOM   6675  CG1 ILE A 815      15.173  15.200  56.737  1.00 54.32           C  
ANISOU 6675  CG1 ILE A 815     6103   9329   5206   1647    133    174       C  
ATOM   6676  CG2 ILE A 815      15.845  17.656  56.509  1.00 56.24           C  
ANISOU 6676  CG2 ILE A 815     6402   9528   5438   1618     29   -168       C  
ATOM   6677  CD1 ILE A 815      13.714  15.101  56.367  1.00 51.30           C  
ANISOU 6677  CD1 ILE A 815     5732   8892   4867   1627    172    250       C  
ATOM   6678  N   LYS A 816      17.133  14.207  59.697  1.00 66.75           N  
ANISOU 6678  N   LYS A 816     7498  11389   6477   1878    120    257       N  
ATOM   6679  CA  LYS A 816      16.762  13.105  60.591  1.00 70.76           C  
ANISOU 6679  CA  LYS A 816     7935  12037   6911   1963    176    445       C  
ATOM   6680  C   LYS A 816      16.377  13.596  61.980  1.00 72.59           C  
ANISOU 6680  C   LYS A 816     8098  12515   6967   2080    168    413       C  
ATOM   6681  O   LYS A 816      17.127  14.343  62.612  1.00 73.35           O  
ANISOU 6681  O   LYS A 816     8170  12737   6962   2121    113    276       O  
ATOM   6682  CB  LYS A 816      17.881  12.059  60.682  1.00 72.20           C  
ANISOU 6682  CB  LYS A 816     8087  12237   7107   1976    189    552       C  
ATOM   6683  CG  LYS A 816      17.548  10.865  61.586  1.00 77.57           C  
ANISOU 6683  CG  LYS A 816     8695  13054   7725   2065    251    765       C  
ATOM   6684  CD  LYS A 816      18.773   9.979  61.838  1.00 81.54           C  
ANISOU 6684  CD  LYS A 816     9157  13603   8220   2101    258    857       C  
ATOM   6685  CE  LYS A 816      18.693   9.251  63.188  1.00 84.71           C  
ANISOU 6685  CE  LYS A 816     9461  14238   8488   2227    295   1017       C  
ATOM   6686  NZ  LYS A 816      17.591   8.244  63.266  1.00 84.69           N  
ANISOU 6686  NZ  LYS A 816     9445  14201   8532   2240    375   1221       N  
ATOM   6687  N   GLY A 817      15.195  13.182  62.430  1.00 73.88           N  
ANISOU 6687  N   GLY A 817     8229  12748   7095   2130    224    538       N  
ATOM   6688  CA  GLY A 817      14.702  13.524  63.756  1.00 76.88           C  
ANISOU 6688  CA  GLY A 817     8537  13372   7301   2250    231    533       C  
ATOM   6689  C   GLY A 817      14.155  14.933  63.872  1.00 78.34           C  
ANISOU 6689  C   GLY A 817     8750  13579   7436   2265    194    339       C  
ATOM   6690  O   GLY A 817      14.060  15.472  64.977  1.00 80.75           O  
ANISOU 6690  O   GLY A 817     9007  14092   7583   2366    180    270       O  
ATOM   6691  N   ASN A 818      13.808  15.535  62.735  1.00 77.48           N  
ANISOU 6691  N   ASN A 818     8720  13259   7458   2169    179    251       N  
ATOM   6692  CA  ASN A 818      13.106  16.819  62.718  1.00 78.51           C  
ANISOU 6692  CA  ASN A 818     8884  13379   7568   2182    157     92       C  
ATOM   6693  C   ASN A 818      11.698  16.654  62.156  1.00 77.80           C  
ANISOU 6693  C   ASN A 818     8809  13197   7556   2157    209    190       C  
ATOM   6694  O   ASN A 818      11.526  16.415  60.958  1.00 75.70           O  
ANISOU 6694  O   ASN A 818     8597  12726   7438   2052    215    227       O  
ATOM   6695  CB  ASN A 818      13.885  17.882  61.931  1.00 78.44           C  
ANISOU 6695  CB  ASN A 818     8949  13216   7638   2101     89   -110       C  
ATOM   6696  CG  ASN A 818      15.130  18.369  62.665  1.00 81.64           C  
ANISOU 6696  CG  ASN A 818     9331  13747   7943   2135     27   -249       C  
ATOM   6697  OD1 ASN A 818      15.099  18.636  63.868  1.00 80.98           O  
ANISOU 6697  OD1 ASN A 818     9192  13877   7701   2239     19   -294       O  
ATOM   6698  ND2 ASN A 818      16.233  18.497  61.932  1.00 83.77           N  
ANISOU 6698  ND2 ASN A 818     9639  13890   8302   2047    -18   -318       N  
ATOM   6699  N   ILE A 819      10.702  16.769  63.035  1.00 78.98           N  
ANISOU 6699  N   ILE A 819     8903  13509   7597   2256    247    234       N  
ATOM   6700  CA  ILE A 819       9.288  16.607  62.662  1.00 79.29           C  
ANISOU 6700  CA  ILE A 819     8937  13500   7690   2246    300    340       C  
ATOM   6701  C   ILE A 819       8.787  17.691  61.703  1.00 77.80           C  
ANISOU 6701  C   ILE A 819     8819  13141   7598   2185    275    205       C  
ATOM   6702  O   ILE A 819       7.928  17.434  60.859  1.00 77.35           O  
ANISOU 6702  O   ILE A 819     8780  12961   7648   2121    302    292       O  
ATOM   6703  CB  ILE A 819       8.353  16.518  63.910  1.00 81.94           C  
ANISOU 6703  CB  ILE A 819     9186  14074   7874   2378    351    421       C  
ATOM   6704  CG1 ILE A 819       8.833  17.434  65.048  1.00 83.02           C  
ANISOU 6704  CG1 ILE A 819     9300  14405   7840   2491    315    253       C  
ATOM   6705  CG2 ILE A 819       8.257  15.080  64.408  1.00 83.51           C  
ANISOU 6705  CG2 ILE A 819     9313  14372   8046   2401    407    657       C  
ATOM   6706  CD1 ILE A 819       8.215  18.823  65.058  1.00 83.12           C  
ANISOU 6706  CD1 ILE A 819     9349  14406   7827   2531    298     69       C  
ATOM   6707  N   ASP A 820       9.346  18.891  61.837  1.00 77.26           N  
ANISOU 6707  N   ASP A 820     8790  13069   7495   2205    220     -4       N  
ATOM   6708  CA  ASP A 820       8.967  20.055  61.029  1.00 75.16           C  
ANISOU 6708  CA  ASP A 820     8593  12649   7316   2162    194   -145       C  
ATOM   6709  C   ASP A 820       9.369  19.968  59.549  1.00 70.77           C  
ANISOU 6709  C   ASP A 820     8109  11847   6933   2020    170   -146       C  
ATOM   6710  O   ASP A 820       8.719  20.581  58.697  1.00 70.28           O  
ANISOU 6710  O   ASP A 820     8091  11649   6962   1974    169   -182       O  
ATOM   6711  CB  ASP A 820       9.536  21.337  61.654  1.00 78.10           C  
ANISOU 6711  CB  ASP A 820     8988  13082   7605   2222    143   -372       C  
ATOM   6712  CG  ASP A 820      10.963  21.157  62.177  1.00 82.82           C  
ANISOU 6712  CG  ASP A 820     9573  13755   8139   2220     96   -439       C  
ATOM   6713  OD1 ASP A 820      11.878  20.858  61.371  1.00 83.73           O  
ANISOU 6713  OD1 ASP A 820     9725  13734   8356   2118     65   -437       O  
ATOM   6714  OD2 ASP A 820      11.167  21.320  63.402  1.00 85.58           O  
ANISOU 6714  OD2 ASP A 820     9872  14313   8331   2323     89   -493       O  
ATOM   6715  N   ALA A 821      10.431  19.216  59.251  1.00 65.16           N  
ANISOU 6715  N   ALA A 821     7408  11089   6262   1956    153   -104       N  
ATOM   6716  CA  ALA A 821      10.992  19.147  57.898  1.00 59.89           C  
ANISOU 6716  CA  ALA A 821     6808  10204   5744   1828    128   -120       C  
ATOM   6717  C   ALA A 821      10.079  18.424  56.911  1.00 56.74           C  
ANISOU 6717  C   ALA A 821     6423   9680   5455   1753    169     26       C  
ATOM   6718  O   ALA A 821       9.490  17.399  57.257  1.00 56.59           O  
ANISOU 6718  O   ALA A 821     6355   9734   5414   1775    217    189       O  
ATOM   6719  CB  ALA A 821      12.361  18.490  57.926  1.00 58.64           C  
ANISOU 6719  CB  ALA A 821     6646  10046   5588   1795    106   -109       C  
ATOM   6720  N   PRO A 822       9.948  18.963  55.683  1.00 53.90           N  
ANISOU 6720  N   PRO A 822     6128   9138   5214   1661    148    -29       N  
ATOM   6721  CA  PRO A 822       9.238  18.255  54.618  1.00 52.45           C  
ANISOU 6721  CA  PRO A 822     5962   8828   5137   1572    176     96       C  
ATOM   6722  C   PRO A 822       9.864  16.891  54.359  1.00 52.84           C  
ANISOU 6722  C   PRO A 822     6009   8840   5228   1517    195    216       C  
ATOM   6723  O   PRO A 822      11.071  16.796  54.121  1.00 52.50           O  
ANISOU 6723  O   PRO A 822     5995   8746   5208   1483    168    161       O  
ATOM   6724  CB  PRO A 822       9.440  19.157  53.403  1.00 49.61           C  
ANISOU 6724  CB  PRO A 822     5676   8291   4882   1487    137    -14       C  
ATOM   6725  CG  PRO A 822       9.617  20.502  53.964  1.00 51.14           C  
ANISOU 6725  CG  PRO A 822     5879   8532   5021   1555    105   -177       C  
ATOM   6726  CD  PRO A 822      10.340  20.322  55.266  1.00 53.24           C  
ANISOU 6726  CD  PRO A 822     6100   8965   5165   1641     99   -210       C  
ATOM   6727  N   GLN A 823       9.049  15.846  54.441  1.00 54.12           N  
ANISOU 6727  N   GLN A 823     6133   9029   5401   1511    243    381       N  
ATOM   6728  CA  GLN A 823       9.492  14.499  54.117  1.00 54.34           C  
ANISOU 6728  CA  GLN A 823     6163   8996   5486   1455    269    505       C  
ATOM   6729  C   GLN A 823       9.309  14.256  52.628  1.00 53.30           C  
ANISOU 6729  C   GLN A 823     6095   8668   5488   1327    263    516       C  
ATOM   6730  O   GLN A 823       8.362  14.762  52.024  1.00 53.20           O  
ANISOU 6730  O   GLN A 823     6095   8604   5514   1289    258    505       O  
ATOM   6731  CB  GLN A 823       8.705  13.456  54.913  1.00 55.54           C  
ANISOU 6731  CB  GLN A 823     6245   9262   5596   1502    326    682       C  
ATOM   6732  CG  GLN A 823       8.857  13.559  56.435  1.00 61.54           C  
ANISOU 6732  CG  GLN A 823     6934  10241   6209   1636    338    694       C  
ATOM   6733  CD  GLN A 823      10.180  13.006  56.954  1.00 64.56           C  
ANISOU 6733  CD  GLN A 823     7306  10672   6552   1670    331    701       C  
ATOM   6734  OE1 GLN A 823      10.909  13.688  57.676  1.00 67.25           O  
ANISOU 6734  OE1 GLN A 823     7631  11122   6797   1740    298    590       O  
ATOM   6735  NE2 GLN A 823      10.490  11.765  56.593  1.00 65.44           N  
ANISOU 6735  NE2 GLN A 823     7423  10703   6739   1620    362    830       N  
ATOM   6736  N   VAL A 824      10.231  13.492  52.048  1.00 51.73           N  
ANISOU 6736  N   VAL A 824     5933   8367   5354   1265    263    537       N  
ATOM   6737  CA  VAL A 824      10.125  13.024  50.671  1.00 50.02           C  
ANISOU 6737  CA  VAL A 824     5775   7973   5256   1145    264    560       C  
ATOM   6738  C   VAL A 824       9.094  11.895  50.582  1.00 50.25           C  
ANISOU 6738  C   VAL A 824     5778   7988   5327   1107    310    721       C  
ATOM   6739  O   VAL A 824       9.279  10.833  51.174  1.00 51.54           O  
ANISOU 6739  O   VAL A 824     5910   8191   5482   1135    348    833       O  
ATOM   6740  CB  VAL A 824      11.490  12.499  50.159  1.00 48.74           C  
ANISOU 6740  CB  VAL A 824     5658   7717   5143   1104    257    533       C  
ATOM   6741  CG1 VAL A 824      11.360  11.921  48.737  1.00 46.66           C  
ANISOU 6741  CG1 VAL A 824     5456   7277   4995    984    263    557       C  
ATOM   6742  CG2 VAL A 824      12.537  13.601  50.204  1.00 47.38           C  
ANISOU 6742  CG2 VAL A 824     5506   7558   4939   1128    209    379       C  
ATOM   6743  N   VAL A 825       8.023  12.120  49.829  1.00 50.13           N  
ANISOU 6743  N   VAL A 825     5772   7913   5361   1042    307    735       N  
ATOM   6744  CA  VAL A 825       6.984  11.101  49.668  1.00 52.08           C  
ANISOU 6744  CA  VAL A 825     5991   8141   5654    989    344    881       C  
ATOM   6745  C   VAL A 825       7.313  10.125  48.535  1.00 50.16           C  
ANISOU 6745  C   VAL A 825     5809   7729   5521    872    350    911       C  
ATOM   6746  O   VAL A 825       7.540  10.531  47.396  1.00 49.54           O  
ANISOU 6746  O   VAL A 825     5792   7536   5497    795    318    824       O  
ATOM   6747  CB  VAL A 825       5.571  11.722  49.458  1.00 53.24           C  
ANISOU 6747  CB  VAL A 825     6105   8326   5797    975    339    898       C  
ATOM   6748  CG1 VAL A 825       4.505  10.626  49.331  1.00 53.53           C  
ANISOU 6748  CG1 VAL A 825     6102   8351   5884    912    375   1054       C  
ATOM   6749  CG2 VAL A 825       5.220  12.659  50.609  1.00 55.64           C  
ANISOU 6749  CG2 VAL A 825     6351   8797   5991   1101    340    864       C  
ATOM   6750  N   GLU A 826       7.330   8.839  48.875  1.00 50.78           N  
ANISOU 6750  N   GLU A 826     5869   7795   5630    863    393   1036       N  
ATOM   6751  CA  GLU A 826       7.542   7.754  47.924  1.00 50.89           C  
ANISOU 6751  CA  GLU A 826     5937   7649   5750    758    408   1077       C  
ATOM   6752  C   GLU A 826       6.694   7.928  46.662  1.00 51.47           C  
ANISOU 6752  C   GLU A 826     6045   7620   5890    639    383   1047       C  
ATOM   6753  O   GLU A 826       5.467   7.992  46.730  1.00 52.65           O  
ANISOU 6753  O   GLU A 826     6147   7819   6037    615    386   1112       O  
ATOM   6754  CB  GLU A 826       7.241   6.410  48.604  1.00 52.30           C  
ANISOU 6754  CB  GLU A 826     6075   7843   5955    768    465   1242       C  
ATOM   6755  CG  GLU A 826       7.170   5.193  47.680  1.00 53.94           C  
ANISOU 6755  CG  GLU A 826     6333   7878   6282    652    487   1298       C  
ATOM   6756  CD  GLU A 826       8.509   4.835  47.046  1.00 56.93           C  
ANISOU 6756  CD  GLU A 826     6789   8132   6708    636    486   1224       C  
ATOM   6757  OE1 GLU A 826       8.510   4.435  45.863  1.00 56.75           O  
ANISOU 6757  OE1 GLU A 826     6833   7959   6769    529    478   1184       O  
ATOM   6758  OE2 GLU A 826       9.556   4.948  47.723  1.00 57.39           O  
ANISOU 6758  OE2 GLU A 826     6840   8251   6716    730    492   1206       O  
ATOM   6759  N   GLY A 827       7.360   8.015  45.515  1.00 50.37           N  
ANISOU 6759  N   GLY A 827     5983   7350   5804    566    359    953       N  
ATOM   6760  CA  GLY A 827       6.679   8.140  44.231  1.00 49.68           C  
ANISOU 6760  CA  GLY A 827     5933   7169   5775    450    332    920       C  
ATOM   6761  C   GLY A 827       6.430   9.568  43.774  1.00 49.15           C  
ANISOU 6761  C   GLY A 827     5870   7133   5671    456    285    818       C  
ATOM   6762  O   GLY A 827       5.943   9.786  42.667  1.00 48.42           O  
ANISOU 6762  O   GLY A 827     5807   6973   5617    366    259    786       O  
ATOM   6763  N   GLU A 828       6.748  10.542  44.622  1.00 48.43           N  
ANISOU 6763  N   GLU A 828     5749   7146   5505    561    275    767       N  
ATOM   6764  CA  GLU A 828       6.580  11.943  44.252  1.00 48.92           C  
ANISOU 6764  CA  GLU A 828     5820   7226   5541    576    235    668       C  
ATOM   6765  C   GLU A 828       7.891  12.540  43.718  1.00 45.73           C  
ANISOU 6765  C   GLU A 828     5478   6750   5146    573    208    545       C  
ATOM   6766  O   GLU A 828       8.933  11.881  43.725  1.00 44.39           O  
ANISOU 6766  O   GLU A 828     5339   6535   4994    571    222    537       O  
ATOM   6767  CB  GLU A 828       5.952  12.750  45.405  1.00 52.88           C  
ANISOU 6767  CB  GLU A 828     6253   7876   5962    685    238    677       C  
ATOM   6768  CG  GLU A 828       4.456  12.379  45.623  1.00 62.38           C  
ANISOU 6768  CG  GLU A 828     7391   9146   7165    671    259    796       C  
ATOM   6769  CD  GLU A 828       3.621  13.413  46.402  1.00 69.51           C  
ANISOU 6769  CD  GLU A 828     8233  10182   7997    768    258    789       C  
ATOM   6770  OE1 GLU A 828       2.604  13.003  47.013  1.00 70.47           O  
ANISOU 6770  OE1 GLU A 828     8283  10397   8094    792    288    900       O  
ATOM   6771  OE2 GLU A 828       3.958  14.622  46.402  1.00 71.18           O  
ANISOU 6771  OE2 GLU A 828     8465  10401   8178    820    231    677       O  
ATOM   6772  N   LYS A 829       7.844  13.773  43.231  1.00 42.25           N  
ANISOU 6772  N   LYS A 829     5055   6300   4700    573    172    456       N  
ATOM   6773  CA  LYS A 829       9.016  14.336  42.568  1.00 38.71           C  
ANISOU 6773  CA  LYS A 829     4663   5773   4271    552    148    349       C  
ATOM   6774  C   LYS A 829       9.948  15.133  43.468  1.00 37.39           C  
ANISOU 6774  C   LYS A 829     4484   5668   4053    643    135    267       C  
ATOM   6775  O   LYS A 829       9.515  15.786  44.420  1.00 36.47           O  
ANISOU 6775  O   LYS A 829     4325   5652   3880    725    132    255       O  
ATOM   6776  CB  LYS A 829       8.613  15.108  41.313  1.00 38.71           C  
ANISOU 6776  CB  LYS A 829     4697   5701   4310    480    117    304       C  
ATOM   6777  CG  LYS A 829       8.359  14.156  40.149  1.00 38.12           C  
ANISOU 6777  CG  LYS A 829     4658   5534   4290    369    122    348       C  
ATOM   6778  CD  LYS A 829       7.684  14.814  38.987  1.00 38.03           C  
ANISOU 6778  CD  LYS A 829     4664   5482   4303    301     93    330       C  
ATOM   6779  CE  LYS A 829       7.633  13.865  37.812  1.00 39.06           C  
ANISOU 6779  CE  LYS A 829     4838   5526   4479    188     95    352       C  
ATOM   6780  NZ  LYS A 829       7.149  14.570  36.599  1.00 41.58           N  
ANISOU 6780  NZ  LYS A 829     5174   5813   4811    123     62    326       N  
ATOM   6781  N   VAL A 830      11.239  15.050  43.157  1.00 33.94           N  
ANISOU 6781  N   VAL A 830     4085   5175   3634    627    128    209       N  
ATOM   6782  CA  VAL A 830      12.271  15.716  43.929  1.00 31.52           C  
ANISOU 6782  CA  VAL A 830     3768   4925   3286    697    111    126       C  
ATOM   6783  C   VAL A 830      13.183  16.530  43.036  1.00 31.39           C  
ANISOU 6783  C   VAL A 830     3797   4822   3309    650     81     26       C  
ATOM   6784  O   VAL A 830      13.495  16.113  41.909  1.00 32.99           O  
ANISOU 6784  O   VAL A 830     4043   4926   3566    571     85     32       O  
ATOM   6785  CB  VAL A 830      13.135  14.710  44.728  1.00 31.62           C  
ANISOU 6785  CB  VAL A 830     3758   4985   3270    743    137    170       C  
ATOM   6786  CG1 VAL A 830      12.396  14.225  45.971  1.00 25.33           C  
ANISOU 6786  CG1 VAL A 830     2900   4312   2411    820    164    257       C  
ATOM   6787  CG2 VAL A 830      13.562  13.533  43.854  1.00 32.04           C  
ANISOU 6787  CG2 VAL A 830     3853   4935   3387    671    164    223       C  
ATOM   6788  N   TYR A 831      13.597  17.691  43.538  1.00 28.97           N  
ANISOU 6788  N   TYR A 831     3479   4554   2974    697     51    -68       N  
ATOM   6789  CA  TYR A 831      14.714  18.432  42.955  1.00 30.15           C  
ANISOU 6789  CA  TYR A 831     3661   4639   3157    662     23   -162       C  
ATOM   6790  C   TYR A 831      16.007  17.781  43.399  1.00 30.56           C  
ANISOU 6790  C   TYR A 831     3699   4720   3190    683     30   -169       C  
ATOM   6791  O   TYR A 831      16.096  17.276  44.524  1.00 30.92           O  
ANISOU 6791  O   TYR A 831     3703   4868   3177    753     42   -137       O  
ATOM   6792  CB  TYR A 831      14.720  19.888  43.410  1.00 31.17           C  
ANISOU 6792  CB  TYR A 831     3781   4792   3270    703    -12   -264       C  
ATOM   6793  CG  TYR A 831      13.649  20.751  42.794  1.00 33.46           C  
ANISOU 6793  CG  TYR A 831     4089   5033   3593    683    -21   -269       C  
ATOM   6794  CD1 TYR A 831      13.428  20.749  41.417  1.00 31.78           C  
ANISOU 6794  CD1 TYR A 831     3915   4717   3443    598    -21   -241       C  
ATOM   6795  CD2 TYR A 831      12.867  21.592  43.594  1.00 35.52           C  
ANISOU 6795  CD2 TYR A 831     4325   5355   3817    756    -29   -303       C  
ATOM   6796  CE1 TYR A 831      12.445  21.546  40.850  1.00 33.87           C  
ANISOU 6796  CE1 TYR A 831     4189   4945   3735    585    -31   -236       C  
ATOM   6797  CE2 TYR A 831      11.886  22.397  43.040  1.00 38.55           C  
ANISOU 6797  CE2 TYR A 831     4720   5694   4234    748    -35   -301       C  
ATOM   6798  CZ  TYR A 831      11.675  22.372  41.667  1.00 38.62           C  
ANISOU 6798  CZ  TYR A 831     4763   5603   4307    662    -36   -262       C  
ATOM   6799  OH  TYR A 831      10.699  23.177  41.114  1.00 40.74           O  
ANISOU 6799  OH  TYR A 831     5038   5837   4606    659    -42   -250       O  
ATOM   6800  N   VAL A 832      17.004  17.799  42.522  1.00 31.04           N  
ANISOU 6800  N   VAL A 832     3793   4703   3298    625     24   -205       N  
ATOM   6801  CA  VAL A 832      18.287  17.126  42.770  1.00 32.51           C  
ANISOU 6801  CA  VAL A 832     3965   4910   3475    640     34   -203       C  
ATOM   6802  C   VAL A 832      19.441  18.063  42.416  1.00 33.59           C  
ANISOU 6802  C   VAL A 832     4108   5019   3636    612      2   -301       C  
ATOM   6803  O   VAL A 832      19.413  18.723  41.369  1.00 35.06           O  
ANISOU 6803  O   VAL A 832     4332   5116   3875    547    -11   -335       O  
ATOM   6804  CB  VAL A 832      18.438  15.831  41.914  1.00 31.83           C  
ANISOU 6804  CB  VAL A 832     3913   4748   3433    592     76   -126       C  
ATOM   6805  CG1 VAL A 832      19.798  15.168  42.164  1.00 31.18           C  
ANISOU 6805  CG1 VAL A 832     3815   4688   3346    619     91   -121       C  
ATOM   6806  CG2 VAL A 832      17.314  14.844  42.198  1.00 31.38           C  
ANISOU 6806  CG2 VAL A 832     3851   4705   3368    604    108    -25       C  
ATOM   6807  N   LEU A 833      20.453  18.111  43.279  1.00 33.18           N  
ANISOU 6807  N   LEU A 833     4015   5049   3545    660    -13   -338       N  
ATOM   6808  CA  LEU A 833      21.652  18.918  43.025  1.00 34.47           C  
ANISOU 6808  CA  LEU A 833     4171   5195   3730    629    -45   -425       C  
ATOM   6809  C   LEU A 833      22.933  18.162  43.360  1.00 35.18           C  
ANISOU 6809  C   LEU A 833     4226   5341   3802    654    -35   -406       C  
ATOM   6810  O   LEU A 833      22.986  17.457  44.374  1.00 36.35           O  
ANISOU 6810  O   LEU A 833     4333   5589   3890    726    -23   -361       O  
ATOM   6811  CB  LEU A 833      21.616  20.222  43.837  1.00 32.85           C  
ANISOU 6811  CB  LEU A 833     3942   5044   3496    658    -93   -528       C  
ATOM   6812  CG  LEU A 833      20.775  21.375  43.291  1.00 36.06           C  
ANISOU 6812  CG  LEU A 833     4385   5369   3945    622   -112   -578       C  
ATOM   6813  CD1 LEU A 833      20.676  22.477  44.327  1.00 30.07           C  
ANISOU 6813  CD1 LEU A 833     3603   4674   3149    671   -152   -678       C  
ATOM   6814  CD2 LEU A 833      21.343  21.914  41.960  1.00 32.64           C  
ANISOU 6814  CD2 LEU A 833     3988   4817   3595    532   -119   -602       C  
ATOM   6815  N   PRO A 834      23.981  18.327  42.527  1.00 36.75           N  
ANISOU 6815  N   PRO A 834     4433   5483   4048    601    -38   -435       N  
ATOM   6816  CA  PRO A 834      25.277  17.759  42.893  1.00 38.26           C  
ANISOU 6816  CA  PRO A 834     4579   5739   4220    630    -32   -424       C  
ATOM   6817  C   PRO A 834      25.970  18.597  43.965  1.00 40.20           C  
ANISOU 6817  C   PRO A 834     4763   6096   4417    663    -84   -508       C  
ATOM   6818  O   PRO A 834      25.776  19.818  44.037  1.00 40.20           O  
ANISOU 6818  O   PRO A 834     4768   6079   4426    634   -127   -598       O  
ATOM   6819  CB  PRO A 834      26.069  17.800  41.586  1.00 36.64           C  
ANISOU 6819  CB  PRO A 834     4400   5439   4081    558    -18   -431       C  
ATOM   6820  CG  PRO A 834      25.446  18.913  40.791  1.00 37.13           C  
ANISOU 6820  CG  PRO A 834     4506   5412   4190    489    -41   -484       C  
ATOM   6821  CD  PRO A 834      24.035  19.090  41.261  1.00 35.42           C  
ANISOU 6821  CD  PRO A 834     4307   5201   3948    516    -46   -474       C  
ATOM   6822  N   LEU A 835      26.776  17.926  44.781  1.00 40.62           N  
ANISOU 6822  N   LEU A 835     4758   6258   4417    723    -80   -477       N  
ATOM   6823  CA  LEU A 835      27.508  18.555  45.870  1.00 40.54           C  
ANISOU 6823  CA  LEU A 835     4681   6377   4346    758   -132   -551       C  
ATOM   6824  C   LEU A 835      29.008  18.361  45.695  1.00 41.46           C  
ANISOU 6824  C   LEU A 835     4747   6530   4474    745   -139   -555       C  
ATOM   6825  O   LEU A 835      29.464  17.255  45.386  1.00 41.09           O  
ANISOU 6825  O   LEU A 835     4694   6479   4438    770    -92   -464       O  
ATOM   6826  CB  LEU A 835      27.064  17.937  47.198  1.00 41.30           C  
ANISOU 6826  CB  LEU A 835     4734   6610   4347    857   -126   -503       C  
ATOM   6827  CG  LEU A 835      25.960  18.551  48.070  1.00 39.47           C  
ANISOU 6827  CG  LEU A 835     4505   6437   4057    897   -149   -547       C  
ATOM   6828  CD1 LEU A 835      25.146  19.653  47.398  1.00 36.57           C  
ANISOU 6828  CD1 LEU A 835     4196   5952   3746    835   -167   -623       C  
ATOM   6829  CD2 LEU A 835      25.065  17.445  48.575  1.00 39.94           C  
ANISOU 6829  CD2 LEU A 835     4562   6540   4072    967   -100   -427       C  
ATOM   6830  N   ARG A 836      29.764  19.441  45.896  1.00 42.37           N  
ANISOU 6830  N   ARG A 836     4825   6680   4592    705   -196   -660       N  
ATOM   6831  CA  ARG A 836      31.228  19.408  45.850  1.00 43.23           C  
ANISOU 6831  CA  ARG A 836     4870   6847   4706    689   -212   -672       C  
ATOM   6832  C   ARG A 836      31.812  18.511  46.938  1.00 45.04           C  
ANISOU 6832  C   ARG A 836     5024   7240   4850    782   -209   -613       C  
ATOM   6833  O   ARG A 836      31.254  18.396  48.034  1.00 43.35           O  
ANISOU 6833  O   ARG A 836     4789   7128   4555    850   -223   -611       O  
ATOM   6834  CB  ARG A 836      31.814  20.813  45.998  1.00 44.00           C  
ANISOU 6834  CB  ARG A 836     4939   6958   4823    623   -282   -803       C  
ATOM   6835  CG  ARG A 836      31.543  21.733  44.828  1.00 44.45           C  
ANISOU 6835  CG  ARG A 836     5057   6854   4977    526   -284   -849       C  
ATOM   6836  CD  ARG A 836      32.509  22.899  44.795  1.00 45.25           C  
ANISOU 6836  CD  ARG A 836     5117   6959   5118    451   -342   -953       C  
ATOM   6837  NE  ARG A 836      32.641  23.581  46.081  1.00 50.35           N  
ANISOU 6837  NE  ARG A 836     5714   7719   5699    474   -408  -1057       N  
ATOM   6838  CZ  ARG A 836      31.779  24.474  46.550  1.00 49.93           C  
ANISOU 6838  CZ  ARG A 836     5697   7638   5637    475   -440  -1147       C  
ATOM   6839  NH1 ARG A 836      30.692  24.790  45.852  1.00 48.50           N  
ANISOU 6839  NH1 ARG A 836     5596   7321   5510    456   -412  -1134       N  
ATOM   6840  NH2 ARG A 836      32.000  25.049  47.723  1.00 47.61           N  
ANISOU 6840  NH2 ARG A 836     5357   7457   5277    497   -500  -1251       N  
ATOM   6841  N   GLU A 837      32.945  17.892  46.621  1.00 45.79           N  
ANISOU 6841  N   GLU A 837     5075   7364   4961    788   -188   -560       N  
ATOM   6842  CA  GLU A 837      33.643  16.989  47.527  1.00 49.67           C  
ANISOU 6842  CA  GLU A 837     5487   8007   5380    879   -179   -488       C  
ATOM   6843  C   GLU A 837      34.043  17.669  48.844  1.00 50.95           C  
ANISOU 6843  C   GLU A 837     5566   8344   5448    907   -254   -569       C  
ATOM   6844  O   GLU A 837      34.602  18.770  48.842  1.00 51.23           O  
ANISOU 6844  O   GLU A 837     5575   8395   5497    838   -315   -683       O  
ATOM   6845  CB  GLU A 837      34.874  16.421  46.821  1.00 51.52           C  
ANISOU 6845  CB  GLU A 837     5685   8230   5659    872   -147   -432       C  
ATOM   6846  CG  GLU A 837      35.448  15.165  47.451  1.00 59.86           C  
ANISOU 6846  CG  GLU A 837     6680   9399   6665    978   -109   -316       C  
ATOM   6847  CD  GLU A 837      36.113  14.267  46.421  1.00 65.33           C  
ANISOU 6847  CD  GLU A 837     7388  10009   7427    984    -40   -231       C  
ATOM   6848  OE1 GLU A 837      37.361  14.288  46.327  1.00 66.14           O  
ANISOU 6848  OE1 GLU A 837     7417  10181   7533    985    -49   -228       O  
ATOM   6849  OE2 GLU A 837      35.379  13.559  45.690  1.00 66.72           O  
ANISOU 6849  OE2 GLU A 837     7648  10048   7653    986     23   -172       O  
ATOM   6850  N   GLY A 838      33.743  17.003  49.958  1.00 50.28           N  
ANISOU 6850  N   GLY A 838     5443   8392   5269   1006   -247   -508       N  
ATOM   6851  CA  GLY A 838      34.126  17.483  51.283  1.00 51.76           C  
ANISOU 6851  CA  GLY A 838     5546   8773   5346   1048   -314   -575       C  
ATOM   6852  C   GLY A 838      33.036  18.277  51.975  1.00 52.46           C  
ANISOU 6852  C   GLY A 838     5667   8883   5381   1053   -350   -666       C  
ATOM   6853  O   GLY A 838      33.288  18.940  52.982  1.00 53.81           O  
ANISOU 6853  O   GLY A 838     5782   9198   5465   1070   -415   -760       O  
ATOM   6854  N   ASN A 839      31.826  18.205  51.426  1.00 49.82           N  
ANISOU 6854  N   ASN A 839     5422   8410   5096   1041   -307   -639       N  
ATOM   6855  CA  ASN A 839      30.652  18.878  51.973  1.00 48.78           C  
ANISOU 6855  CA  ASN A 839     5328   8283   4921   1055   -327   -709       C  
ATOM   6856  C   ASN A 839      30.149  18.183  53.246  1.00 48.78           C  
ANISOU 6856  C   ASN A 839     5284   8451   4800   1171   -313   -637       C  
ATOM   6857  O   ASN A 839      30.416  17.000  53.442  1.00 49.74           O  
ANISOU 6857  O   ASN A 839     5370   8630   4898   1235   -269   -501       O  
ATOM   6858  CB  ASN A 839      29.549  18.914  50.912  1.00 44.62           C  
ANISOU 6858  CB  ASN A 839     4901   7564   4489   1007   -281   -682       C  
ATOM   6859  CG  ASN A 839      28.984  17.539  50.618  1.00 41.33           C  
ANISOU 6859  CG  ASN A 839     4511   7105   4088   1055   -205   -522       C  
ATOM   6860  OD1 ASN A 839      28.098  17.065  51.321  1.00 41.69           O  
ANISOU 6860  OD1 ASN A 839     4554   7212   4073   1124   -181   -461       O  
ATOM   6861  ND2 ASN A 839      29.499  16.891  49.580  1.00 35.63           N  
ANISOU 6861  ND2 ASN A 839     3812   6277   3447   1017   -164   -455       N  
ATOM   6862  N   PRO A 840      29.412  18.911  54.105  1.00 50.03           N  
ANISOU 6862  N   PRO A 840     5442   8687   4880   1201   -348   -724       N  
