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HEADER    TRANSFERASE/DNA                         11-JUL-11   3SUN              
TITLE     RB69 DNA POLYMERASE (Y567A) TERNARY COMPLEX WITH DTTP OPPOSITE 2AP (AT
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*AP*AP*TP*TP*AP*AP*TP*TP*AP*AP*TP*TP*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(*AP*AP*TP*TP*AP*AP*TP*TP*AP*AP*TP*TP*(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, AT RICH, RB69POL, TRANSFERASE-DNA COMPLEX              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.XIA,W.H.KONIGSBERG,J.WANG                                           
REVDAT   3   30-NOV-11 3SUN    1       JRNL                                     
REVDAT   2   16-NOV-11 3SUN    1       JRNL                                     
REVDAT   1   09-NOV-11 3SUN    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.    2.42 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) : 2.42                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 87.72                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 41995                          
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) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2237                            
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) : 2.42                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.48                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2697                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.21                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2890                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 161                          
REMARK   3   BIN FREE R VALUE                    : 0.3410                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7296                                    
REMARK   3   NUCLEIC ACID ATOMS       : 591                                     
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 162                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.33                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.11000                                             
REMARK   3    B22 (A**2) : 0.61000                                              
REMARK   3    B33 (A**2) : -0.51000                                             
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): 0.466         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.277         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.214         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.127        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8183 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11190 ; 1.138 ; 2.057       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   898 ; 5.204 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   371 ;36.287 ;24.124       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1340 ;15.782 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    47 ;15.804 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1185 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6047 ; 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):  4472 ; 1.386 ; 4.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7252 ; 2.455 ; 6.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3711 ; 2.768 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3936 ; 4.124 ; 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   896        A   896                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.4100  -5.6630  38.3000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1551 T22:   0.2403                                     
REMARK   3      T33:   0.1864 T12:  -0.0722                                     
REMARK   3      T13:  -0.0339 T23:   0.0024                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4441 L22:   0.5433                                     
REMARK   3      L33:   0.0127 L12:   0.6370                                     
REMARK   3      L13:   0.1295 L23:   0.0088                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2241 S12:  -0.0177 S13:   0.1868                       
REMARK   3      S21:  -0.0198 S22:   0.1790 S23:  -0.1227                       
REMARK   3      S31:  -0.0160 S32:   0.0069 S33:   0.0450                       
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): -21.5260  -0.5620  36.2510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1318 T22:   0.2089                                     
REMARK   3      T33:   0.0767 T12:   0.1257                                     
REMARK   3      T13:  -0.0297 T23:  -0.0214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1725 L22:   1.7864                                     
REMARK   3      L33:   1.9379 L12:   0.0884                                     
REMARK   3      L13:   0.2359 L23:   1.2489                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0099 S12:   0.0260 S13:  -0.0075                       
REMARK   3      S21:  -0.1454 S22:  -0.1671 S23:   0.1347                       
REMARK   3      S31:  -0.3522 S32:  -0.4139 S33:   0.1770                       
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):  -6.9940 -22.7680  14.2790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1255 T22:   0.1201                                     
REMARK   3      T33:   0.0316 T12:   0.0004                                     
REMARK   3      T13:  -0.0438 T23:  -0.0133                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7755 L22:   1.0327                                     
REMARK   3      L33:   1.5854 L12:  -0.2735                                     
REMARK   3      L13:  -0.0058 L23:   0.0543                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0658 S12:   0.0818 S13:  -0.0305                       
REMARK   3      S21:  -0.1712 S22:  -0.1046 S23:   0.0280                       
REMARK   3      S31:  -0.0665 S32:  -0.0177 S33:   0.0388                       
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):   6.4160 -13.7580  62.1900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1259 T22:   0.1968                                     
REMARK   3      T33:   0.0503 T12:  -0.0358                                     
REMARK   3      T13:  -0.0179 T23:   0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8132 L22:   0.6101                                     
REMARK   3      L33:   0.7625 L12:  -0.5175                                     
REMARK   3      L13:   0.1363 L23:   0.0377                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0359 S12:  -0.2243 S13:   0.0165                       
REMARK   3      S21:   0.0777 S22:   0.0489 S23:  -0.0011                       
REMARK   3      S31:  -0.0398 S32:   0.1055 S33:  -0.0130                       
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):  -6.4940 -30.8560  46.3780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1177 T22:   0.1446                                     
REMARK   3      T33:   0.0958 T12:  -0.0189                                     
REMARK   3      T13:  -0.0060 T23:   0.0386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4958 L22:   3.9921                                     
REMARK   3      L33:   0.2540 L12:   0.0404                                     
REMARK   3      L13:  -0.1518 L23:   0.2415                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0633 S12:  -0.0523 S13:  -0.1186                       
REMARK   3      S21:  -0.0696 S22:   0.0190 S23:  -0.0065                       
REMARK   3      S31:   0.0154 S32:  -0.0451 S33:   0.0443                       
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):  12.3400 -27.9370  47.6760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1108 T22:   0.2047                                     
REMARK   3      T33:   0.1412 T12:  -0.0079                                     
REMARK   3      T13:  -0.0246 T23:   0.0711                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6223 L22:   0.5440                                     
REMARK   3      L33:   0.6843 L12:   0.5032                                     
REMARK   3      L13:  -0.2650 L23:   0.0530                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0141 S12:   0.0803 S13:   0.0762                       
REMARK   3      S21:   0.0190 S22:   0.1251 S23:   0.0468                       
REMARK   3      S31:   0.0449 S32:   0.0428 S33:  -0.1392                       
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   895                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.3830 -22.4140  27.1260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0480 T22:   0.2791                                     
REMARK   3      T33:   0.0220 T12:  -0.0928                                     
REMARK   3      T13:   0.0204 T23:  -0.0473                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9821 L22:   1.0432                                     
REMARK   3      L33:   1.9285 L12:   0.1259                                     
REMARK   3      L13:   0.1596 L23:  -0.3441                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1484 S12:   0.3545 S13:  -0.1172                       
REMARK   3      S21:  -0.1130 S22:   0.1189 S23:  -0.1118                       
REMARK   3      S31:   0.0061 S32:   0.2930 S33:   0.0294                       
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 3SUN 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 RCSB066672.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
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   : 41995                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.420                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 87.720                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.100                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.48                     
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   (%): 52.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
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       37.41950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.68300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.49350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       63.68300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.41950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.49350            
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: 6910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 41860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P, T                               
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. =   2.8 DEGREES          
REMARK 500     DT T   8   C1' -  O4' -  C4' ANGL. DEV. =  -6.4 DEGREES          
REMARK 500     DT T   8   O4' -  C1' -  N1  ANGL. DEV. =   2.8 DEGREES          
REMARK 500     DT T  12   O4' -  C1' -  N1  ANGL. DEV. =   4.0 DEGREES          
REMARK 500     DA T  15   O4' -  C1' -  N9  ANGL. DEV. =   2.6 DEGREES          
REMARK 500     DT T  16   O4' -  C1' -  N1  ANGL. DEV. =   2.2 DEGREES          
REMARK 500     DT T  17   O4' -  C4' -  C3' ANGL. DEV. =  -3.4 DEGREES          
REMARK 500     DA P 103   O4' -  C1' -  N9  ANGL. DEV. =   3.2 DEGREES          
REMARK 500     DT P 105   O4' -  C1' -  N1  ANGL. DEV. =   3.0 DEGREES          
REMARK 500     DT P 106   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DA P 112   O4' -  C1' -  N9  ANGL. DEV. =   2.6 DEGREES          
REMARK 500     DT P 113   O4' -  C1' -  N1  ANGL. DEV. =   1.9 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       32.65    -70.49                                   
REMARK 500    ALA A 129       64.11     33.23                                   
REMARK 500    PHE A 221      -71.49   -123.01                                   
REMARK 500    PRO A 244        2.87    -69.83                                   
REMARK 500    GLU A 254     -137.78     45.32                                   
REMARK 500    ASN A 255       74.09   -152.66                                   
REMARK 500    MET A 256      -85.63     56.48                                   
REMARK 500    SER A 259      113.49   -160.52                                   
REMARK 500    ASN A 316       66.99   -152.69                                   
REMARK 500    SER A 414       68.22     37.73                                   
REMARK 500    ASN A 424       46.88     71.82                                   
REMARK 500    PRO A 458        1.81    -59.45                                   
REMARK 500    CYS A 609      -31.80     86.43                                   
REMARK 500    THR A 622      -61.57     73.50                                   
REMARK 500    LEU A 680       11.96   -142.13                                   
REMARK 500    GLU A 686      -74.88   -101.90                                   
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 A1046        DISTANCE =  5.21 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 897  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 623   OD1                                                    
REMARK 620 2 TTP A 896   O1G 173.4                                              
REMARK 620 3 TTP A 896   O2B  95.8  80.8                                        
REMARK 620 4 ASP A 411   OD2  75.8 105.7 160.7                                  
REMARK 620 5 LEU A 412   O    84.8 101.0  93.9 102.4                            
REMARK 620 6 TTP A 896   O2A  85.3  88.4  78.1  83.9 166.6                      
REMARK 620 7 ASP A 411   OD1 106.4  78.5 152.3  45.7  72.4 119.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 899  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 507   OD1                                                    
REMARK 620 2 LYS A 531   O    73.7                                              
REMARK 620 3 ASN A 505   O    90.5 164.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 898  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 411   OD2                                                    
REMARK 620 2 ASP A 623   OD2  75.8                                              
REMARK 620 3 TTP A 896   O2A  68.1  75.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 901  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 116   OE1                                                    
REMARK 620 2 GLU A 116   OE2  45.3                                              
REMARK 620 3 HOH A 943   O    91.4  88.9                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TTP A 896                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 897                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 898                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 899                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 900                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 901                  
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: 3SUO   RELATED DB: PDB                                   
REMARK 900 RB69 DNA POLYMERASE (Y567A) TERNARY COMPLEX WITH DTTP                
REMARK 900 OPPOSITE 2AP (GC RICH SEQUENCE)                                      
REMARK 900 RELATED ID: 3SUP   RELATED DB: PDB                                   
REMARK 900 RB69 DNA POLYMERASE (Y567A) TERNARY COMPLEX WITH DCTP                
REMARK 900 OPPOSITE 2AP (GC RICH SEQUENCE)                                      
REMARK 900 RELATED ID: 3SUQ   RELATED DB: PDB                                   
REMARK 900 RB69 DNA POLYMERASE (Y567A) TERNARY COMPLEX WITH DCTP                
REMARK 900 OPPOSITE 2AP (AT RICH SEQUENCE)                                      
DBREF  3SUN A    1   895  UNP    Q38087   DPOL_BPR69       1    895             
DBREF  3SUN T    3    18  PDB    3SUN     3SUN             3     18             
DBREF  3SUN P  103   115  PDB    3SUN     3SUN           103    115             
SEQADV 3SUN ALA A  222  UNP  Q38087    ASP   222 ENGINEERED MUTATION            
SEQADV 3SUN ALA A  327  UNP  Q38087    ASP   327 ENGINEERED MUTATION            
SEQADV 3SUN ALA A  567  UNP  Q38087    TYR   567 ENGINEERED MUTATION            
SEQRES   1 A  895  MET LYS GLU PHE TYR LEU THR VAL GLU GLN ILE GLY ASP          
SEQRES   2 A  895  SER ILE PHE GLU ARG TYR ILE ASP SER ASN GLY ARG GLU          
SEQRES   3 A  895  ARG THR ARG GLU VAL GLU TYR LYS PRO SER LEU PHE ALA          
SEQRES   4 A  895  HIS CYS PRO GLU SER GLN ALA THR LYS TYR PHE ASP ILE          
SEQRES   5 A  895  TYR GLY LYS PRO CYS THR ARG LYS LEU PHE ALA ASN MET          
SEQRES   6 A  895  ARG ASP ALA SER GLN TRP ILE LYS ARG MET GLU ASP ILE          
SEQRES   7 A  895  GLY LEU GLU ALA LEU GLY MET ASP ASP PHE LYS LEU ALA          
SEQRES   8 A  895  TYR LEU SER ASP THR TYR ASN TYR GLU ILE LYS TYR ASP          
SEQRES   9 A  895  HIS THR LYS ILE ARG VAL ALA ASN PHE ASP ILE GLU VAL          
SEQRES  10 A  895  THR SER PRO ASP GLY PHE PRO GLU PRO SER GLN ALA LYS          
SEQRES  11 A  895  HIS PRO ILE ASP ALA ILE THR HIS TYR ASP SER ILE ASP          
SEQRES  12 A  895  ASP ARG PHE TYR VAL PHE ASP LEU LEU ASN SER PRO TYR          
SEQRES  13 A  895  GLY ASN VAL GLU GLU TRP SER ILE GLU ILE ALA ALA LYS          
SEQRES  14 A  895  LEU GLN GLU GLN GLY GLY ASP GLU VAL PRO SER GLU ILE          
SEQRES  15 A  895  ILE ASP LYS ILE ILE TYR MET PRO PHE ASP ASN GLU LYS          
SEQRES  16 A  895  GLU LEU LEU MET GLU TYR LEU ASN PHE TRP GLN GLN LYS          
SEQRES  17 A  895  THR PRO VAL ILE LEU THR GLY TRP ASN VAL GLU SER PHE          
SEQRES  18 A  895  ALA ILE PRO TYR VAL TYR ASN ARG ILE LYS ASN ILE PHE          
SEQRES  19 A  895  GLY GLU SER THR ALA LYS ARG LEU SER PRO HIS ARG LYS          
SEQRES  20 A  895  THR ARG VAL LYS VAL ILE GLU ASN MET TYR GLY SER ARG          
SEQRES  21 A  895  GLU ILE ILE THR LEU PHE GLY ILE SER VAL LEU ASP TYR          
SEQRES  22 A  895  ILE ASP LEU TYR LYS LYS PHE SER PHE THR ASN GLN PRO          
SEQRES  23 A  895  SER TYR SER LEU ASP TYR ILE SER GLU PHE GLU LEU ASN          
SEQRES  24 A  895  VAL GLY LYS LEU LYS TYR ASP GLY PRO ILE SER LYS LEU          
SEQRES  25 A  895  ARG GLU SER ASN HIS GLN ARG TYR ILE SER TYR ASN ILE          
SEQRES  26 A  895  ILE ALA VAL TYR ARG VAL LEU GLN ILE ASP ALA LYS ARG          
SEQRES  27 A  895  GLN PHE ILE ASN LEU SER LEU ASP MET GLY TYR TYR ALA          
SEQRES  28 A  895  LYS ILE GLN ILE GLN SER VAL PHE SER PRO ILE LYS THR          
SEQRES  29 A  895  TRP ASP ALA ILE ILE PHE ASN SER LEU LYS GLU GLN ASN          
SEQRES  30 A  895  LYS VAL ILE PRO GLN GLY ARG SER HIS PRO VAL GLN PRO          
SEQRES  31 A  895  TYR PRO GLY ALA PHE VAL LYS GLU PRO ILE PRO ASN ARG          
SEQRES  32 A  895  TYR LYS TYR VAL MET SER PHE ASP LEU THR SER LEU TYR          
SEQRES  33 A  895  PRO SER ILE ILE ARG GLN VAL ASN ILE SER PRO GLU THR          
SEQRES  34 A  895  ILE ALA GLY THR PHE LYS VAL ALA PRO LEU HIS ASP TYR          
SEQRES  35 A  895  ILE ASN ALA VAL ALA GLU ARG PRO SER ASP VAL TYR SER          
SEQRES  36 A  895  CYS SER PRO ASN GLY MET MET TYR TYR LYS ASP ARG ASP          
SEQRES  37 A  895  GLY VAL VAL PRO THR GLU ILE THR LYS VAL PHE ASN GLN          
SEQRES  38 A  895  ARG LYS GLU HIS LYS GLY TYR MET LEU ALA ALA GLN ARG          
SEQRES  39 A  895  ASN GLY GLU ILE ILE LYS GLU ALA LEU HIS ASN PRO ASN          
SEQRES  40 A  895  LEU SER VAL ASP GLU PRO LEU ASP VAL ASP TYR ARG PHE          
SEQRES  41 A  895  ASP PHE SER ASP GLU ILE LYS GLU LYS ILE LYS LYS LEU          
SEQRES  42 A  895  SER ALA LYS SER LEU ASN GLU MET LEU PHE ARG ALA GLN          
SEQRES  43 A  895  ARG THR GLU VAL ALA GLY MET THR ALA GLN ILE ASN ARG          
SEQRES  44 A  895  LYS LEU LEU ILE ASN SER LEU ALA GLY ALA LEU GLY ASN          
SEQRES  45 A  895  VAL TRP PHE ARG TYR TYR ASP LEU ARG ASN ALA THR ALA          
SEQRES  46 A  895  ILE THR THR PHE GLY GLN MET ALA LEU GLN TRP ILE GLU          
SEQRES  47 A  895  ARG LYS VAL ASN GLU TYR LEU ASN GLU VAL CYS GLY THR          
SEQRES  48 A  895  GLU GLY GLU ALA PHE VAL LEU TYR GLY ASP THR ASP SER          
SEQRES  49 A  895  ILE TYR VAL SER ALA ASP LYS ILE ILE ASP LYS VAL GLY          
SEQRES  50 A  895  GLU SER LYS PHE ARG ASP THR ASN HIS TRP VAL ASP PHE          
SEQRES  51 A  895  LEU ASP LYS PHE ALA ARG GLU ARG MET GLU PRO ALA ILE          
SEQRES  52 A  895  ASP ARG GLY PHE ARG GLU MET CYS GLU TYR MET ASN ASN          
SEQRES  53 A  895  LYS GLN HIS LEU MET PHE MET ASP ARG GLU ALA ILE ALA          
SEQRES  54 A  895  GLY PRO PRO LEU GLY SER LYS GLY ILE GLY GLY PHE TRP          
SEQRES  55 A  895  THR GLY LYS LYS ARG TYR ALA LEU ASN VAL TRP ASP MET          
SEQRES  56 A  895  GLU GLY THR ARG TYR ALA GLU PRO LYS LEU LYS ILE MET          
SEQRES  57 A  895  GLY LEU GLU THR GLN LYS SER SER THR PRO LYS ALA VAL          
SEQRES  58 A  895  GLN LYS ALA LEU LYS GLU CYS ILE ARG ARG MET LEU GLN          
SEQRES  59 A  895  GLU GLY GLU GLU SER LEU GLN GLU TYR PHE LYS GLU PHE          
SEQRES  60 A  895  GLU LYS GLU PHE ARG GLN LEU ASN TYR ILE SER ILE ALA          
SEQRES  61 A  895  SER VAL SER SER ALA ASN ASN ILE ALA LYS TYR ASP VAL          
SEQRES  62 A  895  GLY GLY PHE PRO GLY PRO LYS CYS PRO PHE HIS ILE ARG          
SEQRES  63 A  895  GLY ILE LEU THR TYR ASN ARG ALA ILE LYS GLY ASN ILE          
SEQRES  64 A  895  ASP ALA PRO GLN VAL VAL GLU GLY GLU LYS VAL TYR VAL          
SEQRES  65 A  895  LEU PRO LEU ARG GLU GLY ASN PRO PHE GLY ASP LYS CYS          
SEQRES  66 A  895  ILE ALA TRP PRO SER GLY THR GLU ILE THR ASP LEU ILE          
SEQRES  67 A  895  LYS ASP ASP VAL LEU HIS TRP MET ASP TYR THR VAL LEU          
SEQRES  68 A  895  LEU GLU LYS THR PHE ILE LYS PRO LEU GLU GLY PHE THR          
SEQRES  69 A  895  SER ALA ALA LYS LEU ASP TYR GLU LYS LYS ALA                  
SEQRES   1 T   16   DC 2PR  DT  DA  DA  DT  DT  DA  DA  DT  DT  DA  DA          
SEQRES   2 T   16   DT  DT  DG                                                  
SEQRES   1 P   13   DA  DA  DT  DT  DA  DA  DT  DT  DA  DA  DT  DT 2DA          
MODRES 3SUN 2PR T    4   DG  2-AMINOPURINE-2'-DEOXYRIBO-5'-MONOPHOSPHA          
MODRES 3SUN 2DA P  115   DA  2',3'-DIDEOXYADENOSINE-5'-MONOPHOSPHATE            
HET    2PR  T   4      21                                                       
HET    2DA  P 115      20                                                       
HET    TTP  A 896      29                                                       
HET     CA  A 897       1                                                       
HET     CA  A 898       1                                                       
HET     CA  A 899       1                                                       
HET     CA  A 900       1                                                       
HET     CA  A 901       1                                                       
HETNAM     2PR 2-AMINO-9-[2-DEOXYRIBOFURANOSYL]-9H-PURINE-5'-                   
HETNAM   2 2PR  MONOPHOSPHATE                                                   
HETNAM     2DA 2',3'-DIDEOXYADENOSINE-5'-MONOPHOSPHATE                          
HETNAM     TTP THYMIDINE-5'-TRIPHOSPHATE                                        
HETNAM      CA CALCIUM ION                                                      
HETSYN     2PR 2-AMINOPURINE-2'-DEOXYRIBO-5'-MONOPHOSPHATE                      
FORMUL   2  2PR    C10 H14 N5 O6 P                                              
FORMUL   3  2DA    C10 H14 N5 O5 P                                              
FORMUL   4  TTP    C10 H17 N2 O14 P3                                            
FORMUL   5   CA    5(CA 2+)                                                     
FORMUL  10  HOH   *162(H2 O)                                                    
HELIX    1   1 ASN A   64  GLY A   79  1                                  16    
HELIX    2   2 ASP A   87  TYR A   97  1                                  11    
HELIX    3   3 ASP A  104  ILE A  108  5                                   5    
HELIX    4   4 SER A  163  LYS A  169  1                                   7    
HELIX    5   5 LEU A  170  GLY A  174  5                                   5    
HELIX    6   6 PRO A  179  ASP A  184  1                                   6    
HELIX    7   7 ASN A  193  LYS A  208  1                                  16    
HELIX    8   8 PHE A  221  GLY A  235  1                                  15    
HELIX    9   9 GLY A  235  LYS A  240  1                                   6    
HELIX   10  10 ARG A  241  SER A  243  5                                   3    
HELIX   11  11 ASP A  272  SER A  281  1                                  10    
HELIX   12  12 SER A  289  ASN A  299  1                                  11    
HELIX   13  13 PRO A  308  SER A  310  5                                   3    
HELIX   14  14 LYS A  311  GLN A  339  1                                  29    
HELIX   15  15 GLN A  339  LYS A  352  1                                  14    
HELIX   16  16 GLN A  354  PHE A  359  5                                   6    
HELIX   17  17 SER A  360  GLN A  376  1                                  17    
HELIX   18  18 SER A  414  ASN A  424  1                                  11    
HELIX   19  19 PRO A  438  ASN A  444  1                                   7    
HELIX   20  20 GLY A  469  LEU A  503  1                                  35    
HELIX   21  21 SER A  523  LYS A  531  1                                   9    
HELIX   22  22 SER A  534  LEU A  570  1                                  37    
HELIX   23  23 ASP A  579  VAL A  608  1                                  30    
HELIX   24  24 ALA A  629  GLY A  637  1                                   9    
HELIX   25  25 GLU A  638  PHE A  641  5                                   4    
HELIX   26  26 ASP A  643  ARG A  658  1                                  16    
HELIX   27  27 ARG A  658  MET A  674  1                                  17    
HELIX   28  28 LEU A  730  LYS A  734  5                                   5    
HELIX   29  29 PRO A  738  GLU A  755  1                                  18    
HELIX   30  30 GLY A  756  PHE A  771  1                                  16    
HELIX   31  31 ARG A  772  LEU A  774  5                                   3    
HELIX   32  32 ASN A  787  TYR A  791  1                                   5    
HELIX   33  33 PRO A  802  ILE A  815  1                                  14    
HELIX   34  34 THR A  855  MET A  866  1                                  12    
HELIX   35  35 ASP A  867  PHE A  876  1                                  10    
HELIX   36  36 PHE A  876  LYS A  888  1                                  13    
SHEET    1   A 3 PHE A   4  ILE A  11  0                                        
SHEET    2   A 3 SER A  14  ILE A  20 -1  O  ILE A  20   N  PHE A   4           
SHEET    3   A 3 GLU A  26  VAL A  31 -1  O  VAL A  31   N  ILE A  15           
SHEET    1   B 2 SER A  36  HIS A  40  0                                        
SHEET    2   B 2 CYS A  57  LEU A  61 -1  O  LYS A  60   N  LEU A  37           
SHEET    1   C 2 PHE A  50  ASP A  51  0                                        
SHEET    2   C 2 LYS A 378  VAL A 379  1  O  VAL A 379   N  PHE A  50           
SHEET    1   D 6 ILE A 186  PHE A 191  0                                        
SHEET    2   D 6 ARG A 145  LEU A 151  1  N  PHE A 146   O  ILE A 187           
SHEET    3   D 6 ILE A 133  ASP A 140 -1  N  ILE A 136   O  PHE A 149           
SHEET    4   D 6 VAL A 110  VAL A 117 -1  N  ASN A 112   O  TYR A 139           
SHEET    5   D 6 ILE A 212  THR A 214  1  O  ILE A 212   N  ALA A 111           
SHEET    6   D 6 SER A 269  VAL A 270  1  O  SER A 269   N  LEU A 213           
SHEET    1   E 2 ASN A 153  SER A 154  0                                        
SHEET    2   E 2 GLY A 157  ASN A 158 -1  O  GLY A 157   N  SER A 154           
SHEET    1   F 2 THR A 248  ILE A 253  0                                        
SHEET    2   F 2 ARG A 260  LEU A 265 -1  O  ILE A 262   N  LYS A 251           
SHEET    1   G 7 ASN A 402  ARG A 403  0                                        
SHEET    2   G 7 GLY A 700  GLY A 704 -1  O  TRP A 702   N  ASN A 402           
SHEET    3   G 7 ARG A 707  MET A 715 -1  O  ALA A 709   N  PHE A 701           
SHEET    4   G 7 MET A 683  ALA A 689 -1  N  ILE A 688   O  TRP A 713           
SHEET    5   G 7 VAL A 407  LEU A 412 -1  N  VAL A 407   O  ALA A 689           
SHEET    6   G 7 SER A 624  SER A 628 -1  O  VAL A 627   N  MET A 408           
SHEET    7   G 7 VAL A 617  ASP A 621 -1  N  TYR A 619   O  TYR A 626           
SHEET    1   H 4 ASN A 402  ARG A 403  0                                        
SHEET    2   H 4 GLY A 700  GLY A 704 -1  O  TRP A 702   N  ASN A 402           
SHEET    3   H 4 ARG A 707  MET A 715 -1  O  ALA A 709   N  PHE A 701           
SHEET    4   H 4 THR A 718  MET A 728 -1  O  LYS A 726   N  LEU A 710           
SHEET    1   I 3 ILE A 430  THR A 433  0                                        
SHEET    2   I 3 MET A 461  TYR A 463 -1  O  MET A 462   N  ALA A 431           
SHEET    3   I 3 SER A 455  SER A 457 -1  N  SER A 455   O  TYR A 463           
SHEET    1   J 3 SER A 781  SER A 784  0                                        
SHEET    2   J 3 LYS A 829  PRO A 834 -1  O  VAL A 830   N  SER A 783           
SHEET    3   J 3 CYS A 845  PRO A 849 -1  O  TRP A 848   N  TYR A 831           
SHEET    1   K 2 ASP A 792  VAL A 793  0                                        
SHEET    2   K 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  1.59  
LINK         O3' 2PR T   4                 P    DT T   5     1555   1555  1.61  
LINK         O3'  DT P 114                 P   2DA P 115     1555   1555  1.61  
LINK         OD1 ASP A 623                CA    CA A 897     1555   1555  2.22  
LINK         O1G TTP A 896                CA    CA A 897     1555   1555  2.23  
LINK         O2B TTP A 896                CA    CA A 897     1555   1555  2.24  
LINK         OD2 ASP A 411                CA    CA A 897     1555   1555  2.25  
LINK         O   LEU A 412                CA    CA A 897     1555   1555  2.29  
LINK         OD1 ASN A 507                CA    CA A 899     1555   1555  2.34  
LINK         O   LYS A 531                CA    CA A 899     1555   1555  2.39  
LINK         O2A TTP A 896                CA    CA A 897     1555   1555  2.41  
LINK         O   ASN A 505                CA    CA A 899     1555   1555  2.44  
LINK         OD2 ASP A 411                CA    CA A 898     1555   1555  2.69  
LINK         OD2 ASP A 623                CA    CA A 898     1555   1555  2.79  
LINK         OE1 GLU A 116                CA    CA A 901     1555   1555  2.82  
LINK         O2A TTP A 896                CA    CA A 898     1555   1555  2.86  
LINK         OE2 GLU A 116                CA    CA A 901     1555   1555  2.87  
LINK         OD1 ASP A 411                CA    CA A 897     1555   1555  3.06  
LINK        CA    CA A 901                 O   HOH A 943     1555   1555  2.65  
LINK        CA    CA A 900                 O   HOH A1001     1555   1555  2.90  
CISPEP   1 GLU A  254    ASN A  255          0        -4.26                     
SITE     1 AC1 19 ASP A 411  LEU A 412  SER A 414  LEU A 415                    
SITE     2 AC1 19 TYR A 416  ARG A 482  LYS A 486  LYS A 560                    
SITE     3 AC1 19 ASN A 564  THR A 622  ASP A 623   CA A 897                    
SITE     4 AC1 19  CA A 898  HOH A 912  HOH A 942  HOH A1027                    
SITE     5 AC1 19 2DA P 115  2PR T   4   DT T   5                               
SITE     1 AC2  4 ASP A 411  LEU A 412  ASP A 623  TTP A 896                    
SITE     1 AC3  3 ASP A 411  ASP A 623  TTP A 896                               
SITE     1 AC4  3 ASN A 505  ASN A 507  LYS A 531                               
SITE     1 AC5  2 GLU A 716  HOH A1001                                          
SITE     1 AC6  2 GLU A 116  HOH A 943                                          
CRYST1   74.839  120.987  127.366  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      0.013362  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008265  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007851        0.00000                         
ATOM      1  N   MET A   1     -34.442 -21.396  36.059  1.00 75.50           N  
ANISOU    1  N   MET A   1     7976  11615   9097  -1025    750  -1527       N  
ATOM      2  CA  MET A   1     -33.097 -20.867  36.438  1.00 74.09           C  
ANISOU    2  CA  MET A   1     7989  11266   8897   -902    684  -1340       C  
ATOM      3  C   MET A   1     -32.990 -19.359  36.220  1.00 72.31           C  
ANISOU    3  C   MET A   1     7664  11095   8714   -666    589  -1333       C  
ATOM      4  O   MET A   1     -33.635 -18.800  35.328  1.00 72.56           O  
ANISOU    4  O   MET A   1     7519  11254   8795   -540    514  -1430       O  
ATOM      5  CB  MET A   1     -31.970 -21.606  35.697  1.00 73.11           C  
ANISOU    5  CB  MET A   1     8030  10983   8765   -873    601  -1199       C  
ATOM      6  CG  MET A   1     -32.293 -22.027  34.266  1.00 76.20           C  
ANISOU    6  CG  MET A   1     8317  11439   9198   -831    527  -1252       C  
ATOM      7  SD  MET A   1     -30.817 -22.289  33.242  1.00 78.44           S  
ANISOU    7  SD  MET A   1     8759  11553   9490   -700    399  -1085       S  
ATOM      8  CE  MET A   1     -30.395 -20.591  32.850  1.00 72.36           C  
ANISOU    8  CE  MET A   1     7922  10809   8761   -439    293  -1041       C  
ATOM      9  N   LYS A   2     -32.179 -18.710  37.055  1.00 69.55           N  
ANISOU    9  N   LYS A   2     7444  10642   8341   -606    585  -1223       N  
ATOM     10  CA  LYS A   2     -31.976 -17.257  36.993  1.00 67.18           C  
ANISOU   10  CA  LYS A   2     7090  10368   8069   -395    502  -1202       C  
ATOM     11  C   LYS A   2     -31.175 -16.872  35.746  1.00 62.34           C  
ANISOU   11  C   LYS A   2     6509   9692   7486   -219    362  -1112       C  
ATOM     12  O   LYS A   2     -30.352 -17.649  35.264  1.00 59.97           O  
ANISOU   12  O   LYS A   2     6327   9280   7181   -253    334  -1017       O  
ATOM     13  CB  LYS A   2     -31.292 -16.742  38.275  1.00 67.00           C  
ANISOU   13  CB  LYS A   2     7210  10242   8007   -400    542  -1109       C  
ATOM     14  CG  LYS A   2     -31.931 -17.228  39.596  1.00 70.87           C  
ANISOU   14  CG  LYS A   2     7725  10758   8443   -598    696  -1177       C  
ATOM     15  CD  LYS A   2     -33.305 -16.594  39.858  1.00 75.07           C  
ANISOU   15  CD  LYS A   2     8038  11491   8997   -597    761  -1363       C  
ATOM     16  CE  LYS A   2     -34.312 -17.590  40.465  1.00 78.83           C  
ANISOU   16  CE  LYS A   2     8465  12050   9438   -849    927  -1496       C  
ATOM     17  NZ  LYS A   2     -34.055 -17.915  41.903  1.00 79.34           N  
ANISOU   17  NZ  LYS A   2     8716  12013   9417  -1013   1054  -1446       N  
ATOM     18  N   GLU A   3     -31.432 -15.677  35.227  1.00 60.40           N  
ANISOU   18  N   GLU A   3     6169   9515   7266    -32    275  -1150       N  
ATOM     19  CA  GLU A   3     -30.779 -15.203  34.011  1.00 57.23           C  
ANISOU   19  CA  GLU A   3     5808   9058   6879    131    151  -1079       C  
ATOM     20  C   GLU A   3     -29.324 -14.839  34.280  1.00 52.88           C  
ANISOU   20  C   GLU A   3     5439   8338   6315    180    126   -912       C  
ATOM     21  O   GLU A   3     -28.946 -14.579  35.419  1.00 51.43           O  
ANISOU   21  O   GLU A   3     5327   8100   6115    141    176   -864       O  
ATOM     22  CB  GLU A   3     -31.523 -13.991  33.439  1.00 59.47           C  
ANISOU   22  CB  GLU A   3     5968   9451   7177    318     60  -1175       C  
ATOM     23  CG  GLU A   3     -32.858 -14.316  32.786  1.00 66.45           C  
ANISOU   23  CG  GLU A   3     6659  10502   8086    315     39  -1353       C  
ATOM     24  CD  GLU A   3     -33.711 -13.085  32.522  1.00 72.66           C  
ANISOU   24  CD  GLU A   3     7317  11405   8885    506    -52  -1475       C  
ATOM     25  OE1 GLU A   3     -33.932 -12.294  33.470  1.00 78.72           O  
ANISOU   25  OE1 GLU A   3     8058  12204   9647    542    -19  -1505       O  
ATOM     26  OE2 GLU A   3     -34.178 -12.917  31.374  1.00 73.13           O  
ANISOU   26  OE2 GLU A   3     7311  11522   8954    625   -164  -1548       O  
ATOM     27  N   PHE A   4     -28.510 -14.851  33.228  1.00 48.76           N  
ANISOU   27  N   PHE A   4     4990   7737   5801    257     50   -833       N  
ATOM     28  CA  PHE A   4     -27.146 -14.332  33.296  1.00 44.80           C  
ANISOU   28  CA  PHE A   4     4632   7095   5297    322     19   -699       C  
ATOM     29  C   PHE A   4     -26.691 -13.826  31.934  1.00 43.69           C  
ANISOU   29  C   PHE A   4     4522   6921   5156    451    -69   -666       C  
ATOM     30  O   PHE A   4     -27.146 -14.315  30.898  1.00 42.84           O  
ANISOU   30  O   PHE A   4     4365   6862   5051    459   -103   -716       O  
ATOM     31  CB  PHE A   4     -26.155 -15.349  33.906  1.00 43.01           C  
ANISOU   31  CB  PHE A   4     4527   6744   5069    198     66   -610       C  
ATOM     32  CG  PHE A   4     -26.086 -16.674  33.186  1.00 45.69           C  
ANISOU   32  CG  PHE A   4     4881   7064   5414    110     71   -613       C  
ATOM     33  CD1 PHE A   4     -27.032 -17.672  33.431  1.00 48.58           C  
ANISOU   33  CD1 PHE A   4     5191   7500   5768    -28    132   -695       C  
ATOM     34  CD2 PHE A   4     -25.054 -16.937  32.284  1.00 49.14           C  
ANISOU   34  CD2 PHE A   4     5394   7410   5867    154     23   -542       C  
ATOM     35  CE1 PHE A   4     -26.966 -18.902  32.776  1.00 49.07           C  
ANISOU   35  CE1 PHE A   4     5281   7535   5829   -113    134   -698       C  
ATOM     36  CE2 PHE A   4     -24.970 -18.169  31.620  1.00 48.08           C  
ANISOU   36  CE2 PHE A   4     5281   7253   5736     79     24   -547       C  
ATOM     37  CZ  PHE A   4     -25.930 -19.154  31.869  1.00 50.68           C  
ANISOU   37  CZ  PHE A   4     5562   7644   6048    -52     75   -621       C  
ATOM     38  N   TYR A   5     -25.815 -12.825  31.944  1.00 42.78           N  
ANISOU   38  N   TYR A   5     4499   6723   5035    546   -101   -588       N  
ATOM     39  CA  TYR A   5     -25.290 -12.258  30.702  1.00 42.17           C  
ANISOU   39  CA  TYR A   5     4486   6596   4942    654   -168   -551       C  
ATOM     40  C   TYR A   5     -24.218 -13.153  30.105  1.00 42.68           C  
ANISOU   40  C   TYR A   5     4628   6566   5024    590   -153   -480       C  
ATOM     41  O   TYR A   5     -23.642 -14.004  30.782  1.00 42.89           O  
ANISOU   41  O   TYR A   5     4682   6539   5075    487   -106   -441       O  
ATOM     42  CB  TYR A   5     -24.734 -10.841  30.915  1.00 40.95           C  
ANISOU   42  CB  TYR A   5     4414   6379   4766    760   -197   -500       C  
ATOM     43  CG  TYR A   5     -23.524 -10.781  31.830  1.00 40.55           C  
ANISOU   43  CG  TYR A   5     4448   6222   4736    703   -152   -408       C  
ATOM     44  CD1 TYR A   5     -23.681 -10.671  33.213  1.00 38.29           C  
ANISOU   44  CD1 TYR A   5     4145   5946   4458    658   -111   -410       C  
ATOM     45  CD2 TYR A   5     -22.222 -10.839  31.315  1.00 38.11           C  
ANISOU   45  CD2 TYR A   5     4235   5805   4441    694   -149   -331       C  
ATOM     46  CE1 TYR A   5     -22.588 -10.627  34.058  1.00 36.82           C  
ANISOU   46  CE1 TYR A   5     4040   5660   4289    616    -86   -334       C  
ATOM     47  CE2 TYR A   5     -21.115 -10.787  32.159  1.00 36.49           C  
ANISOU   47  CE2 TYR A   5     4090   5510   4264    649   -120   -267       C  
ATOM     48  CZ  TYR A   5     -21.312 -10.681  33.532  1.00 37.65           C  
ANISOU   48  CZ  TYR A   5     4224   5664   4415    616    -97   -267       C  
ATOM     49  OH  TYR A   5     -20.242 -10.621  34.393  1.00 39.69           O  
ANISOU   49  OH  TYR A   5     4548   5834   4700    582    -84   -211       O  
ATOM     50  N   LEU A   6     -23.963 -12.951  28.821  1.00 43.23           N  
ANISOU   50  N   LEU A   6     4741   6610   5074    658   -199   -471       N  
ATOM     51  CA  LEU A   6     -22.895 -13.638  28.136  1.00 43.47           C  
ANISOU   51  CA  LEU A   6     4846   6553   5119    614   -183   -413       C  
ATOM     52  C   LEU A   6     -21.847 -12.607  27.732  1.00 44.55           C  
ANISOU   52  C   LEU A   6     5091   6598   5239    682   -189   -350       C  
ATOM     53  O   LEU A   6     -20.662 -12.748  28.050  1.00 45.57           O  
ANISOU   53  O   LEU A   6     5273   6643   5400    637   -152   -293       O  
ATOM     54  CB  LEU A   6     -23.447 -14.396  26.929  1.00 41.50           C  
ANISOU   54  CB  LEU A   6     4566   6347   4854    612   -213   -462       C  
ATOM     55  CG  LEU A   6     -24.327 -15.605  27.271  1.00 40.35           C  
ANISOU   55  CG  LEU A   6     4323   6279   4728    511   -191   -526       C  
ATOM     56  CD1 LEU A   6     -25.229 -15.957  26.113  1.00 29.05           C  
ANISOU   56  CD1 LEU A   6     2837   4923   3276    541   -243   -603       C  
ATOM     57  CD2 LEU A   6     -23.474 -16.819  27.693  1.00 38.04           C  
ANISOU   57  CD2 LEU A   6     4077   5908   4467    394   -140   -476       C  
ATOM     58  N   THR A   7     -22.300 -11.556  27.060  1.00 43.63           N  
ANISOU   58  N   THR A   7     5012   6496   5069    789   -240   -370       N  
ATOM     59  CA  THR A   7     -21.429 -10.476  26.646  1.00 42.57           C  
ANISOU   59  CA  THR A   7     5004   6271   4900    844   -241   -317       C  
ATOM     60  C   THR A   7     -22.181  -9.162  26.760  1.00 45.69           C  
ANISOU   60  C   THR A   7     5429   6692   5239    961   -300   -344       C  
ATOM     61  O   THR A   7     -23.414  -9.117  26.634  1.00 44.95           O  
ANISOU   61  O   THR A   7     5262   6691   5126   1027   -360   -419       O  
ATOM     62  CB  THR A   7     -20.978 -10.620  25.177  1.00 41.38           C  
ANISOU   62  CB  THR A   7     4945   6070   4710    857   -246   -306       C  
ATOM     63  OG1 THR A   7     -22.133 -10.680  24.335  1.00 40.73           O  
ANISOU   63  OG1 THR A   7     4842   6055   4578    930   -320   -370       O  
ATOM     64  CG2 THR A   7     -20.107 -11.865  24.965  1.00 39.07           C  
ANISOU   64  CG2 THR A   7     4632   5742   4470    754   -189   -285       C  
ATOM     65  N   VAL A   8     -21.420  -8.093  26.976  1.00 46.57           N  
ANISOU   65  N   VAL A   8     5649   6720   5327    989   -286   -292       N  
ATOM     66  CA  VAL A   8     -21.970  -6.749  27.057  1.00 48.35           C  
ANISOU   66  CA  VAL A   8     5942   6941   5488   1107   -347   -308       C  
ATOM     67  C   VAL A   8     -21.063  -5.762  26.306  1.00 47.19           C  
ANISOU   67  C   VAL A   8     5986   6671   5274   1133   -339   -254       C  
ATOM     68  O   VAL A   8     -19.836  -5.831  26.402  1.00 46.04           O  
ANISOU   68  O   VAL A   8     5888   6447   5158   1043   -263   -198       O  
ATOM     69  CB  VAL A   8     -22.216  -6.344  28.538  1.00 47.79           C  
ANISOU   69  CB  VAL A   8     5801   6905   5453   1106   -333   -313       C  
ATOM     70  CG1 VAL A   8     -20.906  -5.950  29.247  1.00 46.42           C  
ANISOU   70  CG1 VAL A   8     5698   6633   5306   1039   -270   -235       C  
ATOM     71  CG2 VAL A   8     -23.267  -5.271  28.629  1.00 47.03           C  
ANISOU   71  CG2 VAL A   8     5715   6854   5300   1245   -414   -371       C  
ATOM     72  N   GLU A   9     -21.675  -4.885  25.522  1.00 47.80           N  
ANISOU   72  N   GLU A   9     6177   6728   5257   1253   -419   -280       N  
ATOM     73  CA  GLU A   9     -20.936  -3.887  24.756  1.00 50.34           C  
ANISOU   73  CA  GLU A   9     6718   6921   5488   1274   -412   -233       C  
ATOM     74  C   GLU A   9     -21.703  -2.580  24.790  1.00 50.61           C  
ANISOU   74  C   GLU A   9     6864   6934   5432   1423   -511   -260       C  
ATOM     75  O   GLU A   9     -22.924  -2.584  24.898  1.00 53.00           O  
ANISOU   75  O   GLU A   9     7076   7330   5729   1534   -606   -335       O  
ATOM     76  CB  GLU A   9     -20.726  -4.322  23.287  1.00 50.61           C  
ANISOU   76  CB  GLU A   9     6854   6911   5464   1260   -411   -233       C  
ATOM     77  CG  GLU A   9     -20.076  -5.704  23.067  1.00 51.95           C  
ANISOU   77  CG  GLU A   9     6916   7105   5717   1131   -328   -222       C  
ATOM     78  CD  GLU A   9     -18.554  -5.750  23.296  1.00 51.99           C  
ANISOU   78  CD  GLU A   9     6956   7030   5769   1003   -207   -166       C  
ATOM     79  OE1 GLU A   9     -17.931  -4.702  23.575  1.00 53.29           O  
ANISOU   79  OE1 GLU A   9     7233   7115   5900    994   -176   -133       O  
ATOM     80  OE2 GLU A   9     -17.979  -6.859  23.183  1.00 50.09           O  
ANISOU   80  OE2 GLU A   9     6625   6807   5599    911   -148   -166       O  
ATOM     81  N   GLN A  10     -20.978  -1.468  24.719  1.00 52.06           N  
ANISOU   81  N   GLN A  10     7240   6994   5545   1425   -490   -209       N  
ATOM     82  CA  GLN A  10     -21.584  -0.167  24.498  1.00 53.52           C  
ANISOU   82  CA  GLN A  10     7598   7123   5616   1574   -593   -228       C  
ATOM     83  C   GLN A  10     -21.315   0.239  23.065  1.00 56.51           C  
ANISOU   83  C   GLN A  10     8225   7383   5865   1598   -615   -210       C  
ATOM     84  O   GLN A  10     -20.161   0.446  22.685  1.00 56.30           O  
ANISOU   84  O   GLN A  10     8338   7246   5807   1480   -513   -149       O  
ATOM     85  CB  GLN A  10     -21.012   0.894  25.435  1.00 52.24           C  
ANISOU   85  CB  GLN A  10     7517   6886   5444   1559   -558   -184       C  
ATOM     86  CG  GLN A  10     -21.756   2.217  25.338  1.00 52.80           C  
ANISOU   86  CG  GLN A  10     7761   6903   5398   1731   -680   -214       C  
ATOM     87  CD  GLN A  10     -21.003   3.394  25.929  1.00 52.42           C  
ANISOU   87  CD  GLN A  10     7876   6737   5305   1703   -640   -158       C  
ATOM     88  OE1 GLN A  10     -20.193   3.249  26.849  1.00 50.14           O  
ANISOU   88  OE1 GLN A  10     7497   6450   5102   1581   -541   -117       O  
ATOM     89  NE2 GLN A  10     -21.286   4.580  25.409  1.00 51.98           N  
ANISOU   89  NE2 GLN A  10     8072   6570   5108   1822   -729   -161       N  
ATOM     90  N   ILE A  11     -22.380   0.329  22.268  1.00 58.76           N  
ANISOU   90  N   ILE A  11     8563   7692   6072   1746   -748   -273       N  
ATOM     91  CA  ILE A  11     -22.289   0.893  20.924  1.00 60.87           C  
ANISOU   91  CA  ILE A  11     9115   7829   6184   1801   -800   -261       C  
ATOM     92  C   ILE A  11     -23.193   2.117  20.850  1.00 62.96           C  
ANISOU   92  C   ILE A  11     9547   8045   6331   2006   -962   -307       C  
ATOM     93  O   ILE A  11     -24.427   1.998  20.776  1.00 64.96           O  
ANISOU   93  O   ILE A  11     9699   8397   6587   2167  -1106   -401       O  
ATOM     94  CB  ILE A  11     -22.623  -0.136  19.809  1.00 61.30           C  
ANISOU   94  CB  ILE A  11     9136   7925   6230   1800   -827   -296       C  
ATOM     95  CG1 ILE A  11     -21.633  -1.306  19.854  1.00 59.92           C  
ANISOU   95  CG1 ILE A  11     8821   7781   6163   1602   -667   -251       C  
ATOM     96  CG2 ILE A  11     -22.581   0.539  18.433  1.00 64.40           C  
ANISOU   96  CG2 ILE A  11     9861   8169   6441   1869   -891   -285       C  
ATOM     97  CD1 ILE A  11     -22.124  -2.585  19.208  1.00 61.19           C  
ANISOU   97  CD1 ILE A  11     8843   8037   6370   1593   -691   -297       C  
ATOM     98  N   GLY A  12     -22.560   3.290  20.893  1.00 63.03           N  
ANISOU   98  N   GLY A  12     9809   7902   6238   1998   -938   -250       N  
ATOM     99  CA  GLY A  12     -23.265   4.568  20.893  1.00 63.21           C  
ANISOU   99  CA  GLY A  12    10033   7849   6137   2190  -1089   -285       C  
ATOM    100  C   GLY A  12     -24.053   4.769  22.170  1.00 62.13           C  
ANISOU  100  C   GLY A  12     9672   7839   6095   2291  -1152   -345       C  
ATOM    101  O   GLY A  12     -23.522   4.623  23.268  1.00 61.76           O  
ANISOU  101  O   GLY A  12     9471   7839   6157   2176  -1040   -308       O  
ATOM    102  N   ASP A  13     -25.329   5.097  22.020  1.00 63.73           N  
ANISOU  102  N   ASP A  13     9858   8100   6256   2511  -1334   -449       N  
ATOM    103  CA  ASP A  13     -26.220   5.272  23.154  1.00 63.61           C  
ANISOU  103  CA  ASP A  13     9619   8221   6328   2621  -1398   -533       C  
ATOM    104  C   ASP A  13     -26.948   3.975  23.468  1.00 62.82           C  
ANISOU  104  C   ASP A  13     9160   8332   6378   2592  -1384   -616       C  
ATOM    105  O   ASP A  13     -27.983   3.976  24.143  1.00 64.13           O  
ANISOU  105  O   ASP A  13     9122   8637   6606   2705  -1460   -727       O  
ATOM    106  CB  ASP A  13     -27.217   6.391  22.866  1.00 66.74           C  
ANISOU  106  CB  ASP A  13    10184   8572   6603   2885  -1608   -624       C  
ATOM    107  CG  ASP A  13     -26.614   7.770  23.052  1.00 70.44           C  
ANISOU  107  CG  ASP A  13    10967   8852   6945   2914  -1614   -552       C  
ATOM    108  OD1 ASP A  13     -27.113   8.732  22.424  1.00 78.30           O  
ANISOU  108  OD1 ASP A  13    12229   9734   7788   3108  -1782   -593       O  
ATOM    109  OD2 ASP A  13     -25.651   7.899  23.835  1.00 69.62           O  
ANISOU  109  OD2 ASP A  13    10852   8709   6891   2746  -1461   -460       O  
ATOM    110  N   SER A  14     -26.393   2.869  22.983  1.00 60.44           N  
ANISOU  110  N   SER A  14     8785   8050   6129   2432  -1280   -569       N  
ATOM    111  CA  SER A  14     -27.004   1.566  23.168  1.00 60.67           C  
ANISOU  111  CA  SER A  14     8509   8258   6286   2382  -1258   -639       C  
ATOM    112  C   SER A  14     -26.051   0.552  23.789  1.00 58.74           C  
ANISOU  112  C   SER A  14     8114   8046   6160   2150  -1072   -556       C  
ATOM    113  O   SER A  14     -24.856   0.518  23.481  1.00 56.53           O  
ANISOU  113  O   SER A  14     7972   7650   5857   2019   -967   -452       O  
ATOM    114  CB  SER A  14     -27.556   1.039  21.840  1.00 62.68           C  
ANISOU  114  CB  SER A  14     8803   8526   6487   2454  -1359   -697       C  
ATOM    115  OG  SER A  14     -28.581   1.893  21.346  1.00 65.17           O  
ANISOU  115  OG  SER A  14     9227   8831   6704   2693  -1559   -800       O  
ATOM    116  N   ILE A  15     -26.600  -0.249  24.695  1.00 58.03           N  
ANISOU  116  N   ILE A  15     7745   8112   6193   2102  -1034   -614       N  
ATOM    117  CA  ILE A  15     -25.916  -1.414  25.223  1.00 55.79           C  
ANISOU  117  CA  ILE A  15     7307   7871   6018   1904   -887   -558       C  
ATOM    118  C   ILE A  15     -26.397  -2.613  24.410  1.00 54.70           C  
ANISOU  118  C   ILE A  15     7055   7816   5912   1873   -904   -612       C  
ATOM    119  O   ILE A  15     -27.609  -2.828  24.265  1.00 54.62           O  
ANISOU  119  O   ILE A  15     6913   7925   5915   1973  -1000   -731       O  
ATOM    120  CB  ILE A  15     -26.212  -1.639  26.746  1.00 55.05           C  
ANISOU  120  CB  ILE A  15     7006   7883   6025   1851   -825   -586       C  
ATOM    121  CG1 ILE A  15     -25.618  -0.518  27.611  1.00 55.44           C  
ANISOU  121  CG1 ILE A  15     7170   7845   6049   1864   -799   -525       C  
ATOM    122  CG2 ILE A  15     -25.714  -3.008  27.214  1.00 53.50           C  
ANISOU  122  CG2 ILE A  15     6657   7738   5933   1663   -701   -549       C  
ATOM    123  CD1 ILE A  15     -24.096  -0.369  27.538  1.00 56.83           C  
ANISOU  123  CD1 ILE A  15     7502   7878   6215   1734   -698   -397       C  
ATOM    124  N   PHE A  16     -25.449  -3.368  23.858  1.00 52.14           N  
ANISOU  124  N   PHE A  16     6780   7431   5601   1739   -815   -534       N  
ATOM    125  CA  PHE A  16     -25.761  -4.657  23.248  1.00 51.56           C  
ANISOU  125  CA  PHE A  16     6586   7432   5571   1678   -808   -573       C  
ATOM    126  C   PHE A  16     -25.397  -5.782  24.214  1.00 48.26           C  
ANISOU  126  C   PHE A  16     5983   7080   5273   1512   -687   -549       C  
ATOM    127  O   PHE A  16     -24.264  -5.863  24.691  1.00 46.38           O  
ANISOU  127  O   PHE A  16     5788   6767   5066   1402   -586   -459       O  
ATOM    128  CB  PHE A  16     -25.062  -4.825  21.892  1.00 51.47           C  
ANISOU  128  CB  PHE A  16     6758   7311   5486   1653   -801   -520       C  
ATOM    129  CG  PHE A  16     -25.696  -4.031  20.777  1.00 52.32           C  
ANISOU  129  CG  PHE A  16     7044   7369   5466   1821   -944   -567       C  
ATOM    130  CD1 PHE A  16     -26.545  -4.651  19.859  1.00 56.19           C  
ANISOU  130  CD1 PHE A  16     7488   7925   5938   1888  -1040   -650       C  
ATOM    131  CD2 PHE A  16     -25.447  -2.667  20.644  1.00 51.45           C  
ANISOU  131  CD2 PHE A  16     7163   7138   5248   1916   -991   -533       C  
ATOM    132  CE1 PHE A  16     -27.141  -3.923  18.816  1.00 57.89           C  
ANISOU  132  CE1 PHE A  16     7885   8084   6028   2059  -1193   -700       C  
ATOM    133  CE2 PHE A  16     -26.029  -1.926  19.612  1.00 57.28           C  
ANISOU  133  CE2 PHE A  16     8102   7810   5852   2082  -1138   -577       C  
ATOM    134  CZ  PHE A  16     -26.877  -2.555  18.690  1.00 59.82           C  
ANISOU  134  CZ  PHE A  16     8378   8196   6155   2160  -1245   -662       C  
ATOM    135  N   GLU A  17     -26.381  -6.628  24.506  1.00 47.18           N  
ANISOU  135  N   GLU A  17     5648   7081   5197   1497   -704   -639       N  
ATOM    136  CA  GLU A  17     -26.213  -7.738  25.428  1.00 44.59           C  
ANISOU  136  CA  GLU A  17     5165   6813   4965   1342   -600   -629       C  
ATOM    137  C   GLU A  17     -26.687  -9.061  24.833  1.00 44.78           C  
ANISOU  137  C   GLU A  17     5081   6911   5022   1273   -599   -682       C  
ATOM    138  O   GLU A  17     -27.795  -9.165  24.311  1.00 46.64           O  
ANISOU  138  O   GLU A  17     5235   7240   5246   1350   -684   -790       O  
ATOM    139  CB  GLU A  17     -26.963  -7.466  26.731  1.00 43.76           C  
ANISOU  139  CB  GLU A  17     4921   6803   4901   1352   -589   -690       C  
ATOM    140  CG  GLU A  17     -26.692  -8.480  27.832  1.00 40.17           C  
ANISOU  140  CG  GLU A  17     4358   6381   4524   1186   -476   -667       C  
ATOM    141  CD  GLU A  17     -27.719  -8.428  28.952  1.00 44.35           C  
ANISOU  141  CD  GLU A  17     4733   7033   5087   1181   -459   -760       C  
ATOM    142  OE1 GLU A  17     -27.490  -9.089  29.993  1.00 43.70           O  
ANISOU  142  OE1 GLU A  17     4598   6959   5048   1049   -365   -736       O  
ATOM    143  OE2 GLU A  17     -28.753  -7.733  28.799  1.00 43.25           O  
ANISOU  143  OE2 GLU A  17     4531   6978   4926   1310   -540   -865       O  
ATOM    144  N   ARG A  18     -25.822 -10.066  24.917  1.00 44.52           N  
ANISOU  144  N   ARG A  18     5051   6833   5033   1133   -508   -614       N  
ATOM    145  CA  ARG A  18     -26.200 -11.450  24.682  1.00 43.84           C  
ANISOU  145  CA  ARG A  18     4856   6811   4989   1035   -484   -657       C  
ATOM    146  C   ARG A  18     -26.390 -12.060  26.062  1.00 44.53           C  
ANISOU  146  C   ARG A  18     4823   6955   5142    920   -405   -670       C  
ATOM    147  O   ARG A  18     -25.576 -11.826  26.950  1.00 43.13           O  
ANISOU  147  O   ARG A  18     4693   6712   4984    873   -345   -595       O  
ATOM    148  CB  ARG A  18     -25.097 -12.176  23.914  1.00 41.75           C  
ANISOU  148  CB  ARG A  18     4691   6449   4723    961   -439   -579       C  
ATOM    149  CG  ARG A  18     -24.795 -11.564  22.545  1.00 41.33           C  
ANISOU  149  CG  ARG A  18     4790   6323   4592   1055   -497   -560       C  
ATOM    150  CD  ARG A  18     -23.609 -12.243  21.857  1.00 43.00           C  
ANISOU  150  CD  ARG A  18     5093   6439   4805    972   -431   -490       C  
ATOM    151  NE  ARG A  18     -23.878 -13.639  21.506  1.00 39.01           N  
ANISOU  151  NE  ARG A  18     4505   5980   4336    892   -419   -525       N  
ATOM    152  CZ  ARG A  18     -22.951 -14.506  21.108  1.00 37.44           C  
ANISOU  152  CZ  ARG A  18     4347   5719   4158    808   -359   -481       C  
ATOM    153  NH1 ARG A  18     -21.677 -14.130  21.004  1.00 36.66           N  
ANISOU  153  NH1 ARG A  18     4353   5519   4056    787   -298   -411       N  
ATOM    154  NH2 ARG A  18     -23.298 -15.750  20.810  1.00 31.07           N  
ANISOU  154  NH2 ARG A  18     3474   4954   3378    742   -359   -518       N  
ATOM    155  N   TYR A  19     -27.471 -12.809  26.266  1.00 46.34           N  
ANISOU  155  N   TYR A  19     4905   7303   5399    869   -404   -770       N  
ATOM    156  CA  TYR A  19     -27.716 -13.387  27.588  1.00 47.64           C  
ANISOU  156  CA  TYR A  19     4979   7515   5608    744   -317   -788       C  
ATOM    157  C   TYR A  19     -28.422 -14.735  27.543  1.00 49.52           C  
ANISOU  157  C   TYR A  19     5110   7831   5873    616   -280   -863       C  
ATOM    158  O   TYR A  19     -28.996 -15.115  26.527  1.00 52.38           O  
ANISOU  158  O   TYR A  19     5427   8248   6229    643   -336   -930       O  
ATOM    159  CB  TYR A  19     -28.495 -12.398  28.473  1.00 48.97           C  
ANISOU  159  CB  TYR A  19     5069   7763   5775    813   -328   -856       C  
ATOM    160  CG  TYR A  19     -29.925 -12.168  28.038  1.00 49.85           C  
ANISOU  160  CG  TYR A  19     5036   8021   5885    898   -400  -1012       C  
ATOM    161  CD1 TYR A  19     -30.218 -11.348  26.946  1.00 51.52           C  
ANISOU  161  CD1 TYR A  19     5288   8234   6055   1070   -525  -1048       C  
ATOM    162  CD2 TYR A  19     -30.985 -12.767  28.718  1.00 52.11           C  
ANISOU  162  CD2 TYR A  19     5150   8442   6209    804   -347  -1134       C  
ATOM    163  CE1 TYR A  19     -31.521 -11.136  26.533  1.00 52.43           C  
ANISOU  163  CE1 TYR A  19     5265   8483   6172   1168   -613  -1207       C  
ATOM    164  CE2 TYR A  19     -32.305 -12.556  28.317  1.00 55.47           C  
ANISOU  164  CE2 TYR A  19     5415   9016   6645    884   -417  -1302       C  
ATOM    165  CZ  TYR A  19     -32.564 -11.740  27.220  1.00 57.09           C  
ANISOU  165  CZ  TYR A  19     5654   9223   6816   1077   -560  -1341       C  
ATOM    166  OH  TYR A  19     -33.866 -11.519  26.806  1.00 58.68           O  
ANISOU  166  OH  TYR A  19     5693   9571   7030   1179   -653  -1522       O  
ATOM    167  N   ILE A  20     -28.362 -15.457  28.657  1.00 50.07           N  
ANISOU  167  N   ILE A  20     5158   7900   5966    472   -187   -852       N  
ATOM    168  CA  ILE A  20     -29.148 -16.668  28.842  1.00 49.63           C  
ANISOU  168  CA  ILE A  20     5009   7921   5927    326   -134   -935       C  
ATOM    169  C   ILE A  20     -30.386 -16.336  29.675  1.00 51.74           C  
ANISOU  169  C   ILE A  20     5125   8329   6205    302    -98  -1063       C  
ATOM    170  O   ILE A  20     -30.277 -15.726  30.742  1.00 51.86           O  
ANISOU  170  O   ILE A  20     5153   8335   6217    303    -54  -1042       O  
ATOM    171  CB  ILE A  20     -28.307 -17.783  29.507  1.00 48.45           C  
ANISOU  171  CB  ILE A  20     4964   7666   5780    171    -52   -848       C  
ATOM    172  CG1 ILE A  20     -27.120 -18.192  28.607  1.00 49.41           C  
ANISOU  172  CG1 ILE A  20     5209   7664   5900    199    -88   -747       C  
ATOM    173  CG2 ILE A  20     -29.171 -18.976  29.853  1.00 48.86           C  
ANISOU  173  CG2 ILE A  20     4945   7786   5833      1     17   -935       C  
ATOM    174  CD1 ILE A  20     -27.490 -18.742  27.211  1.00 47.06           C  
ANISOU  174  CD1 ILE A  20     4880   7402   5597    219   -142   -796       C  
ATOM    175  N   ASP A  21     -31.558 -16.733  29.175  1.00 54.09           N  
ANISOU  175  N   ASP A  21     5274   8760   6518    281   -117  -1206       N  
ATOM    176  CA  ASP A  21     -32.837 -16.401  29.813  1.00 54.25           C  
ANISOU  176  CA  ASP A  21     5114   8940   6558    266    -86  -1366       C  
ATOM    177  C   ASP A  21     -33.244 -17.410  30.893  1.00 56.56           C  
ANISOU  177  C   ASP A  21     5366   9269   6855     38     59  -1412       C  
ATOM    178  O   ASP A  21     -32.493 -18.341  31.196  1.00 57.06           O  
ANISOU  178  O   ASP A  21     5565   9218   6899    -97    123  -1310       O  
ATOM    179  CB  ASP A  21     -33.946 -16.212  28.763  1.00 54.54           C  
ANISOU  179  CB  ASP A  21     4993   9117   6615    371   -189  -1524       C  
ATOM    180  CG  ASP A  21     -34.433 -17.529  28.145  1.00 56.06           C  
ANISOU  180  CG  ASP A  21     5118   9359   6823    234   -168  -1597       C  
ATOM    181  OD1 ASP A  21     -33.925 -18.624  28.480  1.00 55.95           O  
ANISOU  181  OD1 ASP A  21     5193   9267   6800     57    -74  -1523       O  
ATOM    182  OD2 ASP A  21     -35.346 -17.462  27.298  1.00 56.93           O  
ANISOU  182  OD2 ASP A  21     5093   9586   6952    310   -256  -1737       O  
ATOM    183  N   SER A  22     -34.431 -17.226  31.467  1.00 58.73           N  
ANISOU  183  N   SER A  22     5466   9700   7150     -6    111  -1575       N  
ATOM    184  CA  SER A  22     -34.899 -18.103  32.539  1.00 61.15           C  
ANISOU  184  CA  SER A  22     5743  10044   7448   -239    267  -1634       C  
ATOM    185  C   SER A  22     -35.126 -19.555  32.097  1.00 62.39           C  
ANISOU  185  C   SER A  22     5904  10199   7601   -423    317  -1667       C  
ATOM    186  O   SER A  22     -35.192 -20.453  32.938  1.00 64.35           O  
ANISOU  186  O   SER A  22     6215  10417   7820   -637    448  -1667       O  
ATOM    187  CB  SER A  22     -36.156 -17.532  33.215  1.00 62.74           C  
ANISOU  187  CB  SER A  22     5737  10427   7674   -248    324  -1825       C  
ATOM    188  OG  SER A  22     -37.283 -17.610  32.364  1.00 64.74           O  
ANISOU  188  OG  SER A  22     5775  10849   7974   -208    266  -2013       O  
ATOM    189  N   ASN A  23     -35.242 -19.784  30.789  1.00 61.44           N  
ANISOU  189  N   ASN A  23     5740  10102   7502   -343    212  -1693       N  
ATOM    190  CA  ASN A  23     -35.367 -21.140  30.251  1.00 60.30           C  
ANISOU  190  CA  ASN A  23     5617   9942   7352   -500    243  -1713       C  
ATOM    191  C   ASN A  23     -34.065 -21.702  29.667  1.00 59.31           C  
ANISOU  191  C   ASN A  23     5706   9631   7198   -481    195  -1530       C  
ATOM    192  O   ASN A  23     -34.058 -22.791  29.089  1.00 58.65           O  
ANISOU  192  O   ASN A  23     5661   9518   7107   -584    201  -1534       O  
ATOM    193  CB  ASN A  23     -36.485 -21.201  29.211  1.00 62.52           C  
ANISOU  193  CB  ASN A  23     5693  10386   7676   -452    166  -1893       C  
ATOM    194  CG  ASN A  23     -37.841 -20.870  29.796  1.00 65.31           C  
ANISOU  194  CG  ASN A  23     5807  10940   8068   -502    226  -2110       C  
ATOM    195  OD1 ASN A  23     -38.206 -21.345  30.877  1.00 65.50           O  
ANISOU  195  OD1 ASN A  23     5812  10996   8079   -704    382  -2161       O  
ATOM    196  ND2 ASN A  23     -38.598 -20.045  29.084  1.00 66.87           N  
ANISOU  196  ND2 ASN A  23     5826  11273   8308   -316    101  -2247       N  
ATOM    197  N   GLY A  24     -32.970 -20.961  29.821  1.00 57.46           N  
ANISOU  197  N   GLY A  24     5606   9276   6950   -352    151  -1382       N  
ATOM    198  CA  GLY A  24     -31.659 -21.424  29.382  1.00 55.45           C  
ANISOU  198  CA  GLY A  24     5541   8850   6675   -332    116  -1221       C  
ATOM    199  C   GLY A  24     -31.401 -21.278  27.891  1.00 53.83           C  
ANISOU  199  C   GLY A  24     5339   8633   6480   -191     -1  -1205       C  
ATOM    200  O   GLY A  24     -30.609 -22.029  27.315  1.00 52.41           O  
ANISOU  200  O   GLY A  24     5279   8347   6288   -216    -17  -1121       O  
ATOM    201  N   ARG A  25     -32.060 -20.304  27.271  1.00 52.88           N  
ANISOU  201  N   ARG A  25     5100   8617   6374    -37    -87  -1288       N  
ATOM    202  CA  ARG A  25     -31.912 -20.061  25.838  1.00 52.21           C  
ANISOU  202  CA  ARG A  25     5036   8520   6281    105   -206  -1282       C  
ATOM    203  C   ARG A  25     -31.146 -18.785  25.549  1.00 51.21           C  
ANISOU  203  C   ARG A  25     5004   8318   6134    292   -278  -1189       C  
ATOM    204  O   ARG A  25     -31.365 -17.759  26.203  1.00 50.10           O  
ANISOU  204  O   ARG A  25     4824   8214   5996    369   -282  -1207       O  
ATOM    205  CB  ARG A  25     -33.280 -19.995  25.171  1.00 52.73           C  
ANISOU  205  CB  ARG A  25     4920   8750   6367    148   -275  -1462       C  
ATOM    206  CG  ARG A  25     -33.989 -21.333  25.109  1.00 51.75           C  
ANISOU  206  CG  ARG A  25     4711   8693   6260    -39   -216  -1560       C  
ATOM    207  CD  ARG A  25     -35.467 -21.127  24.944  1.00 52.65           C  
ANISOU  207  CD  ARG A  25     4594   9001   6409    -21   -254  -1772       C  
ATOM    208  NE  ARG A  25     -36.194 -22.390  24.889  1.00 52.33           N  
ANISOU  208  NE  ARG A  25     4463   9033   6386   -219   -189  -1883       N  
ATOM    209  CZ  ARG A  25     -37.515 -22.489  24.965  1.00 51.62           C  
ANISOU  209  CZ  ARG A  25     4150   9125   6338   -274   -180  -2091       C  
ATOM    210  NH1 ARG A  25     -38.259 -21.397  25.107  1.00 46.15           N  
ANISOU  210  NH1 ARG A  25     3298   8562   5676   -129   -242  -2215       N  
ATOM    211  NH2 ARG A  25     -38.090 -23.681  24.901  1.00 57.06           N  
ANISOU  211  NH2 ARG A  25     4776   9866   7038   -475   -110  -2184       N  
ATOM    212  N   GLU A  26     -30.250 -18.857  24.568  1.00 51.17           N  
ANISOU  212  N   GLU A  26     5130   8206   6105    355   -327  -1096       N  
ATOM    213  CA  GLU A  26     -29.466 -17.694  24.163  1.00 52.80           C  
ANISOU  213  CA  GLU A  26     5450   8329   6281    511   -384  -1009       C  
ATOM    214  C   GLU A  26     -30.345 -16.647  23.490  1.00 53.65           C  
ANISOU  214  C   GLU A  26     5498   8520   6365    682   -499  -1105       C  
ATOM    215  O   GLU A  26     -31.118 -16.963  22.590  1.00 54.80           O  
ANISOU  215  O   GLU A  26     5580   8738   6504    717   -574  -1202       O  
ATOM    216  CB  GLU A  26     -28.300 -18.087  23.240  1.00 52.18           C  
ANISOU  216  CB  GLU A  26     5524   8120   6180    517   -390   -903       C  
ATOM    217  CG  GLU A  26     -27.226 -16.988  23.151  1.00 53.71           C  
ANISOU  217  CG  GLU A  26     5853   8206   6346    620   -400   -797       C  
ATOM    218  CD  GLU A  26     -26.141 -17.244  22.118  1.00 53.12           C  
ANISOU  218  CD  GLU A  26     5918   8019   6246    633   -401   -717       C  
ATOM    219  OE1 GLU A  26     -25.696 -18.402  21.949  1.00 53.70           O  
ANISOU  219  OE1 GLU A  26     6009   8054   6339    533   -359   -695       O  
ATOM    220  OE2 GLU A  26     -25.719 -16.262  21.478  1.00 54.92           O  
ANISOU  220  OE2 GLU A  26     6249   8192   6428    741   -440   -681       O  
ATOM    221  N   ARG A  27     -30.221 -15.402  23.938  1.00 55.01           N  
ANISOU  221  N   ARG A  27     5703   8679   6522    793   -524  -1082       N  
ATOM    222  CA  ARG A  27     -30.969 -14.284  23.363  1.00 58.91           C  
ANISOU  222  CA  ARG A  27     6174   9228   6981    980   -649  -1167       C  
ATOM    223  C   ARG A  27     -30.077 -13.056  23.180  1.00 58.05           C  
ANISOU  223  C   ARG A  27     6245   8995   6816   1105   -684  -1058       C  
ATOM    224  O   ARG A  27     -28.989 -12.982  23.751  1.00 58.31           O  
ANISOU  224  O   ARG A  27     6374   8926   6853   1039   -599   -937       O  
ATOM    225  CB  ARG A  27     -32.162 -13.912  24.254  1.00 61.38           C  
ANISOU  225  CB  ARG A  27     6299   9691   7331    999   -653  -1307       C  
ATOM    226  CG  ARG A  27     -33.279 -14.941  24.316  1.00 65.52           C  
ANISOU  226  CG  ARG A  27     6625  10363   7906    889   -630  -1457       C  
ATOM    227  CD  ARG A  27     -34.630 -14.261  24.185  1.00 74.13           C  
ANISOU  227  CD  ARG A  27     7544  11610   9011   1025   -734  -1647       C  
ATOM    228  NE  ARG A  27     -35.698 -15.023  24.835  1.00 81.33           N  
ANISOU  228  NE  ARG A  27     8230  12685   9987    886   -660  -1806       N  
ATOM    229  CZ  ARG A  27     -36.264 -14.698  25.999  1.00 83.12           C  
ANISOU  229  CZ  ARG A  27     8326  13008  10248    844   -585  -1889       C  
ATOM    230  NH1 ARG A  27     -35.882 -13.613  26.666  1.00 83.59           N  
ANISOU  230  NH1 ARG A  27     8455  13019  10288    942   -586  -1826       N  
ATOM    231  NH2 ARG A  27     -37.224 -15.461  26.501  1.00 84.90           N  
ANISOU  231  NH2 ARG A  27     8353  13380  10526    694   -502  -2042       N  
ATOM    232  N   THR A  28     -30.546 -12.095  22.388  1.00 59.45           N  
ANISOU  232  N   THR A  28     6476   9177   6935   1283   -813  -1111       N  
ATOM    233  CA  THR A  28     -29.885 -10.793  22.263  1.00 58.53           C  
ANISOU  233  CA  THR A  28     6540   8947   6752   1406   -852  -1029       C  
ATOM    234  C   THR A  28     -30.914  -9.679  22.423  1.00 60.07           C  
ANISOU  234  C   THR A  28     6684   9218   6922   1583   -970  -1142       C  
ATOM    235  O   THR A  28     -32.077  -9.833  22.041  1.00 61.78           O  
ANISOU  235  O   THR A  28     6768   9555   7151   1659  -1066  -1290       O  
ATOM    236  CB  THR A  28     -29.149 -10.641  20.910  1.00 57.90           C  
ANISOU  236  CB  THR A  28     6672   8739   6590   1457   -898   -953       C  
ATOM    237  OG1 THR A  28     -28.425 -11.841  20.624  1.00 58.91           O  
ANISOU  237  OG1 THR A  28     6808   8827   6750   1307   -806   -889       O  
ATOM    238  CG2 THR A  28     -28.164  -9.472  20.937  1.00 54.77           C  
ANISOU  238  CG2 THR A  28     6482   8200   6128   1514   -883   -843       C  
ATOM    239  N   ARG A  29     -30.484  -8.568  23.016  1.00 60.34           N  
ANISOU  239  N   ARG A  29     6816   9184   6926   1649   -964  -1083       N  
ATOM    240  CA  ARG A  29     -31.304  -7.361  23.086  1.00 61.98           C  
ANISOU  240  CA  ARG A  29     7025   9431   7093   1843  -1090  -1178       C  
ATOM    241  C   ARG A  29     -30.445  -6.110  22.961  1.00 62.55           C  
ANISOU  241  C   ARG A  29     7346   9344   7077   1933  -1114  -1066       C  
ATOM    242  O   ARG A  29     -29.242  -6.141  23.219  1.00 62.81           O  
ANISOU  242  O   ARG A  29     7494   9264   7108   1821  -1003   -926       O  
ATOM    243  CB  ARG A  29     -32.153  -7.324  24.365  1.00 61.28           C  
ANISOU  243  CB  ARG A  29     6714   9488   7081   1824  -1051  -1285       C  
ATOM    244  CG  ARG A  29     -31.365  -7.340  25.659  1.00 59.15           C  
ANISOU  244  CG  ARG A  29     6447   9176   6851   1687   -902  -1180       C  
ATOM    245  CD  ARG A  29     -32.283  -7.526  26.847  1.00 58.63           C  
ANISOU  245  CD  ARG A  29     6158   9262   6855   1639   -847  -1297       C  
ATOM    246  NE  ARG A  29     -31.525  -7.834  28.056  1.00 57.88           N  
ANISOU  246  NE  ARG A  29     6072   9124   6797   1478   -697  -1196       N  
ATOM    247  CZ  ARG A  29     -32.000  -8.511  29.099  1.00 56.70           C  
ANISOU  247  CZ  ARG A  29     5763   9075   6706   1343   -593  -1256       C  
ATOM    248  NH1 ARG A  29     -33.249  -8.971  29.103  1.00 59.35           N  
ANISOU  248  NH1 ARG A  29     5894   9574   7081   1333   -604  -1427       N  
ATOM    249  NH2 ARG A  29     -31.218  -8.739  30.141  1.00 52.64           N  
ANISOU  249  NH2 ARG A  29     5300   8493   6207   1213   -475  -1152       N  
ATOM    250  N   GLU A  30     -31.080  -5.021  22.547  1.00 64.29           N  
ANISOU  250  N   GLU A  30     7650   9554   7223   2138  -1264  -1139       N  
ATOM    251  CA  GLU A  30     -30.440  -3.722  22.453  1.00 64.59           C  
ANISOU  251  CA  GLU A  30     7939   9441   7163   2237  -1302  -1054       C  
ATOM    252  C   GLU A  30     -31.183  -2.794  23.404  1.00 64.18           C  
ANISOU  252  C   GLU A  30     7803   9458   7123   2363  -1360  -1142       C  
ATOM    253  O   GLU A  30     -32.403  -2.659  23.318  1.00 64.78           O  
ANISOU  253  O   GLU A  30     7742   9657   7213   2504  -1483  -1304       O  
ATOM    254  CB  GLU A  30     -30.524  -3.208  21.016  1.00 66.83           C  
ANISOU  254  CB  GLU A  30     8454   9621   7319   2384  -1447  -1062       C  
ATOM    255  CG  GLU A  30     -29.740  -1.941  20.737  1.00 69.31           C  
ANISOU  255  CG  GLU A  30     9082   9746   7507   2456  -1471   -959       C  
ATOM    256  CD  GLU A  30     -30.061  -1.345  19.374  1.00 75.36           C  
ANISOU  256  CD  GLU A  30    10094  10411   8127   2629  -1640   -993       C  
ATOM    257  OE1 GLU A  30     -30.322  -2.111  18.414  1.00 75.74           O  
ANISOU  257  OE1 GLU A  30    10131  10483   8163   2626  -1685  -1029       O  
ATOM    258  OE2 GLU A  30     -30.054  -0.100  19.261  1.00 80.37           O  
ANISOU  258  OE2 GLU A  30    10954  10933   8650   2772  -1734   -983       O  
ATOM    259  N   VAL A  31     -30.453  -2.179  24.328  1.00 62.94           N  
ANISOU  259  N   VAL A  31     7716   9229   6968   2311  -1272  -1047       N  
ATOM    260  CA  VAL A  31     -31.071  -1.333  25.348  1.00 62.50           C  
ANISOU  260  CA  VAL A  31     7582   9237   6929   2414  -1307  -1123       C  
ATOM    261  C   VAL A  31     -30.469   0.072  25.363  1.00 62.07           C  
ANISOU  261  C   VAL A  31     7794   9020   6770   2518  -1354  -1041       C  
ATOM    262  O   VAL A  31     -29.255   0.236  25.494  1.00 58.72           O  
ANISOU  262  O   VAL A  31     7526   8462   6322   2400  -1251   -893       O  
ATOM    263  CB  VAL A  31     -30.992  -1.974  26.765  1.00 61.77           C  
ANISOU  263  CB  VAL A  31     7278   9242   6949   2245  -1150  -1115       C  
ATOM    264  CG1 VAL A  31     -31.820  -1.176  27.780  1.00 59.87           C  
ANISOU  264  CG1 VAL A  31     6927   9092   6727   2357  -1187  -1224       C  
ATOM    265  CG2 VAL A  31     -31.463  -3.423  26.729  1.00 62.37           C  
ANISOU  265  CG2 VAL A  31     7131   9453   7115   2110  -1085  -1180       C  
ATOM    266  N   GLU A  32     -31.340   1.071  25.209  1.00 65.17           N  
ANISOU  266  N   GLU A  32     8237   9425   7099   2742  -1516  -1150       N  
ATOM    267  CA  GLU A  32     -30.990   2.487  25.350  1.00 65.91           C  
ANISOU  267  CA  GLU A  32     8578   9376   7089   2865  -1580  -1099       C  
ATOM    268  C   GLU A  32     -30.904   2.797  26.841  1.00 63.21           C  
ANISOU  268  C   GLU A  32     8114   9085   6817   2809  -1482  -1091       C  
ATOM    269  O   GLU A  32     -31.856   3.293  27.445  1.00 65.16           O  
ANISOU  269  O   GLU A  32     8239   9433   7085   2948  -1558  -1221       O  
ATOM    270  CB  GLU A  32     -32.031   3.379  24.652  1.00 68.96           C  
ANISOU  270  CB  GLU A  32     9062   9758   7381   3145  -1809  -1235       C  
ATOM    271  CG  GLU A  32     -31.934   3.381  23.117  1.00 77.88           C  
ANISOU  271  CG  GLU A  32    10423  10774   8395   3221  -1924  -1216       C  
ATOM    272  CD  GLU A  32     -33.277   3.628  22.419  1.00 84.74           C  
ANISOU  272  CD  GLU A  32    11250  11724   9225   3477  -2157  -1405       C  
ATOM    273  OE1 GLU A  32     -33.473   4.723  21.848  1.00 86.96           O  
ANISOU  273  OE1 GLU A  32    11798  11877   9367   3685  -2328  -1428       O  
ATOM    274  OE2 GLU A  32     -34.139   2.723  22.435  1.00 88.04           O  
ANISOU  274  OE2 GLU A  32    11374  12329   9748   3472  -2175  -1539       O  
ATOM    275  N   TYR A  33     -29.757   2.474  27.427  1.00 59.36           N  
ANISOU  275  N   TYR A  33     7657   8530   6369   2608  -1317   -948       N  
ATOM    276  CA  TYR A  33     -29.567   2.544  28.869  1.00 56.20           C  
ANISOU  276  CA  TYR A  33     7137   8177   6041   2520  -1207   -928       C  
ATOM    277  C   TYR A  33     -29.398   3.979  29.326  1.00 55.73           C  
ANISOU  277  C   TYR A  33     7260   8012   5903   2642  -1264   -905       C  
ATOM    278  O   TYR A  33     -28.570   4.717  28.790  1.00 53.53           O  
ANISOU  278  O   TYR A  33     7252   7560   5528   2652  -1281   -803       O  
ATOM    279  CB  TYR A  33     -28.360   1.692  29.276  1.00 53.87           C  
ANISOU  279  CB  TYR A  33     6825   7834   5809   2279  -1034   -791       C  
ATOM    280  CG  TYR A  33     -27.993   1.711  30.749  1.00 49.14           C  
ANISOU  280  CG  TYR A  33     6139   7257   5275   2175   -921   -753       C  
ATOM    281  CD1 TYR A  33     -28.823   1.133  31.713  1.00 48.87           C  
ANISOU  281  CD1 TYR A  33     5864   7382   5323   2140   -876   -849       C  
ATOM    282  CD2 TYR A  33     -26.791   2.273  31.170  1.00 49.68           C  
ANISOU  282  CD2 TYR A  33     6372   7185   5321   2097   -855   -625       C  
ATOM    283  CE1 TYR A  33     -28.471   1.143  33.070  1.00 48.68           C  
ANISOU  283  CE1 TYR A  33     5787   7364   5344   2042   -772   -811       C  
ATOM    284  CE2 TYR A  33     -26.421   2.281  32.512  1.00 48.76           C  
ANISOU  284  CE2 TYR A  33     6188   7079   5258   2006   -763   -591       C  
ATOM    285  CZ  TYR A  33     -27.262   1.722  33.460  1.00 49.88           C  
ANISOU  285  CZ  TYR A  33     6113   7369   5470   1983   -725   -679       C  
ATOM    286  OH  TYR A  33     -26.877   1.742  34.785  1.00 45.76           O  
ANISOU  286  OH  TYR A  33     5554   6844   4987   1892   -637   -641       O  
ATOM    287  N   LYS A  34     -30.205   4.365  30.310  1.00 55.80           N  
ANISOU  287  N   LYS A  34     7125   8128   5949   2727  -1286  -1009       N  
ATOM    288  CA  LYS A  34     -30.113   5.693  30.905  1.00 57.47           C  
ANISOU  288  CA  LYS A  34     7489   8252   6095   2843  -1336   -998       C  
ATOM    289  C   LYS A  34     -29.279   5.625  32.186  1.00 56.59           C  
ANISOU  289  C   LYS A  34     7344   8116   6040   2673  -1179   -898       C  
ATOM    290  O   LYS A  34     -29.778   5.213  33.239  1.00 55.70           O  
ANISOU  290  O   LYS A  34     7016   8136   6010   2625  -1111   -965       O  
ATOM    291  CB  LYS A  34     -31.505   6.285  31.161  1.00 59.57           C  
ANISOU  291  CB  LYS A  34     7636   8641   6357   3069  -1473  -1185       C  
ATOM    292  CG  LYS A  34     -32.314   6.511  29.885  1.00 63.12           C  
ANISOU  292  CG  LYS A  34     8150   9096   6738   3274  -1663  -1294       C  
ATOM    293  CD  LYS A  34     -33.338   7.632  30.032  1.00 69.65           C  
ANISOU  293  CD  LYS A  34     8999   9954   7511   3549  -1840  -1448       C  
ATOM    294  CE  LYS A  34     -34.703   7.108  30.465  1.00 74.62           C  
ANISOU  294  CE  LYS A  34     9273  10830   8248   3626  -1871  -1667       C  
ATOM    295  NZ  LYS A  34     -35.843   7.918  29.918  1.00 75.54           N  
ANISOU  295  NZ  LYS A  34     9405  10987   8308   3936  -2107  -1858       N  
ATOM    296  N   PRO A  35     -27.996   6.022  32.091  1.00 55.03           N  
ANISOU  296  N   PRO A  35     7365   7747   5796   2574  -1121   -746       N  
ATOM    297  CA  PRO A  35     -27.083   5.906  33.214  1.00 53.02           C  
ANISOU  297  CA  PRO A  35     7090   7458   5597   2409   -984   -651       C  
ATOM    298  C   PRO A  35     -27.277   7.020  34.234  1.00 53.71           C  
ANISOU  298  C   PRO A  35     7233   7521   5654   2503  -1012   -674       C  
ATOM    299  O   PRO A  35     -27.932   8.024  33.949  1.00 58.00           O  
ANISOU  299  O   PRO A  35     7883   8038   6116   2699  -1142   -744       O  
ATOM    300  CB  PRO A  35     -25.711   6.028  32.552  1.00 52.86           C  
ANISOU  300  CB  PRO A  35     7284   7267   5531   2292   -932   -510       C  
ATOM    301  CG  PRO A  35     -25.949   6.878  31.339  1.00 53.45           C  
ANISOU  301  CG  PRO A  35     7589   7240   5479   2445  -1060   -525       C  
ATOM    302  CD  PRO A  35     -27.386   6.735  30.950  1.00 55.61           C  
ANISOU  302  CD  PRO A  35     7734   7645   5750   2625  -1189   -672       C  
ATOM    303  N   SER A  36     -26.717   6.833  35.419  1.00 51.77           N  
ANISOU  303  N   SER A  36     6922   7279   5467   2372   -900   -619       N  
ATOM    304  CA  SER A  36     -26.696   7.888  36.415  1.00 52.87           C  
ANISOU  304  CA  SER A  36     7139   7373   5574   2436   -913   -620       C  
ATOM    305  C   SER A  36     -25.273   8.157  36.872  1.00 50.70           C  
ANISOU  305  C   SER A  36     7011   6954   5297   2288   -827   -479       C  
ATOM    306  O   SER A  36     -24.442   7.253  36.904  1.00 49.47           O  
ANISOU  306  O   SER A  36     6801   6789   5206   2114   -729   -405       O  
ATOM    307  CB  SER A  36     -27.573   7.533  37.618  1.00 52.43           C  
ANISOU  307  CB  SER A  36     6855   7478   5588   2441   -868   -721       C  
ATOM    308  OG  SER A  36     -28.931   7.426  37.244  1.00 52.87           O  
ANISOU  308  OG  SER A  36     6762   7676   5649   2589   -951   -878       O  
ATOM    309  N   LEU A  37     -25.008   9.420  37.190  1.00 51.30           N  
ANISOU  309  N   LEU A  37     7276   6917   5298   2366   -872   -453       N  
ATOM    310  CA  LEU A  37     -23.791   9.839  37.865  1.00 50.86           C  
ANISOU  310  CA  LEU A  37     7341   6740   5245   2240   -799   -347       C  
ATOM    311  C   LEU A  37     -24.203  10.776  38.996  1.00 51.90           C  
ANISOU  311  C   LEU A  37     7499   6871   5349   2337   -830   -387       C  
ATOM    312  O   LEU A  37     -25.384  11.094  39.133  1.00 54.15           O  
ANISOU  312  O   LEU A  37     7715   7247   5613   2502   -907   -499       O  
ATOM    313  CB  LEU A  37     -22.831  10.522  36.891  1.00 50.39           C  
ANISOU  313  CB  LEU A  37     7542   6503   5101   2208   -813   -262       C  
ATOM    314  CG  LEU A  37     -22.313   9.701  35.703  1.00 47.27           C  
ANISOU  314  CG  LEU A  37     7152   6089   4718   2107   -775   -220       C  
ATOM    315  CD1 LEU A  37     -21.571  10.604  34.753  1.00 47.70           C  
ANISOU  315  CD1 LEU A  37     7498   5965   4661   2098   -794   -160       C  
ATOM    316  CD2 LEU A  37     -21.426   8.526  36.122  1.00 42.17           C  
ANISOU  316  CD2 LEU A  37     6348   5485   4191   1905   -650   -166       C  
ATOM    317  N   PHE A  38     -23.247  11.200  39.819  1.00 51.88           N  
ANISOU  317  N   PHE A  38     7585   6774   5352   2237   -772   -309       N  
ATOM    318  CA  PHE A  38     -23.573  11.976  41.017  1.00 51.88           C  
ANISOU  318  CA  PHE A  38     7599   6777   5334   2309   -787   -342       C  
ATOM    319  C   PHE A  38     -22.645  13.165  41.263  1.00 51.99           C  
ANISOU  319  C   PHE A  38     7859   6616   5280   2292   -800   -266       C  
ATOM    320  O   PHE A  38     -21.448  13.116  40.974  1.00 50.24           O  
ANISOU  320  O   PHE A  38     7736   6288   5067   2146   -745   -174       O  
ATOM    321  CB  PHE A  38     -23.579  11.072  42.255  1.00 49.93           C  
ANISOU  321  CB  PHE A  38     7151   6637   5184   2193   -690   -350       C  
ATOM    322  CG  PHE A  38     -24.407   9.825  42.102  1.00 47.58           C  
ANISOU  322  CG  PHE A  38     6619   6504   4954   2171   -655   -422       C  
ATOM    323  CD1 PHE A  38     -23.969   8.767  41.308  1.00 45.02           C  
ANISOU  323  CD1 PHE A  38     6233   6194   4679   2057   -614   -379       C  
ATOM    324  CD2 PHE A  38     -25.612   9.698  42.770  1.00 47.20           C  
ANISOU  324  CD2 PHE A  38     6412   6599   4921   2253   -654   -540       C  
ATOM    325  CE1 PHE A  38     -24.725   7.619  41.166  1.00 42.69           C  
ANISOU  325  CE1 PHE A  38     5736   6043   4442   2027   -581   -446       C  
ATOM    326  CE2 PHE A  38     -26.372   8.543  42.643  1.00 46.92           C  
ANISOU  326  CE2 PHE A  38     6164   6718   4948   2211   -610   -615       C  
ATOM    327  CZ  PHE A  38     -25.929   7.504  41.837  1.00 46.65           C  
ANISOU  327  CZ  PHE A  38     6082   6686   4957   2097   -576   -564       C  
ATOM    328  N   ALA A  39     -23.214  14.229  41.812  1.00 53.69           N  
ANISOU  328  N   ALA A  39     8165   6806   5429   2439   -871   -316       N  
ATOM    329  CA  ALA A  39     -22.443  15.384  42.239  1.00 55.68           C  
ANISOU  329  CA  ALA A  39     8644   6899   5614   2425   -882   -254       C  
ATOM    330  C   ALA A  39     -22.671  15.633  43.723  1.00 57.56           C  
ANISOU  330  C   ALA A  39     8808   7183   5880   2441   -859   -284       C  
ATOM    331  O   ALA A  39     -23.738  15.309  44.255  1.00 57.67           O  
ANISOU  331  O   ALA A  39     8649   7341   5924   2534   -867   -380       O  
ATOM    332  CB  ALA A  39     -22.835  16.604  41.433  1.00 56.13           C  
ANISOU  332  CB  ALA A  39     8950   6841   5536   2599  -1005   -279       C  
ATOM    333  N   HIS A  40     -21.664  16.194  44.389  1.00 59.91           N  
ANISOU  333  N   HIS A  40     9234   7361   6167   2342   -823   -209       N  
ATOM    334  CA  HIS A  40     -21.814  16.647  45.773  1.00 62.65           C  
ANISOU  334  CA  HIS A  40     9569   7720   6518   2369   -814   -231       C  
ATOM    335  C   HIS A  40     -22.839  17.773  45.852  1.00 66.49           C  
ANISOU  335  C   HIS A  40    10159   8196   6907   2595   -920   -317       C  
ATOM    336  O   HIS A  40     -22.880  18.658  44.994  1.00 65.77           O  
ANISOU  336  O   HIS A  40    10276   7994   6719   2698  -1008   -314       O  
ATOM    337  CB  HIS A  40     -20.472  17.094  46.360  1.00 60.78           C  
ANISOU  337  CB  HIS A  40     9466   7342   6283   2222   -772   -139       C  
ATOM    338  CG  HIS A  40     -19.551  15.959  46.675  1.00 59.65           C  
ANISOU  338  CG  HIS A  40     9184   7231   6249   2023   -678    -83       C  
ATOM    339  ND1 HIS A  40     -18.371  15.747  45.996  1.00 60.64           N  
ANISOU  339  ND1 HIS A  40     9367   7271   6403   1876   -640    -14       N  
ATOM    340  CD2 HIS A  40     -19.650  14.957  47.582  1.00 57.27           C  
ANISOU  340  CD2 HIS A  40     8696   7035   6031   1953   -620    -95       C  
ATOM    341  CE1 HIS A  40     -17.775  14.671  46.480  1.00 58.63           C  
ANISOU  341  CE1 HIS A  40     8957   7069   6251   1739   -574     10       C  
ATOM    342  NE2 HIS A  40     -18.531  14.172  47.442  1.00 56.91           N  
ANISOU  342  NE2 HIS A  40     8603   6959   6060   1782   -565    -33       N  
ATOM    343  N   CYS A  41     -23.677  17.716  46.879  1.00 71.43           N  
ANISOU  343  N   CYS A  41    10648   8937   7556   2672   -911   -400       N  
ATOM    344  CA  CYS A  41     -24.743  18.696  47.057  1.00 77.70           C  
ANISOU  344  CA  CYS A  41    11500   9750   8274   2901  -1010   -508       C  
ATOM    345  C   CYS A  41     -24.713  19.298  48.458  1.00 79.14           C  
ANISOU  345  C   CYS A  41    11715   9913   8441   2912   -986   -521       C  
ATOM    346  O   CYS A  41     -24.211  18.668  49.393  1.00 77.73           O  
ANISOU  346  O   CYS A  41    11439   9766   8328   2756   -886   -478       O  
ATOM    347  CB  CYS A  41     -26.106  18.047  46.796  1.00 79.57           C  
ANISOU  347  CB  CYS A  41    11502  10182   8551   3024  -1030   -648       C  
ATOM    348  SG  CYS A  41     -26.440  16.563  47.794  1.00 81.65           S  
ANISOU  348  SG  CYS A  41    11443  10642   8938   2867   -878   -688       S  
ATOM    349  N   PRO A  42     -25.243  20.525  48.609  1.00 82.88           N  
ANISOU  349  N   PRO A  42    12342  10327   8823   3104  -1086   -584       N  
ATOM    350  CA  PRO A  42     -25.410  21.073  49.951  1.00 85.23           C  
ANISOU  350  CA  PRO A  42    12650  10628   9105   3139  -1066   -619       C  
ATOM    351  C   PRO A  42     -26.123  20.084  50.878  1.00 86.85           C  
ANISOU  351  C   PRO A  42    12573  11031   9396   3094   -963   -703       C  
ATOM    352  O   PRO A  42     -27.042  19.379  50.448  1.00 87.05           O  
ANISOU  352  O   PRO A  42    12397  11213   9465   3148   -956   -801       O  
ATOM    353  CB  PRO A  42     -26.280  22.306  49.712  1.00 86.62           C  
ANISOU  353  CB  PRO A  42    12969  10766   9179   3403  -1205   -721       C  
ATOM    354  CG  PRO A  42     -25.912  22.757  48.342  1.00 86.02           C  
ANISOU  354  CG  PRO A  42    13103  10551   9029   3445  -1300   -665       C  
ATOM    355  CD  PRO A  42     -25.594  21.509  47.564  1.00 84.71           C  
ANISOU  355  CD  PRO A  42    12782  10457   8947   3291  -1228   -614       C  
ATOM    356  N   GLU A  43     -25.670  20.029  52.128  1.00 88.57           N  
ANISOU  356  N   GLU A  43    12791  11232   9630   2984   -884   -665       N  
ATOM    357  CA  GLU A  43     -26.282  19.205  53.174  1.00 91.63           C  
ANISOU  357  CA  GLU A  43    12964  11778  10073   2925   -775   -739       C  
ATOM    358  C   GLU A  43     -27.798  19.406  53.291  1.00 94.16           C  
ANISOU  358  C   GLU A  43    13134  12260  10381   3117   -797   -925       C  
ATOM    359  O   GLU A  43     -28.538  18.456  53.551  1.00 94.78           O  
ANISOU  359  O   GLU A  43    12981  12510  10519   3069   -707  -1015       O  
ATOM    360  CB  GLU A  43     -25.619  19.510  54.520  1.00 92.81           C  
ANISOU  360  CB  GLU A  43    13213  11847  10204   2831   -723   -680       C  
ATOM    361  CG  GLU A  43     -24.377  18.680  54.819  1.00 94.19           C  
ANISOU  361  CG  GLU A  43    13400  11953  10434   2599   -651   -546       C  
ATOM    362  CD  GLU A  43     -24.622  17.624  55.887  1.00 95.80           C  
ANISOU  362  CD  GLU A  43    13452  12266  10682   2476   -532   -573       C  
ATOM    363  OE1 GLU A  43     -25.017  18.000  57.017  1.00 97.61           O  
ANISOU  363  OE1 GLU A  43    13700  12514  10871   2510   -499   -627       O  
ATOM    364  OE2 GLU A  43     -24.408  16.423  55.601  1.00 93.20           O  
ANISOU  364  OE2 GLU A  43    13001  11992  10418   2342   -471   -539       O  
ATOM    365  N   SER A  44     -28.248  20.642  53.086  1.00 95.95           N  
ANISOU  365  N   SER A  44    13495  12430  10531   3331   -917   -992       N  
ATOM    366  CA  SER A  44     -29.663  20.997  53.207  1.00 98.83           C  
ANISOU  366  CA  SER A  44    13726  12942  10883   3545   -960  -1190       C  
ATOM    367  C   SER A  44     -30.527  20.416  52.078  1.00 99.63           C  
ANISOU  367  C   SER A  44    13647  13179  11028   3635  -1008  -1295       C  
ATOM    368  O   SER A  44     -31.521  21.020  51.667  1.00100.65           O  
ANISOU  368  O   SER A  44    13743  13372  11128   3870  -1120  -1448       O  
ATOM    369  CB  SER A  44     -29.825  22.524  53.288  1.00100.13           C  
ANISOU  369  CB  SER A  44    14114  12985  10945   3765  -1097  -1230       C  
ATOM    370  OG  SER A  44     -29.373  23.165  52.103  1.00100.02           O  
ANISOU  370  OG  SER A  44    14321  12815  10867   3847  -1232  -1156       O  
ATOM    371  N   GLN A  45     -30.148  19.238  51.591  1.00 98.78           N  
ANISOU  371  N   GLN A  45    13426  13116  10991   3456   -931  -1223       N  
ATOM    372  CA  GLN A  45     -30.876  18.582  50.515  1.00100.65           C  
ANISOU  372  CA  GLN A  45    13492  13477  11273   3514   -968  -1311       C  
ATOM    373  C   GLN A  45     -31.081  17.105  50.850  1.00 99.79           C  
ANISOU  373  C   GLN A  45    13128  13528  11261   3314   -811  -1330       C  
ATOM    374  O   GLN A  45     -30.136  16.307  50.800  1.00 98.57           O  
ANISOU  374  O   GLN A  45    13000  13312  11141   3106   -733  -1185       O  
ATOM    375  CB  GLN A  45     -30.136  18.763  49.182  1.00100.73           C  
ANISOU  375  CB  GLN A  45    13687  13338  11247   3521  -1070  -1189       C  
ATOM    376  CG  GLN A  45     -31.034  18.745  47.944  1.00103.17           C  
ANISOU  376  CG  GLN A  45    13926  13723  11552   3701  -1194  -1307       C  
ATOM    377  CD  GLN A  45     -30.455  19.543  46.778  1.00104.39           C  
ANISOU  377  CD  GLN A  45    14369  13682  11612   3794  -1337  -1214       C  
ATOM    378  OE1 GLN A  45     -30.189  18.995  45.707  1.00103.24           O  
ANISOU  378  OE1 GLN A  45    14233  13516  11477   3740  -1356  -1160       O  
ATOM    379  NE2 GLN A  45     -30.258  20.845  46.987  1.00104.96           N  
ANISOU  379  NE2 GLN A  45    14694  13604  11583   3927  -1433  -1198       N  
ATOM    380  N   ALA A  46     -32.319  16.761  51.207  1.00100.15           N  
ANISOU  380  N   ALA A  46    12931  13775  11347   3377   -763  -1521       N  
ATOM    381  CA  ALA A  46     -32.688  15.395  51.588  1.00 98.30           C  
ANISOU  381  CA  ALA A  46    12456  13702  11192   3188   -603  -1569       C  
ATOM    382  C   ALA A  46     -32.494  14.413  50.428  1.00 95.91           C  
ANISOU  382  C   ALA A  46    12078  13421  10941   3100   -613  -1515       C  
ATOM    383  O   ALA A  46     -33.038  14.605  49.335  1.00 96.52           O  
ANISOU  383  O   ALA A  46    12114  13538  11021   3256   -733  -1594       O  
ATOM    384  CB  ALA A  46     -34.128  15.350  52.111  1.00100.24           C  
ANISOU  384  CB  ALA A  46    12455  14166  11466   3283   -552  -1813       C  
ATOM    385  N   THR A  47     -31.705  13.370  50.677  1.00 91.48           N  
ANISOU  385  N   THR A  47    11514  12827  10418   2860   -496  -1384       N  
ATOM    386  CA  THR A  47     -31.363  12.389  49.646  1.00 88.05           C  
ANISOU  386  CA  THR A  47    11028  12395  10030   2757   -496  -1315       C  
ATOM    387  C   THR A  47     -31.086  11.007  50.243  1.00 83.95           C  
ANISOU  387  C   THR A  47    10405  11929   9565   2504   -333  -1266       C  
ATOM    388  O   THR A  47     -30.991  10.858  51.462  1.00 84.25           O  
ANISOU  388  O   THR A  47    10451  11970   9591   2399   -227  -1259       O  
ATOM    389  CB  THR A  47     -30.152  12.868  48.799  1.00 87.47           C  
ANISOU  389  CB  THR A  47    11192  12120   9920   2764   -595  -1139       C  
ATOM    390  OG1 THR A  47     -29.854  11.900  47.786  1.00 87.51           O  
ANISOU  390  OG1 THR A  47    11143  12136   9972   2667   -589  -1082       O  
ATOM    391  CG2 THR A  47     -28.915  13.097  49.676  1.00 86.63           C  
ANISOU  391  CG2 THR A  47    11267  11858   9792   2631   -543   -982       C  
ATOM    392  N   LYS A  48     -30.964  10.001  49.381  1.00 79.94           N  
ANISOU  392  N   LYS A  48     9816  11452   9104   2410   -320  -1232       N  
ATOM    393  CA  LYS A  48     -30.583   8.656  49.820  1.00 76.30           C  
ANISOU  393  CA  LYS A  48     9294  11012   8684   2173   -185  -1169       C  
ATOM    394  C   LYS A  48     -29.230   8.180  49.259  1.00 71.59           C  
ANISOU  394  C   LYS A  48     8835  10263   8102   2058   -207   -981       C  
ATOM    395  O   LYS A  48     -28.882   7.007  49.400  1.00 72.24           O  
ANISOU  395  O   LYS A  48     8875  10354   8220   1881   -121   -928       O  
ATOM    396  CB  LYS A  48     -31.701   7.635  49.531  1.00 77.59           C  
ANISOU  396  CB  LYS A  48     9211  11368   8899   2119   -111  -1318       C  
ATOM    397  CG  LYS A  48     -31.958   7.338  48.050  1.00 77.04           C  
ANISOU  397  CG  LYS A  48     9067  11341   8866   2193   -206  -1345       C  
ATOM    398  CD  LYS A  48     -32.767   6.056  47.874  1.00 76.17           C  
ANISOU  398  CD  LYS A  48     8734  11396   8812   2068   -108  -1454       C  
ATOM    399  CE  LYS A  48     -32.990   5.740  46.407  1.00 73.93           C  
ANISOU  399  CE  LYS A  48     8382  11146   8560   2140   -207  -1477       C  
ATOM    400  NZ  LYS A  48     -33.785   4.496  46.204  1.00 72.60           N  
ANISOU  400  NZ  LYS A  48     7996  11138   8449   2014   -116  -1590       N  
ATOM    401  N   TYR A  49     -28.468   9.087  48.644  1.00 66.76           N  
ANISOU  401  N   TYR A  49     8395   9512   7459   2153   -318   -888       N  
ATOM    402  CA  TYR A  49     -27.160   8.741  48.070  1.00 61.12           C  
ANISOU  402  CA  TYR A  49     7803   8659   6761   2049   -335   -729       C  
ATOM    403  C   TYR A  49     -26.004   9.491  48.729  1.00 60.32           C  
ANISOU  403  C   TYR A  49     7899   8392   6627   2018   -351   -611       C  
ATOM    404  O   TYR A  49     -25.992  10.718  48.776  1.00 60.57           O  
ANISOU  404  O   TYR A  49     8054   8356   6605   2147   -424   -616       O  
ATOM    405  CB  TYR A  49     -27.134   8.991  46.565  1.00 58.13           C  
ANISOU  405  CB  TYR A  49     7459   8252   6375   2147   -437   -719       C  
ATOM    406  CG  TYR A  49     -28.223   8.289  45.796  1.00 56.16           C  
ANISOU  406  CG  TYR A  49     7021   8158   6159   2189   -442   -838       C  
ATOM    407  CD1 TYR A  49     -29.401   8.954  45.457  1.00 54.27           C  
ANISOU  407  CD1 TYR A  49     6708   8016   5896   2383   -523   -987       C  
ATOM    408  CD2 TYR A  49     -28.077   6.962  45.397  1.00 53.79           C  
ANISOU  408  CD2 TYR A  49     6615   7907   5916   2042   -377   -812       C  
ATOM    409  CE1 TYR A  49     -30.405   8.317  44.743  1.00 52.80           C  
ANISOU  409  CE1 TYR A  49     6336   7980   5747   2425   -538  -1112       C  
ATOM    410  CE2 TYR A  49     -29.078   6.314  44.679  1.00 53.50           C  
ANISOU  410  CE2 TYR A  49     6404   8013   5911   2074   -384   -927       C  
ATOM    411  CZ  TYR A  49     -30.237   6.999  44.359  1.00 55.02           C  
ANISOU  411  CZ  TYR A  49     6514   8307   6084   2263   -465  -1079       C  
ATOM    412  OH  TYR A  49     -31.227   6.362  43.652  1.00 58.65           O  
ANISOU  412  OH  TYR A  49     6789   8915   6582   2296   -481  -1208       O  
ATOM    413  N   PHE A  50     -25.027   8.735  49.219  1.00 60.59           N  
ANISOU  413  N   PHE A  50     7967   8359   6693   1849   -291   -511       N  
ATOM    414  CA  PHE A  50     -23.859   9.298  49.902  1.00 60.55           C  
ANISOU  414  CA  PHE A  50     8128   8205   6671   1799   -305   -408       C  
ATOM    415  C   PHE A  50     -22.576   8.694  49.344  1.00 58.08           C  
ANISOU  415  C   PHE A  50     7865   7796   6406   1677   -309   -296       C  
ATOM    416  O   PHE A  50     -22.572   7.556  48.884  1.00 58.24           O  
ANISOU  416  O   PHE A  50     7785   7868   6474   1592   -271   -291       O  
ATOM    417  CB  PHE A  50     -23.945   9.038  51.413  1.00 60.75           C  
ANISOU  417  CB  PHE A  50     8152   8245   6684   1723   -231   -421       C  
ATOM    418  CG  PHE A  50     -25.114   9.714  52.081  1.00 64.21           C  
ANISOU  418  CG  PHE A  50     8548   8774   7075   1837   -214   -538       C  
ATOM    419  CD1 PHE A  50     -26.363   9.095  52.130  1.00 64.35           C  
ANISOU  419  CD1 PHE A  50     8389   8958   7104   1842   -147   -664       C  
ATOM    420  CD2 PHE A  50     -24.965  10.969  52.665  1.00 64.40           C  
ANISOU  420  CD2 PHE A  50     8704   8720   7045   1934   -263   -535       C  
ATOM    421  CE1 PHE A  50     -27.443   9.719  52.743  1.00 66.18           C  
ANISOU  421  CE1 PHE A  50     8561   9286   7299   1947   -126   -793       C  
ATOM    422  CE2 PHE A  50     -26.042  11.602  53.282  1.00 65.00           C  
ANISOU  422  CE2 PHE A  50     8737   8882   7078   2048   -249   -654       C  
ATOM    423  CZ  PHE A  50     -27.281  10.976  53.323  1.00 66.16           C  
ANISOU  423  CZ  PHE A  50     8692   9204   7242   2057   -179   -789       C  
ATOM    424  N   ASP A  51     -21.485   9.450  49.382  1.00 56.01           N  
ANISOU  424  N   ASP A  51     7753   7395   6132   1665   -352   -218       N  
ATOM    425  CA  ASP A  51     -20.207   8.891  48.979  1.00 54.06           C  
ANISOU  425  CA  ASP A  51     7537   7063   5939   1543   -348   -132       C  
ATOM    426  C   ASP A  51     -19.636   8.042  50.112  1.00 54.34           C  
ANISOU  426  C   ASP A  51     7554   7081   6012   1420   -306   -101       C  
ATOM    427  O   ASP A  51     -20.195   8.008  51.210  1.00 56.05           O  
ANISOU  427  O   ASP A  51     7763   7336   6199   1424   -274   -136       O  
ATOM    428  CB  ASP A  51     -19.242   9.981  48.496  1.00 53.31           C  
ANISOU  428  CB  ASP A  51     7599   6834   5823   1559   -401    -76       C  
ATOM    429  CG  ASP A  51     -18.731  10.871  49.604  1.00 55.35           C  
ANISOU  429  CG  ASP A  51     7977   7001   6051   1560   -419    -54       C  
ATOM    430  OD1 ASP A  51     -18.954  10.583  50.803  1.00 55.68           O  
ANISOU  430  OD1 ASP A  51     7991   7072   6093   1537   -393    -70       O  
ATOM    431  OD2 ASP A  51     -18.077  11.878  49.258  1.00 56.51           O  
ANISOU  431  OD2 ASP A  51     8263   7040   6168   1575   -458    -21       O  
ATOM    432  N   ILE A  52     -18.535   7.350  49.849  1.00 53.32           N  
ANISOU  432  N   ILE A  52     7425   6892   5942   1314   -307    -43       N  
ATOM    433  CA  ILE A  52     -17.946   6.443  50.837  1.00 53.79           C  
ANISOU  433  CA  ILE A  52     7480   6923   6034   1210   -288    -18       C  
ATOM    434  C   ILE A  52     -17.598   7.165  52.145  1.00 53.98           C  
ANISOU  434  C   ILE A  52     7615   6872   6022   1216   -310     -7       C  
ATOM    435  O   ILE A  52     -17.513   6.534  53.200  1.00 53.39           O  
ANISOU  435  O   ILE A  52     7558   6786   5941   1158   -294     -4       O  
ATOM    436  CB  ILE A  52     -16.707   5.683  50.266  1.00 54.07           C  
ANISOU  436  CB  ILE A  52     7499   6900   6146   1117   -306     28       C  
ATOM    437  CG1 ILE A  52     -15.484   6.597  50.184  1.00 51.69           C  
ANISOU  437  CG1 ILE A  52     7290   6485   5865   1105   -353     62       C  
ATOM    438  CG2 ILE A  52     -17.024   5.100  48.882  1.00 53.57           C  
ANISOU  438  CG2 ILE A  52     7342   6902   6110   1117   -287     18       C  
ATOM    439  CD1 ILE A  52     -14.245   5.893  49.730  1.00 55.03           C  
ANISOU  439  CD1 ILE A  52     7678   6860   6371   1015   -368     83       C  
ATOM    440  N   TYR A  53     -17.426   8.487  52.061  1.00 53.58           N  
ANISOU  440  N   TYR A  53     7656   6763   5938   1288   -348     -1       N  
ATOM    441  CA  TYR A  53     -17.086   9.317  53.214  1.00 54.89           C  
ANISOU  441  CA  TYR A  53     7938   6852   6066   1303   -376      8       C  
ATOM    442  C   TYR A  53     -18.318   9.884  53.930  1.00 57.55           C  
ANISOU  442  C   TYR A  53     8288   7252   6328   1396   -351    -48       C  
ATOM    443  O   TYR A  53     -18.182  10.687  54.855  1.00 57.87           O  
ANISOU  443  O   TYR A  53     8432   7233   6325   1425   -372    -46       O  
ATOM    444  CB  TYR A  53     -16.154  10.462  52.794  1.00 54.02           C  
ANISOU  444  CB  TYR A  53     7935   6632   5957   1315   -428     41       C  
ATOM    445  CG  TYR A  53     -14.970  10.017  51.968  1.00 52.98           C  
ANISOU  445  CG  TYR A  53     7776   6450   5902   1223   -439     75       C  
ATOM    446  CD1 TYR A  53     -14.929  10.259  50.597  1.00 53.82           C  
ANISOU  446  CD1 TYR A  53     7876   6560   6014   1234   -431     80       C  
ATOM    447  CD2 TYR A  53     -13.893   9.343  52.556  1.00 51.45           C  
ANISOU  447  CD2 TYR A  53     7569   6207   5774   1128   -460     92       C  
ATOM    448  CE1 TYR A  53     -13.847   9.848  49.825  1.00 53.86           C  
ANISOU  448  CE1 TYR A  53     7850   6525   6087   1141   -426     99       C  
ATOM    449  CE2 TYR A  53     -12.811   8.925  51.798  1.00 50.85           C  
ANISOU  449  CE2 TYR A  53     7448   6097   5777   1048   -468    102       C  
ATOM    450  CZ  TYR A  53     -12.795   9.181  50.433  1.00 53.65           C  
ANISOU  450  CZ  TYR A  53     7786   6463   6136   1049   -441    105       C  
ATOM    451  OH  TYR A  53     -11.725   8.778  49.669  1.00 57.41           O  
ANISOU  451  OH  TYR A  53     8213   6911   6688    963   -434    104       O  
ATOM    452  N   GLY A  54     -19.511   9.472  53.501  1.00 58.53           N  
ANISOU  452  N   GLY A  54     8301   7500   6439   1442   -306   -107       N  
ATOM    453  CA  GLY A  54     -20.758   9.920  54.124  1.00 59.58           C  
ANISOU  453  CA  GLY A  54     8411   7717   6510   1530   -272   -188       C  
ATOM    454  C   GLY A  54     -21.086  11.372  53.822  1.00 60.79           C  
ANISOU  454  C   GLY A  54     8643   7843   6613   1676   -330   -215       C  
ATOM    455  O   GLY A  54     -21.689  12.068  54.643  1.00 61.31           O  
ANISOU  455  O   GLY A  54     8748   7923   6622   1751   -324   -267       O  
ATOM    456  N   LYS A  55     -20.661  11.828  52.648  1.00 60.15           N  
ANISOU  456  N   LYS A  55     8601   7709   6542   1713   -386   -182       N  
ATOM    457  CA  LYS A  55     -20.976  13.165  52.152  1.00 60.21           C  
ANISOU  457  CA  LYS A  55     8714   7675   6490   1856   -452   -206       C  
ATOM    458  C   LYS A  55     -22.124  13.041  51.154  1.00 58.33           C  
ANISOU  458  C   LYS A  55     8371   7551   6242   1968   -466   -285       C  
ATOM    459  O   LYS A  55     -22.113  12.128  50.322  1.00 57.94           O  
ANISOU  459  O   LYS A  55     8222   7553   6241   1911   -446   -276       O  
ATOM    460  CB  LYS A  55     -19.743  13.796  51.491  1.00 61.40           C  
ANISOU  460  CB  LYS A  55     9010   7679   6642   1813   -502   -123       C  
ATOM    461  CG  LYS A  55     -18.736  14.410  52.481  1.00 66.04           C  
ANISOU  461  CG  LYS A  55     9729   8144   7220   1751   -516    -72       C  
ATOM    462  CD  LYS A  55     -17.267  14.082  52.141  1.00 69.47           C  
ANISOU  462  CD  LYS A  55    10193   8483   7718   1606   -515      1       C  
ATOM    463  CE  LYS A  55     -16.884  14.366  50.677  1.00 72.02           C  
ANISOU  463  CE  LYS A  55    10564   8761   8040   1599   -530     24       C  
ATOM    464  NZ  LYS A  55     -16.946  15.812  50.293  1.00 73.39           N  
ANISOU  464  NZ  LYS A  55    10925   8835   8124   1687   -580     24       N  
ATOM    465  N   PRO A  56     -23.119  13.951  51.232  1.00 56.76           N  
ANISOU  465  N   PRO A  56     8193   7391   5982   2134   -510   -371       N  
ATOM    466  CA  PRO A  56     -24.340  13.844  50.423  1.00 56.64           C  
ANISOU  466  CA  PRO A  56     8059   7501   5960   2262   -537   -476       C  
ATOM    467  C   PRO A  56     -24.106  14.085  48.932  1.00 56.06           C  
ANISOU  467  C   PRO A  56     8057   7371   5873   2315   -612   -445       C  
ATOM    468  O   PRO A  56     -23.337  14.975  48.560  1.00 57.71           O  
ANISOU  468  O   PRO A  56     8460   7432   6034   2331   -668   -375       O  
ATOM    469  CB  PRO A  56     -25.257  14.938  51.004  1.00 57.24           C  
ANISOU  469  CB  PRO A  56     8173   7605   5971   2439   -582   -578       C  
ATOM    470  CG  PRO A  56     -24.600  15.406  52.248  1.00 57.26           C  
ANISOU  470  CG  PRO A  56     8291   7516   5949   2378   -553   -524       C  
ATOM    471  CD  PRO A  56     -23.139  15.158  52.071  1.00 57.07           C  
ANISOU  471  CD  PRO A  56     8371   7357   5954   2222   -547   -384       C  
ATOM    472  N   CYS A  57     -24.780  13.292  48.101  1.00 56.07           N  
ANISOU  472  N   CYS A  57     7910   7485   5908   2332   -608   -500       N  
ATOM    473  CA  CYS A  57     -24.671  13.367  46.642  1.00 56.29           C  
ANISOU  473  CA  CYS A  57     7996   7472   5919   2381   -676   -480       C  
ATOM    474  C   CYS A  57     -26.042  13.418  46.013  1.00 55.08           C  
ANISOU  474  C   CYS A  57     7733   7445   5749   2554   -742   -616       C  
ATOM    475  O   CYS A  57     -26.996  12.840  46.526  1.00 54.93           O  
ANISOU  475  O   CYS A  57     7516   7584   5771   2569   -696   -722       O  
ATOM    476  CB  CYS A  57     -23.958  12.134  46.090  1.00 55.71           C  
ANISOU  476  CB  CYS A  57     7843   7407   5917   2209   -611   -406       C  
ATOM    477  SG  CYS A  57     -22.318  11.875  46.741  1.00 62.86           S  
ANISOU  477  SG  CYS A  57     8836   8184   6864   2007   -544   -272       S  
ATOM    478  N   THR A  58     -26.137  14.097  44.882  1.00 56.00           N  
ANISOU  478  N   THR A  58     7984   7490   5802   2681   -850   -620       N  
ATOM    479  CA  THR A  58     -27.400  14.170  44.159  1.00 57.66           C  
ANISOU  479  CA  THR A  58     8103   7810   5994   2866   -942   -757       C  
ATOM    480  C   THR A  58     -27.240  13.496  42.802  1.00 56.99           C  
ANISOU  480  C   THR A  58     8011   7722   5921   2830   -966   -725       C  
ATOM    481  O   THR A  58     -26.236  13.688  42.116  1.00 56.46           O  
ANISOU  481  O   THR A  58     8126   7509   5819   2757   -972   -609       O  
ATOM    482  CB  THR A  58     -27.972  15.626  44.073  1.00 59.58           C  
ANISOU  482  CB  THR A  58     8515   7987   6135   3107  -1082   -831       C  
ATOM    483  OG1 THR A  58     -29.026  15.681  43.104  1.00 60.86           O  
ANISOU  483  OG1 THR A  58     8621   8228   6275   3294  -1199   -956       O  
ATOM    484  CG2 THR A  58     -26.898  16.631  43.697  1.00 60.38           C  
ANISOU  484  CG2 THR A  58     8934   7862   6144   3095  -1131   -703       C  
ATOM    485  N   ARG A  59     -28.225  12.679  42.449  1.00 57.45           N  
ANISOU  485  N   ARG A  59     7851   7945   6031   2870   -969   -837       N  
ATOM    486  CA  ARG A  59     -28.157  11.857  41.255  1.00 59.34           C  
ANISOU  486  CA  ARG A  59     8047   8204   6293   2822   -980   -817       C  
ATOM    487  C   ARG A  59     -28.556  12.650  40.021  1.00 61.44           C  
ANISOU  487  C   ARG A  59     8474   8402   6468   3020  -1139   -859       C  
ATOM    488  O   ARG A  59     -29.570  13.340  40.041  1.00 64.65           O  
ANISOU  488  O   ARG A  59     8866   8863   6836   3230  -1250   -991       O  
ATOM    489  CB  ARG A  59     -29.072  10.639  41.421  1.00 59.91           C  
ANISOU  489  CB  ARG A  59     7823   8483   6458   2773   -916   -928       C  
ATOM    490  CG  ARG A  59     -28.942   9.594  40.326  1.00 58.76           C  
ANISOU  490  CG  ARG A  59     7610   8366   6349   2690   -906   -901       C  
ATOM    491  CD  ARG A  59     -29.473   8.242  40.768  1.00 60.93           C  
ANISOU  491  CD  ARG A  59     7618   8813   6721   2557   -795   -967       C  
ATOM    492  NE  ARG A  59     -30.932   8.204  40.847  1.00 64.07           N  
ANISOU  492  NE  ARG A  59     7812   9390   7140   2688   -836  -1162       N  
ATOM    493  CZ  ARG A  59     -31.727   7.669  39.924  1.00 65.76           C  
ANISOU  493  CZ  ARG A  59     7894   9712   7379   2749   -894  -1267       C  
ATOM    494  NH1 ARG A  59     -31.222   7.116  38.827  1.00 63.37           N  
ANISOU  494  NH1 ARG A  59     7654   9350   7074   2694   -917  -1186       N  
ATOM    495  NH2 ARG A  59     -33.039   7.689  40.101  1.00 68.27           N  
ANISOU  495  NH2 ARG A  59     8010  10204   7727   2866   -928  -1464       N  
ATOM    496  N   LYS A  60     -27.754  12.563  38.960  1.00 61.69           N  
ANISOU  496  N   LYS A  60     8669   8310   6460   2956  -1153   -754       N  
ATOM    497  CA  LYS A  60     -28.162  13.082  37.650  1.00 65.77           C  
ANISOU  497  CA  LYS A  60     9342   8763   6883   3125  -1300   -794       C  
ATOM    498  C   LYS A  60     -28.527  11.929  36.723  1.00 65.82           C  
ANISOU  498  C   LYS A  60     9191   8874   6943   3085  -1296   -830       C  
ATOM    499  O   LYS A  60     -27.669  11.130  36.344  1.00 65.76           O  
ANISOU  499  O   LYS A  60     9182   8831   6973   2899  -1200   -726       O  
ATOM    500  CB  LYS A  60     -27.085  13.981  37.013  1.00 66.22           C  
ANISOU  500  CB  LYS A  60     9748   8587   6826   3097  -1328   -663       C  
ATOM    501  CG  LYS A  60     -27.194  15.468  37.368  1.00 69.40           C  
ANISOU  501  CG  LYS A  60    10387   8865   7118   3258  -1429   -679       C  
ATOM    502  CD  LYS A  60     -28.470  16.110  36.785  1.00 75.82           C  
ANISOU  502  CD  LYS A  60    11247   9709   7852   3549  -1622   -827       C  
ATOM    503  CE  LYS A  60     -28.762  17.501  37.365  1.00 75.69           C  
ANISOU  503  CE  LYS A  60    11417   9601   7742   3731  -1726   -871       C  
ATOM    504  NZ  LYS A  60     -29.034  17.515  38.845  1.00 72.21           N  
ANISOU  504  NZ  LYS A  60    10778   9275   7384   3712  -1649   -921       N  
ATOM    505  N   LEU A  61     -29.812  11.829  36.392  1.00 66.68           N  
ANISOU  505  N   LEU A  61     9154   9119   7061   3260  -1402   -991       N  
ATOM    506  CA  LEU A  61     -30.285  10.808  35.473  1.00 66.84           C  
ANISOU  506  CA  LEU A  61     9027   9243   7127   3245  -1420  -1046       C  
ATOM    507  C   LEU A  61     -30.187  11.368  34.070  1.00 68.61           C  
ANISOU  507  C   LEU A  61     9509   9328   7231   3373  -1562  -1024       C  
ATOM    508  O   LEU A  61     -30.746  12.429  33.774  1.00 71.51           O  
ANISOU  508  O   LEU A  61    10035   9635   7502   3599  -1723  -1098       O  
ATOM    509  CB  LEU A  61     -31.727  10.393  35.800  1.00 68.59           C  
ANISOU  509  CB  LEU A  61     8949   9689   7422   3361  -1462  -1250       C  
ATOM    510  CG  LEU A  61     -32.363   9.158  35.131  1.00 70.82           C  
ANISOU  510  CG  LEU A  61     9001  10126   7781   3316  -1453  -1336       C  
ATOM    511  CD1 LEU A  61     -33.030   9.479  33.789  1.00 73.33           C  
ANISOU  511  CD1 LEU A  61     9404  10428   8028   3527  -1647  -1428       C  
ATOM    512  CD2 LEU A  61     -31.373   7.989  34.975  1.00 68.37           C  
ANISOU  512  CD2 LEU A  61     8664   9785   7526   3052  -1300  -1189       C  
ATOM    513  N   PHE A  62     -29.473  10.656  33.206  1.00 67.39           N  
ANISOU  513  N   PHE A  62     9413   9116   7077   3231  -1507   -924       N  
ATOM    514  CA  PHE A  62     -29.242  11.133  31.848  1.00 68.13           C  
ANISOU  514  CA  PHE A  62     9784   9057   7044   3317  -1618   -885       C  
ATOM    515  C   PHE A  62     -30.163  10.485  30.830  1.00 69.42           C  
ANISOU  515  C   PHE A  62     9837   9324   7216   3425  -1726   -998       C  
ATOM    516  O   PHE A  62     -30.572   9.339  30.998  1.00 70.48           O  
ANISOU  516  O   PHE A  62     9683   9629   7468   3337  -1657  -1055       O  
ATOM    517  CB  PHE A  62     -27.777  10.940  31.460  1.00 65.84           C  
ANISOU  517  CB  PHE A  62     9677   8612   6728   3096  -1490   -707       C  
ATOM    518  CG  PHE A  62     -26.826  11.730  32.312  1.00 62.68           C  
ANISOU  518  CG  PHE A  62     9426   8087   6303   3004  -1408   -604       C  
ATOM    519  CD1 PHE A  62     -26.232  11.155  33.423  1.00 57.71           C  
ANISOU  519  CD1 PHE A  62     8618   7521   5790   2820  -1255   -550       C  
ATOM    520  CD2 PHE A  62     -26.543  13.059  32.011  1.00 63.33           C  
ANISOU  520  CD2 PHE A  62     9842   7981   6240   3104  -1493   -568       C  
ATOM    521  CE1 PHE A  62     -25.357  11.882  34.212  1.00 58.38           C  
ANISOU  521  CE1 PHE A  62     8834   7492   5855   2739  -1190   -465       C  
ATOM    522  CE2 PHE A  62     -25.673  13.795  32.797  1.00 60.30           C  
ANISOU  522  CE2 PHE A  62     9593   7483   5834   3011  -1418   -481       C  
ATOM    523  CZ  PHE A  62     -25.077  13.201  33.900  1.00 59.81           C  
ANISOU  523  CZ  PHE A  62     9330   7495   5899   2830  -1268   -432       C  
ATOM    524  N   ALA A  63     -30.493  11.229  29.780  1.00 71.47           N  
ANISOU  524  N   ALA A  63    10341   9472   7341   3616  -1900  -1034       N  
ATOM    525  CA  ALA A  63     -31.300  10.700  28.682  1.00 72.28           C  
ANISOU  525  CA  ALA A  63    10385   9647   7432   3734  -2026  -1138       C  
ATOM    526  C   ALA A  63     -30.583   9.558  27.953  1.00 70.62           C  
ANISOU  526  C   ALA A  63    10145   9429   7259   3521  -1906  -1036       C  
ATOM    527  O   ALA A  63     -31.222   8.598  27.519  1.00 71.75           O  
ANISOU  527  O   ALA A  63    10076   9713   7473   3523  -1928  -1123       O  
ATOM    528  CB  ALA A  63     -31.667  11.804  27.713  1.00 72.53           C  
ANISOU  528  CB  ALA A  63    10746   9524   7290   3982  -2245  -1181       C  
ATOM    529  N   ASN A  64     -29.261   9.671  27.822  1.00 68.28           N  
ANISOU  529  N   ASN A  64    10055   8970   6917   3337  -1780   -865       N  
ATOM    530  CA  ASN A  64     -28.451   8.650  27.149  1.00 67.90           C  
ANISOU  530  CA  ASN A  64     9995   8901   6901   3132  -1656   -767       C  
ATOM    531  C   ASN A  64     -26.980   8.690  27.569  1.00 66.14           C  
ANISOU  531  C   ASN A  64     9880   8560   6691   2899  -1474   -605       C  
ATOM    532  O   ASN A  64     -26.549   9.614  28.262  1.00 67.46           O  
ANISOU  532  O   ASN A  64    10176   8637   6820   2899  -1453   -559       O  
ATOM    533  CB  ASN A  64     -28.589   8.757  25.625  1.00 67.52           C  
ANISOU  533  CB  ASN A  64    10181   8750   6725   3228  -1778   -775       C  
ATOM    534  CG  ASN A  64     -28.130  10.098  25.090  1.00 69.24           C  
ANISOU  534  CG  ASN A  64    10820   8733   6756   3316  -1857   -711       C  
ATOM    535  OD1 ASN A  64     -27.047  10.579  25.423  1.00 67.80           O  
ANISOU  535  OD1 ASN A  64    10803   8418   6539   3171  -1736   -590       O  
ATOM    536  ND2 ASN A  64     -28.954  10.709  24.244  1.00 72.83           N  
ANISOU  536  ND2 ASN A  64    11461   9129   7083   3555  -2067   -800       N  
ATOM    537  N   MET A  65     -26.211   7.700  27.130  1.00 64.71           N  
ANISOU  537  N   MET A  65     9645   8380   6561   2707  -1349   -530       N  
ATOM    538  CA  MET A  65     -24.833   7.540  27.600  1.00 64.03           C  
ANISOU  538  CA  MET A  65     9591   8217   6519   2479  -1172   -403       C  
ATOM    539  C   MET A  65     -23.865   8.641  27.144  1.00 64.94           C  
ANISOU  539  C   MET A  65    10061   8115   6499   2441  -1152   -311       C  
ATOM    540  O   MET A  65     -22.968   9.026  27.900  1.00 64.28           O  
ANISOU  540  O   MET A  65    10016   7969   6441   2319  -1048   -241       O  
ATOM    541  CB  MET A  65     -24.294   6.142  27.264  1.00 61.46           C  
ANISOU  541  CB  MET A  65     9099   7959   6292   2297  -1052   -366       C  
ATOM    542  CG  MET A  65     -24.793   5.049  28.208  1.00 58.56           C  
ANISOU  542  CG  MET A  65     8387   7783   6081   2242  -1000   -418       C  
ATOM    543  SD  MET A  65     -24.287   3.375  27.750  1.00 59.74           S  
ANISOU  543  SD  MET A  65     8363   8005   6332   2054   -885   -386       S  
ATOM    544  CE  MET A  65     -25.396   3.018  26.394  1.00 55.35           C  
ANISOU  544  CE  MET A  65     7812   7503   5716   2199  -1023   -481       C  
ATOM    545  N   ARG A  66     -24.050   9.151  25.928  1.00 67.44           N  
ANISOU  545  N   ARG A  66    10645   8313   6667   2540  -1250   -317       N  
ATOM    546  CA  ARG A  66     -23.195  10.229  25.403  1.00 70.40           C  
ANISOU  546  CA  ARG A  66    11398   8465   6888   2496  -1229   -237       C  
ATOM    547  C   ARG A  66     -23.258  11.482  26.284  1.00 70.16           C  
ANISOU  547  C   ARG A  66    11498   8358   6804   2583  -1278   -235       C  
ATOM    548  O   ARG A  66     -22.224  12.056  26.617  1.00 69.82           O  
ANISOU  548  O   ARG A  66    11602   8193   6732   2441  -1170   -154       O  
ATOM    549  CB  ARG A  66     -23.541  10.569  23.940  1.00 72.71           C  
ANISOU  549  CB  ARG A  66    11986   8635   7007   2610  -1347   -253       C  
ATOM    550  CG  ARG A  66     -23.041   9.543  22.917  1.00 76.27           C  
ANISOU  550  CG  ARG A  66    12417   9091   7471   2468  -1256   -220       C  
ATOM    551  CD  ARG A  66     -23.849   9.599  21.609  1.00 80.96           C  
ANISOU  551  CD  ARG A  66    13199   9634   7927   2640  -1421   -277       C  
ATOM    552  NE  ARG A  66     -23.489   8.521  20.678  1.00 80.03           N  
ANISOU  552  NE  ARG A  66    13031   9543   7832   2516  -1341   -256       N  
ATOM    553  CZ  ARG A  66     -24.118   8.254  19.530  1.00 81.06           C  
ANISOU  553  CZ  ARG A  66    13270   9657   7873   2631  -1462   -304       C  
ATOM    554  NH1 ARG A  66     -25.165   8.975  19.139  1.00 81.18           N  
ANISOU  554  NH1 ARG A  66    13447   9629   7768   2885  -1683   -384       N  
ATOM    555  NH2 ARG A  66     -23.700   7.251  18.763  1.00 78.82           N  
ANISOU  555  NH2 ARG A  66    12933   9398   7618   2499  -1370   -280       N  
ATOM    556  N   ASP A  67     -24.468  11.878  26.678  1.00 70.33           N  
ANISOU  556  N   ASP A  67    11448   8457   6818   2812  -1438   -336       N  
ATOM    557  CA  ASP A  67     -24.663  13.067  27.506  1.00 71.81           C  
ANISOU  557  CA  ASP A  67    11755   8579   6951   2925  -1504   -350       C  
ATOM    558  C   ASP A  67     -24.157  12.897  28.940  1.00 68.65           C  
ANISOU  558  C   ASP A  67    11135   8260   6690   2789  -1371   -315       C  
ATOM    559  O   ASP A  67     -23.799  13.873  29.594  1.00 69.20           O  
ANISOU  559  O   ASP A  67    11352   8229   6711   2792  -1365   -282       O  
ATOM    560  CB  ASP A  67     -26.127  13.517  27.481  1.00 74.55           C  
ANISOU  560  CB  ASP A  67    12076   8995   7255   3224  -1721   -489       C  
ATOM    561  CG  ASP A  67     -26.545  14.062  26.122  1.00 80.54           C  
ANISOU  561  CG  ASP A  67    13156   9614   7832   3392  -1889   -519       C  
ATOM    562  OD1 ASP A  67     -25.724  14.732  25.450  1.00 83.21           O  
ANISOU  562  OD1 ASP A  67    13861   9735   8019   3318  -1860   -425       O  
ATOM    563  OD2 ASP A  67     -27.702  13.822  25.720  1.00 85.29           O  
ANISOU  563  OD2 ASP A  67    13650  10319   8436   3598  -2052   -645       O  
ATOM    564  N   ALA A  68     -24.125  11.656  29.416  1.00 65.25           N  
ANISOU  564  N   ALA A  68    10371   7999   6423   2669  -1269   -323       N  
ATOM    565  CA  ALA A  68     -23.487  11.339  30.689  1.00 63.12           C  
ANISOU  565  CA  ALA A  68     9915   7790   6279   2513  -1133   -279       C  
ATOM    566  C   ALA A  68     -21.977  11.536  30.568  1.00 61.42           C  
ANISOU  566  C   ALA A  68     9865   7428   6045   2298   -995   -162       C  
ATOM    567  O   ALA A  68     -21.350  12.171  31.425  1.00 59.01           O  
ANISOU  567  O   ALA A  68     9617   7058   5746   2232   -941   -118       O  
ATOM    568  CB  ALA A  68     -23.808   9.915  31.101  1.00 63.42           C  
ANISOU  568  CB  ALA A  68     9600   8023   6475   2435  -1066   -316       C  
ATOM    569  N   SER A  69     -21.410  10.988  29.491  1.00 60.03           N  
ANISOU  569  N   SER A  69     9757   7205   5847   2190   -937   -122       N  
ATOM    570  CA  SER A  69     -20.004  11.190  29.143  1.00 59.94           C  
ANISOU  570  CA  SER A  69     9914   7054   5805   1987   -804    -34       C  
ATOM    571  C   SER A  69     -19.645  12.666  28.949  1.00 60.46           C  
ANISOU  571  C   SER A  69    10341   6921   5710   2014   -835      1       C  
ATOM    572  O   SER A  69     -18.585  13.108  29.398  1.00 60.06           O  
ANISOU  572  O   SER A  69    10370   6783   5669   1858   -726     55       O  
ATOM    573  CB  SER A  69     -19.632  10.385  27.891  1.00 60.16           C  
ANISOU  573  CB  SER A  69     9970   7070   5818   1894   -748    -16       C  
ATOM    574  OG  SER A  69     -19.122   9.107  28.237  1.00 62.01           O  
ANISOU  574  OG  SER A  69     9921   7427   6214   1744   -635     -6       O  
ATOM    575  N   GLN A  70     -20.529  13.417  28.289  1.00 61.56           N  
ANISOU  575  N   GLN A  70    10704   6986   5702   2214   -989    -39       N  
ATOM    576  CA  GLN A  70     -20.327  14.852  28.069  1.00 63.98           C  
ANISOU  576  CA  GLN A  70    11393   7086   5831   2266  -1043    -11       C  
ATOM    577  C   GLN A  70     -20.306  15.585  29.397  1.00 62.76           C  
ANISOU  577  C   GLN A  70    11199   6932   5713   2296  -1051    -12       C  
ATOM    578  O   GLN A  70     -19.457  16.449  29.618  1.00 64.58           O  
ANISOU  578  O   GLN A  70    11647   7014   5877   2188   -985     43       O  
ATOM    579  CB  GLN A  70     -21.420  15.443  27.176  1.00 66.71           C  
ANISOU  579  CB  GLN A  70    11971   7361   6014   2515  -1241    -70       C  
ATOM    580  CG  GLN A  70     -21.546  14.801  25.803  1.00 73.64           C  
ANISOU  580  CG  GLN A  70    12925   8223   6831   2513  -1259    -75       C  
ATOM    581  CD  GLN A  70     -20.403  15.154  24.872  1.00 78.26           C  
ANISOU  581  CD  GLN A  70    13838   8611   7287   2319  -1138      8       C  
ATOM    582  OE1 GLN A  70     -19.417  14.418  24.776  1.00 79.30           O  
ANISOU  582  OE1 GLN A  70    13847   8774   7509   2087   -958     55       O  
ATOM    583  NE2 GLN A  70     -20.528  16.288  24.183  1.00 79.57           N  
ANISOU  583  NE2 GLN A  70    14431   8568   7235   2414  -1234     19       N  
ATOM    584  N   TRP A  71     -21.244  15.225  30.273  1.00 60.57           N  
ANISOU  584  N   TRP A  71    10647   6825   5543   2434  -1124    -81       N  
ATOM    585  CA  TRP A  71     -21.328  15.775  31.623  1.00 60.03           C  
ANISOU  585  CA  TRP A  71    10500   6786   5525   2469  -1129    -92       C  
ATOM    586  C   TRP A  71     -19.997  15.641  32.366  1.00 58.58           C  
ANISOU  586  C   TRP A  71    10257   6573   5429   2222   -957    -13       C  
ATOM    587  O   TRP A  71     -19.583  16.577  33.050  1.00 58.23           O  
ANISOU  587  O   TRP A  71    10350   6430   5343   2201   -947     13       O  
ATOM    588  CB  TRP A  71     -22.451  15.081  32.401  1.00 59.40           C  
ANISOU  588  CB  TRP A  71    10078   6924   5569   2601  -1188   -185       C  
ATOM    589  CG  TRP A  71     -22.780  15.692  33.739  1.00 61.75           C  
ANISOU  589  CG  TRP A  71    10305   7258   5899   2678  -1214   -217       C  
ATOM    590  CD1 TRP A  71     -23.586  16.775  33.972  1.00 65.82           C  
ANISOU  590  CD1 TRP A  71    10966   7726   6317   2897  -1356   -282       C  
ATOM    591  CD2 TRP A  71     -22.342  15.237  35.029  1.00 59.42           C  
ANISOU  591  CD2 TRP A  71     9784   7054   5739   2548  -1101   -194       C  
ATOM    592  NE1 TRP A  71     -23.662  17.028  35.323  1.00 66.20           N  
ANISOU  592  NE1 TRP A  71    10886   7834   6432   2902  -1327   -299       N  
ATOM    593  CE2 TRP A  71     -22.907  16.101  35.993  1.00 61.74           C  
ANISOU  593  CE2 TRP A  71    10101   7351   6007   2687  -1172   -243       C  
ATOM    594  CE3 TRP A  71     -21.518  14.193  35.462  1.00 57.78           C  
ANISOU  594  CE3 TRP A  71     9372   6918   5665   2335   -956   -141       C  
ATOM    595  CZ2 TRP A  71     -22.673  15.952  37.362  1.00 62.04           C  
ANISOU  595  CZ2 TRP A  71     9972   7458   6141   2610  -1095   -235       C  
ATOM    596  CZ3 TRP A  71     -21.291  14.042  36.821  1.00 58.41           C  
ANISOU  596  CZ3 TRP A  71     9292   7061   5839   2268   -893   -135       C  
ATOM    597  CH2 TRP A  71     -21.862  14.920  37.755  1.00 59.32           C  
ANISOU  597  CH2 TRP A  71     9443   7175   5920   2400   -958   -178       C  
ATOM    598  N   ILE A  72     -19.326  14.493  32.209  1.00 57.55           N  
ANISOU  598  N   ILE A  72     9928   6522   5416   2043   -832     16       N  
ATOM    599  CA  ILE A  72     -18.056  14.218  32.912  1.00 57.15           C  
ANISOU  599  CA  ILE A  72     9782   6464   5470   1818   -682     71       C  
ATOM    600  C   ILE A  72     -16.955  15.185  32.487  1.00 59.55           C  
ANISOU  600  C   ILE A  72    10389   6570   5668   1680   -610    126       C  
ATOM    601  O   ILE A  72     -16.274  15.779  33.333  1.00 58.71           O  
ANISOU  601  O   ILE A  72    10320   6406   5581   1593   -560    149       O  
ATOM    602  CB  ILE A  72     -17.553  12.753  32.715  1.00 54.72           C  
ANISOU  602  CB  ILE A  72     9215   6275   5303   1669   -576     79       C  
ATOM    603  CG1 ILE A  72     -18.530  11.746  33.326  1.00 49.16           C  
ANISOU  603  CG1 ILE A  72     8204   5763   4712   1763   -622     27       C  
ATOM    604  CG2 ILE A  72     -16.149  12.573  33.317  1.00 50.29           C  
ANISOU  604  CG2 ILE A  72     8587   5683   4836   1449   -438    121       C  
ATOM    605  CD1 ILE A  72     -18.275  10.308  32.914  1.00 47.39           C  
ANISOU  605  CD1 ILE A  72     7768   5643   4596   1655   -549     28       C  
ATOM    606  N   LYS A  73     -16.788  15.324  31.172  1.00 63.15           N  
ANISOU  606  N   LYS A  73    11064   6923   6008   1652   -600    141       N  
ATOM    607  CA  LYS A  73     -15.829  16.263  30.588  1.00 66.89           C  
ANISOU  607  CA  LYS A  73    11868   7195   6352   1512   -523    184       C  
ATOM    608  C   LYS A  73     -16.060  17.683  31.133  1.00 67.78           C  
ANISOU  608  C   LYS A  73    12237   7174   6344   1610   -606    190       C  
ATOM    609  O   LYS A  73     -15.106  18.354  31.554  1.00 66.90           O  
ANISOU  609  O   LYS A  73    12245   6957   6217   1456   -516    220       O  
ATOM    610  CB  LYS A  73     -15.925  16.242  29.056  1.00 68.94           C  
ANISOU  610  CB  LYS A  73    12363   7360   6473   1514   -530    190       C  
ATOM    611  CG  LYS A  73     -15.872  14.840  28.436  1.00 71.17           C  
ANISOU  611  CG  LYS A  73    12404   7775   6860   1451   -471    178       C  
ATOM    612  CD  LYS A  73     -16.194  14.863  26.928  1.00 76.41           C  
ANISOU  612  CD  LYS A  73    13317   8346   7369   1498   -510    177       C  
ATOM    613  CE  LYS A  73     -16.531  13.468  26.383  1.00 75.38           C  
ANISOU  613  CE  LYS A  73    12932   8369   7340   1507   -504    152       C  
ATOM    614  NZ  LYS A  73     -15.410  12.480  26.526  1.00 72.14           N  
ANISOU  614  NZ  LYS A  73    12287   8038   7084   1276   -325    165       N  
ATOM    615  N   ARG A  74     -17.331  18.105  31.131  1.00 67.15           N  
ANISOU  615  N   ARG A  74    12225   7104   6183   1868   -781    150       N  
ATOM    616  CA AARG A  74     -17.752  19.396  31.682  0.50 68.22           C  
ANISOU  616  CA AARG A  74    12586   7128   6207   2011   -890    140       C  
ATOM    617  CA BARG A  74     -17.733  19.402  31.672  0.50 68.33           C  
ANISOU  617  CA BARG A  74    12603   7139   6219   2007   -888    141       C  
ATOM    618  C   ARG A  74     -17.324  19.556  33.138  1.00 68.10           C  
ANISOU  618  C   ARG A  74    12397   7168   6310   1941   -835    149       C  
ATOM    619  O   ARG A  74     -16.842  20.619  33.542  1.00 69.29           O  
ANISOU  619  O   ARG A  74    12771   7175   6380   1896   -824    174       O  
ATOM    620  CB AARG A  74     -19.274  19.546  31.584  0.50 67.68           C  
ANISOU  620  CB AARG A  74    12507   7124   6085   2319  -1092     66       C  
ATOM    621  CB BARG A  74     -19.245  19.608  31.519  0.50 68.04           C  
ANISOU  621  CB BARG A  74    12580   7153   6117   2316  -1093     69       C  
ATOM    622  CG AARG A  74     -19.771  20.668  30.687  0.50 67.14           C  
ANISOU  622  CG AARG A  74    12864   6860   5788   2485  -1237     55       C  
ATOM    623  CG BARG A  74     -19.687  20.122  30.153  0.50 67.50           C  
ANISOU  623  CG BARG A  74    12859   6936   5851   2438  -1204     60       C  
ATOM    624  CD AARG A  74     -21.290  20.769  30.784  0.50 62.95           C  
ANISOU  624  CD AARG A  74    12255   6423   5238   2807  -1448    -46       C  
ATOM    625  CD BARG A  74     -21.209  20.206  30.063  0.50 64.85           C  
ANISOU  625  CD BARG A  74    12477   6682   5481   2759  -1421    -37       C  
ATOM    626  NE AARG A  74     -21.772  22.146  30.888  0.50 61.50           N  
ANISOU  626  NE AARG A  74    12402   6080   4887   3002  -1602    -73       N  
ATOM    627  NE BARG A  74     -21.790  19.012  29.456  0.50 62.23           N  
ANISOU  627  NE BARG A  74    11897   6513   5235   2803  -1443    -84       N  
ATOM    628  CZ AARG A  74     -21.703  22.888  31.992  0.50 56.96           C  
ANISOU  628  CZ AARG A  74    11840   5480   4324   3029  -1609    -74       C  
ATOM    629  CZ BARG A  74     -23.001  18.539  29.735  0.50 60.15           C  
ANISOU  629  CZ BARG A  74    11375   6429   5052   3008  -1566   -185       C  
ATOM    630  NH1AARG A  74     -21.150  22.400  33.093  0.50 54.48           N  
ANISOU  630  NH1AARG A  74    11235   5287   4178   2869  -1470    -48       N  
ATOM    631  NH1BARG A  74     -23.764  19.146  30.633  0.50 56.85           N  
ANISOU  631  NH1BARG A  74    10900   6058   4642   3193  -1674   -256       N  
ATOM    632  NH2AARG A  74     -22.180  24.122  31.992  0.50 55.06           N  
ANISOU  632  NH2AARG A  74    11918   5084   3918   3223  -1762   -104       N  
ATOM    633  NH2BARG A  74     -23.444  17.448  29.126  0.50 60.06           N  
ANISOU  633  NH2BARG A  74    11155   6553   5112   3021  -1574   -224       N  
ATOM    634  N   MET A  75     -17.512  18.495  33.924  1.00 66.73           N  
ANISOU  634  N   MET A  75    11842   7194   6318   1930   -803    125       N  
ATOM    635  CA  MET A  75     -17.189  18.526  35.353  1.00 67.20           C  
ANISOU  635  CA  MET A  75    11724   7316   6491   1878   -761    128       C  
ATOM    636  C   MET A  75     -15.685  18.584  35.616  1.00 67.83           C  
ANISOU  636  C   MET A  75    11827   7322   6624   1615   -609    179       C  
ATOM    637  O   MET A  75     -15.251  19.200  36.588  1.00 66.88           O  
ANISOU  637  O   MET A  75    11733   7156   6520   1570   -593    189       O  
ATOM    638  CB  MET A  75     -17.825  17.340  36.083  1.00 66.49           C  
ANISOU  638  CB  MET A  75    11252   7447   6563   1932   -767     86       C  
ATOM    639  CG  MET A  75     -19.344  17.420  36.209  1.00 66.08           C  
ANISOU  639  CG  MET A  75    11135   7492   6481   2191   -912      9       C  
ATOM    640  SD  MET A  75     -19.897  18.634  37.416  1.00 66.64           S  
ANISOU  640  SD  MET A  75    11298   7523   6498   2350  -1005    -26       S  
ATOM    641  CE  MET A  75     -19.553  17.756  38.945  1.00 65.33           C  
ANISOU  641  CE  MET A  75    10791   7512   6518   2225   -900    -22       C  
ATOM    642  N   GLU A  76     -14.901  17.945  34.748  1.00 70.91           N  
ANISOU  642  N   GLU A  76    12197   7702   7042   1446   -501    199       N  
ATOM    643  CA  GLU A  76     -13.438  18.025  34.796  1.00 74.90           C  
ANISOU  643  CA  GLU A  76    12731   8135   7592   1190   -352    224       C  
ATOM    644  C   GLU A  76     -12.942  19.468  34.594  1.00 78.33           C  
ANISOU  644  C   GLU A  76    13537   8357   7867   1128   -337    247       C  
ATOM    645  O   GLU A  76     -12.100  19.949  35.355  1.00 78.74           O  
ANISOU  645  O   GLU A  76    13600   8360   7958    997   -274    252       O  
ATOM    646  CB  GLU A  76     -12.814  17.086  33.751  1.00 75.84           C  
ANISOU  646  CB  GLU A  76    12773   8286   7756   1041   -243    225       C  
ATOM    647  CG  GLU A  76     -11.280  17.119  33.668  1.00 81.25           C  
ANISOU  647  CG  GLU A  76    13469   8910   8494    771    -78    226       C  
ATOM    648  CD  GLU A  76     -10.728  16.622  32.325  1.00 86.22           C  
ANISOU  648  CD  GLU A  76    14158   9510   9092    633     30    221       C  
ATOM    649  OE1 GLU A  76      -9.839  15.742  32.337  1.00 86.54           O  
ANISOU  649  OE1 GLU A  76    13976   9633   9272    475    141    195       O  
ATOM    650  OE2 GLU A  76     -11.173  17.112  31.259  1.00 89.36           O  
ANISOU  650  OE2 GLU A  76    14834   9797   9322    687      1    238       O  
ATOM    651  N   ASP A  77     -13.480  20.148  33.582  1.00 81.26           N  
ANISOU  651  N   ASP A  77    14223   8599   8054   1225   -403    256       N  
ATOM    652  CA  ASP A  77     -13.025  21.492  33.204  1.00 85.88           C  
ANISOU  652  CA  ASP A  77    15216   8956   8457   1155   -386    281       C  
ATOM    653  C   ASP A  77     -13.320  22.545  34.274  1.00 86.02           C  
ANISOU  653  C   ASP A  77    15345   8909   8430   1261   -475    281       C  
ATOM    654  O   ASP A  77     -12.517  23.457  34.488  1.00 88.13           O  
ANISOU  654  O   ASP A  77    15827   9029   8631   1118   -410    298       O  
ATOM    655  CB  ASP A  77     -13.611  21.915  31.843  1.00 89.26           C  
ANISOU  655  CB  ASP A  77    15982   9250   8681   1256   -456    290       C  
ATOM    656  CG  ASP A  77     -13.121  21.039  30.685  1.00 93.35           C  
ANISOU  656  CG  ASP A  77    16462   9794   9215   1109   -342    294       C  
ATOM    657  OD1 ASP A  77     -11.938  20.622  30.688  1.00 95.26           O  
ANISOU  657  OD1 ASP A  77    16584  10055   9553    856   -167    294       O  
ATOM    658  OD2 ASP A  77     -13.920  20.770  29.760  1.00 95.66           O  
ANISOU  658  OD2 ASP A  77    16840  10085   9421   1252   -431    287       O  
ATOM    659  N   ILE A  78     -14.471  22.416  34.934  1.00 83.97           N  
ANISOU  659  N   ILE A  78    14937   8761   8207   1505   -619    253       N  
ATOM    660  CA  ILE A  78     -14.829  23.265  36.076  1.00 82.32           C  
ANISOU  660  CA  ILE A  78    14774   8524   7980   1622   -704    242       C  
ATOM    661  C   ILE A  78     -13.966  22.905  37.293  1.00 79.12           C  
ANISOU  661  C   ILE A  78    14112   8205   7746   1459   -603    247       C  
ATOM    662  O   ILE A  78     -13.552  23.780  38.058  1.00 79.31           O  
ANISOU  662  O   ILE A  78    14258   8135   7739   1415   -600    256       O  
ATOM    663  CB  ILE A  78     -16.342  23.147  36.416  1.00 82.64           C  
ANISOU  663  CB  ILE A  78    14698   8681   8022   1927   -875    189       C  
ATOM    664  CG1 ILE A  78     -17.191  23.673  35.250  1.00 85.88           C  
ANISOU  664  CG1 ILE A  78    15399   8983   8248   2114  -1006    171       C  
ATOM    665  CG2 ILE A  78     -16.685  23.896  37.703  1.00 84.01           C  
ANISOU  665  CG2 ILE A  78    14869   8852   8199   2039   -946    169       C  
ATOM    666  CD1 ILE A  78     -18.668  23.298  35.323  1.00 87.11           C  
ANISOU  666  CD1 ILE A  78    15383   9288   8428   2402  -1166     94       C  
ATOM    667  N   GLY A  79     -13.686  21.615  37.452  1.00 75.24           N  
ANISOU  667  N   GLY A  79    13279   7883   7427   1372   -529    239       N  
ATOM    668  CA  GLY A  79     -12.893  21.125  38.579  1.00 71.57           C  
ANISOU  668  CA  GLY A  79    12560   7506   7128   1235   -452    236       C  
ATOM    669  C   GLY A  79     -13.756  20.601  39.713  1.00 67.70           C  
ANISOU  669  C   GLY A  79    11812   7175   6737   1394   -532    210       C  
ATOM    670  O   GLY A  79     -13.356  20.640  40.880  1.00 66.03           O  
ANISOU  670  O   GLY A  79    11488   6993   6609   1345   -516    208       O  
ATOM    671  N   LEU A  80     -14.948  20.122  39.361  1.00 65.14           N  
ANISOU  671  N   LEU A  80    11401   6951   6400   1580   -615    184       N  
ATOM    672  CA  LEU A  80     -15.873  19.538  40.321  1.00 63.58           C  
ANISOU  672  CA  LEU A  80    10952   6917   6291   1721   -675    145       C  
ATOM    673  C   LEU A  80     -16.001  18.034  40.108  1.00 60.20           C  
ANISOU  673  C   LEU A  80    10226   6654   5992   1677   -627    133       C  
ATOM    674  O   LEU A  80     -16.128  17.573  38.971  1.00 59.05           O  
ANISOU  674  O   LEU A  80    10095   6518   5823   1672   -618    134       O  
ATOM    675  CB  LEU A  80     -17.242  20.223  40.243  1.00 64.76           C  
ANISOU  675  CB  LEU A  80    11214   7063   6327   1980   -815     98       C  
ATOM    676  CG  LEU A  80     -17.380  21.587  40.936  1.00 67.72           C  
ANISOU  676  CG  LEU A  80    11813   7317   6600   2074   -885     93       C  
ATOM    677  CD1 LEU A  80     -18.800  22.127  40.786  1.00 68.59           C  
ANISOU  677  CD1 LEU A  80    12001   7447   6613   2354  -1036     24       C  
ATOM    678  CD2 LEU A  80     -16.981  21.522  42.415  1.00 65.93           C  
ANISOU  678  CD2 LEU A  80    11434   7142   6474   2005   -842     97       C  
ATOM    679  N   GLU A  81     -15.970  17.282  41.208  1.00 57.03           N  
ANISOU  679  N   GLU A  81     9578   6374   5718   1645   -599    122       N  
ATOM    680  CA  GLU A  81     -15.931  15.819  41.148  1.00 55.77           C  
ANISOU  680  CA  GLU A  81     9150   6356   5685   1576   -546    115       C  
ATOM    681  C   GLU A  81     -17.200  15.200  40.566  1.00 52.77           C  
ANISOU  681  C   GLU A  81     8663   6094   5294   1724   -602     70       C  
ATOM    682  O   GLU A  81     -18.296  15.411  41.074  1.00 55.40           O  
ANISOU  682  O   GLU A  81     8949   6496   5602   1884   -674     20       O  
ATOM    683  CB  GLU A  81     -15.616  15.211  42.525  1.00 55.50           C  
ANISOU  683  CB  GLU A  81     8918   6401   5768   1512   -513    113       C  
ATOM    684  CG  GLU A  81     -15.378  13.693  42.484  1.00 58.34           C  
ANISOU  684  CG  GLU A  81     9035   6879   6252   1420   -457    111       C  
ATOM    685  CD  GLU A  81     -15.089  13.069  43.849  1.00 62.01           C  
ANISOU  685  CD  GLU A  81     9341   7404   6814   1365   -438    109       C  
ATOM    686  OE1 GLU A  81     -14.979  13.804  44.857  1.00 64.65           O  
ANISOU  686  OE1 GLU A  81     9744   7692   7129   1384   -461    110       O  
ATOM    687  OE2 GLU A  81     -14.966  11.825  43.912  1.00 61.83           O  
ANISOU  687  OE2 GLU A  81     9141   7470   6883   1302   -404    105       O  
ATOM    688  N   ALA A  82     -17.028  14.435  39.496  1.00 51.16           N  
ANISOU  688  N   ALA A  82     8413   5915   5109   1664   -567     78       N  
ATOM    689  CA  ALA A  82     -18.107  13.644  38.909  1.00 50.67           C  
ANISOU  689  CA  ALA A  82     8217   5976   5058   1773   -611     32       C  
ATOM    690  C   ALA A  82     -18.027  12.216  39.450  1.00 48.81           C  
ANISOU  690  C   ALA A  82     7701   5882   4963   1682   -547     25       C  
ATOM    691  O   ALA A  82     -17.153  11.437  39.067  1.00 48.73           O  
ANISOU  691  O   ALA A  82     7625   5870   5021   1537   -473     57       O  
ATOM    692  CB  ALA A  82     -18.008  13.650  37.384  1.00 49.83           C  
ANISOU  692  CB  ALA A  82     8251   5805   4878   1768   -617     45       C  
ATOM    693  N   LEU A  83     -18.943  11.887  40.349  1.00 46.75           N  
ANISOU  693  N   LEU A  83     7285   5738   4740   1768   -574    -23       N  
ATOM    694  CA  LEU A  83     -18.919  10.614  41.054  1.00 44.23           C  
ANISOU  694  CA  LEU A  83     6735   5535   4535   1680   -515    -30       C  
ATOM    695  C   LEU A  83     -19.807   9.584  40.349  1.00 44.24           C  
ANISOU  695  C   LEU A  83     6583   5662   4563   1721   -523    -78       C  
ATOM    696  O   LEU A  83     -20.767   9.943  39.661  1.00 43.18           O  
ANISOU  696  O   LEU A  83     6483   5559   4365   1861   -594   -131       O  
ATOM    697  CB  LEU A  83     -19.374  10.803  42.511  1.00 40.61           C  
ANISOU  697  CB  LEU A  83     6210   5128   4094   1721   -520    -59       C  
ATOM    698  CG  LEU A  83     -18.539  11.703  43.419  1.00 40.44           C  
ANISOU  698  CG  LEU A  83     6314   4995   4056   1677   -514    -18       C  
ATOM    699  CD1 LEU A  83     -19.070  13.129  43.436  1.00 41.68           C  
ANISOU  699  CD1 LEU A  83     6651   5082   4104   1823   -589    -41       C  
ATOM    700  CD2 LEU A  83     -18.496  11.140  44.839  1.00 38.79           C  
ANISOU  700  CD2 LEU A  83     5982   4845   3912   1623   -478    -23       C  
ATOM    701  N   GLY A  84     -19.490   8.307  40.537  1.00 42.51           N  
ANISOU  701  N   GLY A  84     6201   5512   4437   1604   -459    -66       N  
ATOM    702  CA  GLY A  84     -20.296   7.235  39.965  1.00 44.48           C  
ANISOU  702  CA  GLY A  84     6298   5883   4720   1621   -457   -113       C  
ATOM    703  C   GLY A  84     -19.504   6.352  39.020  1.00 44.15           C  
ANISOU  703  C   GLY A  84     6233   5819   4721   1507   -413    -72       C  
ATOM    704  O   GLY A  84     -18.387   6.699  38.619  1.00 43.34           O  
ANISOU  704  O   GLY A  84     6245   5608   4613   1428   -386    -18       O  
ATOM    705  N   MET A  85     -20.083   5.202  38.680  1.00 42.89           N  
ANISOU  705  N   MET A  85     5923   5767   4607   1491   -399   -106       N  
ATOM    706  CA  MET A  85     -19.484   4.287  37.719  1.00 42.78           C  
ANISOU  706  CA  MET A  85     5879   5745   4631   1399   -362    -79       C  
ATOM    707  C   MET A  85     -19.555   4.882  36.320  1.00 44.10           C  
ANISOU  707  C   MET A  85     6183   5854   4719   1465   -404    -78       C  
ATOM    708  O   MET A  85     -20.614   4.905  35.699  1.00 42.21           O  
ANISOU  708  O   MET A  85     5928   5676   4436   1577   -466   -133       O  
ATOM    709  CB  MET A  85     -20.168   2.914  37.766  1.00 42.90           C  
ANISOU  709  CB  MET A  85     5709   5885   4705   1366   -341   -121       C  
ATOM    710  CG  MET A  85     -19.628   1.892  36.771  1.00 38.74           C  
ANISOU  710  CG  MET A  85     5147   5356   4218   1280   -308    -99       C  
ATOM    711  SD  MET A  85     -17.827   1.897  36.614  1.00 44.49           S  
ANISOU  711  SD  MET A  85     5959   5958   4987   1149   -252    -26       S  
ATOM    712  CE  MET A  85     -17.298   1.088  38.131  1.00 40.12           C  
ANISOU  712  CE  MET A  85     5301   5421   4523   1055   -217    -13       C  
ATOM    713  N   ASP A  86     -18.409   5.362  35.848  1.00 45.46           N  
ANISOU  713  N   ASP A  86     6497   5905   4870   1389   -369    -23       N  
ATOM    714  CA  ASP A  86     -18.292   5.995  34.539  1.00 47.11           C  
ANISOU  714  CA  ASP A  86     6886   6029   4986   1424   -392    -12       C  
ATOM    715  C   ASP A  86     -18.149   4.982  33.394  1.00 47.34           C  
ANISOU  715  C   ASP A  86     6866   6087   5036   1367   -362    -14       C  
ATOM    716  O   ASP A  86     -18.265   5.349  32.225  1.00 48.94           O  
ANISOU  716  O   ASP A  86     7212   6232   5151   1409   -388    -14       O  
ATOM    717  CB  ASP A  86     -17.131   6.996  34.532  1.00 48.56           C  
ANISOU  717  CB  ASP A  86     7256   6066   5127   1345   -349     37       C  
ATOM    718  CG  ASP A  86     -15.807   6.367  34.944  1.00 51.54           C  
ANISOU  718  CG  ASP A  86     7546   6428   5610   1173   -254     66       C  
ATOM    719  OD1 ASP A  86     -14.789   6.679  34.294  1.00 57.75           O  
ANISOU  719  OD1 ASP A  86     8444   7120   6378   1070   -192     87       O  
ATOM    720  OD2 ASP A  86     -15.774   5.567  35.908  1.00 47.95           O  
ANISOU  720  OD2 ASP A  86     6917   6049   5251   1138   -242     59       O  
ATOM    721  N   ASP A  87     -17.898   3.718  33.728  1.00 46.58           N  
ANISOU  721  N   ASP A  87     6584   6069   5045   1276   -311    -16       N  
ATOM    722  CA  ASP A  87     -17.949   2.637  32.742  1.00 46.36           C  
ANISOU  722  CA  ASP A  87     6486   6087   5043   1238   -292    -27       C  
ATOM    723  C   ASP A  87     -19.372   2.064  32.731  1.00 45.98           C  
ANISOU  723  C   ASP A  87     6309   6166   4996   1339   -355    -88       C  
ATOM    724  O   ASP A  87     -19.778   1.334  33.646  1.00 46.00           O  
ANISOU  724  O   ASP A  87     6150   6259   5067   1316   -342   -112       O  
ATOM    725  CB  ASP A  87     -16.896   1.564  33.057  1.00 45.39           C  
ANISOU  725  CB  ASP A  87     6246   5973   5028   1092   -211     -5       C  
ATOM    726  CG  ASP A  87     -16.870   0.433  32.024  1.00 47.53           C  
ANISOU  726  CG  ASP A  87     6452   6282   5324   1049   -188    -18       C  
ATOM    727  OD1 ASP A  87     -17.831   0.313  31.232  1.00 46.86           O  
ANISOU  727  OD1 ASP A  87     6377   6243   5185   1131   -238    -47       O  
ATOM    728  OD2 ASP A  87     -15.884  -0.343  32.009  1.00 45.00           O  
ANISOU  728  OD2 ASP A  87     6070   5949   5079    939   -126     -6       O  
ATOM    729  N   PHE A  88     -20.124   2.404  31.690  1.00 45.72           N  
ANISOU  729  N   PHE A  88     6357   6134   4881   1446   -425   -121       N  
ATOM    730  CA  PHE A  88     -21.577   2.225  31.698  1.00 47.57           C  
ANISOU  730  CA  PHE A  88     6485   6486   5104   1573   -507   -204       C  
ATOM    731  C   PHE A  88     -22.061   0.782  31.556  1.00 49.18           C  
ANISOU  731  C   PHE A  88     6493   6811   5384   1519   -484   -244       C  
ATOM    732  O   PHE A  88     -23.151   0.434  32.034  1.00 49.19           O  
ANISOU  732  O   PHE A  88     6345   6933   5412   1572   -515   -320       O  
ATOM    733  CB  PHE A  88     -22.244   3.150  30.671  1.00 49.10           C  
ANISOU  733  CB  PHE A  88     6843   6634   5180   1730   -615   -239       C  
ATOM    734  CG  PHE A  88     -21.886   4.604  30.849  1.00 49.91           C  
ANISOU  734  CG  PHE A  88     7162   6610   5192   1791   -646   -206       C  
ATOM    735  CD1 PHE A  88     -22.029   5.226  32.094  1.00 53.53           C  
ANISOU  735  CD1 PHE A  88     7589   7081   5670   1823   -649   -213       C  
ATOM    736  CD2 PHE A  88     -21.391   5.347  29.787  1.00 51.68           C  
ANISOU  736  CD2 PHE A  88     7638   6693   5305   1806   -666   -167       C  
ATOM    737  CE1 PHE A  88     -21.685   6.574  32.280  1.00 52.71           C  
ANISOU  737  CE1 PHE A  88     7695   6852   5480   1876   -679   -182       C  
ATOM    738  CE2 PHE A  88     -21.049   6.698  29.958  1.00 54.57           C  
ANISOU  738  CE2 PHE A  88     8228   6928   5577   1849   -690   -136       C  
ATOM    739  CZ  PHE A  88     -21.198   7.310  31.212  1.00 51.59           C  
ANISOU  739  CZ  PHE A  88     7811   6567   5226   1887   -700   -143       C  
ATOM    740  N   LYS A  89     -21.254  -0.067  30.928  1.00 48.67           N  
ANISOU  740  N   LYS A  89     6425   6715   5353   1406   -424   -202       N  
ATOM    741  CA  LYS A  89     -21.625  -1.471  30.833  1.00 49.09           C  
ANISOU  741  CA  LYS A  89     6308   6867   5475   1343   -399   -234       C  
ATOM    742  C   LYS A  89     -21.591  -2.172  32.191  1.00 46.91           C  
ANISOU  742  C   LYS A  89     5889   6651   5283   1257   -343   -234       C  
ATOM    743  O   LYS A  89     -22.416  -3.045  32.451  1.00 48.38           O  
ANISOU  743  O   LYS A  89     5932   6943   5505   1239   -340   -289       O  
ATOM    744  CB  LYS A  89     -20.854  -2.230  29.739  1.00 49.22           C  
ANISOU  744  CB  LYS A  89     6364   6838   5500   1260   -358   -199       C  
ATOM    745  CG  LYS A  89     -19.380  -1.903  29.584  1.00 51.47           C  
ANISOU  745  CG  LYS A  89     6767   7002   5789   1168   -288   -128       C  
ATOM    746  CD  LYS A  89     -18.886  -2.278  28.177  1.00 50.75           C  
ANISOU  746  CD  LYS A  89     6758   6862   5664   1130   -263   -117       C  
ATOM    747  CE  LYS A  89     -17.398  -1.998  28.008  1.00 53.85           C  
ANISOU  747  CE  LYS A  89     7246   7147   6068   1021   -175    -68       C  
ATOM    748  NZ  LYS A  89     -17.054  -0.549  28.157  1.00 57.34           N  
ANISOU  748  NZ  LYS A  89     7858   7491   6436   1049   -177    -42       N  
ATOM    749  N   LEU A  90     -20.674  -1.766  33.063  1.00 45.02           N  
ANISOU  749  N   LEU A  90     5698   6340   5067   1201   -300   -179       N  
ATOM    750  CA  LEU A  90     -20.658  -2.286  34.426  1.00 44.26           C  
ANISOU  750  CA  LEU A  90     5504   6282   5031   1133   -260   -178       C  
ATOM    751  C   LEU A  90     -21.877  -1.799  35.203  1.00 44.69           C  
ANISOU  751  C   LEU A  90     5497   6423   5061   1217   -291   -243       C  
ATOM    752  O   LEU A  90     -22.545  -2.594  35.866  1.00 45.17           O  
ANISOU  752  O   LEU A  90     5435   6573   5155   1173   -263   -288       O  
ATOM    753  CB  LEU A  90     -19.361  -1.921  35.157  1.00 44.81           C  
ANISOU  753  CB  LEU A  90     5645   6251   5130   1065   -223   -113       C  
ATOM    754  CG  LEU A  90     -18.021  -2.353  34.542  1.00 44.59           C  
ANISOU  754  CG  LEU A  90     5658   6143   5141    975   -183    -68       C  
ATOM    755  CD1 LEU A  90     -16.871  -2.087  35.515  1.00 42.26           C  
ANISOU  755  CD1 LEU A  90     5392   5772   4891    910   -156    -31       C  
ATOM    756  CD2 LEU A  90     -18.032  -3.820  34.109  1.00 42.96           C  
ANISOU  756  CD2 LEU A  90     5355   5984   4984    908   -161    -82       C  
ATOM    757  N   ALA A  91     -22.175  -0.502  35.091  1.00 45.27           N  
ANISOU  757  N   ALA A  91     5663   6466   5070   1336   -347   -256       N  
ATOM    758  CA  ALA A  91     -23.385   0.088  35.678  1.00 45.24           C  
ANISOU  758  CA  ALA A  91     5601   6549   5039   1445   -390   -337       C  
ATOM    759  C   ALA A  91     -24.650  -0.653  35.229  1.00 46.70           C  
ANISOU  759  C   ALA A  91     5633   6873   5237   1481   -414   -439       C  
ATOM    760  O   ALA A  91     -25.480  -1.026  36.065  1.00 45.66           O  
ANISOU  760  O   ALA A  91     5367   6849   5134   1464   -384   -512       O  
ATOM    761  CB  ALA A  91     -23.482   1.564  35.328  1.00 45.21           C  
ANISOU  761  CB  ALA A  91     5748   6476   4954   1586   -467   -339       C  
ATOM    762  N   TYR A  92     -24.772  -0.868  33.915  1.00 46.58           N  
ANISOU  762  N   TYR A  92     5645   6855   5199   1521   -462   -451       N  
ATOM    763  CA  TYR A  92     -25.877  -1.619  33.325  1.00 48.02           C  
ANISOU  763  CA  TYR A  92     5686   7162   5396   1550   -493   -551       C  
ATOM    764  C   TYR A  92     -25.980  -3.018  33.923  1.00 49.84           C  
ANISOU  764  C   TYR A  92     5767   7470   5699   1395   -402   -564       C  
ATOM    765  O   TYR A  92     -27.039  -3.410  34.423  1.00 49.72           O  
ANISOU  765  O   TYR A  92     5601   7583   5709   1389   -387   -665       O  
ATOM    766  CB  TYR A  92     -25.706  -1.710  31.807  1.00 48.85           C  
ANISOU  766  CB  TYR A  92     5880   7221   5461   1594   -553   -537       C  
ATOM    767  CG  TYR A  92     -26.657  -2.674  31.132  1.00 49.42           C  
ANISOU  767  CG  TYR A  92     5808   7412   5557   1597   -581   -629       C  
ATOM    768  CD1 TYR A  92     -26.258  -3.971  30.810  1.00 47.35           C  
ANISOU  768  CD1 TYR A  92     5489   7158   5343   1459   -516   -597       C  
ATOM    769  CD2 TYR A  92     -27.958  -2.290  30.815  1.00 51.08           C  
ANISOU  769  CD2 TYR A  92     5938   7726   5744   1743   -679   -760       C  
ATOM    770  CE1 TYR A  92     -27.137  -4.862  30.194  1.00 49.40           C  
ANISOU  770  CE1 TYR A  92     5621   7525   5624   1453   -541   -685       C  
ATOM    771  CE2 TYR A  92     -28.845  -3.173  30.196  1.00 51.46           C  
ANISOU  771  CE2 TYR A  92     5841   7891   5820   1742   -709   -860       C  
ATOM    772  CZ  TYR A  92     -28.428  -4.454  29.891  1.00 51.24           C  
ANISOU  772  CZ  TYR A  92     5766   7865   5837   1590   -636   -818       C  
ATOM    773  OH  TYR A  92     -29.306  -5.317  29.283  1.00 53.03           O  
ANISOU  773  OH  TYR A  92     5855   8204   6089   1582   -665   -918       O  
ATOM    774  N   LEU A  93     -24.870  -3.755  33.868  1.00 49.22           N  
ANISOU  774  N   LEU A  93     5739   7311   5653   1269   -342   -469       N  
ATOM    775  CA  LEU A  93     -24.794  -5.105  34.428  1.00 49.43           C  
ANISOU  775  CA  LEU A  93     5671   7376   5735   1120   -263   -466       C  
ATOM    776  C   LEU A  93     -25.174  -5.159  35.901  1.00 50.07           C  
ANISOU  776  C   LEU A  93     5690   7502   5831   1066   -206   -493       C  
ATOM    777  O   LEU A  93     -25.750  -6.142  36.362  1.00 52.29           O  
ANISOU  777  O   LEU A  93     5871   7860   6137    969   -150   -544       O  
ATOM    778  CB  LEU A  93     -23.399  -5.710  34.240  1.00 45.46           C  
ANISOU  778  CB  LEU A  93     5251   6760   5261   1019   -224   -363       C  
ATOM    779  CG  LEU A  93     -23.009  -6.238  32.857  1.00 46.04           C  
ANISOU  779  CG  LEU A  93     5357   6804   5334   1011   -243   -344       C  
ATOM    780  CD1 LEU A  93     -21.733  -7.061  32.969  1.00 44.42           C  
ANISOU  780  CD1 LEU A  93     5191   6513   5175    897   -191   -270       C  
ATOM    781  CD2 LEU A  93     -24.112  -7.068  32.213  1.00 43.80           C  
ANISOU  781  CD2 LEU A  93     4959   6629   5052   1012   -261   -428       C  
ATOM    782  N   SER A  94     -24.844  -4.107  36.636  1.00 50.58           N  
ANISOU  782  N   SER A  94     5830   7514   5875   1119   -214   -462       N  
ATOM    783  CA  SER A  94     -25.161  -4.049  38.055  1.00 52.22           C  
ANISOU  783  CA  SER A  94     6002   7754   6086   1074   -160   -485       C  
ATOM    784  C   SER A  94     -26.666  -3.870  38.279  1.00 52.40           C  
ANISOU  784  C   SER A  94     5886   7926   6097   1132   -160   -623       C  
ATOM    785  O   SER A  94     -27.220  -4.400  39.234  1.00 53.40           O  
ANISOU  785  O   SER A  94     5934   8122   6234   1044    -84   -676       O  
ATOM    786  CB  SER A  94     -24.370  -2.927  38.723  1.00 53.36           C  
ANISOU  786  CB  SER A  94     6270   7796   6208   1121   -176   -417       C  
ATOM    787  OG  SER A  94     -24.617  -2.896  40.117  1.00 58.29           O  
ANISOU  787  OG  SER A  94     6877   8442   6830   1074   -122   -435       O  
ATOM    788  N   ASP A  95     -27.317  -3.138  37.380  1.00 53.56           N  
ANISOU  788  N   ASP A  95     6009   8120   6220   1281   -247   -689       N  
ATOM    789  CA  ASP A  95     -28.770  -2.937  37.427  1.00 55.05           C  
ANISOU  789  CA  ASP A  95     6044   8463   6408   1362   -269   -846       C  
ATOM    790  C   ASP A  95     -29.552  -4.166  36.983  1.00 55.80           C  
ANISOU  790  C   ASP A  95     5983   8677   6541   1275   -234   -936       C  
ATOM    791  O   ASP A  95     -30.512  -4.564  37.640  1.00 56.67           O  
ANISOU  791  O   ASP A  95     5946   8914   6672   1218   -170  -1052       O  
ATOM    792  CB  ASP A  95     -29.184  -1.746  36.555  1.00 54.09           C  
ANISOU  792  CB  ASP A  95     5967   8341   6244   1571   -400   -896       C  
ATOM    793  CG  ASP A  95     -28.762  -0.412  37.141  1.00 55.12           C  
ANISOU  793  CG  ASP A  95     6232   8382   6329   1670   -434   -849       C  
ATOM    794  OD1 ASP A  95     -28.567   0.537  36.352  1.00 54.19           O  
ANISOU  794  OD1 ASP A  95     6243   8188   6158   1809   -536   -826       O  
ATOM    795  OD2 ASP A  95     -28.625  -0.308  38.384  1.00 54.21           O  
ANISOU  795  OD2 ASP A  95     6110   8265   6224   1605   -360   -834       O  
ATOM    796  N   THR A  96     -29.130  -4.756  35.867  1.00 55.61           N  
ANISOU  796  N   THR A  96     5996   8610   6523   1256   -269   -887       N  
ATOM    797  CA  THR A  96     -29.851  -5.854  35.230  1.00 55.27           C  
ANISOU  797  CA  THR A  96     5820   8670   6511   1190   -257   -972       C  
ATOM    798  C   THR A  96     -29.658  -7.163  35.991  1.00 55.13           C  
ANISOU  798  C   THR A  96     5767   8656   6523    980   -132   -946       C  
ATOM    799  O   THR A  96     -30.462  -8.086  35.865  1.00 56.45           O  
ANISOU  799  O   THR A  96     5804   8929   6714    892    -90  -1041       O  
ATOM    800  CB  THR A  96     -29.392  -6.028  33.765  1.00 55.53           C  
ANISOU  800  CB  THR A  96     5930   8639   6531   1243   -337   -921       C  
ATOM    801  OG1 THR A  96     -29.307  -4.744  33.136  1.00 56.14           O  
ANISOU  801  OG1 THR A  96     6112   8662   6558   1426   -448   -912       O  
ATOM    802  CG2 THR A  96     -30.358  -6.911  32.974  1.00 57.40           C  
ANISOU  802  CG2 THR A  96     6019   8997   6792   1222   -359  -1037       C  
ATOM    803  N   TYR A  97     -28.587  -7.242  36.776  1.00 52.91           N  
ANISOU  803  N   TYR A  97     5612   8255   6237    899    -79   -823       N  
ATOM    804  CA  TYR A  97     -28.288  -8.447  37.540  1.00 52.18           C  
ANISOU  804  CA  TYR A  97     5534   8135   6156    712     22   -787       C  
ATOM    805  C   TYR A  97     -28.073  -8.118  39.014  1.00 54.16           C  
ANISOU  805  C   TYR A  97     5842   8349   6387    660     88   -759       C  
ATOM    806  O   TYR A  97     -26.962  -8.176  39.538  1.00 52.98           O  
ANISOU  806  O   TYR A  97     5827   8071   6232    618     97   -645       O  
ATOM    807  CB  TYR A  97     -27.115  -9.197  36.904  1.00 49.67           C  
ANISOU  807  CB  TYR A  97     5325   7697   5852    656      7   -670       C  
ATOM    808  CG  TYR A  97     -27.445  -9.595  35.485  1.00 48.41           C  
ANISOU  808  CG  TYR A  97     5109   7582   5704    696    -49   -709       C  
ATOM    809  CD1 TYR A  97     -27.037  -8.811  34.404  1.00 46.89           C  
ANISOU  809  CD1 TYR A  97     4975   7342   5497    831   -138   -673       C  
ATOM    810  CD2 TYR A  97     -28.221 -10.720  35.226  1.00 46.92           C  
ANISOU  810  CD2 TYR A  97     4817   7481   5530    595    -10   -789       C  
ATOM    811  CE1 TYR A  97     -27.366  -9.162  33.095  1.00 45.08           C  
ANISOU  811  CE1 TYR A  97     4712   7149   5269    872   -194   -711       C  
ATOM    812  CE2 TYR A  97     -28.559 -11.076  33.921  1.00 47.92           C  
ANISOU  812  CE2 TYR A  97     4892   7651   5666    636    -68   -831       C  
ATOM    813  CZ  TYR A  97     -28.127 -10.296  32.867  1.00 45.23           C  
ANISOU  813  CZ  TYR A  97     4618   7259   5309    779   -163   -790       C  
ATOM    814  OH  TYR A  97     -28.465 -10.656  31.592  1.00 43.75           O  
ANISOU  814  OH  TYR A  97     4398   7105   5120    820   -223   -831       O  
ATOM    815  N   ASN A  98     -29.181  -7.775  39.661  1.00 56.96           N  
ANISOU  815  N   ASN A  98     6086   8824   6732    667    132   -879       N  
ATOM    816  CA  ASN A  98     -29.211  -7.265  41.021  1.00 59.65           C  
ANISOU  816  CA  ASN A  98     6467   9152   7046    642    193   -880       C  
ATOM    817  C   ASN A  98     -29.166  -8.404  42.053  1.00 59.89           C  
ANISOU  817  C   ASN A  98     6543   9158   7056    437    314   -868       C  
ATOM    818  O   ASN A  98     -29.997  -8.473  42.968  1.00 61.64           O  
ANISOU  818  O   ASN A  98     6704   9461   7254    360    409   -962       O  
ATOM    819  CB  ASN A  98     -30.488  -6.424  41.188  1.00 63.53           C  
ANISOU  819  CB  ASN A  98     6808   9795   7536    743    191  -1037       C  
ATOM    820  CG  ASN A  98     -30.278  -5.189  42.051  1.00 68.03           C  
ANISOU  820  CG  ASN A  98     7448  10323   8076    841    176  -1015       C  
ATOM    821  OD1 ASN A  98     -29.221  -5.013  42.670  1.00 71.13           O  
ANISOU  821  OD1 ASN A  98     7999  10580   8450    811    181   -887       O  
ATOM    822  ND2 ASN A  98     -31.287  -4.322  42.092  1.00 68.15           N  
ANISOU  822  ND2 ASN A  98     7345  10458   8091    967    149  -1150       N  
ATOM    823  N   TYR A  99     -28.193  -9.298  41.891  1.00 57.59           N  
ANISOU  823  N   TYR A  99     6368   8746   6766    350    309   -758       N  
ATOM    824  CA  TYR A  99     -28.107 -10.532  42.676  1.00 57.83           C  
ANISOU  824  CA  TYR A  99     6476   8730   6766    160    403   -741       C  
ATOM    825  C   TYR A  99     -26.808 -11.275  42.388  1.00 54.69           C  
ANISOU  825  C   TYR A  99     6224   8180   6377    125    354   -611       C  
ATOM    826  O   TYR A  99     -26.159 -11.019  41.376  1.00 53.16           O  
ANISOU  826  O   TYR A  99     6029   7947   6221    224    268   -558       O  
ATOM    827  CB  TYR A  99     -29.319 -11.454  42.410  1.00 61.04           C  
ANISOU  827  CB  TYR A  99     6747   9270   7173     38    486   -871       C  
ATOM    828  CG  TYR A  99     -29.601 -11.768  40.943  1.00 61.55           C  
ANISOU  828  CG  TYR A  99     6701   9401   7285     93    420   -909       C  
ATOM    829  CD1 TYR A  99     -30.488 -10.984  40.196  1.00 64.41           C  
ANISOU  829  CD1 TYR A  99     6894   9900   7678    227    367  -1021       C  
ATOM    830  CD2 TYR A  99     -29.003 -12.867  40.311  1.00 62.12           C  
ANISOU  830  CD2 TYR A  99     6843   9395   7365     17    403   -842       C  
ATOM    831  CE1 TYR A  99     -30.761 -11.275  38.852  1.00 64.83           C  
ANISOU  831  CE1 TYR A  99     6861  10007   7766    282    296  -1059       C  
ATOM    832  CE2 TYR A  99     -29.264 -13.163  38.962  1.00 62.40           C  
ANISOU  832  CE2 TYR A  99     6786   9487   7438     66    343   -878       C  
ATOM    833  CZ  TYR A  99     -30.145 -12.363  38.242  1.00 64.43           C  
ANISOU  833  CZ  TYR A  99     6883   9876   7720    196    290   -984       C  
ATOM    834  OH  TYR A  99     -30.416 -12.652  36.921  1.00 65.33           O  
ANISOU  834  OH  TYR A  99     6922  10040   7863    249    222  -1023       O  
ATOM    835  N   GLU A 100     -26.428 -12.181  43.286  1.00 55.72           N  
ANISOU  835  N   GLU A 100     6488   8218   6466    -14    408   -569       N  
ATOM    836  CA  GLU A 100     -25.270 -13.043  43.071  1.00 57.18           C  
ANISOU  836  CA  GLU A 100     6806   8261   6657    -48    357   -468       C  
ATOM    837  C   GLU A 100     -25.559 -13.940  41.875  1.00 56.84           C  
ANISOU  837  C   GLU A 100     6688   8265   6644    -83    349   -499       C  
ATOM    838  O   GLU A 100     -26.496 -14.748  41.919  1.00 57.83           O  
ANISOU  838  O   GLU A 100     6765   8463   6744   -208    428   -578       O  
ATOM    839  CB  GLU A 100     -24.977 -13.886  44.315  1.00 59.88           C  
ANISOU  839  CB  GLU A 100     7325   8494   6932   -187    409   -434       C  
ATOM    840  CG  GLU A 100     -23.772 -14.824  44.173  1.00 65.53           C  
ANISOU  840  CG  GLU A 100     8190   9055   7652   -207    340   -345       C  
ATOM    841  CD  GLU A 100     -23.033 -15.066  45.491  1.00 71.83           C  
ANISOU  841  CD  GLU A 100     9196   9705   8391   -253    327   -284       C  
ATOM    842  OE1 GLU A 100     -21.784 -15.143  45.455  1.00 75.09           O  
ANISOU  842  OE1 GLU A 100     9701   9997   8833   -183    227   -211       O  
ATOM    843  OE2 GLU A 100     -23.688 -15.168  46.557  1.00 71.71           O  
ANISOU  843  OE2 GLU A 100     9253   9694   8298   -356    414   -319       O  
ATOM    844  N   ILE A 101     -24.776 -13.774  40.804  1.00 53.07           N  
ANISOU  844  N   ILE A 101     6199   7747   6216     19    261   -445       N  
ATOM    845  CA  ILE A 101     -24.990 -14.539  39.582  1.00 49.98           C  
ANISOU  845  CA  ILE A 101     5742   7396   5851      3    243   -471       C  
ATOM    846  C   ILE A 101     -24.704 -16.019  39.776  1.00 50.42           C  
ANISOU  846  C   ILE A 101     5904   7371   5883   -136    271   -448       C  
ATOM    847  O   ILE A 101     -23.662 -16.411  40.299  1.00 48.79           O  
ANISOU  847  O   ILE A 101     5843   7028   5666   -151    239   -371       O  
ATOM    848  CB  ILE A 101     -24.213 -13.978  38.375  1.00 48.66           C  
ANISOU  848  CB  ILE A 101     5555   7201   5733    139    154   -422       C  
ATOM    849  CG1 ILE A 101     -24.965 -12.777  37.795  1.00 50.21           C  
ANISOU  849  CG1 ILE A 101     5632   7508   5938    261    127   -480       C  
ATOM    850  CG2 ILE A 101     -24.053 -15.049  37.286  1.00 47.03           C  
ANISOU  850  CG2 ILE A 101     5339   6983   5545    100    134   -421       C  
ATOM    851  CD1 ILE A 101     -24.126 -11.900  36.899  1.00 46.15           C  
ANISOU  851  CD1 ILE A 101     5147   6940   5447    394     49   -422       C  
ATOM    852  N   LYS A 102     -25.680 -16.825  39.377  1.00 53.76           N  
ANISOU  852  N   LYS A 102     6254   7879   6294   -236    326   -527       N  
ATOM    853  CA  LYS A 102     -25.541 -18.263  39.294  1.00 56.13           C  
ANISOU  853  CA  LYS A 102     6648   8110   6567   -366    347   -517       C  
ATOM    854  C   LYS A 102     -25.554 -18.556  37.801  1.00 55.65           C  
ANISOU  854  C   LYS A 102     6496   8095   6555   -310    294   -532       C  
ATOM    855  O   LYS A 102     -26.534 -18.250  37.111  1.00 58.38           O  
ANISOU  855  O   LYS A 102     6685   8578   6920   -287    305   -619       O  
ATOM    856  CB  LYS A 102     -26.725 -18.933  39.997  1.00 59.77           C  
ANISOU  856  CB  LYS A 102     7100   8640   6971   -544    467   -608       C  
ATOM    857  CG  LYS A 102     -26.563 -20.420  40.287  1.00 67.45           C  
ANISOU  857  CG  LYS A 102     8236   9505   7885   -708    504   -589       C  
ATOM    858  CD  LYS A 102     -26.154 -20.665  41.741  1.00 74.27           C  
ANISOU  858  CD  LYS A 102     9311  10240   8669   -795    542   -539       C  
ATOM    859  CE  LYS A 102     -26.392 -22.123  42.148  1.00 77.16           C  
ANISOU  859  CE  LYS A 102     9849  10518   8949   -992    608   -552       C  
ATOM    860  NZ  LYS A 102     -26.519 -22.277  43.628  1.00 77.72           N  
ANISOU  860  NZ  LYS A 102    10107  10507   8918  -1117    689   -545       N  
ATOM    861  N   TYR A 103     -24.462 -19.106  37.283  1.00 53.24           N  
ANISOU  861  N   TYR A 103     6284   7676   6269   -277    229   -458       N  
ATOM    862  CA  TYR A 103     -24.373 -19.348  35.848  1.00 50.74           C  
ANISOU  862  CA  TYR A 103     5896   7391   5991   -220    180   -467       C  
ATOM    863  C   TYR A 103     -24.299 -20.833  35.503  1.00 51.43           C  
ANISOU  863  C   TYR A 103     6060   7422   6060   -330    188   -470       C  
ATOM    864  O   TYR A 103     -23.895 -21.657  36.329  1.00 51.59           O  
ANISOU  864  O   TYR A 103     6229   7332   6040   -420    204   -437       O  
ATOM    865  CB  TYR A 103     -23.206 -18.562  35.231  1.00 48.91           C  
ANISOU  865  CB  TYR A 103     5679   7099   5806    -71    101   -396       C  
ATOM    866  CG  TYR A 103     -21.828 -19.115  35.518  1.00 46.74           C  
ANISOU  866  CG  TYR A 103     5541   6675   5544    -67     60   -321       C  
ATOM    867  CD1 TYR A 103     -21.095 -18.686  36.629  1.00 46.10           C  
ANISOU  867  CD1 TYR A 103     5549   6510   5458    -47     46   -273       C  
ATOM    868  CD2 TYR A 103     -21.245 -20.054  34.666  1.00 44.12           C  
ANISOU  868  CD2 TYR A 103     5246   6288   5230    -73     26   -308       C  
ATOM    869  CE1 TYR A 103     -19.810 -19.195  36.887  1.00 46.71           C  
ANISOU  869  CE1 TYR A 103     5739   6454   5553    -28    -11   -222       C  
ATOM    870  CE2 TYR A 103     -19.978 -20.576  34.919  1.00 42.65           C  
ANISOU  870  CE2 TYR A 103     5172   5971   5062    -54    -23   -260       C  
ATOM    871  CZ  TYR A 103     -19.268 -20.143  36.026  1.00 46.69           C  
ANISOU  871  CZ  TYR A 103     5761   6405   5574    -28    -46   -221       C  
ATOM    872  OH  TYR A 103     -18.018 -20.656  36.257  1.00 47.97           O  
ANISOU  872  OH  TYR A 103     6022   6445   5762      6   -111   -192       O  
ATOM    873  N   ASP A 104     -24.704 -21.166  34.281  1.00 50.88           N  
ANISOU  873  N   ASP A 104     5902   7418   6012   -317    169   -512       N  
ATOM    874  CA  ASP A 104     -24.637 -22.534  33.785  1.00 51.24           C  
ANISOU  874  CA  ASP A 104     6014   7412   6042   -408    169   -518       C  
ATOM    875  C   ASP A 104     -23.681 -22.572  32.591  1.00 50.52           C  
ANISOU  875  C   ASP A 104     5932   7271   5994   -296     91   -472       C  
ATOM    876  O   ASP A 104     -23.977 -22.004  31.531  1.00 51.69           O  
ANISOU  876  O   ASP A 104     5970   7500   6168   -211     63   -500       O  
ATOM    877  CB  ASP A 104     -26.042 -23.017  33.394  1.00 51.19           C  
ANISOU  877  CB  ASP A 104     5896   7534   6020   -515    224   -626       C  
ATOM    878  CG  ASP A 104     -26.114 -24.523  33.136  1.00 54.97           C  
ANISOU  878  CG  ASP A 104     6468   7952   6466   -650    243   -639       C  
ATOM    879  OD1 ASP A 104     -25.064 -25.201  33.054  1.00 56.20           O  
ANISOU  879  OD1 ASP A 104     6769   7970   6616   -635    197   -566       O  
ATOM    880  OD2 ASP A 104     -27.247 -25.037  33.012  1.00 58.44           O  
ANISOU  880  OD2 ASP A 104     6832   8486   6886   -772    303   -733       O  
ATOM    881  N   HIS A 105     -22.540 -23.235  32.764  1.00 48.71           N  
ANISOU  881  N   HIS A 105     5836   6904   5766   -292     55   -410       N  
ATOM    882  CA  HIS A 105     -21.528 -23.293  31.712  1.00 48.15           C  
ANISOU  882  CA  HIS A 105     5773   6783   5740   -192     -6   -377       C  
ATOM    883  C   HIS A 105     -21.986 -24.047  30.458  1.00 48.24           C  
ANISOU  883  C   HIS A 105     5742   6837   5749   -217    -12   -420       C  
ATOM    884  O   HIS A 105     -21.620 -23.666  29.339  1.00 49.03           O  
ANISOU  884  O   HIS A 105     5793   6958   5880   -125    -44   -416       O  
ATOM    885  CB  HIS A 105     -20.189 -23.827  32.244  1.00 49.61           C  
ANISOU  885  CB  HIS A 105     6094   6819   5936   -170    -51   -324       C  
ATOM    886  CG  HIS A 105     -20.172 -25.305  32.479  1.00 53.04           C  
ANISOU  886  CG  HIS A 105     6659   7164   6328   -269    -59   -331       C  
ATOM    887  ND1 HIS A 105     -19.690 -26.199  31.546  1.00 53.97           N  
ANISOU  887  ND1 HIS A 105     6811   7234   6460   -253    -97   -339       N  
ATOM    888  CD2 HIS A 105     -20.575 -26.045  33.540  1.00 52.74           C  
ANISOU  888  CD2 HIS A 105     6748   7067   6226   -387    -32   -334       C  
ATOM    889  CE1 HIS A 105     -19.802 -27.428  32.021  1.00 55.80           C  
ANISOU  889  CE1 HIS A 105     7186   7378   6639   -351   -101   -344       C  
ATOM    890  NE2 HIS A 105     -20.335 -27.361  33.229  1.00 56.21           N  
ANISOU  890  NE2 HIS A 105     7303   7416   6637   -439    -60   -340       N  
ATOM    891  N   THR A 106     -22.809 -25.083  30.639  1.00 49.02           N  
ANISOU  891  N   THR A 106     5605   7164   5857   -302     10   -212       N  
ATOM    892  CA  THR A 106     -23.286 -25.912  29.509  1.00 48.31           C  
ANISOU  892  CA  THR A 106     5449   7071   5836   -364    -36   -230       C  
ATOM    893  C   THR A 106     -24.118 -25.118  28.494  1.00 47.22           C  
ANISOU  893  C   THR A 106     5232   6993   5718   -293    -91   -287       C  
ATOM    894  O   THR A 106     -24.339 -25.579  27.373  1.00 48.75           O  
ANISOU  894  O   THR A 106     5390   7178   5955   -322   -152   -312       O  
ATOM    895  CB  THR A 106     -24.067 -27.199  29.957  1.00 47.47           C  
ANISOU  895  CB  THR A 106     5264   6996   5777   -481     20   -203       C  
ATOM    896  OG1 THR A 106     -25.202 -26.835  30.744  1.00 48.00           O  
ANISOU  896  OG1 THR A 106     5227   7170   5839   -467     91   -207       O  
ATOM    897  CG2 THR A 106     -23.181 -28.136  30.772  1.00 49.94           C  
ANISOU  897  CG2 THR A 106     5671   7231   6071   -551     62   -140       C  
ATOM    898  N   LYS A 107     -24.552 -23.920  28.881  1.00 46.48           N  
ANISOU  898  N   LYS A 107     5118   6955   5586   -192    -73   -309       N  
ATOM    899  CA  LYS A 107     -25.310 -23.045  27.984  1.00 46.59           C  
ANISOU  899  CA  LYS A 107     5069   7024   5608   -101   -126   -360       C  
ATOM    900  C   LYS A 107     -24.411 -22.011  27.303  1.00 44.59           C  
ANISOU  900  C   LYS A 107     4931   6698   5315    -12   -188   -373       C  
ATOM    901  O   LYS A 107     -24.811 -21.420  26.308  1.00 45.92           O  
ANISOU  901  O   LYS A 107     5075   6884   5488     58   -248   -407       O  
ATOM    902  CB  LYS A 107     -26.443 -22.327  28.728  1.00 48.22           C  
ANISOU  902  CB  LYS A 107     5180   7341   5800    -30    -69   -380       C  
ATOM    903  CG  LYS A 107     -27.174 -23.144  29.784  1.00 51.69           C  
ANISOU  903  CG  LYS A 107     5527   7855   6259   -112     23   -354       C  
ATOM    904  CD  LYS A 107     -28.221 -24.071  29.191  1.00 59.56           C  
ANISOU  904  CD  LYS A 107     6375   8923   7332   -197     11   -369       C  
ATOM    905  CE  LYS A 107     -29.081 -24.670  30.294  1.00 59.98           C  
ANISOU  905  CE  LYS A 107     6324   9065   7401   -269    116   -342       C  
ATOM    906  NZ  LYS A 107     -30.210 -25.464  29.745  1.00 65.49           N  
ANISOU  906  NZ  LYS A 107     6859   9847   8178   -356    106   -363       N  
ATOM    907  N   ILE A 108     -23.205 -21.795  27.841  1.00 43.09           N  
ANISOU  907  N   ILE A 108     4862   6426   5083    -15   -173   -344       N  
ATOM    908  CA  ILE A 108     -22.243 -20.831  27.273  1.00 39.92           C  
ANISOU  908  CA  ILE A 108     4574   5949   4645     51   -223   -350       C  
ATOM    909  C   ILE A 108     -21.484 -21.425  26.073  1.00 40.02           C  
ANISOU  909  C   ILE A 108     4628   5896   4681      7   -286   -343       C  
ATOM    910  O   ILE A 108     -20.867 -22.492  26.182  1.00 42.41           O  
ANISOU  910  O   ILE A 108     4950   6160   5003    -79   -277   -315       O  
ATOM    911  CB  ILE A 108     -21.227 -20.346  28.345  1.00 39.79           C  
ANISOU  911  CB  ILE A 108     4663   5879   4576     56   -187   -326       C  
ATOM    912  CG1 ILE A 108     -21.959 -19.744  29.547  1.00 36.45           C  
ANISOU  912  CG1 ILE A 108     4212   5519   4118    107   -123   -338       C  
ATOM    913  CG2 ILE A 108     -20.231 -19.326  27.753  1.00 37.21           C  
ANISOU  913  CG2 ILE A 108     4448   5472   4218    109   -236   -333       C  
ATOM    914  CD1 ILE A 108     -21.143 -19.678  30.813  1.00 35.27           C  
ANISOU  914  CD1 ILE A 108     4145   5337   3918     85    -79   -313       C  
ATOM    915  N   ARG A 109     -21.530 -20.739  24.933  1.00 38.34           N  
ANISOU  915  N   ARG A 109     4436   5670   4462     73   -346   -368       N  
ATOM    916  CA  ARG A 109     -20.862 -21.234  23.737  1.00 37.76           C  
ANISOU  916  CA  ARG A 109     4404   5543   4401     44   -402   -364       C  
ATOM    917  C   ARG A 109     -19.375 -20.909  23.762  1.00 37.33           C  
ANISOU  917  C   ARG A 109     4470   5400   4314     38   -402   -335       C  
ATOM    918  O   ARG A 109     -18.955 -19.768  23.502  1.00 36.40           O  
ANISOU  918  O   ARG A 109     4423   5247   4160    103   -418   -337       O  
ATOM    919  CB  ARG A 109     -21.521 -20.731  22.442  1.00 39.28           C  
ANISOU  919  CB  ARG A 109     4571   5762   4593    115   -468   -399       C  
ATOM    920  CG  ARG A 109     -21.106 -21.546  21.200  1.00 38.16           C  
ANISOU  920  CG  ARG A 109     4448   5585   4466     73   -523   -403       C  
ATOM    921  CD  ARG A 109     -21.820 -21.104  19.938  1.00 42.99           C  
ANISOU  921  CD  ARG A 109     5034   6233   5068    145   -593   -438       C  
ATOM    922  NE  ARG A 109     -23.261 -21.362  19.985  1.00 45.97           N  
ANISOU  922  NE  ARG A 109     5276   6710   5479    150   -608   -475       N  
ATOM    923  CZ  ARG A 109     -23.845 -22.498  19.601  1.00 47.76           C  
ANISOU  923  CZ  ARG A 109     5419   6975   5751     73   -634   -498       C  
ATOM    924  NH1 ARG A 109     -23.119 -23.516  19.135  1.00 42.07           N  
ANISOU  924  NH1 ARG A 109     4748   6193   5043     -7   -648   -491       N  
ATOM    925  NH2 ARG A 109     -25.167 -22.620  19.686  1.00 46.55           N  
ANISOU  925  NH2 ARG A 109     5132   6924   5631     76   -646   -532       N  
ATOM    926  N   VAL A 110     -18.591 -21.929  24.091  1.00 35.83           N  
ANISOU  926  N   VAL A 110     4301   5175   4138    -42   -383   -306       N  
ATOM    927  CA  VAL A 110     -17.149 -21.792  24.190  1.00 35.20           C  
ANISOU  927  CA  VAL A 110     4314   5026   4033    -57   -381   -276       C  
ATOM    928  C   VAL A 110     -16.576 -22.424  22.938  1.00 35.71           C  
ANISOU  928  C   VAL A 110     4403   5053   4112    -77   -422   -275       C  
ATOM    929  O   VAL A 110     -16.877 -23.575  22.618  1.00 35.66           O  
ANISOU  929  O   VAL A 110     4358   5053   4139   -126   -430   -279       O  
ATOM    930  CB  VAL A 110     -16.581 -22.473  25.466  1.00 33.54           C  
ANISOU  930  CB  VAL A 110     4116   4806   3821   -116   -334   -243       C  
ATOM    931  CG1 VAL A 110     -15.074 -22.306  25.528  1.00 33.25           C  
ANISOU  931  CG1 VAL A 110     4162   4712   3761   -127   -341   -216       C  
ATOM    932  CG2 VAL A 110     -17.220 -21.894  26.716  1.00 31.54           C  
ANISOU  932  CG2 VAL A 110     3842   4598   3546    -94   -289   -247       C  
ATOM    933  N   ALA A 111     -15.767 -21.649  22.226  1.00 37.07           N  
ANISOU  933  N   ALA A 111     4645   5184   4256    -39   -446   -270       N  
ATOM    934  CA  ALA A 111     -15.232 -22.046  20.933  1.00 37.49           C  
ANISOU  934  CA  ALA A 111     4729   5207   4308    -40   -481   -270       C  
ATOM    935  C   ALA A 111     -13.730 -21.889  20.891  1.00 38.37           C  
ANISOU  935  C   ALA A 111     4912   5267   4399    -54   -469   -238       C  
ATOM    936  O   ALA A 111     -13.213 -20.820  21.199  1.00 41.33           O  
ANISOU  936  O   ALA A 111     5333   5622   4749    -33   -459   -226       O  
ATOM    937  CB  ALA A 111     -15.856 -21.202  19.841  1.00 38.41           C  
ANISOU  937  CB  ALA A 111     4853   5336   4404     31   -523   -295       C  
ATOM    938  N   ASN A 112     -13.021 -22.954  20.536  1.00 41.22           N  
ANISOU  938  N   ASN A 112     5281   5607   4774    -92   -469   -225       N  
ATOM    939  CA  ASN A 112     -11.638 -22.789  20.091  1.00 45.57           C  
ANISOU  939  CA  ASN A 112     5888   6122   5304    -92   -463   -199       C  
ATOM    940  C   ASN A 112     -11.377 -23.308  18.709  1.00 45.52           C  
ANISOU  940  C   ASN A 112     5903   6101   5291    -77   -486   -208       C  
ATOM    941  O   ASN A 112     -11.966 -24.295  18.275  1.00 47.60           O  
ANISOU  941  O   ASN A 112     6141   6370   5573    -88   -505   -231       O  
ATOM    942  CB  ASN A 112     -10.572 -23.298  21.067  1.00 50.21           C  
ANISOU  942  CB  ASN A 112     6482   6697   5899   -133   -435   -167       C  
ATOM    943  CG  ASN A 112     -11.019 -24.449  21.899  1.00 53.22           C  
ANISOU  943  CG  ASN A 112     6826   7088   6307   -170   -421   -164       C  
ATOM    944  OD1 ASN A 112     -10.398 -24.738  22.918  1.00 59.23           O  
ANISOU  944  OD1 ASN A 112     7591   7846   7066   -194   -399   -138       O  
ATOM    945  ND2 ASN A 112     -12.085 -25.121  21.490  1.00 58.40           N  
ANISOU  945  ND2 ASN A 112     7447   7755   6987   -179   -434   -189       N  
ATOM    946  N   PHE A 113     -10.495 -22.608  18.015  1.00 44.11           N  
ANISOU  946  N   PHE A 113     5774   5903   5081    -54   -483   -191       N  
ATOM    947  CA  PHE A 113     -10.185 -22.940  16.650  1.00 43.46           C  
ANISOU  947  CA  PHE A 113     5723   5811   4978    -29   -498   -197       C  
ATOM    948  C   PHE A 113      -8.737 -22.630  16.375  1.00 43.16           C  
ANISOU  948  C   PHE A 113     5725   5755   4919    -33   -468   -162       C  
ATOM    949  O   PHE A 113      -8.083 -21.941  17.151  1.00 45.44           O  
ANISOU  949  O   PHE A 113     6019   6038   5209    -56   -445   -136       O  
ATOM    950  CB  PHE A 113     -11.103 -22.176  15.687  1.00 44.16           C  
ANISOU  950  CB  PHE A 113     5830   5910   5038     24   -534   -220       C  
ATOM    951  CG  PHE A 113     -10.815 -20.696  15.587  1.00 44.73           C  
ANISOU  951  CG  PHE A 113     5953   5964   5077     55   -524   -197       C  
ATOM    952  CD1 PHE A 113     -10.873 -19.869  16.711  1.00 44.04           C  
ANISOU  952  CD1 PHE A 113     5863   5871   5001     43   -506   -187       C  
ATOM    953  CD2 PHE A 113     -10.525 -20.125  14.353  1.00 41.15           C  
ANISOU  953  CD2 PHE A 113     5561   5496   4578     96   -531   -185       C  
ATOM    954  CE1 PHE A 113     -10.619 -18.494  16.602  1.00 45.38           C  
ANISOU  954  CE1 PHE A 113     6093   6009   5141     68   -499   -169       C  
ATOM    955  CE2 PHE A 113     -10.275 -18.752  14.236  1.00 45.22           C  
ANISOU  955  CE2 PHE A 113     6136   5982   5063    119   -520   -159       C  
ATOM    956  CZ  PHE A 113     -10.323 -17.939  15.362  1.00 43.70           C  
ANISOU  956  CZ  PHE A 113     5943   5773   4887    103   -505   -153       C  
ATOM    957  N   ASP A 114      -8.231 -23.173  15.282  1.00 41.40           N  
ANISOU  957  N   ASP A 114     5528   5528   4676    -15   -468   -163       N  
ATOM    958  CA  ASP A 114      -6.965 -22.738  14.753  1.00 40.83           C  
ANISOU  958  CA  ASP A 114     5489   5448   4576    -10   -435   -129       C  
ATOM    959  C   ASP A 114      -7.023 -22.920  13.256  1.00 41.10           C  
ANISOU  959  C   ASP A 114     5565   5482   4567     35   -445   -142       C  
ATOM    960  O   ASP A 114      -7.920 -23.598  12.720  1.00 39.93           O  
ANISOU  960  O   ASP A 114     5416   5338   4416     57   -483   -181       O  
ATOM    961  CB  ASP A 114      -5.796 -23.509  15.367  1.00 43.52           C  
ANISOU  961  CB  ASP A 114     5802   5795   4939    -39   -404   -107       C  
ATOM    962  CG  ASP A 114      -4.436 -22.845  15.104  1.00 47.16           C  
ANISOU  962  CG  ASP A 114     6275   6264   5381    -49   -365    -68       C  
ATOM    963  OD1 ASP A 114      -4.358 -21.604  14.837  1.00 44.50           O  
ANISOU  963  OD1 ASP A 114     5970   5917   5022    -54   -356    -51       O  
ATOM    964  OD2 ASP A 114      -3.436 -23.591  15.160  1.00 47.15           O  
ANISOU  964  OD2 ASP A 114     6250   6278   5388    -51   -341    -54       O  
ATOM    965  N   ILE A 115      -6.082 -22.278  12.579  1.00 39.63           N  
ANISOU  965  N   ILE A 115     5417   5294   4345     45   -411   -109       N  
ATOM    966  CA  ILE A 115      -6.075 -22.252  11.139  1.00 38.29           C  
ANISOU  966  CA  ILE A 115     5302   5127   4120     94   -413   -113       C  
ATOM    967  C   ILE A 115      -4.689 -22.597  10.648  1.00 39.49           C  
ANISOU  967  C   ILE A 115     5462   5291   4253     93   -359    -85       C  
ATOM    968  O   ILE A 115      -3.695 -22.428  11.377  1.00 38.59           O  
ANISOU  968  O   ILE A 115     5313   5185   4165     53   -321    -53       O  
ATOM    969  CB  ILE A 115      -6.547 -20.884  10.579  1.00 38.32           C  
ANISOU  969  CB  ILE A 115     5362   5116   4081    122   -423    -97       C  
ATOM    970  CG1 ILE A 115      -5.449 -19.828  10.664  1.00 35.80           C  
ANISOU  970  CG1 ILE A 115     5071   4782   3750     91   -368    -42       C  
ATOM    971  CG2 ILE A 115      -7.819 -20.403  11.302  1.00 38.50           C  
ANISOU  971  CG2 ILE A 115     5364   5134   4130    127   -468   -121       C  
ATOM    972  CD1 ILE A 115      -5.860 -18.499  10.017  1.00 37.87           C  
ANISOU  972  CD1 ILE A 115     5410   5015   3965    122   -373    -20       C  
ATOM    973  N   GLU A 116      -4.634 -23.124   9.429  1.00 37.52           N  
ANISOU  973  N   GLU A 116     5252   5048   3954    141   -358   -100       N  
ATOM    974  CA  GLU A 116      -3.374 -23.328   8.755  1.00 38.09           C  
ANISOU  974  CA  GLU A 116     5338   5140   3994    156   -299    -73       C  
ATOM    975  C   GLU A 116      -3.345 -22.430   7.530  1.00 40.54           C  
ANISOU  975  C   GLU A 116     5720   5452   4231    191   -281    -49       C  
ATOM    976  O   GLU A 116      -4.354 -22.298   6.805  1.00 38.12           O  
ANISOU  976  O   GLU A 116     5465   5137   3884    234   -328    -76       O  
ATOM    977  CB  GLU A 116      -3.188 -24.789   8.339  1.00 39.07           C  
ANISOU  977  CB  GLU A 116     5460   5270   4113    193   -303   -110       C  
ATOM    978  CG  GLU A 116      -3.378 -25.821   9.437  1.00 43.26           C  
ANISOU  978  CG  GLU A 116     5939   5787   4710    166   -327   -134       C  
ATOM    979  CD  GLU A 116      -2.337 -25.726  10.532  1.00 48.77           C  
ANISOU  979  CD  GLU A 116     6577   6500   5452    127   -288    -94       C  
ATOM    980  OE1 GLU A 116      -1.216 -25.234  10.273  1.00 49.44           O  
ANISOU  980  OE1 GLU A 116     6651   6615   5518    127   -234    -54       O  
ATOM    981  OE2 GLU A 116      -2.643 -26.140  11.667  1.00 50.76           O  
ANISOU  981  OE2 GLU A 116     6790   6740   5755     95   -310   -100       O  
ATOM    982  N   VAL A 117      -2.183 -21.813   7.320  1.00 40.77           N  
ANISOU  982  N   VAL A 117     5753   5496   4242    171   -212      4       N  
ATOM    983  CA  VAL A 117      -1.916 -21.004   6.137  1.00 42.04           C  
ANISOU  983  CA  VAL A 117     5988   5659   4328    198   -174     40       C  
ATOM    984  C   VAL A 117      -0.543 -21.359   5.558  1.00 43.08           C  
ANISOU  984  C   VAL A 117     6104   5832   4431    203    -92     71       C  
ATOM    985  O   VAL A 117       0.482 -21.098   6.185  1.00 42.28           O  
ANISOU  985  O   VAL A 117     5944   5751   4371    148    -43    108       O  
ATOM    986  CB  VAL A 117      -1.966 -19.494   6.459  1.00 41.28           C  
ANISOU  986  CB  VAL A 117     5921   5529   4235    154   -163     87       C  
ATOM    987  CG1 VAL A 117      -1.664 -18.669   5.205  1.00 42.51           C  
ANISOU  987  CG1 VAL A 117     6166   5678   4307    180   -117    134       C  
ATOM    988  CG2 VAL A 117      -3.315 -19.114   7.062  1.00 39.44           C  
ANISOU  988  CG2 VAL A 117     5698   5261   4027    162   -238     55       C  
ATOM    989  N   THR A 118      -0.530 -21.954   4.364  1.00 45.20           N  
ANISOU  989  N   THR A 118     6426   6120   4630    272    -80     53       N  
ATOM    990  CA  THR A 118       0.716 -22.281   3.682  1.00 48.49           C  
ANISOU  990  CA  THR A 118     6834   6584   5008    293      5     81       C  
ATOM    991  C   THR A 118       1.362 -21.016   3.128  1.00 51.31           C  
ANISOU  991  C   THR A 118     7228   6949   5320    262     77    154       C  
ATOM    992  O   THR A 118       0.708 -20.229   2.445  1.00 51.52           O  
ANISOU  992  O   THR A 118     7342   6945   5287    282     61    170       O  
ATOM    993  CB  THR A 118       0.490 -23.301   2.554  1.00 49.35           C  
ANISOU  993  CB  THR A 118     7000   6707   5044    383     -4     33       C  
ATOM    994  OG1 THR A 118      -0.007 -24.523   3.110  1.00 49.94           O  
ANISOU  994  OG1 THR A 118     7043   6765   5168    400    -65    -32       O  
ATOM    995  CG2 THR A 118       1.790 -23.588   1.800  1.00 49.71           C  
ANISOU  995  CG2 THR A 118     7040   6808   5040    417     95     63       C  
ATOM    996  N   SER A 119       2.644 -20.826   3.435  1.00 55.02           N  
ANISOU  996  N   SER A 119     7628   7459   5819    211    156    199       N  
ATOM    997  CA  SER A 119       3.376 -19.653   2.968  1.00 58.29           C  
ANISOU  997  CA  SER A 119     8067   7880   6200    161    235    273       C  
ATOM    998  C   SER A 119       4.771 -19.993   2.436  1.00 60.75           C  
ANISOU  998  C   SER A 119     8325   8270   6488    165    340    308       C  
ATOM    999  O   SER A 119       5.660 -20.345   3.209  1.00 59.47           O  
ANISOU  999  O   SER A 119     8052   8153   6391    125    366    312       O  
ATOM   1000  CB  SER A 119       3.465 -18.604   4.076  1.00 57.84           C  
ANISOU 1000  CB  SER A 119     7975   7786   6215     58    223    304       C  
ATOM   1001  OG  SER A 119       4.195 -17.474   3.642  1.00 60.10           O  
ANISOU 1001  OG  SER A 119     8290   8070   6475     -4    301    376       O  
ATOM   1002  N   PRO A 120       4.968 -19.866   1.109  1.00 64.03           N  
ANISOU 1002  N   PRO A 120     8817   8707   6804    217    402    335       N  
ATOM   1003  CA  PRO A 120       6.267 -20.140   0.495  1.00 67.09           C  
ANISOU 1003  CA  PRO A 120     9156   9177   7159    229    514    371       C  
ATOM   1004  C   PRO A 120       7.283 -18.992   0.640  1.00 69.07           C  
ANISOU 1004  C   PRO A 120     9360   9451   7432    119    604    455       C  
ATOM   1005  O   PRO A 120       8.422 -19.127   0.177  1.00 70.70           O  
ANISOU 1005  O   PRO A 120     9508   9737   7618    115    707    492       O  
ATOM   1006  CB  PRO A 120       5.914 -20.366  -0.977  1.00 67.86           C  
ANISOU 1006  CB  PRO A 120     9372   9281   7131    328    540    366       C  
ATOM   1007  CG  PRO A 120       4.727 -19.502  -1.205  1.00 68.26           C  
ANISOU 1007  CG  PRO A 120     9537   9252   7146    324    472    372       C  
ATOM   1008  CD  PRO A 120       3.973 -19.430   0.113  1.00 65.04           C  
ANISOU 1008  CD  PRO A 120     9082   8789   6841    274    371    334       C  
ATOM   1009  N   ASP A 121       6.882 -17.892   1.282  1.00 69.25           N  
ANISOU 1009  N   ASP A 121     9408   9405   7499     30    568    482       N  
ATOM   1010  CA  ASP A 121       7.802 -16.772   1.547  1.00 70.47           C  
ANISOU 1010  CA  ASP A 121     9522   9565   7687    -94    642    555       C  
ATOM   1011  C   ASP A 121       7.823 -16.270   3.004  1.00 70.16           C  
ANISOU 1011  C   ASP A 121     9411   9490   7756   -198    584    545       C  
ATOM   1012  O   ASP A 121       7.852 -15.064   3.270  1.00 69.12           O  
ANISOU 1012  O   ASP A 121     9319   9300   7644   -294    593    588       O  
ATOM   1013  CB  ASP A 121       7.608 -15.619   0.541  1.00 71.72           C  
ANISOU 1013  CB  ASP A 121     9815   9671   7762   -113    696    623       C  
ATOM   1014  CG  ASP A 121       6.155 -15.220   0.362  1.00 70.53           C  
ANISOU 1014  CG  ASP A 121     9802   9425   7572    -58    603    600       C  
ATOM   1015  OD1 ASP A 121       5.617 -15.440  -0.744  1.00 71.40           O  
ANISOU 1015  OD1 ASP A 121    10015   9532   7582     39    604    597       O  
ATOM   1016  OD2 ASP A 121       5.554 -14.686   1.315  1.00 70.27           O  
ANISOU 1016  OD2 ASP A 121     9773   9322   7603   -106    529    583       O  
ATOM   1017  N   GLY A 122       7.838 -17.210   3.942  1.00 70.61           N  
ANISOU 1017  N   GLY A 122     9371   9578   7879   -177    525    488       N  
ATOM   1018  CA  GLY A 122       8.026 -16.876   5.351  1.00 71.34           C  
ANISOU 1018  CA  GLY A 122     9383   9658   8067   -269    476    477       C  
ATOM   1019  C   GLY A 122       6.731 -16.775   6.129  1.00 70.48           C  
ANISOU 1019  C   GLY A 122     9332   9464   7984   -254    367    429       C  
ATOM   1020  O   GLY A 122       5.702 -17.303   5.710  1.00 70.76           O  
ANISOU 1020  O   GLY A 122     9438   9469   7980   -163    318    391       O  
ATOM   1021  N   PHE A 123       6.786 -16.098   7.270  1.00 69.61           N  
ANISOU 1021  N   PHE A 123     9188   9320   7941   -345    330    428       N  
ATOM   1022  CA  PHE A 123       5.626 -15.980   8.138  1.00 67.67           C  
ANISOU 1022  CA  PHE A 123     8985   9004   7724   -333    235    382       C  
ATOM   1023  C   PHE A 123       4.498 -15.207   7.456  1.00 66.06           C  
ANISOU 1023  C   PHE A 123     8922   8714   7463   -296    213    390       C  
ATOM   1024  O   PHE A 123       4.700 -14.083   6.992  1.00 66.34           O  
ANISOU 1024  O   PHE A 123     9029   8704   7471   -347    256    441       O  
ATOM   1025  CB  PHE A 123       6.002 -15.316   9.463  1.00 68.71           C  
ANISOU 1025  CB  PHE A 123     9061   9119   7926   -439    206    380       C  
ATOM   1026  CG  PHE A 123       4.885 -15.295  10.465  1.00 68.99           C  
ANISOU 1026  CG  PHE A 123     9127   9096   7990   -421    115    331       C  
ATOM   1027  CD1 PHE A 123       4.730 -16.340  11.372  1.00 68.93           C  
ANISOU 1027  CD1 PHE A 123     9043   9127   8022   -388     64    285       C  
ATOM   1028  CD2 PHE A 123       3.985 -14.230  10.504  1.00 68.26           C  
ANISOU 1028  CD2 PHE A 123     9142   8911   7881   -432     86    333       C  
ATOM   1029  CE1 PHE A 123       3.696 -16.325  12.303  1.00 70.18           C  
ANISOU 1029  CE1 PHE A 123     9226   9238   8202   -374     -9    244       C  
ATOM   1030  CE2 PHE A 123       2.947 -14.204  11.430  1.00 68.89           C  
ANISOU 1030  CE2 PHE A 123     9242   8947   7984   -409     10    286       C  
ATOM   1031  CZ  PHE A 123       2.801 -15.252  12.333  1.00 68.70           C  
ANISOU 1031  CZ  PHE A 123     9136   8968   7998   -384    -34    242       C  
ATOM   1032  N   PRO A 124       3.304 -15.816   7.396  1.00 63.08           N  
ANISOU 1032  N   PRO A 124     8585   8315   7068   -206    144    341       N  
ATOM   1033  CA  PRO A 124       2.169 -15.129   6.803  1.00 61.53           C  
ANISOU 1033  CA  PRO A 124     8511   8048   6819   -158    111    342       C  
ATOM   1034  C   PRO A 124       1.600 -14.108   7.788  1.00 60.54           C  
ANISOU 1034  C   PRO A 124     8419   7849   6735   -209     64    337       C  
ATOM   1035  O   PRO A 124       0.906 -14.474   8.742  1.00 60.01           O  
ANISOU 1035  O   PRO A 124     8315   7776   6712   -195     -2    287       O  
ATOM   1036  CB  PRO A 124       1.172 -16.261   6.521  1.00 60.81           C  
ANISOU 1036  CB  PRO A 124     8422   7975   6707    -56     50    283       C  
ATOM   1037  CG  PRO A 124       1.676 -17.470   7.286  1.00 60.29           C  
ANISOU 1037  CG  PRO A 124     8241   7967   6698    -63     42    247       C  
ATOM   1038  CD  PRO A 124       2.925 -17.101   8.009  1.00 60.55           C  
ANISOU 1038  CD  PRO A 124     8196   8028   6782   -156     90    281       C  
ATOM   1039  N   GLU A 125       1.932 -12.841   7.566  1.00 60.36           N  
ANISOU 1039  N   GLU A 125     8469   7769   6697   -268    103    389       N  
ATOM   1040  CA  GLU A 125       1.469 -11.752   8.414  1.00 58.04           C  
ANISOU 1040  CA  GLU A 125     8227   7391   6433   -314     66    385       C  
ATOM   1041  C   GLU A 125      -0.034 -11.581   8.292  1.00 55.17           C  
ANISOU 1041  C   GLU A 125     7944   6978   6039   -216     -5    353       C  
ATOM   1042  O   GLU A 125      -0.547 -11.441   7.185  1.00 54.82           O  
ANISOU 1042  O   GLU A 125     7985   6920   5926   -142     -1    372       O  
ATOM   1043  CB  GLU A 125       2.184 -10.445   8.061  1.00 61.25           C  
ANISOU 1043  CB  GLU A 125     8711   7736   6826   -402    129    452       C  
ATOM   1044  CG  GLU A 125       3.516 -10.228   8.796  1.00 66.05           C  
ANISOU 1044  CG  GLU A 125     9227   8372   7495   -536    171    470       C  
ATOM   1045  CD  GLU A 125       3.356 -10.024  10.307  1.00 71.21           C  
ANISOU 1045  CD  GLU A 125     9837   9001   8217   -588    108    421       C  
ATOM   1046  OE1 GLU A 125       2.333  -9.441  10.751  1.00 69.97           O  
ANISOU 1046  OE1 GLU A 125     9761   8766   8057   -553     53    394       O  
ATOM   1047  OE2 GLU A 125       4.271 -10.445  11.053  1.00 75.24           O  
ANISOU 1047  OE2 GLU A 125    10230   9577   8781   -660    114    408       O  
ATOM   1048  N   PRO A 126      -0.746 -11.615   9.434  1.00 53.29           N  
ANISOU 1048  N   PRO A 126     7676   6724   5849   -211    -68    302       N  
ATOM   1049  CA  PRO A 126      -2.198 -11.450   9.470  1.00 52.99           C  
ANISOU 1049  CA  PRO A 126     7692   6651   5792   -119   -136    266       C  
ATOM   1050  C   PRO A 126      -2.682 -10.142   8.858  1.00 54.13           C  
ANISOU 1050  C   PRO A 126     7976   6707   5885    -87   -134    303       C  
ATOM   1051  O   PRO A 126      -3.769 -10.103   8.289  1.00 53.18           O  
ANISOU 1051  O   PRO A 126     7910   6577   5719     15   -178    290       O  
ATOM   1052  CB  PRO A 126      -2.514 -11.487  10.968  1.00 52.37           C  
ANISOU 1052  CB  PRO A 126     7554   6568   5778   -151   -179    219       C  
ATOM   1053  CG  PRO A 126      -1.449 -12.338  11.541  1.00 52.55           C  
ANISOU 1053  CG  PRO A 126     7465   6656   5847   -222   -154    214       C  
ATOM   1054  CD  PRO A 126      -0.213 -12.010  10.752  1.00 51.60           C  
ANISOU 1054  CD  PRO A 126     7358   6542   5707   -282    -81    272       C  
ATOM   1055  N   SER A 127      -1.877  -9.089   8.969  1.00 56.71           N  
ANISOU 1055  N   SER A 127     8361   6968   6216   -173    -86    351       N  
ATOM   1056  CA  SER A 127      -2.237  -7.763   8.454  1.00 59.24           C  
ANISOU 1056  CA  SER A 127     8833   7185   6491   -151    -78    394       C  
ATOM   1057  C   SER A 127      -2.338  -7.668   6.920  1.00 61.17           C  
ANISOU 1057  C   SER A 127     9167   7427   6647    -83    -48    446       C  
ATOM   1058  O   SER A 127      -3.085  -6.831   6.402  1.00 63.10           O  
ANISOU 1058  O   SER A 127     9537   7599   6838    -10    -68    469       O  
ATOM   1059  CB  SER A 127      -1.284  -6.694   9.003  1.00 59.96           C  
ANISOU 1059  CB  SER A 127     8967   7199   6615   -279    -32    430       C  
ATOM   1060  OG  SER A 127       0.072  -7.096   8.896  1.00 62.48           O  
ANISOU 1060  OG  SER A 127     9203   7577   6960   -385     33    460       O  
ATOM   1061  N   GLN A 128      -1.591  -8.512   6.203  1.00 61.25           N  
ANISOU 1061  N   GLN A 128     9118   7516   6636    -97      1    465       N  
ATOM   1062  CA  GLN A 128      -1.686  -8.573   4.737  1.00 62.91           C  
ANISOU 1062  CA  GLN A 128     9409   7740   6753    -24     29    508       C  
ATOM   1063  C   GLN A 128      -2.624  -9.695   4.292  1.00 61.13           C  
ANISOU 1063  C   GLN A 128     9141   7589   6496     93    -36    450       C  
ATOM   1064  O   GLN A 128      -3.330  -9.558   3.284  1.00 62.22           O  
ANISOU 1064  O   GLN A 128     9368   7719   6553    192    -61    462       O  
ATOM   1065  CB  GLN A 128      -0.314  -8.776   4.058  1.00 64.43           C  
ANISOU 1065  CB  GLN A 128     9577   7977   6926    -99    130    565       C  
ATOM   1066  CG  GLN A 128       0.936  -8.382   4.854  1.00 69.52           C  
ANISOU 1066  CG  GLN A 128    10157   8613   7643   -250    191    591       C  
ATOM   1067  CD  GLN A 128       0.944  -6.932   5.304  1.00 74.53           C  
ANISOU 1067  CD  GLN A 128    10896   9126   8295   -322    198    626       C  
ATOM   1068  OE1 GLN A 128       1.322  -6.632   6.440  1.00 78.03           O  
ANISOU 1068  OE1 GLN A 128    11286   9546   8814   -415    185    603       O  
ATOM   1069  NE2 GLN A 128       0.518  -6.027   4.424  1.00 74.61           N  
ANISOU 1069  NE2 GLN A 128    11064   9053   8231   -274    213    681       N  
ATOM   1070  N   ALA A 129      -2.606 -10.800   5.043  1.00 57.76           N  
ANISOU 1070  N   ALA A 129     8582   7231   6133     77    -65    389       N  
ATOM   1071  CA  ALA A 129      -3.314 -12.038   4.702  1.00 55.63           C  
ANISOU 1071  CA  ALA A 129     8257   7034   5848    161   -119    330       C  
ATOM   1072  C   ALA A 129      -3.374 -12.270   3.197  1.00 56.68           C  
ANISOU 1072  C   ALA A 129     8464   7193   5880    238   -103    354       C  
ATOM   1073  O   ALA A 129      -4.448 -12.272   2.595  1.00 57.20           O  
ANISOU 1073  O   ALA A 129     8585   7258   5891    336   -167    331       O  
ATOM   1074  CB  ALA A 129      -4.705 -12.055   5.313  1.00 53.68           C  
ANISOU 1074  CB  ALA A 129     7996   6775   5626    224   -212    272       C  
ATOM   1075  N   LYS A 130      -2.204 -12.457   2.599  1.00 57.70           N  
ANISOU 1075  N   LYS A 130     8590   7352   5981    196    -17    398       N  
ATOM   1076  CA  LYS A 130      -2.098 -12.595   1.148  1.00 59.75           C  
ANISOU 1076  CA  LYS A 130     8932   7637   6133    264     16    429       C  
ATOM   1077  C   LYS A 130      -2.071 -14.049   0.684  1.00 58.84           C  
ANISOU 1077  C   LYS A 130     8753   7605   5998    316      1    373       C  
ATOM   1078  O   LYS A 130      -2.113 -14.326  -0.518  1.00 60.62           O  
ANISOU 1078  O   LYS A 130     9045   7859   6126    387     15    382       O  
ATOM   1079  CB  LYS A 130      -0.884 -11.822   0.612  1.00 62.05           C  
ANISOU 1079  CB  LYS A 130     9279   7909   6389    195    130    519       C  
ATOM   1080  CG  LYS A 130       0.444 -12.135   1.295  1.00 62.93           C  
ANISOU 1080  CG  LYS A 130     9273   8061   6576     82    205    532       C  
ATOM   1081  CD  LYS A 130       1.544 -11.241   0.742  1.00 67.74           C  
ANISOU 1081  CD  LYS A 130     9936   8651   7152      4    317    624       C  
ATOM   1082  CE  LYS A 130       2.920 -11.853   0.957  1.00 69.95           C  
ANISOU 1082  CE  LYS A 130    10089   9012   7476    -75    401    635       C  
ATOM   1083  NZ  LYS A 130       3.897 -11.326  -0.030  1.00 71.30           N  
ANISOU 1083  NZ  LYS A 130    10311   9198   7583   -116    521    722       N  
ATOM   1084  N   HIS A 131      -2.005 -14.975   1.636  1.00 55.60           N  
ANISOU 1084  N   HIS A 131     8223   7230   5674    283    -26    316       N  
ATOM   1085  CA  HIS A 131      -2.023 -16.396   1.306  1.00 53.67           C  
ANISOU 1085  CA  HIS A 131     7925   7049   5420    330    -45    258       C  
ATOM   1086  C   HIS A 131      -3.342 -17.032   1.737  1.00 50.36           C  
ANISOU 1086  C   HIS A 131     7473   6629   5032    376   -155    179       C  
ATOM   1087  O   HIS A 131      -3.949 -16.601   2.718  1.00 48.51           O  
ANISOU 1087  O   HIS A 131     7208   6363   4862    348   -201    166       O  
ATOM   1088  CB  HIS A 131      -0.833 -17.127   1.940  1.00 54.63           C  
ANISOU 1088  CB  HIS A 131     7937   7214   5607    265     16    257       C  
ATOM   1089  CG  HIS A 131       0.497 -16.521   1.613  1.00 57.34           C  
ANISOU 1089  CG  HIS A 131     8284   7571   5931    206    126    332       C  
ATOM   1090  ND1 HIS A 131       1.215 -15.766   2.518  1.00 58.71           N  
ANISOU 1090  ND1 HIS A 131     8409   7724   6174    103    166    373       N  
ATOM   1091  CD2 HIS A 131       1.237 -16.553   0.480  1.00 58.76           C  
ANISOU 1091  CD2 HIS A 131     8509   7788   6030    232    208    373       C  
ATOM   1092  CE1 HIS A 131       2.340 -15.360   1.956  1.00 59.94           C  
ANISOU 1092  CE1 HIS A 131     8571   7905   6300     60    266    437       C  
ATOM   1093  NE2 HIS A 131       2.379 -15.826   0.720  1.00 60.70           N  
ANISOU 1093  NE2 HIS A 131     8722   8038   6303    139    298    441       N  
ATOM   1094  N   PRO A 132      -3.793 -18.060   0.998  1.00 48.86           N  
ANISOU 1094  N   PRO A 132     7292   6477   4796    445   -196    125       N  
ATOM   1095  CA  PRO A 132      -5.046 -18.737   1.328  1.00 46.94           C  
ANISOU 1095  CA  PRO A 132     7013   6239   4584    478   -300     48       C  
ATOM   1096  C   PRO A 132      -5.033 -19.429   2.683  1.00 43.55           C  
ANISOU 1096  C   PRO A 132     6470   5811   4266    414   -315     12       C  
ATOM   1097  O   PRO A 132      -4.020 -20.005   3.073  1.00 44.59           O  
ANISOU 1097  O   PRO A 132     6548   5958   4435    371   -259     21       O  
ATOM   1098  CB  PRO A 132      -5.172 -19.788   0.218  1.00 46.82           C  
ANISOU 1098  CB  PRO A 132     7032   6262   4495    545   -322      0       C  
ATOM   1099  CG  PRO A 132      -4.393 -19.231  -0.913  1.00 48.27           C  
ANISOU 1099  CG  PRO A 132     7308   6454   4578    579   -247     60       C  
ATOM   1100  CD  PRO A 132      -3.218 -18.573  -0.258  1.00 48.57           C  
ANISOU 1100  CD  PRO A 132     7310   6478   4666    497   -150    131       C  
ATOM   1101  N   ILE A 133      -6.153 -19.353   3.393  1.00 41.20           N  
ANISOU 1101  N   ILE A 133     6137   5501   4017    413   -390    -26       N  
ATOM   1102  CA  ILE A 133      -6.406 -20.214   4.543  1.00 39.47           C  
ANISOU 1102  CA  ILE A 133     5821   5288   3889    366   -417    -70       C  
ATOM   1103  C   ILE A 133      -6.769 -21.584   3.976  1.00 41.98           C  
ANISOU 1103  C   ILE A 133     6129   5630   4191    398   -459   -135       C  
ATOM   1104  O   ILE A 133      -7.774 -21.718   3.268  1.00 44.25           O  
ANISOU 1104  O   ILE A 133     6448   5930   4436    450   -528   -176       O  
ATOM   1105  CB  ILE A 133      -7.584 -19.689   5.401  1.00 39.57           C  
ANISOU 1105  CB  ILE A 133     5800   5286   3949    360   -478    -91       C  
ATOM   1106  CG1 ILE A 133      -7.295 -18.269   5.897  1.00 38.90           C  
ANISOU 1106  CG1 ILE A 133     5745   5163   3871    337   -443    -34       C  
ATOM   1107  CG2 ILE A 133      -7.900 -20.644   6.563  1.00 35.34           C  
ANISOU 1107  CG2 ILE A 133     5168   4760   3500    311   -501   -134       C  
ATOM   1108  CD1 ILE A 133      -8.462 -17.610   6.605  1.00 37.05           C  
ANISOU 1108  CD1 ILE A 133     5495   4914   3667    353   -498    -53       C  
ATOM   1109  N   ASP A 134      -5.948 -22.591   4.253  1.00 42.59           N  
ANISOU 1109  N   ASP A 134     6167   5715   4300    372   -420   -145       N  
ATOM   1110  CA  ASP A 134      -6.182 -23.927   3.694  1.00 44.05           C  
ANISOU 1110  CA  ASP A 134     6360   5910   4468    402   -454   -207       C  
ATOM   1111  C   ASP A 134      -6.686 -24.987   4.690  1.00 43.41           C  
ANISOU 1111  C   ASP A 134     6208   5816   4472    358   -495   -256       C  
ATOM   1112  O   ASP A 134      -6.992 -26.112   4.300  1.00 43.99           O  
ANISOU 1112  O   ASP A 134     6292   5883   4540    373   -530   -313       O  
ATOM   1113  CB  ASP A 134      -4.967 -24.420   2.899  1.00 46.22           C  
ANISOU 1113  CB  ASP A 134     6673   6200   4689    434   -384   -192       C  
ATOM   1114  CG  ASP A 134      -3.655 -24.239   3.642  1.00 48.94           C  
ANISOU 1114  CG  ASP A 134     6965   6551   5078    389   -299   -136       C  
ATOM   1115  OD1 ASP A 134      -3.629 -24.365   4.887  1.00 48.80           O  
ANISOU 1115  OD1 ASP A 134     6876   6522   5144    333   -305   -132       O  
ATOM   1116  OD2 ASP A 134      -2.638 -23.987   2.962  1.00 54.17           O  
ANISOU 1116  OD2 ASP A 134     7656   7237   5688    410   -226    -96       O  
ATOM   1117  N   ALA A 135      -6.788 -24.622   5.967  1.00 43.30           N  
ANISOU 1117  N   ALA A 135     6128   5791   4532    302   -489   -234       N  
ATOM   1118  CA  ALA A 135      -7.515 -25.436   6.943  1.00 40.81           C  
ANISOU 1118  CA  ALA A 135     5751   5465   4292    258   -530   -273       C  
ATOM   1119  C   ALA A 135      -8.027 -24.592   8.110  1.00 41.12           C  
ANISOU 1119  C   ALA A 135     5737   5503   4384    217   -537   -250       C  
ATOM   1120  O   ALA A 135      -7.373 -23.633   8.527  1.00 40.22           O  
ANISOU 1120  O   ALA A 135     5625   5387   4272    203   -492   -199       O  
ATOM   1121  CB  ALA A 135      -6.638 -26.568   7.456  1.00 40.80           C  
ANISOU 1121  CB  ALA A 135     5726   5448   4329    236   -493   -274       C  
ATOM   1122  N   ILE A 136      -9.210 -24.944   8.612  1.00 41.19           N  
ANISOU 1122  N   ILE A 136     5702   5515   4434    197   -591   -290       N  
ATOM   1123  CA  ILE A 136      -9.702 -24.459   9.901  1.00 39.53           C  
ANISOU 1123  CA  ILE A 136     5432   5307   4281    156   -591   -277       C  
ATOM   1124  C   ILE A 136     -10.313 -25.631  10.644  1.00 39.57           C  
ANISOU 1124  C   ILE A 136     5381   5307   4346    109   -613   -313       C  
ATOM   1125  O   ILE A 136     -11.072 -26.416  10.061  1.00 41.51           O  
ANISOU 1125  O   ILE A 136     5625   5557   4590    111   -662   -363       O  
ATOM   1126  CB  ILE A 136     -10.810 -23.385   9.781  1.00 40.76           C  
ANISOU 1126  CB  ILE A 136     5584   5482   4420    188   -633   -285       C  
ATOM   1127  CG1 ILE A 136     -10.435 -22.300   8.772  1.00 43.46           C  
ANISOU 1127  CG1 ILE A 136     6003   5820   4691    245   -623   -253       C  
ATOM   1128  CG2 ILE A 136     -11.127 -22.769  11.168  1.00 37.95           C  
ANISOU 1128  CG2 ILE A 136     5177   5127   4116    155   -617   -267       C  
ATOM   1129  CD1 ILE A 136     -11.601 -21.384   8.386  1.00 45.92           C  
ANISOU 1129  CD1 ILE A 136     6326   6149   4973    301   -678   -267       C  
ATOM   1130  N   THR A 137      -9.972 -25.750  11.925  1.00 37.13           N  
ANISOU 1130  N   THR A 137     5031   4989   4087     62   -579   -287       N  
ATOM   1131  CA  THR A 137     -10.694 -26.625  12.830  1.00 35.66           C  
ANISOU 1131  CA  THR A 137     4791   4799   3958     12   -593   -309       C  
ATOM   1132  C   THR A 137     -11.262 -25.779  13.948  1.00 36.30           C  
ANISOU 1132  C   THR A 137     4825   4902   4067     -8   -584   -291       C  
ATOM   1133  O   THR A 137     -10.525 -25.126  14.686  1.00 37.18           O  
ANISOU 1133  O   THR A 137     4940   5008   4178    -15   -546   -252       O  
ATOM   1134  CB  THR A 137      -9.808 -27.735  13.416  1.00 37.21           C  
ANISOU 1134  CB  THR A 137     4992   4964   4183    -20   -558   -293       C  
ATOM   1135  OG1 THR A 137      -9.393 -28.617  12.368  1.00 36.48           O  
ANISOU 1135  OG1 THR A 137     4948   4848   4065      6   -567   -318       O  
ATOM   1136  CG2 THR A 137     -10.575 -28.541  14.496  1.00 36.56           C  
ANISOU 1136  CG2 THR A 137     4861   4871   4158    -79   -564   -303       C  
ATOM   1137  N   HIS A 138     -12.579 -25.823  14.074  1.00 38.04           N  
ANISOU 1137  N   HIS A 138     4998   5149   4308    -17   -621   -325       N  
ATOM   1138  CA  HIS A 138     -13.319 -25.019  15.023  1.00 37.92           C  
ANISOU 1138  CA  HIS A 138     4934   5162   4312    -21   -615   -318       C  
ATOM   1139  C   HIS A 138     -14.146 -25.930  15.916  1.00 38.54           C  
ANISOU 1139  C   HIS A 138     4944   5253   4444    -80   -614   -335       C  
ATOM   1140  O   HIS A 138     -15.121 -26.534  15.458  1.00 40.45           O  
ANISOU 1140  O   HIS A 138     5148   5516   4705    -97   -654   -377       O  
ATOM   1141  CB  HIS A 138     -14.230 -24.090  14.236  1.00 38.25           C  
ANISOU 1141  CB  HIS A 138     4973   5237   4323     39   -660   -342       C  
ATOM   1142  CG  HIS A 138     -15.095 -23.214  15.080  1.00 36.59           C  
ANISOU 1142  CG  HIS A 138     4714   5061   4127     55   -657   -343       C  
ATOM   1143  ND1 HIS A 138     -14.977 -21.841  15.079  1.00 36.96           N  
ANISOU 1143  ND1 HIS A 138     4801   5103   4141    111   -650   -322       N  
ATOM   1144  CD2 HIS A 138     -16.120 -23.505  15.914  1.00 35.44           C  
ANISOU 1144  CD2 HIS A 138     4488   4955   4024     26   -657   -362       C  
ATOM   1145  CE1 HIS A 138     -15.885 -21.324  15.888  1.00 37.48           C  
ANISOU 1145  CE1 HIS A 138     4814   5202   4224    126   -648   -333       C  
ATOM   1146  NE2 HIS A 138     -16.591 -22.311  16.407  1.00 39.48           N  
ANISOU 1146  NE2 HIS A 138     4988   5489   4523     75   -649   -356       N  
ATOM   1147  N   TYR A 139     -13.752 -26.029  17.183  1.00 37.65           N  
ANISOU 1147  N   TYR A 139     4819   5132   4355   -116   -568   -302       N  
ATOM   1148  CA  TYR A 139     -14.497 -26.826  18.162  1.00 37.90           C  
ANISOU 1148  CA  TYR A 139     4793   5175   4432   -176   -552   -306       C  
ATOM   1149  C   TYR A 139     -15.532 -25.999  18.895  1.00 39.32           C  
ANISOU 1149  C   TYR A 139     4912   5409   4619   -166   -545   -313       C  
ATOM   1150  O   TYR A 139     -15.212 -24.948  19.454  1.00 38.76           O  
ANISOU 1150  O   TYR A 139     4858   5343   4525   -132   -522   -292       O  
ATOM   1151  CB  TYR A 139     -13.573 -27.497  19.185  1.00 35.98           C  
ANISOU 1151  CB  TYR A 139     4573   4896   4201   -215   -506   -265       C  
ATOM   1152  CG  TYR A 139     -14.333 -28.189  20.304  1.00 38.91           C  
ANISOU 1152  CG  TYR A 139     4895   5278   4610   -275   -480   -258       C  
ATOM   1153  CD1 TYR A 139     -14.538 -27.555  21.526  1.00 36.74           C  
ANISOU 1153  CD1 TYR A 139     4595   5035   4331   -278   -443   -234       C  
ATOM   1154  CD2 TYR A 139     -14.861 -29.472  20.131  1.00 38.92           C  
ANISOU 1154  CD2 TYR A 139     4883   5256   4649   -333   -489   -275       C  
ATOM   1155  CE1 TYR A 139     -15.233 -28.175  22.542  1.00 37.61           C  
ANISOU 1155  CE1 TYR A 139     4663   5159   4467   -332   -410   -222       C  
ATOM   1156  CE2 TYR A 139     -15.558 -30.103  21.153  1.00 38.73           C  
ANISOU 1156  CE2 TYR A 139     4818   5240   4659   -397   -456   -261       C  
ATOM   1157  CZ  TYR A 139     -15.738 -29.445  22.353  1.00 40.01           C  
ANISOU 1157  CZ  TYR A 139     4950   5440   4810   -394   -414   -232       C  
ATOM   1158  OH  TYR A 139     -16.431 -30.048  23.372  1.00 41.46           O  
ANISOU 1158  OH  TYR A 139     5095   5637   5020   -455   -372   -213       O  
ATOM   1159  N   ASP A 140     -16.760 -26.516  18.922  1.00 41.30           N  
ANISOU 1159  N   ASP A 140     5091   5698   4905   -198   -561   -344       N  
ATOM   1160  CA  ASP A 140     -17.898 -25.852  19.540  1.00 41.59           C  
ANISOU 1160  CA  ASP A 140     5051   5800   4952   -184   -553   -356       C  
ATOM   1161  C   ASP A 140     -18.308 -26.617  20.789  1.00 44.66           C  
ANISOU 1161  C   ASP A 140     5390   6201   5378   -257   -502   -338       C  
ATOM   1162  O   ASP A 140     -18.655 -27.800  20.702  1.00 46.07           O  
ANISOU 1162  O   ASP A 140     5542   6366   5594   -328   -506   -347       O  
ATOM   1163  CB  ASP A 140     -19.057 -25.811  18.538  1.00 42.17           C  
ANISOU 1163  CB  ASP A 140     5063   5925   5035   -162   -613   -407       C  
ATOM   1164  CG  ASP A 140     -20.296 -25.169  19.105  1.00 40.09           C  
ANISOU 1164  CG  ASP A 140     4705   5742   4784   -138   -606   -423       C  
ATOM   1165  OD1 ASP A 140     -21.033 -25.843  19.853  1.00 43.57           O  
ANISOU 1165  OD1 ASP A 140     5068   6219   5268   -204   -577   -426       O  
ATOM   1166  OD2 ASP A 140     -20.540 -23.994  18.786  1.00 38.61           O  
ANISOU 1166  OD2 ASP A 140     4525   5582   4564    -50   -627   -432       O  
ATOM   1167  N   SER A 141     -18.286 -25.946  21.943  1.00 45.24           N  
ANISOU 1167  N   SER A 141     5457   6296   5437   -241   -454   -312       N  
ATOM   1168  CA  SER A 141     -18.521 -26.626  23.226  1.00 46.72           C  
ANISOU 1168  CA  SER A 141     5614   6492   5645   -305   -396   -284       C  
ATOM   1169  C   SER A 141     -19.940 -27.148  23.401  1.00 47.52           C  
ANISOU 1169  C   SER A 141     5610   6656   5790   -354   -386   -307       C  
ATOM   1170  O   SER A 141     -20.141 -28.193  24.019  1.00 48.66           O  
ANISOU 1170  O   SER A 141     5735   6789   5965   -435   -350   -286       O  
ATOM   1171  CB  SER A 141     -18.138 -25.742  24.421  1.00 45.64           C  
ANISOU 1171  CB  SER A 141     5504   6367   5471   -270   -349   -256       C  
ATOM   1172  OG  SER A 141     -19.005 -24.632  24.547  1.00 49.79           O  
ANISOU 1172  OG  SER A 141     5982   6953   5982   -208   -348   -282       O  
ATOM   1173  N   ILE A 142     -20.915 -26.419  22.869  1.00 47.87           N  
ANISOU 1173  N   ILE A 142     5584   6768   5837   -304   -418   -347       N  
ATOM   1174  CA  ILE A 142     -22.310 -26.818  22.991  1.00 49.16           C  
ANISOU 1174  CA  ILE A 142     5626   7010   6045   -348   -412   -373       C  
ATOM   1175  C   ILE A 142     -22.624 -28.077  22.175  1.00 49.05           C  
ANISOU 1175  C   ILE A 142     5586   6975   6078   -434   -454   -398       C  
ATOM   1176  O   ILE A 142     -23.268 -28.996  22.677  1.00 49.67           O  
ANISOU 1176  O   ILE A 142     5602   7070   6202   -529   -422   -393       O  
ATOM   1177  CB  ILE A 142     -23.262 -25.656  22.639  1.00 51.31           C  
ANISOU 1177  CB  ILE A 142     5824   7368   6303   -255   -441   -411       C  
ATOM   1178  CG1 ILE A 142     -23.268 -24.642  23.786  1.00 53.06           C  
ANISOU 1178  CG1 ILE A 142     6052   7619   6489   -193   -380   -390       C  
ATOM   1179  CG2 ILE A 142     -24.683 -26.175  22.379  1.00 52.22           C  
ANISOU 1179  CG2 ILE A 142     5796   7573   6470   -302   -459   -450       C  
ATOM   1180  CD1 ILE A 142     -23.926 -23.318  23.463  1.00 56.87           C  
ANISOU 1180  CD1 ILE A 142     6502   8161   6945    -75   -407   -422       C  
ATOM   1181  N   ASP A 143     -22.162 -28.118  20.928  1.00 46.89           N  
ANISOU 1181  N   ASP A 143     5365   6660   5791   -405   -523   -425       N  
ATOM   1182  CA  ASP A 143     -22.322 -29.305  20.095  1.00 47.14           C  
ANISOU 1182  CA  ASP A 143     5396   6656   5857   -481   -569   -456       C  
ATOM   1183  C   ASP A 143     -21.382 -30.424  20.510  1.00 47.27           C  
ANISOU 1183  C   ASP A 143     5500   6575   5886   -552   -533   -418       C  
ATOM   1184  O   ASP A 143     -21.674 -31.607  20.283  1.00 48.34           O  
ANISOU 1184  O   ASP A 143     5630   6673   6063   -642   -545   -434       O  
ATOM   1185  CB  ASP A 143     -22.059 -28.973  18.629  1.00 47.30           C  
ANISOU 1185  CB  ASP A 143     5461   6664   5846   -416   -651   -496       C  
ATOM   1186  CG  ASP A 143     -23.082 -28.032  18.055  1.00 47.50           C  
ANISOU 1186  CG  ASP A 143     5402   6784   5860   -345   -703   -537       C  
ATOM   1187  OD1 ASP A 143     -24.219 -28.000  18.576  1.00 46.35           O  
ANISOU 1187  OD1 ASP A 143     5137   6722   5751   -372   -689   -552       O  
ATOM   1188  OD2 ASP A 143     -22.745 -27.325  17.082  1.00 47.26           O  
ANISOU 1188  OD2 ASP A 143     5426   6748   5783   -258   -755   -553       O  
ATOM   1189  N   ASP A 144     -20.252 -30.041  21.105  1.00 45.01           N  
ANISOU 1189  N   ASP A 144     5296   6244   5561   -509   -492   -370       N  
ATOM   1190  CA  ASP A 144     -19.163 -30.967  21.390  1.00 43.96           C  
ANISOU 1190  CA  ASP A 144     5256   6018   5427   -545   -467   -333       C  
ATOM   1191  C   ASP A 144     -18.744 -31.681  20.091  1.00 44.20           C  
ANISOU 1191  C   ASP A 144     5346   5989   5460   -548   -526   -369       C  
ATOM   1192  O   ASP A 144     -18.779 -32.908  20.002  1.00 44.90           O  
ANISOU 1192  O   ASP A 144     5459   6019   5581   -621   -528   -374       O  
ATOM   1193  CB  ASP A 144     -19.579 -31.941  22.506  1.00 44.96           C  
ANISOU 1193  CB  ASP A 144     5360   6131   5592   -640   -408   -299       C  
ATOM   1194  CG  ASP A 144     -18.457 -32.871  22.935  1.00 45.53           C  
ANISOU 1194  CG  ASP A 144     5535   6107   5658   -663   -380   -253       C  
ATOM   1195  OD1 ASP A 144     -17.283 -32.437  22.954  1.00 44.51           O  
ANISOU 1195  OD1 ASP A 144     5475   5949   5486   -595   -380   -229       O  
ATOM   1196  OD2 ASP A 144     -18.760 -34.041  23.270  1.00 43.85           O  
ANISOU 1196  OD2 ASP A 144     5332   5847   5482   -751   -357   -238       O  
ATOM   1197  N   ARG A 145     -18.397 -30.888  19.073  1.00 42.52           N  
ANISOU 1197  N   ARG A 145     5158   5789   5207   -468   -573   -394       N  
ATOM   1198  CA  ARG A 145     -17.922 -31.405  17.782  1.00 43.83           C  
ANISOU 1198  CA  ARG A 145     5388   5907   5358   -451   -626   -429       C  
ATOM   1199  C   ARG A 145     -16.806 -30.533  17.198  1.00 43.02           C  
ANISOU 1199  C   ARG A 145     5356   5792   5197   -358   -631   -414       C  
ATOM   1200  O   ARG A 145     -16.783 -29.316  17.386  1.00 42.76           O  
ANISOU 1200  O   ARG A 145     5307   5803   5136   -301   -622   -399       O  
ATOM   1201  CB  ARG A 145     -19.058 -31.500  16.747  1.00 45.02           C  
ANISOU 1201  CB  ARG A 145     5481   6103   5522   -465   -697   -497       C  
ATOM   1202  CG  ARG A 145     -20.230 -32.425  17.101  1.00 49.28           C  
ANISOU 1202  CG  ARG A 145     5940   6659   6126   -572   -702   -523       C  
ATOM   1203  CD  ARG A 145     -19.896 -33.916  16.978  1.00 51.61           C  
ANISOU 1203  CD  ARG A 145     6301   6857   6451   -655   -702   -531       C  
ATOM   1204  NE  ARG A 145     -21.064 -34.757  17.259  1.00 55.90           N  
ANISOU 1204  NE  ARG A 145     6767   7413   7059   -772   -708   -557       N  
ATOM   1205  CZ  ARG A 145     -21.440 -35.154  18.476  1.00 56.27           C  
ANISOU 1205  CZ  ARG A 145     6772   7460   7148   -850   -641   -513       C  
ATOM   1206  NH1 ARG A 145     -20.749 -34.799  19.554  1.00 51.18           N  
ANISOU 1206  NH1 ARG A 145     6159   6803   6483   -817   -569   -445       N  
ATOM   1207  NH2 ARG A 145     -22.519 -35.909  18.616  1.00 57.88           N  
ANISOU 1207  NH2 ARG A 145     6902   7678   7413   -965   -647   -539       N  
ATOM   1208  N   PHE A 146     -15.896 -31.172  16.471  1.00 41.48           N  
ANISOU 1208  N   PHE A 146     5241   5537   4984   -344   -643   -419       N  
ATOM   1209  CA  PHE A 146     -14.839 -30.482  15.749  1.00 39.77           C  
ANISOU 1209  CA  PHE A 146     5088   5311   4712   -265   -645   -407       C  
ATOM   1210  C   PHE A 146     -15.292 -30.309  14.304  1.00 40.64           C  
ANISOU 1210  C   PHE A 146     5210   5441   4789   -226   -709   -460       C  
ATOM   1211  O   PHE A 146     -15.456 -31.292  13.578  1.00 41.22           O  
ANISOU 1211  O   PHE A 146     5311   5482   4868   -250   -745   -502       O  
ATOM   1212  CB  PHE A 146     -13.530 -31.289  15.797  1.00 37.32           C  
ANISOU 1212  CB  PHE A 146     4853   4934   4394   -260   -614   -379       C  
ATOM   1213  CG  PHE A 146     -12.985 -31.488  17.183  1.00 32.92           C  
ANISOU 1213  CG  PHE A 146     4292   4358   3857   -287   -558   -325       C  
ATOM   1214  CD1 PHE A 146     -13.549 -32.426  18.043  1.00 35.12           C  
ANISOU 1214  CD1 PHE A 146     4550   4611   4181   -359   -541   -317       C  
ATOM   1215  CD2 PHE A 146     -11.913 -30.729  17.635  1.00 34.62           C  
ANISOU 1215  CD2 PHE A 146     4526   4584   4046   -245   -524   -280       C  
ATOM   1216  CE1 PHE A 146     -13.055 -32.610  19.332  1.00 35.36           C  
ANISOU 1216  CE1 PHE A 146     4586   4628   4221   -377   -491   -262       C  
ATOM   1217  CE2 PHE A 146     -11.407 -30.899  18.924  1.00 32.80           C  
ANISOU 1217  CE2 PHE A 146     4293   4344   3827   -266   -482   -232       C  
ATOM   1218  CZ  PHE A 146     -11.975 -31.842  19.771  1.00 35.67           C  
ANISOU 1218  CZ  PHE A 146     4643   4683   4227   -326   -466   -222       C  
ATOM   1219  N   TYR A 147     -15.518 -29.064  13.895  1.00 39.86           N  
ANISOU 1219  N   TYR A 147     5098   5391   4653   -164   -727   -460       N  
ATOM   1220  CA  TYR A 147     -15.852 -28.786  12.504  1.00 42.08           C  
ANISOU 1220  CA  TYR A 147     5404   5694   4889   -111   -789   -502       C  
ATOM   1221  C   TYR A 147     -14.578 -28.468  11.742  1.00 41.60           C  
ANISOU 1221  C   TYR A 147     5435   5602   4769    -51   -769   -478       C  
ATOM   1222  O   TYR A 147     -13.876 -27.494  12.056  1.00 41.22           O  
ANISOU 1222  O   TYR A 147     5407   5556   4698    -15   -728   -431       O  
ATOM   1223  CB  TYR A 147     -16.877 -27.656  12.378  1.00 42.44           C  
ANISOU 1223  CB  TYR A 147     5392   5811   4922    -67   -824   -515       C  
ATOM   1224  CG  TYR A 147     -18.196 -27.956  13.054  1.00 41.57           C  
ANISOU 1224  CG  TYR A 147     5175   5750   4871   -123   -842   -542       C  
ATOM   1225  CD1 TYR A 147     -18.360 -27.743  14.419  1.00 40.76           C  
ANISOU 1225  CD1 TYR A 147     5020   5660   4808   -157   -785   -507       C  
ATOM   1226  CD2 TYR A 147     -19.280 -28.442  12.328  1.00 43.58           C  
ANISOU 1226  CD2 TYR A 147     5377   6044   5137   -143   -914   -604       C  
ATOM   1227  CE1 TYR A 147     -19.572 -28.011  15.058  1.00 43.44           C  
ANISOU 1227  CE1 TYR A 147     5254   6053   5199   -209   -789   -528       C  
ATOM   1228  CE2 TYR A 147     -20.507 -28.713  12.956  1.00 46.89           C  
ANISOU 1228  CE2 TYR A 147     5681   6520   5614   -202   -925   -628       C  
ATOM   1229  CZ  TYR A 147     -20.639 -28.489  14.325  1.00 46.23           C  
ANISOU 1229  CZ  TYR A 147     5544   6450   5570   -234   -857   -587       C  
ATOM   1230  OH  TYR A 147     -21.829 -28.741  14.967  1.00 48.87           O  
ANISOU 1230  OH  TYR A 147     5762   6848   5960   -292   -855   -606       O  
ATOM   1231  N   VAL A 148     -14.287 -29.311  10.751  1.00 38.93           N  
ANISOU 1231  N   VAL A 148     5153   5235   4406    -43   -796   -513       N  
ATOM   1232  CA  VAL A 148     -13.026 -29.267  10.041  1.00 38.48           C  
ANISOU 1232  CA  VAL A 148     5179   5149   4294      9   -766   -492       C  
ATOM   1233  C   VAL A 148     -13.254 -28.778   8.617  1.00 39.98           C  
ANISOU 1233  C   VAL A 148     5415   5365   4409     77   -814   -523       C  
ATOM   1234  O   VAL A 148     -13.921 -29.434   7.799  1.00 40.90           O  
ANISOU 1234  O   VAL A 148     5543   5485   4511     75   -877   -584       O  
ATOM   1235  CB  VAL A 148     -12.322 -30.645  10.052  1.00 39.19           C  
ANISOU 1235  CB  VAL A 148     5312   5177   4400    -17   -746   -504       C  
ATOM   1236  CG1 VAL A 148     -10.995 -30.599   9.292  1.00 38.09           C  
ANISOU 1236  CG1 VAL A 148     5249   5021   4202     47   -708   -484       C  
ATOM   1237  CG2 VAL A 148     -12.089 -31.106  11.480  1.00 40.46           C  
ANISOU 1237  CG2 VAL A 148     5435   5311   4625    -76   -699   -467       C  
ATOM   1238  N   PHE A 149     -12.693 -27.612   8.330  1.00 39.78           N  
ANISOU 1238  N   PHE A 149     5422   5356   4335    133   -786   -479       N  
ATOM   1239  CA  PHE A 149     -12.829 -27.006   7.016  1.00 40.59           C  
ANISOU 1239  CA  PHE A 149     5582   5484   4358    206   -822   -492       C  
ATOM   1240  C   PHE A 149     -11.521 -27.192   6.265  1.00 40.72           C  
ANISOU 1240  C   PHE A 149     5681   5475   4317    243   -773   -470       C  
ATOM   1241  O   PHE A 149     -10.506 -26.591   6.625  1.00 42.31           O  
ANISOU 1241  O   PHE A 149     5895   5666   4513    248   -705   -410       O  
ATOM   1242  CB  PHE A 149     -13.189 -25.526   7.149  1.00 39.13           C  
ANISOU 1242  CB  PHE A 149     5386   5329   4152    246   -823   -455       C  
ATOM   1243  CG  PHE A 149     -14.490 -25.268   7.880  1.00 36.14           C  
ANISOU 1243  CG  PHE A 149     4920   4986   3825    225   -866   -478       C  
ATOM   1244  CD1 PHE A 149     -14.536 -25.259   9.274  1.00 33.97           C  
ANISOU 1244  CD1 PHE A 149     4581   4706   3621    169   -825   -455       C  
ATOM   1245  CD2 PHE A 149     -15.660 -24.996   7.173  1.00 34.88           C  
ANISOU 1245  CD2 PHE A 149     4739   4875   3638    268   -946   -521       C  
ATOM   1246  CE1 PHE A 149     -15.730 -24.999   9.953  1.00 32.22           C  
ANISOU 1246  CE1 PHE A 149     4275   4526   3443    155   -854   -474       C  
ATOM   1247  CE2 PHE A 149     -16.860 -24.736   7.842  1.00 34.73           C  
ANISOU 1247  CE2 PHE A 149     4625   4902   3667    255   -981   -542       C  
ATOM   1248  CZ  PHE A 149     -16.893 -24.737   9.236  1.00 33.10           C  
ANISOU 1248  CZ  PHE A 149     4354   4690   3532    198   -930   -517       C  
ATOM   1249  N   ASP A 150     -11.549 -28.042   5.241  1.00 39.55           N  
ANISOU 1249  N   ASP A 150     5584   5318   4124    267   -808   -521       N  
ATOM   1250  CA  ASP A 150     -10.342 -28.419   4.505  1.00 41.91           C  
ANISOU 1250  CA  ASP A 150     5960   5598   4367    309   -758   -509       C  
ATOM   1251  C   ASP A 150     -10.322 -27.914   3.052  1.00 42.57           C  
ANISOU 1251  C   ASP A 150     6125   5708   4343    388   -779   -519       C  
ATOM   1252  O   ASP A 150     -11.196 -28.263   2.256  1.00 42.41           O  
ANISOU 1252  O   ASP A 150     6128   5702   4284    409   -858   -582       O  
ATOM   1253  CB  ASP A 150     -10.194 -29.947   4.530  1.00 43.37           C  
ANISOU 1253  CB  ASP A 150     6160   5738   4580    281   -767   -561       C  
ATOM   1254  CG  ASP A 150      -8.869 -30.432   3.951  1.00 42.71           C  
ANISOU 1254  CG  ASP A 150     6145   5635   4447    331   -704   -548       C  
ATOM   1255  OD1 ASP A 150      -8.040 -29.601   3.508  1.00 42.85           O  
ANISOU 1255  OD1 ASP A 150     6192   5680   4410    378   -649   -498       O  
ATOM   1256  OD2 ASP A 150      -8.656 -31.661   3.958  1.00 38.37           O  
ANISOU 1256  OD2 ASP A 150     5621   5040   3916    321   -707   -588       O  
ATOM   1257  N   LEU A 151      -9.313 -27.117   2.705  1.00 42.28           N  
ANISOU 1257  N   LEU A 151     6131   5679   4253    428   -709   -457       N  
ATOM   1258  CA  LEU A 151      -9.180 -26.642   1.328  1.00 42.13           C  
ANISOU 1258  CA  LEU A 151     6202   5684   4122    505   -714   -455       C  
ATOM   1259  C   LEU A 151      -8.431 -27.638   0.445  1.00 44.87           C  
ANISOU 1259  C   LEU A 151     6617   6022   4410    545   -689   -488       C  
ATOM   1260  O   LEU A 151      -7.256 -27.918   0.669  1.00 45.20           O  
ANISOU 1260  O   LEU A 151     6660   6053   4462    543   -606   -454       O  
ATOM   1261  CB  LEU A 151      -8.500 -25.274   1.256  1.00 40.21           C  
ANISOU 1261  CB  LEU A 151     5984   5451   3842    527   -647   -370       C  
ATOM   1262  CG  LEU A 151      -8.526 -24.627  -0.144  1.00 39.53           C  
ANISOU 1262  CG  LEU A 151     5999   5388   3634    608   -654   -357       C  
ATOM   1263  CD1 LEU A 151      -9.959 -24.534  -0.677  1.00 34.60           C  
ANISOU 1263  CD1 LEU A 151     5385   4786   2975    646   -769   -413       C  
ATOM   1264  CD2 LEU A 151      -7.851 -23.252  -0.174  1.00 34.75           C  
ANISOU 1264  CD2 LEU A 151     5427   4780   2997    616   -581   -265       C  
ATOM   1265  N   LEU A 152      -9.117 -28.142  -0.578  1.00 46.79           N  
ANISOU 1265  N   LEU A 152     6918   6275   4587    586   -763   -558       N  
ATOM   1266  CA  LEU A 152      -8.527 -29.105  -1.502  1.00 47.15           C  
ANISOU 1266  CA  LEU A 152     7042   6308   4563    634   -748   -603       C  
ATOM   1267  C   LEU A 152      -7.710 -28.455  -2.616  1.00 47.35           C  
ANISOU 1267  C   LEU A 152     7156   6366   4469    716   -686   -559       C  
ATOM   1268  O   LEU A 152      -6.724 -29.030  -3.060  1.00 49.47           O  
ANISOU 1268  O   LEU A 152     7470   6630   4695    753   -619   -561       O  
ATOM   1269  CB  LEU A 152      -9.592 -30.049  -2.076  1.00 48.00           C  
ANISOU 1269  CB  LEU A 152     7178   6407   4654    634   -859   -707       C  
ATOM   1270  CG  LEU A 152     -10.321 -30.939  -1.057  1.00 48.16           C  
ANISOU 1270  CG  LEU A 152     7120   6388   4791    544   -910   -755       C  
ATOM   1271  CD1 LEU A 152     -11.267 -31.905  -1.742  1.00 51.96           C  
ANISOU 1271  CD1 LEU A 152     7637   6856   5249    536  -1016   -862       C  
ATOM   1272  CD2 LEU A 152      -9.346 -31.708  -0.177  1.00 50.36           C  
ANISOU 1272  CD2 LEU A 152     7378   6616   5141    510   -831   -731       C  
ATOM   1273  N   ASN A 153      -8.098 -27.261  -3.055  1.00 46.43           N  
ANISOU 1273  N   ASN A 153     7065   6281   4296    747   -701   -517       N  
ATOM   1274  CA  ASN A 153      -7.404 -26.617  -4.177  1.00 48.73           C  
ANISOU 1274  CA  ASN A 153     7452   6601   4463    822   -641   -471       C  
ATOM   1275  C   ASN A 153      -6.926 -25.211  -3.863  1.00 48.40           C  
ANISOU 1275  C   ASN A 153     7401   6565   4424    809   -569   -366       C  
ATOM   1276  O   ASN A 153      -7.692 -24.367  -3.393  1.00 48.19           O  
ANISOU 1276  O   ASN A 153     7343   6534   4433    789   -615   -345       O  
ATOM   1277  CB  ASN A 153      -8.265 -26.604  -5.447  1.00 48.60           C  
ANISOU 1277  CB  ASN A 153     7526   6611   4328    897   -731   -525       C  
ATOM   1278  CG  ASN A 153      -8.744 -27.984  -5.846  1.00 48.28           C  
ANISOU 1278  CG  ASN A 153     7507   6559   4277    904   -809   -636       C  
ATOM   1279  OD1 ASN A 153      -7.962 -28.929  -5.936  1.00 53.87           O  
ANISOU 1279  OD1 ASN A 153     8239   7246   4985    910   -758   -664       O  
ATOM   1280  ND2 ASN A 153     -10.036 -28.107  -6.084  1.00 48.11           N  
ANISOU 1280  ND2 ASN A 153     7478   6551   4250    904   -936   -704       N  
ATOM   1281  N   SER A 154      -5.655 -24.968  -4.153  1.00 47.74           N  
ANISOU 1281  N   SER A 154     7347   6492   4301    822   -455   -304       N  
ATOM   1282  CA  SER A 154      -5.009 -23.721  -3.793  1.00 49.05           C  
ANISOU 1282  CA  SER A 154     7501   6656   4480    790   -373   -205       C  
ATOM   1283  C   SER A 154      -3.884 -23.437  -4.780  1.00 50.65           C  
ANISOU 1283  C   SER A 154     7778   6888   4580    835   -266   -148       C  
ATOM   1284  O   SER A 154      -3.396 -24.368  -5.430  1.00 50.67           O  
ANISOU 1284  O   SER A 154     7813   6913   4528    883   -238   -188       O  
ATOM   1285  CB  SER A 154      -4.467 -23.817  -2.366  1.00 46.55           C  
ANISOU 1285  CB  SER A 154     7072   6320   4296    703   -331   -181       C  
ATOM   1286  OG  SER A 154      -3.216 -23.171  -2.262  1.00 49.07           O  
ANISOU 1286  OG  SER A 154     7381   6650   4613    676   -217    -98       O  
ATOM   1287  N   PRO A 155      -3.474 -22.155  -4.906  1.00 50.75           N  
ANISOU 1287  N   PRO A 155     7823   6898   4563    821   -201    -56       N  
ATOM   1288  CA  PRO A 155      -2.328 -21.824  -5.744  1.00 52.04           C  
ANISOU 1288  CA  PRO A 155     8044   7091   4637    846    -82      9       C  
ATOM   1289  C   PRO A 155      -1.118 -22.689  -5.411  1.00 52.14           C  
ANISOU 1289  C   PRO A 155     7981   7133   4695    823      7      5       C  
ATOM   1290  O   PRO A 155      -0.383 -23.099  -6.315  1.00 54.04           O  
ANISOU 1290  O   PRO A 155     8270   7416   4848    880     80      8       O  
ATOM   1291  CB  PRO A 155      -2.054 -20.360  -5.383  1.00 51.79           C  
ANISOU 1291  CB  PRO A 155     8019   7033   4626    788    -28    109       C  
ATOM   1292  CG  PRO A 155      -3.380 -19.823  -5.050  1.00 51.80           C  
ANISOU 1292  CG  PRO A 155     8036   6995   4650    795   -142     87       C  
ATOM   1293  CD  PRO A 155      -4.099 -20.941  -4.345  1.00 50.98           C  
ANISOU 1293  CD  PRO A 155     7848   6892   4630    785   -235    -10       C  
ATOM   1294  N   TYR A 156      -0.942 -22.976  -4.122  1.00 51.57           N  
ANISOU 1294  N   TYR A 156     7796   7044   4754    750     -1     -5       N  
ATOM   1295  CA  TYR A 156       0.195 -23.750  -3.629  1.00 52.82           C  
ANISOU 1295  CA  TYR A 156     7870   7230   4969    730     74     -5       C  
ATOM   1296  C   TYR A 156       0.000 -25.268  -3.692  1.00 52.18           C  
ANISOU 1296  C   TYR A 156     7783   7147   4895    781     27    -99       C  
ATOM   1297  O   TYR A 156       0.885 -26.026  -3.284  1.00 52.63           O  
ANISOU 1297  O   TYR A 156     7777   7223   4997    782     80   -106       O  
ATOM   1298  CB  TYR A 156       0.591 -23.291  -2.213  1.00 52.47           C  
ANISOU 1298  CB  TYR A 156     7713   7171   5053    630     91     36       C  
ATOM   1299  CG  TYR A 156       0.812 -21.792  -2.127  1.00 57.41           C  
ANISOU 1299  CG  TYR A 156     8353   7785   5674    571    137    123       C  
ATOM   1300  CD1 TYR A 156       1.504 -21.117  -3.133  1.00 59.89           C  
ANISOU 1300  CD1 TYR A 156     8732   8127   5894    589    230    190       C  
ATOM   1301  CD2 TYR A 156       0.323 -21.046  -1.052  1.00 56.59           C  
ANISOU 1301  CD2 TYR A 156     8208   7638   5657    497     91    140       C  
ATOM   1302  CE1 TYR A 156       1.698 -19.749  -3.081  1.00 61.48           C  
ANISOU 1302  CE1 TYR A 156     8962   8305   6092    529    274    272       C  
ATOM   1303  CE2 TYR A 156       0.521 -19.665  -0.989  1.00 56.71           C  
ANISOU 1303  CE2 TYR A 156     8253   7628   5667    444    131    216       C  
ATOM   1304  CZ  TYR A 156       1.211 -19.030  -2.011  1.00 59.60           C  
ANISOU 1304  CZ  TYR A 156     8689   8014   5943    457    222    283       C  
ATOM   1305  OH  TYR A 156       1.426 -17.675  -1.986  1.00 62.15           O  
ANISOU 1305  OH  TYR A 156     9055   8301   6260    398    265    361       O  
ATOM   1306  N   GLY A 157      -1.140 -25.715  -4.209  1.00 50.70           N  
ANISOU 1306  N   GLY A 157     7664   6935   4663    826    -75   -171       N  
ATOM   1307  CA  GLY A 157      -1.332 -27.141  -4.429  1.00 52.51           C  
ANISOU 1307  CA  GLY A 157     7912   7153   4887    873   -120   -263       C  
ATOM   1308  C   GLY A 157      -2.743 -27.677  -4.328  1.00 53.13           C  
ANISOU 1308  C   GLY A 157     8009   7189   4987    867   -255   -348       C  
ATOM   1309  O   GLY A 157      -3.556 -27.194  -3.528  1.00 52.56           O  
ANISOU 1309  O   GLY A 157     7885   7095   4990    806   -318   -342       O  
ATOM   1310  N   ASN A 158      -3.016 -28.684  -5.156  1.00 52.60           N  
ANISOU 1310  N   ASN A 158     8017   7116   4852    931   -298   -431       N  
ATOM   1311  CA  ASN A 158      -4.266 -29.429  -5.137  1.00 53.56           C  
ANISOU 1311  CA  ASN A 158     8155   7200   4995    920   -426   -525       C  
ATOM   1312  C   ASN A 158      -4.023 -30.778  -4.471  1.00 54.31           C  
ANISOU 1312  C   ASN A 158     8215   7249   5171    898   -431   -582       C  
ATOM   1313  O   ASN A 158      -3.108 -31.517  -4.853  1.00 56.82           O  
ANISOU 1313  O   ASN A 158     8570   7567   5452    955   -366   -598       O  
ATOM   1314  CB  ASN A 158      -4.800 -29.629  -6.560  1.00 56.59           C  
ANISOU 1314  CB  ASN A 158     8659   7602   5241   1002   -484   -587       C  
ATOM   1315  CG  ASN A 158      -4.838 -28.334  -7.364  1.00 59.89           C  
ANISOU 1315  CG  ASN A 158     9136   8066   5555   1044   -461   -520       C  
ATOM   1316  OD1 ASN A 158      -5.280 -27.290  -6.880  1.00 59.47           O  
ANISOU 1316  OD1 ASN A 158     9040   8015   5542   1002   -478   -463       O  
ATOM   1317  ND2 ASN A 158      -4.372 -28.402  -8.603  1.00 64.34           N  
ANISOU 1317  ND2 ASN A 158     9806   8662   5979   1132   -419   -525       N  
ATOM   1318  N   VAL A 159      -4.834 -31.097  -3.471  1.00 52.01           N  
ANISOU 1318  N   VAL A 159     7857   6917   4989    822   -504   -610       N  
ATOM   1319  CA  VAL A 159      -4.590 -32.274  -2.648  1.00 51.72           C  
ANISOU 1319  CA  VAL A 159     7783   6826   5040    790   -502   -645       C  
ATOM   1320  C   VAL A 159      -5.807 -33.192  -2.574  1.00 52.53           C  
ANISOU 1320  C   VAL A 159     7904   6876   5180    749   -618   -740       C  
ATOM   1321  O   VAL A 159      -6.903 -32.829  -3.010  1.00 52.49           O  
ANISOU 1321  O   VAL A 159     7912   6886   5146    736   -706   -776       O  
ATOM   1322  CB  VAL A 159      -4.136 -31.882  -1.225  1.00 50.74           C  
ANISOU 1322  CB  VAL A 159     7549   6700   5032    720   -452   -572       C  
ATOM   1323  CG1 VAL A 159      -2.713 -31.350  -1.245  1.00 52.10           C  
ANISOU 1323  CG1 VAL A 159     7698   6918   5180    754   -333   -493       C  
ATOM   1324  CG2 VAL A 159      -5.087 -30.852  -0.617  1.00 52.62           C  
ANISOU 1324  CG2 VAL A 159     7725   6949   5317    652   -504   -541       C  
ATOM   1325  N   GLU A 160      -5.603 -34.385  -2.029  1.00 52.19           N  
ANISOU 1325  N   GLU A 160     7860   6769   5199    729   -618   -780       N  
ATOM   1326  CA  GLU A 160      -6.688 -35.328  -1.876  1.00 54.98           C  
ANISOU 1326  CA  GLU A 160     8229   7062   5598    674   -718   -866       C  
ATOM   1327  C   GLU A 160      -7.390 -35.092  -0.553  1.00 56.13           C  
ANISOU 1327  C   GLU A 160     8267   7195   5866    569   -748   -835       C  
ATOM   1328  O   GLU A 160      -6.911 -34.331   0.292  1.00 55.57           O  
ANISOU 1328  O   GLU A 160     8120   7152   5843    548   -687   -752       O  
ATOM   1329  CB  GLU A 160      -6.196 -36.777  -1.997  1.00 56.25           C  
ANISOU 1329  CB  GLU A 160     8465   7146   5761    704   -707   -927       C  
ATOM   1330  CG  GLU A 160      -5.832 -37.203  -3.429  1.00 61.39           C  
ANISOU 1330  CG  GLU A 160     9241   7801   6282    807   -705   -991       C  
ATOM   1331  CD  GLU A 160      -6.849 -36.741  -4.490  1.00 65.90           C  
ANISOU 1331  CD  GLU A 160     9860   8412   6765    816   -798  -1046       C  
ATOM   1332  OE1 GLU A 160      -8.069 -36.973  -4.326  1.00 67.31           O  
ANISOU 1332  OE1 GLU A 160    10018   8567   6988    739   -905  -1103       O  
ATOM   1333  OE2 GLU A 160      -6.419 -36.144  -5.499  1.00 67.88           O  
ANISOU 1333  OE2 GLU A 160    10168   8722   6899    901   -763  -1030       O  
ATOM   1334  N   GLU A 161      -8.543 -35.732  -0.391  1.00 57.23           N  
ANISOU 1334  N   GLU A 161     8400   7294   6051    501   -841   -904       N  
ATOM   1335  CA  GLU A 161      -9.316 -35.615   0.829  1.00 57.19           C  
ANISOU 1335  CA  GLU A 161     8294   7278   6156    400   -868   -882       C  
ATOM   1336  C   GLU A 161      -8.578 -36.243   1.996  1.00 54.66           C  
ANISOU 1336  C   GLU A 161     7945   6903   5920    369   -801   -838       C  
ATOM   1337  O   GLU A 161      -7.698 -37.084   1.806  1.00 54.83           O  
ANISOU 1337  O   GLU A 161     8033   6876   5922    418   -759   -851       O  
ATOM   1338  CB  GLU A 161     -10.693 -36.255   0.655  1.00 59.75           C  
ANISOU 1338  CB  GLU A 161     8615   7577   6509    329   -979   -970       C  
ATOM   1339  CG  GLU A 161     -11.686 -35.354  -0.046  1.00 63.67           C  
ANISOU 1339  CG  GLU A 161     9087   8150   6955    339  -1057   -993       C  
ATOM   1340  CD  GLU A 161     -13.099 -35.887   0.004  1.00 68.49           C  
ANISOU 1340  CD  GLU A 161     9655   8752   7614    253  -1166  -1072       C  
ATOM   1341  OE1 GLU A 161     -13.466 -36.546   1.006  1.00 67.97           O  
ANISOU 1341  OE1 GLU A 161     9536   8639   7652    158  -1166  -1074       O  
ATOM   1342  OE2 GLU A 161     -13.845 -35.634  -0.965  1.00 72.20           O  
ANISOU 1342  OE2 GLU A 161    10145   9270   8018    279  -1252  -1129       O  
ATOM   1343  N   TRP A 162      -8.944 -35.812   3.198  1.00 51.72           N  
ANISOU 1343  N   TRP A 162     7477   6541   5633    296   -793   -788       N  
ATOM   1344  CA  TRP A 162      -8.366 -36.326   4.430  1.00 49.41           C  
ANISOU 1344  CA  TRP A 162     7151   6203   5418    262   -738   -741       C  
ATOM   1345  C   TRP A 162      -9.126 -37.570   4.860  1.00 51.48           C  
ANISOU 1345  C   TRP A 162     7432   6382   5746    186   -788   -795       C  
ATOM   1346  O   TRP A 162     -10.364 -37.596   4.832  1.00 52.15           O  
ANISOU 1346  O   TRP A 162     7484   6471   5858    114   -859   -840       O  
ATOM   1347  CB  TRP A 162      -8.436 -35.243   5.495  1.00 45.94           C  
ANISOU 1347  CB  TRP A 162     6610   5815   5029    221   -708   -664       C  
ATOM   1348  CG  TRP A 162      -8.239 -35.669   6.920  1.00 44.48           C  
ANISOU 1348  CG  TRP A 162     6377   5593   4929    165   -674   -620       C  
ATOM   1349  CD1 TRP A 162      -7.054 -35.776   7.590  1.00 41.11           C  
ANISOU 1349  CD1 TRP A 162     5943   5160   4518    195   -604   -562       C  
ATOM   1350  CD2 TRP A 162      -9.265 -35.975   7.873  1.00 43.77           C  
ANISOU 1350  CD2 TRP A 162     6234   5479   4916     70   -708   -626       C  
ATOM   1351  NE1 TRP A 162      -7.277 -36.150   8.890  1.00 40.62           N  
ANISOU 1351  NE1 TRP A 162     5839   5066   4531    131   -597   -532       N  
ATOM   1352  CE2 TRP A 162      -8.627 -36.273   9.092  1.00 42.11           C  
ANISOU 1352  CE2 TRP A 162     6000   5242   4758     52   -654   -568       C  
ATOM   1353  CE3 TRP A 162     -10.664 -36.039   7.809  1.00 43.95           C  
ANISOU 1353  CE3 TRP A 162     6222   5508   4968      0   -777   -674       C  
ATOM   1354  CZ2 TRP A 162      -9.337 -36.634  10.240  1.00 42.46           C  
ANISOU 1354  CZ2 TRP A 162     5999   5259   4875    -34   -661   -553       C  
ATOM   1355  CZ3 TRP A 162     -11.368 -36.386   8.955  1.00 41.17           C  
ANISOU 1355  CZ3 TRP A 162     5812   5135   4696    -90   -779   -660       C  
ATOM   1356  CH2 TRP A 162     -10.702 -36.681  10.151  1.00 41.82           C  
ANISOU 1356  CH2 TRP A 162     5883   5184   4822   -107   -719   -598       C  
ATOM   1357  N   SER A 163      -8.379 -38.599   5.249  1.00 51.50           N  
ANISOU 1357  N   SER A 163     7486   6309   5772    201   -749   -791       N  
ATOM   1358  CA  SER A 163      -8.974 -39.858   5.665  1.00 52.81           C  
ANISOU 1358  CA  SER A 163     7691   6377   5999    129   -785   -836       C  
ATOM   1359  C   SER A 163      -9.017 -39.961   7.186  1.00 52.33           C  
ANISOU 1359  C   SER A 163     7563   6293   6026     59   -750   -768       C  
ATOM   1360  O   SER A 163      -7.976 -39.980   7.845  1.00 53.00           O  
ANISOU 1360  O   SER A 163     7644   6373   6120    106   -684   -705       O  
ATOM   1361  CB  SER A 163      -8.218 -41.044   5.058  1.00 53.71           C  
ANISOU 1361  CB  SER A 163     7929   6403   6076    198   -772   -882       C  
ATOM   1362  OG  SER A 163      -8.695 -42.275   5.579  1.00 56.42           O  
ANISOU 1362  OG  SER A 163     8322   6633   6484    124   -799   -915       O  
ATOM   1363  N   ILE A 164     -10.230 -40.026   7.724  1.00 50.47           N  
ANISOU 1363  N   ILE A 164     7273   6052   5852    -49   -795   -783       N  
ATOM   1364  CA  ILE A 164     -10.449 -40.222   9.147  1.00 51.76           C  
ANISOU 1364  CA  ILE A 164     7382   6191   6095   -125   -764   -725       C  
ATOM   1365  C   ILE A 164      -9.968 -41.608   9.601  1.00 52.43           C  
ANISOU 1365  C   ILE A 164     7556   6153   6210   -132   -740   -724       C  
ATOM   1366  O   ILE A 164      -9.668 -41.815  10.778  1.00 52.12           O  
ANISOU 1366  O   ILE A 164     7498   6089   6217   -155   -695   -658       O  
ATOM   1367  CB  ILE A 164     -11.943 -39.971   9.539  1.00 51.76           C  
ANISOU 1367  CB  ILE A 164     7295   6223   6149   -241   -813   -745       C  
ATOM   1368  CG1 ILE A 164     -12.103 -39.918  11.070  1.00 51.23           C  
ANISOU 1368  CG1 ILE A 164     7162   6154   6150   -307   -765   -672       C  
ATOM   1369  CG2 ILE A 164     -12.883 -40.989   8.864  1.00 51.40           C  
ANISOU 1369  CG2 ILE A 164     7300   6111   6121   -313   -885   -837       C  
ATOM   1370  CD1 ILE A 164     -13.342 -39.165  11.557  1.00 51.84           C  
ANISOU 1370  CD1 ILE A 164     7123   6309   6267   -386   -788   -669       C  
ATOM   1371  N   GLU A 165      -9.883 -42.536   8.652  1.00 52.77           N  
ANISOU 1371  N   GLU A 165     7706   6119   6223   -105   -772   -796       N  
ATOM   1372  CA  GLU A 165      -9.414 -43.894   8.911  1.00 53.94           C  
ANISOU 1372  CA  GLU A 165     7965   6137   6393    -96   -755   -804       C  
ATOM   1373  C   GLU A 165      -7.927 -43.880   9.212  1.00 52.81           C  
ANISOU 1373  C   GLU A 165     7848   5999   6221     25   -683   -742       C  
ATOM   1374  O   GLU A 165      -7.490 -44.386  10.239  1.00 55.60           O  
ANISOU 1374  O   GLU A 165     8213   6299   6613     24   -643   -684       O  
ATOM   1375  CB  GLU A 165      -9.695 -44.805   7.707  1.00 56.95           C  
ANISOU 1375  CB  GLU A 165     8462   6436   6739    -88   -813   -909       C  
ATOM   1376  CG  GLU A 165     -11.112 -45.387   7.642  1.00 62.20           C  
ANISOU 1376  CG  GLU A 165     9130   7046   7458   -232   -887   -976       C  
ATOM   1377  CD  GLU A 165     -12.181 -44.364   7.267  1.00 66.86           C  
ANISOU 1377  CD  GLU A 165     9604   7755   8044   -291   -943  -1003       C  
ATOM   1378  OE1 GLU A 165     -11.887 -43.422   6.486  1.00 67.02           O  
ANISOU 1378  OE1 GLU A 165     9598   7873   7994   -205   -949  -1010       O  
ATOM   1379  OE2 GLU A 165     -13.325 -44.512   7.756  1.00 67.83           O  
ANISOU 1379  OE2 GLU A 165     9663   7875   8234   -421   -978  -1015       O  
ATOM   1380  N   ILE A 166      -7.156 -43.288   8.309  1.00 51.80           N  
ANISOU 1380  N   ILE A 166     7723   5939   6019    132   -666   -752       N  
ATOM   1381  CA  ILE A 166      -5.719 -43.142   8.487  1.00 48.62           C  
ANISOU 1381  CA  ILE A 166     7322   5568   5585    249   -596   -695       C  
ATOM   1382  C   ILE A 166      -5.430 -42.243   9.685  1.00 47.78           C  
ANISOU 1382  C   ILE A 166     7100   5538   5515    224   -556   -602       C  
ATOM   1383  O   ILE A 166      -4.522 -42.516  10.463  1.00 48.60           O  
ANISOU 1383  O   ILE A 166     7201   5630   5633    273   -510   -544       O  
ATOM   1384  CB  ILE A 166      -5.052 -42.607   7.200  1.00 47.97           C  
ANISOU 1384  CB  ILE A 166     7257   5555   5413    354   -581   -726       C  
ATOM   1385  CG1 ILE A 166      -5.213 -43.634   6.063  1.00 48.96           C  
ANISOU 1385  CG1 ILE A 166     7516   5595   5493    393   -619   -823       C  
ATOM   1386  CG2 ILE A 166      -3.580 -42.307   7.439  1.00 46.18           C  
ANISOU 1386  CG2 ILE A 166     7001   5385   5162    462   -504   -660       C  
ATOM   1387  CD1 ILE A 166      -5.021 -43.076   4.661  1.00 48.60           C  
ANISOU 1387  CD1 ILE A 166     7495   5619   5351    468   -624   -870       C  
ATOM   1388  N   ALA A 167      -6.224 -41.189   9.848  1.00 46.52           N  
ANISOU 1388  N   ALA A 167     6850   5456   5369    153   -577   -590       N  
ATOM   1389  CA  ALA A 167      -6.087 -40.293  10.999  1.00 46.90           C  
ANISOU 1389  CA  ALA A 167     6796   5573   5450    121   -545   -511       C  
ATOM   1390  C   ALA A 167      -6.145 -41.051  12.329  1.00 46.86           C  
ANISOU 1390  C   ALA A 167     6798   5500   5505     73   -529   -466       C  
ATOM   1391  O   ALA A 167      -5.333 -40.808  13.223  1.00 46.11           O  
ANISOU 1391  O   ALA A 167     6667   5435   5418    105   -488   -398       O  
ATOM   1392  CB  ALA A 167      -7.154 -39.199  10.959  1.00 44.10           C  
ANISOU 1392  CB  ALA A 167     6360   5291   5103     49   -578   -519       C  
ATOM   1393  N   ALA A 168      -7.094 -41.982  12.429  1.00 47.76           N  
ANISOU 1393  N   ALA A 168     6963   5524   5659     -6   -564   -504       N  
ATOM   1394  CA  ALA A 168      -7.358 -42.726  13.657  1.00 48.03           C  
ANISOU 1394  CA  ALA A 168     7014   5487   5750    -70   -549   -460       C  
ATOM   1395  C   ALA A 168      -6.241 -43.691  14.054  1.00 48.59           C  
ANISOU 1395  C   ALA A 168     7169   5479   5814     13   -513   -425       C  
ATOM   1396  O   ALA A 168      -6.012 -43.903  15.244  1.00 49.59           O  
ANISOU 1396  O   ALA A 168     7286   5587   5968      0   -485   -357       O  
ATOM   1397  CB  ALA A 168      -8.675 -43.471  13.540  1.00 50.14           C  
ANISOU 1397  CB  ALA A 168     7314   5676   6061   -186   -593   -513       C  
ATOM   1398  N   LYS A 169      -5.566 -44.279  13.068  1.00 47.82           N  
ANISOU 1398  N   LYS A 169     7156   5337   5677    106   -516   -471       N  
ATOM   1399  CA  LYS A 169      -4.481 -45.236  13.325  1.00 49.16           C  
ANISOU 1399  CA  LYS A 169     7411   5432   5836    206   -484   -445       C  
ATOM   1400  C   LYS A 169      -3.306 -44.578  14.059  1.00 48.43           C  
ANISOU 1400  C   LYS A 169     7241   5434   5728    289   -438   -365       C  
ATOM   1401  O   LYS A 169      -3.023 -43.394  13.854  1.00 48.26           O  
ANISOU 1401  O   LYS A 169     7122   5533   5683    302   -427   -351       O  
ATOM   1402  CB  LYS A 169      -3.991 -45.867  12.015  1.00 49.19           C  
ANISOU 1402  CB  LYS A 169     7514   5387   5790    302   -492   -518       C  
ATOM   1403  CG  LYS A 169      -5.103 -46.445  11.139  1.00 54.94           C  
ANISOU 1403  CG  LYS A 169     8320   6032   6523    224   -549   -611       C  
ATOM   1404  CD  LYS A 169      -4.571 -47.203   9.928  1.00 55.36           C  
ANISOU 1404  CD  LYS A 169     8494   6021   6521    328   -557   -687       C  
ATOM   1405  CE  LYS A 169      -4.573 -48.698  10.191  1.00 61.48           C  
ANISOU 1405  CE  LYS A 169     9414   6622   7323    331   -564   -706       C  
ATOM   1406  NZ  LYS A 169      -3.947 -49.464   9.074  1.00 64.90           N  
ANISOU 1406  NZ  LYS A 169     9976   6988   7696    451   -565   -781       N  
ATOM   1407  N   LEU A 170      -2.624 -45.342  14.909  1.00 48.33           N  
ANISOU 1407  N   LEU A 170     7274   5363   5727    342   -415   -313       N  
ATOM   1408  CA  LEU A 170      -1.449 -44.836  15.624  1.00 51.09           C  
ANISOU 1408  CA  LEU A 170     7550   5802   6060    426   -380   -241       C  
ATOM   1409  C   LEU A 170      -0.299 -44.550  14.656  1.00 52.48           C  
ANISOU 1409  C   LEU A 170     7705   6049   6185    553   -356   -262       C  
ATOM   1410  O   LEU A 170      -0.269 -45.093  13.551  1.00 54.43           O  
ANISOU 1410  O   LEU A 170     8031   6247   6404    603   -360   -326       O  
ATOM   1411  CB  LEU A 170      -0.997 -45.831  16.703  1.00 51.36           C  
ANISOU 1411  CB  LEU A 170     7650   5752   6112    467   -368   -183       C  
ATOM   1412  CG  LEU A 170      -2.017 -46.335  17.740  1.00 55.35           C  
ANISOU 1412  CG  LEU A 170     8198   6169   6662    351   -379   -150       C  
ATOM   1413  CD1 LEU A 170      -1.384 -47.385  18.667  1.00 53.65           C  
ANISOU 1413  CD1 LEU A 170     8070   5865   6449    421   -365    -89       C  
ATOM   1414  CD2 LEU A 170      -2.643 -45.201  18.561  1.00 49.25           C  
ANISOU 1414  CD2 LEU A 170     7308   5497   5908    248   -379   -112       C  
ATOM   1415  N   GLN A 171       0.647 -43.705  15.065  1.00 52.18           N  
ANISOU 1415  N   GLN A 171     7563   6131   6133    602   -328   -209       N  
ATOM   1416  CA  GLN A 171       1.810 -43.415  14.219  1.00 51.87           C  
ANISOU 1416  CA  GLN A 171     7488   6173   6048    718   -294   -220       C  
ATOM   1417  C   GLN A 171       2.697 -44.643  13.953  1.00 51.62           C  
ANISOU 1417  C   GLN A 171     7545   6074   5996    857   -276   -230       C  
ATOM   1418  O   GLN A 171       3.257 -44.773  12.861  1.00 51.44           O  
ANISOU 1418  O   GLN A 171     7544   6071   5930    947   -251   -273       O  
ATOM   1419  CB  GLN A 171       2.612 -42.227  14.751  1.00 51.65           C  
ANISOU 1419  CB  GLN A 171     7321   6288   6017    722   -271   -162       C  
ATOM   1420  CG  GLN A 171       1.901 -40.902  14.503  1.00 54.64           C  
ANISOU 1420  CG  GLN A 171     7627   6739   6396    618   -280   -170       C  
ATOM   1421  CD  GLN A 171       2.796 -39.678  14.636  1.00 54.65           C  
ANISOU 1421  CD  GLN A 171     7506   6875   6383    628   -252   -129       C  
ATOM   1422  OE1 GLN A 171       4.019 -39.767  14.555  1.00 55.32           O  
ANISOU 1422  OE1 GLN A 171     7549   7019   6450    720   -219   -107       O  
ATOM   1423  NE2 GLN A 171       2.176 -38.520  14.831  1.00 53.97           N  
ANISOU 1423  NE2 GLN A 171     7361   6838   6307    531   -264   -120       N  
ATOM   1424  N   GLU A 172       2.789 -45.545  14.933  1.00 51.28           N  
ANISOU 1424  N   GLU A 172     7560   5946   5979    878   -285   -192       N  
ATOM   1425  CA  GLU A 172       3.433 -46.855  14.756  1.00 52.60           C  
ANISOU 1425  CA  GLU A 172     7840   6014   6130   1009   -275   -204       C  
ATOM   1426  C   GLU A 172       2.916 -47.566  13.514  1.00 52.43           C  
ANISOU 1426  C   GLU A 172     7943   5890   6088   1021   -284   -293       C  
ATOM   1427  O   GLU A 172       3.655 -48.294  12.860  1.00 54.25           O  
ANISOU 1427  O   GLU A 172     8245   6084   6284   1155   -263   -325       O  
ATOM   1428  CB  GLU A 172       3.135 -47.781  15.938  1.00 54.17           C  
ANISOU 1428  CB  GLU A 172     8122   6096   6364    989   -294   -156       C  
ATOM   1429  CG  GLU A 172       3.791 -47.460  17.261  1.00 56.70           C  
ANISOU 1429  CG  GLU A 172     8359   6491   6694   1014   -291    -67       C  
ATOM   1430  CD  GLU A 172       3.018 -48.067  18.430  1.00 60.04           C  
ANISOU 1430  CD  GLU A 172     8857   6804   7150    933   -312    -20       C  
ATOM   1431  OE1 GLU A 172       2.883 -47.404  19.485  1.00 62.72           O  
ANISOU 1431  OE1 GLU A 172     9116   7214   7502    867   -318     38       O  
ATOM   1432  OE2 GLU A 172       2.516 -49.200  18.286  1.00 59.98           O  
ANISOU 1432  OE2 GLU A 172     8996   6638   7155    928   -320    -43       O  
ATOM   1433  N   GLN A 173       1.633 -47.366  13.218  1.00 52.55           N  
ANISOU 1433  N   GLN A 173     7984   5860   6124    883   -319   -336       N  
ATOM   1434  CA  GLN A 173       0.941 -48.087  12.149  1.00 54.04           C  
ANISOU 1434  CA  GLN A 173     8298   5938   6297    867   -344   -427       C  
ATOM   1435  C   GLN A 173       0.885 -47.310  10.834  1.00 54.05           C  
ANISOU 1435  C   GLN A 173     8260   6028   6247    877   -341   -488       C  
ATOM   1436  O   GLN A 173       0.251 -47.747   9.866  1.00 52.06           O  
ANISOU 1436  O   GLN A 173     8102   5706   5974    857   -371   -571       O  
ATOM   1437  CB  GLN A 173      -0.472 -48.453  12.605  1.00 54.96           C  
ANISOU 1437  CB  GLN A 173     8467   5948   6467    708   -390   -442       C  
ATOM   1438  CG  GLN A 173      -0.508 -49.434  13.767  1.00 57.54           C  
ANISOU 1438  CG  GLN A 173     8872   6154   6835    696   -389   -387       C  
ATOM   1439  CD  GLN A 173      -1.798 -49.360  14.568  1.00 60.86           C  
ANISOU 1439  CD  GLN A 173     9279   6532   7314    521   -415   -366       C  
ATOM   1440  OE1 GLN A 173      -1.802 -49.599  15.773  1.00 61.43           O  
ANISOU 1440  OE1 GLN A 173     9352   6574   7416    493   -403   -292       O  
ATOM   1441  NE2 GLN A 173      -2.897 -49.021  13.903  1.00 62.02           N  
ANISOU 1441  NE2 GLN A 173     9409   6683   7473    406   -450   -430       N  
ATOM   1442  N   GLY A 174       1.564 -46.165  10.802  1.00 54.10           N  
ANISOU 1442  N   GLY A 174     8135   6189   6232    907   -307   -447       N  
ATOM   1443  CA  GLY A 174       1.549 -45.290   9.634  1.00 52.49           C  
ANISOU 1443  CA  GLY A 174     7889   6079   5976    912   -297   -488       C  
ATOM   1444  C   GLY A 174       0.347 -44.363   9.640  1.00 50.84           C  
ANISOU 1444  C   GLY A 174     7624   5904   5787    766   -337   -497       C  
ATOM   1445  O   GLY A 174       0.029 -43.739   8.623  1.00 51.08           O  
ANISOU 1445  O   GLY A 174     7647   5987   5775    755   -345   -539       O  
ATOM   1446  N   GLY A 175      -0.331 -44.287  10.782  1.00 47.86           N  
ANISOU 1446  N   GLY A 175     7213   5501   5473    662   -362   -455       N  
ATOM   1447  CA  GLY A 175      -1.442 -43.365  10.949  1.00 48.76           C  
ANISOU 1447  CA  GLY A 175     7258   5657   5611    532   -396   -456       C  
ATOM   1448  C   GLY A 175      -0.977 -42.035  11.518  1.00 49.12           C  
ANISOU 1448  C   GLY A 175     7171   5834   5659    519   -367   -388       C  
ATOM   1449  O   GLY A 175       0.225 -41.773  11.607  1.00 50.36           O  
ANISOU 1449  O   GLY A 175     7282   6059   5795    605   -323   -348       O  
ATOM   1450  N   ASP A 176      -1.934 -41.205  11.920  1.00 49.34           N  
ANISOU 1450  N   ASP A 176     7135   5896   5714    411   -393   -378       N  
ATOM   1451  CA  ASP A 176      -1.646 -39.869  12.451  1.00 49.42           C  
ANISOU 1451  CA  ASP A 176     7032   6018   5726    386   -373   -322       C  
ATOM   1452  C   ASP A 176      -1.855 -39.760  13.955  1.00 48.49           C  
ANISOU 1452  C   ASP A 176     6865   5899   5659    323   -375   -263       C  
ATOM   1453  O   ASP A 176      -1.496 -38.746  14.554  1.00 50.54           O  
ANISOU 1453  O   ASP A 176     7039   6242   5921    307   -359   -216       O  
ATOM   1454  CB  ASP A 176      -2.498 -38.814  11.747  1.00 48.64           C  
ANISOU 1454  CB  ASP A 176     6899   5973   5610    329   -397   -352       C  
ATOM   1455  CG  ASP A 176      -2.256 -38.768  10.260  1.00 51.98           C  
ANISOU 1455  CG  ASP A 176     7370   6412   5969    394   -393   -403       C  
ATOM   1456  OD1 ASP A 176      -1.095 -38.999   9.833  1.00 55.75           O  
ANISOU 1456  OD1 ASP A 176     7861   6912   6410    491   -349   -393       O  
ATOM   1457  OD2 ASP A 176      -3.232 -38.499   9.520  1.00 52.91           O  
ANISOU 1457  OD2 ASP A 176     7507   6526   6069    354   -434   -452       O  
ATOM   1458  N   GLU A 177      -2.437 -40.800  14.550  1.00 47.51           N  
ANISOU 1458  N   GLU A 177     6804   5677   5571    285   -393   -266       N  
ATOM   1459  CA  GLU A 177      -2.662 -40.880  15.998  1.00 47.51           C  
ANISOU 1459  CA  GLU A 177     6777   5665   5611    230   -390   -208       C  
ATOM   1460  C   GLU A 177      -3.541 -39.744  16.538  1.00 47.28           C  
ANISOU 1460  C   GLU A 177     6663   5701   5600    134   -401   -194       C  
ATOM   1461  O   GLU A 177      -3.255 -39.175  17.600  1.00 46.60           O  
ANISOU 1461  O   GLU A 177     6518   5667   5522    120   -386   -139       O  
ATOM   1462  CB  GLU A 177      -1.327 -40.989  16.758  1.00 47.56           C  
ANISOU 1462  CB  GLU A 177     6761   5704   5607    315   -360   -147       C  
ATOM   1463  CG  GLU A 177      -1.428 -41.516  18.191  1.00 50.02           C  
ANISOU 1463  CG  GLU A 177     7086   5972   5946    287   -359    -89       C  
ATOM   1464  CD  GLU A 177      -0.236 -42.371  18.616  1.00 52.95           C  
ANISOU 1464  CD  GLU A 177     7498   6316   6303    398   -344    -49       C  
ATOM   1465  OE1 GLU A 177      -0.171 -42.712  19.815  1.00 56.42           O  
ANISOU 1465  OE1 GLU A 177     7948   6733   6754    389   -343      7       O  
ATOM   1466  OE2 GLU A 177       0.623 -42.719  17.769  1.00 51.11           O  
ANISOU 1466  OE2 GLU A 177     7289   6086   6045    500   -331    -73       O  
ATOM   1467  N   VAL A 178      -4.601 -39.414  15.797  1.00 45.20           N  
ANISOU 1467  N   VAL A 178     6395   5439   5339     75   -430   -246       N  
ATOM   1468  CA  VAL A 178      -5.648 -38.530  16.309  1.00 45.61           C  
ANISOU 1468  CA  VAL A 178     6377   5539   5414    -14   -443   -240       C  
ATOM   1469  C   VAL A 178      -6.371 -39.291  17.423  1.00 46.52           C  
ANISOU 1469  C   VAL A 178     6510   5592   5574    -89   -442   -215       C  
ATOM   1470  O   VAL A 178      -6.848 -40.403  17.194  1.00 48.31           O  
ANISOU 1470  O   VAL A 178     6807   5727   5823   -118   -456   -244       O  
ATOM   1471  CB  VAL A 178      -6.659 -38.116  15.210  1.00 46.00           C  
ANISOU 1471  CB  VAL A 178     6418   5605   5455    -49   -482   -305       C  
ATOM   1472  CG1 VAL A 178      -7.813 -37.304  15.807  1.00 46.23           C  
ANISOU 1472  CG1 VAL A 178     6373   5682   5511   -132   -495   -300       C  
ATOM   1473  CG2 VAL A 178      -5.969 -37.314  14.097  1.00 44.15           C  
ANISOU 1473  CG2 VAL A 178     6177   5433   5167     25   -477   -322       C  
ATOM   1474  N   PRO A 179      -6.442 -38.709  18.635  1.00 46.73           N  
ANISOU 1474  N   PRO A 179     6479   5664   5611   -121   -422   -161       N  
ATOM   1475  CA  PRO A 179      -6.982 -39.468  19.775  1.00 47.86           C  
ANISOU 1475  CA  PRO A 179     6647   5751   5788   -183   -408   -125       C  
ATOM   1476  C   PRO A 179      -8.352 -40.069  19.477  1.00 48.86           C  
ANISOU 1476  C   PRO A 179     6790   5821   5953   -279   -428   -169       C  
ATOM   1477  O   PRO A 179      -9.262 -39.367  19.022  1.00 47.82           O  
ANISOU 1477  O   PRO A 179     6598   5742   5829   -325   -450   -208       O  
ATOM   1478  CB  PRO A 179      -7.066 -38.424  20.885  1.00 45.41           C  
ANISOU 1478  CB  PRO A 179     6260   5523   5472   -207   -389    -78       C  
ATOM   1479  CG  PRO A 179      -5.991 -37.456  20.546  1.00 47.81           C  
ANISOU 1479  CG  PRO A 179     6524   5902   5740   -133   -388    -72       C  
ATOM   1480  CD  PRO A 179      -6.022 -37.357  19.039  1.00 45.70           C  
ANISOU 1480  CD  PRO A 179     6270   5634   5460   -105   -410   -131       C  
ATOM   1481  N   SER A 180      -8.472 -41.371  19.718  1.00 49.84           N  
ANISOU 1481  N   SER A 180     6999   5838   6101   -306   -423   -162       N  
ATOM   1482  CA  SER A 180      -9.674 -42.123  19.388  1.00 51.50           C  
ANISOU 1482  CA  SER A 180     7236   5979   6354   -406   -444   -206       C  
ATOM   1483  C   SER A 180     -10.934 -41.538  20.023  1.00 52.06           C  
ANISOU 1483  C   SER A 180     7215   6111   6456   -511   -437   -199       C  
ATOM   1484  O   SER A 180     -12.001 -41.586  19.411  1.00 54.42           O  
ANISOU 1484  O   SER A 180     7481   6412   6782   -584   -468   -256       O  
ATOM   1485  CB  SER A 180      -9.508 -43.598  19.763  1.00 52.42           C  
ANISOU 1485  CB  SER A 180     7468   5957   6491   -422   -430   -185       C  
ATOM   1486  OG  SER A 180      -9.445 -43.763  21.165  1.00 53.95           O  
ANISOU 1486  OG  SER A 180     7664   6142   6692   -446   -387   -104       O  
ATOM   1487  N   GLU A 181     -10.798 -40.966  21.225  1.00 51.02           N  
ANISOU 1487  N   GLU A 181     7036   6035   6316   -511   -398   -134       N  
ATOM   1488  CA  GLU A 181     -11.929 -40.363  21.946  1.00 49.82           C  
ANISOU 1488  CA  GLU A 181     6794   5949   6185   -595   -380   -122       C  
ATOM   1489  C   GLU A 181     -12.590 -39.142  21.272  1.00 48.23           C  
ANISOU 1489  C   GLU A 181     6494   5852   5980   -596   -410   -173       C  
ATOM   1490  O   GLU A 181     -13.630 -38.669  21.738  1.00 49.10           O  
ANISOU 1490  O   GLU A 181     6525   6021   6111   -659   -398   -174       O  
ATOM   1491  CB  GLU A 181     -11.545 -40.027  23.396  1.00 51.23           C  
ANISOU 1491  CB  GLU A 181     6960   6163   6343   -582   -331    -43       C  
ATOM   1492  CG  GLU A 181     -10.583 -38.844  23.572  1.00 52.10           C  
ANISOU 1492  CG  GLU A 181     7031   6359   6405   -490   -332    -25       C  
ATOM   1493  CD  GLU A 181      -9.121 -39.263  23.636  1.00 54.14           C  
ANISOU 1493  CD  GLU A 181     7358   6579   6632   -398   -332      8       C  
ATOM   1494  OE1 GLU A 181      -8.806 -40.423  23.289  1.00 57.72           O  
ANISOU 1494  OE1 GLU A 181     7895   6937   7097   -384   -337      6       O  
ATOM   1495  OE2 GLU A 181      -8.279 -38.428  24.033  1.00 49.29           O  
ANISOU 1495  OE2 GLU A 181     6713   6032   5983   -337   -328     34       O  
ATOM   1496  N   ILE A 182     -11.998 -38.628  20.196  1.00 45.76           N  
ANISOU 1496  N   ILE A 182     6186   5563   5636   -520   -444   -212       N  
ATOM   1497  CA  ILE A 182     -12.603 -37.503  19.468  1.00 45.45           C  
ANISOU 1497  CA  ILE A 182     6071   5612   5587   -511   -477   -258       C  
ATOM   1498  C   ILE A 182     -12.935 -37.836  18.009  1.00 46.28           C  
ANISOU 1498  C   ILE A 182     6201   5693   5690   -508   -533   -333       C  
ATOM   1499  O   ILE A 182     -13.543 -37.020  17.307  1.00 46.71           O  
ANISOU 1499  O   ILE A 182     6199   5815   5734   -500   -569   -375       O  
ATOM   1500  CB  ILE A 182     -11.740 -36.208  19.514  1.00 43.97           C  
ANISOU 1500  CB  ILE A 182     5856   5498   5353   -426   -467   -234       C  
ATOM   1501  CG1 ILE A 182     -10.464 -36.356  18.681  1.00 43.99           C  
ANISOU 1501  CG1 ILE A 182     5922   5473   5320   -342   -475   -239       C  
ATOM   1502  CG2 ILE A 182     -11.424 -35.812  20.946  1.00 44.66           C  
ANISOU 1502  CG2 ILE A 182     5921   5614   5435   -429   -421   -169       C  
ATOM   1503  CD1 ILE A 182      -9.924 -35.040  18.154  1.00 41.46           C  
ANISOU 1503  CD1 ILE A 182     5569   5225   4958   -277   -480   -241       C  
ATOM   1504  N   ILE A 183     -12.532 -39.027  17.564  1.00 44.95           N  
ANISOU 1504  N   ILE A 183     6123   5428   5528   -508   -543   -352       N  
ATOM   1505  CA  ILE A 183     -12.737 -39.459  16.178  1.00 44.63           C  
ANISOU 1505  CA  ILE A 183     6126   5354   5476   -499   -597   -428       C  
ATOM   1506  C   ILE A 183     -14.207 -39.334  15.782  1.00 46.36           C  
ANISOU 1506  C   ILE A 183     6274   5612   5727   -585   -645   -485       C  
ATOM   1507  O   ILE A 183     -14.533 -38.788  14.726  1.00 46.36           O  
ANISOU 1507  O   ILE A 183     6252   5663   5699   -555   -695   -540       O  
ATOM   1508  CB  ILE A 183     -12.226 -40.910  15.954  1.00 44.08           C  
ANISOU 1508  CB  ILE A 183     6176   5158   5416   -498   -597   -441       C  
ATOM   1509  CG1 ILE A 183     -10.691 -40.958  15.967  1.00 40.02           C  
ANISOU 1509  CG1 ILE A 183     5724   4623   4858   -382   -564   -402       C  
ATOM   1510  CG2 ILE A 183     -12.774 -41.505  14.659  1.00 42.75           C  
ANISOU 1510  CG2 ILE A 183     6053   4945   5245   -521   -660   -532       C  
ATOM   1511  CD1 ILE A 183     -10.028 -40.252  14.794  1.00 39.42           C  
ANISOU 1511  CD1 ILE A 183     5651   4603   4724   -286   -582   -436       C  
ATOM   1512  N   ASP A 184     -15.080 -39.819  16.663  1.00 47.61           N  
ANISOU 1512  N   ASP A 184     6395   5754   5942   -689   -626   -467       N  
ATOM   1513  CA  ASP A 184     -16.520 -39.816  16.449  1.00 48.70           C  
ANISOU 1513  CA  ASP A 184     6449   5935   6122   -786   -665   -517       C  
ATOM   1514  C   ASP A 184     -17.127 -38.418  16.578  1.00 47.38           C  
ANISOU 1514  C   ASP A 184     6160   5900   5942   -760   -669   -513       C  
ATOM   1515  O   ASP A 184     -18.311 -38.238  16.318  1.00 48.49           O  
ANISOU 1515  O   ASP A 184     6213   6100   6111   -818   -707   -557       O  
ATOM   1516  CB  ASP A 184     -17.210 -40.793  17.423  1.00 50.67           C  
ANISOU 1516  CB  ASP A 184     6692   6125   6434   -912   -628   -489       C  
ATOM   1517  CG  ASP A 184     -17.059 -42.256  17.007  1.00 55.92           C  
ANISOU 1517  CG  ASP A 184     7473   6650   7123   -965   -647   -520       C  
ATOM   1518  OD1 ASP A 184     -16.843 -42.543  15.806  1.00 58.49           O  
ANISOU 1518  OD1 ASP A 184     7859   6940   7425   -929   -706   -589       O  
ATOM   1519  OD2 ASP A 184     -17.171 -43.134  17.888  1.00 61.06           O  
ANISOU 1519  OD2 ASP A 184     8166   7221   7814  -1043   -602   -476       O  
ATOM   1520  N   LYS A 185     -16.313 -37.437  16.969  1.00 46.52           N  
ANISOU 1520  N   LYS A 185     6048   5836   5791   -671   -634   -464       N  
ATOM   1521  CA  LYS A 185     -16.785 -36.067  17.186  1.00 44.42           C  
ANISOU 1521  CA  LYS A 185     5686   5680   5510   -636   -633   -456       C  
ATOM   1522  C   LYS A 185     -16.374 -35.108  16.067  1.00 43.42           C  
ANISOU 1522  C   LYS A 185     5572   5598   5326   -537   -675   -485       C  
ATOM   1523  O   LYS A 185     -16.714 -33.924  16.101  1.00 44.08           O  
ANISOU 1523  O   LYS A 185     5595   5762   5391   -495   -679   -481       O  
ATOM   1524  CB  LYS A 185     -16.306 -35.544  18.548  1.00 43.58           C  
ANISOU 1524  CB  LYS A 185     5565   5595   5398   -619   -563   -380       C  
ATOM   1525  CG  LYS A 185     -16.858 -36.329  19.730  1.00 47.65           C  
ANISOU 1525  CG  LYS A 185     6061   6085   5961   -714   -514   -344       C  
ATOM   1526  CD  LYS A 185     -16.409 -35.755  21.066  1.00 46.40           C  
ANISOU 1526  CD  LYS A 185     5892   5956   5783   -690   -450   -273       C  
ATOM   1527  CE  LYS A 185     -16.983 -36.568  22.217  1.00 45.81           C  
ANISOU 1527  CE  LYS A 185     5805   5855   5745   -783   -396   -232       C  
ATOM   1528  NZ  LYS A 185     -16.725 -35.903  23.532  1.00 47.49           N  
ANISOU 1528  NZ  LYS A 185     6001   6114   5930   -758   -337   -171       N  
ATOM   1529  N   ILE A 186     -15.646 -35.626  15.082  1.00 42.72           N  
ANISOU 1529  N   ILE A 186     5571   5453   5208   -497   -701   -513       N  
ATOM   1530  CA  ILE A 186     -15.201 -34.838  13.933  1.00 41.58           C  
ANISOU 1530  CA  ILE A 186     5453   5342   5001   -406   -735   -538       C  
ATOM   1531  C   ILE A 186     -16.273 -34.775  12.841  1.00 43.32           C  
ANISOU 1531  C   ILE A 186     5642   5604   5215   -417   -814   -612       C  
ATOM   1532  O   ILE A 186     -16.811 -35.801  12.422  1.00 47.52           O  
ANISOU 1532  O   ILE A 186     6190   6093   5772   -480   -855   -665       O  
ATOM   1533  CB  ILE A 186     -13.869 -35.398  13.344  1.00 41.10           C  
ANISOU 1533  CB  ILE A 186     5500   5214   4901   -345   -720   -533       C  
ATOM   1534  CG1 ILE A 186     -12.694 -35.076  14.268  1.00 37.11           C  
ANISOU 1534  CG1 ILE A 186     5010   4702   4388   -306   -652   -458       C  
ATOM   1535  CG2 ILE A 186     -13.593 -34.833  11.941  1.00 43.55           C  
ANISOU 1535  CG2 ILE A 186     5848   5555   5145   -265   -760   -571       C  
ATOM   1536  CD1 ILE A 186     -11.479 -35.919  14.023  1.00 35.35           C  
ANISOU 1536  CD1 ILE A 186     4876   4410   4146   -262   -629   -448       C  
ATOM   1537  N   ILE A 187     -16.582 -33.561  12.400  1.00 42.48           N  
ANISOU 1537  N   ILE A 187     5493   5577   5071   -356   -839   -617       N  
ATOM   1538  CA  ILE A 187     -17.437 -33.330  11.244  1.00 41.35           C  
ANISOU 1538  CA  ILE A 187     5329   5482   4901   -337   -921   -683       C  
ATOM   1539  C   ILE A 187     -16.562 -32.645  10.204  1.00 42.19           C  
ANISOU 1539  C   ILE A 187     5513   5593   4924   -231   -929   -680       C  
ATOM   1540  O   ILE A 187     -16.119 -31.504  10.386  1.00 43.96           O  
ANISOU 1540  O   ILE A 187     5734   5852   5117   -168   -896   -632       O  
ATOM   1541  CB  ILE A 187     -18.695 -32.474  11.608  1.00 41.56           C  
ANISOU 1541  CB  ILE A 187     5234   5604   4952   -349   -946   -691       C  
ATOM   1542  CG1 ILE A 187     -19.638 -33.266  12.534  1.00 40.82           C  
ANISOU 1542  CG1 ILE A 187     5056   5513   4940   -465   -935   -699       C  
ATOM   1543  CG2 ILE A 187     -19.428 -32.004  10.340  1.00 38.34           C  
ANISOU 1543  CG2 ILE A 187     4809   5259   4499   -297  -1036   -751       C  
ATOM   1544  CD1 ILE A 187     -20.790 -32.455  13.144  1.00 38.33           C  
ANISOU 1544  CD1 ILE A 187     4609   5299   4654   -474   -936   -695       C  
ATOM   1545  N   TYR A 188     -16.305 -33.367   9.122  1.00 44.14           N  
ANISOU 1545  N   TYR A 188     5836   5800   5133   -215   -970   -730       N  
ATOM   1546  CA  TYR A 188     -15.280 -33.007   8.151  1.00 45.90           C  
ANISOU 1546  CA  TYR A 188     6152   6014   5275   -120   -960   -723       C  
ATOM   1547  C   TYR A 188     -15.907 -32.472   6.872  1.00 48.08           C  
ANISOU 1547  C   TYR A 188     6438   6345   5485    -65  -1038   -774       C  
ATOM   1548  O   TYR A 188     -16.815 -33.091   6.310  1.00 47.80           O  
ANISOU 1548  O   TYR A 188     6389   6318   5456   -102  -1115   -846       O  
ATOM   1549  CB  TYR A 188     -14.400 -34.233   7.840  1.00 47.60           C  
ANISOU 1549  CB  TYR A 188     6461   6142   5482   -123   -940   -741       C  
ATOM   1550  CG  TYR A 188     -13.426 -34.019   6.705  1.00 47.98           C  
ANISOU 1550  CG  TYR A 188     6602   6186   5441    -26   -930   -745       C  
ATOM   1551  CD1 TYR A 188     -12.360 -33.129   6.838  1.00 47.47           C  
ANISOU 1551  CD1 TYR A 188     6551   6143   5341     38   -862   -676       C  
ATOM   1552  CD2 TYR A 188     -13.570 -34.701   5.497  1.00 51.22           C  
ANISOU 1552  CD2 TYR A 188     7087   6574   5799     -2   -987   -819       C  
ATOM   1553  CE1 TYR A 188     -11.462 -32.918   5.798  1.00 50.31           C  
ANISOU 1553  CE1 TYR A 188     6990   6507   5618    122   -842   -674       C  
ATOM   1554  CE2 TYR A 188     -12.670 -34.499   4.441  1.00 52.98           C  
ANISOU 1554  CE2 TYR A 188     7399   6801   5931     92   -969   -821       C  
ATOM   1555  CZ  TYR A 188     -11.618 -33.600   4.603  1.00 54.24           C  
ANISOU 1555  CZ  TYR A 188     7563   6987   6059    154   -892   -744       C  
ATOM   1556  OH  TYR A 188     -10.717 -33.384   3.578  1.00 57.37           O  
ANISOU 1556  OH  TYR A 188     8040   7393   6366    242   -863   -739       O  
ATOM   1557  N   MET A 189     -15.412 -31.322   6.419  1.00 48.38           N  
ANISOU 1557  N   MET A 189     6505   6421   5458     23  -1019   -735       N  
ATOM   1558  CA  MET A 189     -15.977 -30.640   5.260  1.00 49.77           C  
ANISOU 1558  CA  MET A 189     6697   6653   5560     91  -1089   -768       C  
ATOM   1559  C   MET A 189     -14.877 -30.164   4.303  1.00 49.75           C  
ANISOU 1559  C   MET A 189     6801   6641   5462    182  -1055   -740       C  
ATOM   1560  O   MET A 189     -14.165 -29.205   4.597  1.00 50.48           O  
ANISOU 1560  O   MET A 189     6904   6740   5537    221   -992   -670       O  
ATOM   1561  CB  MET A 189     -16.855 -29.461   5.705  1.00 49.81           C  
ANISOU 1561  CB  MET A 189     6617   6729   5581    108  -1108   -744       C  
ATOM   1562  CG  MET A 189     -18.036 -29.837   6.605  1.00 48.29           C  
ANISOU 1562  CG  MET A 189     6305   6566   5478     24  -1137   -771       C  
ATOM   1563  SD  MET A 189     -18.603 -28.476   7.654  1.00 47.60           S  
ANISOU 1563  SD  MET A 189     6123   6540   5423     47  -1106   -717       S  
ATOM   1564  CE  MET A 189     -17.162 -28.225   8.690  1.00 46.10           C  
ANISOU 1564  CE  MET A 189     5981   6286   5249     38   -989   -633       C  
ATOM   1565  N   PRO A 190     -14.723 -30.848   3.159  1.00 51.43           N  
ANISOU 1565  N   PRO A 190     7094   6837   5611    214  -1095   -796       N  
ATOM   1566  CA  PRO A 190     -13.731 -30.402   2.180  1.00 50.83           C  
ANISOU 1566  CA  PRO A 190     7117   6761   5434    304  -1058   -770       C  
ATOM   1567  C   PRO A 190     -14.304 -29.333   1.252  1.00 50.06           C  
ANISOU 1567  C   PRO A 190     7040   6726   5253    380  -1113   -770       C  
ATOM   1568  O   PRO A 190     -15.515 -29.286   1.044  1.00 50.32           O  
ANISOU 1568  O   PRO A 190     7025   6802   5292    371  -1205   -821       O  
ATOM   1569  CB  PRO A 190     -13.413 -31.681   1.404  1.00 50.97           C  
ANISOU 1569  CB  PRO A 190     7216   6733   5418    307  -1079   -837       C  
ATOM   1570  CG  PRO A 190     -14.677 -32.492   1.480  1.00 52.19           C  
ANISOU 1570  CG  PRO A 190     7321   6886   5624    234  -1175   -919       C  
ATOM   1571  CD  PRO A 190     -15.401 -32.096   2.743  1.00 51.72           C  
ANISOU 1571  CD  PRO A 190     7139   6849   5664    162  -1170   -886       C  
ATOM   1572  N   PHE A 191     -13.443 -28.481   0.706  1.00 50.03           N  
ANISOU 1572  N   PHE A 191     7107   6729   5171    454  -1057   -712       N  
ATOM   1573  CA  PHE A 191     -13.891 -27.429  -0.204  1.00 51.37           C  
ANISOU 1573  CA  PHE A 191     7318   6949   5251    535  -1102   -700       C  
ATOM   1574  C   PHE A 191     -13.059 -27.363  -1.484  1.00 53.70           C  
ANISOU 1574  C   PHE A 191     7737   7244   5424    616  -1074   -692       C  
ATOM   1575  O   PHE A 191     -11.872 -27.702  -1.474  1.00 52.68           O  
ANISOU 1575  O   PHE A 191     7651   7081   5285    616   -986   -661       O  
ATOM   1576  CB  PHE A 191     -13.930 -26.079   0.510  1.00 50.35           C  
ANISOU 1576  CB  PHE A 191     7149   6834   5148    546  -1063   -623       C  
ATOM   1577  CG  PHE A 191     -14.976 -26.003   1.586  1.00 53.44           C  
ANISOU 1577  CG  PHE A 191     7423   7245   5637    490  -1102   -639       C  
ATOM   1578  CD1 PHE A 191     -14.653 -26.277   2.915  1.00 50.68           C  
ANISOU 1578  CD1 PHE A 191     7005   6864   5387    412  -1041   -612       C  
ATOM   1579  CD2 PHE A 191     -16.292 -25.680   1.271  1.00 55.64           C  
ANISOU 1579  CD2 PHE A 191     7655   7581   5904    519  -1201   -682       C  
ATOM   1580  CE1 PHE A 191     -15.621 -26.218   3.913  1.00 51.25           C  
ANISOU 1580  CE1 PHE A 191     6971   6959   5541    362  -1069   -625       C  
ATOM   1581  CE2 PHE A 191     -17.270 -25.620   2.271  1.00 55.60           C  
ANISOU 1581  CE2 PHE A 191     7531   7606   5990    470  -1229   -697       C  
ATOM   1582  CZ  PHE A 191     -16.931 -25.891   3.590  1.00 50.20           C  
ANISOU 1582  CZ  PHE A 191     6786   6888   5401    390  -1159   -667       C  
ATOM   1583  N   ASP A 192     -13.704 -26.938  -2.575  1.00 55.68           N  
ANISOU 1583  N   ASP A 192     8041   7538   5577    689  -1150   -718       N  
ATOM   1584  CA  ASP A 192     -13.077 -26.853  -3.898  1.00 59.37           C  
ANISOU 1584  CA  ASP A 192     8635   8013   5909    775  -1133   -714       C  
ATOM   1585  C   ASP A 192     -12.239 -25.596  -4.074  1.00 58.27           C  
ANISOU 1585  C   ASP A 192     8552   7875   5713    826  -1041   -610       C  
ATOM   1586  O   ASP A 192     -11.199 -25.618  -4.735  1.00 58.65           O  
ANISOU 1586  O   ASP A 192     8685   7914   5684    865   -965   -578       O  
ATOM   1587  CB  ASP A 192     -14.136 -26.905  -5.007  1.00 61.94           C  
ANISOU 1587  CB  ASP A 192     9002   8389   6144    836  -1260   -786       C  
ATOM   1588  CG  ASP A 192     -14.744 -28.282  -5.174  1.00 67.45           C  
ANISOU 1588  CG  ASP A 192     9678   9081   6869    787  -1347   -899       C  
ATOM   1589  OD1 ASP A 192     -14.152 -29.273  -4.681  1.00 69.07           O  
ANISOU 1589  OD1 ASP A 192     9874   9231   7137    726  -1296   -920       O  
ATOM   1590  OD2 ASP A 192     -15.820 -28.373  -5.808  1.00 71.89           O  
ANISOU 1590  OD2 ASP A 192    10235   9691   7390    811  -1469   -968       O  
ATOM   1591  N   ASN A 193     -12.717 -24.494  -3.510  1.00 55.88           N  
ANISOU 1591  N   ASN A 193     8206   7582   5445    826  -1048   -559       N  
ATOM   1592  CA  ASN A 193     -11.983 -23.239  -3.543  1.00 53.97           C  
ANISOU 1592  CA  ASN A 193     8018   7326   5164    858   -963   -458       C  
ATOM   1593  C   ASN A 193     -12.034 -22.574  -2.181  1.00 51.39           C  
ANISOU 1593  C   ASN A 193     7603   6974   4948    797   -927   -410       C  
ATOM   1594  O   ASN A 193     -12.853 -22.941  -1.333  1.00 49.29           O  
ANISOU 1594  O   ASN A 193     7238   6716   4773    749   -980   -453       O  
ATOM   1595  CB  ASN A 193     -12.529 -22.303  -4.624  1.00 54.26           C  
ANISOU 1595  CB  ASN A 193     8145   7392   5079    959  -1016   -437       C  
ATOM   1596  CG  ASN A 193     -14.000 -22.000  -4.439  1.00 56.94           C  
ANISOU 1596  CG  ASN A 193     8422   7769   5444    984  -1137   -480       C  
ATOM   1597  OD1 ASN A 193     -14.368 -21.017  -3.796  1.00 58.14           O  
ANISOU 1597  OD1 ASN A 193     8540   7913   5638    990  -1133   -434       O  
ATOM   1598  ND2 ASN A 193     -14.853 -22.860  -4.985  1.00 59.17           N  
ANISOU 1598  ND2 ASN A 193     8685   8094   5703    999  -1245   -574       N  
ATOM   1599  N   GLU A 194     -11.145 -21.609  -1.980  1.00 50.49           N  
ANISOU 1599  N   GLU A 194     7528   6831   4824    794   -833   -321       N  
ATOM   1600  CA  GLU A 194     -11.063 -20.872  -0.728  1.00 52.09           C  
ANISOU 1600  CA  GLU A 194     7668   7006   5120    739   -794   -274       C  
ATOM   1601  C   GLU A 194     -12.346 -20.080  -0.444  1.00 53.20           C  
ANISOU 1601  C   GLU A 194     7779   7160   5275    776   -874   -284       C  
ATOM   1602  O   GLU A 194     -12.758 -19.956   0.712  1.00 51.54           O  
ANISOU 1602  O   GLU A 194     7481   6942   5159    728   -880   -290       O  
ATOM   1603  CB  GLU A 194      -9.851 -19.937  -0.753  1.00 50.65           C  
ANISOU 1603  CB  GLU A 194     7547   6787   4909    728   -684   -181       C  
ATOM   1604  CG  GLU A 194      -9.554 -19.260   0.566  1.00 50.07           C  
ANISOU 1604  CG  GLU A 194     7415   6678   4931    659   -637   -137       C  
ATOM   1605  CD  GLU A 194      -8.458 -18.218   0.464  1.00 53.21           C  
ANISOU 1605  CD  GLU A 194     7880   7039   5299    642   -540    -47       C  
ATOM   1606  OE1 GLU A 194      -8.141 -17.614   1.510  1.00 52.88           O  
ANISOU 1606  OE1 GLU A 194     7800   6964   5328    581   -502    -13       O  
ATOM   1607  OE2 GLU A 194      -7.916 -18.002  -0.648  1.00 53.10           O  
ANISOU 1607  OE2 GLU A 194     7958   7030   5189    684   -500    -11       O  
ATOM   1608  N   LYS A 195     -12.972 -19.564  -1.502  1.00 56.80           N  
ANISOU 1608  N   LYS A 195     8310   7640   5633    869   -936   -286       N  
ATOM   1609  CA  LYS A 195     -14.114 -18.654  -1.352  1.00 59.71           C  
ANISOU 1609  CA  LYS A 195     8663   8024   5999    929  -1009   -284       C  
ATOM   1610  C   LYS A 195     -15.323 -19.301  -0.682  1.00 59.71           C  
ANISOU 1610  C   LYS A 195     8532   8071   6082    904  -1097   -364       C  
ATOM   1611  O   LYS A 195     -15.909 -18.713   0.229  1.00 59.45           O  
ANISOU 1611  O   LYS A 195     8435   8039   6116    899  -1106   -355       O  
ATOM   1612  CB  LYS A 195     -14.485 -17.970  -2.677  1.00 60.98           C  
ANISOU 1612  CB  LYS A 195     8939   8203   6026   1046  -1059   -265       C  
ATOM   1613  CG  LYS A 195     -13.578 -16.785  -2.998  1.00 66.07           C  
ANISOU 1613  CG  LYS A 195     9707   8789   6607   1072   -969   -161       C  
ATOM   1614  CD  LYS A 195     -13.919 -16.110  -4.315  1.00 69.12           C  
ANISOU 1614  CD  LYS A 195    10224   9188   6852   1192  -1013   -132       C  
ATOM   1615  CE  LYS A 195     -12.905 -15.002  -4.629  1.00 72.66           C  
ANISOU 1615  CE  LYS A 195    10802   9567   7239   1200   -906    -22       C  
ATOM   1616  NZ  LYS A 195     -13.239 -14.240  -5.876  1.00 73.55           N  
ANISOU 1616  NZ  LYS A 195    11057   9681   7206   1322   -943     21       N  
ATOM   1617  N   GLU A 196     -15.682 -20.512  -1.102  1.00 60.15           N  
ANISOU 1617  N   GLU A 196     8550   8166   6137    884  -1157   -442       N  
ATOM   1618  CA  GLU A 196     -16.799 -21.196  -0.452  1.00 60.09           C  
ANISOU 1618  CA  GLU A 196     8413   8203   6216    840  -1233   -516       C  
ATOM   1619  C   GLU A 196     -16.432 -21.688   0.952  1.00 56.77           C  
ANISOU 1619  C   GLU A 196     7902   7750   5919    731  -1165   -510       C  
ATOM   1620  O   GLU A 196     -17.267 -21.662   1.854  1.00 56.18           O  
ANISOU 1620  O   GLU A 196     7722   7701   5923    701  -1192   -532       O  
ATOM   1621  CB  GLU A 196     -17.429 -22.288  -1.335  1.00 61.10           C  
ANISOU 1621  CB  GLU A 196     8530   8379   6308    845  -1331   -606       C  
ATOM   1622  CG  GLU A 196     -16.527 -23.426  -1.767  1.00 68.32           C  
ANISOU 1622  CG  GLU A 196     9497   9260   7203    799  -1293   -634       C  
ATOM   1623  CD  GLU A 196     -17.209 -24.358  -2.774  1.00 75.82           C  
ANISOU 1623  CD  GLU A 196    10459  10252   8098    817  -1402   -729       C  
ATOM   1624  OE1 GLU A 196     -17.638 -25.462  -2.364  1.00 75.59           O  
ANISOU 1624  OE1 GLU A 196    10352  10223   8144    735  -1440   -799       O  
ATOM   1625  OE2 GLU A 196     -17.326 -23.982  -3.970  1.00 76.78           O  
ANISOU 1625  OE2 GLU A 196    10673  10403   8098    911  -1451   -733       O  
ATOM   1626  N   LEU A 197     -15.181 -22.096   1.144  1.00 54.79           N  
ANISOU 1626  N   LEU A 197     7691   7449   5679    680  -1075   -478       N  
ATOM   1627  CA  LEU A 197     -14.724 -22.490   2.474  1.00 51.80           C  
ANISOU 1627  CA  LEU A 197     7239   7039   5405    587  -1010   -463       C  
ATOM   1628  C   LEU A 197     -14.982 -21.352   3.453  1.00 49.42           C  
ANISOU 1628  C   LEU A 197     6901   6730   5148    590   -984   -417       C  
ATOM   1629  O   LEU A 197     -15.644 -21.539   4.474  1.00 49.30           O  
ANISOU 1629  O   LEU A 197     6788   6731   5214    545   -997   -439       O  
ATOM   1630  CB  LEU A 197     -13.241 -22.881   2.475  1.00 50.61           C  
ANISOU 1630  CB  LEU A 197     7140   6841   5247    552   -916   -425       C  
ATOM   1631  CG  LEU A 197     -12.728 -23.545   3.766  1.00 51.49           C  
ANISOU 1631  CG  LEU A 197     7179   6925   5459    461   -860   -419       C  
ATOM   1632  CD1 LEU A 197     -11.519 -24.425   3.482  1.00 48.88           C  
ANISOU 1632  CD1 LEU A 197     6890   6568   5116    441   -801   -414       C  
ATOM   1633  CD2 LEU A 197     -12.390 -22.525   4.854  1.00 49.88           C  
ANISOU 1633  CD2 LEU A 197     6950   6701   5301    436   -802   -357       C  
ATOM   1634  N   LEU A 198     -14.472 -20.173   3.121  1.00 48.39           N  
ANISOU 1634  N   LEU A 198     6855   6572   4960    642   -945   -353       N  
ATOM   1635  CA  LEU A 198     -14.646 -18.997   3.962  1.00 48.16           C  
ANISOU 1635  CA  LEU A 198     6816   6520   4961    653   -920   -309       C  
ATOM   1636  C   LEU A 198     -16.107 -18.567   4.097  1.00 50.23           C  
ANISOU 1636  C   LEU A 198     7021   6831   5234    713  -1003   -345       C  
ATOM   1637  O   LEU A 198     -16.531 -18.200   5.196  1.00 51.50           O  
ANISOU 1637  O   LEU A 198     7115   6993   5460    693   -991   -343       O  
ATOM   1638  CB  LEU A 198     -13.764 -17.841   3.477  1.00 46.85           C  
ANISOU 1638  CB  LEU A 198     6770   6304   4729    690   -861   -232       C  
ATOM   1639  CG  LEU A 198     -12.265 -18.029   3.718  1.00 42.46           C  
ANISOU 1639  CG  LEU A 198     6242   5705   4186    618   -762   -186       C  
ATOM   1640  CD1 LEU A 198     -11.479 -16.939   3.037  1.00 43.72           C  
ANISOU 1640  CD1 LEU A 198     6520   5821   4272    649   -707   -112       C  
ATOM   1641  CD2 LEU A 198     -11.953 -18.044   5.202  1.00 43.99           C  
ANISOU 1641  CD2 LEU A 198     6360   5878   4477    536   -718   -178       C  
ATOM   1642  N   MET A 199     -16.866 -18.624   2.998  1.00 51.63           N  
ANISOU 1642  N   MET A 199     7219   7054   5342    790  -1086   -379       N  
ATOM   1643  CA  MET A 199     -18.296 -18.296   3.019  1.00 54.90           C  
ANISOU 1643  CA  MET A 199     7563   7532   5763    856  -1176   -419       C  
ATOM   1644  C   MET A 199     -19.059 -19.227   3.945  1.00 53.71           C  
ANISOU 1644  C   MET A 199     7264   7430   5713    779  -1201   -480       C  
ATOM   1645  O   MET A 199     -19.865 -18.770   4.754  1.00 52.95           O  
ANISOU 1645  O   MET A 199     7086   7365   5666    794  -1212   -487       O  
ATOM   1646  CB  MET A 199     -18.922 -18.330   1.618  1.00 59.27           C  
ANISOU 1646  CB  MET A 199     8162   8137   6221    948  -1272   -451       C  
ATOM   1647  CG  MET A 199     -18.930 -16.988   0.900  1.00 68.03           C  
ANISOU 1647  CG  MET A 199     9390   9225   7235   1068  -1282   -393       C  
ATOM   1648  SD  MET A 199     -20.144 -16.870  -0.442  1.00 83.47           S  
ANISOU 1648  SD  MET A 199    11360  11266   9088   1201  -1424   -440       S  
ATOM   1649  CE  MET A 199     -19.438 -17.940  -1.705  1.00 79.73           C  
ANISOU 1649  CE  MET A 199    10967  10796   8531   1176  -1436   -469       C  
ATOM   1650  N   GLU A 200     -18.794 -20.526   3.831  1.00 53.87           N  
ANISOU 1650  N   GLU A 200     7254   7454   5760    698  -1204   -522       N  
ATOM   1651  CA  GLU A 200     -19.436 -21.514   4.691  1.00 55.42           C  
ANISOU 1651  CA  GLU A 200     7321   7684   6053    609  -1219   -574       C  