ATOM   6863  CA  PRO A 840      28.961  18.366  55.395  1.00 51.76           C  
ANISOU 6863  CA  PRO A 840     5609   9089   4967   1314   -339   -664       C  
ATOM   6864  C   PRO A 840      27.881  17.284  55.290  1.00 50.06           C  
ANISOU 6864  C   PRO A 840     5429   8829   4763   1368   -260   -504       C  
ATOM   6865  O   PRO A 840      27.664  16.527  56.244  1.00 49.60           O  
ANISOU 6865  O   PRO A 840     5319   8919   4609   1465   -237   -406       O  
ATOM   6866  CB  PRO A 840      28.409  19.600  56.121  1.00 53.18           C  
ANISOU 6866  CB  PRO A 840     5797   9331   5079   1318   -394   -823       C  
ATOM   6867  CG  PRO A 840      28.017  20.536  55.025  1.00 52.85           C  
ANISOU 6867  CG  PRO A 840     5839   9081   5161   1218   -401   -915       C  
ATOM   6868  CD  PRO A 840      29.053  20.334  53.961  1.00 51.28           C  
ANISOU 6868  CD  PRO A 840     5644   8775   5067   1137   -398   -889       C  
ATOM   6869  N   PHE A 841      27.226  17.202  54.139  1.00 47.88           N  
ANISOU 6869  N   PHE A 841     5234   8355   4601   1305   -220   -475       N  
ATOM   6870  CA  PHE A 841      26.197  16.195  53.908  1.00 47.22           C  
ANISOU 6870  CA  PHE A 841     5188   8210   4546   1336   -148   -331       C  
ATOM   6871  C   PHE A 841      26.781  14.796  53.737  1.00 48.07           C  
ANISOU 6871  C   PHE A 841     5271   8316   4678   1370    -94   -176       C  
ATOM   6872  O   PHE A 841      26.069  13.798  53.868  1.00 48.34           O  
ANISOU 6872  O   PHE A 841     5314   8340   4715   1414    -36    -40       O  
ATOM   6873  CB  PHE A 841      25.339  16.589  52.707  1.00 46.56           C  
ANISOU 6873  CB  PHE A 841     5195   7924   4573   1251   -129   -356       C  
ATOM   6874  CG  PHE A 841      24.630  17.902  52.890  1.00 45.84           C  
ANISOU 6874  CG  PHE A 841     5130   7824   4464   1231   -171   -490       C  
ATOM   6875  CD1 PHE A 841      23.479  17.980  53.663  1.00 46.37           C  
ANISOU 6875  CD1 PHE A 841     5192   7967   4461   1296   -158   -474       C  
ATOM   6876  CD2 PHE A 841      25.133  19.065  52.316  1.00 43.78           C  
ANISOU 6876  CD2 PHE A 841     4895   7481   4259   1153   -220   -630       C  
ATOM   6877  CE1 PHE A 841      22.821  19.199  53.849  1.00 48.86           C  
ANISOU 6877  CE1 PHE A 841     5532   8272   4759   1289   -192   -600       C  
ATOM   6878  CE2 PHE A 841      24.491  20.287  52.494  1.00 46.53           C  
ANISOU 6878  CE2 PHE A 841     5271   7809   4600   1140   -255   -754       C  
ATOM   6879  CZ  PHE A 841      23.329  20.357  53.261  1.00 46.84           C  
ANISOU 6879  CZ  PHE A 841     5309   7921   4567   1212   -240   -742       C  
ATOM   6880  N   GLY A 842      28.080  14.735  53.456  1.00 47.96           N  
ANISOU 6880  N   GLY A 842     5225   8313   4687   1350   -113   -194       N  
ATOM   6881  CA  GLY A 842      28.800  13.471  53.386  1.00 50.24           C  
ANISOU 6881  CA  GLY A 842     5481   8616   4992   1396    -65    -56       C  
ATOM   6882  C   GLY A 842      28.540  12.637  52.144  1.00 50.91           C  
ANISOU 6882  C   GLY A 842     5640   8502   5200   1350      2     30       C  
ATOM   6883  O   GLY A 842      28.886  11.455  52.122  1.00 52.10           O  
ANISOU 6883  O   GLY A 842     5777   8647   5373   1400     57    159       O  
ATOM   6884  N   ASP A 843      27.935  13.239  51.114  1.00 49.31           N  
ANISOU 6884  N   ASP A 843     5517   8140   5078   1259      0    -41       N  
ATOM   6885  CA  ASP A 843      27.709  12.552  49.830  1.00 48.56           C  
ANISOU 6885  CA  ASP A 843     5497   7857   5096   1203     56     18       C  
ATOM   6886  C   ASP A 843      27.749  13.499  48.629  1.00 47.91           C  
ANISOU 6886  C   ASP A 843     5475   7638   5092   1095     31    -93       C  
ATOM   6887  O   ASP A 843      27.872  14.715  48.794  1.00 47.52           O  
ANISOU 6887  O   ASP A 843     5413   7623   5019   1061    -28   -213       O  
ATOM   6888  CB  ASP A 843      26.399  11.758  49.844  1.00 47.72           C  
ANISOU 6888  CB  ASP A 843     5433   7691   5007   1220    108    120       C  
ATOM   6889  CG  ASP A 843      26.514  10.418  49.122  1.00 49.48           C  
ANISOU 6889  CG  ASP A 843     5694   7795   5311   1219    179    237       C  
ATOM   6890  OD1 ASP A 843      27.336  10.280  48.191  1.00 46.21           O  
ANISOU 6890  OD1 ASP A 843     5306   7291   4962   1179    192    215       O  
ATOM   6891  OD2 ASP A 843      25.771   9.489  49.495  1.00 57.34           O  
ANISOU 6891  OD2 ASP A 843     6695   8786   6308   1260    226    353       O  
ATOM   6892  N   LYS A 844      27.641  12.934  47.424  1.00 46.35           N  
ANISOU 6892  N   LYS A 844     5341   7284   4984   1043     76    -53       N  
ATOM   6893  CA  LYS A 844      27.850  13.698  46.194  1.00 45.35           C  
ANISOU 6893  CA  LYS A 844     5265   7036   4930    946     60   -138       C  
ATOM   6894  C   LYS A 844      26.625  14.464  45.684  1.00 43.18           C  
ANISOU 6894  C   LYS A 844     5052   6671   4683    883     45   -190       C  
ATOM   6895  O   LYS A 844      26.745  15.304  44.788  1.00 40.09           O  
ANISOU 6895  O   LYS A 844     4695   6196   4343    806     23   -266       O  
ATOM   6896  CB  LYS A 844      28.431  12.809  45.090  1.00 47.52           C  
ANISOU 6896  CB  LYS A 844     5577   7200   5279    921    115    -83       C  
ATOM   6897  CG  LYS A 844      27.490  11.728  44.568  1.00 49.48           C  
ANISOU 6897  CG  LYS A 844     5890   7338   5573    917    175      7       C  
ATOM   6898  CD  LYS A 844      28.221  10.831  43.583  1.00 51.18           C  
ANISOU 6898  CD  LYS A 844     6138   7455   5852    905    229     49       C  
ATOM   6899  CE  LYS A 844      27.328   9.714  43.067  1.00 51.96           C  
ANISOU 6899  CE  LYS A 844     6304   7437   6001    895    288    128       C  
ATOM   6900  NZ  LYS A 844      28.066   8.840  42.108  1.00 50.02           N  
ANISOU 6900  NZ  LYS A 844     6096   7093   5816    889    344    155       N  
ATOM   6901  N   CYS A 845      25.455  14.171  46.246  1.00 41.93           N  
ANISOU 6901  N   CYS A 845     4903   6536   4493    917     59   -141       N  
ATOM   6902  CA  CYS A 845      24.226  14.831  45.810  1.00 40.84           C  
ANISOU 6902  CA  CYS A 845     4815   6325   4379    868     48   -176       C  
ATOM   6903  C   CYS A 845      23.196  14.863  46.907  1.00 40.02           C  
ANISOU 6903  C   CYS A 845     4684   6316   4206    930     44   -149       C  
ATOM   6904  O   CYS A 845      23.261  14.076  47.847  1.00 41.27           O  
ANISOU 6904  O   CYS A 845     4797   6575   4308   1007     65    -71       O  
ATOM   6905  CB  CYS A 845      23.630  14.130  44.588  1.00 40.74           C  
ANISOU 6905  CB  CYS A 845     4871   6165   4443    807     92   -118       C  
ATOM   6906  SG  CYS A 845      23.138  12.416  44.909  1.00 43.15           S  
ANISOU 6906  SG  CYS A 845     5179   6465   4752    857    159     31       S  
ATOM   6907  N   ILE A 846      22.241  15.778  46.764  1.00 39.80           N  
ANISOU 6907  N   ILE A 846     4682   6258   4181    902     21   -206       N  
ATOM   6908  CA  ILE A 846      21.124  15.910  47.686  1.00 36.22           C  
ANISOU 6908  CA  ILE A 846     4208   5889   3666    959     21   -184       C  
ATOM   6909  C   ILE A 846      19.832  16.212  46.917  1.00 36.81           C  
ANISOU 6909  C   ILE A 846     4332   5863   3789    907     30   -175       C  
ATOM   6910  O   ILE A 846      19.839  16.959  45.943  1.00 37.68           O  
ANISOU 6910  O   ILE A 846     4486   5872   3959    837     11   -239       O  
ATOM   6911  CB  ILE A 846      21.404  16.985  48.775  1.00 36.04           C  
ANISOU 6911  CB  ILE A 846     4138   5993   3562   1012    -30   -290       C  
ATOM   6912  CG1 ILE A 846      20.490  16.770  49.993  1.00 37.72           C  
ANISOU 6912  CG1 ILE A 846     4309   6339   3683   1101    -18   -242       C  
ATOM   6913  CG2 ILE A 846      21.319  18.407  48.197  1.00 31.81           C  
ANISOU 6913  CG2 ILE A 846     3639   5379   3069    953    -74   -419       C  
ATOM   6914  CD1 ILE A 846      20.739  17.717  51.149  1.00 35.99           C  
ANISOU 6914  CD1 ILE A 846     4044   6262   3368   1163    -65   -349       C  
ATOM   6915  N   ALA A 847      18.735  15.613  47.367  1.00 37.27           N  
ANISOU 6915  N   ALA A 847     4379   5959   3821    942     61    -86       N  
ATOM   6916  CA  ALA A 847      17.429  15.800  46.766  1.00 37.43           C  
ANISOU 6916  CA  ALA A 847     4432   5910   3879    900     71    -61       C  
ATOM   6917  C   ALA A 847      16.405  16.236  47.819  1.00 39.22           C  
ANISOU 6917  C   ALA A 847     4619   6251   4033    973     68    -56       C  
ATOM   6918  O   ALA A 847      16.436  15.755  48.951  1.00 39.93           O  
ANISOU 6918  O   ALA A 847     4657   6467   4049   1052     83     -6       O  
ATOM   6919  CB  ALA A 847      16.978  14.503  46.086  1.00 37.00           C  
ANISOU 6919  CB  ALA A 847     4404   5774   3879    856    118     55       C  
ATOM   6920  N   TRP A 848      15.506  17.144  47.443  1.00 38.70           N  
ANISOU 6920  N   TRP A 848     4573   6147   3985    952     52   -101       N  
ATOM   6921  CA  TRP A 848      14.411  17.568  48.325  1.00 38.77           C  
ANISOU 6921  CA  TRP A 848     4546   6256   3930   1022     56    -92       C  
ATOM   6922  C   TRP A 848      13.080  17.623  47.564  1.00 38.57           C  
ANISOU 6922  C   TRP A 848     4540   6160   3952    977     72    -39       C  
ATOM   6923  O   TRP A 848      13.086  17.622  46.338  1.00 37.97           O  
ANISOU 6923  O   TRP A 848     4511   5959   3955    890     67    -40       O  
ATOM   6924  CB  TRP A 848      14.738  18.903  49.006  1.00 37.98           C  
ANISOU 6924  CB  TRP A 848     4434   6218   3778   1075     15   -230       C  
ATOM   6925  CG  TRP A 848      14.688  20.096  48.119  1.00 31.60           C  
ANISOU 6925  CG  TRP A 848     3675   5296   3037   1019    -16   -329       C  
ATOM   6926  CD1 TRP A 848      13.676  21.011  48.034  1.00 30.77           C  
ANISOU 6926  CD1 TRP A 848     3579   5173   2939   1037    -22   -364       C  
ATOM   6927  CD2 TRP A 848      15.698  20.525  47.197  1.00 30.75           C  
ANISOU 6927  CD2 TRP A 848     3607   5076   2999    943    -43   -398       C  
ATOM   6928  NE1 TRP A 848      13.992  21.986  47.111  1.00 30.25           N  
ANISOU 6928  NE1 TRP A 848     3560   4986   2949    976    -50   -446       N  
ATOM   6929  CE2 TRP A 848      15.226  21.708  46.580  1.00 29.55           C  
ANISOU 6929  CE2 TRP A 848     3490   4839   2899    914    -64   -467       C  
ATOM   6930  CE3 TRP A 848      16.956  20.023  46.826  1.00 32.43           C  
ANISOU 6930  CE3 TRP A 848     3826   5257   3238    900    -49   -400       C  
ATOM   6931  CZ2 TRP A 848      15.968  22.398  45.611  1.00 31.24           C  
ANISOU 6931  CZ2 TRP A 848     3744   4936   3189    840    -90   -534       C  
ATOM   6932  CZ3 TRP A 848      17.700  20.714  45.859  1.00 27.99           C  
ANISOU 6932  CZ3 TRP A 848     3302   4585   2748    826    -74   -472       C  
ATOM   6933  CH2 TRP A 848      17.199  21.889  45.265  1.00 28.49           C  
ANISOU 6933  CH2 TRP A 848     3399   4565   2861    794    -95   -535       C  
ATOM   6934  N   PRO A 849      11.935  17.641  48.282  1.00 39.52           N  
ANISOU 6934  N   PRO A 849     4620   6374   4023   1037     91     13       N  
ATOM   6935  CA  PRO A 849      10.647  17.643  47.573  1.00 39.09           C  
ANISOU 6935  CA  PRO A 849     4574   6267   4013    993    105     75       C  
ATOM   6936  C   PRO A 849      10.514  18.795  46.582  1.00 39.81           C  
ANISOU 6936  C   PRO A 849     4710   6255   4162    944     73    -12       C  
ATOM   6937  O   PRO A 849      10.913  19.922  46.876  1.00 40.47           O  
ANISOU 6937  O   PRO A 849     4802   6346   4228    982     44   -125       O  
ATOM   6938  CB  PRO A 849       9.628  17.777  48.702  1.00 40.18           C  
ANISOU 6938  CB  PRO A 849     4650   6546   4071   1088    126    118       C  
ATOM   6939  CG  PRO A 849      10.296  17.093  49.858  1.00 41.76           C  
ANISOU 6939  CG  PRO A 849     4809   6863   4195   1158    142    149       C  
ATOM   6940  CD  PRO A 849      11.751  17.486  49.739  1.00 39.94           C  
ANISOU 6940  CD  PRO A 849     4611   6592   3972   1144    106     39       C  
ATOM   6941  N   SER A 850       9.978  18.501  45.402  1.00 39.92           N  
ANISOU 6941  N   SER A 850     4752   6171   4245    857     77     40       N  
ATOM   6942  CA  SER A 850       9.886  19.501  44.344  1.00 40.35           C  
ANISOU 6942  CA  SER A 850     4849   6126   4357    805     49    -24       C  
ATOM   6943  C   SER A 850       8.754  20.492  44.592  1.00 42.84           C  
ANISOU 6943  C   SER A 850     5141   6481   4656    859     46    -36       C  
ATOM   6944  O   SER A 850       7.832  20.221  45.368  1.00 42.31           O  
ANISOU 6944  O   SER A 850     5023   6513   4538    919     69     27       O  
ATOM   6945  CB  SER A 850       9.753  18.836  42.972  1.00 39.12           C  
ANISOU 6945  CB  SER A 850     4730   5865   4270    695     52     33       C  
ATOM   6946  OG  SER A 850       8.494  18.209  42.793  1.00 37.46           O  
ANISOU 6946  OG  SER A 850     4492   5679   4063    672     72    137       O  
ATOM   6947  N   GLY A 851       8.850  21.647  43.938  1.00 46.92           N  
ANISOU 6947  N   GLY A 851     5692   6920   5217    842     19   -113       N  
ATOM   6948  CA  GLY A 851       7.874  22.731  44.075  1.00 50.25           C  
ANISOU 6948  CA  GLY A 851     6098   7358   5635    899     16   -135       C  
ATOM   6949  C   GLY A 851       8.131  23.602  45.287  1.00 54.17           C  
ANISOU 6949  C   GLY A 851     6581   7924   6077   1004     10   -237       C  
ATOM   6950  O   GLY A 851       7.504  24.653  45.451  1.00 56.46           O  
ANISOU 6950  O   GLY A 851     6869   8214   6370   1062      8   -282       O  
ATOM   6951  N   THR A 852       9.055  23.164  46.140  1.00 55.17           N  
ANISOU 6951  N   THR A 852     6697   8112   6152   1032      8   -274       N  
ATOM   6952  CA  THR A 852       9.322  23.844  47.404  1.00 55.73           C  
ANISOU 6952  CA  THR A 852     6749   8274   6152   1132      0   -373       C  
ATOM   6953  C   THR A 852      10.759  24.338  47.478  1.00 56.93           C  
ANISOU 6953  C   THR A 852     6933   8381   6318   1109    -36   -494       C  
ATOM   6954  O   THR A 852      11.673  23.768  46.858  1.00 54.79           O  
ANISOU 6954  O   THR A 852     6682   8051   6086   1032    -46   -478       O  
ATOM   6955  CB  THR A 852       9.059  22.936  48.634  1.00 52.19           C  
ANISOU 6955  CB  THR A 852     6241   7986   5603   1208     29   -308       C  
ATOM   6956  OG1 THR A 852      10.023  21.883  48.653  1.00 52.66           O  
ANISOU 6956  OG1 THR A 852     6299   8052   5656   1164     30   -268       O  
ATOM   6957  CG2 THR A 852       7.653  22.332  48.602  1.00 52.26           C  
ANISOU 6957  CG2 THR A 852     6208   8048   5599   1223     68   -173       C  
ATOM   6958  N   GLU A 853      10.929  25.424  48.227  1.00 58.21           N  
ANISOU 6958  N   GLU A 853     7097   8571   6449   1177    -56   -619       N  
ATOM   6959  CA  GLU A 853      12.219  25.821  48.754  1.00 58.63           C  
ANISOU 6959  CA  GLU A 853     7159   8636   6483   1177    -92   -740       C  
ATOM   6960  C   GLU A 853      12.636  24.730  49.740  1.00 56.63           C  
ANISOU 6960  C   GLU A 853     6855   8529   6131   1220    -80   -692       C  
ATOM   6961  O   GLU A 853      11.816  24.220  50.510  1.00 53.35           O  
ANISOU 6961  O   GLU A 853     6396   8234   5639   1294    -49   -623       O  
ATOM   6962  CB  GLU A 853      12.107  27.170  49.482  1.00 62.27           C  
ANISOU 6962  CB  GLU A 853     7628   9109   6921   1250   -112   -886       C  
ATOM   6963  CG  GLU A 853      11.761  28.376  48.589  1.00 65.15           C  
ANISOU 6963  CG  GLU A 853     8044   9320   7390   1219   -123   -939       C  
ATOM   6964  CD  GLU A 853      12.981  28.990  47.896  1.00 68.67           C  
ANISOU 6964  CD  GLU A 853     8531   9637   7923   1128   -163  -1024       C  
ATOM   6965  OE1 GLU A 853      14.120  28.813  48.388  1.00 67.67           O  
ANISOU 6965  OE1 GLU A 853     8393   9555   7764   1110   -191  -1090       O  
ATOM   6966  OE2 GLU A 853      12.798  29.662  46.858  1.00 70.02           O  
ANISOU 6966  OE2 GLU A 853     8742   9669   8194   1076   -165  -1019       O  
ATOM   6967  N   ILE A 854      13.905  24.356  49.690  1.00 55.20           N  
ANISOU 6967  N   ILE A 854     6675   8341   5955   1174   -103   -718       N  
ATOM   6968  CA  ILE A 854      14.449  23.392  50.627  1.00 55.97           C  
ANISOU 6968  CA  ILE A 854     6725   8578   5964   1218    -95   -675       C  
ATOM   6969  C   ILE A 854      14.432  24.008  52.040  1.00 56.32           C  
ANISOU 6969  C   ILE A 854     6733   8769   5897   1322   -111   -776       C  
ATOM   6970  O   ILE A 854      14.751  25.190  52.204  1.00 55.58           O  
ANISOU 6970  O   ILE A 854     6662   8644   5813   1328   -148   -922       O  
ATOM   6971  CB  ILE A 854      15.864  22.916  50.168  1.00 56.68           C  
ANISOU 6971  CB  ILE A 854     6822   8623   6092   1146   -115   -681       C  
ATOM   6972  CG1 ILE A 854      16.439  21.862  51.120  1.00 58.39           C  
ANISOU 6972  CG1 ILE A 854     6983   8984   6218   1199   -104   -620       C  
ATOM   6973  CG2 ILE A 854      16.816  24.103  49.962  1.00 58.26           C  
ANISOU 6973  CG2 ILE A 854     7048   8754   6334   1105   -167   -833       C  
ATOM   6974  CD1 ILE A 854      17.523  21.013  50.494  1.00 58.01           C  
ANISOU 6974  CD1 ILE A 854     6939   8885   6217   1134   -102   -567       C  
ATOM   6975  N   THR A 855      14.014  23.220  53.033  1.00 55.66           N  
ANISOU 6975  N   THR A 855     6595   8844   5710   1403    -82   -696       N  
ATOM   6976  CA  THR A 855      13.958  23.664  54.438  1.00 57.14           C  
ANISOU 6976  CA  THR A 855     6740   9199   5770   1512    -92   -779       C  
ATOM   6977  C   THR A 855      15.152  24.523  54.867  1.00 58.44           C  
ANISOU 6977  C   THR A 855     6912   9381   5911   1506   -152   -952       C  
ATOM   6978  O   THR A 855      16.304  24.198  54.566  1.00 57.13           O  
ANISOU 6978  O   THR A 855     6745   9187   5775   1443   -178   -958       O  
ATOM   6979  CB  THR A 855      13.773  22.474  55.427  1.00 56.99           C  
ANISOU 6979  CB  THR A 855     6652   9362   5640   1587    -57   -653       C  
ATOM   6980  OG1 THR A 855      13.862  22.948  56.778  1.00 57.83           O  
ANISOU 6980  OG1 THR A 855     6717   9645   5610   1691    -72   -746       O  
ATOM   6981  CG2 THR A 855      14.816  21.382  55.204  1.00 55.01           C  
ANISOU 6981  CG2 THR A 855     6386   9109   5406   1537    -57   -568       C  
ATOM   6982  N   ASP A 856      14.857  25.620  55.566  1.00 61.69           N  
ANISOU 6982  N   ASP A 856     7329   9839   6271   1570   -172  -1092       N  
ATOM   6983  CA  ASP A 856      15.866  26.599  56.008  1.00 65.87           C  
ANISOU 6983  CA  ASP A 856     7870  10376   6781   1560   -233  -1279       C  
ATOM   6984  C   ASP A 856      17.036  25.975  56.779  1.00 67.71           C  
ANISOU 6984  C   ASP A 856     8047  10756   6923   1569   -263  -1286       C  
ATOM   6985  O   ASP A 856      18.151  26.518  56.782  1.00 67.17           O  
ANISOU 6985  O   ASP A 856     7984  10665   6873   1517   -318  -1407       O  
ATOM   6986  CB  ASP A 856      15.215  27.716  56.841  1.00 68.96           C  
ANISOU 6986  CB  ASP A 856     8270  10822   7108   1650   -241  -1423       C  
ATOM   6987  CG  ASP A 856      14.544  28.788  55.979  1.00 71.88           C  
ANISOU 6987  CG  ASP A 856     8707  11004   7599   1620   -235  -1482       C  
ATOM   6988  OD1 ASP A 856      13.344  29.067  56.198  1.00 73.96           O  
ANISOU 6988  OD1 ASP A 856     8974  11289   7840   1699   -196  -1463       O  
ATOM   6989  OD2 ASP A 856      15.214  29.356  55.087  1.00 73.93           O  
ANISOU 6989  OD2 ASP A 856     9013  11099   7978   1522   -268  -1540       O  
ATOM   6990  N   LEU A 857      16.770  24.834  57.418  1.00 69.45           N  
ANISOU 6990  N   LEU A 857     8211  11129   7048   1634   -226  -1149       N  
ATOM   6991  CA  LEU A 857      17.796  24.043  58.108  1.00 71.99           C  
ANISOU 6991  CA  LEU A 857     8472  11599   7283   1653   -244  -1113       C  
ATOM   6992  C   LEU A 857      19.075  23.850  57.282  1.00 71.38           C  
ANISOU 6992  C   LEU A 857     8407  11416   7299   1547   -277  -1118       C  
ATOM   6993  O   LEU A 857      20.187  24.034  57.787  1.00 74.15           O  
ANISOU 6993  O   LEU A 857     8723  11850   7599   1541   -327  -1203       O  
ATOM   6994  CB  LEU A 857      17.235  22.665  58.503  1.00 72.75           C  
ANISOU 6994  CB  LEU A 857     8516  11809   7315   1714   -184   -912       C  
ATOM   6995  CG  LEU A 857      16.256  22.519  59.677  1.00 74.64           C  
ANISOU 6995  CG  LEU A 857     8707  12238   7416   1840   -149   -873       C  
ATOM   6996  CD1 LEU A 857      15.693  21.103  59.717  1.00 73.40           C  
ANISOU 6996  CD1 LEU A 857     8509  12133   7246   1867    -84   -648       C  
ATOM   6997  CD2 LEU A 857      16.911  22.872  61.010  1.00 75.91           C  
ANISOU 6997  CD2 LEU A 857     8815  12610   7419   1920   -191   -987       C  
ATOM   6998  N   ILE A 858      18.909  23.489  56.012  1.00 67.60           N  
ANISOU 6998  N   ILE A 858     7973  10761   6951   1465   -249  -1027       N  
ATOM   6999  CA  ILE A 858      20.036  23.072  55.182  1.00 65.37           C  
ANISOU 6999  CA  ILE A 858     7697  10389   6752   1375   -264   -997       C  
ATOM   7000  C   ILE A 858      20.250  23.938  53.932  1.00 62.04           C  
ANISOU 7000  C   ILE A 858     7342   9760   6471   1269   -285  -1073       C  
ATOM   7001  O   ILE A 858      21.260  23.792  53.235  1.00 60.33           O  
ANISOU 7001  O   ILE A 858     7130   9469   6322   1192   -302  -1071       O  
ATOM   7002  CB  ILE A 858      19.918  21.572  54.803  1.00 65.26           C  
ANISOU 7002  CB  ILE A 858     7667  10372   6757   1374   -208   -801       C  
ATOM   7003  CG1 ILE A 858      18.530  21.268  54.227  1.00 63.86           C  
ANISOU 7003  CG1 ILE A 858     7526  10107   6630   1372   -155   -700       C  
ATOM   7004  CG2 ILE A 858      20.221  20.696  56.030  1.00 68.26           C  
ANISOU 7004  CG2 ILE A 858     7970  10960   7006   1467   -198   -727       C  
ATOM   7005  CD1 ILE A 858      18.302  19.820  53.866  1.00 65.27           C  
ANISOU 7005  CD1 ILE A 858     7695  10271   6836   1364   -100   -516       C  
ATOM   7006  N   LYS A 859      19.310  24.844  53.667  1.00 59.65           N  
ANISOU 7006  N   LYS A 859     7085   9370   6209   1270   -281  -1133       N  
ATOM   7007  CA  LYS A 859      19.372  25.707  52.483  1.00 57.70           C  
ANISOU 7007  CA  LYS A 859     6900   8927   6095   1178   -296  -1190       C  
ATOM   7008  C   LYS A 859      20.742  26.366  52.312  1.00 56.26           C  
ANISOU 7008  C   LYS A 859     6717   8703   5957   1106   -352  -1308       C  
ATOM   7009  O   LYS A 859      21.351  26.266  51.244  1.00 54.25           O  
ANISOU 7009  O   LYS A 859     6484   8328   5799   1016   -353  -1274       O  
ATOM   7010  CB  LYS A 859      18.261  26.768  52.509  1.00 57.99           C  
ANISOU 7010  CB  LYS A 859     6976   8903   6152   1213   -291  -1263       C  
ATOM   7011  CG  LYS A 859      18.251  27.667  51.280  1.00 56.48           C  
ANISOU 7011  CG  LYS A 859     6848   8510   6103   1125   -301  -1304       C  
ATOM   7012  CD  LYS A 859      17.132  28.682  51.323  1.00 59.00           C  
ANISOU 7012  CD  LYS A 859     7203   8770   6444   1171   -291  -1364       C  
ATOM   7013  CE  LYS A 859      17.262  29.658  50.165  1.00 62.18           C  
ANISOU 7013  CE  LYS A 859     7664   8975   6988   1086   -305  -1408       C  
ATOM   7014  NZ  LYS A 859      15.976  30.338  49.856  1.00 65.16           N  
ANISOU 7014  NZ  LYS A 859     8076   9275   7407   1127   -277  -1399       N  
ATOM   7015  N   ASP A 860      21.215  27.016  53.373  1.00 55.81           N  
ANISOU 7015  N   ASP A 860     6630   8754   5820   1145   -399  -1445       N  
ATOM   7016  CA  ASP A 860      22.487  27.734  53.365  1.00 56.69           C  
ANISOU 7016  CA  ASP A 860     6732   8843   5966   1075   -460  -1573       C  
ATOM   7017  C   ASP A 860      23.662  26.856  52.957  1.00 54.42           C  
ANISOU 7017  C   ASP A 860     6404   8578   5695   1020   -465  -1492       C  
ATOM   7018  O   ASP A 860      24.513  27.281  52.177  1.00 54.05           O  
ANISOU 7018  O   ASP A 860     6369   8424   5743    925   -490  -1529       O  
ATOM   7019  CB  ASP A 860      22.750  28.383  54.733  1.00 60.17           C  
ANISOU 7019  CB  ASP A 860     7137   9432   6292   1136   -510  -1728       C  
ATOM   7020  CG  ASP A 860      21.926  29.647  54.948  1.00 66.02           C  
ANISOU 7020  CG  ASP A 860     7931  10100   7055   1163   -520  -1865       C  
ATOM   7021  OD1 ASP A 860      21.496  30.258  53.942  1.00 68.15           O  
ANISOU 7021  OD1 ASP A 860     8261  10181   7452   1108   -504  -1863       O  
ATOM   7022  OD2 ASP A 860      21.707  30.034  56.120  1.00 70.63           O  
ANISOU 7022  OD2 ASP A 860     8494  10818   7526   1243   -541  -1973       O  
ATOM   7023  N   ASP A 861      23.693  25.634  53.476  1.00 54.08           N  
ANISOU 7023  N   ASP A 861     6312   8672   5563   1082   -436  -1373       N  
ATOM   7024  CA  ASP A 861      24.769  24.692  53.182  1.00 55.17           C  
ANISOU 7024  CA  ASP A 861     6409   8845   5710   1051   -432  -1285       C  
ATOM   7025  C   ASP A 861      24.662  24.113  51.776  1.00 53.38           C  
ANISOU 7025  C   ASP A 861     6226   8455   5599    984   -385  -1166       C  
ATOM   7026  O   ASP A 861      25.672  23.834  51.140  1.00 53.04           O  
ANISOU 7026  O   ASP A 861     6171   8371   5612    923   -390  -1141       O  
ATOM   7027  CB  ASP A 861      24.793  23.564  54.212  1.00 56.53           C  
ANISOU 7027  CB  ASP A 861     6515   9210   5754   1149   -411  -1187       C  
ATOM   7028  CG  ASP A 861      25.217  24.040  55.588  1.00 61.11           C  
ANISOU 7028  CG  ASP A 861     7034   9980   6203   1209   -466  -1304       C  
ATOM   7029  OD1 ASP A 861      24.436  23.850  56.550  1.00 63.27           O  
ANISOU 7029  OD1 ASP A 861     7288  10384   6367   1305   -450  -1288       O  
ATOM   7030  OD2 ASP A 861      26.328  24.605  55.707  1.00 61.24           O  
ANISOU 7030  OD2 ASP A 861     7021  10023   6224   1158   -525  -1411       O  
ATOM   7031  N   VAL A 862      23.436  23.931  51.298  1.00 52.60           N  
ANISOU 7031  N   VAL A 862     6178   8275   5534    997   -339  -1095       N  
ATOM   7032  CA  VAL A 862      23.219  23.440  49.943  1.00 50.39           C  
ANISOU 7032  CA  VAL A 862     5944   7843   5358    931   -297   -995       C  
ATOM   7033  C   VAL A 862      23.756  24.466  48.947  1.00 51.02           C  
ANISOU 7033  C   VAL A 862     6062   7775   5547    832   -327  -1079       C  
ATOM   7034  O   VAL A 862      24.550  24.124  48.065  1.00 50.22           O  
ANISOU 7034  O   VAL A 862     5965   7608   5510    766   -318  -1037       O  
ATOM   7035  CB  VAL A 862      21.724  23.097  49.688  1.00 49.39           C  
ANISOU 7035  CB  VAL A 862     5855   7672   5238    962   -249   -907       C  
ATOM   7036  CG1 VAL A 862      21.431  22.961  48.204  1.00 47.84           C  
ANISOU 7036  CG1 VAL A 862     5716   7308   5153    879   -221   -844       C  
ATOM   7037  CG2 VAL A 862      21.348  21.811  50.422  1.00 47.52           C  
ANISOU 7037  CG2 VAL A 862     5578   7560   4917   1039   -209   -784       C  
ATOM   7038  N   LEU A 863      23.363  25.725  49.126  1.00 51.76           N  
ANISOU 7038  N   LEU A 863     6182   7824   5661    826   -358  -1197       N  
ATOM   7039  CA  LEU A 863      23.737  26.799  48.196  1.00 53.72           C  
ANISOU 7039  CA  LEU A 863     6469   7919   6022    734   -383  -1271       C  
ATOM   7040  C   LEU A 863      25.235  27.063  48.195  1.00 52.83           C  
ANISOU 7040  C   LEU A 863     6317   7825   5931    672   -426  -1337       C  
ATOM   7041  O   LEU A 863      25.787  27.554  47.207  1.00 52.69           O  
ANISOU 7041  O   LEU A 863     6320   7687   6014    583   -433  -1348       O  
ATOM   7042  CB  LEU A 863      22.982  28.108  48.504  1.00 55.27           C  
ANISOU 7042  CB  LEU A 863     6701   8060   6239    751   -405  -1386       C  
ATOM   7043  CG  LEU A 863      21.445  28.180  48.564  1.00 57.02           C  
ANISOU 7043  CG  LEU A 863     6958   8262   6446    816   -368  -1346       C  
ATOM   7044  CD1 LEU A 863      20.954  29.569  48.151  1.00 57.77           C  
ANISOU 7044  CD1 LEU A 863     7105   8218   6628    792   -383  -1436       C  
ATOM   7045  CD2 LEU A 863      20.770  27.118  47.714  1.00 56.34           C  
ANISOU 7045  CD2 LEU A 863     6888   8140   6380    808   -314  -1184       C  
ATOM   7046  N   HIS A 864      25.878  26.740  49.310  1.00 51.74           N  
ANISOU 7046  N   HIS A 864     6116   7847   5695    720   -455  -1374       N  
ATOM   7047  CA  HIS A 864      27.302  26.968  49.478  1.00 53.50           C  
ANISOU 7047  CA  HIS A 864     6286   8120   5923    668   -502  -1439       C  
ATOM   7048  C   HIS A 864      28.113  25.806  48.908  1.00 51.10           C  
ANISOU 7048  C   HIS A 864     5949   7839   5628    650   -470  -1314       C  
ATOM   7049  O   HIS A 864      29.209  26.012  48.394  1.00 51.08           O  
ANISOU 7049  O   HIS A 864     5920   7806   5681    578   -491  -1332       O  
ATOM   7050  CB  HIS A 864      27.629  27.184  50.961  1.00 56.11           C  
ANISOU 7050  CB  HIS A 864     6558   8628   6134    730   -552  -1542       C  
ATOM   7051  CG  HIS A 864      29.053  27.565  51.222  1.00 60.85           C  