ATOM   1652  C   GLU A 200     -19.018 -21.340   6.148  1.00 53.15           C  
ANISOU 1652  C   GLU A 200     6991   7360   5844    544  -1131   -534       C  
ATOM   1653  O   GLU A 200     -19.843 -21.483   7.048  1.00 53.42           O  
ANISOU 1653  O   GLU A 200     6915   7434   5947    511  -1138   -557       O  
ATOM   1654  CB  GLU A 200     -19.150 -22.942   4.214  1.00 57.38           C  
ANISOU 1654  CB  GLU A 200     7572   7922   6307    538  -1237   -624       C  
ATOM   1655  CG  GLU A 200     -19.948 -24.041   4.953  1.00 63.36           C  
ANISOU 1655  CG  GLU A 200     8204   8711   7159    440  -1264   -682       C  
ATOM   1656  CD  GLU A 200     -21.470 -23.876   4.838  1.00 68.91           C  
ANISOU 1656  CD  GLU A 200     8796   9508   7878    469  -1358   -735       C  
ATOM   1657  OE1 GLU A 200     -21.985 -23.790   3.696  1.00 69.13           O  
ANISOU 1657  OE1 GLU A 200     8848   9582   7839    535  -1448   -774       O  
ATOM   1658  OE2 GLU A 200     -22.147 -23.834   5.895  1.00 68.83           O  
ANISOU 1658  OE2 GLU A 200     8674   9532   7946    427  -1341   -737       O  
ATOM   1659  N   TYR A 201     -17.748 -21.012   6.378  1.00 50.26           N  
ANISOU 1659  N   TYR A 201     6707   6925   5465    527  -1048   -476       N  
ATOM   1660  CA  TYR A 201     -17.276 -20.798   7.741  1.00 49.33           C  
ANISOU 1660  CA  TYR A 201     6558   6774   5412    469   -972   -440       C  
ATOM   1661  C   TYR A 201     -17.986 -19.613   8.382  1.00 51.26           C  
ANISOU 1661  C   TYR A 201     6775   7036   5666    524   -974   -424       C  
ATOM   1662  O   TYR A 201     -18.289 -19.642   9.580  1.00 50.71           O  
ANISOU 1662  O   TYR A 201     6631   6977   5660    482   -944   -426       O  
ATOM   1663  CB  TYR A 201     -15.756 -20.615   7.804  1.00 46.86           C  
ANISOU 1663  CB  TYR A 201     6332   6393   5081    441   -891   -383       C  
ATOM   1664  CG  TYR A 201     -15.236 -20.522   9.223  1.00 43.98           C  
ANISOU 1664  CG  TYR A 201     5930   5999   4780    375   -823   -353       C  
ATOM   1665  CD1 TYR A 201     -15.267 -21.630  10.070  1.00 45.06           C  
ANISOU 1665  CD1 TYR A 201     5994   6143   4985    295   -807   -375       C  
ATOM   1666  CD2 TYR A 201     -14.728 -19.336   9.721  1.00 42.00           C  
ANISOU 1666  CD2 TYR A 201     5728   5711   4520    392   -777   -304       C  
ATOM   1667  CE1 TYR A 201     -14.803 -21.559  11.374  1.00 44.24           C  
ANISOU 1667  CE1 TYR A 201     5862   6018   4930    241   -750   -347       C  
ATOM   1668  CE2 TYR A 201     -14.263 -19.248  11.024  1.00 46.31           C  
ANISOU 1668  CE2 TYR A 201     6243   6235   5118    333   -723   -283       C  
ATOM   1669  CZ  TYR A 201     -14.299 -20.366  11.846  1.00 45.25           C  
ANISOU 1669  CZ  TYR A 201     6034   6117   5043    261   -711   -304       C  
ATOM   1670  OH  TYR A 201     -13.834 -20.286  13.139  1.00 43.93           O  
ANISOU 1670  OH  TYR A 201     5842   5932   4916    209   -661   -282       O  
ATOM   1671  N   LEU A 202     -18.256 -18.584   7.577  1.00 52.54           N  
ANISOU 1671  N   LEU A 202     7004   7200   5760    625  -1009   -408       N  
ATOM   1672  CA  LEU A 202     -18.982 -17.398   8.037  1.00 52.23           C  
ANISOU 1672  CA  LEU A 202     6955   7171   5718    702  -1019   -395       C  
ATOM   1673  C   LEU A 202     -20.415 -17.689   8.471  1.00 52.16           C  
ANISOU 1673  C   LEU A 202     6810   7252   5757    719  -1075   -451       C  
ATOM   1674  O   LEU A 202     -20.842 -17.233   9.532  1.00 50.40           O  
ANISOU 1674  O   LEU A 202     6531   7040   5577    723  -1046   -449       O  
ATOM   1675  CB  LEU A 202     -18.975 -16.299   6.973  1.00 52.75           C  
ANISOU 1675  CB  LEU A 202     7135   7214   5693    814  -1049   -363       C  
ATOM   1676  CG  LEU A 202     -17.982 -15.157   7.175  1.00 53.03           C  
ANISOU 1676  CG  LEU A 202     7293   7157   5700    826   -978   -293       C  
ATOM   1677  CD1 LEU A 202     -17.910 -14.307   5.929  1.00 54.89           C  
ANISOU 1677  CD1 LEU A 202     7653   7364   5837    926  -1007   -257       C  
ATOM   1678  CD2 LEU A 202     -18.372 -14.302   8.367  1.00 55.06           C  
ANISOU 1678  CD2 LEU A 202     7523   7396   5999    844   -952   -286       C  
ATOM   1679  N   ASN A 203     -21.148 -18.440   7.648  1.00 53.11           N  
ANISOU 1679  N   ASN A 203     6875   7437   5866    727  -1154   -503       N  
ATOM   1680  CA  ASN A 203     -22.534 -18.794   7.944  1.00 54.07           C  
ANISOU 1680  CA  ASN A 203     6852   7658   6035    733  -1213   -560       C  
ATOM   1681  C   ASN A 203     -22.603 -19.681   9.166  1.00 53.50           C  
ANISOU 1681  C   ASN A 203     6677   7596   6056    615  -1161   -575       C  
ATOM   1682  O   ASN A 203     -23.485 -19.520  10.020  1.00 54.79           O  
ANISOU 1682  O   ASN A 203     6732   7818   6268    618  -1154   -592       O  
ATOM   1683  CB  ASN A 203     -23.172 -19.510   6.757  1.00 57.93           C  
ANISOU 1683  CB  ASN A 203     7309   8209   6492    748  -1314   -617       C  
ATOM   1684  CG  ASN A 203     -23.230 -18.647   5.522  1.00 64.43           C  
ANISOU 1684  CG  ASN A 203     8233   9034   7212    877  -1374   -603       C  
ATOM   1685  OD1 ASN A 203     -22.792 -19.060   4.448  1.00 72.24           O  
ANISOU 1685  OD1 ASN A 203     9300  10007   8140    881  -1408   -611       O  
ATOM   1686  ND2 ASN A 203     -23.778 -17.439   5.660  1.00 67.79           N  
ANISOU 1686  ND2 ASN A 203     8666   9478   7613    990  -1388   -580       N  
ATOM   1687  N   PHE A 204     -21.659 -20.619   9.228  1.00 51.05           N  
ANISOU 1687  N   PHE A 204     6404   7229   5763    517  -1120   -567       N  
ATOM   1688  CA  PHE A 204     -21.450 -21.473  10.381  1.00 49.85           C  
ANISOU 1688  CA  PHE A 204     6189   7063   5688    404  -1059   -566       C  
ATOM   1689  C   PHE A 204     -21.279 -20.620  11.642  1.00 49.69           C  
ANISOU 1689  C   PHE A 204     6165   7025   5691    415   -986   -525       C  
ATOM   1690  O   PHE A 204     -21.956 -20.840  12.651  1.00 48.15           O  
ANISOU 1690  O   PHE A 204     5870   6874   5552    378   -963   -538       O  
ATOM   1691  CB  PHE A 204     -20.227 -22.364  10.131  1.00 50.00           C  
ANISOU 1691  CB  PHE A 204     6287   7009   5702    331  -1024   -551       C  
ATOM   1692  CG  PHE A 204     -19.732 -23.087  11.353  1.00 48.46           C  
ANISOU 1692  CG  PHE A 204     6061   6780   5573    232   -952   -532       C  
ATOM   1693  CD1 PHE A 204     -20.369 -24.241  11.803  1.00 49.22           C  
ANISOU 1693  CD1 PHE A 204     6066   6902   5731    144   -961   -568       C  
ATOM   1694  CD2 PHE A 204     -18.619 -22.621  12.043  1.00 46.93           C  
ANISOU 1694  CD2 PHE A 204     5932   6526   5374    223   -877   -477       C  
ATOM   1695  CE1 PHE A 204     -19.910 -24.913  12.930  1.00 49.64           C  
ANISOU 1695  CE1 PHE A 204     6103   6920   5837     58   -893   -544       C  
ATOM   1696  CE2 PHE A 204     -18.152 -23.284  13.172  1.00 46.09           C  
ANISOU 1696  CE2 PHE A 204     5800   6392   5318    140   -818   -458       C  
ATOM   1697  CZ  PHE A 204     -18.801 -24.429  13.618  1.00 47.15           C  
ANISOU 1697  CZ  PHE A 204     5854   6551   5510     62   -824   -488       C  
ATOM   1698  N   TRP A 205     -20.388 -19.634  11.554  1.00 49.55           N  
ANISOU 1698  N   TRP A 205     6259   6942   5626    465   -951   -477       N  
ATOM   1699  CA  TRP A 205     -20.112 -18.706  12.641  1.00 48.58           C  
ANISOU 1699  CA  TRP A 205     6158   6787   5513    481   -889   -442       C  
ATOM   1700  C   TRP A 205     -21.377 -17.970  13.040  1.00 50.83           C  
ANISOU 1700  C   TRP A 205     6369   7139   5806    560   -913   -465       C  
ATOM   1701  O   TRP A 205     -21.615 -17.729  14.221  1.00 51.76           O  
ANISOU 1701  O   TRP A 205     6441   7269   5958    547   -866   -461       O  
ATOM   1702  CB  TRP A 205     -19.047 -17.711  12.192  1.00 48.52           C  
ANISOU 1702  CB  TRP A 205     6290   6700   5448    524   -864   -393       C  
ATOM   1703  CG  TRP A 205     -18.500 -16.826  13.261  1.00 49.41           C  
ANISOU 1703  CG  TRP A 205     6446   6760   5568    519   -801   -358       C  
ATOM   1704  CD1 TRP A 205     -19.065 -15.678  13.749  1.00 49.96           C  
ANISOU 1704  CD1 TRP A 205     6529   6828   5626    596   -798   -356       C  
ATOM   1705  CD2 TRP A 205     -17.261 -16.990  13.958  1.00 45.82           C  
ANISOU 1705  CD2 TRP A 205     6034   6246   5130    438   -737   -324       C  
ATOM   1706  NE1 TRP A 205     -18.259 -15.127  14.718  1.00 45.77           N  
ANISOU 1706  NE1 TRP A 205     6052   6236   5103    560   -737   -327       N  
ATOM   1707  CE2 TRP A 205     -17.141 -15.908  14.858  1.00 47.94           C  
ANISOU 1707  CE2 TRP A 205     6341   6479   5395    461   -702   -306       C  
ATOM   1708  CE3 TRP A 205     -16.237 -17.942  13.905  1.00 46.85           C  
ANISOU 1708  CE3 TRP A 205     6174   6353   5275    353   -710   -309       C  
ATOM   1709  CZ2 TRP A 205     -16.039 -15.756  15.702  1.00 47.16           C  
ANISOU 1709  CZ2 TRP A 205     6283   6326   5308    394   -646   -277       C  
ATOM   1710  CZ3 TRP A 205     -15.146 -17.796  14.746  1.00 46.97           C  
ANISOU 1710  CZ3 TRP A 205     6223   6320   5303    295   -652   -276       C  
ATOM   1711  CH2 TRP A 205     -15.054 -16.711  15.634  1.00 49.15           C  
ANISOU 1711  CH2 TRP A 205     6532   6567   5577    311   -624   -261       C  
ATOM   1712  N   GLN A 206     -22.192 -17.620  12.047  1.00 53.36           N  
ANISOU 1712  N   GLN A 206     6677   7509   6090    650   -988   -490       N  
ATOM   1713  CA  GLN A 206     -23.458 -16.936  12.291  1.00 53.78           C  
ANISOU 1713  CA  GLN A 206     6649   7639   6148    745  -1021   -515       C  
ATOM   1714  C   GLN A 206     -24.450 -17.821  13.028  1.00 52.47           C  
ANISOU 1714  C   GLN A 206     6317   7568   6053    681  -1020   -558       C  
ATOM   1715  O   GLN A 206     -25.195 -17.348  13.883  1.00 50.33           O  
ANISOU 1715  O   GLN A 206     5970   7348   5806    722   -995   -567       O  
ATOM   1716  CB  GLN A 206     -24.061 -16.435  10.978  1.00 57.39           C  
ANISOU 1716  CB  GLN A 206     7131   8132   6543    861  -1111   -531       C  
ATOM   1717  CG  GLN A 206     -24.138 -14.923  10.871  1.00 64.21           C  
ANISOU 1717  CG  GLN A 206     8088   8958   7351    998  -1113   -500       C  
ATOM   1718  CD  GLN A 206     -22.839 -14.272  10.430  1.00 65.99           C  
ANISOU 1718  CD  GLN A 206     8492   9062   7520   1002  -1076   -441       C  
ATOM   1719  OE1 GLN A 206     -21.751 -14.607  10.906  1.00 61.52           O  
ANISOU 1719  OE1 GLN A 206     7972   8428   6974    901  -1009   -414       O  
ATOM   1720  NE2 GLN A 206     -22.957 -13.316   9.517  1.00 68.74           N  
ANISOU 1720  NE2 GLN A 206     8939   9384   7794   1121  -1119   -419       N  
ATOM   1721  N   GLN A 207     -24.444 -19.107  12.688  1.00 53.27           N  
ANISOU 1721  N   GLN A 207     6365   7688   6187    580  -1043   -585       N  
ATOM   1722  CA  GLN A 207     -25.339 -20.077  13.307  1.00 54.66           C  
ANISOU 1722  CA  GLN A 207     6389   7945   6435    496  -1040   -622       C  
ATOM   1723  C   GLN A 207     -24.879 -20.391  14.712  1.00 51.97           C  
ANISOU 1723  C   GLN A 207     6037   7569   6140    410   -943   -593       C  
ATOM   1724  O   GLN A 207     -25.695 -20.591  15.608  1.00 52.82           O  
ANISOU 1724  O   GLN A 207     6028   7746   6294    382   -911   -606       O  
ATOM   1725  CB  GLN A 207     -25.394 -21.370  12.488  1.00 56.20           C  
ANISOU 1725  CB  GLN A 207     6556   8150   6649    408  -1096   -660       C  
ATOM   1726  CG  GLN A 207     -26.174 -21.261  11.187  1.00 65.62           C  
ANISOU 1726  CG  GLN A 207     7718   9410   7803    481  -1207   -707       C  
ATOM   1727  CD  GLN A 207     -27.680 -21.329  11.393  1.00 73.35           C  
ANISOU 1727  CD  GLN A 207     8521  10522   8827    495  -1253   -756       C  
ATOM   1728  OE1 GLN A 207     -28.198 -22.287  11.972  1.00 76.55           O  
ANISOU 1728  OE1 GLN A 207     8810  10971   9304    382  -1235   -781       O  
ATOM   1729  NE2 GLN A 207     -28.393 -20.315  10.905  1.00 76.12           N  
ANISOU 1729  NE2 GLN A 207     8850  10939   9135    635  -1311   -767       N  
ATOM   1730  N   LYS A 208     -23.563 -20.433  14.894  1.00 49.43           N  
ANISOU 1730  N   LYS A 208     5835   7148   5801    371   -895   -551       N  
ATOM   1731  CA  LYS A 208     -22.974 -20.884  16.140  1.00 48.57           C  
ANISOU 1731  CA  LYS A 208     5727   7000   5726    283   -812   -521       C  
ATOM   1732  C   LYS A 208     -21.941 -19.869  16.624  1.00 48.84           C  
ANISOU 1732  C   LYS A 208     5878   6958   5722    325   -762   -476       C  
ATOM   1733  O   LYS A 208     -20.737 -20.162  16.719  1.00 48.56           O  
ANISOU 1733  O   LYS A 208     5924   6846   5678    271   -730   -444       O  
ATOM   1734  CB  LYS A 208     -22.373 -22.285  15.961  1.00 47.92           C  
ANISOU 1734  CB  LYS A 208     5656   6877   5674    168   -808   -521       C  
ATOM   1735  CG  LYS A 208     -23.375 -23.325  15.455  1.00 45.71           C  
ANISOU 1735  CG  LYS A 208     5271   6661   5435    111   -862   -572       C  
ATOM   1736  CD  LYS A 208     -22.729 -24.689  15.288  1.00 50.89           C  
ANISOU 1736  CD  LYS A 208     5962   7257   6118      3   -856   -573       C  
ATOM   1737  CE  LYS A 208     -23.499 -25.574  14.287  1.00 54.86           C  
ANISOU 1737  CE  LYS A 208     6407   7798   6640    -37   -936   -632       C  
ATOM   1738  NZ  LYS A 208     -24.911 -25.851  14.684  1.00 50.30           N  
ANISOU 1738  NZ  LYS A 208     5676   7320   6118    -77   -953   -668       N  
ATOM   1739  N   THR A 209     -22.440 -18.672  16.933  1.00 47.37           N  
ANISOU 1739  N   THR A 209     5695   6792   5512    421   -758   -477       N  
ATOM   1740  CA  THR A 209     -21.613 -17.522  17.294  1.00 45.86           C  
ANISOU 1740  CA  THR A 209     5620   6524   5279    471   -722   -443       C  
ATOM   1741  C   THR A 209     -20.996 -17.712  18.670  1.00 45.04           C  
ANISOU 1741  C   THR A 209     5526   6391   5197    399   -647   -420       C  
ATOM   1742  O   THR A 209     -21.713 -17.899  19.649  1.00 46.67           O  
ANISOU 1742  O   THR A 209     5647   6654   5430    387   -613   -434       O  
ATOM   1743  CB  THR A 209     -22.444 -16.221  17.232  1.00 47.73           C  
ANISOU 1743  CB  THR A 209     5862   6788   5485    604   -743   -456       C  
ATOM   1744  OG1 THR A 209     -23.036 -16.112  15.930  1.00 49.56           O  
ANISOU 1744  OG1 THR A 209     6084   7056   5693    675   -821   -475       O  
ATOM   1745  CG2 THR A 209     -21.584 -14.980  17.512  1.00 43.02           C  
ANISOU 1745  CG2 THR A 209     5405   6095   4844    650   -712   -423       C  
ATOM   1746  N   PRO A 210     -19.657 -17.674  18.747  1.00 44.51           N  
ANISOU 1746  N   PRO A 210     5556   6241   5113    352   -622   -385       N  
ATOM   1747  CA  PRO A 210     -18.959 -17.909  20.005  1.00 43.20           C  
ANISOU 1747  CA  PRO A 210     5404   6048   4961    284   -561   -364       C  
ATOM   1748  C   PRO A 210     -19.218 -16.802  21.006  1.00 41.84           C  
ANISOU 1748  C   PRO A 210     5255   5873   4768    340   -528   -368       C  
ATOM   1749  O   PRO A 210     -19.257 -15.633  20.638  1.00 45.23           O  
ANISOU 1749  O   PRO A 210     5754   6270   5163    422   -546   -370       O  
ATOM   1750  CB  PRO A 210     -17.482 -17.890  19.597  1.00 41.40           C  
ANISOU 1750  CB  PRO A 210     5276   5740   4714    244   -557   -330       C  
ATOM   1751  CG  PRO A 210     -17.484 -18.149  18.136  1.00 41.96           C  
ANISOU 1751  CG  PRO A 210     5363   5808   4772    265   -606   -335       C  
ATOM   1752  CD  PRO A 210     -18.707 -17.457  17.646  1.00 45.19           C  
ANISOU 1752  CD  PRO A 210     5740   6263   5166    359   -647   -363       C  
ATOM   1753  N   VAL A 211     -19.401 -17.180  22.263  1.00 40.79           N  
ANISOU 1753  N   VAL A 211     5075   5771   4651    299   -480   -368       N  
ATOM   1754  CA  VAL A 211     -19.449 -16.221  23.348  1.00 40.88           C  
ANISOU 1754  CA  VAL A 211     5125   5772   4635    342   -442   -373       C  
ATOM   1755  C   VAL A 211     -18.020 -16.072  23.870  1.00 42.17           C  
ANISOU 1755  C   VAL A 211     5384   5858   4780    282   -421   -345       C  
ATOM   1756  O   VAL A 211     -17.509 -14.957  24.010  1.00 44.54           O  
ANISOU 1756  O   VAL A 211     5778   6098   5046    318   -422   -344       O  
ATOM   1757  CB  VAL A 211     -20.418 -16.687  24.453  1.00 40.32           C  
ANISOU 1757  CB  VAL A 211     4954   5785   4582    333   -395   -389       C  
ATOM   1758  CG1 VAL A 211     -20.312 -15.800  25.676  1.00 39.05           C  
ANISOU 1758  CG1 VAL A 211     4846   5609   4383    371   -351   -395       C  
ATOM   1759  CG2 VAL A 211     -21.835 -16.712  23.919  1.00 38.89           C  
ANISOU 1759  CG2 VAL A 211     4665   5691   4422    395   -419   -420       C  
ATOM   1760  N   ILE A 212     -17.380 -17.206  24.144  1.00 39.14           N  
ANISOU 1760  N   ILE A 212     4977   5476   4420    190   -406   -322       N  
ATOM   1761  CA  ILE A 212     -15.980 -17.231  24.510  1.00 38.37           C  
ANISOU 1761  CA  ILE A 212     4952   5319   4309    132   -396   -294       C  
ATOM   1762  C   ILE A 212     -15.191 -17.752  23.310  1.00 40.11           C  
ANISOU 1762  C   ILE A 212     5192   5505   4542    100   -426   -274       C  
ATOM   1763  O   ILE A 212     -15.422 -18.874  22.844  1.00 38.77           O  
ANISOU 1763  O   ILE A 212     4967   5362   4402     66   -435   -273       O  
ATOM   1764  CB  ILE A 212     -15.715 -18.126  25.758  1.00 38.48           C  
ANISOU 1764  CB  ILE A 212     4933   5357   4330     66   -356   -278       C  
ATOM   1765  CG1 ILE A 212     -16.572 -17.709  26.975  1.00 38.36           C  
ANISOU 1765  CG1 ILE A 212     4893   5388   4294    100   -317   -298       C  
ATOM   1766  CG2 ILE A 212     -14.225 -18.173  26.100  1.00 42.51           C  
ANISOU 1766  CG2 ILE A 212     5508   5817   4826     12   -356   -251       C  
ATOM   1767  CD1 ILE A 212     -16.460 -16.246  27.425  1.00 38.43           C  
ANISOU 1767  CD1 ILE A 212     4981   5361   4259    163   -315   -319       C  
ATOM   1768  N   LEU A 213     -14.279 -16.923  22.801  1.00 39.56           N  
ANISOU 1768  N   LEU A 213     5206   5376   4449    108   -439   -260       N  
ATOM   1769  CA  LEU A 213     -13.370 -17.333  21.748  1.00 36.96           C  
ANISOU 1769  CA  LEU A 213     4902   5016   4123     78   -456   -238       C  
ATOM   1770  C   LEU A 213     -11.971 -17.550  22.301  1.00 37.04           C  
ANISOU 1770  C   LEU A 213     4942   4998   4133     11   -436   -210       C  
ATOM   1771  O   LEU A 213     -11.367 -16.634  22.873  1.00 38.24           O  
ANISOU 1771  O   LEU A 213     5148   5116   4266      2   -427   -205       O  
ATOM   1772  CB  LEU A 213     -13.333 -16.296  20.624  1.00 39.06           C  
ANISOU 1772  CB  LEU A 213     5237   5243   4362    133   -480   -235       C  
ATOM   1773  CG  LEU A 213     -12.691 -16.786  19.320  1.00 38.82           C  
ANISOU 1773  CG  LEU A 213     5225   5197   4327    119   -495   -215       C  
ATOM   1774  CD1 LEU A 213     -13.385 -18.043  18.828  1.00 39.06           C  
ANISOU 1774  CD1 LEU A 213     5181   5278   4381    115   -516   -234       C  
ATOM   1775  CD2 LEU A 213     -12.729 -15.708  18.264  1.00 40.62           C  
ANISOU 1775  CD2 LEU A 213     5530   5386   4519    178   -514   -207       C  
ATOM   1776  N   THR A 214     -11.463 -18.766  22.127  1.00 34.62           N  
ANISOU 1776  N   THR A 214     4600   4705   3848    -34   -433   -194       N  
ATOM   1777  CA  THR A 214     -10.141 -19.137  22.625  1.00 36.76           C  
ANISOU 1777  CA  THR A 214     4882   4963   4121    -88   -418   -167       C  
ATOM   1778  C   THR A 214      -9.397 -20.036  21.637  1.00 39.05           C  
ANISOU 1778  C   THR A 214     5165   5248   4422   -105   -423   -149       C  
ATOM   1779  O   THR A 214      -9.913 -20.362  20.560  1.00 40.53           O  
ANISOU 1779  O   THR A 214     5348   5439   4613    -78   -439   -160       O  
ATOM   1780  CB  THR A 214     -10.190 -19.808  24.041  1.00 34.70           C  
ANISOU 1780  CB  THR A 214     4587   4730   3867   -121   -399   -163       C  
ATOM   1781  OG1 THR A 214      -8.855 -20.024  24.514  1.00 34.60           O  
ANISOU 1781  OG1 THR A 214     4588   4708   3850   -162   -395   -137       O  
ATOM   1782  CG2 THR A 214     -10.900 -21.136  24.003  1.00 34.85           C  
ANISOU 1782  CG2 THR A 214     4550   4777   3914   -132   -394   -164       C  
ATOM   1783  N   GLY A 215      -8.188 -20.434  22.023  1.00 38.28           N  
ANISOU 1783  N   GLY A 215     5068   5148   4328   -144   -411   -124       N  
ATOM   1784  CA  GLY A 215      -7.315 -21.254  21.192  1.00 40.53           C  
ANISOU 1784  CA  GLY A 215     5347   5431   4620   -152   -408   -106       C  
ATOM   1785  C   GLY A 215      -5.900 -20.806  21.472  1.00 40.79           C  
ANISOU 1785  C   GLY A 215     5392   5461   4645   -183   -397    -79       C  
ATOM   1786  O   GLY A 215      -5.682 -19.998  22.370  1.00 45.51           O  
ANISOU 1786  O   GLY A 215     6002   6056   5234   -205   -398    -80       O  
ATOM   1787  N   TRP A 216      -4.938 -21.298  20.704  1.00 40.20           N  
ANISOU 1787  N   TRP A 216     5310   5391   4572   -185   -387    -60       N  
ATOM   1788  CA  TRP A 216      -3.543 -20.987  20.985  1.00 39.51           C  
ANISOU 1788  CA  TRP A 216     5213   5317   4483   -219   -375    -35       C  
ATOM   1789  C   TRP A 216      -3.032 -19.890  20.073  1.00 40.40           C  
ANISOU 1789  C   TRP A 216     5360   5411   4579   -229   -362    -23       C  
ATOM   1790  O   TRP A 216      -2.800 -20.105  18.876  1.00 42.60           O  
ANISOU 1790  O   TRP A 216     5649   5689   4847   -207   -347    -14       O  
ATOM   1791  CB  TRP A 216      -2.672 -22.240  20.888  1.00 38.41           C  
ANISOU 1791  CB  TRP A 216     5034   5204   4355   -211   -366    -17       C  
ATOM   1792  CG  TRP A 216      -1.353 -22.083  21.564  1.00 34.76           C  
ANISOU 1792  CG  TRP A 216     4538   4773   3896   -244   -363      5       C  
ATOM   1793  CD1 TRP A 216      -0.148 -21.872  20.966  1.00 33.35           C  
ANISOU 1793  CD1 TRP A 216     4336   4618   3716   -256   -345     27       C  
ATOM   1794  CD2 TRP A 216      -1.101 -22.125  22.973  1.00 35.39           C  
ANISOU 1794  CD2 TRP A 216     4597   4873   3976   -268   -382      8       C  
ATOM   1795  NE1 TRP A 216       0.841 -21.775  21.911  1.00 34.69           N  
ANISOU 1795  NE1 TRP A 216     4463   4826   3892   -290   -355     40       N  
ATOM   1796  CE2 TRP A 216       0.282 -21.926  23.154  1.00 38.28           C  
ANISOU 1796  CE2 TRP A 216     4923   5277   4344   -295   -382     28       C  
ATOM   1797  CE3 TRP A 216      -1.910 -22.310  24.099  1.00 33.05           C  
ANISOU 1797  CE3 TRP A 216     4310   4572   3676   -268   -396     -3       C  
ATOM   1798  CZ2 TRP A 216       0.874 -21.904  24.420  1.00 35.93           C  
ANISOU 1798  CZ2 TRP A 216     4598   5012   4042   -320   -406     33       C  
ATOM   1799  CZ3 TRP A 216      -1.327 -22.284  25.347  1.00 35.71           C  
ANISOU 1799  CZ3 TRP A 216     4629   4937   4002   -290   -414      4       C  
ATOM   1800  CH2 TRP A 216       0.055 -22.084  25.500  1.00 37.01           C  
ANISOU 1800  CH2 TRP A 216     4758   5139   4167   -315   -424     21       C  
ATOM   1801  N   ASN A 217      -2.881 -18.702  20.647  1.00 43.15           N  
ANISOU 1801  N   ASN A 217     5735   5739   4920   -264   -366    -24       N  
ATOM   1802  CA  ASN A 217      -2.357 -17.549  19.926  1.00 44.83           C  
ANISOU 1802  CA  ASN A 217     5992   5923   5119   -288   -350     -8       C  
ATOM   1803  C   ASN A 217      -3.397 -16.969  18.979  1.00 43.79           C  
ANISOU 1803  C   ASN A 217     5923   5751   4965   -240   -352    -16       C  
ATOM   1804  O   ASN A 217      -3.063 -16.265  18.023  1.00 47.19           O  
ANISOU 1804  O   ASN A 217     6399   6154   5376   -243   -333      5       O  
ATOM   1805  CB  ASN A 217      -1.102 -17.953  19.148  1.00 48.69           C  
ANISOU 1805  CB  ASN A 217     6447   6443   5611   -307   -320     24       C  
ATOM   1806  CG  ASN A 217      -0.024 -16.930  19.233  1.00 52.29           C  
ANISOU 1806  CG  ASN A 217     6908   6892   6068   -377   -303     45       C  
ATOM   1807  OD1 ASN A 217       0.035 -16.003  18.428  1.00 55.93           O  
ANISOU 1807  OD1 ASN A 217     7424   7314   6512   -391   -282     62       O  
ATOM   1808  ND2 ASN A 217       0.853 -17.090  20.212  1.00 50.78           N  
ANISOU 1808  ND2 ASN A 217     6660   6738   5896   -425   -314     47       N  
ATOM   1809  N   VAL A 218      -4.662 -17.264  19.248  1.00 40.59           N  
ANISOU 1809  N   VAL A 218     5517   5346   4561   -194   -375    -45       N  
ATOM   1810  CA  VAL A 218      -5.734 -16.871  18.349  1.00 40.18           C  
ANISOU 1810  CA  VAL A 218     5507   5271   4487   -135   -387    -57       C  
ATOM   1811  C   VAL A 218      -5.911 -15.365  18.234  1.00 42.33           C  
ANISOU 1811  C   VAL A 218     5859   5489   4738   -129   -387    -52       C  
ATOM   1812  O   VAL A 218      -6.398 -14.894  17.217  1.00 44.35           O  
ANISOU 1812  O   VAL A 218     6166   5720   4967    -82   -392    -46       O  
ATOM   1813  CB  VAL A 218      -7.095 -17.525  18.705  1.00 39.24           C  
ANISOU 1813  CB  VAL A 218     5353   5176   4379    -92   -412    -92       C  
ATOM   1814  CG1 VAL A 218      -7.021 -19.040  18.541  1.00 40.09           C  
ANISOU 1814  CG1 VAL A 218     5404   5321   4508    -96   -413    -95       C  
ATOM   1815  CG2 VAL A 218      -7.560 -17.120  20.099  1.00 35.59           C  
ANISOU 1815  CG2 VAL A 218     4882   4714   3927   -103   -417   -110       C  
ATOM   1816  N   GLU A 219      -5.523 -14.613  19.261  1.00 43.35           N  
ANISOU 1816  N   GLU A 219     6006   5592   4872   -173   -385    -56       N  
ATOM   1817  CA  GLU A 219      -5.669 -13.156  19.220  1.00 46.69           C  
ANISOU 1817  CA  GLU A 219     6519   5947   5275   -170   -385    -54       C  
ATOM   1818  C   GLU A 219      -4.657 -12.474  18.298  1.00 47.44           C  
ANISOU 1818  C   GLU A 219     6667   6001   5356   -213   -358    -13       C  
ATOM   1819  O   GLU A 219      -4.959 -11.443  17.690  1.00 48.30           O  
ANISOU 1819  O   GLU A 219     6866   6048   5439   -187   -355      0       O  
ATOM   1820  CB  GLU A 219      -5.568 -12.553  20.617  1.00 47.74           C  
ANISOU 1820  CB  GLU A 219     6665   6059   5414   -206   -394    -79       C  
ATOM   1821  CG  GLU A 219      -6.344 -11.265  20.773  1.00 53.73           C  
ANISOU 1821  CG  GLU A 219     7517   6749   6150   -163   -405    -98       C  
ATOM   1822  CD  GLU A 219      -6.004 -10.542  22.058  1.00 60.69           C  
ANISOU 1822  CD  GLU A 219     8432   7598   7029   -210   -412   -124       C  
ATOM   1823  OE1 GLU A 219      -6.761 -10.688  23.044  1.00 62.07           O  
ANISOU 1823  OE1 GLU A 219     8587   7796   7199   -173   -423   -160       O  
ATOM   1824  OE2 GLU A 219      -4.974  -9.834  22.084  1.00 62.72           O  
ANISOU 1824  OE2 GLU A 219     8733   7808   7288   -286   -405   -109       O  
ATOM   1825  N   SER A 220      -3.460 -13.047  18.208  1.00 47.72           N  
ANISOU 1825  N   SER A 220     6648   6075   5408   -275   -336     11       N  
ATOM   1826  CA  SER A 220      -2.378 -12.460  17.417  1.00 47.48           C  
ANISOU 1826  CA  SER A 220     6650   6020   5369   -331   -299     54       C  
ATOM   1827  C   SER A 220      -2.159 -13.133  16.052  1.00 45.42           C  
ANISOU 1827  C   SER A 220     6377   5793   5088   -296   -271     83       C  
ATOM   1828  O   SER A 220      -1.490 -12.572  15.189  1.00 44.78           O  
ANISOU 1828  O   SER A 220     6339   5689   4988   -325   -233    123       O  
ATOM   1829  CB  SER A 220      -1.079 -12.423  18.231  1.00 48.68           C  
ANISOU 1829  CB  SER A 220     6750   6196   5551   -430   -289     61       C  
ATOM   1830  OG  SER A 220      -0.843 -13.667  18.865  1.00 51.78           O  
ANISOU 1830  OG  SER A 220     7044   6665   5966   -425   -302     46       O  
ATOM   1831  N   PHE A 221      -2.725 -14.323  15.849  1.00 44.79           N  
ANISOU 1831  N   PHE A 221     6244   5763   5009   -237   -288     62       N  
ATOM   1832  CA  PHE A 221      -2.669 -14.952  14.524  1.00 45.32           C  
ANISOU 1832  CA  PHE A 221     6315   5857   5049   -192   -269     79       C  
ATOM   1833  C   PHE A 221      -4.032 -15.295  13.919  1.00 44.03           C  
ANISOU 1833  C   PHE A 221     6178   5692   4861   -104   -306     51       C  
ATOM   1834  O   PHE A 221      -4.460 -14.652  12.961  1.00 45.58           O  
ANISOU 1834  O   PHE A 221     6448   5857   5014    -59   -306     66       O  
ATOM   1835  CB  PHE A 221      -1.720 -16.161  14.479  1.00 45.27           C  
ANISOU 1835  CB  PHE A 221     6225   5915   5061   -211   -246     85       C  
ATOM   1836  CG  PHE A 221      -1.595 -16.771  13.097  1.00 49.23           C  
ANISOU 1836  CG  PHE A 221     6740   6440   5525   -161   -222     98       C  
ATOM   1837  CD1 PHE A 221      -2.223 -17.978  12.789  1.00 47.87           C  
ANISOU 1837  CD1 PHE A 221     6543   6296   5350   -102   -248     65       C  
ATOM   1838  CD2 PHE A 221      -0.875 -16.122  12.095  1.00 48.75           C  
ANISOU 1838  CD2 PHE A 221     6725   6369   5427   -176   -173    142       C  
ATOM   1839  CE1 PHE A 221      -2.119 -18.531  11.513  1.00 46.72           C  
ANISOU 1839  CE1 PHE A 221     6421   6170   5162    -53   -230     69       C  
ATOM   1840  CE2 PHE A 221      -0.769 -16.673  10.809  1.00 47.85           C  
ANISOU 1840  CE2 PHE A 221     6632   6280   5267   -123   -148    152       C  
ATOM   1841  CZ  PHE A 221      -1.393 -17.875  10.522  1.00 45.54           C  
ANISOU 1841  CZ  PHE A 221     6317   6016   4968    -58   -179    112       C  
ATOM   1842  N   ALA A 222      -4.700 -16.310  14.473  1.00 41.89           N  
ANISOU 1842  N   ALA A 222     5845   5457   4615    -80   -337     13       N  
ATOM   1843  CA  ALA A 222      -5.927 -16.852  13.876  1.00 39.47           C  
ANISOU 1843  CA  ALA A 222     5540   5165   4292     -9   -375    -18       C  
ATOM   1844  C   ALA A 222      -7.043 -15.814  13.655  1.00 39.02           C  
ANISOU 1844  C   ALA A 222     5543   5073   4209     47   -405    -28       C  
ATOM   1845  O   ALA A 222      -7.549 -15.678  12.532  1.00 36.96           O  
ANISOU 1845  O   ALA A 222     5327   4809   3905    106   -422    -26       O  
ATOM   1846  CB  ALA A 222      -6.440 -18.035  14.671  1.00 37.56           C  
ANISOU 1846  CB  ALA A 222     5221   4960   4090    -12   -399    -54       C  
ATOM   1847  N   ILE A 223      -7.421 -15.087  14.705  1.00 37.44           N  
ANISOU 1847  N   ILE A 223     5349   4849   4029     36   -414    -39       N  
ATOM   1848  CA  ILE A 223      -8.496 -14.099  14.570  1.00 39.27           C  
ANISOU 1848  CA  ILE A 223     5636   5048   4236    102   -442    -51       C  
ATOM   1849  C   ILE A 223      -8.131 -13.010  13.557  1.00 39.13           C  
ANISOU 1849  C   ILE A 223     5725   4972   4170    123   -426    -10       C  
ATOM   1850  O   ILE A 223      -8.893 -12.780  12.632  1.00 39.72           O  
ANISOU 1850  O   ILE A 223     5843   5045   4205    201   -453    -11       O  
ATOM   1851  CB  ILE A 223      -8.907 -13.452  15.907  1.00 39.31           C  
ANISOU 1851  CB  ILE A 223     5639   5033   4265     94   -448    -73       C  
ATOM   1852  CG1 ILE A 223      -9.514 -14.489  16.839  1.00 39.98           C  
ANISOU 1852  CG1 ILE A 223     5626   5176   4387     87   -461   -110       C  
ATOM   1853  CG2 ILE A 223      -9.900 -12.304  15.677  1.00 39.72           C  
ANISOU 1853  CG2 ILE A 223     5763   5043   4286    176   -471    -81       C  
ATOM   1854  CD1 ILE A 223      -9.303 -14.136  18.307  1.00 44.11           C  
ANISOU 1854  CD1 ILE A 223     6139   5689   4932     45   -448   -121       C  
ATOM   1855  N   PRO A 224      -6.965 -12.349  13.721  1.00 39.64           N  
ANISOU 1855  N   PRO A 224     5833   4993   4237     51   -384     27       N  
ATOM   1856  CA  PRO A 224      -6.667 -11.287  12.765  1.00 39.78           C  
ANISOU 1856  CA  PRO A 224     5960   4946   4207     65   -363     72       C  
ATOM   1857  C   PRO A 224      -6.450 -11.798  11.343  1.00 42.11           C  
ANISOU 1857  C   PRO A 224     6272   5271   4457     98   -349     99       C  
ATOM   1858  O   PRO A 224      -6.791 -11.092  10.395  1.00 45.88           O  
ANISOU 1858  O   PRO A 224     6842   5710   4879    155   -353    126       O  
ATOM   1859  CB  PRO A 224      -5.395 -10.635  13.324  1.00 40.07           C  
ANISOU 1859  CB  PRO A 224     6018   4940   4266    -42   -317    103       C  
ATOM   1860  CG  PRO A 224      -4.797 -11.635  14.256  1.00 37.47           C  
ANISOU 1860  CG  PRO A 224     5576   4674   3987   -105   -313     80       C  
ATOM   1861  CD  PRO A 224      -5.935 -12.456  14.778  1.00 39.58           C  
ANISOU 1861  CD  PRO A 224     5779   4988   4271    -44   -358     30       C  
ATOM   1862  N   TYR A 225      -5.917 -13.013  11.191  1.00 43.24           N  
ANISOU 1862  N   TYR A 225     6334   5479   4616     71   -336     90       N  
ATOM   1863  CA  TYR A 225      -5.727 -13.588   9.856  1.00 42.29           C  
ANISOU 1863  CA  TYR A 225     6232   5391   4447    109   -324    106       C  
ATOM   1864  C   TYR A 225      -7.053 -13.881   9.149  1.00 44.17           C  
ANISOU 1864  C   TYR A 225     6486   5649   4647    210   -385     73       C  
ATOM   1865  O   TYR A 225      -7.218 -13.566   7.964  1.00 46.24           O  
ANISOU 1865  O   TYR A 225     6825   5902   4842    267   -387     95       O  
ATOM   1866  CB  TYR A 225      -4.827 -14.837   9.856  1.00 41.27           C  
ANISOU 1866  CB  TYR A 225     6019   5321   4341     67   -294    101       C  
ATOM   1867  CG  TYR A 225      -4.242 -15.083   8.478  1.00 43.64           C  
ANISOU 1867  CG  TYR A 225     6360   5640   4580     92   -256    132       C  
ATOM   1868  CD1 TYR A 225      -5.006 -15.662   7.463  1.00 44.96           C  
ANISOU 1868  CD1 TYR A 225     6553   5832   4696    175   -292    107       C  
ATOM   1869  CD2 TYR A 225      -2.947 -14.683   8.171  1.00 45.06           C  
ANISOU 1869  CD2 TYR A 225     6556   5815   4749     34   -183    185       C  
ATOM   1870  CE1 TYR A 225      -4.488 -15.855   6.192  1.00 45.19           C  
ANISOU 1870  CE1 TYR A 225     6632   5879   4658    205   -256    133       C  
ATOM   1871  CE2 TYR A 225      -2.419 -14.871   6.896  1.00 44.09           C  
ANISOU 1871  CE2 TYR A 225     6474   5714   4563     61   -138    217       C  
ATOM   1872  CZ  TYR A 225      -3.194 -15.456   5.917  1.00 45.80           C  
ANISOU 1872  CZ  TYR A 225     6726   5954   4723    151   -174    190       C  
ATOM   1873  OH  TYR A 225      -2.676 -15.638   4.656  1.00 49.52           O  
ANISOU 1873  OH  TYR A 225     7248   6449   5120    185   -129    219       O  
ATOM   1874  N   VAL A 226      -7.989 -14.497   9.865  1.00 43.53           N  
ANISOU 1874  N   VAL A 226     6332   5602   4606    230   -434     19       N  
ATOM   1875  CA  VAL A 226      -9.281 -14.831   9.274  1.00 44.59           C  
ANISOU 1875  CA  VAL A 226     6460   5768   4714    315   -498    -20       C  
ATOM   1876  C   VAL A 226     -10.013 -13.544   8.914  1.00 45.67           C  
ANISOU 1876  C   VAL A 226     6683   5861   4806    389   -524     -3       C  
ATOM   1877  O   VAL A 226     -10.539 -13.404   7.799  1.00 45.41           O  
ANISOU 1877  O   VAL A 226     6705   5838   4712    467   -557      0       O  
ATOM   1878  CB  VAL A 226     -10.128 -15.730  10.206  1.00 43.47           C  
ANISOU 1878  CB  VAL A 226     6212   5673   4632    306   -537    -77       C  
ATOM   1879  CG1 VAL A 226     -11.594 -15.723   9.800  1.00 45.59           C  
ANISOU 1879  CG1 VAL A 226     6466   5975   4883    390   -607   -117       C  
ATOM   1880  CG2 VAL A 226      -9.589 -17.144  10.191  1.00 42.65           C  
ANISOU 1880  CG2 VAL A 226     6044   5607   4554    260   -525    -95       C  
ATOM   1881  N   TYR A 227     -10.017 -12.602   9.857  1.00 45.18           N  
ANISOU 1881  N   TYR A 227     6644   5750   4773    370   -510      7       N  
ATOM   1882  CA  TYR A 227     -10.650 -11.304   9.659  1.00 45.97           C  
ANISOU 1882  CA  TYR A 227     6839   5794   4835    443   -529     24       C  
ATOM   1883  C   TYR A 227     -10.129 -10.634   8.379  1.00 48.72           C  
ANISOU 1883  C   TYR A 227     7309   6095   5109    470   -506     83       C  
ATOM   1884  O   TYR A 227     -10.916 -10.248   7.509  1.00 50.94           O  
ANISOU 1884  O   TYR A 227     7652   6374   5330    571   -548     88       O  
ATOM   1885  CB  TYR A 227     -10.431 -10.421  10.891  1.00 44.18           C  
ANISOU 1885  CB  TYR A 227     6633   5506   4647    400   -505     27       C  
ATOM   1886  CG  TYR A 227     -11.102  -9.070  10.824  1.00 44.55           C  
ANISOU 1886  CG  TYR A 227     6785   5482   4659    482   -524     40       C  
ATOM   1887  CD1 TYR A 227     -12.443  -8.918  11.184  1.00 44.57           C  
ANISOU 1887  CD1 TYR A 227     6756   5513   4666    578   -577     -4       C  
ATOM   1888  CD2 TYR A 227     -10.400  -7.943  10.403  1.00 41.79           C  
ANISOU 1888  CD2 TYR A 227     6569   5036   4274    464   -487     96       C  
ATOM   1889  CE1 TYR A 227     -13.066  -7.682  11.118  1.00 47.02           C  
ANISOU 1889  CE1 TYR A 227     7167   5757   4942    670   -596      6       C  
ATOM   1890  CE2 TYR A 227     -11.013  -6.702  10.336  1.00 46.87           C  
ANISOU 1890  CE2 TYR A 227     7325   5599   4883    546   -505    110       C  
ATOM   1891  CZ  TYR A 227     -12.347  -6.577  10.693  1.00 48.00           C  
ANISOU 1891  CZ  TYR A 227     7438   5773   5028    656   -561     63       C  
ATOM   1892  OH  TYR A 227     -12.964  -5.348  10.632  1.00 50.37           O  
ANISOU 1892  OH  TYR A 227     7852   5993   5291    754   -580     75       O  
ATOM   1893  N   ASN A 228      -8.808 -10.536   8.247  1.00 48.59           N  
ANISOU 1893  N   ASN A 228     7323   6049   5092    383   -438    129       N  
ATOM   1894  CA  ASN A 228      -8.209  -9.817   7.120  1.00 50.47           C  
ANISOU 1894  CA  ASN A 228     7680   6236   5260    393   -398    195       C  
ATOM   1895  C   ASN A 228      -8.340 -10.492   5.757  1.00 49.90           C  
ANISOU 1895  C   ASN A 228     7625   6218   5117    455   -411    201       C  
ATOM   1896  O   ASN A 228      -8.463  -9.814   4.728  1.00 51.71           O  
ANISOU 1896  O   ASN A 228     7967   6412   5267    518   -409    245       O  
ATOM   1897  CB  ASN A 228      -6.745  -9.500   7.410  1.00 52.26           C  
ANISOU 1897  CB  ASN A 228     7920   6425   5512    271   -317    243       C  
ATOM   1898  CG  ASN A 228      -6.564  -8.152   8.080  1.00 54.50           C  
ANISOU 1898  CG  ASN A 228     8288   6608   5813    231   -298    270       C  
ATOM   1899  OD1 ASN A 228      -6.810  -7.110   7.476  1.00 57.69           O  
ANISOU 1899  OD1 ASN A 228     8822   6936   6164    279   -294    312       O  
ATOM   1900  ND2 ASN A 228      -6.127  -8.167   9.330  1.00 54.86           N  
ANISOU 1900  ND2 ASN A 228     8269   6647   5928    146   -288    245       N  
ATOM   1901  N   ARG A 229      -8.305 -11.822   5.759  1.00 46.77           N  
ANISOU 1901  N   ARG A 229     7124   5901   4745    440   -425    156       N  
ATOM   1902  CA  ARG A 229      -8.400 -12.605   4.538  1.00 46.65           C  
ANISOU 1902  CA  ARG A 229     7121   5940   4665    493   -441    147       C  
ATOM   1903  C   ARG A 229      -9.801 -12.468   3.954  1.00 48.75           C  
ANISOU 1903  C   ARG A 229     7415   6225   4882    611   -529    115       C  
ATOM   1904  O   ARG A 229      -9.963 -12.272   2.746  1.00 49.72           O  
ANISOU 1904  O   ARG A 229     7624   6352   4915    683   -544    138       O  
ATOM   1905  CB  ARG A 229      -8.056 -14.075   4.813  1.00 45.53           C  
ANISOU 1905  CB  ARG A 229     6866   5865   4570    447   -438    100       C  
ATOM   1906  CG  ARG A 229      -7.983 -14.963   3.588  1.00 45.28           C  
ANISOU 1906  CG  ARG A 229     6851   5882   4471    493   -447     85       C  
ATOM   1907  CD  ARG A 229      -6.706 -14.775   2.783  1.00 45.86           C  
ANISOU 1907  CD  ARG A 229     6988   5946   4489    467   -359    147       C  
ATOM   1908  NE  ARG A 229      -6.777 -15.494   1.506  1.00 49.37           N  
ANISOU 1908  NE  ARG A 229     7473   6436   4850    533   -372    130       N  
ATOM   1909  CZ  ARG A 229      -6.047 -15.217   0.425  1.00 49.28           C  
ANISOU 1909  CZ  ARG A 229     7548   6424   4752    553   -311    183       C  
ATOM   1910  NH1 ARG A 229      -5.166 -14.224   0.427  1.00 48.29           N  
ANISOU 1910  NH1 ARG A 229     7477   6255   4617    503   -229    261       N  
ATOM   1911  NH2 ARG A 229      -6.196 -15.946  -0.667  1.00 48.89           N  
ANISOU 1911  NH2 ARG A 229     7533   6419   4622    620   -331    155       N  
ATOM   1912  N   ILE A 230     -10.803 -12.556   4.824  1.00 48.71           N  
ANISOU 1912  N   ILE A 230     7336   6239   4934    631   -587     64       N  
ATOM   1913  CA  ILE A 230     -12.190 -12.333   4.433  1.00 50.23           C  
ANISOU 1913  CA  ILE A 230     7534   6459   5091    742   -675     30       C  
ATOM   1914  C   ILE A 230     -12.368 -10.888   3.958  1.00 51.99           C  
ANISOU 1914  C   ILE A 230     7893   6611   5249    818   -673     87       C  
ATOM   1915  O   ILE A 230     -13.082 -10.640   2.991  1.00 51.43           O  
ANISOU 1915  O   ILE A 230     7881   6557   5101    924   -730     89       O  
ATOM   1916  CB  ILE A 230     -13.184 -12.686   5.583  1.00 48.68           C  
ANISOU 1916  CB  ILE A 230     7217   6304   4976    740   -723    -33       C  
ATOM   1917  CG1 ILE A 230     -13.116 -14.187   5.894  1.00 45.46           C  
ANISOU 1917  CG1 ILE A 230     6690   5961   4623    673   -730    -86       C  
ATOM   1918  CG2 ILE A 230     -14.610 -12.301   5.209  1.00 49.79           C  
ANISOU 1918  CG2 ILE A 230     7355   6480   5084    861   -810    -64       C  
ATOM   1919  CD1 ILE A 230     -14.044 -14.661   6.998  1.00 43.90           C  
ANISOU 1919  CD1 ILE A 230     6370   5808   4503    657   -767   -143       C  
ATOM   1920  N   LYS A 231     -11.694  -9.953   4.627  1.00 53.46           N  
ANISOU 1920  N   LYS A 231     8136   6714   5462    763   -612    133       N  
ATOM   1921  CA  LYS A 231     -11.750  -8.543   4.261  1.00 57.14           C  
ANISOU 1921  CA  LYS A 231     8748   7089   5872    822   -601    192       C  
ATOM   1922  C   LYS A 231     -11.204  -8.320   2.852  1.00 59.26           C  
ANISOU 1922  C   LYS A 231     9137   7339   6041    851   -572    255       C  
ATOM   1923  O   LYS A 231     -11.857  -7.675   2.031  1.00 60.58           O  
ANISOU 1923  O   LYS A 231     9405   7486   6128    964   -614    280       O  
ATOM   1924  CB  LYS A 231     -10.969  -7.691   5.260  1.00 58.64           C  
ANISOU 1924  CB  LYS A 231     8977   7187   6116    730   -535    225       C  
ATOM   1925  CG  LYS A 231     -11.230  -6.195   5.156  1.00 62.56           C  
ANISOU 1925  CG  LYS A 231     9625   7574   6571    793   -533    272       C  
ATOM   1926  CD  LYS A 231      -9.928  -5.409   4.996  1.00 68.85           C  
ANISOU 1926  CD  LYS A 231    10534   8272   7355    693   -444    349       C  
ATOM   1927  CE  LYS A 231      -9.530  -5.305   3.510  1.00 74.04           C  
ANISOU 1927  CE  LYS A 231    11296   8923   7914    726   -415    417       C  
ATOM   1928  NZ  LYS A 231      -8.089  -4.969   3.269  1.00 76.76           N  
ANISOU 1928  NZ  LYS A 231    11700   9212   8255    600   -313    488       N  
ATOM   1929  N   ASN A 232     -10.010  -8.847   2.578  1.00 59.53           N  
ANISOU 1929  N   ASN A 232     9159   7384   6075    756   -499    283       N  
ATOM   1930  CA  ASN A 232      -9.394  -8.711   1.250  1.00 59.62           C  
ANISOU 1930  CA  ASN A 232     9278   7387   5987    776   -455    345       C  
ATOM   1931  C   ASN A 232     -10.232  -9.329   0.126  1.00 59.49           C  
ANISOU 1931  C   ASN A 232     9272   7445   5886    892   -530    313       C  
ATOM   1932  O   ASN A 232     -10.387  -8.733  -0.939  1.00 62.23           O  
ANISOU 1932  O   ASN A 232     9748   7768   6129    975   -536    362       O  
ATOM   1933  CB  ASN A 232      -7.982  -9.312   1.234  1.00 58.87           C  
ANISOU 1933  CB  ASN A 232     9140   7312   5917    656   -361    369       C  
ATOM   1934  CG  ASN A 232      -7.020  -8.605   2.180  1.00 60.49           C  
ANISOU 1934  CG  ASN A 232     9346   7446   6192    535   -286    409       C  
ATOM   1935  OD1 ASN A 232      -7.291  -7.506   2.677  1.00 59.31           O  
ANISOU 1935  OD1 ASN A 232     9267   7210   6057    537   -292    431       O  
ATOM   1936  ND2 ASN A 232      -5.880  -9.241   2.431  1.00 58.78           N  
ANISOU 1936  ND2 ASN A 232     9051   7265   6018    430   -218    414       N  
ATOM   1937  N   ILE A 233     -10.772 -10.520   0.376  1.00 58.54           N  
ANISOU 1937  N   ILE A 233     9023   7412   5808    895   -589    230       N  
ATOM   1938  CA  ILE A 233     -11.520 -11.277  -0.628  1.00 57.73           C  
ANISOU 1938  CA  ILE A 233     8913   7387   5634    986   -668    184       C  
ATOM   1939  C   ILE A 233     -12.948 -10.755  -0.808  1.00 58.40           C  
ANISOU 1939  C   ILE A 233     9015   7487   5686   1112   -774    158       C  
ATOM   1940  O   ILE A 233     -13.438 -10.654  -1.935  1.00 57.74           O  
ANISOU 1940  O   ILE A 233     9009   7432   5500   1215   -828    164       O  
ATOM   1941  CB  ILE A 233     -11.532 -12.800  -0.299  1.00 55.71           C  
ANISOU 1941  CB  ILE A 233     8516   7211   5441    930   -691    104       C  
ATOM   1942  CG1 ILE A 233     -10.126 -13.392  -0.447  1.00 56.39           C  
ANISOU 1942  CG1 ILE A 233     8599   7296   5530    840   -593    131       C  
ATOM   1943  CG2 ILE A 233     -12.488 -13.559  -1.212  1.00 56.17           C  
ANISOU 1943  CG2 ILE A 233     8560   7346   5436   1018   -790     41       C  
ATOM   1944  CD1 ILE A 233      -9.981 -14.806   0.113  1.00 58.25           C  
ANISOU 1944  CD1 ILE A 233     8705   7586   5842    776   -601     61       C  
ATOM   1945  N   PHE A 234     -13.605 -10.420   0.298  1.00 57.34           N  
ANISOU 1945  N   PHE A 234     8810   7341   5635   1110   -803    128       N  
ATOM   1946  CA  PHE A 234     -15.027 -10.094   0.269  1.00 58.78           C  
ANISOU 1946  CA  PHE A 234     8969   7561   5803   1230   -907     89       C  
ATOM   1947  C   PHE A 234     -15.360  -8.633   0.555  1.00 60.51           C  
ANISOU 1947  C   PHE A 234     9288   7695   6006   1303   -904    139       C  
ATOM   1948  O   PHE A 234     -16.387  -8.126   0.091  1.00 62.08           O  
ANISOU 1948  O   PHE A 234     9524   7914   6150   1438   -984    133       O  
ATOM   1949  CB  PHE A 234     -15.786 -10.974   1.260  1.00 58.74           C  
ANISOU 1949  CB  PHE A 234     8788   7630   5901   1193   -956      2       C  
ATOM   1950  CG  PHE A 234     -15.825 -12.428   0.885  1.00 58.00           C  
ANISOU 1950  CG  PHE A 234     8601   7621   5817   1149   -989    -60       C  
ATOM   1951  CD1 PHE A 234     -14.934 -13.328   1.459  1.00 55.43           C  
ANISOU 1951  CD1 PHE A 234     8209   7294   5558   1024   -924    -73       C  
ATOM   1952  CD2 PHE A 234     -16.771 -12.902  -0.019  1.00 57.92           C  
ANISOU 1952  CD2 PHE A 234     8569   7690   5748   1235  -1090   -110       C  
ATOM   1953  CE1 PHE A 234     -14.970 -14.680   1.129  1.00 53.37           C  
ANISOU 1953  CE1 PHE A 234     7876   7097   5307    987   -953   -133       C  
ATOM   1954  CE2 PHE A 234     -16.817 -14.252  -0.353  1.00 59.92           C  
ANISOU 1954  CE2 PHE A 234     8746   8010   6010   1188  -1124   -175       C  
ATOM   1955  CZ  PHE A 234     -15.911 -15.144   0.224  1.00 55.95           C  
ANISOU 1955  CZ  PHE A 234     8189   7492   5576   1065  -1052   -185       C  
ATOM   1956  N   GLY A 235     -14.509  -7.966   1.331  1.00 59.91           N  
ANISOU 1956  N   GLY A 235     9258   7526   5979   1218   -817    186       N  
ATOM   1957  CA  GLY A 235     -14.777  -6.597   1.766  1.00 60.44           C  
ANISOU 1957  CA  GLY A 235     9425   7497   6043   1274   -809    226       C  
ATOM   1958  C   GLY A 235     -14.971  -6.528   3.269  1.00 58.28           C  
ANISOU 1958  C   GLY A 235     9054   7211   5878   1219   -798    182       C  
ATOM   1959  O   GLY A 235     -15.262  -7.535   3.912  1.00 56.01           O  
ANISOU 1959  O   GLY A 235     8613   7009   5662   1170   -819    115       O  
ATOM   1960  N   GLU A 236     -14.822  -5.331   3.821  1.00 59.56           N  
ANISOU 1960  N   GLU A 236     9316   7264   6049   1227   -764    219       N  
ATOM   1961  CA  GLU A 236     -14.868  -5.132   5.264  1.00 62.12           C  
ANISOU 1961  CA  GLU A 236     9575   7562   6465   1171   -743    182       C  
ATOM   1962  C   GLU A 236     -16.209  -5.480   5.923  1.00 62.94           C  
ANISOU 1962  C   GLU A 236     9548   7756   6611   1256   -816    105       C  
ATOM   1963  O   GLU A 236     -16.227  -6.138   6.969  1.00 64.26           O  
ANISOU 1963  O   GLU A 236     9586   7971   6859   1179   -803     54       O  
ATOM   1964  CB  GLU A 236     -14.433  -3.709   5.633  1.00 63.89           C  
ANISOU 1964  CB  GLU A 236     9956   7638   6680   1167   -695    236       C  
ATOM   1965  CG  GLU A 236     -14.354  -3.471   7.138  1.00 67.58           C  
ANISOU 1965  CG  GLU A 236    10372   8072   7233   1101   -669    196       C  
ATOM   1966  CD  GLU A 236     -13.292  -2.468   7.539  1.00 68.97           C  
ANISOU 1966  CD  GLU A 236    10680   8106   7420   1005   -597    247       C  
ATOM   1967  OE1 GLU A 236     -13.313  -1.327   7.023  1.00 69.27           O  
ANISOU 1967  OE1 GLU A 236    10889   8032   7401   1068   -590    301       O  
ATOM   1968  OE2 GLU A 236     -12.448  -2.828   8.391  1.00 69.02           O  
ANISOU 1968  OE2 GLU A 236    10621   8113   7492    865   -550    231       O  
ATOM   1969  N   SER A 237     -17.320  -5.062   5.322  1.00 62.20           N  
ANISOU 1969  N   SER A 237     9481   7689   6461   1413   -890     97       N  
ATOM   1970  CA  SER A 237     -18.629  -5.292   5.936  1.00 63.21           C  
ANISOU 1970  CA  SER A 237     9478   7909   6629   1500   -956     26       C  
ATOM   1971  C   SER A 237     -18.965  -6.784   6.051  1.00 61.15           C  
ANISOU 1971  C   SER A 237     9029   7786   6419   1436   -988    -40       C  
ATOM   1972  O   SER A 237     -19.733  -7.192   6.929  1.00 61.79           O  
ANISOU 1972  O   SER A 237     8972   7941   6565   1439  -1009    -99       O  
ATOM   1973  CB  SER A 237     -19.734  -4.536   5.194  1.00 64.83           C  
ANISOU 1973  CB  SER A 237     9745   8126   6760   1691  -1036     32       C  
ATOM   1974  OG  SER A 237     -19.940  -5.074   3.902  1.00 68.21           O  
ANISOU 1974  OG  SER A 237    10175   8624   7117   1739  -1094     39       O  
ATOM   1975  N   THR A 238     -18.379  -7.589   5.167  1.00 57.67           N  
ANISOU 1975  N   THR A 238     8589   7375   5948   1377   -987    -28       N  
ATOM   1976  CA  THR A 238     -18.532  -9.037   5.223  1.00 54.57           C  
ANISOU 1976  CA  THR A 238     8044   7090   5602   1303  -1010    -86       C  
ATOM   1977  C   THR A 238     -17.655  -9.608   6.341  1.00 53.92           C  
ANISOU 1977  C   THR A 238     7897   6987   5605   1150   -933    -94       C  
ATOM   1978  O   THR A 238     -18.079 -10.512   7.071  1.00 52.06           O  
ANISOU 1978  O   THR A 238     7517   6823   5438   1099   -944   -150       O  
ATOM   1979  CB  THR A 238     -18.201  -9.695   3.868  1.00 54.04           C  
ANISOU 1979  CB  THR A 238     8013   7056   5463   1304  -1037    -76       C  
ATOM   1980  OG1 THR A 238     -19.052  -9.147   2.851  1.00 53.89           O  
ANISOU 1980  OG1 THR A 238     8058   7063   5356   1453  -1118    -69       O  
ATOM   1981  CG2 THR A 238     -18.406 -11.205   3.932  1.00 51.36           C  
ANISOU 1981  CG2 THR A 238     7527   6816   5173   1228  -1066   -144       C  
ATOM   1982  N   ALA A 239     -16.446  -9.061   6.481  1.00 52.77           N  
ANISOU 1982  N   ALA A 239     7856   6742   5454   1078   -855    -37       N  
ATOM   1983  CA  ALA A 239     -15.543  -9.437   7.568  1.00 51.40           C  
ANISOU 1983  CA  ALA A 239     7632   6544   5354    943   -785    -39       C  
ATOM   1984  C   ALA A 239     -16.096  -9.036   8.934  1.00 50.99           C  
ANISOU 1984  C   ALA A 239     7524   6485   5363    948   -781    -72       C  
ATOM   1985  O   ALA A 239     -15.788  -9.673   9.939  1.00 50.28           O  
ANISOU 1985  O   ALA A 239     7345   6419   5339    855   -749    -98       O  
ATOM   1986  CB  ALA A 239     -14.159  -8.837   7.349  1.00 52.95           C  
ANISOU 1986  CB  ALA A 239     7948   6642   5527    868   -709     30       C  
ATOM   1987  N   LYS A 240     -16.920  -7.988   8.960  1.00 52.41           N  
ANISOU 1987  N   LYS A 240     7763   6636   5514   1065   -812    -71       N  
ATOM   1988  CA  LYS A 240     -17.582  -7.531  10.187  1.00 53.18           C  
ANISOU 1988  CA  LYS A 240     7815   6733   5657   1097   -809   -107       C  
ATOM   1989  C   LYS A 240     -18.639  -8.510  10.712  1.00 52.79           C  
ANISOU 1989  C   LYS A 240     7588   6812   5659   1110   -848   -174       C  
ATOM   1990  O   LYS A 240     -19.082  -8.406  11.863  1.00 52.40           O  
ANISOU 1990  O   LYS A 240     7474   6780   5654   1109   -831   -207       O  
ATOM   1991  CB  LYS A 240     -18.192  -6.143   9.985  1.00 54.01           C  
ANISOU 1991  CB  LYS A 240     8041   6770   5712   1237   -833    -88       C  
ATOM   1992  CG  LYS A 240     -17.162  -5.026   9.964  1.00 59.14           C  
ANISOU 1992  CG  LYS A 240     8867   7270   6333   1201   -778    -27       C  
ATOM   1993  CD  LYS A 240     -17.804  -3.678   9.689  1.00 65.69           C  
ANISOU 1993  CD  LYS A 240     9832   8019   7108   1349   -804     -5       C  
ATOM   1994  CE  LYS A 240     -16.787  -2.546   9.770  1.00 68.26           C  
ANISOU 1994  CE  LYS A 240    10341   8181   7412   1296   -746     53       C  
ATOM   1995  NZ  LYS A 240     -16.188  -2.446  11.126  1.00 71.30           N  
ANISOU 1995  NZ  LYS A 240    10705   8523   7863   1184   -694     27       N  
ATOM   1996  N   ARG A 241     -19.019  -9.470   9.873  1.00 51.93           N  
ANISOU 1996  N   ARG A 241     7403   6789   5540   1114   -897   -194       N  
ATOM   1997  CA  ARG A 241     -19.994 -10.496  10.244  1.00 53.18           C  
ANISOU 1997  CA  ARG A 241     7390   7067   5748   1106   -936   -257       C  
ATOM   1998  C   ARG A 241     -19.467 -11.482  11.289  1.00 50.36           C  
ANISOU 1998  C   ARG A 241     6941   6728   5465    967   -882   -275       C  
ATOM   1999  O   ARG A 241     -20.231 -12.291  11.820  1.00 51.19           O  
ANISOU 1999  O   ARG A 241     6909   6921   5620    944   -898   -321       O  
ATOM   2000  CB  ARG A 241     -20.499 -11.242   9.000  1.00 56.30           C  
ANISOU 2000  CB  ARG A 241     7743   7540   6109   1141  -1010   -278       C  
ATOM   2001  CG  ARG A 241     -21.536 -10.467   8.174  1.00 63.09           C  
ANISOU 2001  CG  ARG A 241     8633   8433   6907   1303  -1088   -282       C  
ATOM   2002  CD  ARG A 241     -21.843 -11.149   6.837  1.00 69.68           C  
ANISOU 2002  CD  ARG A 241     9452   9332   7690   1333  -1165   -300       C  
ATOM   2003  NE  ARG A 241     -22.227 -12.550   7.013  1.00 74.32           N  
ANISOU 2003  NE  ARG A 241     9885  10015   8337   1244  -1191   -360       N  
ATOM   2004  CZ  ARG A 241     -22.349 -13.443   6.032  1.00 76.22           C  
ANISOU 2004  CZ  ARG A 241    10099  10310   8550   1227  -1250   -388       C  
ATOM   2005  NH1 ARG A 241     -22.123 -13.101   4.767  1.00 77.05           N  
ANISOU 2005  NH1 ARG A 241    10318  10394   8562   1299  -1290   -362       N  
ATOM   2006  NH2 ARG A 241     -22.698 -14.690   6.323  1.00 76.53           N  
ANISOU 2006  NH2 ARG A 241    10004  10421   8653   1135  -1267   -444       N  
ATOM   2007  N   LEU A 242     -18.169 -11.418  11.581  1.00 48.57           N  
ANISOU 2007  N   LEU A 242     6788   6422   5243    873   -820   -236       N  
ATOM   2008  CA  LEU A 242     -17.582 -12.172  12.699  1.00 46.35           C  
ANISOU 2008  CA  LEU A 242     6438   6147   5025    754   -767   -246       C  
ATOM   2009  C   LEU A 242     -17.971 -11.566  14.053  1.00 46.02           C  
ANISOU 2009  C   LEU A 242     6375   6096   5014    767   -738   -263       C  
ATOM   2010  O   LEU A 242     -17.845 -12.217  15.096  1.00 46.73           O  
ANISOU 2010  O   LEU A 242     6388   6214   5152    690   -705   -280       O  
ATOM   2011  CB  LEU A 242     -16.057 -12.273  12.563  1.00 45.35           C  
ANISOU 2011  CB  LEU A 242     6389   5950   4893    657   -715   -201       C  
ATOM   2012  CG  LEU A 242     -15.509 -13.231  11.489  1.00 45.92           C  
ANISOU 2012  CG  LEU A 242     6457   6044   4947    618   -726   -192       C  
ATOM   2013  CD1 LEU A 242     -14.147 -12.788  10.983  1.00 46.05           C  
ANISOU 2013  CD1 LEU A 242     6582   5985   4929    574   -678   -136       C  
ATOM   2014  CD2 LEU A 242     -15.447 -14.677  11.972  1.00 40.35           C  
ANISOU 2014  CD2 LEU A 242     5638   5396   4296    534   -720   -224       C  
ATOM   2015  N   SER A 243     -18.426 -10.316  14.033  1.00 44.66           N  
ANISOU 2015  N   SER A 243     6281   5882   4807    871   -749   -257       N  
ATOM   2016  CA  SER A 243     -19.035  -9.698  15.205  1.00 45.39           C  
ANISOU 2016  CA  SER A 243     6352   5976   4917    915   -730   -283       C  
ATOM   2017  C   SER A 243     -20.550  -9.870  15.106  1.00 47.64           C  
ANISOU 2017  C   SER A 243     6525   6367   5208   1020   -778   -327       C  
ATOM   2018  O   SER A 243     -21.132  -9.557  14.069  1.00 49.26           O  
ANISOU 2018  O   SER A 243     6750   6591   5375   1118   -834   -325       O  
ATOM   2019  CB  SER A 243     -18.671  -8.219  15.280  1.00 44.34           C  
ANISOU 2019  CB  SER A 243     6376   5727   4743    974   -713   -256       C  
ATOM   2020  OG  SER A 243     -19.575  -7.507  16.105  1.00 46.05           O  
ANISOU 2020  OG  SER A 243     6583   5955   4961   1069   -712   -290       O  
ATOM   2021  N   PRO A 244     -21.197 -10.374  16.177  1.00 47.65           N  
ANISOU 2021  N   PRO A 244     6404   6445   5256    999   -756   -365       N  
ATOM   2022  CA  PRO A 244     -22.658 -10.526  16.127  1.00 48.73           C  
ANISOU 2022  CA  PRO A 244     6415   6696   5404   1092   -796   -407       C  
ATOM   2023  C   PRO A 244     -23.401  -9.185  16.143  1.00 50.96           C  
ANISOU 2023  C   PRO A 244     6756   6960   5647   1255   -814   -415       C  
ATOM   2024  O   PRO A 244     -24.628  -9.167  16.165  1.00 52.10           O  
ANISOU 2024  O   PRO A 244     6793   7204   5798   1350   -845   -450       O  
ATOM   2025  CB  PRO A 244     -22.974 -11.333  17.392  1.00 47.43           C  
ANISOU 2025  CB  PRO A 244     6122   6603   5296   1014   -747   -435       C  
ATOM   2026  CG  PRO A 244     -21.825 -11.073  18.308  1.00 46.89           C  
ANISOU 2026  CG  PRO A 244     6147   6442   5228    933   -684   -411       C  
ATOM   2027  CD  PRO A 244     -20.627 -10.924  17.421  1.00 46.02           C  
ANISOU 2027  CD  PRO A 244     6160   6236   5091    886   -695   -369       C  
ATOM   2028  N   HIS A 245     -22.656  -8.084  16.139  1.00 52.00           N  
ANISOU 2028  N   HIS A 245     7056   6964   5738   1284   -793   -382       N  
ATOM   2029  CA  HIS A 245     -23.232  -6.750  16.074  1.00 54.58           C  
ANISOU 2029  CA  HIS A 245     7473   7244   6020   1442   -810   -384       C  
ATOM   2030  C   HIS A 245     -22.650  -5.967  14.909  1.00 56.98           C  
ANISOU 2030  C   HIS A 245     7944   7440   6266   1488   -840   -334       C  
ATOM   2031  O   HIS A 245     -22.834  -4.754  14.824  1.00 57.58           O  
ANISOU 2031  O   HIS A 245     8145   7435   6299   1604   -846   -322       O  
ATOM   2032  CB  HIS A 245     -22.983  -5.980  17.370  1.00 55.11           C  
ANISOU 2032  CB  HIS A 245     7607   7240   6090   1445   -749   -396       C  
ATOM   2033  CG  HIS A 245     -23.259  -6.769  18.610  1.00 56.21           C  
ANISOU 2033  CG  HIS A 245     7611   7468   6279   1373   -702   -433       C  
ATOM   2034  ND1 HIS A 245     -24.379  -7.560  18.757  1.00 56.95           N  
ANISOU 2034  ND1 HIS A 245     7523   7710   6406   1399   -715   -468       N  
ATOM   2035  CD2 HIS A 245     -22.565  -6.877  19.767  1.00 52.04           C  
ANISOU 2035  CD2 HIS A 245     7103   6901   5767   1275   -642   -437       C  
ATOM   2036  CE1 HIS A 245     -24.355  -8.131  19.948  1.00 55.84           C  
ANISOU 2036  CE1 HIS A 245     7304   7614   6300   1318   -658   -488       C  
ATOM   2037  NE2 HIS A 245     -23.267  -7.730  20.582  1.00 53.88           N  
ANISOU 2037  NE2 HIS A 245     7178   7255   6039   1248   -615   -470       N  
ATOM   2038  N   ARG A 246     -21.939  -6.662  14.021  1.00 58.50           N  
ANISOU 2038  N   ARG A 246     8147   7628   6453   1398   -854   -305       N  
ATOM   2039  CA  ARG A 246     -21.319  -6.043  12.847  1.00 61.08           C  
ANISOU 2039  CA  ARG A 246     8627   7860   6718   1427   -873   -251       C  
ATOM   2040  C   ARG A 246     -20.492  -4.805  13.215  1.00 60.92           C  
ANISOU 2040  C   ARG A 246     8789   7683   6673   1422   -826   -213       C  
ATOM   2041  O   ARG A 246     -20.502  -3.803  12.495  1.00 61.66           O  
ANISOU 2041  O   ARG A 246     9026   7691   6709   1517   -845   -176       O  
ATOM   2042  CB  ARG A 246     -22.374  -5.675  11.783  1.00 64.31           C  
ANISOU 2042  CB  ARG A 246     9040   8320   7075   1591   -953   -253       C  
ATOM   2043  CG  ARG A 246     -23.494  -6.692  11.567  1.00 69.93           C  
ANISOU 2043  CG  ARG A 246     9559   9197   7814   1621  -1012   -306       C  
ATOM   2044  CD  ARG A 246     -23.052  -7.909  10.762  1.00 75.22           C  
ANISOU 2044  CD  ARG A 246    10173   9918   8491   1514  -1035   -304       C  
ATOM   2045  NE  ARG A 246     -24.052  -8.979  10.819  1.00 79.07           N  
ANISOU 2045  NE  ARG A 246    10467  10554   9022   1504  -1081   -362       N  
ATOM   2046  CZ  ARG A 246     -23.940 -10.090  11.550  1.00 77.82           C  
ANISOU 2046  CZ  ARG A 246    10185  10451   8933   1373  -1047   -391       C  
ATOM   2047  NH1 ARG A 246     -22.857 -10.313  12.287  1.00 73.57           N  
ANISOU 2047  NH1 ARG A 246     9690   9839   8424   1249   -972   -369       N  
ATOM   2048  NH2 ARG A 246     -24.913 -10.990  11.534  1.00 79.30           N  
ANISOU 2048  NH2 ARG A 246    10204  10767   9159   1364  -1092   -442       N  
ATOM   2049  N   LYS A 247     -19.798  -4.864  14.348  1.00 61.50           N  
ANISOU 2049  N   LYS A 247     8862   7717   6789   1313   -766   -223       N  
ATOM   2050  CA  LYS A 247     -18.857  -3.811  14.712  1.00 63.77           C  
ANISOU 2050  CA  LYS A 247     9316   7855   7060   1273   -723   -191       C  
ATOM   2051  C   LYS A 247     -17.548  -4.390  15.218  1.00 62.96           C  
ANISOU 2051  C   LYS A 247     9200   7725   6995   1091   -671   -177       C  
ATOM   2052  O   LYS A 247     -17.541  -5.295  16.059  1.00 63.41           O  
ANISOU 2052  O   LYS A 247     9130   7861   7099   1016   -654   -211       O  
ATOM   2053  CB  LYS A 247     -19.448  -2.848  15.745  1.00 66.52           C  
ANISOU 2053  CB  LYS A 247     9711   8157   7405   1363   -710   -228       C  
ATOM   2054  CG  LYS A 247     -18.548  -1.640  16.020  1.00 70.21           C  
ANISOU 2054  CG  LYS A 247    10373   8452   7850   1329   -675   -199       C  
ATOM   2055  CD  LYS A 247     -19.114  -0.728  17.098  1.00 75.94           C  
ANISOU 2055  CD  LYS A 247    11155   9129   8571   1419   -662   -245       C  
ATOM   2056  CE  LYS A 247     -18.040   0.198  17.677  1.00 77.42           C  
ANISOU 2056  CE  LYS A 247    11509   9153   8753   1329   -623   -232       C  
ATOM   2057  NZ  LYS A 247     -17.501   1.172  16.680  1.00 77.33           N  
ANISOU 2057  NZ  LYS A 247    11688   8997   8699   1343   -627   -170       N  
ATOM   2058  N   THR A 248     -16.447  -3.857  14.692  1.00 62.77           N  
ANISOU 2058  N   THR A 248     9308   7593   6948   1023   -647   -124       N  
ATOM   2059  CA  THR A 248     -15.099  -4.268  15.079  1.00 60.89           C  
ANISOU 2059  CA  THR A 248     9066   7326   6743    855   -600   -105       C  
ATOM   2060  C   THR A 248     -14.191  -3.052  15.255  1.00 63.05           C  
ANISOU 2060  C   THR A 248     9507   7449   7000    804   -566    -72       C  
ATOM   2061  O   THR A 248     -14.463  -1.978  14.704  1.00 62.83           O  
ANISOU 2061  O   THR A 248     9619   7327   6928    892   -577    -46       O  
ATOM   2062  CB  THR A 248     -14.450  -5.192  14.022  1.00 59.25           C  
ANISOU 2062  CB  THR A 248     8816   7167   6532    786   -598    -68       C  
ATOM   2063  OG1 THR A 248     -14.316  -4.488  12.778  1.00 59.39           O  
ANISOU 2063  OG1 THR A 248     8960   7115   6489    841   -606    -14       O  
ATOM   2064  CG2 THR A 248     -15.271  -6.456  13.813  1.00 56.72           C  
ANISOU 2064  CG2 THR A 248     8337   6985   6230    817   -634   -104       C  
ATOM   2065  N   ARG A 249     -13.119  -3.231  16.027  1.00 62.66           N  
ANISOU 2065  N   ARG A 249     9445   7376   6988    662   -528    -74       N  
ATOM   2066  CA  ARG A 249     -12.038  -2.250  16.109  1.00 63.50           C  
ANISOU 2066  CA  ARG A 249     9692   7349   7088    572   -495    -40       C  
ATOM   2067  C   ARG A 249     -10.676  -2.915  15.882  1.00 62.43           C  
ANISOU 2067  C   ARG A 249     9507   7235   6978    414   -460     -4       C  
ATOM   2068  O   ARG A 249     -10.324  -3.897  16.545  1.00 61.90           O  
ANISOU 2068  O   ARG A 249     9312   7255   6951    339   -453    -30       O  
ATOM   2069  CB  ARG A 249     -12.079  -1.470  17.435  1.00 64.48           C  
ANISOU 2069  CB  ARG A 249     9873   7402   7224    562   -490    -87       C  
ATOM   2070  CG  ARG A 249     -10.899  -0.511  17.639  1.00 69.25           C  
ANISOU 2070  CG  ARG A 249    10613   7868   7830    444   -460    -62       C  
ATOM   2071  CD  ARG A 249     -11.333   0.901  18.047  1.00 77.09           C  
ANISOU 2071  CD  ARG A 249    11776   8720   8794    519   -468    -82       C  
ATOM   2072  NE  ARG A 249     -11.638   1.020  19.475  1.00 82.42           N  
ANISOU 2072  NE  ARG A 249    12429   9403   9484    527   -475   -155       N  
ATOM   2073  CZ  ARG A 249     -12.849   1.256  19.981  1.00 84.18           C  
ANISOU 2073  CZ  ARG A 249    12649   9648   9687    675   -494   -205       C  
ATOM   2074  NH1 ARG A 249     -13.902   1.410  19.182  1.00 84.56           N  
ANISOU 2074  NH1 ARG A 249    12709   9716   9705    832   -516   -191       N  
ATOM   2075  NH2 ARG A 249     -13.007   1.344  21.296  1.00 84.48           N  
ANISOU 2075  NH2 ARG A 249    12671   9696   9733    671   -492   -270       N  
ATOM   2076  N   VAL A 250      -9.926  -2.366  14.931  1.00 63.39           N  
ANISOU 2076  N   VAL A 250     9733   7279   7074    370   -434     58       N  
ATOM   2077  CA  VAL A 250      -8.577  -2.827  14.611  1.00 64.04           C  
ANISOU 2077  CA  VAL A 250     9779   7377   7177    226   -392     99       C  
ATOM   2078  C   VAL A 250      -7.537  -2.008  15.393  1.00 67.02           C  
ANISOU 2078  C   VAL A 250    10227   7656   7580     96   -363    102       C  
ATOM   2079  O   VAL A 250      -7.427  -0.789  15.213  1.00 66.90           O  
ANISOU 2079  O   VAL A 250    10368   7510   7542     95   -352    127       O  
ATOM   2080  CB  VAL A 250      -8.298  -2.741  13.074  1.00 63.78           C  
ANISOU 2080  CB  VAL A 250     9812   7326   7095    245   -371    170       C  
ATOM   2081  CG1 VAL A 250      -6.920  -3.289  12.730  1.00 60.98           C  
ANISOU 2081  CG1 VAL A 250     9403   7004   6760    105   -319    210       C  
ATOM   2082  CG2 VAL A 250      -9.367  -3.484  12.288  1.00 61.01           C  
ANISOU 2082  CG2 VAL A 250     9402   7068   6713    376   -412    159       C  
ATOM   2083  N   LYS A 251      -6.797  -2.682  16.274  1.00 69.35           N  
ANISOU 2083  N   LYS A 251    10412   8014   7922    -12   -355     74       N  
ATOM   2084  CA  LYS A 251      -5.670  -2.066  16.971  1.00 72.60           C  
ANISOU 2084  CA  LYS A 251    10865   8358   8363   -154   -333     75       C  
ATOM   2085  C   LYS A 251      -4.392  -2.334  16.190  1.00 74.89           C  
ANISOU 2085  C   LYS A 251    11124   8666   8663   -274   -287    136       C  
ATOM   2086  O   LYS A 251      -4.085  -3.479  15.884  1.00 72.85           O  
ANISOU 2086  O   LYS A 251    10738   8521   8418   -287   -277    144       O  
ATOM   2087  CB  LYS A 251      -5.513  -2.627  18.389  1.00 72.49           C  
ANISOU 2087  CB  LYS A 251    10747   8410   8387   -204   -355     12       C  
ATOM   2088  CG  LYS A 251      -6.554  -2.192  19.415  1.00 73.15           C  
ANISOU 2088  CG  LYS A 251    10869   8466   8459   -114   -389    -53       C  
ATOM   2089  CD  LYS A 251      -6.055  -2.524  20.823  1.00 74.27           C  
ANISOU 2089  CD  LYS A 251    10940   8650   8630   -196   -402   -104       C  
ATOM   2090  CE  LYS A 251      -7.138  -3.166  21.691  1.00 76.16           C  
ANISOU 2090  CE  LYS A 251    11100   8972   8864    -98   -425   -160       C  
ATOM   2091  NZ  LYS A 251      -6.572  -4.151  22.673  1.00 71.35           N  
ANISOU 2091  NZ  LYS A 251    10365   8462   8282   -174   -431   -184       N  
ATOM   2092  N   VAL A 252      -3.645  -1.279  15.881  1.00 80.57           N  
ANISOU 2092  N   VAL A 252    11963   9273   9378   -361   -254    177       N  
ATOM   2093  CA  VAL A 252      -2.373  -1.408  15.170  1.00 85.39           C  
ANISOU 2093  CA  VAL A 252    12545   9900  10001   -486   -199    239       C  
ATOM   2094  C   VAL A 252      -1.200  -1.226  16.137  1.00 88.71           C  
ANISOU 2094  C   VAL A 252    12917  10317  10474   -651   -193    218       C  
ATOM   2095  O   VAL A 252      -1.219  -0.327  16.985  1.00 90.17           O  
ANISOU 2095  O   VAL A 252    13187  10405  10669   -692   -216    182       O  
ATOM   2096  CB  VAL A 252      -2.273  -0.398  13.999  1.00 87.43           C  
ANISOU 2096  CB  VAL A 252    12964  10042  10214   -483   -157    313       C  
ATOM   2097  CG1 VAL A 252      -1.087  -0.727  13.092  1.00 87.71           C  
ANISOU 2097  CG1 VAL A 252    12951  10124  10252   -589    -89    383       C  
ATOM   2098  CG2 VAL A 252      -3.571  -0.386  13.190  1.00 88.03           C  
ANISOU 2098  CG2 VAL A 252    13108  10108  10230   -303   -182    324       C  
ATOM   2099  N   ILE A 253      -0.188  -2.086  16.001  1.00 91.75           N  
ANISOU 2099  N   ILE A 253    13164  10809  10888   -738   -164    238       N  
ATOM   2100  CA  ILE A 253       0.988  -2.086  16.884  1.00 95.47           C  
ANISOU 2100  CA  ILE A 253    13555  11308  11410   -891   -165    218       C  
ATOM   2101  C   ILE A 253       2.283  -1.724  16.134  1.00 98.73           C  
ANISOU 2101  C   ILE A 253    13965  11711  11839  -1032    -99    285       C  
ATOM   2102  O   ILE A 253       2.658  -2.399  15.169  1.00 99.45           O  
ANISOU 2102  O   ILE A 253    13988  11881  11919  -1019    -52    335       O  
ATOM   2103  CB  ILE A 253       1.137  -3.455  17.633  1.00 94.22           C  
ANISOU 2103  CB  ILE A 253    13217  11301  11281   -876   -195    175       C  
ATOM   2104  CG1 ILE A 253       0.024  -3.640  18.681  1.00 92.93           C  
ANISOU 2104  CG1 ILE A 253    13059  11140  11110   -778   -255    104       C  
ATOM   2105  CG2 ILE A 253       2.539  -3.623  18.249  1.00 95.04           C  
ANISOU 2105  CG2 ILE A 253    13214  11464  11432  -1029   -189    171       C  
ATOM   2106  CD1 ILE A 253       0.329  -3.093  20.073  1.00 93.37           C  
ANISOU 2106  CD1 ILE A 253    13131  11158  11186   -855   -296     46       C  
ATOM   2107  N   GLU A 254       2.936  -0.647  16.588  1.00102.21           N  
ANISOU 2107  N   GLU A 254    14482  12051  12304  -1165    -95    284       N  
ATOM   2108  CA  GLU A 254       4.249  -0.174  16.087  1.00105.13           C  
ANISOU 2108  CA  GLU A 254    14841  12406  12700  -1332    -34    342       C  
ATOM   2109  C   GLU A 254       4.345  -0.164  14.528  1.00106.67           C  
ANISOU 2109  C   GLU A 254    15081  12595  12853  -1303     46    433       C  
ATOM   2110  O   GLU A 254       3.374   0.262  13.899  1.00105.63           O  
ANISOU 2110  O   GLU A 254    15088  12378  12669  -1187     47    455       O  
ATOM   2111  CB  GLU A 254       5.396  -0.903  16.809  1.00104.91           C  
ANISOU 2111  CB  GLU A 254    14623  12511  12727  -1446    -44    316       C  
ATOM   2112  CG  GLU A 254       5.226  -1.022  18.326  1.00105.44           C  
ANISOU 2112  CG  GLU A 254    14648  12595  12818  -1454   -127    226       C  
ATOM   2113  CD  GLU A 254       6.442  -1.617  19.025  1.00105.62           C  
ANISOU 2113  CD  GLU A 254    14494  12744  12891  -1573   -143    205       C  
ATOM   2114  OE1 GLU A 254       6.368  -2.786  19.468  1.00103.73           O  
ANISOU 2114  OE1 GLU A 254    14122  12634  12657  -1501   -173    177       O  
ATOM   2115  OE2 GLU A 254       7.469  -0.913  19.133  1.00105.71           O  
ANISOU 2115  OE2 GLU A 254    14501  12724  12938  -1738   -128    218       O  
ATOM   2116  N   ASN A 255       5.439  -0.586  13.868  1.00109.58           N  
ANISOU 2116  N   ASN A 255    15345  13053  13237  -1392    114    488       N  
ATOM   2117  CA  ASN A 255       6.731  -1.034  14.415  1.00112.07           C  
ANISOU 2117  CA  ASN A 255    15489  13479  13613  -1533    125    477       C  
ATOM   2118  C   ASN A 255       7.840  -0.770  13.393  1.00114.33           C  
ANISOU 2118  C   ASN A 255    15752  13786  13903  -1651    225    562       C  
ATOM   2119  O   ASN A 255       8.338  -1.708  12.763  1.00114.05           O  
ANISOU 2119  O   ASN A 255    15589  13884  13862  -1625    273    594       O  
ATOM   2120  CB  ASN A 255       6.702  -2.538  14.746  1.00111.02           C  
ANISOU 2120  CB  ASN A 255    15176  13515  13490  -1443     94    438       C  
ATOM   2121  CG  ASN A 255       7.949  -3.007  15.499  1.00112.07           C  
ANISOU 2121  CG  ASN A 255    15132  13765  13685  -1567     86    415       C  
ATOM   2122  OD1 ASN A 255       8.699  -2.204  16.058  1.00113.70           O  
ANISOU 2122  OD1 ASN A 255    15342  13927  13931  -1719     79    407       O  
ATOM   2123  ND2 ASN A 255       8.168  -4.317  15.517  1.00111.07           N  
ANISOU 2123  ND2 ASN A 255    14851  13786  13565  -1499     82    404       N  
ATOM   2124  N   MET A 256       8.225   0.499  13.237  1.00117.70           N  
ANISOU 2124  N   MET A 256    16305  14079  14339  -1781    260    600       N  
ATOM   2125  CA  MET A 256       9.225   0.934  12.237  1.00121.11           C  
ANISOU 2125  CA  MET A 256    16739  14508  14770  -1908    366    692       C  
ATOM   2126  C   MET A 256       8.817   0.519  10.815  1.00121.16           C  
ANISOU 2126  C   MET A 256    16793  14543  14701  -1780    437    765       C  
ATOM   2127  O   MET A 256       8.200   1.300  10.084  1.00121.87           O  
ANISOU 2127  O   MET A 256    17070  14500  14735  -1733    464    816       O  
ATOM   2128  CB  MET A 256      10.640   0.409  12.560  1.00122.42           C  
ANISOU 2128  CB  MET A 256    16689  14825  15001  -2054    395    691       C  
ATOM   2129  CG  MET A 256      10.990   0.300  14.045  1.00124.14           C  
ANISOU 2129  CG  MET A 256    16801  15083  15285  -2131    303    601       C  
ATOM   2130  SD  MET A 256      12.209  -0.996  14.395  1.00125.82           S  
ANISOU 2130  SD  MET A 256    16718  15537  15550  -2174    307    583       S  
ATOM   2131  CE  MET A 256      11.326  -2.490  13.932  1.00122.46           C  
ANISOU 2131  CE  MET A 256    16238  15222  15070  -1931    298    573       C  
ATOM   2132  N   TYR A 257       9.170  -0.713  10.440  1.00120.66           N  
ANISOU 2132  N   TYR A 257    16564  14650  14633  -1719    463    768       N  
ATOM   2133  CA  TYR A 257       8.771  -1.317   9.165  1.00119.84           C  
ANISOU 2133  CA  TYR A 257    16486  14595  14452  -1583    518    820       C  
ATOM   2134  C   TYR A 257       7.648  -2.336   9.380  1.00117.01           C  
ANISOU 2134  C   TYR A 257    16099  14292  14067  -1392    438    755       C  
ATOM   2135  O   TYR A 257       6.742  -2.454   8.553  1.00116.26           O  
ANISOU 2135  O   TYR A 257    16105  14167  13900  -1254    438    774       O  
ATOM   2136  CB  TYR A 257       9.964  -2.001   8.477  1.00120.95           C  
ANISOU 2136  CB  TYR A 257    16471  14885  14598  -1643    614    870       C  
ATOM   2137  CG  TYR A 257      11.233  -1.171   8.424  1.00124.80           C  
ANISOU 2137  CG  TYR A 257    16929  15358  15132  -1855    694    926       C  
ATOM   2138  CD1 TYR A 257      11.424  -0.207   7.428  1.00127.50           C  
ANISOU 2138  CD1 TYR A 257    17416  15599  15429  -1922    789   1020       C  
ATOM   2139  CD2 TYR A 257      12.248  -1.355   9.367  1.00125.87           C  
ANISOU 2139  CD2 TYR A 257    16889  15582  15353  -1991    675    887       C  
ATOM   2140  CE1 TYR A 257      12.591   0.558   7.379  1.00129.70           C  
ANISOU 2140  CE1 TYR A 257    17664  15862  15754  -2132    868   1075       C  
ATOM   2141  CE2 TYR A 257      13.418  -0.597   9.327  1.00128.15           C  
ANISOU 2141  CE2 TYR A 257    17136  15866  15689  -2197    745    935       C  
ATOM   2142  CZ  TYR A 257      13.582   0.356   8.331  1.00130.11           C  
ANISOU 2142  CZ  TYR A 257    17529  16010  15899  -2273    844   1029       C  
ATOM   2143  OH  TYR A 257      14.737   1.103   8.291  1.00131.71           O  
ANISOU 2143  OH  TYR A 257    17686  16205  16152  -2491    919   1079       O  
ATOM   2144  N   GLY A 258       7.723  -3.063  10.496  1.00115.16           N  
ANISOU 2144  N   GLY A 258    15728  14140  13889  -1390    368    678       N  
ATOM   2145  CA  GLY A 258       6.750  -4.104  10.841  1.00112.03           C  
ANISOU 2145  CA  GLY A 258    15285  13803  13478  -1231    295    614       C  
ATOM   2146  C   GLY A 258       5.394  -3.569  11.262  1.00109.72           C  
ANISOU 2146  C   GLY A 258    15132  13395  13163  -1137    220    573       C  
ATOM   2147  O   GLY A 258       5.279  -2.428  11.713  1.00111.04           O  
ANISOU 2147  O   GLY A 258    15413  13436  13343  -1204    203    571       O  
ATOM   2148  N   SER A 259       4.365  -4.400  11.102  1.00106.21           N  
ANISOU 2148  N   SER A 259    14677  12992  12685   -981    175    540       N  
ATOM   2149  CA  SER A 259       2.994  -4.033  11.455  1.00103.28           C  
ANISOU 2149  CA  SER A 259    14414  12537  12291   -871    105    498       C  
ATOM   2150  C   SER A 259       2.109  -5.267  11.631  1.00100.17           C  
ANISOU 2150  C   SER A 259    13936  12236  11890   -736     50    444       C  
ATOM   2151  O   SER A 259       1.839  -6.003  10.674  1.00 99.83           O  
ANISOU 2151  O   SER A 259    13875  12253  11804   -648     67    462       O  
ATOM   2152  CB  SER A 259       2.385  -3.090  10.408  1.00104.30           C  
ANISOU 2152  CB  SER A 259    14724  12551  12353   -812    131    554       C  
ATOM   2153  OG  SER A 259       1.104  -2.634  10.813  1.00102.95           O  
ANISOU 2153  OG  SER A 259    14654  12300  12164   -706     62    513       O  
ATOM   2154  N   ARG A 260       1.673  -5.479  12.870  1.00 96.07           N  
ANISOU 2154  N   ARG A 260    13369  11725  11409   -725    -16    376       N  
ATOM   2155  CA  ARG A 260       0.728  -6.539  13.211  1.00 91.30           C  
ANISOU 2155  CA  ARG A 260    12695  11192  10804   -609    -70    322       C  
ATOM   2156  C   ARG A 260      -0.513  -5.918  13.849  1.00 86.43           C  
ANISOU 2156  C   ARG A 260    12166  10497  10178   -534   -129    278       C  
ATOM   2157  O   ARG A 260      -0.440  -4.816  14.404  1.00 87.24           O  
ANISOU 2157  O   ARG A 260    12357  10501  10290   -588   -136    273       O  
ATOM   2158  CB  ARG A 260       1.383  -7.573  14.140  1.00 91.89           C  
ANISOU 2158  CB  ARG A 260    12612  11372  10931   -657    -86    285       C  
ATOM   2159  CG  ARG A 260       2.124  -6.986  15.335  1.00 95.68           C  
ANISOU 2159  CG  ARG A 260    13069  11828  11458   -777   -102    262       C  
ATOM   2160  CD  ARG A 260       3.464  -7.685  15.555  1.00 99.98           C  
ANISOU 2160  CD  ARG A 260    13470  12476  12041   -867    -76    273       C  
ATOM   2161  NE  ARG A 260       4.191  -7.148  16.710  1.00103.63           N  
ANISOU 2161  NE  ARG A 260    13902  12927  12547   -985   -102    247       N  
ATOM   2162  CZ  ARG A 260       4.994  -6.084  16.681  1.00105.69           C  
ANISOU 2162  CZ  ARG A 260    14207  13126  12823  -1112    -75    272       C  
ATOM   2163  NH1 ARG A 260       5.191  -5.412  15.550  1.00106.08           N  
ANISOU 2163  NH1 ARG A 260    14341  13117  12849  -1139    -13    333       N  
ATOM   2164  NH2 ARG A 260       5.601  -5.687  17.794  1.00105.68           N  
ANISOU 2164  NH2 ARG A 260    14172  13122  12860  -1216   -113    236       N  
ATOM   2165  N   GLU A 261      -1.651  -6.604  13.756  1.00 78.88           N  
ANISOU 2165  N   GLU A 261    11187   9582   9203   -410   -170    245       N  
ATOM   2166  CA  GLU A 261      -2.886  -6.069  14.327  1.00 72.71           C  
ANISOU 2166  CA  GLU A 261    10473   8742   8411   -325   -221    202       C  
ATOM   2167  C   GLU A 261      -3.669  -7.014  15.243  1.00 66.86           C  
ANISOU 2167  C   GLU A 261     9630   8079   7695   -267   -269    139       C  
ATOM   2168  O   GLU A 261      -3.478  -8.229  15.223  1.00 65.12           O  
ANISOU 2168  O   GLU A 261     9296   7955   7491   -266   -270    129       O  
ATOM   2169  CB  GLU A 261      -3.787  -5.420  13.254  1.00 74.43           C  
ANISOU 2169  CB  GLU A 261    10815   8896   8569   -217   -226    232       C  
ATOM   2170  CG  GLU A 261      -4.035  -6.216  11.975  1.00 76.29           C  
ANISOU 2170  CG  GLU A 261    11025   9199   8763   -143   -217    259       C  
ATOM   2171  CD  GLU A 261      -4.656  -5.358  10.867  1.00 78.75           C  
ANISOU 2171  CD  GLU A 261    11480   9434   9006    -55   -216    301       C  
ATOM   2172  OE1 GLU A 261      -4.010  -4.392  10.404  1.00 79.83           O  
ANISOU 2172  OE1 GLU A 261    11727   9483   9120   -112   -170    359       O  
ATOM   2173  OE2 GLU A 261      -5.795  -5.649  10.454  1.00 80.10           O  
ANISOU 2173  OE2 GLU A 261    11655   9635   9144     70   -263    279       O  
ATOM   2174  N   ILE A 262      -4.514  -6.421  16.080  1.00 61.86           N  
ANISOU 2174  N   ILE A 262     9044   7398   7062   -221   -305     97       N  
ATOM   2175  CA  ILE A 262      -5.411  -7.154  16.957  1.00 57.50           C  
ANISOU 2175  CA  ILE A 262     8410   6910   6526   -159   -344     41       C  
ATOM   2176  C   ILE A 262      -6.823  -6.656  16.686  1.00 54.80           C  
ANISOU 2176  C   ILE A 262     8135   6535   6151    -29   -374     22       C  
ATOM   2177  O   ILE A 262      -7.081  -5.446  16.730  1.00 55.60           O  
ANISOU 2177  O   ILE A 262     8356   6537   6230     -3   -377     25       O  
ATOM   2178  CB  ILE A 262      -5.041  -6.976  18.469  1.00 58.13           C  
ANISOU 2178  CB  ILE A 262     8464   6985   6636   -229   -356     -1       C  
ATOM   2179  CG1 ILE A 262      -3.791  -7.792  18.835  1.00 59.47           C  
ANISOU 2179  CG1 ILE A 262     8530   7224   6841   -336   -340      9       C  
ATOM   2180  CG2 ILE A 262      -6.177  -7.461  19.383  1.00 56.31           C  
ANISOU 2180  CG2 ILE A 262     8182   6804   6411   -149   -389    -55       C  
ATOM   2181  CD1 ILE A 262      -2.467  -7.070  18.682  1.00 62.94           C  
ANISOU 2181  CD1 ILE A 262     9007   7615   7292   -456   -311     43       C  
ATOM   2182  N   ILE A 263      -7.730  -7.586  16.393  1.00 50.90           N  
ANISOU 2182  N   ILE A 263     7562   6123   5654     53   -398      2       N  
ATOM   2183  CA  ILE A 263      -9.128  -7.237  16.145  1.00 49.94           C  
ANISOU 2183  CA  ILE A 263     7474   5995   5504    183   -432    -20       C  
ATOM   2184  C   ILE A 263      -9.935  -7.383  17.424  1.00 50.71           C  
ANISOU 2184  C   ILE A 263     7515   6127   5625    217   -453    -77       C  
ATOM   2185  O   ILE A 263      -9.814  -8.385  18.134  1.00 52.11           O  
ANISOU 2185  O   ILE A 263     7585   6381   5836    172   -451   -100       O  
ATOM   2186  CB  ILE A 263      -9.784  -8.112  15.034  1.00 49.75           C  
ANISOU 2186  CB  ILE A 263     7396   6046   5461    257   -454    -15       C  
ATOM   2187  CG1 ILE A 263      -8.846  -8.319  13.834  1.00 49.68           C  
ANISOU 2187  CG1 ILE A 263     7417   6031   5428    213   -425     39       C  
ATOM   2188  CG2 ILE A 263     -11.133  -7.520  14.594  1.00 47.74           C  
ANISOU 2188  CG2 ILE A 263     7190   5779   5170    394   -495    -29       C  
ATOM   2189  CD1 ILE A 263      -8.374  -7.032  13.153  1.00 52.57           C  
ANISOU 2189  CD1 ILE A 263     7930   6291   5754    209   -400     92       C  
ATOM   2190  N   THR A 264     -10.744  -6.374  17.732  1.00 50.94           N  
ANISOU 2190  N   THR A 264     7623   6099   5632    299   -468    -99       N  
ATOM   2191  CA  THR A 264     -11.755  -6.524  18.770  1.00 50.10           C  
ANISOU 2191  CA  THR A 264     7458   6040   5536    361   -483   -153       C  
ATOM   2192  C   THR A 264     -13.073  -6.869  18.088  1.00 48.29           C  
ANISOU 2192  C   THR A 264     7178   5877   5294    484   -515   -166       C  
ATOM   2193  O   THR A 264     -13.562  -6.119  17.247  1.00 48.19           O  
ANISOU 2193  O   THR A 264     7247   5818   5244    575   -534   -150       O  
ATOM   2194  CB  THR A 264     -11.888  -5.263  19.675  1.00 52.59           C  
ANISOU 2194  CB  THR A 264     7882   6263   5837    386   -480   -180       C  
ATOM   2195  OG1 THR A 264     -10.658  -5.046  20.382  1.00 51.71           O  
ANISOU 2195  OG1 THR A 264     7802   6104   5742    259   -459   -177       O  
ATOM   2196  CG2 THR A 264     -13.013  -5.445  20.698  1.00 51.71           C  
ANISOU 2196  CG2 THR A 264     7704   6215   5728    466   -488   -237       C  
ATOM   2197  N   LEU A 265     -13.613  -8.033  18.434  1.00 47.44           N  
ANISOU 2197  N   LEU A 265     6934   5877   5214    483   -523   -193       N  
ATOM   2198  CA  LEU A 265     -14.907  -8.471  17.933  1.00 46.04           C  
ANISOU 2198  CA  LEU A 265     6681   5780   5034    583   -557   -215       C  
ATOM   2199  C   LEU A 265     -15.980  -8.151  18.977  1.00 46.16           C  
ANISOU 2199  C   LEU A 265     6658   5829   5054    658   -557   -262       C  
ATOM   2200  O   LEU A 265     -16.055  -8.803  20.023  1.00 46.80           O  
ANISOU 2200  O   LEU A 265     6654   5964   5163    610   -535   -287       O  
ATOM   2201  CB  LEU A 265     -14.879  -9.971  17.602  1.00 42.93           C  
ANISOU 2201  CB  LEU A 265     6163   5479   4670    528   -564   -217       C  
ATOM   2202  CG  LEU A 265     -13.834 -10.525  16.618  1.00 42.79           C  
ANISOU 2202  CG  LEU A 265     6164   5447   4647    457   -558   -178       C  
ATOM   2203  CD1 LEU A 265     -13.923 -12.053  16.526  1.00 38.46           C  
ANISOU 2203  CD1 LEU A 265     5496   4987   4132    410   -565   -192       C  
ATOM   2204  CD2 LEU A 265     -13.952  -9.908  15.221  1.00 40.72           C  
ANISOU 2204  CD2 LEU A 265     5989   5147   4335    528   -582   -148       C  
ATOM   2205  N   PHE A 266     -16.784  -7.127  18.704  1.00 46.81           N  
ANISOU 2205  N   PHE A 266     6806   5875   5102    782   -578   -272       N  
ATOM   2206  CA  PHE A 266     -17.848  -6.726  19.617  1.00 48.32           C  
ANISOU 2206  CA  PHE A 266     6966   6103   5293    874   -574   -318       C  
ATOM   2207  C   PHE A 266     -18.913  -7.810  19.673  1.00 47.83           C  
ANISOU 2207  C   PHE A 266     6733   6181   5259    901   -588   -346       C  
ATOM   2208  O   PHE A 266     -19.382  -8.279  18.633  1.00 48.57           O  
ANISOU 2208  O   PHE A 266     6773   6327   5352    936   -627   -339       O  
ATOM   2209  CB  PHE A 266     -18.462  -5.387  19.194  1.00 50.91           C  
ANISOU 2209  CB  PHE A 266     7409   6360   5576   1017   -596   -319       C  
ATOM   2210  CG  PHE A 266     -17.602  -4.190  19.521  1.00 58.11           C  
ANISOU 2210  CG  PHE A 266     8493   7122   6462    992   -575   -304       C  
ATOM   2211  CD1 PHE A 266     -16.573  -3.793  18.668  1.00 60.43           C  
ANISOU 2211  CD1 PHE A 266     8902   7319   6741    929   -574   -252       C  
ATOM   2212  CD2 PHE A 266     -17.826  -3.451  20.683  1.00 62.57           C  
ANISOU 2212  CD2 PHE A 266     9110   7646   7018   1030   -552   -344       C  
ATOM   2213  CE1 PHE A 266     -15.777  -2.682  18.967  1.00 61.10           C  
ANISOU 2213  CE1 PHE A 266     9146   7263   6808    890   -554   -239       C  
ATOM   2214  CE2 PHE A 266     -17.033  -2.340  20.995  1.00 64.73           C  
ANISOU 2214  CE2 PHE A 266     9552   7774   7270    998   -538   -338       C  
ATOM   2215  CZ  PHE A 266     -16.007  -1.957  20.133  1.00 64.91           C  
ANISOU 2215  CZ  PHE A 266     9682   7696   7284    922   -540   -284       C  
ATOM   2216  N   GLY A 267     -19.278  -8.209  20.890  1.00 46.29           N  
ANISOU 2216  N   GLY A 267     6456   6046   5087    880   -555   -379       N  
ATOM   2217  CA  GLY A 267     -20.262  -9.266  21.104  1.00 46.04           C  
ANISOU 2217  CA  GLY A 267     6258   6146   5089    884   -556   -404       C  
ATOM   2218  C   GLY A 267     -19.635 -10.620  21.394  1.00 45.64           C  
ANISOU 2218  C   GLY A 267     6127   6136   5078    744   -536   -391       C  
ATOM   2219  O   GLY A 267     -20.345 -11.609  21.612  1.00 46.44           O  
ANISOU 2219  O   GLY A 267     6098   6337   5213    722   -531   -407       O  
ATOM   2220  N   ILE A 268     -18.305 -10.665  21.382  1.00 43.60           N  
ANISOU 2220  N   ILE A 268     5948   5801   4816    650   -523   -360       N  
ATOM   2221  CA  ILE A 268     -17.555 -11.866  21.766  1.00 42.14           C  
ANISOU 2221  CA  ILE A 268     5705   5642   4664    526   -502   -345       C  
ATOM   2222  C   ILE A 268     -16.529 -11.537  22.845  1.00 39.20           C  
ANISOU 2222  C   ILE A 268     5400   5213   4283    458   -467   -338       C  
ATOM   2223  O   ILE A 268     -15.973 -10.442  22.868  1.00 42.23           O  
ANISOU 2223  O   ILE A 268     5896   5510   4638    472   -467   -333       O  
ATOM   2224  CB  ILE A 268     -16.821 -12.511  20.556  1.00 42.05           C  
ANISOU 2224  CB  ILE A 268     5703   5614   4662    471   -527   -314       C  
ATOM   2225  CG1 ILE A 268     -17.814 -12.869  19.451  1.00 41.35           C  
ANISOU 2225  CG1 ILE A 268     5552   5583   4574    536   -572   -327       C  
ATOM   2226  CG2 ILE A 268     -16.057 -13.767  20.988  1.00 40.88           C  
ANISOU 2226  CG2 ILE A 268     5498   5489   4545    358   -505   -300       C  
ATOM   2227  CD1 ILE A 268     -17.170 -13.269  18.176  1.00 39.87           C  
ANISOU 2227  CD1 ILE A 268     5399   5373   4378    508   -599   -301       C  
ATOM   2228  N   SER A 269     -16.280 -12.482  23.736  1.00 35.34           N  
ANISOU 2228  N   SER A 269     4845   4769   3815    382   -439   -337       N  
ATOM   2229  CA  SER A 269     -15.192 -12.341  24.682  1.00 35.72           C  
ANISOU 2229  CA  SER A 269     4946   4773   3852    309   -417   -329       C  
ATOM   2230  C   SER A 269     -14.041 -13.281  24.300  1.00 35.85           C  
ANISOU 2230  C   SER A 269     4945   4783   3891    210   -421   -293       C  
ATOM   2231  O   SER A 269     -14.165 -14.500  24.409  1.00 35.62           O  
ANISOU 2231  O   SER A 269     4833   4811   3889    170   -414   -285       O  
ATOM   2232  CB  SER A 269     -15.682 -12.588  26.107  1.00 35.15           C  
ANISOU 2232  CB  SER A 269     4830   4753   3772    309   -382   -352       C  
ATOM   2233  OG  SER A 269     -16.577 -11.561  26.503  1.00 36.07           O  
ANISOU 2233  OG  SER A 269     4978   4866   3859    408   -373   -387       O  
ATOM   2234  N   VAL A 270     -12.937 -12.698  23.832  1.00 33.94           N  
ANISOU 2234  N   VAL A 270     4785   4471   3640    174   -431   -272       N  
ATOM   2235  CA  VAL A 270     -11.756 -13.457  23.437  1.00 33.63           C  
ANISOU 2235  CA  VAL A 270     4732   4429   3619     91   -431   -239       C  
ATOM   2236  C   VAL A 270     -10.835 -13.673  24.635  1.00 35.34           C  
ANISOU 2236  C   VAL A 270     4947   4646   3835     19   -417   -235       C  
ATOM   2237  O   VAL A 270     -10.427 -12.715  25.305  1.00 35.94           O  
ANISOU 2237  O   VAL A 270     5090   4677   3888      7   -417   -248       O  
ATOM   2238  CB  VAL A 270     -10.959 -12.753  22.307  1.00 32.82           C  
ANISOU 2238  CB  VAL A 270     4705   4260   3505     81   -442   -212       C  
ATOM   2239  CG1 VAL A 270      -9.718 -13.556  21.957  1.00 32.33           C  
ANISOU 2239  CG1 VAL A 270     4616   4208   3461      1   -434   -179       C  
ATOM   2240  CG2 VAL A 270     -11.823 -12.567  21.074  1.00 33.86           C  
ANISOU 2240  CG2 VAL A 270     4845   4392   3626    159   -462   -211       C  
ATOM   2241  N   LEU A 271     -10.522 -14.939  24.898  1.00 35.88           N  
ANISOU 2241  N   LEU A 271     4945   4764   3925    -27   -410   -220       N  
ATOM   2242  CA  LEU A 271      -9.578 -15.311  25.941  1.00 36.40           C  
ANISOU 2242  CA  LEU A 271     5003   4841   3987    -90   -403   -210       C  
ATOM   2243  C   LEU A 271      -8.555 -16.217  25.290  1.00 37.64           C  
ANISOU 2243  C   LEU A 271     5127   5007   4167   -139   -407   -176       C  
ATOM   2244  O   LEU A 271      -8.738 -17.440  25.216  1.00 36.90           O  
ANISOU 2244  O   LEU A 271     4976   4953   4094   -144   -401   -164       O  
ATOM   2245  CB  LEU A 271     -10.276 -16.052  27.080  1.00 34.65           C  
ANISOU 2245  CB  LEU A 271     4731   4674   3761    -83   -384   -221       C  
ATOM   2246  CG  LEU A 271     -11.427 -15.393  27.840  1.00 40.21           C  
ANISOU 2246  CG  LEU A 271     5446   5391   4439    -26   -368   -255       C  
ATOM   2247  CD1 LEU A 271     -12.022 -16.385  28.850  1.00 40.10           C  
ANISOU 2247  CD1 LEU A 271     5371   5442   4424    -33   -339   -252       C  
ATOM   2248  CD2 LEU A 271     -10.983 -14.114  28.537  1.00 39.37           C  
ANISOU 2248  CD2 LEU A 271     5427   5236   4295    -23   -375   -280       C  
ATOM   2249  N   ASP A 272      -7.490 -15.614  24.781  1.00 36.54           N  
ANISOU 2249  N   ASP A 272     5028   4831   4026   -174   -414   -160       N  
ATOM   2250  CA  ASP A 272      -6.450 -16.377  24.117  1.00 36.63           C  
ANISOU 2250  CA  ASP A 272     5006   4857   4055   -212   -411   -129       C  
ATOM   2251  C   ASP A 272      -5.833 -17.293  25.167  1.00 36.84           C  
ANISOU 2251  C   ASP A 272     4985   4925   4087   -247   -412   -120       C  
ATOM   2252  O   ASP A 272      -5.552 -16.859  26.299  1.00 38.27           O  
ANISOU 2252  O   ASP A 272     5182   5109   4251   -271   -420   -131       O  
ATOM   2253  CB  ASP A 272      -5.405 -15.435  23.524  1.00 37.05           C  
ANISOU 2253  CB  ASP A 272     5105   4868   4103   -251   -411   -112       C  
ATOM   2254  CG  ASP A 272      -4.475 -16.127  22.563  1.00 41.36           C  
ANISOU 2254  CG  ASP A 272     5617   5435   4665   -272   -399    -80       C  
ATOM   2255  OD1 ASP A 272      -4.274 -17.353  22.691  1.00 44.46           O  
ANISOU 2255  OD1 ASP A 272     5950   5871   5072   -270   -397    -71       O  
ATOM   2256  OD2 ASP A 272      -3.937 -15.437  21.674  1.00 46.92           O  
ANISOU 2256  OD2 ASP A 272     6358   6107   5363   -289   -388    -61       O  
ATOM   2257  N   TYR A 273      -5.643 -18.561  24.822  1.00 34.87           N  
ANISOU 2257  N   TYR A 273     4686   4706   3857   -246   -407   -100       N  
ATOM   2258  CA  TYR A 273      -5.202 -19.502  25.845  1.00 35.60           C  
ANISOU 2258  CA  TYR A 273     4742   4834   3951   -265   -408    -87       C  
ATOM   2259  C   TYR A 273      -3.757 -19.322  26.282  1.00 34.89           C  
ANISOU 2259  C   TYR A 273     4643   4759   3856   -308   -421    -71       C  
ATOM   2260  O   TYR A 273      -3.392 -19.699  27.393  1.00 36.15           O  
ANISOU 2260  O   TYR A 273     4787   4947   4001   -321   -432    -66       O  
ATOM   2261  CB  TYR A 273      -5.477 -20.957  25.474  1.00 36.15           C  
ANISOU 2261  CB  TYR A 273     4773   4921   4043   -247   -399    -72       C  
ATOM   2262  CG  TYR A 273      -5.769 -21.770  26.711  1.00 35.35           C  
ANISOU 2262  CG  TYR A 273     4654   4844   3935   -252   -394    -64       C  
ATOM   2263  CD1 TYR A 273      -4.736 -22.351  27.454  1.00 32.09           C  
ANISOU 2263  CD1 TYR A 273     4228   4452   3513   -268   -402    -39       C  
ATOM   2264  CD2 TYR A 273      -7.079 -21.912  27.170  1.00 36.30           C  
ANISOU 2264  CD2 TYR A 273     4771   4970   4053   -237   -379    -79       C  
ATOM   2265  CE1 TYR A 273      -5.005 -23.061  28.614  1.00 32.54           C  
ANISOU 2265  CE1 TYR A 273     4282   4527   3554   -268   -396    -26       C  
ATOM   2266  CE2 TYR A 273      -7.361 -22.632  28.315  1.00 36.57           C  
ANISOU 2266  CE2 TYR A 273     4795   5025   4075   -245   -365    -66       C  
ATOM   2267  CZ  TYR A 273      -6.318 -23.205  29.031  1.00 36.51           C  
ANISOU 2267  CZ  TYR A 273     4788   5030   4053   -259   -374    -37       C  
ATOM   2268  OH  TYR A 273      -6.604 -23.909  30.167  1.00 36.01           O  
ANISOU 2268  OH  TYR A 273     4728   4985   3970   -263   -359    -17       O  
ATOM   2269  N   ILE A 274      -2.940 -18.733  25.420  1.00 35.36           N  
ANISOU 2269  N   ILE A 274     4709   4804   3922   -331   -420    -61       N  
ATOM   2270  CA  ILE A 274      -1.576 -18.392  25.809  1.00 38.42           C  
ANISOU 2270  CA  ILE A 274     5078   5212   4310   -383   -433    -50       C  
ATOM   2271  C   ILE A 274      -1.617 -17.322  26.901  1.00 39.78           C  
ANISOU 2271  C   ILE A 274     5290   5367   4457   -416   -455    -78       C  
ATOM   2272  O   ILE A 274      -0.905 -17.407  27.897  1.00 42.36           O  
ANISOU 2272  O   ILE A 274     5596   5727   4771   -446   -480    -80       O  
ATOM   2273  CB  ILE A 274      -0.696 -18.005  24.579  1.00 40.41           C  
ANISOU 2273  CB  ILE A 274     5321   5456   4576   -407   -417    -30       C  
ATOM   2274  CG1 ILE A 274       0.775 -17.844  24.976  1.00 40.78           C  
ANISOU 2274  CG1 ILE A 274     5321   5544   4630   -466   -429    -16       C  
ATOM   2275  CG2 ILE A 274      -1.249 -16.781  23.835  1.00 38.61           C  
ANISOU 2275  CG2 ILE A 274     5163   5168   4340   -410   -405    -40       C  
ATOM   2276  CD1 ILE A 274       1.712 -17.756  23.770  1.00 41.00           C  
ANISOU 2276  CD1 ILE A 274     5319   5584   4674   -487   -400     12       C  
ATOM   2277  N   ASP A 275      -2.504 -16.348  26.732  1.00 42.70           N  
ANISOU 2277  N   ASP A 275     5723   5686   4815   -401   -450   -102       N  
ATOM   2278  CA  ASP A 275      -2.680 -15.287  27.712  1.00 42.30           C  
ANISOU 2278  CA  ASP A 275     5729   5608   4737   -420   -468   -136       C  
ATOM   2279  C   ASP A 275      -3.275 -15.805  29.008  1.00 41.04           C  
ANISOU 2279  C   ASP A 275     5562   5481   4549   -393   -475   -153       C  
ATOM   2280  O   ASP A 275      -2.853 -15.393  30.099  1.00 40.84           O  
ANISOU 2280  O   ASP A 275     5558   5466   4496   -422   -499   -173       O  
ATOM   2281  CB  ASP A 275      -3.519 -14.154  27.121  1.00 44.11           C  
ANISOU 2281  CB  ASP A 275     6033   5767   4958   -393   -457   -156       C  
ATOM   2282  CG  ASP A 275      -2.806 -13.453  25.973  1.00 47.73           C  
ANISOU 2282  CG  ASP A 275     6519   6184   5434   -432   -449   -135       C  
ATOM   2283  OD1 ASP A 275      -1.553 -13.380  26.006  1.00 45.82           O  
ANISOU 2283  OD1 ASP A 275     6248   5957   5204   -502   -456   -119       O  
ATOM   2284  OD2 ASP A 275      -3.493 -12.972  25.046  1.00 50.58           O  
ANISOU 2284  OD2 ASP A 275     6925   6499   5793   -391   -434   -131       O  
ATOM   2285  N   LEU A 276      -4.232 -16.726  28.898  1.00 38.03           N  
ANISOU 2285  N   LEU A 276     5153   5122   4175   -342   -453   -144       N  
ATOM   2286  CA  LEU A 276      -4.773 -17.358  30.094  1.00 37.92           C  
ANISOU 2286  CA  LEU A 276     5129   5145   4135   -321   -448   -148       C  
ATOM   2287  C   LEU A 276      -3.670 -18.133  30.804  1.00 36.70           C  
ANISOU 2287  C   LEU A 276     4939   5035   3971   -351   -470   -124       C  
ATOM   2288  O   LEU A 276      -3.505 -18.021  32.028  1.00 36.46           O  
ANISOU 2288  O   LEU A 276     4927   5028   3901   -358   -487   -136       O  
ATOM   2289  CB  LEU A 276      -5.950 -18.284  29.777  1.00 38.04           C  
ANISOU 2289  CB  LEU A 276     5113   5175   4167   -276   -418   -138       C  
ATOM   2290  CG  LEU A 276      -7.333 -17.704  29.472  1.00 39.69           C  
ANISOU 2290  CG  LEU A 276     5339   5365   4374   -230   -398   -166       C  
ATOM   2291  CD1 LEU A 276      -8.354 -18.842  29.382  1.00 38.45           C  
ANISOU 2291  CD1 LEU A 276     5132   5241   4237   -206   -372   -154       C  
ATOM   2292  CD2 LEU A 276      -7.774 -16.679  30.506  1.00 37.43           C  
ANISOU 2292  CD2 LEU A 276     5106   5072   4045   -212   -396   -202       C  
ATOM   2293  N   TYR A 277      -2.901 -18.900  30.033  1.00 33.75           N  
ANISOU 2293  N   TYR A 277     4516   4676   3630   -360   -471    -92       N  
ATOM   2294  CA  TYR A 277      -1.821 -19.692  30.610  1.00 34.16           C  
ANISOU 2294  CA  TYR A 277     4528   4774   3675   -374   -494    -66       C  
ATOM   2295  C   TYR A 277      -0.745 -18.833  31.289  1.00 36.34           C  
ANISOU 2295  C   TYR A 277     4809   5068   3929   -424   -535    -83       C  
ATOM   2296  O   TYR A 277      -0.276 -19.178  32.375  1.00 38.31           O  
ANISOU 2296  O   TYR A 277     5049   5360   4146   -426   -564    -80       O  
ATOM   2297  CB  TYR A 277      -1.197 -20.593  29.551  1.00 34.49           C  
ANISOU 2297  CB  TYR A 277     4520   4827   3756   -363   -484    -34       C  
ATOM   2298  CG  TYR A 277      -0.243 -21.640  30.083  1.00 29.36           C  
ANISOU 2298  CG  TYR A 277     3827   4226   3101   -352   -503     -2       C  
ATOM   2299  CD1 TYR A 277      -0.679 -22.945  30.324  1.00 24.76           C  
ANISOU 2299  CD1 TYR A 277     3242   3647   2519   -310   -488     24       C  
ATOM   2300  CD2 TYR A 277       1.102 -21.332  30.315  1.00 28.20           C  
ANISOU 2300  CD2 TYR A 277     3641   4122   2952   -383   -537      2       C  
ATOM   2301  CE1 TYR A 277       0.198 -23.916  30.802  1.00 30.01           C  
ANISOU 2301  CE1 TYR A 277     3878   4350   3176   -287   -507     56       C  
ATOM   2302  CE2 TYR A 277       1.990 -22.294  30.795  1.00 31.09           C  
ANISOU 2302  CE2 TYR A 277     3962   4540   3312   -359   -559     31       C  
ATOM   2303  CZ  TYR A 277       1.529 -23.582  31.033  1.00 31.32           C  
ANISOU 2303  CZ  TYR A 277     4001   4564   3335   -304   -544     59       C  
ATOM   2304  OH  TYR A 277       2.404 -24.534  31.492  1.00 32.70           O  
ANISOU 2304  OH  TYR A 277     4142   4783   3500   -268   -568     91       O  
ATOM   2305  N   LYS A 278      -0.360 -17.719  30.667  1.00 34.73           N  
ANISOU 2305  N   LYS A 278     4623   4832   3741   -466   -541   -102       N  
ATOM   2306  CA  LYS A 278       0.664 -16.858  31.269  1.00 36.97           C  
ANISOU 2306  CA  LYS A 278     4910   5128   4010   -530   -583   -123       C  
ATOM   2307  C   LYS A 278       0.200 -16.231  32.587  1.00 36.47           C  
ANISOU 2307  C   LYS A 278     4909   5055   3893   -532   -608   -164       C  
ATOM   2308  O   LYS A 278       0.992 -16.097  33.525  1.00 35.39           O  
ANISOU 2308  O   LYS A 278     4764   4957   3728   -566   -655   -178       O  
ATOM   2309  CB  LYS A 278       1.155 -15.787  30.293  1.00 36.73           C  
ANISOU 2309  CB  LYS A 278     4894   5053   4009   -587   -577   -129       C  
ATOM   2310  CG  LYS A 278       2.074 -16.334  29.220  1.00 40.75           C  
ANISOU 2310  CG  LYS A 278     5328   5594   4559   -601   -560    -89       C  
ATOM   2311  CD  LYS A 278       2.228 -15.360  28.069  1.00 42.45           C  
ANISOU 2311  CD  LYS A 278     5574   5756   4800   -643   -533    -86       C  
ATOM   2312  CE  LYS A 278       3.330 -15.798  27.114  1.00 44.34           C  
ANISOU 2312  CE  LYS A 278     5735   6041   5073   -666   -513    -47       C  
ATOM   2313  NZ  LYS A 278       3.655 -14.728  26.118  1.00 47.75           N  
ANISOU 2313  NZ  LYS A 278     6199   6423   5522   -724   -485    -39       N  
ATOM   2314  N   LYS A 279      -1.082 -15.875  32.667  1.00 35.95           N  
ANISOU 2314  N   LYS A 279     4903   4947   3811   -490   -579   -185       N  
ATOM   2315  CA  LYS A 279      -1.581 -15.213  33.865  1.00 37.79           C  
ANISOU 2315  CA  LYS A 279     5203   5169   3987   -481   -594   -229       C  
ATOM   2316  C   LYS A 279      -1.888 -16.188  34.995  1.00 38.66           C  
ANISOU 2316  C   LYS A 279     5300   5337   4052   -441   -593   -216       C  
ATOM   2317  O   LYS A 279      -1.599 -15.906  36.161  1.00 39.42           O  
ANISOU 2317  O   LYS A 279     5428   5456   4092   -451   -627   -242       O  
ATOM   2318  CB  LYS A 279      -2.809 -14.344  33.577  1.00 39.09           C  
ANISOU 2318  CB  LYS A 279     5437   5271   4146   -442   -561   -260       C  
ATOM   2319  CG  LYS A 279      -2.927 -13.197  34.564  1.00 42.04           C  
ANISOU 2319  CG  LYS A 279     5897   5611   4467   -452   -585   -317       C  
ATOM   2320  CD  LYS A 279      -4.326 -12.618  34.656  1.00 45.34           C  
ANISOU 2320  CD  LYS A 279     6376   5988   4861   -381   -548   -348       C  
ATOM   2321  CE  LYS A 279      -4.519 -11.868  35.992  1.00 44.69           C  
ANISOU 2321  CE  LYS A 279     6376   5898   4708   -370   -566   -405       C  
ATOM   2322  NZ  LYS A 279      -3.500 -10.788  36.213  1.00 47.88           N  
ANISOU 2322  NZ  LYS A 279     6841   6250   5100   -445   -621   -445       N  
ATOM   2323  N   PHE A 280      -2.443 -17.344  34.646  1.00 35.77           N  
ANISOU 2323  N   PHE A 280     4891   4992   3707   -398   -556   -175       N  
ATOM   2324  CA  PHE A 280      -3.004 -18.226  35.657  1.00 36.62           C  
ANISOU 2324  CA  PHE A 280     5003   5140   3772   -358   -539   -158       C  
ATOM   2325  C   PHE A 280      -2.184 -19.488  35.987  1.00 35.85           C  
ANISOU 2325  C   PHE A 280     4858   5093   3672   -355   -558   -110       C  
ATOM   2326  O   PHE A 280      -2.477 -20.166  36.961  1.00 33.53           O  
ANISOU 2326  O   PHE A 280     4579   4831   3332   -327   -549    -90       O  
ATOM   2327  CB  PHE A 280      -4.443 -18.595  35.284  1.00 35.55           C  
ANISOU 2327  CB  PHE A 280     4867   4988   3653   -314   -479   -151       C  
ATOM   2328  CG  PHE A 280      -5.379 -17.416  35.192  1.00 35.70           C  
ANISOU 2328  CG  PHE A 280     4935   4969   3662   -294   -460   -198       C  
ATOM   2329  CD1 PHE A 280      -6.310 -17.335  34.165  1.00 35.43           C  
ANISOU 2329  CD1 PHE A 280     4885   4907   3670   -267   -426   -199       C  
ATOM   2330  CD2 PHE A 280      -5.329 -16.388  36.130  1.00 35.04           C  
ANISOU 2330  CD2 PHE A 280     4916   4876   3521   -295   -480   -244       C  
ATOM   2331  CE1 PHE A 280      -7.183 -16.254  34.075  1.00 34.38           C  
ANISOU 2331  CE1 PHE A 280     4797   4742   3526   -233   -411   -241       C  
ATOM   2332  CE2 PHE A 280      -6.193 -15.307  36.049  1.00 33.84           C  
ANISOU 2332  CE2 PHE A 280     4818   4683   3357   -264   -461   -289       C  
ATOM   2333  CZ  PHE A 280      -7.122 -15.242  35.016  1.00 35.45           C  
ANISOU 2333  CZ  PHE A 280     5001   4861   3605   -228   -426   -285       C  
ATOM   2334  N   SER A 281      -1.160 -19.798  35.199  1.00 35.94           N  
ANISOU 2334  N   SER A 281     4815   5112   3726   -377   -580    -88       N  
ATOM   2335  CA  SER A 281      -0.463 -21.075  35.378  1.00 38.06           C  
ANISOU 2335  CA  SER A 281     5039   5424   3997   -354   -593    -39       C  
ATOM   2336  C   SER A 281       0.640 -21.043  36.436  1.00 39.37           C  
ANISOU 2336  C   SER A 281     5196   5648   4115   -366   -655    -40       C  
ATOM   2337  O   SER A 281       0.992 -22.088  36.984  1.00 37.63           O  
ANISOU 2337  O   SER A 281     4962   5465   3871   -329   -668     -1       O  
ATOM   2338  CB  SER A 281       0.083 -21.604  34.047  1.00 36.72           C  
ANISOU 2338  CB  SER A 281     4813   5247   3893   -354   -582    -13       C  
ATOM   2339  OG  SER A 281       1.227 -20.869  33.658  1.00 38.03           O  
ANISOU 2339  OG  SER A 281     4942   5431   4077   -399   -618    -28       O  
ATOM   2340  N   PHE A 282       1.166 -19.847  36.718  1.00 41.89           N  
ANISOU 2340  N   PHE A 282     5528   5970   4417   -416   -697    -86       N  
ATOM   2341  CA  PHE A 282       2.288 -19.636  37.659  1.00 44.09           C  
ANISOU 2341  CA  PHE A 282     5791   6309   4652   -440   -770   -100       C  
ATOM   2342  C   PHE A 282       3.534 -20.460  37.311  1.00 44.03           C  
ANISOU 2342  C   PHE A 282     5694   6360   4675   -432   -803    -60       C  
ATOM   2343  O   PHE A 282       4.196 -21.055  38.162  1.00 44.39           O  
ANISOU 2343  O   PHE A 282     5719   6468   4678   -405   -850    -42       O  
ATOM   2344  CB  PHE A 282       1.840 -19.792  39.121  1.00 45.32           C  
ANISOU 2344  CB  PHE A 282     6010   6491   4719   -406   -786   -108       C  
ATOM   2345  CG  PHE A 282       0.952 -18.678  39.581  1.00 49.77           C  
ANISOU 2345  CG  PHE A 282     6655   7011   5244   -420   -771   -164       C  
ATOM   2346  CD1 PHE A 282       1.485 -17.576  40.234  1.00 53.87           C  
ANISOU 2346  CD1 PHE A 282     7211   7535   5722   -468   -830   -223       C  
ATOM   2347  CD2 PHE A 282      -0.415 -18.706  39.319  1.00 50.65           C  
ANISOU 2347  CD2 PHE A 282     6806   7076   5362   -386   -698   -162       C  
ATOM   2348  CE1 PHE A 282       0.662 -16.528  40.643  1.00 56.17           C  
ANISOU 2348  CE1 PHE A 282     7589   7778   5975   -471   -814   -279       C  
ATOM   2349  CE2 PHE A 282      -1.240 -17.664  39.716  1.00 50.83           C  
ANISOU 2349  CE2 PHE A 282     6901   7062   5349   -384   -681   -215       C  
ATOM   2350  CZ  PHE A 282      -0.702 -16.575  40.383  1.00 52.77           C  
ANISOU 2350  CZ  PHE A 282     7195   7305   5550   -422   -737   -274       C  
ATOM   2351  N   THR A 283       3.819 -20.492  36.020  1.00 45.18           N  
ANISOU 2351  N   THR A 283     5789   6488   4892   -448   -775    -47       N  
ATOM   2352  CA  THR A 283       5.045 -21.060  35.510  1.00 46.58           C  
ANISOU 2352  CA  THR A 283     5872   6721   5104   -444   -797    -17       C  
ATOM   2353  C   THR A 283       5.735 -19.944  34.751  1.00 48.38           C  
ANISOU 2353  C   THR A 283     6060   6945   5375   -526   -806    -46       C  
ATOM   2354  O   THR A 283       5.128 -18.903  34.477  1.00 51.31           O  
ANISOU 2354  O   THR A 283     6489   7253   5754   -573   -786    -80       O  
ATOM   2355  CB  THR A 283       4.762 -22.204  34.532  1.00 46.63           C  
ANISOU 2355  CB  THR A 283     5857   6706   5153   -384   -743     29       C  
ATOM   2356  OG1 THR A 283       4.035 -21.687  33.407  1.00 46.66           O  
ANISOU 2356  OG1 THR A 283     5884   6643   5199   -408   -689     15       O  
ATOM   2357  CG2 THR A 283       3.966 -23.343  35.215  1.00 41.33           C  
ANISOU 2357  CG2 THR A 283     5237   6021   4445   -314   -724     62       C  
ATOM   2358  N   ASN A 284       7.013 -20.133  34.459  1.00 48.04           N  
ANISOU 2358  N   ASN A 284     5921   6972   5360   -544   -836    -32       N  
ATOM   2359  CA  ASN A 284       7.652 -19.373  33.411  1.00 46.77           C  
ANISOU 2359  CA  ASN A 284     5709   6807   5254   -614   -818    -39       C  
ATOM   2360  C   ASN A 284       8.353 -20.362  32.494  1.00 45.97           C  
ANISOU 2360  C   ASN A 284     5517   6755   5194   -565   -789      6       C  
ATOM   2361  O   ASN A 284       9.280 -21.060  32.897  1.00 44.12           O  
ANISOU 2361  O   ASN A 284     5205   6606   4954   -529   -828     26       O  
ATOM   2362  CB  ASN A 284       8.603 -18.307  33.953  1.00 48.33           C  
ANISOU 2362  CB  ASN A 284     5870   7045   5447   -713   -881    -79       C  
ATOM   2363  CG  ASN A 284       8.894 -17.212  32.923  1.00 49.15           C  
ANISOU 2363  CG  ASN A 284     5964   7107   5602   -807   -849    -92       C  
ATOM   2364  OD1 ASN A 284       8.403 -17.265  31.795  1.00 45.81           O  
ANISOU 2364  OD1 ASN A 284     5562   6632   5212   -789   -781    -69       O  
ATOM   2365  ND2 ASN A 284       9.690 -16.216  33.311  1.00 48.66           N  
ANISOU 2365  ND2 ASN A 284     5878   7068   5545   -911   -900   -128       N  
ATOM   2366  N   GLN A 285       7.872 -20.434  31.261  1.00 44.35           N  
ANISOU 2366  N   GLN A 285     5328   6495   5025   -553   -721     22       N  
ATOM   2367  CA  GLN A 285       8.306 -21.463  30.342  1.00 43.53           C  
ANISOU 2367  CA  GLN A 285     5165   6423   4953   -488   -683     61       C  
ATOM   2368  C   GLN A 285       9.429 -20.975  29.447  1.00 43.59           C  
ANISOU 2368  C   GLN A 285     5080   6480   5001   -542   -666     67       C  
ATOM   2369  O   GLN A 285       9.467 -19.802  29.091  1.00 44.70           O  
ANISOU 2369  O   GLN A 285     5236   6591   5158   -632   -655     48       O  
ATOM   2370  CB  GLN A 285       7.122 -21.957  29.508  1.00 43.08           C  
ANISOU 2370  CB  GLN A 285     5179   6284   4904   -437   -623     72       C  
ATOM   2371  CG  GLN A 285       5.968 -22.535  30.333  1.00 45.12           C  
ANISOU 2371  CG  GLN A 285     5518   6498   5128   -389   -628     70       C  
ATOM   2372  CD  GLN A 285       6.296 -23.873  30.998  1.00 46.80           C  
ANISOU 2372  CD  GLN A 285     5710   6751   5320   -310   -650    102       C  
ATOM   2373  OE1 GLN A 285       7.434 -24.339  30.974  1.00 46.32           O  
ANISOU 2373  OE1 GLN A 285     5571   6760   5268   -283   -672    122       O  
ATOM   2374  NE2 GLN A 285       5.284 -24.494  31.596  1.00 48.90           N  
ANISOU 2374  NE2 GLN A 285     6047   6974   5559   -271   -642    111       N  
ATOM   2375  N   PRO A 286      10.363 -21.875  29.098  1.00 43.72           N  
ANISOU 2375  N   PRO A 286     5003   6576   5035   -485   -660     97       N  
ATOM   2376  CA  PRO A 286      11.406 -21.576  28.119  1.00 43.95           C  
ANISOU 2376  CA  PRO A 286     4934   6663   5103   -522   -626    111       C  
ATOM   2377  C   PRO A 286      10.822 -21.271  26.745  1.00 42.75           C  
ANISOU 2377  C   PRO A 286     4834   6439   4970   -532   -547    119       C  
ATOM   2378  O   PRO A 286      11.393 -20.493  25.989  1.00 45.42           O  
ANISOU 2378  O   PRO A 286     5131   6793   5333   -603   -513    123       O  
ATOM   2379  CB  PRO A 286      12.207 -22.881  28.047  1.00 45.15           C  
ANISOU 2379  CB  PRO A 286     4998   6899   5258   -417   -628    142       C  
ATOM   2380  CG  PRO A 286      11.924 -23.587  29.306  1.00 42.27           C  
ANISOU 2380  CG  PRO A 286     4668   6539   4854   -355   -690    142       C  
ATOM   2381  CD  PRO A 286      10.537 -23.209  29.703  1.00 41.89           C  
ANISOU 2381  CD  PRO A 286     4751   6385   4780   -379   -687    122       C  
ATOM   2382  N   SER A 287       9.687 -21.881  26.436  1.00 41.31           N  
ANISOU 2382  N   SER A 287     4743   6180   4774   -463   -520    121       N  
ATOM   2383  CA  SER A 287       9.055 -21.732  25.133  1.00 39.55           C  
ANISOU 2383  CA  SER A 287     4574   5892   4560   -455   -455    127       C  
ATOM   2384  C   SER A 287       7.549 -21.760  25.286  1.00 37.65           C  
ANISOU 2384  C   SER A 287     4449   5556   4301   -433   -455    109       C  
ATOM   2385  O   SER A 287       7.032 -22.362  26.223  1.00 38.50           O  
ANISOU 2385  O   SER A 287     4585   5653   4390   -394   -489    104       O  
ATOM   2386  CB  SER A 287       9.485 -22.872  24.217  1.00 38.11           C  
ANISOU 2386  CB  SER A 287     4349   5745   4387   -365   -412    152       C  
ATOM   2387  OG  SER A 287       8.889 -22.738  22.940  1.00 43.93           O  
ANISOU 2387  OG  SER A 287     5143   6425   5124   -355   -354    154       O  
ATOM   2388  N   TYR A 288       6.850 -21.111  24.363  1.00 38.21           N  
ANISOU 2388  N   TYR A 288     4582   5562   4375   -455   -416    103       N  
ATOM   2389  CA  TYR A 288       5.385 -21.139  24.341  1.00 37.78           C  
ANISOU 2389  CA  TYR A 288     4623   5427   4305   -427   -413     85       C  
ATOM   2390  C   TYR A 288       4.821 -21.687  23.039  1.00 37.69           C  
ANISOU 2390  C   TYR A 288     4644   5381   4296   -371   -368     93       C  
ATOM   2391  O   TYR A 288       3.729 -21.317  22.616  1.00 38.39           O  
ANISOU 2391  O   TYR A 288     4803   5407   4377   -367   -359     78       O  
ATOM   2392  CB  TYR A 288       4.798 -19.759  24.673  1.00 39.03           C  
ANISOU 2392  CB  TYR A 288     4845   5530   4455   -494   -426     61       C  
ATOM   2393  CG  TYR A 288       5.076 -19.349  26.100  1.00 36.04           C  
ANISOU 2393  CG  TYR A 288     4457   5174   4062   -537   -479     42       C  
ATOM   2394  CD1 TYR A 288       6.180 -18.573  26.403  1.00 33.61           C  
ANISOU 2394  CD1 TYR A 288     4101   4907   3764   -615   -501     38       C  
ATOM   2395  CD2 TYR A 288       4.251 -19.771  27.149  1.00 32.77           C  
ANISOU 2395  CD2 TYR A 288     4082   4746   3624   -502   -507     27       C  
ATOM   2396  CE1 TYR A 288       6.465 -18.206  27.700  1.00 36.81           C  
ANISOU 2396  CE1 TYR A 288     4500   5336   4151   -655   -557     14       C  
ATOM   2397  CE2 TYR A 288       4.529 -19.408  28.467  1.00 33.92           C  
ANISOU 2397  CE2 TYR A 288     4226   4916   3745   -534   -556      7       C  
ATOM   2398  CZ  TYR A 288       5.644 -18.622  28.727  1.00 33.98           C  
ANISOU 2398  CZ  TYR A 288     4189   4963   3760   -610   -586     -2       C  
ATOM   2399  OH  TYR A 288       5.967 -18.248  30.002  1.00 35.78           O  
ANISOU 2399  OH  TYR A 288     4417   5218   3959   -645   -643    -27       O  
ATOM   2400  N   SER A 289       5.562 -22.585  22.407  1.00 39.43           N  
ANISOU 2400  N   SER A 289     4813   5645   4524   -322   -344    112       N  
ATOM   2401  CA  SER A 289       4.965 -23.387  21.349  1.00 42.85           C  
ANISOU 2401  CA  SER A 289     5286   6044   4952   -256   -313    111       C  
ATOM   2402  C   SER A 289       3.941 -24.321  22.008  1.00 40.81           C  
ANISOU 2402  C   SER A 289     5072   5745   4690   -212   -339     98       C  
ATOM   2403  O   SER A 289       4.135 -24.772  23.136  1.00 39.52           O  
ANISOU 2403  O   SER A 289     4888   5603   4527   -205   -371    104       O  
ATOM   2404  CB  SER A 289       6.027 -24.193  20.587  1.00 43.18           C  
ANISOU 2404  CB  SER A 289     5269   6142   4997   -203   -279    131       C  
ATOM   2405  OG  SER A 289       6.524 -25.272  21.367  1.00 46.35           O  
ANISOU 2405  OG  SER A 289     5627   6579   5403   -150   -303    140       O  
ATOM   2406  N   LEU A 290       2.847 -24.588  21.315  1.00 41.08           N  
ANISOU 2406  N   LEU A 290     5165   5724   4719   -186   -328     82       N  
ATOM   2407  CA  LEU A 290       1.879 -25.541  21.817  1.00 41.67           C  
ANISOU 2407  CA  LEU A 290     5275   5760   4796   -154   -346     71       C  
ATOM   2408  C   LEU A 290       2.525 -26.913  22.029  1.00 42.44           C  
ANISOU 2408  C   LEU A 290     5350   5875   4899    -96   -347     87       C  
ATOM   2409  O   LEU A 290       2.195 -27.613  22.991  1.00 43.48           O  
ANISOU 2409  O   LEU A 290     5496   5993   5032    -84   -367     94       O  
ATOM   2410  CB  LEU A 290       0.676 -25.637  20.880  1.00 42.59           C  
ANISOU 2410  CB  LEU A 290     5448   5825   4910   -139   -337     46       C  
ATOM   2411  CG  LEU A 290      -0.466 -26.550  21.330  1.00 42.76           C  
ANISOU 2411  CG  LEU A 290     5502   5806   4941   -124   -353     32       C  
ATOM   2412  CD1 LEU A 290      -0.994 -26.159  22.732  1.00 40.48           C  
ANISOU 2412  CD1 LEU A 290     5211   5517   4650   -161   -372     34       C  
ATOM   2413  CD2 LEU A 290      -1.568 -26.529  20.286  1.00 41.49           C  
ANISOU 2413  CD2 LEU A 290     5380   5607   4777   -115   -351      3       C  
ATOM   2414  N   ASP A 291       3.448 -27.281  21.140  1.00 41.60           N  
ANISOU 2414  N   ASP A 291     5214   5798   4792    -56   -321     97       N  
ATOM   2415  CA  ASP A 291       4.217 -28.524  21.267  1.00 44.07           C  
ANISOU 2415  CA  ASP A 291     5505   6132   5108     14   -319    113       C  
ATOM   2416  C   ASP A 291       4.949 -28.602  22.604  1.00 43.54           C  
ANISOU 2416  C   ASP A 291     5387   6113   5041     11   -351    136       C  
ATOM   2417  O   ASP A 291       4.937 -29.648  23.268  1.00 44.80           O  
ANISOU 2417  O   ASP A 291     5565   6256   5199     60   -369    150       O  
ATOM   2418  CB  ASP A 291       5.229 -28.662  20.122  1.00 46.85           C  
ANISOU 2418  CB  ASP A 291     5819   6527   5455     59   -279    118       C  
ATOM   2419  CG  ASP A 291       4.614 -29.229  18.845  1.00 55.10           C  
ANISOU 2419  CG  ASP A 291     6927   7519   6487    102   -253     94       C  
ATOM   2420  OD1 ASP A 291       3.495 -29.795  18.894  1.00 57.33           O  
ANISOU 2420  OD1 ASP A 291     7277   7733   6773    106   -272     73       O  
ATOM   2421  OD2 ASP A 291       5.269 -29.118  17.784  1.00 61.08           O  
ANISOU 2421  OD2 ASP A 291     7666   8310   7230    132   -213     95       O  
ATOM   2422  N   TYR A 292       5.582 -27.495  22.989  1.00 40.32           N  
ANISOU 2422  N   TYR A 292     4925   5762   4635    -46   -362    142       N  
ATOM   2423  CA  TYR A 292       6.291 -27.420  24.252  1.00 39.81           C  
ANISOU 2423  CA  TYR A 292     4810   5752   4565    -57   -402    157       C  
ATOM   2424  C   TYR A 292       5.358 -27.451  25.472  1.00 39.66           C  
ANISOU 2424  C   TYR A 292     4845   5693   4531    -79   -437    153       C  
ATOM   2425  O   TYR A 292       5.659 -28.120  26.476  1.00 38.67           O  
ANISOU 2425  O   TYR A 292     4713   5588   4391    -44   -467    173       O  
ATOM   2426  CB  TYR A 292       7.216 -26.193  24.315  1.00 40.74           C  
ANISOU 2426  CB  TYR A 292     4854   5938   4689   -127   -408    157       C  
ATOM   2427  CG  TYR A 292       8.194 -26.296  25.458  1.00 41.20           C  
ANISOU 2427  CG  TYR A 292     4841   6072   4740   -124   -456    171       C  
ATOM   2428  CD1 TYR A 292       7.808 -25.961  26.766  1.00 41.88           C  
ANISOU 2428  CD1 TYR A 292     4954   6153   4807   -160   -506    163       C  
ATOM   2429  CD2 TYR A 292       9.481 -26.773  25.251  1.00 42.12           C  
ANISOU 2429  CD2 TYR A 292     4864   6274   4866    -76   -454    190       C  
ATOM   2430  CE1 TYR A 292       8.684 -26.085  27.834  1.00 44.13           C  
ANISOU 2430  CE1 TYR A 292     5180   6511   5076   -151   -558    174       C  
ATOM   2431  CE2 TYR A 292      10.380 -26.897  26.319  1.00 47.75           C  
ANISOU 2431  CE2 TYR A 292     5505   7068   5571    -66   -508    201       C  
ATOM   2432  CZ  TYR A 292       9.971 -26.551  27.608  1.00 48.32           C  
ANISOU 2432  CZ  TYR A 292     5612   7129   5619   -105   -563    193       C  
ATOM   2433  OH  TYR A 292      10.847 -26.669  28.667  1.00 52.69           O  
ANISOU 2433  OH  TYR A 292     6099   7766   6155    -91   -625    202       O  
ATOM   2434  N   ILE A 293       4.235 -26.741  25.392  1.00 37.26           N  
ANISOU 2434  N   ILE A 293     4595   5337   4225   -129   -430    131       N  
ATOM   2435  CA  ILE A 293       3.315 -26.671  26.531  1.00 36.87           C  
ANISOU 2435  CA  ILE A 293     4592   5258   4158   -151   -452    125       C  
ATOM   2436  C   ILE A 293       2.529 -27.971  26.709  1.00 37.28           C  
ANISOU 2436  C   ILE A 293     4695   5260   4210   -104   -443    137       C  
ATOM   2437  O   ILE A 293       2.288 -28.410  27.842  1.00 38.95           O  
ANISOU 2437  O   ILE A 293     4929   5469   4402    -96   -461    154       O  
ATOM   2438  CB  ILE A 293       2.363 -25.455  26.434  1.00 35.74           C  
ANISOU 2438  CB  ILE A 293     4486   5081   4013   -210   -446     96       C  
ATOM   2439  CG1 ILE A 293       3.168 -24.158  26.263  1.00 35.44           C  
ANISOU 2439  CG1 ILE A 293     4412   5077   3976   -266   -454     86       C  
ATOM   2440  CG2 ILE A 293       1.441 -25.374  27.664  1.00 32.39           C  
ANISOU 2440  CG2 ILE A 293     4103   4638   3565   -225   -462     89       C  
ATOM   2441  CD1 ILE A 293       4.000 -23.757  27.479  1.00 32.09           C  
ANISOU 2441  CD1 ILE A 293     3951   4708   3534   -297   -497     88       C  
ATOM   2442  N   SER A 294       2.150 -28.584  25.591  1.00 37.31           N  
ANISOU 2442  N   SER A 294     4722   5222   4233    -75   -416    129       N  
ATOM   2443  CA  SER A 294       1.461 -29.877  25.603  1.00 38.33           C  
ANISOU 2443  CA  SER A 294     4903   5293   4369    -39   -407    137       C  
ATOM   2444  C   SER A 294       2.335 -30.935  26.249  1.00 38.63           C  
ANISOU 2444  C   SER A 294     4936   5345   4397     22   -421    172       C  
ATOM   2445  O   SER A 294       1.883 -31.650  27.138  1.00 40.19           O  
ANISOU 2445  O   SER A 294     5176   5511   4583     31   -427    194       O  
ATOM   2446  CB  SER A 294       1.085 -30.322  24.186  1.00 39.30           C  
ANISOU 2446  CB  SER A 294     5051   5372   4510    -17   -382    114       C  
ATOM   2447  OG  SER A 294       0.264 -29.371  23.546  1.00 38.41           O  
ANISOU 2447  OG  SER A 294     4946   5248   4401    -61   -375     84       O  
ATOM   2448  N   GLU A 295       3.589 -31.018  25.813  1.00 41.48           N  
ANISOU 2448  N   GLU A 295     5244   5757   4759     67   -422    182       N  
ATOM   2449  CA  GLU A 295       4.565 -31.924  26.420  1.00 45.72           C  
ANISOU 2449  CA  GLU A 295     5764   6323   5284    140   -441    216       C  
ATOM   2450  C   GLU A 295       4.676 -31.698  27.929  1.00 44.88           C  
ANISOU 2450  C   GLU A 295     5652   6251   5149    122   -480    239       C  
ATOM   2451  O   GLU A 295       4.680 -32.657  28.694  1.00 46.26           O  
ANISOU 2451  O   GLU A 295     5867   6403   5305    170   -493    271       O  
ATOM   2452  CB  GLU A 295       5.933 -31.783  25.737  1.00 49.86           C  
ANISOU 2452  CB  GLU A 295     6207   6923   5816    184   -436    218       C  
ATOM   2453  CG  GLU A 295       7.137 -32.326  26.537  1.00 59.48           C  
ANISOU 2453  CG  GLU A 295     7373   8209   7018    254   -469    251       C  
ATOM   2454  CD  GLU A 295       7.580 -33.728  26.109  1.00 68.05           C  
ANISOU 2454  CD  GLU A 295     8486   9265   8105    368   -455    269       C  
ATOM   2455  OE1 GLU A 295       7.765 -33.967  24.887  1.00 68.59           O  
ANISOU 2455  OE1 GLU A 295     8551   9322   8188    403   -417    250       O  
ATOM   2456  OE2 GLU A 295       7.766 -34.586  27.003  1.00 72.03           O  
ANISOU 2456  OE2 GLU A 295     9023   9756   8591    429   -482    301       O  
ATOM   2457  N   PHE A 296       4.741 -30.434  28.347  1.00 44.72           N  
ANISOU 2457  N   PHE A 296     5592   6279   5119     54   -498    222       N  
ATOM   2458  CA  PHE A 296       4.904 -30.080  29.762  1.00 43.58           C  
ANISOU 2458  CA  PHE A 296     5444   6176   4938     35   -540    235       C  
ATOM   2459  C   PHE A 296       3.679 -30.463  30.597  1.00 43.57           C  
ANISOU 2459  C   PHE A 296     5526   6114   4914     21   -531    245       C  
ATOM   2460  O   PHE A 296       3.813 -31.059  31.675  1.00 41.86           O  
ANISOU 2460  O   PHE A 296     5338   5906   4662     54   -554    278       O  
ATOM   2461  CB  PHE A 296       5.211 -28.573  29.935  1.00 42.96           C  
ANISOU 2461  CB  PHE A 296     5315   6151   4855    -42   -561    205       C  
ATOM   2462  CG  PHE A 296       5.460 -28.157  31.378  1.00 44.91           C  
ANISOU 2462  CG  PHE A 296     5560   6445   5058    -61   -611    209       C  
ATOM   2463  CD1 PHE A 296       6.757 -28.036  31.870  1.00 46.74           C  
ANISOU 2463  CD1 PHE A 296     5718   6765   5276    -46   -661    217       C  
ATOM   2464  CD2 PHE A 296       4.394 -27.905  32.245  1.00 40.66           C  
ANISOU 2464  CD2 PHE A 296     5091   5869   4487    -91   -610    201       C  
ATOM   2465  CE1 PHE A 296       6.990 -27.670  33.200  1.00 46.11           C  
ANISOU 2465  CE1 PHE A 296     5642   6732   5147    -61   -717    215       C  
ATOM   2466  CE2 PHE A 296       4.611 -27.545  33.563  1.00 41.25           C  
ANISOU 2466  CE2 PHE A 296     5174   5987   4510   -103   -656    202       C  
ATOM   2467  CZ  PHE A 296       5.913 -27.425  34.048  1.00 46.20           C  
ANISOU 2467  CZ  PHE A 296     5735   6698   5120    -88   -713    207       C  
ATOM   2468  N   GLU A 297       2.497 -30.097  30.102  1.00 43.07           N  
ANISOU 2468  N   GLU A 297     5499   5997   4870    -28   -498    219       N  
ATOM   2469  CA  GLU A 297       1.251 -30.263  30.858  1.00 41.23           C  
ANISOU 2469  CA  GLU A 297     5328   5720   4619    -56   -482    224       C  
ATOM   2470  C   GLU A 297       0.701 -31.676  30.771  1.00 41.71           C  
ANISOU 2470  C   GLU A 297     5446   5711   4691    -22   -456    253       C  
ATOM   2471  O   GLU A 297       0.205 -32.215  31.757  1.00 42.25           O  
ANISOU 2471  O   GLU A 297     5563   5759   4732    -22   -450    283       O  
ATOM   2472  CB  GLU A 297       0.183 -29.277  30.372  1.00 39.13           C  
ANISOU 2472  CB  GLU A 297     5067   5432   4370   -116   -459    183       C  
ATOM   2473  CG  GLU A 297       0.510 -27.810  30.604  1.00 38.62           C  
ANISOU 2473  CG  GLU A 297     4971   5414   4290   -158   -480    153       C  
ATOM   2474  CD  GLU A 297       0.514 -27.427  32.073  1.00 39.28           C  
ANISOU 2474  CD  GLU A 297     5071   5531   4322   -170   -505    159       C  
ATOM   2475  OE1 GLU A 297      -0.341 -27.931  32.839  1.00 40.69           O  
ANISOU 2475  OE1 GLU A 297     5296   5688   4477   -166   -487    175       O  
ATOM   2476  OE2 GLU A 297       1.372 -26.616  32.463  1.00 37.55           O  
ANISOU 2476  OE2 GLU A 297     4821   5362   4084   -188   -543    146       O  
ATOM   2477  N   LEU A 298       0.792 -32.275  29.589  1.00 42.77           N  
ANISOU 2477  N   LEU A 298     5582   5807   4862      4   -440    243       N  
ATOM   2478  CA  LEU A 298       0.071 -33.511  29.313  1.00 43.68           C  
ANISOU 2478  CA  LEU A 298     5760   5838   4996     17   -414    257       C  
ATOM   2479  C   LEU A 298       0.992 -34.699  29.109  1.00 46.15           C  
ANISOU 2479  C   LEU A 298     6097   6127   5310     99   -422    286       C  
ATOM   2480  O   LEU A 298       0.532 -35.842  29.095  1.00 47.14           O  
ANISOU 2480  O   LEU A 298     6292   6173   5445    116   -405    305       O  
ATOM   2481  CB  LEU A 298      -0.844 -33.340  28.091  1.00 40.60           C  
ANISOU 2481  CB  LEU A 298     5375   5407   4645    -21   -391    213       C  
ATOM   2482  CG  LEU A 298      -1.789 -32.136  28.081  1.00 37.55           C  
ANISOU 2482  CG  LEU A 298     4963   5042   4260    -87   -384    179       C  
ATOM   2483  CD1 LEU A 298      -2.297 -31.836  26.664  1.00 31.49           C  
ANISOU 2483  CD1 LEU A 298     4186   4254   3524   -102   -375    135       C  
ATOM   2484  CD2 LEU A 298      -2.934 -32.363  29.039  1.00 36.94           C  
ANISOU 2484  CD2 LEU A 298     4919   4943   4175   -130   -365    193       C  
ATOM   2485  N   ASN A 299       2.284 -34.427  28.945  1.00 48.46           N  
ANISOU 2485  N   ASN A 299     6331   6487   5594    151   -445    289       N  
ATOM   2486  CA  ASN A 299       3.273 -35.470  28.705  1.00 53.99           C  
ANISOU 2486  CA  ASN A 299     7040   7179   6294    247   -453    314       C  
ATOM   2487  C   ASN A 299       3.004 -36.198  27.385  1.00 54.27           C  
ANISOU 2487  C   ASN A 299     7115   7143   6363    273   -423    288       C  
ATOM   2488  O   ASN A 299       3.196 -37.409  27.284  1.00 55.89           O  
ANISOU 2488  O   ASN A 299     7381   7286   6570    340   -418    307       O  
ATOM   2489  CB  ASN A 299       3.337 -36.468  29.884  1.00 57.36           C  
ANISOU 2489  CB  ASN A 299     7532   7572   6688    295   -467    369       C  
ATOM   2490  CG  ASN A 299       3.842 -35.832  31.186  1.00 66.48           C  
ANISOU 2490  CG  ASN A 299     8649   8811   7797    291   -506    394       C  
ATOM   2491  OD1 ASN A 299       4.754 -36.361  31.824  1.00 73.96           O  
ANISOU 2491  OD1 ASN A 299     9594   9792   8714    370   -538    432       O  
ATOM   2492  ND2 ASN A 299       3.244 -34.707  31.590  1.00 69.20           N  
ANISOU 2492  ND2 ASN A 299     8970   9191   8133    206   -507    370       N  
ATOM   2493  N   VAL A 300       2.549 -35.458  26.380  1.00 52.93           N  
ANISOU 2493  N   VAL A 300     6918   6978   6215    223   -406    243       N  
ATOM   2494  CA  VAL A 300       2.344 -36.033  25.052  1.00 53.51           C  
ANISOU 2494  CA  VAL A 300     7027   6996   6311    248   -384    210       C  
ATOM   2495  C   VAL A 300       3.498 -35.711  24.113  1.00 55.48           C  
ANISOU 2495  C   VAL A 300     7213   7310   6557    305   -375    196       C  
ATOM   2496  O   VAL A 300       4.176 -34.695  24.274  1.00 56.13           O  
ANISOU 2496  O   VAL A 300     7213   7481   6632    287   -383    200       O  
ATOM   2497  CB  VAL A 300       1.014 -35.580  24.412  1.00 52.53           C  
ANISOU 2497  CB  VAL A 300     6924   6830   6206    167   -371    169       C  
ATOM   2498  CG1 VAL A 300      -0.157 -36.140  25.194  1.00 49.79           C  
ANISOU 2498  CG1 VAL A 300     6636   6414   5866    114   -369    182       C  
ATOM   2499  CG2 VAL A 300       0.942 -34.054  24.314  1.00 48.90           C  
ANISOU 2499  CG2 VAL A 300     6396   6443   5741    110   -374    150       C  
ATOM   2500  N   GLY A 301       3.705 -36.576  23.125  1.00 58.54           N  
ANISOU 2500  N   GLY A 301     7641   7651   6950    371   -357    178       N  
ATOM   2501  CA  GLY A 301       4.779 -36.398  22.149  1.00 60.74           C  
ANISOU 2501  CA  GLY A 301     7865   7992   7223    435   -337    165       C  
ATOM   2502  C   GLY A 301       4.575 -35.222  21.213  1.00 61.00           C  
ANISOU 2502  C   GLY A 301     7854   8067   7256    376   -319    133       C  
ATOM   2503  O   GLY A 301       3.445 -34.891  20.850  1.00 58.75           O  
ANISOU 2503  O   GLY A 301     7609   7736   6979    310   -319    105       O  
ATOM   2504  N   LYS A 302       5.685 -34.595  20.828  1.00 63.85           N  
ANISOU 2504  N   LYS A 302     8130   8521   7609    401   -302    140       N  
ATOM   2505  CA  LYS A 302       5.693 -33.512  19.843  1.00 65.53           C  
ANISOU 2505  CA  LYS A 302     8306   8775   7817    355   -275    119       C  
ATOM   2506  C   LYS A 302       5.120 -33.979  18.496  1.00 65.16           C  
ANISOU 2506  C   LYS A 302     8331   8668   7759    383   -250     80       C  
ATOM   2507  O   LYS A 302       5.266 -35.148  18.115  1.00 64.42           O  
ANISOU 2507  O   LYS A 302     8290   8527   7659    463   -242     68       O  
ATOM   2508  CB  LYS A 302       7.123 -32.999  19.645  1.00 67.78           C  
ANISOU 2508  CB  LYS A 302     8487   9170   8097    384   -253    139       C  
ATOM   2509  CG  LYS A 302       7.226 -31.545  19.208  1.00 72.33           C  
ANISOU 2509  CG  LYS A 302     9011   9800   8672    301   -234    136       C  
ATOM   2510  CD  LYS A 302       8.354 -31.315  18.195  1.00 77.63           C  
ANISOU 2510  CD  LYS A 302     9614  10550   9331    340   -182    142       C  
ATOM   2511  CE  LYS A 302       7.950 -31.778  16.790  1.00 78.39           C  
ANISOU 2511  CE  LYS A 302     9783  10600   9404    390   -142    113       C  
ATOM   2512  NZ  LYS A 302       8.639 -31.037  15.695  1.00 78.16           N  
ANISOU 2512  NZ  LYS A 302     9706  10637   9353    385    -83    119       N  
ATOM   2513  N   LEU A 303       4.468 -33.055  17.794  1.00 64.93           N  
ANISOU 2513  N   LEU A 303     8311   8638   7723    322   -241     58       N  
ATOM   2514  CA  LEU A 303       3.904 -33.305  16.464  1.00 65.39           C  
ANISOU 2514  CA  LEU A 303     8434   8652   7761    343   -224     18       C  
ATOM   2515  C   LEU A 303       4.977 -33.242  15.365  1.00 66.74           C  
ANISOU 2515  C   LEU A 303     8574   8881   7901    409   -175     17       C  
ATOM   2516  O   LEU A 303       5.221 -32.192  14.758  1.00 66.24           O  
ANISOU 2516  O   LEU A 303     8475   8870   7821    376   -147     24       O  
ATOM   2517  CB  LEU A 303       2.766 -32.317  16.188  1.00 65.09           C  
ANISOU 2517  CB  LEU A 303     8416   8595   7721    261   -239     -1       C  
ATOM   2518  CG  LEU A 303       1.326 -32.673  16.591  1.00 63.58           C  
ANISOU 2518  CG  LEU A 303     8281   8327   7549    214   -278    -26       C  
ATOM   2519  CD1 LEU A 303       1.245 -33.708  17.706  1.00 60.88           C  
ANISOU 2519  CD1 LEU A 303     7958   7943   7232    223   -297     -9       C  
ATOM   2520  CD2 LEU A 303       0.564 -31.409  16.976  1.00 59.70           C  
ANISOU 2520  CD2 LEU A 303     7766   7853   7063    135   -294    -23       C  
ATOM   2521  N   LYS A 304       5.607 -34.389  15.125  1.00 68.35           N  
ANISOU 2521  N   LYS A 304     8799   9074   8098    506   -159     12       N  
ATOM   2522  CA  LYS A 304       6.766 -34.499  14.245  1.00 70.24           C  
ANISOU 2522  CA  LYS A 304     8999   9381   8308    589   -105     15       C  
ATOM   2523  C   LYS A 304       6.377 -34.504  12.762  1.00 69.71           C  
ANISOU 2523  C   LYS A 304     8999   9290   8196    614    -76    -26       C  
ATOM   2524  O   LYS A 304       5.384 -35.124  12.374  1.00 67.93           O  
ANISOU 2524  O   LYS A 304     8872   8976   7964    616   -104    -68       O  
ATOM   2525  CB  LYS A 304       7.535 -35.781  14.594  1.00 72.48           C  
ANISOU 2525  CB  LYS A 304     9288   9657   8596    700   -103     21       C  
ATOM   2526  CG  LYS A 304       8.797 -36.029  13.768  1.00 77.82           C  
ANISOU 2526  CG  LYS A 304     9915  10412   9243    805    -43     23       C  
ATOM   2527  CD  LYS A 304       8.822 -37.456  13.202  1.00 81.67           C  
ANISOU 2527  CD  LYS A 304    10499  10825   9708    927    -34    -13       C  
ATOM   2528  CE  LYS A 304       7.904 -37.599  11.976  1.00 80.77           C  
ANISOU 2528  CE  LYS A 304    10495  10637   9557    919    -27    -69       C  
ATOM   2529  NZ  LYS A 304       7.680 -39.014  11.579  1.00 78.83           N  
ANISOU 2529  NZ  LYS A 304    10368  10289   9295   1014    -36   -114       N  
ATOM   2530  N   TYR A 305       7.166 -33.810  11.940  1.00 69.97           N  
ANISOU 2530  N   TYR A 305     8982   9406   8199    629    -19    -13       N  
ATOM   2531  CA  TYR A 305       7.039 -33.912  10.482  1.00 70.98           C  
ANISOU 2531  CA  TYR A 305     9174   9525   8269    677     19    -46       C  
ATOM   2532  C   TYR A 305       8.343 -33.658   9.732  1.00 70.98           C  
ANISOU 2532  C   TYR A 305     9106   9629   8234    739     99    -24       C  
ATOM   2533  O   TYR A 305       9.273 -33.048  10.268  1.00 69.06           O  
ANISOU 2533  O   TYR A 305     8749   9474   8015    712    125     22       O  
ATOM   2534  CB  TYR A 305       5.919 -33.019   9.931  1.00 71.36           C  
ANISOU 2534  CB  TYR A 305     9276   9540   8298    597     -2    -63       C  
ATOM   2535  CG  TYR A 305       5.948 -31.590  10.414  1.00 75.09           C  
ANISOU 2535  CG  TYR A 305     9679  10060   8791    496      0    -20       C  
ATOM   2536  CD1 TYR A 305       6.739 -30.630   9.777  1.00 77.03           C  
ANISOU 2536  CD1 TYR A 305     9875  10384   9008    482     62     13       C  
ATOM   2537  CD2 TYR A 305       5.167 -31.189  11.502  1.00 75.18           C  
ANISOU 2537  CD2 TYR A 305     9683  10034   8847    414    -57    -13       C  
ATOM   2538  CE1 TYR A 305       6.759 -29.310  10.217  1.00 78.67           C  
ANISOU 2538  CE1 TYR A 305    10034  10621   9236    384     62     50       C  
ATOM   2539  CE2 TYR A 305       5.181 -29.874  11.950  1.00 76.70           C  
ANISOU 2539  CE2 TYR A 305     9826  10261   9055    327    -57     19       C  
ATOM   2540  CZ  TYR A 305       5.977 -28.941  11.304  1.00 77.80           C  
ANISOU 2540  CZ  TYR A 305     9924  10467   9169    310     -1     50       C  
ATOM   2541  OH  TYR A 305       5.989 -27.640  11.747  1.00 80.67           O  
ANISOU 2541  OH  TYR A 305    10252  10849   9550    219     -2     80       O  
ATOM   2542  N   ASP A 306       8.383 -34.130   8.486  1.00 71.88           N  
ANISOU 2542  N   ASP A 306     9289   9734   8289    819    138    -58       N  
ATOM   2543  CA  ASP A 306       9.516 -33.929   7.586  1.00 72.38           C  
ANISOU 2543  CA  ASP A 306     9301   9896   8306    885    227    -41       C  
ATOM   2544  C   ASP A 306       9.311 -32.694   6.724  1.00 71.90           C  
ANISOU 2544  C   ASP A 306     9247   9871   8202    816    266    -22       C  
ATOM   2545  O   ASP A 306       8.197 -32.414   6.275  1.00 70.65           O  
ANISOU 2545  O   ASP A 306     9182   9644   8019    775    227    -50       O  
ATOM   2546  CB  ASP A 306       9.722 -35.156   6.687  1.00 73.86           C  
ANISOU 2546  CB  ASP A 306     9571  10054   8439   1023    255    -91       C  
ATOM   2547  CG  ASP A 306      10.344 -36.336   7.427  1.00 74.76           C  
ANISOU 2547  CG  ASP A 306     9663  10156   8587   1119    243    -95       C  
ATOM   2548  OD1 ASP A 306       9.829 -37.466   7.283  1.00 73.66           O  
ANISOU 2548  OD1 ASP A 306     9636   9916   8437   1185    209   -146       O  
ATOM   2549  OD2 ASP A 306      11.348 -36.139   8.147  1.00 75.30           O  
ANISOU 2549  OD2 ASP A 306     9606  10313   8692   1128    265    -49       O  
ATOM   2550  N   GLY A 307      10.401 -31.966   6.495  1.00 72.88           N  
ANISOU 2550  N   GLY A 307     9271  10104   8318    805    342     26       N  
ATOM   2551  CA  GLY A 307      10.385 -30.740   5.708  1.00 72.81           C  
ANISOU 2551  CA  GLY A 307     9265  10132   8268    737    392     58       C  
ATOM   2552  C   GLY A 307       9.885 -29.546   6.500  1.00 71.92           C  
ANISOU 2552  C   GLY A 307     9123   9999   8203    599    347     91       C  
ATOM   2553  O   GLY A 307       9.397 -29.703   7.623  1.00 72.14           O  
ANISOU 2553  O   GLY A 307     9139   9979   8290    557    273     82       O  
ATOM   2554  N   PRO A 308      10.018 -28.334   5.930  1.00 72.11           N  
ANISOU 2554  N   PRO A 308     9143  10056   8199    529    396    131       N  
ATOM   2555  CA  PRO A 308       9.464 -27.159   6.601  1.00 71.33           C  
ANISOU 2555  CA  PRO A 308     9040   9922   8140    404    353    157       C  
ATOM   2556  C   PRO A 308       7.942 -27.144   6.505  1.00 70.05           C  
ANISOU 2556  C   PRO A 308     8998   9656   7964    395    276    118       C  
ATOM   2557  O   PRO A 308       7.370 -27.728   5.574  1.00 69.54           O  
ANISOU 2557  O   PRO A 308     9026   9555   7840    467    271     79       O  
ATOM   2558  CB  PRO A 308      10.066 -25.984   5.818  1.00 72.97           C  
ANISOU 2558  CB  PRO A 308     9231  10185   8311    348    438    212       C  
ATOM   2559  CG  PRO A 308      10.383 -26.547   4.465  1.00 73.91           C  
ANISOU 2559  CG  PRO A 308     9398  10339   8346    451    510    201       C  
ATOM   2560  CD  PRO A 308      10.760 -27.982   4.703  1.00 73.40           C  
ANISOU 2560  CD  PRO A 308     9303  10291   8293    561    500    159       C  
ATOM   2561  N   ILE A 309       7.305 -26.473   7.461  1.00 68.39           N  
ANISOU 2561  N   ILE A 309     8781   9401   7803    307    216    124       N  
ATOM   2562  CA  ILE A 309       5.845 -26.377   7.530  1.00 65.73           C  
ANISOU 2562  CA  ILE A 309     8535   8977   7463    292    140     89       C  
ATOM   2563  C   ILE A 309       5.211 -25.816   6.244  1.00 64.23           C  
ANISOU 2563  C   ILE A 309     8445   8764   7198    309    155     86       C  
ATOM   2564  O   ILE A 309       4.034 -26.054   5.966  1.00 63.41           O  
ANISOU 2564  O   ILE A 309     8419   8601   7074    330     95     44       O  
ATOM   2565  CB  ILE A 309       5.402 -25.575   8.798  1.00 65.39           C  
ANISOU 2565  CB  ILE A 309     8459   8905   7483    196     88    103       C  
ATOM   2566  CG1 ILE A 309       4.183 -26.234   9.478  1.00 65.08           C  
ANISOU 2566  CG1 ILE A 309     8459   8797   7473    203      5     57       C  
ATOM   2567  CG2 ILE A 309       5.262 -24.068   8.505  1.00 64.78           C  
ANISOU 2567  CG2 ILE A 309     8407   8818   7386    122    108    141       C  
ATOM   2568  CD1 ILE A 309       2.819 -25.840   8.947  1.00 64.87           C  
ANISOU 2568  CD1 ILE A 309     8520   8712   7416    200    -39     30       C  
ATOM   2569  N   SER A 310       6.004 -25.097   5.457  1.00 62.23           N  
ANISOU 2569  N   SER A 310     8184   8560   6900    300    235    132       N  
ATOM   2570  CA  SER A 310       5.528 -24.506   4.214  1.00 62.66           C  
ANISOU 2570  CA  SER A 310     8338   8598   6871    321    257    140       C  
ATOM   2571  C   SER A 310       5.397 -25.539   3.079  1.00 61.49           C  
ANISOU 2571  C   SER A 310     8261   8456   6648    432    270     95       C  
ATOM   2572  O   SER A 310       4.923 -25.224   1.983  1.00 60.62           O  
ANISOU 2572  O   SER A 310     8245   8333   6455    466    277     93       O  
ATOM   2573  CB  SER A 310       6.451 -23.351   3.802  1.00 64.45           C  
ANISOU 2573  CB  SER A 310     8540   8872   7075    264    347    213       C  
ATOM   2574  OG  SER A 310       7.791 -23.783   3.641  1.00 65.73           O  
ANISOU 2574  OG  SER A 310     8615   9122   7238    286    430    236       O  
ATOM   2575  N   LYS A 311       5.824 -26.769   3.349  1.00 59.71           N  
ANISOU 2575  N   LYS A 311     7996   8247   6445    491    269     60       N  
ATOM   2576  CA  LYS A 311       5.744 -27.839   2.362  1.00 58.31           C  
ANISOU 2576  CA  LYS A 311     7891   8067   6199    599    277      8       C  
ATOM   2577  C   LYS A 311       5.007 -29.066   2.897  1.00 55.73           C  
ANISOU 2577  C   LYS A 311     7590   7674   5912    633    193    -61       C  
ATOM   2578  O   LYS A 311       4.930 -30.095   2.224  1.00 55.14           O  
ANISOU 2578  O   LYS A 311     7578   7581   5791    719    190   -114       O  
ATOM   2579  CB  LYS A 311       7.140 -28.216   1.871  1.00 59.31           C  
ANISOU 2579  CB  LYS A 311     7963   8278   6294    662    381     32       C  
ATOM   2580  CG  LYS A 311       7.760 -27.184   0.945  1.00 64.82           C  
ANISOU 2580  CG  LYS A 311     8666   9038   6924    645    476     92       C  
ATOM   2581  CD  LYS A 311       9.142 -27.613   0.479  1.00 69.05           C  
ANISOU 2581  CD  LYS A 311     9135   9672   7431    710    586    114       C  
ATOM   2582  CE  LYS A 311       9.815 -26.510  -0.328  1.00 70.93           C  
ANISOU 2582  CE  LYS A 311     9364   9976   7611    672    692    186       C  
ATOM   2583  NZ  LYS A 311      11.155 -26.931  -0.836  1.00 72.45           N  
ANISOU 2583  NZ  LYS A 311     9480  10278   7771    739    809    208       N  
ATOM   2584  N   LEU A 312       4.449 -28.942   4.099  1.00 51.56           N  
ANISOU 2584  N   LEU A 312     7021   7106   5466    562    128    -61       N  
ATOM   2585  CA  LEU A 312       3.758 -30.058   4.743  1.00 50.07           C  
ANISOU 2585  CA  LEU A 312     6850   6851   5322    576     55   -115       C  
ATOM   2586  C   LEU A 312       2.404 -30.397   4.105  1.00 49.30           C  
ANISOU 2586  C   LEU A 312     6854   6688   5189    589    -18   -178       C  
ATOM   2587  O   LEU A 312       2.047 -31.569   3.997  1.00 48.32           O  
ANISOU 2587  O   LEU A 312     6778   6517   5065    633    -54   -236       O  
ATOM   2588  CB  LEU A 312       3.600 -29.801   6.247  1.00 47.91           C  
ANISOU 2588  CB  LEU A 312     6501   6563   5139    497     15    -91       C  
ATOM   2589  CG  LEU A 312       2.975 -30.912   7.091  1.00 43.83           C  
ANISOU 2589  CG  LEU A 312     5995   5981   4676    499    -49   -132       C  
ATOM   2590  CD1 LEU A 312       3.745 -32.207   6.943  1.00 42.29           C  
ANISOU 2590  CD1 LEU A 312     5810   5784   4475    588    -23   -153       C  
ATOM   2591  CD2 LEU A 312       2.902 -30.495   8.553  1.00 43.12           C  
ANISOU 2591  CD2 LEU A 312     5832   5889   4661    422    -77    -98       C  
ATOM   2592  N   ARG A 313       1.654 -29.376   3.700  1.00 47.50           N  
ANISOU 2592  N   ARG A 313     6660   6458   4931    551    -42   -167       N  
ATOM   2593  CA  ARG A 313       0.397 -29.598   2.996  1.00 48.21           C  
ANISOU 2593  CA  ARG A 313     6835   6504   4979    567   -114   -226       C  
ATOM   2594  C   ARG A 313       0.686 -30.261   1.650  1.00 50.24           C  
ANISOU 2594  C   ARG A 313     7176   6771   5142    660    -88   -266       C  
ATOM   2595  O   ARG A 313       0.054 -31.252   1.278  1.00 51.02           O  
ANISOU 2595  O   ARG A 313     7337   6824   5224    695   -143   -338       O  
ATOM   2596  CB  ARG A 313      -0.344 -28.271   2.793  1.00 46.76           C  
ANISOU 2596  CB  ARG A 313     6668   6324   4773    524   -139   -199       C  
ATOM   2597  CG  ARG A 313      -1.766 -28.429   2.326  1.00 42.38           C  
ANISOU 2597  CG  ARG A 313     6176   5734   4194    532   -231   -258       C  
ATOM   2598  CD  ARG A 313      -2.397 -27.102   2.012  1.00 41.55           C  
ANISOU 2598  CD  ARG A 313     6094   5639   4055    513   -251   -227       C  
ATOM   2599  NE  ARG A 313      -3.578 -27.268   1.164  1.00 40.24           N  
ANISOU 2599  NE  ARG A 313     5997   5459   3833    550   -332   -285       N  
ATOM   2600  CZ  ARG A 313      -3.589 -27.102  -0.159  1.00 40.04           C  
ANISOU 2600  CZ  ARG A 313     6059   5455   3701    616   -327   -295       C  
ATOM   2601  NH1 ARG A 313      -2.480 -26.751  -0.813  1.00 37.63           N  
ANISOU 2601  NH1 ARG A 313     5784   5184   3332    652   -234   -246       N  
ATOM   2602  NH2 ARG A 313      -4.718 -27.282  -0.832  1.00 38.83           N  
ANISOU 2602  NH2 ARG A 313     5959   5293   3501    646   -415   -354       N  
ATOM   2603  N   GLU A 314       1.660 -29.703   0.937  1.00 52.96           N  
ANISOU 2603  N   GLU A 314     7523   7176   5424    696      0   -220       N  
ATOM   2604  CA  GLU A 314       2.097 -30.223  -0.349  1.00 54.24           C  
ANISOU 2604  CA  GLU A 314     7762   7363   5485    792     44   -249       C  
ATOM   2605  C   GLU A 314       2.503 -31.692  -0.229  1.00 53.59           C  
ANISOU 2605  C   GLU A 314     7688   7254   5419    857     46   -304       C  
ATOM   2606  O   GLU A 314       2.053 -32.520  -1.016  1.00 54.13           O  
ANISOU 2606  O   GLU A 314     7851   7287   5429    919     10   -376       O  
ATOM   2607  CB  GLU A 314       3.260 -29.376  -0.872  1.00 56.12           C  
ANISOU 2607  CB  GLU A 314     7972   7680   5672    806    158   -175       C  
ATOM   2608  CG  GLU A 314       3.858 -29.819  -2.198  1.00 62.22           C  
ANISOU 2608  CG  GLU A 314     8817   8494   6331    910    226   -193       C  
ATOM   2609  CD  GLU A 314       5.106 -29.020  -2.565  1.00 67.97           C  
ANISOU 2609  CD  GLU A 314     9494   9309   7022    911    353   -111       C  
ATOM   2610  OE1 GLU A 314       5.168 -28.495  -3.702  1.00 71.07           O  
ANISOU 2610  OE1 GLU A 314     9962   9734   7309    948    402    -90       O  
ATOM   2611  OE2 GLU A 314       6.019 -28.910  -1.715  1.00 66.70           O  
ANISOU 2611  OE2 GLU A 314     9217   9187   6937    873    404    -65       O  
ATOM   2612  N   SER A 315       3.329 -32.013   0.767  1.00 51.24           N  
ANISOU 2612  N   SER A 315     7300   6970   5198    845     81   -273       N  
ATOM   2613  CA  SER A 315       3.928 -33.350   0.854  1.00 50.91           C  
ANISOU 2613  CA  SER A 315     7268   6910   5165    925     99   -313       C  
ATOM   2614  C   SER A 315       3.102 -34.374   1.631  1.00 48.03           C  
ANISOU 2614  C   SER A 315     6931   6450   4869    903     10   -369       C  
ATOM   2615  O   SER A 315       3.189 -35.571   1.363  1.00 49.42           O  
ANISOU 2615  O   SER A 315     7171   6577   5028    974      0   -426       O  
ATOM   2616  CB  SER A 315       5.359 -33.282   1.404  1.00 51.45           C  
ANISOU 2616  CB  SER A 315     7227   7052   5269    948    187   -253       C  
ATOM   2617  OG  SER A 315       5.386 -32.737   2.713  1.00 53.46           O  
ANISOU 2617  OG  SER A 315     7383   7311   5618    855    164   -203       O  
ATOM   2618  N   ASN A 316       2.313 -33.909   2.594  1.00 46.33           N  
ANISOU 2618  N   ASN A 316     6671   6205   4727    803    -51   -351       N  
ATOM   2619  CA  ASN A 316       1.531 -34.807   3.444  1.00 44.60           C  
ANISOU 2619  CA  ASN A 316     6466   5900   4578    766   -125   -391       C  
ATOM   2620  C   ASN A 316       0.280 -34.122   3.964  1.00 43.77           C  
ANISOU 2620  C   ASN A 316     6344   5772   4516    664   -197   -389       C  
ATOM   2621  O   ASN A 316       0.151 -33.876   5.174  1.00 46.31           O  
ANISOU 2621  O   ASN A 316     6595   6087   4914    597   -212   -353       O  
ATOM   2622  CB  ASN A 316       2.383 -35.313   4.619  1.00 43.92           C  
ANISOU 2622  CB  ASN A 316     6309   5815   4564    772    -97   -352       C  
ATOM   2623  CG  ASN A 316       1.849 -36.600   5.229  1.00 45.77           C  
ANISOU 2623  CG  ASN A 316     6592   5950   4848    771   -153   -397       C  
ATOM   2624  OD1 ASN A 316       0.717 -37.010   4.975  1.00 47.40           O  
ANISOU 2624  OD1 ASN A 316     6868   6088   5055    735   -219   -454       O  
ATOM   2625  ND2 ASN A 316       2.674 -37.249   6.038  1.00 46.40           N  
ANISOU 2625  ND2 ASN A 316     6636   6023   4969    810   -126   -370       N  
ATOM   2626  N   HIS A 317      -0.637 -33.820   3.050  1.00 42.36           N  
ANISOU 2626  N   HIS A 317     6227   5585   4282    660   -243   -431       N  
ATOM   2627  CA  HIS A 317      -1.898 -33.164   3.394  1.00 44.20           C  
ANISOU 2627  CA  HIS A 317     6443   5805   4547    580   -315   -436       C  
ATOM   2628  C   HIS A 317      -2.619 -33.904   4.516  1.00 43.82           C  
ANISOU 2628  C   HIS A 317     6368   5694   4589    515   -370   -458       C  
ATOM   2629  O   HIS A 317      -3.246 -33.287   5.371  1.00 45.14           O  
ANISOU 2629  O   HIS A 317     6476   5866   4811    442   -397   -432       O  
ATOM   2630  CB  HIS A 317      -2.818 -33.041   2.168  1.00 44.56           C  
ANISOU 2630  CB  HIS A 317     6569   5848   4516    603   -371   -494       C  
ATOM   2631  CG  HIS A 317      -4.203 -32.566   2.501  1.00 46.37           C  
ANISOU 2631  CG  HIS A 317     6774   6065   4780    532   -454   -512       C  
ATOM   2632  ND1 HIS A 317      -5.283 -33.419   2.586  1.00 47.82           N  
ANISOU 2632  ND1 HIS A 317     6979   6196   4995    495   -536   -582       N  
ATOM   2633  CD2 HIS A 317      -4.677 -31.331   2.797  1.00 45.78           C  
ANISOU 2633  CD2 HIS A 317     6653   6025   4716    492   -465   -469       C  
ATOM   2634  CE1 HIS A 317      -6.363 -32.731   2.909  1.00 43.88           C  
ANISOU 2634  CE1 HIS A 317     6435   5712   4524    439   -593   -582       C  
ATOM   2635  NE2 HIS A 317      -6.024 -31.460   3.037  1.00 43.96           N  
ANISOU 2635  NE2 HIS A 317     6409   5773   4521    443   -552   -514       N  
ATOM   2636  N   GLN A 318      -2.521 -35.229   4.489  1.00 43.90           N  
ANISOU 2636  N   GLN A 318     6430   5642   4610    544   -381   -505       N  
ATOM   2637  CA  GLN A 318      -3.127 -36.098   5.485  1.00 44.81           C  
ANISOU 2637  CA  GLN A 318     6537   5685   4804    485   -424   -523       C  
ATOM   2638  C   GLN A 318      -2.726 -35.675   6.912  1.00 46.74           C  
ANISOU 2638  C   GLN A 318     6689   5949   5120    438   -394   -450       C  
ATOM   2639  O   GLN A 318      -3.581 -35.471   7.780  1.00 46.42           O  
ANISOU 2639  O   GLN A 318     6607   5894   5137    358   -431   -441       O  
ATOM   2640  CB  GLN A 318      -2.721 -37.550   5.184  1.00 43.08           C  
ANISOU 2640  CB  GLN A 318     6402   5392   4575    544   -421   -573       C  
ATOM   2641  CG  GLN A 318      -3.360 -38.628   6.046  1.00 42.72           C  
ANISOU 2641  CG  GLN A 318     6378   5251   4604    485   -464   -597       C  
ATOM   2642  CD  GLN A 318      -4.870 -38.538   6.100  1.00 43.77           C  
ANISOU 2642  CD  GLN A 318     6504   5358   4767    386   -543   -639       C  
ATOM   2643  OE1 GLN A 318      -5.544 -38.450   5.066  1.00 42.26           O  
ANISOU 2643  OE1 GLN A 318     6357   5174   4527    388   -591   -700       O  
ATOM   2644  NE2 GLN A 318      -5.415 -38.559   7.316  1.00 41.27           N  
ANISOU 2644  NE2 GLN A 318     6131   5022   4530    301   -556   -607       N  
ATOM   2645  N   ARG A 319      -1.423 -35.519   7.130  1.00 47.62           N  
ANISOU 2645  N   ARG A 319     6765   6103   5224    490   -326   -400       N  
ATOM   2646  CA  ARG A 319      -0.888 -35.203   8.445  1.00 47.33           C  
ANISOU 2646  CA  ARG A 319     6646   6090   5246    456   -301   -335       C  
ATOM   2647  C   ARG A 319      -1.100 -33.725   8.750  1.00 45.36           C  
ANISOU 2647  C   ARG A 319     6329   5903   5002    397   -297   -292       C  
ATOM   2648  O   ARG A 319      -1.305 -33.330   9.904  1.00 42.95           O  
ANISOU 2648  O   ARG A 319     5966   5603   4749    337   -307   -257       O  
ATOM   2649  CB  ARG A 319       0.588 -35.573   8.484  1.00 49.20           C  
ANISOU 2649  CB  ARG A 319     6863   6361   5471    537   -237   -303       C  
ATOM   2650  CG  ARG A 319       1.181 -35.585   9.851  1.00 52.58           C  
ANISOU 2650  CG  ARG A 319     7218   6804   5956    517   -224   -248       C  
ATOM   2651  CD  ARG A 319       2.308 -36.586   9.953  1.00 57.87           C  
ANISOU 2651  CD  ARG A 319     7895   7469   6622    611   -187   -240       C  
ATOM   2652  NE  ARG A 319       1.826 -37.941  10.221  1.00 60.51           N  
ANISOU 2652  NE  ARG A 319     8312   7699   6980    628   -223   -277       N  
ATOM   2653  CZ  ARG A 319       2.618 -38.969  10.519  1.00 60.54           C  
ANISOU 2653  CZ  ARG A 319     8341   7672   6991    711   -204   -270       C  
ATOM   2654  NH1 ARG A 319       3.936 -38.803  10.599  1.00 59.43           N  
ANISOU 2654  NH1 ARG A 319     8133   7611   6836    787   -152   -231       N  
ATOM   2655  NH2 ARG A 319       2.095 -40.166  10.742  1.00 58.22           N  
ANISOU 2655  NH2 ARG A 319     8136   7266   6717    718   -237   -302       N  
ATOM   2656  N   TYR A 320      -1.073 -32.923   7.691  1.00 44.67           N  
ANISOU 2656  N   TYR A 320     6261   5858   4855    419   -282   -295       N  
ATOM   2657  CA  TYR A 320      -1.388 -31.502   7.754  1.00 42.38           C  
ANISOU 2657  CA  TYR A 320     5933   5611   4559    371   -283   -261       C  
ATOM   2658  C   TYR A 320      -2.731 -31.274   8.463  1.00 41.32           C  
ANISOU 2658  C   TYR A 320     5783   5446   4471    300   -347   -277       C  
ATOM   2659  O   TYR A 320      -2.822 -30.475   9.390  1.00 40.50           O  
ANISOU 2659  O   TYR A 320     5624   5361   4405    248   -345   -239       O  
ATOM   2660  CB  TYR A 320      -1.426 -30.948   6.328  1.00 41.72           C  
ANISOU 2660  CB  TYR A 320     5905   5555   4393    415   -270   -274       C  
ATOM   2661  CG  TYR A 320      -1.457 -29.444   6.201  1.00 39.92           C  
ANISOU 2661  CG  TYR A 320     5656   5368   4143    384   -253   -227       C  
ATOM   2662  CD1 TYR A 320      -0.308 -28.692   6.406  1.00 40.33           C  
ANISOU 2662  CD1 TYR A 320     5661   5468   4195    376   -184   -165       C  
ATOM   2663  CD2 TYR A 320      -2.629 -28.777   5.846  1.00 38.44           C  
ANISOU 2663  CD2 TYR A 320     5498   5170   3936    365   -307   -246       C  
ATOM   2664  CE1 TYR A 320      -0.315 -27.317   6.281  1.00 38.46           C  
ANISOU 2664  CE1 TYR A 320     5418   5255   3940    341   -166   -122       C  
ATOM   2665  CE2 TYR A 320      -2.649 -27.390   5.719  1.00 39.73           C  
ANISOU 2665  CE2 TYR A 320     5658   5359   4077    345   -291   -201       C  
ATOM   2666  CZ  TYR A 320      -1.476 -26.670   5.933  1.00 38.43           C  
ANISOU 2666  CZ  TYR A 320     5460   5230   3914    330   -218   -138       C  
ATOM   2667  OH  TYR A 320      -1.454 -25.301   5.808  1.00 38.71           O  
ANISOU 2667  OH  TYR A 320     5503   5276   3928    303   -198    -92       O  
ATOM   2668  N   ILE A 321      -3.756 -32.001   8.034  1.00 40.91           N  
ANISOU 2668  N   ILE A 321     5778   5350   4416    296   -403   -338       N  
ATOM   2669  CA  ILE A 321      -5.113 -31.829   8.556  1.00 41.84           C  
ANISOU 2669  CA  ILE A 321     5873   5450   4574    231   -463   -360       C  
ATOM   2670  C   ILE A 321      -5.258 -32.470   9.932  1.00 40.93           C  
ANISOU 2670  C   ILE A 321     5717   5301   4534    178   -466   -345       C  
ATOM   2671  O   ILE A 321      -5.873 -31.896  10.823  1.00 41.81           O  
ANISOU 2671  O   ILE A 321     5778   5425   4684    124   -479   -325       O  
ATOM   2672  CB  ILE A 321      -6.182 -32.399   7.573  1.00 41.50           C  
ANISOU 2672  CB  ILE A 321     5885   5381   4503    237   -528   -434       C  
ATOM   2673  CG1 ILE A 321      -6.185 -31.610   6.266  1.00 41.88           C  
ANISOU 2673  CG1 ILE A 321     5975   5470   4468    291   -533   -444       C  
ATOM   2674  CG2 ILE A 321      -7.576 -32.416   8.206  1.00 44.12           C  
ANISOU 2674  CG2 ILE A 321     6174   5701   4889    165   -588   -459       C  
ATOM   2675  CD1 ILE A 321      -6.404 -30.105   6.415  1.00 39.67           C  
ANISOU 2675  CD1 ILE A 321     5658   5237   4177    279   -527   -397       C  
ATOM   2676  N   SER A 322      -4.689 -33.661  10.093  1.00 40.52           N  
ANISOU 2676  N   SER A 322     5697   5204   4496    202   -451   -353       N  
ATOM   2677  CA  SER A 322      -4.673 -34.334  11.383  1.00 40.38           C  
ANISOU 2677  CA  SER A 322     5655   5149   4538    162   -446   -329       C  
ATOM   2678  C   SER A 322      -4.004 -33.491  12.479  1.00 40.43           C  
ANISOU 2678  C   SER A 322     5591   5203   4566    146   -410   -263       C  
ATOM   2679  O   SER A 322      -4.549 -33.363  13.582  1.00 40.69           O  
ANISOU 2679  O   SER A 322     5588   5232   4642     89   -421   -243       O  
ATOM   2680  CB  SER A 322      -4.009 -35.712  11.261  1.00 40.57           C  
ANISOU 2680  CB  SER A 322     5739   5112   4563    211   -432   -345       C  
ATOM   2681  OG  SER A 322      -4.873 -36.647  10.618  1.00 37.74           O  
ANISOU 2681  OG  SER A 322     5448   4687   4204    197   -477   -411       O  
ATOM   2682  N   TYR A 323      -2.846 -32.901  12.175  1.00 39.90           N  
ANISOU 2682  N   TYR A 323     5506   5186   4468    192   -368   -230       N  
ATOM   2683  CA  TYR A 323      -2.148 -32.060  13.152  1.00 39.81           C  
ANISOU 2683  CA  TYR A 323     5428   5223   4474    170   -340   -174       C  
ATOM   2684  C   TYR A 323      -2.924 -30.792  13.492  1.00 39.49           C  
ANISOU 2684  C   TYR A 323     5355   5208   4440    113   -357   -164       C  
ATOM   2685  O   TYR A 323      -2.897 -30.321  14.640  1.00 41.12           O  
ANISOU 2685  O   TYR A 323     5518   5430   4676     72   -356   -133       O  
ATOM   2686  CB  TYR A 323      -0.722 -31.727  12.706  1.00 40.66           C  
ANISOU 2686  CB  TYR A 323     5514   5385   4552    222   -289   -143       C  
ATOM   2687  CG  TYR A 323       0.246 -32.893  12.822  1.00 44.89           C  
ANISOU 2687  CG  TYR A 323     6057   5909   5091    286   -266   -138       C  
ATOM   2688  CD1 TYR A 323       1.578 -32.765  12.402  1.00 44.55           C  
ANISOU 2688  CD1 TYR A 323     5982   5924   5022    343   -216   -113       C  
ATOM   2689  CD2 TYR A 323      -0.169 -34.128  13.334  1.00 43.31           C  
ANISOU 2689  CD2 TYR A 323     5897   5639   4919    292   -291   -156       C  
ATOM   2690  CE1 TYR A 323       2.468 -33.820  12.510  1.00 41.77           C  
ANISOU 2690  CE1 TYR A 323     5633   5567   4672    417   -195   -109       C  
ATOM   2691  CE2 TYR A 323       0.710 -35.198  13.439  1.00 44.52           C  
ANISOU 2691  CE2 TYR A 323     6069   5773   5073    363   -272   -150       C  
ATOM   2692  CZ  TYR A 323       2.028 -35.039  13.031  1.00 46.68           C  
ANISOU 2692  CZ  TYR A 323     6306   6111   5320    432   -225   -127       C  
ATOM   2693  OH  TYR A 323       2.896 -36.105  13.135  1.00 45.00           O  
ANISOU 2693  OH  TYR A 323     6108   5884   5106    518   -207   -122       O  
ATOM   2694  N   ASN A 324      -3.628 -30.256  12.503  1.00 38.06           N  
ANISOU 2694  N   ASN A 324     5202   5032   4228    118   -377   -193       N  
ATOM   2695  CA  ASN A 324      -4.529 -29.120  12.716  1.00 38.40           C  
ANISOU 2695  CA  ASN A 324     5226   5092   4274     79   -400   -191       C  
ATOM   2696  C   ASN A 324      -5.606 -29.464  13.765  1.00 38.23           C  
ANISOU 2696  C   ASN A 324     5178   5048   4301     27   -432   -204       C  
ATOM   2697  O   ASN A 324      -5.857 -28.682  14.688  1.00 37.52           O  
ANISOU 2697  O   ASN A 324     5050   4976   4230     -7   -430   -182       O  
ATOM   2698  CB  ASN A 324      -5.150 -28.698  11.370  1.00 38.62           C  
ANISOU 2698  CB  ASN A 324     5298   5125   4253    109   -424   -224       C  
ATOM   2699  CG  ASN A 324      -6.103 -27.511  11.486  1.00 42.44           C  
ANISOU 2699  CG  ASN A 324     5767   5624   4733     88   -451   -223       C  
ATOM   2700  OD1 ASN A 324      -7.275 -27.620  11.124  1.00 42.12           O  
ANISOU 2700  OD1 ASN A 324     5734   5580   4692     88   -500   -263       O  
ATOM   2701  ND2 ASN A 324      -5.600 -26.371  11.965  1.00 39.72           N  
ANISOU 2701  ND2 ASN A 324     5405   5299   4388     74   -422   -179       N  
ATOM   2702  N   ILE A 325      -6.214 -30.646  13.629  1.00 37.24           N  
ANISOU 2702  N   ILE A 325     5073   4881   4193     20   -458   -241       N  
ATOM   2703  CA  ILE A 325      -7.262 -31.102  14.540  1.00 36.56           C  
ANISOU 2703  CA  ILE A 325     4961   4775   4155    -37   -480   -252       C  
ATOM   2704  C   ILE A 325      -6.703 -31.342  15.944  1.00 38.05           C  
ANISOU 2704  C   ILE A 325     5124   4958   4374    -61   -450   -206       C  
ATOM   2705  O   ILE A 325      -7.272 -30.885  16.941  1.00 37.75           O  
ANISOU 2705  O   ILE A 325     5048   4937   4358   -102   -450   -190       O  
ATOM   2706  CB  ILE A 325      -7.921 -32.388  14.016  1.00 37.96           C  
ANISOU 2706  CB  ILE A 325     5175   4900   4345    -50   -512   -301       C  
ATOM   2707  CG1 ILE A 325      -8.608 -32.118  12.673  1.00 36.44           C  
ANISOU 2707  CG1 ILE A 325     5005   4722   4117    -29   -555   -354       C  
ATOM   2708  CG2 ILE A 325      -8.923 -32.953  15.030  1.00 35.44           C  
ANISOU 2708  CG2 ILE A 325     4826   4558   4080   -122   -524   -304       C  
ATOM   2709  CD1 ILE A 325      -8.789 -33.347  11.839  1.00 27.93           C  
ANISOU 2709  CD1 ILE A 325     3987   3593   3033    -22   -584   -407       C  
ATOM   2710  N   ILE A 326      -5.585 -32.053  16.011  1.00 37.28           N  
ANISOU 2710  N   ILE A 326     5050   4843   4272    -26   -426   -185       N  
ATOM   2711  CA  ILE A 326      -4.967 -32.394  17.284  1.00 38.77           C  
ANISOU 2711  CA  ILE A 326     5222   5028   4482    -35   -405   -141       C  
ATOM   2712  C   ILE A 326      -4.580 -31.133  18.066  1.00 37.63           C  
ANISOU 2712  C   ILE A 326     5028   4940   4331    -51   -391   -105       C  
ATOM   2713  O   ILE A 326      -4.827 -31.038  19.267  1.00 37.37           O  
ANISOU 2713  O   ILE A 326     4973   4913   4315    -85   -389    -82       O  
ATOM   2714  CB  ILE A 326      -3.744 -33.326  17.073  1.00 39.32           C  
ANISOU 2714  CB  ILE A 326     5322   5077   4542     25   -385   -127       C  
ATOM   2715  CG1 ILE A 326      -4.215 -34.714  16.610  1.00 41.26           C  
ANISOU 2715  CG1 ILE A 326     5632   5246   4800     32   -400   -162       C  
ATOM   2716  CG2 ILE A 326      -2.922 -33.445  18.351  1.00 38.08           C  
ANISOU 2716  CG2 ILE A 326     5137   4936   4395     30   -368    -75       C  
ATOM   2717  CD1 ILE A 326      -3.124 -35.598  16.026  1.00 39.76           C  
ANISOU 2717  CD1 ILE A 326     5487   5029   4590    111   -382   -164       C  
ATOM   2718  N   ALA A 327      -3.996 -30.165  17.366  1.00 37.00           N  
ANISOU 2718  N   ALA A 327     4938   4898   4224    -28   -381   -102       N  
ATOM   2719  CA  ALA A 327      -3.574 -28.914  17.973  1.00 37.04           C  
ANISOU 2719  CA  ALA A 327     4906   4945   4221    -49   -370    -74       C  
ATOM   2720  C   ALA A 327      -4.752 -28.285  18.705  1.00 36.17           C  
ANISOU 2720  C   ALA A 327     4784   4836   4124    -93   -388    -83       C  
ATOM   2721  O   ALA A 327      -4.653 -27.966  19.888  1.00 38.58           O  
ANISOU 2721  O   ALA A 327     5066   5155   4437   -118   -384    -62       O  
ATOM   2722  CB  ALA A 327      -3.013 -27.968  16.917  1.00 37.09           C  
ANISOU 2722  CB  ALA A 327     4918   4979   4196    -29   -355    -72       C  
ATOM   2723  N   VAL A 328      -5.874 -28.152  18.004  1.00 35.96           N  
ANISOU 2723  N   VAL A 328     4769   4798   4096    -95   -409   -118       N  
ATOM   2724  CA  VAL A 328      -7.120 -27.684  18.610  1.00 33.96           C  
ANISOU 2724  CA  VAL A 328     4495   4552   3857   -126   -424   -133       C  
ATOM   2725  C   VAL A 328      -7.493 -28.501  19.851  1.00 32.86           C  
ANISOU 2725  C   VAL A 328     4337   4401   3747   -161   -416   -120       C  
ATOM   2726  O   VAL A 328      -7.859 -27.931  20.862  1.00 34.36           O  
ANISOU 2726  O   VAL A 328     4505   4611   3939   -183   -409   -108       O  
ATOM   2727  CB  VAL A 328      -8.277 -27.670  17.585  1.00 31.51           C  
ANISOU 2727  CB  VAL A 328     4190   4238   3543   -116   -455   -176       C  
ATOM   2728  CG1 VAL A 328      -9.616 -27.487  18.280  1.00 33.38           C  
ANISOU 2728  CG1 VAL A 328     4388   4491   3804   -147   -468   -193       C  
ATOM   2729  CG2 VAL A 328      -8.057 -26.565  16.580  1.00 27.91           C  
ANISOU 2729  CG2 VAL A 328     3757   3798   3049    -79   -461   -179       C  
ATOM   2730  N   TYR A 329      -7.364 -29.824  19.774  1.00 32.94           N  
ANISOU 2730  N   TYR A 329     4367   4375   3773   -164   -415   -121       N  
ATOM   2731  CA  TYR A 329      -7.759 -30.701  20.863  1.00 34.96           C  
ANISOU 2731  CA  TYR A 329     4620   4608   4054   -201   -405   -103       C  
ATOM   2732  C   TYR A 329      -6.810 -30.607  22.069  1.00 36.84           C  
ANISOU 2732  C   TYR A 329     4855   4861   4281   -195   -384    -56       C  
ATOM   2733  O   TYR A 329      -7.227 -30.804  23.207  1.00 37.48           O  
ANISOU 2733  O   TYR A 329     4930   4944   4368   -225   -371    -35       O  
ATOM   2734  CB  TYR A 329      -7.906 -32.157  20.370  1.00 35.99           C  
ANISOU 2734  CB  TYR A 329     4790   4679   4205   -206   -412   -118       C  
ATOM   2735  CG  TYR A 329      -8.283 -33.153  21.457  1.00 38.21           C  
ANISOU 2735  CG  TYR A 329     5083   4924   4512   -249   -395    -92       C  
ATOM   2736  CD1 TYR A 329      -9.346 -32.901  22.335  1.00 38.88           C  
ANISOU 2736  CD1 TYR A 329     5131   5030   4612   -302   -383    -86       C  
ATOM   2737  CD2 TYR A 329      -7.576 -34.346  21.609  1.00 41.81           C  
ANISOU 2737  CD2 TYR A 329     5591   5322   4972   -230   -387    -70       C  
ATOM   2738  CE1 TYR A 329      -9.690 -33.809  23.342  1.00 42.36           C  
ANISOU 2738  CE1 TYR A 329     5588   5438   5071   -346   -359    -55       C  
ATOM   2739  CE2 TYR A 329      -7.914 -35.272  22.615  1.00 42.34           C  
ANISOU 2739  CE2 TYR A 329     5683   5345   5058   -269   -368    -38       C  
ATOM   2740  CZ  TYR A 329      -8.972 -34.996  23.474  1.00 44.02           C  
ANISOU 2740  CZ  TYR A 329     5859   5581   5284   -332   -352    -28       C  
ATOM   2741  OH  TYR A 329      -9.307 -35.896  24.468  1.00 45.95           O  
ANISOU 2741  OH  TYR A 329     6133   5783   5542   -374   -326     10       O  
ATOM   2742  N   ARG A 330      -5.543 -30.291  21.817  1.00 38.13           N  
ANISOU 2742  N   ARG A 330     5021   5041   4424   -157   -381    -39       N  
ATOM   2743  CA  ARG A 330      -4.566 -30.178  22.892  1.00 37.88           C  
ANISOU 2743  CA  ARG A 330     4979   5035   4380   -150   -373      1       C  
ATOM   2744  C   ARG A 330      -4.862 -29.028  23.840  1.00 38.36           C  
ANISOU 2744  C   ARG A 330     5016   5134   4427   -179   -373      6       C  
ATOM   2745  O   ARG A 330      -4.686 -29.164  25.050  1.00 38.99           O  
ANISOU 2745  O   ARG A 330     5093   5225   4496   -190   -369     32       O  
ATOM   2746  CB  ARG A 330      -3.143 -30.102  22.342  1.00 37.99           C  
ANISOU 2746  CB  ARG A 330     4984   5070   4380   -106   -370     13       C  
ATOM   2747  CG  ARG A 330      -2.559 -31.467  22.153  1.00 38.95           C  
ANISOU 2747  CG  ARG A 330     5132   5158   4508    -64   -366     26       C  
ATOM   2748  CD  ARG A 330      -1.286 -31.462  21.355  1.00 43.44           C  
ANISOU 2748  CD  ARG A 330     5687   5755   5065    -10   -357     31       C  
ATOM   2749  NE  ARG A 330      -0.821 -32.835  21.222  1.00 48.61           N  
ANISOU 2749  NE  ARG A 330     6376   6369   5724     43   -352     39       N  
ATOM   2750  CZ  ARG A 330       0.430 -33.196  20.967  1.00 51.39           C  
ANISOU 2750  CZ  ARG A 330     6713   6748   6066    107   -342     55       C  
ATOM   2751  NH1 ARG A 330       1.384 -32.282  20.808  1.00 49.45           N  
ANISOU 2751  NH1 ARG A 330     6406   6574   5807    114   -333     67       N  
ATOM   2752  NH2 ARG A 330       0.724 -34.487  20.886  1.00 51.00           N  
ANISOU 2752  NH2 ARG A 330     6707   6650   6019    165   -339     60       N  
ATOM   2753  N   VAL A 331      -5.316 -27.902  23.298  1.00 37.33           N  
ANISOU 2753  N   VAL A 331     4875   5019   4290   -187   -378    -20       N  
ATOM   2754  CA  VAL A 331      -5.731 -26.781  24.145  1.00 37.09           C  
ANISOU 2754  CA  VAL A 331     4833   5014   4245   -208   -378    -23       C  
ATOM   2755  C   VAL A 331      -6.889 -27.228  25.033  1.00 35.40           C  
ANISOU 2755  C   VAL A 331     4614   4796   4039   -231   -367    -24       C  
ATOM   2756  O   VAL A 331      -6.904 -26.952  26.242  1.00 35.98           O  
ANISOU 2756  O   VAL A 331     4687   4890   4094   -244   -358     -9       O  
ATOM   2757  CB  VAL A 331      -6.118 -25.534  23.323  1.00 36.98           C  
ANISOU 2757  CB  VAL A 331     4823   5005   4224   -202   -385    -50       C  
ATOM   2758  CG1 VAL A 331      -6.443 -24.385  24.236  1.00 38.66           C  
ANISOU 2758  CG1 VAL A 331     5037   5234   4418   -215   -384    -56       C  
ATOM   2759  CG2 VAL A 331      -4.989 -25.141  22.387  1.00 39.21           C  
ANISOU 2759  CG2 VAL A 331     5112   5289   4496   -187   -385    -42       C  
ATOM   2760  N   LEU A 332      -7.838 -27.953  24.443  1.00 35.74           N  
ANISOU 2760  N   LEU A 332     4655   4818   4108   -240   -366    -43       N  
ATOM   2761  CA  LEU A 332      -8.964 -28.505  25.205  1.00 35.09           C  
ANISOU 2761  CA  LEU A 332     4558   4735   4039   -273   -348    -41       C  
ATOM   2762  C   LEU A 332      -8.475 -29.399  26.330  1.00 34.28           C  
ANISOU 2762  C   LEU A 332     4477   4620   3929   -286   -329      3       C  
ATOM   2763  O   LEU A 332      -8.969 -29.312  27.450  1.00 34.68           O  
ANISOU 2763  O   LEU A 332     4522   4689   3965   -306   -307     19       O  
ATOM   2764  CB  LEU A 332      -9.923 -29.278  24.296  1.00 36.75           C  
ANISOU 2764  CB  LEU A 332     4758   4921   4284   -292   -357    -69       C  
ATOM   2765  CG  LEU A 332     -10.779 -28.399  23.383  1.00 40.13           C  
ANISOU 2765  CG  LEU A 332     5158   5375   4715   -279   -378   -113       C  
ATOM   2766  CD1 LEU A 332     -11.463 -29.268  22.350  1.00 38.67           C  
ANISOU 2766  CD1 LEU A 332     4967   5166   4559   -295   -400   -145       C  
ATOM   2767  CD2 LEU A 332     -11.796 -27.581  24.201  1.00 39.92           C  
ANISOU 2767  CD2 LEU A 332     5091   5393   4683   -287   -362   -121       C  
ATOM   2768  N   GLN A 333      -7.482 -30.235  26.032  1.00 32.91           N  
ANISOU 2768  N   GLN A 333     4332   4415   3758   -265   -338     23       N  
ATOM   2769  CA  GLN A 333      -6.914 -31.129  27.030  1.00 34.85           C  
ANISOU 2769  CA  GLN A 333     4607   4644   3992   -261   -326     69       C  
ATOM   2770  C   GLN A 333      -6.258 -30.363  28.183  1.00 36.03           C  
ANISOU 2770  C   GLN A 333     4750   4840   4099   -250   -328     92       C  
ATOM   2771  O   GLN A 333      -6.479 -30.692  29.354  1.00 37.30           O  
ANISOU 2771  O   GLN A 333     4929   5007   4238   -262   -311    123       O  
ATOM   2772  CB  GLN A 333      -5.914 -32.075  26.383  1.00 34.54           C  
ANISOU 2772  CB  GLN A 333     4597   4566   3961   -223   -338     81       C  
ATOM   2773  CG  GLN A 333      -6.537 -33.183  25.573  1.00 35.77           C  
ANISOU 2773  CG  GLN A 333     4781   4657   4151   -237   -335     63       C  
ATOM   2774  CD  GLN A 333      -5.491 -34.024  24.864  1.00 36.61           C  
ANISOU 2774  CD  GLN A 333     4925   4726   4260   -183   -346     68       C  
ATOM   2775  OE1 GLN A 333      -5.286 -35.200  25.189  1.00 38.92           O  
ANISOU 2775  OE1 GLN A 333     5267   4962   4557   -172   -339     95       O  
ATOM   2776  NE2 GLN A 333      -4.814 -33.425  23.903  1.00 32.97           N  
ANISOU 2776  NE2 GLN A 333     4443   4292   3790   -146   -358     45       N  
ATOM   2777  N   ILE A 334      -5.475 -29.331  27.841  1.00 36.50           N  
ANISOU 2777  N   ILE A 334     4790   4932   4145   -231   -349     76       N  
ATOM   2778  CA  ILE A 334      -4.805 -28.471  28.825  1.00 34.82           C  
ANISOU 2778  CA  ILE A 334     4571   4764   3894   -228   -361     87       C  
ATOM   2779  C   ILE A 334      -5.826 -27.830  29.760  1.00 35.90           C  
ANISOU 2779  C   ILE A 334     4712   4921   4009   -253   -343     76       C  
ATOM   2780  O   ILE A 334      -5.661 -27.874  30.972  1.00 38.60           O  
ANISOU 2780  O   ILE A 334     5069   5283   4313   -253   -340     99       O  
ATOM   2781  CB  ILE A 334      -3.907 -27.390  28.149  1.00 34.69           C  
ANISOU 2781  CB  ILE A 334     4533   4772   3876   -221   -383     67       C  
ATOM   2782  CG1 ILE A 334      -2.750 -28.051  27.380  1.00 30.99           C  
ANISOU 2782  CG1 ILE A 334     4053   4301   3421   -190   -393     82       C  
ATOM   2783  CG2 ILE A 334      -3.375 -26.383  29.188  1.00 32.12           C  
ANISOU 2783  CG2 ILE A 334     4204   4487   3513   -234   -401     66       C  
ATOM   2784  CD1 ILE A 334      -1.973 -27.118  26.484  1.00 27.06           C  
ANISOU 2784  CD1 ILE A 334     3529   3824   2928   -190   -401     66       C  
ATOM   2785  N   ASP A 335      -6.891 -27.265  29.197  1.00 37.73           N  
ANISOU 2785  N   ASP A 335     4928   5149   4259   -266   -332     42       N  
ATOM   2786  CA  ASP A 335      -7.968 -26.680  30.012  1.00 37.86           C  
ANISOU 2786  CA  ASP A 335     4940   5189   4255   -278   -308     28       C  
ATOM   2787  C   ASP A 335      -8.739 -27.697  30.841  1.00 38.93           C  
ANISOU 2787  C   ASP A 335     5080   5323   4389   -300   -272     57       C  
ATOM   2788  O   ASP A 335      -9.186 -27.385  31.948  1.00 38.46           O  
ANISOU 2788  O   ASP A 335     5028   5293   4293   -304   -247     64       O  
ATOM   2789  CB  ASP A 335      -8.960 -25.887  29.162  1.00 36.07           C  
ANISOU 2789  CB  ASP A 335     4688   4965   4050   -275   -307    -14       C  
ATOM   2790  CG  ASP A 335      -9.836 -24.985  30.003  1.00 38.77           C  
ANISOU 2790  CG  ASP A 335     5026   5340   4364   -269   -286    -34       C  
ATOM   2791  OD1 ASP A 335      -9.282 -24.107  30.713  1.00 39.93           O  
ANISOU 2791  OD1 ASP A 335     5199   5500   4471   -258   -295    -40       O  
ATOM   2792  OD2 ASP A 335     -11.074 -25.161  29.966  1.00 39.57           O  
ANISOU 2792  OD2 ASP A 335     5095   5456   4482   -275   -260    -47       O  
ATOM   2793  N   ALA A 336      -8.909 -28.908  30.316  1.00 37.61           N  
ANISOU 2793  N   ALA A 336     4915   5117   4258   -316   -265     74       N  
ATOM   2794  CA  ALA A 336      -9.562 -29.943  31.107  1.00 40.18           C  
ANISOU 2794  CA  ALA A 336     5256   5429   4584   -347   -226    110       C  
ATOM   2795  C   ALA A 336      -8.770 -30.128  32.399  1.00 39.36           C  
ANISOU 2795  C   ALA A 336     5193   5337   4424   -330   -222    155       C  
ATOM   2796  O   ALA A 336      -9.353 -30.320  33.466  1.00 42.67           O  
ANISOU 2796  O   ALA A 336     5626   5774   4813   -347   -183    181       O  
ATOM   2797  CB  ALA A 336      -9.673 -31.262  30.326  1.00 38.91           C  
ANISOU 2797  CB  ALA A 336     5108   5207   4469   -368   -226    120       C  
ATOM   2798  N   LYS A 337      -7.445 -30.032  32.284  1.00 36.78           N  
ANISOU 2798  N   LYS A 337     4882   5010   4082   -293   -262    163       N  
ATOM   2799  CA  LYS A 337      -6.537 -30.161  33.422  1.00 36.16           C  
ANISOU 2799  CA  LYS A 337     4838   4953   3949   -268   -275    202       C  
ATOM   2800  C   LYS A 337      -6.414 -28.879  34.249  1.00 33.80           C  
ANISOU 2800  C   LYS A 337     4535   4711   3598   -262   -287    179       C  
ATOM   2801  O   LYS A 337      -6.606 -28.905  35.471  1.00 30.52           O  
ANISOU 2801  O   LYS A 337     4149   4320   3128   -260   -269    202       O  
ATOM   2802  CB  LYS A 337      -5.144 -30.621  32.962  1.00 36.96           C  
ANISOU 2802  CB  LYS A 337     4944   5042   4057   -228   -316    218       C  
ATOM   2803  CG  LYS A 337      -4.128 -30.747  34.108  1.00 39.75           C  
ANISOU 2803  CG  LYS A 337     5323   5429   4352   -193   -343    256       C  
ATOM   2804  CD  LYS A 337      -2.683 -30.866  33.623  1.00 38.21           C  
ANISOU 2804  CD  LYS A 337     5105   5248   4164   -149   -389    260       C  
ATOM   2805  CE  LYS A 337      -1.731 -31.065  34.803  1.00 39.88           C  
ANISOU 2805  CE  LYS A 337     5335   5501   4316   -110   -423    298       C  
ATOM   2806  NZ  LYS A 337      -0.337 -30.613  34.494  1.00 43.91           N  
ANISOU 2806  NZ  LYS A 337     5795   6062   4827    -81   -476    285       N  
ATOM   2807  N   ARG A 338      -6.072 -27.771  33.591  1.00 31.00           N  
ANISOU 2807  N   ARG A 338     4152   4370   3255   -259   -315    135       N  
ATOM   2808  CA  ARG A 338      -5.824 -26.509  34.306  1.00 33.96           C  
ANISOU 2808  CA  ARG A 338     4535   4786   3584   -256   -335    107       C  
ATOM   2809  C   ARG A 338      -7.089 -25.781  34.749  1.00 33.09           C  
ANISOU 2809  C   ARG A 338     4428   4691   3455   -265   -297     78       C  
ATOM   2810  O   ARG A 338      -7.102 -25.159  35.808  1.00 32.20           O  
ANISOU 2810  O   ARG A 338     4343   4609   3283   -257   -297     68       O  
ATOM   2811  CB  ARG A 338      -4.911 -25.571  33.506  1.00 32.28           C  
ANISOU 2811  CB  ARG A 338     4301   4576   3389   -257   -377     75       C  
ATOM   2812  CG  ARG A 338      -3.446 -26.033  33.389  1.00 34.54           C  
ANISOU 2812  CG  ARG A 338     4573   4874   3676   -243   -417    100       C  
ATOM   2813  CD  ARG A 338      -2.686 -25.947  34.719  1.00 35.57           C  
ANISOU 2813  CD  ARG A 338     4722   5048   3745   -234   -449    116       C  
ATOM   2814  NE  ARG A 338      -1.243 -25.935  34.501  1.00 33.78           N  
ANISOU 2814  NE  ARG A 338     4461   4850   3523   -225   -498    123       N  
ATOM   2815  CZ  ARG A 338      -0.357 -25.336  35.299  1.00 36.12           C  
ANISOU 2815  CZ  ARG A 338     4752   5194   3777   -232   -546    113       C  
ATOM   2816  NH1 ARG A 338      -0.762 -24.690  36.393  1.00 25.89           N  
ANISOU 2816  NH1 ARG A 338     3497   3917   2424   -243   -553     93       N  
ATOM   2817  NH2 ARG A 338       0.943 -25.371  34.991  1.00 30.83           N  
ANISOU 2817  NH2 ARG A 338     4033   4560   3122   -227   -587    119       N  
ATOM   2818  N   GLN A 339      -8.140 -25.858  33.933  1.00 34.71           N  
ANISOU 2818  N   GLN A 339     4603   4878   3706   -275   -269     61       N  
ATOM   2819  CA  GLN A 339      -9.461 -25.303  34.270  1.00 35.61           C  
ANISOU 2819  CA  GLN A 339     4705   5015   3810   -274   -227     35       C  
ATOM   2820  C   GLN A 339      -9.462 -23.772  34.365  1.00 37.12           C  
ANISOU 2820  C   GLN A 339     4909   5220   3973   -252   -245    -14       C  
ATOM   2821  O   GLN A 339     -10.066 -23.191  35.279  1.00 38.57           O  
ANISOU 2821  O   GLN A 339     5110   5434   4111   -236   -219    -31       O  
ATOM   2822  CB  GLN A 339     -10.054 -25.993  35.520  1.00 36.33           C  
ANISOU 2822  CB  GLN A 339     4812   5132   3860   -283   -177     72       C  
ATOM   2823  CG  GLN A 339     -10.484 -27.455  35.232  1.00 39.97           C  
ANISOU 2823  CG  GLN A 339     5260   5564   4364   -317   -147    115       C  
ATOM   2824  CD  GLN A 339     -10.913 -28.274  36.457  1.00 44.74           C  
ANISOU 2824  CD  GLN A 339     5893   6182   4926   -334    -93    166       C  
ATOM   2825  OE1 GLN A 339     -10.919 -29.510  36.406  1.00 47.31           O  
ANISOU 2825  OE1 GLN A 339     6233   6469   5274   -361    -76    212       O  
ATOM   2826  NE2 GLN A 339     -11.277 -27.601  37.547  1.00 41.22           N  
ANISOU 2826  NE2 GLN A 339     5463   5785   4414   -317    -64    160       N  
ATOM   2827  N   PHE A 340      -8.805 -23.135  33.390  1.00 37.33           N  
ANISOU 2827  N   PHE A 340     4621   4660   4902    524   -548   -422       N  
ATOM   2828  CA  PHE A 340      -8.673 -21.673  33.347  1.00 37.16           C  
ANISOU 2828  CA  PHE A 340     4497   4709   4914    523   -483   -407       C  
ATOM   2829  C   PHE A 340      -9.907 -20.951  32.796  1.00 38.00           C  
ANISOU 2829  C   PHE A 340     4573   4906   4958    458   -381   -345       C  
ATOM   2830  O   PHE A 340     -10.218 -19.831  33.227  1.00 37.82           O  
ANISOU 2830  O   PHE A 340     4528   4919   4921    448   -347   -309       O  
ATOM   2831  CB  PHE A 340      -7.440 -21.241  32.539  1.00 35.35           C  
ANISOU 2831  CB  PHE A 340     4143   4505   4784    571   -462   -485       C  
ATOM   2832  CG  PHE A 340      -6.118 -21.638  33.150  1.00 32.37           C  
ANISOU 2832  CG  PHE A 340     3753   4058   4489    652   -568   -572       C  
ATOM   2833  CD1 PHE A 340      -5.938 -21.667  34.534  1.00 32.74           C  
ANISOU 2833  CD1 PHE A 340     3883   4030   4526    687   -670   -563       C  
ATOM   2834  CD2 PHE A 340      -5.036 -21.939  32.332  1.00 29.88           C  
ANISOU 2834  CD2 PHE A 340     3338   3753   4262    698   -569   -675       C  
ATOM   2835  CE1 PHE A 340      -4.716 -22.027  35.086  1.00 32.05           C  
ANISOU 2835  CE1 PHE A 340     3784   3877   4516    778   -788   -656       C  
ATOM   2836  CE2 PHE A 340      -3.803 -22.291  32.876  1.00 31.73           C  
ANISOU 2836  CE2 PHE A 340     3538   3934   4585    786   -677   -779       C  
ATOM   2837  CZ  PHE A 340      -3.643 -22.334  34.257  1.00 31.73           C  
ANISOU 2837  CZ  PHE A 340     3625   3857   4575    833   -796   -770       C  
ATOM   2838  N   ILE A 341     -10.584 -21.563  31.822  1.00 37.14           N  
ANISOU 2838  N   ILE A 341     4463   4834   4814    423   -341   -340       N  
ATOM   2839  CA  ILE A 341     -11.816 -20.988  31.287  1.00 36.77           C  
ANISOU 2839  CA  ILE A 341     4389   4874   4707    374   -266   -298       C  
ATOM   2840  C   ILE A 341     -12.815 -20.914  32.432  1.00 38.17           C  
ANISOU 2840  C   ILE A 341     4627   5053   4821    328   -272   -254       C  
ATOM   2841  O   ILE A 341     -13.371 -19.862  32.703  1.00 39.34           O  
ANISOU 2841  O   ILE A 341     4743   5255   4948    324   -234   -226       O  
ATOM   2842  CB  ILE A 341     -12.414 -21.831  30.129  1.00 38.88           C  
ANISOU 2842  CB  ILE A 341     4654   5175   4945    344   -240   -310       C  
ATOM   2843  CG1 ILE A 341     -11.409 -22.002  28.979  1.00 38.64           C  
ANISOU 2843  CG1 ILE A 341     4573   5138   4970    384   -225   -360       C  
ATOM   2844  CG2 ILE A 341     -13.737 -21.227  29.624  1.00 32.85           C  
ANISOU 2844  CG2 ILE A 341     3856   4504   4121    308   -182   -281       C  
ATOM   2845  CD1 ILE A 341     -11.258 -20.783  28.073  1.00 40.54           C  
ANISOU 2845  CD1 ILE A 341     4747   5439   5218    396   -151   -360       C  
ATOM   2846  N   ASN A 342     -13.010 -22.038  33.116  1.00 40.25           N  
ANISOU 2846  N   ASN A 342     4993   5251   5050    292   -318   -254       N  
ATOM   2847  CA  ASN A 342     -13.885 -22.110  34.275  1.00 39.90           C  
ANISOU 2847  CA  ASN A 342     5030   5194   4937    229   -313   -222       C  
ATOM   2848  C   ASN A 342     -13.550 -21.029  35.309  1.00 40.90           C  
ANISOU 2848  C   ASN A 342     5156   5308   5075    263   -325   -201       C  
ATOM   2849  O   ASN A 342     -14.445 -20.373  35.848  1.00 42.40           O  
ANISOU 2849  O   ASN A 342     5339   5549   5220    225   -279   -176       O  
ATOM   2850  CB  ASN A 342     -13.785 -23.504  34.898  1.00 42.46           C  
ANISOU 2850  CB  ASN A 342     5505   5411   5219    191   -372   -230       C  
ATOM   2851  CG  ASN A 342     -14.446 -23.590  36.262  1.00 44.48           C  
ANISOU 2851  CG  ASN A 342     5880   5624   5395    121   -368   -201       C  
ATOM   2852  OD1 ASN A 342     -15.673 -23.584  36.367  1.00 48.33           O  
ANISOU 2852  OD1 ASN A 342     6364   6177   5823     27   -293   -192       O  
ATOM   2853  ND2 ASN A 342     -13.630 -23.678  37.317  1.00 39.59           N  
ANISOU 2853  ND2 ASN A 342     5371   4896   4775    164   -448   -196       N  
ATOM   2854  N   LEU A 343     -12.259 -20.847  35.574  1.00 38.67           N  
ANISOU 2854  N   LEU A 343     4874   4961   4857    336   -389   -221       N  
ATOM   2855  CA  LEU A 343     -11.806 -19.864  36.540  1.00 37.17           C  
ANISOU 2855  CA  LEU A 343     4687   4750   4686    371   -412   -208       C  
ATOM   2856  C   LEU A 343     -12.207 -18.451  36.112  1.00 37.53           C  
ANISOU 2856  C   LEU A 343     4630   4892   4740    377   -337   -188       C  
ATOM   2857  O   LEU A 343     -12.595 -17.624  36.949  1.00 37.36           O  
ANISOU 2857  O   LEU A 343     4624   4882   4688    371   -323   -159       O  
ATOM   2858  CB  LEU A 343     -10.290 -19.971  36.715  1.00 36.86           C  
ANISOU 2858  CB  LEU A 343     4639   4637   4729    452   -499   -258       C  
ATOM   2859  CG  LEU A 343      -9.563 -18.829  37.424  1.00 35.91           C  
ANISOU 2859  CG  LEU A 343     4484   4506   4655    497   -523   -263       C  
ATOM   2860  CD1 LEU A 343      -9.874 -18.807  38.918  1.00 36.72           C  
ANISOU 2860  CD1 LEU A 343     4714   4542   4696    486   -574   -229       C  
ATOM   2861  CD2 LEU A 343      -8.063 -18.931  37.171  1.00 34.73           C  
ANISOU 2861  CD2 LEU A 343     4269   4319   4610    572   -590   -343       C  
ATOM   2862  N   SER A 344     -12.117 -18.203  34.806  1.00 36.89           N  
ANISOU 2862  N   SER A 344     4460   4869   4688    390   -291   -204       N  
ATOM   2863  CA  SER A 344     -12.465 -16.922  34.191  1.00 36.98           C  
ANISOU 2863  CA  SER A 344     4402   4956   4695    402   -227   -188       C  
ATOM   2864  C   SER A 344     -13.941 -16.597  34.337  1.00 36.27           C  
ANISOU 2864  C   SER A 344     4313   4938   4531    369   -187   -160       C  
ATOM   2865  O   SER A 344     -14.299 -15.500  34.777  1.00 36.90           O  
ANISOU 2865  O   SER A 344     4382   5047   4590    386   -168   -140       O  
ATOM   2866  CB  SER A 344     -12.093 -16.927  32.703  1.00 36.07           C  
ANISOU 2866  CB  SER A 344     4226   4871   4607    415   -189   -215       C  
ATOM   2867  OG  SER A 344     -10.701 -17.070  32.546  1.00 37.69           O  
ANISOU 2867  OG  SER A 344     4405   5026   4889    443   -212   -261       O  
ATOM   2868  N   LEU A 345     -14.790 -17.549  33.957  1.00 34.08           N  
ANISOU 2868  N   LEU A 345     4043   4691   4216    322   -174   -169       N  
ATOM   2869  CA  LEU A 345     -16.225 -17.396  34.132  1.00 34.81           C  
ANISOU 2869  CA  LEU A 345     4117   4861   4246    282   -136   -168       C  
ATOM   2870  C   LEU A 345     -16.569 -17.139  35.606  1.00 36.02           C  
ANISOU 2870  C   LEU A 345     4324   4996   4367    253   -135   -151       C  
ATOM   2871  O   LEU A 345     -17.335 -16.228  35.909  1.00 38.30           O  
ANISOU 2871  O   LEU A 345     4574   5349   4627    263   -105   -151       O  
ATOM   2872  CB  LEU A 345     -16.960 -18.616  33.589  1.00 33.21           C  
ANISOU 2872  CB  LEU A 345     3917   4684   4015    218   -124   -192       C  
ATOM   2873  CG  LEU A 345     -16.736 -18.920  32.103  1.00 32.94           C  
ANISOU 2873  CG  LEU A 345     3840   4673   4004    244   -122   -211       C  
ATOM   2874  CD1 LEU A 345     -16.969 -20.400  31.826  1.00 31.35           C  
ANISOU 2874  CD1 LEU A 345     3678   4446   3786    180   -132   -232       C  
ATOM   2875  CD2 LEU A 345     -17.631 -18.055  31.204  1.00 26.24           C  
ANISOU 2875  CD2 LEU A 345     2917   3923   3130    276    -95   -224       C  
ATOM   2876  N   ASP A 346     -15.979 -17.909  36.519  1.00 37.35           N  
ANISOU 2876  N   ASP A 346     4588   5069   4533    226   -176   -143       N  
ATOM   2877  CA  ASP A 346     -16.261 -17.749  37.959  1.00 38.63           C  
ANISOU 2877  CA  ASP A 346     4832   5196   4650    191   -176   -126       C  
ATOM   2878  C   ASP A 346     -15.961 -16.343  38.437  1.00 37.88           C  
ANISOU 2878  C   ASP A 346     4706   5113   4574    254   -178   -108       C  
ATOM   2879  O   ASP A 346     -16.806 -15.694  39.032  1.00 38.18           O  
ANISOU 2879  O   ASP A 346     4735   5203   4569    237   -137   -106       O  
ATOM   2880  CB  ASP A 346     -15.451 -18.732  38.799  1.00 37.57           C  
ANISOU 2880  CB  ASP A 346     4836   4932   4508    177   -244   -119       C  
ATOM   2881  CG  ASP A 346     -16.149 -20.052  38.996  1.00 42.88           C  
ANISOU 2881  CG  ASP A 346     5607   5575   5112     78   -227   -129       C  
ATOM   2882  OD1 ASP A 346     -17.313 -20.200  38.564  1.00 47.36           O  
ANISOU 2882  OD1 ASP A 346     6117   6233   5644      7   -152   -148       O  
ATOM   2883  OD2 ASP A 346     -15.528 -20.954  39.597  1.00 47.10           O  
ANISOU 2883  OD2 ASP A 346     6282   5988   5625     70   -293   -125       O  
ATOM   2884  N   MET A 347     -14.744 -15.887  38.161  1.00 39.61           N  
ANISOU 2884  N   MET A 347     4906   5287   4858    321   -223   -105       N  
ATOM   2885  CA  MET A 347     -14.280 -14.585  38.600  1.00 40.34           C  
ANISOU 2885  CA  MET A 347     4982   5375   4972    374   -230    -90       C  
ATOM   2886  C   MET A 347     -15.035 -13.461  37.899  1.00 38.76           C  
ANISOU 2886  C   MET A 347     4704   5268   4754    400   -175    -87       C  
ATOM   2887  O   MET A 347     -15.431 -12.481  38.537  1.00 39.43           O  
ANISOU 2887  O   MET A 347     4795   5374   4812    419   -161    -75       O  
ATOM   2888  CB  MET A 347     -12.775 -14.456  38.366  1.00 42.97           C  
ANISOU 2888  CB  MET A 347     5299   5642   5384    423   -282   -107       C  
ATOM   2889  CG  MET A 347     -11.902 -15.061  39.475  1.00 51.27           C  
ANISOU 2889  CG  MET A 347     6437   6589   6454    435   -367   -117       C  
ATOM   2890  SD  MET A 347     -10.140 -15.213  39.025  1.00 60.92           S  
ANISOU 2890  SD  MET A 347     7605   7754   7789    496   -437   -176       S  
ATOM   2891  CE  MET A 347      -9.656 -13.499  38.764  1.00 57.37           C  
ANISOU 2891  CE  MET A 347     7072   7346   7382    519   -390   -178       C  
ATOM   2892  N   GLY A 348     -15.238 -13.612  36.591  1.00 36.97           N  
ANISOU 2892  N   GLY A 348     4419   5091   4537    408   -151   -102       N  
ATOM   2893  CA  GLY A 348     -15.947 -12.616  35.800  1.00 35.31           C  
ANISOU 2893  CA  GLY A 348     4159   4957   4301    447   -118   -105       C  
ATOM   2894  C   GLY A 348     -17.355 -12.365  36.300  1.00 35.85           C  
ANISOU 2894  C   GLY A 348     4206   5103   4311    438    -94   -118       C  
ATOM   2895  O   GLY A 348     -17.758 -11.214  36.481  1.00 36.86           O  
ANISOU 2895  O   GLY A 348     4325   5265   4416    488    -88   -117       O  
ATOM   2896  N   TYR A 349     -18.098 -13.447  36.528  1.00 36.04           N  
ANISOU 2896  N   TYR A 349     4224   5156   4311    370    -77   -141       N  
ATOM   2897  CA  TYR A 349     -19.484 -13.358  36.951  1.00 36.62           C  
ANISOU 2897  CA  TYR A 349     4256   5320   4337    341    -39   -178       C  
ATOM   2898  C   TYR A 349     -19.618 -12.915  38.395  1.00 39.02           C  
ANISOU 2898  C   TYR A 349     4609   5603   4613    323    -24   -168       C  
ATOM   2899  O   TYR A 349     -20.587 -12.225  38.743  1.00 43.13           O  
ANISOU 2899  O   TYR A 349     5082   6203   5102    339      6   -203       O  
ATOM   2900  CB  TYR A 349     -20.202 -14.688  36.753  1.00 37.36           C  
ANISOU 2900  CB  TYR A 349     4335   5449   4412    249    -11   -214       C  
ATOM   2901  CG  TYR A 349     -20.614 -14.940  35.327  1.00 34.88           C  
ANISOU 2901  CG  TYR A 349     3947   5198   4108    271    -17   -245       C  
ATOM   2902  CD1 TYR A 349     -21.511 -14.097  34.686  1.00 35.29           C  
ANISOU 2902  CD1 TYR A 349     3914   5350   4145    337    -18   -288       C  
ATOM   2903  CD2 TYR A 349     -20.111 -16.026  34.619  1.00 35.04           C  
ANISOU 2903  CD2 TYR A 349     3993   5175   4148    235    -31   -239       C  
ATOM   2904  CE1 TYR A 349     -21.890 -14.323  33.373  1.00 39.89           C  
ANISOU 2904  CE1 TYR A 349     4445   5982   4729    365    -37   -320       C  
ATOM   2905  CE2 TYR A 349     -20.485 -16.262  33.298  1.00 37.93           C  
ANISOU 2905  CE2 TYR A 349     4301   5594   4517    256    -38   -268       C  
ATOM   2906  CZ  TYR A 349     -21.372 -15.406  32.686  1.00 36.62           C  
ANISOU 2906  CZ  TYR A 349     4058   5524   4333    319    -42   -306       C  
ATOM   2907  OH  TYR A 349     -21.751 -15.635  31.388  1.00 37.29           O  
ANISOU 2907  OH  TYR A 349     4102   5655   4413    346    -62   -338       O  
ATOM   2908  N   TYR A 350     -18.660 -13.311  39.235  1.00 35.47           N  
ANISOU 2908  N   TYR A 350     4255   5048   4174    296    -51   -131       N  
ATOM   2909  CA  TYR A 350     -18.624 -12.833  40.606  1.00 35.75           C  
ANISOU 2909  CA  TYR A 350     4360   5044   4180    287    -48   -116       C  
ATOM   2910  C   TYR A 350     -18.445 -11.303  40.628  1.00 35.90           C  
ANISOU 2910  C   TYR A 350     4348   5081   4210    379    -60   -104       C  
ATOM   2911  O   TYR A 350     -19.087 -10.605  41.416  1.00 35.23           O  
ANISOU 2911  O   TYR A 350     4267   5031   4088    388    -34   -116       O  
ATOM   2912  CB  TYR A 350     -17.501 -13.518  41.388  1.00 37.96           C  
ANISOU 2912  CB  TYR A 350     4759   5195   4470    264   -101    -83       C  
ATOM   2913  CG  TYR A 350     -17.391 -13.078  42.839  1.00 37.37           C  
ANISOU 2913  CG  TYR A 350     4781   5064   4356    256   -109    -65       C  
ATOM   2914  CD1 TYR A 350     -18.139 -13.704  43.838  1.00 36.86           C  
ANISOU 2914  CD1 TYR A 350     4804   4987   4215    165    -64    -77       C  
ATOM   2915  CD2 TYR A 350     -16.534 -12.046  43.211  1.00 36.26           C  
ANISOU 2915  CD2 TYR A 350     4653   4877   4248    330   -156    -42       C  
ATOM   2916  CE1 TYR A 350     -18.038 -13.313  45.171  1.00 36.91           C  
ANISOU 2916  CE1 TYR A 350     4917   4934   4173    154    -69    -61       C  
ATOM   2917  CE2 TYR A 350     -16.424 -11.647  44.550  1.00 36.00           C  
ANISOU 2917  CE2 TYR A 350     4716   4787   4174    325   -169    -27       C  
ATOM   2918  CZ  TYR A 350     -17.179 -12.282  45.517  1.00 36.57           C  
ANISOU 2918  CZ  TYR A 350     4881   4846   4166    242   -127    -35       C  
ATOM   2919  OH  TYR A 350     -17.077 -11.886  46.831  1.00 38.09           O  
ANISOU 2919  OH  TYR A 350     5186   4978   4309    235   -138    -20       O  
ATOM   2920  N   ALA A 351     -17.582 -10.800  39.751  1.00 32.01           N  
ANISOU 2920  N   ALA A 351     3835   4561   3765    441    -94    -85       N  
ATOM   2921  CA  ALA A 351     -17.233  -9.387  39.745  1.00 34.65           C  
ANISOU 2921  CA  ALA A 351     4173   4887   4106    515   -108    -69       C  
ATOM   2922  C   ALA A 351     -18.211  -8.559  38.921  1.00 35.40           C  
ANISOU 2922  C   ALA A 351     4208   5071   4169    575    -90    -95       C  
ATOM   2923  O   ALA A 351     -18.278  -7.340  39.077  1.00 33.22           O  
ANISOU 2923  O   ALA A 351     3951   4797   3875    639    -99    -89       O  
ATOM   2924  CB  ALA A 351     -15.810  -9.199  39.228  1.00 36.37           C  
ANISOU 2924  CB  ALA A 351     4408   5028   4383    535   -141    -48       C  
ATOM   2925  N   LYS A 352     -18.968  -9.243  38.061  1.00 36.28           N  
ANISOU 2925  N   LYS A 352     4258   5254   4274    560    -74   -129       N  
ATOM   2926  CA  LYS A 352     -19.901  -8.625  37.117  1.00 37.39           C  
ANISOU 2926  CA  LYS A 352     4342   5479   4386    628    -78   -167       C  
ATOM   2927  C   LYS A 352     -19.201  -7.747  36.075  1.00 38.55           C  
ANISOU 2927  C   LYS A 352     4532   5580   4535    698   -106   -141       C  
ATOM   2928  O   LYS A 352     -19.630  -6.624  35.795  1.00 40.75           O  
ANISOU 2928  O   LYS A 352     4829   5878   4775    782   -127   -152       O  
ATOM   2929  CB  LYS A 352     -21.045  -7.905  37.842  1.00 37.19           C  
ANISOU 2929  CB  LYS A 352     4280   5531   4320    668    -67   -213       C  
ATOM   2930  CG  LYS A 352     -21.845  -8.857  38.730  1.00 40.85           C  
ANISOU 2930  CG  LYS A 352     4701   6050   4772    574    -17   -255       C  
ATOM   2931  CD  LYS A 352     -23.141  -8.259  39.249  1.00 39.21           C  
ANISOU 2931  CD  LYS A 352     4421   5950   4529    607      8   -332       C  
ATOM   2932  CE  LYS A 352     -23.700  -9.136  40.358  1.00 41.51           C  
ANISOU 2932  CE  LYS A 352     4703   6269   4800    485     81   -367       C  
ATOM   2933  NZ  LYS A 352     -24.867  -8.521  41.066  1.00 43.86           N  
ANISOU 2933  NZ  LYS A 352     4928   6671   5066    503    124   -452       N  
ATOM   2934  N   ILE A 353     -18.125  -8.287  35.503  1.00 35.97           N  
ANISOU 2934  N   ILE A 353     4230   5189   4248    660   -104   -112       N  
ATOM   2935  CA  ILE A 353     -17.383  -7.643  34.426  1.00 34.70           C  
ANISOU 2935  CA  ILE A 353     4116   4981   4086    694   -107    -95       C  
ATOM   2936  C   ILE A 353     -17.552  -8.427  33.125  1.00 34.89           C  
ANISOU 2936  C   ILE A 353     4115   5033   4110    683   -102   -114       C  
ATOM   2937  O   ILE A 353     -18.132  -9.515  33.120  1.00 37.44           O  
ANISOU 2937  O   ILE A 353     4379   5405   4441    644   -100   -138       O  
ATOM   2938  CB  ILE A 353     -15.863  -7.554  34.762  1.00 36.15           C  
ANISOU 2938  CB  ILE A 353     4340   5071   4325    653    -97    -66       C  
ATOM   2939  CG1 ILE A 353     -15.272  -8.947  35.037  1.00 35.64           C  
ANISOU 2939  CG1 ILE A 353     4239   4984   4318    588    -99    -72       C  
ATOM   2940  CG2 ILE A 353     -15.624  -6.610  35.932  1.00 35.59           C  
ANISOU 2940  CG2 ILE A 353     4308   4963   4249    671   -109    -47       C  
ATOM   2941  CD1 ILE A 353     -13.812  -8.951  35.480  1.00 31.97           C  
ANISOU 2941  CD1 ILE A 353     3792   4438   3919    562   -108    -68       C  
ATOM   2942  N   GLN A 354     -17.049  -7.877  32.024  1.00 33.62           N  
ANISOU 2942  N   GLN A 354     4010   4835   3930    708    -96   -105       N  
ATOM   2943  CA  GLN A 354     -16.893  -8.646  30.799  1.00 34.43           C  
ANISOU 2943  CA  GLN A 354     4106   4941   4035    686    -84   -118       C  
ATOM   2944  C   GLN A 354     -15.925  -9.761  31.144  1.00 35.02           C  
ANISOU 2944  C   GLN A 354     4144   4979   4184    610    -63   -115       C  
ATOM   2945  O   GLN A 354     -14.970  -9.528  31.891  1.00 34.92           O  
ANISOU 2945  O   GLN A 354     4142   4911   4215    587    -56   -101       O  
ATOM   2946  CB  GLN A 354     -16.282  -7.780  29.701  1.00 36.82           C  
ANISOU 2946  CB  GLN A 354     4506   5186   4298    708    -64   -106       C  
ATOM   2947  CG  GLN A 354     -17.048  -6.498  29.382  1.00 43.41           C  
ANISOU 2947  CG  GLN A 354     5424   6024   5047    798    -99   -106       C  
ATOM   2948  CD  GLN A 354     -16.504  -5.784  28.165  1.00 47.71           C  
ANISOU 2948  CD  GLN A 354     6101   6498   5529    806    -76    -95       C  
ATOM   2949  OE1 GLN A 354     -17.121  -5.798  27.093  1.00 50.97           O  
ANISOU 2949  OE1 GLN A 354     6565   6925   5878    854   -105   -112       O  
ATOM   2950  NE2 GLN A 354     -15.337  -5.165  28.314  1.00 49.12           N  
ANISOU 2950  NE2 GLN A 354     6345   6597   5723    752    -23    -72       N  
ATOM   2951  N   ILE A 355     -16.141 -10.967  30.621  1.00 34.23           N  
ANISOU 2951  N   ILE A 355     4002   4905   4098    578    -63   -135       N  
ATOM   2952  CA  ILE A 355     -15.273 -12.084  31.015  1.00 33.50           C  
ANISOU 2952  CA  ILE A 355     3887   4771   4071    521    -61   -139       C  
ATOM   2953  C   ILE A 355     -13.806 -11.806  30.704  1.00 36.19           C  
ANISOU 2953  C   ILE A 355     4246   5043   4460    508    -36   -142       C  
ATOM   2954  O   ILE A 355     -12.941 -12.133  31.509  1.00 37.28           O  
ANISOU 2954  O   ILE A 355     4370   5136   4657    488    -51   -149       O  
ATOM   2955  CB  ILE A 355     -15.702 -13.454  30.430  1.00 31.87           C  
ANISOU 2955  CB  ILE A 355     3650   4594   3866    486    -66   -162       C  
ATOM   2956  CG1 ILE A 355     -17.164 -13.771  30.766  1.00 27.98           C  
ANISOU 2956  CG1 ILE A 355     3123   4179   3330    478    -79   -177       C  
ATOM   2957  CG2 ILE A 355     -14.763 -14.578  30.921  1.00 28.87           C  
ANISOU 2957  CG2 ILE A 355     3268   4154   3546    443    -79   -169       C  
ATOM   2958  CD1 ILE A 355     -17.518 -13.741  32.247  1.00 32.50           C  
ANISOU 2958  CD1 ILE A 355     3693   4754   3902    453    -84   -169       C  
ATOM   2959  N   GLN A 356     -13.534 -11.168  29.563  1.00 38.66           N  
ANISOU 2959  N   GLN A 356     4596   5347   4746    519      1   -146       N  
ATOM   2960  CA  GLN A 356     -12.152 -10.875  29.154  1.00 38.99           C  
ANISOU 2960  CA  GLN A 356     4649   5333   4833    487     48   -167       C  
ATOM   2961  C   GLN A 356     -11.415  -9.888  30.084  1.00 41.25           C  
ANISOU 2961  C   GLN A 356     4947   5577   5148    481     52   -161       C  
ATOM   2962  O   GLN A 356     -10.204  -9.679  29.942  1.00 40.97           O  
ANISOU 2962  O   GLN A 356     4898   5502   5166    444     91   -195       O  
ATOM   2963  CB  GLN A 356     -12.079 -10.414  27.686  1.00 39.40           C  
ANISOU 2963  CB  GLN A 356     4765   5377   4829    482    102   -175       C  
ATOM   2964  CG  GLN A 356     -12.588  -8.984  27.408  1.00 38.86           C  
ANISOU 2964  CG  GLN A 356     4800   5295   4672    518    109   -145       C  
ATOM   2965  CD  GLN A 356     -14.027  -8.945  26.912  1.00 38.58           C  
ANISOU 2965  CD  GLN A 356     4795   5309   4553    584     60   -133       C  
ATOM   2966  OE1 GLN A 356     -14.803  -9.857  27.165  1.00 40.72           O  
ANISOU 2966  OE1 GLN A 356     4993   5638   4840    597     19   -142       O  
ATOM   2967  NE2 GLN A 356     -14.385  -7.878  26.209  1.00 40.89           N  
ANISOU 2967  NE2 GLN A 356     5204   5576   4755    626     60   -121       N  
ATOM   2968  N   SER A 357     -12.148  -9.295  31.027  1.00 40.40           N  
ANISOU 2968  N   SER A 357     4858   5483   5009    516     16   -128       N  
ATOM   2969  CA  SER A 357     -11.572  -8.352  31.984  1.00 39.84           C  
ANISOU 2969  CA  SER A 357     4808   5371   4958    515     11   -119       C  
ATOM   2970  C   SER A 357     -10.927  -9.031  33.195  1.00 39.10           C  
ANISOU 2970  C   SER A 357     4662   5253   4941    500    -33   -134       C  
ATOM   2971  O   SER A 357     -10.329  -8.354  34.039  1.00 38.11           O  
ANISOU 2971  O   SER A 357     4547   5091   4843    498    -47   -135       O  
ATOM   2972  CB  SER A 357     -12.621  -7.341  32.449  1.00 39.82           C  
ANISOU 2972  CB  SER A 357     4859   5389   4882    566    -11    -83       C  
ATOM   2973  OG  SER A 357     -12.856  -6.358  31.458  1.00 42.75           O  
ANISOU 2973  OG  SER A 357     5314   5748   5181    589     18    -74       O  
ATOM   2974  N   VAL A 358     -11.032 -10.360  33.271  1.00 37.44           N  
ANISOU 2974  N   VAL A 358     4413   5055   4760    492    -63   -149       N  
ATOM   2975  CA  VAL A 358     -10.342 -11.132  34.315  1.00 37.83           C  
ANISOU 2975  CA  VAL A 358     4441   5062   4871    488   -121   -170       C  
ATOM   2976  C   VAL A 358      -8.825 -10.942  34.277  1.00 37.77           C  
ANISOU 2976  C   VAL A 358     4391   5010   4950    477   -120   -227       C  
ATOM   2977  O   VAL A 358      -8.161 -11.120  35.298  1.00 39.44           O  
ANISOU 2977  O   VAL A 358     4594   5179   5212    490   -181   -250       O  
ATOM   2978  CB  VAL A 358     -10.675 -12.666  34.293  1.00 38.39           C  
ANISOU 2978  CB  VAL A 358     4504   5136   4946    480   -156   -180       C  
ATOM   2979  CG1 VAL A 358     -12.152 -12.907  34.589  1.00 38.09           C  
ANISOU 2979  CG1 VAL A 358     4496   5145   4832    472   -155   -142       C  
ATOM   2980  CG2 VAL A 358     -10.234 -13.333  32.975  1.00 34.10           C  
ANISOU 2980  CG2 VAL A 358     3921   4603   4431    468   -124   -219       C  
ATOM   2981  N   PHE A 359      -8.287 -10.577  33.111  1.00 35.94           N  
ANISOU 2981  N   PHE A 359     4136   4787   4732    450    -50   -258       N  
ATOM   2982  CA  PHE A 359      -6.858 -10.261  32.975  1.00 36.95           C  
ANISOU 2982  CA  PHE A 359     4208   4888   4943    422    -24   -332       C  
ATOM   2983  C   PHE A 359      -6.452  -9.019  33.763  1.00 37.40           C  
ANISOU 2983  C   PHE A 359     4286   4918   5009    411    -24   -328       C  
ATOM   2984  O   PHE A 359      -5.266  -8.696  33.873  1.00 37.53           O  
ANISOU 2984  O   PHE A 359     4245   4913   5101    381    -10   -399       O  
ATOM   2985  CB  PHE A 359      -6.479 -10.073  31.500  1.00 36.67           C  
ANISOU 2985  CB  PHE A 359     4163   4869   4901    375     75   -367       C  
ATOM   2986  CG  PHE A 359      -6.541 -11.335  30.689  1.00 36.78           C  
ANISOU 2986  CG  PHE A 359     4141   4904   4928    381     76   -394       C  
ATOM   2987  CD1 PHE A 359      -5.601 -12.337  30.866  1.00 34.92           C  
ANISOU 2987  CD1 PHE A 359     3823   4658   4788    394     35   -474       C  
ATOM   2988  CD2 PHE A 359      -7.540 -11.518  29.740  1.00 41.15           C  
ANISOU 2988  CD2 PHE A 359     4750   5487   5400    382    108   -349       C  
ATOM   2989  CE1 PHE A 359      -5.657 -13.499  30.118  1.00 36.71           C  
ANISOU 2989  CE1 PHE A 359     4027   4897   5023    404     33   -501       C  
ATOM   2990  CE2 PHE A 359      -7.606 -12.686  28.980  1.00 38.48           C  
ANISOU 2990  CE2 PHE A 359     4386   5165   5071    385    108   -375       C  
ATOM   2991  CZ  PHE A 359      -6.660 -13.673  29.170  1.00 36.93           C  
ANISOU 2991  CZ  PHE A 359     4112   4953   4965    394     74   -448       C  
ATOM   2992  N   SER A 360      -7.442  -8.324  34.313  1.00 37.78           N  
ANISOU 2992  N   SER A 360     4408   4968   4979    435    -39   -254       N  
ATOM   2993  CA  SER A 360      -7.197  -7.046  34.953  1.00 36.47           C  
ANISOU 2993  CA  SER A 360     4282   4772   4802    427    -33   -242       C  
ATOM   2994  C   SER A 360      -7.715  -6.989  36.397  1.00 35.75           C  
ANISOU 2994  C   SER A 360     4223   4667   4693    471   -112   -202       C  
ATOM   2995  O   SER A 360      -8.915  -6.790  36.630  1.00 35.25           O  
ANISOU 2995  O   SER A 360     4213   4628   4551    502   -118   -143       O  
ATOM   2996  CB  SER A 360      -7.796  -5.935  34.108  1.00 35.31           C  
ANISOU 2996  CB  SER A 360     4221   4630   4564    414     38   -201       C  
ATOM   2997  OG  SER A 360      -7.660  -4.693  34.756  1.00 36.77           O  
ANISOU 2997  OG  SER A 360     4466   4780   4726    410     39   -183       O  
ATOM   2998  N   PRO A 361      -6.806  -7.180  37.371  1.00 34.07           N  
ANISOU 2998  N   PRO A 361     3976   4415   4554    475   -175   -245       N  
ATOM   2999  CA  PRO A 361      -7.166  -7.101  38.787  1.00 33.68           C  
ANISOU 2999  CA  PRO A 361     3977   4337   4482    512   -250   -211       C  
ATOM   3000  C   PRO A 361      -7.823  -5.773  39.151  1.00 36.05           C  
ANISOU 3000  C   PRO A 361     4351   4638   4710    518   -223   -158       C  
ATOM   3001  O   PRO A 361      -8.797  -5.755  39.915  1.00 36.94           O  
ANISOU 3001  O   PRO A 361     4517   4759   4760    549   -248   -110       O  
ATOM   3002  CB  PRO A 361      -5.829  -7.273  39.527  1.00 33.40           C  
ANISOU 3002  CB  PRO A 361     3893   4253   4543    516   -322   -285       C  
ATOM   3003  CG  PRO A 361      -4.790  -7.552  38.497  1.00 35.03           C  
ANISOU 3003  CG  PRO A 361     4002   4475   4833    483   -280   -369       C  
ATOM   3004  CD  PRO A 361      -5.459  -7.739  37.165  1.00 34.52           C  
ANISOU 3004  CD  PRO A 361     3942   4457   4718    457   -191   -338       C  
ATOM   3005  N   ILE A 362      -7.315  -4.675  38.595  1.00 36.06           N  
ANISOU 3005  N   ILE A 362     4362   4627   4714    485   -165   -172       N  
ATOM   3006  CA  ILE A 362      -7.860  -3.355  38.898  1.00 34.86           C  
ANISOU 3006  CA  ILE A 362     4296   4460   4488    498   -147   -127       C  
ATOM   3007  C   ILE A 362      -9.303  -3.272  38.437  1.00 38.11           C  
ANISOU 3007  C   ILE A 362     4757   4918   4803    542   -125    -71       C  
ATOM   3008  O   ILE A 362     -10.184  -2.899  39.225  1.00 38.67           O  
ANISOU 3008  O   ILE A 362     4875   5000   4819    587   -153    -35       O  
ATOM   3009  CB  ILE A 362      -6.999  -2.216  38.303  1.00 35.12           C  
ANISOU 3009  CB  ILE A 362     4356   4457   4531    440    -83   -157       C  
ATOM   3010  CG1 ILE A 362      -5.765  -1.993  39.198  1.00 30.24           C  
ANISOU 3010  CG1 ILE A 362     3692   3797   4002    408   -122   -217       C  
ATOM   3011  CG2 ILE A 362      -7.835  -0.920  38.103  1.00 26.48           C  
ANISOU 3011  CG2 ILE A 362     3385   3347   3328    463    -51   -100       C  
ATOM   3012  CD1 ILE A 362      -4.640  -1.236  38.544  1.00 31.52           C  
ANISOU 3012  CD1 ILE A 362     3835   3932   4206    319    -47   -282       C  
ATOM   3013  N   LYS A 363      -9.543  -3.660  37.183  1.00 36.87           N  
ANISOU 3013  N   LYS A 363     4585   4793   4630    530    -80    -76       N  
ATOM   3014  CA  LYS A 363     -10.888  -3.660  36.619  1.00 37.42           C  
ANISOU 3014  CA  LYS A 363     4688   4914   4617    578    -71    -41       C  
ATOM   3015  C   LYS A 363     -11.805  -4.558  37.447  1.00 37.14           C  
ANISOU 3015  C   LYS A 363     4614   4925   4574    608   -116    -29       C  
ATOM   3016  O   LYS A 363     -12.936  -4.193  37.766  1.00 40.02           O  
ANISOU 3016  O   LYS A 363     5003   5328   4874    654   -125     -9       O  
ATOM   3017  CB  LYS A 363     -10.846  -4.100  35.149  1.00 36.37           C  
ANISOU 3017  CB  LYS A 363     4544   4801   4476    556    -24    -56       C  
ATOM   3018  CG  LYS A 363     -12.198  -4.283  34.469  1.00 36.90           C  
ANISOU 3018  CG  LYS A 363     4628   4925   4466    609    -31    -37       C  
ATOM   3019  CD  LYS A 363     -13.081  -3.030  34.502  1.00 38.23           C  
ANISOU 3019  CD  LYS A 363     4888   5094   4544    677    -45    -13       C  
ATOM   3020  CE  LYS A 363     -12.655  -1.989  33.489  1.00 40.54           C  
ANISOU 3020  CE  LYS A 363     5297   5327   4781    667     -5     -8       C  
ATOM   3021  NZ  LYS A 363     -13.720  -0.958  33.320  1.00 38.07           N  
ANISOU 3021  NZ  LYS A 363     5087   5015   4364    759    -42      8       N  
ATOM   3022  N   THR A 364     -11.288  -5.721  37.809  1.00 36.51           N  
ANISOU 3022  N   THR A 364     4480   4837   4556    578   -141    -49       N  
ATOM   3023  CA  THR A 364     -12.020  -6.696  38.605  1.00 34.65           C  
ANISOU 3023  CA  THR A 364     4234   4626   4306    582   -175    -40       C  
ATOM   3024  C   THR A 364     -12.440  -6.144  39.961  1.00 36.13           C  
ANISOU 3024  C   THR A 364     4471   4800   4458    603   -201    -19       C  
ATOM   3025  O   THR A 364     -13.614  -6.217  40.321  1.00 39.55           O  
ANISOU 3025  O   THR A 364     4912   5282   4833    616   -191     -9       O  
ATOM   3026  CB  THR A 364     -11.167  -7.957  38.781  1.00 32.60           C  
ANISOU 3026  CB  THR A 364     3942   4330   4114    553   -212    -69       C  
ATOM   3027  OG1 THR A 364     -10.916  -8.511  37.483  1.00 26.22           O  
ANISOU 3027  OG1 THR A 364     3086   3543   3332    537   -180    -91       O  
ATOM   3028  CG2 THR A 364     -11.877  -8.990  39.656  1.00 31.24           C  
ANISOU 3028  CG2 THR A 364     3797   4160   3911    543   -244    -57       C  
ATOM   3029  N   TRP A 365     -11.485  -5.596  40.709  1.00 36.37           N  
ANISOU 3029  N   TRP A 365     4529   4766   4525    601   -233    -24       N  
ATOM   3030  CA  TRP A 365     -11.786  -4.994  42.005  1.00 35.49           C  
ANISOU 3030  CA  TRP A 365     4477   4632   4376    621   -260     -5       C  
ATOM   3031  C   TRP A 365     -12.675  -3.761  41.883  1.00 36.86           C  
ANISOU 3031  C   TRP A 365     4683   4841   4480    663   -227     15       C  
ATOM   3032  O   TRP A 365     -13.584  -3.573  42.689  1.00 40.36           O  
ANISOU 3032  O   TRP A 365     5155   5311   4870    685   -227     25       O  
ATOM   3033  CB  TRP A 365     -10.510  -4.701  42.800  1.00 35.08           C  
ANISOU 3033  CB  TRP A 365     4446   4502   4382    614   -314    -23       C  
ATOM   3034  CG  TRP A 365      -9.937  -5.948  43.392  1.00 33.39           C  
ANISOU 3034  CG  TRP A 365     4230   4246   4211    602   -378    -46       C  
ATOM   3035  CD1 TRP A 365      -8.780  -6.577  43.034  1.00 29.33           C  
ANISOU 3035  CD1 TRP A 365     3663   3699   3782    593   -417    -95       C  
ATOM   3036  CD2 TRP A 365     -10.521  -6.740  44.432  1.00 32.01           C  
ANISOU 3036  CD2 TRP A 365     4123   4051   3987    599   -413    -29       C  
ATOM   3037  NE1 TRP A 365      -8.600  -7.706  43.796  1.00 30.95           N  
ANISOU 3037  NE1 TRP A 365     3907   3858   3993    601   -492   -108       N  
ATOM   3038  CE2 TRP A 365      -9.658  -7.833  44.659  1.00 31.70           C  
ANISOU 3038  CE2 TRP A 365     4090   3954   3999    598   -487    -62       C  
ATOM   3039  CE3 TRP A 365     -11.693  -6.633  45.195  1.00 32.53           C  
ANISOU 3039  CE3 TRP A 365     4252   4142   3967    595   -386      2       C  
ATOM   3040  CZ2 TRP A 365      -9.927  -8.813  45.618  1.00 30.78           C  
ANISOU 3040  CZ2 TRP A 365     4071   3787   3838    590   -538    -53       C  
ATOM   3041  CZ3 TRP A 365     -11.960  -7.612  46.153  1.00 34.51           C  
ANISOU 3041  CZ3 TRP A 365     4586   4352   4175    570   -418      7       C  
ATOM   3042  CH2 TRP A 365     -11.075  -8.682  46.357  1.00 32.47           C  
ANISOU 3042  CH2 TRP A 365     4361   4019   3957    567   -496    -15       C  
ATOM   3043  N   ASP A 366     -12.447  -2.943  40.862  1.00 35.28           N  
ANISOU 3043  N   ASP A 366     4490   4639   4276    674   -198     14       N  
ATOM   3044  CA  ASP A 366     -13.272  -1.760  40.685  1.00 36.24           C  
ANISOU 3044  CA  ASP A 366     4666   4780   4323    730   -183     28       C  
ATOM   3045  C   ASP A 366     -14.748  -2.156  40.629  1.00 37.45           C  
ANISOU 3045  C   ASP A 366     4786   5022   4423    772   -176     21       C  
ATOM   3046  O   ASP A 366     -15.574  -1.539  41.302  1.00 41.33           O  
ANISOU 3046  O   ASP A 366     5301   5540   4863    820   -183     17       O  
ATOM   3047  CB  ASP A 366     -12.845  -0.943  39.456  1.00 36.12           C  
ANISOU 3047  CB  ASP A 366     4695   4737   4293    730   -153     29       C  
ATOM   3048  CG  ASP A 366     -13.389   0.474  39.483  1.00 39.97           C  
ANISOU 3048  CG  ASP A 366     5282   5206   4701    793   -159     43       C  
ATOM   3049  OD1 ASP A 366     -13.346   1.091  40.568  1.00 44.88           O  
ANISOU 3049  OD1 ASP A 366     5941   5798   5312    810   -183     51       O  
ATOM   3050  OD2 ASP A 366     -13.859   0.981  38.435  1.00 36.20           O  
ANISOU 3050  OD2 ASP A 366     4857   4733   4163    832   -148     44       O  
ATOM   3051  N   ALA A 367     -15.077  -3.196  39.862  1.00 36.91           N  
ANISOU 3051  N   ALA A 367     4654   5002   4369    750   -161      7       N  
ATOM   3052  CA  ALA A 367     -16.472  -3.662  39.770  1.00 38.39           C  
ANISOU 3052  CA  ALA A 367     4789   5282   4514    775   -151    -18       C  
ATOM   3053  C   ALA A 367     -16.996  -4.263  41.082  1.00 36.94           C  
ANISOU 3053  C   ALA A 367     4592   5122   4321    742   -145    -27       C  
ATOM   3054  O   ALA A 367     -18.060  -3.876  41.561  1.00 38.58           O  
ANISOU 3054  O   ALA A 367     4785   5391   4482    776   -133    -54       O  
ATOM   3055  CB  ALA A 367     -16.645  -4.638  38.630  1.00 37.33           C  
ANISOU 3055  CB  ALA A 367     4598   5189   4397    750   -138    -33       C  
ATOM   3056  N   ILE A 368     -16.249  -5.199  41.663  1.00 36.82           N  
ANISOU 3056  N   ILE A 368     4589   5055   4346    676   -155    -14       N  
ATOM   3057  CA  ILE A 368     -16.639  -5.803  42.936  1.00 35.86           C  
ANISOU 3057  CA  ILE A 368     4497   4930   4200    633   -149    -18       C  
ATOM   3058  C   ILE A 368     -16.988  -4.694  43.935  1.00 37.36           C  
ANISOU 3058  C   ILE A 368     4734   5116   4346    673   -148    -16       C  
ATOM   3059  O   ILE A 368     -18.079  -4.689  44.508  1.00 38.52           O  
ANISOU 3059  O   ILE A 368     4867   5326   4442    670   -111    -45       O  
ATOM   3060  CB  ILE A 368     -15.525  -6.707  43.517  1.00 34.84           C  
ANISOU 3060  CB  ILE A 368     4418   4708   4111    582   -190      0       C  
ATOM   3061  CG1 ILE A 368     -15.388  -7.999  42.704  1.00 33.98           C  
ANISOU 3061  CG1 ILE A 368     4271   4607   4033    540   -189    -11       C  
ATOM   3062  CG2 ILE A 368     -15.815  -7.044  44.979  1.00 33.21           C  
ANISOU 3062  CG2 ILE A 368     4293   4468   3857    545   -193      3       C  
ATOM   3063  CD1 ILE A 368     -14.043  -8.750  42.920  1.00 29.16           C  
ANISOU 3063  CD1 ILE A 368     3697   3901   3481    523   -251     -8       C  
ATOM   3064  N   ILE A 369     -16.071  -3.746  44.105  1.00 37.44           N  
ANISOU 3064  N   ILE A 369     4794   5057   4376    707   -183      8       N  
ATOM   3065  CA  ILE A 369     -16.252  -2.663  45.065  1.00 40.29           C  
ANISOU 3065  CA  ILE A 369     5214   5398   4696    747   -191     13       C  
ATOM   3066  C   ILE A 369     -17.453  -1.793  44.694  1.00 40.72           C  
ANISOU 3066  C   ILE A 369     5239   5535   4697    820   -165    -16       C  
ATOM   3067  O   ILE A 369     -18.280  -1.467  45.552  1.00 43.55           O  
ANISOU 3067  O   ILE A 369     5607   5933   5009    840   -145    -41       O  
ATOM   3068  CB  ILE A 369     -14.937  -1.852  45.281  1.00 40.25           C  
ANISOU 3068  CB  ILE A 369     5270   5295   4729    757   -236     39       C  
ATOM   3069  CG1 ILE A 369     -13.880  -2.764  45.926  1.00 43.34           C  
ANISOU 3069  CG1 ILE A 369     5684   5612   5171    703   -280     44       C  
ATOM   3070  CG2 ILE A 369     -15.182  -0.639  46.168  1.00 37.80           C  
ANISOU 3070  CG2 ILE A 369     5028   4963   4370    805   -245     44       C  
ATOM   3071  CD1 ILE A 369     -12.455  -2.198  45.961  1.00 43.60           C  
ANISOU 3071  CD1 ILE A 369     5737   5562   5265    701   -327     44       C  
ATOM   3072  N   PHE A 370     -17.565  -1.456  43.414  1.00 40.75           N  
ANISOU 3072  N   PHE A 370     5212   5566   4706    863   -169    -22       N  
ATOM   3073  CA  PHE A 370     -18.722  -0.724  42.919  1.00 39.19           C  
ANISOU 3073  CA  PHE A 370     4988   5444   4457    951   -168    -62       C  
ATOM   3074  C   PHE A 370     -20.023  -1.440  43.277  1.00 39.64           C  
ANISOU 3074  C   PHE A 370     4955   5614   4494    939   -130   -122       C  
ATOM   3075  O   PHE A 370     -20.911  -0.840  43.881  1.00 42.14           O  
ANISOU 3075  O   PHE A 370     5257   5984   4769    991   -120   -168       O  
ATOM   3076  CB  PHE A 370     -18.601  -0.483  41.408  1.00 39.76           C  
ANISOU 3076  CB  PHE A 370     5062   5516   4530    991   -185    -60       C  
ATOM   3077  CG  PHE A 370     -19.911  -0.148  40.724  1.00 41.22           C  
ANISOU 3077  CG  PHE A 370     5201   5794   4667   1084   -201   -118       C  
ATOM   3078  CD1 PHE A 370     -20.380  -0.939  39.683  1.00 38.52           C  
ANISOU 3078  CD1 PHE A 370     4786   5514   4335   1079   -198   -146       C  
ATOM   3079  CD2 PHE A 370     -20.668   0.952  41.117  1.00 42.88           C  
ANISOU 3079  CD2 PHE A 370     5441   6029   4824   1187   -228   -154       C  
ATOM   3080  CE1 PHE A 370     -21.572  -0.644  39.047  1.00 38.49           C  
ANISOU 3080  CE1 PHE A 370     4734   5598   4293   1174   -229   -213       C  
ATOM   3081  CE2 PHE A 370     -21.872   1.250  40.486  1.00 43.95           C  
ANISOU 3081  CE2 PHE A 370     5525   6253   4921   1292   -260   -226       C  
ATOM   3082  CZ  PHE A 370     -22.321   0.449  39.446  1.00 41.87           C  
ANISOU 3082  CZ  PHE A 370     5183   6053   4672   1286   -264   -258       C  
ATOM   3083  N   ASN A 371     -20.138  -2.721  42.933  1.00 38.31           N  
ANISOU 3083  N   ASN A 371     4724   5479   4352    863   -103   -131       N  
ATOM   3084  CA  ASN A 371     -21.368  -3.449  43.240  1.00 38.21           C  
ANISOU 3084  CA  ASN A 371     4624   5574   4319    826    -54   -198       C  
ATOM   3085  C   ASN A 371     -21.659  -3.494  44.725  1.00 37.47           C  
ANISOU 3085  C   ASN A 371     4566   5479   4194    777    -11   -211       C  
ATOM   3086  O   ASN A 371     -22.798  -3.303  45.140  1.00 37.97           O  
ANISOU 3086  O   ASN A 371     4567   5637   4223    791     32   -285       O  
ATOM   3087  CB  ASN A 371     -21.353  -4.854  42.646  1.00 38.10           C  
ANISOU 3087  CB  ASN A 371     4561   5581   4335    739    -32   -201       C  
ATOM   3088  CG  ASN A 371     -21.699  -4.858  41.171  1.00 39.09           C  
ANISOU 3088  CG  ASN A 371     4618   5760   4473    793    -57   -226       C  
ATOM   3089  OD1 ASN A 371     -22.847  -4.634  40.799  1.00 41.74           O  
ANISOU 3089  OD1 ASN A 371     4870   6201   4788    846    -55   -301       O  
ATOM   3090  ND2 ASN A 371     -20.708  -5.118  40.325  1.00 33.68           N  
ANISOU 3090  ND2 ASN A 371     3969   5005   3821    783    -84   -175       N  
ATOM   3091  N   SER A 372     -20.616  -3.721  45.518  1.00 38.23           N  
ANISOU 3091  N   SER A 372     4762   5465   4298    723    -25   -149       N  
ATOM   3092  CA  SER A 372     -20.747  -3.802  46.965  1.00 41.05           C  
ANISOU 3092  CA  SER A 372     5190   5794   4612    672      8   -152       C  
ATOM   3093  C   SER A 372     -21.299  -2.499  47.538  1.00 42.88           C  
ANISOU 3093  C   SER A 372     5430   6059   4805    756     13   -183       C  
ATOM   3094  O   SER A 372     -22.204  -2.522  48.371  1.00 43.30           O  
ANISOU 3094  O   SER A 372     5468   6172   4811    729     75   -238       O  
ATOM   3095  CB  SER A 372     -19.399  -4.148  47.600  1.00 41.84           C  
ANISOU 3095  CB  SER A 372     5407   5758   4732    629    -40    -82       C  
ATOM   3096  OG  SER A 372     -19.504  -4.287  49.007  1.00 41.77           O  
ANISOU 3096  OG  SER A 372     5494   5706   4668    578    -16    -82       O  
ATOM   3097  N   LEU A 373     -20.763  -1.372  47.067  1.00 44.88           N  
ANISOU 3097  N   LEU A 373     5712   6269   5072    852    -47   -154       N  
ATOM   3098  CA  LEU A 373     -21.194  -0.044  47.509  1.00 47.20           C  
ANISOU 3098  CA  LEU A 373     6032   6575   5325    948    -59   -179       C  
ATOM   3099  C   LEU A 373     -22.576   0.347  46.984  1.00 49.05           C  
ANISOU 3099  C   LEU A 373     6158   6942   5536   1031    -41   -272       C  
ATOM   3100  O   LEU A 373     -23.372   0.937  47.719  1.00 48.23           O  
ANISOU 3100  O   LEU A 373     6040   6893   5393   1077    -15   -333       O  
ATOM   3101  CB  LEU A 373     -20.160   1.019  47.124  1.00 47.24           C  
ANISOU 3101  CB  LEU A 373     6123   6480   5344   1013   -128   -121       C  
ATOM   3102  CG  LEU A 373     -18.820   1.006  47.880  1.00 47.63           C  
ANISOU 3102  CG  LEU A 373     6275   6405   5418    956   -158    -55       C  
ATOM   3103  CD1 LEU A 373     -17.848   1.959  47.221  1.00 47.26           C  
ANISOU 3103  CD1 LEU A 373     6287   6277   5394    998   -209    -16       C  
ATOM   3104  CD2 LEU A 373     -18.967   1.358  49.356  1.00 46.92           C  
ANISOU 3104  CD2 LEU A 373     6259   6286   5282    949   -146    -60       C  
ATOM   3105  N   LYS A 374     -22.859   0.011  45.724  1.00 50.66           N  
ANISOU 3105  N   LYS A 374     6283   7198   5765   1057    -60   -293       N  
ATOM   3106  CA  LYS A 374     -24.176   0.277  45.125  1.00 54.48           C  
ANISOU 3106  CA  LYS A 374     6652   7813   6235   1145    -62   -396       C  
ATOM   3107  C   LYS A 374     -25.319  -0.368  45.915  1.00 56.48           C  
ANISOU 3107  C   LYS A 374     6797   8187   6475   1080     25   -494       C  
ATOM   3108  O   LYS A 374     -26.395   0.216  46.042  1.00 56.14           O  
ANISOU 3108  O   LYS A 374     6670   8249   6412   1165     31   -600       O  
ATOM   3109  CB  LYS A 374     -24.222  -0.176  43.657  1.00 55.48           C  
ANISOU 3109  CB  LYS A 374     6723   7968   6389   1165    -99   -400       C  
ATOM   3110  CG  LYS A 374     -25.636  -0.327  43.101  1.00 57.96           C  
ANISOU 3110  CG  LYS A 374     6890   8433   6699   1226    -98   -524       C  
ATOM   3111  CD  LYS A 374     -25.670  -0.403  41.591  1.00 60.71           C  
ANISOU 3111  CD  LYS A 374     7219   8791   7059   1289   -164   -527       C  
ATOM   3112  CE  LYS A 374     -27.093  -0.644  41.098  1.00 62.33           C  
ANISOU 3112  CE  LYS A 374     7262   9153   7267   1348   -173   -667       C  
ATOM   3113  NZ  LYS A 374     -27.574  -2.043  41.292  1.00 61.83           N  
ANISOU 3113  NZ  LYS A 374     7076   9178   7239   1202    -87   -714       N  
ATOM   3114  N   GLU A 375     -25.078  -1.571  46.437  1.00 58.90           N  
ANISOU 3114  N   GLU A 375     7112   8477   6791    929     92   -468       N  
ATOM   3115  CA  GLU A 375     -26.072  -2.285  47.235  1.00 62.37           C  
ANISOU 3115  CA  GLU A 375     7478   9014   7206    828    196   -557       C  
ATOM   3116  C   GLU A 375     -26.496  -1.500  48.467  1.00 62.68           C  
ANISOU 3116  C   GLU A 375     7549   9069   7197    853    239   -602       C  
ATOM   3117  O   GLU A 375     -27.631  -1.629  48.922  1.00 64.91           O  
ANISOU 3117  O   GLU A 375     7729   9474   7459    822    322   -720       O  
ATOM   3118  CB  GLU A 375     -25.562  -3.671  47.647  1.00 64.05           C  
ANISOU 3118  CB  GLU A 375     7755   9163   7416    658    251   -502       C  
ATOM   3119  CG  GLU A 375     -25.755  -4.748  46.585  1.00 70.33           C  
ANISOU 3119  CG  GLU A 375     8467  10006   8249    600    256   -518       C  
ATOM   3120  CD  GLU A 375     -27.222  -4.982  46.224  1.00 77.59           C  
ANISOU 3120  CD  GLU A 375     9212  11098   9171    591    316   -661       C  
ATOM   3121  OE1 GLU A 375     -28.042  -5.238  47.138  1.00 80.15           O  
ANISOU 3121  OE1 GLU A 375     9499  11494   9459    503    419   -744       O  
ATOM   3122  OE2 GLU A 375     -27.552  -4.916  45.019  1.00 79.44           O  
ANISOU 3122  OE2 GLU A 375     9345  11397   9442    668    262   -698       O  
ATOM   3123  N   GLN A 376     -25.582  -0.681  48.989  1.00 60.91           N  
ANISOU 3123  N   GLN A 376     7461   8726   6957    904    186   -517       N  
ATOM   3124  CA  GLN A 376     -25.831   0.111  50.190  1.00 59.45           C  
ANISOU 3124  CA  GLN A 376     7333   8533   6721    931    217   -545       C  
ATOM   3125  C   GLN A 376     -26.258   1.543  49.874  1.00 58.59           C  
ANISOU 3125  C   GLN A 376     7195   8463   6605   1110    152   -596       C  
ATOM   3126  O   GLN A 376     -26.331   2.388  50.779  1.00 57.24           O  
ANISOU 3126  O   GLN A 376     7087   8269   6393   1159    158   -610       O  
ATOM   3127  CB  GLN A 376     -24.582   0.135  51.064  1.00 59.92           C  
ANISOU 3127  CB  GLN A 376     7572   8433   6763    877    192   -430       C  
ATOM   3128  CG  GLN A 376     -24.120  -1.238  51.537  1.00 65.10           C  
ANISOU 3128  CG  GLN A 376     8296   9029   7411    717    238   -382       C  
ATOM   3129  CD  GLN A 376     -22.770  -1.178  52.211  1.00 67.64           C  
ANISOU 3129  CD  GLN A 376     8786   9187   7726    695    175   -276       C  
ATOM   3130  OE1 GLN A 376     -21.746  -1.447  51.585  1.00 69.78           O  
ANISOU 3130  OE1 GLN A 376     9087   9379   8049    699    102   -205       O  
ATOM   3131  NE2 GLN A 376     -22.755  -0.795  53.485  1.00 69.37           N  
ANISOU 3131  NE2 GLN A 376     9114   9358   7885    678    200   -275       N  
ATOM   3132  N   ASN A 377     -26.542   1.799  48.594  1.00 55.21           N  
ANISOU 3132  N   ASN A 377     6687   8084   6208   1212     85   -625       N  
ATOM   3133  CA  ASN A 377     -26.881   3.133  48.087  1.00 56.62           C  
ANISOU 3133  CA  ASN A 377     6868   8276   6369   1398     -4   -667       C  
ATOM   3134  C   ASN A 377     -25.759   4.161  48.251  1.00 56.77           C  
ANISOU 3134  C   ASN A 377     7066   8139   6366   1456    -77   -557       C  
ATOM   3135  O   ASN A 377     -26.009   5.368  48.336  1.00 58.96           O  
ANISOU 3135  O   ASN A 377     7392   8402   6606   1592   -132   -588       O  
ATOM   3136  CB  ASN A 377     -28.194   3.651  48.701  1.00 58.74           C  
ANISOU 3136  CB  ASN A 377     7028   8678   6611   1476     35   -818       C  
ATOM   3137  CG  ASN A 377     -29.417   2.879  48.217  1.00 60.73           C  
ANISOU 3137  CG  ASN A 377     7075   9104   6894   1454     85   -960       C  
ATOM   3138  OD1 ASN A 377     -29.428   2.325  47.113  1.00 61.81           O  
ANISOU 3138  OD1 ASN A 377     7153   9265   7066   1452     46   -955       O  
ATOM   3139  ND2 ASN A 377     -30.457   2.849  49.042  1.00 58.29           N  
ANISOU 3139  ND2 ASN A 377     6653   8922   6573   1434    175  -1097       N  
ATOM   3140  N   LYS A 378     -24.522   3.680  48.302  1.00 54.22           N  
ANISOU 3140  N   LYS A 378     6838   7696   6065   1352    -79   -439       N  
ATOM   3141  CA  LYS A 378     -23.373   4.566  48.366  1.00 52.59           C  
ANISOU 3141  CA  LYS A 378     6786   7346   5849   1384   -143   -344       C  
ATOM   3142  C   LYS A 378     -22.817   4.808  46.963  1.00 50.75           C  
ANISOU 3142  C   LYS A 378     6585   7062   5635   1429   -209   -298       C  
ATOM   3143  O   LYS A 378     -23.045   4.010  46.057  1.00 48.97           O  
ANISOU 3143  O   LYS A 378     6274   6891   5440   1402   -202   -313       O  
ATOM   3144  CB  LYS A 378     -22.311   4.013  49.315  1.00 52.50           C  
ANISOU 3144  CB  LYS A 378     6859   7236   5853   1256   -116   -262       C  
ATOM   3145  CG  LYS A 378     -22.742   4.047  50.779  1.00 55.93           C  
ANISOU 3145  CG  LYS A 378     7321   7687   6244   1223    -59   -297       C  
ATOM   3146  CD  LYS A 378     -21.770   3.316  51.698  1.00 56.69           C  
ANISOU 3146  CD  LYS A 378     7511   7684   6346   1098    -44   -224       C  
ATOM   3147  CE  LYS A 378     -22.308   3.270  53.131  1.00 59.90           C  
ANISOU 3147  CE  LYS A 378     7962   8105   6691   1056     22   -264       C  
ATOM   3148  NZ  LYS A 378     -21.425   2.483  54.041  1.00 58.95           N  
ANISOU 3148  NZ  LYS A 378     7957   7880   6562    941     24   -199       N  
ATOM   3149  N   VAL A 379     -22.105   5.923  46.801  1.00 50.84           N  
ANISOU 3149  N   VAL A 379     6731   6964   5621   1490   -268   -247       N  
ATOM   3150  CA  VAL A 379     -21.619   6.389  45.500  1.00 51.26           C  
ANISOU 3150  CA  VAL A 379     6853   6953   5668   1535   -324   -210       C  
ATOM   3151  C   VAL A 379     -20.094   6.370  45.452  1.00 50.47           C  
ANISOU 3151  C   VAL A 379     6851   6725   5601   1432   -322   -115       C  
ATOM   3152  O   VAL A 379     -19.428   6.874  46.361  1.00 51.85           O  
ANISOU 3152  O   VAL A 379     7107   6821   5771   1403   -324    -80       O  
ATOM   3153  CB  VAL A 379     -22.110   7.825  45.213  1.00 52.77           C  
ANISOU 3153  CB  VAL A 379     7147   7116   5786   1694   -395   -245       C  
ATOM   3154  CG1 VAL A 379     -21.583   8.321  43.876  1.00 53.88           C  
ANISOU 3154  CG1 VAL A 379     7402   7171   5900   1727   -447   -203       C  
ATOM   3155  CG2 VAL A 379     -23.630   7.886  45.229  1.00 53.42           C  
ANISOU 3155  CG2 VAL A 379     7114   7338   5846   1816   -411   -365       C  
ATOM   3156  N   ILE A 380     -19.542   5.794  44.390  1.00 48.65           N  
ANISOU 3156  N   ILE A 380     6604   6476   5406   1377   -318    -84       N  
ATOM   3157  CA  ILE A 380     -18.085   5.642  44.275  1.00 47.35           C  
ANISOU 3157  CA  ILE A 380     6496   6207   5286   1271   -307    -17       C  
ATOM   3158  C   ILE A 380     -17.401   6.949  43.846  1.00 47.78           C  
ANISOU 3158  C   ILE A 380     6708   6149   5298   1299   -337     14       C  
ATOM   3159  O   ILE A 380     -17.992   7.737  43.095  1.00 50.89           O  
ANISOU 3159  O   ILE A 380     7176   6536   5623   1399   -371     -5       O  
ATOM   3160  CB  ILE A 380     -17.689   4.466  43.334  1.00 45.41           C  
ANISOU 3160  CB  ILE A 380     6170   5986   5098   1192   -280     -5       C  
ATOM   3161  CG1 ILE A 380     -17.904   4.827  41.857  1.00 43.72           C  
ANISOU 3161  CG1 ILE A 380     5997   5768   4847   1245   -298    -11       C  
ATOM   3162  CG2 ILE A 380     -18.432   3.189  43.730  1.00 44.94           C  
ANISOU 3162  CG2 ILE A 380     5977   6030   5069   1157   -249    -38       C  
ATOM   3163  CD1 ILE A 380     -17.425   3.760  40.876  1.00 44.21           C  
ANISOU 3163  CD1 ILE A 380     5994   5843   4960   1166   -269      1       C  
ATOM   3164  N   PRO A 381     -16.161   7.193  44.322  1.00 45.84           N  
ANISOU 3164  N   PRO A 381     6521   5809   5087   1213   -328     53       N  
ATOM   3165  CA  PRO A 381     -15.482   8.422  43.908  1.00 47.46           C  
ANISOU 3165  CA  PRO A 381     6882   5902   5247   1214   -341     76       C  
ATOM   3166  C   PRO A 381     -15.030   8.372  42.446  1.00 47.96           C  
ANISOU 3166  C   PRO A 381     6986   5931   5304   1173   -319     88       C  
ATOM   3167  O   PRO A 381     -14.963   7.296  41.859  1.00 48.71           O  
ANISOU 3167  O   PRO A 381     6975   6083   5452   1126   -292     83       O  
ATOM   3168  CB  PRO A 381     -14.279   8.504  44.861  1.00 44.94           C  
ANISOU 3168  CB  PRO A 381     6579   5512   4985   1116   -334     97       C  
ATOM   3169  CG  PRO A 381     -14.012   7.103  45.250  1.00 44.69           C  
ANISOU 3169  CG  PRO A 381     6404   5538   5039   1047   -317     92       C  
ATOM   3170  CD  PRO A 381     -15.353   6.417  45.283  1.00 45.15           C  
ANISOU 3170  CD  PRO A 381     6374   5708   5073   1115   -313     68       C  
ATOM   3171  N   GLN A 382     -14.765   9.542  41.871  1.00 48.40           N  
ANISOU 3171  N   GLN A 382     7215   5890   5286   1191   -328    101       N  
ATOM   3172  CA  GLN A 382     -14.217   9.661  40.526  1.00 50.31           C  
ANISOU 3172  CA  GLN A 382     7541   6073   5501   1133   -294    113       C  
ATOM   3173  C   GLN A 382     -12.749   9.250  40.537  1.00 50.97           C  
ANISOU 3173  C   GLN A 382     7577   6114   5674    969   -229    120       C  
ATOM   3174  O   GLN A 382     -12.034   9.523  41.502  1.00 50.55           O  
ANISOU 3174  O   GLN A 382     7517   6023   5665    913   -228    120       O  
ATOM   3175  CB  GLN A 382     -14.338  11.114  40.049  1.00 51.32           C  
ANISOU 3175  CB  GLN A 382     7905   6088   5505   1191   -321    123       C  
ATOM   3176  CG  GLN A 382     -14.020  11.348  38.574  1.00 50.53           C  
ANISOU 3176  CG  GLN A 382     7943   5917   5339   1149   -290    134       C  
ATOM   3177  CD  GLN A 382     -14.128  12.820  38.150  1.00 55.98           C  
ANISOU 3177  CD  GLN A 382     8914   6471   5886   1203   -323    147       C  
ATOM   3178  OE1 GLN A 382     -14.320  13.725  38.974  1.00 48.65           O  
ANISOU 3178  OE1 GLN A 382     8075   5495   4915   1264   -367    148       O  
ATOM   3179  NE2 GLN A 382     -14.000  13.059  36.844  1.00 60.20           N  
ANISOU 3179  NE2 GLN A 382     9606   6933   6336   1180   -302    156       N  
ATOM   3180  N   GLY A 383     -12.309   8.592  39.468  1.00 51.54           N  
ANISOU 3180  N   GLY A 383     7611   6196   5775    897   -179    115       N  
ATOM   3181  CA  GLY A 383     -10.902   8.251  39.304  1.00 52.97           C  
ANISOU 3181  CA  GLY A 383     7742   6342   6040    744   -112    101       C  
ATOM   3182  C   GLY A 383     -10.059   9.503  39.155  1.00 55.85           C  
ANISOU 3182  C   GLY A 383     8278   6587   6357    664    -73    100       C  
ATOM   3183  O   GLY A 383     -10.423  10.423  38.420  1.00 57.68           O  
ANISOU 3183  O   GLY A 383     8700   6746   6470    696    -70    118       O  
ATOM   3184  N   ARG A 384      -8.939   9.545  39.868  1.00 56.43           N  
ANISOU 3184  N   ARG A 384     8293   6634   6515    559    -50     74       N  
ATOM   3185  CA  ARG A 384      -8.048  10.698  39.831  1.00 57.94           C  
ANISOU 3185  CA  ARG A 384     8628   6714   6673    457     -4     61       C  
ATOM   3186  C   ARG A 384      -6.681  10.344  39.264  1.00 57.91           C  
ANISOU 3186  C   ARG A 384     8548   6699   6756    285     91      4       C  
ATOM   3187  O   ARG A 384      -6.238   9.193  39.328  1.00 57.69           O  
ANISOU 3187  O   ARG A 384     8326   6750   6844    255     96    -33       O  
ATOM   3188  CB  ARG A 384      -7.898  11.310  41.224  1.00 59.77           C  
ANISOU 3188  CB  ARG A 384     8872   6917   6922    479    -60     62       C  
ATOM   3189  CG  ARG A 384      -9.081  12.161  41.664  1.00 66.07           C  
ANISOU 3189  CG  ARG A 384     9811   7687   7604    626   -131    105       C  
ATOM   3190  CD  ARG A 384      -9.152  12.266  43.186  1.00 71.46           C  
ANISOU 3190  CD  ARG A 384    10440   8385   8327    673   -196    104       C  
ATOM   3191  NE  ARG A 384      -9.964  13.407  43.623  1.00 79.05           N  
ANISOU 3191  NE  ARG A 384    11570   9292   9175    783   -248    130       N  
ATOM   3192  CZ  ARG A 384     -11.278  13.372  43.846  1.00 81.02           C  
ANISOU 3192  CZ  ARG A 384    11820   9598   9365    939   -304    143       C  
ATOM   3193  NH1 ARG A 384     -11.967  12.242  43.678  1.00 78.98           N  
ANISOU 3193  NH1 ARG A 384    11406   9453   9148    992   -310    137       N  
ATOM   3194  NH2 ARG A 384     -11.907  14.476  44.240  1.00 78.52           N  
ANISOU 3194  NH2 ARG A 384    11659   9226   8950   1040   -354    152       N  
ATOM   3195  N   SER A 385      -6.030  11.353  38.694  1.00 57.64           N  
ANISOU 3195  N   SER A 385     8678   6564   6659    172    167    -12       N  
ATOM   3196  CA  SER A 385      -4.646  11.264  38.265  1.00 56.16           C  
ANISOU 3196  CA  SER A 385     8428   6359   6550    -15    273    -88       C  
ATOM   3197  C   SER A 385      -3.715  11.291  39.483  1.00 53.13           C  
ANISOU 3197  C   SER A 385     7911   5987   6290    -73    244   -146       C  
ATOM   3198  O   SER A 385      -3.928  12.064  40.420  1.00 52.53           O  
ANISOU 3198  O   SER A 385     7917   5863   6179    -26    181   -121       O  
ATOM   3199  CB  SER A 385      -4.330  12.442  37.346  1.00 58.96           C  
ANISOU 3199  CB  SER A 385     9034   6590   6778   -129    372    -88       C  
ATOM   3200  OG  SER A 385      -2.967  12.451  36.976  1.00 65.24           O  
ANISOU 3200  OG  SER A 385     9768   7372   7650   -332    493   -178       O  
ATOM   3201  N   HIS A 386      -2.697  10.436  39.470  1.00 48.67           N  
ANISOU 3201  N   HIS A 386     7142   5485   5868   -163    278   -231       N  
ATOM   3202  CA  HIS A 386      -1.646  10.460  40.492  1.00 46.87           C  
ANISOU 3202  CA  HIS A 386     6781   5264   5764   -229    248   -312       C  
ATOM   3203  C   HIS A 386      -0.272  10.299  39.848  1.00 44.19           C  
ANISOU 3203  C   HIS A 386     6329   4938   5524   -411    361   -436       C  
ATOM   3204  O   HIS A 386      -0.154   9.639  38.822  1.00 43.77           O  
ANISOU 3204  O   HIS A 386     6219   4926   5485   -451    436   -461       O  
ATOM   3205  CB  HIS A 386      -1.846   9.345  41.528  1.00 46.27           C  
ANISOU 3205  CB  HIS A 386     6521   5269   5790   -108    123   -313       C  
ATOM   3206  CG  HIS A 386      -3.198   9.341  42.170  1.00 44.20           C  
ANISOU 3206  CG  HIS A 386     6339   5013   5442     57     30   -210       C  
ATOM   3207  ND1 HIS A 386      -3.471  10.031  43.327  1.00 45.09           N  
ANISOU 3207  ND1 HIS A 386     6527   5084   5521    116    -46   -180       N  
ATOM   3208  CD2 HIS A 386      -4.348   8.718  41.823  1.00 44.59           C  
ANISOU 3208  CD2 HIS A 386     6395   5112   5435    170      5   -142       C  
ATOM   3209  CE1 HIS A 386      -4.735   9.841  43.664  1.00 46.11           C  
ANISOU 3209  CE1 HIS A 386     6702   5240   5577    256   -106   -103       C  
ATOM   3210  NE2 HIS A 386      -5.289   9.048  42.768  1.00 40.96           N  
ANISOU 3210  NE2 HIS A 386     6005   4647   4914    289    -77    -82       N  
ATOM   3211  N   PRO A 387       0.769  10.910  40.439  1.00 43.77           N  
ANISOU 3211  N   PRO A 387     6237   4854   5539   -524    376   -525       N  
ATOM   3212  CA  PRO A 387       2.121  10.600  39.976  1.00 46.44           C  
ANISOU 3212  CA  PRO A 387     6408   5232   6004   -689    473   -674       C  
ATOM   3213  C   PRO A 387       2.623   9.267  40.534  1.00 46.19           C  
ANISOU 3213  C   PRO A 387     6100   5306   6143   -617    378   -756       C  
ATOM   3214  O   PRO A 387       2.301   8.911  41.665  1.00 47.18           O  
ANISOU 3214  O   PRO A 387     6175   5447   6305   -485    232   -723       O  
ATOM   3215  CB  PRO A 387       2.961  11.757  40.529  1.00 45.72           C  
ANISOU 3215  CB  PRO A 387     6372   5074   5926   -825    506   -746       C  
ATOM   3216  CG  PRO A 387       2.208  12.243  41.692  1.00 44.04           C  
ANISOU 3216  CG  PRO A 387     6264   4814   5654   -687    370   -650       C  
ATOM   3217  CD  PRO A 387       0.759  12.040  41.384  1.00 42.76           C  
ANISOU 3217  CD  PRO A 387     6238   4646   5363   -527    327   -502       C  
ATOM   3218  N   VAL A 388       3.401   8.547  39.735  1.00 47.84           N  
ANISOU 3218  N   VAL A 388     6150   5580   6448   -703    460   -865       N  
ATOM   3219  CA  VAL A 388       4.002   7.291  40.160  1.00 49.19           C  
ANISOU 3219  CA  VAL A 388     6064   5842   6782   -638    370   -965       C  
ATOM   3220  C   VAL A 388       5.103   7.571  41.190  1.00 51.44           C  
ANISOU 3220  C   VAL A 388     6212   6134   7198   -684    301  -1099       C  
ATOM   3221  O   VAL A 388       6.011   8.367  40.943  1.00 53.55           O  
ANISOU 3221  O   VAL A 388     6463   6384   7498   -855    407  -1209       O  
ATOM   3222  CB  VAL A 388       4.552   6.481  38.949  1.00 49.86           C  
ANISOU 3222  CB  VAL A 388     6017   5996   6932   -716    484  -1059       C  
ATOM   3223  CG1 VAL A 388       5.279   5.230  39.419  1.00 52.58           C  
ANISOU 3223  CG1 VAL A 388     6098   6428   7452   -642    378  -1182       C  
ATOM   3224  CG2 VAL A 388       3.424   6.081  38.001  1.00 47.03           C  
ANISOU 3224  CG2 VAL A 388     5786   5633   6449   -650    525   -927       C  
ATOM   3225  N   GLN A 389       4.995   6.933  42.352  1.00 51.60           N  
ANISOU 3225  N   GLN A 389     6149   6174   7283   -534    123  -1093       N  
ATOM   3226  CA  GLN A 389       5.991   7.070  43.412  1.00 53.72           C  
ANISOU 3226  CA  GLN A 389     6286   6448   7677   -544     20  -1223       C  
ATOM   3227  C   GLN A 389       6.470   5.698  43.903  1.00 54.25           C  
ANISOU 3227  C   GLN A 389     6144   6584   7885   -423   -125  -1318       C  
ATOM   3228  O   GLN A 389       5.661   4.786  44.085  1.00 55.41           O  
ANISOU 3228  O   GLN A 389     6321   6739   7993   -277   -212  -1219       O  
ATOM   3229  CB  GLN A 389       5.419   7.872  44.589  1.00 52.39           C  
ANISOU 3229  CB  GLN A 389     6277   6202   7426   -474    -83  -1122       C  
ATOM   3230  CG  GLN A 389       5.457   9.384  44.420  1.00 53.10           C  
ANISOU 3230  CG  GLN A 389     6537   6215   7424   -613     28  -1098       C  
ATOM   3231  CD  GLN A 389       4.810  10.131  45.593  1.00 52.69           C  
ANISOU 3231  CD  GLN A 389     6649   6087   7284   -524    -81   -994       C  
ATOM   3232  OE1 GLN A 389       3.661   9.879  45.950  1.00 48.57           O  
ANISOU 3232  OE1 GLN A 389     6238   5549   6667   -379   -150   -853       O  
ATOM   3233  NE2 GLN A 389       5.548  11.064  46.180  1.00 52.26           N  
ANISOU 3233  NE2 GLN A 389     6607   5987   7261   -619    -87  -1073       N  
ATOM   3234  N   PRO A 390       7.786   5.543  44.117  1.00 48.01           N  
ANISOU 3234  N   PRO A 390     6787   5635   5822   -685    173    345       N  
ATOM   3235  CA  PRO A 390       8.283   4.344  44.797  1.00 47.14           C  
ANISOU 3235  CA  PRO A 390     6596   5621   5694   -698    151    315       C  
ATOM   3236  C   PRO A 390       7.747   4.297  46.222  1.00 46.49           C  
ANISOU 3236  C   PRO A 390     6499   5545   5619   -712     95    231       C  
ATOM   3237  O   PRO A 390       7.503   5.353  46.814  1.00 46.32           O  
ANISOU 3237  O   PRO A 390     6510   5454   5634   -744     78    196       O  
ATOM   3238  CB  PRO A 390       9.800   4.560  44.839  1.00 49.86           C  
ANISOU 3238  CB  PRO A 390     6880   5980   6083   -784    183    350       C  
ATOM   3239  CG  PRO A 390      10.082   5.591  43.769  1.00 52.18           C  
ANISOU 3239  CG  PRO A 390     7222   6200   6403   -798    238    422       C  
ATOM   3240  CD  PRO A 390       8.872   6.471  43.755  1.00 50.40           C  
ANISOU 3240  CD  PRO A 390     7085   5886   6179   -760    218    399       C  
ATOM   3241  N   TYR A 391       7.549   3.092  46.759  1.00 42.22           N  
ANISOU 3241  N   TYR A 391     5913   5086   5043   -683     68    201       N  
ATOM   3242  CA  TYR A 391       7.126   2.939  48.146  1.00 38.65           C  
ANISOU 3242  CA  TYR A 391     5441   4655   4591   -693     21    130       C  
ATOM   3243  C   TYR A 391       7.684   1.662  48.779  1.00 38.82           C  
ANISOU 3243  C   TYR A 391     5387   4772   4590   -699      6    117       C  
ATOM   3244  O   TYR A 391       8.007   0.722  48.058  1.00 38.04           O  
ANISOU 3244  O   TYR A 391     5265   4722   4467   -671     24    157       O  
ATOM   3245  CB  TYR A 391       5.600   3.075  48.287  1.00 38.42           C  
ANISOU 3245  CB  TYR A 391     5463   4597   4536   -627     -4     95       C  
ATOM   3246  CG  TYR A 391       4.747   1.948  47.725  1.00 37.75           C  
ANISOU 3246  CG  TYR A 391     5379   4559   4407   -551     -9    107       C  
ATOM   3247  CD1 TYR A 391       4.353   1.934  46.384  1.00 38.69           C  
ANISOU 3247  CD1 TYR A 391     5540   4654   4506   -497     14    152       C  
ATOM   3248  CD2 TYR A 391       4.298   0.922  48.552  1.00 35.19           C  
ANISOU 3248  CD2 TYR A 391     5013   4298   4059   -530    -37     73       C  
ATOM   3249  CE1 TYR A 391       3.549   0.921  45.883  1.00 37.44           C  
ANISOU 3249  CE1 TYR A 391     5380   4534   4312   -427      1    153       C  
ATOM   3250  CE2 TYR A 391       3.506  -0.094  48.066  1.00 33.78           C  
ANISOU 3250  CE2 TYR A 391     4831   4151   3850   -467    -46     82       C  
ATOM   3251  CZ  TYR A 391       3.130  -0.093  46.740  1.00 38.57           C  
ANISOU 3251  CZ  TYR A 391     5478   4734   4444   -417    -30    117       C  
ATOM   3252  OH  TYR A 391       2.336  -1.119  46.286  1.00 39.03           O  
ANISOU 3252  OH  TYR A 391     5529   4823   4477   -355    -47    116       O  
ATOM   3253  N   PRO A 392       7.844   1.641  50.123  1.00 37.90           N  
ANISOU 3253  N   PRO A 392     5237   4683   4480   -731    -29     62       N  
ATOM   3254  CA  PRO A 392       8.486   0.491  50.772  1.00 36.30           C  
ANISOU 3254  CA  PRO A 392     4966   4570   4257   -737    -42     54       C  
ATOM   3255  C   PRO A 392       7.624  -0.758  50.880  1.00 34.54           C  
ANISOU 3255  C   PRO A 392     4736   4398   3989   -671    -56     52       C  
ATOM   3256  O   PRO A 392       6.409  -0.680  51.080  1.00 31.52           O  
ANISOU 3256  O   PRO A 392     4389   3994   3592   -629    -71     29       O  
ATOM   3257  CB  PRO A 392       8.843   1.014  52.173  1.00 35.85           C  
ANISOU 3257  CB  PRO A 392     4883   4519   4217   -784    -77     -8       C  
ATOM   3258  CG  PRO A 392       7.905   2.137  52.414  1.00 38.74           C  
ANISOU 3258  CG  PRO A 392     5313   4809   4598   -776    -91    -44       C  
ATOM   3259  CD  PRO A 392       7.687   2.773  51.058  1.00 39.53           C  
ANISOU 3259  CD  PRO A 392     5466   4837   4716   -767    -55      7       C  
ATOM   3260  N   GLY A 393       8.279  -1.907  50.764  1.00 33.57           N  
ANISOU 3260  N   GLY A 393     4565   4342   3847   -662    -52     76       N  
ATOM   3261  CA  GLY A 393       7.594  -3.180  50.833  1.00 32.82           C  
ANISOU 3261  CA  GLY A 393     4461   4292   3719   -606    -66     79       C  
ATOM   3262  C   GLY A 393       7.990  -4.007  52.036  1.00 34.88           C  
ANISOU 3262  C   GLY A 393     4669   4620   3963   -615    -89     56       C  
ATOM   3263  O   GLY A 393       7.910  -3.556  53.181  1.00 36.17           O  
ANISOU 3263  O   GLY A 393     4825   4790   4127   -637   -110     14       O  
ATOM   3264  N   ALA A 394       8.437  -5.225  51.751  1.00 35.34           N  
ANISOU 3264  N   ALA A 394     4695   4730   4003   -591    -87     84       N  
ATOM   3265  CA  ALA A 394       8.620  -6.251  52.748  1.00 34.80           C  
ANISOU 3265  CA  ALA A 394     4585   4724   3913   -581   -108     73       C  
ATOM   3266  C   ALA A 394      10.027  -6.242  53.332  1.00 37.02           C  
ANISOU 3266  C   ALA A 394     4814   5057   4195   -623   -112     66       C  
ATOM   3267  O   ALA A 394      10.953  -5.664  52.753  1.00 36.08           O  
ANISOU 3267  O   ALA A 394     4680   4930   4097   -660    -94     80       O  
ATOM   3268  CB  ALA A 394       8.321  -7.594  52.139  1.00 34.12           C  
ANISOU 3268  CB  ALA A 394     4496   4659   3810   -529   -109    104       C  
ATOM   3269  N   PHE A 395      10.169  -6.883  54.489  1.00 36.40           N  
ANISOU 3269  N   PHE A 395     4704   5033   4095   -616   -135     47       N  
ATOM   3270  CA  PHE A 395      11.466  -7.096  55.087  1.00 36.19           C  
ANISOU 3270  CA  PHE A 395     4622   5067   4062   -643   -146     39       C  
ATOM   3271  C   PHE A 395      12.018  -8.480  54.718  1.00 36.86           C  
ANISOU 3271  C   PHE A 395     4676   5204   4125   -607   -143     76       C  
ATOM   3272  O   PHE A 395      11.304  -9.497  54.769  1.00 36.69           O  
ANISOU 3272  O   PHE A 395     4668   5188   4084   -559   -149     92       O  
ATOM   3273  CB  PHE A 395      11.395  -6.924  56.607  1.00 35.93           C  
ANISOU 3273  CB  PHE A 395     4574   5069   4010   -650   -176     -7       C  
ATOM   3274  CG  PHE A 395      12.678  -7.272  57.313  1.00 35.61           C  
ANISOU 3274  CG  PHE A 395     4474   5100   3956   -667   -195    -20       C  
ATOM   3275  CD1 PHE A 395      13.760  -6.386  57.302  1.00 38.21           C  
ANISOU 3275  CD1 PHE A 395     4770   5433   4316   -724   -200    -43       C  
ATOM   3276  CD2 PHE A 395      12.813  -8.490  57.973  1.00 33.90           C  
ANISOU 3276  CD2 PHE A 395     4233   4948   3700   -624   -208     -7       C  
ATOM   3277  CE1 PHE A 395      14.962  -6.716  57.946  1.00 37.33           C  
ANISOU 3277  CE1 PHE A 395     4596   5394   4194   -738   -221    -59       C  
ATOM   3278  CE2 PHE A 395      14.010  -8.827  58.620  1.00 32.18           C  
ANISOU 3278  CE2 PHE A 395     3961   4802   3466   -632   -229    -21       C  
ATOM   3279  CZ  PHE A 395      15.082  -7.942  58.603  1.00 32.10           C  
ANISOU 3279  CZ  PHE A 395     3912   4801   3484   -687   -237    -49       C  
ATOM   3280  N   VAL A 396      13.293  -8.500  54.344  1.00 37.24           N  
ANISOU 3280  N   VAL A 396     4681   5288   4180   -629   -134     88       N  
ATOM   3281  CA  VAL A 396      14.014  -9.737  54.088  1.00 36.74           C  
ANISOU 3281  CA  VAL A 396     4583   5282   4094   -593   -134    117       C  
ATOM   3282  C   VAL A 396      15.264  -9.757  54.959  1.00 39.01           C  
ANISOU 3282  C   VAL A 396     4807   5640   4374   -619   -152     96       C  
ATOM   3283  O   VAL A 396      16.107  -8.869  54.850  1.00 42.30           O  
ANISOU 3283  O   VAL A 396     5193   6062   4819   -672   -144     84       O  
ATOM   3284  CB  VAL A 396      14.415  -9.874  52.600  1.00 34.62           C  
ANISOU 3284  CB  VAL A 396     4318   5003   3834   -578   -103    157       C  
ATOM   3285  CG1 VAL A 396      15.027 -11.242  52.343  1.00 34.15           C  
ANISOU 3285  CG1 VAL A 396     4230   5000   3745   -527   -107    181       C  
ATOM   3286  CG2 VAL A 396      13.216  -9.657  51.686  1.00 32.13           C  
ANISOU 3286  CG2 VAL A 396     4066   4617   3526   -553    -89    171       C  
ATOM   3287  N   LYS A 397      15.371 -10.766  55.821  1.00 39.43           N  
ANISOU 3287  N   LYS A 397     4842   5747   4393   -582   -176     92       N  
ATOM   3288  CA  LYS A 397      16.521 -10.942  56.708  1.00 38.34           C  
ANISOU 3288  CA  LYS A 397     4644   5686   4239   -593   -199     71       C  
ATOM   3289  C   LYS A 397      17.735 -11.413  55.925  1.00 39.32           C  
ANISOU 3289  C   LYS A 397     4719   5856   4365   -587   -185     97       C  
ATOM   3290  O   LYS A 397      17.603 -12.253  55.037  1.00 39.69           O  
ANISOU 3290  O   LYS A 397     4782   5897   4400   -541   -169    135       O  
ATOM   3291  CB  LYS A 397      16.189 -11.979  57.789  1.00 39.04           C  
ANISOU 3291  CB  LYS A 397     4735   5815   4283   -542   -225     70       C  
ATOM   3292  CG  LYS A 397      17.221 -12.081  58.919  1.00 40.09           C  
ANISOU 3292  CG  LYS A 397     4813   6029   4390   -544   -256     39       C  
ATOM   3293  CD  LYS A 397      16.783 -13.046  60.017  1.00 41.21           C  
ANISOU 3293  CD  LYS A 397     4968   6207   4483   -488   -277     45       C  
ATOM   3294  CE  LYS A 397      17.899 -13.282  61.051  1.00 43.08           C  
ANISOU 3294  CE  LYS A 397     5150   6534   4685   -476   -311     19       C  
ATOM   3295  NZ  LYS A 397      18.113 -12.095  61.962  1.00 39.96           N  
ANISOU 3295  NZ  LYS A 397     4736   6155   4293   -519   -338    -44       N  
ATOM   3296  N   GLU A 398      18.915 -10.887  56.258  1.00 40.59           N  
ANISOU 3296  N   GLU A 398     4817   6066   4539   -629   -193     75       N  
ATOM   3297  CA  GLU A 398      20.167 -11.400  55.699  1.00 41.00           C  
ANISOU 3297  CA  GLU A 398     4809   6182   4587   -619   -182     97       C  
ATOM   3298  C   GLU A 398      20.584 -12.678  56.436  1.00 41.22           C  
ANISOU 3298  C   GLU A 398     4812   6284   4567   -557   -212     97       C  
ATOM   3299  O   GLU A 398      20.846 -12.644  57.643  1.00 42.78           O  
ANISOU 3299  O   GLU A 398     4984   6523   4746   -560   -247     61       O  
ATOM   3300  CB  GLU A 398      21.285 -10.357  55.791  1.00 43.27           C  
ANISOU 3300  CB  GLU A 398     5029   6497   4915   -691   -181     73       C  
ATOM   3301  CG  GLU A 398      22.553 -10.710  54.983  1.00 44.62           C  
ANISOU 3301  CG  GLU A 398     5131   6730   5091   -688   -156    104       C  
ATOM   3302  CD  GLU A 398      22.405 -10.441  53.486  1.00 49.49           C  
ANISOU 3302  CD  GLU A 398     5772   7303   5728   -691   -102    155       C  
ATOM   3303  OE1 GLU A 398      22.080  -9.289  53.117  1.00 50.25           O  
ANISOU 3303  OE1 GLU A 398     5891   7334   5869   -749    -80    156       O  
ATOM   3304  OE2 GLU A 398      22.623 -11.376  52.675  1.00 47.46           O  
ANISOU 3304  OE2 GLU A 398     5515   7077   5442   -629    -82    193       O  
ATOM   3305  N   PRO A 399      20.647 -13.809  55.718  1.00 39.80           N  
ANISOU 3305  N   PRO A 399     4642   6118   4364   -494   -200    137       N  
ATOM   3306  CA  PRO A 399      21.094 -15.028  56.382  1.00 40.30           C  
ANISOU 3306  CA  PRO A 399     4685   6245   4383   -433   -228    141       C  
ATOM   3307  C   PRO A 399      22.616 -15.140  56.351  1.00 41.43           C  
ANISOU 3307  C   PRO A 399     4744   6477   4520   -433   -232    135       C  
ATOM   3308  O   PRO A 399      23.258 -14.591  55.452  1.00 42.67           O  
ANISOU 3308  O   PRO A 399     4865   6642   4705   -466   -203    146       O  
ATOM   3309  CB  PRO A 399      20.486 -16.133  55.516  1.00 39.18           C  
ANISOU 3309  CB  PRO A 399     4592   6067   4226   -367   -216    181       C  
ATOM   3310  CG  PRO A 399      20.439 -15.532  54.122  1.00 38.39           C  
ANISOU 3310  CG  PRO A 399     4503   5927   4156   -389   -177    200       C  
ATOM   3311  CD  PRO A 399      20.339 -14.029  54.289  1.00 38.37           C  
ANISOU 3311  CD  PRO A 399     4493   5894   4191   -471   -165    176       C  
ATOM   3312  N   ILE A 400      23.178 -15.844  57.326  1.00 41.37           N  
ANISOU 3312  N   ILE A 400     4705   6538   4475   -395   -267    120       N  
ATOM   3313  CA  ILE A 400      24.575 -16.231  57.270  1.00 41.35           C  
ANISOU 3313  CA  ILE A 400     4624   6628   4459   -374   -275    118       C  
ATOM   3314  C   ILE A 400      24.660 -17.408  56.296  1.00 43.07           C  
ANISOU 3314  C   ILE A 400     4861   6849   4653   -299   -258    162       C  
ATOM   3315  O   ILE A 400      24.036 -18.453  56.520  1.00 41.91           O  
ANISOU 3315  O   ILE A 400     4768   6680   4477   -235   -273    180       O  
ATOM   3316  CB  ILE A 400      25.136 -16.614  58.656  1.00 39.99           C  
ANISOU 3316  CB  ILE A 400     4414   6532   4248   -347   -323     86       C  
ATOM   3317  CG1 ILE A 400      24.973 -15.448  59.641  1.00 41.21           C  
ANISOU 3317  CG1 ILE A 400     4557   6680   4421   -414   -347     33       C  
ATOM   3318  CG2 ILE A 400      26.608 -17.017  58.545  1.00 38.86           C  
ANISOU 3318  CG2 ILE A 400     4185   6490   4092   -322   -333     81       C  
ATOM   3319  CD1 ILE A 400      25.023 -15.862  61.138  1.00 39.15           C  
ANISOU 3319  CD1 ILE A 400     4293   6474   4109   -373   -396      3       C  
ATOM   3320  N   PRO A 401      25.397 -17.225  55.186  1.00 43.92           N  
ANISOU 3320  N   PRO A 401     4929   6982   4777   -305   -225    181       N  
ATOM   3321  CA  PRO A 401      25.582 -18.310  54.229  1.00 44.22           C  
ANISOU 3321  CA  PRO A 401     4983   7033   4788   -225   -211    215       C  
ATOM   3322  C   PRO A 401      26.157 -19.512  54.950  1.00 43.81           C  
ANISOU 3322  C   PRO A 401     4912   7046   4690   -149   -249    212       C  
ATOM   3323  O   PRO A 401      27.160 -19.382  55.654  1.00 47.11           O  
ANISOU 3323  O   PRO A 401     5257   7547   5097   -157   -269    189       O  
ATOM   3324  CB  PRO A 401      26.609 -17.738  53.246  1.00 44.17           C  
ANISOU 3324  CB  PRO A 401     4908   7076   4801   -251   -171    229       C  
ATOM   3325  CG  PRO A 401      26.373 -16.282  53.297  1.00 46.84           C  
ANISOU 3325  CG  PRO A 401     5235   7371   5189   -351   -152    215       C  
ATOM   3326  CD  PRO A 401      26.061 -15.988  54.742  1.00 42.95           C  
ANISOU 3326  CD  PRO A 401     4746   6873   4699   -384   -196    173       C  
ATOM   3327  N   ASN A 402      25.507 -20.661  54.799  1.00 43.32           N  
ANISOU 3327  N   ASN A 402     4915   6943   4602    -76   -262    234       N  
ATOM   3328  CA  ASN A 402      25.889 -21.866  55.529  1.00 43.82           C  
ANISOU 3328  CA  ASN A 402     4977   7050   4622      2   -299    237       C  
ATOM   3329  C   ASN A 402      25.036 -23.063  55.145  1.00 42.71           C  
ANISOU 3329  C   ASN A 402     4918   6840   4470     73   -308    265       C  
ATOM   3330  O   ASN A 402      24.105 -22.945  54.353  1.00 42.71           O  
ANISOU 3330  O   ASN A 402     4973   6760   4495     61   -290    277       O  
ATOM   3331  CB  ASN A 402      25.790 -21.641  57.047  1.00 43.57           C  
ANISOU 3331  CB  ASN A 402     4937   7041   4578    -22   -331    213       C  
ATOM   3332  CG  ASN A 402      26.816 -22.458  57.834  1.00 46.22           C  
ANISOU 3332  CG  ASN A 402     5226   7469   4866     44   -366    206       C  
ATOM   3333  OD1 ASN A 402      27.468 -23.362  57.293  1.00 41.40           O  
ANISOU 3333  OD1 ASN A 402     4602   6896   4232    115   -369    223       O  
ATOM   3334  ND2 ASN A 402      26.961 -22.140  59.123  1.00 45.28           N  
ANISOU 3334  ND2 ASN A 402     5084   7391   4728     26   -396    180       N  
ATOM   3335  N   ARG A 403      25.391 -24.217  55.699  1.00 42.27           N  
ANISOU 3335  N   ARG A 403     4868   6815   4378    148   -340    274       N  
ATOM   3336  CA  ARG A 403      24.562 -25.398  55.669  1.00 42.41           C  
ANISOU 3336  CA  ARG A 403     4963   6761   4391    209   -358    300       C  
ATOM   3337  C   ARG A 403      23.710 -25.360  56.926  1.00 43.11           C  
ANISOU 3337  C   ARG A 403     5086   6812   4480    182   -372    306       C  
ATOM   3338  O   ARG A 403      24.176 -24.929  57.987  1.00 44.31           O  
ANISOU 3338  O   ARG A 403     5198   7027   4611    162   -384    289       O  
ATOM   3339  CB  ARG A 403      25.433 -26.656  55.670  1.00 43.74           C  
ANISOU 3339  CB  ARG A 403     5122   6979   4520    308   -383    311       C  
ATOM   3340  CG  ARG A 403      26.339 -26.782  56.914  1.00 47.91           C  
ANISOU 3340  CG  ARG A 403     5598   7599   5008    328   -409    301       C  
ATOM   3341  CD  ARG A 403      27.120 -28.077  56.930  1.00 50.28           C  
ANISOU 3341  CD  ARG A 403     5896   7941   5267    435   -437    314       C  
ATOM   3342  NE  ARG A 403      28.232 -28.053  55.986  1.00 55.00           N  
ANISOU 3342  NE  ARG A 403     6432   8613   5851    468   -425    300       N  
ATOM   3343  CZ  ARG A 403      29.021 -29.093  55.741  1.00 59.39           C  
ANISOU 3343  CZ  ARG A 403     6980   9215   6371    567   -445    306       C  
ATOM   3344  NH1 ARG A 403      28.826 -30.246  56.374  1.00 58.93           N  
ANISOU 3344  NH1 ARG A 403     6975   9127   6289    640   -480    326       N  
ATOM   3345  NH2 ARG A 403      30.012 -28.979  54.866  1.00 60.83           N  
ANISOU 3345  NH2 ARG A 403     7101   9473   6540    595   -429    294       N  
ATOM   3346  N   TYR A 404      22.463 -25.801  56.814  1.00 42.95           N  
ANISOU 3346  N   TYR A 404     5138   6695   4484    184   -372    328       N  
ATOM   3347  CA  TYR A 404      21.595 -25.923  57.981  1.00 42.36           C  
ANISOU 3347  CA  TYR A 404     5098   6587   4409    169   -380    344       C  
ATOM   3348  C   TYR A 404      20.961 -27.299  57.987  1.00 42.96           C  
ANISOU 3348  C   TYR A 404     5236   6594   4491    230   -396    383       C  
ATOM   3349  O   TYR A 404      20.236 -27.669  57.059  1.00 45.26           O  
ANISOU 3349  O   TYR A 404     5572   6806   4819    236   -393    392       O  
ATOM   3350  CB  TYR A 404      20.542 -24.811  58.000  1.00 40.90           C  
ANISOU 3350  CB  TYR A 404     4931   6350   4260     88   -357    332       C  
ATOM   3351  CG  TYR A 404      21.141 -23.417  58.076  1.00 39.05           C  
ANISOU 3351  CG  TYR A 404     4640   6172   4027     23   -344    293       C  
ATOM   3352  CD1 TYR A 404      21.394 -22.825  59.306  1.00 37.51           C  
ANISOU 3352  CD1 TYR A 404     4414   6030   3808     -3   -356    272       C  
ATOM   3353  CD2 TYR A 404      21.476 -22.704  56.919  1.00 35.97           C  
ANISOU 3353  CD2 TYR A 404     4226   5779   3660     -9   -322    278       C  
ATOM   3354  CE1 TYR A 404      21.943 -21.558  59.395  1.00 35.45           C  
ANISOU 3354  CE1 TYR A 404     4101   5811   3556    -66   -351    231       C  
ATOM   3355  CE2 TYR A 404      22.034 -21.431  56.998  1.00 36.20           C  
ANISOU 3355  CE2 TYR A 404     4204   5852   3700    -74   -309    247       C  
ATOM   3356  CZ  TYR A 404      22.257 -20.866  58.249  1.00 36.51           C  
ANISOU 3356  CZ  TYR A 404     4213   5935   3724   -105   -327    221       C  
ATOM   3357  OH  TYR A 404      22.802 -19.611  58.375  1.00 38.20           O  
ANISOU 3357  OH  TYR A 404     4375   6184   3956   -173   -321    185       O  
ATOM   3358  N   LYS A 405      21.251 -28.054  59.039  1.00 43.32           N  
ANISOU 3358  N   LYS A 405     5286   6671   4502    277   -416    406       N  
ATOM   3359  CA  LYS A 405      20.905 -29.468  59.110  1.00 43.47           C  
ANISOU 3359  CA  LYS A 405     5361   6632   4526    344   -434    448       C  
ATOM   3360  C   LYS A 405      19.413 -29.690  59.399  1.00 44.11           C  
ANISOU 3360  C   LYS A 405     5498   6613   4649    311   -423    482       C  
ATOM   3361  O   LYS A 405      18.735 -30.349  58.624  1.00 44.85           O  
ANISOU 3361  O   LYS A 405     5637   6618   4787    323   -428    496       O  
ATOM   3362  CB  LYS A 405      21.805 -30.156  60.140  1.00 45.14           C  
ANISOU 3362  CB  LYS A 405     5556   6916   4680    410   -457    465       C  
ATOM   3363  CG  LYS A 405      21.684 -31.656  60.205  1.00 49.47           C  
ANISOU 3363  CG  LYS A 405     6158   7409   5229    488   -478    510       C  
ATOM   3364  CD  LYS A 405      22.728 -32.250  61.133  1.00 51.64           C  
ANISOU 3364  CD  LYS A 405     6412   7768   5440    562   -501    523       C  
ATOM   3365  CE  LYS A 405      22.528 -33.748  61.268  1.00 53.88           C  
ANISOU 3365  CE  LYS A 405     6759   7984   5728    640   -522    574       C  
ATOM   3366  NZ  LYS A 405      23.625 -34.389  62.046  1.00 59.47           N  
ANISOU 3366  NZ  LYS A 405     7451   8775   6370    726   -547    586       N  
ATOM   3367  N   TYR A 406      18.910 -29.135  60.503  1.00 44.94           N  
ANISOU 3367  N   TYR A 406     5600   6735   4741    272   -409    492       N  
ATOM   3368  CA  TYR A 406      17.490 -29.222  60.841  1.00 43.24           C  
ANISOU 3368  CA  TYR A 406     5427   6437   4564    237   -391    525       C  
ATOM   3369  C   TYR A 406      16.838 -27.843  60.792  1.00 43.45           C  
ANISOU 3369  C   TYR A 406     5437   6463   4608    159   -367    493       C  
ATOM   3370  O   TYR A 406      17.281 -26.910  61.464  1.00 44.28           O  
ANISOU 3370  O   TYR A 406     5505   6641   4677    134   -362    464       O  
ATOM   3371  CB  TYR A 406      17.275 -29.866  62.216  1.00 41.57           C  
ANISOU 3371  CB  TYR A 406     5234   6239   4320    270   -390    577       C  
ATOM   3372  CG  TYR A 406      17.746 -31.291  62.305  1.00 41.20           C  
ANISOU 3372  CG  TYR A 406     5216   6174   4263    349   -412    618       C  
ATOM   3373  CD1 TYR A 406      18.917 -31.617  62.990  1.00 41.85           C  
ANISOU 3373  CD1 TYR A 406     5276   6345   4280    411   -431    620       C  
ATOM   3374  CD2 TYR A 406      17.030 -32.318  61.699  1.00 39.20           C  
ANISOU 3374  CD2 TYR A 406     5012   5813   4068    364   -419    653       C  
ATOM   3375  CE1 TYR A 406      19.358 -32.933  63.072  1.00 42.75           C  
ANISOU 3375  CE1 TYR A 406     5421   6440   4382    490   -454    659       C  
ATOM   3376  CE2 TYR A 406      17.463 -33.634  61.769  1.00 39.27           C  
ANISOU 3376  CE2 TYR A 406     5054   5796   4072    438   -443    690       C  
ATOM   3377  CZ  TYR A 406      18.624 -33.937  62.454  1.00 43.86           C  
ANISOU 3377  CZ  TYR A 406     5616   6465   4583    503   -459    695       C  
ATOM   3378  OH  TYR A 406      19.051 -35.249  62.519  1.00 46.14           O  
ANISOU 3378  OH  TYR A 406     5941   6724   4866    583   -484    733       O  
ATOM   3379  N   VAL A 407      15.788 -27.729  59.984  1.00 43.09           N  
ANISOU 3379  N   VAL A 407     5420   6333   4619    124   -356    493       N  
ATOM   3380  CA  VAL A 407      15.076 -26.470  59.795  1.00 43.36           C  
ANISOU 3380  CA  VAL A 407     5445   6354   4675     55   -334    463       C  
ATOM   3381  C   VAL A 407      13.563 -26.686  59.880  1.00 43.41           C  
ANISOU 3381  C   VAL A 407     5489   6277   4730     30   -320    492       C  
ATOM   3382  O   VAL A 407      13.027 -27.619  59.275  1.00 43.08           O  
ANISOU 3382  O   VAL A 407     5478   6159   4732     49   -331    516       O  
ATOM   3383  CB  VAL A 407      15.417 -25.817  58.427  1.00 41.40           C  
ANISOU 3383  CB  VAL A 407     5184   6098   4447     35   -334    421       C  
ATOM   3384  CG1 VAL A 407      14.615 -24.540  58.227  1.00 41.51           C  
ANISOU 3384  CG1 VAL A 407     5198   6089   4485    -31   -312    395       C  
ATOM   3385  CG2 VAL A 407      16.895 -25.516  58.319  1.00 40.19           C  
ANISOU 3385  CG2 VAL A 407     4984   6032   4253     52   -341    395       C  
ATOM   3386  N   MET A 408      12.894 -25.832  60.653  1.00 44.09           N  
ANISOU 3386  N   MET A 408     5568   6377   4808    -11   -299    489       N  
ATOM   3387  CA  MET A 408      11.436 -25.739  60.651  1.00 43.72           C  
ANISOU 3387  CA  MET A 408     5542   6261   4807    -45   -280    507       C  
ATOM   3388  C   MET A 408      11.104 -24.340  60.209  1.00 42.65           C  
ANISOU 3388  C   MET A 408     5395   6128   4680    -96   -268    458       C  
ATOM   3389  O   MET A 408      11.664 -23.366  60.733  1.00 42.78           O  
ANISOU 3389  O   MET A 408     5388   6210   4658   -114   -263    426       O  
ATOM   3390  CB  MET A 408      10.826 -25.908  62.040  1.00 47.87           C  
ANISOU 3390  CB  MET A 408     6072   6807   5311    -42   -259    549       C  
ATOM   3391  CG  MET A 408      11.253 -27.099  62.861  1.00 56.31           C  
ANISOU 3391  CG  MET A 408     7150   7894   6351     11   -265    605       C  
ATOM   3392  SD  MET A 408      10.018 -27.331  64.167  1.00 68.20           S  
ANISOU 3392  SD  MET A 408     8667   9391   7854      6   -227    669       S  
ATOM   3393  CE  MET A 408       8.680 -27.980  63.161  1.00 60.56           C  
ANISOU 3393  CE  MET A 408     7722   8299   6990    -27   -223    695       C  
ATOM   3394  N   SER A 409      10.191 -24.226  59.255  1.00 39.65           N  
ANISOU 3394  N   SER A 409     5034   5677   4354   -118   -266    450       N  
ATOM   3395  CA  SER A 409       9.716 -22.920  58.861  1.00 37.64           C  
ANISOU 3395  CA  SER A 409     4776   5417   4110   -162   -252    410       C  
ATOM   3396  C   SER A 409       8.277 -22.725  59.316  1.00 38.01           C  
ANISOU 3396  C   SER A 409     4833   5425   4186   -186   -234    425       C  
ATOM   3397  O   SER A 409       7.576 -23.687  59.648  1.00 36.52           O  
ANISOU 3397  O   SER A 409     4654   5200   4023   -174   -231    470       O  
ATOM   3398  CB  SER A 409       9.866 -22.715  57.357  1.00 36.85           C  
ANISOU 3398  CB  SER A 409     4685   5277   4038   -164   -263    381       C  
ATOM   3399  OG  SER A 409       9.067 -23.624  56.614  1.00 37.27           O  
ANISOU 3399  OG  SER A 409     4764   5257   4141   -146   -277    398       O  
ATOM   3400  N   PHE A 410       7.866 -21.463  59.348  1.00 36.69           N  
ANISOU 3400  N   PHE A 410     4661   5266   4014   -221   -220    391       N  
ATOM   3401  CA  PHE A 410       6.543 -21.044  59.778  1.00 33.54           C  
ANISOU 3401  CA  PHE A 410     4267   4843   3634   -242   -200    396       C  
ATOM   3402  C   PHE A 410       6.170 -19.876  58.886  1.00 33.10           C  
ANISOU 3402  C   PHE A 410     4219   4759   3597   -270   -199    350       C  
ATOM   3403  O   PHE A 410       7.017 -19.045  58.563  1.00 33.90           O  
ANISOU 3403  O   PHE A 410     4317   4886   3677   -283   -203    314       O  
ATOM   3404  CB  PHE A 410       6.571 -20.583  61.237  1.00 32.07           C  
ANISOU 3404  CB  PHE A 410     4067   4722   3396   -241   -183    401       C  
ATOM   3405  CG  PHE A 410       6.757 -21.707  62.231  1.00 36.35           C  
ANISOU 3405  CG  PHE A 410     4605   5292   3914   -207   -178    456       C  
ATOM   3406  CD1 PHE A 410       8.030 -22.176  62.557  1.00 31.18           C  
ANISOU 3406  CD1 PHE A 410     3943   4688   3218   -178   -195    461       C  
ATOM   3407  CD2 PHE A 410       5.650 -22.289  62.857  1.00 36.58           C  
ANISOU 3407  CD2 PHE A 410     4635   5301   3961   -203   -154    507       C  
ATOM   3408  CE1 PHE A 410       8.187 -23.217  63.459  1.00 30.74           C  
ANISOU 3408  CE1 PHE A 410     3888   4655   3137   -141   -190    515       C  
ATOM   3409  CE2 PHE A 410       5.802 -23.330  63.763  1.00 30.83           C  
ANISOU 3409  CE2 PHE A 410     3907   4594   3212   -170   -145    567       C  
ATOM   3410  CZ  PHE A 410       7.077 -23.797  64.062  1.00 30.92           C  
ANISOU 3410  CZ  PHE A 410     3919   4651   3179   -137   -163    571       C  
ATOM   3411  N   ASP A 411       4.906 -19.786  58.510  1.00 32.54           N  
ANISOU 3411  N   ASP A 411     4159   4637   3569   -281   -193    352       N  
ATOM   3412  CA  ASP A 411       4.489 -18.781  57.552  1.00 37.61           C  
ANISOU 3412  CA  ASP A 411     4814   5246   4231   -299   -195    312       C  
ATOM   3413  C   ASP A 411       3.100 -18.255  57.896  1.00 37.85           C  
ANISOU 3413  C   ASP A 411     4844   5256   4280   -312   -179    308       C  
ATOM   3414  O   ASP A 411       2.266 -18.999  58.411  1.00 41.63           O  
ANISOU 3414  O   ASP A 411     5312   5724   4783   -307   -170    343       O  
ATOM   3415  CB  ASP A 411       4.579 -19.369  56.127  1.00 39.43           C  
ANISOU 3415  CB  ASP A 411     5060   5425   4496   -282   -217    308       C  
ATOM   3416  CG  ASP A 411       3.489 -18.885  55.222  1.00 44.13           C  
ANISOU 3416  CG  ASP A 411     5671   5967   5130   -288   -221    286       C  
ATOM   3417  OD1 ASP A 411       2.346 -19.372  55.340  1.00 48.27           O  
ANISOU 3417  OD1 ASP A 411     6190   6457   5693   -288   -223    301       O  
ATOM   3418  OD2 ASP A 411       3.767 -18.006  54.384  1.00 49.81           O  
ANISOU 3418  OD2 ASP A 411     6406   6679   5841   -291   -222    256       O  
ATOM   3419  N   LEU A 412       2.860 -16.972  57.621  1.00 36.54           N  
ANISOU 3419  N   LEU A 412     4690   5087   4108   -327   -173    268       N  
ATOM   3420  CA  LEU A 412       1.578 -16.344  57.944  1.00 38.34           C  
ANISOU 3420  CA  LEU A 412     4917   5302   4349   -333   -159    258       C  
ATOM   3421  C   LEU A 412       0.522 -16.596  56.891  1.00 38.74           C  
ANISOU 3421  C   LEU A 412     4974   5292   4453   -328   -170    256       C  
ATOM   3422  O   LEU A 412       0.817 -16.563  55.693  1.00 41.81           O  
ANISOU 3422  O   LEU A 412     5382   5646   4857   -322   -188    238       O  
ATOM   3423  CB  LEU A 412       1.760 -14.838  58.145  1.00 38.78           C  
ANISOU 3423  CB  LEU A 412     4986   5375   4374   -348   -153    212       C  
ATOM   3424  CG  LEU A 412       2.321 -14.450  59.516  1.00 34.38           C  
ANISOU 3424  CG  LEU A 412     4417   4881   3765   -350   -143    205       C  
ATOM   3425  CD1 LEU A 412       3.174 -13.215  59.396  1.00 29.19           C  
ANISOU 3425  CD1 LEU A 412     3772   4232   3086   -370   -151    158       C  
ATOM   3426  CD2 LEU A 412       1.208 -14.264  60.528  1.00 34.70           C  
ANISOU 3426  CD2 LEU A 412     4447   4943   3792   -338   -123    212       C  
ATOM   3427  N   THR A 413      -0.712 -16.826  57.335  1.00 39.99           N  
ANISOU 3427  N   THR A 413     5115   5441   4637   -327   -158    272       N  
ATOM   3428  CA  THR A 413      -1.829 -17.097  56.422  1.00 38.54           C  
ANISOU 3428  CA  THR A 413     4929   5203   4511   -323   -173    266       C  
ATOM   3429  C   THR A 413      -2.260 -15.840  55.668  1.00 37.11           C  
ANISOU 3429  C   THR A 413     4770   5002   4326   -319   -178    219       C  
ATOM   3430  O   THR A 413      -2.651 -14.833  56.272  1.00 34.07           O  
ANISOU 3430  O   THR A 413     4387   4641   3917   -321   -160    200       O  
ATOM   3431  CB  THR A 413      -3.028 -17.756  57.150  1.00 39.77           C  
ANISOU 3431  CB  THR A 413     5049   5358   4703   -327   -157    303       C  
ATOM   3432  OG1 THR A 413      -2.747 -19.142  57.349  1.00 42.40           O  
ANISOU 3432  OG1 THR A 413     5369   5679   5063   -329   -162    349       O  
ATOM   3433  CG2 THR A 413      -4.312 -17.669  56.325  1.00 41.08           C  
ANISOU 3433  CG2 THR A 413     5204   5478   4925   -325   -171    283       C  
ATOM   3434  N   SER A 414      -2.151 -15.922  54.341  1.00 36.14           N  
ANISOU 3434  N   SER A 414     4670   4838   4226   -306   -204    200       N  
ATOM   3435  CA  SER A 414      -2.570 -14.860  53.429  1.00 35.94           C  
ANISOU 3435  CA  SER A 414     4671   4786   4200   -294   -212    161       C  
ATOM   3436  C   SER A 414      -2.260 -13.484  54.000  1.00 33.93           C  
ANISOU 3436  C   SER A 414     4434   4557   3901   -306   -190    140       C  
ATOM   3437  O   SER A 414      -3.168 -12.733  54.339  1.00 34.41           O  
ANISOU 3437  O   SER A 414     4494   4618   3962   -301   -180    122       O  
ATOM   3438  CB  SER A 414      -4.066 -15.000  53.139  1.00 36.64           C  
ANISOU 3438  CB  SER A 414     4743   4846   4334   -282   -223    152       C  
ATOM   3439  OG  SER A 414      -4.500 -14.006  52.240  1.00 42.94           O  
ANISOU 3439  OG  SER A 414     5569   5619   5127   -262   -234    115       O  
ATOM   3440  N   LEU A 415      -0.978 -13.152  54.103  1.00 32.95           N  
ANISOU 3440  N   LEU A 415     4323   4453   3743   -319   -184    138       N  
ATOM   3441  CA  LEU A 415      -0.577 -12.034  54.963  1.00 33.08           C  
ANISOU 3441  CA  LEU A 415     4347   4499   3724   -337   -167    118       C  
ATOM   3442  C   LEU A 415      -1.208 -10.694  54.650  1.00 33.92           C  
ANISOU 3442  C   LEU A 415     4482   4577   3828   -332   -163     83       C  
ATOM   3443  O   LEU A 415      -1.858 -10.110  55.518  1.00 38.40           O  
ANISOU 3443  O   LEU A 415     5045   5161   4383   -330   -153     68       O  
ATOM   3444  CB  LEU A 415       0.946 -11.894  55.085  1.00 32.66           C  
ANISOU 3444  CB  LEU A 415     4296   4472   3643   -357   -165    119       C  
ATOM   3445  CG  LEU A 415       1.394 -10.780  56.033  1.00 29.35           C  
ANISOU 3445  CG  LEU A 415     3881   4080   3192   -379   -156     92       C  
ATOM   3446  CD1 LEU A 415       0.874 -11.003  57.476  1.00 31.27           C  
ANISOU 3446  CD1 LEU A 415     4100   4368   3413   -372   -147     96       C  
ATOM   3447  CD2 LEU A 415       2.903 -10.636  56.024  1.00 29.19           C  
ANISOU 3447  CD2 LEU A 415     3855   4082   3154   -402   -158     90       C  
ATOM   3448  N   TYR A 416      -1.025 -10.184  53.439  1.00 35.18           N  
ANISOU 3448  N   TYR A 416     4674   4696   3995   -325   -171     72       N  
ATOM   3449  CA  TYR A 416      -1.484  -8.814  53.168  1.00 36.39           C  
ANISOU 3449  CA  TYR A 416     4863   4820   4143   -319   -167     42       C  
ATOM   3450  C   TYR A 416      -2.999  -8.644  53.350  1.00 34.91           C  
ANISOU 3450  C   TYR A 416     4671   4623   3970   -292   -170     27       C  
ATOM   3451  O   TYR A 416      -3.425  -7.725  54.047  1.00 36.04           O  
ANISOU 3451  O   TYR A 416     4823   4772   4099   -290   -162      2       O  
ATOM   3452  CB  TYR A 416      -0.970  -8.279  51.821  1.00 36.30           C  
ANISOU 3452  CB  TYR A 416     4890   4767   4134   -312   -169     41       C  
ATOM   3453  CG  TYR A 416       0.481  -7.813  51.862  1.00 35.91           C  
ANISOU 3453  CG  TYR A 416     4848   4728   4069   -347   -156     47       C  
ATOM   3454  CD1 TYR A 416       1.305  -8.119  52.950  1.00 36.26           C  
ANISOU 3454  CD1 TYR A 416     4860   4818   4098   -378   -153     50       C  
ATOM   3455  CD2 TYR A 416       1.035  -7.088  50.804  1.00 36.34           C  
ANISOU 3455  CD2 TYR A 416     4937   4748   4123   -349   -147     52       C  
ATOM   3456  CE1 TYR A 416       2.637  -7.709  52.987  1.00 40.29           C  
ANISOU 3456  CE1 TYR A 416     5367   5341   4600   -412   -145     51       C  
ATOM   3457  CE2 TYR A 416       2.369  -6.673  50.828  1.00 36.03           C  
ANISOU 3457  CE2 TYR A 416     4895   4719   4077   -387   -133     61       C  
ATOM   3458  CZ  TYR A 416       3.160  -6.992  51.920  1.00 38.81           C  
ANISOU 3458  CZ  TYR A 416     5209   5118   4420   -420   -134     58       C  
ATOM   3459  OH  TYR A 416       4.474  -6.594  51.968  1.00 43.85           O  
ANISOU 3459  OH  TYR A 416     5834   5770   5056   -459   -124     63       O  
ATOM   3460  N   PRO A 417      -3.812  -9.547  52.769  1.00 34.40           N  
ANISOU 3460  N   PRO A 417     4588   4547   3937   -269   -184     38       N  
ATOM   3461  CA  PRO A 417      -5.244  -9.416  53.021  1.00 34.88           C  
ANISOU 3461  CA  PRO A 417     4631   4607   4014   -247   -186     25       C  
ATOM   3462  C   PRO A 417      -5.590  -9.559  54.513  1.00 33.67           C  
ANISOU 3462  C   PRO A 417     4441   4503   3849   -258   -165     34       C  
ATOM   3463  O   PRO A 417      -6.528  -8.938  54.991  1.00 32.89           O  
ANISOU 3463  O   PRO A 417     4336   4415   3745   -240   -157     15       O  
ATOM   3464  CB  PRO A 417      -5.841 -10.558  52.198  1.00 34.32           C  
ANISOU 3464  CB  PRO A 417     4537   4517   3986   -230   -210     38       C  
ATOM   3465  CG  PRO A 417      -4.823 -10.801  51.112  1.00 33.94           C  
ANISOU 3465  CG  PRO A 417     4519   4445   3931   -227   -223     43       C  
ATOM   3466  CD  PRO A 417      -3.532 -10.652  51.831  1.00 35.33           C  
ANISOU 3466  CD  PRO A 417     4699   4649   4076   -260   -203     58       C  
ATOM   3467  N   SER A 418      -4.811 -10.344  55.246  1.00 33.94           N  
ANISOU 3467  N   SER A 418     4452   4570   3873   -281   -156     62       N  
ATOM   3468  CA  SER A 418      -5.029 -10.490  56.679  1.00 33.20           C  
ANISOU 3468  CA  SER A 418     4328   4530   3757   -286   -133     75       C  
ATOM   3469  C   SER A 418      -4.700  -9.181  57.394  1.00 34.37           C  
ANISOU 3469  C   SER A 418     4502   4696   3859   -285   -125     39       C  
ATOM   3470  O   SER A 418      -5.396  -8.777  58.324  1.00 32.43           O  
ANISOU 3470  O   SER A 418     4244   4484   3593   -267   -110     28       O  
ATOM   3471  CB  SER A 418      -4.211 -11.656  57.242  1.00 33.33           C  
ANISOU 3471  CB  SER A 418     4319   4575   3768   -304   -128    116       C  
ATOM   3472  OG  SER A 418      -4.641 -12.902  56.705  1.00 28.31           O  
ANISOU 3472  OG  SER A 418     3658   3917   3180   -304   -138    149       O  
ATOM   3473  N   ILE A 419      -3.649  -8.503  56.947  1.00 33.95           N  
ANISOU 3473  N   ILE A 419     4485   4620   3793   -302   -135     19       N  
ATOM   3474  CA  ILE A 419      -3.339  -7.199  57.508  1.00 33.43           C  
ANISOU 3474  CA  ILE A 419     4448   4557   3696   -305   -134    -22       C  
ATOM   3475  C   ILE A 419      -4.483  -6.222  57.204  1.00 33.83           C  
ANISOU 3475  C   ILE A 419     4523   4577   3753   -274   -135    -54       C  
ATOM   3476  O   ILE A 419      -5.002  -5.565  58.113  1.00 34.80           O  
ANISOU 3476  O   ILE A 419     4647   4724   3850   -255   -129    -81       O  
ATOM   3477  CB  ILE A 419      -1.975  -6.668  57.014  1.00 34.76           C  
ANISOU 3477  CB  ILE A 419     4646   4701   3862   -337   -143    -33       C  
ATOM   3478  CG1 ILE A 419      -0.852  -7.616  57.452  1.00 34.08           C  
ANISOU 3478  CG1 ILE A 419     4530   4657   3764   -360   -143     -6       C  
ATOM   3479  CG2 ILE A 419      -1.746  -5.244  57.522  1.00 34.29           C  
ANISOU 3479  CG2 ILE A 419     4618   4629   3783   -344   -148    -81       C  
ATOM   3480  CD1 ILE A 419       0.528  -7.236  56.961  1.00 33.93           C  
ANISOU 3480  CD1 ILE A 419     4524   4623   3746   -393   -150    -12       C  
ATOM   3481  N   ILE A 420      -4.880  -6.151  55.933  1.00 31.41           N  
ANISOU 3481  N   ILE A 420     4237   4221   3476   -263   -145    -53       N  
ATOM   3482  CA  ILE A 420      -6.007  -5.317  55.515  1.00 31.43           C  
ANISOU 3482  CA  ILE A 420     4263   4194   3486   -226   -150    -80       C  
ATOM   3483  C   ILE A 420      -7.191  -5.472  56.466  1.00 34.56           C  
ANISOU 3483  C   ILE A 420     4620   4635   3874   -198   -138    -85       C  
ATOM   3484  O   ILE A 420      -7.746  -4.473  56.936  1.00 36.61           O  
ANISOU 3484  O   ILE A 420     4899   4898   4113   -171   -135   -120       O  
ATOM   3485  CB  ILE A 420      -6.421  -5.608  54.037  1.00 30.15           C  
ANISOU 3485  CB  ILE A 420     4114   3987   3356   -207   -165    -71       C  
ATOM   3486  CG1 ILE A 420      -5.473  -4.878  53.088  1.00 27.46           C  
ANISOU 3486  CG1 ILE A 420     3827   3597   3010   -219   -170    -74       C  
ATOM   3487  CG2 ILE A 420      -7.857  -5.168  53.740  1.00 25.50           C  
ANISOU 3487  CG2 ILE A 420     3525   3386   2777   -161   -173    -93       C  
ATOM   3488  CD1 ILE A 420      -5.561  -5.307  51.653  1.00 19.74           C  
ANISOU 3488  CD1 ILE A 420     2864   2586   2052   -199   -184    -59       C  
ATOM   3489  N   ARG A 421      -7.550  -6.721  56.758  1.00 34.43           N  
ANISOU 3489  N   ARG A 421     4551   4654   3876   -203   -129    -48       N  
ATOM   3490  CA  ARG A 421      -8.691  -7.032  57.622  1.00 36.00           C  
ANISOU 3490  CA  ARG A 421     4703   4902   4075   -180   -110    -39       C  
ATOM   3491  C   ARG A 421      -8.447  -6.788  59.108  1.00 37.40           C  
ANISOU 3491  C   ARG A 421     4869   5139   4203   -177    -88    -42       C  
ATOM   3492  O   ARG A 421      -9.366  -6.408  59.828  1.00 41.39           O  
ANISOU 3492  O   ARG A 421     5355   5682   4689   -143    -72    -54       O  
ATOM   3493  CB  ARG A 421      -9.123  -8.481  57.426  1.00 35.69           C  
ANISOU 3493  CB  ARG A 421     4609   4871   4080   -193   -107      8       C  
ATOM   3494  CG  ARG A 421      -9.703  -8.796  56.072  1.00 35.74           C  
ANISOU 3494  CG  ARG A 421     4615   4829   4137   -184   -134      3       C  
ATOM   3495  CD  ARG A 421      -9.728 -10.292  55.883  1.00 37.57           C  
ANISOU 3495  CD  ARG A 421     4802   5058   4413   -208   -139     46       C  
ATOM   3496  NE  ARG A 421     -10.728 -10.917  56.745  1.00 37.73           N  
ANISOU 3496  NE  ARG A 421     4759   5120   4456   -208   -115     76       N  
ATOM   3497  CZ  ARG A 421     -10.601 -12.131  57.274  1.00 37.06           C  
ANISOU 3497  CZ  ARG A 421     4633   5052   4396   -234   -101    126       C  
ATOM   3498  NH1 ARG A 421      -9.509 -12.844  57.038  1.00 30.49           N  
ANISOU 3498  NH1 ARG A 421     3820   4200   3565   -257   -113    147       N  
ATOM   3499  NH2 ARG A 421     -11.567 -12.627  58.045  1.00 30.77           N  
ANISOU 3499  NH2 ARG A 421     3777   4292   3621   -234    -73    159       N  
ATOM   3500  N   GLN A 422      -7.226  -7.022  59.575  1.00 37.49           N  
ANISOU 3500  N   GLN A 422     4889   5166   4191   -205    -88    -32       N  
ATOM   3501  CA  GLN A 422      -6.915  -6.864  60.994  1.00 37.30           C  
ANISOU 3501  CA  GLN A 422     4854   5204   4113   -196    -72    -37       C  
ATOM   3502  C   GLN A 422      -6.887  -5.395  61.405  1.00 39.49           C  
ANISOU 3502  C   GLN A 422     5175   5477   4354   -173    -83    -99       C  
ATOM   3503  O   GLN A 422      -7.382  -5.029  62.484  1.00 42.49           O  