ANISOU 7051  CG  HIS A 864     7096   9289   6734    671   -612  -1627       C  
ATOM   7052  ND1 HIS A 864      30.035  26.636  51.497  1.00 62.46           N  
ANISOU 7052  ND1 HIS A 864     7226   9623   6881    686   -615  -1557       N  
ATOM   7053  CD2 HIS A 864      29.660  28.775  51.258  1.00 64.48           C  
ANISOU 7053  CD2 HIS A 864     7553   9698   7248    594   -673  -1774       C  
ATOM   7054  CE1 HIS A 864      31.185  27.257  51.687  1.00 66.37           C  
ANISOU 7054  CE1 HIS A 864     7670  10158   7391    621   -676  -1656       C  
ATOM   7055  NE2 HIS A 864      30.984  28.556  51.550  1.00 67.73           N  
ANISOU 7055  NE2 HIS A 864     7884  10218   7631    560   -714  -1791       N  
ATOM   7056  N   TRP A 865      27.565  24.594  48.995  1.00 49.02           N  
ANISOU 7056  N   TRP A 865     5686   7626   5315    717   -418  -1186       N  
ATOM   7057  CA  TRP A 865      28.260  23.390  48.525  1.00 47.99           C  
ANISOU 7057  CA  TRP A 865     5528   7516   5190    716   -380  -1065       C  
ATOM   7058  C   TRP A 865      27.763  22.849  47.176  1.00 46.16           C  
ANISOU 7058  C   TRP A 865     5359   7135   5045    675   -322   -962       C  
ATOM   7059  O   TRP A 865      28.177  21.771  46.748  1.00 46.68           O  
ANISOU 7059  O   TRP A 865     5415   7203   5117    682   -281   -860       O  
ATOM   7060  CB  TRP A 865      28.231  22.305  49.607  1.00 48.08           C  
ANISOU 7060  CB  TRP A 865     5485   7694   5087    819   -363   -989       C  
ATOM   7061  CG  TRP A 865      29.134  22.626  50.761  1.00 47.65           C  
ANISOU 7061  CG  TRP A 865     5352   7807   4945    849   -422  -1073       C  
ATOM   7062  CD1 TRP A 865      28.786  23.235  51.941  1.00 47.23           C  
ANISOU 7062  CD1 TRP A 865     5276   7871   4800    901   -464  -1171       C  
ATOM   7063  CD2 TRP A 865      30.541  22.380  50.836  1.00 47.38           C  
ANISOU 7063  CD2 TRP A 865     5247   7851   4903    829   -447  -1071       C  
ATOM   7064  NE1 TRP A 865      29.890  23.372  52.745  1.00 48.48           N  
ANISOU 7064  NE1 TRP A 865     5353   8178   4889    909   -518  -1233       N  
ATOM   7065  CE2 TRP A 865      30.982  22.859  52.094  1.00 49.04           C  
ANISOU 7065  CE2 TRP A 865     5390   8231   5012    865   -510  -1170       C  
ATOM   7066  CE3 TRP A 865      31.475  21.801  49.964  1.00 46.78           C  
ANISOU 7066  CE3 TRP A 865     5155   7728   4892    787   -421   -997       C  
ATOM   7067  CZ2 TRP A 865      32.319  22.771  52.504  1.00 46.98           C  
ANISOU 7067  CZ2 TRP A 865     5041   8095   4713    855   -552  -1191       C  
ATOM   7068  CZ3 TRP A 865      32.799  21.710  50.371  1.00 45.85           C  
ANISOU 7068  CZ3 TRP A 865     4949   7731   4740    784   -457  -1013       C  
ATOM   7069  CH2 TRP A 865      33.209  22.199  51.635  1.00 46.68           C  
ANISOU 7069  CH2 TRP A 865     4983   8008   4744    815   -525  -1108       C  
ATOM   7070  N   MET A 866      26.880  23.602  46.519  1.00 45.85           N  
ANISOU 7070  N   MET A 866     5384   6969   5068    635   -318   -992       N  
ATOM   7071  CA  MET A 866      26.382  23.282  45.179  1.00 43.88           C  
ANISOU 7071  CA  MET A 866     5193   6580   4897    585   -272   -911       C  
ATOM   7072  C   MET A 866      27.518  23.192  44.179  1.00 42.24           C  
ANISOU 7072  C   MET A 866     4980   6313   4758    511   -266   -894       C  
ATOM   7073  O   MET A 866      28.330  24.116  44.079  1.00 42.46           O  
ANISOU 7073  O   MET A 866     4986   6322   4825    456   -306   -976       O  
ATOM   7074  CB  MET A 866      25.483  24.408  44.682  1.00 44.88           C  
ANISOU 7074  CB  MET A 866     5375   6593   5083    547   -284   -966       C  
ATOM   7075  CG  MET A 866      24.036  24.331  45.036  1.00 44.86           C  
ANISOU 7075  CG  MET A 866     5402   6596   5046    605   -264   -938       C  
ATOM   7076  SD  MET A 866      23.295  25.802  44.328  1.00 43.66           S  
ANISOU 7076  SD  MET A 866     5306   6302   4981    555   -281  -1006       S  
ATOM   7077  CE  MET A 866      23.180  25.316  42.609  1.00 45.14           C  
ANISOU 7077  CE  MET A 866     5539   6360   5252    477   -240   -900       C  
ATOM   7078  N   ASP A 867      27.550  22.102  43.414  1.00 40.47           N  
ANISOU 7078  N   ASP A 867     4773   6053   4550    508   -214   -789       N  
ATOM   7079  CA  ASP A 867      28.595  21.908  42.408  1.00 39.15           C  
ANISOU 7079  CA  ASP A 867     4601   5835   4439    449   -197   -763       C  
ATOM   7080  C   ASP A 867      28.130  22.390  41.040  1.00 36.44           C  
ANISOU 7080  C   ASP A 867     4320   5348   4176    374   -179   -752       C  
ATOM   7081  O   ASP A 867      27.523  21.633  40.284  1.00 33.94           O  
ANISOU 7081  O   ASP A 867     4050   4975   3872    371   -134   -676       O  
ATOM   7082  CB  ASP A 867      29.039  20.442  42.343  1.00 36.98           C  
ANISOU 7082  CB  ASP A 867     4310   5605   4137    494   -147   -664       C  
ATOM   7083  CG  ASP A 867      30.392  20.270  41.674  1.00 38.53           C  
ANISOU 7083  CG  ASP A 867     4474   5797   4370    456   -137   -653       C  
ATOM   7084  OD1 ASP A 867      30.732  21.055  40.762  1.00 39.60           O  
ANISOU 7084  OD1 ASP A 867     4625   5853   4570    378   -146   -688       O  
ATOM   7085  OD2 ASP A 867      31.126  19.339  42.058  1.00 38.65           O  
ANISOU 7085  OD2 ASP A 867     4444   5892   4349    508   -115   -601       O  
ATOM   7086  N   TYR A 868      28.422  23.656  40.749  1.00 36.36           N  
ANISOU 7086  N   TYR A 868     4311   5284   4221    312   -216   -828       N  
ATOM   7087  CA  TYR A 868      28.047  24.301  39.495  1.00 36.23           C  
ANISOU 7087  CA  TYR A 868     4346   5138   4282    241   -205   -817       C  
ATOM   7088  C   TYR A 868      28.751  23.698  38.296  1.00 36.54           C  
ANISOU 7088  C   TYR A 868     4391   5137   4355    196   -164   -750       C  
ATOM   7089  O   TYR A 868      28.154  23.585  37.233  1.00 36.45           O  
ANISOU 7089  O   TYR A 868     4430   5044   4373    164   -133   -700       O  
ATOM   7090  CB  TYR A 868      28.368  25.796  39.536  1.00 37.14           C  
ANISOU 7090  CB  TYR A 868     4452   5204   4457    185   -253   -909       C  
ATOM   7091  CG  TYR A 868      27.487  26.628  40.440  1.00 38.98           C  
ANISOU 7091  CG  TYR A 868     4699   5438   4674    221   -288   -986       C  
ATOM   7092  CD1 TYR A 868      26.283  27.157  39.979  1.00 39.34           C  
ANISOU 7092  CD1 TYR A 868     4801   5394   4754    220   -278   -974       C  
ATOM   7093  CD2 TYR A 868      27.880  26.921  41.745  1.00 43.55           C  
ANISOU 7093  CD2 TYR A 868     5231   6113   5202    260   -332  -1074       C  
ATOM   7094  CE1 TYR A 868      25.475  27.937  40.807  1.00 41.61           C  
ANISOU 7094  CE1 TYR A 868     5100   5682   5028    262   -305  -1045       C  
ATOM   7095  CE2 TYR A 868      27.081  27.706  42.581  1.00 44.98           C  
ANISOU 7095  CE2 TYR A 868     5428   6298   5364    299   -361  -1155       C  
ATOM   7096  CZ  TYR A 868      25.884  28.207  42.105  1.00 42.88           C  
ANISOU 7096  CZ  TYR A 868     5220   5935   5137    303   -345  -1140       C  
ATOM   7097  OH  TYR A 868      25.100  28.973  42.930  1.00 47.01           O  
ANISOU 7097  OH  TYR A 868     5757   6463   5641    351   -368  -1220       O  
ATOM   7098  N   THR A 869      30.023  23.331  38.463  1.00 38.10           N  
ANISOU 7098  N   THR A 869     4533   5400   4543    196   -163   -750       N  
ATOM   7099  CA  THR A 869      30.816  22.749  37.376  1.00 36.18           C  
ANISOU 7099  CA  THR A 869     4288   5131   4326    163   -120   -691       C  
ATOM   7100  C   THR A 869      30.197  21.435  36.898  1.00 35.36           C  
ANISOU 7100  C   THR A 869     4232   5009   4194    202    -62   -609       C  
ATOM   7101  O   THR A 869      29.967  21.251  35.702  1.00 34.82           O  
ANISOU 7101  O   THR A 869     4210   4866   4155    162    -28   -569       O  
ATOM   7102  CB  THR A 869      32.290  22.527  37.795  1.00 37.66           C  
ANISOU 7102  CB  THR A 869     4395   5411   4502    171   -129   -701       C  
ATOM   7103  OG1 THR A 869      32.850  23.758  38.276  1.00 40.14           O  
ANISOU 7103  OG1 THR A 869     4664   5743   4846    124   -188   -785       O  
ATOM   7104  CG2 THR A 869      33.123  22.024  36.614  1.00 34.30           C  
ANISOU 7104  CG2 THR A 869     3967   4959   4107    139    -79   -642       C  
ATOM   7105  N   VAL A 870      29.918  20.534  37.838  1.00 35.77           N  
ANISOU 7105  N   VAL A 870     4272   5130   4188    277    -53   -584       N  
ATOM   7106  CA  VAL A 870      29.254  19.274  37.515  1.00 38.27           C  
ANISOU 7106  CA  VAL A 870     4635   5422   4485    312     -1   -510       C  
ATOM   7107  C   VAL A 870      27.904  19.574  36.866  1.00 40.19           C  
ANISOU 7107  C   VAL A 870     4944   5578   4747    276      1   -501       C  
ATOM   7108  O   VAL A 870      27.534  18.982  35.845  1.00 39.70           O  
ANISOU 7108  O   VAL A 870     4932   5451   4700    250     40   -456       O  
ATOM   7109  CB  VAL A 870      29.075  18.391  38.768  1.00 38.65           C  
ANISOU 7109  CB  VAL A 870     4654   5559   4473    400      4   -479       C  
ATOM   7110  CG1 VAL A 870      28.103  17.250  38.493  1.00 38.03           C  
ANISOU 7110  CG1 VAL A 870     4629   5434   4385    425     52   -405       C  
ATOM   7111  CG2 VAL A 870      30.429  17.838  39.224  1.00 39.44           C  
ANISOU 7111  CG2 VAL A 870     4687   5745   4552    443     13   -463       C  
ATOM   7112  N   LEU A 871      27.195  20.529  37.456  1.00 40.36           N  
ANISOU 7112  N   LEU A 871     4965   5603   4766    277    -41   -548       N  
ATOM   7113  CA  LEU A 871      25.890  20.932  36.988  1.00 41.20           C  
ANISOU 7113  CA  LEU A 871     5123   5644   4889    252    -43   -538       C  
ATOM   7114  C   LEU A 871      25.970  21.411  35.540  1.00 40.77           C  
ANISOU 7114  C   LEU A 871     5104   5500   4888    175    -32   -528       C  
ATOM   7115  O   LEU A 871      25.176  21.002  34.699  1.00 42.13           O  
ANISOU 7115  O   LEU A 871     5322   5622   5063    152     -7   -482       O  
ATOM   7116  CB  LEU A 871      25.370  22.050  37.886  1.00 44.04           C  
ANISOU 7116  CB  LEU A 871     5467   6024   5243    272    -91   -603       C  
ATOM   7117  CG  LEU A 871      23.874  22.185  38.122  1.00 46.98           C  
ANISOU 7117  CG  LEU A 871     5869   6382   5600    297    -93   -587       C  
ATOM   7118  CD1 LEU A 871      23.664  23.146  39.279  1.00 49.08           C  
ANISOU 7118  CD1 LEU A 871     6108   6694   5846    338   -135   -664       C  
ATOM   7119  CD2 LEU A 871      23.145  22.664  36.854  1.00 50.31           C  
ANISOU 7119  CD2 LEU A 871     6340   6706   6071    236    -85   -561       C  
ATOM   7120  N   LEU A 872      26.940  22.269  35.255  1.00 40.81           N  
ANISOU 7120  N   LEU A 872     5082   5492   4932    134    -51   -568       N  
ATOM   7121  CA  LEU A 872      27.116  22.798  33.917  1.00 42.88           C  
ANISOU 7121  CA  LEU A 872     5368   5680   5243     63    -39   -550       C  
ATOM   7122  C   LEU A 872      27.465  21.696  32.919  1.00 44.02           C  
ANISOU 7122  C   LEU A 872     5536   5816   5374     51     13   -494       C  
ATOM   7123  O   LEU A 872      26.898  21.652  31.826  1.00 45.67           O  
ANISOU 7123  O   LEU A 872     5789   5971   5591     12     33   -459       O  
ATOM   7124  CB  LEU A 872      28.178  23.900  33.894  1.00 40.79           C  
ANISOU 7124  CB  LEU A 872     5061   5408   5028     18    -67   -598       C  
ATOM   7125  CG  LEU A 872      28.356  24.588  32.538  1.00 45.57           C  
ANISOU 7125  CG  LEU A 872     5686   5940   5689    -56    -55   -571       C  
ATOM   7126  CD1 LEU A 872      27.070  25.318  32.133  1.00 45.65           C  
ANISOU 7126  CD1 LEU A 872     5742   5880   5723    -73    -67   -559       C  
ATOM   7127  CD2 LEU A 872      29.549  25.534  32.543  1.00 47.29           C  
ANISOU 7127  CD2 LEU A 872     5852   6154   5961   -105    -78   -608       C  
ATOM   7128  N   GLU A 873      28.388  20.814  33.298  1.00 44.47           N  
ANISOU 7128  N   GLU A 873     5562   5928   5406     88     36   -485       N  
ATOM   7129  CA  GLU A 873      28.821  19.726  32.417  1.00 45.46           C  
ANISOU 7129  CA  GLU A 873     5710   6042   5520     88     91   -440       C  
ATOM   7130  C   GLU A 873      27.722  18.724  32.095  1.00 44.16           C  
ANISOU 7130  C   GLU A 873     5606   5843   5330    101    120   -401       C  
ATOM   7131  O   GLU A 873      27.514  18.377  30.933  1.00 44.38           O  
ANISOU 7131  O   GLU A 873     5678   5826   5360     64    151   -379       O  
ATOM   7132  CB  GLU A 873      30.033  18.992  33.000  1.00 46.40           C  
ANISOU 7132  CB  GLU A 873     5778   6230   5622    138    111   -436       C  
ATOM   7133  CG  GLU A 873      31.352  19.708  32.776  1.00 52.08           C  
ANISOU 7133  CG  GLU A 873     6439   6979   6371    106    101   -457       C  
ATOM   7134  CD  GLU A 873      31.652  19.965  31.305  1.00 56.50           C  
ANISOU 7134  CD  GLU A 873     7023   7488   6958     45    132   -436       C  
ATOM   7135  OE1 GLU A 873      32.374  20.952  31.014  1.00 55.40           O  
ANISOU 7135  OE1 GLU A 873     6843   7350   6857     -5    113   -453       O  
ATOM   7136  OE2 GLU A 873      31.163  19.181  30.448  1.00 55.91           O  
ANISOU 7136  OE2 GLU A 873     7005   7372   6865     44    175   -404       O  
ATOM   7137  N   LYS A 874      27.021  18.268  33.126  1.00 43.65           N  
ANISOU 7137  N   LYS A 874     5540   5806   5240    152    110   -394       N  
ATOM   7138  CA  LYS A 874      26.056  17.189  32.973  1.00 43.80           C  
ANISOU 7138  CA  LYS A 874     5605   5797   5239    164    139   -352       C  
ATOM   7139  C   LYS A 874      24.791  17.566  32.205  1.00 43.54           C  
ANISOU 7139  C   LYS A 874     5620   5711   5213    112    127   -342       C  
ATOM   7140  O   LYS A 874      24.372  16.832  31.305  1.00 44.97           O  
ANISOU 7140  O   LYS A 874     5848   5849   5389     82    156   -317       O  
ATOM   7141  CB  LYS A 874      25.710  16.575  34.336  1.00 43.83           C  
ANISOU 7141  CB  LYS A 874     5585   5854   5214    235    135   -333       C  
ATOM   7142  CG  LYS A 874      26.431  15.259  34.597  1.00 46.11           C  
ANISOU 7142  CG  LYS A 874     5866   6160   5492    287    182   -296       C  
ATOM   7143  CD  LYS A 874      26.600  14.953  36.076  1.00 48.26           C  
ANISOU 7143  CD  LYS A 874     6086   6516   5733    366    171   -279       C  
ATOM   7144  CE  LYS A 874      25.272  14.903  36.814  1.00 48.22           C  
ANISOU 7144  CE  LYS A 874     6089   6525   5706    385    155   -257       C  
ATOM   7145  NZ  LYS A 874      25.456  14.421  38.210  1.00 48.30           N  
ANISOU 7145  NZ  LYS A 874     6048   6626   5677    468    154   -227       N  
ATOM   7146  N   THR A 875      24.196  18.705  32.548  1.00 41.77           N  
ANISOU 7146  N   THR A 875     5382   5490   4998    102     84   -364       N  
ATOM   7147  CA  THR A 875      22.862  19.045  32.046  1.00 39.70           C  
ANISOU 7147  CA  THR A 875     5154   5194   4738     69     70   -345       C  
ATOM   7148  C   THR A 875      22.875  19.982  30.840  1.00 38.62           C  
ANISOU 7148  C   THR A 875     5034   5012   4628      5     61   -348       C  
ATOM   7149  O   THR A 875      21.892  20.060  30.097  1.00 38.65           O  
ANISOU 7149  O   THR A 875     5068   4990   4628    -30     58   -319       O  
ATOM   7150  CB  THR A 875      21.977  19.684  33.153  1.00 39.24           C  
ANISOU 7150  CB  THR A 875     5072   5165   4671    109     35   -357       C  
ATOM   7151  OG1 THR A 875      22.475  20.989  33.465  1.00 36.32           O  
ANISOU 7151  OG1 THR A 875     4674   4797   4329    108      1   -408       O  
ATOM   7152  CG2 THR A 875      21.966  18.831  34.416  1.00 37.91           C  
ANISOU 7152  CG2 THR A 875     4879   5057   4469    177     44   -346       C  
ATOM   7153  N   PHE A 876      23.978  20.696  30.651  1.00 38.26           N  
ANISOU 7153  N   PHE A 876     4963   4964   4610    -11     56   -375       N  
ATOM   7154  CA  PHE A 876      24.043  21.702  29.603  1.00 38.21           C  
ANISOU 7154  CA  PHE A 876     4964   4917   4635    -68     48   -368       C  
ATOM   7155  C   PHE A 876      25.059  21.357  28.524  1.00 39.82           C  
ANISOU 7155  C   PHE A 876     5174   5116   4839   -104     84   -355       C  
ATOM   7156  O   PHE A 876      24.684  21.192  27.363  1.00 41.94           O  
ANISOU 7156  O   PHE A 876     5477   5365   5093   -145    102   -324       O  
ATOM   7157  CB  PHE A 876      24.298  23.097  30.186  1.00 36.62           C  
ANISOU 7157  CB  PHE A 876     4729   4704   4480    -69      9   -407       C  
ATOM   7158  CG  PHE A 876      24.336  24.184  29.156  1.00 32.91           C  
ANISOU 7158  CG  PHE A 876     4267   4184   4055   -125      2   -388       C  
ATOM   7159  CD1 PHE A 876      23.166  24.635  28.560  1.00 31.28           C  
ANISOU 7159  CD1 PHE A 876     4088   3945   3853   -143     -6   -351       C  
ATOM   7160  CD2 PHE A 876      25.542  24.763  28.786  1.00 32.42           C  
ANISOU 7160  CD2 PHE A 876     4175   4110   4031   -161      6   -398       C  
ATOM   7161  CE1 PHE A 876      23.203  25.641  27.590  1.00 34.41           C  
ANISOU 7161  CE1 PHE A 876     4487   4296   4290   -190     -9   -320       C  
ATOM   7162  CE2 PHE A 876      25.589  25.768  27.823  1.00 33.68           C  
ANISOU 7162  CE2 PHE A 876     4338   4223   4237   -214      4   -368       C  
ATOM   7163  CZ  PHE A 876      24.416  26.211  27.227  1.00 33.73           C  
ANISOU 7163  CZ  PHE A 876     4375   4193   4246   -226     -3   -327       C  
ATOM   7164  N   ILE A 877      26.332  21.236  28.901  1.00 40.94           N  
ANISOU 7164  N   ILE A 877     5278   5287   4990    -87     95   -377       N  
ATOM   7165  CA  ILE A 877      27.397  21.067  27.910  1.00 40.78           C  
ANISOU 7165  CA  ILE A 877     5252   5270   4972   -117    130   -363       C  
ATOM   7166  C   ILE A 877      27.302  19.758  27.132  1.00 40.95           C  
ANISOU 7166  C   ILE A 877     5318   5291   4951   -112    179   -341       C  
ATOM   7167  O   ILE A 877      27.388  19.762  25.897  1.00 42.38           O  
ANISOU 7167  O   ILE A 877     5523   5460   5119   -152    204   -322       O  
ATOM   7168  CB  ILE A 877      28.804  21.269  28.507  1.00 42.20           C  
ANISOU 7168  CB  ILE A 877     5370   5490   5174   -100    130   -388       C  
ATOM   7169  CG1 ILE A 877      28.930  22.697  29.046  1.00 42.09           C  
ANISOU 7169  CG1 ILE A 877     5318   5463   5211   -125     79   -419       C  
ATOM   7170  CG2 ILE A 877      29.891  20.993  27.438  1.00 40.97           C  
ANISOU 7170  CG2 ILE A 877     5204   5348   5016   -124    175   -365       C  
ATOM   7171  CD1 ILE A 877      30.343  23.092  29.460  1.00 46.96           C  
ANISOU 7171  CD1 ILE A 877     5866   6119   5857   -132     71   -444       C  
ATOM   7172  N   LYS A 878      27.108  18.649  27.839  1.00 39.87           N  
ANISOU 7172  N   LYS A 878     5193   5165   4790    -62    194   -345       N  
ATOM   7173  CA  LYS A 878      26.990  17.354  27.174  1.00 41.89           C  
ANISOU 7173  CA  LYS A 878     5497   5404   5014    -56    241   -333       C  
ATOM   7174  C   LYS A 878      25.833  17.303  26.160  1.00 40.11           C  
ANISOU 7174  C   LYS A 878     5327   5145   4767   -109    238   -319       C  
ATOM   7175  O   LYS A 878      26.063  16.938  25.011  1.00 40.97           O  
ANISOU 7175  O   LYS A 878     5468   5247   4853   -138    271   -318       O  
ATOM   7176  CB  LYS A 878      26.939  16.186  28.172  1.00 44.86           C  
ANISOU 7176  CB  LYS A 878     5876   5788   5381      7    259   -330       C  
ATOM   7177  CG  LYS A 878      27.295  14.854  27.526  1.00 51.25           C  
ANISOU 7177  CG  LYS A 878     6727   6572   6173     22    318   -325       C  
ATOM   7178  CD  LYS A 878      27.298  13.682  28.504  1.00 59.54           C  
ANISOU 7178  CD  LYS A 878     7779   7620   7225     88    341   -310       C  
ATOM   7179  CE  LYS A 878      27.438  12.352  27.741  1.00 62.74           C  
ANISOU 7179  CE  LYS A 878     8242   7974   7623     96    402   -311       C  
ATOM   7180  NZ  LYS A 878      27.476  11.164  28.644  1.00 65.73           N  
ANISOU 7180  NZ  LYS A 878     8624   8335   8014    163    432   -285       N  
ATOM   7181  N   PRO A 879      24.602  17.691  26.563  1.00 39.24           N  
ANISOU 7181  N   PRO A 879     5224   5026   4659   -119    199   -309       N  
ATOM   7182  CA  PRO A 879      23.546  17.763  25.551  1.00 39.09           C  
ANISOU 7182  CA  PRO A 879     5245   4989   4618   -173    190   -291       C  
ATOM   7183  C   PRO A 879      23.878  18.698  24.391  1.00 37.99           C  
ANISOU 7183  C   PRO A 879     5103   4854   4479   -222    189   -278       C  
ATOM   7184  O   PRO A 879      23.650  18.329  23.249  1.00 37.31           O  
ANISOU 7184  O   PRO A 879     5052   4770   4356   -260    208   -270       O  
ATOM   7185  CB  PRO A 879      22.343  18.299  26.333  1.00 40.31           C  
ANISOU 7185  CB  PRO A 879     5387   5144   4784   -166    146   -276       C  
ATOM   7186  CG  PRO A 879      22.600  17.870  27.729  1.00 40.28           C  
ANISOU 7186  CG  PRO A 879     5358   5157   4791   -103    146   -289       C  
ATOM   7187  CD  PRO A 879      24.076  18.019  27.903  1.00 38.85           C  
ANISOU 7187  CD  PRO A 879     5146   4991   4626    -80    163   -312       C  
ATOM   7188  N   LEU A 880      24.424  19.881  24.674  1.00 38.85           N  
ANISOU 7188  N   LEU A 880     5168   4965   4627   -221    169   -276       N  
ATOM   7189  CA  LEU A 880      24.797  20.815  23.603  1.00 38.74           C  
ANISOU 7189  CA  LEU A 880     5146   4953   4623   -267    171   -250       C  
ATOM   7190  C   LEU A 880      25.823  20.206  22.629  1.00 39.32           C  
ANISOU 7190  C   LEU A 880     5228   5048   4665   -279    222   -250       C  
ATOM   7191  O   LEU A 880      25.681  20.329  21.402  1.00 38.78           O  
ANISOU 7191  O   LEU A 880     5179   4992   4563   -319    236   -225       O  
ATOM   7192  CB  LEU A 880      25.292  22.152  24.169  1.00 37.19           C  
ANISOU 7192  CB  LEU A 880     4901   4742   4489   -267    142   -251       C  
ATOM   7193  CG  LEU A 880      25.605  23.236  23.127  1.00 38.45           C  
ANISOU 7193  CG  LEU A 880     5046   4892   4673   -317    144   -210       C  
ATOM   7194  CD1 LEU A 880      24.395  23.496  22.237  1.00 39.56           C  
ANISOU 7194  CD1 LEU A 880     5218   5028   4786   -347    132   -165       C  
ATOM   7195  CD2 LEU A 880      26.064  24.524  23.776  1.00 35.35           C  
ANISOU 7195  CD2 LEU A 880     4609   4469   4355   -322    114   -219       C  
ATOM   7196  N   GLU A 881      26.837  19.541  23.181  1.00 40.23           N  
ANISOU 7196  N   GLU A 881     5325   5175   4785   -238    250   -277       N  
ATOM   7197  CA  GLU A 881      27.841  18.839  22.374  1.00 41.76           C  
ANISOU 7197  CA  GLU A 881     5525   5392   4948   -233    305   -281       C  
ATOM   7198  C   GLU A 881      27.169  17.804  21.479  1.00 39.90           C  
ANISOU 7198  C   GLU A 881     5355   5149   4654   -247    332   -291       C  
ATOM   7199  O   GLU A 881      27.543  17.645  20.314  1.00 39.36           O  
ANISOU 7199  O   GLU A 881     5305   5104   4546   -270    367   -287       O  
ATOM   7200  CB  GLU A 881      28.891  18.179  23.267  1.00 44.76           C  
ANISOU 7200  CB  GLU A 881     5874   5788   5345   -175    329   -304       C  
ATOM   7201  CG  GLU A 881      30.198  17.877  22.560  1.00 54.97           C  
ANISOU 7201  CG  GLU A 881     7147   7115   6624   -164    383   -300       C  
ATOM   7202  CD  GLU A 881      31.416  18.182  23.420  1.00 65.56           C  
ANISOU 7202  CD  GLU A 881     8414   8490   8005   -130    382   -302       C  
ATOM   7203  OE1 GLU A 881      32.355  18.825  22.895  1.00 70.63           O  
ANISOU 7203  OE1 GLU A 881     9010   9164   8661   -154    397   -282       O  
ATOM   7204  OE2 GLU A 881      31.438  17.794  24.616  1.00 65.98           O  
ANISOU 7204  OE2 GLU A 881     8451   8547   8073    -83    366   -318       O  
ATOM   7205  N   GLY A 882      26.165  17.120  22.031  1.00 37.52           N  
ANISOU 7205  N   GLY A 882     5088   4821   4346   -237    315   -304       N  
ATOM   7206  CA  GLY A 882      25.330  16.199  21.271  1.00 35.14           C  
ANISOU 7206  CA  GLY A 882     4849   4506   3997   -264    327   -319       C  
ATOM   7207  C   GLY A 882      24.655  16.871  20.084  1.00 35.30           C  
ANISOU 7207  C   GLY A 882     4883   4549   3979   -326    308   -295       C  
ATOM   7208  O   GLY A 882      24.692  16.340  18.968  1.00 36.98           O  
ANISOU 7208  O   GLY A 882     5134   4780   4137   -352    337   -311       O  
ATOM   7209  N   PHE A 883      24.047  18.037  20.313  1.00 33.60           N  
ANISOU 7209  N   PHE A 883     4637   4338   3790   -346    262   -258       N  
ATOM   7210  CA  PHE A 883      23.346  18.756  19.245  1.00 33.66           C  
ANISOU 7210  CA  PHE A 883     4650   4373   3766   -398    241   -219       C  
ATOM   7211  C   PHE A 883      24.321  19.158  18.163  1.00 34.39           C  
ANISOU 7211  C   PHE A 883     4731   4502   3834   -415    275   -202       C  
ATOM   7212  O   PHE A 883      24.119  18.851  16.986  1.00 37.32           O  
ANISOU 7212  O   PHE A 883     5131   4910   4138   -448    291   -199       O  
ATOM   7213  CB  PHE A 883      22.646  20.035  19.739  1.00 30.28           C  
ANISOU 7213  CB  PHE A 883     4187   3935   3385   -403    191   -176       C  
ATOM   7214  CG  PHE A 883      21.727  19.837  20.909  1.00 28.88           C  
ANISOU 7214  CG  PHE A 883     4007   3732   3233   -377    158   -186       C  
ATOM   7215  CD1 PHE A 883      21.250  18.570  21.256  1.00 26.36           C  
ANISOU 7215  CD1 PHE A 883     3721   3404   2889   -369    167   -217       C  
ATOM   7216  CD2 PHE A 883      21.302  20.937  21.646  1.00 27.21           C  
ANISOU 7216  CD2 PHE A 883     3761   3504   3072   -360    121   -163       C  
ATOM   7217  CE1 PHE A 883      20.395  18.397  22.336  1.00 20.40           C  
ANISOU 7217  CE1 PHE A 883     2958   2635   2157   -344    140   -215       C  
ATOM   7218  CE2 PHE A 883      20.440  20.774  22.725  1.00 30.46           C  
ANISOU 7218  CE2 PHE A 883     4168   3905   3500   -330     95   -171       C  
ATOM   7219  CZ  PHE A 883      19.991  19.493  23.079  1.00 23.18           C  
ANISOU 7219  CZ  PHE A 883     3272   2985   2549   -322    105   -192       C  
ATOM   7220  N   THR A 884      25.381  19.841  18.587  1.00 33.11           N  
ANISOU 7220  N   THR A 884     4522   4334   3723   -394    285   -190       N  
ATOM   7221  CA  THR A 884      26.306  20.504  17.683  1.00 31.58           C  
ANISOU 7221  CA  THR A 884     4299   4175   3523   -414    313   -154       C  
ATOM   7222  C   THR A 884      27.080  19.520  16.821  1.00 34.82           C  
ANISOU 7222  C   THR A 884     4734   4625   3869   -405    373   -181       C  
ATOM   7223  O   THR A 884      27.272  19.777  15.632  1.00 38.14           O  
ANISOU 7223  O   THR A 884     5157   5096   4240   -433    395   -151       O  
ATOM   7224  CB  THR A 884      27.281  21.437  18.436  1.00 31.20           C  
ANISOU 7224  CB  THR A 884     4190   4110   3555   -401    307   -138       C  
ATOM   7225  OG1 THR A 884      27.954  20.702  19.465  1.00 30.74           O  
ANISOU 7225  OG1 THR A 884     4121   4040   3518   -353    320   -187       O  
ATOM   7226  CG2 THR A 884      26.527  22.596  19.074  1.00 26.78           C  
ANISOU 7226  CG2 THR A 884     3609   3509   3057   -414    252   -112       C  
ATOM   7227  N   SER A 885      27.512  18.401  17.402  1.00 33.73           N  
ANISOU 7227  N   SER A 885     4616   4469   3730   -361    401   -235       N  
ATOM   7228  CA  SER A 885      28.224  17.382  16.630  1.00 36.91           C  
ANISOU 7228  CA  SER A 885     5050   4899   4076   -341    463   -270       C  
ATOM   7229  C   SER A 885      27.291  16.716  15.614  1.00 37.86           C  
ANISOU 7229  C   SER A 885     5236   5033   4116   -376    465   -297       C  
ATOM   7230  O   SER A 885      27.668  16.538  14.463  1.00 37.69           O  
ANISOU 7230  O   SER A 885     5230   5063   4028   -387    503   -302       O  
ATOM   7231  CB  SER A 885      28.929  16.349  17.522  1.00 38.62           C  
ANISOU 7231  CB  SER A 885     5270   5085   4320   -278    496   -315       C  
ATOM   7232  OG  SER A 885      28.022  15.658  18.359  1.00 41.59           O  
ANISOU 7232  OG  SER A 885     5681   5407   4712   -266    469   -343       O  
ATOM   7233  N   ALA A 886      26.067  16.392  16.028  1.00 35.98           N  
ANISOU 7233  N   ALA A 886     5031   4760   3881   -395    423   -313       N  
ATOM   7234  CA  ALA A 886      25.059  15.905  15.084  1.00 37.07           C  
ANISOU 7234  CA  ALA A 886     5221   4918   3945   -443    411   -334       C  
ATOM   7235  C   ALA A 886      24.868  16.897  13.936  1.00 37.15           C  
ANISOU 7235  C   ALA A 886     5211   5001   3904   -487    398   -280       C  
ATOM   7236  O   ALA A 886      24.742  16.497  12.776  1.00 38.50           O  
ANISOU 7236  O   ALA A 886     5416   5225   3989   -514    417   -301       O  
ATOM   7237  CB  ALA A 886      23.728  15.638  15.787  1.00 34.54           C  
ANISOU 7237  CB  ALA A 886     4920   4557   3647   -464    359   -340       C  
ATOM   7238  N   ALA A 887      24.873  18.188  14.265  1.00 36.47           N  
ANISOU 7238  N   ALA A 887     5070   4917   3871   -492    368   -210       N  
ATOM   7239  CA  ALA A 887      24.658  19.242  13.275  1.00 36.24           C  
ANISOU 7239  CA  ALA A 887     5014   4948   3809   -530    355   -138       C  
ATOM   7240  C   ALA A 887      25.940  19.703  12.574  1.00 37.81           C  
ANISOU 7240  C   ALA A 887     5178   5194   3995   -521    405   -104       C  
ATOM   7241  O   ALA A 887      25.892  20.603  11.726  1.00 37.84           O  
ANISOU 7241  O   ALA A 887     5154   5250   3974   -550    402    -32       O  
ATOM   7242  CB  ALA A 887      23.957  20.417  13.924  1.00 36.77           C  
ANISOU 7242  CB  ALA A 887     5041   4983   3946   -539    301    -76       C  
ATOM   7243  N   LYS A 888      27.073  19.077  12.914  1.00 38.53           N  
ANISOU 7243  N   LYS A 888     5266   5271   4101   -480    453   -148       N  
ATOM   7244  CA  LYS A 888      28.406  19.449  12.394  1.00 39.99           C  
ANISOU 7244  CA  LYS A 888     5408   5504   4284   -466    506   -115       C  
ATOM   7245  C   LYS A 888      28.758  20.914  12.663  1.00 40.64           C  
ANISOU 7245  C   LYS A 888     5419   5576   4445   -485    484    -30       C  
ATOM   7246  O   LYS A 888      29.253  21.614  11.773  1.00 41.41           O  
ANISOU 7246  O   LYS A 888     5482   5730   4522   -506    508     37       O  
ATOM   7247  CB  LYS A 888      28.567  19.155  10.888  1.00 40.61           C  
ANISOU 7247  CB  LYS A 888     5508   5673   4250   -481    549   -110       C  
ATOM   7248  CG  LYS A 888      27.756  17.992  10.327  1.00 46.25           C  
ANISOU 7248  CG  LYS A 888     6299   6402   4872   -489    550   -188       C  
ATOM   7249  CD  LYS A 888      28.493  16.673  10.365  1.00 49.81           C  
ANISOU 7249  CD  LYS A 888     6792   6837   5296   -441    609   -278       C  
ATOM   7250  CE  LYS A 888      27.913  15.735   9.319  1.00 51.30           C  
ANISOU 7250  CE  LYS A 888     7052   7068   5373   -461    623   -348       C  
ATOM   7251  NZ  LYS A 888      28.468  14.356   9.408  1.00 56.28           N  
ANISOU 7251  NZ  LYS A 888     7737   7659   5986   -412    679   -447       N  
ATOM   7252  N   LEU A 889      28.485  21.365  13.885  1.00 40.82           N  
ANISOU 7252  N   LEU A 889     5423   5527   4558   -479    439    -33       N  
ATOM   7253  CA  LEU A 889      28.856  22.700  14.348  1.00 43.64           C  
ANISOU 7253  CA  LEU A 889     5719   5854   5007   -496    415     27       C  
ATOM   7254  C   LEU A 889      29.801  22.646  15.541  1.00 44.43           C  
ANISOU 7254  C   LEU A 889     5782   5918   5183   -464    417    -10       C  
ATOM   7255  O   LEU A 889      29.950  21.609  16.206  1.00 44.40           O  
ANISOU 7255  O   LEU A 889     5801   5902   5169   -423    428    -76       O  
ATOM   7256  CB  LEU A 889      27.613  23.502  14.766  1.00 45.62           C  
ANISOU 7256  CB  LEU A 889     5976   6056   5300   -516    353     55       C  
ATOM   7257  CG  LEU A 889      26.819  24.366  13.779  1.00 45.82           C  
ANISOU 7257  CG  LEU A 889     6000   6108   5301   -554    336    137       C  
ATOM   7258  CD1 LEU A 889      27.639  24.714  12.545  1.00 51.28           C  
ANISOU 7258  CD1 LEU A 889     6663   6870   5952   -576    383    203       C  
ATOM   7259  CD2 LEU A 889      25.534  23.697  13.385  1.00 47.64           C  
ANISOU 7259  CD2 LEU A 889     6282   6366   5453   -561    313    118       C  
ATOM   7260  N   ASP A 890      30.423  23.781  15.818  1.00 44.45           N  
ANISOU 7260  N   ASP A 890     5724   5901   5265   -487    405     35       N  
ATOM   7261  CA  ASP A 890      31.176  23.953  17.043  1.00 45.08           C  
ANISOU 7261  CA  ASP A 890     5759   5946   5421   -468    390      1       C  
ATOM   7262  C   ASP A 890      30.541  25.041  17.901  1.00 44.09           C  
ANISOU 7262  C   ASP A 890     5622   5751   5381   -487    328      6       C  
ATOM   7263  O   ASP A 890      30.171  26.108  17.401  1.00 40.87           O  
ANISOU 7263  O   ASP A 890     5203   5319   5008   -526    312     67       O  
ATOM   7264  CB  ASP A 890      32.645  24.256  16.731  1.00 48.71           C  
ANISOU 7264  CB  ASP A 890     6152   6450   5906   -478    431     33       C  
ATOM   7265  CG  ASP A 890      33.406  23.018  16.259  1.00 54.00           C  
ANISOU 7265  CG  ASP A 890     6831   7185   6500   -435    494      6       C  
ATOM   7266  OD1 ASP A 890      33.293  21.957  16.923  1.00 56.31           O  
ANISOU 7266  OD1 ASP A 890     7157   7468   6771   -385    498    -60       O  
ATOM   7267  OD2 ASP A 890      34.112  23.100  15.228  1.00 55.34           O  
ANISOU 7267  OD2 ASP A 890     6976   7418   6635   -447    544     52       O  
ATOM   7268  N   TYR A 891      30.385  24.762  19.190  1.00 43.24           N  
ANISOU 7268  N   TYR A 891     5516   5610   5304   -454    296    -56       N  
ATOM   7269  CA  TYR A 891      29.848  25.768  20.092  1.00 44.00           C  
ANISOU 7269  CA  TYR A 891     5600   5642   5477   -463    240    -65       C  
ATOM   7270  C   TYR A 891      30.957  26.693  20.578  1.00 45.45           C  
ANISOU 7270  C   TYR A 891     5717   5808   5746   -490    230    -65       C  
ATOM   7271  O   TYR A 891      30.691  27.798  21.035  1.00 45.69           O  
ANISOU 7271  O   TYR A 891     5732   5777   5852   -514    190    -62       O  
ATOM   7272  CB  TYR A 891      29.051  25.141  21.252  1.00 43.99           C  
ANISOU 7272  CB  TYR A 891     5630   5621   5464   -416    208   -129       C  
ATOM   7273  CG  TYR A 891      29.809  24.124  22.071  1.00 43.49           C  
ANISOU 7273  CG  TYR A 891     5552   5591   5381   -370    224   -183       C  
ATOM   7274  CD1 TYR A 891      29.845  22.785  21.696  1.00 42.72           C  
ANISOU 7274  CD1 TYR A 891     5490   5528   5213   -340    265   -195       C  
ATOM   7275  CD2 TYR A 891      30.479  24.500  23.229  1.00 44.75           C  
ANISOU 7275  CD2 TYR A 891     5664   5746   5594   -356    197   -222       C  
ATOM   7276  CE1 TYR A 891      30.542  21.849  22.450  1.00 46.40           C  
ANISOU 7276  CE1 TYR A 891     5941   6020   5668   -289    284   -234       C  
ATOM   7277  CE2 TYR A 891      31.177  23.572  23.992  1.00 44.89           C  
ANISOU 7277  CE2 TYR A 891     5661   5805   5590   -308    211   -260       C  
ATOM   7278  CZ  TYR A 891      31.203  22.251  23.599  1.00 44.11           C  
ANISOU 7278  CZ  TYR A 891     5597   5736   5427   -272    257   -261       C  
ATOM   7279  OH  TYR A 891      31.901  21.336  24.347  1.00 40.49           O  
ANISOU 7279  OH  TYR A 891     5117   5313   4953   -217    275   -288       O  
ATOM   7280  N   GLU A 892      32.198  26.233  20.466  1.00 47.87           N  
ANISOU 7280  N   GLU A 892     5981   6167   6041   -486    266    -68       N  
ATOM   7281  CA  GLU A 892      33.366  27.062  20.752  1.00 51.54           C  
ANISOU 7281  CA  GLU A 892     6371   6630   6582   -522    260    -58       C  
ATOM   7282  C   GLU A 892      34.137  27.303  19.465  1.00 52.46           C  
ANISOU 7282  C   GLU A 892     6455   6790   6690   -561    311     20       C  
ATOM   7283  O   GLU A 892      34.369  26.372  18.699  1.00 53.68           O  
ANISOU 7283  O   GLU A 892     6625   7007   6763   -535    362     34       O  
ATOM   7284  CB  GLU A 892      34.261  26.402  21.802  1.00 52.69           C  
ANISOU 7284  CB  GLU A 892     6476   6818   6727   -484    256   -119       C  
ATOM   7285  CG  GLU A 892      33.642  26.386  23.193  1.00 56.23           C  
ANISOU 7285  CG  GLU A 892     6940   7232   7193   -451    202   -192       C  
ATOM   7286  CD  GLU A 892      34.563  25.830  24.260  1.00 58.04           C  
ANISOU 7286  CD  GLU A 892     7118   7515   7418   -413    194   -243       C  
ATOM   7287  OE1 GLU A 892      34.864  26.569  25.225  1.00 60.49           O  
ANISOU 7287  OE1 GLU A 892     7386   7811   7787   -431    146   -286       O  
ATOM   7288  OE2 GLU A 892      34.979  24.658  24.145  1.00 59.69           O  
ANISOU 7288  OE2 GLU A 892     7330   7782   7568   -364    236   -243       O  
ATOM   7289  N   LYS A 893      34.514  28.554  19.221  1.00 54.15           N  
ANISOU 7289  N   LYS A 893     6623   6966   6986   -623    299     71       N  
ATOM   7290  CA  LYS A 893      35.247  28.906  18.013  1.00 57.87           C  
ANISOU 7290  CA  LYS A 893     7053   7481   7455   -663    348    161       C  
ATOM   7291  C   LYS A 893      36.578  28.158  17.926  1.00 59.69           C  
ANISOU 7291  C   LYS A 893     7227   7800   7651   -645    395    156       C  
ATOM   7292  O   LYS A 893      37.405  28.223  18.837  1.00 59.32           O  
ANISOU 7292  O   LYS A 893     7124   7761   7655   -648    375    115       O  
ATOM   7293  CB  LYS A 893      35.474  30.418  17.930  1.00 59.49           C  
ANISOU 7293  CB  LYS A 893     7213   7616   7776   -737    325    219       C  
ATOM   7294  CG  LYS A 893      35.923  30.892  16.552  1.00 62.29           C  
ANISOU 7294  CG  LYS A 893     7534   8009   8126   -780    376    336       C  
ATOM   7295  CD  LYS A 893      36.320  32.362  16.557  1.00 65.64           C  
ANISOU 7295  CD  LYS A 893     7903   8355   8682   -858    356    397       C  
ATOM   7296  CE  LYS A 893      36.890  32.777  15.205  1.00 68.14           C  
ANISOU 7296  CE  LYS A 893     8175   8724   8992   -899    414    526       C  
ATOM   7297  NZ  LYS A 893      37.423  34.171  15.213  1.00 67.05           N  
ANISOU 7297  NZ  LYS A 893     7974   8507   8995   -982    401    595       N  
ATOM   7298  N   LYS A 894      36.757  27.427  16.831  1.00 63.15           N  
ANISOU 7298  N   LYS A 894     7681   8314   8001   -622    457    194       N  
ATOM   7299  CA  LYS A 894      38.026  26.776  16.520  1.00 66.44           C  
ANISOU 7299  CA  LYS A 894     8041   8822   8380   -599    515    206       C  
ATOM   7300  C   LYS A 894      39.050  27.824  16.081  1.00 68.56           C  
ANISOU 7300  C   LYS A 894     8217   9111   8721   -666    531    289       C  
ATOM   7301  O   LYS A 894      38.688  28.830  15.464  1.00 68.29           O  
ANISOU 7301  O   LYS A 894     8180   9037   8728   -722    523    362       O  
ATOM   7302  CB  LYS A 894      37.837  25.727  15.420  1.00 66.89           C  
ANISOU 7302  CB  LYS A 894     8149   8949   8316   -552    579    215       C  
ATOM   7303  CG  LYS A 894      36.969  26.195  14.254  1.00 69.31           C  
ANISOU 7303  CG  LYS A 894     8499   9254   8582   -584    587    280       C  
ATOM   7304  CD  LYS A 894      37.360  25.522  12.950  1.00 73.87           C  
ANISOU 7304  CD  LYS A 894     9083   9933   9051   -559    663    315       C  
ATOM   7305  CE  LYS A 894      36.615  26.137  11.771  1.00 75.92           C  
ANISOU 7305  CE  LYS A 894     9367  10210   9268   -597    669    395       C  
ATOM   7306  NZ  LYS A 894      37.261  25.808  10.467  1.00 77.93           N  
ANISOU 7306  NZ  LYS A 894     9602  10580   9429   -584    746    450       N  
ATOM   7307  N   ALA A 895      40.319  27.587  16.409  1.00 70.60           N  
ANISOU 7307  N   ALA A 895     8396   9431   8998   -660    553    286       N  
ATOM   7308  CA  ALA A 895      41.404  28.498  16.046  1.00 73.72           C  
ANISOU 7308  CA  ALA A 895     8690   9855   9464   -728    571    366       C  
ATOM   7309  C   ALA A 895      41.656  28.507  14.535  1.00 75.62           C  
ANISOU 7309  C   ALA A 895     8918  10170   9643   -735    645    467       C  
ATOM   7310  O   ALA A 895      41.658  27.451  13.891  1.00 75.92           O  
ANISOU 7310  O   ALA A 895     8993  10285   9570   -668    702    457       O  
ATOM   7311  CB  ALA A 895      42.679  28.137  16.801  1.00 73.76           C  
ANISOU 7311  CB  ALA A 895     8606   9926   9495   -713    575    336       C  
ATOM   7312  N   SER A 896      41.859  29.701  13.979  1.00 77.17           N  
ANISOU 7312  N   SER A 896     9066  10342   9913   -814    646    564       N  
ATOM   7313  CA  SER A 896      42.143  29.855  12.547  1.00 79.68           C  
ANISOU 7313  CA  SER A 896     9360  10740  10176   -826    716    677       C  
ATOM   7314  C   SER A 896      43.440  30.629  12.288  1.00 81.77           C  
ANISOU 7314  C   SER A 896     9501  11050  10519   -893    745    772       C  
ATOM   7315  O   SER A 896      43.987  31.271  13.192  1.00 80.72           O  
ANISOU 7315  O   SER A 896     9304  10863  10501   -948    698    754       O  
ATOM   7316  CB  SER A 896      40.967  30.529  11.823  1.00 79.46           C  
ANISOU 7316  CB  SER A 896     9395  10654  10141   -854    702    737       C  
ATOM   7317  OG  SER A 896      41.002  31.941  11.967  1.00 77.73           O  
ANISOU 7317  OG  SER A 896     9132  10345  10058   -940    666    808       O  
ATOM   7318  N   LEU A 897      43.910  30.573  11.043  1.00 84.25           N  
ANISOU 7318  N   LEU A 897     9778  11466  10767   -889    821    873       N  
ATOM   7319  CA  LEU A 897      45.123  31.273  10.617  1.00 86.99           C  
ANISOU 7319  CA  LEU A 897    10003  11873  11178   -952    861    985       C  
ATOM   7320  C   LEU A 897      45.011  32.792  10.775  1.00 88.86           C  
ANISOU 7320  C   LEU A 897    10200  11995  11568  -1062    814   1061       C  
ATOM   7321  O   LEU A 897      46.021  33.492  10.839  1.00 89.28           O  
ANISOU 7321  O   LEU A 897    10146  12060  11718  -1134    821   1129       O  
ATOM   7322  CB  LEU A 897      45.479  30.911   9.167  1.00 88.13           C  
ANISOU 7322  CB  LEU A 897    10125  12155  11205   -918    957   1083       C  
ATOM   7323  CG  LEU A 897      46.031  29.520   8.796  1.00 88.18           C  
ANISOU 7323  CG  LEU A 897    10136  12297  11071   -816   1029   1035       C  
ATOM   7324  CD1 LEU A 897      47.328  29.197   9.539  1.00 87.21           C  
ANISOU 7324  CD1 LEU A 897     9912  12228  10994   -805   1041   1009       C  
ATOM   7325  CD2 LEU A 897      44.998  28.399   8.985  1.00 88.50           C  
ANISOU 7325  CD2 LEU A 897    10306  12312  11007   -730   1014    910       C  
ATOM   7326  N   PHE A 898      43.778  33.287  10.852  1.00 90.96           N  
ANISOU 7326  N   PHE A 898    10552  12148  11860  -1074    766   1048       N  
ATOM   7327  CA  PHE A 898      43.513  34.709  11.079  1.00 94.93           C  
ANISOU 7327  CA  PHE A 898    11036  12516  12515  -1167    718   1106       C  
ATOM   7328  C   PHE A 898      43.968  35.231  12.444  1.00 97.47           C  
ANISOU 7328  C   PHE A 898    11317  12741  12975  -1224    647   1022       C  
ATOM   7329  O   PHE A 898      44.140  36.440  12.620  1.00 98.06           O  
ANISOU 7329  O   PHE A 898    11350  12715  13195  -1316    617   1074       O  
ATOM   7330  CB  PHE A 898      42.034  35.023  10.843  1.00 94.89           C  
ANISOU 7330  CB  PHE A 898    11136  12422  12495  -1149    688   1110       C  
ATOM   7331  CG  PHE A 898      41.755  35.597   9.489  1.00 95.77           C  
ANISOU 7331  CG  PHE A 898    11241  12569  12580  -1169    738   1266       C  
ATOM   7332  CD1 PHE A 898      41.431  36.943   9.347  1.00 96.96           C  
ANISOU 7332  CD1 PHE A 898    11378  12602  12862  -1241    716   1364       C  
ATOM   7333  CD2 PHE A 898      41.839  34.804   8.351  1.00 96.24           C  
ANISOU 7333  CD2 PHE A 898    11306  12779  12483  -1113    809   1318       C  
ATOM   7334  CE1 PHE A 898      41.181  37.489   8.094  1.00 97.84           C  
ANISOU 7334  CE1 PHE A 898    11476  12750  12947  -1256    764   1524       C  
ATOM   7335  CE2 PHE A 898      41.596  35.341   7.094  1.00 98.13           C  
ANISOU 7335  CE2 PHE A 898    11532  13067  12685  -1129    855   1467       C  
ATOM   7336  CZ  PHE A 898      41.264  36.687   6.967  1.00 98.19           C  
ANISOU 7336  CZ  PHE A 898    11521  12961  12824  -1200    833   1577       C  
ATOM   7337  N   ASP A 899      44.151  34.322  13.400  1.00 99.84           N  
ANISOU 7337  N   ASP A 899    11630  13073  13232  -1170    620    892       N  
ATOM   7338  CA  ASP A 899      44.771  34.653  14.679  1.00103.60           C  
ANISOU 7338  CA  ASP A 899    12050  13500  13812  -1216    558    809       C  
ATOM   7339  C   ASP A 899      46.293  34.673  14.494  1.00108.46           C  
ANISOU 7339  C   ASP A 899    12532  14222  14456  -1260    597    870       C  
ATOM   7340  O   ASP A 899      46.888  33.638  14.186  1.00109.53           O  
ANISOU 7340  O   ASP A 899    12640  14493  14485  -1191    652    871       O  
ATOM   7341  CB  ASP A 899      44.395  33.625  15.756  1.00101.28           C  
ANISOU 7341  CB  ASP A 899    11814  13217  13450  -1133    518    660       C  
ATOM   7342  CG  ASP A 899      42.909  33.295  15.775  1.00 99.00           C  
ANISOU 7342  CG  ASP A 899    11655  12862  13099  -1072    497    609       C  
ATOM   7343  OD1 ASP A 899      42.079  34.228  15.833  1.00 97.56           O  
ANISOU 7343  OD1 ASP A 899    11516  12560  12992  -1113    458    622       O  
ATOM   7344  OD2 ASP A 899      42.573  32.092  15.746  1.00 97.20           O  
ANISOU 7344  OD2 ASP A 899    11481  12700  12750   -983    520    556       O  
ATOM   7345  N   MET A 900      46.934  35.831  14.649  1.00113.37           N  
ANISOU 7345  N   MET A 900    13070  14785  15223  -1372    572    924       N  
ATOM   7346  CA  MET A 900      46.278  37.110  14.902  1.00117.52           C  
ANISOU 7346  CA  MET A 900    13628  15139  15885  -1454    517    933       C  
ATOM   7347  C   MET A 900      46.927  38.175  14.016  1.00121.51           C  
ANISOU 7347  C   MET A 900    14047  15628  16494  -1556    556   1092       C  
ATOM   7348  O   MET A 900      48.101  38.058  13.648  1.00121.73           O  
ANISOU 7348  O   MET A 900    13963  15768  16521  -1588    601   1163       O  
ATOM   7349  CB  MET A 900      46.383  37.490  16.388  1.00117.83           C  
ANISOU 7349  CB  MET A 900    13658  15088  16023  -1497    425    796       C  
ATOM   7350  CG  MET A 900      45.536  38.699  16.809  1.00118.59           C  
ANISOU 7350  CG  MET A 900    13814  14993  16253  -1559    363    770       C  
ATOM   7351  SD  MET A 900      45.552  39.079  18.579  1.00119.04           S  
ANISOU 7351  SD  MET A 900    13874  14954  16402  -1596    254    586       S  
ATOM   7352  CE  MET A 900      47.295  39.381  18.883  1.00119.73           C  
ANISOU 7352  CE  MET A 900    13797  15122  16574  -1703    245    604       C  
ATOM   7353  N   PHE A 901      46.153  39.201  13.669  1.00125.28           N  
ANISOU 7353  N   PHE A 901    14572  15968  17061  -1603    543   1155       N  
ATOM   7354  CA  PHE A 901      46.651  40.321  12.867  1.00130.25           C  
ANISOU 7354  CA  PHE A 901    15126  16556  17808  -1705    577   1316       C  
ATOM   7355  C   PHE A 901      46.553  41.671  13.589  1.00134.37           C  
ANISOU 7355  C   PHE A 901    15642  16880  18532  -1815    508   1292       C  
ATOM   7356  O   PHE A 901      47.105  42.671  13.121  1.00135.86           O  
ANISOU 7356  O   PHE A 901    15757  17014  18851  -1918    527   1415       O  
ATOM   7357  CB  PHE A 901      45.944  40.366  11.507  1.00129.55           C  
ANISOU 7357  CB  PHE A 901    15084  16498  17642  -1662    644   1458       C  
ATOM   7358  CG  PHE A 901      46.507  39.400  10.500  1.00127.97           C  
ANISOU 7358  CG  PHE A 901    14841  16500  17282  -1599    731   1534       C  
ATOM   7359  CD1 PHE A 901      47.468  39.816   9.583  1.00128.29           C  
ANISOU 7359  CD1 PHE A 901    14770  16623  17349  -1657    798   1695       C  
ATOM   7360  CD2 PHE A 901      46.084  38.074  10.473  1.00125.64           C  
ANISOU 7360  CD2 PHE A 901    14615  16309  16812  -1481    747   1443       C  
ATOM   7361  CE1 PHE A 901      47.996  38.929   8.652  1.00127.18           C  
ANISOU 7361  CE1 PHE A 901    14591  16676  17055  -1591    883   1760       C  
ATOM   7362  CE2 PHE A 901      46.608  37.181   9.546  1.00124.66           C  
ANISOU 7362  CE2 PHE A 901    14457  16365  16542  -1419    830   1501       C  
ATOM   7363  CZ  PHE A 901      47.565  37.610   8.635  1.00125.69           C  
ANISOU 7363  CZ  PHE A 901    14478  16585  16692  -1470    899   1657       C  
ATOM   7364  N   ASP A 902      45.853  41.688  14.725  1.00110.94           N  
ATOM   7365  CA  ASP A 902      45.803  42.864  15.602  1.00114.94           C  
ATOM   7366  C   ASP A 902      47.152  43.115  16.282  1.00117.15           C  
ATOM   7367  O   ASP A 902      47.485  44.260  16.603  1.00117.52           O  
ATOM   7368  CB  ASP A 902      44.693  42.724  16.658  1.00115.23           C  
ATOM   7369  CG  ASP A 902      43.385  43.410  16.249  1.00115.85           C  
ATOM   7370  OD1 ASP A 902      43.346  44.101  15.205  1.00115.99           O  
ATOM   7371  OD2 ASP A 902      42.388  43.264  16.989  1.00115.61           O  
ATOM   7372  N   PHE A 903      47.911  42.036  16.492  1.00119.78           N  
ATOM   7373  CA  PHE A 903      49.266  42.068  17.073  1.00121.79           C  
ATOM   7374  C   PHE A 903      49.333  42.815  18.408  1.00122.08           C  
ATOM   7375  O   PHE A 903      48.663  42.443  19.374  1.00122.38           O  
ATOM   7376  CB  PHE A 903      50.285  42.639  16.070  1.00122.79           C  
ATOM   7377  CG  PHE A 903      51.712  42.228  16.343  1.00124.52           C  
ATOM   7378  CD1 PHE A 903      52.574  43.073  17.043  1.00125.10           C  
ATOM   7379  CD2 PHE A 903      52.197  41.000  15.891  1.00124.90           C  
ATOM   7380  CE1 PHE A 903      53.896  42.698  17.295  1.00124.99           C  
ATOM   7381  CE2 PHE A 903      53.516  40.616  16.138  1.00124.92           C  
ATOM   7382  CZ  PHE A 903      54.367  41.468  16.840  1.00125.17           C  
TER    7383      PHE A 903                                                      
ATOM   7384  P    DC T   3      -5.549  -0.446  38.582  1.00 87.25           P  
ANISOU 7384  P    DC T   3    10075  12204  10872    727    -74    174       P  
ATOM   7385  OP1  DC T   3      -6.728  -0.785  39.420  1.00 86.50           O  
ANISOU 7385  OP1  DC T   3     9953  12151  10761    747    -74    194       O  
ATOM   7386  OP2  DC T   3      -4.569  -1.498  38.214  1.00 84.72           O  
ANISOU 7386  OP2  DC T   3     9751  11855  10585    711    -48    198       O  
ATOM   7387  O5'  DC T   3      -6.031   0.306  37.238  1.00 82.85           O  
ANISOU 7387  O5'  DC T   3     9557  11599  10321    701    -88    139       O  
ATOM   7388  C5'  DC T   3      -7.066  -0.224  36.382  1.00 74.42           C  
ANISOU 7388  C5'  DC T   3     8504  10504   9269    682    -80    148       C  
ATOM   7389  C4'  DC T   3      -6.560  -0.379  34.947  1.00 66.30           C  
ANISOU 7389  C4'  DC T   3     7507   9418   8265    643    -70    136       C  
ATOM   7390  O4'  DC T   3      -5.583  -1.440  34.814  1.00 68.78           O  
ANISOU 7390  O4'  DC T   3     7812   9716   8607    632    -41    156       O  
ATOM   7391  C3'  DC T   3      -7.567  -0.722  33.859  1.00 57.11           C  
ANISOU 7391  C3'  DC T   3     6364   8221   7115    617    -65    136       C  
ATOM   7392  O3'  DC T   3      -7.045  -0.237  32.620  1.00 41.42           O  
ANISOU 7392  O3'  DC T   3     4410   6190   5136    582    -71    111       O  
ATOM   7393  C2'  DC T   3      -7.612  -2.251  33.904  1.00 59.53           C  
ANISOU 7393  C2'  DC T   3     6649   8521   7447    613    -30    172       C  
ATOM   7394  C1'  DC T   3      -6.214  -2.636  34.393  1.00 65.54           C  
ANISOU 7394  C1'  DC T   3     7395   9287   8220    619    -16    182       C  
ATOM   7395  N1   DC T   3      -6.122  -3.539  35.595  1.00 69.15           N  
ANISOU 7395  N1   DC T   3     7813   9781   8682    646     -1    221       N  
ATOM   7396  C2   DC T   3      -4.845  -3.898  36.091  1.00 69.01           C  
ANISOU 7396  C2   DC T   3     7777   9767   8676    652     10    233       C  
ATOM   7397  O2   DC T   3      -3.807  -3.490  35.532  1.00 65.06           O  
ANISOU 7397  O2   DC T   3     7294   9241   8183    637      9    210       O  
ATOM   7398  N3   DC T   3      -4.781  -4.703  37.187  1.00 70.04           N  
ANISOU 7398  N3   DC T   3     7870   9932   8811    675     20    272       N  
ATOM   7399  C4   DC T   3      -5.903  -5.137  37.779  1.00 70.24           C  
ANISOU 7399  C4   DC T   3     7875   9986   8826    690     22    297       C  
ATOM   7400  N4   DC T   3      -5.785  -5.927  38.852  1.00 68.34           N  
ANISOU 7400  N4   DC T   3     7597   9781   8589    709     31    338       N  
ATOM   7401  C5   DC T   3      -7.200  -4.776  37.296  1.00 70.94           C  
ANISOU 7401  C5   DC T   3     7981  10071   8901    685     12    283       C  
ATOM   7402  C6   DC T   3      -7.261  -3.984  36.215  1.00 69.97           C  
ANISOU 7402  C6   DC T   3     7895   9913   8777    663      0    245       C  
HETATM 7403  P   2PR T   4      -7.462   1.182  32.010  1.00 33.13           P  
ANISOU 7403  P   2PR T   4     3389   5128   4070    571   -107     78       P  
HETATM 7404  OP1 2PR T   4      -9.223   0.940  32.360  1.00 39.73           O  
ANISOU 7404  OP1 2PR T   4     4212   5983   4899    587   -113     93       O  
HETATM 7405  OP2 2PR T   4      -6.357   2.186  33.053  1.00 41.06           O  
ANISOU 7405  OP2 2PR T   4     4382   6163   5056    600   -127     60       O  
HETATM 7406  O5' 2PR T   4      -6.803   0.778  30.487  1.00 37.10           O  
ANISOU 7406  O5' 2PR T   4     3921   5580   4594    521    -90     70       O  
HETATM 7407  C5' 2PR T   4      -5.388   0.785  30.322  1.00 31.83           C  
ANISOU 7407  C5' 2PR T   4     3258   4901   3934    510    -80     60       C  
HETATM 7408  C4' 2PR T   4      -5.200   0.364  28.879  1.00 31.01           C  
ANISOU 7408  C4' 2PR T   4     3179   4755   3847    462    -65     52       C  
HETATM 7409  O4' 2PR T   4      -5.832   1.321  28.034  1.00 30.93           O  
ANISOU 7409  O4' 2PR T   4     3198   4729   3824    439    -93     34       O  
HETATM 7410  C3' 2PR T   4      -3.753   0.314  28.457  1.00 30.66           C  
ANISOU 7410  C3' 2PR T   4     3142   4692   3813    441    -51     39       C  
HETATM 7411  O3' 2PR T   4      -3.234  -0.985  28.706  1.00 30.85           O  
ANISOU 7411  O3' 2PR T   4     3144   4714   3865    444    -15     58       O  
HETATM 7412  C2' 2PR T   4      -3.847   0.600  26.977  1.00 32.79           C  
ANISOU 7412  C2' 2PR T   4     3445   4928   4084    392    -55     20       C  
HETATM 7413  C1' 2PR T   4      -4.999   1.583  26.902  1.00 33.83           C  
ANISOU 7413  C1' 2PR T   4     3591   5066   4195    396    -91     15       C  
HETATM 7414  N9  2PR T   4      -4.410   2.945  27.009  1.00 33.89           N  
ANISOU 7414  N9  2PR T   4     3612   5077   4186    400   -125     -7       N  
HETATM 7415  C8  2PR T   4      -4.528   3.801  28.043  1.00 30.14           C  
ANISOU 7415  C8  2PR T   4     3125   4629   3698    439   -151    -11       C  
HETATM 7416  N7  2PR T   4      -3.820   4.917  27.750  1.00 35.07           N  
ANISOU 7416  N7  2PR T   4     3767   5244   4314    428   -176    -33       N  
HETATM 7417  C5  2PR T   4      -3.266   4.749  26.521  1.00 35.34           C  
ANISOU 7417  C5  2PR T   4     3824   5248   4355    381   -166    -41       C  
HETATM 7418  C6  2PR T   4      -2.458   5.542  25.707  1.00 34.81           C  
ANISOU 7418  C6  2PR T   4     3782   5161   4284    348   -181    -60       C  
HETATM 7419  N1  2PR T   4      -2.058   5.081  24.511  1.00 33.44           N  
ANISOU 7419  N1  2PR T   4     3627   4963   4117    300   -163    -65       N  
HETATM 7420  C2  2PR T   4      -2.434   3.846  24.085  1.00 30.87           C  
ANISOU 7420  C2  2PR T   4     3296   4629   3804    284   -129    -53       C  
HETATM 7421  N2  2PR T   4      -2.020   3.403  22.874  1.00 26.34           N  
ANISOU 7421  N2  2PR T   4     2739   4033   3236    233   -109    -62       N  
HETATM 7422  N3  2PR T   4      -3.217   3.054  24.859  1.00 24.76           N  
ANISOU 7422  N3  2PR T   4     2499   3871   3038    316   -114    -33       N  
HETATM 7423  C4  2PR T   4      -3.639   3.495  26.067  1.00 30.89           C  
ANISOU 7423  C4  2PR T   4     3257   4674   3805    364   -132    -26       C  
ATOM   7424  P    DT T   5      -1.677  -1.179  28.950  1.00 32.74           P  
ANISOU 7424  P    DT T   5     3373   4949   4118    445      1     53       P  
ATOM   7425  OP1  DT T   5      -1.542  -2.492  29.612  1.00 36.18           O  
ANISOU 7425  OP1  DT T   5     3774   5391   4580    463     31     82       O  
ATOM   7426  OP2  DT T   5      -1.108   0.031  29.585  1.00 36.61           O  
ANISOU 7426  OP2  DT T   5     3867   5459   4583    466    -29     38       O  
ATOM   7427  O5'  DT T   5      -1.046  -1.236  27.483  1.00 31.00           O  
ANISOU 7427  O5'  DT T   5     3179   4689   3910    394     14     28       O  
ATOM   7428  C5'  DT T   5      -1.545  -2.126  26.485  1.00 32.43           C  
ANISOU 7428  C5'  DT T   5     3367   4845   4111    359     38     28       C  
ATOM   7429  C4'  DT T   5      -0.892  -1.789  25.160  1.00 32.72           C  
ANISOU 7429  C4'  DT T   5     3431   4853   4147    309     42     -2       C  
ATOM   7430  O4'  DT T   5      -1.274  -0.435  24.820  1.00 34.85           O  
ANISOU 7430  O4'  DT T   5     3730   5128   4385    300      3    -16       O  
ATOM   7431  C3'  DT T   5       0.633  -1.745  25.182  1.00 33.87           C  
ANISOU 7431  C3'  DT T   5     3573   4991   4305    303     54    -17       C  
ATOM   7432  O3'  DT T   5       1.211  -3.047  25.027  1.00 34.14           O  
ANISOU 7432  O3'  DT T   5     3586   5008   4378    293     94    -13       O  
ATOM   7433  C2'  DT T   5       0.924  -0.832  24.000  1.00 32.72           C  
ANISOU 7433  C2'  DT T   5     3463   4830   4140    259     38    -47       C  
ATOM   7434  C1'  DT T   5      -0.226   0.169  24.084  1.00 32.70           C  
ANISOU 7434  C1'  DT T   5     3477   4840   4107    268     -1    -42       C  
ATOM   7435  N1   DT T   5       0.161   1.477  24.714  1.00 34.42           N  
ANISOU 7435  N1   DT T   5     3701   5074   4302    292    -37    -50       N  
ATOM   7436  C2   DT T   5       0.903   2.342  23.941  1.00 33.28           C  
ANISOU 7436  C2   DT T   5     3582   4917   4146    260    -52    -73       C  
ATOM   7437  O2   DT T   5       1.246   2.090  22.803  1.00 35.69           O  
ANISOU 7437  O2   DT T   5     3903   5201   4456    213    -37    -87       O  