ANISOU 3503  O   GLN A 422     5544   5908   4690   -138    -69   -116       O  
ATOM   3504  CB  GLN A 422      -5.595  -7.556  61.339  1.00 36.37           C  
ANISOU 3504  CB  GLN A 422     4732   5106   3981   -228    -76    -12       C  
ATOM   3505  CG  GLN A 422      -5.018  -7.188  62.704  1.00 39.39           C  
ANISOU 3505  CG  GLN A 422     5117   5549   4302   -216    -71    -31       C  
ATOM   3506  CD  GLN A 422      -4.111  -8.257  63.287  1.00 38.76           C  
ANISOU 3506  CD  GLN A 422     5012   5512   4204   -232    -66     11       C  
ATOM   3507  OE1 GLN A 422      -4.149  -9.422  62.880  1.00 39.17           O  
ANISOU 3507  OE1 GLN A 422     5038   5556   4290   -247    -57     64       O  
ATOM   3508  NE2 GLN A 422      -3.294  -7.865  64.257  1.00 37.44           N  
ANISOU 3508  NE2 GLN A 422     4853   5389   3984   -226    -74    -16       N  
ATOM   3509  N   VAL A 423      -6.322  -4.564  60.531  1.00 38.21           N  
ANISOU 3509  N   VAL A 423     5061   5250   4207   -191   -106   -131       N  
ATOM   3510  CA  VAL A 423      -6.113  -3.142  60.797  1.00 35.15           C  
ANISOU 3510  CA  VAL A 423     4723   4838   3796   -179   -122   -191       C  
ATOM   3511  C   VAL A 423      -7.315  -2.333  60.333  1.00 35.92           C  
ANISOU 3511  C   VAL A 423     4842   4902   3903   -137   -124   -219       C  
ATOM   3512  O   VAL A 423      -7.524  -1.201  60.778  1.00 37.93           O  
ANISOU 3512  O   VAL A 423     5132   5147   4132   -109   -134   -270       O  
ATOM   3513  CB  VAL A 423      -4.840  -2.628  60.072  1.00 34.44           C  
ANISOU 3513  CB  VAL A 423     4672   4688   3724   -225   -143   -205       C  
ATOM   3514  CG1 VAL A 423      -4.527  -1.192  60.459  1.00 32.95           C  
ANISOU 3514  CG1 VAL A 423     4533   4468   3520   -222   -163   -267       C  
ATOM   3515  CG2 VAL A 423      -3.652  -3.516  60.373  1.00 33.21           C  
ANISOU 3515  CG2 VAL A 423     4489   4566   3564   -264   -143   -175       C  
ATOM   3516  N   ASN A 424      -8.093  -2.928  59.429  1.00 36.47           N  
ANISOU 3516  N   ASN A 424     4892   4956   4010   -128   -119   -189       N  
ATOM   3517  CA  ASN A 424      -9.274  -2.294  58.812  1.00 36.49           C  
ANISOU 3517  CA  ASN A 424     4909   4929   4026    -84   -124   -211       C  
ATOM   3518  C   ASN A 424      -8.887  -1.200  57.825  1.00 33.29           C  
ANISOU 3518  C   ASN A 424     4573   4442   3633    -86   -146   -241       C  
ATOM   3519  O   ASN A 424      -9.428  -0.104  57.833  1.00 33.78           O  
ANISOU 3519  O   ASN A 424     4674   4477   3683    -48   -155   -282       O  
ATOM   3520  CB  ASN A 424     -10.262  -1.773  59.862  1.00 37.31           C  
ANISOU 3520  CB  ASN A 424     4998   5084   4094    -32   -111   -240       C  
ATOM   3521  CG  ASN A 424     -11.696  -1.783  59.366  1.00 40.02           C  
ANISOU 3521  CG  ASN A 424     5317   5431   4458     14   -107   -241       C  
ATOM   3522  OD1 ASN A 424     -12.145  -2.750  58.741  1.00 44.25           O  
ANISOU 3522  OD1 ASN A 424     5809   5969   5034      2   -104   -203       O  
ATOM   3523  ND2 ASN A 424     -12.430  -0.713  59.651  1.00 38.92           N  
ANISOU 3523  ND2 ASN A 424     5202   5292   4293     68   -111   -287       N  
ATOM   3524  N   ILE A 425      -7.935  -1.523  56.971  1.00 33.12           N  
ANISOU 3524  N   ILE A 425     4568   4382   3635   -128   -153   -216       N  
ATOM   3525  CA  ILE A 425      -7.443  -0.593  55.972  1.00 32.65           C  
ANISOU 3525  CA  ILE A 425     4571   4245   3589   -136   -167   -230       C  
ATOM   3526  C   ILE A 425      -8.405  -0.514  54.797  1.00 33.93           C  
ANISOU 3526  C   ILE A 425     4748   4372   3771    -94   -174   -225       C  
ATOM   3527  O   ILE A 425      -8.707  -1.521  54.165  1.00 34.48           O  
ANISOU 3527  O   ILE A 425     4784   4455   3863    -93   -175   -195       O  
ATOM   3528  CB  ILE A 425      -6.033  -0.994  55.513  1.00 32.58           C  
ANISOU 3528  CB  ILE A 425     4567   4219   3593   -192   -166   -201       C  
ATOM   3529  CG1 ILE A 425      -5.105  -1.060  56.739  1.00 28.89           C  
ANISOU 3529  CG1 ILE A 425     4080   3794   3103   -227   -164   -211       C  
ATOM   3530  CG2 ILE A 425      -5.513  -0.017  54.476  1.00 28.36           C  
ANISOU 3530  CG2 ILE A 425     4095   3607   3074   -201   -172   -205       C  
ATOM   3531  CD1 ILE A 425      -3.815  -1.807  56.515  1.00 25.44           C  
ANISOU 3531  CD1 ILE A 425     3624   3367   2676   -278   -161   -178       C  
ATOM   3532  N   SER A 426      -8.896   0.695  54.540  1.00 35.12           N  
ANISOU 3532  N   SER A 426     4952   4478   3916    -57   -183   -259       N  
ATOM   3533  CA  SER A 426      -9.867   0.964  53.495  1.00 35.49           C  
ANISOU 3533  CA  SER A 426     5019   4491   3974     -6   -194   -262       C  
ATOM   3534  C   SER A 426      -9.814   2.459  53.254  1.00 38.00           C  
ANISOU 3534  C   SER A 426     5415   4740   4282     18   -203   -294       C  
ATOM   3535  O   SER A 426      -9.401   3.196  54.147  1.00 39.13           O  
ANISOU 3535  O   SER A 426     5581   4877   4412      3   -202   -323       O  
ATOM   3536  CB  SER A 426     -11.269   0.568  53.943  1.00 34.96           C  
ANISOU 3536  CB  SER A 426     4899   4479   3904     42   -194   -275       C  
ATOM   3537  OG  SER A 426     -12.088   0.240  52.825  1.00 37.38           O  
ANISOU 3537  OG  SER A 426     5198   4772   4232     80   -209   -267       O  
ATOM   3538  N   PRO A 427     -10.203   2.914  52.041  1.00 40.00           N  
ANISOU 3538  N   PRO A 427     5713   4940   4543     55   -212   -288       N  
ATOM   3539  CA  PRO A 427     -10.241   4.349  51.736  1.00 40.60           C  
ANISOU 3539  CA  PRO A 427     5870   4942   4613     84   -219   -312       C  
ATOM   3540  C   PRO A 427     -11.092   5.174  52.717  1.00 43.26           C  
ANISOU 3540  C   PRO A 427     6218   5290   4930    131   -228   -366       C  
ATOM   3541  O   PRO A 427     -10.710   6.300  53.069  1.00 45.03           O  
ANISOU 3541  O   PRO A 427     6501   5460   5150    128   -234   -394       O  
ATOM   3542  CB  PRO A 427     -10.846   4.402  50.327  1.00 39.56           C  
ANISOU 3542  CB  PRO A 427     5768   4776   4485    136   -229   -295       C  
ATOM   3543  CG  PRO A 427     -11.407   3.020  50.081  1.00 41.53           C  
ANISOU 3543  CG  PRO A 427     5944   5093   4745    144   -234   -278       C  
ATOM   3544  CD  PRO A 427     -10.525   2.104  50.854  1.00 37.15           C  
ANISOU 3544  CD  PRO A 427     5336   4581   4197     74   -219   -258       C  
ATOM   3545  N   GLU A 428     -12.210   4.616  53.172  1.00 42.40           N  
ANISOU 3545  N   GLU A 428     6049   5250   4810    173   -229   -379       N  
ATOM   3546  CA  GLU A 428     -13.144   5.373  54.005  1.00 44.04           C  
ANISOU 3546  CA  GLU A 428     6262   5477   4993    233   -234   -429       C  
ATOM   3547  C   GLU A 428     -13.002   5.118  55.511  1.00 45.45           C  
ANISOU 3547  C   GLU A 428     6396   5725   5148    215   -222   -449       C  
ATOM   3548  O   GLU A 428     -13.770   5.660  56.298  1.00 46.07           O  
ANISOU 3548  O   GLU A 428     6472   5833   5199    269   -224   -490       O  
ATOM   3549  CB  GLU A 428     -14.587   5.123  53.549  1.00 43.19           C  
ANISOU 3549  CB  GLU A 428     6120   5406   4885    304   -242   -436       C  
ATOM   3550  CG  GLU A 428     -15.239   3.844  54.073  1.00 42.85           C  
ANISOU 3550  CG  GLU A 428     5974   5457   4849    298   -228   -418       C  
ATOM   3551  CD  GLU A 428     -14.750   2.564  53.398  1.00 48.82           C  
ANISOU 3551  CD  GLU A 428     6688   6223   5638    244   -225   -369       C  
ATOM   3552  OE1 GLU A 428     -13.591   2.507  52.917  1.00 46.10           O  
ANISOU 3552  OE1 GLU A 428     6381   5833   5301    194   -225   -345       O  
ATOM   3553  OE2 GLU A 428     -15.542   1.596  53.361  1.00 51.69           O  
ANISOU 3553  OE2 GLU A 428     6977   6641   6021    253   -224   -355       O  
ATOM   3554  N   THR A 429     -12.026   4.304  55.914  1.00 46.13           N  
ANISOU 3554  N   THR A 429     6447   5839   5240    147   -210   -420       N  
ATOM   3555  CA  THR A 429     -11.868   3.961  57.333  1.00 47.73           C  
ANISOU 3555  CA  THR A 429     6605   6115   5415    135   -198   -433       C  
ATOM   3556  C   THR A 429     -10.696   4.682  57.996  1.00 47.82           C  
ANISOU 3556  C   THR A 429     6662   6094   5414     96   -209   -462       C  
ATOM   3557  O   THR A 429     -10.426   4.486  59.180  1.00 46.71           O  
ANISOU 3557  O   THR A 429     6493   6011   5244     90   -204   -479       O  
ATOM   3558  CB  THR A 429     -11.743   2.433  57.556  1.00 47.66           C  
ANISOU 3558  CB  THR A 429     6515   6177   5416     97   -177   -382       C  
ATOM   3559  OG1 THR A 429     -10.696   1.907  56.735  1.00 47.30           O  
ANISOU 3559  OG1 THR A 429     6480   6093   5400     36   -180   -344       O  
ATOM   3560  CG2 THR A 429     -13.037   1.739  57.210  1.00 48.07           C  
ANISOU 3560  CG2 THR A 429     6510   6271   5482    136   -169   -363       C  
ATOM   3561  N   ILE A 430     -10.013   5.522  57.223  1.00 48.16           N  
ANISOU 3561  N   ILE A 430     6773   6044   5481     72   -224   -468       N  
ATOM   3562  CA  ILE A 430      -8.910   6.328  57.729  1.00 48.15           C  
ANISOU 3562  CA  ILE A 430     6815   5996   5482     30   -239   -500       C  
ATOM   3563  C   ILE A 430      -9.437   7.298  58.790  1.00 49.92           C  
ANISOU 3563  C   ILE A 430     7069   6227   5673     84   -257   -569       C  
ATOM   3564  O   ILE A 430     -10.414   8.014  58.560  1.00 52.07           O  
ANISOU 3564  O   ILE A 430     7375   6472   5936    150   -265   -596       O  
ATOM   3565  CB  ILE A 430      -8.204   7.086  56.583  1.00 48.29           C  
ANISOU 3565  CB  ILE A 430     6901   5907   5540     -5   -246   -484       C  
ATOM   3566  CG1 ILE A 430      -7.572   6.100  55.592  1.00 45.47           C  
ANISOU 3566  CG1 ILE A 430     6514   5553   5208    -54   -228   -417       C  
ATOM   3567  CG2 ILE A 430      -7.150   8.050  57.119  1.00 47.88           C  
ANISOU 3567  CG2 ILE A 430     6893   5796   5502    -51   -266   -522       C  
ATOM   3568  CD1 ILE A 430      -7.461   6.655  54.173  1.00 43.94           C  
ANISOU 3568  CD1 ILE A 430     6380   5273   5042    -52   -225   -387       C  
ATOM   3569  N   ALA A 431      -8.786   7.303  59.950  1.00 49.78           N  
ANISOU 3569  N   ALA A 431     7035   6247   5631     63   -266   -601       N  
ATOM   3570  CA  ALA A 431      -9.228   8.094  61.086  1.00 50.75           C  
ANISOU 3570  CA  ALA A 431     7179   6392   5712    120   -286   -672       C  
ATOM   3571  C   ALA A 431      -8.294   9.256  61.403  1.00 52.12           C  
ANISOU 3571  C   ALA A 431     7418   6484   5902     90   -323   -730       C  
ATOM   3572  O   ALA A 431      -8.748  10.306  61.857  1.00 53.48           O  
ANISOU 3572  O   ALA A 431     7640   6623   6056    144   -349   -794       O  
ATOM   3573  CB  ALA A 431      -9.394   7.203  62.307  1.00 51.65           C  
ANISOU 3573  CB  ALA A 431     7223   6626   5775    138   -269   -671       C  
ATOM   3574  N   GLY A 432      -6.994   9.057  61.177  1.00 52.03           N  
ANISOU 3574  N   GLY A 432     7403   6442   5926      4   -328   -708       N  
ATOM   3575  CA  GLY A 432      -5.973  10.068  61.479  1.00 49.20           C  
ANISOU 3575  CA  GLY A 432     7093   6005   5595    -41   -365   -760       C  
ATOM   3576  C   GLY A 432      -4.567   9.491  61.459  1.00 48.61           C  
ANISOU 3576  C   GLY A 432     6980   5939   5549   -133   -365   -731       C  
ATOM   3577  O   GLY A 432      -4.352   8.375  60.972  1.00 48.53           O  
ANISOU 3577  O   GLY A 432     6919   5977   5543   -163   -334   -664       O  
ATOM   3578  N   THR A 433      -3.611  10.253  61.986  1.00 47.42           N  
ANISOU 3578  N   THR A 433     6855   5742   5421   -176   -402   -785       N  
ATOM   3579  CA  THR A 433      -2.211   9.836  62.035  1.00 47.81           C  
ANISOU 3579  CA  THR A 433     6866   5800   5501   -263   -408   -767       C  
ATOM   3580  C   THR A 433      -1.620   9.960  63.444  1.00 50.83           C  
ANISOU 3580  C   THR A 433     7228   6235   5851   -264   -449   -841       C  
ATOM   3581  O   THR A 433      -2.161  10.667  64.296  1.00 53.63           O  
ANISOU 3581  O   THR A 433     7615   6591   6172   -204   -480   -915       O  
ATOM   3582  CB  THR A 433      -1.324  10.637  61.036  1.00 48.49           C  
ANISOU 3582  CB  THR A 433     6994   5764   5667   -341   -412   -749       C  
ATOM   3583  OG1 THR A 433      -1.231  12.005  61.452  1.00 48.06           O  
ANISOU 3583  OG1 THR A 433     7003   5620   5639   -339   -457   -825       O  
ATOM   3584  CG2 THR A 433      -1.882  10.580  59.612  1.00 45.12           C  
ANISOU 3584  CG2 THR A 433     6595   5284   5264   -331   -373   -677       C  
ATOM   3585  N   PHE A 434      -0.513   9.264  63.692  1.00 50.85           N  
ANISOU 3585  N   PHE A 434     7176   6285   5861   -324   -451   -823       N  
ATOM   3586  CA  PHE A 434       0.228   9.443  64.942  1.00 51.45           C  
ANISOU 3586  CA  PHE A 434     7232   6404   5913   -332   -497   -896       C  
ATOM   3587  C   PHE A 434       1.718   9.632  64.674  1.00 52.46           C  
ANISOU 3587  C   PHE A 434     7340   6486   6106   -432   -519   -897       C  
ATOM   3588  O   PHE A 434       2.205   9.348  63.581  1.00 50.55           O  
ANISOU 3588  O   PHE A 434     7087   6205   5916   -492   -487   -827       O  
ATOM   3589  CB  PHE A 434      -0.028   8.287  65.929  1.00 49.44           C  
ANISOU 3589  CB  PHE A 434     6919   6291   5577   -280   -484   -885       C  
ATOM   3590  CG  PHE A 434       0.375   6.929  65.410  1.00 49.03           C  
ANISOU 3590  CG  PHE A 434     6805   6297   5527   -317   -441   -795       C  
ATOM   3591  CD1 PHE A 434      -0.533   6.136  64.712  1.00 48.82           C  
ANISOU 3591  CD1 PHE A 434     6765   6294   5491   -289   -391   -722       C  
ATOM   3592  CD2 PHE A 434       1.656   6.439  65.624  1.00 46.96           C  
ANISOU 3592  CD2 PHE A 434     6497   6068   5278   -377   -455   -789       C  
ATOM   3593  CE1 PHE A 434      -0.172   4.884  64.230  1.00 46.73           C  
ANISOU 3593  CE1 PHE A 434     6449   6077   5231   -319   -358   -644       C  
ATOM   3594  CE2 PHE A 434       2.031   5.189  65.143  1.00 47.41           C  
ANISOU 3594  CE2 PHE A 434     6501   6176   5335   -404   -419   -709       C  
ATOM   3595  CZ  PHE A 434       1.110   4.407  64.445  1.00 48.22           C  
ANISOU 3595  CZ  PHE A 434     6597   6295   5429   -375   -370   -637       C  
ATOM   3596  N   LYS A 435       2.425  10.125  65.685  1.00 56.29           N  
ANISOU 3596  N   LYS A 435     7820   6980   6587   -445   -574   -979       N  
ATOM   3597  CA  LYS A 435       3.870  10.346  65.615  1.00 58.57           C  
ANISOU 3597  CA  LYS A 435     8080   7234   6939   -539   -604   -994       C  
ATOM   3598  C   LYS A 435       4.610   9.009  65.509  1.00 55.99           C  
ANISOU 3598  C   LYS A 435     7675   7004   6596   -572   -574   -928       C  
ATOM   3599  O   LYS A 435       4.382   8.108  66.308  1.00 53.19           O  
ANISOU 3599  O   LYS A 435     7282   6760   6166   -519   -570   -926       O  
ATOM   3600  CB  LYS A 435       4.342  11.142  66.845  1.00 60.92           C  
ANISOU 3600  CB  LYS A 435     8388   7531   7229   -532   -679  -1111       C  
ATOM   3601  CG  LYS A 435       5.634  11.929  66.637  1.00 63.62           C  
ANISOU 3601  CG  LYS A 435     8723   7784   7666   -635   -722  -1147       C  
ATOM   3602  CD  LYS A 435       6.020  12.746  67.876  1.00 69.91           C  
ANISOU 3602  CD  LYS A 435     9532   8574   8456   -621   -807  -1275       C  
ATOM   3603  CE  LYS A 435       6.795  11.912  68.906  1.00 71.01           C  
ANISOU 3603  CE  LYS A 435     9597   8843   8539   -614   -837  -1306       C  
ATOM   3604  NZ  LYS A 435       7.642  12.764  69.803  1.00 71.24           N  
ANISOU 3604  NZ  LYS A 435     9625   8844   8600   -641   -927  -1426       N  
ATOM   3605  N   VAL A 436       5.500   8.906  64.523  1.00 56.14           N  
ANISOU 3605  N   VAL A 436     7670   6976   6684   -656   -553   -871       N  
ATOM   3606  CA  VAL A 436       6.167   7.644  64.174  1.00 54.17           C  
ANISOU 3606  CA  VAL A 436     7353   6806   6425   -685   -518   -798       C  
ATOM   3607  C   VAL A 436       7.513   7.400  64.870  1.00 53.57           C  
ANISOU 3607  C   VAL A 436     7214   6784   6358   -734   -557   -834       C  
ATOM   3608  O   VAL A 436       8.494   8.119  64.645  1.00 53.47           O  
ANISOU 3608  O   VAL A 436     7191   6708   6417   -812   -583   -860       O  
ATOM   3609  CB  VAL A 436       6.341   7.486  62.634  1.00 54.71           C  
ANISOU 3609  CB  VAL A 436     7424   6812   6550   -734   -465   -707       C  
ATOM   3610  CG1 VAL A 436       5.037   7.094  61.995  1.00 51.50           C  
ANISOU 3610  CG1 VAL A 436     7053   6405   6111   -670   -422   -654       C  
ATOM   3611  CG2 VAL A 436       6.892   8.781  61.992  1.00 58.30           C  
ANISOU 3611  CG2 VAL A 436     7916   7139   7094   -806   -478   -722       C  
ATOM   3612  N   ALA A 437       7.538   6.375  65.718  1.00 51.19           N  
ANISOU 3612  N   ALA A 437     6867   6601   5982   -687   -560   -834       N  
ATOM   3613  CA  ALA A 437       8.772   5.900  66.335  1.00 49.81           C  
ANISOU 3613  CA  ALA A 437     6626   6497   5801   -721   -592   -857       C  
ATOM   3614  C   ALA A 437       9.465   4.962  65.348  1.00 47.04           C  
ANISOU 3614  C   ALA A 437     6226   6168   5479   -768   -546   -765       C  
ATOM   3615  O   ALA A 437       8.824   4.442  64.443  1.00 42.67           O  
ANISOU 3615  O   ALA A 437     5688   5601   4924   -753   -492   -689       O  
ATOM   3616  CB  ALA A 437       8.469   5.175  67.646  1.00 48.26           C  
ANISOU 3616  CB  ALA A 437     6410   6421   5507   -639   -612   -888       C  
ATOM   3617  N   PRO A 438      10.780   4.746  65.512  1.00 48.19           N  
ANISOU 3617  N   PRO A 438     6309   6349   5650   -823   -570   -776       N  
ATOM   3618  CA  PRO A 438      11.452   3.836  64.577  1.00 46.61           C  
ANISOU 3618  CA  PRO A 438     6061   6176   5472   -860   -525   -690       C  
ATOM   3619  C   PRO A 438      10.803   2.464  64.614  1.00 45.19           C  
ANISOU 3619  C   PRO A 438     5873   6079   5220   -790   -487   -627       C  
ATOM   3620  O   PRO A 438      10.478   1.965  65.687  1.00 45.16           O  
ANISOU 3620  O   PRO A 438     5861   6153   5144   -729   -506   -654       O  
ATOM   3621  CB  PRO A 438      12.885   3.757  65.121  1.00 46.49           C  
ANISOU 3621  CB  PRO A 438     5974   6214   5477   -908   -568   -730       C  
ATOM   3622  CG  PRO A 438      13.079   5.042  65.863  1.00 50.15           C  
ANISOU 3622  CG  PRO A 438     6457   6624   5974   -934   -632   -832       C  
ATOM   3623  CD  PRO A 438      11.724   5.378  66.455  1.00 48.74           C  
ANISOU 3623  CD  PRO A 438     6349   6432   5738   -855   -639   -869       C  
ATOM   3624  N   LEU A 439      10.600   1.871  63.444  1.00 43.93           N  
ANISOU 3624  N   LEU A 439     5715   5899   5077   -797   -433   -543       N  
ATOM   3625  CA  LEU A 439      10.034   0.529  63.348  1.00 44.29           C  
ANISOU 3625  CA  LEU A 439     5750   6010   5068   -740   -398   -480       C  
ATOM   3626  C   LEU A 439      10.588  -0.396  64.448  1.00 43.39           C  
ANISOU 3626  C   LEU A 439     5586   6006   4895   -707   -422   -494       C  
ATOM   3627  O   LEU A 439       9.835  -1.097  65.132  1.00 42.63           O  
ANISOU 3627  O   LEU A 439     5497   5966   4734   -642   -416   -484       O  
ATOM   3628  CB  LEU A 439      10.307  -0.045  61.950  1.00 42.97           C  
ANISOU 3628  CB  LEU A 439     5571   5819   4936   -766   -352   -399       C  
ATOM   3629  CG  LEU A 439       9.569  -1.333  61.593  1.00 45.42           C  
ANISOU 3629  CG  LEU A 439     5882   6169   5206   -711   -316   -333       C  
ATOM   3630  CD1 LEU A 439       8.114  -1.076  61.186  1.00 44.33           C  
ANISOU 3630  CD1 LEU A 439     5801   5977   5063   -672   -294   -320       C  
ATOM   3631  CD2 LEU A 439      10.320  -2.076  60.500  1.00 47.14           C  
ANISOU 3631  CD2 LEU A 439     6069   6394   5449   -736   -286   -269       C  
ATOM   3632  N   HIS A 440      11.907  -0.330  64.611  1.00 43.61           N  
ANISOU 3632  N   HIS A 440     5562   6062   4946   -755   -450   -517       N  
ATOM   3633  CA AHIS A 440      12.697  -1.103  65.591  0.50 45.49           C  
ANISOU 3633  CA AHIS A 440     5746   6403   5134   -730   -480   -536       C  
ATOM   3634  CA BHIS A 440      12.642  -1.156  65.559  0.50 45.64           C  
ANISOU 3634  CA BHIS A 440     5766   6422   5151   -728   -477   -531       C  
ATOM   3635  C   HIS A 440      12.117  -1.053  67.004  1.00 45.80           C  
ANISOU 3635  C   HIS A 440     5804   6499   5101   -663   -514   -592       C  
ATOM   3636  O   HIS A 440      12.181  -2.030  67.759  1.00 45.22           O  
ANISOU 3636  O   HIS A 440     5707   6515   4960   -609   -517   -577       O  
ATOM   3637  CB AHIS A 440      14.141  -0.574  65.598  0.50 47.16           C  
ANISOU 3637  CB AHIS A 440     5902   6618   5397   -801   -517   -578       C  
ATOM   3638  CB BHIS A 440      14.116  -0.798  65.424  0.50 47.31           C  
ANISOU 3638  CB BHIS A 440     5920   6641   5415   -797   -506   -559       C  
ATOM   3639  CG AHIS A 440      15.048  -1.229  66.597  0.50 49.62           C  
ANISOU 3639  CG AHIS A 440     6156   7035   5662   -777   -557   -608       C  
ATOM   3640  CG BHIS A 440      14.455  -0.296  64.052  0.50 50.07           C  
ANISOU 3640  CG BHIS A 440     6270   6908   5846   -868   -472   -518       C  
ATOM   3641  ND1AHIS A 440      15.249  -0.724  67.865  0.50 53.27           N  
ANISOU 3641  ND1AHIS A 440     6612   7538   6091   -756   -619   -696       N  
ATOM   3642  ND1BHIS A 440      14.605  -1.139  62.971  0.50 50.41           N  
ANISOU 3642  ND1BHIS A 440     6299   6957   5898   -870   -422   -435       N  
ATOM   3643  CD2AHIS A 440      15.849  -2.318  66.498  0.50 51.32           C  
ANISOU 3643  CD2AHIS A 440     6316   7326   5857   -767   -549   -565       C  
ATOM   3644  CD2BHIS A 440      14.579   0.963  63.567  0.50 50.14           C  
ANISOU 3644  CD2BHIS A 440     6300   6824   5928   -932   -478   -545       C  
ATOM   3645  CE1AHIS A 440      16.115  -1.485  68.511  0.50 52.11           C  
ANISOU 3645  CE1AHIS A 440     6408   7488   5902   -732   -646   -705       C  
ATOM   3646  CE1BHIS A 440      14.851  -0.422  61.888  0.50 51.23           C  
ANISOU 3646  CE1BHIS A 440     6411   6983   6071   -930   -396   -411       C  
ATOM   3647  NE2AHIS A 440      16.495  -2.460  67.703  0.50 50.63           N  
ANISOU 3647  NE2AHIS A 440     6191   7323   5723   -739   -603   -624       N  
ATOM   3648  NE2BHIS A 440      14.838   0.856  62.223  0.50 50.29           N  
ANISOU 3648  NE2BHIS A 440     6313   6800   5994   -971   -427   -473       N  
ATOM   3649  N   ASP A 441      11.554   0.100  67.357  1.00 44.19           N  
ANISOU 3649  N   ASP A 441     5644   6240   4907   -663   -539   -657       N  
ATOM   3650  CA  ASP A 441      10.969   0.309  68.667  1.00 45.12           C  
ANISOU 3650  CA  ASP A 441     5783   6407   4953   -594   -571   -718       C  
ATOM   3651  C   ASP A 441       9.601  -0.342  68.832  1.00 44.50           C  
ANISOU 3651  C   ASP A 441     5739   6354   4815   -519   -527   -667       C  
ATOM   3652  O   ASP A 441       9.206  -0.658  69.955  1.00 44.51           O  
ANISOU 3652  O   ASP A 441     5742   6431   4738   -449   -538   -688       O  
ATOM   3653  CB  ASP A 441      10.886   1.800  68.978  1.00 47.06           C  
ANISOU 3653  CB  ASP A 441     6066   6583   5233   -617   -618   -811       C  
ATOM   3654  CG  ASP A 441      12.239   2.409  69.254  1.00 50.63           C  
ANISOU 3654  CG  ASP A 441     6475   7030   5732   -679   -678   -880       C  
ATOM   3655  OD1 ASP A 441      13.121   1.697  69.775  1.00 50.68           O  
ANISOU 3655  OD1 ASP A 441     6425   7125   5708   -672   -700   -883       O  
ATOM   3656  OD2 ASP A 441      12.420   3.606  68.958  1.00 57.53           O  
ANISOU 3656  OD2 ASP A 441     7372   7812   6677   -736   -705   -931       O  
ATOM   3657  N   TYR A 442       8.885  -0.532  67.723  1.00 42.89           N  
ANISOU 3657  N   TYR A 442     5559   6090   4647   -532   -476   -601       N  
ATOM   3658  CA  TYR A 442       7.612  -1.258  67.742  1.00 42.77           C  
ANISOU 3658  CA  TYR A 442     5564   6098   4589   -471   -431   -546       C  
ATOM   3659  C   TYR A 442       7.863  -2.756  67.757  1.00 43.76           C  
ANISOU 3659  C   TYR A 442     5649   6294   4682   -450   -404   -471       C  
ATOM   3660  O   TYR A 442       7.146  -3.503  68.424  1.00 44.23           O  
ANISOU 3660  O   TYR A 442     5709   6413   4684   -389   -383   -441       O  
ATOM   3661  CB  TYR A 442       6.737  -0.882  66.544  1.00 40.66           C  
ANISOU 3661  CB  TYR A 442     5336   5739   4374   -489   -395   -510       C  
ATOM   3662  CG  TYR A 442       6.284   0.557  66.566  1.00 45.36           C  
ANISOU 3662  CG  TYR A 442     5981   6261   4994   -495   -418   -578       C  
ATOM   3663  CD1 TYR A 442       5.378   1.009  67.527  1.00 46.85           C  
ANISOU 3663  CD1 TYR A 442     6198   6473   5129   -431   -431   -626       C  
ATOM   3664  CD2 TYR A 442       6.768   1.474  65.644  1.00 43.35           C  
ANISOU 3664  CD2 TYR A 442     5744   5911   4814   -561   -426   -591       C  
ATOM   3665  CE1 TYR A 442       4.960   2.324  67.554  1.00 44.94           C  
ANISOU 3665  CE1 TYR A 442     6006   6161   4910   -430   -456   -692       C  
ATOM   3666  CE2 TYR A 442       6.354   2.799  65.670  1.00 43.30           C  
ANISOU 3666  CE2 TYR A 442     5790   5829   4834   -566   -449   -651       C  
ATOM   3667  CZ  TYR A 442       5.450   3.214  66.626  1.00 43.97           C  
ANISOU 3667  CZ  TYR A 442     5905   5936   4866   -498   -467   -704       C  
ATOM   3668  OH  TYR A 442       5.041   4.532  66.669  1.00 46.66           O  
ANISOU 3668  OH  TYR A 442     6301   6198   5231   -496   -494   -769       O  
ATOM   3669  N   ILE A 443       8.883  -3.181  67.011  1.00 43.38           N  
ANISOU 3669  N   ILE A 443     5568   6238   4676   -500   -402   -441       N  
ATOM   3670  CA  ILE A 443       9.314  -4.575  66.977  1.00 42.97           C  
ANISOU 3670  CA  ILE A 443     5478   6248   4599   -482   -383   -376       C  
ATOM   3671  C   ILE A 443       9.692  -5.053  68.380  1.00 43.97           C  
ANISOU 3671  C   ILE A 443     5581   6475   4650   -431   -410   -400       C  
ATOM   3672  O   ILE A 443       9.349  -6.165  68.774  1.00 43.46           O  
ANISOU 3672  O   ILE A 443     5509   6466   4540   -381   -386   -345       O  
ATOM   3673  CB  ILE A 443      10.478  -4.776  65.976  1.00 42.45           C  
ANISOU 3673  CB  ILE A 443     5380   6162   4589   -542   -382   -353       C  
ATOM   3674  CG1 ILE A 443       9.953  -4.641  64.537  1.00 42.54           C  
ANISOU 3674  CG1 ILE A 443     5418   6088   4658   -572   -344   -307       C  
ATOM   3675  CG2 ILE A 443      11.153  -6.137  66.181  1.00 39.19           C  
ANISOU 3675  CG2 ILE A 443     4925   5825   4142   -516   -378   -305       C  
ATOM   3676  CD1 ILE A 443      11.019  -4.300  63.486  1.00 39.03           C  
ANISOU 3676  CD1 ILE A 443     4951   5604   4274   -638   -342   -299       C  
ATOM   3677  N   ASN A 444      10.370  -4.191  69.132  1.00 46.23           N  
ANISOU 3677  N   ASN A 444     5858   6781   4925   -440   -462   -482       N  
ATOM   3678  CA  ASN A 444      10.810  -4.513  70.488  1.00 47.90           C  
ANISOU 3678  CA  ASN A 444     6048   7091   5060   -386   -497   -517       C  
ATOM   3679  C   ASN A 444       9.804  -4.150  71.577  1.00 47.78           C  
ANISOU 3679  C   ASN A 444     6069   7111   4977   -315   -501   -552       C  
ATOM   3680  O   ASN A 444      10.076  -4.345  72.761  1.00 49.48           O  
ANISOU 3680  O   ASN A 444     6272   7411   5116   -258   -530   -584       O  
ATOM   3681  CB  ASN A 444      12.167  -3.873  70.770  1.00 48.40           C  
ANISOU 3681  CB  ASN A 444     6074   7171   5146   -428   -558   -593       C  
ATOM   3682  CG  ASN A 444      13.277  -4.544  70.011  1.00 50.81           C  
ANISOU 3682  CG  ASN A 444     6329   7485   5491   -474   -552   -551       C  
ATOM   3683  OD1 ASN A 444      13.387  -5.769  70.012  1.00 53.65           O  
ANISOU 3683  OD1 ASN A 444     6670   7897   5816   -438   -527   -485       O  
ATOM   3684  ND2 ASN A 444      14.098  -3.752  69.338  1.00 53.92           N  
ANISOU 3684  ND2 ASN A 444     6701   7826   5961   -552   -572   -585       N  
ATOM   3685  N   ALA A 445       8.646  -3.637  71.161  1.00 46.14           N  
ANISOU 3685  N   ALA A 445     5903   6840   4790   -313   -472   -545       N  
ATOM   3686  CA  ALA A 445       7.553  -3.288  72.068  1.00 45.47           C  
ANISOU 3686  CA  ALA A 445     5851   6785   4642   -242   -466   -571       C  
ATOM   3687  C   ALA A 445       7.956  -2.245  73.109  1.00 45.92           C  
ANISOU 3687  C   ALA A 445     5918   6869   4661   -218   -530   -681       C  
ATOM   3688  O   ALA A 445       7.419  -2.238  74.223  1.00 44.39           O  
ANISOU 3688  O   ALA A 445     5737   6744   4383   -139   -536   -705       O  
ATOM   3689  CB  ALA A 445       6.992  -4.544  72.748  1.00 45.11           C  
ANISOU 3689  CB  ALA A 445     5793   6825   4521   -171   -425   -497       C  
ATOM   3690  N   VAL A 446       8.889  -1.363  72.743  1.00 45.88           N  
ANISOU 3690  N   VAL A 446     5905   6808   4718   -286   -579   -746       N  
ATOM   3691  CA  VAL A 446       9.335  -0.300  73.658  1.00 48.82           C  
ANISOU 3691  CA  VAL A 446     6288   7192   5071   -272   -651   -862       C  
ATOM   3692  C   VAL A 446       8.715   1.062  73.360  1.00 49.78           C  
ANISOU 3692  C   VAL A 446     6460   7216   5239   -292   -668   -925       C  
ATOM   3693  O   VAL A 446       8.631   1.912  74.247  1.00 49.76           O  
ANISOU 3693  O   VAL A 446     6481   7224   5202   -253   -719  -1019       O  
ATOM   3694  CB  VAL A 446      10.881  -0.194  73.769  1.00 48.69           C  
ANISOU 3694  CB  VAL A 446     6220   7193   5085   -326   -709   -911       C  
ATOM   3695  CG1 VAL A 446      11.445  -1.460  74.398  1.00 50.25           C  
ANISOU 3695  CG1 VAL A 446     6375   7506   5212   -278   -705   -868       C  
ATOM   3696  CG2 VAL A 446      11.527   0.080  72.413  1.00 48.83           C  
ANISOU 3696  CG2 VAL A 446     6219   7117   5215   -432   -697   -884       C  
ATOM   3697  N   ALA A 447       8.262   1.258  72.123  1.00 50.91           N  
ANISOU 3697  N   ALA A 447     6624   7264   5456   -345   -626   -875       N  
ATOM   3698  CA  ALA A 447       7.632   2.518  71.727  1.00 51.80           C  
ANISOU 3698  CA  ALA A 447     6790   7276   5616   -362   -636   -924       C  
ATOM   3699  C   ALA A 447       6.277   2.680  72.419  1.00 52.34           C  
ANISOU 3699  C   ALA A 447     6900   7376   5612   -268   -620   -938       C  
ATOM   3700  O   ALA A 447       5.660   1.690  72.818  1.00 52.32           O  
ANISOU 3700  O   ALA A 447     6883   7455   5542   -207   -577   -877       O  
ATOM   3701  CB  ALA A 447       7.474   2.571  70.225  1.00 50.81           C  
ANISOU 3701  CB  ALA A 447     6675   7053   5576   -430   -592   -856       C  
ATOM   3702  N   GLU A 448       5.815   3.920  72.567  1.00 51.73           N  
ANISOU 3702  N   GLU A 448     6872   7233   5548   -256   -652  -1015       N  
ATOM   3703  CA  GLU A 448       4.509   4.155  73.180  1.00 53.32           C  
ANISOU 3703  CA  GLU A 448     7113   7465   5681   -163   -635  -1033       C  
ATOM   3704  C   GLU A 448       3.378   3.576  72.343  1.00 52.07           C  
ANISOU 3704  C   GLU A 448     6961   7290   5534   -151   -560   -936       C  
ATOM   3705  O   GLU A 448       3.471   3.513  71.108  1.00 50.62           O  
ANISOU 3705  O   GLU A 448     6778   7028   5427   -219   -533   -883       O  
ATOM   3706  CB  GLU A 448       4.271   5.643  73.456  1.00 57.08           C  
ANISOU 3706  CB  GLU A 448     7645   7867   6174   -149   -690  -1141       C  
ATOM   3707  CG  GLU A 448       4.258   6.547  72.233  1.00 65.55           C  
ANISOU 3707  CG  GLU A 448     8755   8797   7355   -225   -690  -1141       C  
ATOM   3708  CD  GLU A 448       4.092   8.019  72.593  1.00 74.27           C  
ANISOU 3708  CD  GLU A 448     9920   9823   8478   -209   -751  -1253       C  
ATOM   3709  OE1 GLU A 448       3.072   8.371  73.240  1.00 75.75           O  
ANISOU 3709  OE1 GLU A 448    10144  10039   8599   -117   -753  -1292       O  
ATOM   3710  OE2 GLU A 448       4.982   8.821  72.219  1.00 76.42           O  
ANISOU 3710  OE2 GLU A 448    10201  10003   8834   -289   -797  -1300       O  
ATOM   3711  N   ARG A 449       2.319   3.139  73.022  1.00 51.54           N  
ANISOU 3711  N   ARG A 449     6895   7300   5387    -64   -526   -914       N  
ATOM   3712  CA  ARG A 449       1.127   2.628  72.346  1.00 50.08           C  
ANISOU 3712  CA  ARG A 449     6711   7105   5211    -46   -459   -831       C  
ATOM   3713  C   ARG A 449       0.510   3.750  71.508  1.00 49.13           C  
ANISOU 3713  C   ARG A 449     6642   6873   5151    -63   -465   -864       C  
ATOM   3714  O   ARG A 449       0.077   4.768  72.053  1.00 51.95           O  
ANISOU 3714  O   ARG A 449     7041   7214   5483    -14   -497   -944       O  
ATOM   3715  CB  ARG A 449       0.129   2.059  73.360  1.00 50.06           C  
ANISOU 3715  CB  ARG A 449     6696   7212   5113     53   -422   -807       C  
ATOM   3716  CG  ARG A 449      -0.957   1.189  72.747  1.00 48.51           C  
ANISOU 3716  CG  ARG A 449     6478   7025   4928     62   -350   -707       C  
ATOM   3717  CD  ARG A 449      -1.545   0.244  73.771  1.00 46.70           C  
ANISOU 3717  CD  ARG A 449     6214   6917   4612    138   -308   -656       C  
ATOM   3718  NE  ARG A 449      -2.642  -0.549  73.219  1.00 48.36           N  
ANISOU 3718  NE  ARG A 449     6399   7132   4842    144   -241   -564       N  
ATOM   3719  CZ  ARG A 449      -3.938  -0.344  73.463  1.00 47.71           C  
ANISOU 3719  CZ  ARG A 449     6318   7078   4731    206   -206   -557       C  
ATOM   3720  NH1 ARG A 449      -4.333   0.642  74.261  1.00 46.00           N  
ANISOU 3720  NH1 ARG A 449     6133   6888   4456    277   -230   -637       N  
ATOM   3721  NH2 ARG A 449      -4.848  -1.137  72.910  1.00 45.46           N  
ANISOU 3721  NH2 ARG A 449     6001   6796   4477    200   -150   -473       N  
ATOM   3722  N   PRO A 450       0.514   3.584  70.175  1.00 48.28           N  
ANISOU 3722  N   PRO A 450     6536   6688   5121   -128   -437   -804       N  
ATOM   3723  CA  PRO A 450       0.074   4.603  69.217  1.00 47.46           C  
ANISOU 3723  CA  PRO A 450     6482   6470   5082   -151   -442   -824       C  
ATOM   3724  C   PRO A 450      -1.287   5.218  69.538  1.00 48.49           C  
ANISOU 3724  C   PRO A 450     6649   6601   5173    -69   -433   -855       C  
ATOM   3725  O   PRO A 450      -1.407   6.449  69.605  1.00 48.70           O  
ANISOU 3725  O   PRO A 450     6729   6559   5215    -57   -471   -931       O  
ATOM   3726  CB  PRO A 450       0.007   3.826  67.906  1.00 46.20           C  
ANISOU 3726  CB  PRO A 450     6302   6274   4977   -202   -395   -729       C  
ATOM   3727  CG  PRO A 450       1.066   2.795  68.052  1.00 43.93           C  
ANISOU 3727  CG  PRO A 450     5962   6044   4685   -242   -392   -689       C  
ATOM   3728  CD  PRO A 450       1.018   2.377  69.487  1.00 47.55           C  
ANISOU 3728  CD  PRO A 450     6397   6612   5057   -179   -402   -714       C  
ATOM   3729  N   SER A 451      -2.289   4.364  69.737  1.00 48.42           N  
ANISOU 3729  N   SER A 451     6611   6668   5119    -14   -383   -798       N  
ATOM   3730  CA  SER A 451      -3.655   4.801  70.027  1.00 49.30           C  
ANISOU 3730  CA  SER A 451     6743   6797   5191     68   -365   -816       C  
ATOM   3731  C   SER A 451      -4.367   3.833  70.962  1.00 49.58           C  
ANISOU 3731  C   SER A 451     6731   6960   5148    138   -322   -774       C  
ATOM   3732  O   SER A 451      -4.140   2.623  70.920  1.00 47.75           O  
ANISOU 3732  O   SER A 451     6449   6780   4913    113   -288   -697       O  
ATOM   3733  CB  SER A 451      -4.461   4.958  68.728  1.00 49.04           C  
ANISOU 3733  CB  SER A 451     6728   6686   5219     53   -337   -774       C  
ATOM   3734  OG  SER A 451      -5.827   5.259  68.982  1.00 47.74           O  
ANISOU 3734  OG  SER A 451     6573   6550   5017    135   -316   -786       O  
ATOM   3735  N   ASP A 452      -5.232   4.386  71.803  1.00 51.74           N  
ANISOU 3735  N   ASP A 452     7021   7282   5357    227   -323   -822       N  
ATOM   3736  CA  ASP A 452      -6.106   3.600  72.663  1.00 53.99           C  
ANISOU 3736  CA  ASP A 452     7261   7687   5566    303   -273   -777       C  
ATOM   3737  C   ASP A 452      -7.514   3.585  72.052  1.00 53.28           C  
ANISOU 3737  C   ASP A 452     7162   7587   5496    335   -228   -738       C  
ATOM   3738  O   ASP A 452      -8.432   2.953  72.581  1.00 54.09           O  
ANISOU 3738  O   ASP A 452     7220   7780   5551    392   -178   -690       O  
ATOM   3739  CB  ASP A 452      -6.109   4.194  74.079  1.00 56.12           C  
ANISOU 3739  CB  ASP A 452     7550   8033   5740    391   -303   -858       C  
ATOM   3740  CG  ASP A 452      -6.894   3.354  75.075  1.00 61.92           C  
ANISOU 3740  CG  ASP A 452     8237   8904   6385    473   -246   -805       C  
ATOM   3741  OD1 ASP A 452      -7.868   3.885  75.649  1.00 65.73           O  
ANISOU 3741  OD1 ASP A 452     8731   9434   6811    563   -234   -839       O  
ATOM   3742  OD2 ASP A 452      -6.547   2.170  75.287  1.00 64.16           O  
ANISOU 3742  OD2 ASP A 452     8472   9249   6656    450   -212   -726       O  
ATOM   3743  N   VAL A 453      -7.660   4.262  70.912  1.00 50.87           N  
ANISOU 3743  N   VAL A 453     6894   7172   5263    297   -245   -753       N  
ATOM   3744  CA  VAL A 453      -8.968   4.499  70.295  1.00 50.12           C  
ANISOU 3744  CA  VAL A 453     6800   7057   5187    336   -217   -737       C  
ATOM   3745  C   VAL A 453      -9.097   3.862  68.914  1.00 49.05           C  
ANISOU 3745  C   VAL A 453     6644   6860   5133    268   -194   -663       C  
ATOM   3746  O   VAL A 453     -10.152   3.325  68.584  1.00 46.66           O  
ANISOU 3746  O   VAL A 453     6302   6589   4839    292   -153   -612       O  
ATOM   3747  CB  VAL A 453      -9.272   6.020  70.178  1.00 49.78           C  
ANISOU 3747  CB  VAL A 453     6830   6938   5147    377   -261   -830       C  
ATOM   3748  CG1 VAL A 453     -10.566   6.262  69.409  1.00 48.89           C  
ANISOU 3748  CG1 VAL A 453     6718   6799   5059    416   -236   -811       C  
ATOM   3749  CG2 VAL A 453      -9.348   6.658  71.557  1.00 51.60           C  
ANISOU 3749  CG2 VAL A 453     7080   7234   5290    463   -286   -910       C  
ATOM   3750  N   TYR A 454      -8.020   3.928  68.124  1.00 48.38           N  
ANISOU 3750  N   TYR A 454     6583   6692   5106    187   -220   -659       N  
ATOM   3751  CA  TYR A 454      -8.035   3.488  66.734  1.00 46.29           C  
ANISOU 3751  CA  TYR A 454     6312   6362   4915    128   -206   -601       C  
ATOM   3752  C   TYR A 454      -7.109   2.309  66.422  1.00 46.76           C  
ANISOU 3752  C   TYR A 454     6330   6434   5001     57   -194   -535       C  
ATOM   3753  O   TYR A 454      -6.166   2.022  67.162  1.00 46.13           O  
ANISOU 3753  O   TYR A 454     6239   6395   4894     38   -206   -543       O  
ATOM   3754  CB  TYR A 454      -7.687   4.658  65.818  1.00 46.78           C  
ANISOU 3754  CB  TYR A 454     6444   6304   5028    100   -243   -646       C  
ATOM   3755  CG  TYR A 454      -8.555   5.883  66.008  1.00 49.32           C  
ANISOU 3755  CG  TYR A 454     6816   6594   5330    171   -261   -713       C  
ATOM   3756  CD1 TYR A 454      -9.904   5.884  65.623  1.00 48.88           C  
ANISOU 3756  CD1 TYR A 454     6749   6551   5271    229   -236   -696       C  
ATOM   3757  CD2 TYR A 454      -8.027   7.046  66.562  1.00 49.94           C  
ANISOU 3757  CD2 TYR A 454     6952   6628   5395    183   -307   -796       C  
ATOM   3758  CE1 TYR A 454     -10.701   7.016  65.794  1.00 49.29           C  
ANISOU 3758  CE1 TYR A 454     6848   6577   5302    302   -254   -759       C  
ATOM   3759  CE2 TYR A 454      -8.814   8.182  66.736  1.00 54.00           C  
ANISOU 3759  CE2 TYR A 454     7518   7108   5891    253   -328   -862       C  
ATOM   3760  CZ  TYR A 454     -10.146   8.163  66.347  1.00 52.24           C  
ANISOU 3760  CZ  TYR A 454     7286   6903   5661    315   -300   -842       C  
ATOM   3761  OH  TYR A 454     -10.910   9.295  66.526  1.00 51.07           O  
ANISOU 3761  OH  TYR A 454     7190   6722   5491    392   -321   -908       O  
ATOM   3762  N   SER A 455      -7.393   1.645  65.303  1.00 46.34           N  
ANISOU 3762  N   SER A 455     6258   6349   5001     25   -173   -475       N  
ATOM   3763  CA  SER A 455      -6.601   0.519  64.815  1.00 45.70           C  
ANISOU 3763  CA  SER A 455     6143   6270   4951    -37   -162   -412       C  
ATOM   3764  C   SER A 455      -5.387   1.043  64.054  1.00 44.74           C  
ANISOU 3764  C   SER A 455     6061   6066   4871   -101   -192   -430       C  
ATOM   3765  O   SER A 455      -5.524   1.877  63.157  1.00 43.32           O  
ANISOU 3765  O   SER A 455     5926   5805   4728   -109   -205   -450       O  
ATOM   3766  CB  SER A 455      -7.464  -0.380  63.924  1.00 45.74           C  
ANISOU 3766  CB  SER A 455     6113   6272   4996    -39   -132   -349       C  
ATOM   3767  OG  SER A 455      -6.735  -1.496  63.452  1.00 44.60           O  
ANISOU 3767  OG  SER A 455     5939   6128   4880    -92   -124   -292       O  
ATOM   3768  N   CYS A 456      -4.201   0.552  64.409  1.00 44.18           N  
ANISOU 3768  N   CYS A 456     5971   6020   4795   -144   -201   -420       N  
ATOM   3769  CA  CYS A 456      -2.965   1.212  63.992  1.00 44.36           C  
ANISOU 3769  CA  CYS A 456     6026   5980   4851   -201   -232   -449       C  
ATOM   3770  C   CYS A 456      -1.985   0.377  63.178  1.00 44.66           C  
ANISOU 3770  C   CYS A 456     6038   6003   4926   -263   -225   -395       C  
ATOM   3771  O   CYS A 456      -1.958  -0.855  63.273  1.00 45.08           O  
ANISOU 3771  O   CYS A 456     6047   6111   4970   -264   -204   -342       O  
ATOM   3772  CB  CYS A 456      -2.260   1.813  65.206  1.00 43.97           C  
ANISOU 3772  CB  CYS A 456     5984   5962   4762   -195   -266   -515       C  
ATOM   3773  SG  CYS A 456      -3.158   3.205  65.898  1.00 48.00           S  
ANISOU 3773  SG  CYS A 456     6545   6453   5239   -128   -289   -600       S  
ATOM   3774  N   SER A 457      -1.190   1.084  62.374  1.00 42.73           N  
ANISOU 3774  N   SER A 457     5825   5682   4727   -312   -241   -408       N  
ATOM   3775  CA  SER A 457      -0.091   0.505  61.609  1.00 41.81           C  
ANISOU 3775  CA  SER A 457     5689   5552   4646   -371   -237   -366       C  
ATOM   3776  C   SER A 457       1.165   1.360  61.813  1.00 41.24           C  
ANISOU 3776  C   SER A 457     5630   5447   4594   -423   -267   -410       C  
ATOM   3777  O   SER A 457       1.078   2.592  61.810  1.00 44.13           O  
ANISOU 3777  O   SER A 457     6041   5749   4978   -427   -287   -460       O  
ATOM   3778  CB  SER A 457      -0.452   0.429  60.121  1.00 40.89           C  
ANISOU 3778  CB  SER A 457     5593   5372   4572   -380   -217   -322       C  
ATOM   3779  OG  SER A 457       0.665   0.025  59.350  1.00 40.18           O  
ANISOU 3779  OG  SER A 457     5489   5267   4512   -431   -212   -286       O  
ATOM   3780  N   PRO A 458       2.336   0.713  61.986  1.00 38.91           N  
ANISOU 3780  N   PRO A 458     5293   5191   4300   -463   -272   -393       N  
ATOM   3781  CA  PRO A 458       3.604   1.405  62.291  1.00 39.28           C  
ANISOU 3781  CA  PRO A 458     5336   5221   4369   -517   -304   -436       C  
ATOM   3782  C   PRO A 458       4.082   2.440  61.256  1.00 39.41           C  
ANISOU 3782  C   PRO A 458     5388   5136   4451   -571   -305   -439       C  
ATOM   3783  O   PRO A 458       5.148   3.035  61.435  1.00 41.12           O  
ANISOU 3783  O   PRO A 458     5595   5330   4698   -624   -330   -472       O  
ATOM   3784  CB  PRO A 458       4.617   0.255  62.400  1.00 38.74           C  
ANISOU 3784  CB  PRO A 458     5209   5220   4290   -541   -299   -398       C  
ATOM   3785  CG  PRO A 458       3.959  -0.908  61.701  1.00 37.95           C  
ANISOU 3785  CG  PRO A 458     5096   5139   4183   -514   -261   -326       C  
ATOM   3786  CD  PRO A 458       2.508  -0.749  61.975  1.00 36.79           C  
ANISOU 3786  CD  PRO A 458     4976   4991   4012   -456   -251   -335       C  
ATOM   3787  N   ASN A 459       3.313   2.662  60.195  1.00 38.18           N  
ANISOU 3787  N   ASN A 459     5270   4920   4317   -557   -280   -405       N  
ATOM   3788  CA  ASN A 459       3.656   3.712  59.243  1.00 40.81           C  
ANISOU 3788  CA  ASN A 459     5645   5155   4707   -599   -277   -403       C  
ATOM   3789  C   ASN A 459       3.072   5.057  59.677  1.00 42.34           C  
ANISOU 3789  C   ASN A 459     5897   5282   4909   -581   -304   -468       C  
ATOM   3790  O   ASN A 459       3.338   6.089  59.049  1.00 42.27           O  
ANISOU 3790  O   ASN A 459     5931   5181   4950   -616   -306   -473       O  
ATOM   3791  CB  ASN A 459       3.222   3.348  57.815  1.00 39.72           C  
ANISOU 3791  CB  ASN A 459     5525   4982   4586   -588   -239   -334       C  
ATOM   3792  CG  ASN A 459       1.711   3.439  57.610  1.00 43.11           C  
ANISOU 3792  CG  ASN A 459     5992   5396   4993   -519   -231   -335       C  
ATOM   3793  OD1 ASN A 459       0.926   3.151  58.515  1.00 48.48           O  
ANISOU 3793  OD1 ASN A 459     6660   6127   5632   -472   -240   -363       O  
ATOM   3794  ND2 ASN A 459       1.301   3.826  56.410  1.00 45.33           N  
ANISOU 3794  ND2 ASN A 459     6314   5610   5298   -509   -212   -303       N  
ATOM   3795  N   GLY A 460       2.286   5.031  60.757  1.00 42.48           N  
ANISOU 3795  N   GLY A 460     5916   5348   4876   -524   -322   -515       N  
ATOM   3796  CA  GLY A 460       1.698   6.239  61.346  1.00 43.08           C  
ANISOU 3796  CA  GLY A 460     6045   5375   4948   -492   -352   -587       C  
ATOM   3797  C   GLY A 460       0.206   6.420  61.120  1.00 44.34           C  
ANISOU 3797  C   GLY A 460     6242   5522   5081   -418   -337   -584       C  
ATOM   3798  O   GLY A 460      -0.370   7.424  61.550  1.00 46.53           O  
ANISOU 3798  O   GLY A 460     6568   5758   5352   -381   -361   -643       O  
ATOM   3799  N   MET A 461      -0.422   5.448  60.458  1.00 41.18           N  
ANISOU 3799  N   MET A 461     5820   5158   4669   -392   -301   -520       N  
ATOM   3800  CA  MET A 461      -1.829   5.546  60.073  1.00 41.60           C  
ANISOU 3800  CA  MET A 461     5901   5201   4706   -326   -285   -512       C  
ATOM   3801  C   MET A 461      -2.787   4.949  61.114  1.00 41.84           C  
ANISOU 3801  C   MET A 461     5897   5324   4677   -260   -280   -528       C  
ATOM   3802  O   MET A 461      -2.453   3.970  61.790  1.00 40.46           O  
ANISOU 3802  O   MET A 461     5669   5233   4473   -266   -273   -510       O  
ATOM   3803  CB  MET A 461      -2.043   4.886  58.711  1.00 42.41           C  
ANISOU 3803  CB  MET A 461     5997   5284   4833   -332   -253   -439       C  
ATOM   3804  CG  MET A 461      -1.388   5.628  57.557  1.00 43.27           C  
ANISOU 3804  CG  MET A 461     6151   5297   4994   -377   -249   -417       C  
ATOM   3805  SD  MET A 461      -2.174   7.222  57.235  1.00 49.58           S  
ANISOU 3805  SD  MET A 461     7038   5991   5810   -339   -264   -458       S  
ATOM   3806  CE  MET A 461      -3.773   6.684  56.640  1.00 44.64           C  
ANISOU 3806  CE  MET A 461     6412   5394   5154   -254   -245   -432       C  
ATOM   3807  N   MET A 462      -3.967   5.560  61.246  1.00 41.91           N  
ANISOU 3807  N   MET A 462     5938   5320   4667   -195   -283   -558       N  
ATOM   3808  CA  MET A 462      -4.982   5.113  62.212  1.00 42.39           C  
ANISOU 3808  CA  MET A 462     5966   5469   4670   -126   -273   -572       C  
ATOM   3809  C   MET A 462      -6.305   4.899  61.508  1.00 41.54           C  
ANISOU 3809  C   MET A 462     5857   5361   4565    -76   -249   -541       C  
ATOM   3810  O   MET A 462      -6.691   5.691  60.651  1.00 41.90           O  
ANISOU 3810  O   MET A 462     5953   5328   4638    -62   -255   -550       O  
ATOM   3811  CB  MET A 462      -5.181   6.125  63.347  1.00 43.04           C  
ANISOU 3811  CB  MET A 462     6081   5558   4715    -81   -303   -654       C  
ATOM   3812  CG  MET A 462      -3.900   6.548  64.055  1.00 45.84           C  
ANISOU 3812  CG  MET A 462     6443   5902   5071   -127   -340   -703       C  
ATOM   3813  SD  MET A 462      -4.158   7.274  65.689  1.00 50.18           S  
ANISOU 3813  SD  MET A 462     7010   6504   5553    -58   -377   -799       S  
ATOM   3814  CE  MET A 462      -5.008   8.804  65.303  1.00 47.57           C  
ANISOU 3814  CE  MET A 462     6764   6070   5242     -9   -400   -860       C  
ATOM   3815  N   TYR A 463      -7.000   3.835  61.893  1.00 42.14           N  
ANISOU 3815  N   TYR A 463     5873   5523   4614    -46   -222   -506       N  
ATOM   3816  CA  TYR A 463      -8.259   3.441  61.269  1.00 41.44           C  
ANISOU 3816  CA  TYR A 463     5765   5446   4533     -4   -201   -475       C  
ATOM   3817  C   TYR A 463      -9.348   3.187  62.304  1.00 44.11           C  
ANISOU 3817  C   TYR A 463     6062   5873   4824     62   -183   -486       C  
ATOM   3818  O   TYR A 463      -9.072   2.737  63.424  1.00 44.71           O  
ANISOU 3818  O   TYR A 463     6105   6024   4859     66   -174   -487       O  
ATOM   3819  CB  TYR A 463      -8.045   2.194  60.417  1.00 39.34           C  
ANISOU 3819  CB  TYR A 463     5457   5190   4302    -46   -182   -404       C  
ATOM   3820  CG  TYR A 463      -6.960   2.370  59.383  1.00 38.64           C  
ANISOU 3820  CG  TYR A 463     5403   5026   4254   -105   -193   -387       C  
ATOM   3821  CD1 TYR A 463      -5.619   2.144  59.700  1.00 36.25           C  
ANISOU 3821  CD1 TYR A 463     5092   4728   3953   -163   -199   -382       C  
ATOM   3822  CD2 TYR A 463      -7.274   2.777  58.089  1.00 37.72           C  
ANISOU 3822  CD2 TYR A 463     5324   4838   4170    -97   -196   -375       C  
ATOM   3823  CE1 TYR A 463      -4.619   2.315  58.741  1.00 40.90           C  
ANISOU 3823  CE1 TYR A 463     5705   5254   4580   -216   -204   -361       C  
ATOM   3824  CE2 TYR A 463      -6.287   2.952  57.126  1.00 38.33           C  
ANISOU 3824  CE2 TYR A 463     5432   4851   4279   -147   -199   -352       C  
ATOM   3825  CZ  TYR A 463      -4.966   2.720  57.453  1.00 39.35           C  
ANISOU 3825  CZ  TYR A 463     5548   4988   4414   -208   -201   -344       C  
ATOM   3826  OH  TYR A 463      -3.996   2.895  56.495  1.00 38.96           O  
ANISOU 3826  OH  TYR A 463     5523   4883   4398   -255   -199   -317       O  
ATOM   3827  N   TYR A 464     -10.585   3.483  61.914  1.00 45.64           N  
ANISOU 3827  N   TYR A 464     6258   6064   5021    118   -176   -492       N  
ATOM   3828  CA  TYR A 464     -11.757   3.280  62.759  1.00 47.52           C  
ANISOU 3828  CA  TYR A 464     6451   6387   5218    185   -153   -498       C  
ATOM   3829  C   TYR A 464     -11.978   1.806  63.053  1.00 47.87           C  
ANISOU 3829  C   TYR A 464     6413   6512   5265    166   -117   -430       C  
ATOM   3830  O   TYR A 464     -11.853   0.960  62.159  1.00 47.11           O  
ANISOU 3830  O   TYR A 464     6291   6393   5215    122   -111   -379       O  
ATOM   3831  CB  TYR A 464     -13.010   3.834  62.074  1.00 49.84           C  
ANISOU 3831  CB  TYR A 464     6756   6655   5524    244   -155   -513       C  
ATOM   3832  CG  TYR A 464     -13.010   5.332  61.843  1.00 55.69           C  
ANISOU 3832  CG  TYR A 464     7582   7316   6260    280   -188   -579       C  
ATOM   3833  CD1 TYR A 464     -13.000   5.857  60.550  1.00 56.02           C  
ANISOU 3833  CD1 TYR A 464     7677   7264   6345    271   -206   -576       C  
ATOM   3834  CD2 TYR A 464     -13.036   6.226  62.920  1.00 59.14           C  
ANISOU 3834  CD2 TYR A 464     8052   7771   6648    328   -202   -644       C  
ATOM   3835  CE1 TYR A 464     -13.007   7.231  60.331  1.00 60.75           C  
ANISOU 3835  CE1 TYR A 464     8358   7782   6943    303   -234   -630       C  
ATOM   3836  CE2 TYR A 464     -13.043   7.605  62.713  1.00 62.37           C  
ANISOU 3836  CE2 TYR A 464     8544   8097   7058    361   -237   -706       C  
ATOM   3837  CZ  TYR A 464     -13.028   8.100  61.417  1.00 65.05           C  
ANISOU 3837  CZ  TYR A 464     8935   8337   7446    346   -251   -696       C  
ATOM   3838  OH  TYR A 464     -13.040   9.464  61.211  1.00 68.17           O  
ANISOU 3838  OH  TYR A 464     9416   8642   7845    379   -283   -752       O  
ATOM   3839  N   LYS A 465     -12.318   1.507  64.302  1.00 48.29           N  
ANISOU 3839  N   LYS A 465     6425   6657   5266    202    -93   -429       N  
ATOM   3840  CA  LYS A 465     -12.654   0.147  64.707  1.00 51.16           C  
ANISOU 3840  CA  LYS A 465     6709   7099   5630    191    -53   -359       C  
ATOM   3841  C   LYS A 465     -14.166  -0.102  64.678  1.00 54.70           C  
ANISOU 3841  C   LYS A 465     7101   7595   6085    241    -23   -339       C  
ATOM   3842  O   LYS A 465     -14.609  -1.251  64.605  1.00 55.34           O  
ANISOU 3842  O   LYS A 465     7115   7716   6197    220      7   -275       O  
ATOM   3843  CB  LYS A 465     -12.116  -0.140  66.113  1.00 51.60           C  
ANISOU 3843  CB  LYS A 465     6749   7236   5623    202    -38   -357       C  
ATOM   3844  CG  LYS A 465     -10.596  -0.219  66.221  1.00 51.36           C  
ANISOU 3844  CG  LYS A 465     6749   7176   5590    146    -64   -365       C  
ATOM   3845  CD  LYS A 465     -10.144  -0.350  67.671  1.00 50.63           C  
ANISOU 3845  CD  LYS A 465     6645   7169   5424    174    -56   -375       C  
ATOM   3846  CE  LYS A 465     -10.345  -1.762  68.204  1.00 50.27           C  
ANISOU 3846  CE  LYS A 465     6531   7204   5367    169    -10   -292       C  
ATOM   3847  NZ  LYS A 465      -9.889  -1.880  69.619  1.00 51.79           N  
ANISOU 3847  NZ  LYS A 465     6715   7484   5478    206     -2   -300       N  
ATOM   3848  N   ASP A 466     -14.948   0.977  64.730  1.00 58.30           N  
ANISOU 3848  N   ASP A 466     7586   8047   6519    307    -33   -395       N  
ATOM   3849  CA  ASP A 466     -16.397   0.893  64.947  1.00 61.67           C  
ANISOU 3849  CA  ASP A 466     7955   8538   6938    369     -3   -385       C  
ATOM   3850  C   ASP A 466     -17.245   0.612  63.696  1.00 62.81           C  
ANISOU 3850  C   ASP A 466     8072   8643   7150    362     -9   -365       C  
ATOM   3851  O   ASP A 466     -18.470   0.475  63.799  1.00 63.89           O  
ANISOU 3851  O   ASP A 466     8150   8835   7291    408     15   -356       O  
ATOM   3852  CB  ASP A 466     -16.908   2.139  65.695  1.00 64.66           C  
ANISOU 3852  CB  ASP A 466     8372   8945   7253    458    -10   -457       C  
ATOM   3853  CG  ASP A 466     -16.708   3.433  64.909  1.00 67.93           C  
ANISOU 3853  CG  ASP A 466     8875   9256   7679    474    -60   -525       C  
ATOM   3854  OD1 ASP A 466     -15.915   4.290  65.352  1.00 72.52           O  
ANISOU 3854  OD1 ASP A 466     9525   9802   8229    479    -89   -580       O  
ATOM   3855  OD2 ASP A 466     -17.347   3.602  63.854  1.00 69.39           O  
ANISOU 3855  OD2 ASP A 466     9063   9393   7908    482    -71   -524       O  
ATOM   3856  N   ARG A 467     -16.607   0.558  62.526  1.00 62.47           N  
ANISOU 3856  N   ARG A 467     8068   8510   7156    310    -40   -361       N  
ATOM   3857  CA  ARG A 467     -17.260   0.066  61.298  1.00 64.24           C  
ANISOU 3857  CA  ARG A 467     8263   8701   7445    297    -50   -337       C  
ATOM   3858  C   ARG A 467     -16.312  -0.607  60.304  1.00 62.19           C  
ANISOU 3858  C   ARG A 467     8022   8374   7233    224    -70   -304       C  
ATOM   3859  O   ARG A 467     -15.086  -0.483  60.395  1.00 61.17           O  
ANISOU 3859  O   ARG A 467     7940   8210   7092    183    -80   -307       O  
ATOM   3860  CB  ARG A 467     -18.151   1.111  60.594  1.00 66.79           C  
ANISOU 3860  CB  ARG A 467     8619   8987   7770    362    -74   -387       C  
ATOM   3861  CG  ARG A 467     -17.809   2.577  60.808  1.00 72.37           C  
ANISOU 3861  CG  ARG A 467     9418   9648   8433    406    -98   -453       C  
ATOM   3862  CD  ARG A 467     -16.529   3.009  60.109  1.00 73.91           C  
ANISOU 3862  CD  ARG A 467     9695   9744   8643    353   -129   -463       C  
ATOM   3863  NE  ARG A 467     -16.587   4.422  59.732  1.00 79.70           N  
ANISOU 3863  NE  ARG A 467    10515  10406   9363    399   -159   -520       N  
ATOM   3864  CZ  ARG A 467     -16.478   5.450  60.576  1.00 81.49           C  
ANISOU 3864  CZ  ARG A 467    10789  10629   9544    440   -168   -575       C  
ATOM   3865  NH1 ARG A 467     -16.301   5.248  61.877  1.00 83.98           N  
ANISOU 3865  NH1 ARG A 467    11074  11019   9815    447   -150   -584       N  
ATOM   3866  NH2 ARG A 467     -16.550   6.693  60.115  1.00 80.59           N  
ANISOU 3866  NH2 ARG A 467    10757  10436   9428    480   -198   -623       N  
ATOM   3867  N   ASP A 468     -16.898  -1.328  59.360  1.00 60.01           N  
ANISOU 3867  N   ASP A 468     7705   8083   7013    212    -77   -277       N  
ATOM   3868  CA  ASP A 468     -16.110  -2.108  58.429  1.00 57.65           C  
ANISOU 3868  CA  ASP A 468     7415   7732   6758    152    -94   -245       C  
ATOM   3869  C   ASP A 468     -15.927  -1.353  57.134  1.00 52.63           C  
ANISOU 3869  C   ASP A 468     6848   7013   6135    165   -131   -276       C  
ATOM   3870  O   ASP A 468     -16.848  -0.711  56.638  1.00 52.59           O  
ANISOU 3870  O   ASP A 468     6853   6997   6134    220   -146   -307       O  
ATOM   3871  CB  ASP A 468     -16.732  -3.491  58.212  1.00 60.39           C  
ANISOU 3871  CB  ASP A 468     7676   8110   7159    125    -83   -196       C  
ATOM   3872  CG  ASP A 468     -16.609  -4.382  59.450  1.00 66.55           C  
ANISOU 3872  CG  ASP A 468     8397   8961   7929     99    -42   -148       C  
ATOM   3873  OD1 ASP A 468     -17.270  -4.092  60.475  1.00 67.49           O  
ANISOU 3873  OD1 ASP A 468     8483   9148   8012    137    -11   -151       O  
ATOM   3874  OD2 ASP A 468     -15.838  -5.368  59.403  1.00 70.80           O  
ANISOU 3874  OD2 ASP A 468     8923   9488   8488     44    -39   -105       O  
ATOM   3875  N   GLY A 469     -14.708  -1.408  56.619  1.00 53.28           N  
ANISOU 3875  N   GLY A 469     6994   6617   6632    141    559   -111       N  
ATOM   3876  CA  GLY A 469     -14.387  -0.777  55.358  1.00 48.58           C  
ANISOU 3876  CA  GLY A 469     6300   6059   6097    152    408    -90       C  
ATOM   3877  C   GLY A 469     -14.801  -1.686  54.234  1.00 45.70           C  
ANISOU 3877  C   GLY A 469     5815   5720   5829    157    319    -47       C  
ATOM   3878  O   GLY A 469     -14.787  -2.918  54.389  1.00 45.04           O  
ANISOU 3878  O   GLY A 469     5740   5664   5708    143    331    -29       O  
ATOM   3879  N   VAL A 470     -15.162  -1.087  53.101  1.00 42.10           N  
ANISOU 3879  N   VAL A 470     5262   5245   5489    177    221    -30       N  
ATOM   3880  CA  VAL A 470     -15.545  -1.863  51.925  1.00 41.08           C  
ANISOU 3880  CA  VAL A 470     5046   5125   5439    183    105      8       C  
ATOM   3881  C   VAL A 470     -14.419  -2.795  51.444  1.00 39.54           C  
ANISOU 3881  C   VAL A 470     4918   5017   5089    157     17     37       C  
ATOM   3882  O   VAL A 470     -14.687  -3.906  50.992  1.00 40.22           O  
ANISOU 3882  O   VAL A 470     4966   5117   5199    150    -22     60       O  
ATOM   3883  CB  VAL A 470     -16.111  -0.976  50.776  1.00 41.76           C  
ANISOU 3883  CB  VAL A 470     5057   5154   5658    212    -11     23       C  
ATOM   3884  CG1 VAL A 470     -15.023  -0.100  50.137  1.00 40.51           C  
ANISOU 3884  CG1 VAL A 470     4986   5029   5375    208    -97     35       C  
ATOM   3885  CG2 VAL A 470     -16.796  -1.842  49.734  1.00 39.54           C  
ANISOU 3885  CG2 VAL A 470     4695   4847   5480    219   -132     54       C  
ATOM   3886  N   VAL A 471     -13.169  -2.346  51.561  1.00 39.23           N  
ANISOU 3886  N   VAL A 471     4969   5022   4912    142     -8     31       N  
ATOM   3887  CA  VAL A 471     -12.015  -3.179  51.194  1.00 39.27           C  
ANISOU 3887  CA  VAL A 471     5027   5092   4802    117    -71     52       C  
ATOM   3888  C   VAL A 471     -11.839  -4.420  52.103  1.00 38.61           C  
ANISOU 3888  C   VAL A 471     4976   5042   4653    100    -18     52       C  
ATOM   3889  O   VAL A 471     -11.757  -5.536  51.596  1.00 38.83           O  
ANISOU 3889  O   VAL A 471     4983   5097   4672     90    -57     78       O  
ATOM   3890  CB  VAL A 471     -10.708  -2.340  51.039  1.00 40.01           C  
ANISOU 3890  CB  VAL A 471     5184   5201   4817    105   -109     43       C  
ATOM   3891  CG1 VAL A 471      -9.467  -3.221  51.042  1.00 34.88           C  
ANISOU 3891  CG1 VAL A 471     4574   4598   4081     79   -143     52       C  
ATOM   3892  CG2 VAL A 471     -10.773  -1.515  49.762  1.00 36.50           C  
ANISOU 3892  CG2 VAL A 471     4727   4724   4418    118   -173     62       C  
ATOM   3893  N   PRO A 472     -11.808  -4.243  53.437  1.00 39.60           N  
ANISOU 3893  N   PRO A 472     5171   5152   4723     96     70     22       N  
ATOM   3894  CA  PRO A 472     -11.838  -5.447  54.283  1.00 39.87           C  
ANISOU 3894  CA  PRO A 472     5257   5197   4695     84    126     27       C  
ATOM   3895  C   PRO A 472     -13.041  -6.356  54.001  1.00 41.26           C  
ANISOU 3895  C   PRO A 472     5343   5350   4983     90    181     46       C  
ATOM   3896  O   PRO A 472     -12.890  -7.585  53.968  1.00 42.32           O  
ANISOU 3896  O   PRO A 472     5481   5513   5086     77    170     68       O  
ATOM   3897  CB  PRO A 472     -11.925  -4.882  55.699  1.00 37.52           C  
ANISOU 3897  CB  PRO A 472     5077   4852   4326     84    229    -10       C  
ATOM   3898  CG  PRO A 472     -11.274  -3.571  55.609  1.00 39.49           C  
ANISOU 3898  CG  PRO A 472     5351   5098   4555     87    175    -35       C  
ATOM   3899  CD  PRO A 472     -11.557  -3.029  54.235  1.00 40.17           C  
ANISOU 3899  CD  PRO A 472     5312   5193   4758    100    112    -17       C  
ATOM   3900  N   THR A 473     -14.211  -5.758  53.783  1.00 41.80           N  
ANISOU 3900  N   THR A 473     5322   5358   5204    109    233     34       N  
ATOM   3901  CA  THR A 473     -15.429  -6.528  53.550  1.00 43.03           C  
ANISOU 3901  CA  THR A 473     5367   5466   5517    116    281     43       C  
ATOM   3902  C   THR A 473     -15.287  -7.398  52.307  1.00 41.36           C  
ANISOU 3902  C   THR A 473     5093   5295   5326    110    140     78       C  
ATOM   3903  O   THR A 473     -15.493  -8.608  52.374  1.00 41.89           O  
ANISOU 3903  O   THR A 473     5141   5370   5404     97    160     92       O  
ATOM   3904  CB  THR A 473     -16.698  -5.620  53.472  1.00 46.05           C  
ANISOU 3904  CB  THR A 473     5637   5752   6108    141    341     21       C  
ATOM   3905  OG1 THR A 473     -17.006  -5.113  54.776  1.00 51.15           O  
ANISOU 3905  OG1 THR A 473     6351   6340   6744    142    527    -15       O  
ATOM   3906  CG2 THR A 473     -17.920  -6.390  52.957  1.00 47.17           C  
ANISOU 3906  CG2 THR A 473     5625   5830   6467    149    339     29       C  
ATOM   3907  N   GLU A 474     -14.911  -6.792  51.184  1.00 40.14           N  
ANISOU 3907  N   GLU A 474     4928   5157   5167    117      5     91       N  
ATOM   3908  CA  GLU A 474     -14.850  -7.533  49.918  1.00 39.90           C  
ANISOU 3908  CA  GLU A 474     4871   5142   5146    112   -125    120       C  
ATOM   3909  C   GLU A 474     -13.663  -8.484  49.777  1.00 36.51           C  
ANISOU 3909  C   GLU A 474     4521   4786   4567     86   -152    139       C  
ATOM   3910  O   GLU A 474     -13.769  -9.499  49.097  1.00 38.83           O  
ANISOU 3910  O   GLU A 474     4796   5086   4870     77   -208    158       O  
ATOM   3911  CB  GLU A 474     -14.955  -6.600  48.707  1.00 39.98           C  
ANISOU 3911  CB  GLU A 474     4878   5117   5194    130   -253    130       C  
ATOM   3912  CG  GLU A 474     -16.333  -5.940  48.554  1.00 44.15           C  
ANISOU 3912  CG  GLU A 474     5296   5551   5927    160   -276    118       C  
ATOM   3913  CD  GLU A 474     -17.505  -6.922  48.630  1.00 43.96           C  
ANISOU 3913  CD  GLU A 474     5152   5471   6079    162   -267    114       C  
ATOM   3914  OE1 GLU A 474     -18.392  -6.723  49.478  1.00 47.16           O  
ANISOU 3914  OE1 GLU A 474     5464   5815   6639    173   -145     88       O  
ATOM   3915  OE2 GLU A 474     -17.555  -7.885  47.845  1.00 46.54           O  
ANISOU 3915  OE2 GLU A 474     5477   5804   6404    152   -369    132       O  
ATOM   3916  N   ILE A 475     -12.543  -8.170  50.420  1.00 36.04           N  
ANISOU 3916  N   ILE A 475     4542   4769   4384     75   -118    131       N  
ATOM   3917  CA  ILE A 475     -11.376  -9.047  50.358  1.00 34.24           C  
ANISOU 3917  CA  ILE A 475     4367   4591   4050     53   -145    146       C  
ATOM   3918  C   ILE A 475     -11.609 -10.316  51.181  1.00 33.89           C  
ANISOU 3918  C   ILE A 475     4326   4561   3992     43    -85    153       C  
ATOM   3919  O   ILE A 475     -11.119 -11.391  50.834  1.00 32.79           O  
ANISOU 3919  O   ILE A 475     4193   4449   3818     28   -117    172       O  
ATOM   3920  CB  ILE A 475     -10.092  -8.315  50.779  1.00 33.30           C  
ANISOU 3920  CB  ILE A 475     4315   4491   3845     45   -152    132       C  
ATOM   3921  CG1 ILE A 475      -8.908  -8.841  49.984  1.00 31.42           C  
ANISOU 3921  CG1 ILE A 475     4096   4275   3566     26   -206    148       C  
ATOM   3922  CG2 ILE A 475      -9.840  -8.410  52.299  1.00 31.89           C  
ANISOU 3922  CG2 ILE A 475     4199   4316   3603     42    -94    112       C  
ATOM   3923  CD1 ILE A 475      -7.609  -8.098  50.285  1.00 36.72           C  
ANISOU 3923  CD1 ILE A 475     4803   4943   4205     17   -221    130       C  
ATOM   3924  N   THR A 476     -12.392 -10.169  52.249  1.00 36.06           N  
ANISOU 3924  N   THR A 476     4603   4801   4296     51     17    136       N  
ATOM   3925  CA  THR A 476     -12.765 -11.258  53.148  1.00 37.34           C  
ANISOU 3925  CA  THR A 476     4790   4952   4444     43    108    142       C  
ATOM   3926  C   THR A 476     -13.539 -12.358  52.426  1.00 38.16           C  
ANISOU 3926  C   THR A 476     4800   5046   4653     38     94    161       C  
ATOM   3927  O   THR A 476     -13.255 -13.547  52.609  1.00 36.70           O  
ANISOU 3927  O   THR A 476     4639   4882   4424     23    104    180       O  
ATOM   3928  CB  THR A 476     -13.597 -10.705  54.324  1.00 40.41           C  
ANISOU 3928  CB  THR A 476     5214   5277   4861     52    255    115       C  
ATOM   3929  OG1 THR A 476     -12.764  -9.849  55.115  1.00 40.19           O  
ANISOU 3929  OG1 THR A 476     5308   5256   4707     52    255     95       O  
ATOM   3930  CG2 THR A 476     -14.163 -11.828  55.205  1.00 38.18           C  
ANISOU 3930  CG2 THR A 476     4969   4957   4579     43    383    123       C  
ATOM   3931  N   LYS A 477     -14.494 -11.948  51.592  1.00 39.07           N  
ANISOU 3931  N   LYS A 477     4811   5120   4913     51     55    155       N  
ATOM   3932  CA  LYS A 477     -15.330 -12.878  50.836  1.00 39.15           C  
ANISOU 3932  CA  LYS A 477     4725   5100   5049     47     11    165       C  
ATOM   3933  C   LYS A 477     -14.523 -13.718  49.848  1.00 40.16           C  
ANISOU 3933  C   LYS A 477     4887   5279   5092     31   -103    189       C  
ATOM   3934  O   LYS A 477     -14.705 -14.940  49.774  1.00 40.98           O  
ANISOU 3934  O   LYS A 477     4969   5384   5218     17    -96    201       O  
ATOM   3935  CB  LYS A 477     -16.446 -12.134  50.116  1.00 41.12           C  
ANISOU 3935  CB  LYS A 477     4866   5277   5482     68    -51    152       C  
ATOM   3936  CG  LYS A 477     -17.517 -11.554  51.032  1.00 43.20           C  
ANISOU 3936  CG  LYS A 477     5054   5458   5901     83     89    124       C  
ATOM   3937  CD  LYS A 477     -18.388 -10.547  50.275  1.00 47.86           C  
ANISOU 3937  CD  LYS A 477     5540   5973   6672    109     -4    111       C  
ATOM   3938  CE  LYS A 477     -19.427  -9.895  51.188  1.00 54.52           C  
ANISOU 3938  CE  LYS A 477     6295   6719   7700    125    156     80       C  
ATOM   3939  NZ  LYS A 477     -20.177  -8.792  50.505  1.00 56.82           N  
ANISOU 3939  NZ  LYS A 477     6483   6930   8175    155     56     67       N  
ATOM   3940  N   VAL A 478     -13.630 -13.078  49.094  1.00 38.84           N  
ANISOU 3940  N   VAL A 478     4781   5142   4836     31   -189    194       N  
ATOM   3941  CA  VAL A 478     -12.781 -13.820  48.156  1.00 35.90           C  
ANISOU 3941  CA  VAL A 478     4459   4800   4382     14   -263    213       C  
ATOM   3942  C   VAL A 478     -11.771 -14.673  48.926  1.00 36.80           C  
ANISOU 3942  C   VAL A 478     4618   4963   4400     -3   -204    223       C  
ATOM   3943  O   VAL A 478     -11.460 -15.801  48.517  1.00 35.59           O  
ANISOU 3943  O   VAL A 478     4471   4823   4228    -19   -223    237       O  
ATOM   3944  CB  VAL A 478     -12.072 -12.905  47.142  1.00 34.76           C  
ANISOU 3944  CB  VAL A 478     4381   4651   4175     16   -337    216       C  
ATOM   3945  CG1 VAL A 478     -11.241 -13.727  46.169  1.00 33.98           C  
ANISOU 3945  CG1 VAL A 478     4349   4561   4001     -5   -376    231       C  
ATOM   3946  CG2 VAL A 478     -13.086 -12.069  46.378  1.00 33.15           C  
ANISOU 3946  CG2 VAL A 478     4151   4385   4059     37   -421    211       C  
ATOM   3947  N   PHE A 479     -11.283 -14.150  50.054  1.00 37.85           N  
ANISOU 3947  N   PHE A 479     4790   5112   4478      1   -144    214       N  
ATOM   3948  CA  PHE A 479     -10.369 -14.916  50.900  1.00 34.58           C  
ANISOU 3948  CA  PHE A 479     4431   4726   3981    -10   -118    223       C  
ATOM   3949  C   PHE A 479     -10.999 -16.228  51.343  1.00 35.82           C  
ANISOU 3949  C   PHE A 479     4571   4874   4163    -17    -64    238       C  
ATOM   3950  O   PHE A 479     -10.356 -17.284  51.287  1.00 36.14           O  
ANISOU 3950  O   PHE A 479     4630   4935   4168    -29    -82    257       O  
ATOM   3951  CB  PHE A 479      -9.924 -14.128  52.135  1.00 35.10           C  
ANISOU 3951  CB  PHE A 479     4567   4788   3980     -3    -83    207       C  
ATOM   3952  CG  PHE A 479      -9.211 -14.980  53.158  1.00 37.47           C  
ANISOU 3952  CG  PHE A 479     4945   5093   4198    -10    -77    219       C  
ATOM   3953  CD1 PHE A 479      -7.926 -15.468  52.905  1.00 38.65           C  
ANISOU 3953  CD1 PHE A 479     5104   5260   4320    -19   -154    230       C  
ATOM   3954  CD2 PHE A 479      -9.840 -15.334  54.346  1.00 39.50           C  
ANISOU 3954  CD2 PHE A 479     5272   5320   4416     -6     11    220       C  
ATOM   3955  CE1 PHE A 479      -7.272 -16.276  53.833  1.00 42.55           C  
ANISOU 3955  CE1 PHE A 479     5668   5744   4754    -22   -178    244       C  
ATOM   3956  CE2 PHE A 479      -9.190 -16.134  55.293  1.00 43.01           C  
ANISOU 3956  CE2 PHE A 479     5821   5753   4766    -10      0    236       C  
ATOM   3957  CZ  PHE A 479      -7.903 -16.608  55.033  1.00 43.12           C  
ANISOU 3957  CZ  PHE A 479     5836   5789   4760    -16   -112    249       C  
ATOM   3958  N   ASN A 480     -12.246 -16.155  51.806  1.00 37.01           N  
ANISOU 3958  N   ASN A 480     4682   4985   4394     -9     15    229       N  
ATOM   3959  CA  ASN A 480     -12.962 -17.345  52.271  1.00 37.97           C  
ANISOU 3959  CA  ASN A 480     4783   5080   4565    -17     94    241       C  
ATOM   3960  C   ASN A 480     -13.112 -18.380  51.162  1.00 38.65           C  
ANISOU 3960  C   ASN A 480     4801   5174   4711    -30     23    254       C  
ATOM   3961  O   ASN A 480     -12.922 -19.574  51.405  1.00 40.39           O  
ANISOU 3961  O   ASN A 480     5038   5400   4910    -42     50    272       O  
ATOM   3962  CB  ASN A 480     -14.308 -16.983  52.908  1.00 35.96           C  
ANISOU 3962  CB  ASN A 480     4480   4754   4427     -8    218    222       C  
ATOM   3963  CG  ASN A 480     -14.155 -16.408  54.329  1.00 39.91           C  
ANISOU 3963  CG  ASN A 480     5101   5230   4832     -2    337    212       C  
ATOM   3964  OD1 ASN A 480     -13.215 -16.744  55.057  1.00 35.97           O  
ANISOU 3964  OD1 ASN A 480     4730   4755   4182     -7    330    226       O  
ATOM   3965  ND2 ASN A 480     -15.089 -15.545  54.723  1.00 36.46           N  
ANISOU 3965  ND2 ASN A 480     4633   4730   4490     10    438    186       N  
ATOM   3966  N   GLN A 481     -13.402 -17.909  49.948  1.00 38.75           N  
ANISOU 3966  N   GLN A 481     4761   5177   4785    -26    -74    245       N  
ATOM   3967  CA  GLN A 481     -13.442 -18.761  48.760  1.00 40.27           C  
ANISOU 3967  CA  GLN A 481     4930   5366   5006    -39   -164    252       C  
ATOM   3968  C   GLN A 481     -12.091 -19.408  48.499  1.00 39.64           C  
ANISOU 3968  C   GLN A 481     4924   5333   4806    -54   -185    269       C  
ATOM   3969  O   GLN A 481     -12.016 -20.603  48.224  1.00 40.45           O  
ANISOU 3969  O   GLN A 481     5021   5435   4913    -69   -188    280       O  
ATOM   3970  CB  GLN A 481     -13.865 -17.960  47.533  1.00 41.28           C  
ANISOU 3970  CB  GLN A 481     5043   5459   5183    -30   -281    240       C  
ATOM   3971  CG  GLN A 481     -15.326 -17.564  47.540  1.00 50.64           C  
ANISOU 3971  CG  GLN A 481     6122   6573   6546    -15   -296    222       C  
ATOM   3972  CD  GLN A 481     -15.614 -16.368  46.643  1.00 57.75           C  
ANISOU 3972  CD  GLN A 481     7029   7436   7478      3   -413    213       C  
ATOM   3973  OE1 GLN A 481     -15.164 -16.310  45.489  1.00 57.35           O  
ANISOU 3973  OE1 GLN A 481     7060   7380   7348     -1   -528    220       O  
ATOM   3974  NE2 GLN A 481     -16.373 -15.403  47.172  1.00 58.80           N  
ANISOU 3974  NE2 GLN A 481     7091   7528   7723     24   -376    197       N  
ATOM   3975  N   ARG A 482     -11.027 -18.615  48.585  1.00 38.26           N  
ANISOU 3975  N   ARG A 482     4806   5185   4544    -51   -194    268       N  
ATOM   3976  CA  ARG A 482      -9.678 -19.134  48.392  1.00 40.27           C  
ANISOU 3976  CA  ARG A 482     5108   5463   4728    -64   -204    280       C  
ATOM   3977  C   ARG A 482      -9.376 -20.253  49.394  1.00 41.37           C  
ANISOU 3977  C   ARG A 482     5255   5616   4849    -69   -158    298       C  
ATOM   3978  O   ARG A 482      -8.883 -21.317  49.026  1.00 43.66           O  
ANISOU 3978  O   ARG A 482     5546   5907   5136    -82   -166    311       O  
ATOM   3979  CB  ARG A 482      -8.645 -18.005  48.496  1.00 38.00           C  
ANISOU 3979  CB  ARG A 482     4859   5185   4394    -58   -215    271       C  
ATOM   3980  CG  ARG A 482      -7.225 -18.422  48.148  1.00 33.94           C  
ANISOU 3980  CG  ARG A 482     4368   4669   3859    -72   -221    276       C  
ATOM   3981  CD  ARG A 482      -6.460 -18.760  49.403  1.00 37.93           C  
ANISOU 3981  CD  ARG A 482     4879   5185   4349    -69   -219    283       C  
ATOM   3982  NE  ARG A 482      -5.134 -19.289  49.118  1.00 38.42           N  
ANISOU 3982  NE  ARG A 482     4933   5227   4439    -80   -232    287       N  
ATOM   3983  CZ  ARG A 482      -4.075 -19.104  49.898  1.00 39.31           C  
ANISOU 3983  CZ  ARG A 482     5045   5323   4570    -76   -269    283       C  
ATOM   3984  NH1 ARG A 482      -4.185 -18.389  51.015  1.00 39.47           N  
ANISOU 3984  NH1 ARG A 482     5101   5348   4547    -62   -301    275       N  
ATOM   3985  NH2 ARG A 482      -2.901 -19.621  49.556  1.00 33.40           N  
ANISOU 3985  NH2 ARG A 482     4261   4537   3892    -86   -277    284       N  
ATOM   3986  N   LYS A 483      -9.690 -19.990  50.653  1.00 41.43           N  
ANISOU 3986  N   LYS A 483     5284   5621   4836    -58   -107    298       N  
ATOM   3987  CA  LYS A 483      -9.530 -20.933  51.752  1.00 44.55           C  
ANISOU 3987  CA  LYS A 483     5725   6011   5192    -59    -61    318       C  
ATOM   3988  C   LYS A 483     -10.233 -22.287  51.498  1.00 43.64           C  
ANISOU 3988  C   LYS A 483     5567   5880   5133    -71    -24    333       C  
ATOM   3989  O   LYS A 483      -9.674 -23.350  51.769  1.00 41.78           O  
ANISOU 3989  O   LYS A 483     5359   5646   4870    -77    -24    355       O  
ATOM   3990  CB  LYS A 483     -10.076 -20.261  53.018  1.00 46.87           C  
ANISOU 3990  CB  LYS A 483     6081   6281   5449    -46     12    310       C  
ATOM   3991  CG  LYS A 483      -9.842 -20.972  54.319  1.00 51.41           C  
ANISOU 3991  CG  LYS A 483     6764   6830   5940    -44     59    331       C  
ATOM   3992  CD  LYS A 483     -10.453 -20.141  55.432  1.00 59.29           C  
ANISOU 3992  CD  LYS A 483     7852   7786   6889    -34    150    315       C  
ATOM   3993  CE  LYS A 483     -10.415 -20.861  56.763  1.00 63.24           C  
ANISOU 3993  CE  LYS A 483     8508   8235   7284    -33    218    337       C  
ATOM   3994  NZ  LYS A 483     -11.024 -20.007  57.819  1.00 67.11           N  
ANISOU 3994  NZ  LYS A 483     9117   8668   7714    -25    332    318       N  
ATOM   3995  N   GLU A 484     -11.456 -22.238  50.980  1.00 43.54           N  
ANISOU 3995  N   GLU A 484     5482   5844   5218    -73     -2    320       N  
ATOM   3996  CA  GLU A 484     -12.202 -23.450  50.657  1.00 43.74           C  
ANISOU 3996  CA  GLU A 484     5450   5843   5326    -87     22    326       C  
ATOM   3997  C   GLU A 484     -11.457 -24.273  49.596  1.00 43.24           C  
ANISOU 3997  C   GLU A 484     5388   5799   5243   -102    -55    334       C  
ATOM   3998  O   GLU A 484     -11.250 -25.473  49.778  1.00 43.12           O  
ANISOU 3998  O   GLU A 484     5378   5780   5226   -113    -29    352       O  
ATOM   3999  CB  GLU A 484     -13.617 -23.087  50.192  1.00 45.49           C  
ANISOU 3999  CB  GLU A 484     5574   6016   5694    -85     24    303       C  
ATOM   4000  CG  GLU A 484     -14.573 -24.258  49.981  1.00 52.16           C  
ANISOU 4000  CG  GLU A 484     6340   6812   6668   -100     52    302       C  
ATOM   4001  CD  GLU A 484     -15.903 -23.845  49.333  1.00 58.10           C  
ANISOU 4001  CD  GLU A 484     6973   7496   7605    -97      6    272       C  
ATOM   4002  OE1 GLU A 484     -16.464 -22.783  49.702  1.00 60.00           O  
ANISOU 4002  OE1 GLU A 484     7180   7708   7910    -80     41    257       O  
ATOM   4003  OE2 GLU A 484     -16.392 -24.594  48.457  1.00 59.30           O  
ANISOU 4003  OE2 GLU A 484     7066   7613   7852   -110    -76    263       O  
ATOM   4004  N   HIS A 485     -11.039 -23.634  48.501  1.00 40.90           N  
ANISOU 4004  N   HIS A 485     5101   5512   4928   -103   -134    320       N  
ATOM   4005  CA  HIS A 485     -10.332 -24.362  47.437  1.00 40.19           C  
ANISOU 4005  CA  HIS A 485     5037   5419   4814   -120   -178    321       C  
ATOM   4006  C   HIS A 485      -8.976 -24.904  47.892  1.00 38.89           C  
ANISOU 4006  C   HIS A 485     4907   5274   4594   -123   -151    340       C  
ATOM   4007  O   HIS A 485      -8.628 -26.042  47.587  1.00 40.70           O  
ANISOU 4007  O   HIS A 485     5137   5493   4835   -136   -142    350       O  
ATOM   4008  CB  HIS A 485     -10.222 -23.541  46.147  1.00 38.08           C  
ANISOU 4008  CB  HIS A 485     4810   5134   4525   -122   -248    303       C  
ATOM   4009  CG  HIS A 485     -11.547 -23.252  45.507  1.00 36.03           C  
ANISOU 4009  CG  HIS A 485     4519   4833   4337   -119   -319    286       C  
ATOM   4010  ND1 HIS A 485     -12.259 -24.203  44.805  1.00 33.13           N  
ANISOU 4010  ND1 HIS A 485     4137   4423   4027   -134   -373    277       N  
ATOM   4011  CD2 HIS A 485     -12.293 -22.124  45.470  1.00 35.94           C  
ANISOU 4011  CD2 HIS A 485     4483   4803   4370   -102   -360    273       C  
ATOM   4012  CE1 HIS A 485     -13.382 -23.672  44.358  1.00 32.77           C  
ANISOU 4012  CE1 HIS A 485     4054   4329   4068   -125   -460    260       C  
ATOM   4013  NE2 HIS A 485     -13.432 -22.413  44.754  1.00 39.76           N  
ANISOU 4013  NE2 HIS A 485     4929   5227   4950   -105   -450    258       N  
ATOM   4014  N   LYS A 486      -8.232 -24.112  48.652  1.00 38.26           N  
ANISOU 4014  N   LYS A 486     4852   5212   4474   -109   -148    343       N  
ATOM   4015  CA  LYS A 486      -6.952 -24.578  49.182  1.00 38.16           C  
ANISOU 4015  CA  LYS A 486     4858   5198   4443   -108   -153    359       C  
ATOM   4016  C   LYS A 486      -7.132 -25.837  50.044  1.00 39.85           C  
ANISOU 4016  C   LYS A 486     5080   5404   4655   -108   -126    386       C  
ATOM   4017  O   LYS A 486      -6.308 -26.760  49.985  1.00 41.09           O  
ANISOU 4017  O   LYS A 486     5234   5547   4832   -113   -137    401       O  
ATOM   4018  CB  LYS A 486      -6.234 -23.479  49.968  1.00 36.95           C  
ANISOU 4018  CB  LYS A 486     4732   5050   4258    -93   -181    353       C  
ATOM   4019  CG  LYS A 486      -4.741 -23.741  50.085  1.00 36.91           C  
ANISOU 4019  CG  LYS A 486     4721   5020   4283    -94   -220    358       C  
ATOM   4020  CD  LYS A 486      -4.094 -23.043  51.245  1.00 33.07           C  
ANISOU 4020  CD  LYS A 486     4271   4523   3773    -78   -278    357       C  
ATOM   4021  CE  LYS A 486      -2.680 -23.587  51.416  1.00 37.86           C  
ANISOU 4021  CE  LYS A 486     4849   5083   4453    -77   -340    364       C  
ATOM   4022  NZ  LYS A 486      -1.735 -22.592  52.006  1.00 37.63           N  
ANISOU 4022  NZ  LYS A 486     4823   5022   4453    -66   -423    346       N  
ATOM   4023  N   GLY A 487      -8.213 -25.863  50.828  1.00 37.50           N  
ANISOU 4023  N   GLY A 487     4795   5105   4349   -102    -79    392       N  
ATOM   4024  CA  GLY A 487      -8.616 -27.051  51.575  1.00 38.35           C  
ANISOU 4024  CA  GLY A 487     4924   5191   4457   -104    -26    419       C  
ATOM   4025  C   GLY A 487      -8.739 -28.270  50.684  1.00 39.40           C  
ANISOU 4025  C   GLY A 487     5005   5315   4651   -123    -23    423       C  
ATOM   4026  O   GLY A 487      -8.151 -29.311  50.986  1.00 39.11           O  
ANISOU 4026  O   GLY A 487     4987   5264   4608   -125    -21    447       O  
ATOM   4027  N   TYR A 488      -9.483 -28.134  49.579  1.00 39.62           N  
ANISOU 4027  N   TYR A 488     4978   5341   4736   -136    -36    397       N  
ATOM   4028  CA  TYR A 488      -9.610 -29.205  48.571  1.00 38.88           C  
ANISOU 4028  CA  TYR A 488     4854   5228   4690   -156    -50    391       C  
ATOM   4029  C   TYR A 488      -8.275 -29.608  47.960  1.00 37.39           C  
ANISOU 4029  C   TYR A 488     4693   5039   4476   -163    -73    395       C  
ATOM   4030  O   TYR A 488      -8.061 -30.777  47.652  1.00 38.45           O  
ANISOU 4030  O   TYR A 488     4820   5152   4636   -176    -58    403       O  
ATOM   4031  CB  TYR A 488     -10.573 -28.834  47.425  1.00 40.07           C  
ANISOU 4031  CB  TYR A 488     4973   5358   4894   -167   -101    359       C  
ATOM   4032  CG  TYR A 488     -11.984 -28.461  47.843  1.00 41.69           C  
ANISOU 4032  CG  TYR A 488     5116   5540   5186   -161    -82    348       C  
ATOM   4033  CD1 TYR A 488     -12.579 -29.026  48.978  1.00 38.98           C  
ANISOU 4033  CD1 TYR A 488     4744   5176   4889   -160     15    365       C  
ATOM   4034  CD2 TYR A 488     -12.729 -27.549  47.090  1.00 41.25           C  
ANISOU 4034  CD2 TYR A 488     5031   5462   5179   -158   -154    320       C  
ATOM   4035  CE1 TYR A 488     -13.868 -28.677  49.357  1.00 40.98           C  
ANISOU 4035  CE1 TYR A 488     4929   5385   5257   -157     64    350       C  
ATOM   4036  CE2 TYR A 488     -14.024 -27.193  47.457  1.00 43.42           C  
ANISOU 4036  CE2 TYR A 488     5223   5695   5579   -152   -136    306       C  
ATOM   4037  CZ  TYR A 488     -14.591 -27.760  48.595  1.00 44.98           C  
ANISOU 4037  CZ  TYR A 488     5377   5869   5843   -152    -14    319       C  
ATOM   4038  OH  TYR A 488     -15.876 -27.413  48.970  1.00 40.85           O  
ANISOU 4038  OH  TYR A 488     4760   5284   5477   -148     37    301       O  
ATOM   4039  N   MET A 489      -7.382 -28.645  47.766  1.00 35.89           N  
ANISOU 4039  N   MET A 489     4526   4859   4253   -155    -98    386       N  
ATOM   4040  CA  MET A 489      -6.118 -28.948  47.124  1.00 35.14           C  
ANISOU 4040  CA  MET A 489     4440   4739   4171   -163    -93    383       C  
ATOM   4041  C   MET A 489      -5.203 -29.767  48.033  1.00 37.36           C  
ANISOU 4041  C   MET A 489     4706   5007   4481   -154    -91    412       C  
ATOM   4042  O   MET A 489      -4.593 -30.741  47.578  1.00 36.28           O  
ANISOU 4042  O   MET A 489     4556   4837   4393   -164    -68    415       O  
ATOM   4043  CB  MET A 489      -5.414 -27.676  46.690  1.00 36.68           C  
ANISOU 4043  CB  MET A 489     4654   4930   4352   -159   -104    364       C  
ATOM   4044  CG  MET A 489      -4.044 -27.934  46.093  1.00 38.41           C  
ANISOU 4044  CG  MET A 489     4871   5101   4621   -169    -67    358       C  
ATOM   4045  SD  MET A 489      -3.071 -26.443  46.070  1.00 47.84           S  
ANISOU 4045  SD  MET A 489     6063   6278   5835   -161    -68    341       S  
ATOM   4046  CE  MET A 489      -2.461 -26.404  47.757  1.00 44.95           C  
ANISOU 4046  CE  MET A 489     5648   5927   5505   -136   -141    363       C  
ATOM   4047  N   LEU A 490      -5.110 -29.370  49.306  1.00 36.15           N  
ANISOU 4047  N   LEU A 490     4570   4869   4298   -133   -121    431       N  
ATOM   4048  CA  LEU A 490      -4.224 -30.038  50.256  1.00 37.10           C  
ANISOU 4048  CA  LEU A 490     4701   4960   4436   -119   -157    460       C  
ATOM   4049  C   LEU A 490      -4.668 -31.464  50.598  1.00 39.46           C  
ANISOU 4049  C   LEU A 490     5011   5243   4741   -123   -126    490       C  
ATOM   4050  O   LEU A 490      -3.826 -32.361  50.740  1.00 43.49           O  
ANISOU 4050  O   LEU A 490     5508   5714   5303   -119   -149    510       O  
ATOM   4051  CB  LEU A 490      -4.020 -29.205  51.527  1.00 35.65           C  
ANISOU 4051  CB  LEU A 490     4575   4777   4192    -96   -216    471       C  
ATOM   4052  CG  LEU A 490      -3.185 -27.922  51.412  1.00 36.10           C  
ANISOU 4052  CG  LEU A 490     4615   4831   4271    -90   -270    445       C  
ATOM   4053  CD1 LEU A 490      -3.144 -27.192  52.752  1.00 34.57           C  
ANISOU 4053  CD1 LEU A 490     4505   4631   4000    -69   -337    453       C  
ATOM   4054  CD2 LEU A 490      -1.760 -28.191  50.884  1.00 34.41           C  
ANISOU 4054  CD2 LEU A 490     4330   4564   4181    -93   -303    438       C  
ATOM   4055  N   ALA A 491      -5.974 -31.685  50.711  1.00 37.81           N  
ANISOU 4055  N   ALA A 491     4813   5051   4501   -131    -71    491       N  
ATOM   4056  CA  ALA A 491      -6.480 -33.037  50.899  1.00 38.55           C  
ANISOU 4056  CA  ALA A 491     4908   5122   4618   -139    -24    514       C  
ATOM   4057  C   ALA A 491      -6.139 -33.885  49.684  1.00 39.43           C  
ANISOU 4057  C   ALA A 491     4966   5217   4798   -159    -15    499       C  
ATOM   4058  O   ALA A 491      -5.696 -35.023  49.832  1.00 43.61           O  
ANISOU 4058  O   ALA A 491     5492   5715   5364   -160     -6    522       O  
ATOM   4059  CB  ALA A 491      -7.971 -33.039  51.161  1.00 37.60           C  
ANISOU 4059  CB  ALA A 491     4787   5003   4495   -147     47    510       C  
ATOM   4060  N   ALA A 492      -6.314 -33.331  48.485  1.00 39.06           N  
ANISOU 4060  N   ALA A 492     4897   5181   4763   -175    -16    461       N  
ATOM   4061  CA  ALA A 492      -5.964 -34.056  47.256  1.00 39.59           C  
ANISOU 4061  CA  ALA A 492     4955   5216   4871   -197      3    441       C  
ATOM   4062  C   ALA A 492      -4.475 -34.412  47.261  1.00 41.01           C  
ANISOU 4062  C   ALA A 492     5121   5359   5103   -191      9    451       C  
ATOM   4063  O   ALA A 492      -4.078 -35.516  46.876  1.00 41.53           O  
ANISOU 4063  O   ALA A 492     5174   5383   5223   -201     43    454       O  
ATOM   4064  CB  ALA A 492      -6.322 -33.240  46.025  1.00 37.43           C  
ANISOU 4064  CB  ALA A 492     4709   4943   4572   -213    -10    400       C  
ATOM   4065  N   GLN A 493      -3.668 -33.469  47.735  1.00 40.07           N  
ANISOU 4065  N   GLN A 493     4996   5243   4986   -173    -27    454       N  
ATOM   4066  CA  GLN A 493      -2.231 -33.645  47.851  1.00 40.83           C  
ANISOU 4066  CA  GLN A 493     5051   5285   5175   -163    -40    460       C  
ATOM   4067  C   GLN A 493      -1.860 -34.701  48.893  1.00 41.00           C  
ANISOU 4067  C   GLN A 493     5061   5278   5238   -145    -84    502       C  
ATOM   4068  O   GLN A 493      -0.966 -35.511  48.652  1.00 39.91           O  
ANISOU 4068  O   GLN A 493     4877   5078   5209   -145    -71    507       O  
ATOM   4069  CB  GLN A 493      -1.591 -32.295  48.179  1.00 40.88           C  
ANISOU 4069  CB  GLN A 493     5049   5296   5189   -149    -87    449       C  
ATOM   4070  CG  GLN A 493      -0.097 -32.291  48.308  1.00 37.84           C  
ANISOU 4070  CG  GLN A 493     4597   4837   4943   -138   -114    447       C  
ATOM   4071  CD  GLN A 493       0.413 -30.907  48.626  1.00 43.14           C  
ANISOU 4071  CD  GLN A 493     5256   5509   5628   -127   -167    431       C  
ATOM   4072  OE1 GLN A 493       0.694 -30.587  49.785  1.00 46.12           O  
ANISOU 4072  OE1 GLN A 493     5641   5884   6000   -104   -278    449       O  
ATOM   4073  NE2 GLN A 493       0.510 -30.063  47.603  1.00 37.20           N  
ANISOU 4073  NE2 GLN A 493     4504   4750   4881   -145    -91    396       N  
ATOM   4074  N   ARG A 494      -2.543 -34.685  50.044  1.00 43.07           N  
ANISOU 4074  N   ARG A 494     5378   5571   5416   -129   -126    533       N  
ATOM   4075  CA  ARG A 494      -2.332 -35.695  51.105  1.00 42.18           C  
ANISOU 4075  CA  ARG A 494     5300   5420   5307   -110   -170    580       C  
ATOM   4076  C   ARG A 494      -2.786 -37.077  50.637  1.00 40.05           C  
ANISOU 4076  C   ARG A 494     5012   5134   5071   -127    -97    590       C  
ATOM   4077  O   ARG A 494      -2.129 -38.078  50.896  1.00 39.97           O  
ANISOU 4077  O   ARG A 494     4988   5069   5130   -118   -119    617       O  
ATOM   4078  CB  ARG A 494      -3.087 -35.332  52.388  1.00 41.35           C  
ANISOU 4078  CB  ARG A 494     5300   5335   5076    -94   -196    608       C  
ATOM   4079  CG  ARG A 494      -2.521 -34.160  53.160  1.00 43.06           C  
ANISOU 4079  CG  ARG A 494     5565   5548   5249    -72   -292    606       C  
ATOM   4080  CD  ARG A 494      -3.239 -33.979  54.496  1.00 41.55           C  
ANISOU 4080  CD  ARG A 494     5520   5352   4917    -57   -298    635       C  
ATOM   4081  NE  ARG A 494      -4.649 -33.586  54.361  1.00 37.11           N  
ANISOU 4081  NE  ARG A 494     4972   4836   4290    -74   -177    619       N  
ATOM   4082  CZ  ARG A 494      -5.075 -32.328  54.305  1.00 34.92           C  
ANISOU 4082  CZ  ARG A 494     4697   4597   3972    -75   -163    588       C  
ATOM   4083  NH1 ARG A 494      -4.210 -31.330  54.353  1.00 34.58           N  
ANISOU 4083  NH1 ARG A 494     4650   4558   3932    -64   -255    570       N  
ATOM   4084  NH2 ARG A 494      -6.369 -32.062  54.200  1.00 33.48           N  
ANISOU 4084  NH2 ARG A 494     4512   4440   3770    -88    -57    574       N  
ATOM   4085  N   ASN A 495      -3.925 -37.119  49.957  1.00 38.88           N  
ANISOU 4085  N   ASN A 495     4862   5023   4886   -152    -24    566       N  
ATOM   4086  CA  ASN A 495      -4.408 -38.357  49.362  1.00 40.45           C  
ANISOU 4086  CA  ASN A 495     5040   5201   5126   -174     39    564       C  
ATOM   4087  C   ASN A 495      -3.384 -38.919  48.383  1.00 41.57           C  
ANISOU 4087  C   ASN A 495     5137   5296   5363   -184     61    544       C  
ATOM   4088  O   ASN A 495      -3.139 -40.131  48.365  1.00 43.47           O  
ANISOU 4088  O   ASN A 495     5360   5490   5664   -187     86    561       O  
ATOM   4089  CB  ASN A 495      -5.738 -38.130  48.644  1.00 39.28           C  
ANISOU 4089  CB  ASN A 495     4889   5086   4950   -199     81    530       C  
ATOM   4090  CG  ASN A 495      -6.903 -37.946  49.598  1.00 38.87           C  
ANISOU 4090  CG  ASN A 495     4861   5052   4854   -194    103    548       C  
ATOM   4091  OD1 ASN A 495      -6.862 -38.372  50.762  1.00 39.73           O  
ANISOU 4091  OD1 ASN A 495     5019   5141   4936   -177    115    592       O  
ATOM   4092  ND2 ASN A 495      -7.967 -37.318  49.100  1.00 35.87           N  
ANISOU 4092  ND2 ASN A 495     4460   4694   4476   -208    113    515       N  
ATOM   4093  N   GLY A 496      -2.784 -38.032  47.583  1.00 40.82           N  
ANISOU 4093  N   GLY A 496     5027   5197   5286   -190     67    509       N  
ATOM   4094  CA  GLY A 496      -1.746 -38.413  46.630  1.00 38.18           C  
ANISOU 4094  CA  GLY A 496     4660   4795   5051   -203    125    484       C  
ATOM   4095  C   GLY A 496      -0.637 -39.190  47.308  1.00 39.95           C  
ANISOU 4095  C   GLY A 496     4825   4954   5400   -180     96    517       C  
ATOM   4096  O   GLY A 496      -0.222 -40.251  46.823  1.00 39.80           O  
ANISOU 4096  O   GLY A 496     4778   4873   5472   -190    155    514       O  
ATOM   4097  N   GLU A 497      -0.180 -38.674  48.449  1.00 39.86           N  
ANISOU 4097  N   GLU A 497     4803   4945   5396   -149     -8    548       N  
ATOM   4098  CA  GLU A 497       0.956 -39.256  49.162  1.00 42.62           C  
ANISOU 4098  CA  GLU A 497     5099   5215   5881   -122    -83    579       C  
ATOM   4099  C   GLU A 497       0.644 -40.611  49.779  1.00 43.10           C  
ANISOU 4099  C   GLU A 497     5188   5253   5937   -112   -100    625       C  
ATOM   4100  O   GLU A 497       1.516 -41.484  49.837  1.00 45.16           O  
ANISOU 4100  O   GLU A 497     5390   5429   6341   -100   -119    641       O  
ATOM   4101  CB  GLU A 497       1.483 -38.294  50.223  1.00 44.02           C  
ANISOU 4101  CB  GLU A 497     5285   5388   6053    -91   -222    596       C  
ATOM   4102  CG  GLU A 497       2.063 -37.013  49.648  1.00 45.23           C  
ANISOU 4102  CG  GLU A 497     5388   5538   6261    -98   -208    552       C  
ATOM   4103  CD  GLU A 497       3.135 -37.270  48.616  1.00 51.19           C  
ANISOU 4103  CD  GLU A 497     6036   6199   7215   -112   -115    518       C  
ATOM   4104  OE1 GLU A 497       4.149 -37.926  48.950  1.00 51.25           O  
ANISOU 4104  OE1 GLU A 497     5958   6108   7406    -93   -168    533       O  
ATOM   4105  OE2 GLU A 497       2.958 -36.815  47.466  1.00 54.48           O  
ANISOU 4105  OE2 GLU A 497     6463   6627   7610   -141     15    476       O  
ATOM   4106  N   ILE A 498      -0.595 -40.780  50.234  1.00 41.70           N  
ANISOU 4106  N   ILE A 498     5094   5138   5612   -118    -85    645       N  
ATOM   4107  CA  ILE A 498      -1.076 -42.069  50.715  1.00 40.09           C  
ANISOU 4107  CA  ILE A 498     4928   4911   5394   -116    -67    685       C  
ATOM   4108  C   ILE A 498      -0.966 -43.084  49.579  1.00 40.64           C  
ANISOU 4108  C   ILE A 498     4934   4944   5562   -142     33    658       C  
ATOM   4109  O   ILE A 498      -0.360 -44.138  49.759  1.00 41.72           O  
ANISOU 4109  O   ILE A 498     5041   5010   5799   -131     24    685       O  
ATOM   4110  CB  ILE A 498      -2.525 -41.969  51.262  1.00 39.22           C  
ANISOU 4110  CB  ILE A 498     4904   4860   5137   -125    -26    699       C  
ATOM   4111  CG1 ILE A 498      -2.532 -41.256  52.608  1.00 38.57           C  
ANISOU 4111  CG1 ILE A 498     4923   4781   4952    -96   -112    736       C  
ATOM   4112  CG2 ILE A 498      -3.173 -43.344  51.414  1.00 35.93           C  
ANISOU 4112  CG2 ILE A 498     4510   4414   4729   -136     40    727       C  
ATOM   4113  CD1 ILE A 498      -3.899 -40.674  52.979  1.00 43.43           C  
ANISOU 4113  CD1 ILE A 498     5608   5451   5443   -108    -42    731       C  
ATOM   4114  N   ILE A 499      -1.519 -42.756  48.409  1.00 39.95           N  
ANISOU 4114  N   ILE A 499     4841   4893   5445   -176    118    606       N  
ATOM   4115  CA  ILE A 499      -1.397 -43.630  47.228  1.00 43.22           C  
ANISOU 4115  CA  ILE A 499     5230   5260   5931   -205    214    571       C  
ATOM   4116  C   ILE A 499       0.077 -43.931  46.893  1.00 45.28           C  
ANISOU 4116  C   ILE A 499     5419   5428   6358   -195    239    564       C  
ATOM   4117  O   ILE A 499       0.425 -45.065  46.557  1.00 45.99           O  
ANISOU 4117  O   ILE A 499     5480   5449   6544   -202    296    564       O  
ATOM   4118  CB  ILE A 499      -2.125 -43.051  45.973  1.00 43.43           C  
ANISOU 4118  CB  ILE A 499     5300   5321   5880   -241    274    511       C  
ATOM   4119  CG1 ILE A 499      -3.643 -43.024  46.186  1.00 42.38           C  
ANISOU 4119  CG1 ILE A 499     5206   5251   5647   -255    253    512       C  
ATOM   4120  CG2 ILE A 499      -1.803 -43.882  44.729  1.00 40.70           C  
ANISOU 4120  CG2 ILE A 499     4967   4904   5594   -271    374    470       C  
ATOM   4121  CD1 ILE A 499      -4.384 -42.062  45.269  1.00 38.55           C  
ANISOU 4121  CD1 ILE A 499     4764   4801   5082   -277    248    463       C  
ATOM   4122  N   LYS A 500       0.930 -42.915  46.997  1.00 45.85           N  
ANISOU 4122  N   LYS A 500     5452   5485   6483   -179    201    554       N  
ATOM   4123  CA  LYS A 500       2.368 -43.083  46.778  1.00 46.34           C  
ANISOU 4123  CA  LYS A 500     5417   5437   6751   -167    223    545       C  
ATOM   4124  C   LYS A 500       3.003 -44.070  47.753  1.00 48.75           C  
ANISOU 4124  C   LYS A 500     5666   5673   7185   -133    129    598       C  
ATOM   4125  O   LYS A 500       3.835 -44.879  47.350  1.00 50.32           O  
ANISOU 4125  O   LYS A 500     5786   5768   7565   -132    188    590       O  
ATOM   4126  CB  LYS A 500       3.090 -41.737  46.847  1.00 46.12           C  
ANISOU 4126  CB  LYS A 500     5348   5402   6774   -156    183    526       C  
ATOM   4127  CG  LYS A 500       3.026 -40.915  45.562  1.00 44.34           C  
ANISOU 4127  CG  LYS A 500     5159   5179   6508   -190    317    467       C  
ATOM   4128  CD  LYS A 500       3.796 -39.617  45.730  1.00 44.87           C  
ANISOU 4128  CD  LYS A 500     5174   5227   6648   -177    281    452       C  
ATOM   4129  CE  LYS A 500       3.584 -38.664  44.568  1.00 45.48           C  
ANISOU 4129  CE  LYS A 500     5322   5314   6644   -209    405    402       C  
ATOM   4130  NZ  LYS A 500       3.910 -37.266  44.958  1.00 40.85           N  
ANISOU 4130  NZ  LYS A 500     4710   4750   6063   -196    339    397       N  
ATOM   4131  N   GLU A 501       2.614 -43.996  49.030  1.00 51.19           N  
ANISOU 4131  N   GLU A 501     6030   6024   7398   -104    -12    651       N  
ATOM   4132  CA  GLU A 501       3.047 -44.973  50.039  1.00 52.50           C  
ANISOU 4132  CA  GLU A 501     6190   6119   7638    -70   -121    710       C  
ATOM   4133  C   GLU A 501       2.632 -46.390  49.644  1.00 51.78           C  
ANISOU 4133  C   GLU A 501     6105   6003   7567    -86    -23    720       C  
ATOM   4134  O   GLU A 501       3.424 -47.328  49.736  1.00 50.88           O  
ANISOU 4134  O   GLU A 501     5925   5788   7621    -69    -41    740       O  
ATOM   4135  CB  GLU A 501       2.466 -44.635  51.413  1.00 53.78           C  
ANISOU 4135  CB  GLU A 501     6475   6328   7631    -43   -258    764       C  
ATOM   4136  CG  GLU A 501       3.378 -43.807  52.307  1.00 64.56           C  
ANISOU 4136  CG  GLU A 501     7836   7644   9049     -6   -441    781       C  
ATOM   4137  CD  GLU A 501       4.306 -44.663  53.173  1.00 72.03           C  
ANISOU 4137  CD  GLU A 501     8770   8465  10134     36   -603    834       C  
ATOM   4138  OE1 GLU A 501       5.035 -45.529  52.629  1.00 72.86           O  
ANISOU 4138  OE1 GLU A 501     8754   8481  10448     38   -564    828       O  
ATOM   4139  OE2 GLU A 501       4.314 -44.453  54.408  1.00 74.80           O  
ANISOU 4139  OE2 GLU A 501     9245   8793  10384     68   -774    882       O  
ATOM   4140  N   ALA A 502       1.391 -46.527  49.185  1.00 50.85           N  
ANISOU 4140  N   ALA A 502     6057   5967   7296   -120     75    703       N  
ATOM   4141  CA  ALA A 502       0.834 -47.825  48.830  1.00 52.61           C  
ANISOU 4141  CA  ALA A 502     6294   6171   7524   -140    163    707       C  
ATOM   4142  C   ALA A 502       1.524 -48.450  47.614  1.00 54.96           C  
ANISOU 4142  C   ALA A 502     6518   6390   7975   -162    283    660       C  
ATOM   4143  O   ALA A 502       1.459 -49.660  47.420  1.00 56.24           O  
ANISOU 4143  O   ALA A 502     6671   6501   8197   -170    339    668       O  
ATOM   4144  CB  ALA A 502      -0.664 -47.709  48.597  1.00 51.00           C  
ANISOU 4144  CB  ALA A 502     6166   6058   7153   -172    222    690       C  
ATOM   4145  N   LEU A 503       2.187 -47.623  46.806  1.00 55.98           N  
ANISOU 4145  N   LEU A 503     6605   6497   8167   -173    337    609       N  
ATOM   4146  CA  LEU A 503       2.865 -48.098  45.601  1.00 56.46           C  
ANISOU 4146  CA  LEU A 503     6624   6464   8365   -197    487    558       C  
ATOM   4147  C   LEU A 503       4.201 -48.781  45.906  1.00 58.51           C  
ANISOU 4147  C   LEU A 503     6759   6589   8884   -167    477    578       C  
ATOM   4148  O   LEU A 503       4.776 -49.448  45.038  1.00 57.91           O  
ANISOU 4148  O   LEU A 503     6642   6411   8951   -185    620    542       O  
ATOM   4149  CB  LEU A 503       3.036 -46.957  44.584  1.00 56.18           C  
ANISOU 4149  CB  LEU A 503     6617   6435   8293   -223    579    496       C  
ATOM   4150  CG  LEU A 503       1.808 -46.669  43.700  1.00 53.75           C  
ANISOU 4150  CG  LEU A 503     6442   6206   7776   -265    635    455       C  
ATOM   4151  CD1 LEU A 503       1.758 -45.210  43.225  1.00 49.04           C  
ANISOU 4151  CD1 LEU A 503     5894   5651   7089   -275    643    421       C  
ATOM   4152  CD2 LEU A 503       1.734 -47.631  42.514  1.00 51.84           C  
ANISOU 4152  CD2 LEU A 503     6261   5888   7550   -303    783    408       C  
ATOM   4153  N   HIS A 504       4.680 -48.611  47.141  1.00 60.48           N  
ANISOU 4153  N   HIS A 504     6959   6824   9196   -122    303    635       N  
ATOM   4154  CA  HIS A 504       5.898 -49.279  47.612  1.00 62.91           C  
ANISOU 4154  CA  HIS A 504     7143   6991   9768    -85    235    663       C  
ATOM   4155  C   HIS A 504       5.669 -50.771  47.803  1.00 63.73           C  
ANISOU 4155  C   HIS A 504     7260   7051   9905    -80    251    699       C  
ATOM   4156  O   HIS A 504       6.604 -51.564  47.706  1.00 65.04           O  
ANISOU 4156  O   HIS A 504     7317   7083  10313    -63    270    703       O  
ATOM   4157  CB  HIS A 504       6.397 -48.675  48.929  1.00 63.19           C  
ANISOU 4157  CB  HIS A 504     7157   7013   9837    -36      1    715       C  
ATOM   4158  CG  HIS A 504       6.751 -47.221  48.842  1.00 64.66           C  
ANISOU 4158  CG  HIS A 504     7314   7227  10026    -37    -32    681       C  
ATOM   4159  ND1 HIS A 504       7.168 -46.620  47.674  1.00 65.87           N  
ANISOU 4159  ND1 HIS A 504     7405   7350  10272    -69    139    612       N  
ATOM   4160  CD2 HIS A 504       6.778 -46.255  49.791  1.00 64.12           C  
ANISOU 4160  CD2 HIS A 504     7284   7200   9880    -11   -211    706       C  
ATOM   4161  CE1 HIS A 504       7.419 -45.343  47.903  1.00 66.54           C  
ANISOU 4161  CE1 HIS A 504     7476   7463  10345    -62     67    598       C  
ATOM   4162  NE2 HIS A 504       7.191 -45.097  49.180  1.00 65.50           N  
ANISOU 4162  NE2 HIS A 504     7399   7376  10112    -28   -150    652       N  
ATOM   4163  N   ASN A 505       4.424 -51.138  48.086  1.00 63.55           N  
ANISOU 4163  N   ASN A 505     7359   7129   9657    -94    248    724       N  
ATOM   4164  CA  ASN A 505       4.052 -52.527  48.292  1.00 65.82           C  
ANISOU 4164  CA  ASN A 505     7672   7382   9954    -93    271    759       C  
ATOM   4165  C   ASN A 505       2.776 -52.900  47.540  1.00 64.97           C  
ANISOU 4165  C   ASN A 505     7654   7356   9677   -143    405    723       C  
ATOM   4166  O   ASN A 505       1.791 -53.292  48.167  1.00 65.93           O  
ANISOU 4166  O   ASN A 505     7856   7535   9661   -145    371    762       O  
ATOM   4167  CB  ASN A 505       3.882 -52.812  49.792  1.00 68.03           C  
ANISOU 4167  CB  ASN A 505     8020   7662  10167    -49     90    847       C  
ATOM   4168  CG  ASN A 505       5.210 -52.852  50.539  1.00 72.48           C  
ANISOU 4168  CG  ASN A 505     8498   8099  10940      4    -79    887       C  
ATOM   4169  OD1 ASN A 505       5.546 -51.925  51.282  1.00 73.29           O  
ANISOU 4169  OD1 ASN A 505     8621   8211  11015     32   -236    907       O  
ATOM   4170  ND2 ASN A 505       5.971 -53.929  50.344  1.00 72.11           N  
ANISOU 4170  ND2 ASN A 505     8355   7924  11118     19    -58    897       N  
ATOM   4171  N   PRO A 506       2.788 -52.799  46.195  1.00 65.29           N  
ANISOU 4171  N   PRO A 506     7689   7384   9735   -185    559    648       N  
ATOM   4172  CA  PRO A 506       1.567 -53.079  45.436  1.00 66.41           C  
ANISOU 4172  CA  PRO A 506     7924   7589   9719   -233    648    607       C  
ATOM   4173  C   PRO A 506       1.158 -54.550  45.512  1.00 70.03           C  
ANISOU 4173  C   PRO A 506     8392   8003  10214   -242    688    627       C  
ATOM   4174  O   PRO A 506       2.008 -55.442  45.403  1.00 72.94           O  
ANISOU 4174  O   PRO A 506     8695   8262  10756   -229    736    634       O  
ATOM   4175  CB  PRO A 506       1.948 -52.699  44.004  1.00 66.15           C  
ANISOU 4175  CB  PRO A 506     7911   7512   9711   -269    791    526       C  
ATOM   4176  CG  PRO A 506       3.415 -52.885  43.943  1.00 65.97           C  
ANISOU 4176  CG  PRO A 506     7777   7362   9927   -245    841    525       C  
ATOM   4177  CD  PRO A 506       3.939 -52.542  45.308  1.00 65.68           C  
ANISOU 4177  CD  PRO A 506     7659   7334   9965   -191    665    596       C  
ATOM   4178  N   ASN A 507      -0.133 -54.795  45.715  1.00 71.16           N  
ANISOU 4178  N   ASN A 507     8604   8219  10215   -263    674    635       N  
ATOM   4179  CA  ASN A 507      -0.648 -56.154  45.809  1.00 72.86           C  
ANISOU 4179  CA  ASN A 507     8829   8392  10461   -275    716    652       C  
ATOM   4180  C   ASN A 507      -0.836 -56.796  44.448  1.00 74.25           C  
ANISOU 4180  C   ASN A 507     9032   8518  10662   -324    840    575       C  
ATOM   4181  O   ASN A 507      -1.170 -56.120  43.476  1.00 73.72           O  
ANISOU 4181  O   ASN A 507     9022   8480  10509   -357    876    509       O  
ATOM   4182  CB  ASN A 507      -1.954 -56.179  46.598  1.00 72.28           C  
ANISOU 4182  CB  ASN A 507     8810   8393  10262   -281    670    688       C  
ATOM   4183  CG  ASN A 507      -1.736 -55.931  48.071  1.00 74.46           C  
ANISOU 4183  CG  ASN A 507     9103   8680  10509   -232    567    775       C  
ATOM   4184  OD1 ASN A 507      -1.187 -54.899  48.464  1.00 76.96           O  
ANISOU 4184  OD1 ASN A 507     9416   9026  10799   -205    486    787       O  
ATOM   4185  ND2 ASN A 507      -2.152 -56.879  48.899  1.00 74.21           N  
ANISOU 4185  ND2 ASN A 507     9107   8611  10478   -221    567    834       N  
ATOM   4186  N   LEU A 508      -0.609 -58.105  44.384  1.00 76.98           N  
ANISOU 4186  N   LEU A 508     9353   8777  11120   -326    900    585       N  
ATOM   4187  CA  LEU A 508      -0.807 -58.851  43.146  1.00 79.34           C  
ANISOU 4187  CA  LEU A 508     9697   9012  11436   -374   1018    511       C  
ATOM   4188  C   LEU A 508      -2.235 -59.381  43.045  1.00 79.91           C  
ANISOU 4188  C   LEU A 508     9824   9124  11416   -412   1002    494       C  
ATOM   4189  O   LEU A 508      -2.542 -60.492  43.497  1.00 80.38           O  
ANISOU 4189  O   LEU A 508     9859   9143  11537   -411   1017    527       O  
ATOM   4190  CB  LEU A 508       0.234 -59.961  42.991  1.00 80.46           C  
ANISOU 4190  CB  LEU A 508     9779   9023  11769   -361   1109    517       C  
ATOM   4191  CG  LEU A 508       1.552 -59.512  42.353  1.00 82.39           C  
ANISOU 4191  CG  LEU A 508     9983   9182  12138   -352   1199    481       C  
ATOM   4192  CD1 LEU A 508       2.595 -59.093  43.391  1.00 81.28           C  
ANISOU 4192  CD1 LEU A 508     9722   9020  12139   -291   1104    549       C  
ATOM   4193  CD2 LEU A 508       2.088 -60.606  41.438  1.00 87.15           C  
ANISOU 4193  CD2 LEU A 508    10593   9646  12875   -376   1364    430       C  
ATOM   4194  N   SER A 509      -3.097 -58.557  42.452  1.00 80.15           N  
ANISOU 4194  N   SER A 509     9921   9220  11314   -443    967    442       N  
ATOM   4195  CA  SER A 509      -4.518 -58.859  42.288  1.00 80.23           C  
ANISOU 4195  CA  SER A 509     9964   9256  11263   -481    929    414       C  
ATOM   4196  C   SER A 509      -5.085 -58.169  41.053  1.00 79.83           C  
ANISOU 4196  C   SER A 509    10012   9215  11103   -523    902    327       C  
ATOM   4197  O   SER A 509      -4.431 -57.316  40.446  1.00 79.41           O  
ANISOU 4197  O   SER A 509    10015   9163  10994   -521    920    297       O  
ATOM   4198  CB  SER A 509      -5.304 -58.411  43.526  1.00 79.85           C  
ANISOU 4198  CB  SER A 509     9871   9291  11179   -458    853    479       C  
ATOM   4199  OG  SER A 509      -5.127 -57.026  43.768  1.00 80.83           O  
ANISOU 4199  OG  SER A 509    10000   9492  11217   -436    793    488       O  
ATOM   4200  N   VAL A 510      -6.303 -58.553  40.682  1.00 80.35           N  
ANISOU 4200  N   VAL A 510    10106   9272  11151   -562    852    286       N  
ATOM   4201  CA  VAL A 510      -7.054 -57.832  39.663  1.00 80.79           C  
ANISOU 4201  CA  VAL A 510    10260   9334  11102   -598    772    210       C  
ATOM   4202  C   VAL A 510      -8.228 -57.121  40.341  1.00 79.61           C  
ANISOU 4202  C   VAL A 510    10042   9264  10942   -592    664    232       C  
ATOM   4203  O   VAL A 510      -9.206 -57.753  40.756  1.00 80.27           O  
ANISOU 4203  O   VAL A 510    10059   9333  11108   -608    640    238       O  
ATOM   4204  CB  VAL A 510      -7.502 -58.751  38.487  1.00 82.56           C  
ANISOU 4204  CB  VAL A 510    10589   9455  11326   -650    771    128       C  
ATOM   4205  CG1 VAL A 510      -8.452 -58.015  37.538  1.00 81.88           C  
ANISOU 4205  CG1 VAL A 510    10615   9362  11135   -684    636     54       C  
ATOM   4206  CG2 VAL A 510      -6.282 -59.260  37.718  1.00 83.62           C  
ANISOU 4206  CG2 VAL A 510    10816   9498  11457   -656    907     98       C  
ATOM   4207  N   ASP A 511      -8.088 -55.804  40.477  1.00 77.47           N  
ANISOU 4207  N   ASP A 511     9783   9066  10588   -571    617    243       N  
ATOM   4208  CA  ASP A 511      -9.098 -54.940  41.087  1.00 74.44           C  
ANISOU 4208  CA  ASP A 511     9338   8752  10194   -562    529    260       C  
ATOM   4209  C   ASP A 511      -9.309 -53.691  40.229  1.00 73.36           C  
ANISOU 4209  C   ASP A 511     9288   8640   9947   -571    437    209       C  
ATOM   4210  O   ASP A 511      -8.678 -53.546  39.176  1.00 72.92           O  
ANISOU 4210  O   ASP A 511     9356   8539   9810   -586    451    163       O  
ATOM   4211  CB  ASP A 511      -8.702 -54.565  42.527  1.00 73.23           C  
ANISOU 4211  CB  ASP A 511     9103   8669  10054   -515    569    348       C  
ATOM   4212  CG  ASP A 511      -7.195 -54.308  42.697  1.00 72.23           C  
ANISOU 4212  CG  ASP A 511     8994   8551   9898   -481    622    383       C  
ATOM   4213  OD1 ASP A 511      -6.583 -53.598  41.867  1.00 68.07           O  
ANISOU 4213  OD1 ASP A 511     8533   8024   9308   -484    620    344       O  
ATOM   4214  OD2 ASP A 511      -6.624 -54.808  43.691  1.00 73.10           O  
ANISOU 4214  OD2 ASP A 511     9055   8657  10062   -449    663    450       O  
ATOM   4215  N   GLU A 512     -10.207 -52.811  40.671  1.00 72.65           N  
ANISOU 4215  N   GLU A 512     9142   8604   9858   -563    354    217       N  
ATOM   4216  CA  GLU A 512     -10.445 -51.522  40.005  1.00 72.02           C  
ANISOU 4216  CA  GLU A 512     9134   8549   9680   -564    255    180       C  
ATOM   4217  C   GLU A 512     -10.057 -50.341  40.912  1.00 68.33           C  
ANISOU 4217  C   GLU A 512     8616   8176   9168   -523    272    235       C  
ATOM   4218  O   GLU A 512      -9.989 -50.492  42.137  1.00 67.21           O  
ANISOU 4218  O   GLU A 512     8382   8076   9079   -497    330    297       O  
ATOM   4219  CB  GLU A 512     -11.911 -51.384  39.551  1.00 73.43           C  
ANISOU 4219  CB  GLU A 512     9294   8688   9916   -593    112    128       C  
ATOM   4220  CG  GLU A 512     -12.358 -52.362  38.446  1.00 79.20           C  
ANISOU 4220  CG  GLU A 512    10110   9310  10673   -638     44     57       C  
ATOM   4221  CD  GLU A 512     -11.901 -51.991  37.023  1.00 82.55           C  
ANISOU 4221  CD  GLU A 512    10751   9676  10937   -658    -18     -5       C  
ATOM   4222  OE1 GLU A 512     -12.316 -52.704  36.082  1.00 83.98           O  
ANISOU 4222  OE1 GLU A 512    11037   9757  11116   -696    -96    -70       O  
ATOM   4223  OE2 GLU A 512     -11.141 -51.011  36.828  1.00 81.69           O  
ANISOU 4223  OE2 GLU A 512    10727   9609  10704   -637     14      7       O  
ATOM   4224  N   PRO A 513      -9.787 -49.164  40.312  1.00 65.89           N  
ANISOU 4224  N   PRO A 513     8389   7892   8754   -517    221    212       N  
ATOM   4225  CA  PRO A 513      -9.595 -47.968  41.133  1.00 62.79           C  
ANISOU 4225  CA  PRO A 513     7947   7584   8327   -481    217    255       C  
ATOM   4226  C   PRO A 513     -10.871 -47.645  41.897  1.00 60.11           C  
ANISOU 4226  C   PRO A 513     7504   7273   8060   -477    162    268       C  
ATOM   4227  O   PRO A 513     -11.968 -47.824  41.363  1.00 60.75           O  
ANISOU 4227  O   PRO A 513     7573   7306   8204   -503     76    223       O  
ATOM   4228  CB  PRO A 513      -9.295 -46.871  40.103  1.00 62.67           C  
ANISOU 4228  CB  PRO A 513     8052   7564   8194   -486    164    214       C  
ATOM   4229  CG  PRO A 513      -9.807 -47.401  38.801  1.00 64.59           C  
ANISOU 4229  CG  PRO A 513     8416   7718   8409   -526     96    146       C  
ATOM   4230  CD  PRO A 513      -9.596 -48.878  38.877  1.00 65.66           C  
ANISOU 4230  CD  PRO A 513     8524   7803   8622   -543    174    147       C  
ATOM   4231  N   LEU A 514     -10.720 -47.197  43.139  1.00 57.31           N  
ANISOU 4231  N   LEU A 514     7084   6980   7712   -445    214    326       N  
ATOM   4232  CA  LEU A 514     -11.852 -46.834  43.987  1.00 56.80           C  
ANISOU 4232  CA  LEU A 514     6931   6929   7720   -439    208    342       C  
ATOM   4233  C   LEU A 514     -12.556 -45.574  43.479  1.00 57.37           C  
ANISOU 4233  C   LEU A 514     7005   7017   7777   -440    103    303       C  
ATOM   4234  O   LEU A 514     -11.911 -44.647  42.983  1.00 56.39           O  
ANISOU 4234  O   LEU A 514     6954   6928   7544   -428     62    293       O  
ATOM   4235  CB  LEU A 514     -11.382 -46.643  45.434  1.00 55.58           C  
ANISOU 4235  CB  LEU A 514     6758   6821   7540   -403    296    414       C  
ATOM   4236  CG  LEU A 514     -11.392 -47.822  46.420  1.00 57.57           C  
ANISOU 4236  CG  LEU A 514     6986   7038   7851   -399    396    465       C  
ATOM   4237  CD1 LEU A 514     -11.663 -49.182  45.767  1.00 59.38           C  
ANISOU 4237  CD1 LEU A 514     7195   7197   8170   -432    410    438       C  
ATOM   4238  CD2 LEU A 514     -10.107 -47.863  47.241  1.00 56.01           C  
ANISOU 4238  CD2 LEU A 514     6842   6867   7574   -363    430    527       C  
ATOM   4239  N   ASP A 515     -13.879 -45.550  43.593  1.00 57.78           N  
ANISOU 4239  N   ASP A 515     6970   7029   7957   -453     64    280       N  
ATOM   4240  CA  ASP A 515     -14.658 -44.394  43.170  1.00 58.54           C  
ANISOU 4240  CA  ASP A 515     7045   7122   8074   -451    -48    245       C  
ATOM   4241  C   ASP A 515     -14.744 -43.414  44.337  1.00 56.45           C  
ANISOU 4241  C   ASP A 515     6731   6915   7801   -419     25    287       C  
ATOM   4242  O   ASP A 515     -15.535 -43.619  45.262  1.00 57.74           O  
ANISOU 4242  O   ASP A 515     6801   7050   8086   -418    110    306       O  
ATOM   4243  CB  ASP A 515     -16.055 -44.836  42.713  1.00 61.32           C  
ANISOU 4243  CB  ASP A 515     7306   7379   8615   -480   -141    193       C  
ATOM   4244  CG  ASP A 515     -16.880 -43.696  42.119  1.00 66.47           C  
ANISOU 4244  CG  ASP A 515     7937   8003   9314   -477   -297    151       C  
ATOM   4245  OD1 ASP A 515     -17.979 -43.992  41.590  1.00 67.92           O  
ANISOU 4245  OD1 ASP A 515     8048   8091   9668   -500   -418    101       O  
ATOM   4246  OD2 ASP A 515     -16.448 -42.518  42.178  1.00 66.37           O  
ANISOU 4246  OD2 ASP A 515     7976   8055   9187   -452   -311    166       O  
ATOM   4247  N   VAL A 516     -13.917 -42.367  44.293  1.00 51.55           N  
ANISOU 4247  N   VAL A 516     6183   6362   7040   -396      7    301       N  
ATOM   4248  CA  VAL A 516     -13.823 -41.388  45.391  1.00 49.44           C  
ANISOU 4248  CA  VAL A 516     5898   6151   6737   -365     71    339       C  
ATOM   4249  C   VAL A 516     -13.680 -39.951  44.887  1.00 47.55           C  
ANISOU 4249  C   VAL A 516     5698   5950   6419   -351    -17    319       C  
ATOM   4250  O   VAL A 516     -13.200 -39.718  43.775  1.00 47.54           O  
ANISOU 4250  O   VAL A 516     5777   5945   6340   -359   -101    290       O  
ATOM   4251  CB  VAL A 516     -12.660 -41.704  46.389  1.00 49.12           C  
ANISOU 4251  CB  VAL A 516     5909   6155   6599   -343    173    399       C  
ATOM   4252  CG1 VAL A 516     -12.994 -42.903  47.263  1.00 49.67           C  
ANISOU 4252  CG1 VAL A 516     5946   6182   6744   -349    280    434       C  
ATOM   4253  CG2 VAL A 516     -11.332 -41.939  45.658  1.00 47.02           C  
ANISOU 4253  CG2 VAL A 516     5719   5907   6239   -342    145    397       C  
ATOM   4254  N   ASP A 517     -14.120 -38.997  45.705  1.00 46.08           N  
ANISOU 4254  N   ASP A 517     5469   5787   6253   -330     16    334       N  
ATOM   4255  CA  ASP A 517     -13.875 -37.582  45.453  1.00 45.57           C  
ANISOU 4255  CA  ASP A 517     5441   5764   6108   -311    -47    324       C  
ATOM   4256  C   ASP A 517     -12.633 -37.202  46.245  1.00 45.08           C  
ANISOU 4256  C   ASP A 517     5443   5769   5915   -287     22    367       C  
ATOM   4257  O   ASP A 517     -12.606 -37.301  47.479  1.00 45.17           O  
ANISOU 4257  O   ASP A 517     5447   5792   5923   -273    115    405       O  
ATOM   4258  CB  ASP A 517     -15.085 -36.724  45.846  1.00 47.27           C  
ANISOU 4258  CB  ASP A 517     5567   5953   6439   -303    -56    309       C  
ATOM   4259  CG  ASP A 517     -14.910 -35.241  45.507  1.00 46.99           C  
ANISOU 4259  CG  ASP A 517     5569   5954   6331   -284   -132    297       C  
ATOM   4260  OD1 ASP A 517     -15.941 -34.546  45.396  1.00 48.43           O  
ANISOU 4260  OD1 ASP A 517     5678   6096   6627   -279   -185    272       O  
ATOM   4261  OD2 ASP A 517     -13.765 -34.756  45.357  1.00 45.41           O  
ANISOU 4261  OD2 ASP A 517     5461   5811   5982   -272   -136    311       O  
ATOM   4262  N   TYR A 518     -11.609 -36.770  45.514  1.00 43.14           N  
ANISOU 4262  N   TYR A 518     5272   5550   5568   -284    -25    359       N  
ATOM   4263  CA  TYR A 518     -10.269 -36.598  46.055  1.00 43.01           C  
ANISOU 4263  CA  TYR A 518     5301   5574   5467   -266     19    392       C  
ATOM   4264  C   TYR A 518     -10.079 -35.319  46.857  1.00 44.04           C  
ANISOU 4264  C   TYR A 518     5440   5749   5546   -240     21    407       C  
ATOM   4265  O   TYR A 518      -9.065 -35.168  47.553  1.00 43.95           O  
ANISOU 4265  O   TYR A 518     5457   5759   5483   -222     41    436       O  
ATOM   4266  CB  TYR A 518      -9.235 -36.690  44.925  1.00 42.60           C  
ANISOU 4266  CB  TYR A 518     5315   5507   5363   -277     -2    372       C  
ATOM   4267  CG  TYR A 518      -9.112 -38.087  44.373  1.00 40.16           C  
ANISOU 4267  CG  TYR A 518     5016   5150   5092   -300     22    364       C  
ATOM   4268  CD1 TYR A 518      -9.917 -38.515  43.316  1.00 41.56           C  
ANISOU 4268  CD1 TYR A 518     5220   5279   5294   -327    -32    323       C  
ATOM   4269  CD2 TYR A 518      -8.207 -38.994  44.928  1.00 36.76           C  
ANISOU 4269  CD2 TYR A 518     4573   4712   4681   -293     86    397       C  
ATOM   4270  CE1 TYR A 518      -9.816 -39.821  42.816  1.00 44.12           C  
ANISOU 4270  CE1 TYR A 518     5562   5553   5651   -350     -9    311       C  
ATOM   4271  CE2 TYR A 518      -8.092 -40.289  44.441  1.00 37.88           C  
ANISOU 4271  CE2 TYR A 518     4721   4805   4865   -314    117    389       C  
ATOM   4272  CZ  TYR A 518      -8.897 -40.698  43.388  1.00 42.47           C  
ANISOU 4272  CZ  TYR A 518     5332   5343   5460   -344     77    345       C  
ATOM   4273  OH  TYR A 518      -8.780 -41.982  42.915  1.00 43.88           O  
ANISOU 4273  OH  TYR A 518     5526   5468   5678   -366    110    333       O  
ATOM   4274  N   ARG A 519     -11.053 -34.411  46.760  1.00 42.11           N  
ANISOU 4274  N   ARG A 519     5166   5505   5328   -237    -10    385       N  
ATOM   4275  CA  ARG A 519     -11.024 -33.146  47.491  1.00 41.41           C  
ANISOU 4275  CA  ARG A 519     5085   5450   5197   -214     -2    393       C  
ATOM   4276  C   ARG A 519     -11.195 -33.363  48.990  1.00 43.53           C  
ANISOU 4276  C   ARG A 519     5360   5719   5462   -200     87    429       C  
ATOM   4277  O   ARG A 519     -11.152 -32.405  49.771  1.00 45.19           O  
ANISOU 4277  O   ARG A 519     5599   5948   5624   -181    107    436       O  
ATOM   4278  CB  ARG A 519     -12.128 -32.211  46.992  1.00 40.57           C  
ANISOU 4278  CB  ARG A 519     4937   5328   5148   -214    -55    360       C  
ATOM   4279  CG  ARG A 519     -12.043 -31.857  45.514  1.00 36.87           C  
ANISOU 4279  CG  ARG A 519     4509   4844   4658   -225   -161    327       C  
ATOM   4280  CD  ARG A 519     -13.256 -31.056  45.062  1.00 34.88           C  
ANISOU 4280  CD  ARG A 519     4211   4555   4487   -222   -244    297       C  
ATOM   4281  NE  ARG A 519     -14.502 -31.816  45.207  1.00 35.63           N  
ANISOU 4281  NE  ARG A 519     4206   4591   4739   -235   -246    284       N  
ATOM   4282  CZ  ARG A 519     -15.708 -31.268  45.331  1.00 35.72           C  
ANISOU 4282  CZ  ARG A 519     4124   4555   4893   -228   -277    264       C  
ATOM   4283  NH1 ARG A 519     -15.853 -29.955  45.327  1.00 38.12           N  
ANISOU 4283  NH1 ARG A 519     4430   4870   5185   -208   -315    257       N  
ATOM   4284  NH2 ARG A 519     -16.778 -32.034  45.461  1.00 38.95           N  
ANISOU 4284  NH2 ARG A 519     4426   4894   5479   -242   -267    248       N  
ATOM   4285  N   PHE A 520     -11.403 -34.616  49.389  1.00 42.50           N  
ANISOU 4285  N   PHE A 520     5221   5556   5372   -210    146    450       N  
ATOM   4286  CA  PHE A 520     -11.648 -34.939  50.786  1.00 43.63           C  
ANISOU 4286  CA  PHE A 520     5406   5675   5497   -199    246    487       C  
ATOM   4287  C   PHE A 520     -10.669 -35.993  51.265  1.00 43.68           C  
ANISOU 4287  C   PHE A 520     5475   5673   5449   -193    253    528       C  
ATOM   4288  O   PHE A 520     -10.337 -36.904  50.509  1.00 44.62           O  
ANISOU 4288  O   PHE A 520     5561   5784   5608   -208    226    524       O  
ATOM   4289  CB  PHE A 520     -13.083 -35.435  50.969  1.00 44.91           C  
ANISOU 4289  CB  PHE A 520     5498   5776   5790   -215    338    476       C  
ATOM   4290  CG  PHE A 520     -14.127 -34.503  50.412  1.00 46.65           C  
ANISOU 4290  CG  PHE A 520     5630   5982   6114   -220    310    432       C  
ATOM   4291  CD1 PHE A 520     -14.297 -33.223  50.944  1.00 43.27           C  
ANISOU 4291  CD1 PHE A 520     5222   5567   5652   -201    333    426       C  
ATOM   4292  CD2 PHE A 520     -14.952 -34.911  49.358  1.00 49.98           C  
ANISOU 4292  CD2 PHE A 520     5950   6364   6678   -241    248    394       C  
ATOM   4293  CE1 PHE A 520     -15.263 -32.351  50.429  1.00 43.63           C  
ANISOU 4293  CE1 PHE A 520     5175   5588   5813   -202    299    387       C  
ATOM   4294  CE2 PHE A 520     -15.933 -34.049  48.833  1.00 49.12           C  
ANISOU 4294  CE2 PHE A 520     5754   6223   6687   -242    190    354       C  
ATOM   4295  CZ  PHE A 520     -16.084 -32.766  49.370  1.00 48.58           C  
ANISOU 4295  CZ  PHE A 520     5694   6169   6594   -221    219    352       C  
ATOM   4296  N   ASP A 521     -10.204 -35.865  52.510  1.00 43.47           N  
ANISOU 4296  N   ASP A 521     5550   5636   5331   -172    280    567       N  
ATOM   4297  CA  ASP A 521      -9.295 -36.856  53.099  1.00 43.79           C  
ANISOU 4297  CA  ASP A 521     5663   5650   5326   -161    264    613       C  
ATOM   4298  C   ASP A 521      -9.917 -38.257  53.071  1.00 43.38           C  
ANISOU 4298  C   ASP A 521     5586   5549   5347   -179    346    629       C  
ATOM   4299  O   ASP A 521     -11.088 -38.446  53.407  1.00 39.58           O  
ANISOU 4299  O   ASP A 521     5092   5029   4918   -192    457    625       O  
ATOM   4300  CB  ASP A 521      -8.902 -36.483  54.538  1.00 45.26           C  
ANISOU 4300  CB  ASP A 521     5999   5808   5389   -134    265    652       C  
ATOM   4301  CG  ASP A 521      -7.927 -35.312  54.600  1.00 48.98           C  
ANISOU 4301  CG  ASP A 521     6498   6316   5798   -115    150    640       C  
ATOM   4302  OD1 ASP A 521      -6.770 -35.453  54.135  1.00 45.36           O  
ANISOU 4302  OD1 ASP A 521     6001   5868   5367   -108     47    640       O  
ATOM   4303  OD2 ASP A 521      -8.321 -34.249  55.134  1.00 52.39           O  
ANISOU 4303  OD2 ASP A 521     6984   6755   6167   -107    172    628       O  
ATOM   4304  N   PHE A 522      -9.126 -39.234  52.646  1.00 43.18           N  
ANISOU 4304  N   PHE A 522     5543   5515   5348   -182    301    643       N  
ATOM   4305  CA  PHE A 522      -9.581 -40.607  52.625  1.00 41.78           C  
ANISOU 4305  CA  PHE A 522     5348   5289   5239   -198    372    659       C  
ATOM   4306  C   PHE A 522     -10.019 -41.021  54.013  1.00 44.53           C  
ANISOU 4306  C   PHE A 522     5812   5577   5532   -188    471    709       C  
ATOM   4307  O   PHE A 522      -9.379 -40.660  55.007  1.00 45.50           O  
ANISOU 4307  O   PHE A 522     6065   5685   5537   -160    437    747       O  
ATOM   4308  CB  PHE A 522      -8.470 -41.528  52.130  1.00 39.66           C  
ANISOU 4308  CB  PHE A 522     5062   5011   4996   -196    309    672       C  
ATOM   4309  CG  PHE A 522      -8.151 -41.363  50.668  1.00 39.33           C  
ANISOU 4309  CG  PHE A 522     4932   5001   5012   -215    257    621       C  
ATOM   4310  CD1 PHE A 522      -9.156 -41.048  49.748  1.00 39.90           C  
ANISOU 4310  CD1 PHE A 522     4941   5086   5132   -241    268    570       C  
ATOM   4311  CD2 PHE A 522      -6.853 -41.540  50.207  1.00 32.66           C  
ANISOU 4311  CD2 PHE A 522     4077   4152   4182   -206    199    621       C  
ATOM   4312  CE1 PHE A 522      -8.869 -40.899  48.385  1.00 41.13           C  
ANISOU 4312  CE1 PHE A 522     5065   5252   5310   -259    217    523       C  
ATOM   4313  CE2 PHE A 522      -6.549 -41.405  48.854  1.00 38.58           C  
ANISOU 4313  CE2 PHE A 522     4780   4908   4969   -226    185    572       C  
ATOM   4314  CZ  PHE A 522      -7.560 -41.084  47.933  1.00 38.97           C  
ANISOU 4314  CZ  PHE A 522     4807   4973   5027   -253    192    525       C  
ATOM   4315  N   SER A 523     -11.126 -41.760  54.075  1.00 45.80           N  
ANISOU 4315  N   SER A 523     5937   5685   5780   -211    595    708       N  
ATOM   4316  CA  SER A 523     -11.562 -42.399  55.310  1.00 46.22           C  
ANISOU 4316  CA  SER A 523     6115   5655   5791   -206    728    758       C  
ATOM   4317  C   SER A 523     -10.656 -43.587  55.613  1.00 48.75           C  
ANISOU 4317  C   SER A 523     6511   5941   6072   -193    685    811       C  
ATOM   4318  O   SER A 523     -10.003 -44.132  54.710  1.00 47.04           O  
ANISOU 4318  O   SER A 523     6203   5754   5918   -198    595    797       O  
ATOM   4319  CB  SER A 523     -13.023 -42.851  55.206  1.00 46.40           C  
ANISOU 4319  CB  SER A 523     6050   5616   5965   -238    888    735       C  
ATOM   4320  OG  SER A 523     -13.163 -43.983  54.369  1.00 45.62           O  
ANISOU 4320  OG  SER A 523     5841   5502   5989   -262    876    720       O  
ATOM   4321  N   ASP A 524     -10.617 -43.975  56.887  1.00 51.18           N  
ANISOU 4321  N   ASP A 524     7000   6172   6274   -176    754    870       N  
ATOM   4322  CA  ASP A 524      -9.822 -45.112  57.326  1.00 54.33           C  
ANISOU 4322  CA  ASP A 524     7494   6516   6633   -159    708    929       C  
ATOM   4323  C   ASP A 524     -10.183 -46.374  56.546  1.00 54.62           C  
ANISOU 4323  C   ASP A 524     7401   6533   6819   -187    765    919       C  
ATOM   4324  O   ASP A 524      -9.298 -47.085  56.068  1.00 54.29           O  
ANISOU 4324  O   ASP A 524     7315   6499   6815   -179    666    930       O  
ATOM   4325  CB  ASP A 524      -9.971 -45.327  58.840  1.00 57.74           C  
ANISOU 4325  CB  ASP A 524     8181   6845   6913   -140    794    996       C  
ATOM   4326  CG  ASP A 524      -9.376 -44.184  59.659  1.00 62.01           C  
ANISOU 4326  CG  ASP A 524     8888   7391   7282   -109    694   1009       C  
ATOM   4327  OD1 ASP A 524      -8.590 -43.372  59.109  1.00 61.33           O  
ANISOU 4327  OD1 ASP A 524     8711   7385   7205    -96    532    977       O  
ATOM   4328  OD2 ASP A 524      -9.694 -44.100  60.864  1.00 66.42           O  
ANISOU 4328  OD2 ASP A 524     9683   7860   7695    -98    786   1050       O  
ATOM   4329  N   GLU A 525     -11.483 -46.627  56.403  1.00 56.78           N  
ANISOU 4329  N   GLU A 525     7605   6772   7198   -219    926    893       N  
ATOM   4330  CA  GLU A 525     -11.996 -47.743  55.606  1.00 58.10           C  
ANISOU 4330  CA  GLU A 525     7636   6913   7527   -252    978    871       C  
ATOM   4331  C   GLU A 525     -11.379 -47.724  54.205  1.00 56.54           C  
ANISOU 4331  C   GLU A 525     7290   6795   7398   -261    829    819       C  
ATOM   4332  O   GLU A 525     -10.841 -48.740  53.746  1.00 57.05           O  
ANISOU 4332  O   GLU A 525     7324   6844   7510   -265    793    828       O  
ATOM   4333  CB  GLU A 525     -13.526 -47.673  55.532  1.00 60.74           C  
ANISOU 4333  CB  GLU A 525     7877   7197   8005   -287   1142    831       C  
ATOM   4334  CG  GLU A 525     -14.231 -48.984  55.169  1.00 66.30           C  
ANISOU 4334  CG  GLU A 525     8486   7825   8878   -321   1239    823       C  
ATOM   4335  CD  GLU A 525     -15.736 -48.943  55.432  1.00 69.47           C  
ANISOU 4335  CD  GLU A 525     8813   8137   9445   -351   1429    795       C  
ATOM   4336  OE1 GLU A 525     -16.138 -48.869  56.615  1.00 72.58           O  
ANISOU 4336  OE1 GLU A 525     9346   8447   9784   -344   1605    837       O  
ATOM   4337  OE2 GLU A 525     -16.517 -48.996  54.458  1.00 69.60           O  
ANISOU 4337  OE2 GLU A 525     8639   8150   9657   -383   1402    728       O  
ATOM   4338  N   ILE A 526     -11.437 -46.561  53.551  1.00 53.10           N  
ANISOU 4338  N   ILE A 526     6783   6433   6961   -263    755    768       N  
ATOM   4339  CA  ILE A 526     -10.831 -46.367  52.235  1.00 51.56           C  
ANISOU 4339  CA  ILE A 526     6491   6300   6801   -272    630    719       C  
ATOM   4340  C   ILE A 526      -9.318 -46.606  52.255  1.00 52.23           C  
ANISOU 4340  C   ILE A 526     6624   6398   6821   -244    533    750       C  
ATOM   4341  O   ILE A 526      -8.784 -47.253  51.352  1.00 53.68           O  
ANISOU 4341  O   ILE A 526     6749   6580   7068   -256    495    729       O  
ATOM   4342  CB  ILE A 526     -11.165 -44.958  51.642  1.00 51.24           C  
ANISOU 4342  CB  ILE A 526     6396   6323   6752   -275    572    666       C  
ATOM   4343  CG1 ILE A 526     -12.574 -44.935  51.033  1.00 50.43           C  
ANISOU 4343  CG1 ILE A 526     6183   6192   6785   -309    616    613       C  
ATOM   4344  CG2 ILE A 526     -10.132 -44.522  50.599  1.00 49.88           C  
ANISOU 4344  CG2 ILE A 526     6196   6206   6549   -271    450    635       C  
ATOM   4345  CD1 ILE A 526     -12.750 -45.800  49.781  1.00 49.03           C  
ANISOU 4345  CD1 ILE A 526     5922   5994   6712   -340    565    567       C  
ATOM   4346  N   LYS A 527      -8.637 -46.093  53.280  1.00 51.45           N  
ANISOU 4346  N   LYS A 527     6637   6299   6614   -209    491    797       N  
ATOM   4347  CA  LYS A 527      -7.185 -46.262  53.404  1.00 52.67           C  
ANISOU 4347  CA  LYS A 527     6822   6446   6746   -179    376    827       C  
ATOM   4348  C   LYS A 527      -6.763 -47.725  53.551  1.00 54.65           C  
ANISOU 4348  C   LYS A 527     7086   6626   7054   -175    389    868       C  
ATOM   4349  O   LYS A 527      -5.693 -48.122  53.077  1.00 54.16           O  
ANISOU 4349  O   LYS A 527     6974   6549   7056   -164    315    867       O  
ATOM   4350  CB  LYS A 527      -6.623 -45.424  54.554  1.00 51.72           C  
ANISOU 4350  CB  LYS A 527     6831   6319   6503   -142    300    867       C  
ATOM   4351  CG  LYS A 527      -6.422 -43.963  54.181  1.00 51.27           C  
ANISOU 4351  CG  LYS A 527     6735   6333   6414   -139    237    822       C  
ATOM   4352  CD  LYS A 527      -5.706 -43.182  55.261  1.00 52.70           C  
ANISOU 4352  CD  LYS A 527     7042   6498   6486   -103    135    856       C  
ATOM   4353  CE  LYS A 527      -6.627 -42.834  56.409  1.00 55.22           C  
ANISOU 4353  CE  LYS A 527     7516   6789   6677    -99    221    883       C  
ATOM   4354  NZ  LYS A 527      -6.026 -41.749  57.226  1.00 57.56           N  
ANISOU 4354  NZ  LYS A 527     7932   7083   6857    -70    113    893       N  
ATOM   4355  N   GLU A 528      -7.614 -48.513  54.206  1.00 56.20           N  
ANISOU 4355  N   GLU A 528     7345   6766   7241   -184    497    902       N  
ATOM   4356  CA  GLU A 528      -7.382 -49.936  54.375  1.00 56.90           C  
ANISOU 4356  CA  GLU A 528     7453   6780   7385   -182    527    943       C  
ATOM   4357  C   GLU A 528      -7.484 -50.609  53.029  1.00 56.19           C  
ANISOU 4357  C   GLU A 528     7214   6704   7430   -216    550    887       C  
ATOM   4358  O   GLU A 528      -6.647 -51.439  52.690  1.00 57.42           O  
ANISOU 4358  O   GLU A 528     7341   6826   7652   -209    512    898       O  
ATOM   4359  CB  GLU A 528      -8.387 -50.553  55.359  1.00 58.81           C  
ANISOU 4359  CB  GLU A 528     7806   6949   7590   -190    669    989       C  
ATOM   4360  CG  GLU A 528      -8.204 -50.125  56.825  1.00 62.72           C  
ANISOU 4360  CG  GLU A 528     8518   7394   7920   -154    658   1055       C  
ATOM   4361  CD  GLU A 528      -6.790 -50.372  57.360  1.00 66.28           C  
ANISOU 4361  CD  GLU A 528     9066   7805   8314   -108    484   1111       C  
ATOM   4362  OE1 GLU A 528      -6.257 -49.492  58.070  1.00 68.04           O  
ANISOU 4362  OE1 GLU A 528     9406   8026   8418    -78    376   1131       O  
ATOM   4363  OE2 GLU A 528      -6.209 -51.440  57.068  1.00 65.08           O  
ANISOU 4363  OE2 GLU A 528     8867   7610   8251   -102    445   1132       O  
ATOM   4364  N   LYS A 529      -8.501 -50.227  52.258  1.00 56.19           N  
ANISOU 4364  N   LYS A 529     7131   6744   7476   -253    604    825       N  
ATOM   4365  CA  LYS A 529      -8.735 -50.799  50.928  1.00 56.76           C  
ANISOU 4365  CA  LYS A 529     7094   6817   7656   -289    612    764       C  
ATOM   4366  C   LYS A 529      -7.602 -50.473  49.946  1.00 56.42           C  
ANISOU 4366  C   LYS A 529     7012   6806   7619   -284    524    728       C  
ATOM   4367  O   LYS A 529      -7.247 -51.297  49.101  1.00 56.65           O  
ANISOU 4367  O   LYS A 529     7001   6802   7722   -301    534    702       O  
ATOM   4368  CB  LYS A 529     -10.084 -50.340  50.367  1.00 57.06           C  
ANISOU 4368  CB  LYS A 529     7063   6872   7746   -325    649    704       C  
ATOM   4369  CG  LYS A 529     -11.282 -51.071  50.952  1.00 60.64           C  
ANISOU 4369  CG  LYS A 529     7505   7257   8279   -346    771    719       C  
ATOM   4370  CD  LYS A 529     -12.608 -50.500  50.455  1.00 62.32           C  
ANISOU 4370  CD  LYS A 529     7623   7469   8586   -378    790    658       C  
ATOM   4371  CE  LYS A 529     -13.768 -51.398  50.875  1.00 65.82           C  
ANISOU 4371  CE  LYS A 529     8020   7818   9170   -405    924    662       C  
ATOM   4372  NZ  LYS A 529     -15.063 -50.667  50.876  1.00 65.72           N  
ANISOU 4372  NZ  LYS A 529     7922   7781   9269   -424    967    619       N  
ATOM   4373  N   ILE A 530      -7.037 -49.277  50.082  1.00 54.78           N  
ANISOU 4373  N   ILE A 530     6824   6649   7341   -262    455    726       N  
ATOM   4374  CA  ILE A 530      -5.928 -48.828  49.248  1.00 55.50           C  
ANISOU 4374  CA  ILE A 530     6882   6756   7450   -256    397    695       C  
ATOM   4375  C   ILE A 530      -4.695 -49.719  49.426  1.00 56.66           C  
ANISOU 4375  C   ILE A 530     7019   6837   7670   -233    378    730       C  
ATOM   4376  O   ILE A 530      -3.942 -49.947  48.477  1.00 55.59           O  
ANISOU 4376  O   ILE A 530     6837   6675   7610   -243    390    694       O  
ATOM   4377  CB  ILE A 530      -5.588 -47.339  49.524  1.00 54.77           C  
ANISOU 4377  CB  ILE A 530     6809   6720   7279   -235    331    691       C  
ATOM   4378  CG1 ILE A 530      -6.722 -46.437  49.027  1.00 54.61           C  
ANISOU 4378  CG1 ILE A 530     6777   6755   7216   -259    344    643       C  
ATOM   4379  CG2 ILE A 530      -4.282 -46.929  48.851  1.00 54.15           C  
ANISOU 4379  CG2 ILE A 530     6695   6633   7245   -225    288    667       C  
ATOM   4380  CD1 ILE A 530      -6.530 -44.972  49.359  1.00 52.63           C  
ANISOU 4380  CD1 ILE A 530     6549   6559   6888   -239    290    640       C  
ATOM   4381  N   LYS A 531      -4.512 -50.235  50.637  1.00 59.18           N  
ANISOU 4381  N   LYS A 531     7396   7116   7975   -203    356    800       N  
ATOM   4382  CA  LYS A 531      -3.368 -51.089  50.953  1.00 61.88           C  
ANISOU 4382  CA  LYS A 531     7730   7380   8403   -174    310    843       C  
ATOM   4383  C   LYS A 531      -3.441 -52.488  50.327  1.00 61.53           C  
ANISOU 4383  C   LYS A 531     7640   7277   8462   -197    390    833       C  
ATOM   4384  O   LYS A 531      -2.460 -53.221  50.358  1.00 63.20           O  
ANISOU 4384  O   LYS A 531     7821   7416   8778   -176    363    857       O  
ATOM   4385  CB  LYS A 531      -3.170 -51.184  52.469  1.00 64.98           C  
ANISOU 4385  CB  LYS A 531     8234   7731   8725   -133    235    925       C  
ATOM   4386  CG  LYS A 531      -2.733 -49.871  53.112  1.00 68.45           C  
ANISOU 4386  CG  LYS A 531     8725   8202   9079   -104    126    935       C  
ATOM   4387  CD  LYS A 531      -2.622 -50.008  54.619  1.00 73.55           C  
ANISOU 4387  CD  LYS A 531     9532   8789   9624    -65     45   1014       C  
ATOM   4388  CE  LYS A 531      -2.019 -48.760  55.240  1.00 75.33           C  
ANISOU 4388  CE  LYS A 531     9815   9029   9777    -36    -92   1019       C  
ATOM   4389  NZ  LYS A 531      -1.500 -49.052  56.605  1.00 79.98           N  
ANISOU 4389  NZ  LYS A 531    10573   9523  10293      9   -227   1097       N  
ATOM   4390  N   LYS A 532      -4.584 -52.843  49.743  1.00 60.84           N  
ANISOU 4390  N   LYS A 532     7541   7210   8364   -239    478    794       N  
ATOM   4391  CA  LYS A 532      -4.754 -54.146  49.095  1.00 60.82           C  
ANISOU 4391  CA  LYS A 532     7503   7150   8456   -265    551    775       C  
ATOM   4392  C   LYS A 532      -4.965 -54.037  47.575  1.00 58.87           C  
ANISOU 4392  C   LYS A 532     7214   6917   8237   -309    589    686       C  
ATOM   4393  O   LYS A 532      -5.430 -54.981  46.927  1.00 57.31           O  
ANISOU 4393  O   LYS A 532     7003   6677   8094   -342    647    653       O  
ATOM   4394  CB  LYS A 532      -5.909 -54.914  49.752  1.00 62.25           C  
ANISOU 4394  CB  LYS A 532     7719   7307   8626   -280    618    807       C  
ATOM   4395  CG  LYS A 532      -5.592 -55.431  51.150  1.00 67.74           C  
ANISOU 4395  CG  LYS A 532     8498   7946   9293   -240    603    900       C  
ATOM   4396  CD  LYS A 532      -6.862 -55.810  51.916  1.00 72.41           C  
ANISOU 4396  CD  LYS A 532     9151   8514   9847   -255    700    931       C  
ATOM   4397  CE  LYS A 532      -6.550 -56.167  53.371  1.00 75.97           C  
ANISOU 4397  CE  LYS A 532     9743   8898  10223   -213    687   1028       C  
ATOM   4398  NZ  LYS A 532      -7.781 -56.418  54.187  1.00 78.97           N  
ANISOU 4398  NZ  LYS A 532    10210   9238  10557   -230    820   1059       N  
ATOM   4399  N   LEU A 533      -4.615 -52.885  47.011  1.00 56.67           N  
ANISOU 4399  N   LEU A 533     6933   6685   7913   -309    554    646       N  
ATOM   4400  CA  LEU A 533      -4.835 -52.641  45.592  1.00 56.21           C  
ANISOU 4400  CA  LEU A 533     6885   6629   7845   -348    581    565       C  
ATOM   4401  C   LEU A 533      -3.603 -52.952  44.765  1.00 55.50           C  
ANISOU 4401  C   LEU A 533     6787   6472   7829   -349    632    536       C  
ATOM   4402  O   LEU A 533      -2.488 -52.924  45.284  1.00 55.68           O  
ANISOU 4402  O   LEU A 533     6768   6463   7923   -314    621    575       O  
ATOM   4403  CB  LEU A 533      -5.259 -51.191  45.350  1.00 55.61           C  
ANISOU 4403  CB  LEU A 533     6831   6627   7670   -352    529    535       C  
ATOM   4404  CG  LEU A 533      -6.695 -50.791  45.677  1.00 55.53           C  
ANISOU 4404  CG  LEU A 533     6822   6665   7611   -366    499    530       C  
ATOM   4405  CD1 LEU A 533      -6.843 -49.294  45.519  1.00 54.41           C  
ANISOU 4405  CD1 LEU A 533     6698   6589   7386   -360    443    508       C  
ATOM   4406  CD2 LEU A 533      -7.691 -51.529  44.789  1.00 55.46           C  
ANISOU 4406  CD2 LEU A 533     6813   6616   7642   -411    512    475       C  
ATOM   4407  N   SER A 534      -3.821 -53.238  43.481  1.00 55.49           N  
ANISOU 4407  N   SER A 534     6832   6432   7819   -390    686    466       N  
ATOM   4408  CA  SER A 534      -2.741 -53.443  42.514  1.00 58.25           C  
ANISOU 4408  CA  SER A 534     7204   6700   8228   -399    775    424       C  
ATOM   4409  C   SER A 534      -2.180 -52.117  42.011  1.00 59.93           C  
ANISOU 4409  C   SER A 534     7451   6932   8388   -396    779    395       C  
ATOM   4410  O   SER A 534      -2.878 -51.100  42.000  1.00 59.19           O  
ANISOU 4410  O   SER A 534     7393   6915   8182   -400    708    385       O  
ATOM   4411  CB  SER A 534      -3.235 -54.257  41.314  1.00 59.28           C  
ANISOU 4411  CB  SER A 534     7418   6765   8340   -448    837    356       C  
ATOM   4412  OG  SER A 534      -4.097 -53.483  40.488  1.00 58.97           O  
ANISOU 4412  OG  SER A 534     7477   6758   8170   -480    786    299       O  
ATOM   4413  N   ALA A 535      -0.925 -52.149  41.566  1.00 62.20           N  
ANISOU 4413  N   ALA A 535     7722   7137   8776   -389    874    379       N  
ATOM   4414  CA  ALA A 535      -0.258 -50.974  41.003  1.00 62.08           C  
ANISOU 4414  CA  ALA A 535     7739   7111   8738   -389    915    348       C  
ATOM   4415  C   ALA A 535      -1.101 -50.279  39.929  1.00 62.16           C  
ANISOU 4415  C   ALA A 535     7900   7145   8572   -428    913    287       C  
ATOM   4416  O   ALA A 535      -1.149 -49.049  39.880  1.00 62.75           O  
ANISOU 4416  O   ALA A 535     8002   7271   8569   -421    872    282       O  
ATOM   4417  CB  ALA A 535       1.119 -51.356  40.452  1.00 61.93           C  
ANISOU 4417  CB  ALA A 535     7687   6957   8885   -388   1067    325       C  
ATOM   4418  N   LYS A 536      -1.770 -51.070  39.089  1.00 62.28           N  
ANISOU 4418  N   LYS A 536     8019   7115   8528   -466    941    241       N  
ATOM   4419  CA  LYS A 536      -2.629 -50.547  38.024  1.00 63.98           C  
ANISOU 4419  CA  LYS A 536     8402   7329   8578   -503    902    182       C  
ATOM   4420  C   LYS A 536      -3.727 -49.641  38.589  1.00 62.22           C  
ANISOU 4420  C   LYS A 536     8149   7225   8268   -492    740    203       C  
ATOM   4421  O   LYS A 536      -3.874 -48.493  38.164  1.00 60.93           O  
ANISOU 4421  O   LYS A 536     8063   7086   8002   -494    702    183       O  
ATOM   4422  CB  LYS A 536      -3.238 -51.698  37.207  1.00 66.41           C  
ANISOU 4422  CB  LYS A 536     8816   7561   8856   -544    919    132       C  
ATOM   4423  CG  LYS A 536      -3.890 -51.272  35.886  1.00 69.90           C  
ANISOU 4423  CG  LYS A 536     9480   7952   9126   -585    879     59       C  
ATOM   4424  CD  LYS A 536      -4.042 -52.460  34.939  1.00 74.74           C  
ANISOU 4424  CD  LYS A 536    10231   8446   9720   -627    937      1       C  
ATOM   4425  CE  LYS A 536      -5.059 -52.190  33.828  1.00 76.11           C  
ANISOU 4425  CE  LYS A 536    10626   8573   9720   -666    812    -67       C  
ATOM   4426  NZ  LYS A 536      -4.506 -51.392  32.699  1.00 76.30           N  
ANISOU 4426  NZ  LYS A 536    10892   8509   9591   -683    896   -113       N  
ATOM   4427  N   SER A 537      -4.481 -50.167  39.553  1.00 60.95           N  
ANISOU 4427  N   SER A 537     7879   7122   8156   -480    662    244       N  
ATOM   4428  CA  SER A 537      -5.527 -49.403  40.235  1.00 58.30           C  
ANISOU 4428  CA  SER A 537     7495   6883   7775   -468    539    267       C  