ATOM   7438  N3   DT T   5       1.229   3.525  24.544  1.00 34.67           N  
ANISOU 7438  N3   DT T   5     3762   5106   4305    283    -86    -80       N  
ATOM   7439  C4   DT T   5       0.897   3.920  25.828  1.00 36.28           C  
ANISOU 7439  C4   DT T   5     3948   5337   4501    334   -104    -69       C  
ATOM   7440  O4   DT T   5       1.253   5.010  26.262  1.00 35.97           O  
ANISOU 7440  O4   DT T   5     3912   5307   4448    350   -134    -81       O  
ATOM   7441  C5   DT T   5       0.121   2.967  26.606  1.00 35.40           C  
ANISOU 7441  C5   DT T   5     3810   5242   4398    365    -86    -45       C  
ATOM   7442  C7   DT T   5      -0.272   3.301  28.021  1.00 26.82           C  
ANISOU 7442  C7   DT T   5     2700   4190   3301    417   -103    -34       C  
ATOM   7443  C6   DT T   5      -0.208   1.799  26.020  1.00 31.99           C  
ANISOU 7443  C6   DT T   5     3375   4795   3985    343    -55    -35       C  
ATOM   7444  P    DC T   6       2.743  -3.281  25.421  1.00 33.78           P  
ANISOU 7444  P    DC T   6     3523   4958   4354    301    110    -20       P  
ATOM   7445  OP1  DC T   6       2.980  -4.738  25.521  1.00 37.86           O  
ANISOU 7445  OP1  DC T   6     4009   5459   4917    301    149     -6       O  
ATOM   7446  OP2  DC T   6       3.071  -2.420  26.575  1.00 37.68           O  
ANISOU 7446  OP2  DC T   6     4010   5480   4825    342     82    -10       O  
ATOM   7447  O5'  DC T   6       3.551  -2.709  24.159  1.00 36.51           O  
ANISOU 7447  O5'  DC T   6     3898   5282   4692    251    112    -58       O  
ATOM   7448  C5'  DC T   6       3.364  -3.202  22.829  1.00 30.98           C  
ANISOU 7448  C5'  DC T   6     3211   4557   4002    200    133    -77       C  
ATOM   7449  C4'  DC T   6       4.241  -2.425  21.859  1.00 31.56           C  
ANISOU 7449  C4'  DC T   6     3311   4620   4060    157    127   -111       C  
ATOM   7450  O4'  DC T   6       4.005  -0.997  21.992  1.00 32.46           O  
ANISOU 7450  O4'  DC T   6     3450   4750   4134    165     84   -112       O  
ATOM   7451  C3'  DC T   6       5.745  -2.597  22.052  1.00 33.63           C  
ANISOU 7451  C3'  DC T   6     3559   4874   4344    158    145   -126       C  
ATOM   7452  O3'  DC T   6       6.353  -2.480  20.778  1.00 32.25           O  
ANISOU 7452  O3'  DC T   6     3404   4683   4168    102    159   -159       O  
ATOM   7453  C2'  DC T   6       6.092  -1.433  22.985  1.00 29.94           C  
ANISOU 7453  C2'  DC T   6     3098   4428   3850    194    109   -118       C  
ATOM   7454  C1'  DC T   6       5.197  -0.344  22.406  1.00 30.13           C  
ANISOU 7454  C1'  DC T   6     3155   4459   3834    176     74   -123       C  
ATOM   7455  N1   DC T   6       4.916   0.767  23.370  1.00 32.02           N  
ANISOU 7455  N1   DC T   6     3398   4721   4046    217     34   -111       N  
ATOM   7456  C2   DC T   6       5.246   2.092  23.022  1.00 34.03           C  
ANISOU 7456  C2   DC T   6     3678   4977   4273    202      1   -128       C  
ATOM   7457  O2   DC T   6       5.752   2.335  21.915  1.00 38.55           O  
ANISOU 7457  O2   DC T   6     4271   5534   4841    154      5   -150       O  
ATOM   7458  N3   DC T   6       4.992   3.088  23.916  1.00 31.33           N  
ANISOU 7458  N3   DC T   6     3336   4655   3911    240    -35   -121       N  
ATOM   7459  C4   DC T   6       4.437   2.812  25.110  1.00 32.31           C  
ANISOU 7459  C4   DC T   6     3437   4801   4038    289    -38    -99       C  
ATOM   7460  N4   DC T   6       4.205   3.831  25.957  1.00 29.56           N  
ANISOU 7460  N4   DC T   6     3088   4474   3670    323    -73    -97       N  
ATOM   7461  C5   DC T   6       4.093   1.472  25.482  1.00 25.88           C  
ANISOU 7461  C5   DC T   6     2597   3988   3248    303     -6    -78       C  
ATOM   7462  C6   DC T   6       4.342   0.501  24.589  1.00 29.46           C  
ANISOU 7462  C6   DC T   6     3051   4418   3725    267     28    -85       C  
ATOM   7463  P    DG T   7       7.905  -2.735  20.471  1.00 32.77           P  
ANISOU 7463  P    DG T   7     3460   4733   4257     82    184   -187       P  
ATOM   7464  OP1  DG T   7       7.970  -3.436  19.163  1.00 37.00           O  
ANISOU 7464  OP1  DG T   7     4000   5250   4808     25    217   -215       O  
ATOM   7465  OP2  DG T   7       8.539  -3.345  21.657  1.00 38.66           O  
ANISOU 7465  OP2  DG T   7     4171   5481   5037    128    197   -168       O  
ATOM   7466  O5'  DG T   7       8.480  -1.267  20.279  1.00 33.44           O  
ANISOU 7466  O5'  DG T   7     3575   4829   4304     71    150   -201       O  
ATOM   7467  C5'  DG T   7       8.054  -0.455  19.193  1.00 33.36           C  
ANISOU 7467  C5'  DG T   7     3598   4819   4258     26    130   -217       C  
ATOM   7468  C4'  DG T   7       9.045   0.668  18.966  1.00 32.64           C  
ANISOU 7468  C4'  DG T   7     3526   4731   4145     10    109   -235       C  
ATOM   7469  O4'  DG T   7       8.809   1.754  19.904  1.00 33.47           O  
ANISOU 7469  O4'  DG T   7     3637   4852   4226     53     67   -217       O  
ATOM   7470  C3'  DG T   7      10.507   0.286  19.149  1.00 34.34           C  
ANISOU 7470  C3'  DG T   7     3723   4937   4387     11    135   -253       C  
ATOM   7471  O3'  DG T   7      11.247   1.056  18.207  1.00 35.44           O  
ANISOU 7471  O3'  DG T   7     3887   5074   4506    -36    128   -281       O  
ATOM   7472  C2'  DG T   7      10.783   0.641  20.619  1.00 32.94           C  
ANISOU 7472  C2'  DG T   7     3530   4773   4213     74    115   -230       C  
ATOM   7473  C1'  DG T   7       9.874   1.852  20.843  1.00 34.45           C  
ANISOU 7473  C1'  DG T   7     3744   4981   4364     88     68   -216       C  
ATOM   7474  N9   DG T   7       9.292   2.008  22.186  1.00 34.94           N  
ANISOU 7474  N9   DG T   7     3791   5062   4424    148     48   -188       N  
ATOM   7475  C8   DG T   7       8.685   1.056  22.982  1.00 36.59           C  
ANISOU 7475  C8   DG T   7     3973   5277   4652    183     64   -163       C  
ATOM   7476  N7   DG T   7       8.253   1.521  24.129  1.00 32.92           N  
ANISOU 7476  N7   DG T   7     3499   4835   4175    231     39   -142       N  
ATOM   7477  C5   DG T   7       8.582   2.871  24.087  1.00 31.09           C  
ANISOU 7477  C5   DG T   7     3289   4610   3915    229      4   -156       C  
ATOM   7478  C6   DG T   7       8.384   3.911  25.027  1.00 29.26           C  
ANISOU 7478  C6   DG T   7     3058   4400   3661    268    -33   -149       C  
ATOM   7479  O6   DG T   7       7.846   3.852  26.127  1.00 29.97           O  
ANISOU 7479  O6   DG T   7     3129   4512   3747    312    -42   -129       O  
ATOM   7480  N1   DG T   7       8.882   5.138  24.597  1.00 30.53           N  
ANISOU 7480  N1   DG T   7     3242   4557   3801    249    -62   -169       N  
ATOM   7481  C2   DG T   7       9.503   5.339  23.393  1.00 28.30           C  
ANISOU 7481  C2   DG T   7     2981   4255   3517    198    -55   -190       C  
ATOM   7482  N2   DG T   7       9.926   6.585  23.101  1.00 33.32           N  
ANISOU 7482  N2   DG T   7     3638   4889   4133    184    -87   -205       N  
ATOM   7483  N3   DG T   7       9.696   4.375  22.516  1.00 34.09           N  
ANISOU 7483  N3   DG T   7     3715   4971   4268    160    -20   -198       N  
ATOM   7484  C4   DG T   7       9.219   3.176  22.911  1.00 30.99           C  
ANISOU 7484  C4   DG T   7     3298   4579   3898    179      9   -182       C  
ATOM   7485  P    DC T   8      12.840   1.005  18.071  1.00 36.41           P  
ANISOU 7485  P    DC T   8     4001   5188   4646    -51    149   -308       P  
ATOM   7486  OP1  DC T   8      13.133   1.567  16.739  1.00 32.89           O  
ANISOU 7486  OP1  DC T   8     3582   4741   4175   -115    146   -335       O  
ATOM   7487  OP2  DC T   8      13.365  -0.333  18.442  1.00 35.50           O  
ANISOU 7487  OP2  DC T   8     3849   5058   4580    -36    192   -311       O  
ATOM   7488  O5'  DC T   8      13.312   2.023  19.210  1.00 35.79           O  
ANISOU 7488  O5'  DC T   8     3923   5122   4554     -2    113   -292       O  
ATOM   7489  C5'  DC T   8      13.202   3.433  19.026  1.00 33.78           C  
ANISOU 7489  C5'  DC T   8     3697   4878   4260    -10     70   -293       C  
ATOM   7490  C4'  DC T   8      13.827   4.125  20.212  1.00 33.95           C  
ANISOU 7490  C4'  DC T   8     3710   4910   4280     39     47   -283       C  
ATOM   7491  O4'  DC T   8      12.965   3.947  21.366  1.00 36.61           O  
ANISOU 7491  O4'  DC T   8     4030   5259   4619     95     34   -254       O  
ATOM   7492  C3'  DC T   8      15.185   3.551  20.605  1.00 36.98           C  
ANISOU 7492  C3'  DC T   8     4070   5286   4695     50     76   -295       C  
ATOM   7493  O3'  DC T   8      16.091   4.624  20.752  1.00 38.83           O  
ANISOU 7493  O3'  DC T   8     4316   5525   4913     51     52   -306       O  
ATOM   7494  C2'  DC T   8      14.925   2.831  21.926  1.00 32.44           C  
ANISOU 7494  C2'  DC T   8     3464   4719   4144    109     83   -268       C  
ATOM   7495  C1'  DC T   8      13.806   3.710  22.476  1.00 35.73           C  
ANISOU 7495  C1'  DC T   8     3894   5154   4528    138     42   -247       C  
ATOM   7496  N1   DC T   8      12.985   3.206  23.655  1.00 34.40           N  
ANISOU 7496  N1   DC T   8     3702   5002   4368    190     39   -216       N  
ATOM   7497  C2   DC T   8      12.519   4.159  24.588  1.00 34.56           C  
ANISOU 7497  C2   DC T   8     3724   5044   4362    231      1   -202       C  
ATOM   7498  O2   DC T   8      12.788   5.353  24.441  1.00 31.67           O  
ANISOU 7498  O2   DC T   8     3379   4682   3973    224    -30   -214       O  
ATOM   7499  N3   DC T   8      11.771   3.751  25.640  1.00 35.58           N  
ANISOU 7499  N3   DC T   8     3833   5192   4495    275     -2   -175       N  
ATOM   7500  C4   DC T   8      11.491   2.453  25.798  1.00 37.00           C  
ANISOU 7500  C4   DC T   8     3989   5366   4702    281     30   -159       C  
ATOM   7501  N4   DC T   8      10.756   2.130  26.863  1.00 33.36           N  
ANISOU 7501  N4   DC T   8     3507   4926   4241    324     24   -131       N  
ATOM   7502  C5   DC T   8      11.942   1.456  24.865  1.00 35.15           C  
ANISOU 7502  C5   DC T   8     3751   5106   4499    243     69   -172       C  
ATOM   7503  C6   DC T   8      12.681   1.882  23.819  1.00 32.86           C  
ANISOU 7503  C6   DC T   8     3482   4800   4204    198     72   -202       C  
ATOM   7504  P    DC T   9      17.629   4.531  20.335  1.00 37.34           P  
ANISOU 7504  P    DC T   9     4123   5325   4740     25     75   -335       P  
ATOM   7505  OP1  DC T   9      17.719   4.602  18.866  1.00 39.56           O  
ANISOU 7505  OP1  DC T   9     4425   5597   5008    -43     86   -361       O  
ATOM   7506  OP2  DC T   9      18.313   3.429  21.039  1.00 36.47           O  
ANISOU 7506  OP2  DC T   9     3977   5207   4672     53    109   -332       O  
ATOM   7507  O5'  DC T   9      18.131   5.915  20.966  1.00 32.07           O  
ANISOU 7507  O5'  DC T   9     3468   4670   4048     50     33   -332       O  
ATOM   7508  C5'  DC T   9      17.359   7.101  20.777  1.00 34.25           C  
ANISOU 7508  C5'  DC T   9     3771   4955   4289     45    -11   -325       C  
ATOM   7509  C4'  DC T   9      17.162   7.902  22.056  1.00 32.24           C  
ANISOU 7509  C4'  DC T   9     3510   4716   4024    102    -47   -308       C  
ATOM   7510  O4'  DC T   9      16.086   7.351  22.843  1.00 33.13           O  
ANISOU 7510  O4'  DC T   9     3607   4840   4142    142    -46   -283       O  
ATOM   7511  C3'  DC T   9      18.348   7.905  23.000  1.00 35.27           C  
ANISOU 7511  C3'  DC T   9     3873   5105   4423    137    -41   -311       C  
ATOM   7512  O3'  DC T   9      19.236   8.912  22.568  1.00 36.80           O  
ANISOU 7512  O3'  DC T   9     4085   5295   4604    113    -60   -330       O  
ATOM   7513  C2'  DC T   9      17.703   8.232  24.342  1.00 37.20           C  
ANISOU 7513  C2'  DC T   9     4104   5371   4661    196    -67   -288       C  
ATOM   7514  C1'  DC T   9      16.304   7.653  24.212  1.00 33.98           C  
ANISOU 7514  C1'  DC T   9     3695   4965   4251    198    -62   -271       C  
ATOM   7515  N1   DC T   9      16.040   6.433  25.045  1.00 31.90           N  
ANISOU 7515  N1   DC T   9     3401   4709   4012    233    -35   -250       N  
ATOM   7516  C2   DC T   9      15.504   6.560  26.339  1.00 32.42           C  
ANISOU 7516  C2   DC T   9     3448   4799   4071    286    -52   -228       C  
ATOM   7517  O2   DC T   9      15.265   7.669  26.828  1.00 34.99           O  
ANISOU 7517  O2   DC T   9     3782   5139   4373    307    -89   -229       O  
ATOM   7518  N3   DC T   9      15.253   5.441  27.058  1.00 33.41           N  
ANISOU 7518  N3   DC T   9     3545   4932   4218    314    -28   -206       N  
ATOM   7519  C4   DC T   9      15.501   4.239  26.544  1.00 32.72           C  
ANISOU 7519  C4   DC T   9     3445   4825   4160    292     10   -205       C  
ATOM   7520  N4   DC T   9      15.228   3.186  27.321  1.00 35.40           N  
ANISOU 7520  N4   DC T   9     3754   5172   4523    322     30   -180       N  
ATOM   7521  C5   DC T   9      16.045   4.075  25.234  1.00 30.78           C  
ANISOU 7521  C5   DC T   9     3216   4553   3924    239     31   -231       C  
ATOM   7522  C6   DC T   9      16.294   5.188  24.527  1.00 31.28           C  
ANISOU 7522  C6   DC T   9     3310   4614   3962    210      7   -252       C  
ATOM   7523  P    DG T  10      20.738   9.023  23.110  1.00 41.33           P  
ANISOU 7523  P    DG T  10     4645   5868   5192    129    -51   -343       P  
ATOM   7524  OP1  DG T  10      21.389  10.105  22.334  1.00 36.94           O  
ANISOU 7524  OP1  DG T  10     4113   5305   4616     91    -72   -363       O  
ATOM   7525  OP2  DG T  10      21.356   7.677  23.164  1.00 38.44           O  
ANISOU 7525  OP2  DG T  10     4252   5491   4861    128     -5   -346       O  
ATOM   7526  O5'  DG T  10      20.493   9.484  24.628  1.00 38.25           O  
ANISOU 7526  O5'  DG T  10     4238   5499   4796    194    -79   -324       O  
ATOM   7527  C5'  DG T  10      20.021  10.777  24.950  1.00 35.11           C  
ANISOU 7527  C5'  DG T  10     3855   5113   4373    210   -124   -322       C  
ATOM   7528  C4'  DG T  10      20.213  11.003  26.437  1.00 38.05           C  
ANISOU 7528  C4'  DG T  10     4204   5507   4745    270   -138   -311       C  
ATOM   7529  O4'  DG T  10      19.388  10.084  27.200  1.00 38.77           O  
ANISOU 7529  O4'  DG T  10     4273   5613   4846    303   -124   -288       O  
ATOM   7530  C3'  DG T  10      21.639  10.816  26.947  1.00 38.34           C  
ANISOU 7530  C3'  DG T  10     4224   5545   4799    282   -123   -319       C  
ATOM   7531  O3'  DG T  10      21.901  11.865  27.890  1.00 37.87           O  
ANISOU 7531  O3'  DG T  10     4161   5504   4725    318   -157   -322       O  
ATOM   7532  C2'  DG T  10      21.634   9.419  27.580  1.00 33.23           C  
ANISOU 7532  C2'  DG T  10     3546   4902   4178    306    -88   -300       C  
ATOM   7533  C1'  DG T  10      20.182   9.249  28.017  1.00 35.69           C  
ANISOU 7533  C1'  DG T  10     3853   5229   4477    330    -99   -279       C  
ATOM   7534  N9   DG T  10      19.680   7.876  27.899  1.00 36.51           N  
ANISOU 7534  N9   DG T  10     3941   5327   4603    327    -64   -262       N  
ATOM   7535  C8   DG T  10      19.845   7.013  26.845  1.00 31.82           C  
ANISOU 7535  C8   DG T  10     3351   4709   4031    285    -30   -271       C  
ATOM   7536  N7   DG T  10      19.277   5.850  27.038  1.00 36.74           N  
ANISOU 7536  N7   DG T  10     3955   5331   4675    294     -5   -252       N  
ATOM   7537  C5   DG T  10      18.696   5.938  28.298  1.00 32.95           C  
ANISOU 7537  C5   DG T  10     3457   4878   4185    344    -23   -227       C  
ATOM   7538  C6   DG T  10      17.956   4.989  29.054  1.00 32.11           C  
ANISOU 7538  C6   DG T  10     3325   4785   4091    374    -10   -197       C  
ATOM   7539  O6   DG T  10      17.649   3.832  28.750  1.00 33.27           O  
ANISOU 7539  O6   DG T  10     3459   4918   4264    363     20   -186       O  
ATOM   7540  N1   DG T  10      17.550   5.485  30.291  1.00 31.63           N  
ANISOU 7540  N1   DG T  10     3251   4757   4009    420    -36   -180       N  
ATOM   7541  C2   DG T  10      17.850   6.751  30.748  1.00 33.54           C  
ANISOU 7541  C2   DG T  10     3504   5017   4225    436    -70   -193       C  
ATOM   7542  N2   DG T  10      17.401   7.077  31.971  1.00 28.31           N  
ANISOU 7542  N2   DG T  10     2825   4389   3544    479    -91   -178       N  
ATOM   7543  N3   DG T  10      18.545   7.647  30.049  1.00 33.66           N  
ANISOU 7543  N3   DG T  10     3543   5016   4231    410    -83   -220       N  
ATOM   7544  C4   DG T  10      18.940   7.182  28.840  1.00 35.27           C  
ANISOU 7544  C4   DG T  10     3760   5189   4452    364    -58   -235       C  
ATOM   7545  P    DC T  11      23.182  11.847  28.837  1.00 38.42           P  
ANISOU 7545  P    DC T  11     4208   5584   4805    348   -152   -325       P  
ATOM   7546  OP1  DC T  11      23.466  13.273  29.098  1.00 42.23           O  
ANISOU 7546  OP1  DC T  11     4703   6074   5268    358   -192   -340       O  
ATOM   7547  OP2  DC T  11      24.246  10.998  28.228  1.00 40.55           O  
ANISOU 7547  OP2  DC T  11     4472   5833   5101    319   -114   -333       O  
ATOM   7548  O5'  DC T  11      22.675  11.125  30.178  1.00 40.87           O  
ANISOU 7548  O5'  DC T  11     4487   5923   5121    399   -145   -298       O  
ATOM   7549  C5'  DC T  11      21.863  11.815  31.132  1.00 39.92           C  
ANISOU 7549  C5'  DC T  11     4359   5830   4977    438   -176   -291       C  
ATOM   7550  C4'  DC T  11      21.911  11.176  32.514  1.00 45.18           C  
ANISOU 7550  C4'  DC T  11     4990   6527   5648    484   -168   -269       C  
ATOM   7551  O4'  DC T  11      21.218   9.903  32.528  1.00 46.41           O  
ANISOU 7551  O4'  DC T  11     5132   6683   5819    486   -140   -244       O  
ATOM   7552  C3'  DC T  11      23.300  10.901  33.097  1.00 48.40           C  
ANISOU 7552  C3'  DC T  11     5379   6940   6072    497   -155   -268       C  
ATOM   7553  O3'  DC T  11      23.270  11.339  34.450  1.00 50.16           O  
ANISOU 7553  O3'  DC T  11     5580   7201   6277    541   -176   -260       O  
ATOM   7554  C2'  DC T  11      23.486   9.390  32.965  1.00 46.66           C  
ANISOU 7554  C2'  DC T  11     5139   6707   5884    489   -115   -247       C  
ATOM   7555  C1'  DC T  11      22.057   8.855  32.973  1.00 44.90           C  
ANISOU 7555  C1'  DC T  11     4914   6492   5655    495   -111   -228       C  
ATOM   7556  N1   DC T  11      21.809   7.659  32.080  1.00 46.46           N  
ANISOU 7556  N1   DC T  11     5112   6661   5881    464    -76   -220       N  
ATOM   7557  C2   DC T  11      21.089   6.545  32.562  1.00 45.93           C  
ANISOU 7557  C2   DC T  11     5021   6604   5828    482    -57   -190       C  
ATOM   7558  O2   DC T  11      20.659   6.544  33.724  1.00 46.89           O  
ANISOU 7558  O2   DC T  11     5121   6759   5936    520    -70   -168       O  
ATOM   7559  N3   DC T  11      20.875   5.484  31.736  1.00 45.25           N  
ANISOU 7559  N3   DC T  11     4933   6490   5769    454    -25   -186       N  
ATOM   7560  C4   DC T  11      21.340   5.495  30.480  1.00 44.08           C  
ANISOU 7560  C4   DC T  11     4806   6309   5633    409    -10   -212       C  
ATOM   7561  N4   DC T  11      21.104   4.425  29.709  1.00 36.01           N  
ANISOU 7561  N4   DC T  11     3780   5263   4639    382     22   -210       N  
ATOM   7562  C5   DC T  11      22.077   6.610  29.970  1.00 43.52           C  
ANISOU 7562  C5   DC T  11     4759   6231   5545    390    -28   -241       C  
ATOM   7563  C6   DC T  11      22.278   7.654  30.791  1.00 46.57           C  
ANISOU 7563  C6   DC T  11     5147   6641   5906    419    -61   -243       C  
ATOM   7564  P    DC T  12      24.529  11.303  35.425  1.00 50.37           P  
ANISOU 7564  P    DC T  12     5582   7245   6311    566   -175   -257       P  
ATOM   7565  OP1  DC T  12      24.212  12.250  36.514  1.00 52.65           O  
ANISOU 7565  OP1  DC T  12     5861   7573   6569    602   -208   -262       O  
ATOM   7566  OP2  DC T  12      25.772  11.427  34.639  1.00 54.12           O  
ANISOU 7566  OP2  DC T  12     6070   7689   6804    536   -164   -277       O  
ATOM   7567  O5'  DC T  12      24.478   9.817  36.017  1.00 50.55           O  
ANISOU 7567  O5'  DC T  12     5572   7278   6357    581   -144   -221       O  
ATOM   7568  C5'  DC T  12      23.367   9.443  36.810  1.00 44.20           C  
ANISOU 7568  C5'  DC T  12     4750   6505   5538    607   -148   -196       C  
ATOM   7569  C4'  DC T  12      23.435   7.980  37.167  1.00 43.09           C  
ANISOU 7569  C4'  DC T  12     4580   6365   5426    614   -118   -161       C  
ATOM   7570  O4'  DC T  12      23.111   7.195  36.004  1.00 41.21           O  
ANISOU 7570  O4'  DC T  12     4355   6088   5214    580    -92   -161       O  
ATOM   7571  C3'  DC T  12      24.812   7.506  37.621  1.00 45.29           C  
ANISOU 7571  C3'  DC T  12     4835   6641   5730    620   -105   -151       C  
ATOM   7572  O3'  DC T  12      24.768   7.254  39.025  1.00 41.77           O  
ANISOU 7572  O3'  DC T  12     4356   6240   5273    657   -114   -122       O  
ATOM   7573  C2'  DC T  12      25.091   6.249  36.792  1.00 41.29           C  
ANISOU 7573  C2'  DC T  12     4323   6095   5270    592    -68   -141       C  
ATOM   7574  C1'  DC T  12      23.752   5.946  36.137  1.00 40.61           C  
ANISOU 7574  C1'  DC T  12     4253   6000   5178    578    -62   -138       C  
ATOM   7575  N1   DC T  12      23.833   5.333  34.778  1.00 39.13           N  
ANISOU 7575  N1   DC T  12     4080   5765   5020    537    -34   -152       N  
ATOM   7576  C2   DC T  12      23.212   4.094  34.529  1.00 41.51           C  
ANISOU 7576  C2   DC T  12     4368   6054   5351    530     -7   -130       C  
ATOM   7577  O2   DC T  12      22.606   3.514  35.453  1.00 38.77           O  
ANISOU 7577  O2   DC T  12     3995   5732   5003    558     -8    -96       O  
ATOM   7578  N3   DC T  12      23.292   3.566  33.268  1.00 39.44           N  
ANISOU 7578  N3   DC T  12     4119   5751   5115    490     19   -148       N  
ATOM   7579  C4   DC T  12      23.945   4.226  32.299  1.00 39.83           C  
ANISOU 7579  C4   DC T  12     4195   5777   5160    457     19   -184       C  
ATOM   7580  N4   DC T  12      23.997   3.681  31.078  1.00 40.57           N  
ANISOU 7580  N4   DC T  12     4301   5837   5278    416     46   -203       N  
ATOM   7581  C5   DC T  12      24.582   5.484  32.537  1.00 39.96           C  
ANISOU 7581  C5   DC T  12     4227   5807   5148    464     -9   -204       C  
ATOM   7582  C6   DC T  12      24.496   5.991  33.775  1.00 40.94           C  
ANISOU 7582  C6   DC T  12     4337   5967   5249    505    -34   -188       C  
ATOM   7583  P    DG T  13      26.084   6.820  39.812  1.00 41.75           P  
ANISOU 7583  P    DG T  13     4323   6248   5292    670   -107   -104       P  
ATOM   7584  OP1  DG T  13      26.001   7.295  41.210  1.00 39.46           O  
ANISOU 7584  OP1  DG T  13     4011   6014   4968    706   -132    -91       O  
ATOM   7585  OP2  DG T  13      27.276   7.167  39.003  1.00 41.75           O  
ANISOU 7585  OP2  DG T  13     4340   6211   5313    646   -101   -133       O  
ATOM   7586  O5'  DG T  13      25.930   5.231  39.804  1.00 42.55           O  
ANISOU 7586  O5'  DG T  13     4398   6334   5436    666    -76    -65       O  
ATOM   7587  C5'  DG T  13      24.762   4.602  40.342  1.00 38.95           C  
ANISOU 7587  C5'  DG T  13     3924   5903   4971    682    -75    -32       C  
ATOM   7588  C4'  DG T  13      24.976   3.101  40.427  1.00 40.79           C  
ANISOU 7588  C4'  DG T  13     4126   6119   5253    678    -47      7       C  
ATOM   7589  O4'  DG T  13      24.937   2.529  39.096  1.00 40.90           O  
ANISOU 7589  O4'  DG T  13     4157   6079   5304    645    -20    -10       O  
ATOM   7590  C3'  DG T  13      26.302   2.631  41.029  1.00 39.24           C  
ANISOU 7590  C3'  DG T  13     3899   5921   5088    686    -42     26       C  
ATOM   7591  O3'  DG T  13      26.022   1.471  41.812  1.00 39.33           O  
ANISOU 7591  O3'  DG T  13     3871   5950   5123    701    -33     77       O  
ATOM   7592  C2'  DG T  13      27.180   2.346  39.806  1.00 39.53           C  
ANISOU 7592  C2'  DG T  13     3949   5899   5169    654    -17     -2       C  
ATOM   7593  C1'  DG T  13      26.153   1.875  38.785  1.00 39.97           C  
ANISOU 7593  C1'  DG T  13     4024   5927   5235    631      1    -10       C  
ATOM   7594  N9   DG T  13      26.354   2.234  37.386  1.00 42.96           N  
ANISOU 7594  N9   DG T  13     4437   6263   5622    595     13    -53       N  
ATOM   7595  C8   DG T  13      26.843   3.413  36.860  1.00 40.91           C  
ANISOU 7595  C8   DG T  13     4210   5998   5337    581     -1    -94       C  
ATOM   7596  N7   DG T  13      26.853   3.429  35.553  1.00 40.73           N  
ANISOU 7596  N7   DG T  13     4213   5937   5327    544     15   -125       N  
ATOM   7597  C5   DG T  13      26.327   2.187  35.195  1.00 43.40           C  
ANISOU 7597  C5   DG T  13     4535   6254   5701    533     43   -106       C  
ATOM   7598  C6   DG T  13      26.093   1.615  33.916  1.00 42.52           C  
ANISOU 7598  C6   DG T  13     4437   6103   5615    495     71   -126       C  
ATOM   7599  O6   DG T  13      26.307   2.117  32.810  1.00 42.57           O  
ANISOU 7599  O6   DG T  13     4473   6087   5615    461     76   -164       O  
ATOM   7600  N1   DG T  13      25.561   0.326  33.994  1.00 42.96           N  
ANISOU 7600  N1   DG T  13     4467   6148   5708    497     94    -98       N  
ATOM   7601  C2   DG T  13      25.274  -0.334  35.173  1.00 42.81           C  
ANISOU 7601  C2   DG T  13     4412   6154   5699    532     89    -52       C  
ATOM   7602  N2   DG T  13      24.757  -1.568  35.069  1.00 36.80           N  
ANISOU 7602  N2   DG T  13     3628   5376   4977    528    112    -27       N  
ATOM   7603  N3   DG T  13      25.486   0.189  36.378  1.00 43.61           N  
ANISOU 7603  N3   DG T  13     4501   6295   5773    566     63    -31       N  
ATOM   7604  C4   DG T  13      26.015   1.443  36.312  1.00 42.82           C  
ANISOU 7604  C4   DG T  13     4426   6205   5637    565     42    -62       C  
ATOM   7605  P    DC T  14      27.156   0.632  42.559  1.00 44.27           P  
ANISOU 7605  P    DC T  14     4455   6576   5791    711    -26    115       P  
ATOM   7606  OP1  DC T  14      26.497  -0.069  43.680  1.00 44.52           O  
ANISOU 7606  OP1  DC T  14     4451   6650   5816    733    -33    168       O  
ATOM   7607  OP2  DC T  14      28.305   1.531  42.828  1.00 37.68           O  
ANISOU 7607  OP2  DC T  14     3626   5750   4942    716    -42     91       O  
ATOM   7608  O5'  DC T  14      27.611  -0.438  41.453  1.00 43.87           O  
ANISOU 7608  O5'  DC T  14     4400   6459   5810    682      8    110       O  
ATOM   7609  C5'  DC T  14      26.709  -1.375  40.880  1.00 41.65           C  
ANISOU 7609  C5'  DC T  14     4116   6153   5556    669     30    123       C  
ATOM   7610  C4'  DC T  14      27.359  -2.118  39.717  1.00 46.00           C  
ANISOU 7610  C4'  DC T  14     4667   6640   6170    639     62    102       C  
ATOM   7611  O4'  DC T  14      27.503  -1.231  38.581  1.00 44.89           O  
ANISOU 7611  O4'  DC T  14     4570   6476   6010    613     65     46       O  
ATOM   7612  C3'  DC T  14      28.755  -2.693  39.957  1.00 45.72           C  
ANISOU 7612  C3'  DC T  14     4599   6582   6189    638     72    114       C  
ATOM   7613  O3'  DC T  14      28.678  -4.103  39.842  1.00 50.48           O  
ANISOU 7613  O3'  DC T  14     5169   7154   6858    632     95    144       O  
ATOM   7614  C2'  DC T  14      29.632  -2.110  38.845  1.00 45.18           C  
ANISOU 7614  C2'  DC T  14     4560   6475   6130    610     84     57       C  
ATOM   7615  C1'  DC T  14      28.584  -1.712  37.810  1.00 46.87           C  
ANISOU 7615  C1'  DC T  14     4815   6679   6315    589     90     24       C  
ATOM   7616  N1   DC T  14      28.944  -0.633  36.819  1.00 45.15           N  
ANISOU 7616  N1   DC T  14     4639   6446   6070    564     87    -31       N  
ATOM   7617  C2   DC T  14      28.773  -0.868  35.445  1.00 45.18           C  
ANISOU 7617  C2   DC T  14     4664   6409   6092    526    113    -66       C  
ATOM   7618  O2   DC T  14      28.348  -1.963  35.049  1.00 45.45           O  
ANISOU 7618  O2   DC T  14     4683   6419   6169    514    138    -55       O  
ATOM   7619  N3   DC T  14      29.079   0.120  34.567  1.00 45.27           N  
ANISOU 7619  N3   DC T  14     4713   6410   6077    501    108   -112       N  
ATOM   7620  C4   DC T  14      29.531   1.295  35.008  1.00 48.31           C  
ANISOU 7620  C4   DC T  14     5114   6820   6420    514     81   -124       C  
ATOM   7621  N4   DC T  14      29.820   2.226  34.092  1.00 48.04           N  
ANISOU 7621  N4   DC T  14     5116   6773   6363    487     76   -167       N  
ATOM   7622  C5   DC T  14      29.711   1.564  36.401  1.00 46.48           C  
ANISOU 7622  C5   DC T  14     4861   6629   6170    554     56    -92       C  
ATOM   7623  C6   DC T  14      29.403   0.581  37.257  1.00 46.98           C  
ANISOU 7623  C6   DC T  14     4888   6706   6258    576     60    -46       C  
ATOM   7624  P    DG T  15      29.704  -5.097  40.576  1.00 53.50           P  
ANISOU 7624  P    DG T  15     5498   7524   7305    643    100    186       P  
ATOM   7625  OP1  DG T  15      28.859  -6.141  41.207  1.00 49.63           O  
ANISOU 7625  OP1  DG T  15     4975   7046   6836    656    101    242       O  
ATOM   7626  OP2  DG T  15      30.697  -4.326  41.366  1.00 48.67           O  
ANISOU 7626  OP2  DG T  15     4882   6941   6669    659     77    188       O  
ATOM   7627  O5'  DG T  15      30.532  -5.736  39.373  1.00 51.88           O  
ANISOU 7627  O5'  DG T  15     5290   7251   7171    611    134    150       O  
ATOM   7628  C5'  DG T  15      29.900  -6.338  38.243  1.00 52.51           C  
ANISOU 7628  C5'  DG T  15     5381   7291   7280    585    163    127       C  
ATOM   7629  C4'  DG T  15      30.870  -6.318  37.077  1.00 51.85           C  
ANISOU 7629  C4'  DG T  15     5308   7157   7234    552    189     72       C  
ATOM   7630  O4'  DG T  15      30.835  -4.997  36.474  1.00 49.17           O  
ANISOU 7630  O4'  DG T  15     5019   6832   6831    539    178     25       O  
ATOM   7631  C3'  DG T  15      32.333  -6.580  37.460  1.00 52.89           C  
ANISOU 7631  C3'  DG T  15     5408   7270   7417    557    191     78       C  
ATOM   7632  O3'  DG T  15      32.882  -7.610  36.634  1.00 53.88           O  
ANISOU 7632  O3'  DG T  15     5510   7339   7625    532    225     59       O  
ATOM   7633  C2'  DG T  15      33.023  -5.231  37.247  1.00 49.79           C  
ANISOU 7633  C2'  DG T  15     5052   6893   6973    552    176     36       C  
ATOM   7634  C1'  DG T  15      32.160  -4.660  36.126  1.00 49.51           C  
ANISOU 7634  C1'  DG T  15     5063   6853   6896    526    185     -8       C  
ATOM   7635  N9   DG T  15      32.287  -3.218  35.907  1.00 47.08           N  
ANISOU 7635  N9   DG T  15     4799   6568   6520    522    165    -43       N  
ATOM   7636  C8   DG T  15      32.549  -2.234  36.834  1.00 46.79           C  
ANISOU 7636  C8   DG T  15     4770   6574   6434    548    132    -32       C  
ATOM   7637  N7   DG T  15      32.608  -1.034  36.327  1.00 42.68           N  
ANISOU 7637  N7   DG T  15     4290   6062   5864    536    119    -72       N  
ATOM   7638  C5   DG T  15      32.377  -1.236  34.978  1.00 42.69           C  
ANISOU 7638  C5   DG T  15     4313   6027   5881    498    145   -110       C  
ATOM   7639  C6   DG T  15      32.330  -0.298  33.923  1.00 42.27           C  
ANISOU 7639  C6   DG T  15     4303   5966   5791    468    145   -158       C  
ATOM   7640  O6   DG T  15      32.490   0.926  34.023  1.00 44.05           O  
ANISOU 7640  O6   DG T  15     4556   6213   5967    473    119   -175       O  
ATOM   7641  N1   DG T  15      32.075  -0.904  32.684  1.00 38.71           N  
ANISOU 7641  N1   DG T  15     3860   5478   5369    430    176   -185       N  
ATOM   7642  C2   DG T  15      31.882  -2.263  32.507  1.00 42.15           C  
ANISOU 7642  C2   DG T  15     4265   5887   5864    424    205   -170       C  
ATOM   7643  N2   DG T  15      31.636  -2.701  31.260  1.00 40.43           N  
ANISOU 7643  N2   DG T  15     4058   5637   5666    384    235   -204       N  
ATOM   7644  N3   DG T  15      31.929  -3.153  33.496  1.00 43.14           N  
ANISOU 7644  N3   DG T  15     4348   6016   6028    453    205   -125       N  
ATOM   7645  C4   DG T  15      32.178  -2.570  34.700  1.00 43.77           C  
ANISOU 7645  C4   DG T  15     4420   6132   6076    489    174    -95       C  
ATOM   7646  P    DC T  16      34.228  -8.388  37.025  1.00 55.45           P  
ANISOU 7646  P    DC T  16     5659   7506   7905    536    234     75       P  
ATOM   7647  OP1  DC T  16      34.306  -9.585  36.156  1.00 56.49           O  
ANISOU 7647  OP1  DC T  16     5765   7580   8120    511    271     58       O  
ATOM   7648  OP2  DC T  16      34.281  -8.561  38.500  1.00 54.56           O  
ANISOU 7648  OP2  DC T  16     5514   7430   7788    573    204    142       O  
ATOM   7649  O5'  DC T  16      35.367  -7.331  36.599  1.00 54.37           O  
ANISOU 7649  O5'  DC T  16     5549   7366   7744    524    231     25       O  
ATOM   7650  C5'  DC T  16      36.016  -7.370  35.327  1.00 50.83           C  
ANISOU 7650  C5'  DC T  16     5112   6873   7328    487    262    -36       C  
ATOM   7651  C4'  DC T  16      35.181  -6.823  34.173  1.00 50.63           C  
ANISOU 7651  C4'  DC T  16     5135   6847   7255    457    274    -83       C  
ATOM   7652  O4'  DC T  16      34.748  -5.465  34.445  1.00 50.53           O  
ANISOU 7652  O4'  DC T  16     5166   6881   7151    468    243    -87       O  
ATOM   7653  C3'  DC T  16      35.916  -6.752  32.838  1.00 51.30           C  
ANISOU 7653  C3'  DC T  16     5234   6893   7365    415    305   -149       C  
ATOM   7654  O3'  DC T  16      35.064  -7.148  31.775  1.00 52.11           O  
ANISOU 7654  O3'  DC T  16     5352   6977   7471    384    331   -177       O  
ATOM   7655  C2'  DC T  16      36.278  -5.278  32.711  1.00 49.53           C  
ANISOU 7655  C2'  DC T  16     5053   6697   7068    411    284   -178       C  
ATOM   7656  C1'  DC T  16      35.070  -4.622  33.360  1.00 47.74           C  
ANISOU 7656  C1'  DC T  16     4852   6518   6768    436    252   -146       C  
ATOM   7657  N1   DC T  16      35.341  -3.226  33.844  1.00 45.23           N  
ANISOU 7657  N1   DC T  16     4565   6238   6381    451    218   -151       N  
ATOM   7658  C2   DC T  16      35.327  -2.149  32.935  1.00 45.27           C  
ANISOU 7658  C2   DC T  16     4617   6247   6337    424    215   -198       C  
ATOM   7659  O2   DC T  16      35.084  -2.354  31.732  1.00 41.61           O  
ANISOU 7659  O2   DC T  16     4170   5758   5883    386    240   -235       O  
ATOM   7660  N3   DC T  16      35.586  -0.894  33.406  1.00 45.57           N  
ANISOU 7660  N3   DC T  16     4679   6318   6318    439    184   -202       N  
ATOM   7661  C4   DC T  16      35.840  -0.685  34.708  1.00 45.03           C  
ANISOU 7661  C4   DC T  16     4591   6279   6238    479    157   -164       C  
ATOM   7662  N4   DC T  16      36.077   0.573  35.121  1.00 40.91           N  
ANISOU 7662  N4   DC T  16     4093   5789   5661    492    127   -173       N  
ATOM   7663  C5   DC T  16      35.860  -1.768  35.643  1.00 45.52           C  
ANISOU 7663  C5   DC T  16     4606   6343   6346    504    160   -115       C  
ATOM   7664  C6   DC T  16      35.609  -3.000  35.172  1.00 46.47           C  
ANISOU 7664  C6   DC T  16     4704   6429   6526    490    190   -109       C  
ATOM   7665  P    DG T  17      35.601  -8.085  30.589  1.00 50.27           P  
ANISOU 7665  P    DG T  17     5098   6690   7313    343    377   -225       P  
ATOM   7666  OP1  DG T  17      34.453  -8.290  29.674  1.00 52.89           O  
ANISOU 7666  OP1  DG T  17     5452   7018   7625    317    393   -245       O  
ATOM   7667  OP2  DG T  17      36.278  -9.249  31.200  1.00 50.20           O  
ANISOU 7667  OP2  DG T  17     5030   6650   7395    360    387   -195       O  
ATOM   7668  O5'  DG T  17      36.733  -7.221  29.852  1.00 50.06           O  
ANISOU 7668  O5'  DG T  17     5094   6656   7270    315    384   -282       O  
ATOM   7669  C5'  DG T  17      36.491  -6.552  28.619  1.00 47.01           C  
ANISOU 7669  C5'  DG T  17     4751   6271   6838    273    396   -335       C  
ATOM   7670  C4'  DG T  17      37.483  -5.418  28.391  1.00 44.70           C  
ANISOU 7670  C4'  DG T  17     4485   5989   6508    261    385   -368       C  
ATOM   7671  O4'  DG T  17      37.457  -4.456  29.470  1.00 45.89           O  
ANISOU 7671  O4'  DG T  17     4652   6180   6604    300    343   -332       O  
ATOM   7672  C3'  DG T  17      38.933  -5.840  28.288  1.00 44.16           C  
ANISOU 7672  C3'  DG T  17     4383   5888   6506    252    406   -393       C  
ATOM   7673  O3'  DG T  17      39.148  -6.141  26.926  1.00 44.33           O  
ANISOU 7673  O3'  DG T  17     4409   5883   6550    201    444   -452       O  
ATOM   7674  C2'  DG T  17      39.719  -4.596  28.706  1.00 45.81           C  
ANISOU 7674  C2'  DG T  17     4616   6123   6666    263    377   -396       C  
ATOM   7675  C1'  DG T  17      38.728  -3.824  29.571  1.00 46.76           C  
ANISOU 7675  C1'  DG T  17     4764   6289   6715    298    336   -352       C  
ATOM   7676  N9   DG T  17      39.037  -3.789  30.995  1.00 43.70           N  
ANISOU 7676  N9   DG T  17     4351   5921   6331    346    308   -300       N  
ATOM   7677  C8   DG T  17      39.402  -4.842  31.804  1.00 46.79           C  
ANISOU 7677  C8   DG T  17     4692   6296   6790    371    313   -262       C  
ATOM   7678  N7   DG T  17      39.589  -4.498  33.053  1.00 45.40           N  
ANISOU 7678  N7   DG T  17     4506   6150   6595    410    281   -218       N  
ATOM   7679  C5   DG T  17      39.319  -3.137  33.066  1.00 42.50           C  
ANISOU 7679  C5   DG T  17     4184   5819   6144    413    254   -231       C  
ATOM   7680  C6   DG T  17      39.356  -2.214  34.137  1.00 44.05           C  
ANISOU 7680  C6   DG T  17     4390   6059   6287    447    215   -203       C  
ATOM   7681  O6   DG T  17      39.635  -2.439  35.327  1.00 45.10           O  
ANISOU 7681  O6   DG T  17     4493   6211   6431    481    196   -158       O  
ATOM   7682  N1   DG T  17      39.020  -0.921  33.721  1.00 43.75           N  
ANISOU 7682  N1   DG T  17     4402   6046   6176    436    197   -232       N  
ATOM   7683  C2   DG T  17      38.687  -0.573  32.430  1.00 44.26           C  
ANISOU 7683  C2   DG T  17     4501   6095   6220    397    214   -278       C  
ATOM   7684  N2   DG T  17      38.389   0.718  32.208  1.00 45.87           N  
ANISOU 7684  N2   DG T  17     4748   6324   6355    391    190   -297       N  
ATOM   7685  N3   DG T  17      38.650  -1.436  31.420  1.00 42.40           N  
ANISOU 7685  N3   DG T  17     4257   5822   6030    363    250   -303       N  
ATOM   7686  C4   DG T  17      38.976  -2.690  31.810  1.00 41.66           C  
ANISOU 7686  C4   DG T  17     4115   5704   6009    374    269   -280       C  
ATOM   7687  P    DG T  18      40.475  -6.840  26.412  1.00 40.57           P  
ANISOU 7687  P    DG T  18     3896   5365   6156    176    480   -495       P  
ATOM   7688  OP1  DG T  18      41.483  -5.800  26.133  1.00 41.64           O  
ANISOU 7688  OP1  DG T  18     4054   5510   6256    161    473   -528       O  
ATOM   7689  OP2  DG T  18      40.066  -7.789  25.357  1.00 45.72           O  
ANISOU 7689  OP2  DG T  18     4534   5987   6851    138    521   -532       O  
ATOM   7690  O5'  DG T  18      40.945  -7.673  27.697  1.00 44.37           O  
ANISOU 7690  O5'  DG T  18     4323   5829   6706    223    470   -442       O  
ATOM   7691  C5'  DG T  18      42.320  -8.023  27.848  1.00 41.22           C  
ANISOU 7691  C5'  DG T  18     3887   5400   6373    223    483   -456       C  
ATOM   7692  C4'  DG T  18      42.806  -7.665  29.242  1.00 38.63           C  
ANISOU 7692  C4'  DG T  18     3546   5093   6039    271    446   -401       C  
ATOM   7693  O4'  DG T  18      44.145  -8.180  29.406  1.00 36.16           O  
ANISOU 7693  O4'  DG T  18     3189   4745   5804    272    460   -412       O  
ATOM   7694  C3'  DG T  18      42.910  -6.180  29.566  1.00 36.45           C  
ANISOU 7694  C3'  DG T  18     3317   4861   5671    282    411   -399       C  
ATOM   7695  O3'  DG T  18      42.543  -5.970  30.931  1.00 35.54           O  
ANISOU 7695  O3'  DG T  18     3196   4778   5530    330    372   -334       O  
ATOM   7696  C2'  DG T  18      44.380  -5.849  29.291  1.00 35.86           C  
ANISOU 7696  C2'  DG T  18     3234   4769   5623    266    421   -437       C  
ATOM   7697  C1'  DG T  18      45.048  -7.140  29.744  1.00 34.21           C  
ANISOU 7697  C1'  DG T  18     2961   4518   5518    280    438   -419       C  
ATOM   7698  N9   DG T  18      46.352  -7.473  29.163  1.00 31.54           N  
ANISOU 7698  N9   DG T  18     2596   4141   5246    254    467   -466       N  
ATOM   7699  C8   DG T  18      47.473  -7.772  29.897  1.00 30.45           C  
ANISOU 7699  C8   DG T  18     2417   3984   5167    276    461   -448       C  
ATOM   7700  N7   DG T  18      48.513  -8.061  29.172  1.00 32.73           N  
ANISOU 7700  N7   DG T  18     2685   4237   5511    247    492   -500       N  
ATOM   7701  C5   DG T  18      48.056  -7.962  27.858  1.00 35.17           C  
ANISOU 7701  C5   DG T  18     3023   4543   5796    201    522   -558       C  
ATOM   7702  C6   DG T  18      48.746  -8.170  26.624  1.00 35.69           C  
ANISOU 7702  C6   DG T  18     3083   4580   5897    152    564   -633       C  
ATOM   7703  O6   DG T  18      49.931  -8.493  26.439  1.00 34.63           O  
ANISOU 7703  O6   DG T  18     2916   4415   5828    140    584   -664       O  
ATOM   7704  N1   DG T  18      47.926  -7.970  25.515  1.00 35.16           N  
ANISOU 7704  N1   DG T  18     3051   4524   5783    112    584   -673       N  
ATOM   7705  C2   DG T  18      46.599  -7.616  25.587  1.00 38.64           C  
ANISOU 7705  C2   DG T  18     3529   4998   6154    120    564   -644       C  
ATOM   7706  N2   DG T  18      45.974  -7.467  24.405  1.00 42.18           N  
ANISOU 7706  N2   DG T  18     4008   5454   6566     75    586   -689       N  
ATOM   7707  N3   DG T  18      45.938  -7.424  26.732  1.00 37.55           N  
ANISOU 7707  N3   DG T  18     3396   4884   5985    167    526   -576       N  
ATOM   7708  C4   DG T  18      46.721  -7.608  27.835  1.00 33.48           C  
ANISOU 7708  C4   DG T  18     2846   4361   5511    205    507   -537       C  
TER    7709       DG T  18                                                      
ATOM   7710  O5'  DC P 103      36.036  11.990  28.914  1.00133.29           O  
ANISOU 7710  O5'  DC P 103    16151  17516  16978    288    -48   -460       O  
ATOM   7711  C5'  DC P 103      36.745  11.327  29.961  1.00133.59           C  
ANISOU 7711  C5'  DC P 103    16154  17560  17045    324    -37   -444       C  
ATOM   7712  C4'  DC P 103      36.655   9.808  29.880  1.00133.61           C  
ANISOU 7712  C4'  DC P 103    16129  17547  17088    321      3   -431       C  
ATOM   7713  O4'  DC P 103      36.714   9.261  31.222  1.00135.01           O  
ANISOU 7713  O4'  DC P 103    16274  17743  17282    370      0   -399       O  
ATOM   7714  C3'  DC P 103      35.386   9.263  29.235  1.00132.69           C  
ANISOU 7714  C3'  DC P 103    16023  17425  16966    303     15   -424       C  
ATOM   7715  O3'  DC P 103      35.709   8.709  27.969  1.00130.12           O  
ANISOU 7715  O3'  DC P 103    15704  17072  16663    253     49   -450       O  
ATOM   7716  C2'  DC P 103      34.848   8.188  30.179  1.00134.00           C  
ANISOU 7716  C2'  DC P 103    16157  17601  17155    340     26   -389       C  
ATOM   7717  C1'  DC P 103      35.730   8.259  31.425  1.00135.38           C  
ANISOU 7717  C1'  DC P 103    16305  17792  17341    381     15   -373       C  
ATOM   7718  N1   DC P 103      34.974   8.526  32.717  1.00136.07           N  
ANISOU 7718  N1   DC P 103    16381  17917  17403    429    -14   -341       N  
ATOM   7719  C2   DC P 103      34.971   7.568  33.756  1.00136.38           C  
ANISOU 7719  C2   DC P 103    16382  17968  17466    462     -5   -306       C  
ATOM   7720  O2   DC P 103      35.587   6.500  33.625  1.00136.63           O  
ANISOU 7720  O2   DC P 103    16389  17977  17546    454     25   -299       O  
ATOM   7721  N3   DC P 103      34.285   7.840  34.901  1.00136.17           N  
ANISOU 7721  N3   DC P 103    16347  17981  17412    502    -31   -279       N  
ATOM   7722  C4   DC P 103      33.625   8.996  35.038  1.00136.04           C  
ANISOU 7722  C4   DC P 103    16354  17986  17348    511    -62   -289       C  
ATOM   7723  N4   DC P 103      32.968   9.210  36.183  1.00135.61           N  
ANISOU 7723  N4   DC P 103    16287  17972  17268    549    -85   -266       N  
ATOM   7724  C5   DC P 103      33.610   9.982  34.001  1.00136.01           C  
ANISOU 7724  C5   DC P 103    16387  17966  17323    479    -73   -324       C  
ATOM   7725  C6   DC P 103      34.289   9.707  32.876  1.00136.08           C  
ANISOU 7725  C6   DC P 103    16408  17940  17357    439    -49   -347       C  
ATOM   7726  P    DG P 104      34.711   8.897  26.729  1.00128.28           P  
ANISOU 7726  P    DG P 104    15503  16832  16404    208     51   -464       P  
ATOM   7727  OP1  DG P 104      34.739  10.324  26.336  1.00128.60           O  
ANISOU 7727  OP1  DG P 104    15577  16881  16404    192     17   -479       O  
ATOM   7728  OP2  DG P 104      33.424   8.258  27.087  1.00128.47           O  
ANISOU 7728  OP2  DG P 104    15520  16866  16428    229     52   -436       O  
ATOM   7729  O5'  DG P 104      35.380   8.021  25.563  1.00125.15           O  
ANISOU 7729  O5'  DG P 104    15100  16407  16043    157     96   -494       O  
ATOM   7730  C5'  DG P 104      36.661   7.405  25.729  1.00119.83           C  
ANISOU 7730  C5'  DG P 104    14399  15718  15414    158    122   -506       C  
ATOM   7731  C4'  DG P 104      36.584   5.892  25.878  1.00115.68           C  
ANISOU 7731  C4'  DG P 104    13837  15174  14940    165    160   -496       C  
ATOM   7732  O4'  DG P 104      37.157   5.492  27.148  1.00114.26           O  
ANISOU 7732  O4'  DG P 104    13623  14998  14791    214    156   -470       O  
ATOM   7733  C3'  DG P 104      35.201   5.254  25.915  1.00113.83           C  
ANISOU 7733  C3'  DG P 104    13602  14945  14704    174    163   -473       C  
ATOM   7734  O3'  DG P 104      34.638   5.191  24.588  1.00111.06           O  
ANISOU 7734  O3'  DG P 104    13274  14585  14338    122    179   -498       O  
ATOM   7735  C2'  DG P 104      35.539   3.888  26.512  1.00113.33           C  
ANISOU 7735  C2'  DG P 104    13494  14866  14701    197    192   -456       C  
ATOM   7736  C1'  DG P 104      36.729   4.170  27.428  1.00111.93           C  
ANISOU 7736  C1'  DG P 104    13297  14692  14539    227    181   -449       C  
ATOM   7737  N9   DG P 104      36.398   4.031  28.848  1.00108.83           N  
ANISOU 7737  N9   DG P 104    12883  14321  14146    283    159   -405       N  
ATOM   7738  C8   DG P 104      36.329   5.038  29.781  1.00107.59           C  
ANISOU 7738  C8   DG P 104    12736  14194  13948    318    120   -387       C  
ATOM   7739  N7   DG P 104      36.013   4.626  30.976  1.00106.51           N  
ANISOU 7739  N7   DG P 104    12573  14076  13818    362    109   -348       N  
ATOM   7740  C5   DG P 104      35.859   3.253  30.834  1.00104.86           C  
ANISOU 7740  C5   DG P 104    12335  13845  13661    356    142   -335       C  
ATOM   7741  C6   DG P 104      35.517   2.268  31.796  1.00102.62           C  
ANISOU 7741  C6   DG P 104    12015  13568  13408    390    146   -293       C  
ATOM   7742  O6   DG P 104      35.277   2.431  32.999  1.00101.06           O  
ANISOU 7742  O6   DG P 104    11804  13401  13193    431    121   -257       O  
ATOM   7743  N1   DG P 104      35.466   0.985  31.244  1.00101.44           N  
ANISOU 7743  N1   DG P 104    11842  13386  13314    371    182   -294       N  
ATOM   7744  C2   DG P 104      35.718   0.691  29.922  1.00101.57           C  
ANISOU 7744  C2   DG P 104    11869  13370  13353    324    213   -336       C  
ATOM   7745  N2   DG P 104      35.622  -0.599  29.569  1.00 99.10           N  
ANISOU 7745  N2   DG P 104    11528  13028  13097    311    247   -335       N  
ATOM   7746  N3   DG P 104      36.039   1.606  29.011  1.00104.18           N  
ANISOU 7746  N3   DG P 104    12235  13699  13651    290    211   -376       N  
ATOM   7747  C4   DG P 104      36.093   2.866  29.530  1.00106.22           C  
ANISOU 7747  C4   DG P 104    12517  13986  13856    309    173   -372       C  
ATOM   7748  P    DC P 105      33.511   4.131  24.145  1.00109.33           P  
ANISOU 7748  P    DC P 105    13047  14357  14135    110    204   -490       P  
ATOM   7749  OP1  DC P 105      33.212   4.370  22.712  1.00108.60           O  
ANISOU 7749  OP1  DC P 105    12984  14260  14020     50    215   -522       O  
ATOM   7750  OP2  DC P 105      32.412   4.155  25.139  1.00107.84           O  
ANISOU 7750  OP2  DC P 105    12857  14189  13930    156    178   -448       O  
ATOM   7751  O5'  DC P 105      34.288   2.736  24.298  1.00106.13           O  
ANISOU 7751  O5'  DC P 105    12598  13926  13801    113    246   -495       O  
ATOM   7752  C5'  DC P 105      33.890   1.564  23.603  1.00100.24           C  
ANISOU 7752  C5'  DC P 105    11836  13159  13092     87    283   -507       C  
ATOM   7753  C4'  DC P 105      33.225   0.554  24.525  1.00 94.36           C  
ANISOU 7753  C4'  DC P 105    11059  12412  12381    129    288   -467       C  
ATOM   7754  O4'  DC P 105      33.753   0.591  25.877  1.00 91.25           O  
ANISOU 7754  O4'  DC P 105    10642  12027  12002    181    269   -434       O  
ATOM   7755  C3'  DC P 105      31.737   0.764  24.740  1.00 91.36           C  
ANISOU 7755  C3'  DC P 105    10699  12053  11962    145    266   -438       C  
ATOM   7756  O3'  DC P 105      31.033   0.490  23.512  1.00 89.72           O  
ANISOU 7756  O3'  DC P 105    10509  11836  11745     98    286   -462       O  
ATOM   7757  C2'  DC P 105      31.531  -0.230  25.881  1.00 90.02           C  
ANISOU 7757  C2'  DC P 105    10489  11880  11834    192    270   -397       C  
ATOM   7758  C1'  DC P 105      32.791  -0.023  26.724  1.00 88.91           C  
ANISOU 7758  C1'  DC P 105    10327  11740  11713    219    262   -390       C  
ATOM   7759  N1   DC P 105      32.546   0.780  27.992  1.00 85.16           N  
ANISOU 7759  N1   DC P 105     9858  11300  11200    268    220   -353       N  
ATOM   7760  C2   DC P 105      32.150   0.122  29.177  1.00 81.05           C  
ANISOU 7760  C2   DC P 105     9307  10791  10699    312    213   -307       C  
ATOM   7761  O2   DC P 105      32.004  -1.108  29.190  1.00 77.64           O  
ANISOU 7761  O2   DC P 105     8843  10338  10318    313    239   -294       O  
ATOM   7762  N3   DC P 105      31.939   0.860  30.300  1.00 79.24           N  
ANISOU 7762  N3   DC P 105     9080  10596  10431    353    177   -278       N  
ATOM   7763  C4   DC P 105      32.100   2.189  30.277  1.00 80.33           C  
ANISOU 7763  C4   DC P 105     9250  10754  10519    352    148   -294       C  
ATOM   7764  N4   DC P 105      31.880   2.868  31.407  1.00 77.75           N  
ANISOU 7764  N4   DC P 105     8922  10462  10157    393    114   -268       N  
ATOM   7765  C5   DC P 105      32.499   2.880  29.090  1.00 81.52           C  
ANISOU 7765  C5   DC P 105     9432  10889  10651    309    153   -338       C  
ATOM   7766  C6   DC P 105      32.706   2.143  27.988  1.00 84.08           C  
ANISOU 7766  C6   DC P 105     9754  11183  11010    267    189   -365       C  
ATOM   7767  P    DG P 106      29.671  -0.350  23.376  1.00 87.67           P  
ANISOU 7767  P    DG P 106    10244  11575  11493     99    297   -443       P  
ATOM   7768  OP1  DG P 106      29.382  -0.475  21.928  1.00 87.97           O  
ANISOU 7768  OP1  DG P 106    10301  11603  11521     39    320   -482       O  
ATOM   7769  OP2  DG P 106      28.654   0.245  24.274  1.00 87.38           O  
ANISOU 7769  OP2  DG P 106    10220  11565  11414    140    258   -403       O  
ATOM   7770  O5'  DG P 106      30.074  -1.797  23.932  1.00 85.17           O  
ANISOU 7770  O5'  DG P 106     9877  11234  11252    121    328   -430       O  
ATOM   7771  C5'  DG P 106      29.214  -2.911  23.747  1.00 79.20           C  
ANISOU 7771  C5'  DG P 106     9101  10464  10526    118    351   -420       C  
ATOM   7772  C4'  DG P 106      28.676  -3.450  25.063  1.00 75.17           C  
ANISOU 7772  C4'  DG P 106     8564   9962  10035    173    337   -366       C  
ATOM   7773  O4'  DG P 106      29.151  -2.700  26.213  1.00 70.98           O  
ANISOU 7773  O4'  DG P 106     8032   9454   9482    215    304   -338       O  
ATOM   7774  C3'  DG P 106      27.155  -3.426  25.146  1.00 75.29           C  
ANISOU 7774  C3'  DG P 106     8596   9995  10015    183    322   -340       C  
ATOM   7775  O3'  DG P 106      26.707  -4.734  25.476  1.00 77.81           O  
ANISOU 7775  O3'  DG P 106     8879  10298  10388    198    344   -316       O  
ATOM   7776  C2'  DG P 106      26.845  -2.408  26.243  1.00 71.20           C  
ANISOU 7776  C2'  DG P 106     8093   9513   9447    226    278   -306       C  
ATOM   7777  C1'  DG P 106      28.079  -2.536  27.122  1.00 67.93           C  
ANISOU 7777  C1'  DG P 106     7649   9096   9066    254    277   -295       C  
ATOM   7778  N9   DG P 106      28.345  -1.382  27.986  1.00 63.37           N  
ANISOU 7778  N9   DG P 106     7086   8549   8443    285    238   -280       N  
ATOM   7779  C8   DG P 106      28.589  -0.084  27.601  1.00 61.21           C  
ANISOU 7779  C8   DG P 106     6849   8288   8119    270    216   -305       C  
ATOM   7780  N7   DG P 106      28.802   0.731  28.596  1.00 60.40           N  
ANISOU 7780  N7   DG P 106     6749   8213   7988    306    183   -286       N  
ATOM   7781  C5   DG P 106      28.693  -0.079  29.721  1.00 59.41           C  
ANISOU 7781  C5   DG P 106     6587   8095   7891    346    184   -245       C  
ATOM   7782  C6   DG P 106      28.820   0.239  31.099  1.00 57.00           C  
ANISOU 7782  C6   DG P 106     6265   7820   7572    393    157   -210       C  
ATOM   7783  O6   DG P 106      29.068   1.341  31.601  1.00 57.18           O  
ANISOU 7783  O6   DG P 106     6303   7868   7553    409    127   -213       O  
ATOM   7784  N1   DG P 106      28.635  -0.869  31.927  1.00 53.86           N  
ANISOU 7784  N1   DG P 106     5828   7424   7213    419    167   -170       N  
ATOM   7785  C2   DG P 106      28.355  -2.138  31.474  1.00 55.28           C  
ANISOU 7785  C2   DG P 106     5986   7575   7444    404    199   -164       C  
ATOM   7786  N2   DG P 106      28.199  -3.089  32.407  1.00 51.38           N  
ANISOU 7786  N2   DG P 106     5452   7085   6984    434    202   -120       N  
ATOM   7787  N3   DG P 106      28.227  -2.449  30.184  1.00 57.42           N  
ANISOU 7787  N3   DG P 106     6271   7816   7731    362    226   -200       N  
ATOM   7788  C4   DG P 106      28.411  -1.381  29.364  1.00 59.78           C  
ANISOU 7788  C4   DG P 106     6609   8116   7988    334    217   -239       C  
ATOM   7789  P    DC P 107      25.197  -5.189  25.210  1.00 80.47           P  
ANISOU 7789  P    DC P 107     9224  10640  10712    194    346   -300       P  
ATOM   7790  OP1  DC P 107      25.231  -6.453  24.436  1.00 78.50           O  
ANISOU 7790  OP1  DC P 107     8948  10355  10522    164    389   -322       O  
ATOM   7791  OP2  DC P 107      24.435  -4.018  24.708  1.00 79.49           O  
ANISOU 7791  OP2  DC P 107     9148  10541  10515    178    320   -310       O  
ATOM   7792  O5'  DC P 107      24.674  -5.504  26.689  1.00 78.21           O  
ANISOU 7792  O5'  DC P 107     8913  10373  10431    252    325   -240       O  
ATOM   7793  C5'  DC P 107      25.284  -6.495  27.512  1.00 72.79           C  
ANISOU 7793  C5'  DC P 107     8178   9671   9807    278    337   -213       C  
ATOM   7794  C4'  DC P 107      24.694  -6.412  28.909  1.00 70.14           C  
ANISOU 7794  C4'  DC P 107     7830   9367   9451    330    307   -156       C  
ATOM   7795  O4'  DC P 107      25.188  -5.226  29.582  1.00 67.19           O  
ANISOU 7795  O4'  DC P 107     7474   9025   9030    351    274   -151       O  
ATOM   7796  C3'  DC P 107      23.174  -6.310  28.960  1.00 69.78           C  
ANISOU 7796  C3'  DC P 107     7803   9344   9366    337    293   -135       C  
ATOM   7797  O3'  DC P 107      22.692  -7.190  29.964  1.00 71.81           O  
ANISOU 7797  O3'  DC P 107     8024   9608   9652    372    292    -84       O  
ATOM   7798  C2'  DC P 107      22.896  -4.841  29.295  1.00 66.75           C  
ANISOU 7798  C2'  DC P 107     7457   8998   8906    351    255   -136       C  
ATOM   7799  C1'  DC P 107      24.113  -4.506  30.151  1.00 62.34           C  
ANISOU 7799  C1'  DC P 107     6882   8449   8357    375    243   -127       C  
ATOM   7800  N1   DC P 107      24.511  -3.056  30.207  1.00 55.36           N  
ANISOU 7800  N1   DC P 107     6030   7587   7415    377    214   -147       N  
ATOM   7801  C2   DC P 107      24.839  -2.482  31.449  1.00 49.03           C  
ANISOU 7801  C2   DC P 107     5220   6819   6591    417    185   -120       C  
ATOM   7802  O2   DC P 107      24.781  -3.177  32.470  1.00 44.12           O  
ANISOU 7802  O2   DC P 107     4562   6208   5992    448    183    -79       O  
ATOM   7803  N3   DC P 107      25.209  -1.174  31.494  1.00 46.26           N  
ANISOU 7803  N3   DC P 107     4897   6487   6194    419    159   -141       N  
ATOM   7804  C4   DC P 107      25.264  -0.454  30.365  1.00 47.56           C  
ANISOU 7804  C4   DC P 107     5098   6638   6335    382    159   -182       C  
ATOM   7805  N4   DC P 107      25.630   0.828  30.451  1.00 45.86           N  
ANISOU 7805  N4   DC P 107     4907   6440   6076    385    132   -199       N  
ATOM   7806  C5   DC P 107      24.940  -1.016  29.093  1.00 48.03           C  
ANISOU 7806  C5   DC P 107     5168   6668   6414    339    188   -207       C  
ATOM   7807  C6   DC P 107      24.576  -2.307  29.062  1.00 52.19           C  
ANISOU 7807  C6   DC P 107     5667   7177   6987    338    215   -191       C  
ATOM   7808  P    DG P 108      21.144  -7.594  29.996  1.00 73.86           P  
ANISOU 7808  P    DG P 108     8288   9880   9896    378    289    -59       P  
ATOM   7809  OP1  DG P 108      21.089  -9.049  30.277  1.00 74.48           O  
ANISOU 7809  OP1  DG P 108     8320   9934  10045    385    313    -30       O  
ATOM   7810  OP2  DG P 108      20.461  -7.028  28.806  1.00 72.28           O  
ANISOU 7810  OP2  DG P 108     8130   9677   9657    342    293    -98       O  
ATOM   7811  O5'  DG P 108      20.613  -6.790  31.263  1.00 68.80           O  
ANISOU 7811  O5'  DG P 108     7654   9290   9199    421    250    -20       O  
ATOM   7812  C5'  DG P 108      21.147  -7.062  32.554  1.00 66.97           C  
ANISOU 7812  C5'  DG P 108     7387   9075   8984    458    237     22       C  
ATOM   7813  C4'  DG P 108      20.638  -6.033  33.545  1.00 64.38           C  
ANISOU 7813  C4'  DG P 108     7073   8799   8589    491    199     44       C  
ATOM   7814  O4'  DG P 108      21.283  -4.764  33.270  1.00 61.47           O  