ATOM   4429  C   SER A 537      -4.953 -48.246  41.048  1.00 55.93           C  
ANISOU 4429  C   SER A 537     7133   6652   7464   -430    523    311       C  
ATOM   4430  O   SER A 537      -5.540 -47.164  41.088  1.00 56.66           O  
ANISOU 4430  O   SER A 537     7243   6804   7483   -426    447    305       O  
ATOM   4431  CB  SER A 537      -6.366 -50.311  41.137  1.00 56.99           C  
ANISOU 4431  CB  SER A 537     7233   6736   7683   -466    507    303       C  
ATOM   4432  OG  SER A 537      -7.094 -51.244  40.367  1.00 57.50           O  
ANISOU 4432  OG  SER A 537     7347   6737   7763   -505    495    254       O  
ATOM   4433  N   LEU A 538      -3.814 -48.478  41.693  1.00 53.53           N  
ANISOU 4433  N   LEU A 538     6759   6333   7249   -401    581    352       N  
ATOM   4434  CA  LEU A 538      -3.142 -47.434  42.459  1.00 54.07           C  
ANISOU 4434  CA  LEU A 538     6772   6448   7324   -365    550    389       C  
ATOM   4435  C   LEU A 538      -2.667 -46.286  41.565  1.00 53.16           C  
ANISOU 4435  C   LEU A 538     6727   6321   7152   -374    582    346       C  
ATOM   4436  O   LEU A 538      -2.918 -45.119  41.865  1.00 51.14           O  
ANISOU 4436  O   LEU A 538     6471   6131   6829   -361    517    354       O  
ATOM   4437  CB  LEU A 538      -1.967 -48.011  43.259  1.00 55.27           C  
ANISOU 4437  CB  LEU A 538     6833   6556   7612   -333    578    436       C  
ATOM   4438  CG  LEU A 538      -2.298 -48.819  44.517  1.00 55.67           C  
ANISOU 4438  CG  LEU A 538     6829   6625   7699   -309    523    500       C  
ATOM   4439  CD1 LEU A 538      -1.034 -49.458  45.060  1.00 57.00           C  
ANISOU 4439  CD1 LEU A 538     6925   6719   8014   -278    533    540       C  
ATOM   4440  CD2 LEU A 538      -2.953 -47.948  45.577  1.00 54.98           C  
ANISOU 4440  CD2 LEU A 538     6743   6625   7523   -287    432    539       C  
ATOM   4441  N   ASN A 539      -2.000 -46.625  40.463  1.00 53.38           N  
ANISOU 4441  N   ASN A 539     6828   6253   7202   -398    695    301       N  
ATOM   4442  CA  ASN A 539      -1.487 -45.624  39.540  1.00 53.46           C  
ANISOU 4442  CA  ASN A 539     6934   6224   7156   -410    761    260       C  
ATOM   4443  C   ASN A 539      -2.574 -44.750  38.911  1.00 54.18           C  
ANISOU 4443  C   ASN A 539     7150   6359   7076   -429    675    229       C  
ATOM   4444  O   ASN A 539      -2.395 -43.534  38.779  1.00 53.11           O  
ANISOU 4444  O   ASN A 539     7048   6247   6885   -421    663    225       O  
ATOM   4445  CB  ASN A 539      -0.605 -46.269  38.471  1.00 55.36           C  
ANISOU 4445  CB  ASN A 539     7256   6327   7452   -436    934    216       C  
ATOM   4446  CG  ASN A 539       0.840 -46.397  38.911  1.00 56.14           C  
ANISOU 4446  CG  ASN A 539     7222   6356   7751   -411   1037    237       C  
ATOM   4447  OD1 ASN A 539       1.367 -47.498  39.031  1.00 56.07           O  
ANISOU 4447  OD1 ASN A 539     7149   6277   7880   -409   1106    244       O  
ATOM   4448  ND2 ASN A 539       1.484 -45.264  39.170  1.00 59.04           N  
ANISOU 4448  ND2 ASN A 539     7539   6733   8158   -392   1039    246       N  
ATOM   4449  N   GLU A 540      -3.700 -45.365  38.546  1.00 54.88           N  
ANISOU 4449  N   GLU A 540     7300   6450   7101   -453    603    207       N  
ATOM   4450  CA  GLU A 540      -4.837 -44.618  38.011  1.00 56.07           C  
ANISOU 4450  CA  GLU A 540     7550   6630   7124   -467    482    179       C  
ATOM   4451  C   GLU A 540      -5.430 -43.696  39.077  1.00 53.12           C  
ANISOU 4451  C   GLU A 540     7059   6368   6756   -437    375    220       C  
ATOM   4452  O   GLU A 540      -5.766 -42.551  38.788  1.00 54.52           O  
ANISOU 4452  O   GLU A 540     7293   6571   6852   -434    312    208       O  
ATOM   4453  CB  GLU A 540      -5.899 -45.551  37.410  1.00 57.99           C  
ANISOU 4453  CB  GLU A 540     7865   6829   7340   -500    408    141       C  
ATOM   4454  CG  GLU A 540      -7.172 -44.842  36.877  1.00 67.46           C  
ANISOU 4454  CG  GLU A 540     9148   8037   8445   -513    241    109       C  
ATOM   4455  CD  GLU A 540      -6.923 -43.864  35.710  1.00 74.18           C  
ANISOU 4455  CD  GLU A 540    10211   8828   9146   -525    235     70       C  
ATOM   4456  OE1 GLU A 540      -6.069 -44.158  34.839  1.00 78.60           O  
ANISOU 4456  OE1 GLU A 540    10925   9292   9647   -545    364     41       O  
ATOM   4457  OE2 GLU A 540      -7.597 -42.804  35.656  1.00 74.11           O  
ANISOU 4457  OE2 GLU A 540    10223   8855   9079   -515    111     69       O  
ATOM   4458  N   MET A 541      -5.532 -44.187  40.310  1.00 51.46           N  
ANISOU 4458  N   MET A 541     6704   6213   6637   -415    363    269       N  
ATOM   4459  CA  MET A 541      -6.008 -43.366  41.421  1.00 47.23           C  
ANISOU 4459  CA  MET A 541     6077   5766   6101   -386    291    308       C  
ATOM   4460  C   MET A 541      -5.082 -42.182  41.661  1.00 46.46           C  
ANISOU 4460  C   MET A 541     5974   5697   5982   -362    310    322       C  
ATOM   4461  O   MET A 541      -5.546 -41.066  41.907  1.00 47.99           O  
ANISOU 4461  O   MET A 541     6167   5946   6123   -350    247    325       O  
ATOM   4462  CB  MET A 541      -6.139 -44.191  42.698  1.00 46.37           C  
ANISOU 4462  CB  MET A 541     5860   5685   6074   -368    300    361       C  
ATOM   4463  CG  MET A 541      -7.406 -45.010  42.784  1.00 47.15           C  
ANISOU 4463  CG  MET A 541     5933   5773   6207   -387    267    354       C  
ATOM   4464  SD  MET A 541      -7.642 -45.728  44.432  1.00 47.29           S  
ANISOU 4464  SD  MET A 541     5857   5816   6295   -363    299    424       S  
ATOM   4465  CE  MET A 541      -8.380 -44.359  45.320  1.00 41.06           C  
ANISOU 4465  CE  MET A 541     5044   5098   5460   -341    252    443       C  
ATOM   4466  N   LEU A 542      -3.775 -42.423  41.580  1.00 44.21           N  
ANISOU 4466  N   LEU A 542     5675   5361   5760   -355    400    328       N  
ATOM   4467  CA  LEU A 542      -2.792 -41.362  41.743  1.00 42.54           C  
ANISOU 4467  CA  LEU A 542     5443   5153   5567   -336    425    335       C  
ATOM   4468  C   LEU A 542      -3.007 -40.245  40.728  1.00 42.35           C  
ANISOU 4468  C   LEU A 542     5535   5119   5436   -352    428    294       C  
ATOM   4469  O   LEU A 542      -3.045 -39.069  41.099  1.00 41.86           O  
ANISOU 4469  O   LEU A 542     5456   5109   5339   -335    379    304       O  
ATOM   4470  CB  LEU A 542      -1.361 -41.908  41.647  1.00 42.00           C  
ANISOU 4470  CB  LEU A 542     5328   4997   5633   -331    532    337       C  
ATOM   4471  CG  LEU A 542      -0.270 -40.849  41.855  1.00 41.29           C  
ANISOU 4471  CG  LEU A 542     5188   4888   5611   -312    557    340       C  
ATOM   4472  CD1 LEU A 542      -0.464 -40.104  43.196  1.00 34.08           C  
ANISOU 4472  CD1 LEU A 542     4197   4066   4687   -277    426    383       C  
ATOM   4473  CD2 LEU A 542       1.153 -41.429  41.713  1.00 36.62           C  
ANISOU 4473  CD2 LEU A 542     4522   4182   5209   -308    669    335       C  
ATOM   4474  N   PHE A 543      -3.161 -40.628  39.459  1.00 43.22           N  
ANISOU 4474  N   PHE A 543     5782   5154   5485   -385    481    249       N  
ATOM   4475  CA  PHE A 543      -3.411 -39.689  38.371  1.00 42.67           C  
ANISOU 4475  CA  PHE A 543     5873   5051   5289   -403    477    210       C  
ATOM   4476  C   PHE A 543      -4.630 -38.822  38.659  1.00 42.51           C  
ANISOU 4476  C   PHE A 543     5848   5113   5192   -392    322    217       C  
ATOM   4477  O   PHE A 543      -4.612 -37.611  38.428  1.00 43.15           O  
ANISOU 4477  O   PHE A 543     5982   5206   5207   -385    299    212       O  
ATOM   4478  CB  PHE A 543      -3.588 -40.441  37.051  1.00 46.53           C  
ANISOU 4478  CB  PHE A 543     6543   5434   5701   -441    528    162       C  
ATOM   4479  CG  PHE A 543      -3.948 -39.556  35.881  1.00 51.54           C  
ANISOU 4479  CG  PHE A 543     7395   6013   6174   -460    501    124       C  
ATOM   4480  CD1 PHE A 543      -2.954 -38.899  35.156  1.00 55.21           C  
ANISOU 4480  CD1 PHE A 543     7985   6392   6599   -468    650    105       C  
ATOM   4481  CD2 PHE A 543      -5.278 -39.393  35.495  1.00 52.02           C  
ANISOU 4481  CD2 PHE A 543     7540   6088   6137   -468    326    106       C  
ATOM   4482  CE1 PHE A 543      -3.280 -38.085  34.069  1.00 58.57           C  
ANISOU 4482  CE1 PHE A 543     8647   6751   6855   -485    628     75       C  
ATOM   4483  CE2 PHE A 543      -5.616 -38.585  34.413  1.00 56.13           C  
ANISOU 4483  CE2 PHE A 543     8282   6543   6503   -482    271     74       C  
ATOM   4484  CZ  PHE A 543      -4.614 -37.929  33.696  1.00 58.63           C  
ANISOU 4484  CZ  PHE A 543     8754   6777   6746   -490    424     61       C  
ATOM   4485  N   ARG A 544      -5.683 -39.442  39.179  1.00 42.57           N  
ANISOU 4485  N   ARG A 544     5784   5165   5226   -392    227    228       N  
ATOM   4486  CA  ARG A 544      -6.920 -38.721  39.494  1.00 42.42           C  
ANISOU 4486  CA  ARG A 544     5733   5204   5180   -382     92    230       C  
ATOM   4487  C   ARG A 544      -6.757 -37.773  40.693  1.00 38.33           C  
ANISOU 4487  C   ARG A 544     5100   4772   4692   -348     83    270       C  
ATOM   4488  O   ARG A 544      -7.252 -36.642  40.675  1.00 39.70           O  
ANISOU 4488  O   ARG A 544     5287   4975   4820   -338     16    266       O  
ATOM   4489  CB  ARG A 544      -8.075 -39.704  39.702  1.00 43.85           C  
ANISOU 4489  CB  ARG A 544     5858   5383   5421   -395     20    225       C  
ATOM   4490  CG  ARG A 544      -8.448 -40.504  38.444  1.00 50.46           C  
ANISOU 4490  CG  ARG A 544     6829   6127   6218   -430    -16    176       C  
ATOM   4491  CD  ARG A 544      -9.499 -41.573  38.745  1.00 51.70           C  
ANISOU 4491  CD  ARG A 544     6900   6273   6473   -444    -79    170       C  
ATOM   4492  NE  ARG A 544      -9.732 -42.464  37.605  1.00 56.72           N  
ANISOU 4492  NE  ARG A 544     7666   6811   7076   -480   -114    121       N  
ATOM   4493  CZ  ARG A 544     -10.619 -43.463  37.590  1.00 57.27           C  
ANISOU 4493  CZ  ARG A 544     7686   6842   7233   -500   -179    102       C  
ATOM   4494  NH1 ARG A 544     -11.377 -43.716  38.651  1.00 56.11           N  
ANISOU 4494  NH1 ARG A 544     7358   6742   7220   -488   -193    130       N  
ATOM   4495  NH2 ARG A 544     -10.753 -44.215  36.507  1.00 53.80           N  
ANISOU 4495  NH2 ARG A 544     7389   6304   6748   -533   -220     51       N  
ATOM   4496  N   ALA A 545      -6.057 -38.228  41.722  1.00 34.90           N  
ANISOU 4496  N   ALA A 545     4565   4365   4329   -330    141    308       N  
ATOM   4497  CA  ALA A 545      -5.722 -37.373  42.847  1.00 35.29           C  
ANISOU 4497  CA  ALA A 545     4539   4476   4392   -299    128    343       C  
ATOM   4498  C   ALA A 545      -4.955 -36.149  42.348  1.00 38.28           C  
ANISOU 4498  C   ALA A 545     4968   4845   4730   -295    148    327       C  
ATOM   4499  O   ALA A 545      -5.323 -35.007  42.649  1.00 37.65           O  
ANISOU 4499  O   ALA A 545     4883   4811   4610   -280     96    329       O  
ATOM   4500  CB  ALA A 545      -4.896 -38.136  43.862  1.00 34.84           C  
ANISOU 4500  CB  ALA A 545     4405   4420   4414   -281    166    383       C  
ATOM   4501  N   GLN A 546      -3.910 -36.399  41.558  1.00 38.88           N  
ANISOU 4501  N   GLN A 546     5094   4849   4828   -308    239    308       N  
ATOM   4502  CA  GLN A 546      -3.042 -35.337  41.058  1.00 39.70           C  
ANISOU 4502  CA  GLN A 546     5244   4919   4920   -307    296    292       C  
ATOM   4503  C   GLN A 546      -3.822 -34.336  40.228  1.00 39.99           C  
ANISOU 4503  C   GLN A 546     5401   4958   4834   -317    246    267       C  
ATOM   4504  O   GLN A 546      -3.614 -33.127  40.345  1.00 39.70           O  
ANISOU 4504  O   GLN A 546     5368   4942   4775   -304    235    269       O  
ATOM   4505  CB  GLN A 546      -1.882 -35.918  40.252  1.00 40.87           C  
ANISOU 4505  CB  GLN A 546     5435   4960   5132   -326    440    271       C  
ATOM   4506  CG  GLN A 546      -0.911 -36.742  41.096  1.00 42.62           C  
ANISOU 4506  CG  GLN A 546     5518   5161   5514   -310    479    297       C  
ATOM   4507  CD  GLN A 546       0.339 -37.160  40.339  1.00 45.94           C  
ANISOU 4507  CD  GLN A 546     5950   5456   6047   -326    641    272       C  
ATOM   4508  OE1 GLN A 546       1.448 -37.044  40.857  1.00 47.91           O  
ANISOU 4508  OE1 GLN A 546     6083   5663   6458   -309    678    283       O  
ATOM   4509  NE2 GLN A 546       0.167 -37.646  39.111  1.00 44.26           N  
ANISOU 4509  NE2 GLN A 546     5885   5167   5764   -359    739    235       N  
ATOM   4510  N   ARG A 547      -4.735 -34.848  39.408  1.00 40.18           N  
ANISOU 4510  N   ARG A 547     5527   4952   4788   -338    199    243       N  
ATOM   4511  CA  ARG A 547      -5.600 -34.010  38.593  1.00 40.77           C  
ANISOU 4511  CA  ARG A 547     5728   5012   4752   -345    109    220       C  
ATOM   4512  C   ARG A 547      -6.525 -33.148  39.450  1.00 39.74           C  
ANISOU 4512  C   ARG A 547     5496   4967   4635   -320     -8    239       C  
ATOM   4513  O   ARG A 547      -6.740 -31.971  39.154  1.00 39.94           O  
ANISOU 4513  O   ARG A 547     5578   4994   4602   -311    -54    233       O  
ATOM   4514  CB  ARG A 547      -6.409 -34.867  37.605  1.00 43.07           C  
ANISOU 4514  CB  ARG A 547     6145   5236   4985   -372     47    188       C  
ATOM   4515  CG  ARG A 547      -5.692 -35.153  36.285  1.00 45.07           C  
ANISOU 4515  CG  ARG A 547     6608   5369   5147   -402    152    154       C  
ATOM   4516  CD  ARG A 547      -5.335 -33.867  35.572  1.00 48.66           C  
ANISOU 4516  CD  ARG A 547     7216   5777   5497   -401    181    145       C  
ATOM   4517  NE  ARG A 547      -4.610 -34.077  34.318  1.00 57.95           N  
ANISOU 4517  NE  ARG A 547     8626   6817   6575   -430    318    113       N  
ATOM   4518  CZ  ARG A 547      -5.187 -34.264  33.133  1.00 60.30           C  
ANISOU 4518  CZ  ARG A 547     9175   7015   6723   -454    253     79       C  
ATOM   4519  NH1 ARG A 547      -6.514 -34.289  33.024  1.00 60.24           N  
ANISOU 4519  NH1 ARG A 547     9186   7028   6674   -451     27     72       N  
ATOM   4520  NH2 ARG A 547      -4.434 -34.437  32.055  1.00 61.27           N  
ANISOU 4520  NH2 ARG A 547     9535   6999   6745   -482    414     50       N  
ATOM   4521  N   THR A 548      -7.063 -33.741  40.514  1.00 38.55           N  
ANISOU 4521  N   THR A 548     5207   4876   4565   -308    -40    262       N  
ATOM   4522  CA  THR A 548      -7.899 -33.011  41.462  1.00 37.48           C  
ANISOU 4522  CA  THR A 548     4974   4807   4458   -285   -109    280       C  
ATOM   4523  C   THR A 548      -7.086 -31.935  42.177  1.00 36.87           C  
ANISOU 4523  C   THR A 548     4860   4774   4374   -262    -71    299       C  
ATOM   4524  O   THR A 548      -7.572 -30.824  42.394  1.00 39.78           O  
ANISOU 4524  O   THR A 548     5221   5173   4722   -248   -121    298       O  
ATOM   4525  CB  THR A 548      -8.557 -33.966  42.489  1.00 37.97           C  
ANISOU 4525  CB  THR A 548     4921   4900   4606   -281   -109    301       C  
ATOM   4526  OG1 THR A 548      -9.385 -34.913  41.799  1.00 36.08           O  
ANISOU 4526  OG1 THR A 548     4703   4611   4395   -305   -156    277       O  
ATOM   4527  CG2 THR A 548      -9.396 -33.206  43.505  1.00 31.86           C  
ANISOU 4527  CG2 THR A 548     4063   4175   3867   -260   -141    317       C  
ATOM   4528  N   GLU A 549      -5.846 -32.258  42.529  1.00 37.37           N  
ANISOU 4528  N   GLU A 549     4897   4831   4471   -259     10    314       N  
ATOM   4529  CA  GLU A 549      -4.977 -31.300  43.205  1.00 37.52           C  
ANISOU 4529  CA  GLU A 549     4875   4875   4506   -239     29    327       C  
ATOM   4530  C   GLU A 549      -4.756 -30.076  42.313  1.00 39.00           C  
ANISOU 4530  C   GLU A 549     5147   5034   4636   -243     38    303       C  
ATOM   4531  O   GLU A 549      -4.908 -28.931  42.775  1.00 38.74           O  
ANISOU 4531  O   GLU A 549     5094   5041   4586   -226      0    307       O  
ATOM   4532  CB  GLU A 549      -3.641 -31.944  43.585  1.00 38.20           C  
ANISOU 4532  CB  GLU A 549     4909   4927   4678   -236     94    341       C  
ATOM   4533  CG  GLU A 549      -2.694 -31.005  44.322  1.00 37.86           C  
ANISOU 4533  CG  GLU A 549     4811   4891   4681   -215     86    350       C  
ATOM   4534  CD  GLU A 549      -1.355 -31.636  44.659  1.00 43.58           C  
ANISOU 4534  CD  GLU A 549     5466   5559   5534   -210    124    360       C  
ATOM   4535  OE1 GLU A 549      -1.249 -32.892  44.660  1.00 42.50           O  
ANISOU 4535  OE1 GLU A 549     5309   5395   5443   -216    148    370       O  
ATOM   4536  OE2 GLU A 549      -0.402 -30.863  44.929  1.00 43.32           O  
ANISOU 4536  OE2 GLU A 549     5388   5498   5574   -200    123    355       O  
ATOM   4537  N   VAL A 550      -4.424 -30.340  41.043  1.00 37.10           N  
ANISOU 4537  N   VAL A 550     5019   4717   4359   -267     96    279       N  
ATOM   4538  CA  VAL A 550      -4.163 -29.313  40.030  1.00 37.95           C  
ANISOU 4538  CA  VAL A 550     5255   4771   4394   -276    129    258       C  
ATOM   4539  C   VAL A 550      -5.350 -28.344  39.847  1.00 39.87           C  
ANISOU 4539  C   VAL A 550     5547   5044   4558   -265      8    254       C  
ATOM   4540  O   VAL A 550      -5.157 -27.123  39.737  1.00 39.13           O  
ANISOU 4540  O   VAL A 550     5486   4948   4432   -256      9    253       O  
ATOM   4541  CB  VAL A 550      -3.710 -29.952  38.657  1.00 38.86           C  
ANISOU 4541  CB  VAL A 550     5533   4775   4459   -307    228    231       C  
ATOM   4542  CG1 VAL A 550      -3.719 -28.928  37.535  1.00 40.20           C  
ANISOU 4542  CG1 VAL A 550     5890   4872   4512   -317    250    212       C  
ATOM   4543  CG2 VAL A 550      -2.304 -30.558  38.766  1.00 35.13           C  
ANISOU 4543  CG2 VAL A 550     5002   4246   4102   -315    382    230       C  
ATOM   4544  N   ALA A 551      -6.566 -28.888  39.831  1.00 39.75           N  
ANISOU 4544  N   ALA A 551     5521   5045   4535   -267    -96    252       N  
ATOM   4545  CA  ALA A 551      -7.779 -28.079  39.701  1.00 40.75           C  
ANISOU 4545  CA  ALA A 551     5663   5184   4636   -254   -226    246       C  
ATOM   4546  C   ALA A 551      -7.959 -27.199  40.923  1.00 40.22           C  
ANISOU 4546  C   ALA A 551     5463   5195   4623   -227   -238    265       C  
ATOM   4547  O   ALA A 551      -8.296 -26.018  40.804  1.00 41.87           O  
ANISOU 4547  O   ALA A 551     5696   5406   4805   -213   -287    262       O  
ATOM   4548  CB  ALA A 551      -8.999 -28.968  39.515  1.00 43.82           C  
ANISOU 4548  CB  ALA A 551     6032   5556   5061   -263   -331    235       C  
ATOM   4549  N   GLY A 552      -7.736 -27.782  42.099  1.00 39.68           N  
ANISOU 4549  N   GLY A 552     5274   5181   4622   -219   -193    285       N  
ATOM   4550  CA  GLY A 552      -7.768 -27.033  43.355  1.00 37.55           C  
ANISOU 4550  CA  GLY A 552     4912   4972   4382   -195   -189    302       C  
ATOM   4551  C   GLY A 552      -6.648 -26.008  43.406  1.00 36.98           C  
ANISOU 4551  C   GLY A 552     4863   4901   4286   -187   -147    302       C  
ATOM   4552  O   GLY A 552      -6.842 -24.905  43.908  1.00 36.30           O  
ANISOU 4552  O   GLY A 552     4755   4844   4194   -170   -171    302       O  
ATOM   4553  N   MET A 553      -5.476 -26.372  42.882  1.00 34.89           N  
ANISOU 4553  N   MET A 553     4636   4593   4027   -202    -74    298       N  
ATOM   4554  CA  MET A 553      -4.374 -25.429  42.765  1.00 37.64           C  
ANISOU 4554  CA  MET A 553     4999   4915   4387   -200    -19    291       C  
ATOM   4555  C   MET A 553      -4.757 -24.198  41.936  1.00 36.92           C  
ANISOU 4555  C   MET A 553     5004   4800   4224   -199    -40    277       C  
ATOM   4556  O   MET A 553      -4.503 -23.066  42.358  1.00 37.80           O  
ANISOU 4556  O   MET A 553     5090   4929   4344   -185    -45    277       O  
ATOM   4557  CB  MET A 553      -3.117 -26.097  42.187  1.00 39.93           C  
ANISOU 4557  CB  MET A 553     5308   5133   4732   -218     88    283       C  
ATOM   4558  CG  MET A 553      -1.916 -25.154  42.030  1.00 44.46           C  
ANISOU 4558  CG  MET A 553     5876   5654   5363   -220    167    272       C  
ATOM   4559  SD  MET A 553      -1.339 -24.396  43.583  1.00 52.60           S  
ANISOU 4559  SD  MET A 553     6767   6736   6483   -193    101    282       S  
ATOM   4560  CE  MET A 553      -0.117 -25.589  44.139  1.00 55.02           C  
ANISOU 4560  CE  MET A 553     6965   6993   6945   -194    131    290       C  
ATOM   4561  N   THR A 554      -5.358 -24.425  40.768  1.00 33.56           N  
ANISOU 4561  N   THR A 554     4701   4323   3725   -213    -63    266       N  
ATOM   4562  CA  THR A 554      -5.805 -23.349  39.891  1.00 32.10           C  
ANISOU 4562  CA  THR A 554     4642   4097   3459   -211   -107    256       C  
ATOM   4563  C   THR A 554      -6.766 -22.420  40.595  1.00 32.32           C  
ANISOU 4563  C   THR A 554     4592   4183   3503   -185   -209    263       C  
ATOM   4564  O   THR A 554      -6.621 -21.195  40.549  1.00 34.10           O  
ANISOU 4564  O   THR A 554     4844   4403   3708   -174   -210    262       O  
ATOM   4565  CB  THR A 554      -6.527 -23.919  38.672  1.00 35.75           C  
ANISOU 4565  CB  THR A 554     5258   4489   3836   -227   -170    244       C  
ATOM   4566  OG1 THR A 554      -5.596 -24.672  37.886  1.00 36.37           O  
ANISOU 4566  OG1 THR A 554     5446   4491   3882   -254    -48    233       O  
ATOM   4567  CG2 THR A 554      -7.158 -22.794  37.822  1.00 33.60           C  
ANISOU 4567  CG2 THR A 554     5129   4162   3473   -219   -261    239       C  
ATOM   4568  N   ALA A 555      -7.749 -23.029  41.250  1.00 32.12           N  
ANISOU 4568  N   ALA A 555     4471   4204   3530   -177   -279    268       N  
ATOM   4569  CA  ALA A 555      -8.822 -22.315  41.911  1.00 29.81           C  
ANISOU 4569  CA  ALA A 555     4097   3948   3283   -154   -356    269       C  
ATOM   4570  C   ALA A 555      -8.302 -21.498  43.086  1.00 31.04           C  
ANISOU 4570  C   ALA A 555     4172   4159   3463   -137   -302    277       C  
ATOM   4571  O   ALA A 555      -8.735 -20.365  43.287  1.00 32.54           O  
ANISOU 4571  O   ALA A 555     4350   4355   3657   -120   -335    273       O  
ATOM   4572  CB  ALA A 555      -9.900 -23.303  42.362  1.00 25.30           C  
ANISOU 4572  CB  ALA A 555     3435   3389   2787   -154   -401    270       C  
ATOM   4573  N   GLN A 556      -7.364 -22.055  43.849  1.00 29.83           N  
ANISOU 4573  N   GLN A 556     3971   4035   3329   -141   -232    286       N  
ATOM   4574  CA  GLN A 556      -6.915 -21.373  45.066  1.00 32.47           C  
ANISOU 4574  CA  GLN A 556     4246   4411   3682   -125   -211    291       C  
ATOM   4575  C   GLN A 556      -5.836 -20.311  44.820  1.00 33.16           C  
ANISOU 4575  C   GLN A 556     4363   4475   3759   -125   -181    282       C  
ATOM   4576  O   GLN A 556      -5.935 -19.201  45.342  1.00 33.25           O  
ANISOU 4576  O   GLN A 556     4361   4505   3769   -111   -198    276       O  
ATOM   4577  CB  GLN A 556      -6.536 -22.367  46.187  1.00 29.93           C  
ANISOU 4577  CB  GLN A 556     3867   4116   3388   -124   -187    307       C  
ATOM   4578  CG  GLN A 556      -5.156 -23.010  46.114  1.00 30.10           C  
ANISOU 4578  CG  GLN A 556     3884   4113   3440   -135   -151    312       C  
ATOM   4579  CD  GLN A 556      -4.029 -22.079  46.544  1.00 32.62           C  
ANISOU 4579  CD  GLN A 556     4186   4418   3788   -128   -148    304       C  
ATOM   4580  OE1 GLN A 556      -4.265 -21.018  47.126  1.00 31.50           O  
ANISOU 4580  OE1 GLN A 556     4044   4298   3624   -114   -177    297       O  
ATOM   4581  NE2 GLN A 556      -2.796 -22.466  46.235  1.00 27.21           N  
ANISOU 4581  NE2 GLN A 556     3480   3684   3173   -139   -111    300       N  
ATOM   4582  N   ILE A 557      -4.830 -20.636  44.008  1.00 33.25           N  
ANISOU 4582  N   ILE A 557     4418   4437   3779   -144   -123    277       N  
ATOM   4583  CA  ILE A 557      -3.728 -19.706  43.761  1.00 32.89           C  
ANISOU 4583  CA  ILE A 557     4387   4348   3760   -148    -68    266       C  
ATOM   4584  C   ILE A 557      -4.133 -18.445  42.987  1.00 33.09           C  
ANISOU 4584  C   ILE A 557     4499   4346   3728   -144    -76    258       C  
ATOM   4585  O   ILE A 557      -3.509 -17.389  43.134  1.00 33.48           O  
ANISOU 4585  O   ILE A 557     4540   4378   3804   -141    -47    249       O  
ATOM   4586  CB  ILE A 557      -2.511 -20.392  43.102  1.00 32.26           C  
ANISOU 4586  CB  ILE A 557     4322   4196   3738   -170     31    259       C  
ATOM   4587  CG1 ILE A 557      -1.235 -19.594  43.399  1.00 34.11           C  
ANISOU 4587  CG1 ILE A 557     4500   4385   4073   -172     84    246       C  
ATOM   4588  CG2 ILE A 557      -2.731 -20.612  41.589  1.00 31.95           C  
ANISOU 4588  CG2 ILE A 557     4429   4087   3622   -190     89    254       C  
ATOM   4589  CD1 ILE A 557       0.070 -20.427  43.344  1.00 38.09           C  
ANISOU 4589  CD1 ILE A 557     4939   4818   4714   -187    166    239       C  
ATOM   4590  N   ASN A 558      -5.170 -18.558  42.168  1.00 34.01           N  
ANISOU 4590  N   ASN A 558     4700   4449   3775   -144   -127    261       N  
ATOM   4591  CA  ASN A 558      -5.629 -17.415  41.399  1.00 34.78           C  
ANISOU 4591  CA  ASN A 558     4896   4506   3813   -137   -160    259       C  
ATOM   4592  C   ASN A 558      -6.525 -16.492  42.191  1.00 34.65           C  
ANISOU 4592  C   ASN A 558     4806   4540   3818   -110   -239    259       C  
ATOM   4593  O   ASN A 558      -6.483 -15.274  42.008  1.00 36.08           O  
ANISOU 4593  O   ASN A 558     5024   4699   3984   -100   -243    256       O  
ATOM   4594  CB  ASN A 558      -6.256 -17.872  40.099  1.00 36.41           C  
ANISOU 4594  CB  ASN A 558     5251   4647   3937   -147   -205    260       C  
ATOM   4595  CG  ASN A 558      -5.208 -18.293  39.100  1.00 39.23           C  
ANISOU 4595  CG  ASN A 558     5740   4918   4248   -175    -85    255       C  
ATOM   4596  OD1 ASN A 558      -4.401 -17.475  38.681  1.00 43.40           O  
ANISOU 4596  OD1 ASN A 558     6340   5388   4763   -182      9    251       O  
ATOM   4597  ND2 ASN A 558      -5.186 -19.575  38.740  1.00 38.63           N  
ANISOU 4597  ND2 ASN A 558     5694   4824   4161   -193    -67    252       N  
ATOM   4598  N   ARG A 559      -7.298 -17.070  43.104  1.00 35.27           N  
ANISOU 4598  N   ARG A 559     4784   4675   3941   -100   -283    262       N  
ATOM   4599  CA  ARG A 559      -8.011 -16.283  44.108  1.00 35.17           C  
ANISOU 4599  CA  ARG A 559     4692   4704   3968    -77   -314    258       C  
ATOM   4600  C   ARG A 559      -7.066 -15.558  45.059  1.00 34.56           C  
ANISOU 4600  C   ARG A 559     4577   4653   3901    -73   -263    251       C  
ATOM   4601  O   ARG A 559      -7.323 -14.405  45.437  1.00 37.99           O  
ANISOU 4601  O   ARG A 559     5001   5091   4342    -57   -274    242       O  
ATOM   4602  CB  ARG A 559      -9.010 -17.151  44.864  1.00 35.42           C  
ANISOU 4602  CB  ARG A 559     4641   4767   4051    -71   -334    262       C  
ATOM   4603  CG  ARG A 559     -10.213 -17.485  44.018  1.00 33.59           C  
ANISOU 4603  CG  ARG A 559     4419   4493   3851    -69   -418    260       C  
ATOM   4604  CD  ARG A 559     -11.187 -18.430  44.714  1.00 36.49           C  
ANISOU 4604  CD  ARG A 559     4689   4873   4303    -68   -417    260       C  
ATOM   4605  NE  ARG A 559     -12.411 -18.571  43.919  1.00 35.68           N  
ANISOU 4605  NE  ARG A 559     4572   4710   4274    -63   -524    252       N  
ATOM   4606  CZ  ARG A 559     -12.509 -19.286  42.800  1.00 34.40           C  
ANISOU 4606  CZ  ARG A 559     4482   4502   4084    -78   -602    251       C  
ATOM   4607  NH1 ARG A 559     -11.456 -19.953  42.328  1.00 35.67           N  
ANISOU 4607  NH1 ARG A 559     4733   4673   4148   -100   -555    257       N  
ATOM   4608  NH2 ARG A 559     -13.667 -19.338  42.152  1.00 34.60           N  
ANISOU 4608  NH2 ARG A 559     4492   4459   4194    -72   -733    239       N  
ATOM   4609  N   LYS A 560      -5.966 -16.217  45.417  1.00 33.56           N  
ANISOU 4609  N   LYS A 560     4430   4532   3789    -86   -218    252       N  
ATOM   4610  CA  LYS A 560      -4.880 -15.590  46.195  1.00 33.46           C  
ANISOU 4610  CA  LYS A 560     4385   4519   3808    -85   -198    241       C  
ATOM   4611  C   LYS A 560      -4.233 -14.403  45.456  1.00 33.99           C  
ANISOU 4611  C   LYS A 560     4493   4537   3884    -90   -164    228       C  
ATOM   4612  O   LYS A 560      -3.987 -13.348  46.039  1.00 36.30           O  
ANISOU 4612  O   LYS A 560     4766   4832   4195    -81   -174    214       O  
ATOM   4613  CB  LYS A 560      -3.818 -16.640  46.552  1.00 35.09           C  
ANISOU 4613  CB  LYS A 560     4554   4717   4063    -98   -179    245       C  
ATOM   4614  CG  LYS A 560      -2.481 -16.082  47.059  1.00 35.06           C  
ANISOU 4614  CG  LYS A 560     4508   4679   4134   -101   -177    229       C  
ATOM   4615  CD  LYS A 560      -1.458 -17.191  47.240  1.00 33.48           C  
ANISOU 4615  CD  LYS A 560     4258   4447   4017   -111   -171    234       C  
ATOM   4616  CE  LYS A 560      -0.085 -16.612  47.459  1.00 37.44           C  
ANISOU 4616  CE  LYS A 560     4701   4883   4644   -117   -172    212       C  
ATOM   4617  NZ  LYS A 560       0.876 -17.628  47.948  1.00 40.24           N  
ANISOU 4617  NZ  LYS A 560     4984   5197   5110   -119   -206    215       N  
ATOM   4618  N   LEU A 561      -3.960 -14.583  44.171  1.00 33.12           N  
ANISOU 4618  N   LEU A 561     4458   4371   3756   -106   -116    233       N  
ATOM   4619  CA  LEU A 561      -3.434 -13.507  43.357  1.00 35.00           C  
ANISOU 4619  CA  LEU A 561     4766   4543   3990   -112    -61    225       C  
ATOM   4620  C   LEU A 561      -4.404 -12.342  43.327  1.00 36.16           C  
ANISOU 4620  C   LEU A 561     4947   4702   4091    -91   -121    226       C  
ATOM   4621  O   LEU A 561      -3.986 -11.188  43.419  1.00 37.27           O  
ANISOU 4621  O   LEU A 561     5090   4819   4253    -88    -97    216       O  
ATOM   4622  CB  LEU A 561      -3.139 -13.976  41.932  1.00 35.79           C  
ANISOU 4622  CB  LEU A 561     4991   4563   4046   -133     14    232       C  
ATOM   4623  CG  LEU A 561      -2.539 -12.928  40.988  1.00 39.45           C  
ANISOU 4623  CG  LEU A 561     5565   4931   4493   -144    106    227       C  
ATOM   4624  CD1 LEU A 561      -1.165 -12.458  41.480  1.00 39.31           C  
ANISOU 4624  CD1 LEU A 561     5451   4875   4609   -157    200    207       C  
ATOM   4625  CD2 LEU A 561      -2.455 -13.470  39.561  1.00 41.45           C  
ANISOU 4625  CD2 LEU A 561     5998   5091   4660   -165    182    235       C  
ATOM   4626  N   LEU A 562      -5.694 -12.643  43.202  1.00 34.07           N  
ANISOU 4626  N   LEU A 562     4696   4464   3786    -77   -201    237       N  
ATOM   4627  CA  LEU A 562      -6.689 -11.586  43.160  1.00 34.80           C  
ANISOU 4627  CA  LEU A 562     4802   4553   3868    -53   -267    238       C  
ATOM   4628  C   LEU A 562      -6.681 -10.796  44.462  1.00 34.91           C  
ANISOU 4628  C   LEU A 562     4721   4613   3929    -39   -263    222       C  
ATOM   4629  O   LEU A 562      -6.633  -9.567  44.430  1.00 32.93           O  
ANISOU 4629  O   LEU A 562     4490   4340   3684    -29   -260    215       O  
ATOM   4630  CB  LEU A 562      -8.096 -12.118  42.829  1.00 33.29           C  
ANISOU 4630  CB  LEU A 562     4613   4361   3676    -40   -364    248       C  
ATOM   4631  CG  LEU A 562      -9.204 -11.076  42.602  1.00 35.35           C  
ANISOU 4631  CG  LEU A 562     4882   4590   3960    -13   -452    249       C  
ATOM   4632  CD1 LEU A 562      -8.838 -10.068  41.495  1.00 30.79           C  
ANISOU 4632  CD1 LEU A 562     4449   3936   3315    -12   -461    258       C  
ATOM   4633  CD2 LEU A 562     -10.573 -11.733  42.302  1.00 30.30           C  
ANISOU 4633  CD2 LEU A 562     4212   3928   3370     -1   -564    253       C  
ATOM   4634  N   ILE A 563      -6.709 -11.491  45.602  1.00 37.41           N  
ANISOU 4634  N   ILE A 563     4959   4984   4271    -38   -259    217       N  
ATOM   4635  CA  ILE A 563      -6.753 -10.777  46.884  1.00 37.09           C  
ANISOU 4635  CA  ILE A 563     4870   4973   4250    -25   -255    199       C  
ATOM   4636  C   ILE A 563      -5.450 -10.037  47.170  1.00 37.24           C  
ANISOU 4636  C   ILE A 563     4891   4973   4287    -35   -231    181       C  
ATOM   4637  O   ILE A 563      -5.479  -8.924  47.690  1.00 39.00           O  
ANISOU 4637  O   ILE A 563     5110   5191   4518    -25   -235    163       O  
ATOM   4638  CB  ILE A 563      -7.198 -11.646  48.099  1.00 36.57           C  
ANISOU 4638  CB  ILE A 563     4761   4949   4184    -21   -252    199       C  
ATOM   4639  CG1 ILE A 563      -6.310 -12.878  48.301  1.00 36.30           C  
ANISOU 4639  CG1 ILE A 563     4720   4927   4144    -38   -246    209       C  
ATOM   4640  CG2 ILE A 563      -8.639 -12.027  47.958  1.00 36.48           C  
ANISOU 4640  CG2 ILE A 563     4723   4937   4200     -9   -262    207       C  
ATOM   4641  CD1 ILE A 563      -6.661 -13.691  49.553  1.00 27.14           C  
ANISOU 4641  CD1 ILE A 563     3551   3795   2966    -33   -241    213       C  
ATOM   4642  N   ASN A 564      -4.319 -10.645  46.812  1.00 35.98           N  
ANISOU 4642  N   ASN A 564     4727   4788   4154    -55   -203    183       N  
ATOM   4643  CA  ASN A 564      -3.021  -9.995  46.985  1.00 33.66           C  
ANISOU 4643  CA  ASN A 564     4411   4453   3927    -67   -180    162       C  
ATOM   4644  C   ASN A 564      -2.887  -8.803  46.065  1.00 32.53           C  
ANISOU 4644  C   ASN A 564     4316   4255   3789    -69   -134    158       C  
ATOM   4645  O   ASN A 564      -2.113  -7.882  46.337  1.00 32.51           O  
ANISOU 4645  O   ASN A 564     4289   4215   3847    -75   -118    136       O  
ATOM   4646  CB  ASN A 564      -1.880 -10.976  46.721  1.00 34.12           C  
ANISOU 4646  CB  ASN A 564     4435   4474   4055    -88   -146    164       C  
ATOM   4647  CG  ASN A 564      -1.571 -11.843  47.921  1.00 32.98           C  
ANISOU 4647  CG  ASN A 564     4237   4361   3934    -85   -212    162       C  
ATOM   4648  OD1 ASN A 564      -1.999 -11.550  49.036  1.00 35.91           O  
ANISOU 4648  OD1 ASN A 564     4614   4768   4263    -70   -274    154       O  
ATOM   4649  ND2 ASN A 564      -0.826 -12.919  47.699  1.00 29.63           N  
ANISOU 4649  ND2 ASN A 564     3776   3908   3572    -98   -194    169       N  
ATOM   4650  N   SER A 565      -3.648  -8.827  44.974  1.00 30.36           N  
ANISOU 4650  N   SER A 565     4120   3964   3451    -66   -122    180       N  
ATOM   4651  CA  SER A 565      -3.592  -7.760  43.989  1.00 34.47           C  
ANISOU 4651  CA  SER A 565     4726   4418   3952    -66    -82    184       C  
ATOM   4652  C   SER A 565      -4.301  -6.503  44.450  1.00 35.30           C  
ANISOU 4652  C   SER A 565     4822   4538   4052    -42   -129    176       C  
ATOM   4653  O   SER A 565      -3.991  -5.413  43.969  1.00 35.05           O  
ANISOU 4653  O   SER A 565     4839   4450   4027    -43    -93    173       O  
ATOM   4654  CB  SER A 565      -4.160  -8.216  42.655  1.00 34.81           C  
ANISOU 4654  CB  SER A 565     4895   4418   3913    -68    -81    210       C  
ATOM   4655  OG  SER A 565      -3.206  -9.043  42.013  1.00 43.18           O  
ANISOU 4655  OG  SER A 565     5995   5428   4984    -96     11    212       O  
ATOM   4656  N   LEU A 566      -5.253  -6.662  45.369  1.00 35.58           N  
ANISOU 4656  N   LEU A 566     4800   4637   4082    -23   -193    171       N  
ATOM   4657  CA  LEU A 566      -5.954  -5.519  45.925  1.00 38.19           C  
ANISOU 4657  CA  LEU A 566     5112   4973   4424      0   -220    158       C  
ATOM   4658  C   LEU A 566      -4.973  -4.695  46.756  1.00 38.65           C  
ANISOU 4658  C   LEU A 566     5137   5025   4523     -9   -193    127       C  
ATOM   4659  O   LEU A 566      -4.976  -3.468  46.669  1.00 39.75           O  
ANISOU 4659  O   LEU A 566     5293   5130   4679     -1   -183    116       O  
ATOM   4660  CB  LEU A 566      -7.181  -5.957  46.740  1.00 39.36           C  
ANISOU 4660  CB  LEU A 566     5208   5170   4578     19   -258    157       C  
ATOM   4661  CG  LEU A 566      -8.105  -4.878  47.339  1.00 40.19           C  
ANISOU 4661  CG  LEU A 566     5287   5268   4717     45   -265    141       C  
ATOM   4662  CD1 LEU A 566      -8.552  -3.876  46.307  1.00 41.90           C  
ANISOU 4662  CD1 LEU A 566     5546   5427   4947     61   -298    155       C  
ATOM   4663  CD2 LEU A 566      -9.326  -5.504  47.998  1.00 45.12           C  
ANISOU 4663  CD2 LEU A 566     5856   5912   5374     59   -267    140       C  
ATOM   4664  N   ALA A 567      -4.124  -5.381  47.529  1.00 38.34           N  
ANISOU 4664  N   ALA A 567     5054   5005   4509    -24   -196    112       N  
ATOM   4665  CA  ALA A 567      -3.053  -4.737  48.302  1.00 37.88           C  
ANISOU 4665  CA  ALA A 567     4962   4921   4509    -35   -204     77       C  
ATOM   4666  C   ALA A 567      -2.084  -3.968  47.409  1.00 37.56           C  
ANISOU 4666  C   ALA A 567     4926   4803   4541    -52   -143     71       C  
ATOM   4667  O   ALA A 567      -1.699  -2.837  47.727  1.00 35.63           O  
ANISOU 4667  O   ALA A 567     4671   4525   4344    -53   -142     44       O  
ATOM   4668  CB  ALA A 567      -2.303  -5.761  49.109  1.00 38.34           C  
ANISOU 4668  CB  ALA A 567     4980   4993   4595    -47   -246     68       C  
ATOM   4669  N   GLY A 568      -1.689  -4.598  46.301  1.00 37.57           N  
ANISOU 4669  N   GLY A 568     4955   4767   4553    -67    -79     94       N  
ATOM   4670  CA  GLY A 568      -0.900  -3.947  45.264  1.00 35.61           C  
ANISOU 4670  CA  GLY A 568     4745   4424   4360    -85     22     94       C  
ATOM   4671  C   GLY A 568      -1.644  -2.819  44.560  1.00 36.98           C  
ANISOU 4671  C   GLY A 568     5013   4571   4468    -70     39    110       C  
ATOM   4672  O   GLY A 568      -1.062  -1.766  44.293  1.00 38.17           O  
ANISOU 4672  O   GLY A 568     5178   4651   4673    -78    100     97       O  
ATOM   4673  N   ALA A 569      -2.926  -3.027  44.252  1.00 35.45           N  
ANISOU 4673  N   ALA A 569     4879   4419   4173    -46    -21    137       N  
ATOM   4674  CA  ALA A 569      -3.723  -2.020  43.522  1.00 35.03           C  
ANISOU 4674  CA  ALA A 569     4920   4326   4065    -26    -35    157       C  
ATOM   4675  C   ALA A 569      -3.762  -0.685  44.264  1.00 33.77           C  
ANISOU 4675  C   ALA A 569     4713   4166   3954    -14    -47    131       C  
ATOM   4676  O   ALA A 569      -3.730   0.373  43.641  1.00 35.69           O  
ANISOU 4676  O   ALA A 569     5026   4342   4195     -9    -14    139       O  
ATOM   4677  CB  ALA A 569      -5.142  -2.523  43.231  1.00 32.06           C  
ANISOU 4677  CB  ALA A 569     4579   3985   3619      0   -132    183       C  
ATOM   4678  N   LEU A 570      -3.802  -0.745  45.594  1.00 32.39           N  
ANISOU 4678  N   LEU A 570     4438   4054   3815     -9    -90     99       N  
ATOM   4679  CA  LEU A 570      -3.675   0.446  46.435  1.00 33.18           C  
ANISOU 4679  CA  LEU A 570     4500   4146   3960     -3    -97     65       C  
ATOM   4680  C   LEU A 570      -2.404   1.257  46.109  1.00 35.19           C  
ANISOU 4680  C   LEU A 570     4753   4319   4297    -28    -27     45       C  
ATOM   4681  O   LEU A 570      -2.334   2.458  46.386  1.00 38.63           O  
ANISOU 4681  O   LEU A 570     5184   4722   4769    -23    -20     23       O  
ATOM   4682  CB  LEU A 570      -3.746   0.070  47.923  1.00 31.97           C  
ANISOU 4682  CB  LEU A 570     4282   4055   3810     -1   -150     31       C  
ATOM   4683  CG  LEU A 570      -5.093  -0.527  48.385  1.00 35.18           C  
ANISOU 4683  CG  LEU A 570     4687   4522   4159     23   -185     44       C  
ATOM   4684  CD1 LEU A 570      -5.012  -1.137  49.778  1.00 32.06           C  
ANISOU 4684  CD1 LEU A 570     4271   4170   3742     19   -212     18       C  
ATOM   4685  CD2 LEU A 570      -6.243   0.493  48.338  1.00 32.46           C  
ANISOU 4685  CD2 LEU A 570     4354   4160   3820     52   -186     45       C  
ATOM   4686  N   GLY A 571      -1.430   0.605  45.476  1.00 34.48           N  
ANISOU 4686  N   GLY A 571     4665   4185   4253    -54     39     52       N  
ATOM   4687  CA  GLY A 571      -0.207   1.255  45.026  1.00 34.18           C  
ANISOU 4687  CA  GLY A 571     4616   4043   4326    -81    138     35       C  
ATOM   4688  C   GLY A 571      -0.084   1.462  43.525  1.00 34.76           C  
ANISOU 4688  C   GLY A 571     4819   4024   4365    -90    261     71       C  
ATOM   4689  O   GLY A 571       0.989   1.812  43.044  1.00 32.96           O  
ANISOU 4689  O   GLY A 571     4591   3692   4242   -118    384     59       O  
ATOM   4690  N   ASN A 572      -1.168   1.247  42.776  1.00 36.22           N  
ANISOU 4690  N   ASN A 572     5125   4228   4408    -68    227    114       N  
ATOM   4691  CA  ASN A 572      -1.170   1.568  41.343  1.00 35.11           C  
ANISOU 4691  CA  ASN A 572     5163   3982   4194    -73    320    152       C  
ATOM   4692  C   ASN A 572      -2.004   2.806  41.042  1.00 37.80           C  
ANISOU 4692  C   ASN A 572     5593   4294   4474    -44    273    172       C  
ATOM   4693  O   ASN A 572      -3.207   2.827  41.312  1.00 39.79           O  
ANISOU 4693  O   ASN A 572     5839   4612   4668    -10    141    185       O  
ATOM   4694  CB  ASN A 572      -1.643   0.389  40.495  1.00 34.58           C  
ANISOU 4694  CB  ASN A 572     5210   3918   4010    -72    306    187       C  
ATOM   4695  CG  ASN A 572      -1.528   0.662  38.998  1.00 35.24           C  
ANISOU 4695  CG  ASN A 572     5527   3868   3993    -81    408    224       C  
ATOM   4696  OD1 ASN A 572      -2.285   1.455  38.443  1.00 32.31           O  
ANISOU 4696  OD1 ASN A 572     5290   3456   3532    -56    351    253       O  
ATOM   4697  ND2 ASN A 572      -0.581   0.000  38.342  1.00 30.20           N  
ANISOU 4697  ND2 ASN A 572     4954   3147   3373   -115    563    223       N  
ATOM   4698  N   VAL A 573      -1.356   3.831  40.481  1.00 39.41           N  
ANISOU 4698  N   VAL A 573     5874   4388   4713    -57    388    173       N  
ATOM   4699  CA  VAL A 573      -2.001   5.122  40.187  1.00 39.77           C  
ANISOU 4699  CA  VAL A 573     6007   4388   4717    -30    354    193       C  
ATOM   4700  C   VAL A 573      -3.321   5.020  39.399  1.00 40.95           C  
ANISOU 4700  C   VAL A 573     6311   4530   4719      7    230    243       C  
ATOM   4701  O   VAL A 573      -4.114   5.966  39.405  1.00 41.64           O  
ANISOU 4701  O   VAL A 573     6425   4602   4793     40    147    257       O  
ATOM   4702  CB  VAL A 573      -1.028   6.148  39.508  1.00 41.35           C  
ANISOU 4702  CB  VAL A 573     6301   4443   4969    -54    527    194       C  
ATOM   4703  CG1 VAL A 573       0.234   6.355  40.356  1.00 40.45           C  
ANISOU 4703  CG1 VAL A 573     6001   4318   5049    -89    619    136       C  
ATOM   4704  CG2 VAL A 573      -0.660   5.723  38.069  1.00 43.92           C  
ANISOU 4704  CG2 VAL A 573     6857   4641   5192    -73    661    235       C  
ATOM   4705  N   TRP A 574      -3.559   3.878  38.751  1.00 40.37           N  
ANISOU 4705  N   TRP A 574     6329   4458   4552      3    204    268       N  
ATOM   4706  CA  TRP A 574      -4.770   3.682  37.939  1.00 42.90           C  
ANISOU 4706  CA  TRP A 574     6805   4752   4746     36     58    312       C  
ATOM   4707  C   TRP A 574      -5.958   3.134  38.735  1.00 41.37           C  
ANISOU 4707  C   TRP A 574     6458   4674   4588     66   -118    303       C  
ATOM   4708  O   TRP A 574      -7.084   3.065  38.232  1.00 38.13           O  
ANISOU 4708  O   TRP A 574     6123   4238   4126     98   -270    332       O  
ATOM   4709  CB  TRP A 574      -4.477   2.823  36.696  1.00 43.98           C  
ANISOU 4709  CB  TRP A 574     7163   4799   4749     15    115    343       C  
ATOM   4710  CG  TRP A 574      -3.527   3.508  35.773  1.00 48.66           C  
ANISOU 4710  CG  TRP A 574     7954   5240   5294    -10    302    359       C  
ATOM   4711  CD1 TRP A 574      -2.174   3.337  35.712  1.00 49.90           C  
ANISOU 4711  CD1 TRP A 574     8093   5343   5525    -55    527    335       C  
ATOM   4712  CD2 TRP A 574      -3.848   4.517  34.809  1.00 53.22           C  
ANISOU 4712  CD2 TRP A 574     8776   5682   5761      8    290    401       C  
ATOM   4713  NE1 TRP A 574      -1.631   4.164  34.757  1.00 53.91           N  
ANISOU 4713  NE1 TRP A 574     8820   5687   5976    -69    684    359       N  
ATOM   4714  CE2 TRP A 574      -2.635   4.903  34.188  1.00 56.12           C  
ANISOU 4714  CE2 TRP A 574     9281   5917   6127    -30    540    402       C  
ATOM   4715  CE3 TRP A 574      -5.043   5.127  34.403  1.00 57.15           C  
ANISOU 4715  CE3 TRP A 574     9392   6145   6178     55     91    439       C  
ATOM   4716  CZ2 TRP A 574      -2.581   5.873  33.180  1.00 59.06           C  
ANISOU 4716  CZ2 TRP A 574     9929   6124   6388    -25    611    443       C  
ATOM   4717  CZ3 TRP A 574      -4.990   6.097  33.392  1.00 63.12           C  
ANISOU 4717  CZ3 TRP A 574    10421   6738   6822     63    130    482       C  
ATOM   4718  CH2 TRP A 574      -3.765   6.458  32.796  1.00 62.85           C  
ANISOU 4718  CH2 TRP A 574    10544   6576   6759     23    395    485       C  
ATOM   4719  N   PHE A 575      -5.708   2.767  39.986  1.00 39.74           N  
ANISOU 4719  N   PHE A 575     6042   4577   4479     56    -98    262       N  
ATOM   4720  CA  PHE A 575      -6.770   2.257  40.836  1.00 39.65           C  
ANISOU 4720  CA  PHE A 575     5891   4662   4511     81   -220    249       C  
ATOM   4721  C   PHE A 575      -7.570   3.414  41.408  1.00 39.71           C  
ANISOU 4721  C   PHE A 575     5828   4670   4589    115   -281    240       C  
ATOM   4722  O   PHE A 575      -7.005   4.393  41.887  1.00 41.26           O  
ANISOU 4722  O   PHE A 575     5987   4856   4833    109   -209    217       O  
ATOM   4723  CB  PHE A 575      -6.191   1.384  41.949  1.00 38.14           C  
ANISOU 4723  CB  PHE A 575     5546   4570   4374     57   -170    212       C  
ATOM   4724  CG  PHE A 575      -7.214   0.544  42.679  1.00 36.35           C  
ANISOU 4724  CG  PHE A 575     5213   4428   4172     75   -262    205       C  
ATOM   4725  CD1 PHE A 575      -8.204  -0.146  41.984  1.00 35.04           C  
ANISOU 4725  CD1 PHE A 575     5097   4247   3971     91   -363    234       C  
ATOM   4726  CD2 PHE A 575      -7.148   0.404  44.058  1.00 31.62           C  
ANISOU 4726  CD2 PHE A 575     4476   3906   3631     72   -243    169       C  
ATOM   4727  CE1 PHE A 575      -9.132  -0.928  42.659  1.00 33.98           C  
ANISOU 4727  CE1 PHE A 575     4849   4173   3888    104   -427    225       C  
ATOM   4728  CE2 PHE A 575      -8.059  -0.383  44.733  1.00 33.35           C  
ANISOU 4728  CE2 PHE A 575     4614   4185   3873     85   -293    163       C  
ATOM   4729  CZ  PHE A 575      -9.054  -1.048  44.035  1.00 31.84           C  
ANISOU 4729  CZ  PHE A 575     4446   3978   3674    100   -375    191       C  
ATOM   4730  N   ARG A 576      -8.890   3.296  41.343  1.00 38.96           N  
ANISOU 4730  N   ARG A 576     5912   4545   4345    306   -219    -51       N  
ATOM   4731  CA  ARG A 576      -9.795   4.324  41.847  1.00 39.84           C  
ANISOU 4731  CA  ARG A 576     6056   4624   4459    339   -230    -86       C  
ATOM   4732  C   ARG A 576      -9.550   4.632  43.326  1.00 39.95           C  
ANISOU 4732  C   ARG A 576     6041   4639   4501    269   -219   -111       C  
ATOM   4733  O   ARG A 576      -9.761   5.759  43.773  1.00 40.66           O  
ANISOU 4733  O   ARG A 576     6177   4680   4592    275   -216   -128       O  
ATOM   4734  CB  ARG A 576     -11.242   3.885  41.640  1.00 40.00           C  
ANISOU 4734  CB  ARG A 576     6044   4683   4472    416   -274   -131       C  
ATOM   4735  CG  ARG A 576     -12.293   4.944  41.979  1.00 40.76           C  
ANISOU 4735  CG  ARG A 576     6174   4752   4562    472   -288   -168       C  
ATOM   4736  CD  ARG A 576     -13.698   4.382  41.823  1.00 40.26           C  
ANISOU 4736  CD  ARG A 576     6059   4740   4497    541   -332   -214       C  
ATOM   4737  NE  ARG A 576     -13.915   3.836  40.490  1.00 40.54           N  
ANISOU 4737  NE  ARG A 576     6104   4787   4511    603   -357   -203       N  
ATOM   4738  CZ  ARG A 576     -14.378   4.533  39.454  1.00 42.36           C  
ANISOU 4738  CZ  ARG A 576     6403   4987   4706    693   -371   -200       C  
ATOM   4739  NH1 ARG A 576     -14.689   5.815  39.594  1.00 36.96           N  
ANISOU 4739  NH1 ARG A 576     5784   4251   4008    729   -362   -203       N  
ATOM   4740  NH2 ARG A 576     -14.535   3.938  38.275  1.00 37.81           N  
ANISOU 4740  NH2 ARG A 576     5830   4431   4106    752   -398   -194       N  
ATOM   4741  N   TYR A 577      -9.099   3.631  44.075  1.00 40.01           N  
ANISOU 4741  N   TYR A 577     5977   4700   4526    207   -217   -114       N  
ATOM   4742  CA  TYR A 577      -8.918   3.777  45.512  1.00 39.61           C  
ANISOU 4742  CA  TYR A 577     5892   4664   4493    150   -211   -141       C  
ATOM   4743  C   TYR A 577      -7.444   3.752  45.887  1.00 40.09           C  
ANISOU 4743  C   TYR A 577     5949   4715   4567     65   -183   -112       C  
ATOM   4744  O   TYR A 577      -7.093   3.454  47.034  1.00 38.67           O  
ANISOU 4744  O   TYR A 577     5725   4569   4400     12   -181   -129       O  
ATOM   4745  CB  TYR A 577      -9.701   2.698  46.270  1.00 40.74           C  
ANISOU 4745  CB  TYR A 577     5952   4882   4645    152   -230   -171       C  
ATOM   4746  CG  TYR A 577     -11.141   2.584  45.835  1.00 39.62           C  
ANISOU 4746  CG  TYR A 577     5798   4758   4497    231   -259   -199       C  
ATOM   4747  CD1 TYR A 577     -11.536   1.588  44.950  1.00 38.24           C  
ANISOU 4747  CD1 TYR A 577     5592   4612   4325    263   -281   -192       C  
ATOM   4748  CD2 TYR A 577     -12.104   3.484  46.292  1.00 37.70           C  
ANISOU 4748  CD2 TYR A 577     5575   4504   4246    278   -269   -237       C  
ATOM   4749  CE1 TYR A 577     -12.857   1.481  44.533  1.00 39.46           C  
ANISOU 4749  CE1 TYR A 577     5729   4785   4479    335   -314   -223       C  
ATOM   4750  CE2 TYR A 577     -13.431   3.384  45.884  1.00 37.79           C  
ANISOU 4750  CE2 TYR A 577     5567   4537   4253    353   -297   -265       C  
ATOM   4751  CZ  TYR A 577     -13.799   2.380  45.005  1.00 39.01           C  
ANISOU 4751  CZ  TYR A 577     5686   4722   4415    379   -320   -258       C  
ATOM   4752  OH  TYR A 577     -15.105   2.268  44.588  1.00 38.89           O  
ANISOU 4752  OH  TYR A 577     5646   4730   4401    452   -353   -290       O  
ATOM   4753  N   TYR A 578      -6.595   4.070  44.905  1.00 41.07           N  
ANISOU 4753  N   TYR A 578     6118   4798   4687     56   -161    -66       N  
ATOM   4754  CA  TYR A 578      -5.157   4.276  45.103  1.00 40.07           C  
ANISOU 4754  CA  TYR A 578     5994   4653   4578    -23   -132    -33       C  
ATOM   4755  C   TYR A 578      -4.888   5.212  46.271  1.00 40.46           C  
ANISOU 4755  C   TYR A 578     6055   4668   4649    -72   -131    -65       C  
ATOM   4756  O   TYR A 578      -5.402   6.322  46.311  1.00 38.09           O  
ANISOU 4756  O   TYR A 578     5813   4310   4351    -43   -137    -84       O  
ATOM   4757  CB  TYR A 578      -4.538   4.871  43.836  1.00 41.86           C  
ANISOU 4757  CB  TYR A 578     6282   4825   4797    -10   -104     22       C  
ATOM   4758  CG  TYR A 578      -3.098   5.318  43.977  1.00 42.03           C  
ANISOU 4758  CG  TYR A 578     6309   4817   4844    -93    -69     59       C  
ATOM   4759  CD1 TYR A 578      -2.785   6.639  44.314  1.00 41.05           C  
ANISOU 4759  CD1 TYR A 578     6235   4615   4747   -127    -57     58       C  
ATOM   4760  CD2 TYR A 578      -2.050   4.421  43.778  1.00 41.18           C  
ANISOU 4760  CD2 TYR A 578     6152   4757   4736   -136    -50     93       C  
ATOM   4761  CE1 TYR A 578      -1.468   7.057  44.441  1.00 37.90           C  
ANISOU 4761  CE1 TYR A 578     5834   4187   4382   -209    -28     90       C  
ATOM   4762  CE2 TYR A 578      -0.727   4.826  43.898  1.00 41.67           C  
ANISOU 4762  CE2 TYR A 578     6210   4798   4826   -212    -18    126       C  
ATOM   4763  CZ  TYR A 578      -0.443   6.149  44.228  1.00 42.53           C  
ANISOU 4763  CZ  TYR A 578     6364   4829   4967   -251     -8    125       C  
ATOM   4764  OH  TYR A 578       0.868   6.549  44.349  1.00 42.47           O  
ANISOU 4764  OH  TYR A 578     6344   4798   4995   -333     22    156       O  
ATOM   4765  N   ASP A 579      -4.087   4.736  47.220  1.00 41.37           N  
ANISOU 4765  N   ASP A 579     6117   4822   4778   -140   -128    -74       N  
ATOM   4766  CA  ASP A 579      -3.615   5.540  48.338  1.00 42.90           C  
ANISOU 4766  CA  ASP A 579     6318   4991   4993   -192   -131   -107       C  
ATOM   4767  C   ASP A 579      -2.347   4.918  48.939  1.00 43.77           C  
ANISOU 4767  C   ASP A 579     6371   5143   5117   -270   -122    -96       C  
ATOM   4768  O   ASP A 579      -2.376   3.835  49.560  1.00 42.00           O  
ANISOU 4768  O   ASP A 579     6084   4994   4880   -277   -130   -106       O  
ATOM   4769  CB  ASP A 579      -4.699   5.707  49.410  1.00 43.69           C  
ANISOU 4769  CB  ASP A 579     6407   5115   5080   -155   -158   -168       C  
ATOM   4770  CG  ASP A 579      -4.364   6.794  50.416  1.00 45.90           C  
ANISOU 4770  CG  ASP A 579     6714   5352   5376   -189   -168   -211       C  
ATOM   4771  OD1 ASP A 579      -5.309   7.408  50.946  1.00 54.92           O  
ANISOU 4771  OD1 ASP A 579     7880   6481   6505   -141   -187   -258       O  
ATOM   4772  OD2 ASP A 579      -3.169   7.045  50.687  1.00 46.76           O  
ANISOU 4772  OD2 ASP A 579     6818   5440   5509   -260   -160   -203       O  
ATOM   4773  N   LEU A 580      -1.242   5.635  48.761  1.00 43.44           N  
ANISOU 4773  N   LEU A 580     6351   5051   5103   -328   -104    -74       N  
ATOM   4774  CA  LEU A 580       0.070   5.162  49.157  1.00 42.23           C  
ANISOU 4774  CA  LEU A 580     6146   4934   4967   -401    -93    -60       C  
ATOM   4775  C   LEU A 580       0.158   5.016  50.672  1.00 42.98           C  
ANISOU 4775  C   LEU A 580     6198   5071   5060   -430   -120   -116       C  
ATOM   4776  O   LEU A 580       0.872   4.146  51.161  1.00 43.62           O  
ANISOU 4776  O   LEU A 580     6219   5217   5137   -465   -120   -112       O  
ATOM   4777  CB  LEU A 580       1.144   6.114  48.631  1.00 43.45           C  
ANISOU 4777  CB  LEU A 580     6332   5017   5159   -458    -68    -25       C  
ATOM   4778  CG  LEU A 580       2.252   5.519  47.761  1.00 42.85           C  
ANISOU 4778  CG  LEU A 580     6226   4968   5089   -492    -34     40       C  
ATOM   4779  CD1 LEU A 580       1.694   4.539  46.762  1.00 38.20           C  
ANISOU 4779  CD1 LEU A 580     5633   4421   4459   -423    -24     74       C  
ATOM   4780  CD2 LEU A 580       2.986   6.620  47.046  1.00 40.33           C  
ANISOU 4780  CD2 LEU A 580     5951   4566   4807   -532     -2     84       C  
ATOM   4781  N   ARG A 581      -0.580   5.847  51.409  1.00 42.10           N  
ANISOU 4781  N   ARG A 581     6120   4929   4947   -407   -143   -170       N  
ATOM   4782  CA  ARG A 581      -0.695   5.675  52.864  1.00 42.07           C  
ANISOU 4782  CA  ARG A 581     6079   4976   4928   -414   -169   -227       C  
ATOM   4783  C   ARG A 581      -1.282   4.307  53.208  1.00 40.75           C  
ANISOU 4783  C   ARG A 581     5854   4904   4727   -379   -169   -221       C  
ATOM   4784  O   ARG A 581      -0.821   3.650  54.145  1.00 42.70           O  
ANISOU 4784  O   ARG A 581     6049   5215   4961   -404   -177   -234       O  
ATOM   4785  CB  ARG A 581      -1.548   6.774  53.502  1.00 42.36           C  
ANISOU 4785  CB  ARG A 581     6166   4968   4962   -377   -193   -286       C  
ATOM   4786  CG  ARG A 581      -0.953   8.185  53.452  1.00 43.04           C  
ANISOU 4786  CG  ARG A 581     6310   4954   5090   -416   -201   -305       C  
ATOM   4787  CD  ARG A 581      -1.997   9.205  53.883  1.00 44.37           C  
ANISOU 4787  CD  ARG A 581     6538   5073   5249   -359   -225   -361       C  
ATOM   4788  NE  ARG A 581      -3.216   9.093  53.076  1.00 44.63           N  
ANISOU 4788  NE  ARG A 581     6598   5102   5257   -281   -215   -340       N  
ATOM   4789  CZ  ARG A 581      -4.370   9.705  53.338  1.00 45.50           C  
ANISOU 4789  CZ  ARG A 581     6748   5194   5347   -210   -232   -382       C  
ATOM   4790  NH1 ARG A 581      -4.505  10.488  54.405  1.00 48.76           N  
ANISOU 4790  NH1 ARG A 581     7182   5589   5757   -202   -261   -450       N  
ATOM   4791  NH2 ARG A 581      -5.401   9.527  52.526  1.00 45.26           N  
ANISOU 4791  NH2 ARG A 581     6734   5166   5296   -142   -224   -360       N  
ATOM   4792  N   ASN A 582      -2.295   3.881  52.454  1.00 38.41           N  
ANISOU 4792  N   ASN A 582     5565   4612   4415   -322   -163   -200       N  
ATOM   4793  CA  ASN A 582      -2.894   2.570  52.675  1.00 37.32           C  
ANISOU 4793  CA  ASN A 582     5372   4553   4257   -293   -164   -190       C  
ATOM   4794  C   ASN A 582      -1.997   1.415  52.212  1.00 38.59           C  
ANISOU 4794  C   ASN A 582     5489   4753   4421   -326   -151   -144       C  
ATOM   4795  O   ASN A 582      -1.894   0.397  52.904  1.00 37.86           O  
ANISOU 4795  O   ASN A 582     5341   4726   4317   -335   -154   -141       O  
ATOM   4796  CB  ASN A 582      -4.306   2.486  52.079  1.00 36.74           C  
ANISOU 4796  CB  ASN A 582     5314   4474   4173   -222   -169   -192       C  
ATOM   4797  CG  ASN A 582      -5.353   3.214  52.938  1.00 38.26           C  
ANISOU 4797  CG  ASN A 582     5521   4667   4351   -179   -183   -243       C  
ATOM   4798  OD1 ASN A 582      -5.123   3.479  54.116  1.00 37.35           O  
ANISOU 4798  OD1 ASN A 582     5393   4574   4224   -197   -190   -278       O  
ATOM   4799  ND2 ASN A 582      -6.505   3.532  52.345  1.00 37.49           N  
ANISOU 4799  ND2 ASN A 582     5449   4547   4247   -117   -189   -251       N  
ATOM   4800  N   ALA A 583      -1.333   1.574  51.064  1.00 39.28           N  
ANISOU 4800  N   ALA A 583     5600   4801   4522   -341   -136   -105       N  
ATOM   4801  CA  ALA A 583      -0.372   0.566  50.605  1.00 37.30           C  
ANISOU 4801  CA  ALA A 583     5311   4588   4273   -369   -123    -64       C  
ATOM   4802  C   ALA A 583       0.772   0.437  51.614  1.00 37.89           C  
ANISOU 4802  C   ALA A 583     5345   4699   4354   -430   -124    -74       C  
ATOM   4803  O   ALA A 583       1.167  -0.673  51.982  1.00 39.68           O  
ANISOU 4803  O   ALA A 583     5520   4987   4569   -439   -126    -62       O  
ATOM   4804  CB  ALA A 583       0.150   0.900  49.216  1.00 36.02           C  
ANISOU 4804  CB  ALA A 583     5186   4382   4120   -367   -101    -19       C  
ATOM   4805  N   THR A 584       1.264   1.580  52.081  1.00 36.57           N  
ANISOU 4805  N   THR A 584     5201   4489   4203   -468   -128   -101       N  
ATOM   4806  CA  THR A 584       2.352   1.632  53.063  1.00 39.15           C  
ANISOU 4806  CA  THR A 584     5491   4846   4539   -526   -137   -122       C  
ATOM   4807  C   THR A 584       1.945   1.026  54.410  1.00 38.06           C  
ANISOU 4807  C   THR A 584     5314   4776   4371   -509   -158   -159       C  
ATOM   4808  O   THR A 584       2.730   0.329  55.045  1.00 38.96           O  
ANISOU 4808  O   THR A 584     5380   4949   4476   -535   -163   -157       O  
ATOM   4809  CB  THR A 584       2.900   3.095  53.240  1.00 37.90           C  
ANISOU 4809  CB  THR A 584     5370   4615   4415   -571   -142   -149       C  
ATOM   4810  OG1 THR A 584       3.744   3.419  52.128  1.00 42.64           O  
ANISOU 4810  OG1 THR A 584     5983   5172   5045   -607   -115   -100       O  
ATOM   4811  CG2 THR A 584       3.730   3.227  54.476  1.00 42.69           C  
ANISOU 4811  CG2 THR A 584     5939   5255   5027   -619   -166   -193       C  
ATOM   4812  N   ALA A 585       0.718   1.292  54.841  1.00 36.76           N  
ANISOU 4812  N   ALA A 585     5171   4607   4188   -461   -168   -189       N  
ATOM   4813  CA  ALA A 585       0.210   0.710  56.074  1.00 36.06           C  
ANISOU 4813  CA  ALA A 585     5047   4588   4067   -437   -180   -215       C  
ATOM   4814  C   ALA A 585       0.371  -0.800  56.038  1.00 34.58           C  
ANISOU 4814  C   ALA A 585     4806   4466   3867   -433   -170   -173       C  
ATOM   4815  O   ALA A 585       0.787  -1.410  57.005  1.00 36.35           O  
ANISOU 4815  O   ALA A 585     4989   4751   4070   -442   -176   -179       O  
ATOM   4816  CB  ALA A 585      -1.249   1.086  56.269  1.00 35.62           C  
ANISOU 4816  CB  ALA A 585     5016   4522   3996   -377   -184   -240       C  
ATOM   4817  N   ILE A 586       0.057  -1.391  54.896  1.00 36.79           N  
ANISOU 4817  N   ILE A 586     5089   4732   4159   -415   -157   -132       N  
ATOM   4818  CA  ILE A 586       0.045  -2.833  54.753  1.00 35.89           C  
ANISOU 4818  CA  ILE A 586     4931   4666   4038   -404   -152    -95       C  
ATOM   4819  C   ILE A 586       1.475  -3.353  54.884  1.00 37.16           C  
ANISOU 4819  C   ILE A 586     5060   4860   4199   -447   -150    -77       C  
ATOM   4820  O   ILE A 586       1.769  -4.184  55.749  1.00 38.10           O  
ANISOU 4820  O   ILE A 586     5139   5038   4300   -451   -155    -72       O  
ATOM   4821  CB  ILE A 586      -0.599  -3.225  53.406  1.00 35.46           C  
ANISOU 4821  CB  ILE A 586     4894   4581   3999   -371   -147    -67       C  
ATOM   4822  CG1 ILE A 586      -2.101  -2.900  53.424  1.00 33.23           C  
ANISOU 4822  CG1 ILE A 586     4629   4283   3716   -324   -153    -87       C  
ATOM   4823  CG2 ILE A 586      -0.372  -4.689  53.083  1.00 34.61           C  
ANISOU 4823  CG2 ILE A 586     4747   4511   3893   -366   -147    -30       C  
ATOM   4824  CD1 ILE A 586      -2.747  -2.868  52.043  1.00 30.86           C  
ANISOU 4824  CD1 ILE A 586     4358   3940   3428   -286   -156    -73       C  
ATOM   4825  N   THR A 587       2.368  -2.814  54.065  1.00 35.76           N  
ANISOU 4825  N   THR A 587     4901   4646   4041   -478   -142    -64       N  
ATOM   4826  CA  THR A 587       3.730  -3.330  53.965  1.00 36.63           C  
ANISOU 4826  CA  THR A 587     4976   4788   4153   -514   -137    -41       C  
ATOM   4827  C   THR A 587       4.562  -3.093  55.233  1.00 38.38           C  
ANISOU 4827  C   THR A 587     5166   5049   4366   -552   -152    -74       C  
ATOM   4828  O   THR A 587       5.373  -3.940  55.635  1.00 38.01           O  
ANISOU 4828  O   THR A 587     5076   5060   4308   -563   -155    -61       O  
ATOM   4829  CB  THR A 587       4.432  -2.764  52.733  1.00 36.85           C  
ANISOU 4829  CB  THR A 587     5027   4770   4204   -536   -118    -14       C  
ATOM   4830  OG1 THR A 587       4.486  -1.332  52.826  1.00 39.09           O  
ANISOU 4830  OG1 THR A 587     5347   4996   4509   -564   -118    -40       O  
ATOM   4831  CG2 THR A 587       3.651  -3.163  51.459  1.00 35.99           C  
ANISOU 4831  CG2 THR A 587     4947   4635   4094   -487   -108     17       C  
ATOM   4832  N   THR A 588       4.338  -1.956  55.878  1.00 39.07           N  
ANISOU 4832  N   THR A 588     5279   5107   4458   -564   -164   -119       N  
ATOM   4833  CA  THR A 588       5.074  -1.620  57.095  1.00 39.66           C  
ANISOU 4833  CA  THR A 588     5329   5217   4524   -594   -187   -162       C  
ATOM   4834  C   THR A 588       4.584  -2.466  58.277  1.00 38.37           C  
ANISOU 4834  C   THR A 588     5136   5126   4316   -556   -198   -173       C  
ATOM   4835  O   THR A 588       5.379  -2.914  59.101  1.00 38.01           O  
ANISOU 4835  O   THR A 588     5052   5139   4250   -569   -211   -182       O  
ATOM   4836  CB  THR A 588       4.995  -0.105  57.373  1.00 39.32           C  
ANISOU 4836  CB  THR A 588     5326   5112   4503   -616   -202   -212       C  
ATOM   4837  OG1 THR A 588       5.102   0.587  56.127  1.00 35.49           O  
ANISOU 4837  OG1 THR A 588     4878   4551   4057   -636   -183   -186       O  
ATOM   4838  CG2 THR A 588       6.129   0.345  58.275  1.00 39.64           C  
ANISOU 4838  CG2 THR A 588     5337   5174   4550   -663   -229   -255       C  
ATOM   4839  N   PHE A 589       3.279  -2.713  58.336  1.00 37.93           N  
ANISOU 4839  N   PHE A 589     5098   5069   4246   -509   -190   -168       N  
ATOM   4840  CA  PHE A 589       2.724  -3.631  59.336  1.00 37.94           C  
ANISOU 4840  CA  PHE A 589     5069   5138   4208   -472   -190   -161       C  
ATOM   4841  C   PHE A 589       3.337  -5.017  59.141  1.00 35.47           C  
ANISOU 4841  C   PHE A 589     4716   4870   3891   -476   -182   -112       C  
ATOM   4842  O   PHE A 589       3.719  -5.679  60.106  1.00 36.83           O  
ANISOU 4842  O   PHE A 589     4856   5106   4033   -468   -188   -109       O  
ATOM   4843  CB  PHE A 589       1.193  -3.682  59.224  1.00 36.74           C  
ANISOU 4843  CB  PHE A 589     4935   4973   4053   -426   -178   -156       C  
ATOM   4844  CG  PHE A 589       0.501  -4.380  60.374  1.00 36.24           C  
ANISOU 4844  CG  PHE A 589     4842   4976   3951   -388   -172   -151       C  
ATOM   4845  CD1 PHE A 589       0.370  -5.774  60.395  1.00 35.66           C  
ANISOU 4845  CD1 PHE A 589     4732   4942   3874   -377   -158    -99       C  
ATOM   4846  CD2 PHE A 589      -0.068  -3.641  61.410  1.00 36.16           C  
ANISOU 4846  CD2 PHE A 589     4844   4988   3908   -360   -178   -195       C  
ATOM   4847  CE1 PHE A 589      -0.302  -6.419  61.442  1.00 32.93           C  
ANISOU 4847  CE1 PHE A 589     4360   4656   3496   -344   -146    -84       C  
ATOM   4848  CE2 PHE A 589      -0.734  -4.271  62.460  1.00 35.72           C  
ANISOU 4848  CE2 PHE A 589     4760   5000   3813   -321   -166   -183       C  
ATOM   4849  CZ  PHE A 589      -0.849  -5.669  62.475  1.00 36.14           C  
ANISOU 4849  CZ  PHE A 589     4774   5091   3865   -315   -147   -123       C  
ATOM   4850  N   GLY A 590       3.440  -5.434  57.882  1.00 34.57           N  
ANISOU 4850  N   GLY A 590     4607   4723   3806   -481   -170    -75       N  
ATOM   4851  CA  GLY A 590       4.094  -6.684  57.520  1.00 34.35           C  
ANISOU 4851  CA  GLY A 590     4547   4727   3777   -481   -166    -32       C  
ATOM   4852  C   GLY A 590       5.514  -6.770  58.033  1.00 36.56           C  
ANISOU 4852  C   GLY A 590     4795   5050   4045   -512   -176    -40       C  
ATOM   4853  O   GLY A 590       5.891  -7.768  58.651  1.00 37.04           O  
ANISOU 4853  O   GLY A 590     4823   5167   4082   -499   -180    -21       O  
ATOM   4854  N   GLN A 591       6.303  -5.723  57.789  1.00 37.99           N  
ANISOU 4854  N   GLN A 591     4984   5205   4245   -552   -181    -65       N  
ATOM   4855  CA  GLN A 591       7.693  -5.683  58.248  1.00 39.74           C  
ANISOU 4855  CA  GLN A 591     5168   5469   4463   -587   -194    -79       C  
ATOM   4856  C   GLN A 591       7.783  -5.848  59.758  1.00 41.94           C  
ANISOU 4856  C   GLN A 591     5424   5810   4702   -573   -217   -111       C  
ATOM   4857  O   GLN A 591       8.637  -6.574  60.263  1.00 44.50           O  
ANISOU 4857  O   GLN A 591     5708   6195   5005   -572   -227   -104       O  
ATOM   4858  CB  GLN A 591       8.373  -4.380  57.829  1.00 41.56           C  
ANISOU 4858  CB  GLN A 591     5409   5651   4730   -639   -196   -105       C  
ATOM   4859  CG  GLN A 591       8.761  -4.309  56.353  1.00 40.30           C  
ANISOU 4859  CG  GLN A 591     5259   5450   4603   -657   -170    -63       C  
ATOM   4860  CD  GLN A 591       9.818  -3.251  56.077  1.00 43.18           C  
ANISOU 4860  CD  GLN A 591     5614   5785   5006   -719   -168    -76       C  
ATOM   4861  OE1 GLN A 591      10.446  -2.715  57.003  1.00 41.95           O  
ANISOU 4861  OE1 GLN A 591     5434   5648   4857   -753   -193   -120       O  
ATOM   4862  NE2 GLN A 591      10.022  -2.940  54.796  1.00 43.55           N  
ANISOU 4862  NE2 GLN A 591     5679   5788   5082   -732   -138    -37       N  
ATOM   4863  N   MET A 592       6.888  -5.172  60.472  1.00 41.58           N  
ANISOU 4863  N   MET A 592     5405   5753   4642   -556   -225   -148       N  
ATOM   4864  CA  MET A 592       6.795  -5.299  61.915  1.00 40.17           C  
ANISOU 4864  CA  MET A 592     5211   5636   4415   -529   -243   -178       C  
ATOM   4865  C   MET A 592       6.424  -6.713  62.348  1.00 39.73           C  
ANISOU 4865  C   MET A 592     5134   5638   4324   -485   -230   -130       C  
ATOM   4866  O   MET A 592       7.107  -7.294  63.189  1.00 40.47           O  
ANISOU 4866  O   MET A 592     5197   5798   4383   -473   -243   -130       O  
ATOM   4867  CB  MET A 592       5.779  -4.304  62.476  1.00 40.89           C  
ANISOU 4867  CB  MET A 592     5339   5702   4494   -508   -250   -224       C  
ATOM   4868  CG  MET A 592       5.744  -4.265  63.997  1.00 41.92           C  
ANISOU 4868  CG  MET A 592     5458   5902   4569   -474   -271   -264       C  
ATOM   4869  SD  MET A 592       4.386  -3.268  64.615  1.00 44.73           S  
ANISOU 4869  SD  MET A 592     5857   6238   4902   -432   -273   -311       S  
ATOM   4870  CE  MET A 592       2.970  -4.256  64.126  1.00 39.51           C  
ANISOU 4870  CE  MET A 592     5197   5576   4240   -392   -228   -241       C  
ATOM   4871  N   ALA A 593       5.348  -7.260  61.781  1.00 37.82           N  
ANISOU 4871  N   ALA A 593     4906   5368   4094   -461   -205    -90       N  
ATOM   4872  CA  ALA A 593       4.843  -8.584  62.178  1.00 36.75           C  
ANISOU 4872  CA  ALA A 593     4752   5274   3936   -424   -190    -40       C  
ATOM   4873  C   ALA A 593       5.939  -9.655  62.179  1.00 37.20           C  
ANISOU 4873  C   ALA A 593     4777   5372   3985   -426   -196     -7       C  
ATOM   4874  O   ALA A 593       6.070 -10.431  63.135  1.00 36.34           O  
ANISOU 4874  O   ALA A 593     4648   5322   3836   -398   -197     12       O  
ATOM   4875  CB  ALA A 593       3.695  -9.003  61.279  1.00 34.99           C  
ANISOU 4875  CB  ALA A 593     4544   5003   3747   -410   -170     -5       C  
ATOM   4876  N   LEU A 594       6.725  -9.668  61.105  1.00 37.55           N  
ANISOU 4876  N   LEU A 594     4818   5387   4062   -454   -199      1       N  
ATOM   4877  CA  LEU A 594       7.782 -10.646  60.894  1.00 37.94           C  
ANISOU 4877  CA  LEU A 594     4837   5471   4106   -453   -204     30       C  
ATOM   4878  C   LEU A 594       8.912 -10.493  61.904  1.00 39.46           C  
ANISOU 4878  C   LEU A 594     5000   5731   4264   -459   -227      1       C  
ATOM   4879  O   LEU A 594       9.361 -11.481  62.500  1.00 39.27           O  
ANISOU 4879  O   LEU A 594     4952   5762   4209   -431   -232     26       O  
ATOM   4880  CB  LEU A 594       8.336 -10.532  59.467  1.00 38.61           C  
ANISOU 4880  CB  LEU A 594     4926   5513   4231   -478   -197     42       C  
ATOM   4881  CG  LEU A 594       9.334 -11.624  59.075  1.00 42.38           C  
ANISOU 4881  CG  LEU A 594     5375   6023   4703   -467   -200     75       C  
ATOM   4882  CD1 LEU A 594       8.667 -12.993  59.170  1.00 44.13           C  
ANISOU 4882  CD1 LEU A 594     5600   6248   4918   -424   -196    120       C  
ATOM   4883  CD2 LEU A 594       9.887 -11.392  57.688  1.00 40.17           C  
ANISOU 4883  CD2 LEU A 594     5098   5710   4456   -486   -190     85       C  
ATOM   4884  N   GLN A 595       9.371  -9.260  62.095  1.00 37.87           N  
ANISOU 4884  N   GLN A 595     4797   5521   4069   -494   -243    -53       N  
ATOM   4885  CA  GLN A 595      10.480  -9.022  62.996  1.00 39.91           C  
ANISOU 4885  CA  GLN A 595     5021   5840   4301   -503   -272    -91       C  
ATOM   4886  C   GLN A 595      10.031  -9.186  64.439  1.00 41.23           C  
ANISOU 4886  C   GLN A 595     5191   6065   4410   -459   -285   -108       C  
ATOM   4887  O   GLN A 595      10.770  -9.714  65.272  1.00 45.25           O  
ANISOU 4887  O   GLN A 595     5670   6645   4878   -436   -304   -112       O  
ATOM   4888  CB  GLN A 595      11.129  -7.663  62.716  1.00 41.78           C  
ANISOU 4888  CB  GLN A 595     5255   6044   4575   -560   -289   -145       C  
ATOM   4889  CG  GLN A 595      12.217  -7.739  61.638  1.00 41.99           C  
ANISOU 4889  CG  GLN A 595     5253   6060   4642   -600   -281   -124       C  
ATOM   4890  CD  GLN A 595      12.346  -6.480  60.791  1.00 45.90           C  
ANISOU 4890  CD  GLN A 595     5764   6483   5192   -656   -274   -144       C  
ATOM   4891  OE1 GLN A 595      13.402  -5.845  60.760  1.00 44.57           O  
ANISOU 4891  OE1 GLN A 595     5563   6321   5052   -704   -288   -171       O  
ATOM   4892  NE2 GLN A 595      11.280  -6.131  60.076  1.00 44.65           N  
ANISOU 4892  NE2 GLN A 595     5655   6256   5054   -651   -250   -127       N  
ATOM   4893  N   TRP A 596       8.800  -8.769  64.714  1.00 42.60           N  
ANISOU 4893  N   TRP A 596     5397   6211   4576   -441   -272   -116       N  
ATOM   4894  CA  TRP A 596       8.156  -9.003  65.998  1.00 41.88           C  
ANISOU 4894  CA  TRP A 596     5311   6175   4426   -389   -272   -119       C  
ATOM   4895  C   TRP A 596       8.188 -10.496  66.319  1.00 42.24           C  
ANISOU 4895  C   TRP A 596     5339   6269   4442   -349   -255    -53       C  
ATOM   4896  O   TRP A 596       8.695 -10.898  67.367  1.00 44.91           O  
ANISOU 4896  O   TRP A 596     5659   6680   4725   -315   -270    -56       O  
ATOM   4897  CB  TRP A 596       6.712  -8.480  65.972  1.00 41.07           C  
ANISOU 4897  CB  TRP A 596     5244   6032   4330   -374   -250   -122       C  
ATOM   4898  CG  TRP A 596       5.919  -8.754  67.207  1.00 40.31           C  
ANISOU 4898  CG  TRP A 596     5151   5994   4173   -317   -239   -115       C  
ATOM   4899  CD1 TRP A 596       5.292  -9.920  67.534  1.00 40.76           C  
ANISOU 4899  CD1 TRP A 596     5198   6081   4208   -279   -208    -48       C  
ATOM   4900  CD2 TRP A 596       5.647  -7.836  68.276  1.00 39.71           C  
ANISOU 4900  CD2 TRP A 596     5087   5952   4049   -288   -257   -176       C  
ATOM   4901  NE1 TRP A 596       4.654  -9.790  68.752  1.00 41.45           N  
ANISOU 4901  NE1 TRP A 596     5288   6226   4233   -228   -199    -56       N  
ATOM   4902  CE2 TRP A 596       4.852  -8.520  69.224  1.00 40.24           C  
ANISOU 4902  CE2 TRP A 596     5150   6079   4060   -228   -230   -137       C  
ATOM   4903  CE3 TRP A 596       5.995  -6.504  68.524  1.00 38.81           C  
ANISOU 4903  CE3 TRP A 596     4988   5821   3936   -306   -293   -260       C  
ATOM   4904  CZ2 TRP A 596       4.404  -7.918  70.408  1.00 43.46           C  
ANISOU 4904  CZ2 TRP A 596     5569   6540   4403   -178   -237   -180       C  
ATOM   4905  CZ3 TRP A 596       5.551  -5.906  69.699  1.00 42.66           C  
ANISOU 4905  CZ3 TRP A 596     5490   6355   4365   -257   -307   -309       C  
ATOM   4906  CH2 TRP A 596       4.765  -6.615  70.629  1.00 41.91           C  
ANISOU 4906  CH2 TRP A 596     5391   6329   4204   -190   -278   -270       C  
ATOM   4907  N   ILE A 597       7.669 -11.322  65.414  1.00 40.04           N  
ANISOU 4907  N   ILE A 597     5067   5948   4200   -351   -228      6       N  
ATOM   4908  CA  ILE A 597       7.551 -12.747  65.717  1.00 39.55           C  
ANISOU 4908  CA  ILE A 597     4993   5916   4117   -313   -212     72       C  
ATOM   4909  C   ILE A 597       8.909 -13.459  65.756  1.00 39.97           C  
ANISOU 4909  C   ILE A 597     5018   6012   4155   -308   -233     83       C  
ATOM   4910  O   ILE A 597       9.054 -14.453  66.470  1.00 39.84           O  
ANISOU 4910  O   ILE A 597     4993   6044   4100   -267   -230    123       O  
ATOM   4911  CB  ILE A 597       6.501 -13.469  64.821  1.00 37.12           C  
ANISOU 4911  CB  ILE A 597     4700   5547   3857   -314   -183    127       C  
ATOM   4912  CG1 ILE A 597       5.837 -14.621  65.583  1.00 38.45           C  
ANISOU 4912  CG1 ILE A 597     4863   5744   4002   -272   -160    190       C  
ATOM   4913  CG2 ILE A 597       7.109 -13.939  63.503  1.00 38.65           C  
ANISOU 4913  CG2 ILE A 597     4891   5697   4098   -337   -189    144       C  
ATOM   4914  CD1 ILE A 597       5.010 -14.183  66.801  1.00 41.82           C  
ANISOU 4914  CD1 ILE A 597     5294   6215   4382   -242   -144    183       C  
ATOM   4915  N   GLU A 598       9.886 -12.934  65.005  1.00 39.26           N  
ANISOU 4915  N   GLU A 598     4915   5908   4095   -348   -252     50       N  
ATOM   4916  CA  GLU A 598      11.289 -13.356  65.112  1.00 39.39           C  
ANISOU 4916  CA  GLU A 598     4896   5977   4094   -345   -275     45       C  
ATOM   4917  C   GLU A 598      11.794 -13.209  66.551  1.00 40.45           C  
ANISOU 4917  C   GLU A 598     5012   6194   4164   -314   -302     12       C  
ATOM   4918  O   GLU A 598      12.363 -14.145  67.130  1.00 40.10           O  
ANISOU 4918  O   GLU A 598     4950   6208   4078   -273   -311     39       O  
ATOM   4919  CB  GLU A 598      12.186 -12.538  64.176  1.00 38.66           C  
ANISOU 4919  CB  GLU A 598     4785   5858   4045   -399   -287      8       C  
ATOM   4920  CG  GLU A 598      13.666 -12.934  64.240  1.00 40.46           C  
ANISOU 4920  CG  GLU A 598     4966   6147   4260   -398   -311      1       C  
ATOM   4921  CD  GLU A 598      14.605 -11.992  63.478  1.00 42.06           C  
ANISOU 4921  CD  GLU A 598     5140   6334   4506   -457   -320    -36       C  
ATOM   4922  OE1 GLU A 598      14.241 -10.824  63.209  1.00 44.04           O  
ANISOU 4922  OE1 GLU A 598     5409   6535   4791   -501   -318    -71       O  
ATOM   4923  OE2 GLU A 598      15.733 -12.422  63.166  1.00 40.08           O  
ANISOU 4923  OE2 GLU A 598     4848   6123   4258   -459   -329    -29       O  
ATOM   4924  N   ARG A 599      11.589 -12.031  67.124  1.00 39.31           N  
ANISOU 4924  N   ARG A 599     4875   6054   4008   -329   -318    -49       N  
ATOM   4925  CA  ARG A 599      11.988 -11.798  68.497  1.00 40.25           C  
ANISOU 4925  CA  ARG A 599     4981   6252   4062   -293   -349    -91       C  
ATOM   4926  C   ARG A 599      11.304 -12.808  69.423  1.00 40.00           C  
ANISOU 4926  C   ARG A 599     4963   6267   3968   -224   -327    -35       C  
ATOM   4927  O   ARG A 599      11.957 -13.423  70.272  1.00 41.20           O  
ANISOU 4927  O   ARG A 599     5097   6494   4063   -178   -344    -27       O  
ATOM   4928  CB  ARG A 599      11.664 -10.363  68.904  1.00 41.47           C  
ANISOU 4928  CB  ARG A 599     5150   6390   4217   -314   -369   -168       C  
ATOM   4929  CG  ARG A 599      12.118 -10.002  70.306  1.00 42.49           C  
ANISOU 4929  CG  ARG A 599     5266   6600   4276   -275   -410   -226       C  
ATOM   4930  CD  ARG A 599      11.879  -8.525  70.593  1.00 43.96           C  
ANISOU 4930  CD  ARG A 599     5470   6759   4475   -299   -438   -312       C  
ATOM   4931  NE  ARG A 599      10.463  -8.151  70.555  1.00 46.04           N  
ANISOU 4931  NE  ARG A 599     5777   6976   4738   -285   -405   -300       N  
ATOM   4932  CZ  ARG A 599       9.570  -8.464  71.493  1.00 46.17           C  
ANISOU 4932  CZ  ARG A 599     5813   7039   4689   -218   -387   -282       C  
ATOM   4933  NH1 ARG A 599       9.930  -9.189  72.546  1.00 44.85           N  
ANISOU 4933  NH1 ARG A 599     5631   6963   4447   -158   -396   -267       N  
ATOM   4934  NH2 ARG A 599       8.312  -8.057  71.376  1.00 46.77           N  
ANISOU 4934  NH2 ARG A 599     5923   7075   4773   -209   -356   -274       N  
ATOM   4935  N   LYS A 600      10.004 -13.005  69.218  1.00 39.28           N  
ANISOU 4935  N   LYS A 600     4902   6132   3892   -216   -287      7       N  
ATOM   4936  CA  LYS A 600       9.188 -13.853  70.090  1.00 40.57           C  
ANISOU 4936  CA  LYS A 600     5077   6332   4006   -157   -257     66       C  
ATOM   4937  C   LYS A 600       9.570 -15.326  70.034  1.00 41.23           C  
ANISOU 4937  C   LYS A 600     5151   6431   4082   -129   -245    142       C  
ATOM   4938  O   LYS A 600       9.608 -16.000  71.061  1.00 41.67           O  
ANISOU 4938  O   LYS A 600     5206   6551   4076    -72   -239    177       O  
ATOM   4939  CB  LYS A 600       7.697 -13.675  69.783  1.00 39.70           C  
ANISOU 4939  CB  LYS A 600     4991   6167   3926   -164   -217     93       C  
ATOM   4940  CG  LYS A 600       7.107 -12.358  70.258  1.00 39.77           C  
ANISOU 4940  CG  LYS A 600     5016   6178   3916   -163   -224     27       C  
ATOM   4941  CD  LYS A 600       6.952 -12.328  71.781  1.00 42.96           C  
ANISOU 4941  CD  LYS A 600     5421   6673   4229    -97   -226     18       C  
ATOM   4942  CE  LYS A 600       5.941 -11.283  72.239  1.00 40.80           C  
ANISOU 4942  CE  LYS A 600     5169   6399   3936    -80   -217    -26       C  
ATOM   4943  NZ  LYS A 600       5.789 -11.304  73.728  1.00 44.33           N  
ANISOU 4943  NZ  LYS A 600     5617   6941   4284     -4   -216    -33       N  
ATOM   4944  N   VAL A 601       9.857 -15.822  68.835  1.00 43.87           N  
ANISOU 4944  N   VAL A 601     5481   6708   4478   -163   -242    167       N  
ATOM   4945  CA  VAL A 601      10.249 -17.219  68.660  1.00 44.46           C  
ANISOU 4945  CA  VAL A 601     5551   6787   4554   -135   -236    234       C  
ATOM   4946  C   VAL A 601      11.615 -17.494  69.286  1.00 45.88           C  
ANISOU 4946  C   VAL A 601     5706   7046   4681   -103   -271    215       C  
ATOM   4947  O   VAL A 601      11.771 -18.485  69.999  1.00 47.86           O  
ANISOU 4947  O   VAL A 601     5958   7339   4886    -48   -266    265       O  
ATOM   4948  CB  VAL A 601      10.217 -17.636  67.190  1.00 43.55           C  
ANISOU 4948  CB  VAL A 601     5440   6593   4513   -171   -229    256       C  
ATOM   4949  CG1 VAL A 601      10.977 -18.940  66.980  1.00 44.28           C  
ANISOU 4949  CG1 VAL A 601     5525   6695   4603   -140   -236    304       C  
ATOM   4950  CG2 VAL A 601       8.781 -17.765  66.726  1.00 43.72           C  
ANISOU 4950  CG2 VAL A 601     5486   6545   4581   -185   -195    291       C  
ATOM   4951  N   ASN A 602      12.588 -16.621  69.029  1.00 44.99           N  
ANISOU 4951  N   ASN A 602     5567   6952   4576   -135   -306    145       N  
ATOM   4952  CA  ASN A 602      13.882 -16.691  69.708  1.00 45.99           C  
ANISOU 4952  CA  ASN A 602     5660   7162   4652   -107   -346    112       C  
ATOM   4953  C   ASN A 602      13.730 -16.711  71.233  1.00 47.12           C  
ANISOU 4953  C   ASN A 602     5810   7385   4710    -45   -355    106       C  
ATOM   4954  O   ASN A 602      14.250 -17.614  71.900  1.00 46.68           O  
ANISOU 4954  O   ASN A 602     5748   7390   4600     14   -364    141       O  
ATOM   4955  CB  ASN A 602      14.783 -15.527  69.288  1.00 46.16           C  
ANISOU 4955  CB  ASN A 602     5648   7187   4705   -163   -380     31       C  
ATOM   4956  CG  ASN A 602      15.456 -15.756  67.942  1.00 48.70           C  
ANISOU 4956  CG  ASN A 602     5948   7467   5087   -204   -377     43       C  
ATOM   4957  OD1 ASN A 602      15.362 -16.839  67.349  1.00 48.41           O  
ANISOU 4957  OD1 ASN A 602     5922   7406   5065   -182   -357    104       O  
ATOM   4958  ND2 ASN A 602      16.151 -14.730  67.456  1.00 46.88           N  
ANISOU 4958  ND2 ASN A 602     5689   7230   4895   -260   -397    -16       N  
ATOM   4959  N   GLU A 603      13.005 -15.726  71.772  1.00 46.43           N  
ANISOU 4959  N   GLU A 603     5737   7298   4605    -51   -353     64       N  
ATOM   4960  CA  GLU A 603      12.715 -15.658  73.213  1.00 45.88           C  
ANISOU 4960  CA  GLU A 603     5679   7307   4448     15   -358     56       C  
ATOM   4961  C   GLU A 603      12.158 -16.977  73.751  1.00 46.72           C  
ANISOU 4961  C   GLU A 603     5806   7434   4512     78   -317    156       C  
ATOM   4962  O   GLU A 603      12.630 -17.484  74.783  1.00 47.93           O  
ANISOU 4962  O   GLU A 603     5956   7670   4586    147   -331    170       O  
ATOM   4963  CB  GLU A 603      11.747 -14.510  73.530  1.00 45.07           C  
ANISOU 4963  CB  GLU A 603     5598   7186   4342      2   -350      9       C  
ATOM   4964  CG  GLU A 603      12.375 -13.115  73.469  1.00 44.93           C  
ANISOU 4964  CG  GLU A 603     5564   7166   4342    -42   -401    -99       C  
ATOM   4965  CD  GLU A 603      11.406 -12.012  73.866  1.00 47.18           C  
ANISOU 4965  CD  GLU A 603     5876   7433   4616    -42   -397   -148       C  
ATOM   4966  OE1 GLU A 603      10.219 -12.323  74.118  1.00 43.92           O  
ANISOU 4966  OE1 GLU A 603     5490   7013   4184    -10   -350    -96       O  
ATOM   4967  OE2 GLU A 603      11.830 -10.831  73.929  1.00 47.62           O  
ANISOU 4967  OE2 GLU A 603     5925   7482   4687    -74   -440   -240       O  
ATOM   4968  N   TYR A 604      11.179 -17.536  73.035  1.00 44.17           N  
ANISOU 4968  N   TYR A 604     5503   7035   4245     55   -270    224       N  
ATOM   4969  CA  TYR A 604      10.554 -18.791  73.417  1.00 43.23           C  
ANISOU 4969  CA  TYR A 604     5403   6916   4108    101   -227    325       C  
ATOM   4970  C   TYR A 604      11.549 -19.934  73.367  1.00 42.80           C  
ANISOU 4970  C   TYR A 604     5340   6882   4040    134   -243    368       C  
ATOM   4971  O   TYR A 604      11.706 -20.674  74.334  1.00 42.86           O  
ANISOU 4971  O   TYR A 604     5356   6949   3979    202   -236    416       O  
ATOM   4972  CB  TYR A 604       9.345 -19.113  72.530  1.00 44.83           C  
ANISOU 4972  CB  TYR A 604     5621   7023   4389     59   -182    379       C  
ATOM   4973  CG  TYR A 604       8.665 -20.418  72.896  1.00 45.67           C  
ANISOU 4973  CG  TYR A 604     5743   7119   4492     96   -137    486       C  
ATOM   4974  CD1 TYR A 604       8.781 -21.550  72.080  1.00 44.42           C  
ANISOU 4974  CD1 TYR A 604     5589   6895   4392     83   -131    546       C  
ATOM   4975  CD2 TYR A 604       7.927 -20.528  74.078  1.00 48.49           C  
ANISOU 4975  CD2 TYR A 604     6110   7530   4785    147   -101    530       C  
ATOM   4976  CE1 TYR A 604       8.158 -22.767  72.433  1.00 46.49           C  
ANISOU 4976  CE1 TYR A 604     5867   7137   4659    113    -92    647       C  
ATOM   4977  CE2 TYR A 604       7.305 -21.727  74.438  1.00 50.85           C  
ANISOU 4977  CE2 TYR A 604     6420   7815   5085    177    -55    638       C  
ATOM   4978  CZ  TYR A 604       7.423 -22.840  73.615  1.00 50.72           C  
ANISOU 4978  CZ  TYR A 604     6409   7725   5137    157    -52    696       C  
ATOM   4979  OH  TYR A 604       6.804 -24.009  73.993  1.00 51.88           O  
ANISOU 4979  OH  TYR A 604     6569   7849   5293    182     -7    803       O  
ATOM   4980  N   LEU A 605      12.230 -20.065  72.238  1.00 44.84           N  
ANISOU 4980  N   LEU A 605     5584   7094   4360     91   -264    350       N  
ATOM   4981  CA  LEU A 605      13.121 -21.196  72.016  1.00 45.47           C  
ANISOU 4981  CA  LEU A 605     5657   7183   4436    123   -278    391       C  
ATOM   4982  C   LEU A 605      14.360 -21.173  72.897  1.00 47.66           C  
ANISOU 4982  C   LEU A 605     5910   7564   4636    176   -322    354       C  
ATOM   4983  O   LEU A 605      14.968 -22.207  73.116  1.00 50.36           O  
ANISOU 4983  O   LEU A 605     6253   7933   4949    228   -329    399       O  
ATOM   4984  CB  LEU A 605      13.489 -21.315  70.537  1.00 43.53           C  
ANISOU 4984  CB  LEU A 605     5401   6866   4272     70   -286    380       C  
ATOM   4985  CG  LEU A 605      12.376 -21.852  69.632  1.00 43.34           C  
ANISOU 4985  CG  LEU A 605     5404   6740   4322     39   -249    435       C  
ATOM   4986  CD1 LEU A 605      12.852 -21.847  68.203  1.00 43.33           C  
ANISOU 4986  CD1 LEU A 605     5393   6682   4387     -3   -263    412       C  
ATOM   4987  CD2 LEU A 605      11.925 -23.265  70.028  1.00 43.04           C  
ANISOU 4987  CD2 LEU A 605     5393   6684   4278     87   -224    530       C  
ATOM   4988  N   ASN A 606      14.733 -20.001  73.399  1.00 49.69           N  
ANISOU 4988  N   ASN A 606     6145   7875   4861    165   -354    268       N  
ATOM   4989  CA  ASN A 606      15.776 -19.916  74.413  1.00 51.85           C  
ANISOU 4989  CA  ASN A 606     6394   8255   5052    223   -400    226       C  
ATOM   4990  C   ASN A 606      15.302 -20.441  75.777  1.00 55.01           C  
ANISOU 4990  C   ASN A 606     6823   8720   5358    310   -382    276       C  
ATOM   4991  O   ASN A 606      16.088 -21.037  76.518  1.00 56.68           O  
ANISOU 4991  O   ASN A 606     7027   9009   5500    381   -407    288       O  
ATOM   4992  CB  ASN A 606      16.332 -18.484  74.519  1.00 50.71           C  
ANISOU 4992  CB  ASN A 606     6216   8142   4910    181   -447    112       C  
ATOM   4993  CG  ASN A 606      17.421 -18.193  73.477  1.00 52.00           C  
ANISOU 4993  CG  ASN A 606     6333   8286   5137    122   -478     65       C  
ATOM   4994  OD1 ASN A 606      18.562 -18.668  73.592  1.00 46.39           O  
ANISOU 4994  OD1 ASN A 606     5589   7636   4403    153   -512     56       O  
ATOM   4995  ND2 ASN A 606      17.070 -17.406  72.454  1.00 46.11           N  
ANISOU 4995  ND2 ASN A 606     5586   7462   4472     40   -465     38       N  
ATOM   4996  N   GLU A 607      14.019 -20.247  76.090  1.00 57.72           N  
ANISOU 4996  N   GLU A 607     7197   9035   5698    308   -336    311       N  
ATOM   4997  CA  GLU A 607      13.458 -20.650  77.391  1.00 61.68           C  
ANISOU 4997  CA  GLU A 607     7725   9602   6108    391   -309    364       C  
ATOM   4998  C   GLU A 607      13.409 -22.169  77.541  1.00 62.13           C  
ANISOU 4998  C   GLU A 607     7805   9650   6152    442   -275    479       C  
ATOM   4999  O   GLU A 607      14.078 -22.731  78.411  1.00 63.18           O  
ANISOU 4999  O   GLU A 607     7940   9861   6202    522   -293    500       O  
ATOM   5000  CB  GLU A 607      12.076 -20.028  77.620  1.00 63.12           C  
ANISOU 5000  CB  GLU A 607     7928   9758   6296    374   -264    372       C  
ATOM   5001  CG  GLU A 607      11.839 -19.590  79.062  1.00 71.06           C  
ANISOU 5001  CG  GLU A 607     8945  10865   7189    453   -265    353       C  
ATOM   5002  CD  GLU A 607      12.927 -18.647  79.579  1.00 78.29           C  
ANISOU 5002  CD  GLU A 607     9837  11860   8052    472   -341    234       C  
ATOM   5003  OE1 GLU A 607      13.242 -17.652  78.884  1.00 80.48           O  
ANISOU 5003  OE1 GLU A 607    10092  12097   8390    401   -378    145       O  
ATOM   5004  OE2 GLU A 607      13.469 -18.904  80.679  1.00 80.04           O  
ANISOU 5004  OE2 GLU A 607    10059  12180   8171    560   -365    230       O  
ATOM   5005  N   VAL A 608      12.607 -22.823  76.702  1.00 61.85           N  
ANISOU 5005  N   VAL A 608     7787   9516   6198    399   -230    552       N  
ATOM   5006  CA  VAL A 608      12.798 -24.243  76.408  1.00 62.08           C  
ANISOU 5006  CA  VAL A 608     7833   9505   6251    424   -213    643       C  
ATOM   5007  C   VAL A 608      14.155 -24.286  75.718  1.00 61.60           C  
ANISOU 5007  C   VAL A 608     7745   9452   6209    413   -270    586       C  
ATOM   5008  O   VAL A 608      14.568 -23.289  75.140  1.00 63.17           O  
ANISOU 5008  O   VAL A 608     7913   9648   6439    358   -302    496       O  
ATOM   5009  CB  VAL A 608      11.633 -24.853  75.539  1.00 62.83           C  
ANISOU 5009  CB  VAL A 608     7948   9482   6444    369   -162    718       C  
ATOM   5010  CG1 VAL A 608      10.821 -23.776  74.825  1.00 61.75           C  
ANISOU 5010  CG1 VAL A 608     7799   9292   6370    291   -152    662       C  
ATOM   5011  CG2 VAL A 608      12.138 -25.916  74.545  1.00 63.18           C  
ANISOU 5011  CG2 VAL A 608     7999   9454   6555    357   -174    756       C  
ATOM   5012  N   CYS A 609      14.870 -25.403  75.808  1.00 59.52           N  
ANISOU 5012  N   CYS A 609     7490   9202   5924    468   -281    637       N  
ATOM   5013  CA  CYS A 609      16.265 -25.454  75.349  1.00 57.34           C  
ANISOU 5013  CA  CYS A 609     7180   8960   5648    475   -337    581       C  
ATOM   5014  C   CYS A 609      17.219 -25.003  76.445  1.00 55.34           C  
ANISOU 5014  C   CYS A 609     6901   8832   5293    539   -383    522       C  
ATOM   5015  O   CYS A 609      18.354 -25.473  76.505  1.00 56.45           O  
ANISOU 5015  O   CYS A 609     7021   9024   5403    585   -423    509       O  
ATOM   5016  CB  CYS A 609      16.514 -24.609  74.087  1.00 57.04           C  
ANISOU 5016  CB  CYS A 609     7109   8871   5692    386   -356    504       C  
ATOM   5017  SG  CYS A 609      15.872 -25.275  72.530  1.00 59.15           S  
ANISOU 5017  SG  CYS A 609     7398   9001   6076    325   -325    553       S  
ATOM   5018  N   GLY A 610      16.766 -24.081  77.293  1.00 52.72           N  
ANISOU 5018  N   GLY A 610     6569   8552   4910    545   -382    481       N  
ATOM   5019  CA  GLY A 610      17.556 -23.625  78.438  1.00 52.14           C  
ANISOU 5019  CA  GLY A 610     6475   8602   4735    612   -430    420       C  
ATOM   5020  C   GLY A 610      18.835 -22.912  78.038  1.00 50.76           C  
ANISOU 5020  C   GLY A 610     6242   8469   4577    581   -499    312       C  
ATOM   5021  O   GLY A 610      19.862 -23.031  78.716  1.00 50.84           O  
ANISOU 5021  O   GLY A 610     6227   8575   4517    646   -549    276       O  
ATOM   5022  N   THR A 611      18.766 -22.181  76.929  1.00 48.00           N  
ANISOU 5022  N   THR A 611     5869   8048   4320    483   -500    263       N  
ATOM   5023  CA  THR A 611      19.908 -21.447  76.391  1.00 48.86           C  
ANISOU 5023  CA  THR A 611     5917   8183   4464    436   -554    168       C  
ATOM   5024  C   THR A 611      19.741 -19.942  76.632  1.00 50.31           C  
ANISOU 5024  C   THR A 611     6080   8377   4656    382   -580     69       C  
ATOM   5025  O   THR A 611      18.700 -19.492  77.111  1.00 49.88           O  
ANISOU 5025  O   THR A 611     6062   8306   4582    383   -553     74       O  
ATOM   5026  CB  THR A 611      20.113 -21.723  74.865  1.00 48.14           C  
ANISOU 5026  CB  THR A 611     5811   8005   4474    366   -538    186       C  
ATOM   5027  OG1 THR A 611      18.906 -21.444  74.145  1.00 44.71           O  
ANISOU 5027  OG1 THR A 611     5411   7467   4108    301   -488    215       O  
ATOM   5028  CG2 THR A 611      20.510 -23.163  74.617  1.00 46.77           C  
ANISOU 5028  CG2 THR A 611     5653   7826   4292    424   -528    265       C  
ATOM   5029  N   GLU A 612      20.771 -19.166  76.307  1.00 52.93           N  
ANISOU 5029  N   GLU A 612     6354   8737   5020    337   -632    -21       N  
ATOM   5030  CA  GLU A 612      20.694 -17.715  76.459  1.00 54.50           C  
ANISOU 5030  CA  GLU A 612     6534   8935   5240    279   -662   -120       C  
ATOM   5031  C   GLU A 612      21.132 -16.988  75.208  1.00 52.64           C  
ANISOU 5031  C   GLU A 612     6258   8635   5110    174   -668   -163       C  
ATOM   5032  O   GLU A 612      22.254 -17.166  74.737  1.00 52.04           O  
ANISOU 5032  O   GLU A 612     6127   8587   5060    159   -695   -183       O  
ATOM   5033  CB  GLU A 612      21.493 -17.227  77.675  1.00 56.85           C  
ANISOU 5033  CB  GLU A 612     6798   9345   5457    334   -733   -205       C  
ATOM   5034  CG  GLU A 612      20.755 -17.386  79.007  1.00 63.08           C  
ANISOU 5034  CG  GLU A 612     7637  10192   6140    427   -726   -187       C  
ATOM   5035  CD  GLU A 612      19.488 -16.536  79.114  1.00 66.04           C  
ANISOU 5035  CD  GLU A 612     8054  10510   6528    395   -693   -199       C  
ATOM   5036  OE1 GLU A 612      19.475 -15.406  78.569  1.00 65.25           O  
ANISOU 5036  OE1 GLU A 612     7935  10358   6498    310   -711   -274       O  
ATOM   5037  OE2 GLU A 612      18.516 -16.997  79.764  1.00 65.85           O  
ANISOU 5037  OE2 GLU A 612     8081  10497   6443    456   -648   -133       O  
ATOM   5038  N   GLY A 613      20.215 -16.185  74.673  1.00 53.60           N  
ANISOU 5038  N   GLY A 613     6406   8670   5289    106   -637   -173       N  
ATOM   5039  CA  GLY A 613      20.483 -15.289  73.547  1.00 54.22           C  
ANISOU 5039  CA  GLY A 613     6454   8681   5465      5   -639   -216       C  
ATOM   5040  C   GLY A 613      20.914 -15.907  72.228  1.00 53.41           C  
ANISOU 5040  C   GLY A 613     6332   8533   5428    -32   -611   -165       C  
ATOM   5041  O   GLY A 613      21.682 -15.295  71.473  1.00 53.45           O  
ANISOU 5041  O   GLY A 613     6289   8524   5495    -98   -626   -207       O  
ATOM   5042  N   GLU A 614      20.442 -17.111  71.930  1.00 51.52           N  
ANISOU 5042  N   GLU A 614     6129   8269   5177     11   -570    -76       N  
ATOM   5043  CA  GLU A 614      20.805 -17.698  70.652  1.00 51.60           C  
ANISOU 5043  CA  GLU A 614     6126   8233   5245    -15   -547    -33       C  
ATOM   5044  C   GLU A 614      19.783 -17.311  69.593  1.00 49.29           C  
ANISOU 5044  C   GLU A 614     5872   7832   5025    -79   -501     -9       C  
ATOM   5045  O   GLU A 614      18.588 -17.279  69.863  1.00 49.81           O  
ANISOU 5045  O   GLU A 614     5988   7855   5084    -72   -473     18       O  
ATOM   5046  CB  GLU A 614      21.012 -19.211  70.746  1.00 53.00           C  
ANISOU 5046  CB  GLU A 614     6319   8435   5383     63   -537     41       C  
ATOM   5047  CG  GLU A 614      21.949 -19.735  69.652  1.00 56.57           C  
ANISOU 5047  CG  GLU A 614     6734   8885   5877     53   -538     55       C  
ATOM   5048  CD  GLU A 614      23.115 -20.570  70.173  1.00 61.96           C  
ANISOU 5048  CD  GLU A 614     7378   9662   6504    127   -574     58       C  
ATOM   5049  OE1 GLU A 614      23.295 -20.707  71.409  1.00 57.77           O  
ANISOU 5049  OE1 GLU A 614     6847   9204   5898    187   -604     44       O  
ATOM   5050  OE2 GLU A 614      23.870 -21.091  69.320  1.00 68.44           O  
ANISOU 5050  OE2 GLU A 614     8169  10486   7350    131   -574     72       O  
ATOM   5051  N   ALA A 615      20.270 -16.984  68.400  1.00 48.29           N  
ANISOU 5051  N   ALA A 615     5716   7667   4964   -137   -493    -19       N  
ATOM   5052  CA  ALA A 615      19.399 -16.655  67.281  1.00 47.64           C  
ANISOU 5052  CA  ALA A 615     5668   7486   4947   -190   -452      5       C  
ATOM   5053  C   ALA A 615      18.964 -17.933  66.579  1.00 47.54           C  
ANISOU 5053  C   ALA A 615     5689   7430   4943   -153   -420     83       C  
ATOM   5054  O   ALA A 615      19.669 -18.457  65.713  1.00 49.64           O  
ANISOU 5054  O   ALA A 615     5933   7698   5232   -149   -418    101       O  
ATOM   5055  CB  ALA A 615      20.089 -15.702  66.315  1.00 45.24           C  
ANISOU 5055  CB  ALA A 615     5322   7160   4706   -264   -454    -36       C  
ATOM   5056  N   PHE A 616      17.802 -18.440  66.976  1.00 47.55           N  
ANISOU 5056  N   PHE A 616     5744   7396   4929   -123   -397    128       N  
ATOM   5057  CA  PHE A 616      17.214 -19.624  66.344  1.00 46.71           C  
ANISOU 5057  CA  PHE A 616     5673   7233   4841    -94   -369    200       C  
ATOM   5058  C   PHE A 616      16.673 -19.326  64.941  1.00 45.20           C  
ANISOU 5058  C   PHE A 616     5499   6954   4720   -145   -344    206       C  
ATOM   5059  O   PHE A 616      16.796 -20.156  64.038  1.00 45.20           O  
ANISOU 5059  O   PHE A 616     5508   6921   4746   -128   -336    241       O  
ATOM   5060  CB  PHE A 616      16.113 -20.217  67.228  1.00 45.62           C  
ANISOU 5060  CB  PHE A 616     5580   7083   4673    -54   -350    249       C  
ATOM   5061  CG  PHE A 616      16.625 -20.862  68.484  1.00 45.41           C  
ANISOU 5061  CG  PHE A 616     5546   7137   4570     15   -368    266       C  
ATOM   5062  CD1 PHE A 616      16.902 -22.227  68.518  1.00 44.48           C  
ANISOU 5062  CD1 PHE A 616     5441   7023   4435     74   -367    328       C  
ATOM   5063  CD2 PHE A 616      16.825 -20.110  69.638  1.00 46.91           C  
ANISOU 5063  CD2 PHE A 616     5721   7399   4704     27   -390    219       C  
ATOM   5064  CE1 PHE A 616      17.366 -22.837  69.684  1.00 45.60           C  
ANISOU 5064  CE1 PHE A 616     5581   7241   4502    145   -384    349       C  
ATOM   5065  CE2 PHE A 616      17.295 -20.713  70.817  1.00 46.27           C  
ANISOU 5065  CE2 PHE A 616     5636   7401   4544    101   -409    235       C  
ATOM   5066  CZ  PHE A 616      17.564 -22.075  70.834  1.00 45.20           C  
ANISOU 5066  CZ  PHE A 616     5515   7270   4390    160   -404    303       C  
ATOM   5067  N   VAL A 617      16.078 -18.146  64.761  1.00 43.48           N  
ANISOU 5067  N   VAL A 617     5289   6699   4531   -199   -334    169       N  
ATOM   5068  CA  VAL A 617      15.570 -17.743  63.445  1.00 40.48           C  
ANISOU 5068  CA  VAL A 617     4927   6241   4212   -243   -312    172       C  
ATOM   5069  C   VAL A 617      16.743 -17.374  62.541  1.00 42.11           C  
ANISOU 5069  C   VAL A 617     5093   6465   4443   -271   -319    148       C  
ATOM   5070  O   VAL A 617      17.419 -16.367  62.754  1.00 42.99           O  
ANISOU 5070  O   VAL A 617     5168   6608   4557   -311   -333     99       O  
ATOM   5071  CB  VAL A 617      14.561 -16.574  63.541  1.00 39.26           C  
ANISOU 5071  CB  VAL A 617     4798   6042   4079   -287   -299    142       C  
ATOM   5072  CG1 VAL A 617      14.107 -16.134  62.146  1.00 32.77           C  
ANISOU 5072  CG1 VAL A 617     3994   5141   3315   -326   -278    145       C  
ATOM   5073  CG2 VAL A 617      13.355 -16.965  64.434  1.00 32.37           C  
ANISOU 5073  CG2 VAL A 617     3958   5159   3180   -256   -285    172       C  
ATOM   5074  N   LEU A 618      16.992 -18.209  61.542  1.00 42.62           N  
ANISOU 5074  N   LEU A 618     5161   6508   4525   -249   -310    182       N  
ATOM   5075  CA  LEU A 618      18.149 -18.025  60.672  1.00 42.45           C  
ANISOU 5075  CA  LEU A 618     5097   6515   4519   -263   -311    169       C  
ATOM   5076  C   LEU A 618      17.830 -17.094  59.511  1.00 41.78           C  
ANISOU 5076  C   LEU A 618     5022   6369   4483   -316   -286    159       C  
ATOM   5077  O   LEU A 618      18.706 -16.384  59.007  1.00 44.50           O  
ANISOU 5077  O   LEU A 618     5326   6736   4845   -352   -282    138       O  
ATOM   5078  CB  LEU A 618      18.665 -19.382  60.174  1.00 43.13           C  
ANISOU 5078  CB  LEU A 618     5180   6616   4591   -201   -315    208       C  
ATOM   5079  CG  LEU A 618      17.801 -20.237  59.243  1.00 42.98           C  
ANISOU 5079  CG  LEU A 618     5213   6522   4597   -172   -301    248       C  
ATOM   5080  CD1 LEU A 618      18.346 -20.168  57.814  1.00 43.11           C  
ANISOU 5080  CD1 LEU A 618     5216   6526   4636   -174   -287    248       C  
ATOM   5081  CD2 LEU A 618      17.777 -21.666  59.723  1.00 39.84           C  
ANISOU 5081  CD2 LEU A 618     4834   6131   4173   -105   -316    287       C  
ATOM   5082  N   TYR A 619      16.566 -17.078  59.114  1.00 39.69           N  
ANISOU 5082  N   TYR A 619     4810   6030   4240   -319   -269    176       N  
ATOM   5083  CA  TYR A 619      16.146 -16.386  57.914  1.00 40.70           C  
ANISOU 5083  CA  TYR A 619     4959   6096   4409   -352   -246    175       C  
ATOM   5084  C   TYR A 619      14.663 -16.118  57.958  1.00 41.53           C  
ANISOU 5084  C   TYR A 619     5116   6132   4532   -361   -236    179       C  
ATOM   5085  O   TYR A 619      13.910 -16.829  58.633  1.00 44.02           O  
ANISOU 5085  O   TYR A 619     5452   6439   4833   -331   -242    197       O  
ATOM   5086  CB  TYR A 619      16.456 -17.259  56.695  1.00 42.13           C  
ANISOU 5086  CB  TYR A 619     5145   6266   4597   -314   -237    207       C  
ATOM   5087  CG  TYR A 619      16.122 -16.647  55.364  1.00 40.54           C  
ANISOU 5087  CG  TYR A 619     4965   6010   4427   -334   -212    210       C  
ATOM   5088  CD1 TYR A 619      15.053 -17.127  54.598  1.00 42.42           C  
ANISOU 5088  CD1 TYR A 619     5254   6182   4682   -307   -208    229       C  
ATOM   5089  CD2 TYR A 619      16.871 -15.588  54.862  1.00 39.64           C  
ANISOU 5089  CD2 TYR A 619     4821   5912   4329   -380   -194    196       C  
ATOM   5090  CE1 TYR A 619      14.745 -16.560  53.352  1.00 39.94           C  
ANISOU 5090  CE1 TYR A 619     4963   5823   4390   -316   -187    231       C  
ATOM   5091  CE2 TYR A 619      16.573 -15.020  53.628  1.00 39.96           C  
ANISOU 5091  CE2 TYR A 619     4885   5904   4394   -392   -168    206       C  
ATOM   5092  CZ  TYR A 619      15.521 -15.509  52.880  1.00 36.11           C  
ANISOU 5092  CZ  TYR A 619     4451   5356   3912   -356   -165    223       C  
ATOM   5093  OH  TYR A 619      15.251 -14.929  51.667  1.00 38.81           O  
ANISOU 5093  OH  TYR A 619     4819   5657   4271   -361   -141    232       O  
ATOM   5094  N   GLY A 620      14.252 -15.098  57.214  1.00 40.52           N  
ANISOU 5094  N   GLY A 620     5006   5955   4435   -400   -219    165       N  
ATOM   5095  CA  GLY A 620      12.848 -14.763  57.033  1.00 36.86           C  
ANISOU 5095  CA  GLY A 620     4589   5424   3992   -405   -209    166       C  
ATOM   5096  C   GLY A 620      12.672 -13.873  55.819  1.00 35.43           C  
ANISOU 5096  C   GLY A 620     4428   5192   3843   -432   -189    160       C  
ATOM   5097  O   GLY A 620      13.595 -13.164  55.413  1.00 36.79           O  
ANISOU 5097  O   GLY A 620     4575   5380   4024   -464   -180    150       O  
ATOM   5098  N   ASP A 621      11.483 -13.903  55.240  1.00 34.46           N  
ANISOU 5098  N   ASP A 621     4347   5008   3739   -419   -182    170       N  
ATOM   5099  CA  ASP A 621      11.207 -13.139  54.042  1.00 36.20           C  
ANISOU 5099  CA  ASP A 621     4593   5178   3982   -432   -164    169       C  
ATOM   5100  C   ASP A 621       9.734 -12.786  54.019  1.00 35.92           C  
ANISOU 5100  C   ASP A 621     4600   5085   3964   -429   -163    161       C  
ATOM   5101  O   ASP A 621       8.894 -13.645  53.752  1.00 36.14           O  
ANISOU 5101  O   ASP A 621     4646   5088   3999   -393   -171    177       O  
ATOM   5102  CB  ASP A 621      11.594 -13.944  52.787  1.00 36.24           C  
ANISOU 5102  CB  ASP A 621     4601   5180   3987   -393   -159    196       C  
ATOM   5103  CG  ASP A 621      11.481 -13.131  51.493  1.00 40.45           C  
ANISOU 5103  CG  ASP A 621     5161   5673   4535   -399   -137    201       C  
ATOM   5104  OD1 ASP A 621      10.679 -12.167  51.433  1.00 40.21           O  
ANISOU 5104  OD1 ASP A 621     5161   5596   4522   -422   -129    187       O  
ATOM   5105  OD2 ASP A 621      12.186 -13.471  50.519  1.00 40.30           O  
ANISOU 5105  OD2 ASP A 621     5134   5671   4508   -374   -126    220       O  
ATOM   5106  N   THR A 622       9.437 -11.522  54.320  1.00 34.39           N  
ANISOU 5106  N   THR A 622     4419   4869   3780   -465   -157    134       N  
ATOM   5107  CA  THR A 622       8.087 -10.962  54.224  1.00 33.06           C  
ANISOU 5107  CA  THR A 622     4289   4647   3625   -461   -154    122       C  
ATOM   5108  C   THR A 622       7.142 -11.434  55.326  1.00 34.24           C  
ANISOU 5108  C   THR A 622     4437   4808   3765   -444   -164    118       C  
ATOM   5109  O   THR A 622       6.648 -10.616  56.099  1.00 35.18           O  
ANISOU 5109  O   THR A 622     4565   4924   3879   -459   -165     91       O  
ATOM   5110  CB  THR A 622       7.449 -11.200  52.819  1.00 34.71           C  
ANISOU 5110  CB  THR A 622     4531   4807   3852   -430   -148    140       C  
ATOM   5111  OG1 THR A 622       8.321 -10.691  51.806  1.00 32.29           O  
ANISOU 5111  OG1 THR A 622     4227   4495   3547   -440   -131    150       O  
ATOM   5112  CG2 THR A 622       6.073 -10.533  52.698  1.00 30.66           C  
ANISOU 5112  CG2 THR A 622     4054   4242   3353   -423   -148    124       C  
ATOM   5113  N   ASP A 623       6.894 -12.744  55.383  1.00 35.39           N  
ANISOU 5113  N   ASP A 623     4573   4965   3908   -412   -172    146       N  
ATOM   5114  CA  ASP A 623       5.880 -13.320  56.267  1.00 34.76           C  
ANISOU 5114  CA  ASP A 623     4491   4890   3826   -395   -174    156       C  
ATOM   5115  C   ASP A 623       6.295 -14.673  56.842  1.00 35.54           C  
ANISOU 5115  C   ASP A 623     4566   5026   3911   -373   -182    188       C  
ATOM   5116  O   ASP A 623       5.515 -15.327  57.529  1.00 35.16           O  
ANISOU 5116  O   ASP A 623     4514   4981   3864   -357   -180    209       O  
ATOM   5117  CB  ASP A 623       4.546 -13.457  55.521  1.00 35.20           C  
ANISOU 5117  CB  ASP A 623     4570   4889   3913   -377   -174    161       C  
ATOM   5118  CG  ASP A 623       4.464 -14.712  54.678  1.00 38.14           C  
ANISOU 5118  CG  ASP A 623     4943   5240   4308   -349   -186    189       C  
ATOM   5119  OD1 ASP A 623       3.372 -15.306  54.635  1.00 42.55           O  
ANISOU 5119  OD1 ASP A 623     5503   5770   4893   -334   -192    200       O  
ATOM   5120  OD2 ASP A 623       5.469 -15.117  54.052  1.00 45.21           O  
ANISOU 5120  OD2 ASP A 623     5835   6147   5196   -340   -192    197       O  
ATOM   5121  N   SER A 624       7.528 -15.085  56.560  1.00 37.05           N  
ANISOU 5121  N   SER A 624     4741   5247   4090   -369   -189    196       N  
ATOM   5122  CA  SER A 624       8.001 -16.409  56.938  1.00 37.76           C  
ANISOU 5122  CA  SER A 624     4814   5367   4168   -340   -199    227       C  
ATOM   5123  C   SER A 624       9.203 -16.357  57.882  1.00 38.07           C  
ANISOU 5123  C   SER A 624     4823   5476   4167   -344   -205    220       C  
ATOM   5124  O   SER A 624       9.982 -15.407  57.866  1.00 39.44           O  
ANISOU 5124  O   SER A 624     4982   5673   4330   -372   -204    190       O  
ATOM   5125  CB  SER A 624       8.355 -17.210  55.681  1.00 37.57           C  
ANISOU 5125  CB  SER A 624     4797   5315   4161   -314   -208    243       C  
ATOM   5126  OG  SER A 624       9.504 -16.663  55.059  1.00 40.51           O  
ANISOU 5126  OG  SER A 624     5158   5714   4522   -324   -204    228       O  
ATOM   5127  N   ILE A 625       9.340 -17.373  58.723  1.00 38.26           N  
ANISOU 5127  N   ILE A 625     4835   5533   4169   -316   -211    248       N  
ATOM   5128  CA  ILE A 625      10.553 -17.521  59.530  1.00 37.88           C  
ANISOU 5128  CA  ILE A 625     4756   5556   4079   -307   -223    243       C  
ATOM   5129  C   ILE A 625      11.107 -18.925  59.350  1.00 36.99           C  
ANISOU 5129  C   ILE A 625     4639   5456   3961   -264   -234    281       C  
ATOM   5130  O   ILE A 625      10.353 -19.891  59.219  1.00 36.26           O  
ANISOU 5130  O   ILE A 625     4567   5322   3889   -240   -233    317       O  
ATOM   5131  CB  ILE A 625      10.340 -17.202  61.039  1.00 38.49           C  
ANISOU 5131  CB  ILE A 625     4826   5682   4117   -304   -223    235       C  
ATOM   5132  CG1 ILE A 625       9.254 -18.095  61.654  1.00 38.10           C  
ANISOU 5132  CG1 ILE A 625     4793   5616   4067   -276   -210    280       C  
ATOM   5133  CG2 ILE A 625      10.038 -15.714  61.243  1.00 39.04           C  
ANISOU 5133  CG2 ILE A 625     4899   5746   4188   -343   -219    186       C  
ATOM   5134  CD1 ILE A 625       9.128 -17.991  63.155  1.00 32.43           C  
ANISOU 5134  CD1 ILE A 625     4067   4957   3298   -258   -206    283       C  
ATOM   5135  N   TYR A 626      12.426 -19.019  59.292  1.00 36.55           N  
ANISOU 5135  N   TYR A 626     4554   5452   3881   -255   -246    271       N  
ATOM   5136  CA  TYR A 626      13.097 -20.306  59.228  1.00 37.09           C  
ANISOU 5136  CA  TYR A 626     4616   5541   3936   -206   -259    302       C  
ATOM   5137  C   TYR A 626      13.864 -20.498  60.521  1.00 37.54           C  
ANISOU 5137  C   TYR A 626     4647   5676   3943   -186   -272    302       C  
ATOM   5138  O   TYR A 626      14.696 -19.661  60.901  1.00 33.94           O  
ANISOU 5138  O   TYR A 626     4156   5276   3464   -208   -280    264       O  
ATOM   5139  CB  TYR A 626      13.988 -20.398  57.979  1.00 35.82           C  
ANISOU 5139  CB  TYR A 626     4443   5382   3786   -198   -263    293       C  
ATOM   5140  CG  TYR A 626      13.146 -20.456  56.730  1.00 40.51           C  
ANISOU 5140  CG  TYR A 626     5071   5900   4422   -200   -256    298       C  
ATOM   5141  CD1 TYR A 626      12.555 -19.297  56.211  1.00 38.21           C  
ANISOU 5141  CD1 TYR A 626     4791   5574   4154   -242   -240    274       C  
ATOM   5142  CD2 TYR A 626      12.894 -21.669  56.087  1.00 42.89           C  
ANISOU 5142  CD2 TYR A 626     5396   6160   4740   -154   -269    323       C  
ATOM   5143  CE1 TYR A 626      11.746 -19.343  55.086  1.00 40.98           C  
ANISOU 5143  CE1 TYR A 626     5175   5859   4538   -237   -236    276       C  
ATOM   5144  CE2 TYR A 626      12.083 -21.720  54.941  1.00 41.24           C  
ANISOU 5144  CE2 TYR A 626     5219   5883   4569   -151   -269    320       C  
ATOM   5145  CZ  TYR A 626      11.514 -20.550  54.454  1.00 39.57           C  
ANISOU 5145  CZ  TYR A 626     5015   5645   4373   -191   -252    297       C  
ATOM   5146  OH  TYR A 626      10.714 -20.569  53.333  1.00 40.56           O  
ANISOU 5146  OH  TYR A 626     5171   5709   4530   -181   -255    291       O  
ATOM   5147  N   VAL A 627      13.547 -21.591  61.206  1.00 38.52           N  
ANISOU 5147  N   VAL A 627     4786   5800   4051   -144   -275    344       N  
ATOM   5148  CA  VAL A 627      14.093 -21.860  62.536  1.00 40.52           C  
ANISOU 5148  CA  VAL A 627     5023   6126   4249   -113   -286    352       C  
ATOM   5149  C   VAL A 627      15.080 -23.027  62.510  1.00 40.92           C  
ANISOU 5149  C   VAL A 627     5063   6208   4276    -57   -305    378       C  
ATOM   5150  O   VAL A 627      14.728 -24.142  62.112  1.00 42.05           O  
ANISOU 5150  O   VAL A 627     5235   6301   4442    -25   -305    421       O  
ATOM   5151  CB  VAL A 627      12.954 -22.187  63.536  1.00 40.97           C  
ANISOU 5151  CB  VAL A 627     5106   6167   4295   -101   -269    391       C  
ATOM   5152  CG1 VAL A 627      13.518 -22.545  64.905  1.00 39.56           C  
ANISOU 5152  CG1 VAL A 627     4915   6067   4049    -56   -278    405       C  
ATOM   5153  CG2 VAL A 627      11.953 -21.026  63.625  1.00 41.01           C  
ANISOU 5153  CG2 VAL A 627     5119   6147   4317   -148   -250    363       C  
ATOM   5154  N   SER A 628      16.308 -22.767  62.946  1.00 41.23           N  
ANISOU 5154  N   SER A 628     5061   6330   4273    -44   -324    349       N  
ATOM   5155  CA  SER A 628      17.302 -23.820  63.149  1.00 42.78           C  
ANISOU 5155  CA  SER A 628     5245   6573   4435     19   -345    371       C  
ATOM   5156  C   SER A 628      16.864 -24.754  64.280  1.00 42.41           C  
ANISOU 5156  C   SER A 628     5228   6533   4354     70   -345    423       C  
ATOM   5157  O   SER A 628      16.706 -24.323  65.421  1.00 43.77           O  
ANISOU 5157  O   SER A 628     5395   6753   4485     71   -344    417       O  
ATOM   5158  CB  SER A 628      18.665 -23.209  63.468  1.00 43.90           C  
ANISOU 5158  CB  SER A 628     5328   6811   4541     18   -368    323       C  
ATOM   5159  OG  SER A 628      19.691 -24.169  63.317  1.00 51.61           O  
ANISOU 5159  OG  SER A 628     6287   7830   5493     78   -388    338       O  
ATOM   5160  N   ALA A 629      16.659 -26.028  63.953  1.00 41.50           N  
ANISOU 5160  N   ALA A 629     5144   6367   4256    113   -346    474       N  
ATOM   5161  CA  ALA A 629      16.087 -26.985  64.896  1.00 41.74           C  
ANISOU 5161  CA  ALA A 629     5209   6382   4267    155   -337    538       C  
ATOM   5162  C   ALA A 629      17.132 -27.898  65.516  1.00 42.66           C  
ANISOU 5162  C   ALA A 629     5320   6559   4328    231   -361    561       C  
ATOM   5163  O   ALA A 629      16.791 -28.782  66.295  1.00 41.05           O  
ANISOU 5163  O   ALA A 629     5148   6345   4105    275   -354    622       O  
ATOM   5164  CB  ALA A 629      15.003 -27.812  64.222  1.00 41.22           C  
ANISOU 5164  CB  ALA A 629     5188   6206   4267    148   -323    585       C  
ATOM   5165  N   ASP A 630      18.397 -27.674  65.168  1.00 45.09           N  
ANISOU 5165  N   ASP A 630     5586   6932   4612    247   -387    516       N  
ATOM   5166  CA  ASP A 630      19.510 -28.496  65.641  1.00 47.96           C  
ANISOU 5166  CA  ASP A 630     5938   7362   4923    325   -414    530       C  
ATOM   5167  C   ASP A 630      19.486 -28.680  67.159  1.00 50.44           C  
ANISOU 5167  C   ASP A 630     6260   7736   5170    368   -416    558       C  
ATOM   5168  O   ASP A 630      19.642 -29.799  67.653  1.00 52.74           O  
ANISOU 5168  O   ASP A 630     6580   8026   5432    438   -423    613       O  
ATOM   5169  CB  ASP A 630      20.860 -27.892  65.214  1.00 49.77           C  
ANISOU 5169  CB  ASP A 630     6102   7675   5133    323   -439    466       C  
ATOM   5170  CG  ASP A 630      21.087 -27.919  63.697  1.00 51.47           C  
ANISOU 5170  CG  ASP A 630     6310   7845   5401    303   -436    448       C  
ATOM   5171  OD1 ASP A 630      20.163 -28.255  62.920  1.00 53.50           O  
ANISOU 5171  OD1 ASP A 630     6611   8005   5710    285   -420    472       O  
ATOM   5172  OD2 ASP A 630      22.216 -27.593  63.277  1.00 54.90           O  
ANISOU 5172  OD2 ASP A 630     6690   8347   5822    308   -451    408       O  
ATOM   5173  N   LYS A 631      19.275 -27.594  67.897  1.00 50.01           N  
ANISOU 5173  N   LYS A 631     6184   7731   5088    332   -411    522       N  
ATOM   5174  CA  LYS A 631      19.295 -27.679  69.360  1.00 51.83           C  
ANISOU 5174  CA  LYS A 631     6420   8031   5242    382   -415    542       C  
ATOM   5175  C   LYS A 631      18.053 -28.322  69.952  1.00 52.62           C  
ANISOU 5175  C   LYS A 631     6576   8072   5345    396   -377    623       C  
ATOM   5176  O   LYS A 631      18.074 -28.772  71.099  1.00 55.57           O  
ANISOU 5176  O   LYS A 631     6967   8495   5654    457   -375    664       O  
ATOM   5177  CB  LYS A 631      19.561 -26.314  70.000  1.00 50.75           C  
ANISOU 5177  CB  LYS A 631     6240   7972   5069    348   -429    469       C  
ATOM   5178  CG  LYS A 631      21.005 -25.861  69.830  1.00 52.66           C  
ANISOU 5178  CG  LYS A 631     6417   8299   5290    353   -472    399       C  
ATOM   5179  CD  LYS A 631      21.195 -24.402  70.188  1.00 56.08           C  
ANISOU 5179  CD  LYS A 631     6807   8784   5715    298   -489    317       C  
ATOM   5180  CE  LYS A 631      22.677 -24.025  70.174  1.00 59.79           C  
ANISOU 5180  CE  LYS A 631     7205   9347   6167    305   -535    251       C  
ATOM   5181  NZ  LYS A 631      23.241 -23.851  68.797  1.00 62.59           N  
ANISOU 5181  NZ  LYS A 631     7524   9671   6587    257   -531    230       N  
ATOM   5182  N   ILE A 632      16.976 -28.382  69.175  1.00 52.35           N  
ANISOU 5182  N   ILE A 632     6569   7935   5386    343   -348    647       N  
ATOM   5183  CA  ILE A 632      15.764 -29.050  69.641  1.00 54.41           C  
ANISOU 5183  CA  ILE A 632     6876   8133   5664    349   -309    728       C  
ATOM   5184  C   ILE A 632      16.008 -30.548  69.621  1.00 54.85           C  
ANISOU 5184  C   ILE A 632     6967   8148   5725    412   -315    801       C  
ATOM   5185  O   ILE A 632      15.675 -31.250  70.574  1.00 56.63           O  
ANISOU 5185  O   ILE A 632     7222   8378   5917    459   -295    873       O  
ATOM   5186  CB  ILE A 632      14.520 -28.723  68.780  1.00 53.76           C  
ANISOU 5186  CB  ILE A 632     6807   7952   5668    274   -281    731       C  
ATOM   5187  CG1 ILE A 632      14.495 -27.243  68.355  1.00 56.45           C  
ANISOU 5187  CG1 ILE A 632     7113   8315   6019    210   -285    647       C  
ATOM   5188  CG2 ILE A 632      13.241 -29.141  69.505  1.00 51.22           C  
ANISOU 5188  CG2 ILE A 632     6516   7589   5356    273   -237    808       C  
ATOM   5189  CD1 ILE A 632      14.356 -26.230  69.485  1.00 59.22           C  
ANISOU 5189  CD1 ILE A 632     7448   8745   6307    207   -278    616       C  
ATOM   5190  N   ILE A 633      16.606 -31.008  68.524  1.00 54.59           N  
ANISOU 5190  N   ILE A 633     6931   8076   5733    416   -341    780       N  
ATOM   5191  CA  ILE A 633      17.008 -32.392  68.332  1.00 56.16           C  
ANISOU 5191  CA  ILE A 633     7164   8233   5940    480   -357    832       C  
ATOM   5192  C   ILE A 633      18.055 -32.777  69.370  1.00 59.82           C  
ANISOU 5192  C   ILE A 633     7621   8795   6312    566   -378    846       C  
ATOM   5193  O   ILE A 633      18.012 -33.876  69.929  1.00 62.46           O  
ANISOU 5193  O   ILE A 633     7996   9107   6628    628   -374    921       O  
ATOM   5194  CB  ILE A 633      17.572 -32.607  66.889  1.00 56.39           C  
ANISOU 5194  CB  ILE A 633     7185   8221   6021    474   -385    788       C  
ATOM   5195  CG1 ILE A 633      16.569 -32.135  65.820  1.00 50.71           C  
ANISOU 5195  CG1 ILE A 633     6471   7412   5385    394   -369    766       C  
ATOM   5196  CG2 ILE A 633      17.992 -34.061  66.657  1.00 54.34           C  
ANISOU 5196  CG2 ILE A 633     6964   7913   5770    547   -407    836       C  
ATOM   5197  CD1 ILE A 633      15.381 -33.040  65.617  1.00 49.69           C  
ANISOU 5197  CD1 ILE A 633     6391   7163   5327    382   -351    831       C  
ATOM   5198  N   ASP A 634      18.978 -31.855  69.642  1.00 63.74           N  
ANISOU 5198  N   ASP A 634     8065   9401   6752    569   -402    774       N  
ATOM   5199  CA  ASP A 634      20.054 -32.076  70.611  1.00 67.72           C  
ANISOU 5199  CA  ASP A 634     8551  10014   7164    650   -431    771       C  
ATOM   5200  C   ASP A 634      19.554 -32.431  72.010  1.00 69.64           C  
ANISOU 5200  C   ASP A 634     8830  10286   7344    700   -408    839       C  
ATOM   5201  O   ASP A 634      20.017 -33.413  72.585  1.00 72.13           O  
ANISOU 5201  O   ASP A 634     9172  10622   7612    786   -419    893       O  
ATOM   5202  CB  ASP A 634      20.999 -30.869  70.676  1.00 68.73           C  
ANISOU 5202  CB  ASP A 634     8610  10250   7255    628   -461    673       C  
ATOM   5203  CG  ASP A 634      22.006 -30.841  69.529  1.00 72.82           C  
ANISOU 5203  CG  ASP A 634     9086  10778   7804    621   -490    620       C  
ATOM   5204  OD1 ASP A 634      22.055 -31.812  68.733  1.00 71.85           O  
ANISOU 5204  OD1 ASP A 634     8992  10588   7720    649   -492    654       O  
ATOM   5205  OD2 ASP A 634      22.754 -29.839  69.426  1.00 75.19           O  
ANISOU 5205  OD2 ASP A 634     9323  11154   8091    590   -511    543       O  
ATOM   5206  N   LYS A 635      18.615 -31.646  72.543  1.00 69.96           N  
ANISOU 5206  N   LYS A 635     8871  10329   7381    653   -376    840       N  
ATOM   5207  CA  LYS A 635      18.099 -31.857  73.904  1.00 70.61           C  
ANISOU 5207  CA  LYS A 635     8982  10451   7394    703   -348    904       C  
ATOM   5208  C   LYS A 635      17.588 -33.273  74.141  1.00 71.08           C  
ANISOU 5208  C   LYS A 635     9103  10435   7470    751   -318   1020       C  
ATOM   5209  O   LYS A 635      17.962 -33.914  75.128  1.00 72.00           O  
ANISOU 5209  O   LYS A 635     9243  10605   7510    838   -319   1075       O  
ATOM   5210  CB  LYS A 635      17.004 -30.844  74.255  1.00 70.98           C  
ANISOU 5210  CB  LYS A 635     9024  10497   7449    640   -311    890       C  
ATOM   5211  CG  LYS A 635      17.512 -29.571  74.923  1.00 72.72           C  
ANISOU 5211  CG  LYS A 635     9200  10831   7599    640   -338    801       C  
ATOM   5212  CD  LYS A 635      16.420 -28.924  75.789  1.00 74.02           C  
ANISOU 5212  CD  LYS A 635     9378  11014   7732    627   -297    817       C  
ATOM   5213  CE  LYS A 635      16.447 -29.400  77.252  1.00 76.18           C  
ANISOU 5213  CE  LYS A 635     9677  11369   7898    725   -284    878       C  
ATOM   5214  NZ  LYS A 635      17.614 -28.879  78.036  1.00 73.79           N  
ANISOU 5214  NZ  LYS A 635     9343  11198   7497    787   -340    803       N  
ATOM   5215  N   VAL A 636      16.739 -33.760  73.239  1.00 69.96           N  
ANISOU 5215  N   VAL A 636     8986  10167   7428    696   -295   1058       N  
ATOM   5216  CA  VAL A 636      16.265 -35.141  73.322  1.00 70.93           C  
ANISOU 5216  CA  VAL A 636     9165  10198   7587    730   -272   1166       C  
ATOM   5217  C   VAL A 636      17.363 -36.132  72.934  1.00 71.68           C  
ANISOU 5217  C   VAL A 636     9277  10284   7674    802   -316   1170       C  
ATOM   5218  O   VAL A 636      17.393 -37.252  73.441  1.00 73.36           O  
ANISOU 5218  O   VAL A 636     9537  10465   7871    868   -308   1257       O  
ATOM   5219  CB  VAL A 636      14.980 -35.402  72.487  1.00 70.43           C  
ANISOU 5219  CB  VAL A 636     9122   9997   7642    649   -239   1202       C  
ATOM   5220  CG1 VAL A 636      13.821 -34.586  73.029  1.00 71.22           C  
ANISOU 5220  CG1 VAL A 636     9208  10108   7743    593   -189   1216       C  
ATOM   5221  CG2 VAL A 636      15.204 -35.116  71.008  1.00 69.53           C  
ANISOU 5221  CG2 VAL A 636     8986   9827   7603    594   -273   1122       C  
ATOM   5222  N   GLY A 637      18.259 -35.709  72.042  1.00 70.44           N  
ANISOU 5222  N   GLY A 637     9082  10156   7527    790   -360   1080       N  
ATOM   5223  CA  GLY A 637      19.390 -36.534  71.627  1.00 69.26           C  
ANISOU 5223  CA  GLY A 637     8938  10014   7363    862   -404   1071       C  
ATOM   5224  C   GLY A 637      19.100 -37.288  70.351  1.00 67.68           C  
ANISOU 5224  C   GLY A 637     8768   9687   7262    838   -412   1080       C  
ATOM   5225  O   GLY A 637      18.108 -38.010  70.260  1.00 68.11           O  
ANISOU 5225  O   GLY A 637     8870   9628   7382    818   -386   1151       O  
ATOM   5226  N   GLU A 638      19.985 -37.129  69.371  1.00 66.60           N  
ANISOU 5226  N   GLU A 638     8599   9571   7136    844   -451   1006       N  
ATOM   5227  CA  GLU A 638      19.789 -37.689  68.037  1.00 66.06           C  
ANISOU 5227  CA  GLU A 638     8552   9395   7154    824   -465    994       C  
ATOM   5228  C   GLU A 638      19.716 -39.217  68.024  1.00 66.87           C  
ANISOU 5228  C   GLU A 638     8723   9402   7285    892   -477   1070       C  
ATOM   5229  O   GLU A 638      19.030 -39.804  67.188  1.00 65.61           O  
ANISOU 5229  O   GLU A 638     8599   9118   7213    864   -478   1086       O  
ATOM   5230  CB  GLU A 638      20.897 -37.208  67.105  1.00 64.66           C  
ANISOU 5230  CB  GLU A 638     8323   9282   6963    833   -500    905       C  
ATOM   5231  CG  GLU A 638      20.418 -36.899  65.701  1.00 63.47           C  
ANISOU 5231  CG  GLU A 638     8168   9054   6894    767   -500    860       C  
ATOM   5232  CD  GLU A 638      21.545 -36.464  64.785  1.00 65.41           C  
ANISOU 5232  CD  GLU A 638     8362   9369   7122    782   -528    782       C  
ATOM   5233  OE1 GLU A 638      22.420 -37.306  64.487  1.00 66.58           O  
ANISOU 5233  OE1 GLU A 638     8519   9529   7250    864   -559    781       O  
ATOM   5234  OE2 GLU A 638      21.556 -35.286  64.362  1.00 62.58           O  
ANISOU 5234  OE2 GLU A 638     7955   9052   6771    714   -516    724       O  
ATOM   5235  N   SER A 639      20.423 -39.849  68.959  1.00 68.78           N  
ANISOU 5235  N   SER A 639     8982   9699   7451    984   -488   1113       N  
ATOM   5236  CA  SER A 639      20.491 -41.307  69.046  1.00 70.62           C  
ANISOU 5236  CA  SER A 639     9283   9847   7703   1060   -502   1188       C  
ATOM   5237  C   SER A 639      19.175 -41.916  69.510  1.00 70.54           C  
ANISOU 5237  C   SER A 639     9329   9719   7754   1024   -460   1288       C  
ATOM   5238  O   SER A 639      18.943 -43.117  69.338  1.00 69.74           O  
ANISOU 5238  O   SER A 639     9288   9504   7704   1059   -469   1350       O  
ATOM   5239  CB  SER A 639      21.620 -41.730  69.989  1.00 72.17           C  
ANISOU 5239  CB  SER A 639     9481  10146   7793   1174   -525   1208       C  
ATOM   5240  OG  SER A 639      22.883 -41.486  69.397  1.00 73.59           O  
ANISOU 5240  OG  SER A 639     9612  10414   7934   1218   -570   1123       O  
ATOM   5241  N   LYS A 640      18.319 -41.077  70.089  1.00 70.04           N  
ANISOU 5241  N   LYS A 640     9243   9681   7687    954   -415   1302       N  
ATOM   5242  CA  LYS A 640      17.026 -41.513  70.609  1.00 71.10           C  
ANISOU 5242  CA  LYS A 640     9417   9721   7876    913   -365   1400       C  
ATOM   5243  C   LYS A 640      15.983 -41.803  69.522  1.00 69.89           C  
ANISOU 5243  C   LYS A 640     9280   9419   7855    831   -362   1399       C  
ATOM   5244  O   LYS A 640      14.889 -42.283  69.833  1.00 71.08           O  
ANISOU 5244  O   LYS A 640     9460   9478   8070    792   -324   1482       O  
ATOM   5245  CB  LYS A 640      16.478 -40.490  71.615  1.00 71.89           C  
ANISOU 5245  CB  LYS A 640     9484   9911   7921    875   -317   1411       C  
ATOM   5246  CG  LYS A 640      16.887 -40.721  73.079  1.00 75.68           C  
ANISOU 5246  CG  LYS A 640     9980  10484   8290    961   -299   1478       C  
ATOM   5247  CD  LYS A 640      18.353 -40.378  73.341  1.00 79.94           C  
ANISOU 5247  CD  LYS A 640    10489  11161   8725   1040   -347   1407       C  
ATOM   5248  CE  LYS A 640      18.617 -40.102  74.817  1.00 83.08           C  
ANISOU 5248  CE  LYS A 640    10884  11682   9002   1107   -329   1443       C  
ATOM   5249  NZ  LYS A 640      20.013 -39.632  75.057  1.00 83.38           N  
ANISOU 5249  NZ  LYS A 640    10878  11861   8942   1174   -381   1360       N  
ATOM   5250  N   PHE A 641      16.320 -41.532  68.259  1.00 66.64           N  
ANISOU 5250  N   PHE A 641     8847   8988   7484    808   -401   1309       N  
ATOM   5251  CA  PHE A 641      15.360 -41.678  67.161  1.00 65.41           C  
ANISOU 5251  CA  PHE A 641     8703   8705   7446    734   -406   1292       C  
ATOM   5252  C   PHE A 641      15.501 -42.984  66.385  1.00 65.84           C  
ANISOU 5252  C   PHE A 641     8811   8634   7570    777   -449   1307       C  
ATOM   5253  O   PHE A 641      16.606 -43.377  66.005  1.00 66.80           O  
ANISOU 5253  O   PHE A 641     8942   8788   7652    855   -493   1269       O  
ATOM   5254  CB  PHE A 641      15.430 -40.479  66.205  1.00 63.55           C  
ANISOU 5254  CB  PHE A 641     8413   8516   7216    675   -417   1185       C  
ATOM   5255  CG  PHE A 641      15.030 -39.174  66.836  1.00 59.80           C  
ANISOU 5255  CG  PHE A 641     7890   8132   6698    617   -377   1168       C  
ATOM   5256  CD1 PHE A 641      15.974 -38.172  67.044  1.00 56.72           C  
ANISOU 5256  CD1 PHE A 641     7453   7878   6222    632   -386   1101       C  
ATOM   5257  CD2 PHE A 641      13.711 -38.948  67.225  1.00 58.63           C  
ANISOU 5257  CD2 PHE A 641     7743   7934   6599    548   -331   1216       C  
ATOM   5258  CE1 PHE A 641      15.611 -36.963  67.630  1.00 54.57           C  
ANISOU 5258  CE1 PHE A 641     7140   7682   5913    582   -354   1078       C  
ATOM   5259  CE2 PHE A 641      13.337 -37.737  67.818  1.00 55.21           C  
ANISOU 5259  CE2 PHE A 641     7269   7586   6122    503   -296   1195       C  
ATOM   5260  CZ  PHE A 641      14.289 -36.746  68.016  1.00 55.02           C  
ANISOU 5260  CZ  PHE A 641     7204   7689   6012    520   -309   1124       C  
ATOM   5261  N   ARG A 642      14.366 -43.636  66.143  1.00 66.36           N  
ANISOU 5261  N   ARG A 642     8911   8559   7744    726   -438   1359       N  
ATOM   5262  CA  ARG A 642      14.320 -44.926  65.452  1.00 67.76           C  
ANISOU 5262  CA  ARG A 642     9145   8596   8003    759   -482   1376       C  
ATOM   5263  C   ARG A 642      14.623 -44.793  63.965  1.00 65.85           C  
ANISOU 5263  C   ARG A 642     8896   8325   7799    758   -536   1270       C  
ATOM   5264  O   ARG A 642      15.289 -45.644  63.381  1.00 66.79           O  
ANISOU 5264  O   ARG A 642     9052   8397   7927    830   -587   1249       O  
ATOM   5265  CB  ARG A 642      12.950 -45.591  65.632  1.00 70.55           C  
ANISOU 5265  CB  ARG A 642     9528   8805   8473    693   -455   1459       C  
ATOM   5266  CG  ARG A 642      12.611 -45.977  67.072  1.00 77.39           C  
ANISOU 5266  CG  ARG A 642    10414   9680   9312    704   -397   1584       C  
ATOM   5267  CD  ARG A 642      11.287 -46.749  67.171  1.00 83.80           C  
ANISOU 5267  CD  ARG A 642    11251  10337  10251    636   -371   1673       C  
ATOM   5268  NE  ARG A 642      10.107 -45.900  66.969  1.00 86.26           N  
ANISOU 5268  NE  ARG A 642    11511  10643  10622    529   -335   1656       N  
ATOM   5269  CZ  ARG A 642       9.397 -45.839  65.843  1.00 86.83           C  
ANISOU 5269  CZ  ARG A 642    11569  10623  10798    462   -366   1595       C  
ATOM   5270  NH1 ARG A 642       9.737 -46.577  64.788  1.00 86.64           N  
ANISOU 5270  NH1 ARG A 642    11581  10503  10834    491   -435   1542       N  
ATOM   5271  NH2 ARG A 642       8.341 -45.034  65.772  1.00 84.72           N  
ANISOU 5271  NH2 ARG A 642    11253  10363  10573    372   -330   1583       N  
ATOM   5272  N   ASP A 643      14.113 -43.728  63.358  1.00 63.28           N  
ANISOU 5272  N   ASP A 643     8522   8028   7492    682   -525   1206       N  
ATOM   5273  CA  ASP A 643      14.309 -43.464  61.940  1.00 60.83           C  
ANISOU 5273  CA  ASP A 643     8202   7700   7212    678   -569   1108       C  
ATOM   5274  C   ASP A 643      13.943 -42.018  61.643  1.00 58.31           C  
ANISOU 5274  C   ASP A 643     7823   7457   6875    602   -541   1049       C  
ATOM   5275  O   ASP A 643      13.633 -41.258  62.563  1.00 58.13           O  
ANISOU 5275  O   ASP A 643     7768   7504   6814    561   -493   1079       O  
ATOM   5276  CB  ASP A 643      13.485 -44.431  61.075  1.00 62.11           C  
ANISOU 5276  CB  ASP A 643     8409   7694   7496    660   -607   1109       C  
ATOM   5277  CG  ASP A 643      12.025 -44.504  61.491  1.00 62.68           C  
ANISOU 5277  CG  ASP A 643     8481   7674   7661    569   -571   1172       C  
ATOM   5278  OD1 ASP A 643      11.509 -43.527  62.072  1.00 64.08           O  
ANISOU 5278  OD1 ASP A 643     8613   7920   7812    507   -519   1186       O  
ATOM   5279  OD2 ASP A 643      11.388 -45.544  61.225  1.00 63.32           O  
ANISOU 5279  OD2 ASP A 643     8604   7611   7844    559   -596   1206       O  
ATOM   5280  N   THR A 644      13.981 -41.646  60.364  1.00 55.01           N  
ANISOU 5280  N   THR A 644     7393   7026   6483    591   -572    966       N  
ATOM   5281  CA  THR A 644      13.691 -40.282  59.943  1.00 51.83           C  
ANISOU 5281  CA  THR A 644     6939   6689   6065    526   -549    907       C  
ATOM   5282  C   THR A 644      12.307 -39.816  60.419  1.00 51.92           C  
ANISOU 5282  C   THR A 644     6936   6658   6133    434   -507    945       C  
ATOM   5283  O   THR A 644      12.176 -38.758  61.047  1.00 48.33           O  
ANISOU 5283  O   THR A 644     6442   6290   5631    393   -466    945       O  
ATOM   5284  CB  THR A 644      13.790 -40.147  58.409  1.00 51.00           C  
ANISOU 5284  CB  THR A 644     6835   6552   5990    533   -590    823       C  
ATOM   5285  OG1 THR A 644      15.094 -40.550  57.972  1.00 51.53           O  
ANISOU 5285  OG1 THR A 644     6910   6670   6000    623   -624    789       O  
ATOM   5286  CG2 THR A 644      13.545 -38.712  57.982  1.00 49.07           C  
ANISOU 5286  CG2 THR A 644     6542   6376   5727    471   -564    768       C  
ATOM   5287  N   ASN A 645      11.290 -40.627  60.129  1.00 52.95           N  
ANISOU 5287  N   ASN A 645     7098   6656   6366    405   -521    976       N  
ATOM   5288  CA  ASN A 645       9.904 -40.276  60.402  1.00 54.04           C  
ANISOU 5288  CA  ASN A 645     7217   6745   6571    318   -486   1007       C  
ATOM   5289  C   ASN A 645       9.625 -40.063  61.890  1.00 54.93           C  
ANISOU 5289  C   ASN A 645     7315   6912   6644    299   -425   1091       C  
ATOM   5290  O   ASN A 645       8.628 -39.440  62.259  1.00 56.63           O  
ANISOU 5290  O   ASN A 645     7501   7131   6885    232   -384   1110       O  
ATOM   5291  CB  ASN A 645       8.962 -41.339  59.814  1.00 55.94           C  
ANISOU 5291  CB  ASN A 645     7490   6826   6937    296   -519   1025       C  
ATOM   5292  CG  ASN A 645       7.588 -40.778  59.455  1.00 56.01           C  
ANISOU 5292  CG  ASN A 645     7468   6787   7025    207   -504   1011       C  
ATOM   5293  OD1 ASN A 645       7.470 -39.847  58.649  1.00 58.07           O  
ANISOU 5293  OD1 ASN A 645     7703   7086   7274    184   -513    935       O  
ATOM   5294  ND2 ASN A 645       6.544 -41.348  60.046  1.00 52.72           N  
ANISOU 5294  ND2 ASN A 645     7053   6289   6691    157   -479   1086       N  
ATOM   5295  N   HIS A 646      10.518 -40.573  62.733  1.00 53.46           N  
ANISOU 5295  N   HIS A 646     7149   6773   6389    365   -420   1138       N  
ATOM   5296  CA  HIS A 646      10.433 -40.381  64.169  1.00 53.78           C  
ANISOU 5296  CA  HIS A 646     7179   6882   6371    367   -366   1214       C  
ATOM   5297  C   HIS A 646      10.812 -38.953  64.578  1.00 51.78           C  
ANISOU 5297  C   HIS A 646     6878   6772   6024    353   -339   1165       C  
ATOM   5298  O   HIS A 646      10.088 -38.328  65.345  1.00 52.47           O  
ANISOU 5298  O   HIS A 646     6942   6897   6099    310   -292   1197       O  
ATOM   5299  CB  HIS A 646      11.293 -41.428  64.897  1.00 57.14           C  
ANISOU 5299  CB  HIS A 646     7647   7312   6751    453   -375   1278       C  
ATOM   5300  CG  HIS A 646      11.013 -41.548  66.366  1.00 59.64           C  
ANISOU 5300  CG  HIS A 646     7968   7670   7024    462   -319   1377       C  
ATOM   5301  ND1 HIS A 646      11.917 -42.100  67.250  1.00 63.90           N  
ANISOU 5301  ND1 HIS A 646     8534   8263   7482    547   -318   1428       N  
ATOM   5302  CD2 HIS A 646       9.934 -41.195  67.107  1.00 61.80           C  
ANISOU 5302  CD2 HIS A 646     8222   7943   7316    404   -261   1436       C  
ATOM   5303  CE1 HIS A 646      11.408 -42.082  68.470  1.00 63.84           C  
ANISOU 5303  CE1 HIS A 646     8527   8286   7443    542   -262   1515       C  
ATOM   5304  NE2 HIS A 646      10.205 -41.539  68.410  1.00 63.74           N  
ANISOU 5304  NE2 HIS A 646     8484   8243   7490    456   -224   1523       N  
ATOM   5305  N   TRP A 647      11.927 -38.422  64.078  1.00 49.67           N  
ANISOU 5305  N   TRP A 647     6594   6585   5694    389   -370   1089       N  
ATOM   5306  CA  TRP A 647      12.262 -37.028  64.406  1.00 49.23           C  
ANISOU 5306  CA  TRP A 647     6489   6653   5562    366   -349   1037       C  
ATOM   5307  C   TRP A 647      11.373 -36.021  63.651  1.00 48.04           C  
ANISOU 5307  C   TRP A 647     6311   6481   5461    286   -338    983       C  
ATOM   5308  O   TRP A 647      11.167 -34.897  64.111  1.00 48.22           O  
ANISOU 5308  O   TRP A 647     6300   6576   5444    250   -309    962       O  
ATOM   5309  CB  TRP A 647      13.772 -36.718  64.289  1.00 47.89           C  
ANISOU 5309  CB  TRP A 647     6301   6587   5308    426   -378    981       C  
ATOM   5310  CG  TRP A 647      14.353 -36.742  62.888  1.00 51.14           C  
ANISOU 5310  CG  TRP A 647     6709   6977   5743    439   -420    909       C  
ATOM   5311  CD1 TRP A 647      15.096 -37.749  62.323  1.00 52.20           C  
ANISOU 5311  CD1 TRP A 647     6873   7078   5884    508   -461    905       C  
ATOM   5312  CD2 TRP A 647      14.259 -35.710  61.892  1.00 46.58           C  
ANISOU 5312  CD2 TRP A 647     6102   6416   5182    390   -423    833       C  
ATOM   5313  NE1 TRP A 647      15.455 -37.410  61.038  1.00 50.24           N  
ANISOU 5313  NE1 TRP A 647     6611   6829   5650    506   -487    831       N  
ATOM   5314  CE2 TRP A 647      14.954 -36.166  60.749  1.00 49.66           C  
ANISOU 5314  CE2 TRP A 647     6502   6785   5584    434   -463    790       C  
ATOM   5315  CE3 TRP A 647      13.653 -34.449  61.853  1.00 44.19           C  
ANISOU 5315  CE3 TRP A 647     5765   6142   4882    318   -396    800       C  
ATOM   5316  CZ2 TRP A 647      15.055 -35.403  59.578  1.00 48.86           C  
ANISOU 5316  CZ2 TRP A 647     6378   6693   5494    408   -472    720       C  
ATOM   5317  CZ3 TRP A 647      13.755 -33.692  60.692  1.00 43.57           C  
ANISOU 5317  CZ3 TRP A 647     5668   6067   4820    290   -407    731       C  
ATOM   5318  CH2 TRP A 647      14.447 -34.174  59.569  1.00 46.81           C  
ANISOU 5318  CH2 TRP A 647     6088   6458   5239    335   -443    694       C  
ATOM   5319  N   VAL A 648      10.832 -36.440  62.508  1.00 47.74           N  
ANISOU 5319  N   VAL A 648     6290   6340   5509    264   -365    960       N  
ATOM   5320  CA  VAL A 648       9.889 -35.618  61.751  1.00 46.91           C  
ANISOU 5320  CA  VAL A 648     6164   6204   5458    194   -358    914       C  
ATOM   5321  C   VAL A 648       8.583 -35.495  62.544  1.00 48.66           C  
ANISOU 5321  C   VAL A 648     6375   6395   5718    139   -312    973       C  
ATOM   5322  O   VAL A 648       8.067 -34.391  62.724  1.00 48.56           O  
ANISOU 5322  O   VAL A 648     6332   6430   5690     93   -284    949       O  
ATOM   5323  CB  VAL A 648       9.659 -36.170  60.310  1.00 46.71           C  
ANISOU 5323  CB  VAL A 648     6160   6078   5510    196   -405    871       C  
ATOM   5324  CG1 VAL A 648       8.527 -35.422  59.600  1.00 47.04           C  
ANISOU 5324  CG1 VAL A 648     6182   6079   5611    127   -399    832       C  
ATOM   5325  CG2 VAL A 648      10.934 -36.074  59.490  1.00 40.21           C  
ANISOU 5325  CG2 VAL A 648     5338   5304   4635    251   -441    807       C  
ATOM   5326  N   ASP A 649       8.078 -36.626  63.040  1.00 51.69           N  
ANISOU 5326  N   ASP A 649     6785   6703   6153    146   -304   1054       N  
ATOM   5327  CA  ASP A 649       6.946 -36.647  63.985  1.00 52.86           C  
ANISOU 5327  CA  ASP A 649     6921   6835   6330    103   -251   1129       C  
ATOM   5328  C   ASP A 649       7.198 -35.761  65.202  1.00 50.85           C  
ANISOU 5328  C   ASP A 649     6642   6705   5973    113   -205   1146       C  
ATOM   5329  O   ASP A 649       6.321 -35.008  65.616  1.00 49.62           O  
ANISOU 5329  O   ASP A 649     6458   6576   5819     68   -165   1154       O  
ATOM   5330  CB  ASP A 649       6.641 -38.077  64.463  1.00 54.02           C  
ANISOU 5330  CB  ASP A 649     7102   6890   6534    120   -245   1226       C  
ATOM   5331  CG  ASP A 649       5.617 -38.798  63.586  1.00 58.45           C  
ANISOU 5331  CG  ASP A 649     7670   7309   7229     71   -269   1230       C  
ATOM   5332  OD1 ASP A 649       4.900 -38.137  62.796  1.00 59.65           O  
ANISOU 5332  OD1 ASP A 649     7795   7441   7429     19   -279   1171       O  
ATOM   5333  OD2 ASP A 649       5.520 -40.042  63.701  1.00 62.35           O  
ANISOU 5333  OD2 ASP A 649     8199   7708   7784     87   -281   1293       O  
ATOM   5334  N   PHE A 650       8.401 -35.860  65.764  1.00 51.22           N  
ANISOU 5334  N   PHE A 650     6700   6830   5930    178   -215   1148       N  
ATOM   5335  CA  PHE A 650       8.770 -35.102  66.957  1.00 51.94           C  
ANISOU 5335  CA  PHE A 650     6772   7045   5918    201   -182   1158       C  
ATOM   5336  C   PHE A 650       8.650 -33.591  66.741  1.00 50.16           C  
ANISOU 5336  C   PHE A 650     6507   6889   5661    158   -176   1077       C  
ATOM   5337  O   PHE A 650       7.992 -32.896  67.517  1.00 50.42           O  
ANISOU 5337  O   PHE A 650     6521   6969   5667    136   -135   1092       O  
ATOM   5338  CB  PHE A 650      10.185 -35.471  67.425  1.00 51.92           C  
ANISOU 5338  CB  PHE A 650     6784   7114   5828    281   -207   1158       C  
ATOM   5339  CG  PHE A 650      10.694 -34.615  68.560  1.00 55.08           C  
ANISOU 5339  CG  PHE A 650     7162   7649   6119    310   -187   1148       C  
ATOM   5340  CD1 PHE A 650      10.079 -34.649  69.813  1.00 58.58           C  
ANISOU 5340  CD1 PHE A 650     7609   8127   6524    320   -137   1222       C  
ATOM   5341  CD2 PHE A 650      11.788 -33.780  68.379  1.00 55.84           C  
ANISOU 5341  CD2 PHE A 650     7232   7837   6149    328   -218   1064       C  
ATOM   5342  CE1 PHE A 650      10.544 -33.854  70.863  1.00 59.82           C  
ANISOU 5342  CE1 PHE A 650     7747   8410   6574    355   -125   1205       C  
ATOM   5343  CE2 PHE A 650      12.263 -32.986  69.423  1.00 57.60           C  
ANISOU 5343  CE2 PHE A 650     7432   8180   6275    353   -209   1045       C  
ATOM   5344  CZ  PHE A 650      11.638 -33.020  70.666  1.00 58.26           C  
ANISOU 5344  CZ  PHE A 650     7523   8297   6315    370   -165   1112       C  
ATOM   5345  N   LEU A 651       9.285 -33.097  65.684  1.00 48.16           N  
ANISOU 5345  N   LEU A 651     6245   6641   5412    151   -215    993       N  
ATOM   5346  CA  LEU A 651       9.279 -31.671  65.374  1.00 47.26           C  
ANISOU 5346  CA  LEU A 651     6099   6584   5274    112   -213    915       C  
ATOM   5347  C   LEU A 651       7.863 -31.172  65.046  1.00 47.70           C  
ANISOU 5347  C   LEU A 651     6143   6584   5396     46   -188    913       C  
ATOM   5348  O   LEU A 651       7.443 -30.107  65.513  1.00 47.30           O  
ANISOU 5348  O   LEU A 651     6071   6588   5315     19   -162    890       O  
ATOM   5349  CB  LEU A 651      10.266 -31.369  64.240  1.00 44.86           C  
ANISOU 5349  CB  LEU A 651     5788   6290   4967    120   -256    838       C  
ATOM   5350  CG  LEU A 651      11.747 -31.656  64.505  1.00 44.59           C  
ANISOU 5350  CG  LEU A 651     5751   6329   4862    183   -282    826       C  
ATOM   5351  CD1 LEU A 651      12.556 -31.418  63.248  1.00 40.77           C  
ANISOU 5351  CD1 LEU A 651     5257   5846   4389    187   -316    758       C  
ATOM   5352  CD2 LEU A 651      12.310 -30.810  65.668  1.00 43.85           C  
ANISOU 5352  CD2 LEU A 651     5630   6353   4677    197   -268    812       C  
ATOM   5353  N   ASP A 652       7.134 -31.969  64.267  1.00 49.16           N  
ANISOU 5353  N   ASP A 652     6343   6661   5673     25   -199    934       N  
ATOM   5354  CA  ASP A 652       5.731 -31.717  63.945  1.00 49.83           C  