ANISOU 7814  O4'  DG P 108     6737   8439   8179    483    183      7       O  
ATOM   7815  C3'  DG P 108      19.129  -5.784  33.502  1.00 63.18           C  
ANISOU 7815  C3'  DG P 108     6942   8671   8394    495    188     53       C  
ATOM   7816  O3'  DG P 108      18.620  -5.849  34.836  1.00 64.86           O  
ANISOU 7816  O3'  DG P 108     7133   8926   8587    534    167    100       O  
ATOM   7817  C2'  DG P 108      19.001  -4.405  32.851  1.00 60.84           C  
ANISOU 7817  C2'  DG P 108     6693   8383   8040    479    169     11       C  
ATOM   7818  C1'  DG P 108      20.314  -3.742  33.250  1.00 58.83           C  
ANISOU 7818  C1'  DG P 108     6437   8135   7781    488    158     -1       C  
ATOM   7819  N9   DG P 108      20.770  -2.688  32.343  1.00 56.10           N  
ANISOU 7819  N9   DG P 108     6129   7778   7408    460    151    -48       N  
ATOM   7820  C8   DG P 108      20.782  -2.698  30.967  1.00 53.35           C  
ANISOU 7820  C8   DG P 108     5805   7398   7068    417    171    -87       C  
ATOM   7821  N7   DG P 108      21.254  -1.599  30.444  1.00 50.53           N  
ANISOU 7821  N7   DG P 108     5479   7041   6678    400    157   -121       N  
ATOM   7822  C5   DG P 108      21.571  -0.806  31.544  1.00 50.05           C  
ANISOU 7822  C5   DG P 108     5415   7014   6589    435    127   -106       C  
ATOM   7823  C6   DG P 108      22.126   0.499  31.617  1.00 46.73           C  
ANISOU 7823  C6   DG P 108     5018   6608   6130    437    101   -128       C  
ATOM   7824  O6   DG P 108      22.444   1.244  30.682  1.00 46.86           O  
ANISOU 7824  O6   DG P 108     5065   6610   6130    406     97   -164       O  
ATOM   7825  N1   DG P 108      22.292   0.936  32.931  1.00 45.94           N  
ANISOU 7825  N1   DG P 108     4902   6543   6009    479     76   -104       N  
ATOM   7826  C2   DG P 108      21.964   0.197  34.046  1.00 47.37           C  
ANISOU 7826  C2   DG P 108     5049   6747   6203    512     76    -62       C  
ATOM   7827  N2   DG P 108      22.183   0.760  35.242  1.00 45.06           N  
ANISOU 7827  N2   DG P 108     4744   6493   5885    547     50    -44       N  
ATOM   7828  N3   DG P 108      21.447  -1.026  33.991  1.00 51.35           N  
ANISOU 7828  N3   DG P 108     5530   7237   6743    510     99    -37       N  
ATOM   7829  C4   DG P 108      21.280  -1.464  32.717  1.00 51.21           C  
ANISOU 7829  C4   DG P 108     5528   7182   6748    472    124    -62       C  
ATOM   7830  P    DG P 109      17.114  -5.476  35.239  1.00 68.18           P  
ANISOU 7830  P    DG P 109     7566   9383   8956    551    147    118       P  
ATOM   7831  OP1  DG P 109      16.758  -6.326  36.401  1.00 68.75           O  
ANISOU 7831  OP1  DG P 109     7597   9480   9044    580    144    174       O  
ATOM   7832  OP2  DG P 109      16.262  -5.482  34.027  1.00 65.57           O  
ANISOU 7832  OP2  DG P 109     7266   9029   8621    521    160     90       O  
ATOM   7833  O5'  DG P 109      17.247  -3.962  35.749  1.00 65.66           O  
ANISOU 7833  O5'  DG P 109     7273   9104   8573    568    113    101       O  
ATOM   7834  C5'  DG P 109      18.090  -3.649  36.866  1.00 63.80           C  
ANISOU 7834  C5'  DG P 109     7016   8898   8328    595     96    119       C  
ATOM   7835  C4'  DG P 109      17.771  -2.292  37.490  1.00 63.19           C  
ANISOU 7835  C4'  DG P 109     6958   8866   8184    616     62    108       C  
ATOM   7836  O4'  DG P 109      18.435  -1.206  36.778  1.00 60.61           O  
ANISOU 7836  O4'  DG P 109     6666   8525   7840    598     53     61       O  
ATOM   7837  C3'  DG P 109      16.298  -1.912  37.547  1.00 62.50           C  
ANISOU 7837  C3'  DG P 109     6886   8803   8056    623     48    110       C  
ATOM   7838  O3'  DG P 109      16.069  -1.238  38.785  1.00 65.26           O  
ANISOU 7838  O3'  DG P 109     7226   9209   8363    656     20    125       O  
ATOM   7839  C2'  DG P 109      16.119  -1.023  36.312  1.00 59.87           C  
ANISOU 7839  C2'  DG P 109     6599   8445   7705    595     44     62       C  
ATOM   7840  C1'  DG P 109      17.478  -0.327  36.207  1.00 57.92           C  
ANISOU 7840  C1'  DG P 109     6360   8189   7459    589     38     35       C  
ATOM   7841  N9   DG P 109      17.894   0.000  34.840  1.00 53.63           N  
ANISOU 7841  N9   DG P 109     5848   7603   6925    550     48     -6       N  
ATOM   7842  C8   DG P 109      17.778  -0.807  33.729  1.00 52.19           C  
ANISOU 7842  C8   DG P 109     5672   7380   6778    517     77    -16       C  
ATOM   7843  N7   DG P 109      18.237  -0.257  32.636  1.00 52.05           N  
ANISOU 7843  N7   DG P 109     5683   7336   6757    483     81    -56       N  
ATOM   7844  C5   DG P 109      18.692   0.991  33.039  1.00 47.77           C  
ANISOU 7844  C5   DG P 109     5157   6815   6179    496     52    -71       C  
ATOM   7845  C6   DG P 109      19.292   2.024  32.278  1.00 47.66           C  
ANISOU 7845  C6   DG P 109     5174   6788   6147    472     40   -109       C  
ATOM   7846  O6   DG P 109      19.553   2.034  31.062  1.00 49.37           O  
ANISOU 7846  O6   DG P 109     5412   6973   6374    432     55   -137       O  
ATOM   7847  N1   DG P 109      19.604   3.132  33.063  1.00 44.91           N  
ANISOU 7847  N1   DG P 109     4830   6469   5765    498      9   -114       N  
ATOM   7848  C2   DG P 109      19.366   3.222  34.415  1.00 44.56           C  
ANISOU 7848  C2   DG P 109     4762   6465   5704    540     -8    -87       C  
ATOM   7849  N2   DG P 109      19.737   4.367  34.996  1.00 39.31           N  
ANISOU 7849  N2   DG P 109     4105   5825   5008    558    -37   -100       N  
ATOM   7850  N3   DG P 109      18.801   2.260  35.143  1.00 47.53           N  
ANISOU 7850  N3   DG P 109     5109   6857   6093    561      2    -50       N  
ATOM   7851  C4   DG P 109      18.487   1.170  34.393  1.00 49.74           C  
ANISOU 7851  C4   DG P 109     5384   7106   6408    538     32    -43       C  
ATOM   7852  P    DC P 110      14.642  -0.615  39.189  1.00 70.22           P  
ANISOU 7852  P    DC P 110     7864   9876   8941    672     -1    126       P  
ATOM   7853  OP1  DC P 110      14.690  -0.454  40.663  1.00 69.98           O  
ANISOU 7853  OP1  DC P 110     7803   9903   8883    706    -19    154       O  
ATOM   7854  OP2  DC P 110      13.555  -1.395  38.540  1.00 66.80           O  
ANISOU 7854  OP2  DC P 110     7435   9422   8525    658     17    136       O  
ATOM   7855  O5'  DC P 110      14.643   0.836  38.504  1.00 65.80           O  
ANISOU 7855  O5'  DC P 110     7346   9308   8346    661    -21     74       O  
ATOM   7856  C5'  DC P 110      15.714   1.753  38.759  1.00 60.92           C  
ANISOU 7856  C5'  DC P 110     6734   8698   7715    666    -37     52       C  
ATOM   7857  C4'  DC P 110      15.604   2.981  37.873  1.00 55.41           C  
ANISOU 7857  C4'  DC P 110     6077   7982   6993    648    -54      6       C  
ATOM   7858  O4'  DC P 110      15.985   2.686  36.514  1.00 53.50           O  
ANISOU 7858  O4'  DC P 110     5858   7688   6782    611    -34    -14       O  
ATOM   7859  C3'  DC P 110      14.198   3.548  37.763  1.00 52.91           C  
ANISOU 7859  C3'  DC P 110     5777   7680   6645    652    -71     -3       C  
ATOM   7860  O3'  DC P 110      14.172   4.638  38.669  1.00 50.03           O  
ANISOU 7860  O3'  DC P 110     5409   7357   6244    679   -101    -16       O  
ATOM   7861  C2'  DC P 110      14.030   3.927  36.283  1.00 48.92           C  
ANISOU 7861  C2'  DC P 110     5310   7129   6147    615    -69    -35       C  
ATOM   7862  C1'  DC P 110      15.418   3.683  35.695  1.00 47.11           C  
ANISOU 7862  C1'  DC P 110     5085   6867   5948    593    -52    -47       C  
ATOM   7863  N1   DC P 110      15.523   3.230  34.250  1.00 42.85           N  
ANISOU 7863  N1   DC P 110     4567   6279   5436    550    -29    -63       N  
ATOM   7864  C2   DC P 110      16.148   4.058  33.297  1.00 41.60           C  
ANISOU 7864  C2   DC P 110     4438   6095   5271    521    -36    -99       C  
ATOM   7865  O2   DC P 110      16.594   5.157  33.637  1.00 39.64           O  
ANISOU 7865  O2   DC P 110     4200   5862   5000    532    -62   -116       O  
ATOM   7866  N3   DC P 110      16.251   3.636  32.011  1.00 42.19           N  
ANISOU 7866  N3   DC P 110     4531   6131   5367    479    -14   -114       N  
ATOM   7867  C4   DC P 110      15.759   2.443  31.656  1.00 42.55           C  
ANISOU 7867  C4   DC P 110     4565   6161   5440    468     14    -98       C  
ATOM   7868  N4   DC P 110      15.885   2.065  30.375  1.00 38.53           N  
ANISOU 7868  N4   DC P 110     4073   5617   4950    425     36   -117       N  
ATOM   7869  C5   DC P 110      15.118   1.584  32.608  1.00 40.86           C  
ANISOU 7869  C5   DC P 110     4320   5969   5236    499     21    -61       C  
ATOM   7870  C6   DC P 110      15.036   2.008  33.874  1.00 39.88           C  
ANISOU 7870  C6   DC P 110     4180   5885   5089    538     -1    -43       C  
ATOM   7871  P    DG P 111      12.831   5.405  39.038  1.00 49.60           P  
ANISOU 7871  P    DG P 111     5360   7333   6152    695   -125    -26       P  
ATOM   7872  OP1  DG P 111      13.058   6.071  40.338  1.00 49.24           O  
ANISOU 7872  OP1  DG P 111     5293   7339   6076    728   -147    -28       O  
ATOM   7873  OP2  DG P 111      11.680   4.487  38.849  1.00 52.30           O  
ANISOU 7873  OP2  DG P 111     5696   7672   6502    692   -110      0       O  
ATOM   7874  O5'  DG P 111      12.726   6.507  37.876  1.00 48.58           O  
ANISOU 7874  O5'  DG P 111     5272   7169   6018    670   -143    -67       O  
ATOM   7875  C5'  DG P 111      13.839   7.332  37.551  1.00 46.77           C  
ANISOU 7875  C5'  DG P 111     5059   6924   5789    660   -154    -95       C  
ATOM   7876  C4'  DG P 111      13.553   8.155  36.313  1.00 45.47           C  
ANISOU 7876  C4'  DG P 111     4931   6721   5622    630   -168   -125       C  
ATOM   7877  O4'  DG P 111      13.814   7.398  35.103  1.00 45.69           O  
ANISOU 7877  O4'  DG P 111     4976   6706   5679    592   -141   -123       O  
ATOM   7878  C3'  DG P 111      12.116   8.638  36.211  1.00 44.59           C  
ANISOU 7878  C3'  DG P 111     4830   6619   5493    634   -186   -131       C  
ATOM   7879  O3'  DG P 111      12.228  10.020  36.055  1.00 43.10           O  
ANISOU 7879  O3'  DG P 111     4659   6428   5290    633   -219   -163       O  
ATOM   7880  C2'  DG P 111      11.549   7.923  34.979  1.00 45.03           C  
ANISOU 7880  C2'  DG P 111     4905   6636   5567    599   -167   -124       C  
ATOM   7881  C1'  DG P 111      12.805   7.671  34.153  1.00 43.85           C  
ANISOU 7881  C1'  DG P 111     4768   6452   5440    569   -149   -133       C  
ATOM   7882  N9   DG P 111      12.789   6.511  33.270  1.00 42.86           N  
ANISOU 7882  N9   DG P 111     4647   6296   5342    539   -116   -120       N  
ATOM   7883  C8   DG P 111      12.256   5.272  33.534  1.00 38.67           C  
ANISOU 7883  C8   DG P 111     4095   5770   4827    547    -90    -91       C  
ATOM   7884  N7   DG P 111      12.428   4.432  32.553  1.00 43.48           N  
ANISOU 7884  N7   DG P 111     4712   6346   5464    514    -62    -90       N  
ATOM   7885  C5   DG P 111      13.127   5.141  31.576  1.00 41.00           C  
ANISOU 7885  C5   DG P 111     4426   6005   5149    481    -69   -120       C  
ATOM   7886  C6   DG P 111      13.591   4.756  30.286  1.00 41.95           C  
ANISOU 7886  C6   DG P 111     4563   6087   5289    436    -47   -136       C  
ATOM   7887  O6   DG P 111      13.485   3.665  29.708  1.00 45.77           O  
ANISOU 7887  O6   DG P 111     5041   6551   5799    415    -15   -129       O  
ATOM   7888  N1   DG P 111      14.249   5.789  29.625  1.00 40.26           N  
ANISOU 7888  N1   DG P 111     4375   5860   5062    412    -64   -165       N  
ATOM   7889  C2   DG P 111      14.430   7.049  30.142  1.00 37.73           C  
ANISOU 7889  C2   DG P 111     4062   5556   4716    431    -99   -177       C  
ATOM   7890  N2   DG P 111      15.087   7.913  29.358  1.00 35.08           N  
ANISOU 7890  N2   DG P 111     3751   5203   4374    402   -112   -202       N  
ATOM   7891  N3   DG P 111      14.004   7.425  31.345  1.00 36.96           N  
ANISOU 7891  N3   DG P 111     3947   5493   4602    474   -119   -165       N  
ATOM   7892  C4   DG P 111      13.359   6.429  32.009  1.00 41.85           C  
ANISOU 7892  C4   DG P 111     4542   6129   5230    497   -102   -137       C  
ATOM   7893  P    DG P 112      10.964  10.979  35.958  1.00 43.89           P  
ANISOU 7893  P    DG P 112     4770   6532   5373    639   -249   -180       P  
ATOM   7894  OP1  DG P 112      11.426  12.282  36.482  1.00 44.89           O  
ANISOU 7894  OP1  DG P 112     4896   6674   5487    656   -281   -209       O  
ATOM   7895  OP2  DG P 112       9.731  10.318  36.446  1.00 42.86           O  
ANISOU 7895  OP2  DG P 112     4623   6426   5237    656   -241   -159       O  
ATOM   7896  O5'  DG P 112      10.788  11.094  34.375  1.00 42.36           O  
ANISOU 7896  O5'  DG P 112     4613   6289   5193    593   -249   -189       O  
ATOM   7897  C5'  DG P 112      11.853  11.570  33.570  1.00 41.89           C  
ANISOU 7897  C5'  DG P 112     4574   6199   5142    565   -253   -207       C  
ATOM   7898  C4'  DG P 112      11.481  11.373  32.115  1.00 43.23           C  
ANISOU 7898  C4'  DG P 112     4774   6330   5323    519   -246   -207       C  
ATOM   7899  O4'  DG P 112      11.651   9.981  31.743  1.00 39.91           O  
ANISOU 7899  O4'  DG P 112     4347   5897   4919    503   -206   -187       O  
ATOM   7900  C3'  DG P 112      10.033  11.739  31.783  1.00 41.62           C  
ANISOU 7900  C3'  DG P 112     4581   6123   5112    515   -266   -207       C  
ATOM   7901  O3'  DG P 112      10.086  12.810  30.867  1.00 40.96           O  
ANISOU 7901  O3'  DG P 112     4524   6012   5026    486   -294   -226       O  
ATOM   7902  C2'  DG P 112       9.478  10.462  31.164  1.00 39.84           C  
ANISOU 7902  C2'  DG P 112     4356   5883   4897    495   -233   -185       C  
ATOM   7903  C1'  DG P 112      10.747   9.745  30.706  1.00 38.49           C  
ANISOU 7903  C1'  DG P 112     4187   5694   4742    472   -202   -184       C  
ATOM   7904  N9   DG P 112      10.555   8.312  30.497  1.00 39.49           N  
ANISOU 7904  N9   DG P 112     4303   5816   4887    463   -164   -162       N  
ATOM   7905  C8   DG P 112       9.935   7.421  31.341  1.00 39.77           C  
ANISOU 7905  C8   DG P 112     4312   5873   4926    492   -148   -137       C  
ATOM   7906  N7   DG P 112       9.888   6.204  30.884  1.00 40.30           N  
ANISOU 7906  N7   DG P 112     4374   5925   5015    475   -115   -122       N  
ATOM   7907  C5   DG P 112      10.512   6.292  29.645  1.00 39.41           C  
ANISOU 7907  C5   DG P 112     4285   5778   4911    430   -106   -141       C  
ATOM   7908  C6   DG P 112      10.755   5.295  28.673  1.00 36.10           C  
ANISOU 7908  C6   DG P 112     3870   5330   4515    394    -72   -141       C  
ATOM   7909  O6   DG P 112      10.462   4.102  28.723  1.00 36.48           O  
ANISOU 7909  O6   DG P 112     3901   5376   4585    395    -43   -123       O  
ATOM   7910  N1   DG P 112      11.415   5.789  27.554  1.00 38.18           N  
ANISOU 7910  N1   DG P 112     4160   5570   4778    351    -74   -166       N  
ATOM   7911  C2   DG P 112      11.791   7.098  27.386  1.00 39.77           C  
ANISOU 7911  C2   DG P 112     4380   5770   4959    344   -106   -185       C  
ATOM   7912  N2   DG P 112      12.411   7.394  26.239  1.00 40.28           N  
ANISOU 7912  N2   DG P 112     4468   5811   5024    298   -103   -205       N  
ATOM   7913  N3   DG P 112      11.567   8.050  28.286  1.00 41.36           N  
ANISOU 7913  N3   DG P 112     4578   5995   5142    380   -139   -185       N  
ATOM   7914  C4   DG P 112      10.925   7.581  29.389  1.00 39.48           C  
ANISOU 7914  C4   DG P 112     4314   5783   4903    422   -136   -164       C  
ATOM   7915  P    DC P 113       8.843  13.724  30.461  1.00 43.87           P  
ANISOU 7915  P    DC P 113     4906   6372   5390    480   -330   -234       P  
ATOM   7916  OP1  DC P 113       9.182  15.069  30.964  1.00 41.46           O  
ANISOU 7916  OP1  DC P 113     4598   6073   5080    499   -367   -257       O  
ATOM   7917  OP2  DC P 113       7.553  13.077  30.782  1.00 45.19           O  
ANISOU 7917  OP2  DC P 113     5062   6554   5555    496   -321   -217       O  
ATOM   7918  O5'  DC P 113       8.935  13.719  28.869  1.00 41.31           O  
ANISOU 7918  O5'  DC P 113     4615   6009   5072    423   -328   -234       O  
ATOM   7919  C5'  DC P 113      10.212  13.775  28.256  1.00 41.60           C  
ANISOU 7919  C5'  DC P 113     4665   6028   5113    393   -318   -243       C  
ATOM   7920  C4'  DC P 113      10.231  12.998  26.959  1.00 39.11           C  
ANISOU 7920  C4'  DC P 113     4369   5688   4803    343   -293   -235       C  
ATOM   7921  O4'  DC P 113      10.156  11.577  27.219  1.00 38.45           O  
ANISOU 7921  O4'  DC P 113     4269   5613   4728    352   -251   -219       O  
ATOM   7922  C3'  DC P 113       9.062  13.351  26.046  1.00 39.73           C  
ANISOU 7922  C3'  DC P 113     4467   5750   4877    314   -314   -230       C  
ATOM   7923  O3'  DC P 113       9.590  13.827  24.804  1.00 32.57           O  
ANISOU 7923  O3'  DC P 113     3587   4819   3968    261   -323   -239       O  
ATOM   7924  C2'  DC P 113       8.261  12.045  25.953  1.00 38.88           C  
ANISOU 7924  C2'  DC P 113     4352   5646   4774    313   -280   -212       C  
ATOM   7925  C1'  DC P 113       9.334  10.994  26.235  1.00 39.83           C  
ANISOU 7925  C1'  DC P 113     4457   5771   4905    317   -238   -210       C  
ATOM   7926  N1   DC P 113       8.810   9.658  26.708  1.00 39.57           N  
ANISOU 7926  N1   DC P 113     4403   5750   4882    336   -204   -190       N  
ATOM   7927  C2   DC P 113       9.077   8.507  25.940  1.00 40.11           C  
ANISOU 7927  C2   DC P 113     4473   5801   4965    304   -165   -186       C  
ATOM   7928  O2   DC P 113       9.745   8.604  24.903  1.00 41.91           O  
ANISOU 7928  O2   DC P 113     4720   6009   5195    260   -158   -201       O  
ATOM   7929  N3   DC P 113       8.599   7.302  26.357  1.00 38.77           N  
ANISOU 7929  N3   DC P 113     4282   5639   4808    321   -135   -167       N  
ATOM   7930  C4   DC P 113       7.884   7.217  27.485  1.00 37.09           C  
ANISOU 7930  C4   DC P 113     4049   5452   4591    367   -143   -151       C  
ATOM   7931  N4   DC P 113       7.448   6.005  27.845  1.00 28.31           N  
ANISOU 7931  N4   DC P 113     2916   4346   3493    380   -114   -130       N  
ATOM   7932  C5   DC P 113       7.587   8.375  28.283  1.00 38.76           C  
ANISOU 7932  C5   DC P 113     4258   5684   4785    399   -181   -157       C  
ATOM   7933  C6   DC P 113       8.065   9.562  27.861  1.00 39.99           C  
ANISOU 7933  C6   DC P 113     4434   5829   4931    383   -211   -178       C  
ATOM   7934  P    DG P 114       8.631  14.496  23.726  1.00 39.82           P  
ANISOU 7934  P    DG P 114     4530   5718   4882    222   -354   -234       P  
ATOM   7935  OP1  DG P 114       9.394  15.549  23.027  1.00 39.89           O  
ANISOU 7935  OP1  DG P 114     4558   5711   4887    188   -382   -246       O  
ATOM   7936  OP2  DG P 114       7.327  14.793  24.357  1.00 42.21           O  
ANISOU 7936  OP2  DG P 114     4822   6030   5185    255   -378   -226       O  
ATOM   7937  O5'  DG P 114       8.394  13.302  22.691  1.00 35.46           O  
ANISOU 7937  O5'  DG P 114     3988   5156   4329    178   -317   -225       O  
ATOM   7938  C5'  DG P 114       9.543  12.641  22.194  1.00 39.88           C  
ANISOU 7938  C5'  DG P 114     4551   5711   4892    150   -282   -234       C  
ATOM   7939  C4'  DG P 114       9.187  11.779  21.006  1.00 41.26           C  
ANISOU 7939  C4'  DG P 114     4738   5873   5064     99   -255   -229       C  
ATOM   7940  O4'  DG P 114       8.818  10.460  21.481  1.00 42.53           O  
ANISOU 7940  O4'  DG P 114     4880   6043   5238    122   -216   -220       O  
ATOM   7941  C3'  DG P 114       8.017  12.278  20.177  1.00 42.22           C  
ANISOU 7941  C3'  DG P 114     4879   5986   5176     68   -284   -219       C  
ATOM   7942  O3'  DG P 114       8.366  12.074  18.808  1.00 43.64           O  
ANISOU 7942  O3'  DG P 114     5079   6154   5347      2   -272   -225       O  
ATOM   7943  C2'  DG P 114       6.824  11.451  20.682  1.00 40.12           C  
ANISOU 7943  C2'  DG P 114     4599   5729   4916     98   -270   -203       C  
ATOM   7944  C1'  DG P 114       7.484  10.151  21.139  1.00 39.31           C  
ANISOU 7944  C1'  DG P 114     4476   5633   4827    114   -220   -205       C  
ATOM   7945  N9   DG P 114       6.898   9.503  22.314  1.00 37.03           N  
ANISOU 7945  N9   DG P 114     4161   5360   4548    168   -207   -192       N  
ATOM   7946  C8   DG P 114       6.492  10.078  23.496  1.00 34.26           C  
ANISOU 7946  C8   DG P 114     3796   5027   4195    221   -232   -187       C  
ATOM   7947  N7   DG P 114       6.014   9.215  24.355  1.00 36.34           N  
ANISOU 7947  N7   DG P 114     4035   5306   4466    258   -211   -173       N  
ATOM   7948  C5   DG P 114       6.116   7.985  23.703  1.00 36.80           C  
ANISOU 7948  C5   DG P 114     4092   5353   4536    230   -171   -168       C  
ATOM   7949  C6   DG P 114       5.761   6.669  24.115  1.00 35.49           C  
ANISOU 7949  C6   DG P 114     3905   5194   4385    247   -135   -153       C  
ATOM   7950  O6   DG P 114       5.257   6.309  25.186  1.00 32.82           O  
ANISOU 7950  O6   DG P 114     3544   4875   4051    292   -132   -137       O  
ATOM   7951  N1   DG P 114       6.034   5.712  23.134  1.00 32.95           N  
ANISOU 7951  N1   DG P 114     3589   4855   4077    205   -100   -157       N  
ATOM   7952  C2   DG P 114       6.578   5.989  21.903  1.00 32.92           C  
ANISOU 7952  C2   DG P 114     3608   4833   4068    151    -98   -175       C  
ATOM   7953  N2   DG P 114       6.785   4.954  21.072  1.00 31.16           N  
ANISOU 7953  N2   DG P 114     3385   4596   3859    114    -60   -182       N  
ATOM   7954  N3   DG P 114       6.910   7.209  21.510  1.00 34.94           N  
ANISOU 7954  N3   DG P 114     3885   5085   4306    133   -132   -187       N  
ATOM   7955  C4   DG P 114       6.658   8.153  22.448  1.00 35.23           C  
ANISOU 7955  C4   DG P 114     3917   5135   4334    175   -167   -182       C  
HETATM 7956  P   2DA P 115       7.401  12.485  17.595  1.00 45.11           P  
ANISOU 7956  P   2DA P 115     5289   6331   5519    -50   -297   -214       P  
HETATM 7957  OP1 2DA P 115       8.200  12.286  16.321  1.00 45.80           O  
ANISOU 7957  OP1 2DA P 115     5394   6413   5595   -117   -278   -226       O  
HETATM 7958  OP2 2DA P 115       6.786  13.830  17.870  1.00 40.25           O  
ANISOU 7958  OP2 2DA P 115     4680   5711   4902    -34   -353   -204       O  
HETATM 7959  O5' 2DA P 115       6.226  11.381  17.705  1.00 43.04           O  
ANISOU 7959  O5' 2DA P 115     5017   6073   5263    -37   -272   -200       O  
HETATM 7960  C5' 2DA P 115       6.001  10.463  16.647  1.00 42.21           C  
ANISOU 7960  C5' 2DA P 115     4920   5965   5154    -87   -241   -202       C  
HETATM 7961  C4' 2DA P 115       5.425   9.138  17.138  1.00 40.10           C  
ANISOU 7961  C4' 2DA P 115     4633   5702   4901    -59   -202   -196       C  
HETATM 7962  O4' 2DA P 115       5.482   8.931  18.555  1.00 36.59           O  
ANISOU 7962  O4' 2DA P 115     4164   5267   4471      8   -197   -191       O  
HETATM 7963  C3' 2DA P 115       3.956   9.064  16.762  1.00 37.82           C  
ANISOU 7963  C3' 2DA P 115     4351   5412   4607    -68   -218   -178       C  
HETATM 7964  C2' 2DA P 115       3.340   8.236  17.871  1.00 40.29           C  
ANISOU 7964  C2' 2DA P 115     4638   5733   4936    -12   -198   -167       C  
HETATM 7965  C1' 2DA P 115       4.467   7.975  18.854  1.00 36.72           C  
ANISOU 7965  C1' 2DA P 115     4167   5289   4498     28   -177   -176       C  
HETATM 7966  N9  2DA P 115       3.927   8.069  20.232  1.00 36.46           N  
ANISOU 7966  N9  2DA P 115     4113   5269   4471     93   -189   -164       N  
HETATM 7967  C8  2DA P 115       3.778   9.178  20.983  1.00 33.76           C  
ANISOU 7967  C8  2DA P 115     3770   4935   4124    127   -229   -162       C  
HETATM 7968  N7  2DA P 115       3.244   8.835  22.177  1.00 32.11           N  
ANISOU 7968  N7  2DA P 115     3536   4742   3921    182   -224   -152       N  
HETATM 7969  C5  2DA P 115       3.055   7.495  22.159  1.00 34.72           C  
ANISOU 7969  C5  2DA P 115     3854   5074   4263    181   -183   -143       C  
HETATM 7970  C6  2DA P 115       2.554   6.579  23.080  1.00 33.45           C  
ANISOU 7970  C6  2DA P 115     3669   4929   4114    221   -161   -127       C  
HETATM 7971  N6  2DA P 115       2.124   7.011  24.286  1.00 27.06           N  
ANISOU 7971  N6  2DA P 115     2841   4139   3299    273   -181   -120       N  
HETATM 7972  N1  2DA P 115       2.501   5.257  22.754  1.00 33.55           N  
ANISOU 7972  N1  2DA P 115     3672   4935   4141    207   -120   -121       N  
HETATM 7973  C2  2DA P 115       2.927   4.829  21.551  1.00 31.88           C  
ANISOU 7973  C2  2DA P 115     3476   4705   3934    155    -99   -133       C  
HETATM 7974  N3  2DA P 115       3.418   5.696  20.648  1.00 30.00           N  
ANISOU 7974  N3  2DA P 115     3262   4456   3681    114   -118   -149       N  
HETATM 7975  C4  2DA P 115       3.489   7.020  20.929  1.00 33.21           C  
ANISOU 7975  C4  2DA P 115     3679   4867   4073    126   -161   -152       C  
TER    7976      2DA P 115                                                      
HETATM 7977  N1  DCP A 904      -0.062   5.974  19.226  1.00 36.59           N  
ANISOU 7977  N1  DCP A 904     4128   5281   4494     70   -163   -118       N  
HETATM 7978  C2  DCP A 904      -0.445   5.138  20.270  1.00 35.46           C  
ANISOU 7978  C2  DCP A 904     3959   5150   4365    118   -142   -106       C  
HETATM 7979  N3  DCP A 904      -0.692   5.667  21.520  1.00 35.64           N  
ANISOU 7979  N3  DCP A 904     3965   5189   4386    173   -163    -98       N  
HETATM 7980  C4  DCP A 904      -0.512   7.017  21.751  1.00 35.12           C  
ANISOU 7980  C4  DCP A 904     3909   5125   4309    182   -205   -106       C  
HETATM 7981  C5  DCP A 904      -0.200   7.871  20.697  1.00 34.97           C  
ANISOU 7981  C5  DCP A 904     3917   5091   4280    136   -229   -116       C  
HETATM 7982  C6  DCP A 904       0.136   7.318  19.463  1.00 33.65           C  
ANISOU 7982  C6  DCP A 904     3765   4909   4110     80   -206   -122       C  
HETATM 7983  O2  DCP A 904      -0.570   3.925  20.101  1.00 36.25           O  
ANISOU 7983  O2  DCP A 904     4047   5246   4479    110   -104   -101       O  
HETATM 7984  N4  DCP A 904      -0.636   7.483  22.985  1.00 36.88           N  
ANISOU 7984  N4  DCP A 904     4114   5368   4532    235   -222   -104       N  
HETATM 7985  C1' DCP A 904      -0.138   5.463  17.840  1.00 37.32           C  
ANISOU 7985  C1' DCP A 904     4237   5360   4582      7   -145   -125       C  
HETATM 7986  C2' DCP A 904      -1.577   5.563  17.345  1.00 34.43           C  
ANISOU 7986  C2' DCP A 904     3881   4992   4208     -8   -165   -109       C  
HETATM 7987  C3' DCP A 904      -1.561   6.736  16.403  1.00 34.09           C  
ANISOU 7987  C3' DCP A 904     3866   4942   4146    -53   -205   -112       C  
HETATM 7988  C4' DCP A 904      -0.126   6.750  15.908  1.00 36.14           C  
ANISOU 7988  C4' DCP A 904     4132   5198   4401    -85   -187   -133       C  
HETATM 7989  O4' DCP A 904       0.658   6.228  16.959  1.00 38.57           O  
ANISOU 7989  O4' DCP A 904     4418   5512   4726    -39   -160   -139       O  
HETATM 7990  O3' DCP A 904      -2.514   6.559  15.378  1.00 38.53           O  
ANISOU 7990  O3' DCP A 904     4442   5497   4699    -97   -210   -104       O  
HETATM 7991  C5' DCP A 904       0.388   8.139  15.581  1.00 37.58           C  
ANISOU 7991  C5' DCP A 904     4333   5376   4569   -104   -229   -137       C  
HETATM 7992  O5' DCP A 904       0.122   9.047  16.626  1.00 40.50           O  
ANISOU 7992  O5' DCP A 904     4695   5750   4944    -52   -265   -129       O  
HETATM 7993  PA  DCP A 904      -0.042  10.616  16.287  1.00 39.63           P  
ANISOU 7993  PA  DCP A 904     4602   5631   4823    -68   -325   -125       P  
HETATM 7994  O1A DCP A 904       0.575  11.403  17.411  1.00 41.52           O  
ANISOU 7994  O1A DCP A 904     4830   5875   5071    -18   -344   -132       O  
HETATM 7995  O2A DCP A 904       0.577  11.000  14.961  1.00 48.67           O  
ANISOU 7995  O2A DCP A 904     5772   6769   5953   -138   -332   -130       O  
HETATM 7996  O3A DCP A 904      -1.626  10.916  16.224  1.00 40.67           O  
ANISOU 7996  O3A DCP A 904     4737   5759   4958    -62   -356   -105       O  
HETATM 7997  PB  DCP A 904      -2.705  10.172  15.287  1.00 35.96           P  
ANISOU 7997  PB  DCP A 904     4148   5158   4355   -102   -344    -91       P  
HETATM 7998  O1B DCP A 904      -3.324   9.008  16.013  1.00 36.70           O  
ANISOU 7998  O1B DCP A 904     4222   5261   4460    -62   -309    -87       O  
HETATM 7999  O2B DCP A 904      -2.134   9.735  13.955  1.00 35.71           O  
ANISOU 7999  O2B DCP A 904     4134   5125   4307   -172   -323    -99       O  
HETATM 8000  O3B DCP A 904      -3.819  11.302  15.132  1.00 37.21           O  
ANISOU 8000  O3B DCP A 904     4315   5308   4516   -103   -402    -74       O  
HETATM 8001  PG  DCP A 904      -3.507  12.695  14.396  1.00 37.00           P  
ANISOU 8001  PG  DCP A 904     4308   5269   4483   -143   -454    -70       P  
HETATM 8002  O1G DCP A 904      -2.177  12.618  13.691  1.00 37.87           O  
ANISOU 8002  O1G DCP A 904     4431   5381   4577   -187   -434    -83       O  
HETATM 8003  O2G DCP A 904      -4.598  12.932  13.397  1.00 34.84           O  