ANISOU 5354  CA  ASP A 652     6414   6685   5833    -34   -179    939       C  
ATOM   5355  C   ASP A 652       4.894 -31.505  65.205  1.00 50.56           C  
ANISOU 5355  C   ASP A 652     6490   6815   5905    -47   -123   1002       C  
ATOM   5356  O   ASP A 652       4.143 -30.529  65.299  1.00 50.62           O  
ANISOU 5356  O   ASP A 652     6473   6849   5912    -83    -99    977       O  
ATOM   5357  CB  ASP A 652       5.176 -32.882  63.122  1.00 51.09           C  
ANISOU 5357  CB  ASP A 652     6594   6722   6096    -45   -205    964       C  
ATOM   5358  CG  ASP A 652       3.771 -32.631  62.602  1.00 54.25           C  
ANISOU 5358  CG  ASP A 652     6973   7056   6582   -105   -196    956       C  
ATOM   5359  OD1 ASP A 652       3.326 -31.464  62.519  1.00 56.37           O  
ANISOU 5359  OD1 ASP A 652     7217   7368   6832   -135   -179    912       O  
ATOM   5360  OD2 ASP A 652       3.106 -33.623  62.256  1.00 59.50           O  
ANISOU 5360  OD2 ASP A 652     7647   7622   7337   -122   -209    992       O  
ATOM   5361  N   LYS A 653       5.036 -32.409  66.172  1.00 50.74           N  
ANISOU 5361  N   LYS A 653     6528   6843   5907    -12   -101   1086       N  
ATOM   5362  CA  LYS A 653       4.318 -32.286  67.436  1.00 52.17           C  
ANISOU 5362  CA  LYS A 653     6696   7070   6058    -13    -42   1156       C  
ATOM   5363  C   LYS A 653       4.782 -31.055  68.209  1.00 50.02           C  
ANISOU 5363  C   LYS A 653     6407   6922   5677      8    -27   1111       C  
ATOM   5364  O   LYS A 653       3.965 -30.344  68.791  1.00 49.65           O  
ANISOU 5364  O   LYS A 653     6337   6915   5612    -11     12   1119       O  
ATOM   5365  CB  LYS A 653       4.463 -33.556  68.286  1.00 53.87           C  
ANISOU 5365  CB  LYS A 653     6936   7264   6268     28    -20   1261       C  
ATOM   5366  CG  LYS A 653       3.560 -33.590  69.520  1.00 57.86           C  
ANISOU 5366  CG  LYS A 653     7427   7804   6753     26     49   1351       C  
ATOM   5367  CD  LYS A 653       3.366 -35.013  70.038  1.00 62.78           C  
ANISOU 5367  CD  LYS A 653     8075   8361   7417     45     73   1468       C  
ATOM   5368  CE  LYS A 653       2.249 -35.092  71.079  1.00 62.51           C  
ANISOU 5368  CE  LYS A 653     8019   8345   7386     30    150   1567       C  
ATOM   5369  NZ  LYS A 653       1.967 -36.499  71.490  1.00 63.46           N  
ANISOU 5369  NZ  LYS A 653     8163   8384   7565     38    178   1689       N  
ATOM   5370  N   PHE A 654       6.085 -30.799  68.195  1.00 48.16           N  
ANISOU 5370  N   PHE A 654     6180   6747   5372     48    -62   1061       N  
ATOM   5371  CA  PHE A 654       6.648 -29.659  68.918  1.00 48.51           C  
ANISOU 5371  CA  PHE A 654     6207   6905   5317     68    -60   1011       C  
ATOM   5372  C   PHE A 654       6.144 -28.330  68.349  1.00 48.21           C  
ANISOU 5372  C   PHE A 654     6147   6875   5297     16    -61    931       C  
ATOM   5373  O   PHE A 654       5.848 -27.396  69.091  1.00 47.86           O  
ANISOU 5373  O   PHE A 654     6087   6898   5198     17    -39    912       O  
ATOM   5374  CB  PHE A 654       8.178 -29.726  68.918  1.00 48.04           C  
ANISOU 5374  CB  PHE A 654     6155   6903   5194    117   -102    971       C  
ATOM   5375  CG  PHE A 654       8.843 -28.557  69.596  1.00 50.57           C  
ANISOU 5375  CG  PHE A 654     6455   7336   5423    134   -110    908       C  
ATOM   5376  CD1 PHE A 654       9.624 -27.662  68.866  1.00 50.25           C  
ANISOU 5376  CD1 PHE A 654     6395   7320   5376    112   -147    816       C  
ATOM   5377  CD2 PHE A 654       8.697 -28.349  70.965  1.00 51.47           C  
ANISOU 5377  CD2 PHE A 654     6568   7532   5458    173    -81    941       C  
ATOM   5378  CE1 PHE A 654      10.245 -26.572  69.495  1.00 51.36           C  
ANISOU 5378  CE1 PHE A 654     6514   7557   5443    122   -159    754       C  
ATOM   5379  CE2 PHE A 654       9.309 -27.258  71.599  1.00 50.10           C  
ANISOU 5379  CE2 PHE A 654     6375   7459   5202    190    -97    874       C  
ATOM   5380  CZ  PHE A 654      10.081 -26.374  70.868  1.00 46.31           C  
ANISOU 5380  CZ  PHE A 654     5875   6995   4726    162   -138    779       C  
ATOM   5381  N   ALA A 655       6.028 -28.257  67.030  1.00 47.62           N  
ANISOU 5381  N   ALA A 655     6072   6728   5293    -22    -89    886       N  
ATOM   5382  CA  ALA A 655       5.523 -27.055  66.390  1.00 48.25           C  
ANISOU 5382  CA  ALA A 655     6136   6804   5394    -68    -92    816       C  
ATOM   5383  C   ALA A 655       4.041 -26.837  66.700  1.00 49.39           C  
ANISOU 5383  C   ALA A 655     6266   6924   5577   -100    -50    849       C  
ATOM   5384  O   ALA A 655       3.631 -25.744  67.102  1.00 49.28           O  
ANISOU 5384  O   ALA A 655     6237   6958   5527   -111    -32    815       O  
ATOM   5385  CB  ALA A 655       5.761 -27.117  64.891  1.00 46.69           C  
ANISOU 5385  CB  ALA A 655     5945   6538   5258    -92   -130    767       C  
ATOM   5386  N   ARG A 656       3.250 -27.889  66.520  1.00 51.72           N  
ANISOU 5386  N   ARG A 656     6564   7143   5946   -113    -36    915       N  
ATOM   5387  CA  ARG A 656       1.803 -27.820  66.701  1.00 54.74           C  
ANISOU 5387  CA  ARG A 656     6923   7494   6380   -148      3    951       C  
ATOM   5388  C   ARG A 656       1.404 -27.504  68.146  1.00 55.54           C  
ANISOU 5388  C   ARG A 656     7012   7679   6412   -123     57   1000       C  
ATOM   5389  O   ARG A 656       0.550 -26.648  68.381  1.00 57.41           O  
ANISOU 5389  O   ARG A 656     7226   7945   6643   -141     84    982       O  
ATOM   5390  CB  ARG A 656       1.159 -29.127  66.221  1.00 56.01           C  
ANISOU 5390  CB  ARG A 656     7088   7552   6643   -169      1   1013       C  
ATOM   5391  CG  ARG A 656      -0.368 -29.174  66.293  1.00 64.32           C  
ANISOU 5391  CG  ARG A 656     8107   8564   7768   -212     39   1053       C  
ATOM   5392  CD  ARG A 656      -0.967 -30.299  65.435  1.00 68.56           C  
ANISOU 5392  CD  ARG A 656     8643   8981   8427   -246     16   1082       C  
ATOM   5393  NE  ARG A 656      -0.211 -31.545  65.546  1.00 74.10           N  
ANISOU 5393  NE  ARG A 656     9377   9639   9139   -218     -1   1134       N  
ATOM   5394  CZ  ARG A 656       0.641 -31.995  64.629  1.00 75.63           C  
ANISOU 5394  CZ  ARG A 656     9601   9786   9350   -201    -58   1091       C  
ATOM   5395  NH1 ARG A 656       0.848 -31.311  63.507  1.00 75.17           N  
ANISOU 5395  NH1 ARG A 656     9545   9719   9299   -211   -100    998       N  
ATOM   5396  NH2 ARG A 656       1.288 -33.135  64.834  1.00 77.20           N  
ANISOU 5396  NH2 ARG A 656     9831   9948   9554   -169    -71   1142       N  
ATOM   5397  N   GLU A 657       2.041 -28.173  69.104  1.00 55.15           N  
ANISOU 5397  N   GLU A 657     6978   7673   6304    -76     71   1059       N  
ATOM   5398  CA  GLU A 657       1.639 -28.092  70.507  1.00 55.48           C  
ANISOU 5398  CA  GLU A 657     7010   7792   6277    -42    126   1122       C  
ATOM   5399  C   GLU A 657       2.366 -27.039  71.325  1.00 52.84           C  
ANISOU 5399  C   GLU A 657     6678   7573   5825      2    120   1066       C  
ATOM   5400  O   GLU A 657       1.839 -26.572  72.335  1.00 51.18           O  
ANISOU 5400  O   GLU A 657     6456   7433   5555     27    162   1088       O  
ATOM   5401  CB  GLU A 657       1.782 -29.455  71.188  1.00 57.19           C  
ANISOU 5401  CB  GLU A 657     7244   7991   6495     -8    151   1231       C  
ATOM   5402  CG  GLU A 657       0.789 -30.489  70.685  1.00 65.90           C  
ANISOU 5402  CG  GLU A 657     8338   8982   7718    -55    170   1303       C  
ATOM   5403  CD  GLU A 657       0.669 -31.681  71.610  1.00 72.75           C  
ANISOU 5403  CD  GLU A 657     9219   9839   8583    -24    214   1428       C  
ATOM   5404  OE1 GLU A 657       1.641 -31.963  72.341  1.00 77.20           O  
ANISOU 5404  OE1 GLU A 657     9811  10461   9059     39    210   1452       O  
ATOM   5405  OE2 GLU A 657      -0.398 -32.337  71.607  1.00 77.43           O  
ANISOU 5405  OE2 GLU A 657     9792  10365   9263    -63    252   1505       O  
ATOM   5406  N   ARG A 658       3.564 -26.660  70.895  1.00 50.33           N  
ANISOU 5406  N   ARG A 658     6373   7275   5475     13     68    992       N  
ATOM   5407  CA  ARG A 658       4.383 -25.755  71.687  1.00 49.40           C  
ANISOU 5407  CA  ARG A 658     6255   7263   5251     54     53    936       C  
ATOM   5408  C   ARG A 658       4.625 -24.426  70.988  1.00 48.32           C  
ANISOU 5408  C   ARG A 658     6108   7132   5118     18     18    826       C  
ATOM   5409  O   ARG A 658       4.392 -23.365  71.564  1.00 48.67           O  
ANISOU 5409  O   ARG A 658     6145   7237   5111     25     26    781       O  
ATOM   5410  CB  ARG A 658       5.711 -26.416  72.064  1.00 49.30           C  
ANISOU 5410  CB  ARG A 658     6259   7290   5182    106     24    948       C  
ATOM   5411  CG  ARG A 658       5.575 -27.806  72.705  1.00 56.27           C  
ANISOU 5411  CG  ARG A 658     7161   8157   6063    147     55   1062       C  
ATOM   5412  CD  ARG A 658       5.042 -27.764  74.142  1.00 59.64           C  
ANISOU 5412  CD  ARG A 658     7587   8663   6410    195    108   1126       C  
ATOM   5413  NE  ARG A 658       5.168 -29.077  74.765  1.00 65.94           N  
ANISOU 5413  NE  ARG A 658     8407   9451   7195    242    134   1236       N  
ATOM   5414  CZ  ARG A 658       5.443 -29.284  76.050  1.00 69.29           C  
ANISOU 5414  CZ  ARG A 658     8844   9965   7518    317    160   1288       C  
ATOM   5415  NH1 ARG A 658       5.619 -28.260  76.876  1.00 71.68           N  
ANISOU 5415  NH1 ARG A 658     9137  10377   7721    355    158   1234       N  
ATOM   5416  NH2 ARG A 658       5.545 -30.524  76.510  1.00 70.82           N  
ANISOU 5416  NH2 ARG A 658     9063  10136   7709    357    184   1394       N  
ATOM   5417  N   MET A 659       5.081 -24.484  69.744  1.00 47.43           N  
ANISOU 5417  N   MET A 659     5999   6956   5066    -18    -19    784       N  
ATOM   5418  CA  MET A 659       5.494 -23.278  69.036  1.00 47.20           C  
ANISOU 5418  CA  MET A 659     5963   6931   5039    -49    -52    687       C  
ATOM   5419  C   MET A 659       4.326 -22.408  68.574  1.00 46.18           C  
ANISOU 5419  C   MET A 659     5826   6765   4955    -92    -34    657       C  
ATOM   5420  O   MET A 659       4.308 -21.203  68.842  1.00 45.25           O  
ANISOU 5420  O   MET A 659     5704   6688   4800    -97    -39    595       O  
ATOM   5421  CB  MET A 659       6.420 -23.625  67.873  1.00 46.95           C  
ANISOU 5421  CB  MET A 659     5936   6854   5048    -65    -93    658       C  
ATOM   5422  CG  MET A 659       7.769 -24.129  68.341  1.00 50.51           C  
ANISOU 5422  CG  MET A 659     6389   7363   5442    -19   -118    662       C  
ATOM   5423  SD  MET A 659       9.013 -24.093  67.047  1.00 49.48           S  
ANISOU 5423  SD  MET A 659     6252   7209   5338    -34   -166    604       S  
ATOM   5424  CE  MET A 659       9.287 -22.334  66.892  1.00 57.09           C  
ANISOU 5424  CE  MET A 659     7197   8213   6283    -74   -179    508       C  
ATOM   5425  N   GLU A 660       3.356 -23.013  67.890  1.00 45.87           N  
ANISOU 5425  N   GLU A 660     5785   6647   4996   -120    -18    697       N  
ATOM   5426  CA  GLU A 660       2.194 -22.259  67.400  1.00 45.66           C  
ANISOU 5426  CA  GLU A 660     5748   6585   5015   -157     -4    670       C  
ATOM   5427  C   GLU A 660       1.436 -21.540  68.524  1.00 43.47           C  
ANISOU 5427  C   GLU A 660     5459   6373   4684   -137     34    674       C  
ATOM   5428  O   GLU A 660       1.105 -20.367  68.377  1.00 43.04           O  
ANISOU 5428  O   GLU A 660     5403   6330   4620   -150     30    612       O  
ATOM   5429  CB  GLU A 660       1.273 -23.134  66.545  1.00 45.49           C  
ANISOU 5429  CB  GLU A 660     5721   6472   5091   -187      2    713       C  
ATOM   5430  CG  GLU A 660       1.778 -23.334  65.111  1.00 48.30           C  
ANISOU 5430  CG  GLU A 660     6090   6758   5503   -209    -42    672       C  
ATOM   5431  CD  GLU A 660       1.047 -24.445  64.360  1.00 52.56           C  
ANISOU 5431  CD  GLU A 660     6628   7207   6136   -229    -47    715       C  
ATOM   5432  OE1 GLU A 660      -0.101 -24.796  64.732  1.00 50.65           O  
ANISOU 5432  OE1 GLU A 660     6366   6945   5934   -242    -14    765       O  
ATOM   5433  OE2 GLU A 660       1.627 -24.966  63.382  1.00 53.34           O  
ANISOU 5433  OE2 GLU A 660     6742   7256   6269   -229    -84    698       O  
ATOM   5434  N   PRO A 661       1.184 -22.223  69.660  1.00 44.90           N  
ANISOU 5434  N   PRO A 661     5635   6600   4826   -101     72    749       N  
ATOM   5435  CA  PRO A 661       0.522 -21.513  70.769  1.00 45.16           C  
ANISOU 5435  CA  PRO A 661     5656   6708   4794    -71    109    751       C  
ATOM   5436  C   PRO A 661       1.317 -20.332  71.303  1.00 44.34           C  
ANISOU 5436  C   PRO A 661     5564   6679   4605    -44     81    668       C  
ATOM   5437  O   PRO A 661       0.725 -19.318  71.673  1.00 46.99           O  
ANISOU 5437  O   PRO A 661     5895   7049   4910    -36     93    626       O  
ATOM   5438  CB  PRO A 661       0.376 -22.594  71.843  1.00 44.78           C  
ANISOU 5438  CB  PRO A 661     5605   6698   4712    -30    153    854       C  
ATOM   5439  CG  PRO A 661       0.254 -23.855  71.060  1.00 47.76           C  
ANISOU 5439  CG  PRO A 661     5982   6983   5181    -62    151    915       C  
ATOM   5440  CD  PRO A 661       1.230 -23.680  69.912  1.00 46.03           C  
ANISOU 5440  CD  PRO A 661     5780   6717   4992    -87     90    842       C  
ATOM   5441  N   ALA A 662       2.641 -20.463  71.331  1.00 43.76           N  
ANISOU 5441  N   ALA A 662     5502   6628   4495    -30     42    641       N  
ATOM   5442  CA  ALA A 662       3.526 -19.376  71.741  1.00 44.35           C  
ANISOU 5442  CA  ALA A 662     5583   6766   4503    -12      5    555       C  
ATOM   5443  C   ALA A 662       3.538 -18.245  70.710  1.00 43.62           C  
ANISOU 5443  C   ALA A 662     5494   6624   4458    -64    -25    469       C  
ATOM   5444  O   ALA A 662       3.606 -17.065  71.065  1.00 46.80           O  
ANISOU 5444  O   ALA A 662     5899   7060   4821    -59    -40    398       O  
ATOM   5445  CB  ALA A 662       4.932 -19.899  71.985  1.00 44.11           C  
ANISOU 5445  CB  ALA A 662     5557   6773   4431     14    -29    553       C  
ATOM   5446  N   ILE A 663       3.462 -18.614  69.439  1.00 41.96           N  
ANISOU 5446  N   ILE A 663     5284   6330   4329   -108    -34    476       N  
ATOM   5447  CA  ILE A 663       3.369 -17.649  68.345  1.00 41.10           C  
ANISOU 5447  CA  ILE A 663     5181   6167   4270   -154    -56    409       C  
ATOM   5448  C   ILE A 663       2.036 -16.881  68.389  1.00 41.50           C  
ANISOU 5448  C   ILE A 663     5231   6203   4335   -161    -30    395       C  
ATOM   5449  O   ILE A 663       2.021 -15.642  68.313  1.00 39.19           O  
ANISOU 5449  O   ILE A 663     4947   5913   4029   -170    -45    325       O  
ATOM   5450  CB  ILE A 663       3.591 -18.354  66.982  1.00 39.41           C  
ANISOU 5450  CB  ILE A 663     4969   5873   4131   -187    -71    426       C  
ATOM   5451  CG1 ILE A 663       5.083 -18.660  66.800  1.00 39.51           C  
ANISOU 5451  CG1 ILE A 663     4982   5907   4123   -182   -104    410       C  
ATOM   5452  CG2 ILE A 663       3.061 -17.507  65.829  1.00 35.63           C  
ANISOU 5452  CG2 ILE A 663     4498   5331   3708   -227    -79    379       C  
ATOM   5453  CD1 ILE A 663       5.388 -19.885  65.940  1.00 39.99           C  
ANISOU 5453  CD1 ILE A 663     5046   5916   4233   -185   -113    455       C  
ATOM   5454  N   ASP A 664       0.932 -17.619  68.529  1.00 43.02           N  
ANISOU 5454  N   ASP A 664     5411   6379   4557   -155      9    462       N  
ATOM   5455  CA  ASP A 664      -0.404 -17.024  68.683  1.00 45.34           C  
ANISOU 5455  CA  ASP A 664     5695   6672   4862   -154     39    458       C  
ATOM   5456  C   ASP A 664      -0.438 -15.997  69.818  1.00 44.86           C  
ANISOU 5456  C   ASP A 664     5639   6690   4716   -113     45    414       C  
ATOM   5457  O   ASP A 664      -0.876 -14.870  69.606  1.00 45.54           O  
ANISOU 5457  O   ASP A 664     5734   6767   4803   -119     37    353       O  
ATOM   5458  CB  ASP A 664      -1.477 -18.102  68.922  1.00 47.38           C  
ANISOU 5458  CB  ASP A 664     5927   6917   5157   -150     85    548       C  
ATOM   5459  CG  ASP A 664      -1.689 -19.019  67.714  1.00 54.03           C  
ANISOU 5459  CG  ASP A 664     6765   7669   6096   -191     73    579       C  
ATOM   5460  OD1 ASP A 664      -2.270 -20.119  67.895  1.00 54.67           O  
ANISOU 5460  OD1 ASP A 664     6827   7730   6216   -194    102    658       O  
ATOM   5461  OD2 ASP A 664      -1.280 -18.653  66.585  1.00 56.82           O  
ANISOU 5461  OD2 ASP A 664     7134   7969   6487   -219     35    527       O  
ATOM   5462  N   ARG A 665       0.025 -16.386  71.009  1.00 44.99           N  
ANISOU 5462  N   ARG A 665     5654   6784   4658    -67     57    444       N  
ATOM   5463  CA  ARG A 665       0.110 -15.471  72.155  1.00 47.63           C  
ANISOU 5463  CA  ARG A 665     5996   7201   4901    -18     55    397       C  
ATOM   5464  C   ARG A 665       0.919 -14.225  71.814  1.00 46.00           C  
ANISOU 5464  C   ARG A 665     5808   6984   4684    -37      1    291       C  
ATOM   5465  O   ARG A 665       0.545 -13.109  72.196  1.00 44.92           O  
ANISOU 5465  O   ARG A 665     5683   6870   4515    -18     -6    229       O  
ATOM   5466  CB  ARG A 665       0.741 -16.155  73.369  1.00 51.27           C  
ANISOU 5466  CB  ARG A 665     6455   7746   5279     38     65    440       C  
ATOM   5467  CG  ARG A 665      -0.251 -16.829  74.300  1.00 58.52           C  
ANISOU 5467  CG  ARG A 665     7357   8714   6163     83    128    529       C  
ATOM   5468  CD  ARG A 665       0.361 -17.122  75.677  1.00 62.49           C  
ANISOU 5468  CD  ARG A 665     7867   9319   6556    157    135    553       C  
ATOM   5469  NE  ARG A 665       1.606 -17.887  75.589  1.00 65.60           N  
ANISOU 5469  NE  ARG A 665     8270   9711   6944    156    102    568       N  
ATOM   5470  CZ  ARG A 665       1.684 -19.205  75.397  1.00 67.27           C  
ANISOU 5470  CZ  ARG A 665     8477   9890   7193    149    125    660       C  
ATOM   5471  NH1 ARG A 665       0.587 -19.944  75.263  1.00 64.55           N  
ANISOU 5471  NH1 ARG A 665     8117   9507   6901    133    180    748       N  
ATOM   5472  NH2 ARG A 665       2.876 -19.787  75.328  1.00 68.26           N  
ANISOU 5472  NH2 ARG A 665     8612  10018   7304    156     89    662       N  
ATOM   5473  N   GLY A 666       2.026 -14.439  71.097  1.00 42.45           N  
ANISOU 5473  N   GLY A 666     5363   6500   4266    -72    -36    273       N  
ATOM   5474  CA  GLY A 666       2.888 -13.367  70.619  1.00 39.91           C  
ANISOU 5474  CA  GLY A 666     5054   6157   3953   -103    -84    184       C  
ATOM   5475  C   GLY A 666       2.161 -12.376  69.735  1.00 40.06           C  
ANISOU 5475  C   GLY A 666     5088   6109   4026   -138    -87    139       C  
ATOM   5476  O   GLY A 666       2.296 -11.168  69.923  1.00 40.05           O  
ANISOU 5476  O   GLY A 666     5101   6110   4005   -139   -111     64       O  
ATOM   5477  N   PHE A 667       1.391 -12.873  68.768  1.00 40.13           N  
ANISOU 5477  N   PHE A 667     5092   6053   4102   -165    -64    183       N  
ATOM   5478  CA  PHE A 667       0.659 -11.983  67.850  1.00 39.23           C  
ANISOU 5478  CA  PHE A 667     4992   5873   4039   -192    -67    144       C  
ATOM   5479  C   PHE A 667      -0.574 -11.323  68.482  1.00 41.80           C  
ANISOU 5479  C   PHE A 667     5320   6224   4339   -158    -42    130       C  
ATOM   5480  O   PHE A 667      -0.950 -10.217  68.096  1.00 41.48           O  
ANISOU 5480  O   PHE A 667     5299   6149   4312   -165    -55     73       O  
ATOM   5481  CB  PHE A 667       0.275 -12.704  66.566  1.00 36.76           C  
ANISOU 5481  CB  PHE A 667     4676   5488   3805   -226    -59    185       C  
ATOM   5482  CG  PHE A 667       1.377 -12.753  65.538  1.00 37.92           C  
ANISOU 5482  CG  PHE A 667     4831   5590   3985   -263    -90    168       C  
ATOM   5483  CD1 PHE A 667       1.992 -11.580  65.094  1.00 36.71           C  
ANISOU 5483  CD1 PHE A 667     4698   5414   3836   -288   -117    102       C  
ATOM   5484  CD2 PHE A 667       1.770 -13.966  64.984  1.00 36.73           C  
ANISOU 5484  CD2 PHE A 667     4670   5419   3867   -272    -91    219       C  
ATOM   5485  CE1 PHE A 667       2.997 -11.616  64.138  1.00 34.33           C  
ANISOU 5485  CE1 PHE A 667     4401   5079   3566   -321   -139     92       C  
ATOM   5486  CE2 PHE A 667       2.770 -14.018  64.016  1.00 38.66           C  
ANISOU 5486  CE2 PHE A 667     4921   5631   4138   -299   -116    204       C  
ATOM   5487  CZ  PHE A 667       3.387 -12.838  63.591  1.00 38.01           C  
ANISOU 5487  CZ  PHE A 667     4852   5533   4055   -324   -137    143       C  
ATOM   5488  N   ARG A 668      -1.190 -11.995  69.454  1.00 44.89           N  
ANISOU 5488  N   ARG A 668     5690   6675   4690   -117     -5    184       N  
ATOM   5489  CA  ARG A 668      -2.304 -11.403  70.212  1.00 49.85           C  
ANISOU 5489  CA  ARG A 668     6315   7346   5281    -73     24    174       C  
ATOM   5490  C   ARG A 668      -1.837 -10.185  70.992  1.00 50.32           C  
ANISOU 5490  C   ARG A 668     6399   7449   5270    -41     -6     89       C  
ATOM   5491  O   ARG A 668      -2.572  -9.204  71.104  1.00 52.73           O  
ANISOU 5491  O   ARG A 668     6718   7753   5566    -20     -5     42       O  
ATOM   5492  CB  ARG A 668      -2.979 -12.417  71.151  1.00 50.68           C  
ANISOU 5492  CB  ARG A 668     6389   7515   5354    -34     77    260       C  
ATOM   5493  CG  ARG A 668      -3.824 -13.462  70.418  1.00 56.44           C  
ANISOU 5493  CG  ARG A 668     7088   8193   6163    -65    109    338       C  
ATOM   5494  CD  ARG A 668      -4.865 -14.118  71.323  1.00 64.30           C  
ANISOU 5494  CD  ARG A 668     8049   9246   7137    -29    171    416       C  
ATOM   5495  NE  ARG A 668      -4.278 -15.060  72.279  1.00 71.42           N  
ANISOU 5495  NE  ARG A 668     8945  10206   7986      0    191    482       N  
ATOM   5496  CZ  ARG A 668      -3.952 -16.326  72.005  1.00 74.19           C  
ANISOU 5496  CZ  ARG A 668     9285  10523   8380    -26    199    555       C  
ATOM   5497  NH1 ARG A 668      -4.137 -16.827  70.785  1.00 74.19           N  
ANISOU 5497  NH1 ARG A 668     9278  10433   8477    -81    185    567       N  
ATOM   5498  NH2 ARG A 668      -3.427 -17.094  72.954  1.00 74.00           N  
ANISOU 5498  NH2 ARG A 668     9262  10556   8299     10    218    613       N  
ATOM   5499  N   GLU A 669      -0.610 -10.253  71.509  1.00 50.56           N  
ANISOU 5499  N   GLU A 669     6437   7517   5259    -36    -37     67       N  
ATOM   5500  CA  GLU A 669       0.024  -9.125  72.191  1.00 50.78           C  
ANISOU 5500  CA  GLU A 669     6487   7578   5230    -13    -79    -23       C  
ATOM   5501  C   GLU A 669       0.209  -7.969  71.222  1.00 49.60           C  
ANISOU 5501  C   GLU A 669     6363   7345   5136    -60   -116    -97       C  
ATOM   5502  O   GLU A 669      -0.164  -6.836  71.530  1.00 50.27           O  
ANISOU 5502  O   GLU A 669     6471   7428   5200    -38   -132   -165       O  
ATOM   5503  CB  GLU A 669       1.370  -9.531  72.807  1.00 51.33           C  
ANISOU 5503  CB  GLU A 669     6550   7700   5254     -4   -111    -31       C  
ATOM   5504  CG  GLU A 669       2.014  -8.444  73.676  1.00 53.35           C  
ANISOU 5504  CG  GLU A 669     6824   8001   5447     27   -159   -128       C  
ATOM   5505  CD  GLU A 669       3.416  -8.799  74.169  1.00 54.39           C  
ANISOU 5505  CD  GLU A 669     6943   8182   5541     30   -199   -145       C  
ATOM   5506  OE1 GLU A 669       3.698  -9.988  74.430  1.00 55.78           O  
ANISOU 5506  OE1 GLU A 669     7100   8398   5696     48   -178    -71       O  
ATOM   5507  OE2 GLU A 669       4.239  -7.875  74.312  1.00 55.45           O  
ANISOU 5507  OE2 GLU A 669     7085   8313   5669     16   -255   -234       O  
ATOM   5508  N   MET A 670       0.757  -8.271  70.044  1.00 48.91           N  
ANISOU 5508  N   MET A 670     6274   7189   5119   -121   -127    -81       N  
ATOM   5509  CA  MET A 670       0.985  -7.266  68.998  1.00 47.59           C  
ANISOU 5509  CA  MET A 670     6132   6939   5010   -170   -155   -135       C  
ATOM   5510  C   MET A 670      -0.299  -6.563  68.563  1.00 48.19           C  
ANISOU 5510  C   MET A 670     6227   6971   5112   -159   -138   -150       C  
ATOM   5511  O   MET A 670      -0.314  -5.343  68.390  1.00 48.18           O  
ANISOU 5511  O   MET A 670     6258   6930   5120   -165   -163   -218       O  
ATOM   5512  CB  MET A 670       1.653  -7.896  67.779  1.00 46.63           C  
ANISOU 5512  CB  MET A 670     6002   6762   4954   -225   -159    -99       C  
ATOM   5513  CG  MET A 670       2.360  -6.891  66.877  1.00 45.43           C  
ANISOU 5513  CG  MET A 670     5872   6542   4848   -276   -191   -153       C  
ATOM   5514  SD  MET A 670       2.976  -7.626  65.358  1.00 41.55           S  
ANISOU 5514  SD  MET A 670     5372   5991   4426   -328   -186   -104       S  
ATOM   5515  CE  MET A 670       1.467  -7.759  64.412  1.00 38.75           C  
ANISOU 5515  CE  MET A 670     5031   5577   4115   -320   -155    -70       C  
ATOM   5516  N   CYS A 671      -1.358  -7.351  68.370  1.00 48.63           N  
ANISOU 5516  N   CYS A 671     6263   7030   5184   -144    -96    -86       N  
ATOM   5517  CA  CYS A 671      -2.676  -6.852  67.976  1.00 46.51           C  
ANISOU 5517  CA  CYS A 671     6002   6731   4940   -127    -77    -91       C  
ATOM   5518  C   CYS A 671      -3.205  -5.863  69.017  1.00 46.78           C  
ANISOU 5518  C   CYS A 671     6051   6811   4910    -71    -79   -148       C  
ATOM   5519  O   CYS A 671      -3.730  -4.807  68.664  1.00 44.94           O  
ANISOU 5519  O   CYS A 671     5847   6536   4692    -63    -91   -200       O  
ATOM   5520  CB  CYS A 671      -3.641  -8.031  67.783  1.00 45.67           C  
ANISOU 5520  CB  CYS A 671     5858   6635   4860   -121    -33     -9       C  
ATOM   5521  SG  CYS A 671      -5.403  -7.609  67.717  1.00 51.20           S  
ANISOU 5521  SG  CYS A 671     6546   7335   5573    -84     -1     -7       S  
ATOM   5522  N   GLU A 672      -3.041  -6.213  70.294  1.00 47.27           N  
ANISOU 5522  N   GLU A 672     6098   6963   4900    -25    -68   -138       N  
ATOM   5523  CA  GLU A 672      -3.373  -5.339  71.416  1.00 47.54           C  
ANISOU 5523  CA  GLU A 672     6149   7056   4859     39    -75   -197       C  
ATOM   5524  C   GLU A 672      -2.495  -4.084  71.419  1.00 45.82           C  
ANISOU 5524  C   GLU A 672     5973   6800   4637     24   -135   -296       C  
ATOM   5525  O   GLU A 672      -2.970  -2.970  71.677  1.00 45.41           O  
ANISOU 5525  O   GLU A 672     5951   6737   4565     58   -152   -365       O  
ATOM   5526  CB  GLU A 672      -3.189  -6.098  72.736  1.00 51.44           C  
ANISOU 5526  CB  GLU A 672     6618   7656   5270     92    -53   -159       C  
ATOM   5527  CG  GLU A 672      -3.987  -5.539  73.908  1.00 57.83           C  
ANISOU 5527  CG  GLU A 672     7432   8546   5996    177    -36   -188       C  
ATOM   5528  CD  GLU A 672      -5.485  -5.758  73.741  1.00 65.62           C  
ANISOU 5528  CD  GLU A 672     8393   9542   7000    202     21   -137       C  
ATOM   5529  OE1 GLU A 672      -5.888  -6.820  73.197  1.00 64.61           O  
ANISOU 5529  OE1 GLU A 672     8229   9396   6925    168     60    -50       O  
ATOM   5530  OE2 GLU A 672      -6.259  -4.863  74.157  1.00 70.85           O  
ANISOU 5530  OE2 GLU A 672     9068  10227   7624    258     23   -187       O  
ATOM   5531  N   TYR A 673      -1.212  -4.283  71.137  1.00 42.93           N  
ANISOU 5531  N   TYR A 673     5606   6413   4292    -26   -168   -304       N  
ATOM   5532  CA  TYR A 673      -0.246  -3.193  71.044  1.00 43.08           C  
ANISOU 5532  CA  TYR A 673     5655   6388   4324    -56   -225   -391       C  
ATOM   5533  C   TYR A 673      -0.627  -2.193  69.950  1.00 41.84           C  
ANISOU 5533  C   TYR A 673     5534   6128   4236    -92   -236   -426       C  
ATOM   5534  O   TYR A 673      -0.580  -0.984  70.169  1.00 40.99           O  
ANISOU 5534  O   TYR A 673     5463   5989   4123    -83   -272   -506       O  
ATOM   5535  CB  TYR A 673       1.152  -3.772  70.808  1.00 43.40           C  
ANISOU 5535  CB  TYR A 673     5676   6429   4386   -108   -248   -377       C  
ATOM   5536  CG  TYR A 673       2.303  -2.788  70.871  1.00 47.71           C  
ANISOU 5536  CG  TYR A 673     6238   6945   4945   -144   -308   -461       C  
ATOM   5537  CD1 TYR A 673       2.447  -1.905  71.949  1.00 45.65           C  
ANISOU 5537  CD1 TYR A 673     5995   6721   4629   -101   -349   -547       C  
ATOM   5538  CD2 TYR A 673       3.282  -2.773  69.865  1.00 46.88           C  
ANISOU 5538  CD2 TYR A 673     6125   6777   4909   -220   -324   -456       C  
ATOM   5539  CE1 TYR A 673       3.521  -1.015  72.012  1.00 49.09           C  
ANISOU 5539  CE1 TYR A 673     6441   7124   5088   -141   -409   -628       C  
ATOM   5540  CE2 TYR A 673       4.361  -1.888  69.923  1.00 51.07           C  
ANISOU 5540  CE2 TYR A 673     6662   7280   5462   -261   -377   -529       C  
ATOM   5541  CZ  TYR A 673       4.473  -1.013  71.000  1.00 50.31           C  
ANISOU 5541  CZ  TYR A 673     6583   7214   5320   -224   -421   -616       C  
ATOM   5542  OH  TYR A 673       5.544  -0.150  71.061  1.00 51.97           O  
ANISOU 5542  OH  TYR A 673     6794   7390   5561   -270   -477   -692       O  
ATOM   5543  N   MET A 674      -1.028  -2.699  68.785  1.00 41.40           N  
ANISOU 5543  N   MET A 674     5471   6018   4241   -128   -207   -366       N  
ATOM   5544  CA  MET A 674      -1.486  -1.835  67.684  1.00 41.53           C  
ANISOU 5544  CA  MET A 674     5523   5941   4318   -153   -213   -388       C  
ATOM   5545  C   MET A 674      -2.988  -1.541  67.745  1.00 42.11           C  
ANISOU 5545  C   MET A 674     5604   6018   4378    -98   -186   -387       C  
ATOM   5546  O   MET A 674      -3.536  -0.902  66.849  1.00 42.38           O  
ANISOU 5546  O   MET A 674     5666   5980   4455   -106   -188   -400       O  
ATOM   5547  CB  MET A 674      -1.102  -2.432  66.326  1.00 41.06           C  
ANISOU 5547  CB  MET A 674     5455   5821   4327   -212   -202   -334       C  
ATOM   5548  CG  MET A 674       0.399  -2.381  66.026  1.00 41.99           C  
ANISOU 5548  CG  MET A 674     5569   5916   4468   -271   -231   -347       C  
ATOM   5549  SD  MET A 674       0.979  -0.707  65.685  1.00 48.53           S  
ANISOU 5549  SD  MET A 674     6447   6660   5333   -308   -274   -429       S  
ATOM   5550  CE  MET A 674       2.586  -0.731  66.462  1.00 47.68           C  
ANISOU 5550  CE  MET A 674     6313   6596   5209   -342   -313   -466       C  
ATOM   5551  N   ASN A 675      -3.643  -2.018  68.806  1.00 42.45           N  
ANISOU 5551  N   ASN A 675     5620   6149   4359    -38   -160   -369       N  
ATOM   5552  CA  ASN A 675      -5.084  -1.820  69.019  1.00 41.31           C  
ANISOU 5552  CA  ASN A 675     5472   6030   4196     20   -130   -364       C  
ATOM   5553  C   ASN A 675      -5.966  -2.184  67.791  1.00 39.60           C  
ANISOU 5553  C   ASN A 675     5242   5758   4046     -1   -104   -315       C  
ATOM   5554  O   ASN A 675      -6.966  -1.518  67.481  1.00 39.22           O  
ANISOU 5554  O   ASN A 675     5209   5685   4007     31    -99   -338       O  
ATOM   5555  CB  ASN A 675      -5.339  -0.389  69.551  1.00 41.78           C  
ANISOU 5555  CB  ASN A 675     5577   6078   4219     68   -161   -457       C  
ATOM   5556  CG  ASN A 675      -6.783  -0.152  69.963  1.00 39.92           C  
ANISOU 5556  CG  ASN A 675     5333   5886   3949    143   -129   -458       C  
ATOM   5557  OD1 ASN A 675      -7.471  -1.063  70.423  1.00 42.22           O  
ANISOU 5557  OD1 ASN A 675     5576   6253   4214    173    -82   -396       O  
ATOM   5558  ND2 ASN A 675      -7.254   1.075  69.784  1.00 38.63           N  
ANISOU 5558  ND2 ASN A 675     5216   5675   3788    173   -154   -527       N  
ATOM   5559  N   ASN A 676      -5.605  -3.261  67.101  1.00 38.86           N  
ANISOU 5559  N   ASN A 676     5121   5648   3997    -49    -91   -250       N  
ATOM   5560  CA  ASN A 676      -6.297  -3.607  65.848  1.00 38.98           C  
ANISOU 5560  CA  ASN A 676     5128   5606   4078    -72    -78   -212       C  
ATOM   5561  C   ASN A 676      -7.748  -4.036  66.047  1.00 40.20           C  
ANISOU 5561  C   ASN A 676     5242   5801   4231    -29    -39   -177       C  
ATOM   5562  O   ASN A 676      -8.164  -4.341  67.159  1.00 38.65           O  
ANISOU 5562  O   ASN A 676     5016   5685   3983     12    -12   -160       O  
ATOM   5563  CB  ASN A 676      -5.522  -4.651  65.053  1.00 34.66           C  
ANISOU 5563  CB  ASN A 676     4563   5030   3576   -128    -79   -159       C  
ATOM   5564  CG  ASN A 676      -4.143  -4.177  64.656  1.00 35.08           C  
ANISOU 5564  CG  ASN A 676     4649   5039   3641   -173   -113   -191       C  
ATOM   5565  OD1 ASN A 676      -3.172  -4.924  64.766  1.00 32.73           O  
ANISOU 5565  OD1 ASN A 676     4334   4761   3341   -202   -117   -164       O  
ATOM   5566  ND2 ASN A 676      -4.044  -2.928  64.196  1.00 31.94           N  
ANISOU 5566  ND2 ASN A 676     4298   4581   3258   -179   -138   -248       N  
ATOM   5567  N   LYS A 677      -8.506  -4.050  64.952  1.00 42.13           N  
ANISOU 5567  N   LYS A 677     5484   5993   4532    -37    -37   -165       N  
ATOM   5568  CA  LYS A 677      -9.927  -4.387  64.975  1.00 41.58           C  
ANISOU 5568  CA  LYS A 677     5370   5955   4475     -2     -6   -136       C  
ATOM   5569  C   LYS A 677     -10.173  -5.866  65.248  1.00 42.48           C  
ANISOU 5569  C   LYS A 677     5420   6113   4607    -20     29    -55       C  
ATOM   5570  O   LYS A 677     -11.173  -6.223  65.868  1.00 42.82           O  
ANISOU 5570  O   LYS A 677     5415   6215   4638     13     66    -24       O  
ATOM   5571  CB  LYS A 677     -10.557  -4.009  63.640  1.00 43.34           C  
ANISOU 5571  CB  LYS A 677     5608   6104   4755     -7    -23   -151       C  
ATOM   5572  CG  LYS A 677     -12.068  -4.151  63.558  1.00 43.62           C  
ANISOU 5572  CG  LYS A 677     5598   6168   4809     32      1   -137       C  
ATOM   5573  CD  LYS A 677     -12.531  -3.867  62.144  1.00 41.97           C  
ANISOU 5573  CD  LYS A 677     5407   5884   4656     26    -25   -153       C  
ATOM   5574  CE  LYS A 677     -13.969  -3.384  62.120  1.00 47.38           C  
ANISOU 5574  CE  LYS A 677     6068   6592   5343     83    -14   -173       C  
ATOM   5575  NZ  LYS A 677     -14.937  -4.412  62.580  1.00 44.31           N  
ANISOU 5575  NZ  LYS A 677     5593   6269   4974     88     24   -118       N  
ATOM   5576  N   GLN A 678      -9.265  -6.722  64.780  1.00 42.09           N  
ANISOU 5576  N   GLN A 678     5370   6035   4589    -71     19    -20       N  
ATOM   5577  CA  GLN A 678      -9.461  -8.166  64.852  1.00 41.60           C  
ANISOU 5577  CA  GLN A 678     5254   5993   4558    -93     45     58       C  
ATOM   5578  C   GLN A 678      -8.129  -8.883  64.700  1.00 40.80           C  
ANISOU 5578  C   GLN A 678     5166   5873   4461   -134     29     82       C  
ATOM   5579  O   GLN A 678      -7.350  -8.561  63.811  1.00 41.31           O  
ANISOU 5579  O   GLN A 678     5268   5881   4549   -163     -5     52       O  
ATOM   5580  CB  GLN A 678     -10.439  -8.618  63.756  1.00 41.35           C  
ANISOU 5580  CB  GLN A 678     5193   5914   4603   -107     44     78       C  
ATOM   5581  CG  GLN A 678     -10.803 -10.096  63.795  1.00 43.51           C  
ANISOU 5581  CG  GLN A 678     5409   6199   4924   -132     69    156       C  
ATOM   5582  CD  GLN A 678     -11.787 -10.513  62.704  1.00 42.83           C  
ANISOU 5582  CD  GLN A 678     5290   6064   4918   -146     58    165       C  
ATOM   5583  OE1 GLN A 678     -12.112  -9.736  61.803  1.00 43.31           O  
ANISOU 5583  OE1 GLN A 678     5378   6082   4997   -136     30    115       O  
ATOM   5584  NE2 GLN A 678     -12.266 -11.753  62.789  1.00 40.78           N  
ANISOU 5584  NE2 GLN A 678     4974   5809   4709   -169     79    230       N  
ATOM   5585  N   HIS A 679      -7.868  -9.854  65.569  1.00 40.46           N  
ANISOU 5585  N   HIS A 679     5093   5884   4396   -133     55    138       N  
ATOM   5586  CA  HIS A 679      -6.635 -10.629  65.488  1.00 39.77           C  
ANISOU 5586  CA  HIS A 679     5014   5786   4310   -165     40    164       C  
ATOM   5587  C   HIS A 679      -6.752 -11.660  64.371  1.00 40.10           C  
ANISOU 5587  C   HIS A 679     5039   5766   4430   -203     32    205       C  
ATOM   5588  O   HIS A 679      -7.649 -12.509  64.391  1.00 39.15           O  
ANISOU 5588  O   HIS A 679     4877   5648   4349   -205     57    258       O  
ATOM   5589  CB  HIS A 679      -6.317 -11.296  66.829  1.00 39.13           C  
ANISOU 5589  CB  HIS A 679     4913   5784   4172   -142     69    210       C  
ATOM   5590  CG  HIS A 679      -5.338 -12.428  66.734  1.00 38.25           C  
ANISOU 5590  CG  HIS A 679     4797   5662   4073   -168     61    258       C  
ATOM   5591  ND1 HIS A 679      -4.077 -12.280  66.200  1.00 34.37           N  
ANISOU 5591  ND1 HIS A 679     4336   5140   3583   -194     23    226       N  
ATOM   5592  CD2 HIS A 679      -5.430 -13.723  67.126  1.00 38.80           C  
ANISOU 5592  CD2 HIS A 679     4837   5751   4156   -171     89    337       C  
ATOM   5593  CE1 HIS A 679      -3.438 -13.436  66.256  1.00 34.74           C  
ANISOU 5593  CE1 HIS A 679     4371   5189   3638   -206     25    279       C  
ATOM   5594  NE2 HIS A 679      -4.237 -14.328  66.812  1.00 38.60           N  
ANISOU 5594  NE2 HIS A 679     4827   5704   4136   -192     63    347       N  
ATOM   5595  N   LEU A 680      -5.851 -11.566  63.393  1.00 39.14           N  
ANISOU 5595  N   LEU A 680     4950   5590   4332   -231     -3    181       N  
ATOM   5596  CA  LEU A 680      -5.863 -12.470  62.247  1.00 38.68           C  
ANISOU 5596  CA  LEU A 680     4883   5472   4341   -259    -19    208       C  
ATOM   5597  C   LEU A 680      -4.466 -12.860  61.793  1.00 39.32           C  
ANISOU 5597  C   LEU A 680     4988   5533   4420   -282    -44    209       C  
ATOM   5598  O   LEU A 680      -4.302 -13.423  60.700  1.00 39.70           O  
ANISOU 5598  O   LEU A 680     5040   5528   4515   -298    -64    217       O  
ATOM   5599  CB  LEU A 680      -6.614 -11.851  61.069  1.00 35.44           C  
ANISOU 5599  CB  LEU A 680     4486   5005   3975   -259    -38    171       C  
ATOM   5600  CG  LEU A 680      -8.079 -11.479  61.277  1.00 35.23           C  
ANISOU 5600  CG  LEU A 680     4431   4993   3961   -234    -19    165       C  
ATOM   5601  CD1 LEU A 680      -8.472 -10.439  60.248  1.00 32.88           C  
ANISOU 5601  CD1 LEU A 680     4167   4648   3680   -223    -44    110       C  
ATOM   5602  CD2 LEU A 680      -8.991 -12.706  61.228  1.00 31.33           C  
ANISOU 5602  CD2 LEU A 680     3881   4496   3525   -244     -2    222       C  
ATOM   5603  N   MET A 681      -3.464 -12.550  62.613  1.00 36.76           N  
ANISOU 5603  N   MET A 681     4676   5253   4039   -278    -45    196       N  
ATOM   5604  CA  MET A 681      -2.105 -12.975  62.306  1.00 38.22           C  
ANISOU 5604  CA  MET A 681     4873   5431   4218   -296    -66    200       C  
ATOM   5605  C   MET A 681      -1.943 -14.437  62.698  1.00 38.14           C  
ANISOU 5605  C   MET A 681     4837   5438   4216   -293    -54    266       C  
ATOM   5606  O   MET A 681      -1.581 -14.754  63.834  1.00 41.32           O  
ANISOU 5606  O   MET A 681     5229   5900   4572   -276    -39    290       O  
ATOM   5607  CB  MET A 681      -1.069 -12.100  63.008  1.00 38.50           C  
ANISOU 5607  CB  MET A 681     4925   5507   4195   -295    -78    157       C  
ATOM   5608  CG  MET A 681      -1.077 -10.631  62.579  1.00 36.65           C  
ANISOU 5608  CG  MET A 681     4722   5242   3959   -303    -93     92       C  
ATOM   5609  SD  MET A 681      -0.518 -10.375  60.886  1.00 37.27           S  
ANISOU 5609  SD  MET A 681     4827   5245   4090   -335   -116     77       S  
ATOM   5610  CE  MET A 681      -2.030  -9.929  60.033  1.00 28.15           C  
ANISOU 5610  CE  MET A 681     3684   4036   2975   -321   -110     67       C  
ATOM   5611  N   PHE A 682      -2.244 -15.324  61.758  1.00 36.15           N  
ANISOU 5611  N   PHE A 682     4578   5133   4025   -306    -63    295       N  
ATOM   5612  CA  PHE A 682      -2.171 -16.757  62.015  1.00 38.55           C  
ANISOU 5612  CA  PHE A 682     4861   5435   4350   -305    -55    358       C  
ATOM   5613  C   PHE A 682      -0.944 -17.332  61.326  1.00 38.76           C  
ANISOU 5613  C   PHE A 682     4904   5440   4383   -312    -84    358       C  
ATOM   5614  O   PHE A 682      -0.866 -17.366  60.095  1.00 38.25           O  
ANISOU 5614  O   PHE A 682     4854   5322   4358   -321   -108    337       O  
ATOM   5615  CB  PHE A 682      -3.450 -17.481  61.552  1.00 39.29           C  
ANISOU 5615  CB  PHE A 682     4929   5484   4516   -313    -47    391       C  
ATOM   5616  CG  PHE A 682      -4.736 -16.911  62.125  1.00 41.01           C  
ANISOU 5616  CG  PHE A 682     5122   5726   4733   -305    -17    392       C  
ATOM   5617  CD1 PHE A 682      -4.792 -16.411  63.431  1.00 43.35           C  
ANISOU 5617  CD1 PHE A 682     5412   6096   4964   -283     15    398       C  
ATOM   5618  CD2 PHE A 682      -5.902 -16.906  61.361  1.00 39.56           C  
ANISOU 5618  CD2 PHE A 682     4920   5498   4612   -313    -22    384       C  
ATOM   5619  CE1 PHE A 682      -5.990 -15.890  63.955  1.00 44.52           C  
ANISOU 5619  CE1 PHE A 682     5535   6273   5107   -267     45    399       C  
ATOM   5620  CE2 PHE A 682      -7.106 -16.391  61.870  1.00 40.46           C  
ANISOU 5620  CE2 PHE A 682     5005   5642   4727   -302      7    384       C  
ATOM   5621  CZ  PHE A 682      -7.152 -15.882  63.169  1.00 43.75           C  
ANISOU 5621  CZ  PHE A 682     5415   6133   5076   -278     43    393       C  
ATOM   5622  N   MET A 683       0.023 -17.765  62.129  1.00 40.04           N  
ANISOU 5622  N   MET A 683     5065   5649   4500   -300    -81    380       N  
ATOM   5623  CA  MET A 683       1.276 -18.305  61.601  1.00 41.76           C  
ANISOU 5623  CA  MET A 683     5293   5858   4714   -300   -107    379       C  
ATOM   5624  C   MET A 683       1.403 -19.775  61.992  1.00 42.35           C  
ANISOU 5624  C   MET A 683     5359   5930   4803   -285   -102    444       C  
ATOM   5625  O   MET A 683       1.477 -20.115  63.172  1.00 45.06           O  
ANISOU 5625  O   MET A 683     5692   6323   5106   -267    -81    482       O  
ATOM   5626  CB  MET A 683       2.480 -17.470  62.083  1.00 39.83           C  
ANISOU 5626  CB  MET A 683     5056   5670   4409   -298   -116    340       C  
ATOM   5627  CG  MET A 683       3.845 -18.059  61.772  1.00 39.97           C  
ANISOU 5627  CG  MET A 683     5075   5699   4414   -292   -138    344       C  
ATOM   5628  SD  MET A 683       5.250 -17.078  62.363  1.00 43.52           S  
ANISOU 5628  SD  MET A 683     5518   6216   4800   -295   -153    294       S  
ATOM   5629  CE  MET A 683       5.445 -15.978  60.955  1.00 36.75           C  
ANISOU 5629  CE  MET A 683     4676   5308   3978   -330   -165    242       C  
ATOM   5630  N   ASP A 684       1.433 -20.638  60.987  1.00 42.85           N  
ANISOU 5630  N   ASP A 684     5429   5934   4920   -288   -124    457       N  
ATOM   5631  CA  ASP A 684       1.497 -22.081  61.201  1.00 44.26           C  
ANISOU 5631  CA  ASP A 684     5603   6089   5124   -275   -125    517       C  
ATOM   5632  C   ASP A 684       2.785 -22.661  60.616  1.00 43.61           C  
ANISOU 5632  C   ASP A 684     5536   6001   5031   -257   -156    509       C  
ATOM   5633  O   ASP A 684       3.370 -22.083  59.691  1.00 40.18           O  
ANISOU 5633  O   ASP A 684     5114   5561   4593   -260   -177    461       O  
ATOM   5634  CB  ASP A 684       0.294 -22.770  60.538  1.00 46.09           C  
ANISOU 5634  CB  ASP A 684     5826   6245   5440   -290   -129    538       C  
ATOM   5635  CG  ASP A 684      -1.046 -22.283  61.079  1.00 50.26           C  
ANISOU 5635  CG  ASP A 684     6329   6781   5985   -307    -97    550       C  
ATOM   5636  OD1 ASP A 684      -1.283 -22.371  62.307  1.00 51.03           O  
ANISOU 5636  OD1 ASP A 684     6412   6929   6050   -299    -60    594       O  
ATOM   5637  OD2 ASP A 684      -1.876 -21.828  60.261  1.00 55.16           O  
ANISOU 5637  OD2 ASP A 684     6946   7364   6650   -322   -108    516       O  
ATOM   5638  N   ARG A 685       3.208 -23.809  61.149  1.00 42.58           N  
ANISOU 5638  N   ARG A 685     5407   5874   4897   -235   -156    561       N  
ATOM   5639  CA  ARG A 685       4.341 -24.541  60.605  1.00 41.66           C  
ANISOU 5639  CA  ARG A 685     5305   5749   4775   -209   -186    559       C  
ATOM   5640  C   ARG A 685       4.143 -24.831  59.123  1.00 42.99           C  
ANISOU 5640  C   ARG A 685     5487   5844   5002   -212   -218    531       C  
ATOM   5641  O   ARG A 685       3.079 -25.289  58.702  1.00 44.41           O  
ANISOU 5641  O   ARG A 685     5667   5959   5247   -226   -223    543       O  
ATOM   5642  CB  ARG A 685       4.558 -25.841  61.368  1.00 41.22           C  
ANISOU 5642  CB  ARG A 685     5253   5690   4718   -182   -182    626       C  
ATOM   5643  CG  ARG A 685       5.900 -26.513  61.087  1.00 40.88           C  
ANISOU 5643  CG  ARG A 685     5223   5660   4648   -143   -211    624       C  
ATOM   5644  CD  ARG A 685       5.794 -27.529  59.959  1.00 42.36           C  
ANISOU 5644  CD  ARG A 685     5431   5763   4902   -132   -244    626       C  
ATOM   5645  NE  ARG A 685       4.960 -28.674  60.325  1.00 42.39           N  
ANISOU 5645  NE  ARG A 685     5440   5702   4962   -134   -238    690       N  
ATOM   5646  CZ  ARG A 685       4.543 -29.600  59.471  1.00 45.96           C  
ANISOU 5646  CZ  ARG A 685     5909   6065   5490   -132   -268    694       C  
ATOM   5647  NH1 ARG A 685       4.876 -29.525  58.188  1.00 49.59           N  
ANISOU 5647  NH1 ARG A 685     6381   6495   5965   -120   -306    638       N  
ATOM   5648  NH2 ARG A 685       3.788 -30.604  59.896  1.00 46.90           N  
ANISOU 5648  NH2 ARG A 685     6030   6123   5668   -141   -260    756       N  
ATOM   5649  N   GLU A 686       5.174 -24.540  58.339  1.00 42.18           N  
ANISOU 5649  N   GLU A 686     5394   5758   4874   -198   -239    491       N  
ATOM   5650  CA  GLU A 686       5.167 -24.857  56.925  1.00 42.76           C  
ANISOU 5650  CA  GLU A 686     5485   5775   4989   -186   -271    463       C  
ATOM   5651  C   GLU A 686       6.002 -26.114  56.654  1.00 40.75           C  
ANISOU 5651  C   GLU A 686     5243   5503   4736   -144   -298    482       C  
ATOM   5652  O   GLU A 686       5.446 -27.185  56.450  1.00 41.36           O  
ANISOU 5652  O   GLU A 686     5332   5515   4867   -135   -316    507       O  
ATOM   5653  CB  GLU A 686       5.637 -23.651  56.105  1.00 44.43           C  
ANISOU 5653  CB  GLU A 686     5698   6011   5173   -194   -271    409       C  
ATOM   5654  CG  GLU A 686       5.215 -23.707  54.656  1.00 50.51           C  
ANISOU 5654  CG  GLU A 686     6487   6723   5983   -184   -296    378       C  
ATOM   5655  CD  GLU A 686       5.010 -22.339  54.044  1.00 59.05           C  
ANISOU 5655  CD  GLU A 686     7572   7812   7052   -204   -285    337       C  
ATOM   5656  OE1 GLU A 686       3.875 -22.063  53.593  1.00 64.06           O  
ANISOU 5656  OE1 GLU A 686     8213   8403   7725   -215   -289    323       O  
ATOM   5657  OE2 GLU A 686       5.973 -21.540  54.014  1.00 60.71           O  
ANISOU 5657  OE2 GLU A 686     7778   8073   7218   -208   -272    320       O  
ATOM   5658  N   ALA A 687       7.324 -26.002  56.694  1.00 39.62           N  
ANISOU 5658  N   ALA A 687     5097   5420   4539   -119   -302    471       N  
ATOM   5659  CA  ALA A 687       8.189 -27.137  56.348  1.00 39.76           C  
ANISOU 5659  CA  ALA A 687     5127   5428   4552    -70   -329    483       C  
ATOM   5660  C   ALA A 687       8.952 -27.730  57.524  1.00 41.03           C  
ANISOU 5660  C   ALA A 687     5280   5638   4670    -45   -323    524       C  
ATOM   5661  O   ALA A 687       9.348 -27.020  58.452  1.00 40.71           O  
ANISOU 5661  O   ALA A 687     5219   5669   4579    -58   -300    525       O  
ATOM   5662  CB  ALA A 687       9.167 -26.742  55.263  1.00 37.63           C  
ANISOU 5662  CB  ALA A 687     4858   5186   4255    -47   -344    439       C  
ATOM   5663  N   ILE A 688       9.152 -29.043  57.469  1.00 41.02           N  
ANISOU 5663  N   ILE A 688     5300   5596   4690     -5   -346    555       N  
ATOM   5664  CA  ILE A 688      10.141 -29.703  58.303  1.00 40.99           C  
ANISOU 5664  CA  ILE A 688     5294   5640   4639     38   -348    587       C  
ATOM   5665  C   ILE A 688      11.200 -30.304  57.392  1.00 41.11           C  
ANISOU 5665  C   ILE A 688     5320   5658   4641     93   -382    563       C  
ATOM   5666  O   ILE A 688      10.894 -31.101  56.502  1.00 43.21           O  
ANISOU 5666  O   ILE A 688     5613   5849   4956    115   -411    557       O  
ATOM   5667  CB  ILE A 688       9.531 -30.789  59.205  1.00 41.65           C  
ANISOU 5667  CB  ILE A 688     5397   5678   4752     47   -342    656       C  
ATOM   5668  CG1 ILE A 688       8.418 -30.191  60.073  1.00 41.81           C  
ANISOU 5668  CG1 ILE A 688     5402   5701   4783     -3   -303    683       C  
ATOM   5669  CG2 ILE A 688      10.620 -31.406  60.081  1.00 40.09           C  
ANISOU 5669  CG2 ILE A 688     5201   5538   4494    100   -345    689       C  
ATOM   5670  CD1 ILE A 688       7.636 -31.212  60.872  1.00 44.28           C  
ANISOU 5670  CD1 ILE A 688     5728   5960   5135     -3   -288    759       C  
ATOM   5671  N   ALA A 689      12.447 -29.911  57.617  1.00 40.12           N  
ANISOU 5671  N   ALA A 689     5170   5622   4450    117   -380    545       N  
ATOM   5672  CA  ALA A 689      13.539 -30.303  56.740  1.00 37.57           C  
ANISOU 5672  CA  ALA A 689     4847   5323   4107    170   -406    519       C  
ATOM   5673  C   ALA A 689      14.738 -30.812  57.523  1.00 38.80           C  
ANISOU 5673  C   ALA A 689     4987   5550   4204    222   -413    537       C  
ATOM   5674  O   ALA A 689      15.015 -30.354  58.638  1.00 38.92           O  
ANISOU 5674  O   ALA A 689     4979   5632   4177    208   -396    550       O  
ATOM   5675  CB  ALA A 689      13.939 -29.144  55.864  1.00 36.33           C  
ANISOU 5675  CB  ALA A 689     4663   5208   3932    146   -395    468       C  
ATOM   5676  N   GLY A 690      15.447 -31.759  56.921  1.00 39.61           N  
ANISOU 5676  N   GLY A 690     5106   5643   4302    288   -443    535       N  
ATOM   5677  CA  GLY A 690      16.641 -32.339  57.514  1.00 39.59           C  
ANISOU 5677  CA  GLY A 690     5090   5708   4243    350   -456    549       C  
ATOM   5678  C   GLY A 690      17.210 -33.446  56.643  1.00 41.33           C  
ANISOU 5678  C   GLY A 690     5336   5897   4469    428   -492    541       C  
ATOM   5679  O   GLY A 690      16.564 -33.870  55.679  1.00 41.98           O  
ANISOU 5679  O   GLY A 690     5454   5894   4604    433   -510    529       O  
ATOM   5680  N   PRO A 691      18.421 -33.929  56.980  1.00 40.46           N  
ANISOU 5680  N   PRO A 691     5211   5858   4306    495   -506    545       N  
ATOM   5681  CA  PRO A 691      19.004 -35.068  56.270  1.00 40.86           C  
ANISOU 5681  CA  PRO A 691     5289   5880   4354    581   -543    540       C  
ATOM   5682  C   PRO A 691      18.306 -36.358  56.676  1.00 41.60           C  
ANISOU 5682  C   PRO A 691     5444   5867   4493    610   -566    588       C  
ATOM   5683  O   PRO A 691      17.752 -36.419  57.776  1.00 43.28           O  
ANISOU 5683  O   PRO A 691     5667   6064   4714    578   -549    636       O  
ATOM   5684  CB  PRO A 691      20.460 -35.108  56.772  1.00 40.84           C  
ANISOU 5684  CB  PRO A 691     5243   5996   4277    639   -548    535       C  
ATOM   5685  CG  PRO A 691      20.579 -34.081  57.838  1.00 40.46           C  
ANISOU 5685  CG  PRO A 691     5149   6029   4196    581   -518    540       C  
ATOM   5686  CD  PRO A 691      19.217 -33.539  58.154  1.00 39.25           C  
ANISOU 5686  CD  PRO A 691     5016   5808   4090    499   -494    556       C  
ATOM   5687  N   PRO A 692      18.331 -37.390  55.813  1.00 42.48           N  
ANISOU 5687  N   PRO A 692     5600   5906   4635    672   -605    577       N  
ATOM   5688  CA  PRO A 692      17.870 -38.700  56.291  1.00 45.20           C  
ANISOU 5688  CA  PRO A 692     6003   6149   5022    706   -631    627       C  
ATOM   5689  C   PRO A 692      18.677 -39.140  57.517  1.00 47.30           C  
ANISOU 5689  C   PRO A 692     6264   6479   5230    755   -627    674       C  
ATOM   5690  O   PRO A 692      19.880 -38.881  57.580  1.00 49.21           O  
ANISOU 5690  O   PRO A 692     6466   6830   5400    803   -628    650       O  
ATOM   5691  CB  PRO A 692      18.136 -39.624  55.092  1.00 43.36           C  
ANISOU 5691  CB  PRO A 692     5809   5854   4812    782   -681    590       C  
ATOM   5692  CG  PRO A 692      18.050 -38.740  53.910  1.00 41.01           C  
ANISOU 5692  CG  PRO A 692     5486   5581   4514    757   -675    528       C  
ATOM   5693  CD  PRO A 692      18.592 -37.395  54.361  1.00 43.70           C  
ANISOU 5693  CD  PRO A 692     5759   6050   4795    708   -628    521       C  
ATOM   5694  N   LEU A 693      18.029 -39.772  58.492  1.00 50.45           N  
ANISOU 5694  N   LEU A 693     6698   6814   5657    744   -619    741       N  
ATOM   5695  CA  LEU A 693      18.732 -40.173  59.721  1.00 52.27           C  
ANISOU 5695  CA  LEU A 693     6928   7107   5826    795   -613    791       C  
ATOM   5696  C   LEU A 693      19.837 -41.187  59.417  1.00 52.67           C  
ANISOU 5696  C   LEU A 693     7001   7168   5842    907   -656    782       C  
ATOM   5697  O   LEU A 693      19.591 -42.213  58.777  1.00 51.52           O  
ANISOU 5697  O   LEU A 693     6910   6915   5750    948   -692    785       O  
ATOM   5698  CB  LEU A 693      17.764 -40.740  60.769  1.00 52.48           C  
ANISOU 5698  CB  LEU A 693     6993   7054   5891    767   -593    875       C  
ATOM   5699  CG  LEU A 693      17.954 -40.454  62.272  1.00 53.85           C  
ANISOU 5699  CG  LEU A 693     7150   7312   5999    769   -558    930       C  
ATOM   5700  CD1 LEU A 693      17.522 -41.666  63.089  1.00 50.80           C  
ANISOU 5700  CD1 LEU A 693     6823   6839   5639    804   -556   1023       C  
ATOM   5701  CD2 LEU A 693      19.371 -40.050  62.666  1.00 55.13           C  
ANISOU 5701  CD2 LEU A 693     7268   7620   6059    830   -568    898       C  
ATOM   5702  N   GLY A 694      21.050 -40.873  59.870  1.00 53.43           N  
ANISOU 5702  N   GLY A 694     7054   7396   5852    958   -656    767       N  
ATOM   5703  CA  GLY A 694      22.194 -41.767  59.742  1.00 53.35           C  
ANISOU 5703  CA  GLY A 694     7056   7418   5796   1072   -693    761       C  
ATOM   5704  C   GLY A 694      23.059 -41.522  58.522  1.00 55.09           C  
ANISOU 5704  C   GLY A 694     7242   7697   5993   1113   -713    687       C  
ATOM   5705  O   GLY A 694      24.087 -42.191  58.348  1.00 57.30           O  
ANISOU 5705  O   GLY A 694     7524   8020   6229   1214   -744    674       O  
ATOM   5706  N   SER A 695      22.649 -40.565  57.684  1.00 52.77           N  
ANISOU 5706  N   SER A 695     6916   7408   5725   1041   -694    641       N  
ATOM   5707  CA  SER A 695      23.339 -40.249  56.425  1.00 50.13           C  
ANISOU 5707  CA  SER A 695     6549   7126   5372   1073   -704    576       C  
ATOM   5708  C   SER A 695      24.309 -39.073  56.571  1.00 50.35           C  
ANISOU 5708  C   SER A 695     6486   7309   5335   1050   -675    544       C  
ATOM   5709  O   SER A 695      24.337 -38.406  57.607  1.00 49.57           O  
ANISOU 5709  O   SER A 695     6352   7271   5212   1000   -651    563       O  
ATOM   5710  CB  SER A 695      22.316 -39.922  55.340  1.00 48.04           C  
ANISOU 5710  CB  SER A 695     6307   6773   5174   1014   -701    547       C  
ATOM   5711  OG  SER A 695      21.644 -38.711  55.639  1.00 42.98           O  
ANISOU 5711  OG  SER A 695     5631   6152   4549    905   -659    548       O  
ATOM   5712  N   LYS A 696      25.092 -38.822  55.522  1.00 50.41           N  
ANISOU 5712  N   LYS A 696     6456   7380   5317   1088   -677    496       N  
ATOM   5713  CA  LYS A 696      26.025 -37.694  55.496  1.00 51.20           C  
ANISOU 5713  CA  LYS A 696     6464   7621   5368   1060   -648    464       C  
ATOM   5714  C   LYS A 696      25.465 -36.454  54.780  1.00 49.31           C  
ANISOU 5714  C   LYS A 696     6196   7379   5160    962   -611    438       C  
ATOM   5715  O   LYS A 696      26.175 -35.469  54.590  1.00 47.53           O  
ANISOU 5715  O   LYS A 696     5896   7256   4907    931   -585    412       O  
ATOM   5716  CB  LYS A 696      27.363 -38.115  54.885  1.00 54.00           C  
ANISOU 5716  CB  LYS A 696     6780   8067   5669   1162   -665    435       C  
ATOM   5717  CG  LYS A 696      28.239 -38.943  55.824  1.00 61.61           C  
ANISOU 5717  CG  LYS A 696     7740   9087   6581   1251   -694    456       C  
ATOM   5718  CD  LYS A 696      29.030 -40.017  55.072  1.00 66.95           C  
ANISOU 5718  CD  LYS A 696     8436   9772   7229   1381   -729    439       C  
ATOM   5719  CE  LYS A 696      28.122 -41.151  54.562  1.00 69.49           C  
ANISOU 5719  CE  LYS A 696     8864   9936   7603   1423   -764    451       C  
ATOM   5720  NZ  LYS A 696      28.912 -42.300  54.023  1.00 71.97           N  
ANISOU 5720  NZ  LYS A 696     9207  10254   7885   1563   -806    434       N  
ATOM   5721  N   GLY A 697      24.191 -36.500  54.402  1.00 47.90           N  
ANISOU 5721  N   GLY A 697     6076   7082   5043    914   -611    445       N  
ATOM   5722  CA  GLY A 697      23.533 -35.336  53.818  1.00 49.08           C  
ANISOU 5722  CA  GLY A 697     6206   7220   5222    823   -577    424       C  
ATOM   5723  C   GLY A 697      23.490 -34.153  54.768  1.00 48.82           C  
ANISOU 5723  C   GLY A 697     6122   7248   5180    733   -543    431       C  
ATOM   5724  O   GLY A 697      23.387 -34.328  55.985  1.00 52.08           O  
ANISOU 5724  O   GLY A 697     6539   7668   5583    723   -547    461       O  
ATOM   5725  N   ILE A 698      23.572 -32.945  54.219  1.00 46.42           N  
ANISOU 5725  N   ILE A 698     5772   6988   4878    671   -511    404       N  
ATOM   5726  CA  ILE A 698      23.595 -31.733  55.054  1.00 44.67           C  
ANISOU 5726  CA  ILE A 698     5499   6823   4649    585   -483    401       C  
ATOM   5727  C   ILE A 698      22.203 -31.136  55.344  1.00 43.20           C  
ANISOU 5727  C   ILE A 698     5348   6553   4511    499   -466    412       C  
ATOM   5728  O   ILE A 698      22.087 -30.179  56.108  1.00 41.66           O  
ANISOU 5728  O   ILE A 698     5122   6394   4312    432   -447    408       O  
ATOM   5729  CB  ILE A 698      24.533 -30.638  54.468  1.00 43.02           C  
ANISOU 5729  CB  ILE A 698     5213   6712   4420    555   -455    369       C  
ATOM   5730  CG1 ILE A 698      23.983 -30.121  53.134  1.00 39.18           C  
ANISOU 5730  CG1 ILE A 698     4745   6176   3964    527   -432    355       C  
ATOM   5731  CG2 ILE A 698      25.946 -31.175  54.345  1.00 43.79           C  
ANISOU 5731  CG2 ILE A 698     5262   6909   4468    637   -468    360       C  
ATOM   5732  CD1 ILE A 698      24.731 -28.943  52.546  1.00 37.93           C  
ANISOU 5732  CD1 ILE A 698     4517   6100   3796    485   -395    335       C  
ATOM   5733  N   GLY A 699      21.159 -31.680  54.717  1.00 42.65           N  
ANISOU 5733  N   GLY A 699     5342   6376   4488    504   -476    420       N  
ATOM   5734  CA  GLY A 699      19.788 -31.235  54.977  1.00 41.13           C  
ANISOU 5734  CA  GLY A 699     5181   6103   4343    430   -462    432       C  
ATOM   5735  C   GLY A 699      19.349 -30.014  54.185  1.00 40.94           C  
ANISOU 5735  C   GLY A 699     5143   6074   4340    364   -434    403       C  
ATOM   5736  O   GLY A 699      18.338 -30.054  53.477  1.00 41.68           O  
ANISOU 5736  O   GLY A 699     5276   6083   4477    348   -437    398       O  
ATOM   5737  N   GLY A 700      20.099 -28.921  54.308  1.00 40.68           N  
ANISOU 5737  N   GLY A 700     5051   6127   4279    327   -410    384       N  
ATOM   5738  CA  GLY A 700      19.766 -27.679  53.615  1.00 39.07           C  
ANISOU 5738  CA  GLY A 700     4832   5919   4093    263   -380    362       C  
ATOM   5739  C   GLY A 700      20.886 -26.661  53.608  1.00 39.94           C  
ANISOU 5739  C   GLY A 700     4872   6128   4174    234   -356    342       C  
ATOM   5740  O   GLY A 700      21.930 -26.867  54.245  1.00 39.97           O  
ANISOU 5740  O   GLY A 700     4832   6213   4143    259   -365    342       O  
ATOM   5741  N   PHE A 701      20.678 -25.567  52.877  1.00 38.57           N  
ANISOU 5741  N   PHE A 701     4688   5947   4018    181   -327    328       N  
ATOM   5742  CA  PHE A 701      21.664 -24.484  52.811  1.00 38.92           C  
ANISOU 5742  CA  PHE A 701     4665   6074   4050    139   -300    313       C  
ATOM   5743  C   PHE A 701      21.088 -23.170  52.285  1.00 37.84           C  
ANISOU 5743  C   PHE A 701     4532   5902   3944     64   -268    304       C  
ATOM   5744  O   PHE A 701      20.095 -23.163  51.571  1.00 38.18           O  
ANISOU 5744  O   PHE A 701     4627   5869   4010     64   -264    307       O  
ATOM   5745  CB  PHE A 701      22.916 -24.901  51.999  1.00 39.61           C  
ANISOU 5745  CB  PHE A 701     4710   6234   4106    200   -295    312       C  
ATOM   5746  CG  PHE A 701      22.708 -24.945  50.491  1.00 37.21           C  
ANISOU 5746  CG  PHE A 701     4433   5898   3806    233   -278    315       C  
ATOM   5747  CD1 PHE A 701      22.463 -26.142  49.851  1.00 34.66           C  
ANISOU 5747  CD1 PHE A 701     4160   5537   3474    318   -304    318       C  
ATOM   5748  CD2 PHE A 701      22.800 -23.785  49.720  1.00 36.33           C  
ANISOU 5748  CD2 PHE A 701     4300   5798   3706    183   -237    314       C  
ATOM   5749  CE1 PHE A 701      22.283 -26.189  48.461  1.00 38.01           C  
ANISOU 5749  CE1 PHE A 701     4611   5937   3893    359   -293    314       C  
ATOM   5750  CE2 PHE A 701      22.626 -23.821  48.346  1.00 36.09           C  
ANISOU 5750  CE2 PHE A 701     4297   5747   3670    223   -219    318       C  
ATOM   5751  CZ  PHE A 701      22.366 -25.031  47.711  1.00 35.03           C  
ANISOU 5751  CZ  PHE A 701     4212   5578   3520    314   -249    316       C  
ATOM   5752  N   TRP A 702      21.732 -22.067  52.657  1.00 38.43           N  
ANISOU 5752  N   TRP A 702     4550   6031   4021      2   -248    290       N  
ATOM   5753  CA  TRP A 702      21.437 -20.740  52.123  1.00 37.29           C  
ANISOU 5753  CA  TRP A 702     4401   5861   3905    -68   -215    284       C  
ATOM   5754  C   TRP A 702      22.699 -20.173  51.481  1.00 37.07           C  
ANISOU 5754  C   TRP A 702     4306   5907   3871    -80   -185    286       C  
ATOM   5755  O   TRP A 702      23.792 -20.351  52.025  1.00 38.02           O  
ANISOU 5755  O   TRP A 702     4363   6110   3973    -71   -195    279       O  
ATOM   5756  CB  TRP A 702      20.998 -19.798  53.241  1.00 36.36           C  
ANISOU 5756  CB  TRP A 702     4278   5729   3806   -142   -219    265       C  
ATOM   5757  CG  TRP A 702      19.512 -19.682  53.433  1.00 35.91           C  
ANISOU 5757  CG  TRP A 702     4288   5585   3772   -160   -223    265       C  
ATOM   5758  CD1 TRP A 702      18.720 -18.640  53.046  1.00 34.86           C  
ANISOU 5758  CD1 TRP A 702     4182   5396   3669   -212   -203    258       C  
ATOM   5759  CD2 TRP A 702      18.647 -20.626  54.076  1.00 34.86           C  
ANISOU 5759  CD2 TRP A 702     4198   5412   3634   -126   -248    275       C  
ATOM   5760  NE1 TRP A 702      17.421 -18.877  53.393  1.00 34.35           N  
ANISOU 5760  NE1 TRP A 702     4171   5265   3617   -210   -215    260       N  
ATOM   5761  CE2 TRP A 702      17.342 -20.088  54.033  1.00 36.15           C  
ANISOU 5761  CE2 TRP A 702     4407   5500   3826   -161   -241    272       C  
ATOM   5762  CE3 TRP A 702      18.847 -21.874  54.685  1.00 36.21           C  
ANISOU 5762  CE3 TRP A 702     4374   5602   3781    -68   -275    291       C  
ATOM   5763  CZ2 TRP A 702      16.231 -20.755  54.574  1.00 34.98           C  
ANISOU 5763  CZ2 TRP A 702     4303   5301   3689   -146   -256    285       C  
ATOM   5764  CZ3 TRP A 702      17.749 -22.537  55.229  1.00 39.95           C  
ANISOU 5764  CZ3 TRP A 702     4896   6017   4266    -54   -289    307       C  
ATOM   5765  CH2 TRP A 702      16.453 -21.970  55.170  1.00 40.40           C  
ANISOU 5765  CH2 TRP A 702     4990   6003   4355    -95   -278    305       C  
ATOM   5766  N   THR A 703      22.549 -19.507  50.333  1.00 33.93           N  
ANISOU 5766  N   THR A 703     3919   5485   3489    -96   -149    298       N  
ATOM   5767  CA  THR A 703      23.650 -18.727  49.745  1.00 33.97           C  
ANISOU 5767  CA  THR A 703     3857   5554   3498   -126   -109    308       C  
ATOM   5768  C   THR A 703      23.507 -17.234  50.056  1.00 33.18           C  
ANISOU 5768  C   THR A 703     3738   5427   3440   -229    -87    300       C  
ATOM   5769  O   THR A 703      24.489 -16.497  50.030  1.00 38.54           O  
ANISOU 5769  O   THR A 703     4347   6160   4135   -276    -64    302       O  
ATOM   5770  CB  THR A 703      23.785 -18.904  48.201  1.00 32.33           C  
ANISOU 5770  CB  THR A 703     3665   5348   3273    -73    -74    336       C  
ATOM   5771  OG1 THR A 703      22.819 -18.083  47.521  1.00 37.24           O  
ANISOU 5771  OG1 THR A 703     4340   5892   3918   -107    -50    345       O  
ATOM   5772  CG2 THR A 703      23.602 -20.345  47.791  1.00 30.81           C  
ANISOU 5772  CG2 THR A 703     3513   5151   3043     32   -104    337       C  
ATOM   5773  N   GLY A 704      22.286 -16.800  50.345  1.00 30.77           N  
ANISOU 5773  N   GLY A 704     3495   5039   3156   -261    -97    289       N  
ATOM   5774  CA  GLY A 704      21.975 -15.384  50.568  1.00 32.16           C  
ANISOU 5774  CA  GLY A 704     3672   5176   3374   -349    -79    278       C  
ATOM   5775  C   GLY A 704      20.468 -15.183  50.568  1.00 34.83           C  
ANISOU 5775  C   GLY A 704     4090   5419   3723   -354    -87    272       C  
ATOM   5776  O   GLY A 704      19.705 -16.166  50.611  1.00 35.64           O  
ANISOU 5776  O   GLY A 704     4240   5493   3808   -298   -111    273       O  
ATOM   5777  N   LYS A 705      20.031 -13.924  50.534  1.00 33.65           N  
ANISOU 5777  N   LYS A 705     3956   5219   3608   -420    -69    265       N  
ATOM   5778  CA  LYS A 705      18.598 -13.612  50.508  1.00 35.62           C  
ANISOU 5778  CA  LYS A 705     4280   5384   3871   -424    -75    258       C  
ATOM   5779  C   LYS A 705      17.919 -14.256  49.295  1.00 36.74           C  
ANISOU 5779  C   LYS A 705     4474   5488   3997   -359    -66    282       C  
ATOM   5780  O   LYS A 705      18.435 -14.191  48.176  1.00 35.88           O  
ANISOU 5780  O   LYS A 705     4358   5396   3878   -336    -35    308       O  
ATOM   5781  CB  LYS A 705      18.349 -12.095  50.480  1.00 36.80           C  
ANISOU 5781  CB  LYS A 705     4438   5485   4059   -499    -54    249       C  
ATOM   5782  CG  LYS A 705      18.817 -11.323  51.690  1.00 36.64           C  
ANISOU 5782  CG  LYS A 705     4376   5484   4061   -566    -72    213       C  
ATOM   5783  CD  LYS A 705      18.515  -9.843  51.520  1.00 35.77           C  
ANISOU 5783  CD  LYS A 705     4285   5312   3994   -635    -52    206       C  
ATOM   5784  CE  LYS A 705      18.786  -9.063  52.812  1.00 36.77           C  
ANISOU 5784  CE  LYS A 705     4381   5445   4143   -697    -81    157       C  
ATOM   5785  NZ  LYS A 705      18.320  -7.641  52.746  1.00 32.26           N  
ANISOU 5785  NZ  LYS A 705     3842   4799   3617   -759    -70    142       N  
ATOM   5786  N   LYS A 706      16.764 -14.881  49.532  1.00 38.03           N  
ANISOU 5786  N   LYS A 706     4689   5604   4158   -326    -93    272       N  
ATOM   5787  CA  LYS A 706      15.922 -15.436  48.463  1.00 38.40           C  
ANISOU 5787  CA  LYS A 706     4790   5604   4197   -268    -95    283       C  
ATOM   5788  C   LYS A 706      16.590 -16.577  47.672  1.00 39.05           C  
ANISOU 5788  C   LYS A 706     4863   5727   4248   -193   -100    299       C  
ATOM   5789  O   LYS A 706      16.205 -16.859  46.533  1.00 41.89           O  
ANISOU 5789  O   LYS A 706     5259   6061   4596   -141    -96    307       O  
ATOM   5790  CB  LYS A 706      15.422 -14.312  47.528  1.00 36.90           C  
ANISOU 5790  CB  LYS A 706     4635   5365   4022   -289    -64    292       C  
ATOM   5791  CG  LYS A 706      14.580 -13.244  48.246  1.00 36.38           C  
ANISOU 5791  CG  LYS A 706     4590   5246   3985   -350    -66    272       C  
ATOM   5792  CD  LYS A 706      13.964 -12.254  47.279  1.00 35.28           C  
ANISOU 5792  CD  LYS A 706     4496   5052   3859   -357    -40    283       C  
ATOM   5793  CE  LYS A 706      13.118 -11.200  48.011  1.00 40.89           C  
ANISOU 5793  CE  LYS A 706     5231   5710   4598   -410    -44    259       C  
ATOM   5794  NZ  LYS A 706      11.786 -11.698  48.489  1.00 41.50           N  
ANISOU 5794  NZ  LYS A 706     5343   5748   4678   -386    -77    237       N  
ATOM   5795  N   ARG A 707      17.583 -17.225  48.280  1.00 40.40           N  
ANISOU 5795  N   ARG A 707     4613   5602   5133   -229    135    554       N  
ATOM   5796  CA  ARG A 707      18.332 -18.291  47.619  1.00 40.81           C  
ANISOU 5796  CA  ARG A 707     4655   5717   5134   -225     76    519       C  
ATOM   5797  C   ARG A 707      18.695 -19.424  48.578  1.00 41.73           C  
ANISOU 5797  C   ARG A 707     4777   5858   5219   -195     38    469       C  
ATOM   5798  O   ARG A 707      19.649 -19.306  49.354  1.00 42.76           O  
ANISOU 5798  O   ARG A 707     4907   6014   5326   -199     47    404       O  
ATOM   5799  CB  ARG A 707      19.608 -17.728  46.990  1.00 43.20           C  
ANISOU 5799  CB  ARG A 707     4947   6061   5406   -262     91    465       C  
ATOM   5800  CG  ARG A 707      19.406 -17.041  45.650  1.00 44.78           C  
ANISOU 5800  CG  ARG A 707     5143   6256   5616   -296    104    514       C  
ATOM   5801  CD  ARG A 707      20.713 -16.461  45.112  1.00 46.50           C  
ANISOU 5801  CD  ARG A 707     5354   6516   5800   -339    125    454       C  
ATOM   5802  NE  ARG A 707      21.664 -17.496  44.701  1.00 48.79           N  
ANISOU 5802  NE  ARG A 707     5626   6872   6039   -337     80    391       N  
ATOM   5803  CZ  ARG A 707      21.675 -18.077  43.504  1.00 50.27           C  
ANISOU 5803  CZ  ARG A 707     5806   7091   6204   -352     48    404       C  
ATOM   5804  NH1 ARG A 707      20.784 -17.727  42.575  1.00 52.74           N  
ANISOU 5804  NH1 ARG A 707     6127   7380   6533   -372     47    484       N  
ATOM   5805  NH2 ARG A 707      22.572 -19.017  43.236  1.00 46.44           N  
ANISOU 5805  NH2 ARG A 707     5304   6661   5681   -347     16    338       N  
ATOM   5806  N   TYR A 708      17.952 -20.528  48.512  1.00 40.88           N  
ANISOU 5806  N   TYR A 708     4675   5746   5110   -166     -7    502       N  
ATOM   5807  CA  TYR A 708      18.186 -21.647  49.423  1.00 40.43           C  
ANISOU 5807  CA  TYR A 708     4630   5704   5027   -135    -45    466       C  
ATOM   5808  C   TYR A 708      17.602 -22.976  48.958  1.00 41.58           C  
ANISOU 5808  C   TYR A 708     4783   5853   5162   -111    -98    493       C  
ATOM   5809  O   TYR A 708      16.801 -23.027  48.014  1.00 44.07           O  
ANISOU 5809  O   TYR A 708     5094   6159   5492   -121   -104    548       O  
ATOM   5810  CB  TYR A 708      17.658 -21.317  50.822  1.00 39.77           C  
ANISOU 5810  CB  TYR A 708     4566   5583   4963   -128    -16    470       C  
ATOM   5811  CG  TYR A 708      16.177 -21.045  50.893  1.00 38.25           C  
ANISOU 5811  CG  TYR A 708     4381   5336   4817   -125      8    541       C  
ATOM   5812  CD1 TYR A 708      15.669 -19.770  50.630  1.00 39.92           C  
ANISOU 5812  CD1 TYR A 708     4584   5508   5075   -145     65    578       C  
ATOM   5813  CD2 TYR A 708      15.285 -22.052  51.241  1.00 34.07           C  
ANISOU 5813  CD2 TYR A 708     3867   4791   4288   -102    -24    571       C  
ATOM   5814  CE1 TYR A 708      14.304 -19.512  50.695  1.00 40.00           C  
ANISOU 5814  CE1 TYR A 708     4593   5469   5137   -136     87    645       C  
ATOM   5815  CE2 TYR A 708      13.921 -21.805  51.316  1.00 36.72           C  
ANISOU 5815  CE2 TYR A 708     4202   5081   4668   -100     -1    634       C  
ATOM   5816  CZ  TYR A 708      13.437 -20.537  51.042  1.00 39.56           C  
ANISOU 5816  CZ  TYR A 708     4546   5406   5079   -114     53    671       C  
ATOM   5817  OH  TYR A 708      12.086 -20.296  51.108  1.00 40.22           O  
ANISOU 5817  OH  TYR A 708     4622   5446   5214   -107     76    735       O  
ATOM   5818  N   ALA A 709      18.013 -24.046  49.636  1.00 38.53           N  
ANISOU 5818  N   ALA A 709     4409   5482   4750    -82   -136    457       N  
ATOM   5819  CA  ALA A 709      17.519 -25.389  49.360  1.00 38.85           C  
ANISOU 5819  CA  ALA A 709     4464   5520   4779    -59   -182    476       C  
ATOM   5820  C   ALA A 709      17.285 -26.152  50.661  1.00 38.03           C  
ANISOU 5820  C   ALA A 709     4387   5397   4666    -30   -203    470       C  
ATOM   5821  O   ALA A 709      18.082 -26.068  51.596  1.00 34.24           O  
ANISOU 5821  O   ALA A 709     3909   4931   4170    -20   -205    427       O  
ATOM   5822  CB  ALA A 709      18.490 -26.150  48.465  1.00 39.48           C  
ANISOU 5822  CB  ALA A 709     4529   5641   4830    -53   -214    432       C  
ATOM   5823  N   LEU A 710      16.184 -26.892  50.708  1.00 36.00           N  
ANISOU 5823  N   LEU A 710     4153   5111   4416    -21   -219    514       N  
ATOM   5824  CA  LEU A 710      15.840 -27.677  51.876  1.00 37.86           C  
ANISOU 5824  CA  LEU A 710     4421   5324   4639      0   -239    515       C  
ATOM   5825  C   LEU A 710      15.352 -29.046  51.449  1.00 39.00           C  
ANISOU 5825  C   LEU A 710     4587   5460   4770     16   -280    533       C  
ATOM   5826  O   LEU A 710      14.651 -29.183  50.439  1.00 40.30           O  
ANISOU 5826  O   LEU A 710     4746   5623   4945      0   -280    568       O  
ATOM   5827  CB  LEU A 710      14.755 -26.980  52.707  1.00 37.23           C  
ANISOU 5827  CB  LEU A 710     4353   5206   4586    -15   -199    553       C  
ATOM   5828  CG  LEU A 710      15.068 -25.664  53.427  1.00 37.85           C  
ANISOU 5828  CG  LEU A 710     4422   5280   4681    -35   -148    534       C  
ATOM   5829  CD1 LEU A 710      13.774 -25.062  54.003  1.00 39.11           C  
ANISOU 5829  CD1 LEU A 710     4590   5393   4878    -50   -102    577       C  
ATOM   5830  CD2 LEU A 710      16.110 -25.855  54.531  1.00 31.82           C  
ANISOU 5830  CD2 LEU A 710     3670   4539   3881    -28   -163    479       C  
ATOM   5831  N   ASN A 711      15.743 -30.058  52.215  1.00 39.46           N  
ANISOU 5831  N   ASN A 711     4673   5514   4805     45   -315    510       N  
ATOM   5832  CA  ASN A 711      15.218 -31.400  52.049  1.00 39.25           C  
ANISOU 5832  CA  ASN A 711     4679   5467   4766     60   -348    526       C  
ATOM   5833  C   ASN A 711      14.043 -31.574  52.999  1.00 39.49           C  
ANISOU 5833  C   ASN A 711     4744   5460   4799     51   -340    566       C  
ATOM   5834  O   ASN A 711      14.237 -31.752  54.209  1.00 39.76           O  
ANISOU 5834  O   ASN A 711     4804   5485   4819     63   -349    555       O  
ATOM   5835  CB  ASN A 711      16.298 -32.438  52.344  1.00 39.92           C  
ANISOU 5835  CB  ASN A 711     4778   5562   4830    100   -391    483       C  
ATOM   5836  CG  ASN A 711      15.877 -33.830  51.954  1.00 38.32           C  
ANISOU 5836  CG  ASN A 711     4608   5334   4617    114   -420    494       C  
ATOM   5837  OD1 ASN A 711      15.463 -34.063  50.821  1.00 42.17           O  
ANISOU 5837  OD1 ASN A 711     5090   5825   5108     94   -413    505       O  
ATOM   5838  ND2 ASN A 711      15.990 -34.766  52.883  1.00 37.09           N  
ANISOU 5838  ND2 ASN A 711     4492   5154   4447    144   -451    492       N  
ATOM   5839  N   VAL A 712      12.835 -31.522  52.440  1.00 38.01           N  
ANISOU 5839  N   VAL A 712     4556   5259   4629     27   -325    612       N  
ATOM   5840  CA  VAL A 712      11.606 -31.425  53.221  1.00 38.02           C  
ANISOU 5840  CA  VAL A 712     4576   5228   4642     11   -304    651       C  
ATOM   5841  C   VAL A 712      10.886 -32.765  53.296  1.00 39.68           C  
ANISOU 5841  C   VAL A 712     4829   5417   4832     12   -333    669       C  
ATOM   5842  O   VAL A 712      10.716 -33.443  52.282  1.00 41.86           O  
ANISOU 5842  O   VAL A 712     5104   5700   5099      7   -351    676       O  
ATOM   5843  CB  VAL A 712      10.648 -30.337  52.635  1.00 37.98           C  
ANISOU 5843  CB  VAL A 712     4533   5220   4677    -16   -263    695       C  
ATOM   5844  CG1 VAL A 712       9.362 -30.260  53.422  1.00 35.80           C  
ANISOU 5844  CG1 VAL A 712     4270   4912   4419    -31   -238    731       C  
ATOM   5845  CG2 VAL A 712      11.325 -28.981  52.615  1.00 34.93           C  
ANISOU 5845  CG2 VAL A 712     4113   4845   4313    -20   -229    679       C  
ATOM   5846  N   TRP A 713      10.459 -33.123  54.506  1.00 40.75           N  
ANISOU 5846  N   TRP A 713     5003   5526   4955     12   -332    673       N  
ATOM   5847  CA  TRP A 713       9.756 -34.373  54.778  1.00 42.58           C  
ANISOU 5847  CA  TRP A 713     5283   5732   5164      8   -355    690       C  
ATOM   5848  C   TRP A 713       8.255 -34.154  55.026  1.00 43.90           C  
ANISOU 5848  C   TRP A 713     5451   5881   5349    -26   -324    732       C  
ATOM   5849  O   TRP A 713       7.443 -35.076  54.883  1.00 43.77           O  
ANISOU 5849  O   TRP A 713     5464   5850   5318    -41   -335    752       O  
ATOM   5850  CB  TRP A 713      10.396 -35.082  55.978  1.00 42.19           C  
ANISOU 5850  CB  TRP A 713     5283   5666   5082     31   -384    666       C  
ATOM   5851  CG  TRP A 713      11.847 -35.398  55.756  1.00 43.73           C  
ANISOU 5851  CG  TRP A 713     5471   5880   5265     70   -418    627       C  
ATOM   5852  CD1 TRP A 713      12.911 -34.566  55.977  1.00 44.12           C  
ANISOU 5852  CD1 TRP A 713     5488   5959   5319     83   -415    596       C  
ATOM   5853  CD2 TRP A 713      12.394 -36.619  55.245  1.00 42.57           C  
ANISOU 5853  CD2 TRP A 713     5347   5724   5104     99   -457    612       C  
ATOM   5854  NE1 TRP A 713      14.083 -35.196  55.644  1.00 42.43           N  
ANISOU 5854  NE1 TRP A 713     5269   5759   5094    121   -452    564       N  
ATOM   5855  CE2 TRP A 713      13.797 -36.456  55.186  1.00 42.07           C  
ANISOU 5855  CE2 TRP A 713     5256   5687   5040    134   -477    572       C  
ATOM   5856  CE3 TRP A 713      11.835 -37.837  54.828  1.00 45.37           C  
ANISOU 5856  CE3 TRP A 713     5741   6049   5447     97   -473    625       C  
ATOM   5857  CZ2 TRP A 713      14.656 -37.468  54.733  1.00 41.50           C  
ANISOU 5857  CZ2 TRP A 713     5193   5611   4965    174   -511    546       C  
ATOM   5858  CZ3 TRP A 713      12.692 -38.845  54.370  1.00 45.48           C  
ANISOU 5858  CZ3 TRP A 713     5770   6055   5455    134   -505    598       C  
ATOM   5859  CH2 TRP A 713      14.087 -38.648  54.325  1.00 41.48           C  
ANISOU 5859  CH2 TRP A 713     5232   5572   4955    174   -523    559       C  
ATOM   5860  N   ASP A 714       7.896 -32.931  55.407  1.00 44.17           N  
ANISOU 5860  N   ASP A 714     5453   5914   5415    -39   -280    743       N  
ATOM   5861  CA  ASP A 714       6.509 -32.585  55.654  1.00 43.30           C  
ANISOU 5861  CA  ASP A 714     5331   5788   5333    -67   -244    780       C  
ATOM   5862  C   ASP A 714       6.261 -31.127  55.291  1.00 43.74           C  
ANISOU 5862  C   ASP A 714     5328   5850   5442    -72   -198    799       C  
ATOM   5863  O   ASP A 714       6.947 -30.230  55.794  1.00 42.32           O  
ANISOU 5863  O   ASP A 714     5139   5668   5274    -66   -173    773       O  
ATOM   5864  CB  ASP A 714       6.136 -32.859  57.115  1.00 42.94           C  
ANISOU 5864  CB  ASP A 714     5331   5715   5269    -80   -230    770       C  
ATOM   5865  CG  ASP A 714       4.630 -32.918  57.336  1.00 45.08           C  
ANISOU 5865  CG  ASP A 714     5600   5969   5561   -111   -199    805       C  
ATOM   5866  OD1 ASP A 714       3.983 -31.847  57.337  1.00 40.54           O  
ANISOU 5866  OD1 ASP A 714     4978   5390   5035   -122   -150    823       O  
ATOM   5867  OD2 ASP A 714       4.096 -34.039  57.522  1.00 47.44           O  
ANISOU 5867  OD2 ASP A 714     5940   6256   5827   -125   -221    813       O  
ATOM   5868  N   MET A 715       5.286 -30.904  54.406  1.00 44.45           N  
ANISOU 5868  N   MET A 715     5380   5947   5564    -86   -188    845       N  
ATOM   5869  CA  MET A 715       4.922 -29.559  53.967  1.00 45.36           C  
ANISOU 5869  CA  MET A 715     5437   6061   5736    -88   -148    876       C  
ATOM   5870  C   MET A 715       3.474 -29.216  54.292  1.00 44.52           C  
ANISOU 5870  C   MET A 715     5305   5935   5676   -104   -109    918       C  
ATOM   5871  O   MET A 715       2.550 -29.739  53.671  1.00 45.85           O  
ANISOU 5871  O   MET A 715     5457   6117   5846   -119   -127    958       O  
ATOM   5872  CB  MET A 715       5.181 -29.392  52.470  1.00 46.56           C  
ANISOU 5872  CB  MET A 715     5553   6246   5893    -88   -172    901       C  
ATOM   5873  CG  MET A 715       5.021 -27.967  51.963  1.00 51.17           C  
ANISOU 5873  CG  MET A 715     6081   6827   6533    -87   -136    935       C  
ATOM   5874  SD  MET A 715       6.254 -26.838  52.652  1.00 57.31           S  
ANISOU 5874  SD  MET A 715     6864   7590   7323    -72    -97    884       S  
ATOM   5875  CE  MET A 715       5.878 -25.342  51.746  1.00 58.94           C  
ANISOU 5875  CE  MET A 715     7009   7789   7597    -73    -59    938       C  
ATOM   5876  N   GLU A 716       3.305 -28.313  55.255  1.00 45.09           N  
ANISOU 5876  N   GLU A 716     5370   5978   5785   -104    -54    906       N  
ATOM   5877  CA  GLU A 716       1.999 -27.874  55.801  1.00 46.10           C  
ANISOU 5877  CA  GLU A 716     5472   6079   5964   -117     -4    934       C  
ATOM   5878  C   GLU A 716       0.942 -28.973  56.026  1.00 43.21           C  
ANISOU 5878  C   GLU A 716     5125   5717   5577   -139    -20    951       C  
ATOM   5879  O   GLU A 716      -0.246 -28.792  55.749  1.00 41.54           O  
ANISOU 5879  O   GLU A 716     4870   5505   5409   -148     -1    995       O  
ATOM   5880  CB  GLU A 716       1.436 -26.650  55.045  1.00 46.73           C  
ANISOU 5880  CB  GLU A 716     5481   6153   6122   -106     32    985       C  
ATOM   5881  CG  GLU A 716       1.183 -26.831  53.557  1.00 53.29           C  
ANISOU 5881  CG  GLU A 716     6272   7020   6955   -104    -14   1040       C  
ATOM   5882  CD  GLU A 716       1.106 -25.506  52.786  1.00 60.05           C  
ANISOU 5882  CD  GLU A 716     7069   7869   7878    -89     13   1085       C  
ATOM   5883  OE1 GLU A 716       1.606 -25.466  51.635  1.00 58.77           O  
ANISOU 5883  OE1 GLU A 716     6892   7738   7698    -88    -26   1107       O  
ATOM   5884  OE2 GLU A 716       0.548 -24.514  53.321  1.00 62.86           O  
ANISOU 5884  OE2 GLU A 716     7394   8187   8303    -79     74   1099       O  
ATOM   5885  N   GLY A 717       1.396 -30.108  56.545  1.00 41.05           N  
ANISOU 5885  N   GLY A 717     4916   5446   5237   -147    -56    917       N  
ATOM   5886  CA  GLY A 717       0.498 -31.203  56.891  1.00 42.38           C  
ANISOU 5886  CA  GLY A 717     5115   5611   5375   -173    -69    925       C  
ATOM   5887  C   GLY A 717       0.584 -32.395  55.967  1.00 41.35           C  
ANISOU 5887  C   GLY A 717     5007   5507   5199   -178   -129    937       C  
ATOM   5888  O   GLY A 717       0.003 -33.441  56.245  1.00 42.77           O  
ANISOU 5888  O   GLY A 717     5225   5682   5343   -202   -144    937       O  
ATOM   5889  N   THR A 718       1.300 -32.234  54.861  1.00 39.80           N  
ANISOU 5889  N   THR A 718     4787   5334   4999   -160   -159    943       N  
ATOM   5890  CA  THR A 718       1.507 -33.328  53.934  1.00 40.24           C  
ANISOU 5890  CA  THR A 718     4865   5413   5010   -168   -210    946       C  
ATOM   5891  C   THR A 718       2.803 -34.027  54.311  1.00 40.34           C  
ANISOU 5891  C   THR A 718     4937   5415   4975   -146   -241    895       C  
ATOM   5892  O   THR A 718       3.884 -33.443  54.219  1.00 41.86           O  
ANISOU 5892  O   THR A 718     5118   5613   5172   -120   -243    871       O  
ATOM   5893  CB  THR A 718       1.562 -32.844  52.456  1.00 40.98           C  
ANISOU 5893  CB  THR A 718     4903   5545   5124   -169   -225    980       C  
ATOM   5894  OG1 THR A 718       0.307 -32.260  52.078  1.00 39.61           O  
ANISOU 5894  OG1 THR A 718     4669   5384   4996   -187   -204   1036       O  
ATOM   5895  CG2 THR A 718       1.863 -34.007  51.520  1.00 41.66           C  
ANISOU 5895  CG2 THR A 718     5017   5654   5158   -184   -271    972       C  
ATOM   5896  N   ARG A 719       2.681 -35.266  54.763  1.00 40.34           N  
ANISOU 5896  N   ARG A 719     4998   5399   4930   -156   -264    881       N  
ATOM   5897  CA  ARG A 719       3.835 -36.120  54.987  1.00 42.56           C  
ANISOU 5897  CA  ARG A 719     5334   5669   5169   -132   -300    842       C  
ATOM   5898  C   ARG A 719       4.176 -36.855  53.699  1.00 43.47           C  
ANISOU 5898  C   ARG A 719     5450   5803   5265   -132   -333    839       C  
ATOM   5899  O   ARG A 719       3.435 -37.745  53.269  1.00 44.93           O  
ANISOU 5899  O   ARG A 719     5655   5987   5428   -161   -343    854       O  
ATOM   5900  CB  ARG A 719       3.552 -37.127  56.105  1.00 41.45           C  
ANISOU 5900  CB  ARG A 719     5265   5494   4990   -143   -309    831       C  
ATOM   5901  CG  ARG A 719       4.784 -37.894  56.575  1.00 43.41           C  
ANISOU 5901  CG  ARG A 719     5569   5725   5202   -109   -347    797       C  
ATOM   5902  CD  ARG A 719       5.825 -36.975  57.211  1.00 45.48           C  
ANISOU 5902  CD  ARG A 719     5813   5995   5474    -80   -342    772       C  
ATOM   5903  NE  ARG A 719       5.306 -36.294  58.399  1.00 49.58           N  
ANISOU 5903  NE  ARG A 719     6336   6501   6000   -103   -305    775       N  
ATOM   5904  CZ  ARG A 719       5.271 -36.829  59.619  1.00 51.57           C  
ANISOU 5904  CZ  ARG A 719     6647   6730   6216   -114   -312    767       C  
ATOM   5905  NH1 ARG A 719       5.725 -38.061  59.828  1.00 51.16           N  
ANISOU 5905  NH1 ARG A 719     6656   6659   6122    -99   -358    762       N  
ATOM   5906  NH2 ARG A 719       4.784 -36.129  60.636  1.00 51.67           N  
ANISOU 5906  NH2 ARG A 719     6661   6736   6236   -143   -271    764       N  
ATOM   5907  N   TYR A 720       5.294 -36.487  53.084  1.00 41.82           N  
ANISOU 5907  N   TYR A 720     5218   5612   5061   -105   -346    817       N  
ATOM   5908  CA  TYR A 720       5.677 -37.094  51.816  1.00 42.87           C  
ANISOU 5908  CA  TYR A 720     5347   5765   5175   -110   -370    808       C  
ATOM   5909  C   TYR A 720       6.112 -38.529  52.026  1.00 43.53           C  
ANISOU 5909  C   TYR A 720     5498   5820   5222    -98   -398    778       C  
ATOM   5910  O   TYR A 720       6.687 -38.860  53.062  1.00 45.61           O  
ANISOU 5910  O   TYR A 720     5801   6055   5474    -68   -409    757       O  
ATOM   5911  CB  TYR A 720       6.834 -36.334  51.172  1.00 42.55           C  
ANISOU 5911  CB  TYR A 720     5268   5751   5149    -86   -373    785       C  
ATOM   5912  CG  TYR A 720       6.577 -34.881  50.866  1.00 40.13           C  
ANISOU 5912  CG  TYR A 720     4899   5466   4881    -95   -345    813       C  
ATOM   5913  CD1 TYR A 720       5.524 -34.496  50.041  1.00 43.79           C  
ANISOU 5913  CD1 TYR A 720     5322   5952   5362   -129   -335    863       C  
ATOM   5914  CD2 TYR A 720       7.422 -33.889  51.365  1.00 42.67           C  
ANISOU 5914  CD2 TYR A 720     5201   5789   5223    -69   -329    792       C  
ATOM   5915  CE1 TYR A 720       5.295 -33.158  49.745  1.00 41.92           C  
ANISOU 5915  CE1 TYR A 720     5030   5731   5168   -132   -310    896       C  
ATOM   5916  CE2 TYR A 720       7.209 -32.546  51.067  1.00 42.84           C  
ANISOU 5916  CE2 TYR A 720     5171   5823   5284    -76   -299    818       C  
ATOM   5917  CZ  TYR A 720       6.138 -32.194  50.256  1.00 42.32           C  
ANISOU 5917  CZ  TYR A 720     5068   5773   5241   -105   -290    872       C  
ATOM   5918  OH  TYR A 720       5.912 -30.874  49.955  1.00 50.53           O  
ANISOU 5918  OH  TYR A 720     6056   6818   6324   -108   -261    904       O  
ATOM   5919  N   ALA A 721       5.841 -39.374  51.039  1.00 43.45           N  
ANISOU 5919  N   ALA A 721     5500   5817   5191   -124   -408    778       N  
ATOM   5920  CA  ALA A 721       6.357 -40.735  51.028  1.00 44.70           C  
ANISOU 5920  CA  ALA A 721     5721   5943   5321   -111   -429    746       C  
ATOM   5921  C   ALA A 721       7.846 -40.723  50.729  1.00 46.04           C  
ANISOU 5921  C   ALA A 721     5881   6115   5496    -64   -444    702       C  
ATOM   5922  O   ALA A 721       8.583 -41.588  51.192  1.00 49.85           O  
ANISOU 5922  O   ALA A 721     6409   6563   5969    -28   -463    673       O  
ATOM   5923  CB  ALA A 721       5.618 -41.587  50.012  1.00 43.95           C  
ANISOU 5923  CB  ALA A 721     5641   5856   5201   -161   -427    754       C  
ATOM   5924  N   GLU A 722       8.277 -39.733  49.953  1.00 46.79           N  
ANISOU 5924  N   GLU A 722     5916   6253   5610    -66   -435    698       N  
ATOM   5925  CA  GLU A 722       9.683 -39.534  49.626  1.00 46.31           C  
ANISOU 5925  CA  GLU A 722     5834   6204   5557    -28   -444    654       C  
ATOM   5926  C   GLU A 722      10.039 -38.062  49.854  1.00 43.55           C  
ANISOU 5926  C   GLU A 722     5431   5885   5233    -18   -430    661       C  
ATOM   5927  O   GLU A 722       9.232 -37.192  49.537  1.00 42.09           O  
ANISOU 5927  O   GLU A 722     5210   5721   5062    -50   -411    699       O  
ATOM   5928  CB  GLU A 722       9.950 -39.940  48.172  1.00 47.72           C  
ANISOU 5928  CB  GLU A 722     6001   6406   5725    -54   -441    632       C  
ATOM   5929  CG  GLU A 722       9.855 -41.453  47.891  1.00 57.19           C  
ANISOU 5929  CG  GLU A 722     7258   7571   6902    -61   -448    610       C  
ATOM   5930  CD  GLU A 722      10.851 -42.302  48.699  1.00 65.12           C  
ANISOU 5930  CD  GLU A 722     8304   8528   7911      2   -467    573       C  
ATOM   5931  OE1 GLU A 722      11.976 -41.822  48.982  1.00 68.38           O  
ANISOU 5931  OE1 GLU A 722     8688   8951   8342     49   -476    545       O  
ATOM   5932  OE2 GLU A 722      10.512 -43.462  49.041  1.00 65.46           O  
ANISOU 5932  OE2 GLU A 722     8408   8523   7940      4   -473    572       O  
ATOM   5933  N   PRO A 723      11.238 -37.774  50.411  1.00 42.84           N  
ANISOU 5933  N   PRO A 723     5332   5794   5149     26   -440    625       N  
ATOM   5934  CA  PRO A 723      11.583 -36.368  50.655  1.00 42.19           C  
ANISOU 5934  CA  PRO A 723     5203   5738   5088     29   -421    627       C  
ATOM   5935  C   PRO A 723      11.563 -35.559  49.360  1.00 44.26           C  
ANISOU 5935  C   PRO A 723     5415   6039   5361     -2   -403    635       C  
ATOM   5936  O   PRO A 723      11.958 -36.054  48.300  1.00 45.79           O  
ANISOU 5936  O   PRO A 723     5604   6250   5543    -12   -410    613       O  
ATOM   5937  CB  PRO A 723      13.007 -36.439  51.213  1.00 40.76           C  
ANISOU 5937  CB  PRO A 723     5021   5562   4905     76   -439    579       C  
ATOM   5938  CG  PRO A 723      13.546 -37.777  50.745  1.00 40.91           C  
ANISOU 5938  CG  PRO A 723     5069   5565   4912     99   -464    549       C  
ATOM   5939  CD  PRO A 723      12.354 -38.681  50.748  1.00 43.54           C  
ANISOU 5939  CD  PRO A 723     5449   5865   5231     73   -466    582       C  
ATOM   5940  N   LYS A 724      11.079 -34.331  49.448  1.00 44.74           N  
ANISOU 5940  N   LYS A 724     5442   6112   5446    -20   -378    667       N  
ATOM   5941  CA  LYS A 724      11.047 -33.444  48.301  1.00 45.22           C  
ANISOU 5941  CA  LYS A 724     5457   6207   5519    -49   -362    684       C  
ATOM   5942  C   LYS A 724      11.995 -32.271  48.550  1.00 43.56           C  
ANISOU 5942  C   LYS A 724     5215   6011   5326    -34   -344    660       C  
ATOM   5943  O   LYS A 724      12.085 -31.743  49.665  1.00 44.58           O  
ANISOU 5943  O   LYS A 724     5348   6122   5467    -16   -330    656       O  
ATOM   5944  CB  LYS A 724       9.605 -32.974  48.033  1.00 47.76           C  
ANISOU 5944  CB  LYS A 724     5761   6528   5859    -84   -347    751       C  
ATOM   5945  CG  LYS A 724       9.451 -31.906  46.938  1.00 57.78           C  
ANISOU 5945  CG  LYS A 724     6981   7829   7145   -113   -333    786       C  
ATOM   5946  CD  LYS A 724       8.005 -31.388  46.824  1.00 64.35           C  
ANISOU 5946  CD  LYS A 724     7788   8659   8005   -138   -321    859       C  
ATOM   5947  CE  LYS A 724       7.939 -29.844  46.837  1.00 68.49           C  
ANISOU 5947  CE  LYS A 724     8268   9180   8574   -135   -289    891       C  
ATOM   5948  NZ  LYS A 724       8.681 -29.161  45.727  1.00 68.16           N  
ANISOU 5948  NZ  LYS A 724     8200   9171   8528   -152   -289    889       N  
ATOM   5949  N   LEU A 725      12.711 -31.877  47.507  1.00 41.33           N  
ANISOU 5949  N   LEU A 725     4904   5761   5039    -47   -341    641       N  
ATOM   5950  CA  LEU A 725      13.585 -30.727  47.581  1.00 41.24           C  
ANISOU 5950  CA  LEU A 725     4863   5767   5041    -43   -319    618       C  
ATOM   5951  C   LEU A 725      12.804 -29.425  47.424  1.00 41.95           C  
ANISOU 5951  C   LEU A 725     4925   5852   5162    -68   -287    672       C  
ATOM   5952  O   LEU A 725      12.214 -29.172  46.373  1.00 42.46           O  
ANISOU 5952  O   LEU A 725     4971   5932   5230   -100   -286    714       O  
ATOM   5953  CB  LEU A 725      14.689 -30.820  46.519  1.00 40.40           C  
ANISOU 5953  CB  LEU A 725     4737   5697   4915    -53   -325    572       C  
ATOM   5954  CG  LEU A 725      15.578 -32.070  46.515  1.00 38.86           C  
ANISOU 5954  CG  LEU A 725     4560   5505   4699    -24   -352    513       C  
ATOM   5955  CD1 LEU A 725      16.565 -31.997  45.365  1.00 38.91           C  
ANISOU 5955  CD1 LEU A 725     4540   5550   4692    -42   -346    468       C  
ATOM   5956  CD2 LEU A 725      16.309 -32.260  47.847  1.00 36.84           C  
ANISOU 5956  CD2 LEU A 725     4317   5236   4447     24   -363    479       C  
ATOM   5957  N   LYS A 726      12.796 -28.603  48.472  1.00 42.52           N  
ANISOU 5957  N   LYS A 726     4995   5903   5258    -55   -260    672       N  
ATOM   5958  CA  LYS A 726      12.316 -27.230  48.337  1.00 42.42           C  
ANISOU 5958  CA  LYS A 726     4954   5880   5284    -73   -220    712       C  
ATOM   5959  C   LYS A 726      13.485 -26.323  47.969  1.00 42.29           C  
ANISOU 5959  C   LYS A 726     4917   5887   5265    -81   -202    675       C  
ATOM   5960  O   LYS A 726      14.329 -25.999  48.810  1.00 43.16           O  
ANISOU 5960  O   LYS A 726     5032   5997   5371    -67   -188    627       O  
ATOM   5961  CB  LYS A 726      11.628 -26.739  49.606  1.00 40.99           C  
ANISOU 5961  CB  LYS A 726     4782   5660   5133    -62   -189    729       C  
ATOM   5962  CG  LYS A 726      10.961 -25.390  49.428  1.00 45.10           C  
ANISOU 5962  CG  LYS A 726     5273   6159   5704    -76   -143    777       C  
ATOM   5963  CD  LYS A 726      10.490 -24.827  50.757  1.00 45.74           C  
ANISOU 5963  CD  LYS A 726     5363   6199   5817    -68   -100    776       C  
ATOM   5964  CE  LYS A 726      10.199 -23.341  50.641  1.00 47.56           C  
ANISOU 5964  CE  LYS A 726     5565   6403   6103    -78    -45    806       C  
ATOM   5965  NZ  LYS A 726       8.891 -23.100  49.975  1.00 49.49           N  
ANISOU 5965  NZ  LYS A 726     5780   6632   6391    -81    -40    886       N  
ATOM   5966  N   ILE A 727      13.534 -25.936  46.701  1.00 40.90           N  
ANISOU 5966  N   ILE A 727     4719   5734   5087   -109   -202    697       N  
ATOM   5967  CA  ILE A 727      14.605 -25.095  46.191  1.00 38.86           C  
ANISOU 5967  CA  ILE A 727     4443   5500   4822   -125   -183    663       C  
ATOM   5968  C   ILE A 727      14.030 -23.765  45.716  1.00 39.28           C  
ANISOU 5968  C   ILE A 727     4475   5536   4912   -149   -148    722       C  
ATOM   5969  O   ILE A 727      13.174 -23.736  44.824  1.00 41.91           O  
ANISOU 5969  O   ILE A 727     4797   5872   5254   -170   -159    785       O  
ATOM   5970  CB  ILE A 727      15.371 -25.799  45.048  1.00 37.15           C  
ANISOU 5970  CB  ILE A 727     4222   5328   4566   -143   -211    628       C  
ATOM   5971  CG1 ILE A 727      15.738 -27.229  45.465  1.00 35.74           C  
ANISOU 5971  CG1 ILE A 727     4064   5153   4361   -113   -246    581       C  
ATOM   5972  CG2 ILE A 727      16.613 -25.005  44.698  1.00 35.82           C  
ANISOU 5972  CG2 ILE A 727     4036   5187   4387   -160   -189    579       C  
ATOM   5973  CD1 ILE A 727      16.516 -28.043  44.439  1.00 34.94           C  
ANISOU 5973  CD1 ILE A 727     3960   5089   4226   -126   -266    536       C  
ATOM   5974  N   MET A 728      14.478 -22.673  46.331  1.00 38.46           N  
ANISOU 5974  N   MET A 728     4369   5414   4832   -149   -105    703       N  
ATOM   5975  CA  MET A 728      14.000 -21.329  45.954  1.00 38.71           C  
ANISOU 5975  CA  MET A 728     4384   5418   4906   -167    -64    758       C  
ATOM   5976  C   MET A 728      15.112 -20.452  45.371  1.00 37.81           C  
ANISOU 5976  C   MET A 728     4263   5325   4777   -196    -41    724       C  
ATOM   5977  O   MET A 728      16.212 -20.361  45.920  1.00 33.17           O  
ANISOU 5977  O   MET A 728     3680   4754   4168   -196    -29    651       O  
ATOM   5978  CB  MET A 728      13.329 -20.599  47.135  1.00 39.25           C  
ANISOU 5978  CB  MET A 728     4456   5431   5025   -149    -18    776       C  
ATOM   5979  CG  MET A 728      12.287 -21.407  47.929  1.00 39.94           C  
ANISOU 5979  CG  MET A 728     4553   5497   5126   -124    -32    799       C  
ATOM   5980  SD  MET A 728      11.000 -22.233  46.966  1.00 46.86           S  
ANISOU 5980  SD  MET A 728     5415   6385   6005   -127    -77    877       S  
ATOM   5981  CE  MET A 728      10.056 -20.861  46.303  1.00 43.18           C  
ANISOU 5981  CE  MET A 728     4915   5887   5607   -137    -43    969       C  
ATOM   5982  N   GLY A 729      14.811 -19.816  44.247  1.00 37.71           N  
ANISOU 5982  N   GLY A 729     4238   5316   4776   -225    -37    779       N  
ATOM   5983  CA  GLY A 729      15.689 -18.803  43.674  1.00 37.70           C  
ANISOU 5983  CA  GLY A 729     4233   5324   4766   -259     -7    760       C  
ATOM   5984  C   GLY A 729      16.913 -19.327  42.948  1.00 38.00           C  
ANISOU 5984  C   GLY A 729     4271   5423   4745   -286    -30    692       C  
ATOM   5985  O   GLY A 729      17.435 -18.659  42.058  1.00 37.07           O  
ANISOU 5985  O   GLY A 729     4149   5323   4612   -327    -16    693       O  
ATOM   5986  N   LEU A 730      17.376 -20.513  43.337  1.00 36.75           N  
ANISOU 5986  N   LEU A 730     4115   5292   4554   -263    -62    634       N  
ATOM   5987  CA  LEU A 730      18.551 -21.113  42.729  1.00 36.19           C  
ANISOU 5987  CA  LEU A 730     4039   5278   4436   -281    -81    562       C  
ATOM   5988  C   LEU A 730      18.300 -21.457  41.266  1.00 38.03           C  
ANISOU 5988  C   LEU A 730     4268   5541   4642   -321   -105    595       C  
ATOM   5989  O   LEU A 730      17.158 -21.635  40.847  1.00 38.28           O  
ANISOU 5989  O   LEU A 730     4302   5558   4685   -326   -124    671       O  
ATOM   5990  CB  LEU A 730      19.004 -22.343  43.515  1.00 34.90           C  
ANISOU 5990  CB  LEU A 730     3878   5128   4254   -239   -111    502       C  
ATOM   5991  CG  LEU A 730      19.276 -22.136  45.014  1.00 35.62           C  
ANISOU 5991  CG  LEU A 730     3975   5198   4362   -205    -95    468       C  
ATOM   5992  CD1 LEU A 730      19.846 -23.402  45.625  1.00 37.70           C  
ANISOU 5992  CD1 LEU A 730     4240   5481   4602   -166   -133    413       C  
ATOM   5993  CD2 LEU A 730      20.210 -20.958  45.297  1.00 28.70           C  
ANISOU 5993  CD2 LEU A 730     3089   4331   3485   -228    -51    426       C  
ATOM   5994  N   GLU A 731      19.384 -21.550  40.502  1.00 39.07           N  
ANISOU 5994  N   GLU A 731     4392   5719   4735   -354   -103    536       N  
ATOM   5995  CA  GLU A 731      19.332 -21.705  39.048  1.00 39.39           C  
ANISOU 5995  CA  GLU A 731     4431   5795   4741   -409   -117    557       C  
ATOM   5996  C   GLU A 731      18.497 -22.894  38.567  1.00 40.16           C  
ANISOU 5996  C   GLU A 731     4535   5901   4823   -409   -158    589       C  
ATOM   5997  O   GLU A 731      18.062 -22.909  37.412  1.00 39.84           O  
ANISOU 5997  O   GLU A 731     4495   5884   4757   -460   -171    633       O  
ATOM   5998  CB  GLU A 731      20.751 -21.743  38.459  1.00 40.78           C  
ANISOU 5998  CB  GLU A 731     4596   6021   4877   -443   -103    468       C  
ATOM   5999  CG  GLU A 731      21.496 -20.374  38.444  1.00 43.35           C  
ANISOU 5999  CG  GLU A 731     4917   6348   5204   -475    -59    451       C  
ATOM   6000  CD  GLU A 731      21.837 -19.828  39.848  1.00 42.73           C  
ANISOU 6000  CD  GLU A 731     4836   6240   5158   -432    -33    420       C  
ATOM   6001  OE1 GLU A 731      21.940 -20.616  40.810  1.00 38.99           O  
ANISOU 6001  OE1 GLU A 731     4358   5762   4693   -380    -51    385       O  
ATOM   6002  OE2 GLU A 731      21.999 -18.599  39.986  1.00 45.98           O  
ANISOU 6002  OE2 GLU A 731     5253   6632   5585   -455      7    433       O  
ATOM   6003  N   THR A 732      18.262 -23.871  39.452  1.00 39.58           N  
ANISOU 6003  N   THR A 732     4468   5809   4760   -357   -177    568       N  
ATOM   6004  CA  THR A 732      17.355 -24.996  39.153  1.00 39.71           C  
ANISOU 6004  CA  THR A 732     4497   5827   4766   -356   -212    600       C  
ATOM   6005  C   THR A 732      15.917 -24.515  38.928  1.00 39.98           C  
ANISOU 6005  C   THR A 732     4529   5838   4822   -370   -220    707       C  
ATOM   6006  O   THR A 732      15.123 -25.217  38.307  1.00 39.62           O  
ANISOU 6006  O   THR A 732     4488   5807   4758   -393   -248    746       O  
ATOM   6007  CB  THR A 732      17.344 -26.077  40.280  1.00 40.19           C  
ANISOU 6007  CB  THR A 732     4569   5863   4837   -295   -229    562       C  
ATOM   6008  OG1 THR A 732      16.970 -25.486  41.531  1.00 38.01           O  
ANISOU 6008  OG1 THR A 732     4295   5545   4600   -254   -215    586       O  
ATOM   6009  CG2 THR A 732      18.704 -26.749  40.435  1.00 36.86           C  
ANISOU 6009  CG2 THR A 732     4144   5465   4397   -275   -229    463       C  
ATOM   6010  N   GLN A 733      15.605 -23.315  39.434  1.00 39.19           N  
ANISOU 6010  N   GLN A 733     4420   5704   4764   -357   -195    752       N  
ATOM   6011  CA  GLN A 733      14.256 -22.728  39.376  1.00 38.14           C  
ANISOU 6011  CA  GLN A 733     4279   5544   4669   -358   -197    855       C  
ATOM   6012  C   GLN A 733      14.077 -21.697  38.264  1.00 40.22           C  
ANISOU 6012  C   GLN A 733     4531   5821   4931   -408   -191    921       C  
ATOM   6013  O   GLN A 733      12.955 -21.299  37.966  1.00 44.28           O  
ANISOU 6013  O   GLN A 733     5031   6321   5472   -414   -202   1014       O  
ATOM   6014  CB  GLN A 733      13.898 -22.070  40.713  1.00 36.03           C  
ANISOU 6014  CB  GLN A 733     4010   5220   4459   -308   -166    867       C  
ATOM   6015  CG  GLN A 733      14.190 -22.933  41.933  1.00 36.12           C  
ANISOU 6015  CG  GLN A 733     4037   5218   4469   -262   -170    802       C  
ATOM   6016  CD  GLN A 733      13.669 -24.346  41.771  1.00 40.78           C  
ANISOU 6016  CD  GLN A 733     4638   5823   5032   -257   -211    803       C  
ATOM   6017  OE1 GLN A 733      14.446 -25.294  41.716  1.00 41.67           O  
ANISOU 6017  OE1 GLN A 733     4763   5960   5109   -253   -228    736       O  
ATOM   6018  NE2 GLN A 733      12.349 -24.490  41.652  1.00 37.57           N  
ANISOU 6018  NE2 GLN A 733     4225   5404   4645   -260   -225    878       N  
ATOM   6019  N   LYS A 734      15.175 -21.253  37.661  1.00 40.40           N  
ANISOU 6019  N   LYS A 734     4558   5871   4923   -445   -175    874       N  
ATOM   6020  CA  LYS A 734      15.116 -20.209  36.640  1.00 42.00           C  
ANISOU 6020  CA  LYS A 734     4756   6083   5120   -496   -167    934       C  
ATOM   6021  C   LYS A 734      14.961 -20.796  35.232  1.00 41.61           C  
ANISOU 6021  C   LYS A 734     4707   6092   5012   -563   -203    958       C  
ATOM   6022  O   LYS A 734      15.680 -21.724  34.855  1.00 42.47           O  
ANISOU 6022  O   LYS A 734     4824   6242   5070   -585   -212    881       O  
ATOM   6023  CB  LYS A 734      16.350 -19.300  36.729  1.00 43.22           C  
ANISOU 6023  CB  LYS A 734     4917   6236   5270   -511   -124    874       C  
ATOM   6024  CG  LYS A 734      16.418 -18.462  38.019  1.00 45.47           C  
ANISOU 6024  CG  LYS A 734     5202   6462   5612   -461    -81    863       C  
ATOM   6025  CD  LYS A 734      17.719 -17.663  38.147  1.00 49.02           C  
ANISOU 6025  CD  LYS A 734     5659   6917   6049   -482    -38    791       C  
ATOM   6026  CE  LYS A 734      17.651 -16.271  37.492  1.00 52.56           C  
ANISOU 6026  CE  LYS A 734     6115   7343   6514   -523     -7    853       C  
ATOM   6027  NZ  LYS A 734      16.973 -15.237  38.357  1.00 54.94           N  
ANISOU 6027  NZ  LYS A 734     6418   7569   6887   -485     32    906       N  
ATOM   6028  N   SER A 735      14.023 -20.248  34.461  1.00 39.39           N  
ANISOU 6028  N   SER A 735     4415   5814   4736   -595   -223   1064       N  
ATOM   6029  CA  SER A 735      13.753 -20.714  33.098  1.00 38.98           C  
ANISOU 6029  CA  SER A 735     4364   5822   4623   -670   -260   1100       C  
ATOM   6030  C   SER A 735      14.885 -20.406  32.110  1.00 38.45           C  
ANISOU 6030  C   SER A 735     4313   5799   4499   -740   -245   1051       C  
ATOM   6031  O   SER A 735      14.928 -20.964  31.011  1.00 40.78           O  
ANISOU 6031  O   SER A 735     4614   6151   4730   -810   -269   1050       O  
ATOM   6032  CB  SER A 735      12.451 -20.107  32.585  1.00 39.76           C  
ANISOU 6032  CB  SER A 735     4444   5916   4748   -685   -289   1237       C  
ATOM   6033  OG  SER A 735      12.533 -18.688  32.571  1.00 47.13           O  
ANISOU 6033  OG  SER A 735     5374   6811   5721   -680   -263   1292       O  
ATOM   6034  N   SER A 736      15.787 -19.515  32.499  1.00 35.11           N  
ANISOU 6034  N   SER A 736     3896   5350   4094   -728   -203   1009       N  
ATOM   6035  CA  SER A 736      16.912 -19.148  31.655  1.00 37.55           C  
ANISOU 6035  CA  SER A 736     4218   5698   4351   -795   -182    955       C  
ATOM   6036  C   SER A 736      18.049 -20.172  31.741  1.00 37.74           C  
ANISOU 6036  C   SER A 736     4245   5759   4335   -797   -170    822       C  
ATOM   6037  O   SER A 736      18.990 -20.145  30.939  1.00 38.90           O  
ANISOU 6037  O   SER A 736     4399   5950   4432   -859   -154    764       O  
ATOM   6038  CB  SER A 736      17.409 -17.748  32.017  1.00 35.78           C  
ANISOU 6038  CB  SER A 736     4000   5433   4162   -786   -139    963       C  
ATOM   6039  OG  SER A 736      17.640 -17.646  33.405  1.00 36.05           O  
ANISOU 6039  OG  SER A 736     4029   5420   4250   -710   -110    914       O  
ATOM   6040  N   THR A 737      17.956 -21.068  32.716  1.00 37.38           N  
ANISOU 6040  N   THR A 737     4192   5693   4315   -730   -177    777       N  
ATOM   6041  CA  THR A 737      18.966 -22.102  32.914  1.00 38.67           C  
ANISOU 6041  CA  THR A 737     4355   5883   4454   -718   -169    659       C  
ATOM   6042  C   THR A 737      18.650 -23.256  31.979  1.00 40.62           C  
ANISOU 6042  C   THR A 737     4610   6173   4652   -765   -196    651       C  
ATOM   6043  O   THR A 737      17.487 -23.694  31.900  1.00 40.07           O  
ANISOU 6043  O   THR A 737     4543   6097   4586   -762   -228    723       O  
ATOM   6044  CB  THR A 737      18.998 -22.616  34.384  1.00 37.44           C  
ANISOU 6044  CB  THR A 737     4194   5686   4346   -626   -167    618       C  
ATOM   6045  OG1 THR A 737      19.219 -21.518  35.271  1.00 37.59           O  
ANISOU 6045  OG1 THR A 737     4209   5667   4408   -591   -139    625       O  
ATOM   6046  CG2 THR A 737      20.102 -23.649  34.592  1.00 34.59           C  
ANISOU 6046  CG2 THR A 737     3827   5349   3965   -607   -161    501       C  
ATOM   6047  N   PRO A 738      19.678 -23.757  31.269  1.00 32.96           N  
ANISOU 6047  N   PRO A 738     3684   5360   3478   -697    124   -345       N  
ATOM   6048  CA  PRO A 738      19.494 -24.888  30.367  1.00 35.77           C  
ANISOU 6048  CA  PRO A 738     4022   5721   3846   -718    153   -410       C  
ATOM   6049  C   PRO A 738      18.751 -26.043  31.037  1.00 36.32           C  
ANISOU 6049  C   PRO A 738     4105   5707   3989   -676    166   -409       C  
ATOM   6050  O   PRO A 738      18.949 -26.296  32.230  1.00 34.82           O  
ANISOU 6050  O   PRO A 738     3922   5467   3841   -612    169   -374       O  
ATOM   6051  CB  PRO A 738      20.931 -25.302  30.038  1.00 34.73           C  
ANISOU 6051  CB  PRO A 738     3854   5633   3709   -704    183   -474       C  
ATOM   6052  CG  PRO A 738      21.693 -24.048  30.144  1.00 35.61           C  
ANISOU 6052  CG  PRO A 738     3954   5803   3773   -730    161   -434       C  
ATOM   6053  CD  PRO A 738      21.087 -23.320  31.309  1.00 32.76           C  
ANISOU 6053  CD  PRO A 738     3633   5383   3429   -702    124   -362       C  
ATOM   6054  N   LYS A 739      17.908 -26.726  30.269  1.00 36.15           N  
ANISOU 6054  N   LYS A 739     4086   5674   3976   -721    170   -443       N  
ATOM   6055  CA  LYS A 739      17.130 -27.855  30.779  1.00 41.32           C  
ANISOU 6055  CA  LYS A 739     4752   6243   4705   -706    179   -437       C  
ATOM   6056  C   LYS A 739      17.999 -28.909  31.494  1.00 40.83           C  
ANISOU 6056  C   LYS A 739     4696   6104   4714   -634    208   -462       C  
ATOM   6057  O   LYS A 739      17.755 -29.235  32.663  1.00 40.41           O  
ANISOU 6057  O   LYS A 739     4652   5991   4711   -585    209   -396       O  
ATOM   6058  CB  LYS A 739      16.299 -28.474  29.642  1.00 44.79           C  
ANISOU 6058  CB  LYS A 739     5191   6688   5138   -786    173   -494       C  
ATOM   6059  CG  LYS A 739      15.451 -29.696  30.016  1.00 54.41           C  
ANISOU 6059  CG  LYS A 739     6423   7811   6441   -799    177   -492       C  
ATOM   6060  CD  LYS A 739      14.209 -29.322  30.814  1.00 62.15           C  
ANISOU 6060  CD  LYS A 739     7388   8789   7437   -805    158   -384       C  
ATOM   6061  CE  LYS A 739      13.255 -30.504  30.927  1.00 66.70           C  
ANISOU 6061  CE  LYS A 739     7965   9290   8088   -854    158   -379       C  
ATOM   6062  NZ  LYS A 739      12.541 -30.508  32.236  1.00 64.87           N  
ANISOU 6062  NZ  LYS A 739     7719   9030   7898   -818    166   -264       N  
ATOM   6063  N   ALA A 740      19.026 -29.408  30.804  1.00 39.85           N  
ANISOU 6063  N   ALA A 740     4560   5991   4589   -622    233   -551       N  
ATOM   6064  CA  ALA A 740      19.871 -30.488  31.330  1.00 39.96           C  
ANISOU 6064  CA  ALA A 740     4575   5930   4680   -541    261   -579       C  
ATOM   6065  C   ALA A 740      20.645 -30.054  32.581  1.00 40.46           C  
ANISOU 6065  C   ALA A 740     4619   6004   4750   -465    251   -503       C  
ATOM   6066  O   ALA A 740      20.943 -30.871  33.469  1.00 38.98           O  
ANISOU 6066  O   ALA A 740     4437   5742   4633   -393    258   -471       O  
ATOM   6067  CB  ALA A 740      20.826 -30.972  30.254  1.00 40.33           C  
ANISOU 6067  CB  ALA A 740     4602   6007   4713   -532    296   -698       C  
ATOM   6068  N   VAL A 741      20.958 -28.758  32.627  1.00 39.27           N  
ANISOU 6068  N   VAL A 741     4451   5945   4524   -487    230   -473       N  
ATOM   6069  CA  VAL A 741      21.697 -28.137  33.718  1.00 36.93           C  
ANISOU 6069  CA  VAL A 741     4140   5679   4215   -437    210   -414       C  
ATOM   6070  C   VAL A 741      20.807 -27.971  34.942  1.00 36.50           C  
ANISOU 6070  C   VAL A 741     4118   5579   4170   -415    190   -326       C  
ATOM   6071  O   VAL A 741      21.265 -28.110  36.072  1.00 39.45           O  
ANISOU 6071  O   VAL A 741     4488   5944   4556   -353    179   -278       O  
ATOM   6072  CB  VAL A 741      22.298 -26.772  33.288  1.00 35.90           C  
ANISOU 6072  CB  VAL A 741     3987   5648   4004   -487    190   -418       C  
ATOM   6073  CG1 VAL A 741      23.019 -26.094  34.452  1.00 32.34           C  
ANISOU 6073  CG1 VAL A 741     3527   5224   3536   -452    158   -366       C  
ATOM   6074  CG2 VAL A 741      23.257 -26.957  32.126  1.00 33.81           C  
ANISOU 6074  CG2 VAL A 741     3676   5452   3718   -508    219   -495       C  
ATOM   6075  N   GLN A 742      19.530 -27.690  34.716  1.00 39.02           N  
ANISOU 6075  N   GLN A 742     4463   5886   4478   -463    185   -304       N  
ATOM   6076  CA  GLN A 742      18.562 -27.630  35.803  1.00 39.03           C  
ANISOU 6076  CA  GLN A 742     4486   5857   4487   -439    180   -223       C  
ATOM   6077  C   GLN A 742      18.498 -28.976  36.516  1.00 41.04           C  
ANISOU 6077  C   GLN A 742     4744   6033   4815   -393    199   -189       C  
ATOM   6078  O   GLN A 742      18.443 -29.027  37.745  1.00 44.69           O  
ANISOU 6078  O   GLN A 742     5214   6490   5276   -343    196   -116       O  
ATOM   6079  CB  GLN A 742      17.182 -27.277  35.274  1.00 38.63           C  
ANISOU 6079  CB  GLN A 742     4441   5813   4423   -496    177   -207       C  
ATOM   6080  CG  GLN A 742      16.993 -25.843  34.816  1.00 38.28           C  
ANISOU 6080  CG  GLN A 742     4401   5832   4312   -527    153   -205       C  
ATOM   6081  CD  GLN A 742      15.555 -25.599  34.379  1.00 38.42           C  
ANISOU 6081  CD  GLN A 742     4412   5861   4326   -566    147   -174       C  
ATOM   6082  OE1 GLN A 742      14.860 -26.529  33.994  1.00 40.22           O  
ANISOU 6082  OE1 GLN A 742     4624   6065   4593   -601    158   -179       O  
ATOM   6083  NE2 GLN A 742      15.105 -24.354  34.449  1.00 36.61           N  
ANISOU 6083  NE2 GLN A 742     4192   5665   4053   -559    128   -140       N  
ATOM   6084  N   LYS A 743      18.521 -30.061  35.744  1.00 41.67           N  
ANISOU 6084  N   LYS A 743     4824   6051   4958   -412    217   -242       N  
ATOM   6085  CA  LYS A 743      18.447 -31.407  36.311  1.00 43.44           C  
ANISOU 6085  CA  LYS A 743     5062   6172   5271   -375    233   -208       C  
ATOM   6086  C   LYS A 743      19.739 -31.805  37.022  1.00 44.35           C  
ANISOU 6086  C   LYS A 743     5164   6274   5411   -282    233   -192       C  
ATOM   6087  O   LYS A 743      19.697 -32.435  38.094  1.00 44.65           O  
ANISOU 6087  O   LYS A 743     5213   6262   5490   -230    232   -106       O  
ATOM   6088  CB  LYS A 743      18.087 -32.437  35.239  1.00 44.41           C  
ANISOU 6088  CB  LYS A 743     5201   6214   5459   -426    249   -285       C  
ATOM   6089  CG  LYS A 743      16.647 -32.349  34.738  1.00 46.49           C  
ANISOU 6089  CG  LYS A 743     5470   6480   5715   -522    241   -277       C  
ATOM   6090  CD  LYS A 743      16.533 -33.034  33.380  1.00 54.81           C  
ANISOU 6090  CD  LYS A 743     6537   7494   6794   -587    245   -392       C  
ATOM   6091  CE  LYS A 743      15.111 -33.009  32.841  1.00 58.63           C  
ANISOU 6091  CE  LYS A 743     7015   7991   7269   -693    226   -384       C  
ATOM   6092  NZ  LYS A 743      15.061 -33.400  31.398  1.00 60.50           N  
ANISOU 6092  NZ  LYS A 743     7265   8230   7494   -767    220   -511       N  
ATOM   6093  N   ALA A 744      20.876 -31.425  36.433  1.00 43.00           N  
ANISOU 6093  N   ALA A 744     4964   6163   5212   -262    232   -263       N  
ATOM   6094  CA  ALA A 744      22.188 -31.776  36.982  1.00 40.17           C  
ANISOU 6094  CA  ALA A 744     4573   5814   4877   -172    228   -252       C  
ATOM   6095  C   ALA A 744      22.410 -31.070  38.296  1.00 39.53           C  
ANISOU 6095  C   ALA A 744     4484   5797   4741   -138    194   -162       C  
ATOM   6096  O   ALA A 744      22.833 -31.689  39.282  1.00 39.92           O  
ANISOU 6096  O   ALA A 744     4525   5819   4822    -64    184    -91       O  
ATOM   6097  CB  ALA A 744      23.287 -31.436  36.011  1.00 40.91           C  
ANISOU 6097  CB  ALA A 744     4619   5982   4944   -170    239   -346       C  
ATOM   6098  N   LEU A 745      22.092 -29.779  38.316  1.00 38.48           N  
ANISOU 6098  N   LEU A 745     4357   5743   4522   -192    175   -163       N  
ATOM   6099  CA  LEU A 745      22.221 -28.985  39.534  1.00 38.46           C  
ANISOU 6099  CA  LEU A 745     4360   5801   4452   -169    141    -98       C  
ATOM   6100  C   LEU A 745      21.258 -29.454  40.627  1.00 38.82           C  
ANISOU 6100  C   LEU A 745     4439   5806   4505   -143    148     -5       C  
ATOM   6101  O   LEU A 745      21.580 -29.376  41.814  1.00 37.89           O  
ANISOU 6101  O   LEU A 745     4321   5726   4348    -94    126     60       O  
ATOM   6102  CB  LEU A 745      22.043 -27.493  39.232  1.00 37.67           C  
ANISOU 6102  CB  LEU A 745     4272   5769   4271   -232    121   -131       C  
ATOM   6103  CG  LEU A 745      23.152 -26.781  38.435  1.00 37.30           C  
ANISOU 6103  CG  LEU A 745     4187   5789   4195   -268    105   -196       C  
ATOM   6104  CD1 LEU A 745      22.679 -25.424  37.964  1.00 32.64           C  
ANISOU 6104  CD1 LEU A 745     3626   5229   3546   -342     89   -216       C  
ATOM   6105  CD2 LEU A 745      24.436 -26.639  39.261  1.00 38.56           C  
ANISOU 6105  CD2 LEU A 745     4306   6013   4333   -227     69   -177       C  
ATOM   6106  N   LYS A 746      20.087 -29.946  40.215  1.00 39.53           N  
ANISOU 6106  N   LYS A 746     4552   5830   4638   -182    177      5       N  
ATOM   6107  CA  LYS A 746      19.089 -30.479  41.145  1.00 40.76           C  
ANISOU 6107  CA  LYS A 746     4727   5952   4806   -171    192    102       C  
ATOM   6108  C   LYS A 746      19.554 -31.762  41.823  1.00 40.88           C  
ANISOU 6108  C   LYS A 746     4742   5898   4891   -110    195    173       C  
ATOM   6109  O   LYS A 746      19.429 -31.898  43.044  1.00 43.78           O  
ANISOU 6109  O   LYS A 746     5116   6292   5226    -70    190    273       O  
ATOM   6110  CB  LYS A 746      17.742 -30.703  40.464  1.00 40.67           C  
ANISOU 6110  CB  LYS A 746     4726   5898   4830   -241    218     97       C  
ATOM   6111  CG  LYS A 746      16.611 -30.789  41.451  1.00 39.86           C  
ANISOU 6111  CG  LYS A 746     4629   5809   4708   -242    237    200       C  
ATOM   6112  CD  LYS A 746      15.282 -31.075  40.789  1.00 43.88           C  
ANISOU 6112  CD  LYS A 746     5127   6286   5257   -319    257    205       C  
ATOM   6113  CE  LYS A 746      14.168 -31.077  41.835  1.00 46.40           C  
ANISOU 6113  CE  LYS A 746     5435   6647   5548   -317    284    316       C  
ATOM   6114  NZ  LYS A 746      13.102 -32.082  41.554  1.00 50.77           N  
ANISOU 6114  NZ  LYS A 746     5971   7136   6182   -390    304    366       N  
ATOM   6115  N   GLU A 747      20.093 -32.690  41.035  1.00 39.84           N  
ANISOU 6115  N   GLU A 747     4605   5681   4851    -98    204    124       N  
ATOM   6116  CA  GLU A 747      20.726 -33.892  41.580  1.00 40.45           C  
ANISOU 6116  CA  GLU A 747     4682   5677   5010    -23    202    185       C  
ATOM   6117  C   GLU A 747      21.937 -33.540  42.464  1.00 41.11           C  
ANISOU 6117  C   GLU A 747     4730   5850   5040     60    167    226       C  
ATOM   6118  O   GLU A 747      22.144 -34.170  43.507  1.00 42.97           O  
ANISOU 6118  O   GLU A 747     4967   6068   5291    122    153    336       O  
ATOM   6119  CB  GLU A 747      21.106 -34.864  40.455  1.00 40.68           C  
ANISOU 6119  CB  GLU A 747     4716   5593   5148    -16    223     97       C  
ATOM   6120  CG  GLU A 747      21.712 -36.215  40.887  1.00 43.84           C  
ANISOU 6120  CG  GLU A 747     5125   5872   5661     74    224    154       C  
ATOM   6121  CD  GLU A 747      20.728 -37.179  41.567  1.00 49.15           C  
ANISOU 6121  CD  GLU A 747     5844   6425   6405     52    232    273       C  
ATOM   6122  OE1 GLU A 747      21.145 -38.319  41.857  1.00 51.68           O  
ANISOU 6122  OE1 GLU A 747     6183   6621   6831    119    231    327       O  
ATOM   6123  OE2 GLU A 747      19.558 -36.816  41.828  1.00 50.86           O  
ANISOU 6123  OE2 GLU A 747     6076   6673   6577    -30    239    321       O  
ATOM   6124  N   CYS A 748      22.718 -32.534  42.061  1.00 39.32           N  
ANISOU 6124  N   CYS A 748     4470   5724   4747     53    147    146       N  
ATOM   6125  CA  CYS A 748      23.805 -32.032  42.902  1.00 39.59           C  
ANISOU 6125  CA  CYS A 748     4463   5862   4715    107    103    179       C  
ATOM   6126  C   CYS A 748      23.257 -31.629  44.276  1.00 39.75           C  
ANISOU 6126  C   CYS A 748     4512   5942   4649    112     82    278       C  
ATOM   6127  O   CYS A 748      23.752 -32.079  45.307  1.00 41.83           O  
ANISOU 6127  O   CYS A 748     4762   6234   4899    178     54    371       O  
ATOM   6128  CB  CYS A 748      24.542 -30.858  42.244  1.00 39.10           C  
ANISOU 6128  CB  CYS A 748     4366   5901   4590     65     84     82       C  
ATOM   6129  SG  CYS A 748      25.732 -31.297  40.910  1.00 45.75           S  
ANISOU 6129  SG  CYS A 748     5142   6739   5503     89    105    -19       S  
ATOM   6130  N   ILE A 749      22.209 -30.815  44.283  1.00 38.66           N  
ANISOU 6130  N   ILE A 749     4411   5829   4448     49     97    262       N  
ATOM   6131  CA  ILE A 749      21.588 -30.384  45.524  1.00 39.13           C  
ANISOU 6131  CA  ILE A 749     4499   5955   4415     57     90    339       C  
ATOM   6132  C   ILE A 749      21.010 -31.579  46.285  1.00 42.17           C  
ANISOU 6132  C   ILE A 749     4897   6283   4845     91    113    467       C  
ATOM   6133  O   ILE A 749      21.188 -31.682  47.507  1.00 43.51           O  
ANISOU 6133  O   ILE A 749     5068   6517   4947    137     93    561       O  
ATOM   6134  CB  ILE A 749      20.502 -29.316  45.272  1.00 40.11           C  
ANISOU 6134  CB  ILE A 749     4655   6106   4478     -3    112    290       C  
ATOM   6135  CG1 ILE A 749      21.132 -28.030  44.711  1.00 38.79           C  
ANISOU 6135  CG1 ILE A 749     4485   5993   4259    -38     80    184       C  
ATOM   6136  CG2 ILE A 749      19.691 -29.054  46.558  1.00 33.32           C  
ANISOU 6136  CG2 ILE A 749     3823   5311   3527     18    125    369       C  
ATOM   6137  CD1 ILE A 749      20.148 -27.086  44.005  1.00 37.58           C  
ANISOU 6137  CD1 ILE A 749     4360   5832   4087    -95    102    126       C  
ATOM   6138  N   ARG A 750      20.348 -32.489  45.564  1.00 40.99           N  
ANISOU 6138  N   ARG A 750     4757   6013   4804     62    151    474       N  
ATOM   6139  CA  ARG A 750      19.832 -33.722  46.174  1.00 41.72           C  
ANISOU 6139  CA  ARG A 750     4864   6024   4962     79    170    602       C  
ATOM   6140  C   ARG A 750      20.923 -34.526  46.881  1.00 42.43           C  
ANISOU 6140  C   ARG A 750     4939   6098   5084    169    136    687       C  
ATOM   6141  O   ARG A 750      20.734 -34.969  48.010  1.00 44.15           O  
ANISOU 6141  O   ARG A 750     5165   6339   5270    200    131    824       O  
ATOM   6142  CB  ARG A 750      19.112 -34.617  45.159  1.00 41.40           C  
ANISOU 6142  CB  ARG A 750     4841   5839   5051     22    205    576       C  
ATOM   6143  CG  ARG A 750      18.221 -35.661  45.845  1.00 46.86           C  
ANISOU 6143  CG  ARG A 750     5554   6455   5798      3    229    719       C  
ATOM   6144  CD  ARG A 750      17.825 -36.824  44.941  1.00 49.49           C  
ANISOU 6144  CD  ARG A 750     5911   6611   6284    -46    247    698       C  
ATOM   6145  NE  ARG A 750      18.988 -37.560  44.441  1.00 53.30           N  
ANISOU 6145  NE  ARG A 750     6399   6988   6863     24    229    646       N  
ATOM   6146  CZ  ARG A 750      19.675 -38.468  45.131  1.00 51.23           C  
ANISOU 6146  CZ  ARG A 750     6146   6655   6665    108    212    748       C  
ATOM   6147  NH1 ARG A 750      19.335 -38.774  46.375  1.00 53.30           N  
ANISOU 6147  NH1 ARG A 750     6413   6942   6894    123    208    918       N  
ATOM   6148  NH2 ARG A 750      20.712 -39.070  44.569  1.00 49.44           N  
ANISOU 6148  NH2 ARG A 750     5917   6338   6531    184    201    684       N  
ATOM   6149  N   ARG A 751      22.061 -34.719  46.219  1.00 42.78           N  
ANISOU 6149  N   ARG A 751     4955   6113   5189    214    115    614       N  
ATOM   6150  CA  ARG A 751      23.172 -35.450  46.839  1.00 44.84           C  
ANISOU 6150  CA  ARG A 751     5185   6366   5485    315     78    694       C  
ATOM   6151  C   ARG A 751      23.736 -34.728  48.062  1.00 44.42           C  
ANISOU 6151  C   ARG A 751     5107   6479   5292    352     27    759       C  
ATOM   6152  O   ARG A 751      23.927 -35.340  49.110  1.00 45.70           O  
ANISOU 6152  O   ARG A 751     5267   6658   5441    411      3    899       O  
ATOM   6153  CB  ARG A 751      24.260 -35.773  45.823  1.00 43.52           C  
ANISOU 6153  CB  ARG A 751     4978   6149   5410    365     74    593       C  
ATOM   6154  CG  ARG A 751      23.883 -36.951  44.965  1.00 47.12           C  
ANISOU 6154  CG  ARG A 751     5469   6417   6019    366    116    566       C  
ATOM   6155  CD  ARG A 751      24.614 -36.946  43.650  1.00 47.90           C  
ANISOU 6155  CD  ARG A 751     5537   6488   6174    381    134    412       C  
ATOM   6156  NE  ARG A 751      24.215 -38.084  42.828  1.00 52.30           N  
ANISOU 6156  NE  ARG A 751     6141   6859   6872    379    172    367       N  
ATOM   6157  CZ  ARG A 751      24.845 -39.255  42.801  1.00 50.27           C  
ANISOU 6157  CZ  ARG A 751     5887   6472   6742    481    176    392       C  
ATOM   6158  NH1 ARG A 751      25.917 -39.461  43.553  1.00 49.13           N  
ANISOU 6158  NH1 ARG A 751     5689   6376   6602    599    141    475       N  
ATOM   6159  NH2 ARG A 751      24.398 -40.221  42.017  1.00 47.52           N  
ANISOU 6159  NH2 ARG A 751     5596   5942   6518    465    210    331       N  
ATOM   6160  N   MET A 752      23.960 -33.426  47.930  1.00 43.02           N  
ANISOU 6160  N   MET A 752     4915   6421   5008    310      8    660       N  
ATOM   6161  CA  MET A 752      24.391 -32.596  49.047  1.00 43.03           C  
ANISOU 6161  CA  MET A 752     4906   6581   4864    323    -44    693       C  
ATOM   6162  C   MET A 752      23.490 -32.735  50.277  1.00 43.76           C  
ANISOU 6162  C   MET A 752     5039   6718   4868    325    -32    816       C  
ATOM   6163  O   MET A 752      23.971 -32.986  51.381  1.00 46.30           O  
ANISOU 6163  O   MET A 752     5348   7124   5122    378    -75    922       O  
ATOM   6164  CB  MET A 752      24.439 -31.137  48.614  1.00 41.13           C  
ANISOU 6164  CB  MET A 752     4669   6421   4536    254    -56    558       C  
ATOM   6165  CG  MET A 752      25.651 -30.776  47.777  1.00 39.88           C  
ANISOU 6165  CG  MET A 752     4452   6289   4412    252    -87    461       C  
ATOM   6166  SD  MET A 752      25.450 -29.139  47.062  1.00 41.55           S  
ANISOU 6166  SD  MET A 752     4687   6550   4550    149    -89    317       S  
ATOM   6167  CE  MET A 752      25.360 -28.130  48.541  1.00 33.09           C  
ANISOU 6167  CE  MET A 752     3654   5609   3311    140   -141    342       C  
ATOM   6168  N   LEU A 753      22.184 -32.596  50.086  1.00 43.21           N  
ANISOU 6168  N   LEU A 753     5012   6608   4797    267     25    809       N  
ATOM   6169  CA  LEU A 753      21.271 -32.538  51.225  1.00 43.97           C  
ANISOU 6169  CA  LEU A 753     5139   6778   4790    263     48    912       C  
ATOM   6170  C   LEU A 753      20.934 -33.914  51.784  1.00 45.41           C  
ANISOU 6170  C   LEU A 753     5324   6889   5040    292     67   1085       C  
ATOM   6171  O   LEU A 753      20.696 -34.056  52.984  1.00 47.62           O  
ANISOU 6171  O   LEU A 753     5612   7261   5219    315     65   1209       O  
ATOM   6172  CB  LEU A 753      19.985 -31.778  50.878  1.00 41.72           C  
ANISOU 6172  CB  LEU A 753     4883   6501   4469    197    105    845       C  
ATOM   6173  CG  LEU A 753      20.011 -30.435  50.135  1.00 39.92           C  
ANISOU 6173  CG  LEU A 753     4663   6304   4200    158     99    682       C  
ATOM   6174  CD1 LEU A 753      18.638 -29.751  50.221  1.00 35.12           C  
ANISOU 6174  CD1 LEU A 753     4081   5730   3534    123    154    663       C  
ATOM   6175  CD2 LEU A 753      21.128 -29.507  50.609  1.00 37.97           C  
ANISOU 6175  CD2 LEU A 753     4414   6164   3849    179     32    618       C  
ATOM   6176  N   GLN A 754      20.921 -34.923  50.917  1.00 46.68           N  
ANISOU 6176  N   GLN A 754     5485   6883   5369    288     86   1093       N  
ATOM   6177  CA  GLN A 754      20.537 -36.288  51.313  1.00 47.30           C  
ANISOU 6177  CA  GLN A 754     5578   6850   5542    302    104   1255       C  
ATOM   6178  C   GLN A 754      21.705 -37.270  51.510  1.00 47.82           C  
ANISOU 6178  C   GLN A 754     5626   6845   5698    397     56   1337       C  
ATOM   6179  O   GLN A 754      21.635 -38.157  52.364  1.00 49.18           O  
ANISOU 6179  O   GLN A 754     5809   6988   5888    433     48   1513       O  
ATOM   6180  CB  GLN A 754      19.526 -36.871  50.316  1.00 45.73           C  
ANISOU 6180  CB  GLN A 754     5404   6494   5479    224    158   1223       C  
ATOM   6181  CG  GLN A 754      18.284 -36.008  50.113  1.00 45.93           C  
ANISOU 6181  CG  GLN A 754     5433   6589   5430    138    206   1164       C  
ATOM   6182  CD  GLN A 754      17.300 -36.587  49.110  1.00 45.13           C  
ANISOU 6182  CD  GLN A 754     5343   6348   5456     52    248   1133       C  
ATOM   6183  OE1 GLN A 754      17.488 -37.688  48.595  1.00 45.08           O  
ANISOU 6183  OE1 GLN A 754     5355   6176   5596     48    244   1153       O  
ATOM   6184  NE2 GLN A 754      16.241 -35.838  48.827  1.00 44.89           N  
ANISOU 6184  NE2 GLN A 754     5302   6382   5371    -17    284   1081       N  
ATOM   6185  N   GLU A 755      22.772 -37.110  50.730  1.00 47.45           N  
ANISOU 6185  N   GLU A 755     5546   6775   5706    441     26   1220       N  
ATOM   6186  CA  GLU A 755      23.827 -38.124  50.679  1.00 49.68           C  
ANISOU 6186  CA  GLU A 755     5803   6965   6107    543     -8   1279       C  
ATOM   6187  C   GLU A 755      25.204 -37.650  51.166  1.00 49.85           C  
ANISOU 6187  C   GLU A 755     5757   7135   6049    627    -79   1277       C  
ATOM   6188  O   GLU A 755      25.937 -38.434  51.775  1.00 51.84           O  
ANISOU 6188  O   GLU A 755     5981   7374   6341    724   -121   1405       O  
ATOM   6189  CB  GLU A 755      23.897 -38.754  49.281  1.00 50.07           C  
ANISOU 6189  CB  GLU A 755     5864   6829   6330    541     26   1163       C  
ATOM   6190  CG  GLU A 755      22.664 -39.613  48.947  1.00 52.53           C  
ANISOU 6190  CG  GLU A 755     6242   6966   6752    468     78   1205       C  
ATOM   6191  CD  GLU A 755      22.598 -40.097  47.497  1.00 54.11           C  
ANISOU 6191  CD  GLU A 755     6465   6998   7098    443    112   1057       C  
ATOM   6192  OE1 GLU A 755      21.574 -40.712  47.137  1.00 57.04           O  
ANISOU 6192  OE1 GLU A 755     6888   7232   7552    364    147   1071       O  
ATOM   6193  OE2 GLU A 755      23.548 -39.878  46.718  1.00 51.98           O  
ANISOU 6193  OE2 GLU A 755     6159   6739   6854    496    104    928       O  
ATOM   6194  N   GLY A 756      25.543 -36.384  50.911  1.00 47.61           N  
ANISOU 6194  N   GLY A 756     5444   6988   5657    585    -97   1141       N  
ATOM   6195  CA  GLY A 756      26.793 -35.788  51.393  1.00 48.29           C  
ANISOU 6195  CA  GLY A 756     5461   7235   5652    635   -170   1131       C  
ATOM   6196  C   GLY A 756      27.820 -35.392  50.337  1.00 50.16           C  
ANISOU 6196  C   GLY A 756     5631   7484   5943    648   -183    985       C  
ATOM   6197  O   GLY A 756      27.541 -35.446  49.133  1.00 47.26           O  
ANISOU 6197  O   GLY A 756     5278   7009   5668    612   -129    870       O  
ATOM   6198  N   GLU A 757      29.019 -35.017  50.803  1.00 52.11           N  
ANISOU 6198  N   GLU A 757     5798   7876   6125    694   -255    997       N  
ATOM   6199  CA  GLU A 757      30.083 -34.462  49.949  1.00 52.85           C  
ANISOU 6199  CA  GLU A 757     5809   8031   6240    693   -272    870       C  
ATOM   6200  C   GLU A 757      30.675 -35.456  48.948  1.00 53.53           C  
ANISOU 6200  C   GLU A 757     5847   7993   6499    781   -235    841       C  
ATOM   6201  O   GLU A 757      30.955 -35.096  47.799  1.00 52.99           O  
ANISOU 6201  O   GLU A 757     5750   7912   6472    748   -199    702       O  
ATOM   6202  CB  GLU A 757      31.212 -33.824  50.785  1.00 52.49           C  
ANISOU 6202  CB  GLU A 757     5679   8188   6077    709   -367    901       C  
ATOM   6203  CG  GLU A 757      32.357 -33.272  49.919  1.00 54.28           C  
ANISOU 6203  CG  GLU A 757     5802   8493   6329    698   -386    785       C  
ATOM   6204  CD  GLU A 757      33.334 -32.381  50.658  1.00 55.59           C  
ANISOU 6204  CD  GLU A 757     5889   8868   6364    666   -483    789       C  
ATOM   6205  OE1 GLU A 757      33.919 -32.815  51.670  1.00 57.48           O  
ANISOU 6205  OE1 GLU A 757     6076   9201   6564    741   -554    915       O  
ATOM   6206  OE2 GLU A 757      33.537 -31.242  50.200  1.00 57.82           O  
ANISOU 6206  OE2 GLU A 757     6161   9223   6587    560   -494    669       O  
ATOM   6207  N   GLU A 758      30.879 -36.692  49.390  1.00 54.64           N  
ANISOU 6207  N   GLU A 758     5981   8043   6737    896   -243    971       N  
ATOM   6208  CA  GLU A 758      31.460 -37.716  48.532  1.00 56.15           C  
ANISOU 6208  CA  GLU A 758     6135   8101   7100   1003   -207    943       C  
ATOM   6209  C   GLU A 758      30.528 -38.066  47.366  1.00 54.66           C  
ANISOU 6209  C   GLU A 758     6030   7727   7011    947   -119    830       C  
ATOM   6210  O   GLU A 758      30.971 -38.182  46.219  1.00 54.41           O  
ANISOU 6210  O   GLU A 758     5965   7652   7057    968    -76    700       O  
ATOM   6211  CB  GLU A 758      31.825 -38.958  49.344  1.00 59.08           C  
ANISOU 6211  CB  GLU A 758     6493   8396   7558   1144   -240   1123       C  
ATOM   6212  CG  GLU A 758      32.949 -39.777  48.723  1.00 67.27           C  
ANISOU 6212  CG  GLU A 758     7443   9372   8743   1295   -232   1100       C  
ATOM   6213  CD  GLU A 758      33.468 -40.856  49.648  1.00 72.41           C  
ANISOU 6213  CD  GLU A 758     8066   9977   9469   1449   -283   1296       C  
ATOM   6214  OE1 GLU A 758      33.525 -42.024  49.212  1.00 74.41           O  
ANISOU 6214  OE1 GLU A 758     8346  10027   9898   1559   -245   1316       O  
ATOM   6215  OE2 GLU A 758      33.811 -40.539  50.809  1.00 74.73           O  
ANISOU 6215  OE2 GLU A 758     8315  10435   9645   1460   -364   1430       O  
ATOM   6216  N   SER A 759      29.238 -38.213  47.661  1.00 52.42           N  
ANISOU 6216  N   SER A 759     5849   7353   6715    870    -93    878       N  
ATOM   6217  CA  SER A 759      28.240 -38.463  46.628  1.00 50.49           C  
ANISOU 6217  CA  SER A 759     5682   6955   6549    793    -22    777       C  
ATOM   6218  C   SER A 759      28.202 -37.339  45.584  1.00 48.51           C  
ANISOU 6218  C   SER A 759     5413   6788   6231    697      4    599       C  
ATOM   6219  O   SER A 759      28.182 -37.604  44.382  1.00 47.56           O  
ANISOU 6219  O   SER A 759     5301   6580   6190    687     53    476       O  
ATOM   6220  CB  SER A 759      26.862 -38.661  47.247  1.00 50.13           C  
ANISOU 6220  CB  SER A 759     5727   6841   6480    714     -6    874       C  
ATOM   6221  OG  SER A 759      25.989 -39.253  46.303  1.00 52.02           O  
ANISOU 6221  OG  SER A 759     6033   6904   6829    658     53    803       O  
ATOM   6222  N   LEU A 760      28.218 -36.093  46.050  1.00 46.02           N  
ANISOU 6222  N   LEU A 760     5078   6641   5767    627    -31    589       N  
ATOM   6223  CA  LEU A 760      28.255 -34.936  45.165  1.00 44.74           C  
ANISOU 6223  CA  LEU A 760     4899   6562   5537    535    -17    444       C  
ATOM   6224  C   LEU A 760      29.441 -35.012  44.187  1.00 46.28           C  
ANISOU 6224  C   LEU A 760     5007   6788   5788    585     -5    344       C  
ATOM   6225  O   LEU A 760      29.274 -34.826  42.975  1.00 45.17           O  
ANISOU 6225  O   LEU A 760     4874   6614   5673    535     43    220       O  
ATOM   6226  CB  LEU A 760      28.283 -33.648  45.997  1.00 41.38           C  
ANISOU 6226  CB  LEU A 760     4467   6302   4955    472    -69    460       C  
ATOM   6227  CG  LEU A 760      28.191 -32.232  45.410  1.00 39.67           C  
ANISOU 6227  CG  LEU A 760     4251   6173   4647    362    -71    342       C  
ATOM   6228  CD1 LEU A 760      29.449 -31.431  45.681  1.00 40.28           C  
ANISOU 6228  CD1 LEU A 760     4246   6409   4652    361   -133    320       C  
ATOM   6229  CD2 LEU A 760      27.825 -32.174  43.929  1.00 39.13           C  
ANISOU 6229  CD2 LEU A 760     4198   6029   4640    307    -11    222       C  
ATOM   6230  N   GLN A 761      30.624 -35.302  44.723  1.00 47.22           N  
ANISOU 6230  N   GLN A 761     5038   6983   5919    687    -49    405       N  
ATOM   6231  CA  GLN A 761      31.839 -35.445  43.923  1.00 47.72           C  
ANISOU 6231  CA  GLN A 761     4996   7099   6036    755    -35    329       C  
ATOM   6232  C   GLN A 761      31.726 -36.532  42.849  1.00 48.61           C  
ANISOU 6232  C   GLN A 761     5134   7046   6291    821     40    251       C  
ATOM   6233  O   GLN A 761      32.238 -36.366  41.744  1.00 48.63           O  
ANISOU 6233  O   GLN A 761     5085   7083   6309    818     84    127       O  
ATOM   6234  CB  GLN A 761      33.049 -35.690  44.833  1.00 49.09           C  
ANISOU 6234  CB  GLN A 761     5062   7385   6206    867   -101    433       C  
ATOM   6235  CG  GLN A 761      33.509 -34.434  45.571  1.00 51.82           C  
ANISOU 6235  CG  GLN A 761     5356   7934   6401    787   -178    455       C  
ATOM   6236  CD  GLN A 761      34.405 -34.695  46.789  1.00 57.23           C  
ANISOU 6236  CD  GLN A 761     5957   8733   7055    879   -264    592       C  
ATOM   6237  OE1 GLN A 761      34.742 -33.760  47.519  1.00 58.28           O  
ANISOU 6237  OE1 GLN A 761     6056   9026   7060    812   -337    614       O  
ATOM   6238  NE2 GLN A 761      34.786 -35.954  47.013  1.00 56.77           N  
ANISOU 6238  NE2 GLN A 761     5867   8590   7112   1031   -261    684       N  
ATOM   6239  N   GLU A 762      31.047 -37.634  43.168  1.00 50.27           N  
ANISOU 6239  N   GLU A 762     5424   7076   6598    872     55    322       N  
ATOM   6240  CA  GLU A 762      30.809 -38.701  42.194  1.00 52.22           C  
ANISOU 6240  CA  GLU A 762     5720   7137   6984    922    121    238       C  
ATOM   6241  C   GLU A 762      29.959 -38.203  41.018  1.00 49.20           C  
ANISOU 6241  C   GLU A 762     5397   6728   6569    789    174     91       C  
ATOM   6242  O   GLU A 762      30.327 -38.388  39.849  1.00 47.72           O  
ANISOU 6242  O   GLU A 762     5188   6524   6419    806    226    -47       O  
ATOM   6243  CB  GLU A 762      30.153 -39.917  42.864  1.00 56.92           C  
ANISOU 6243  CB  GLU A 762     6403   7534   7692    977    117    360       C  
ATOM   6244  CG  GLU A 762      29.920 -41.114  41.929  1.00 65.18           C  
ANISOU 6244  CG  GLU A 762     7513   8356   8896   1029    177    271       C  
ATOM   6245  CD  GLU A 762      29.163 -42.264  42.596  1.00 74.01           C  
ANISOU 6245  CD  GLU A 762     8731   9260  10130   1053    168    401       C  
ATOM   6246  OE1 GLU A 762      28.096 -42.661  42.068  1.00 75.73           O  
ANISOU 6246  OE1 GLU A 762     9047   9327  10400    959    201    348       O  
ATOM   6247  OE2 GLU A 762      29.633 -42.769  43.644  1.00 77.49           O  
ANISOU 6247  OE2 GLU A 762     9148   9689  10608   1158    123    564       O  
ATOM   6248  N   TYR A 763      28.833 -37.561  41.327  1.00 45.13           N  
ANISOU 6248  N   TYR A 763     4951   6223   5975    662    161    122       N  
ATOM   6249  CA  TYR A 763      27.934 -37.089  40.282  1.00 45.51           C  
ANISOU 6249  CA  TYR A 763     5053   6250   5989    537    200      4       C  
ATOM   6250  C   TYR A 763      28.596 -36.042  39.387  1.00 45.23           C  
ANISOU 6250  C   TYR A 763     4947   6370   5867    490    212   -112       C  
ATOM   6251  O   TYR A 763      28.534 -36.137  38.154  1.00 43.00           O  
ANISOU 6251  O   TYR A 763     4672   6064   5601    459    261   -240       O  
ATOM   6252  CB  TYR A 763      26.623 -36.555  40.856  1.00 44.45           C  
ANISOU 6252  CB  TYR A 763     4989   6113   5787    425    183     72       C  
ATOM   6253  CG  TYR A 763      25.646 -36.132  39.779  1.00 44.95           C  
ANISOU 6253  CG  TYR A 763     5101   6155   5825    304    217    -35       C  
ATOM   6254  CD1 TYR A 763      25.383 -34.776  39.541  1.00 41.74           C  
ANISOU 6254  CD1 TYR A 763     4681   5880   5298    210    205    -73       C  
ATOM   6255  CD2 TYR A 763      24.998 -37.086  38.980  1.00 43.87           C  
ANISOU 6255  CD2 TYR A 763     5023   5863   5784    283    255    -99       C  
ATOM   6256  CE1 TYR A 763      24.490 -34.380  38.550  1.00 39.54           C  
ANISOU 6256  CE1 TYR A 763     4439   5590   4994    107    230   -156       C  
ATOM   6257  CE2 TYR A 763      24.108 -36.702  37.982  1.00 43.02           C  
ANISOU 6257  CE2 TYR A 763     4949   5753   5642    168    277   -193       C  
ATOM   6258  CZ  TYR A 763      23.859 -35.346  37.774  1.00 44.34           C  
ANISOU 6258  CZ  TYR A 763     5094   6064   5687     85    264   -214       C  
ATOM   6259  OH  TYR A 763      22.980 -34.960  36.789  1.00 48.18           O  
ANISOU 6259  OH  TYR A 763     5610   6558   6139    -21    279   -292       O  
ATOM   6260  N   PHE A 764      29.243 -35.064  40.014  1.00 43.89           N  
ANISOU 6260  N   PHE A 764     4711   6361   5602    478    166    -65       N  
ATOM   6261  CA  PHE A 764      29.949 -34.030  39.279  1.00 44.67           C  
ANISOU 6261  CA  PHE A 764     4739   6612   5623    423    170   -151       C  
ATOM   6262  C   PHE A 764      30.745 -34.603  38.108  1.00 46.89           C  
ANISOU 6262  C   PHE A 764     4960   6893   5964    485    229   -262       C  
ATOM   6263  O   PHE A 764      30.510 -34.228  36.954  1.00 45.95           O  
ANISOU 6263  O   PHE A 764     4851   6797   5810    410    272   -370       O  
ATOM   6264  CB  PHE A 764      30.879 -33.233  40.190  1.00 42.64           C  
ANISOU 6264  CB  PHE A 764     4399   6512   5289    431    106    -81       C  
ATOM   6265  CG  PHE A 764      31.568 -32.118  39.480  1.00 43.17           C  
ANISOU 6265  CG  PHE A 764     4395   6730   5278    352    105   -155       C  
ATOM   6266  CD1 PHE A 764      30.869 -30.959  39.151  1.00 41.60           C  
ANISOU 6266  CD1 PHE A 764     4249   6563   4992    215     98   -190       C  
ATOM   6267  CD2 PHE A 764      32.895 -32.241  39.087  1.00 40.34           C  
ANISOU 6267  CD2 PHE A 764     3911   6479   4938    414    116   -185       C  
ATOM   6268  CE1 PHE A 764      31.494 -29.927  38.470  1.00 42.84           C  
ANISOU 6268  CE1 PHE A 764     4347   6846   5084    132     96   -244       C  
ATOM   6269  CE2 PHE A 764      33.528 -31.219  38.407  1.00 42.72           C  
ANISOU 6269  CE2 PHE A 764     4140   6925   5168    326    118   -242       C  
ATOM   6270  CZ  PHE A 764      32.830 -30.053  38.096  1.00 41.37           C  
ANISOU 6270  CZ  PHE A 764     4034   6774   4912    178    106   -268       C  
ATOM   6271  N   LYS A 765      31.667 -35.517  38.415  1.00 48.73           N  
ANISOU 6271  N   LYS A 765     5129   7103   6282    630    233   -233       N  
ATOM   6272  CA  LYS A 765      32.481 -36.186  37.401  1.00 53.37           C  
ANISOU 6272  CA  LYS A 765     5654   7687   6936    723    297   -341       C  
ATOM   6273  C   LYS A 765      31.637 -36.841  36.303  1.00 54.01           C  
ANISOU 6273  C   LYS A 765     5832   7621   7068    694    362   -462       C  
ATOM   6274  O   LYS A 765      31.938 -36.693  35.119  1.00 53.87           O  
ANISOU 6274  O   LYS A 765     5783   7663   7021    674    418   -591       O  
ATOM   6275  CB  LYS A 765      33.399 -37.232  38.041  1.00 56.23           C  
ANISOU 6275  CB  LYS A 765     5952   8005   7406    906    287   -273       C  
ATOM   6276  CG  LYS A 765      34.575 -36.665  38.827  1.00 62.73           C  
ANISOU 6276  CG  LYS A 765     6638   9017   8179    952    230   -184       C  
ATOM   6277  CD  LYS A 765      35.474 -37.784  39.374  1.00 69.83           C  
ANISOU 6277  CD  LYS A 765     7465   9871   9195   1151    221   -112       C  
ATOM   6278  CE  LYS A 765      34.789 -38.572  40.501  1.00 73.37           C  
ANISOU 6278  CE  LYS A 765     8010  10155   9711   1202    174     28       C  
ATOM   6279  NZ  LYS A 765      35.355 -39.944  40.708  1.00 75.09           N  
ANISOU 6279  NZ  LYS A 765     8206  10241  10083   1401    187     76       N  
ATOM   6280  N   GLU A 766      30.580 -37.547  36.703  1.00 54.91           N  