ANISOU 8003  O2G DCP A 904     4049   4986   4204   -187   -482    -49       O  
HETATM 8004  O3G DCP A 904      -3.451  13.806  15.417  1.00 40.83           O  
ANISOU 8004  O3G DCP A 904     4781   5749   4983    -92   -492    -73       O  
HETATM 8005 CA    CA A 905      -0.758  11.095  12.700  1.00 38.29          CA  
HETATM 8006 CA    CA A 906       2.767  11.712  14.006  1.00 63.47          CA  
HETATM 8007 CA    CA A 907      -3.496  48.538  12.629  1.00 63.30          CA  
HETATM 8008 CA    CA A 908      -2.911  15.977  10.160  1.00 72.21          CA  
HETATM 8009 CA    CA A 909      -3.394  24.437  52.322  1.00 67.85          CA  
HETATM 8010  O   HOH A 910      13.028  20.680  52.343  1.00 36.71           O  
HETATM 8011  O   HOH A 911     -10.780  -8.458  19.626  1.00 18.52           O  
HETATM 8012  O   HOH A 912     -15.166  21.841  32.638  1.00 19.73           O  
HETATM 8013  O   HOH A 913       9.886  -1.355  15.574  1.00 17.60           O  
HETATM 8014  O   HOH A 914     -29.306  -6.826  33.136  1.00 25.53           O  
HETATM 8015  O   HOH A 915      -7.968   4.929  56.130  1.00 44.21           O  
HETATM 8016  O   HOH A 916      28.155  34.508  39.604  1.00 45.27           O  
HETATM 8017  O   HOH A 917      -7.065 -11.668  32.949  1.00 41.12           O  
HETATM 8018  O   HOH A 918      -5.848  33.486  41.826  1.00 33.21           O  
HETATM 8019  O   HOH A 919      -4.893   2.475   1.890  1.00 21.19           O  
HETATM 8020  O   HOH A 920       4.145  -4.480  14.753  1.00 27.97           O  
HETATM 8021  O   HOH A 921     -10.266  11.010  41.552  1.00 32.08           O  
HETATM 8022  O   HOH A 922      11.157  22.415  57.811  1.00 43.50           O  
HETATM 8023  O   HOH A 923       9.251  28.474  19.608  1.00 26.71           O  
HETATM 8024  O   HOH A 924      -9.780   5.722  63.294  1.00 37.81           O  
HETATM 8025  O   HOH A 925     -22.064   6.976  39.685  1.00 19.23           O  
HETATM 8026  O   HOH A 926      -5.507  10.757  43.787  1.00 51.20           O  
HETATM 8027  O   HOH A 927     -22.039  21.153  47.238  1.00 12.46           O  
HETATM 8028  O   HOH A 928     -25.023  20.557  29.597  1.00 32.28           O  
HETATM 8029  O   HOH A 929      32.434  22.629  19.695  1.00 39.32           O  
HETATM 8030  O   HOH A 930     -19.112 -22.195  27.040  1.00 31.54           O  
HETATM 8031  O   HOH A 931     -26.077   6.658  43.338  1.00 20.16           O  
HETATM 8032  O   HOH A 932     -16.989   1.455  56.173  1.00 56.79           O  
HETATM 8033  O   HOH A 933     -16.213  39.134  57.039  1.00 26.56           O  
HETATM 8034  O   HOH A 934     -14.534   0.790  46.833  1.00 35.70           O  
HETATM 8035  O   HOH A 935      30.745  15.512  20.583  1.00 53.53           O  
HETATM 8036  O   HOH A 936      21.307   1.048 -11.398  1.00 31.54           O  
HETATM 8037  O   HOH A 937      29.246  32.045  36.504  1.00 44.39           O  
HETATM 8038  O   HOH A 938       7.196  14.977  47.533  1.00 41.74           O  
HETATM 8039  O   HOH A 939      31.391  29.947  22.304  1.00 30.88           O  
HETATM 8040  O   HOH A 940     -17.612  39.686  43.525  1.00 43.11           O  
HETATM 8041  O   HOH A 941     -10.014   7.158  11.862  1.00 27.28           O  
HETATM 8042  O   HOH A 942      -5.821   8.739  16.524  1.00 27.43           O  
HETATM 8043  O   HOH A 943      14.501   6.755   2.927  1.00 23.54           O  
HETATM 8044  O   HOH A 944       5.298  31.351   8.892  1.00 20.63           O  
HETATM 8045  O   HOH A 945     -15.887   3.212  58.041  1.00 39.49           O  
HETATM 8046  O   HOH A 946      -4.960   7.833   7.813  1.00 19.77           O  
HETATM 8047  O   HOH A 947     -24.479  11.415  25.452  1.00 23.80           O  
HETATM 8048  O   HOH A 948      13.047   1.551   6.240  1.00 36.86           O  
HETATM 8049  O   HOH A 949      -1.430  26.742  61.126  1.00 21.06           O  
HETATM 8050  O   HOH A 950     -18.425  -4.826  26.198  1.00 26.73           O  
HETATM 8051  O   HOH A 951      -0.838  22.032  46.814  1.00 24.00           O  
HETATM 8052  O   HOH A 952      31.128  22.725  33.519  1.00 49.51           O  
HETATM 8053  O   HOH A 953     -33.311 -15.924  40.798  1.00 27.95           O  
HETATM 8054  O   HOH A 954     -19.981  11.023  15.558  1.00 30.93           O  
HETATM 8055  O   HOH A 955     -28.709  17.012  48.669  1.00 35.59           O  
HETATM 8056  O   HOH A 956      10.142  10.391  16.635  1.00 28.73           O  
HETATM 8057  O   HOH A 957       0.718  16.153  34.252  1.00 21.94           O  
HETATM 8058  O   HOH A 958      20.698  20.615  -5.532  1.00 33.90           O  
HETATM 8059  O   HOH A 959     -29.857  19.403  43.384  1.00 27.30           O  
HETATM 8060  O   HOH A 960      18.924   6.539  17.406  1.00 29.88           O  
HETATM 8061  O   HOH A 961     -23.162  23.206  37.754  1.00 27.83           O  
HETATM 8062  O   HOH A 962     -37.823   8.192  36.142  1.00 36.95           O  
HETATM 8063  O   HOH A 963      20.948   7.535  14.185  1.00 26.14           O  
HETATM 8064  O   HOH A 964      -5.933  27.980  73.123  1.00 32.16           O  
HETATM 8065  O   HOH A 965      -2.758   9.352   1.578  1.00 23.77           O  
HETATM 8066  O   HOH A 966     -38.941  16.335  42.937  1.00 45.63           O  
HETATM 8067  O   HOH A 967      -6.472   9.247  -0.865  1.00 37.37           O  
HETATM 8068  O   HOH A 968     -18.861   2.852  35.443  1.00 20.46           O  
HETATM 8069  O   HOH A 969     -22.872   4.169  25.440  1.00 22.56           O  
HETATM 8070  O   HOH A 970       7.394  -8.556  20.805  1.00 38.92           O  
HETATM 8071  O   HOH A 971      20.850   6.505  38.683  1.00 32.87           O  
HETATM 8072  O   HOH A 972     -33.615  19.593  42.878  1.00 31.05           O  
HETATM 8073  O   HOH A 973     -21.447 -22.359  25.950  1.00 25.12           O  
HETATM 8074  O   HOH A 974     -19.719 -13.990  40.193  1.00 35.05           O  
HETATM 8075  O   HOH A 975      -3.991   5.603  53.702  1.00 37.08           O  
HETATM 8076  O   HOH A 976      -5.531  21.590  63.694  1.00 24.20           O  
HETATM 8077  O   HOH A 977       8.878  26.776  49.448  1.00 42.00           O  
HETATM 8078  O   HOH A 978      15.838   5.414  -3.302  1.00 35.78           O  
HETATM 8079  O   HOH A 979      27.593  31.889  11.639  1.00 35.96           O  
HETATM 8080  O   HOH A 980     -20.393 -12.545  22.350  1.00 28.86           O  
HETATM 8081  O   HOH A 981       4.615  -9.702   7.290  1.00 36.66           O  
HETATM 8082  O   HOH A 982      16.145   2.076   9.946  1.00 20.05           O  
HETATM 8083  O   HOH A 983     -20.036   4.476  12.850  1.00 26.14           O  
HETATM 8084  O   HOH A 984     -18.711   5.183  19.918  1.00 26.26           O  
HETATM 8085  O   HOH A 985     -21.199  -1.674   7.478  1.00 36.66           O  
HETATM 8086  O   HOH A 986      14.589  21.903   8.404  1.00 33.88           O  
HETATM 8087  O   HOH A 987      -7.578  20.319  51.069  1.00 34.51           O  
HETATM 8088  O   HOH A 988       2.460   0.715  18.511  1.00 27.36           O  
HETATM 8089  O   HOH A 989      -2.341  12.781  52.173  1.00 32.72           O  
HETATM 8090  O   HOH A 990     -18.373 -17.914  35.220  1.00 33.89           O  
HETATM 8091  O   HOH A 991     -25.489 -21.462  20.799  1.00 29.64           O  
HETATM 8092  O   HOH A 992     -26.965  13.573  51.448  1.00 26.79           O  
HETATM 8093  O   HOH A 993      -4.292 -13.089  22.553  1.00 33.21           O  
HETATM 8094  O   HOH A 994      14.927  30.752  22.712  1.00 28.36           O  
HETATM 8095  O   HOH A 995      12.018  26.201  30.743  1.00 24.61           O  
HETATM 8096  O   HOH A 996     -15.079 -13.978  14.023  1.00 30.30           O  
HETATM 8097  O   HOH A 997      -2.822   8.436  56.182  1.00 44.46           O  
HETATM 8098  O   HOH A 998      -5.049  22.550  52.385  1.00 36.18           O  
HETATM 8099  O   HOH A 999      -0.437  42.704  43.027  1.00 63.92           O  
HETATM 8100  O   HOH A1000      -3.133  -6.169  -5.598  1.00 35.14           O  
HETATM 8101  O   HOH A1001     -31.596  -6.869  24.122  1.00 26.48           O  
HETATM 8102  O   HOH A1002     -27.851  24.318  29.848  1.00 40.03           O  
HETATM 8103  O   HOH A1003      12.037   1.022  -4.926  1.00 18.33           O  
HETATM 8104  O   HOH A1004       4.126  34.612  38.219  1.00 45.62           O  
HETATM 8105  O   HOH A1005     -12.614   8.049  42.252  1.00 32.93           O  
HETATM 8106  O  AHOH A1006      -8.546 -15.963   1.293  0.50  2.57           O  
HETATM 8107  O  BHOH A1006      -6.117 -16.125   1.743  0.50  9.08           O  
HETATM 8108  O   HOH A1007      -2.123  -6.634  29.902  1.00 21.43           O  
HETATM 8109  O   HOH A1008     -10.112  27.683  27.570  1.00 23.37           O  
HETATM 8110  O   HOH A1009      10.312  22.965  51.868  1.00 35.64           O  
HETATM 8111  O   HOH A1010     -44.239  16.121  35.538  1.00 29.26           O  
HETATM 8112  O   HOH A1011      23.641  16.523  38.906  1.00 34.09           O  
HETATM 8113  O   HOH A1012      -6.389  36.311  64.853  1.00 22.46           O  
HETATM 8114  O   HOH A1013      -4.067  -1.934  53.560  1.00 44.16           O  
HETATM 8115  O   HOH A1014       8.939  35.967   4.545  1.00 27.66           O  
HETATM 8116  O   HOH A1015     -22.836   4.789  21.271  1.00 31.37           O  
HETATM 8117  O   HOH A1016     -42.677  14.874  41.442  1.00 41.21           O  
HETATM 8118  O   HOH A1017      20.090  19.607   4.241  1.00 34.63           O  
HETATM 8119  O   HOH A1018     -12.980 -18.586   4.466  1.00 36.68           O  
HETATM 8120  O   HOH A1019     -17.878 -19.312  33.044  1.00 27.61           O  
HETATM 8121  O   HOH A1020      20.434  30.370  44.433  1.00 20.14           O  
HETATM 8122  O   HOH A1021      -4.442  10.519  36.192  1.00 30.40           O  
HETATM 8123  O   HOH A1022      -9.158  28.669  61.505  1.00 25.60           O  
HETATM 8124  O   HOH A1023      16.955  31.616  36.958  1.00 43.83           O  
HETATM 8125  O   HOH A1024       9.342  25.410  42.298  1.00 28.15           O  
HETATM 8126  O   HOH A1025     -26.713  -7.853  33.573  1.00 29.88           O  
HETATM 8127  O   HOH A1026     -27.220  17.791  41.000  1.00 29.97           O  
HETATM 8128  O   HOH A1027     -13.535  -4.853  29.406  1.00 41.84           O  
HETATM 8129  O   HOH A1028     -13.296  25.118  20.949  1.00 29.94           O  
HETATM 8130  O   HOH A1029      16.833  18.396   4.204  1.00 26.75           O  
HETATM 8131  O   HOH A1030      15.970  29.696   3.336  1.00 30.94           O  
HETATM 8132  O   HOH A1031     -40.610  16.810  38.993  1.00 27.51           O  
HETATM 8133  O   HOH A1032       3.510  17.213  45.824  1.00 27.43           O  
HETATM 8134  O   HOH A1033       4.322 -14.416  -0.976  1.00 33.23           O  
HETATM 8135  O   HOH A1034     -23.053  -3.241  39.570  1.00 38.85           O  
HETATM 8136  O   HOH A1035     -10.024  -9.396  -4.351  1.00 24.49           O  
HETATM 8137  O   HOH A1036      -1.755   0.415  20.843  1.00 22.23           O  
HETATM 8138  O   HOH A1037      -1.292 -14.555  11.746  1.00 32.76           O  
HETATM 8139  O   HOH A1038     -20.587   7.106  42.140  1.00 32.93           O  
HETATM 8140  O   HOH A1039       0.773  33.222  67.967  1.00 50.54           O  
HETATM 8141  O   HOH A1040      18.437   9.833   7.535  1.00 23.79           O  
HETATM 8142  O   HOH A1041     -21.715   8.298  64.833  1.00 34.71           O  
HETATM 8143  O   HOH A1042      19.373  31.608   2.719  1.00 37.80           O  
HETATM 8144  O   HOH A1043      14.501  29.466  33.730  1.00 37.74           O  
HETATM 8145  O   HOH A1044      10.968   1.311   3.067  1.00 28.62           O  
HETATM 8146  O   HOH A1045      -4.217  51.577  51.974  1.00 34.51           O  
HETATM 8147  O   HOH A1046       5.979  17.248  11.697  1.00 32.24           O  
HETATM 8148  O   HOH A1047      30.281  16.947  42.858  1.00 35.28           O  
HETATM 8149  O   HOH A1048      23.471  24.697  58.988  1.00 33.04           O  
HETATM 8150  O   HOH A1049      -5.066  -9.321  -0.210  1.00 32.50           O  
HETATM 8151  O   HOH A1050     -13.917  25.847  11.868  1.00 30.63           O  
HETATM 8152  O   HOH A1051       4.997  27.024  37.878  1.00 42.43           O  
HETATM 8153  O   HOH A1052       4.739  14.972  42.778  1.00 43.02           O  
HETATM 8154  O   HOH A1053       4.451   4.230  18.309  1.00 20.03           O  
HETATM 8155  O   HOH A1054      -3.757  33.048  10.165  1.00 20.75           O  
HETATM 8156  O   HOH A1055      18.199  20.209  -7.000  1.00 26.80           O  
HETATM 8157  O   HOH A1056      -6.816  18.316  49.348  1.00 23.69           O  
HETATM 8158  O   HOH A1057      21.611  23.488   7.063  1.00 25.52           O  
HETATM 8159  O   HOH A1058       1.367 -13.264   1.220  1.00 25.05           O  
HETATM 8160  O   HOH A1059     -14.113  38.554  21.712  1.00 25.49           O  
HETATM 8161  O   HOH A1060      -3.066  46.309  13.120  1.00 33.97           O  
HETATM 8162  O   HOH A1061      18.249  16.572  62.794  1.00 51.10           O  
HETATM 8163  O   HOH A1062     -39.843  12.369  35.820  1.00 47.72           O  
HETATM 8164  O   HOH A1063     -34.463 -15.962  25.658  1.00 21.21           O  
HETATM 8165  O   HOH A1064       5.191 -22.697   3.858  1.00 25.90           O  
HETATM 8166  O   HOH A1065      31.747  24.744  41.509  1.00 31.72           O  
HETATM 8167  O   HOH A1066     -24.706  17.346  61.746  1.00 31.47           O  
HETATM 8168  O   HOH A1067       3.587  30.808  59.539  1.00 23.63           O  
HETATM 8169  O   HOH A1068      -1.878  18.272   8.198  1.00 41.88           O  
HETATM 8170  O   HOH A1069       1.818  14.310  42.734  1.00 32.54           O  
HETATM 8171  O   HOH A1070      -8.847 -17.156  25.369  1.00 42.61           O  
HETATM 8172  O   HOH A1071      -0.562  -9.150  26.951  1.00 28.98           O  
HETATM 8173  O   HOH A1072       9.207  19.364  30.283  1.00 22.27           O  
HETATM 8174  O   HOH A1073      -3.286  27.582  65.090  1.00 31.41           O  
HETATM 8175  O   HOH A1074       5.157  20.181 -11.819  1.00 42.24           O  
HETATM 8176  O   HOH A1075      -0.795  23.607  13.635  1.00 25.03           O  
HETATM 8177  O   HOH A1076      40.368  25.406  18.582  1.00 42.29           O  
HETATM 8178  O   HOH A1077      49.114  34.184  12.393  1.00 22.96           O  
HETATM 8179  O   HOH A1078     -20.557   1.119  54.928  1.00 37.08           O  
HETATM 8180  O   HOH A1079     -14.624  42.463  40.171  1.00 38.35           O  
HETATM 8181  O   HOH A1080       0.780  30.484  41.725  1.00 61.28           O  
HETATM 8182  O   HOH A1081     -33.045  24.935  33.174  1.00 37.81           O  
HETATM 8183  O   HOH A1082      13.656   5.235  -4.850  1.00 32.42           O  
HETATM 8184  O   HOH A1083      21.032   9.290  -1.001  1.00 42.80           O  
HETATM 8185  O   HOH A1084      21.482  17.292   5.136  1.00 28.31           O  
HETATM 8186  O   HOH A1085     -21.613  27.849  38.485  1.00 40.44           O  
HETATM 8187  O   HOH A1086      -4.545 -16.784  32.627  1.00 41.31           O  
HETATM 8188  O   HOH A1087      -0.618  16.313   9.495  1.00 67.93           O  
HETATM 8189  O   HOH A1088       3.999  27.637  29.442  1.00 35.99           O  
HETATM 8190  O   HOH A1089     -21.710  30.893  61.477  1.00 37.42           O  
HETATM 8191  O   HOH A1090       7.025  12.201  13.895  1.00 33.34           O  
HETATM 8192  O   HOH A1091      14.841  23.243  37.517  1.00 20.97           O  
HETATM 8193  O   HOH A1092      12.423  22.155  37.133  1.00 14.07           O  
HETATM 8194  O   HOH A1093      12.301  20.659  34.872  1.00  8.87           O  
HETATM 8195  O   HOH A1094      -4.967  14.567   1.198  1.00 23.82           O  
HETATM 8196  O   HOH A1095      -4.267  18.494  -5.697  1.00 36.21           O  
HETATM 8197  O   HOH A1096       0.796  21.551   1.981  1.00 29.30           O  
HETATM 8198  O   HOH A1097       4.600   1.964  12.433  1.00 21.10           O  
HETATM 8199  O   HOH A1098       2.540   0.567  13.660  1.00 25.12           O  
HETATM 8200  O   HOH A1099      13.544  -1.503  13.226  1.00 29.25           O  
HETATM 8201  O   HOH A1100      14.966   0.824  12.568  1.00 39.63           O  
HETATM 8202  O   HOH A1101      22.698   4.162  16.832  1.00 46.57           O  
HETATM 8203  O   HOH A1102     -16.938  32.645  40.319  1.00 36.80           O  
HETATM 8204  O   HOH A1103     -15.877  30.756  39.165  1.00 31.30           O  
HETATM 8205  O   HOH A1104     -13.972  30.812  36.980  1.00 33.60           O  
HETATM 8206  O   HOH A1105      -9.526  30.754  33.904  1.00 30.70           O  
HETATM 8207  O   HOH A1106     -20.440  35.465  19.331  1.00 36.35           O  
HETATM 8208  O   HOH A1107     -19.803  33.144  20.622  1.00 34.92           O  
HETATM 8209  O   HOH A1108     -11.683  -2.921  -2.065  1.00 29.62           O  
HETATM 8210  O   HOH A1109     -16.116  -5.131  -0.637  1.00 27.33           O  
HETATM 8211  O   HOH A1110      -3.407  13.215  61.560  1.00 23.52           O  
HETATM 8212  O   HOH A1111     -18.924  22.265  33.612  1.00 34.26           O  
HETATM 8213  O   HOH A1112      15.777  11.557  24.044  1.00 24.66           O  
HETATM 8214  O   HOH A1113      23.632  12.531  -3.051  1.00 27.36           O  
HETATM 8215  O   HOH A1114     -29.428  19.738  56.708  1.00 44.28           O  
HETATM 8216  O   HOH A1115     -14.291  22.698  21.084  1.00 19.55           O  
HETATM 8217  O   HOH A1116     -17.307  23.798  20.869  1.00 27.14           O  
HETATM 8218  O   HOH A1117     -19.922  19.722  26.038  1.00 38.96           O  
HETATM 8219  O   HOH A1118     -20.124  18.612  21.413  1.00 31.62           O  
HETATM 8220  O   HOH A1119     -20.275  15.106  23.682  1.00 43.13           O  
HETATM 8221  O   HOH A1120     -13.850  19.620  27.323  1.00 21.44           O  
HETATM 8222  O   HOH A1121     -13.382  21.818  25.843  1.00 25.14           O  
HETATM 8223  O   HOH A1122     -15.071  22.070  24.041  1.00 28.40           O  
HETATM 8224  O   HOH A1123      18.522  12.789  39.252  1.00 28.44           O  
HETATM 8225  O   HOH A1124      -3.050   2.684  20.101  1.00 30.10           O  
HETATM 8226  O   HOH A1125      -3.220   9.433  21.762  1.00 21.75           O  
HETATM 8227  O   HOH A1126     -32.522  11.736  23.048  1.00 36.52           O  
HETATM 8228  O   HOH A1127      -6.779   6.857  28.097  1.00 27.60           O  
HETATM 8229  O   HOH A1128      -1.018  27.906  63.452  1.00 23.16           O  
HETATM 8230  O  AHOH A1129      -9.858 -14.604  21.926  0.50 12.79           O  
HETATM 8231  O  BHOH A1129     -11.726 -15.028  21.274  0.50 21.59           O  
HETATM 8232  O   HOH A1130     -11.227 -11.231  19.575  1.00 28.64           O  
HETATM 8233  O   HOH A1131     -19.202 -14.976  23.200  1.00 31.24           O  
HETATM 8234  O   HOH A1132     -15.350 -21.539  29.400  1.00 36.08           O  
HETATM 8235  O   HOH A1133     -15.826  -5.166  36.779  1.00 42.06           O  
HETATM 8236  O   HOH A1134     -17.722  -6.330  38.288  1.00 44.16           O  
HETATM 8237  O   HOH A1135     -11.624  -9.070  43.420  1.00 45.85           O  
HETATM 8238  O   HOH A1136      -5.057  30.960  19.449  1.00 21.06           O  
HETATM 8239  O   HOH A1137     -21.700   9.286  38.016  1.00 23.19           O  
HETATM 8240  O   HOH A1138     -11.236 -12.460  34.562  1.00 41.80           O  
HETATM 8241  O   HOH A1139     -11.251   0.317  61.648  1.00 48.62           O  
HETATM 8242  O   HOH A1140     -23.914   1.373  30.307  1.00 23.37           O  
HETATM 8243  O   HOH A1141      -0.876   9.944  23.748  1.00 30.96           O  
HETATM 8244  O   HOH A1142      12.906   3.347  -0.714  1.00 16.37           O  
HETATM 8245  O   HOH A1143     -24.454  -2.561  52.342  1.00 36.58           O  
HETATM 8246  O   HOH A1144      -8.298  32.409  10.344  1.00 21.34           O  
HETATM 8247  O   HOH A1145      -8.187 -15.856  -1.446  1.00 26.72           O  
HETATM 8248  O   HOH A1146     -26.882  18.225  63.277  1.00 30.57           O  
HETATM 8249  O   HOH A1147     -27.552 -17.224  45.974  1.00 31.27           O  
HETATM 8250  O   HOH A1148     -32.288 -15.473  46.596  1.00 41.11           O  
HETATM 8251  O   HOH A1149      -5.635 -18.057   3.612  1.00 20.02           O  
HETATM 8252  O   HOH A1150      30.825  14.177  48.623  1.00 32.70           O  
HETATM 8253  O   HOH A1151     -43.023 -12.914  40.108  1.00 48.29           O  
HETATM 8254  O   HOH A1152      -4.794  18.701  26.833  1.00 22.77           O  
HETATM 8255  O   HOH A1153     -19.029   0.714  36.935  1.00 30.20           O  
HETATM 8256  O   HOH A1154      17.944   2.201  17.233  1.00 35.61           O  
HETATM 8257  O   HOH A1155     -12.918 -12.952  18.574  1.00 26.41           O  
HETATM 8258  O   HOH A1156      -5.415   4.408  31.396  1.00 21.73           O  
HETATM 8259  O   HOH A1157      11.611   0.236  14.742  1.00 22.28           O  
HETATM 8260  O   HOH T  28       4.869   1.699  19.351  1.00 22.65           O  
HETATM 8261  O   HOH T 108      21.078  10.576  19.682  1.00 24.20           O  
HETATM 8262  O   HOH T 169      13.145   7.322  22.673  1.00 29.99           O  
HETATM 8263  O   HOH T 180      17.929  10.412  30.557  1.00 26.90           O  
HETATM 8264  O   HOH T 239       5.184  -5.518  24.715  1.00 29.29           O  
HETATM 8265  O   HOH T 240     -10.019  -1.456  37.552  1.00 36.91           O  
HETATM 8266  O   HOH P  49      10.322  14.675  36.052  1.00 31.69           O  
HETATM 8267  O   HOH P  91      10.402   4.774  36.211  1.00 32.59           O  
HETATM 8268  O   HOH P 125       7.926  17.772  22.838  1.00 31.41           O  
HETATM 8269  O   HOH P 131       4.695  13.703  19.225  1.00 22.91           O  
HETATM 8270  O   HOH P 142       7.475   4.720  18.431  1.00 36.17           O  
HETATM 8271  O   HOH P 158      17.418  -1.619  30.627  1.00 34.22           O  
HETATM 8272  O   HOH P 165      12.903  -0.439  36.170  1.00 39.51           O  
HETATM 8273  O   HOH P 187       9.012   2.204  29.973  1.00 23.45           O  
HETATM 8274  O   HOH P 203      20.417   0.577  27.091  1.00 42.02           O  
CONECT  972 8009                                                                
CONECT  973 8009                                                                
CONECT 3409 8005                                                                
CONECT 3410 8005 8006                                                           
CONECT 3414 8005                                                                
CONECT 4158 8007                                                                
CONECT 4176 8007                                                                
CONECT 4376 8007                                                                
CONECT 5111 8005                                                                
CONECT 5112 8006                                                                
CONECT 7392 7403                                                                
CONECT 7403 7392 7404 7405 7406                                                 
CONECT 7404 7403                                                                
CONECT 7405 7403                                                                
CONECT 7406 7403 7407                                                           
CONECT 7407 7406 7408                                                           
CONECT 7408 7407 7409 7410                                                      
CONECT 7409 7408 7413                                                           
CONECT 7410 7408 7411 7412                                                      
CONECT 7411 7410 7424                                                           
CONECT 7412 7410 7413                                                           
CONECT 7413 7409 7412 7414                                                      
CONECT 7414 7413 7415 7423                                                      
CONECT 7415 7414 7416                                                           
CONECT 7416 7415 7417                                                           
CONECT 7417 7416 7418 7423                                                      
CONECT 7418 7417 7419                                                           
CONECT 7419 7418 7420                                                           
CONECT 7420 7419 7421 7422                                                      
CONECT 7421 7420                                                                
CONECT 7422 7420 7423                                                           
CONECT 7423 7414 7417 7422                                                      
CONECT 7424 7411                                                                
CONECT 7942 7956                                                                
CONECT 7956 7942 7957 7958 7959                                                 
CONECT 7957 7956                                                                
CONECT 7958 7956                                                                
CONECT 7959 7956 7960                                                           
CONECT 7960 7959 7961                                                           
CONECT 7961 7960 7962 7963                                                      
CONECT 7962 7961 7965                                                           
CONECT 7963 7961 7964                                                           
CONECT 7964 7963 7965                                                           
CONECT 7965 7962 7964 7966                                                      
CONECT 7966 7965 7967 7975                                                      
CONECT 7967 7966 7968                                                           
CONECT 7968 7967 7969                                                           
CONECT 7969 7968 7970 7975                                                      
CONECT 7970 7969 7971 7972                                                      
CONECT 7971 7970                                                                
CONECT 7972 7970 7973                                                           
CONECT 7973 7972 7974                                                           
CONECT 7974 7973 7975                                                           
CONECT 7975 7966 7969 7974                                                      
CONECT 7977 7978 7982 7985                                                      
CONECT 7978 7977 7979 7983                                                      
CONECT 7979 7978 7980                                                           
CONECT 7980 7979 7981 7984                                                      
CONECT 7981 7980 7982                                                           
CONECT 7982 7977 7981                                                           
CONECT 7983 7978                                                                
CONECT 7984 7980                                                                
CONECT 7985 7977 7986 7989                                                      
CONECT 7986 7985 7987                                                           
CONECT 7987 7986 7988 7990                                                      
CONECT 7988 7987 7989 7991                                                      
CONECT 7989 7985 7988                                                           
CONECT 7990 7987                                                                
CONECT 7991 7988 7992                                                           
CONECT 7992 7991 7993                                                           
CONECT 7993 7992 7994 7995 7996                                                 
CONECT 7994 7993                                                                
CONECT 7995 7993 8005 8006                                                      
CONECT 7996 7993 7997                                                           
CONECT 7997 7996 7998 7999 8000                                                 
CONECT 7998 7997                                                                
CONECT 7999 7997 8005                                                           
CONECT 8000 7997 8001                                                           
CONECT 8001 8000 8002 8003 8004                                                 
CONECT 8002 8001 8005                                                           
CONECT 8003 8001                                                                
CONECT 8004 8001                                                                
CONECT 8005 3409 3410 3414 5111                                                 
CONECT 8005 7995 7999 8002                                                      
CONECT 8006 3410 5112 7995                                                      
CONECT 8007 4158 4176 4376 8161                                                 
CONECT 8008 8169 8188                                                           
CONECT 8009  972  973 8098                                                      
CONECT 8098 8009                                                                
CONECT 8161 8007                                                                
CONECT 8169 8008                                                                
CONECT 8188 8008                                                                
MASTER      524    0    8   38   36    0   10    6 8254    3   92   73          
END

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Related entries of code: 3sup

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
3sq4	RCSB PDB PDBbind	13aa, >3SQ4_3\|Chain... *
3suo	RCSB PDB PDBbind	13aa, >3SUO_3\|Chain... at 100%
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
No complexes with the same small molecule ligand are found!

Entry Information

PDB ID	3sup
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	RB69 DNA Polymerase (Y567A) mutant
Ligand Name	dCTP Opposite 2AP (GC rich sequence) DNA
EC.Number	E.C.2.7.7.7
Resolution	2.32(Å)
Affinity (Kd/Ki/IC50)	Kd=317uM
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
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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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