ANISOU 6280  N   GLU A 766     6060   7554   7250    682    352   -418       N  
ATOM   6281  CA  GLU A 766      29.733 -38.270  35.763  1.00 56.06           C  
ANISOU 6281  CA  GLU A 766     6301   7544   7453    646    400   -528       C  
ATOM   6282  C   GLU A 766      29.053 -37.307  34.799  1.00 55.11           C  
ANISOU 6282  C   GLU A 766     6205   7514   7219    489    416   -618       C  
ATOM   6283  O   GLU A 766      29.051 -37.540  33.587  1.00 55.74           O  
ANISOU 6283  O   GLU A 766     6298   7588   7294    472    469   -759       O  
ATOM   6284  CB  GLU A 766      28.703 -39.132  36.499  1.00 58.27           C  
ANISOU 6284  CB  GLU A 766     6689   7624   7826    641    376   -437       C  
ATOM   6285  CG  GLU A 766      29.307 -40.340  37.215  1.00 64.71           C  
ANISOU 6285  CG  GLU A 766     7502   8305   8780    804    370   -359       C  
ATOM   6286  CD  GLU A 766      28.357 -41.021  38.206  1.00 68.25           C  
ANISOU 6286  CD  GLU A 766     8043   8587   9303    786    334   -217       C  
ATOM   6287  OE1 GLU A 766      27.198 -40.566  38.377  1.00 67.44           O  
ANISOU 6287  OE1 GLU A 766     8001   8483   9142    647    318   -181       O  
ATOM   6288  OE2 GLU A 766      28.787 -42.023  38.820  1.00 70.54           O  
ANISOU 6288  OE2 GLU A 766     8340   8751   9710    914    323   -133       O  
ATOM   6289  N   PHE A 767      28.505 -36.215  35.331  1.00 52.37           N  
ANISOU 6289  N   PHE A 767     5866   7255   6778    383    370   -537       N  
ATOM   6290  CA  PHE A 767      27.882 -35.203  34.486  1.00 50.55           C  
ANISOU 6290  CA  PHE A 767     5652   7112   6440    242    376   -599       C  
ATOM   6291  C   PHE A 767      28.899 -34.583  33.517  1.00 51.03           C  
ANISOU 6291  C   PHE A 767     5625   7335   6429    236    410   -690       C  
ATOM   6292  O   PHE A 767      28.638 -34.483  32.317  1.00 50.21           O  
ANISOU 6292  O   PHE A 767     5537   7258   6283    174    450   -799       O  
ATOM   6293  CB  PHE A 767      27.174 -34.125  35.314  1.00 45.61           C  
ANISOU 6293  CB  PHE A 767     5050   6542   5736    152    321   -494       C  
ATOM   6294  CG  PHE A 767      26.437 -33.108  34.479  1.00 43.44           C  
ANISOU 6294  CG  PHE A 767     4801   6337   5368     18    322   -542       C  
ATOM   6295  CD1 PHE A 767      26.881 -31.795  34.410  1.00 43.09           C  
ANISOU 6295  CD1 PHE A 767     4709   6439   5224    -41    300   -529       C  
ATOM   6296  CD2 PHE A 767      25.306 -33.469  33.750  1.00 46.02           C  
ANISOU 6296  CD2 PHE A 767     5197   6580   5707    -52    340   -595       C  
ATOM   6297  CE1 PHE A 767      26.207 -30.846  33.643  1.00 42.30           C  
ANISOU 6297  CE1 PHE A 767     4635   6392   5044   -156    297   -558       C  
ATOM   6298  CE2 PHE A 767      24.625 -32.535  32.974  1.00 44.29           C  
ANISOU 6298  CE2 PHE A 767     4994   6434   5400   -166    334   -627       C  
ATOM   6299  CZ  PHE A 767      25.078 -31.220  32.919  1.00 44.99           C  
ANISOU 6299  CZ  PHE A 767     5039   6661   5396   -213    314   -603       C  
ATOM   6300  N   GLU A 768      30.053 -34.185  34.049  1.00 52.30           N  
ANISOU 6300  N   GLU A 768     5687   7614   6572    296    393   -640       N  
ATOM   6301  CA  GLU A 768      31.139 -33.615  33.252  1.00 55.00           C  
ANISOU 6301  CA  GLU A 768     5922   8125   6850    291    426   -705       C  
ATOM   6302  C   GLU A 768      31.596 -34.540  32.119  1.00 55.78           C  
ANISOU 6302  C   GLU A 768     5999   8206   6991    370    508   -842       C  
ATOM   6303  O   GLU A 768      31.907 -34.079  31.026  1.00 53.95           O  
ANISOU 6303  O   GLU A 768     5724   8094   6680    315    553   -930       O  
ATOM   6304  CB  GLU A 768      32.321 -33.252  34.152  1.00 57.62           C  
ANISOU 6304  CB  GLU A 768     6141   8576   7177    353    386   -618       C  
ATOM   6305  CG  GLU A 768      33.253 -32.207  33.549  1.00 64.51           C  
ANISOU 6305  CG  GLU A 768     6903   9652   7956    286    397   -644       C  
ATOM   6306  CD  GLU A 768      34.464 -31.902  34.420  1.00 72.70           C  
ANISOU 6306  CD  GLU A 768     7815  10816   8991    339    351   -562       C  
ATOM   6307  OE1 GLU A 768      35.040 -30.802  34.255  1.00 77.26           O  
ANISOU 6307  OE1 GLU A 768     8318  11551   9486    242    331   -547       O  
ATOM   6308  OE2 GLU A 768      34.848 -32.753  35.258  1.00 74.43           O  
ANISOU 6308  OE2 GLU A 768     8008  10980   9292    471    331   -507       O  
ATOM   6309  N   LYS A 769      31.619 -35.843  32.389  1.00 59.10           N  
ANISOU 6309  N   LYS A 769     6452   8470   7534    498    527   -860       N  
ATOM   6310  CA  LYS A 769      31.952 -36.842  31.375  1.00 62.96           C  
ANISOU 6310  CA  LYS A 769     6943   8902   8077    587    606  -1008       C  
ATOM   6311  C   LYS A 769      30.914 -36.929  30.261  1.00 62.74           C  
ANISOU 6311  C   LYS A 769     7017   8817   8005    477    636  -1128       C  
ATOM   6312  O   LYS A 769      31.264 -37.184  29.107  1.00 64.24           O  
ANISOU 6312  O   LYS A 769     7188   9060   8160    494    705  -1272       O  
ATOM   6313  CB  LYS A 769      32.138 -38.221  32.015  1.00 66.01           C  
ANISOU 6313  CB  LYS A 769     7361   9099   8622    750    609   -988       C  
ATOM   6314  CG  LYS A 769      33.588 -38.674  32.140  1.00 71.54           C  
ANISOU 6314  CG  LYS A 769     7933   9871   9379    929    643   -994       C  
ATOM   6315  CD  LYS A 769      34.392 -37.813  33.115  1.00 75.30           C  
ANISOU 6315  CD  LYS A 769     8288  10518   9806    934    583   -850       C  
ATOM   6316  CE  LYS A 769      35.858 -38.248  33.170  1.00 78.85           C  
ANISOU 6316  CE  LYS A 769     8585  11065  10309   1110    615   -854       C  
ATOM   6317  NZ  LYS A 769      36.587 -37.563  34.276  1.00 78.70           N  
ANISOU 6317  NZ  LYS A 769     8453  11192  10256   1116    539   -701       N  
ATOM   6318  N   GLU A 770      29.645 -36.722  30.614  1.00 60.43           N  
ANISOU 6318  N   GLU A 770     6824   8430   7707    366    586  -1068       N  
ATOM   6319  CA  GLU A 770      28.536 -36.885  29.669  1.00 60.29           C  
ANISOU 6319  CA  GLU A 770     6902   8349   7657    257    599  -1166       C  
ATOM   6320  C   GLU A 770      28.073 -35.577  29.033  1.00 57.67           C  
ANISOU 6320  C   GLU A 770     6558   8176   7178    102    583  -1161       C  
ATOM   6321  O   GLU A 770      27.240 -35.592  28.121  1.00 58.04           O  
ANISOU 6321  O   GLU A 770     6665   8212   7174      7    591  -1242       O  
ATOM   6322  CB  GLU A 770      27.346 -37.605  30.330  1.00 60.65           C  
ANISOU 6322  CB  GLU A 770     7057   8187   7798    228    557  -1109       C  
ATOM   6323  CG  GLU A 770      27.627 -39.057  30.762  1.00 69.56           C  
ANISOU 6323  CG  GLU A 770     8227   9115   9087    366    575  -1124       C  
ATOM   6324  CD  GLU A 770      28.090 -39.961  29.610  1.00 76.00           C  
ANISOU 6324  CD  GLU A 770     9061   9877   9940    438    646  -1316       C  
ATOM   6325  OE1 GLU A 770      29.306 -40.261  29.539  1.00 77.66           O  
ANISOU 6325  OE1 GLU A 770     9193  10133  10181    583    691  -1358       O  
ATOM   6326  OE2 GLU A 770      27.243 -40.364  28.778  1.00 75.97           O  
ANISOU 6326  OE2 GLU A 770     9144   9791   9929    351    656  -1430       O  
ATOM   6327  N   PHE A 771      28.615 -34.455  29.504  1.00 55.60           N  
ANISOU 6327  N   PHE A 771     6220   8058   6848     76    555  -1065       N  
ATOM   6328  CA  PHE A 771      28.152 -33.137  29.070  1.00 53.52           C  
ANISOU 6328  CA  PHE A 771     5955   7920   6461    -67    528  -1032       C  
ATOM   6329  C   PHE A 771      28.207 -32.924  27.556  1.00 54.76           C  
ANISOU 6329  C   PHE A 771     6100   8189   6518   -134    579  -1151       C  
ATOM   6330  O   PHE A 771      27.244 -32.432  26.969  1.00 54.79           O  
ANISOU 6330  O   PHE A 771     6158   8209   6453   -250    558  -1156       O  
ATOM   6331  CB  PHE A 771      28.922 -32.020  29.777  1.00 51.56           C  
ANISOU 6331  CB  PHE A 771     5626   7798   6165    -80    493   -925       C  
ATOM   6332  CG  PHE A 771      28.381 -30.636  29.494  1.00 49.45           C  
ANISOU 6332  CG  PHE A 771     5374   7622   5793   -221    456   -874       C  
ATOM   6333  CD1 PHE A 771      29.075 -29.757  28.664  1.00 46.04           C  
ANISOU 6333  CD1 PHE A 771     4873   7355   5263   -287    477   -892       C  
ATOM   6334  CD2 PHE A 771      27.175 -30.215  30.057  1.00 46.22           C  
ANISOU 6334  CD2 PHE A 771     5046   7131   5385   -284    402   -801       C  
ATOM   6335  CE1 PHE A 771      28.580 -28.486  28.397  1.00 44.25           C  
ANISOU 6335  CE1 PHE A 771     4670   7192   4952   -414    439   -834       C  
ATOM   6336  CE2 PHE A 771      26.671 -28.939  29.800  1.00 43.12           C  
ANISOU 6336  CE2 PHE A 771     4670   6807   4907   -397    368   -752       C  
ATOM   6337  CZ  PHE A 771      27.373 -28.074  28.970  1.00 45.14           C  
ANISOU 6337  CZ  PHE A 771     4868   7208   5075   -462    383   -766       C  
ATOM   6338  N   ARG A 772      29.326 -33.293  26.934  1.00 56.50           N  
ANISOU 6338  N   ARG A 772     6244   8498   6725    -57    645  -1241       N  
ATOM   6339  CA  ARG A 772      29.541 -33.030  25.504  1.00 60.11           C  
ANISOU 6339  CA  ARG A 772     6675   9101   7064   -117    703  -1349       C  
ATOM   6340  C   ARG A 772      28.679 -33.891  24.577  1.00 60.24           C  
ANISOU 6340  C   ARG A 772     6785   9029   7073   -143    728  -1488       C  
ATOM   6341  O   ARG A 772      28.658 -33.675  23.367  1.00 60.80           O  
ANISOU 6341  O   ARG A 772     6851   9222   7029   -208    767  -1579       O  
ATOM   6342  CB  ARG A 772      31.029 -33.155  25.135  1.00 61.34           C  
ANISOU 6342  CB  ARG A 772     6706   9402   7199    -22    776  -1405       C  
ATOM   6343  CG  ARG A 772      31.889 -32.013  25.666  1.00 64.00           C  
ANISOU 6343  CG  ARG A 772     6932   9891   7493    -57    749  -1279       C  
ATOM   6344  CD  ARG A 772      33.355 -32.204  25.311  1.00 69.70           C  
ANISOU 6344  CD  ARG A 772     7512  10771   8201     38    824  -1328       C  
ATOM   6345  NE  ARG A 772      34.200 -31.115  25.809  1.00 70.15           N  
ANISOU 6345  NE  ARG A 772     7456  10979   8219    -14    792  -1206       N  
ATOM   6346  CZ  ARG A 772      34.628 -30.090  25.073  1.00 70.40           C  
ANISOU 6346  CZ  ARG A 772     7416  11202   8130   -130    811  -1181       C  
ATOM   6347  NH1 ARG A 772      34.294 -29.992  23.790  1.00 70.07           N  
ANISOU 6347  NH1 ARG A 772     7401  11242   7981   -202    865  -1264       N  
ATOM   6348  NH2 ARG A 772      35.396 -29.159  25.621  1.00 70.48           N  
ANISOU 6348  NH2 ARG A 772     7330  11327   8124   -184    772  -1070       N  
ATOM   6349  N   GLN A 773      27.961 -34.847  25.161  1.00 61.16           N  
ANISOU 6349  N   GLN A 773     6989   8939   7310   -101    702  -1497       N  
ATOM   6350  CA  GLN A 773      27.133 -35.795  24.414  1.00 61.97           C  
ANISOU 6350  CA  GLN A 773     7189   8926   7430   -129    716  -1631       C  
ATOM   6351  C   GLN A 773      25.648 -35.463  24.475  1.00 59.48           C  
ANISOU 6351  C   GLN A 773     6955   8551   7096   -268    644  -1571       C  
ATOM   6352  O   GLN A 773      24.835 -36.105  23.812  1.00 58.53           O  
ANISOU 6352  O   GLN A 773     6910   8356   6974   -326    640  -1672       O  
ATOM   6353  CB  GLN A 773      27.340 -37.202  24.958  1.00 64.40           C  
ANISOU 6353  CB  GLN A 773     7543   9027   7901      8    736  -1687       C  
ATOM   6354  CG  GLN A 773      28.732 -37.754  24.753  1.00 73.50           C  
ANISOU 6354  CG  GLN A 773     8619  10221   9086    169    814  -1775       C  
ATOM   6355  CD  GLN A 773      28.924 -39.062  25.483  1.00 80.44           C  
ANISOU 6355  CD  GLN A 773     9544  10873  10145    316    821  -1791       C  
ATOM   6356  OE1 GLN A 773      29.707 -39.149  26.432  1.00 84.09           O  
ANISOU 6356  OE1 GLN A 773     9941  11321  10689    434    815  -1691       O  
ATOM   6357  NE2 GLN A 773      28.189 -40.088  25.060  1.00 83.36           N  
ANISOU 6357  NE2 GLN A 773    10031  11061  10582    303    825  -1909       N  
ATOM   6358  N   LEU A 774      25.293 -34.469  25.284  1.00 57.71           N  
ANISOU 6358  N   LEU A 774     6710   8360   6858   -321    587  -1410       N  
ATOM   6359  CA  LEU A 774      23.895 -34.081  25.449  1.00 55.71           C  
ANISOU 6359  CA  LEU A 774     6516   8061   6592   -436    522  -1336       C  
ATOM   6360  C   LEU A 774      23.434 -33.234  24.271  1.00 55.83           C  
ANISOU 6360  C   LEU A 774     6525   8230   6458   -560    512  -1366       C  
ATOM   6361  O   LEU A 774      24.241 -32.554  23.629  1.00 55.79           O  
ANISOU 6361  O   LEU A 774     6460   8385   6352   -569    545  -1383       O  
ATOM   6362  CB  LEU A 774      23.693 -33.331  26.763  1.00 52.56           C  
ANISOU 6362  CB  LEU A 774     6100   7642   6229   -430    471  -1165       C  
ATOM   6363  CG  LEU A 774      24.235 -34.031  28.010  1.00 53.31           C  
ANISOU 6363  CG  LEU A 774     6189   7617   6449   -308    473  -1109       C  
ATOM   6364  CD1 LEU A 774      24.188 -33.091  29.199  1.00 51.77           C  
ANISOU 6364  CD1 LEU A 774     5969   7453   6248   -310    426   -954       C  
ATOM   6365  CD2 LEU A 774      23.481 -35.326  28.304  1.00 55.49           C  
ANISOU 6365  CD2 LEU A 774     6544   7698   6844   -289    468  -1136       C  
ATOM   6366  N   ASN A 775      22.138 -33.286  23.985  1.00 55.54           N  
ANISOU 6366  N   ASN A 775     6544   8152   6407   -659    466  -1361       N  
ATOM   6367  CA  ASN A 775      21.571 -32.512  22.887  1.00 55.31           C  
ANISOU 6367  CA  ASN A 775     6510   8266   6238   -778    444  -1372       C  
ATOM   6368  C   ASN A 775      21.731 -31.008  23.122  1.00 51.25           C  
ANISOU 6368  C   ASN A 775     5946   7876   5652   -813    416  -1230       C  
ATOM   6369  O   ASN A 775      21.508 -30.517  24.236  1.00 50.44           O  
ANISOU 6369  O   ASN A 775     5840   7713   5611   -789    381  -1107       O  
ATOM   6370  CB  ASN A 775      20.102 -32.889  22.664  1.00 57.15           C  
ANISOU 6370  CB  ASN A 775     6800   8430   6483   -873    389  -1379       C  
ATOM   6371  CG  ASN A 775      19.508 -32.216  21.445  1.00 59.25           C  
ANISOU 6371  CG  ASN A 775     7059   8853   6600   -992    359  -1397       C  
ATOM   6372  OD1 ASN A 775      18.836 -31.191  21.559  1.00 64.44           O  
ANISOU 6372  OD1 ASN A 775     7697   9575   7213  -1051    308  -1271       O  
ATOM   6373  ND2 ASN A 775      19.770 -32.774  20.271  1.00 59.86           N  
ANISOU 6373  ND2 ASN A 775     7152   8997   6594  -1020    393  -1553       N  
ATOM   6374  N   TYR A 776      22.108 -30.299  22.061  1.00 49.29           N  
ANISOU 6374  N   TYR A 776     5664   7796   5268   -871    432  -1251       N  
ATOM   6375  CA  TYR A 776      22.450 -28.876  22.112  1.00 49.66           C  
ANISOU 6375  CA  TYR A 776     5666   7959   5244   -911    412  -1127       C  
ATOM   6376  C   TYR A 776      21.322 -27.980  22.616  1.00 49.41           C  
ANISOU 6376  C   TYR A 776     5660   7892   5223   -967    337   -990       C  
ATOM   6377  O   TYR A 776      21.587 -26.955  23.235  1.00 47.78           O  
ANISOU 6377  O   TYR A 776     5434   7698   5021   -963    315   -878       O  
ATOM   6378  CB  TYR A 776      22.938 -28.387  20.739  1.00 51.11           C  
ANISOU 6378  CB  TYR A 776     5813   8333   5273   -980    444  -1171       C  
ATOM   6379  CG  TYR A 776      21.847 -28.165  19.699  1.00 49.30           C  
ANISOU 6379  CG  TYR A 776     5618   8176   4939  -1089    403  -1178       C  
ATOM   6380  CD1 TYR A 776      21.558 -26.882  19.235  1.00 46.86           C  
ANISOU 6380  CD1 TYR A 776     5292   7982   4531  -1175    361  -1057       C  
ATOM   6381  CD2 TYR A 776      21.110 -29.235  19.177  1.00 49.99           C  
ANISOU 6381  CD2 TYR A 776     5753   8216   5026  -1110    398  -1302       C  
ATOM   6382  CE1 TYR A 776      20.562 -26.664  18.278  1.00 46.94           C  
ANISOU 6382  CE1 TYR A 776     5323   8072   4439  -1270    314  -1048       C  
ATOM   6383  CE2 TYR A 776      20.104 -29.027  18.223  1.00 47.43           C  
ANISOU 6383  CE2 TYR A 776     5449   7976   4596  -1218    349  -1305       C  
ATOM   6384  CZ  TYR A 776      19.840 -27.738  17.778  1.00 47.65           C  
ANISOU 6384  CZ  TYR A 776     5451   8133   4521  -1293    307  -1173       C  
ATOM   6385  OH  TYR A 776      18.860 -27.512  16.834  1.00 48.32           O  
ANISOU 6385  OH  TYR A 776     5548   8315   4497  -1393    251  -1162       O  
ATOM   6386  N   ILE A 777      20.076 -28.363  22.341  1.00 50.30           N  
ANISOU 6386  N   ILE A 777     5813   7961   5339  -1019    298  -1004       N  
ATOM   6387  CA  ILE A 777      18.919 -27.640  22.875  1.00 48.62           C  
ANISOU 6387  CA  ILE A 777     5613   7710   5148  -1053    233   -878       C  
ATOM   6388  C   ILE A 777      18.853 -27.765  24.389  1.00 46.68           C  
ANISOU 6388  C   ILE A 777     5379   7331   5027   -973    227   -810       C  
ATOM   6389  O   ILE A 777      18.656 -26.771  25.082  1.00 47.91           O  
ANISOU 6389  O   ILE A 777     5530   7481   5191   -963    197   -698       O  
ATOM   6390  CB  ILE A 777      17.598 -28.102  22.229  1.00 49.00           C  
ANISOU 6390  CB  ILE A 777     5683   7759   5173  -1130    191   -908       C  
ATOM   6391  CG1 ILE A 777      17.514 -27.583  20.786  1.00 52.77           C  
ANISOU 6391  CG1 ILE A 777     6147   8403   5500  -1220    177   -930       C  
ATOM   6392  CG2 ILE A 777      16.395 -27.605  23.021  1.00 45.72           C  
ANISOU 6392  CG2 ILE A 777     5270   7287   4815  -1137    135   -782       C  
ATOM   6393  CD1 ILE A 777      16.540 -28.357  19.896  1.00 48.64           C  
ANISOU 6393  CD1 ILE A 777     5643   7906   4931  -1302    145  -1017       C  
ATOM   6394  N   SER A 778      19.041 -28.980  24.897  1.00 46.41           N  
ANISOU 6394  N   SER A 778     5363   7187   5085   -915    256   -878       N  
ATOM   6395  CA  SER A 778      18.972 -29.240  26.337  1.00 45.14           C  
ANISOU 6395  CA  SER A 778     5211   6905   5033   -841    252   -809       C  
ATOM   6396  C   SER A 778      20.037 -28.481  27.132  1.00 43.42           C  
ANISOU 6396  C   SER A 778     4966   6714   4817   -777    261   -748       C  
ATOM   6397  O   SER A 778      19.863 -28.243  28.328  1.00 43.74           O  
ANISOU 6397  O   SER A 778     5014   6694   4912   -732    243   -664       O  
ATOM   6398  CB  SER A 778      19.082 -30.738  26.624  1.00 45.79           C  
ANISOU 6398  CB  SER A 778     5321   6862   5215   -791    281   -889       C  
ATOM   6399  OG  SER A 778      20.436 -31.164  26.564  1.00 51.58           O  
ANISOU 6399  OG  SER A 778     6035   7602   5963   -714    330   -960       O  
ATOM   6400  N   ILE A 779      21.132 -28.101  26.471  1.00 42.05           N  
ANISOU 6400  N   ILE A 779     4756   6641   4579   -780    289   -789       N  
ATOM   6401  CA  ILE A 779      22.200 -27.342  27.142  1.00 40.70           C  
ANISOU 6401  CA  ILE A 779     4548   6510   4406   -741    291   -733       C  
ATOM   6402  C   ILE A 779      22.302 -25.860  26.752  1.00 40.63           C  
ANISOU 6402  C   ILE A 779     4527   6601   4311   -814    262   -661       C  
ATOM   6403  O   ILE A 779      23.173 -25.146  27.252  1.00 38.33           O  
ANISOU 6403  O   ILE A 779     4207   6344   4015   -803    256   -615       O  
ATOM   6404  CB  ILE A 779      23.588 -28.039  27.051  1.00 41.62           C  
ANISOU 6404  CB  ILE A 779     4616   6656   4543   -671    344   -810       C  
ATOM   6405  CG1 ILE A 779      24.015 -28.258  25.593  1.00 41.20           C  
ANISOU 6405  CG1 ILE A 779     4535   6713   4405   -711    391   -913       C  
ATOM   6406  CG2 ILE A 779      23.589 -29.343  27.872  1.00 41.39           C  
ANISOU 6406  CG2 ILE A 779     4606   6493   4628   -574    360   -840       C  
ATOM   6407  CD1 ILE A 779      25.419 -28.804  25.454  1.00 44.05           C  
ANISOU 6407  CD1 ILE A 779     4830   7128   4777   -633    452   -986       C  
ATOM   6408  N   ALA A 780      21.395 -25.403  25.888  1.00 40.53           N  
ANISOU 6408  N   ALA A 780     4534   6630   4235   -891    238   -644       N  
ATOM   6409  CA  ALA A 780      21.294 -23.988  25.513  1.00 39.97           C  
ANISOU 6409  CA  ALA A 780     4463   6630   4094   -960    202   -556       C  
ATOM   6410  C   ALA A 780      20.705 -23.152  26.656  1.00 40.80           C  
ANISOU 6410  C   ALA A 780     4603   6651   4249   -934    155   -457       C  
ATOM   6411  O   ALA A 780      19.800 -23.615  27.357  1.00 41.61           O  
ANISOU 6411  O   ALA A 780     4731   6668   4411   -892    143   -445       O  
ATOM   6412  CB  ALA A 780      20.425 -23.845  24.277  1.00 35.94           C  
ANISOU 6412  CB  ALA A 780     3963   6190   3503  -1038    185   -559       C  
ATOM   6413  N   SER A 781      21.211 -21.930  26.833  1.00 39.61           N  
ANISOU 6413  N   SER A 781     4454   6523   4073   -962    131   -388       N  
ATOM   6414  CA  SER A 781      20.598 -20.943  27.738  1.00 39.17           C  
ANISOU 6414  CA  SER A 781     4443   6391   4049   -943     84   -304       C  
ATOM   6415  C   SER A 781      19.284 -20.441  27.139  1.00 38.69           C  
ANISOU 6415  C   SER A 781     4408   6330   3964   -975     51   -249       C  
ATOM   6416  O   SER A 781      19.032 -20.653  25.949  1.00 36.10           O  
ANISOU 6416  O   SER A 781     4061   6079   3576  -1031     54   -264       O  
ATOM   6417  CB  SER A 781      21.538 -19.755  27.963  1.00 40.52           C  
ANISOU 6417  CB  SER A 781     4617   6578   4202   -980     62   -256       C  
ATOM   6418  OG  SER A 781      22.516 -20.038  28.957  1.00 42.40           O  
ANISOU 6418  OG  SER A 781     4835   6797   4478   -936     72   -285       O  
ATOM   6419  N   VAL A 782      18.442 -19.807  27.962  1.00 36.49           N  
ANISOU 6419  N   VAL A 782     4166   5974   3725   -932     19   -187       N  
ATOM   6420  CA  VAL A 782      17.206 -19.168  27.481  1.00 37.91           C  
ANISOU 6420  CA  VAL A 782     4360   6155   3889   -945    -17   -118       C  
ATOM   6421  C   VAL A 782      17.095 -17.745  28.023  1.00 39.31           C  
ANISOU 6421  C   VAL A 782     4585   6269   4082   -924    -55    -41       C  
ATOM   6422  O   VAL A 782      17.550 -17.466  29.123  1.00 41.87           O  
ANISOU 6422  O   VAL A 782     4939   6527   4444   -879    -53    -52       O  
ATOM   6423  CB  VAL A 782      15.925 -19.965  27.881  1.00 38.27           C  
ANISOU 6423  CB  VAL A 782     4393   6170   3976   -898    -14   -123       C  
ATOM   6424  CG1 VAL A 782      14.672 -19.332  27.277  1.00 37.60           C  
ANISOU 6424  CG1 VAL A 782     4302   6113   3873   -911    -55    -47       C  
ATOM   6425  CG2 VAL A 782      16.017 -21.412  27.435  1.00 38.99           C  
ANISOU 6425  CG2 VAL A 782     4453   6292   4068   -922     19   -208       C  
ATOM   6426  N   SER A 783      16.478 -16.856  27.255  1.00 41.95           N  
ANISOU 6426  N   SER A 783     4931   6619   4388   -955    -92     36       N  
ATOM   6427  CA  SER A 783      16.256 -15.469  27.668  1.00 43.87           C  
ANISOU 6427  CA  SER A 783     5231   6782   4658   -929   -131    112       C  
ATOM   6428  C   SER A 783      15.156 -14.808  26.836  1.00 45.23           C  
ANISOU 6428  C   SER A 783     5401   6971   4812   -932   -172    205       C  
ATOM   6429  O   SER A 783      14.938 -15.175  25.681  1.00 46.80           O  
ANISOU 6429  O   SER A 783     5558   7272   4952   -994   -180    222       O  
ATOM   6430  CB  SER A 783      17.549 -14.655  27.531  1.00 43.90           C  
ANISOU 6430  CB  SER A 783     5263   6774   4643   -997   -143    125       C  
ATOM   6431  OG  SER A 783      17.394 -13.370  28.104  1.00 45.95           O  
ANISOU 6431  OG  SER A 783     5593   6923   4943   -970   -182    180       O  
ATOM   6432  N   SER A 784      14.469 -13.831  27.426  1.00 46.14           N  
ANISOU 6432  N   SER A 784     5561   6993   4977   -859   -200    264       N  
ATOM   6433  CA  SER A 784      13.521 -13.006  26.688  1.00 46.57           C  
ANISOU 6433  CA  SER A 784     5617   7052   5027   -848   -246    370       C  
ATOM   6434  C   SER A 784      14.306 -12.041  25.824  1.00 47.61           C  
ANISOU 6434  C   SER A 784     5786   7183   5122   -937   -281    442       C  
ATOM   6435  O   SER A 784      15.376 -11.610  26.219  1.00 48.46           O  
ANISOU 6435  O   SER A 784     5938   7233   5241   -974   -276    418       O  
ATOM   6436  CB  SER A 784      12.637 -12.214  27.641  1.00 46.56           C  
ANISOU 6436  CB  SER A 784     5656   6939   5098   -725   -258    404       C  
ATOM   6437  OG  SER A 784      11.846 -13.078  28.423  1.00 48.99           O  
ANISOU 6437  OG  SER A 784     5919   7265   5432   -648   -222    356       O  
ATOM   6438  N   ALA A 785      13.767 -11.698  24.658  1.00 49.27           N  
ANISOU 6438  N   ALA A 785     5972   7463   5285   -977   -320    538       N  
ATOM   6439  CA  ALA A 785      14.447 -10.813  23.721  1.00 51.78           C  
ANISOU 6439  CA  ALA A 785     6319   7798   5557  -1073   -353    629       C  
ATOM   6440  C   ALA A 785      13.756  -9.459  23.615  1.00 54.31           C  
ANISOU 6440  C   ALA A 785     6694   8014   5927  -1023   -412    763       C  
ATOM   6441  O   ALA A 785      12.970  -9.215  22.689  1.00 55.75           O  
ANISOU 6441  O   ALA A 785     6846   8264   6072  -1026   -454    867       O  
ATOM   6442  CB  ALA A 785      14.530 -11.468  22.355  1.00 54.42           C  
ANISOU 6442  CB  ALA A 785     6588   8312   5779  -1171   -352    643       C  
ATOM   6443  N   ASN A 786      14.052  -8.581  24.563  1.00 54.08           N  
ANISOU 6443  N   ASN A 786     6748   7818   5981   -974   -420    758       N  
ATOM   6444  CA  ASN A 786      13.511  -7.230  24.543  1.00 57.40           C  
ANISOU 6444  CA  ASN A 786     7240   8103   6465   -918   -475    875       C  
ATOM   6445  C   ASN A 786      14.502  -6.196  24.002  1.00 58.54           C  
ANISOU 6445  C   ASN A 786     7453   8184   6607  -1033   -511    963       C  
ATOM   6446  O   ASN A 786      15.713  -6.300  24.233  1.00 57.95           O  
ANISOU 6446  O   ASN A 786     7393   8109   6515  -1128   -488    902       O  
ATOM   6447  CB  ASN A 786      13.034  -6.837  25.939  1.00 58.02           C  
ANISOU 6447  CB  ASN A 786     7379   8023   6644   -777   -463    810       C  
ATOM   6448  CG  ASN A 786      12.039  -7.828  26.509  1.00 58.70           C  
ANISOU 6448  CG  ASN A 786     7391   8180   6734   -671   -422    739       C  
ATOM   6449  OD1 ASN A 786      11.145  -8.287  25.800  1.00 56.38           O  
ANISOU 6449  OD1 ASN A 786     7016   7999   6406   -656   -434    793       O  
ATOM   6450  ND2 ASN A 786      12.196  -8.174  27.796  1.00 55.03           N  
ANISOU 6450  ND2 ASN A 786     6948   7657   6303   -605   -378    623       N  
ATOM   6451  N   ASN A 787      13.969  -5.211  23.278  1.00 59.89           N  
ANISOU 6451  N   ASN A 787     7658   8305   6794  -1026   -569   1117       N  
ATOM   6452  CA  ASN A 787      14.733  -4.070  22.752  1.00 61.51           C  
ANISOU 6452  CA  ASN A 787     7938   8422   7011  -1131   -613   1235       C  
ATOM   6453  C   ASN A 787      15.758  -4.400  21.661  1.00 61.63           C  
ANISOU 6453  C   ASN A 787     7901   8605   6910  -1309   -601   1279       C  
ATOM   6454  O   ASN A 787      16.736  -3.671  21.492  1.00 64.15           O  
ANISOU 6454  O   ASN A 787     8272   8866   7238  -1424   -616   1337       O  
ATOM   6455  CB  ASN A 787      15.411  -3.299  23.894  1.00 61.42           C  
ANISOU 6455  CB  ASN A 787     8036   8200   7101  -1123   -617   1169       C  
ATOM   6456  CG  ASN A 787      14.418  -2.748  24.902  1.00 64.72           C  
ANISOU 6456  CG  ASN A 787     8523   8439   7628   -943   -629   1135       C  
ATOM   6457  OD1 ASN A 787      13.379  -2.189  24.532  1.00 63.62           O  
ANISOU 6457  OD1 ASN A 787     8393   8250   7528   -846   -666   1244       O  
ATOM   6458  ND2 ASN A 787      14.741  -2.891  26.190  1.00 64.16           N  
ANISOU 6458  ND2 ASN A 787     8496   8280   7603   -893   -597    986       N  
ATOM   6459  N   ILE A 788      15.532  -5.481  20.915  1.00 60.21           N  
ANISOU 6459  N   ILE A 788     7619   8637   6620  -1336   -572   1251       N  
ATOM   6460  CA  ILE A 788      16.463  -5.906  19.859  1.00 60.20           C  
ANISOU 6460  CA  ILE A 788     7559   8822   6491  -1490   -547   1272       C  
ATOM   6461  C   ILE A 788      16.861  -4.743  18.945  1.00 63.50           C  
ANISOU 6461  C   ILE A 788     8021   9223   6883  -1601   -597   1462       C  
ATOM   6462  O   ILE A 788      18.030  -4.610  18.581  1.00 65.12           O  
ANISOU 6462  O   ILE A 788     8218   9488   7036  -1738   -573   1480       O  
ATOM   6463  CB  ILE A 788      15.896  -7.071  19.016  1.00 59.42           C  
ANISOU 6463  CB  ILE A 788     7361   8942   6274  -1493   -526   1233       C  
ATOM   6464  CG1 ILE A 788      15.471  -8.232  19.922  1.00 57.00           C  
ANISOU 6464  CG1 ILE A 788     7015   8637   6004  -1393   -480   1060       C  
ATOM   6465  CG2 ILE A 788      16.917  -7.545  17.980  1.00 56.96           C  
ANISOU 6465  CG2 ILE A 788     6993   8829   5821  -1641   -486   1228       C  
ATOM   6466  CD1 ILE A 788      14.497  -9.195  19.267  1.00 60.43           C  
ANISOU 6466  CD1 ILE A 788     7370   9227   6362  -1369   -483   1035       C  
ATOM   6467  N   ALA A 789      15.890  -3.897  18.603  1.00 65.73           N  
ANISOU 6467  N   ALA A 789     8346   9424   7206  -1538   -664   1611       N  
ATOM   6468  CA  ALA A 789      16.122  -2.736  17.741  1.00 66.78           C  
ANISOU 6468  CA  ALA A 789     8529   9518   7326  -1631   -722   1819       C  
ATOM   6469  C   ALA A 789      17.072  -1.714  18.357  1.00 66.62           C  
ANISOU 6469  C   ALA A 789     8611   9293   7409  -1699   -734   1846       C  
ATOM   6470  O   ALA A 789      17.913  -1.160  17.651  1.00 68.06           O  
ANISOU 6470  O   ALA A 789     8806   9510   7544  -1853   -746   1966       O  
ATOM   6471  CB  ALA A 789      14.803  -2.074  17.375  1.00 68.64           C  
ANISOU 6471  CB  ALA A 789     8788   9690   7603  -1519   -796   1970       C  
ATOM   6472  N   LYS A 790      16.936  -1.470  19.662  1.00 64.56           N  
ANISOU 6472  N   LYS A 790     8421   8826   7282  -1595   -734   1734       N  
ATOM   6473  CA  LYS A 790      17.768  -0.490  20.378  1.00 65.22           C  
ANISOU 6473  CA  LYS A 790     8614   8694   7473  -1655   -755   1735       C  
ATOM   6474  C   LYS A 790      19.273  -0.762  20.234  1.00 64.26           C  
ANISOU 6474  C   LYS A 790     8450   8679   7285  -1840   -715   1694       C  
ATOM   6475  O   LYS A 790      20.075   0.170  20.160  1.00 63.91           O  
ANISOU 6475  O   LYS A 790     8471   8528   7284  -1967   -748   1783       O  
ATOM   6476  CB  LYS A 790      17.394  -0.441  21.870  1.00 64.78           C  
ANISOU 6476  CB  LYS A 790     8625   8448   7539  -1507   -748   1576       C  
ATOM   6477  CG  LYS A 790      18.045   0.717  22.640  1.00 67.18           C  
ANISOU 6477  CG  LYS A 790     9065   8495   7964  -1554   -788   1574       C  
ATOM   6478  CD  LYS A 790      18.393   0.356  24.088  1.00 65.82           C  
ANISOU 6478  CD  LYS A 790     8921   8243   7843  -1496   -755   1363       C  
ATOM   6479  CE  LYS A 790      17.253   0.650  25.061  1.00 65.30           C  
ANISOU 6479  CE  LYS A 790     8930   8006   7877  -1286   -763   1290       C  
ATOM   6480  NZ  LYS A 790      17.736   0.703  26.483  1.00 62.00           N  
ANISOU 6480  NZ  LYS A 790     8580   7463   7514  -1256   -750   1111       N  
ATOM   6481  N   TYR A 791      19.640  -2.040  20.190  1.00 62.38           N  
ANISOU 6481  N   TYR A 791     8102   8651   6950  -1852   -646   1562       N  
ATOM   6482  CA  TYR A 791      21.041  -2.449  20.137  1.00 61.82           C  
ANISOU 6482  CA  TYR A 791     7968   8703   6817  -1998   -597   1502       C  
ATOM   6483  C   TYR A 791      21.529  -2.870  18.741  1.00 62.21           C  
ANISOU 6483  C   TYR A 791     7917   9010   6708  -2126   -561   1589       C  
ATOM   6484  O   TYR A 791      22.705  -3.201  18.568  1.00 61.98           O  
ANISOU 6484  O   TYR A 791     7821   9111   6619  -2245   -513   1552       O  
ATOM   6485  CB  TYR A 791      21.306  -3.546  21.183  1.00 58.96           C  
ANISOU 6485  CB  TYR A 791     7558   8378   6467  -1920   -540   1287       C  
ATOM   6486  CG  TYR A 791      21.132  -3.060  22.611  1.00 57.02           C  
ANISOU 6486  CG  TYR A 791     7410   7900   6356  -1828   -569   1197       C  
ATOM   6487  CD1 TYR A 791      20.010  -3.417  23.370  1.00 56.71           C  
ANISOU 6487  CD1 TYR A 791     7395   7783   6368  -1649   -566   1111       C  
ATOM   6488  CD2 TYR A 791      22.077  -2.221  23.197  1.00 52.66           C  
ANISOU 6488  CD2 TYR A 791     6924   7211   5873  -1927   -600   1197       C  
ATOM   6489  CE1 TYR A 791      19.854  -2.956  24.692  1.00 54.28           C  
ANISOU 6489  CE1 TYR A 791     7179   7276   6167  -1561   -587   1021       C  
ATOM   6490  CE2 TYR A 791      21.928  -1.760  24.499  1.00 52.25           C  
ANISOU 6490  CE2 TYR A 791     6970   6952   5929  -1847   -630   1101       C  
ATOM   6491  CZ  TYR A 791      20.825  -2.124  25.239  1.00 54.61           C  
ANISOU 6491  CZ  TYR A 791     7296   7185   6268  -1660   -619   1011       C  
ATOM   6492  OH  TYR A 791      20.708  -1.653  26.525  1.00 58.78           O  
ANISOU 6492  OH  TYR A 791     7922   7525   6887  -1582   -642    910       O  
ATOM   6493  N   ASP A 792      20.631  -2.836  17.755  1.00 62.75           N  
ANISOU 6493  N   ASP A 792     7972   9164   6706  -2099   -586   1706       N  
ATOM   6494  CA  ASP A 792      20.948  -3.243  16.386  1.00 64.31           C  
ANISOU 6494  CA  ASP A 792     8080   9622   6732  -2209   -555   1785       C  
ATOM   6495  C   ASP A 792      21.558  -2.083  15.601  1.00 66.53           C  
ANISOU 6495  C   ASP A 792     8396   9891   6989  -2370   -592   2001       C  
ATOM   6496  O   ASP A 792      20.865  -1.120  15.264  1.00 67.38           O  
ANISOU 6496  O   ASP A 792     8580   9877   7143  -2355   -666   2174       O  
ATOM   6497  CB  ASP A 792      19.690  -3.777  15.681  1.00 65.29           C  
ANISOU 6497  CB  ASP A 792     8169   9863   6776  -2116   -573   1808       C  
ATOM   6498  CG  ASP A 792      19.981  -4.378  14.296  1.00 71.31           C  
ANISOU 6498  CG  ASP A 792     8837  10921   7337  -2222   -535   1850       C  
ATOM   6499  OD1 ASP A 792      21.038  -4.068  13.694  1.00 73.95           O  
ANISOU 6499  OD1 ASP A 792     9144  11361   7593  -2372   -506   1927       O  
ATOM   6500  OD2 ASP A 792      19.137  -5.166  13.801  1.00 70.86           O  
ANISOU 6500  OD2 ASP A 792     8730  11000   7194  -2159   -535   1803       O  
ATOM   6501  N   VAL A 793      22.855  -2.185  15.315  1.00 67.04           N  
ANISOU 6501  N   VAL A 793     8400  10086   6986  -2522   -539   1998       N  
ATOM   6502  CA  VAL A 793      23.570  -1.168  14.542  1.00 68.74           C  
ANISOU 6502  CA  VAL A 793     8631  10320   7165  -2702   -562   2207       C  
ATOM   6503  C   VAL A 793      24.125  -1.774  13.247  1.00 69.84           C  
ANISOU 6503  C   VAL A 793     8649  10793   7093  -2817   -494   2253       C  
ATOM   6504  O   VAL A 793      25.244  -2.302  13.220  1.00 70.32           O  
ANISOU 6504  O   VAL A 793     8618  11012   7090  -2904   -416   2167       O  
ATOM   6505  CB  VAL A 793      24.699  -0.496  15.370  1.00 69.53           C  
ANISOU 6505  CB  VAL A 793     8769  10268   7382  -2812   -568   2196       C  
ATOM   6506  CG1 VAL A 793      25.421   0.588  14.542  1.00 72.88           C  
ANISOU 6506  CG1 VAL A 793     9208  10706   7775  -3018   -596   2432       C  
ATOM   6507  CG2 VAL A 793      24.136   0.104  16.651  1.00 67.73           C  
ANISOU 6507  CG2 VAL A 793     8671   9715   7348  -2695   -635   2132       C  
ATOM   6508  N   GLY A 794      23.326  -1.697  12.181  1.00 70.11           N  
ANISOU 6508  N   GLY A 794     8680  10944   7015  -2810   -523   2386       N  
ATOM   6509  CA  GLY A 794      23.682  -2.277  10.883  1.00 69.45           C  
ANISOU 6509  CA  GLY A 794     8490  11191   6707  -2906   -462   2425       C  
ATOM   6510  C   GLY A 794      23.934  -3.772  10.951  1.00 67.55           C  
ANISOU 6510  C   GLY A 794     8146  11147   6372  -2842   -367   2176       C  
ATOM   6511  O   GLY A 794      24.800  -4.304  10.246  1.00 66.08           O  
ANISOU 6511  O   GLY A 794     7861  11213   6032  -2936   -283   2143       O  
ATOM   6512  N   GLY A 795      23.176  -4.443  11.817  1.00 66.52           N  
ANISOU 6512  N   GLY A 795     8040  10897   6338  -2678   -377   2004       N  
ATOM   6513  CA  GLY A 795      23.323  -5.877  12.044  1.00 63.41           C  
ANISOU 6513  CA  GLY A 795     7568  10635   5892  -2601   -297   1763       C  
ATOM   6514  C   GLY A 795      24.333  -6.223  13.120  1.00 59.91           C  
ANISOU 6514  C   GLY A 795     7097  10114   5550  -2591   -242   1612       C  
ATOM   6515  O   GLY A 795      24.466  -7.387  13.495  1.00 58.40           O  
ANISOU 6515  O   GLY A 795     6852   9988   5349  -2509   -181   1414       O  
ATOM   6516  N   PHE A 796      25.040  -5.213  13.621  1.00 58.77           N  
ANISOU 6516  N   PHE A 796     6994   9829   5508  -2677   -270   1710       N  
ATOM   6517  CA  PHE A 796      26.084  -5.428  14.620  1.00 56.83           C  
ANISOU 6517  CA  PHE A 796     6715   9526   5352  -2689   -230   1587       C  
ATOM   6518  C   PHE A 796      25.717  -4.818  15.971  1.00 56.45           C  
ANISOU 6518  C   PHE A 796     6775   9174   5499  -2612   -301   1559       C  
ATOM   6519  O   PHE A 796      24.905  -3.890  16.020  1.00 57.33           O  
ANISOU 6519  O   PHE A 796     6992   9107   5684  -2591   -381   1683       O  
ATOM   6520  CB  PHE A 796      27.413  -4.880  14.111  1.00 56.03           C  
ANISOU 6520  CB  PHE A 796     6547   9551   5190  -2875   -194   1696       C  
ATOM   6521  CG  PHE A 796      28.025  -5.702  13.011  1.00 56.78           C  
ANISOU 6521  CG  PHE A 796     6512   9972   5091  -2932    -94   1663       C  
ATOM   6522  CD1 PHE A 796      28.748  -6.859  13.308  1.00 54.75           C  
ANISOU 6522  CD1 PHE A 796     6149   9850   4803  -2877     -3   1466       C  
ATOM   6523  CD2 PHE A 796      27.888  -5.315  11.670  1.00 56.11           C  
ANISOU 6523  CD2 PHE A 796     6408  10062   4848  -3035    -90   1831       C  
ATOM   6524  CE1 PHE A 796      29.330  -7.622  12.284  1.00 57.59           C  
ANISOU 6524  CE1 PHE A 796     6390  10510   4982  -2916     98   1420       C  
ATOM   6525  CE2 PHE A 796      28.459  -6.069  10.635  1.00 53.39           C  
ANISOU 6525  CE2 PHE A 796     5946  10035   4307  -3085      9   1789       C  
ATOM   6526  CZ  PHE A 796      29.185  -7.219  10.936  1.00 56.50           C  
ANISOU 6526  CZ  PHE A 796     6236  10556   4674  -3023    107   1576       C  
ATOM   6527  N   PRO A 797      26.309  -5.342  17.072  1.00 55.89           N  
ANISOU 6527  N   PRO A 797     6679   9049   5509  -2563   -272   1396       N  
ATOM   6528  CA  PRO A 797      25.966  -4.908  18.438  1.00 55.07           C  
ANISOU 6528  CA  PRO A 797     6675   8680   5571  -2478   -331   1337       C  
ATOM   6529  C   PRO A 797      26.365  -3.477  18.736  1.00 56.95           C  
ANISOU 6529  C   PRO A 797     7002   8730   5906  -2593   -403   1471       C  
ATOM   6530  O   PRO A 797      27.527  -3.104  18.553  1.00 58.69           O  
ANISOU 6530  O   PRO A 797     7173   9020   6108  -2749   -389   1526       O  
ATOM   6531  CB  PRO A 797      26.764  -5.864  19.334  1.00 53.08           C  
ANISOU 6531  CB  PRO A 797     6347   8480   5340  -2433   -276   1151       C  
ATOM   6532  CG  PRO A 797      27.115  -7.019  18.462  1.00 53.72           C  
ANISOU 6532  CG  PRO A 797     6303   8826   5282  -2432   -186   1084       C  
ATOM   6533  CD  PRO A 797      27.279  -6.452  17.090  1.00 55.01           C  
ANISOU 6533  CD  PRO A 797     6440   9132   5327  -2567   -180   1251       C  
ATOM   6534  N   GLY A 798      25.398  -2.687  19.193  1.00 57.88           N  
ANISOU 6534  N   GLY A 798     7249   8611   6130  -2515   -478   1522       N  
ATOM   6535  CA  GLY A 798      25.654  -1.314  19.632  1.00 59.30           C  
ANISOU 6535  CA  GLY A 798     7544   8557   6430  -2601   -554   1625       C  
ATOM   6536  C   GLY A 798      26.170  -1.265  21.061  1.00 58.16           C  
ANISOU 6536  C   GLY A 798     7438   8264   6395  -2578   -571   1476       C  
ATOM   6537  O   GLY A 798      26.395  -2.307  21.672  1.00 56.13           O  
ANISOU 6537  O   GLY A 798     7108   8102   6115  -2499   -520   1310       O  
ATOM   6538  N   PRO A 799      26.359  -0.049  21.607  1.00 59.79           N  
ANISOU 6538  N   PRO A 799     7766   8233   6720  -2647   -646   1534       N  
ATOM   6539  CA  PRO A 799      26.924   0.079  22.949  1.00 59.89           C  
ANISOU 6539  CA  PRO A 799     7820   8114   6823  -2647   -671   1391       C  
ATOM   6540  C   PRO A 799      26.033  -0.588  23.990  1.00 58.77           C  
ANISOU 6540  C   PRO A 799     7713   7898   6718  -2432   -659   1219       C  
ATOM   6541  O   PRO A 799      24.807  -0.475  23.908  1.00 57.90           O  
ANISOU 6541  O   PRO A 799     7670   7695   6636  -2291   -672   1242       O  
ATOM   6542  CB  PRO A 799      26.965   1.595  23.174  1.00 62.81           C  
ANISOU 6542  CB  PRO A 799     8343   8209   7314  -2743   -762   1497       C  
ATOM   6543  CG  PRO A 799      26.871   2.196  21.806  1.00 63.65           C  
ANISOU 6543  CG  PRO A 799     8447   8361   7376  -2852   -774   1724       C  
ATOM   6544  CD  PRO A 799      26.020   1.263  21.026  1.00 61.02           C  
ANISOU 6544  CD  PRO A 799     8033   8218   6933  -2723   -716   1731       C  
ATOM   6545  N   LYS A 800      26.658  -1.297  24.933  1.00 58.19           N  
ANISOU 6545  N   LYS A 800     7585   7885   6642  -2409   -633   1060       N  
ATOM   6546  CA  LYS A 800      25.963  -1.991  26.032  1.00 57.17           C  
ANISOU 6546  CA  LYS A 800     7479   7704   6540  -2221   -617    896       C  
ATOM   6547  C   LYS A 800      25.049  -3.156  25.610  1.00 53.93           C  
ANISOU 6547  C   LYS A 800     6996   7436   6061  -2072   -553    860       C  
ATOM   6548  O   LYS A 800      24.201  -3.587  26.389  1.00 53.58           O  
ANISOU 6548  O   LYS A 800     6985   7328   6046  -1912   -544    762       O  
ATOM   6549  CB  LYS A 800      25.189  -0.991  26.911  1.00 57.78           C  
ANISOU 6549  CB  LYS A 800     7724   7499   6730  -2136   -683    872       C  
ATOM   6550  CG  LYS A 800      26.007  -0.361  28.029  1.00 63.21           C  
ANISOU 6550  CG  LYS A 800     8484   8049   7484  -2214   -737    785       C  
ATOM   6551  CD  LYS A 800      26.177  -1.307  29.233  1.00 65.86           C  
ANISOU 6551  CD  LYS A 800     8774   8454   7796  -2114   -708    603       C  
ATOM   6552  CE  LYS A 800      25.035  -1.180  30.242  1.00 65.38           C  
ANISOU 6552  CE  LYS A 800     8827   8228   7787  -1923   -718    503       C  
ATOM   6553  NZ  LYS A 800      24.901  -2.412  31.068  1.00 65.36           N  
ANISOU 6553  NZ  LYS A 800     8749   8352   7732  -1797   -665    367       N  
ATOM   6554  N   CYS A 801      25.236  -3.673  24.396  1.00 52.45           N  
ANISOU 6554  N   CYS A 801     6706   7446   5776  -2132   -507    934       N  
ATOM   6555  CA  CYS A 801      24.418  -4.774  23.880  1.00 50.94           C  
ANISOU 6555  CA  CYS A 801     6447   7395   5513  -2017   -453    897       C  
ATOM   6556  C   CYS A 801      24.507  -6.045  24.729  1.00 48.84           C  
ANISOU 6556  C   CYS A 801     6117   7202   5238  -1910   -401    727       C  
ATOM   6557  O   CYS A 801      25.567  -6.646  24.830  1.00 50.79           O  
ANISOU 6557  O   CYS A 801     6275   7575   5449  -1967   -363    665       O  
ATOM   6558  CB  CYS A 801      24.795  -5.093  22.432  1.00 51.78           C  
ANISOU 6558  CB  CYS A 801     6457   7717   5501  -2120   -412    990       C  
ATOM   6559  SG  CYS A 801      23.904  -6.501  21.719  1.00 49.97           S  
ANISOU 6559  SG  CYS A 801     6144   7671   5170  -2006   -350    925       S  
ATOM   6560  N   PRO A 802      23.382  -6.465  25.332  1.00 48.97           N  
ANISOU 6560  N   PRO A 802     6171   7144   5290  -1752   -399    659       N  
ATOM   6561  CA  PRO A 802      23.361  -7.690  26.138  1.00 46.63           C  
ANISOU 6561  CA  PRO A 802     5821   6907   4989  -1648   -352    516       C  
ATOM   6562  C   PRO A 802      23.802  -8.912  25.334  1.00 47.66           C  
ANISOU 6562  C   PRO A 802     5829   7251   5030  -1671   -284    478       C  
ATOM   6563  O   PRO A 802      23.621  -8.960  24.112  1.00 48.47           O  
ANISOU 6563  O   PRO A 802     5895   7460   5060  -1723   -270    551       O  
ATOM   6564  CB  PRO A 802      21.895  -7.822  26.534  1.00 43.16           C  
ANISOU 6564  CB  PRO A 802     5435   6375   4588  -1497   -360    498       C  
ATOM   6565  CG  PRO A 802      21.375  -6.451  26.491  1.00 46.59           C  
ANISOU 6565  CG  PRO A 802     5977   6644   5082  -1502   -422    597       C  
ATOM   6566  CD  PRO A 802      22.061  -5.816  25.312  1.00 48.73           C  
ANISOU 6566  CD  PRO A 802     6231   6975   5310  -1658   -440    723       C  
ATOM   6567  N   PHE A 803      24.389  -9.879  26.036  1.00 46.99           N  
ANISOU 6567  N   PHE A 803     5684   7223   4946  -1627   -245    363       N  
ATOM   6568  CA  PHE A 803      24.936 -11.090  25.434  1.00 45.51           C  
ANISOU 6568  CA  PHE A 803     5385   7217   4689  -1632   -177    303       C  
ATOM   6569  C   PHE A 803      23.913 -11.780  24.550  1.00 46.51           C  
ANISOU 6569  C   PHE A 803     5497   7412   4764  -1580   -149    303       C  
ATOM   6570  O   PHE A 803      24.233 -12.225  23.448  1.00 47.14           O  
ANISOU 6570  O   PHE A 803     5509   7644   4757  -1636   -108    310       O  
ATOM   6571  CB  PHE A 803      25.382 -12.033  26.547  1.00 44.40           C  
ANISOU 6571  CB  PHE A 803     5207   7078   4585  -1548   -151    184       C  
ATOM   6572  CG  PHE A 803      26.142 -13.241  26.074  1.00 42.96           C  
ANISOU 6572  CG  PHE A 803     4912   7060   4351  -1542    -81    114       C  
ATOM   6573  CD1 PHE A 803      27.491 -13.152  25.760  1.00 41.27           C  
ANISOU 6573  CD1 PHE A 803     4612   6965   4104  -1634    -59    122       C  
ATOM   6574  CD2 PHE A 803      25.518 -14.483  25.993  1.00 38.27           C  
ANISOU 6574  CD2 PHE A 803     4295   6496   3749  -1442    -37     36       C  
ATOM   6575  CE1 PHE A 803      28.210 -14.278  25.349  1.00 39.58           C  
ANISOU 6575  CE1 PHE A 803     4289   6902   3847  -1607     13     49       C  
ATOM   6576  CE2 PHE A 803      26.227 -15.604  25.587  1.00 36.54           C  
ANISOU 6576  CE2 PHE A 803     3983   6406   3494  -1423     28    -40       C  
ATOM   6577  CZ  PHE A 803      27.581 -15.499  25.269  1.00 36.66           C  
ANISOU 6577  CZ  PHE A 803     3911   6543   3474  -1496     56    -36       C  
ATOM   6578  N   HIS A 804      22.678 -11.861  25.037  1.00 46.41           N  
ANISOU 6578  N   HIS A 804     5541   7295   4797  -1477   -171    293       N  
ATOM   6579  CA  HIS A 804      21.639 -12.597  24.334  1.00 45.13           C  
ANISOU 6579  CA  HIS A 804     5358   7195   4593  -1429   -154    283       C  
ATOM   6580  C   HIS A 804      21.137 -11.861  23.090  1.00 46.20           C  
ANISOU 6580  C   HIS A 804     5507   7379   4667  -1499   -185    405       C  
ATOM   6581  O   HIS A 804      20.687 -12.496  22.128  1.00 45.25           O  
ANISOU 6581  O   HIS A 804     5343   7378   4469  -1510   -166    399       O  
ATOM   6582  CB  HIS A 804      20.502 -13.011  25.279  1.00 41.90           C  
ANISOU 6582  CB  HIS A 804     4985   6683   4251  -1302   -162    237       C  
ATOM   6583  CG  HIS A 804      19.677 -11.873  25.799  1.00 41.10           C  
ANISOU 6583  CG  HIS A 804     4968   6437   4213  -1257   -217    312       C  
ATOM   6584  ND1 HIS A 804      20.157 -10.950  26.705  1.00 40.36           N  
ANISOU 6584  ND1 HIS A 804     4938   6218   4177  -1258   -247    319       N  
ATOM   6585  CD2 HIS A 804      18.385 -11.537  25.569  1.00 38.49           C  
ANISOU 6585  CD2 HIS A 804     4663   6065   3897  -1199   -247    374       C  
ATOM   6586  CE1 HIS A 804      19.203 -10.082  26.992  1.00 42.48           C  
ANISOU 6586  CE1 HIS A 804     5279   6365   4496  -1197   -288    375       C  
ATOM   6587  NE2 HIS A 804      18.118 -10.413  26.314  1.00 39.10           N  
ANISOU 6587  NE2 HIS A 804     4822   5989   4045  -1155   -287    416       N  
ATOM   6588  N   ILE A 805      21.239 -10.533  23.107  1.00 46.35           N  
ANISOU 6588  N   ILE A 805     5588   7305   4718  -1550   -236    514       N  
ATOM   6589  CA  ILE A 805      20.902  -9.722  21.936  1.00 47.27           C  
ANISOU 6589  CA  ILE A 805     5720   7462   4778  -1625   -272    656       C  
ATOM   6590  C   ILE A 805      22.023  -9.823  20.903  1.00 47.82           C  
ANISOU 6590  C   ILE A 805     5721   7705   4743  -1758   -234    686       C  
ATOM   6591  O   ILE A 805      21.763  -9.954  19.707  1.00 48.52           O  
ANISOU 6591  O   ILE A 805     5776   7931   4729  -1809   -228    744       O  
ATOM   6592  CB  ILE A 805      20.647  -8.241  22.306  1.00 49.19           C  
ANISOU 6592  CB  ILE A 805     6063   7523   5105  -1632   -341    772       C  
ATOM   6593  CG1 ILE A 805      19.631  -8.124  23.454  1.00 48.25           C  
ANISOU 6593  CG1 ILE A 805     6008   7237   5088  -1485   -365    724       C  
ATOM   6594  CG2 ILE A 805      20.214  -7.436  21.068  1.00 48.10           C  
ANISOU 6594  CG2 ILE A 805     5941   7423   4912  -1699   -383    940       C  
ATOM   6595  CD1 ILE A 805      18.196  -8.538  23.096  1.00 46.04           C  
ANISOU 6595  CD1 ILE A 805     5709   6989   4795  -1387   -374    745       C  
ATOM   6596  N   ARG A 806      23.266  -9.774  21.380  1.00 48.16           N  
ANISOU 6596  N   ARG A 806     5738   7755   4806  -1815   -209    644       N  
ATOM   6597  CA  ARG A 806      24.441 -10.046  20.549  1.00 48.90           C  
ANISOU 6597  CA  ARG A 806     5742   8035   4802  -1927   -155    648       C  
ATOM   6598  C   ARG A 806      24.228 -11.337  19.762  1.00 48.08           C  
ANISOU 6598  C   ARG A 806     5564   8107   4598  -1890    -92    556       C  
ATOM   6599  O   ARG A 806      24.423 -11.371  18.547  1.00 51.16           O  
ANISOU 6599  O   ARG A 806     5908   8663   4868  -1969    -65    606       O  
ATOM   6600  CB  ARG A 806      25.700 -10.148  21.415  1.00 47.17           C  
ANISOU 6600  CB  ARG A 806     5481   7808   4633  -1954   -132    578       C  
ATOM   6601  CG  ARG A 806      26.967 -10.448  20.636  1.00 47.54           C  
ANISOU 6601  CG  ARG A 806     5416   8061   4587  -2058    -68    579       C  
ATOM   6602  CD  ARG A 806      28.199 -10.432  21.531  1.00 46.76           C  
ANISOU 6602  CD  ARG A 806     5266   7957   4545  -2089    -59    528       C  
ATOM   6603  NE  ARG A 806      28.504  -9.094  22.024  1.00 49.52           N  
ANISOU 6603  NE  ARG A 806     5682   8168   4966  -2186   -132    629       N  
ATOM   6604  CZ  ARG A 806      29.488  -8.324  21.566  1.00 55.52           C  
ANISOU 6604  CZ  ARG A 806     6399   8998   5698  -2345   -136    730       C  
ATOM   6605  NH1 ARG A 806      30.292  -8.754  20.601  1.00 61.00           N  
ANISOU 6605  NH1 ARG A 806     6971   9920   6285  -2418    -63    746       N  
ATOM   6606  NH2 ARG A 806      29.680  -7.120  22.082  1.00 57.16           N  
ANISOU 6606  NH2 ARG A 806     6685   9047   5986  -2435   -211    812       N  
ATOM   6607  N   GLY A 807      23.797 -12.379  20.471  1.00 45.68           N  
ANISOU 6607  N   GLY A 807     5255   7762   4342  -1771    -70    423       N  
ATOM   6608  CA  GLY A 807      23.440 -13.658  19.869  1.00 44.57           C  
ANISOU 6608  CA  GLY A 807     5065   7742   4130  -1725    -19    318       C  
ATOM   6609  C   GLY A 807      22.378 -13.557  18.794  1.00 44.93           C  
ANISOU 6609  C   GLY A 807     5127   7854   4090  -1747    -49    383       C  
ATOM   6610  O   GLY A 807      22.464 -14.236  17.768  1.00 47.69           O  
ANISOU 6610  O   GLY A 807     5427   8370   4323  -1782     -8    337       O  
ATOM   6611  N   ILE A 808      21.376 -12.712  19.019  1.00 44.58           N  
ANISOU 6611  N   ILE A 808     5150   7687   4099  -1723   -121    488       N  
ATOM   6612  CA  ILE A 808      20.299 -12.541  18.040  1.00 46.67           C  
ANISOU 6612  CA  ILE A 808     5425   8018   4290  -1738   -163    570       C  
ATOM   6613  C   ILE A 808      20.836 -11.828  16.800  1.00 48.26           C  
ANISOU 6613  C   ILE A 808     5607   8362   4368  -1867   -166    695       C  
ATOM   6614  O   ILE A 808      20.508 -12.192  15.666  1.00 45.01           O  
ANISOU 6614  O   ILE A 808     5161   8116   3825  -1911   -161    706       O  
ATOM   6615  CB  ILE A 808      19.094 -11.773  18.627  1.00 45.50           C  
ANISOU 6615  CB  ILE A 808     5344   7705   4240  -1662   -238    659       C  
ATOM   6616  CG1 ILE A 808      18.433 -12.601  19.730  1.00 42.46           C  
ANISOU 6616  CG1 ILE A 808     4964   7219   3951  -1541   -227    540       C  
ATOM   6617  CG2 ILE A 808      18.085 -11.429  17.522  1.00 47.67           C  
ANISOU 6617  CG2 ILE A 808     5616   8066   4432  -1688   -293    777       C  
ATOM   6618  CD1 ILE A 808      17.419 -11.839  20.545  1.00 41.01           C  
ANISOU 6618  CD1 ILE A 808     4839   6868   3874  -1449   -283    608       C  
ATOM   6619  N   LEU A 809      21.679 -10.825  17.037  1.00 49.00           N  
ANISOU 6619  N   LEU A 809     5723   8396   4501  -1935   -176    789       N  
ATOM   6620  CA  LEU A 809      22.289 -10.063  15.962  1.00 52.56           C  
ANISOU 6620  CA  LEU A 809     6154   8971   4845  -2070   -177    929       C  
ATOM   6621  C   LEU A 809      23.241 -10.923  15.141  1.00 53.85           C  
ANISOU 6621  C   LEU A 809     6222   9369   4867  -2135    -88    842       C  
ATOM   6622  O   LEU A 809      23.388 -10.717  13.938  1.00 56.31           O  
ANISOU 6622  O   LEU A 809     6502   9858   5034  -2230    -76    928       O  
ATOM   6623  CB  LEU A 809      22.989  -8.822  16.516  1.00 52.66           C  
ANISOU 6623  CB  LEU A 809     6215   8843   4951  -2137   -211   1042       C  
ATOM   6624  CG  LEU A 809      22.020  -7.805  17.129  1.00 53.85           C  
ANISOU 6624  CG  LEU A 809     6472   8763   5226  -2075   -300   1143       C  
ATOM   6625  CD1 LEU A 809      22.777  -6.682  17.828  1.00 53.97           C  
ANISOU 6625  CD1 LEU A 809     6546   8611   5347  -2139   -332   1215       C  
ATOM   6626  CD2 LEU A 809      21.055  -7.249  16.074  1.00 53.46           C  
ANISOU 6626  CD2 LEU A 809     6446   8759   5107  -2093   -357   1304       C  
ATOM   6627  N   THR A 810      23.870 -11.895  15.795  1.00 53.65           N  
ANISOU 6627  N   THR A 810     6152   9351   4882  -2077    -24    674       N  
ATOM   6628  CA  THR A 810      24.671 -12.892  15.097  1.00 54.87           C  
ANISOU 6628  CA  THR A 810     6216   9716   4916  -2099     69    557       C  
ATOM   6629  C   THR A 810      23.770 -13.796  14.254  1.00 54.69           C  
ANISOU 6629  C   THR A 810     6188   9805   4786  -2065     77    477       C  
ATOM   6630  O   THR A 810      24.119 -14.145  13.128  1.00 57.50           O  
ANISOU 6630  O   THR A 810     6492  10372   4982  -2127    128    456       O  
ATOM   6631  CB  THR A 810      25.476 -13.741  16.080  1.00 54.97           C  
ANISOU 6631  CB  THR A 810     6184   9683   5017  -2022    127    400       C  
ATOM   6632  OG1 THR A 810      26.198 -12.882  16.966  1.00 60.15           O  
ANISOU 6632  OG1 THR A 810     6850  10225   5777  -2056    101    470       O  
ATOM   6633  CG2 THR A 810      26.459 -14.623  15.346  1.00 55.54           C  
ANISOU 6633  CG2 THR A 810     6157   9972   4974  -2041    229    293       C  
ATOM   6634  N   TYR A 811      22.612 -14.164  14.801  1.00 53.12           N  
ANISOU 6634  N   TYR A 811     6042   9473   4669  -1972     27    431       N  
ATOM   6635  CA  TYR A 811      21.632 -14.963  14.071  1.00 51.52           C  
ANISOU 6635  CA  TYR A 811     5838   9358   4377  -1951     16    363       C  
ATOM   6636  C   TYR A 811      21.160 -14.257  12.805  1.00 54.32           C  
ANISOU 6636  C   TYR A 811     6196   9859   4586  -2046    -30    510       C  
ATOM   6637  O   TYR A 811      21.147 -14.859  11.722  1.00 55.18           O  
ANISOU 6637  O   TYR A 811     6269  10164   4533  -2093      1    451       O  
ATOM   6638  CB  TYR A 811      20.439 -15.285  14.962  1.00 47.92           C  
ANISOU 6638  CB  TYR A 811     5429   8728   4049  -1848    -39    325       C  
ATOM   6639  CG  TYR A 811      19.344 -16.104  14.305  1.00 46.14           C  
ANISOU 6639  CG  TYR A 811     5199   8581   3751  -1837    -63    258       C  
ATOM   6640  CD1 TYR A 811      19.564 -17.435  13.940  1.00 44.67           C  
ANISOU 6640  CD1 TYR A 811     4982   8487   3502  -1827     -2     74       C  
ATOM   6641  CD2 TYR A 811      18.075 -15.557  14.077  1.00 43.45           C  
ANISOU 6641  CD2 TYR A 811     4884   8216   3411  -1835   -152    375       C  
ATOM   6642  CE1 TYR A 811      18.563 -18.194  13.350  1.00 45.66           C  
ANISOU 6642  CE1 TYR A 811     5110   8677   3564  -1833    -33      3       C  
ATOM   6643  CE2 TYR A 811      17.059 -16.313  13.489  1.00 43.27           C  
ANISOU 6643  CE2 TYR A 811     4846   8276   3320  -1838   -184    315       C  
ATOM   6644  CZ  TYR A 811      17.312 -17.634  13.126  1.00 47.42           C  
ANISOU 6644  CZ  TYR A 811     5347   8889   3780  -1846   -127    125       C  
ATOM   6645  OH  TYR A 811      16.324 -18.407  12.540  1.00 49.49           O  
ANISOU 6645  OH  TYR A 811     5601   9229   3976  -1865   -165     53       O  
ATOM   6646  N   ASN A 812      20.794 -12.983  12.950  1.00 55.87           N  
ANISOU 6646  N   ASN A 812     6438   9956   4836  -2072   -104    700       N  
ATOM   6647  CA  ASN A 812      20.211 -12.199  11.859  1.00 58.87           C  
ANISOU 6647  CA  ASN A 812     6828  10442   5098  -2149   -166    875       C  
ATOM   6648  C   ASN A 812      21.162 -11.971  10.692  1.00 63.60           C  
ANISOU 6648  C   ASN A 812     7378  11269   5517  -2277   -115    938       C  
ATOM   6649  O   ASN A 812      20.731 -11.905   9.541  1.00 67.73           O  
ANISOU 6649  O   ASN A 812     7887  11968   5878  -2340   -139   1010       O  
ATOM   6650  CB  ASN A 812      19.649 -10.876  12.382  1.00 56.96           C  
ANISOU 6650  CB  ASN A 812     6653  10008   4980  -2129   -254   1064       C  
ATOM   6651  CG  ASN A 812      18.415 -11.074  13.244  1.00 53.79           C  
ANISOU 6651  CG  ASN A 812     6288   9437   4711  -2002   -310   1025       C  
ATOM   6652  OD1 ASN A 812      17.874 -12.179  13.323  1.00 53.08           O  
ANISOU 6652  OD1 ASN A 812     6170   9388   4608  -1947   -293    879       O  
ATOM   6653  ND2 ASN A 812      17.965 -10.008  13.899  1.00 50.08           N  
ANISOU 6653  ND2 ASN A 812     5881   8777   4373  -1954   -374   1152       N  
ATOM   6654  N   ARG A 813      22.450 -11.849  10.996  1.00 65.20           N  
ANISOU 6654  N   ARG A 813     7548  11481   5743  -2318    -45    916       N  
ATOM   6655  CA  ARG A 813      23.477 -11.752   9.965  1.00 67.35           C  
ANISOU 6655  CA  ARG A 813     7755  11990   5845  -2436     25    957       C  
ATOM   6656  C   ARG A 813      23.624 -13.067   9.206  1.00 69.32           C  
ANISOU 6656  C   ARG A 813     7945  12455   5938  -2420    106    764       C  
ATOM   6657  O   ARG A 813      23.853 -13.070   7.994  1.00 74.03           O  
ANISOU 6657  O   ARG A 813     8502  13292   6334  -2508    139    803       O  
ATOM   6658  CB  ARG A 813      24.819 -11.342  10.572  1.00 65.36           C  
ANISOU 6658  CB  ARG A 813     7466  11696   5671  -2481     80    973       C  
ATOM   6659  CG  ARG A 813      24.862  -9.896  11.016  1.00 63.09           C  
ANISOU 6659  CG  ARG A 813     7238  11236   5496  -2544      4   1182       C  
ATOM   6660  CD  ARG A 813      26.284  -9.371  11.104  1.00 63.39           C  
ANISOU 6660  CD  ARG A 813     7220  11327   5539  -2654     57   1242       C  
ATOM   6661  NE  ARG A 813      27.167 -10.230  11.898  1.00 64.41           N  
ANISOU 6661  NE  ARG A 813     7284  11456   5734  -2592    134   1054       N  
ATOM   6662  CZ  ARG A 813      27.131 -10.342  13.226  1.00 60.58           C  
ANISOU 6662  CZ  ARG A 813     6836  10755   5427  -2501    106    969       C  
ATOM   6663  NH1 ARG A 813      26.246  -9.656  13.940  1.00 55.52           N  
ANISOU 6663  NH1 ARG A 813     6300   9878   4917  -2456     12   1039       N  
ATOM   6664  NH2 ARG A 813      27.981 -11.153  13.843  1.00 59.55           N  
ANISOU 6664  NH2 ARG A 813     6635  10654   5339  -2448    175    814       N  
ATOM   6665  N   ALA A 814      23.481 -14.178   9.922  1.00 68.30           N  
ANISOU 6665  N   ALA A 814     7815  12237   5898  -2308    137    557       N  
ATOM   6666  CA  ALA A 814      23.637 -15.505   9.342  1.00 69.48           C  
ANISOU 6666  CA  ALA A 814     7923  12544   5931  -2276    215    347       C  
ATOM   6667  C   ALA A 814      22.498 -15.856   8.391  1.00 71.24           C  
ANISOU 6667  C   ALA A 814     8173  12880   6016  -2298    162    332       C  
ATOM   6668  O   ALA A 814      22.685 -16.641   7.461  1.00 72.11           O  
ANISOU 6668  O   ALA A 814     8251  13191   5956  -2323    220    205       O  
ATOM   6669  CB  ALA A 814      23.749 -16.554  10.440  1.00 67.92           C  
ANISOU 6669  CB  ALA A 814     7729  12186   5889  -2150    251    151       C  
ATOM   6670  N   ILE A 815      21.329 -15.267   8.624  1.00 72.05           N  
ANISOU 6670  N   ILE A 815     8329  12858   6187  -2286     51    458       N  
ATOM   6671  CA  ILE A 815      20.123 -15.624   7.876  1.00 73.98           C  
ANISOU 6671  CA  ILE A 815     8590  13192   6325  -2300    -18    445       C  
ATOM   6672  C   ILE A 815      19.644 -14.554   6.886  1.00 78.49           C  
ANISOU 6672  C   ILE A 815     9166  13896   6760  -2395    -95    676       C  
ATOM   6673  O   ILE A 815      18.532 -14.648   6.354  1.00 79.23           O  
ANISOU 6673  O   ILE A 815     9270  14051   6782  -2405   -177    708       O  
ATOM   6674  CB  ILE A 815      18.961 -16.023   8.819  1.00 71.54           C  
ANISOU 6674  CB  ILE A 815     8321  12675   6186  -2201    -88    391       C  
ATOM   6675  CG1 ILE A 815      18.605 -14.869   9.765  1.00 67.74           C  
ANISOU 6675  CG1 ILE A 815     7878  11979   5881  -2158   -156    572       C  
ATOM   6676  CG2 ILE A 815      19.309 -17.308   9.569  1.00 69.25           C  
ANISOU 6676  CG2 ILE A 815     8027  12291   5993  -2117    -15    153       C  
ATOM   6677  CD1 ILE A 815      17.142 -14.796  10.126  1.00 65.81           C  
ANISOU 6677  CD1 ILE A 815     7659  11625   5722  -2097   -255    621       C  
ATOM   6678  N   LYS A 816      20.483 -13.546   6.647  1.00 81.98           N  
ANISOU 6678  N   LYS A 816     9597  14384   7169  -2471    -74    844       N  
ATOM   6679  CA  LYS A 816      20.200 -12.513   5.650  1.00 86.36           C  
ANISOU 6679  CA  LYS A 816    10155  15074   7584  -2572   -138   1082       C  
ATOM   6680  C   LYS A 816      19.980 -13.142   4.283  1.00 89.06           C  
ANISOU 6680  C   LYS A 816    10462  15715   7662  -2641   -125   1020       C  
ATOM   6681  O   LYS A 816      20.658 -14.105   3.918  1.00 88.74           O  
ANISOU 6681  O   LYS A 816    10382  15823   7511  -2649    -24    822       O  
ATOM   6682  CB  LYS A 816      21.348 -11.495   5.574  1.00 88.44           C  
ANISOU 6682  CB  LYS A 816    10404  15357   7844  -2661    -95   1249       C  
ATOM   6683  CG  LYS A 816      21.203 -10.288   6.495  1.00 89.58           C  
ANISOU 6683  CG  LYS A 816    10607  15231   8197  -2641   -168   1432       C  
ATOM   6684  CD  LYS A 816      20.376  -9.179   5.851  1.00 92.56           C  
ANISOU 6684  CD  LYS A 816    11026  15616   8529  -2690   -279   1697       C  
ATOM   6685  CE  LYS A 816      20.225  -7.985   6.785  1.00 94.25           C  
ANISOU 6685  CE  LYS A 816    11312  15538   8963  -2657   -349   1862       C  
ATOM   6686  NZ  LYS A 816      19.564  -6.826   6.116  1.00 96.40           N  
ANISOU 6686  NZ  LYS A 816    11624  15806   9197  -2704   -452   2141       N  
ATOM   6687  N   GLY A 817      19.021 -12.594   3.542  1.00 92.83           N  
ANISOU 6687  N   GLY A 817    10953  16281   8039  -2685   -229   1187       N  
ATOM   6688  CA  GLY A 817      18.697 -13.067   2.195  1.00 97.15           C  
ANISOU 6688  CA  GLY A 817    11471  17127   8314  -2763   -238   1154       C  
ATOM   6689  C   GLY A 817      18.148 -14.482   2.183  1.00 97.52           C  
ANISOU 6689  C   GLY A 817    11515  17210   8330  -2711   -227    876       C  
ATOM   6690  O   GLY A 817      18.419 -15.260   1.264  1.00 99.86           O  
ANISOU 6690  O   GLY A 817    11787  17743   8413  -2764   -172    727       O  
ATOM   6691  N   ASN A 818      17.376 -14.812   3.212  1.00 95.43           N  
ANISOU 6691  N   ASN A 818    11277  16706   8276  -2610   -278    805       N  
ATOM   6692  CA  ASN A 818      16.827 -16.149   3.357  1.00 95.35           C  
ANISOU 6692  CA  ASN A 818    11271  16684   8276  -2565   -273    551       C  
ATOM   6693  C   ASN A 818      15.382 -16.098   3.836  1.00 94.46           C  
ANISOU 6693  C   ASN A 818    11170  16434   8287  -2512   -397    608       C  
ATOM   6694  O   ASN A 818      15.092 -15.644   4.948  1.00 92.94           O  
ANISOU 6694  O   ASN A 818    10995  15999   8317  -2427   -425    683       O  
ATOM   6695  CB  ASN A 818      17.697 -16.980   4.300  1.00 94.61           C  
ANISOU 6695  CB  ASN A 818    11182  16436   8329  -2485   -160    337       C  
ATOM   6696  CG  ASN A 818      17.513 -18.460   4.099  1.00 95.66           C  
ANISOU 6696  CG  ASN A 818    11320  16617   8409  -2466   -122     55       C  
ATOM   6697  OD1 ASN A 818      16.566 -19.058   4.614  1.00 95.17           O  
ANISOU 6697  OD1 ASN A 818    11277  16423   8458  -2420   -181    -29       O  
ATOM   6698  ND2 ASN A 818      18.422 -19.067   3.342  1.00 96.08           N  
ANISOU 6698  ND2 ASN A 818    11355  16858   8294  -2502    -19    -97       N  
ATOM   6699  N   ILE A 819      14.483 -16.571   2.980  1.00 95.33           N  
ANISOU 6699  N   ILE A 819    11263  16715   8242  -2567   -471    567       N  
ATOM   6700  CA  ILE A 819      13.046 -16.426   3.188  1.00 94.42           C  
ANISOU 6700  CA  ILE A 819    11136  16538   8203  -2538   -602    656       C  
ATOM   6701  C   ILE A 819      12.438 -17.418   4.178  1.00 91.79           C  
ANISOU 6701  C   ILE A 819    10808  16014   8053  -2461   -603    471       C  
ATOM   6702  O   ILE A 819      11.591 -17.037   4.987  1.00 90.35           O  
ANISOU 6702  O   ILE A 819    10618  15665   8046  -2388   -671    572       O  
ATOM   6703  CB  ILE A 819      12.264 -16.466   1.844  1.00 97.77           C  
ANISOU 6703  CB  ILE A 819    11527  17243   8378  -2640   -699    712       C  
ATOM   6704  CG1 ILE A 819      13.019 -17.275   0.775  1.00100.21           C  
ANISOU 6704  CG1 ILE A 819    11839  17802   8434  -2735   -621    523       C  
ATOM   6705  CG2 ILE A 819      12.018 -15.050   1.336  1.00 99.42           C  
ANISOU 6705  CG2 ILE A 819    11721  17527   8525  -2668   -782   1033       C  
ATOM   6706  CD1 ILE A 819      12.771 -18.780   0.811  1.00100.14           C  
ANISOU 6706  CD1 ILE A 819    11843  17791   8414  -2738   -594    210       C  
ATOM   6707  N   ASP A 820      12.875 -18.675   4.120  1.00 90.97           N  
ANISOU 6707  N   ASP A 820    10719  15933   7912  -2474   -526    206       N  
ATOM   6708  CA  ASP A 820      12.239 -19.754   4.887  1.00 89.09           C  
ANISOU 6708  CA  ASP A 820    10489  15539   7822  -2426   -535     26       C  
ATOM   6709  C   ASP A 820      12.912 -20.107   6.225  1.00 85.44           C  
ANISOU 6709  C   ASP A 820    10056  14820   7587  -2320   -441    -70       C  
ATOM   6710  O   ASP A 820      12.557 -21.102   6.862  1.00 84.11           O  
ANISOU 6710  O   ASP A 820     9901  14522   7536  -2284   -431   -230       O  
ATOM   6711  CB  ASP A 820      12.018 -21.008   4.013  1.00 92.37           C  
ANISOU 6711  CB  ASP A 820    10911  16114   8073  -2509   -536   -208       C  
ATOM   6712  CG  ASP A 820      13.265 -21.433   3.232  1.00 95.56           C  
ANISOU 6712  CG  ASP A 820    11337  16672   8299  -2549   -422   -360       C  
ATOM   6713  OD1 ASP A 820      14.371 -20.899   3.480  1.00 97.41           O  
ANISOU 6713  OD1 ASP A 820    11574  16877   8560  -2510   -330   -302       O  
ATOM   6714  OD2 ASP A 820      13.130 -22.317   2.359  1.00 96.92           O  
ANISOU 6714  OD2 ASP A 820    11522  17002   8301  -2623   -423   -544       O  
ATOM   6715  N   ALA A 821      13.871 -19.283   6.645  1.00 82.28           N  
ANISOU 6715  N   ALA A 821     9665  14351   7245  -2279   -380     36       N  
ATOM   6716  CA  ALA A 821      14.433 -19.369   7.989  1.00 78.54           C  
ANISOU 6716  CA  ALA A 821     9213  13638   6990  -2177   -313     -7       C  
ATOM   6717  C   ALA A 821      13.609 -18.479   8.919  1.00 76.24           C  
ANISOU 6717  C   ALA A 821     8923  13174   6873  -2109   -389    175       C  
ATOM   6718  O   ALA A 821      13.310 -17.336   8.567  1.00 78.11           O  
ANISOU 6718  O   ALA A 821     9151  13456   7070  -2128   -453    384       O  
ATOM   6719  CB  ALA A 821      15.899 -18.943   7.995  1.00 78.44           C  
ANISOU 6719  CB  ALA A 821     9204  13648   6953  -2177   -214      7       C  
ATOM   6720  N   PRO A 822      13.229 -19.001  10.102  1.00 72.53           N  
ANISOU 6720  N   PRO A 822     8463  12505   6592  -2023   -381    100       N  
ATOM   6721  CA  PRO A 822      12.346 -18.287  11.035  1.00 71.06           C  
ANISOU 6721  CA  PRO A 822     8273  12160   6566  -1945   -445    244       C  
ATOM   6722  C   PRO A 822      12.968 -17.039  11.664  1.00 69.92           C  
ANISOU 6722  C   PRO A 822     8156  11897   6513  -1893   -429    398       C  
ATOM   6723  O   PRO A 822      14.156 -17.025  11.987  1.00 69.65           O  
ANISOU 6723  O   PRO A 822     8145  11818   6502  -1887   -349    345       O  
ATOM   6724  CB  PRO A 822      12.044 -19.334  12.111  1.00 69.44           C  
ANISOU 6724  CB  PRO A 822     8073  11795   6515  -1879   -413     95       C  
ATOM   6725  CG  PRO A 822      13.167 -20.297  12.029  1.00 70.38           C  
ANISOU 6725  CG  PRO A 822     8215  11923   6601  -1893   -316    -97       C  
ATOM   6726  CD  PRO A 822      13.552 -20.354  10.587  1.00 71.92           C  
ANISOU 6726  CD  PRO A 822     8401  12347   6579  -1995   -312   -128       C  
ATOM   6727  N   GLN A 823      12.144 -16.008  11.830  1.00 68.99           N  
ANISOU 6727  N   GLN A 823     8035  11728   6450  -1855   -508    584       N  
ATOM   6728  CA  GLN A 823      12.575 -14.714  12.343  1.00 67.45           C  
ANISOU 6728  CA  GLN A 823     7878  11409   6342  -1812   -511    742       C  
ATOM   6729  C   GLN A 823      12.336 -14.628  13.845  1.00 65.76           C  
ANISOU 6729  C   GLN A 823     7688  10965   6331  -1693   -495    717       C  
ATOM   6730  O   GLN A 823      11.348 -15.169  14.358  1.00 64.74           O  
ANISOU 6730  O   GLN A 823     7532  10789   6275  -1635   -520    672       O  
ATOM   6731  CB  GLN A 823      11.813 -13.582  11.645  1.00 70.18           C  
ANISOU 6731  CB  GLN A 823     8213  11816   6635  -1825   -608    965       C  
ATOM   6732  CG  GLN A 823      11.862 -13.604  10.115  1.00 75.15           C  
ANISOU 6732  CG  GLN A 823     8814  12697   7042  -1945   -641   1017       C  
ATOM   6733  CD  GLN A 823      13.197 -13.143   9.553  1.00 78.42           C  
ANISOU 6733  CD  GLN A 823     9254  13186   7356  -2028   -582   1056       C  
ATOM   6734  OE1 GLN A 823      13.736 -13.752   8.629  1.00 80.18           O  
ANISOU 6734  OE1 GLN A 823     9456  13603   7406  -2119   -541    968       O  
ATOM   6735  NE2 GLN A 823      13.738 -12.063  10.110  1.00 79.15           N  
ANISOU 6735  NE2 GLN A 823     9392  13128   7555  -2002   -575   1184       N  
ATOM   6736  N   VAL A 824      13.246 -13.945  14.540  1.00 63.82           N  
ANISOU 6736  N   VAL A 824     7491  10589   6169  -1666   -455    749       N  
ATOM   6737  CA  VAL A 824      13.138 -13.714  15.978  1.00 59.89           C  
ANISOU 6737  CA  VAL A 824     7027   9881   5848  -1556   -440    732       C  
ATOM   6738  C   VAL A 824      12.078 -12.640  16.228  1.00 60.39           C  
ANISOU 6738  C   VAL A 824     7102   9855   5988  -1481   -517    896       C  
ATOM   6739  O   VAL A 824      12.148 -11.552  15.659  1.00 61.74           O  
ANISOU 6739  O   VAL A 824     7297  10034   6127  -1509   -562   1054       O  
ATOM   6740  CB  VAL A 824      14.501 -13.282  16.585  1.00 58.48           C  
ANISOU 6740  CB  VAL A 824     6894   9604   5720  -1566   -382    710       C  
ATOM   6741  CG1 VAL A 824      14.345 -12.805  18.023  1.00 59.48           C  
ANISOU 6741  CG1 VAL A 824     7067   9520   6013  -1458   -382    714       C  
ATOM   6742  CG2 VAL A 824      15.503 -14.422  16.529  1.00 57.95           C  
ANISOU 6742  CG2 VAL A 824     6803   9611   5605  -1606   -301    539       C  
ATOM   6743  N   VAL A 825      11.093 -12.956  17.066  1.00 58.81           N  
ANISOU 6743  N   VAL A 825     6882   9573   5890  -1382   -528    864       N  
ATOM   6744  CA  VAL A 825      10.054 -11.988  17.413  1.00 59.05           C  
ANISOU 6744  CA  VAL A 825     6915   9516   6006  -1283   -590   1005       C  
ATOM   6745  C   VAL A 825      10.421 -11.206  18.675  1.00 58.43           C  
ANISOU 6745  C   VAL A 825     6909   9224   6068  -1188   -563   1011       C  
ATOM   6746  O   VAL A 825      10.700 -11.792  19.725  1.00 56.55           O  
ANISOU 6746  O   VAL A 825     6684   8902   5901  -1143   -506    886       O  
ATOM   6747  CB  VAL A 825       8.664 -12.646  17.634  1.00 59.48           C  
ANISOU 6747  CB  VAL A 825     6893   9615   6093  -1221   -619    984       C  
ATOM   6748  CG1 VAL A 825       7.573 -11.581  17.602  1.00 59.69           C  
ANISOU 6748  CG1 VAL A 825     6899   9608   6172  -1127   -692   1157       C  
ATOM   6749  CG2 VAL A 825       8.384 -13.741  16.598  1.00 59.29           C  
ANISOU 6749  CG2 VAL A 825     6801   9788   5937  -1328   -637    915       C  
ATOM   6750  N   GLU A 826      10.412  -9.880  18.555  1.00 58.84           N  
ANISOU 6750  N   GLU A 826     7013   9187   6155  -1161   -608   1159       N  
ATOM   6751  CA  GLU A 826      10.540  -8.975  19.690  1.00 56.64           C  
ANISOU 6751  CA  GLU A 826     6813   8696   6013  -1062   -599   1176       C  
ATOM   6752  C   GLU A 826       9.674  -9.437  20.866  1.00 53.98           C  
ANISOU 6752  C   GLU A 826     6450   8287   5773   -929   -572   1091       C  
ATOM   6753  O   GLU A 826       8.487  -9.724  20.699  1.00 51.10           O  
ANISOU 6753  O   GLU A 826     6011   7994   5409   -871   -601   1127       O  
ATOM   6754  CB  GLU A 826      10.157  -7.550  19.262  1.00 60.64           C  
ANISOU 6754  CB  GLU A 826     7365   9120   6553  -1026   -670   1366       C  
ATOM   6755  CG  GLU A 826      10.058  -6.521  20.398  1.00 65.30           C  
ANISOU 6755  CG  GLU A 826     8045   9473   7292   -903   -672   1383       C  
ATOM   6756  CD  GLU A 826      11.383  -6.273  21.116  1.00 67.86           C  
ANISOU 6756  CD  GLU A 826     8456   9671   7655   -958   -628   1297       C  
ATOM   6757  OE1 GLU A 826      11.344  -6.007  22.340  1.00 69.96           O  
ANISOU 6757  OE1 GLU A 826     8778   9780   8024   -860   -604   1220       O  
ATOM   6758  OE2 GLU A 826      12.453  -6.340  20.465  1.00 65.65           O  
ANISOU 6758  OE2 GLU A 826     8184   9463   7297  -1099   -618   1305       O  
ATOM   6759  N   GLY A 827      10.286  -9.518  22.047  1.00 52.46           N  
ANISOU 6759  N   GLY A 827     6311   7968   5654   -888   -518    984       N  
ATOM   6760  CA  GLY A 827       9.574  -9.908  23.262  1.00 51.23           C  
ANISOU 6760  CA  GLY A 827     6139   7746   5582   -765   -483    907       C  
ATOM   6761  C   GLY A 827       9.543 -11.401  23.537  1.00 50.54           C  
ANISOU 6761  C   GLY A 827     5985   7754   5464   -794   -432    777       C  
ATOM   6762  O   GLY A 827       9.322 -11.816  24.676  1.00 49.62           O  
ANISOU 6762  O   GLY A 827     5868   7577   5410   -716   -389    699       O  
ATOM   6763  N   GLU A 828       9.769 -12.213  22.505  1.00 50.85           N  
ANISOU 6763  N   GLU A 828     5974   7939   5407   -907   -438    754       N  
ATOM   6764  CA  GLU A 828       9.734 -13.666  22.664  1.00 51.84           C  
ANISOU 6764  CA  GLU A 828     6046   8140   5510   -941   -395    629       C  
ATOM   6765  C   GLU A 828      11.016 -14.204  23.295  1.00 49.21           C  
ANISOU 6765  C   GLU A 828     5756   7752   5187   -971   -332    509       C  
ATOM   6766  O   GLU A 828      11.964 -13.462  23.552  1.00 49.02           O  
ANISOU 6766  O   GLU A 828     5796   7653   5178   -980   -325    520       O  
ATOM   6767  CB  GLU A 828       9.449 -14.368  21.331  1.00 55.12           C  
ANISOU 6767  CB  GLU A 828     6399   8728   5818  -1046   -426    630       C  
ATOM   6768  CG  GLU A 828       7.962 -14.449  20.978  1.00 66.07           C  
ANISOU 6768  CG  GLU A 828     7704  10195   7202  -1015   -480    704       C  
ATOM   6769  CD  GLU A 828       7.665 -15.403  19.816  1.00 74.85           C  
ANISOU 6769  CD  GLU A 828     8754  11481   8205  -1130   -510    665       C  
ATOM   6770  OE1 GLU A 828       6.574 -15.285  19.212  1.00 77.24           O  
ANISOU 6770  OE1 GLU A 828     8987  11884   8476  -1134   -575    750       O  
ATOM   6771  OE2 GLU A 828       8.516 -16.271  19.503  1.00 79.16           O  
ANISOU 6771  OE2 GLU A 828     9318  12066   8695  -1214   -469    545       O  
ATOM   6772  N   LYS A 829      11.035 -15.504  23.545  1.00 47.14           N  
ANISOU 6772  N   LYS A 829     5458   7529   4924   -988   -292    399       N  
ATOM   6773  CA  LYS A 829      12.183 -16.135  24.162  1.00 45.84           C  
ANISOU 6773  CA  LYS A 829     5322   7320   4774  -1001   -235    290       C  
ATOM   6774  C   LYS A 829      13.117 -16.788  23.142  1.00 45.48           C  
ANISOU 6774  C   LYS A 829     5263   7378   4641  -1105   -215    224       C  
ATOM   6775  O   LYS A 829      12.674 -17.270  22.097  1.00 44.41           O  
ANISOU 6775  O   LYS A 829     5087   7354   4432  -1168   -235    219       O  
ATOM   6776  CB  LYS A 829      11.714 -17.116  25.236  1.00 46.88           C  
ANISOU 6776  CB  LYS A 829     5433   7405   4974   -938   -197    219       C  
ATOM   6777  CG  LYS A 829      11.099 -16.401  26.444  1.00 45.22           C  
ANISOU 6777  CG  LYS A 829     5246   7094   4843   -824   -195    267       C  
ATOM   6778  CD  LYS A 829      11.068 -17.277  27.668  1.00 47.82           C  
ANISOU 6778  CD  LYS A 829     5570   7373   5226   -769   -146    197       C  
ATOM   6779  CE  LYS A 829      10.572 -16.510  28.884  1.00 46.79           C  
ANISOU 6779  CE  LYS A 829     5469   7158   5153   -654   -136    232       C  
ATOM   6780  NZ  LYS A 829      10.403 -17.433  30.027  1.00 46.12           N  
ANISOU 6780  NZ  LYS A 829     5368   7051   5105   -607    -88    181       N  
ATOM   6781  N   VAL A 830      14.416 -16.766  23.437  1.00 44.69           N  
ANISOU 6781  N   VAL A 830     5190   7248   4541  -1123   -177    173       N  
ATOM   6782  CA  VAL A 830      15.426 -17.350  22.547  1.00 43.19           C  
ANISOU 6782  CA  VAL A 830     4980   7161   4270  -1206   -145    104       C  
ATOM   6783  C   VAL A 830      16.341 -18.316  23.286  1.00 41.60           C  
ANISOU 6783  C   VAL A 830     4774   6922   4110  -1177    -85    -14       C  
ATOM   6784  O   VAL A 830      16.636 -18.114  24.473  1.00 38.15           O  
ANISOU 6784  O   VAL A 830     4363   6383   3750  -1114    -74    -17       O  
ATOM   6785  CB  VAL A 830      16.298 -16.272  21.845  1.00 44.10           C  
ANISOU 6785  CB  VAL A 830     5112   7323   4321  -1277   -157    182       C  
ATOM   6786  CG1 VAL A 830      15.510 -15.553  20.770  1.00 44.73           C  
ANISOU 6786  CG1 VAL A 830     5186   7478   4331  -1323   -215    298       C  
ATOM   6787  CG2 VAL A 830      16.866 -15.275  22.855  1.00 45.05           C  
ANISOU 6787  CG2 VAL A 830     5282   7317   4519  -1241   -165    228       C  
ATOM   6788  N   TYR A 831      16.772 -19.366  22.579  1.00 40.14           N  
ANISOU 6788  N   TYR A 831     4559   6821   3871  -1219    -47   -112       N  
ATOM   6789  CA  TYR A 831      17.873 -20.214  23.038  1.00 39.61           C  
ANISOU 6789  CA  TYR A 831     4481   6737   3833  -1193     12   -217       C  
ATOM   6790  C   TYR A 831      19.164 -19.492  22.739  1.00 39.94           C  
ANISOU 6790  C   TYR A 831     4512   6835   3827  -1236     30   -193       C  
ATOM   6791  O   TYR A 831      19.238 -18.780  21.743  1.00 41.50           O  
ANISOU 6791  O   TYR A 831     4704   7125   3939  -1310     12   -131       O  
ATOM   6792  CB  TYR A 831      17.888 -21.560  22.322  1.00 40.50           C  
ANISOU 6792  CB  TYR A 831     4569   6910   3907  -1214     48   -339       C  
ATOM   6793  CG  TYR A 831      16.832 -22.534  22.794  1.00 42.58           C  
ANISOU 6793  CG  TYR A 831     4840   7099   4238  -1179     39   -381       C  
ATOM   6794  CD1 TYR A 831      16.623 -22.757  24.156  1.00 44.13           C  
ANISOU 6794  CD1 TYR A 831     5051   7172   4544  -1100     44   -367       C  
ATOM   6795  CD2 TYR A 831      16.053 -23.247  21.883  1.00 41.94           C  
ANISOU 6795  CD2 TYR A 831     4748   7078   4107  -1234     23   -435       C  
ATOM   6796  CE1 TYR A 831      15.656 -23.654  24.603  1.00 45.17           C  
ANISOU 6796  CE1 TYR A 831     5184   7241   4739  -1079     39   -390       C  
ATOM   6797  CE2 TYR A 831      15.074 -24.156  22.323  1.00 44.69           C  
ANISOU 6797  CE2 TYR A 831     5099   7356   4527  -1220     11   -468       C  
ATOM   6798  CZ  TYR A 831      14.887 -24.352  23.685  1.00 46.14           C  
ANISOU 6798  CZ  TYR A 831     5294   7415   4824  -1143     22   -439       C  
ATOM   6799  OH  TYR A 831      13.937 -25.233  24.152  1.00 48.53           O  
ANISOU 6799  OH  TYR A 831     5592   7651   5196  -1139     13   -455       O  
ATOM   6800  N   VAL A 832      20.172 -19.666  23.601  1.00 39.40           N  
ANISOU 6800  N   VAL A 832     4436   6720   3813  -1195     62   -232       N  
ATOM   6801  CA  VAL A 832      21.475 -18.996  23.445  1.00 37.72           C  
ANISOU 6801  CA  VAL A 832     4199   6566   3567  -1242     78   -207       C  
ATOM   6802  C   VAL A 832      22.651 -19.974  23.604  1.00 39.95           C  
ANISOU 6802  C   VAL A 832     4428   6894   3859  -1209    142   -312       C  
ATOM   6803  O   VAL A 832      22.660 -20.795  24.525  1.00 38.92           O  
ANISOU 6803  O   VAL A 832     4299   6682   3806  -1127    156   -370       O  
ATOM   6804  CB  VAL A 832      21.666 -17.837  24.450  1.00 36.88           C  
ANISOU 6804  CB  VAL A 832     4132   6360   3522  -1233     36   -124       C  
ATOM   6805  CG1 VAL A 832      22.871 -16.969  24.055  1.00 36.02           C  
ANISOU 6805  CG1 VAL A 832     3997   6321   3369  -1320     38    -74       C  
ATOM   6806  CG2 VAL A 832      20.393 -16.977  24.577  1.00 35.08           C  
ANISOU 6806  CG2 VAL A 832     3963   6050   3316  -1222    -23    -33       C  
ATOM   6807  N   LEU A 833      23.631 -19.880  22.696  1.00 40.57           N  
ANISOU 6807  N   LEU A 833     4452   7107   3855  -1270    181   -326       N  
ATOM   6808  CA  LEU A 833      24.852 -20.684  22.770  1.00 40.52           C  
ANISOU 6808  CA  LEU A 833     4378   7164   3854  -1233    246   -417       C  
ATOM   6809  C   LEU A 833      26.133 -19.876  22.547  1.00 42.28           C  
ANISOU 6809  C   LEU A 833     4539   7492   4033  -1301    262   -365       C  
ATOM   6810  O   LEU A 833      26.181 -19.027  21.652  1.00 42.11           O  
ANISOU 6810  O   LEU A 833     4512   7561   3926  -1401    253   -289       O  
ATOM   6811  CB  LEU A 833      24.811 -21.858  21.788  1.00 38.37           C  
ANISOU 6811  CB  LEU A 833     4081   6976   3522  -1216    305   -537       C  
ATOM   6812  CG  LEU A 833      23.964 -23.075  22.160  1.00 39.75           C  
ANISOU 6812  CG  LEU A 833     4296   7042   3765  -1138    307   -628       C  
ATOM   6813  CD1 LEU A 833      23.899 -24.052  20.990  1.00 38.46           C  
ANISOU 6813  CD1 LEU A 833     4122   6966   3524  -1148    357   -751       C  
ATOM   6814  CD2 LEU A 833      24.514 -23.761  23.404  1.00 40.18           C  
ANISOU 6814  CD2 LEU A 833     4339   6993   3935  -1034    324   -665       C  
ATOM   6815  N   PRO A 834      27.174 -20.141  23.367  1.00 43.27           N  
ANISOU 6815  N   PRO A 834     4611   7613   4217  -1252    283   -394       N  
ATOM   6816  CA  PRO A 834      28.491 -19.550  23.144  1.00 43.57           C  
ANISOU 6816  CA  PRO A 834     4565   7774   4216  -1319    305   -355       C  
ATOM   6817  C   PRO A 834      29.191 -20.210  21.950  1.00 45.81           C  
ANISOU 6817  C   PRO A 834     4763   8238   4405  -1329    393   -429       C  
ATOM   6818  O   PRO A 834      28.966 -21.396  21.665  1.00 45.54           O  
ANISOU 6818  O   PRO A 834     4726   8207   4371  -1245    441   -545       O  
ATOM   6819  CB  PRO A 834      29.236 -19.864  24.444  1.00 41.04           C  
ANISOU 6819  CB  PRO A 834     4208   7394   3990  -1243    296   -379       C  
ATOM   6820  CG  PRO A 834      28.616 -21.119  24.929  1.00 42.65           C  
ANISOU 6820  CG  PRO A 834     4446   7502   4258  -1118    312   -469       C  
ATOM   6821  CD  PRO A 834      27.158 -20.992  24.575  1.00 42.61           C  
ANISOU 6821  CD  PRO A 834     4536   7416   4238  -1137    280   -451       C  
ATOM   6822  N   LEU A 835      30.032 -19.440  21.270  1.00 46.17           N  
ANISOU 6822  N   LEU A 835     4740   8431   4372  -1433    414   -363       N  
ATOM   6823  CA  LEU A 835      30.765 -19.922  20.108  1.00 49.12           C  
ANISOU 6823  CA  LEU A 835     5021   9006   4635  -1450    505   -423       C  
ATOM   6824  C   LEU A 835      32.272 -19.768  20.292  1.00 50.58           C  
ANISOU 6824  C   LEU A 835     5074   9322   4822  -1467    550   -408       C  
ATOM   6825  O   LEU A 835      32.740 -18.712  20.711  1.00 51.63           O  
ANISOU 6825  O   LEU A 835     5188   9451   4977  -1561    501   -295       O  
ATOM   6826  CB  LEU A 835      30.312 -19.162  18.856  1.00 49.87           C  
ANISOU 6826  CB  LEU A 835     5142   9208   4599  -1575    502   -344       C  
ATOM   6827  CG  LEU A 835      29.224 -19.695  17.913  1.00 47.13           C  
ANISOU 6827  CG  LEU A 835     4859   8880   4167  -1567    510   -404       C  
ATOM   6828  CD1 LEU A 835      28.274 -20.691  18.545  1.00 48.06           C  
ANISOU 6828  CD1 LEU A 835     5050   8832   4377  -1452    487   -507       C  
ATOM   6829  CD2 LEU A 835      28.457 -18.527  17.313  1.00 44.83           C  
ANISOU 6829  CD2 LEU A 835     4630   8596   3808  -1687    444   -257       C  
ATOM   6830  N   ARG A 836      33.023 -20.825  19.976  1.00 53.09           N  
ANISOU 6830  N   ARG A 836     5298   9753   5120  -1375    641   -526       N  
ATOM   6831  CA  ARG A 836      34.492 -20.782  20.014  1.00 55.94           C  
ANISOU 6831  CA  ARG A 836     5505  10277   5472  -1379    697   -518       C  
ATOM   6832  C   ARG A 836      35.022 -19.682  19.116  1.00 58.80           C  
ANISOU 6832  C   ARG A 836     5805  10818   5719  -1547    714   -402       C  
ATOM   6833  O   ARG A 836      34.450 -19.405  18.054  1.00 59.29           O  
ANISOU 6833  O   ARG A 836     5913  10948   5667  -1621    730   -379       O  
ATOM   6834  CB  ARG A 836      35.120 -22.117  19.592  1.00 54.65           C  
ANISOU 6834  CB  ARG A 836     5253  10220   5291  -1240    806   -672       C  
ATOM   6835  CG  ARG A 836      34.901 -23.260  20.574  1.00 55.64           C  
ANISOU 6835  CG  ARG A 836     5415  10176   5551  -1068    796   -772       C  
ATOM   6836  CD  ARG A 836      35.808 -24.451  20.304  1.00 56.49           C  
ANISOU 6836  CD  ARG A 836     5413  10385   5665   -923    901   -905       C  
ATOM   6837  NE  ARG A 836      35.838 -24.854  18.896  1.00 59.28           N  
ANISOU 6837  NE  ARG A 836     5745  10895   5884   -928   1000  -1005       N  
ATOM   6838  CZ  ARG A 836      34.922 -25.614  18.298  1.00 57.68           C  
ANISOU 6838  CZ  ARG A 836     5648  10620   5648   -886   1020  -1122       C  
ATOM   6839  NH1 ARG A 836      33.865 -26.071  18.966  1.00 56.27           N  
ANISOU 6839  NH1 ARG A 836     5599  10213   5569   -838    951  -1147       N  
ATOM   6840  NH2 ARG A 836      35.063 -25.915  17.019  1.00 58.23           N  
ANISOU 6840  NH2 ARG A 836     5690  10859   5578   -898   1110  -1217       N  
ATOM   6841  N   GLU A 837      36.111 -19.059  19.557  1.00 61.06           N  
ANISOU 6841  N   GLU A 837     5983  11184   6032  -1613    705   -321       N  
ATOM   6842  CA  GLU A 837      36.808 -18.043  18.780  1.00 65.31           C  
ANISOU 6842  CA  GLU A 837     6438  11904   6472  -1782    726   -199       C  
ATOM   6843  C   GLU A 837      37.229 -18.602  17.417  1.00 66.60           C  
ANISOU 6843  C   GLU A 837     6508  12312   6486  -1773    852   -264       C  
ATOM   6844  O   GLU A 837      37.616 -19.772  17.303  1.00 65.89           O  
ANISOU 6844  O   GLU A 837     6349  12292   6394  -1626    938   -410       O  
ATOM   6845  CB  GLU A 837      38.026 -17.532  19.557  1.00 68.46           C  
ANISOU 6845  CB  GLU A 837     6712  12362   6936  -1839    702   -128       C  
ATOM   6846  CG  GLU A 837      38.573 -16.198  19.057  1.00 76.36           C  
ANISOU 6846  CG  GLU A 837     7663  13477   7874  -2055    682     38       C  
ATOM   6847  CD  GLU A 837      39.868 -15.802  19.740  1.00 81.54           C  
ANISOU 6847  CD  GLU A 837     8171  14224   8587  -2120    664     95       C  
ATOM   6848  OE1 GLU A 837      40.937 -15.944  19.110  1.00 84.42           O  
ANISOU 6848  OE1 GLU A 837     8359  14838   8878  -2155    755    106       O  
ATOM   6849  OE2 GLU A 837      39.819 -15.361  20.908  1.00 84.57           O  
ANISOU 6849  OE2 GLU A 837     8608  14441   9083  -2137    561    126       O  
ATOM   6850  N   GLY A 838      37.125 -17.763  16.389  1.00 66.90           N  
ANISOU 6850  N   GLY A 838     6550  12473   6396  -1926    863   -156       N  
ATOM   6851  CA  GLY A 838      37.484 -18.152  15.025  1.00 69.05           C  
ANISOU 6851  CA  GLY A 838     6739  13002   6496  -1940    983   -204       C  
ATOM   6852  C   GLY A 838      36.340 -18.773  14.241  1.00 69.21           C  
ANISOU 6852  C   GLY A 838     6878  12991   6429  -1883    998   -303       C  
ATOM   6853  O   GLY A 838      36.544 -19.293  13.142  1.00 70.88           O  
ANISOU 6853  O   GLY A 838     7037  13405   6491  -1868   1099   -384       O  
ATOM   6854  N   ASN A 839      35.139 -18.728  14.816  1.00 66.64           N  
ANISOU 6854  N   ASN A 839     6708  12422   6192  -1854    897   -301       N  
ATOM   6855  CA  ASN A 839      33.930 -19.219  14.165  1.00 64.43           C  
ANISOU 6855  CA  ASN A 839     6544  12093   5842  -1820    886   -377       C  
ATOM   6856  C   ASN A 839      33.531 -18.309  12.999  1.00 66.99           C  
ANISOU 6856  C   ASN A 839     6896  12553   6004  -1977    874   -244       C  
ATOM   6857  O   ASN A 839      33.886 -17.126  12.994  1.00 67.13           O  
ANISOU 6857  O   ASN A 839     6892  12602   6015  -2115    835    -65       O  
ATOM   6858  CB  ASN A 839      32.794 -19.353  15.189  1.00 61.44           C  
ANISOU 6858  CB  ASN A 839     6304  11430   5613  -1751    781   -390       C  
ATOM   6859  CG  ASN A 839      32.286 -18.010  15.688  1.00 58.55           C  
ANISOU 6859  CG  ASN A 839     6014  10928   5306  -1863    668   -206       C  
ATOM   6860  OD1 ASN A 839      31.430 -17.391  15.058  1.00 58.91           O  
ANISOU 6860  OD1 ASN A 839     6137  10966   5280  -1944    620   -117       O  
ATOM   6861  ND2 ASN A 839      32.806 -17.558  16.827  1.00 52.52           N  
ANISOU 6861  ND2 ASN A 839     5231  10053   4671  -1862    623   -152       N  
ATOM   6862  N   PRO A 840      32.792 -18.854  12.010  1.00 67.94           N  
ANISOU 6862  N   PRO A 840     7068  12752   5993  -1963    900   -328       N  
ATOM   6863  CA  PRO A 840      32.469 -18.088  10.809  1.00 69.40           C  
ANISOU 6863  CA  PRO A 840     7268  13103   5998  -2105    894   -204       C  
ATOM   6864  C   PRO A 840      31.234 -17.205  10.978  1.00 67.77           C  
ANISOU 6864  C   PRO A 840     7193  12723   5835  -2175    761    -56       C  
ATOM   6865  O   PRO A 840      30.804 -16.558  10.021  1.00 69.48           O  
ANISOU 6865  O   PRO A 840     7435  13051   5912  -2285    737     63       O  
ATOM   6866  CB  PRO A 840      32.197 -19.184   9.778  1.00 71.16           C  
ANISOU 6866  CB  PRO A 840     7492  13479   6065  -2043    974   -387       C  
ATOM   6867  CG  PRO A 840      31.582 -20.282  10.578  1.00 69.26           C  
ANISOU 6867  CG  PRO A 840     7325  13022   5968  -1889    949   -563       C  
ATOM   6868  CD  PRO A 840      32.202 -20.206  11.960  1.00 67.77           C  
ANISOU 6868  CD  PRO A 840     7100  12668   5982  -1822    929   -540       C  
ATOM   6869  N   PHE A 841      30.666 -17.194  12.180  1.00 65.26           N  
ANISOU 6869  N   PHE A 841     6951  12141   5703  -2103    678    -62       N  
ATOM   6870  CA  PHE A 841      29.537 -16.324  12.494  1.00 64.32           C  
ANISOU 6870  CA  PHE A 841     6947  11842   5648  -2147    557     76       C  
ATOM   6871  C   PHE A 841      30.021 -14.945  12.925  1.00 64.11           C  
ANISOU 6871  C   PHE A 841     6918  11754   5687  -2259    503    274       C  
ATOM   6872  O   PHE A 841      29.241 -13.990  12.976  1.00 63.50           O  
ANISOU 6872  O   PHE A 841     6928  11557   5641  -2317    410    421       O  
ATOM   6873  CB  PHE A 841      28.652 -16.952  13.571  1.00 63.22           C  
ANISOU 6873  CB  PHE A 841     6891  11462   5667  -2018    500    -24       C  
ATOM   6874  CG  PHE A 841      27.970 -18.219  13.132  1.00 64.16           C  
ANISOU 6874  CG  PHE A 841     7036  11607   5735  -1931    530   -200       C  
ATOM   6875  CD1 PHE A 841      27.002 -18.194  12.129  1.00 65.64           C  
ANISOU 6875  CD1 PHE A 841     7272  11874   5794  -1981    498   -180       C  
ATOM   6876  CD2 PHE A 841      28.292 -19.436  13.723  1.00 64.39           C  
ANISOU 6876  CD2 PHE A 841     7043  11576   5846  -1803    585   -381       C  
ATOM   6877  CE1 PHE A 841      26.365 -19.366  11.713  1.00 66.38           C  
ANISOU 6877  CE1 PHE A 841     7394  11990   5838  -1918    517   -352       C  
ATOM   6878  CE2 PHE A 841      27.660 -20.614  13.321  1.00 66.10           C  
ANISOU 6878  CE2 PHE A 841     7295  11794   6025  -1733    609   -548       C  
ATOM   6879  CZ  PHE A 841      26.693 -20.577  12.311  1.00 66.69           C  
ANISOU 6879  CZ  PHE A 841     7420  11950   5968  -1797    574   -540       C  
ATOM   6880  N   GLY A 842      31.312 -14.860  13.240  1.00 63.34           N  
ANISOU 6880  N   GLY A 842     6717  11735   5616  -2286    560    274       N  
ATOM   6881  CA  GLY A 842      31.983 -13.591  13.481  1.00 64.20           C  
ANISOU 6881  CA  GLY A 842     6803  11828   5764  -2423    522    455       C  
ATOM   6882  C   GLY A 842      31.767 -12.966  14.844  1.00 61.63           C  
ANISOU 6882  C   GLY A 842     6553  11234   5629  -2405    423    502       C  
ATOM   6883  O   GLY A 842      32.181 -11.830  15.077  1.00 62.46           O  
ANISOU 6883  O   GLY A 842     6666  11286   5779  -2527    373    651       O  
ATOM   6884  N   ASP A 843      31.125 -13.699  15.746  1.00 60.11           N  
ANISOU 6884  N   ASP A 843     6421  10873   5545  -2260    396    374       N  
ATOM   6885  CA  ASP A 843      30.857 -13.193  17.088  1.00 58.44           C  
ANISOU 6885  CA  ASP A 843     6286  10417   5500  -2227    309    398       C  
ATOM   6886  C   ASP A 843      30.909 -14.333  18.097  1.00 56.73           C  
ANISOU 6886  C   ASP A 843     6054  10121   5379  -2070    330    229       C  
ATOM   6887  O   ASP A 843      30.985 -15.505  17.716  1.00 56.92           O  
ANISOU 6887  O   ASP A 843     6028  10248   5353  -1982    405     95       O  
ATOM   6888  CB  ASP A 843      29.500 -12.479  17.131  1.00 58.95           C  
ANISOU 6888  CB  ASP A 843     6490  10306   5602  -2229    215    489       C  
ATOM   6889  CG  ASP A 843      29.518 -11.222  17.998  1.00 59.39           C  
ANISOU 6889  CG  ASP A 843     6621  10167   5776  -2291    125    607       C  
ATOM   6890  OD1 ASP A 843      30.334 -11.140  18.939  1.00 60.09           O  
ANISOU 6890  OD1 ASP A 843     6677  10205   5951  -2294    119    572       O  
ATOM   6891  OD2 ASP A 843      28.707 -10.309  17.740  1.00 61.21           O  
ANISOU 6891  OD2 ASP A 843     6946  10295   6017  -2334     56    732       O  
ATOM   6892  N   LYS A 844      30.857 -13.982  19.380  1.00 55.27           N  
ANISOU 6892  N   LYS A 844     5920   9750   5329  -2037    264    235       N  
ATOM   6893  CA  LYS A 844      31.077 -14.937  20.473  1.00 53.76           C  
ANISOU 6893  CA  LYS A 844     5706   9488   5232  -1902    277    104       C  
ATOM   6894  C   LYS A 844      29.874 -15.804  20.860  1.00 50.88           C  
ANISOU 6894  C   LYS A 844     5425   8993   4913  -1765    264      8       C  
ATOM   6895  O   LYS A 844      30.024 -16.780  21.595  1.00 50.28           O  
ANISOU 6895  O   LYS A 844     5327   8877   4901  -1649    287   -101       O  
ATOM   6896  CB  LYS A 844      31.647 -14.224  21.708  1.00 55.07           C  
ANISOU 6896  CB  LYS A 844     5880   9539   5504  -1933    212    146       C  
ATOM   6897  CG  LYS A 844      30.880 -12.995  22.166  1.00 56.83           C  
ANISOU 6897  CG  LYS A 844     6233   9573   5787  -1992    114    251       C  
ATOM   6898  CD  LYS A 844      31.492 -12.425  23.443  1.00 61.00           C  
ANISOU 6898  CD  LYS A 844     6772   9994   6413  -2016     52    258       C  
ATOM   6899  CE  LYS A 844      30.694 -11.238  23.971  1.00 58.89           C  
ANISOU 6899  CE  LYS A 844     6648   9517   6212  -2054    -42    337       C  
ATOM   6900  NZ  LYS A 844      31.099 -10.880  25.351  1.00 55.54           N  
ANISOU 6900  NZ  LYS A 844     6254   8973   5877  -2047   -103    303       N  
ATOM   6901  N   CYS A 845      28.691 -15.462  20.366  1.00 49.51           N  
ANISOU 6901  N   CYS A 845     5341   8760   4710  -1780    225     58       N  
ATOM   6902  CA  CYS A 845      27.497 -16.229  20.697  1.00 50.03           C  
ANISOU 6902  CA  CYS A 845     5477   8714   4819  -1668    209    -19       C  
ATOM   6903  C   CYS A 845      26.423 -16.109  19.633  1.00 50.62           C  
ANISOU 6903  C   CYS A 845     5598   8828   4808  -1702    192     22       C  
ATOM   6904  O   CYS A 845      26.423 -15.151  18.851  1.00 52.15           O  
ANISOU 6904  O   CYS A 845     5800   9086   4930  -1808    170    143       O  
ATOM   6905  CB  CYS A 845      26.923 -15.769  22.034  1.00 47.44           C  
ANISOU 6905  CB  CYS A 845     5230   8180   4614  -1615    136      9       C  
ATOM   6906  SG  CYS A 845      26.270 -14.112  21.961  1.00 48.47           S  
ANISOU 6906  SG  CYS A 845     5454   8203   4758  -1704     49    172       S  
ATOM   6907  N   ILE A 846      25.511 -17.084  19.622  1.00 48.71           N  
ANISOU 6907  N   ILE A 846     5385   8549   4575  -1617    199    -72       N  
ATOM   6908  CA  ILE A 846      24.354 -17.077  18.720  1.00 49.81           C  
ANISOU 6908  CA  ILE A 846     5565   8722   4640  -1641    170    -43       C  
ATOM   6909  C   ILE A 846      23.042 -17.392  19.466  1.00 47.74           C  
ANISOU 6909  C   ILE A 846     5370   8301   4470  -1556    119    -63       C  
ATOM   6910  O   ILE A 846      23.039 -18.101  20.484  1.00 45.63           O  
ANISOU 6910  O   ILE A 846     5108   7930   4299  -1466    131   -146       O  
ATOM   6911  CB  ILE A 846      24.560 -18.009  17.476  1.00 51.05           C  
ANISOU 6911  CB  ILE A 846     5669   9065   4661  -1662    238   -144       C  
ATOM   6912  CG1 ILE A 846      23.453 -17.781  16.436  1.00 50.90           C  
ANISOU 6912  CG1 ILE A 846     5687   9114   4540  -1718    194    -89       C  
ATOM   6913  CG2 ILE A 846      24.659 -19.483  17.899  1.00 52.78           C  
ANISOU 6913  CG2 ILE A 846     5873   9249   4933  -1556    291   -322       C  
ATOM   6914  CD1 ILE A 846      23.806 -18.213  15.029  1.00 53.82           C  
ANISOU 6914  CD1 ILE A 846     6009   9706   4734  -1782    251   -143       C  
ATOM   6915  N   ALA A 847      21.940 -16.847  18.955  1.00 46.95           N  
ANISOU 6915  N   ALA A 847     5311   8192   4335  -1585     61     24       N  
ATOM   6916  CA  ALA A 847      20.621 -17.053  19.548  1.00 46.11           C  
ANISOU 6916  CA  ALA A 847     5251   7964   4305  -1513     12     24       C  
ATOM   6917  C   ALA A 847      19.567 -17.305  18.478  1.00 48.37           C  
ANISOU 6917  C   ALA A 847     5535   8342   4500  -1547    -17     37       C  
ATOM   6918  O   ALA A 847      19.615 -16.711  17.399  1.00 50.38           O  
ANISOU 6918  O   ALA A 847     5780   8720   4643  -1631    -33    119       O  
ATOM   6919  CB  ALA A 847      20.238 -15.855  20.385  1.00 45.47           C  
ANISOU 6919  CB  ALA A 847     5225   7738   4313  -1491    -48    142       C  
ATOM   6920  N   TRP A 848      18.612 -18.180  18.774  1.00 46.36           N  
ANISOU 6920  N   TRP A 848     5287   8038   4288  -1491    -28    -37       N  
ATOM   6921  CA  TRP A 848      17.523 -18.447  17.840  1.00 48.10           C  
ANISOU 6921  CA  TRP A 848     5500   8347   4429  -1529    -69    -27       C  
ATOM   6922  C   TRP A 848      16.234 -18.696  18.626  1.00 47.38           C  
ANISOU 6922  C   TRP A 848     5424   8140   4440  -1461   -113    -17       C  
ATOM   6923  O   TRP A 848      16.306 -19.021  19.808  1.00 48.56           O  
ANISOU 6923  O   TRP A 848     5588   8160   4704  -1385    -92    -59       O  
ATOM   6924  CB  TRP A 848      17.878 -19.619  16.908  1.00 48.85           C  
ANISOU 6924  CB  TRP A 848     5566   8575   4418  -1571    -19   -174       C  
ATOM   6925  CG  TRP A 848      17.851 -20.961  17.574  1.00 47.05           C  
ANISOU 6925  CG  TRP A 848     5341   8260   4275  -1506     22   -329       C  
ATOM   6926  CD1 TRP A 848      16.885 -21.916  17.442  1.00 44.98           C  
ANISOU 6926  CD1 TRP A 848     5084   7982   4024  -1506      1   -409       C  
ATOM   6927  CD2 TRP A 848      18.825 -21.492  18.485  1.00 41.41           C  
ANISOU 6927  CD2 TRP A 848     4625   7458   3653  -1437     84   -409       C  
ATOM   6928  NE1 TRP A 848      17.201 -23.013  18.208  1.00 47.67           N  
ANISOU 6928  NE1 TRP A 848     5434   8216   4462  -1441     49   -532       N  
ATOM   6929  CE2 TRP A 848      18.384 -22.777  18.861  1.00 43.11           C  
ANISOU 6929  CE2 TRP A 848     4851   7596   3934  -1391     99   -531       C  
ATOM   6930  CE3 TRP A 848      20.033 -21.008  19.009  1.00 42.98           C  
ANISOU 6930  CE3 TRP A 848     4808   7639   3883  -1415    122   -385       C  
ATOM   6931  CZ2 TRP A 848      19.104 -23.591  19.746  1.00 42.85           C  
ANISOU 6931  CZ2 TRP A 848     4818   7464   3999  -1312    153   -620       C  
ATOM   6932  CZ3 TRP A 848      20.751 -21.814  19.892  1.00 42.33           C  
ANISOU 6932  CZ3 TRP A 848     4717   7476   3893  -1337    172   -478       C  
ATOM   6933  CH2 TRP A 848      20.283 -23.095  20.249  1.00 42.31           C  
ANISOU 6933  CH2 TRP A 848     4729   7393   3955  -1280    188   -590       C  
ATOM   6934  N   PRO A 849      15.057 -18.529  17.984  1.00 48.92           N  
ANISOU 6934  N   PRO A 849     5606   8395   4586  -1489   -176     47       N  
ATOM   6935  CA  PRO A 849      13.772 -18.615  18.710  1.00 49.04           C  
ANISOU 6935  CA  PRO A 849     5616   8319   4696  -1426   -220     81       C  
ATOM   6936  C   PRO A 849      13.598 -19.921  19.480  1.00 48.68           C  
ANISOU 6936  C   PRO A 849     5566   8198   4732  -1384   -181    -51       C  
ATOM   6937  O   PRO A 849      13.784 -21.001  18.919  1.00 49.62           O  
ANISOU 6937  O   PRO A 849     5674   8377   4801  -1429   -155   -174       O  
ATOM   6938  CB  PRO A 849      12.724 -18.507  17.595  1.00 48.18           C  
ANISOU 6938  CB  PRO A 849     5473   8342   4489  -1487   -288    144       C  
ATOM   6939  CG  PRO A 849      13.426 -17.772  16.492  1.00 50.00           C  
ANISOU 6939  CG  PRO A 849     5709   8698   4590  -1564   -295    212       C  
ATOM   6940  CD  PRO A 849      14.849 -18.254  16.548  1.00 49.44           C  
ANISOU 6940  CD  PRO A 849     5651   8634   4499  -1581   -211     97       C  
ATOM   6941  N   SER A 850      13.249 -19.803  20.761  1.00 48.36           N  
ANISOU 6941  N   SER A 850     5538   8022   4815  -1297   -177    -24       N  
ATOM   6942  CA  SER A 850      13.122 -20.949  21.649  1.00 49.61           C  
ANISOU 6942  CA  SER A 850     5696   8095   5061  -1254   -140   -121       C  
ATOM   6943  C   SER A 850      11.988 -21.878  21.235  1.00 52.06           C  
ANISOU 6943  C   SER A 850     5970   8447   5363  -1296   -169   -162       C  
ATOM   6944  O   SER A 850      10.983 -21.437  20.669  1.00 52.06           O  
ANISOU 6944  O   SER A 850     5936   8521   5322  -1326   -229    -82       O  
ATOM   6945  CB  SER A 850      12.904 -20.487  23.084  1.00 48.45           C  
ANISOU 6945  CB  SER A 850     5566   7818   5025  -1156   -132    -65       C  
ATOM   6946  OG  SER A 850      11.553 -20.121  23.290  1.00 50.71           O  
ANISOU 6946  OG  SER A 850     5825   8101   5342  -1127   -177     21       O  
ATOM   6947  N   GLY A 851      12.166 -23.163  21.530  1.00 54.20           N  
ANISOU 6947  N   GLY A 851     6247   8667   5678  -1299   -130   -281       N  
ATOM   6948  CA  GLY A 851      11.170 -24.190  21.235  1.00 59.45           C  
ANISOU 6948  CA  GLY A 851     6887   9348   6353  -1354   -156   -336       C  
ATOM   6949  C   GLY A 851      11.259 -24.713  19.818  1.00 62.98           C  
ANISOU 6949  C   GLY A 851     7332   9917   6680  -1455   -173   -429       C  
ATOM   6950  O   GLY A 851      10.394 -25.476  19.376  1.00 65.39           O  
ANISOU 6950  O   GLY A 851     7617  10255   6974  -1525   -211   -478       O  
ATOM   6951  N   THR A 852      12.304 -24.292  19.103  1.00 64.93           N  
ANISOU 6951  N   THR A 852     7598  10240   6833  -1471   -147   -454       N  
ATOM   6952  CA  THR A 852      12.517 -24.692  17.707  1.00 64.88           C  
ANISOU 6952  CA  THR A 852     7591  10374   6685  -1563   -153   -547       C  
ATOM   6953  C   THR A 852      13.952 -25.160  17.479  1.00 64.99           C  
ANISOU 6953  C   THR A 852     7634  10393   6666  -1545    -72   -671       C  
ATOM   6954  O   THR A 852      14.907 -24.565  17.994  1.00 63.35           O  
ANISOU 6954  O   THR A 852     7431  10152   6489  -1487    -29   -626       O  
ATOM   6955  CB  THR A 852      12.212 -23.540  16.698  1.00 65.52           C  
ANISOU 6955  CB  THR A 852     7646  10614   6633  -1619   -211   -426       C  
ATOM   6956  OG1 THR A 852      13.245 -22.547  16.768  1.00 64.33           O  
ANISOU 6956  OG1 THR A 852     7508  10474   6460  -1586   -177   -352       O  
ATOM   6957  CG2 THR A 852      10.840 -22.887  16.957  1.00 63.00           C  
ANISOU 6957  CG2 THR A 852     7286  10296   6354  -1612   -293   -280       C  
ATOM   6958  N   GLU A 853      14.091 -26.237  16.713  1.00 66.44           N  
ANISOU 6958  N   GLU A 853     7834  10621   6791  -1595    -51   -831       N  
ATOM   6959  CA  GLU A 853      15.378 -26.632  16.160  1.00 66.23           C  
ANISOU 6959  CA  GLU A 853     7821  10650   6693  -1584     27   -956       C  
ATOM   6960  C   GLU A 853      15.882 -25.471  15.303  1.00 66.19           C  
ANISOU 6960  C   GLU A 853     7789  10817   6541  -1626     25   -862       C  
ATOM   6961  O   GLU A 853      15.105 -24.870  14.551  1.00 65.03           O  
ANISOU 6961  O   GLU A 853     7626  10788   6293  -1701    -43   -778       O  
ATOM   6962  CB  GLU A 853      15.224 -27.892  15.297  1.00 67.57           C  
ANISOU 6962  CB  GLU A 853     8018  10854   6799  -1640     38  -1148       C  
ATOM   6963  CG  GLU A 853      14.862 -29.175  16.060  1.00 68.99           C  
ANISOU 6963  CG  GLU A 853     8236  10847   7131  -1608     46  -1254       C  
ATOM   6964  CD  GLU A 853      16.076 -29.953  16.580  1.00 70.12           C  
ANISOU 6964  CD  GLU A 853     8406  10878   7359  -1507    139  -1369       C  
ATOM   6965  OE1 GLU A 853      17.225 -29.486  16.420  1.00 67.59           O  
ANISOU 6965  OE1 GLU A 853     8064  10632   6986  -1458    199  -1367       O  
ATOM   6966  OE2 GLU A 853      15.874 -31.047  17.153  1.00 70.59           O  
ANISOU 6966  OE2 GLU A 853     8503  10775   7542  -1478    149  -1454       O  
ATOM   6967  N   ILE A 854      17.165 -25.136  15.438  1.00 65.63           N  
ANISOU 6967  N   ILE A 854     7708  10765   6462  -1583     94   -863       N  
ATOM   6968  CA  ILE A 854      17.741 -24.052  14.649  1.00 67.70           C  
ANISOU 6968  CA  ILE A 854     7944  11189   6591  -1634     99   -766       C  
ATOM   6969  C   ILE A 854      17.760 -24.442  13.165  1.00 70.59           C  
ANISOU 6969  C   ILE A 854     8305  11753   6765  -1719    110   -864       C  
ATOM   6970  O   ILE A 854      18.068 -25.588  12.819  1.00 72.56           O  
ANISOU 6970  O   ILE A 854     8570  12012   6989  -1709    162  -1051       O  
ATOM   6971  CB  ILE A 854      19.135 -23.608  15.170  1.00 67.40           C  
ANISOU 6971  CB  ILE A 854     7883  11134   6592  -1581    170   -740       C  
ATOM   6972  CG1 ILE A 854      19.593 -22.339  14.446  1.00 69.15           C  
ANISOU 6972  CG1 ILE A 854     8077  11505   6692  -1652    162   -600       C  
ATOM   6973  CG2 ILE A 854      20.166 -24.733  15.050  1.00 68.68           C  
ANISOU 6973  CG2 ILE A 854     8035  11309   6752  -1530    264   -924       C  
ATOM   6974  CD1 ILE A 854      20.650 -21.553  15.182  1.00 70.04           C  
ANISOU 6974  CD1 ILE A 854     8169  11571   6874  -1621    194   -513       C  
ATOM   6975  N   THR A 855      17.390 -23.495  12.303  1.00 70.53           N  
ANISOU 6975  N   THR A 855     8280  11898   6622  -1801     57   -736       N  
ATOM   6976  CA  THR A 855      17.233 -23.763  10.871  1.00 70.85           C  
ANISOU 6976  CA  THR A 855     8315  12148   6457  -1894     50   -807       C  
ATOM   6977  C   THR A 855      18.419 -24.544  10.297  1.00 71.42           C  
ANISOU 6977  C   THR A 855     8383  12317   6438  -1882    160   -990       C  
ATOM   6978  O   THR A 855      19.576 -24.305  10.664  1.00 70.46           O  
ANISOU 6978  O   THR A 855     8235  12185   6352  -1830    238   -981       O  
ATOM   6979  CB  THR A 855      16.948 -22.476  10.060  1.00 71.03           C  
ANISOU 6979  CB  THR A 855     8314  12335   6340  -1976    -11   -609       C  
ATOM   6980  OG1 THR A 855      16.760 -22.808   8.676  1.00 74.86           O  
ANISOU 6980  OG1 THR A 855     8794  13041   6609  -2069    -21   -683       O  
ATOM   6981  CG2 THR A 855      18.080 -21.461  10.209  1.00 69.57           C  
ANISOU 6981  CG2 THR A 855     8105  12177   6151  -1967     41   -485       C  
ATOM   6982  N   ASP A 856      18.108 -25.481   9.405  1.00 72.68           N  
ANISOU 6982  N   ASP A 856     8564  12572   6479  -1928    164  -1162       N  
ATOM   6983  CA  ASP A 856      19.084 -26.445   8.895  1.00 73.16           C  
ANISOU 6983  CA  ASP A 856     8631  12700   6466  -1897    271  -1379       C  
ATOM   6984  C   ASP A 856      20.298 -25.818   8.230  1.00 72.63           C  
ANISOU 6984  C   ASP A 856     8511  12832   6253  -1908    357  -1341       C  
ATOM   6985  O   ASP A 856      21.376 -26.419   8.207  1.00 73.33           O  
ANISOU 6985  O   ASP A 856     8582  12940   6339  -1840    466  -1481       O  
ATOM   6986  CB  ASP A 856      18.414 -27.427   7.931  1.00 76.35           C  
ANISOU 6986  CB  ASP A 856     9078  13188   6744  -1964    246  -1568       C  
ATOM   6987  CG  ASP A 856      17.891 -28.669   8.632  1.00 78.48           C  
ANISOU 6987  CG  ASP A 856     9403  13233   7183  -1917    232  -1725       C  
ATOM   6988  OD1 ASP A 856      16.811 -29.160   8.231  1.00 82.63           O  
ANISOU 6988  OD1 ASP A 856     9962  13761   7671  -1998    151  -1788       O  
ATOM   6989  OD2 ASP A 856      18.557 -29.158   9.576  1.00 76.81           O  
ANISOU 6989  OD2 ASP A 856     9199  12845   7140  -1807    298  -1779       O  
ATOM   6990  N   LEU A 857      20.126 -24.606   7.715  1.00 71.20           N  
ANISOU 6990  N   LEU A 857     8300  12793   5958  -1991    308  -1141       N  
ATOM   6991  CA  LEU A 857      21.176 -23.926   6.952  1.00 73.29           C  
ANISOU 6991  CA  LEU A 857     8511  13276   6061  -2033    381  -1075       C  
ATOM   6992  C   LEU A 857      22.428 -23.613   7.768  1.00 70.59           C  
ANISOU 6992  C   LEU A 857     8121  12862   5839  -1958    466  -1033       C  
ATOM   6993  O   LEU A 857      23.508 -23.435   7.206  1.00 71.35           O  
ANISOU 6993  O   LEU A 857     8160  13133   5818  -1972    558  -1045       O  
ATOM   6994  CB  LEU A 857      20.621 -22.657   6.292  1.00 75.25           C  
ANISOU 6994  CB  LEU A 857     8745  13665   6180  -2143    296   -841       C  
ATOM   6995  CG  LEU A 857      19.408 -22.922   5.381  1.00 80.61           C  
ANISOU 6995  CG  LEU A 857     9456  14458   6715  -2226    204   -870       C  
ATOM   6996  CD1 LEU A 857      18.489 -21.706   5.310  1.00 81.70           C  
ANISOU 6996  CD1 LEU A 857     9589  14607   6845  -2289     81   -606       C  
ATOM   6997  CD2 LEU A 857      19.814 -23.432   3.980  1.00 79.84           C  
ANISOU 6997  CD2 LEU A 857     9349  14638   6348  -2293    265  -1016       C  
ATOM   6998  N   ILE A 858      22.274 -23.560   9.089  1.00 67.20           N  
ANISOU 6998  N   ILE A 858     7708  12190   5634  -1882    434   -984       N  
ATOM   6999  CA  ILE A 858      23.366 -23.200   9.991  1.00 64.54           C  
ANISOU 6999  CA  ILE A 858     7327  11773   5423  -1817    491   -929       C  
ATOM   7000  C   ILE A 858      23.459 -24.104  11.220  1.00 61.51           C  
ANISOU 7000  C   ILE A 858     6964  11159   5248  -1693    509  -1044       C  
ATOM   7001  O   ILE A 858      24.348 -23.940  12.056  1.00 60.52           O  
ANISOU 7001  O   ILE A 858     6799  10961   5233  -1630    551  -1014       O  
ATOM   7002  CB  ILE A 858      23.270 -21.717  10.432  1.00 63.61           C  
ANISOU 7002  CB  ILE A 858     7200  11614   5355  -1871    423   -676       C  
ATOM   7003  CG1 ILE A 858      21.897 -21.423  11.050  1.00 61.39           C  
ANISOU 7003  CG1 ILE A 858     6981  11159   5185  -1866    307   -585       C  
ATOM   7004  CG2 ILE A 858      23.596 -20.788   9.249  1.00 67.39           C  
ANISOU 7004  CG2 ILE A 858     7642  12333   5632  -1990    431   -545       C  
ATOM   7005  CD1 ILE A 858      21.787 -20.076  11.730  1.00 59.50           C  
ANISOU 7005  CD1 ILE A 858     6749  10820   5039  -1883    244   -366       C  
ATOM   7006  N   LYS A 859      22.543 -25.059  11.327  1.00 62.03           N  
ANISOU 7006  N   LYS A 859     7089  11115   5364  -1666    473  -1166       N  
ATOM   7007  CA  LYS A 859      22.558 -26.008  12.439  1.00 61.10           C  
ANISOU 7007  CA  LYS A 859     6999  10777   5439  -1555    488  -1269       C  
ATOM   7008  C   LYS A 859      23.905 -26.730  12.518  1.00 61.77           C  
ANISOU 7008  C   LYS A 859     7040  10887   5544  -1460    604  -1408       C  
ATOM   7009  O   LYS A 859      24.492 -26.847  13.590  1.00 61.27           O  
ANISOU 7009  O   LYS A 859     6955  10693   5633  -1369    626  -1389       O  
ATOM   7010  CB  LYS A 859      21.407 -27.018  12.316  1.00 59.19           C  
ANISOU 7010  CB  LYS A 859     6826  10440   5225  -1564    439  -1393       C  
ATOM   7011  CG  LYS A 859      21.296 -27.952  13.512  1.00 58.29           C  
ANISOU 7011  CG  LYS A 859     6746  10084   5318  -1462    443  -1467       C  
ATOM   7012  CD  LYS A 859      20.284 -29.072  13.317  1.00 57.57           C  
ANISOU 7012  CD  LYS A 859     6721   9898   5255  -1484    404  -1606       C  
ATOM   7013  CE  LYS A 859      20.331 -30.010  14.525  1.00 57.41           C  
ANISOU 7013  CE  LYS A 859     6732   9636   5445  -1380    420  -1664       C  
ATOM   7014  NZ  LYS A 859      19.245 -31.028  14.568  1.00 52.99           N  
ANISOU 7014  NZ  LYS A 859     6238   8945   4951  -1414    369  -1762       N  
ATOM   7015  N   ASP A 860      24.384 -27.190  11.365  1.00 65.71           N  
ANISOU 7015  N   ASP A 860     7520  11568   5880  -1478    678  -1545       N  
ATOM   7016  CA  ASP A 860      25.643 -27.925  11.244  1.00 69.26           C  
ANISOU 7016  CA  ASP A 860     7918  12073   6324  -1378    799  -1696       C  
ATOM   7017  C   ASP A 860      26.839 -27.111  11.746  1.00 66.83           C  
ANISOU 7017  C   ASP A 860     7512  11828   6052  -1351    847  -1567       C  
ATOM   7018  O   ASP A 860      27.707 -27.632  12.446  1.00 64.65           O  
ANISOU 7018  O   ASP A 860     7192  11478   5893  -1235    907  -1626       O  
ATOM   7019  CB  ASP A 860      25.852 -28.353   9.784  1.00 73.65           C  
ANISOU 7019  CB  ASP A 860     8469  12854   6660  -1419    868  -1852       C  
ATOM   7020  CG  ASP A 860      24.586 -28.948   9.158  1.00 81.65           C  
ANISOU 7020  CG  ASP A 860     9577  13840   7606  -1487    799  -1959       C  
ATOM   7021  OD1 ASP A 860      24.658 -30.071   8.609  1.00 86.05           O  
ANISOU 7021  OD1 ASP A 860    10175  14403   8116  -1445    853  -2189       O  
ATOM   7022  OD2 ASP A 860      23.514 -28.297   9.219  1.00 83.47           O  
ANISOU 7022  OD2 ASP A 860     9841  14042   7833  -1582    688  -1817       O  
ATOM   7023  N   ASP A 861      26.857 -25.829  11.390  1.00 66.57           N  
ANISOU 7023  N   ASP A 861     7445  11929   5921  -1463    813  -1382       N  
ATOM   7024  CA  ASP A 861      27.916 -24.915  11.789  1.00 65.93           C  
ANISOU 7024  CA  ASP A 861     7273  11915   5862  -1475    844  -1240       C  
ATOM   7025  C   ASP A 861      27.862 -24.593  13.280  1.00 63.69           C  
ANISOU 7025  C   ASP A 861     7002  11407   5789  -1423    781  -1137       C  
ATOM   7026  O   ASP A 861      28.907 -24.488  13.929  1.00 62.96           O  
ANISOU 7026  O   ASP A 861     6836  11312   5775  -1369    823  -1113       O  
ATOM   7027  CB  ASP A 861      27.841 -23.618  10.975  1.00 67.56           C  
ANISOU 7027  CB  ASP A 861     7457  12301   5913  -1624    813  -1060       C  
ATOM   7028  CG  ASP A 861      28.134 -23.828   9.495  1.00 72.23           C  
ANISOU 7028  CG  ASP A 861     8013  13163   6268  -1681    890  -1143       C  
ATOM   7029  OD1 ASP A 861      27.350 -23.323   8.664  1.00 74.50           O  
ANISOU 7029  OD1 ASP A 861     8342  13550   6416  -1789    834  -1068       O  
ATOM   7030  OD2 ASP A 861      29.138 -24.493   9.160  1.00 72.46           O  
ANISOU 7030  OD2 ASP A 861     7971  13314   6245  -1613   1007  -1283       O  
ATOM   7031  N   VAL A 862      26.649 -24.430  13.815  1.00 60.31           N  
ANISOU 7031  N   VAL A 862     6662  10808   5444  -1440    680  -1076       N  
ATOM   7032  CA  VAL A 862      26.472 -24.089  15.229  1.00 56.66           C  
ANISOU 7032  CA  VAL A 862     6222  10142   5164  -1393    618   -980       C  
ATOM   7033  C   VAL A 862      26.948 -25.240  16.109  1.00 56.89           C  
ANISOU 7033  C   VAL A 862     6243  10040   5335  -1254    663  -1109       C  
ATOM   7034  O   VAL A 862      27.712 -25.034  17.051  1.00 54.60           O  
ANISOU 7034  O   VAL A 862     5906   9694   5146  -1200    670  -1058       O  
ATOM   7035  CB  VAL A 862      25.008 -23.696  15.567  1.00 54.51           C  
ANISOU 7035  CB  VAL A 862     6037   9734   4942  -1433    510   -891       C  
ATOM   7036  CG1 VAL A 862      24.796 -23.626  17.072  1.00 53.86           C  
ANISOU 7036  CG1 VAL A 862     5981   9440   5042  -1360    464   -835       C  
ATOM   7037  CG2 VAL A 862      24.664 -22.356  14.956  1.00 54.37           C  
ANISOU 7037  CG2 VAL A 862     6021   9816   4821  -1552    456   -720       C  
ATOM   7038  N   LEU A 863      26.510 -26.452  15.773  1.00 57.56           N  
ANISOU 7038  N   LEU A 863     6372  10076   5422  -1200    688  -1274       N  
ATOM   7039  CA  LEU A 863      26.922 -27.655  16.487  1.00 57.97           C  
ANISOU 7039  CA  LEU A 863     6426   9992   5607  -1063    732  -1401       C  
ATOM   7040  C   LEU A 863      28.435 -27.818  16.560  1.00 58.15           C  
ANISOU 7040  C   LEU A 863     6344  10115   5634   -982    824  -1441       C  
ATOM   7041  O   LEU A 863      28.963 -28.324  17.548  1.00 57.21           O  
ANISOU 7041  O   LEU A 863     6202   9881   5655   -870    837  -1456       O  
ATOM   7042  CB  LEU A 863      26.312 -28.897  15.836  1.00 59.51           C  
ANISOU 7042  CB  LEU A 863     6689  10142   5780  -1038    753  -1588       C  
ATOM   7043  CG  LEU A 863      24.834 -29.175  16.111  1.00 60.11           C  
ANISOU 7043  CG  LEU A 863     6862  10062   5916  -1083    663  -1577       C  
ATOM   7044  CD1 LEU A 863      24.447 -30.515  15.513  1.00 62.99           C  
ANISOU 7044  CD1 LEU A 863     7289  10371   6272  -1058    690  -1781       C  
ATOM   7045  CD2 LEU A 863      24.556 -29.157  17.605  1.00 59.01           C  
ANISOU 7045  CD2 LEU A 863     6742   9719   5961  -1022    611  -1476       C  
ATOM   7046  N   HIS A 864      29.125 -27.387  15.512  1.00 59.59           N  
ANISOU 7046  N   HIS A 864     6456  10526   5660  -1038    888  -1450       N  
ATOM   7047  CA  HIS A 864      30.562 -27.595  15.405  1.00 62.58           C  
ANISOU 7047  CA  HIS A 864     6716  11038   6022   -962    989  -1500       C  
ATOM   7048  C   HIS A 864      31.357 -26.523  16.150  1.00 61.91           C  
ANISOU 7048  C   HIS A 864     6544  10996   5985   -998    966  -1325       C  
ATOM   7049  O   HIS A 864      32.473 -26.783  16.609  1.00 62.26           O  
ANISOU 7049  O   HIS A 864     6488  11079   6089   -910   1020  -1343       O  
ATOM   7050  CB  HIS A 864      30.979 -27.660  13.934  1.00 65.67           C  
ANISOU 7050  CB  HIS A 864     7060  11678   6212  -1007   1080  -1593       C  
ATOM   7051  CG  HIS A 864      32.386 -28.124  13.725  1.00 72.09           C  
ANISOU 7051  CG  HIS A 864     7748  12637   7006   -903   1203  -1684       C  
ATOM   7052  ND1 HIS A 864      33.423 -27.257  13.446  1.00 73.27           N  
ANISOU 7052  ND1 HIS A 864     7765  13003   7070   -962   1252  -1577       N  
ATOM   7053  CD2 HIS A 864      32.930 -29.363  13.762  1.00 74.06           C  
ANISOU 7053  CD2 HIS A 864     7977  12847   7317   -742   1286  -1867       C  
ATOM   7054  CE1 HIS A 864      34.544 -27.943  13.319  1.00 75.29           C  
ANISOU 7054  CE1 HIS A 864     7913  13364   7330   -837   1365  -1690       C  
ATOM   7055  NE2 HIS A 864      34.273 -29.223  13.506  1.00 76.55           N  
ANISOU 7055  NE2 HIS A 864     8141  13366   7580   -694   1388  -1869       N  
ATOM   7056  N   TRP A 865      30.772 -25.331  16.283  1.00 59.46           N  
ANISOU 7056  N   TRP A 865     6271  10670   5651  -1125    880  -1159       N  
ATOM   7057  CA  TRP A 865      31.469 -24.186  16.870  1.00 56.23           C  
ANISOU 7057  CA  TRP A 865     5793  10299   5271  -1190    848   -994       C  
ATOM   7058  C   TRP A 865      30.999 -23.836  18.287  1.00 53.95           C  
ANISOU 7058  C   TRP A 865     5565   9794   5142  -1168    751   -902       C  
ATOM   7059  O   TRP A 865      31.483 -22.869  18.883  1.00 52.20           O  
ANISOU 7059  O   TRP A 865     5306   9575   4954  -1226    710   -774       O  
ATOM   7060  CB  TRP A 865      31.390 -22.962  15.943  1.00 55.86           C  
ANISOU 7060  CB  TRP A 865     5735  10412   5078  -1355    833   -863       C  
ATOM   7061  CG  TRP A 865      32.312 -23.041  14.740  1.00 59.58           C  
ANISOU 7061  CG  TRP A 865     6101  11151   5386  -1388    942   -910       C  
ATOM   7062  CD1 TRP A 865      31.961 -23.367  13.452  1.00 62.50           C  
ANISOU 7062  CD1 TRP A 865     6490  11667   5590  -1423    991   -992       C  
ATOM   7063  CD2 TRP A 865      33.728 -22.802  14.716  1.00 59.53           C  
ANISOU 7063  CD2 TRP A 865     5947  11314   5358  -1391   1017   -881       C  
ATOM   7064  NE1 TRP A 865      33.066 -23.342  12.634  1.00 62.39           N  
ANISOU 7064  NE1 TRP A 865     6353  11904   5447  -1442   1100  -1017       N  
ATOM   7065  CE2 TRP A 865      34.164 -22.999  13.380  1.00 63.17           C  
ANISOU 7065  CE2 TRP A 865     6342  12025   5635  -1423   1119   -946       C  
ATOM   7066  CE3 TRP A 865      34.672 -22.440  15.691  1.00 59.64           C  
ANISOU 7066  CE3 TRP A 865     5870  11307   5482  -1374   1005   -805       C  
ATOM   7067  CZ2 TRP A 865      35.505 -22.841  12.993  1.00 64.07           C  
ANISOU 7067  CZ2 TRP A 865     6294  12370   5677  -1435   1219   -932       C  
ATOM   7068  CZ3 TRP A 865      36.006 -22.285  15.307  1.00 62.24           C  
ANISOU 7068  CZ3 TRP A 865     6037  11864   5747  -1393   1094   -789       C  
ATOM   7069  CH2 TRP A 865      36.408 -22.486  13.966  1.00 63.61           C  
ANISOU 7069  CH2 TRP A 865     6140  12287   5741  -1420   1204   -850       C  
ATOM   7070  N   MET A 866      30.073 -24.629  18.823  1.00 52.40           N  
ANISOU 7070  N   MET A 866     5459   9413   5035  -1090    715   -970       N  
ATOM   7071  CA  MET A 866      29.588 -24.459  20.200  1.00 50.68           C  
ANISOU 7071  CA  MET A 866     5298   8998   4960  -1052    634   -899       C  
ATOM   7072  C   MET A 866      30.737 -24.502  21.178  1.00 49.39           C  
ANISOU 7072  C   MET A 866     5050   8831   4885   -982    647   -877       C  
ATOM   7073  O   MET A 866      31.571 -25.401  21.113  1.00 49.77           O  
ANISOU 7073  O   MET A 866     5026   8931   4954   -882    718   -974       O  
ATOM   7074  CB  MET A 866      28.692 -25.616  20.602  1.00 50.43           C  
ANISOU 7074  CB  MET A 866     5348   8797   5015   -960    622   -996       C  
ATOM   7075  CG  MET A 866      27.364 -25.689  19.974  1.00 51.61           C  
ANISOU 7075  CG  MET A 866     5588   8907   5115  -1020    586  -1014       C  
ATOM   7076  SD  MET A 866      26.688 -27.265  20.480  1.00 53.07           S  
ANISOU 7076  SD  MET A 866     5842   8905   5419   -907    591  -1145       S  
ATOM   7077  CE  MET A 866      26.229 -26.923  22.182  1.00 48.72           C  
ANISOU 7077  CE  MET A 866     5328   8168   5016   -866    513  -1021       C  
ATOM   7078  N   ASP A 867      30.765 -23.566  22.113  1.00 49.02           N  
ANISOU 7078  N   ASP A 867     5014   8720   4893  -1026    574   -755       N  
ATOM   7079  CA  ASP A 867      31.791 -23.606  23.139  1.00 49.15           C  
ANISOU 7079  CA  ASP A 867     4951   8732   4990   -966    569   -731       C  
ATOM   7080  C   ASP A 867      31.268 -24.342  24.370  1.00 48.37           C  
ANISOU 7080  C   ASP A 867     4916   8445   5016   -853    528   -752       C  
ATOM   7081  O   ASP A 867      30.791 -23.726  25.326  1.00 46.83           O  
ANISOU 7081  O   ASP A 867     4780   8142   4872   -877    452   -671       O  
ATOM   7082  CB  ASP A 867      32.259 -22.197  23.487  1.00 50.05           C  
ANISOU 7082  CB  ASP A 867     5037   8892   5088  -1086    513   -597       C  
ATOM   7083  CG  ASP A 867      33.650 -22.178  24.090  1.00 52.84           C  
ANISOU 7083  CG  ASP A 867     5262   9336   5478  -1059    525   -581       C  
ATOM   7084  OD1 ASP A 867      34.010 -23.131  24.825  1.00 52.16           O  
ANISOU 7084  OD1 ASP A 867     5141   9204   5473   -926    539   -639       O  
ATOM   7085  OD2 ASP A 867      34.377 -21.193  23.834  1.00 52.18           O  
ANISOU 7085  OD2 ASP A 867     5109   9372   5344  -1177    517   -499       O  
ATOM   7086  N   TYR A 868      31.356 -25.670  24.325  1.00 49.19           N  
ANISOU 7086  N   TYR A 868     5011   8510   5169   -729    581   -863       N  
ATOM   7087  CA  TYR A 868      30.969 -26.522  25.444  1.00 48.97           C  
ANISOU 7087  CA  TYR A 868     5033   8311   5261   -617    552   -878       C  
ATOM   7088  C   TYR A 868      31.694 -26.125  26.725  1.00 49.43           C  
ANISOU 7088  C   TYR A 868     5040   8358   5383   -586    503   -792       C  
ATOM   7089  O   TYR A 868      31.124 -26.206  27.803  1.00 50.12           O  
ANISOU 7089  O   TYR A 868     5193   8313   5540   -551    446   -747       O  
ATOM   7090  CB  TYR A 868      31.269 -27.993  25.139  1.00 50.76           C  
ANISOU 7090  CB  TYR A 868     5241   8509   5537   -484    625  -1008       C  
ATOM   7091  CG  TYR A 868      30.370 -28.655  24.104  1.00 52.40           C  
ANISOU 7091  CG  TYR A 868     5528   8678   5704   -499    660  -1116       C  
ATOM   7092  CD1 TYR A 868      29.143 -29.217  24.467  1.00 51.18           C  
ANISOU 7092  CD1 TYR A 868     5485   8348   5613   -490    619  -1129       C  
ATOM   7093  CD2 TYR A 868      30.769 -28.754  22.766  1.00 52.29           C  
ANISOU 7093  CD2 TYR A 868     5470   8816   5582   -527    734  -1209       C  
ATOM   7094  CE1 TYR A 868      28.323 -29.845  23.514  1.00 52.34           C  
ANISOU 7094  CE1 TYR A 868     5700   8464   5722   -517    642  -1234       C  
ATOM   7095  CE2 TYR A 868      29.961 -29.370  21.807  1.00 51.53           C  
ANISOU 7095  CE2 TYR A 868     5449   8694   5435   -548    759  -1320       C  
ATOM   7096  CZ  TYR A 868      28.741 -29.915  22.187  1.00 53.33           C  
ANISOU 7096  CZ  TYR A 868     5789   8740   5735   -547    709  -1334       C  
ATOM   7097  OH  TYR A 868      27.944 -30.527  21.240  1.00 51.82           O  
ANISOU 7097  OH  TYR A 868     5668   8529   5492   -582    724  -1448       O  
ATOM   7098  N   THR A 869      32.953 -25.700  26.604  1.00 52.23           N  
ANISOU 7098  N   THR A 869     5273   8867   5707   -604    524   -770       N  
ATOM   7099  CA  THR A 869      33.757 -25.352  27.777  1.00 51.99           C  
ANISOU 7099  CA  THR A 869     5177   8850   5727   -583    472   -695       C  
ATOM   7100  C   THR A 869      33.216 -24.106  28.455  1.00 49.92           C  
ANISOU 7100  C   THR A 869     4989   8528   5451   -696    381   -596       C  
ATOM   7101  O   THR A 869      33.002 -24.104  29.660  1.00 49.94           O  
ANISOU 7101  O   THR A 869     5032   8433   5510   -656    320   -555       O  
ATOM   7102  CB  THR A 869      35.258 -25.164  27.445  1.00 54.11           C  
ANISOU 7102  CB  THR A 869     5278   9318   5963   -589    514   -690       C  
ATOM   7103  OG1 THR A 869      35.731 -26.276  26.677  1.00 56.13           O  
ANISOU 7103  OG1 THR A 869     5466   9638   6222   -476    612   -797       O  
ATOM   7104  CG2 THR A 869      36.085 -25.067  28.726  1.00 57.13           C  
ANISOU 7104  CG2 THR A 869     5585   9713   6408   -546    454   -626       C  
ATOM   7105  N   VAL A 870      32.990 -23.049  27.682  1.00 49.41           N  
ANISOU 7105  N   VAL A 870     4947   8520   5309   -834    373   -556       N  
ATOM   7106  CA  VAL A 870      32.367 -21.847  28.231  1.00 47.95           C  
ANISOU 7106  CA  VAL A 870     4850   8252   5117   -933    290   -471       C  
ATOM   7107  C   VAL A 870      30.966 -22.162  28.771  1.00 47.87           C  
ANISOU 7107  C   VAL A 870     4971   8068   5150   -879    258   -479       C  
ATOM   7108  O   VAL A 870      30.594 -21.726  29.865  1.00 49.72           O  
ANISOU 7108  O   VAL A 870     5264   8206   5420   -874    194   -434       O  
ATOM   7109  CB  VAL A 870      32.332 -20.706  27.196  1.00 46.20           C  
ANISOU 7109  CB  VAL A 870     4634   8109   4811  -1084    289   -418       C  
ATOM   7110  CG1 VAL A 870      31.322 -19.636  27.578  1.00 46.84           C  
ANISOU 7110  CG1 VAL A 870     4840   8061   4897  -1158    212   -347       C  
ATOM   7111  CG2 VAL A 870      33.701 -20.099  27.057  1.00 44.58           C  
ANISOU 7111  CG2 VAL A 870     4305   8059   4576  -1166    294   -375       C  
ATOM   7112  N   LEU A 871      30.213 -22.946  28.010  1.00 48.41           N  
ANISOU 7112  N   LEU A 871     5079   8106   5210   -841    305   -540       N  
ATOM   7113  CA  LEU A 871      28.838 -23.302  28.356  1.00 47.97           C  
ANISOU 7113  CA  LEU A 871     5130   7905   5191   -804    281   -545       C  
ATOM   7114  C   LEU A 871      28.759 -23.942  29.735  1.00 48.33           C  
ANISOU 7114  C   LEU A 871     5196   7847   5322   -701    255   -537       C  
ATOM   7115  O   LEU A 871      27.990 -23.502  30.596  1.00 48.16           O  
ANISOU 7115  O   LEU A 871     5246   7731   5320   -703    204   -486       O  
ATOM   7116  CB  LEU A 871      28.292 -24.276  27.320  1.00 47.77           C  
ANISOU 7116  CB  LEU A 871     5121   7881   5149   -778    338   -630       C  
ATOM   7117  CG  LEU A 871      26.891 -24.073  26.755  1.00 49.86           C  
ANISOU 7117  CG  LEU A 871     5473   8089   5383   -832    318   -622       C  
ATOM   7118  CD1 LEU A 871      26.424 -25.392  26.168  1.00 47.63           C  
ANISOU 7118  CD1 LEU A 871     5208   7773   5116   -779    365   -725       C  
ATOM   7119  CD2 LEU A 871      25.883 -23.538  27.773  1.00 44.79           C  
ANISOU 7119  CD2 LEU A 871     4908   7323   4785   -830    254   -546       C  
ATOM   7120  N   LEU A 872      29.568 -24.980  29.928  1.00 48.96           N  
ANISOU 7120  N   LEU A 872     5207   7949   5446   -604    293   -585       N  
ATOM   7121  CA  LEU A 872      29.621 -25.716  31.180  1.00 49.67           C  
ANISOU 7121  CA  LEU A 872     5304   7954   5615   -498    271   -567       C  
ATOM   7122  C   LEU A 872      30.005 -24.833  32.375  1.00 49.53           C  
ANISOU 7122  C   LEU A 872     5281   7948   5592   -521    200   -489       C  
ATOM   7123  O   LEU A 872      29.346 -24.886  33.418  1.00 50.96           O  
ANISOU 7123  O   LEU A 872     5527   8034   5800   -486    161   -449       O  
ATOM   7124  CB  LEU A 872      30.582 -26.898  31.045  1.00 49.77           C  
ANISOU 7124  CB  LEU A 872     5232   8002   5677   -386    324   -625       C  
ATOM   7125  CG  LEU A 872      30.802 -27.806  32.254  1.00 49.49           C  
ANISOU 7125  CG  LEU A 872     5189   7886   5728   -261    305   -596       C  
ATOM   7126  CD1 LEU A 872      29.575 -28.655  32.543  1.00 47.89           C  
ANISOU 7126  CD1 LEU A 872     5092   7521   5584   -217    307   -602       C  
ATOM   7127  CD2 LEU A 872      32.012 -28.681  32.007  1.00 50.52           C  
ANISOU 7127  CD2 LEU A 872     5210   8084   5900   -154    355   -643       C  
ATOM   7128  N   GLU A 873      31.060 -24.030  32.215  1.00 49.69           N  
ANISOU 7128  N   GLU A 873     5221   8088   5571   -587    185   -469       N  
ATOM   7129  CA  GLU A 873      31.521 -23.094  33.250  1.00 50.47           C  
ANISOU 7129  CA  GLU A 873     5314   8207   5656   -634    111   -408       C  
ATOM   7130  C   GLU A 873      30.442 -22.099  33.643  1.00 49.71           C  
ANISOU 7130  C   GLU A 873     5338   8014   5536   -702     60   -373       C  
ATOM   7131  O   GLU A 873      30.149 -21.930  34.824  1.00 48.65           O  
ANISOU 7131  O   GLU A 873     5254   7819   5411   -671     10   -345       O  
ATOM   7132  CB  GLU A 873      32.762 -22.328  32.784  1.00 52.29           C  
ANISOU 7132  CB  GLU A 873     5438   8586   5845   -725    105   -394       C  
ATOM   7133  CG  GLU A 873      34.063 -23.125  32.856  1.00 58.08           C  
ANISOU 7133  CG  GLU A 873     6026   9438   6604   -646    134   -410       C  
ATOM   7134  CD  GLU A 873      34.565 -23.337  34.289  1.00 60.42           C  
ANISOU 7134  CD  GLU A 873     6291   9731   6934   -580     69   -371       C  
ATOM   7135  OE1 GLU A 873      35.321 -24.312  34.501  1.00 62.18           O  
ANISOU 7135  OE1 GLU A 873     6417  10009   7201   -465     93   -380       O  
ATOM   7136  OE2 GLU A 873      34.214 -22.538  35.194  1.00 57.63           O  
ANISOU 7136  OE2 GLU A 873     6010   9325   6560   -636     -7   -332       O  
ATOM   7137  N   LYS A 874      29.843 -21.465  32.638  1.00 50.75           N  
ANISOU 7137  N   LYS A 874     5514   8137   5631   -785     75   -373       N  
ATOM   7138  CA  LYS A 874      28.837 -20.426  32.845  1.00 51.53           C  
ANISOU 7138  CA  LYS A 874     5721   8147   5712   -844     31   -336       C  
ATOM   7139  C   LYS A 874      27.566 -20.926  33.524  1.00 49.41           C  
ANISOU 7139  C   LYS A 874     5537   7761   5475   -762     29   -337       C  
ATOM   7140  O   LYS A 874      27.097 -20.320  34.488  1.00 49.85           O  
ANISOU 7140  O   LYS A 874     5659   7752   5529   -756    -17   -310       O  
ATOM   7141  CB  LYS A 874      28.469 -19.785  31.511  1.00 51.81           C  
ANISOU 7141  CB  LYS A 874     5773   8209   5704   -937     50   -324       C  
ATOM   7142  CG  LYS A 874      29.087 -18.429  31.282  1.00 59.01           C  
ANISOU 7142  CG  LYS A 874     6679   9161   6581  -1062      9   -275       C  
ATOM   7143  CD  LYS A 874      28.759 -17.899  29.882  1.00 66.51           C  
ANISOU 7143  CD  LYS A 874     7638  10151   7481  -1151     32   -246       C  
ATOM   7144  CE  LYS A 874      27.274 -18.052  29.540  1.00 66.94           C  
ANISOU 7144  CE  LYS A 874     7780  10118   7538  -1114     38   -245       C  
ATOM   7145  NZ  LYS A 874      26.931 -17.316  28.301  1.00 71.24           N  
ANISOU 7145  NZ  LYS A 874     8341  10698   8027  -1208     40   -195       N  
ATOM   7146  N   THR A 875      27.020 -22.031  33.015  1.00 46.44           N  
ANISOU 7146  N   THR A 875     5158   7362   5124   -704     80   -370       N  
ATOM   7147  CA  THR A 875      25.679 -22.472  33.395  1.00 43.14           C  
ANISOU 7147  CA  THR A 875     4814   6844   4735   -655     83   -362       C  
ATOM   7148  C   THR A 875      25.671 -23.498  34.520  1.00 42.53           C  
ANISOU 7148  C   THR A 875     4734   6718   4708   -553     86   -356       C  
ATOM   7149  O   THR A 875      24.723 -23.548  35.299  1.00 42.48           O  
ANISOU 7149  O   THR A 875     4786   6641   4713   -519     74   -324       O  
ATOM   7150  CB  THR A 875      24.862 -22.989  32.164  1.00 43.57           C  
ANISOU 7150  CB  THR A 875     4879   6889   4785   -675    124   -394       C  
ATOM   7151  OG1 THR A 875      25.552 -24.069  31.513  1.00 41.51           O  
ANISOU 7151  OG1 THR A 875     4558   6673   4542   -642    174   -458       O  
ATOM   7152  CG2 THR A 875      24.655 -21.864  31.170  1.00 40.19           C  
ANISOU 7152  CG2 THR A 875     4466   6505   4298   -774    110   -373       C  
ATOM   7153  N   PHE A 876      26.736 -24.291  34.624  1.00 42.04           N  
ANISOU 7153  N   PHE A 876     4600   6700   4672   -501    104   -377       N  
ATOM   7154  CA  PHE A 876      26.769 -25.378  35.593  1.00 40.57           C  
ANISOU 7154  CA  PHE A 876     4409   6464   4541   -398    107   -359       C  
ATOM   7155  C   PHE A 876      27.790 -25.201  36.727  1.00 41.35           C  
ANISOU 7155  C   PHE A 876     4463   6617   4631   -361     62   -321       C  
ATOM   7156  O   PHE A 876      27.435 -25.307  37.905  1.00 43.06           O  
ANISOU 7156  O   PHE A 876     4716   6796   4847   -316     32   -273       O  
ATOM   7157  CB  PHE A 876      26.959 -26.718  34.873  1.00 40.75           C  
ANISOU 7157  CB  PHE A 876     4398   6462   4623   -339    164   -411       C  
ATOM   7158  CG  PHE A 876      27.008 -27.904  35.795  1.00 41.91           C  
ANISOU 7158  CG  PHE A 876     4545   6538   4841   -231    167   -380       C  
ATOM   7159  CD1 PHE A 876      25.852 -28.369  36.416  1.00 40.06           C  
ANISOU 7159  CD1 PHE A 876     4382   6202   4638   -211    164   -337       C  
ATOM   7160  CD2 PHE A 876      28.209 -28.562  36.036  1.00 40.60           C  
ANISOU 7160  CD2 PHE A 876     4301   6411   4713   -148    173   -383       C  
ATOM   7161  CE1 PHE A 876      25.892 -29.465  37.271  1.00 38.08           C  
ANISOU 7161  CE1 PHE A 876     4134   5880   4453   -120    166   -290       C  
ATOM   7162  CE2 PHE A 876      28.255 -29.659  36.880  1.00 41.97           C  
ANISOU 7162  CE2 PHE A 876     4478   6510   4958    -44    172   -339       C  
ATOM   7163  CZ  PHE A 876      27.089 -30.109  37.504  1.00 38.90           C  
ANISOU 7163  CZ  PHE A 876     4171   6011   4599    -35    167   -289       C  
ATOM   7164  N   ILE A 877      29.042 -24.924  36.376  1.00 40.09           N  
ANISOU 7164  N   ILE A 877     4216   6560   4455   -384     57   -338       N  
ATOM   7165  CA  ILE A 877      30.115 -24.853  37.370  1.00 40.05           C  
ANISOU 7165  CA  ILE A 877     4146   6628   4443   -351      8   -303       C  
ATOM   7166  C   ILE A 877      29.990 -23.639  38.298  1.00 39.31           C  
ANISOU 7166  C   ILE A 877     4104   6545   4289   -418    -63   -272       C  
ATOM   7167  O   ILE A 877      30.134 -23.768  39.513  1.00 37.88           O  
ANISOU 7167  O   ILE A 877     3929   6369   4093   -371   -108   -234       O  
ATOM   7168  CB  ILE A 877      31.528 -24.954  36.708  1.00 40.61           C  
ANISOU 7168  CB  ILE A 877     4087   6824   4519   -356     26   -328       C  
ATOM   7169  CG1 ILE A 877      31.762 -26.377  36.200  1.00 40.29           C  
ANISOU 7169  CG1 ILE A 877     3997   6763   4548   -242     92   -362       C  
ATOM   7170  CG2 ILE A 877      32.649 -24.570  37.692  1.00 42.04           C  
ANISOU 7170  CG2 ILE A 877     4189   7106   4677   -357    -42   -285       C  
ATOM   7171  CD1 ILE A 877      32.931 -26.514  35.230  1.00 46.43           C  
ANISOU 7171  CD1 ILE A 877     4651   7665   5326   -239    137   -408       C  
ATOM   7172  N   LYS A 878      29.713 -22.470  37.725  1.00 40.80           N  
ANISOU 7172  N   LYS A 878     4334   6731   4437   -526    -75   -288       N  
ATOM   7173  CA  LYS A 878      29.621 -21.239  38.506  1.00 43.10           C  
ANISOU 7173  CA  LYS A 878     4686   7014   4677   -593   -143   -275       C  
ATOM   7174  C   LYS A 878      28.491 -21.285  39.550  1.00 42.20           C  
ANISOU 7174  C   LYS A 878     4672   6812   4549   -535   -155   -258       C  
ATOM   7175  O   LYS A 878      28.716 -20.928  40.705  1.00 41.73           O  
ANISOU 7175  O   LYS A 878     4634   6772   4448   -526   -209   -247       O  
ATOM   7176  CB  LYS A 878      29.486 -20.011  37.602  1.00 43.05           C  
ANISOU 7176  CB  LYS A 878     4715   6998   4647   -715   -150   -288       C  
ATOM   7177  CG  LYS A 878      30.327 -18.843  38.072  1.00 50.12           C  
ANISOU 7177  CG  LYS A 878     5603   7936   5503   -813   -223   -285       C  
ATOM   7178  CD  LYS A 878      29.550 -17.544  38.039  1.00 55.95           C  
ANISOU 7178  CD  LYS A 878     6458   8579   6220   -889   -255   -288       C  
ATOM   7179  CE  LYS A 878      30.395 -16.394  38.569  1.00 58.94           C  
ANISOU 7179  CE  LYS A 878     6844   8981   6569   -997   -335   -294       C  
ATOM   7180  NZ  LYS A 878      29.634 -15.585  39.571  1.00 60.13           N  
ANISOU 7180  NZ  LYS A 878     7125   9028   6693   -988   -383   -320       N  
ATOM   7181  N   PRO A 879      27.288 -21.741  39.152  1.00 40.30           N  
ANISOU 7181  N   PRO A 879     4486   6491   4336   -498   -104   -256       N  
ATOM   7182  CA  PRO A 879      26.218 -21.920  40.134  1.00 41.65           C  
ANISOU 7182  CA  PRO A 879     4731   6600   4495   -437   -103   -231       C  
ATOM   7183  C   PRO A 879      26.579 -22.922  41.233  1.00 43.80           C  
ANISOU 7183  C   PRO A 879     4971   6897   4772   -347   -112   -191       C  
ATOM   7184  O   PRO A 879      26.371 -22.635  42.415  1.00 45.93           O  
ANISOU 7184  O   PRO A 879     5283   7177   4989   -322   -146   -169       O  
ATOM   7185  CB  PRO A 879      25.055 -22.458  39.293  1.00 39.90           C  
ANISOU 7185  CB  PRO A 879     4536   6309   4316   -423    -45   -231       C  
ATOM   7186  CG  PRO A 879      25.309 -21.931  37.931  1.00 40.85           C  
ANISOU 7186  CG  PRO A 879     4635   6447   4439   -503    -34   -263       C  
ATOM   7187  CD  PRO A 879      26.800 -21.947  37.772  1.00 41.18           C  
ANISOU 7187  CD  PRO A 879     4593   6576   4476   -527    -52   -278       C  
ATOM   7188  N   LEU A 880      27.123 -24.076  40.848  1.00 43.22           N  
ANISOU 7188  N   LEU A 880     4828   6836   4758   -296    -83   -180       N  
ATOM   7189  CA  LEU A 880      27.514 -25.091  41.816  1.00 43.85           C  
ANISOU 7189  CA  LEU A 880     4874   6932   4855   -203    -94   -126       C  
ATOM   7190  C   LEU A 880      28.583 -24.586  42.790  1.00 47.04           C  
ANISOU 7190  C   LEU A 880     5237   7438   5198   -208   -166   -108       C  
ATOM   7191  O   LEU A 880      28.507 -24.856  44.002  1.00 46.92           O  
ANISOU 7191  O   LEU A 880     5240   7443   5146   -154   -197    -55       O  
ATOM   7192  CB  LEU A 880      27.984 -26.363  41.115  1.00 43.49           C  
ANISOU 7192  CB  LEU A 880     4762   6865   4896   -141    -49   -128       C  
ATOM   7193  CG  LEU A 880      28.182 -27.595  42.004  1.00 42.89           C  
ANISOU 7193  CG  LEU A 880     4665   6767   4865    -31    -52    -56       C  
ATOM   7194  CD1 LEU A 880      26.884 -27.986  42.682  1.00 41.10           C  
ANISOU 7194  CD1 LEU A 880     4522   6456   4638     -9    -35     -1       C  
ATOM   7195  CD2 LEU A 880      28.727 -28.751  41.184  1.00 44.97           C  
ANISOU 7195  CD2 LEU A 880     4869   6993   5225     35     -7    -78       C  
ATOM   7196  N   GLU A 881      29.558 -23.848  42.252  1.00 47.00           N  
ANISOU 7196  N   GLU A 881     5174   7505   5177   -280   -195   -148       N  
ATOM   7197  CA  GLU A 881      30.594 -23.177  43.041  1.00 48.47           C  
ANISOU 7197  CA  GLU A 881     5316   7796   5303   -319   -274   -142       C  
ATOM   7198  C   GLU A 881      29.958 -22.370  44.166  1.00 44.77           C  
ANISOU 7198  C   GLU A 881     4948   7312   4751   -341   -322   -144       C  
ATOM   7199  O   GLU A 881      30.363 -22.471  45.317  1.00 42.33           O  
ANISOU 7199  O   GLU A 881     4628   7070   4386   -309   -377   -113       O  
ATOM   7200  CB  GLU A 881      31.401 -22.238  42.140  1.00 53.84           C  
ANISOU 7200  CB  GLU A 881     5945   8535   5978   -432   -291   -188       C  
ATOM   7201  CG  GLU A 881      32.707 -21.734  42.736  1.00 63.84           C  
ANISOU 7201  CG  GLU A 881     7128   9928   7201   -483   -373   -181       C  
ATOM   7202  CD  GLU A 881      33.875 -22.647  42.398  1.00 74.68           C  
ANISOU 7202  CD  GLU A 881     8348  11404   8624   -424   -359   -153       C  
ATOM   7203  OE1 GLU A 881      34.520 -23.161  43.345  1.00 76.36           O  
ANISOU 7203  OE1 GLU A 881     8497  11694   8823   -357   -409   -106       O  
ATOM   7204  OE2 GLU A 881      34.138 -22.855  41.182  1.00 76.07           O  
ANISOU 7204  OE2 GLU A 881     8465  11590   8848   -437   -298   -177       O  
ATOM   7205  N   GLY A 882      28.949 -21.576  43.809  1.00 43.89           N  
ANISOU 7205  N   GLY A 882     4933   7117   4626   -390   -299   -183       N  
ATOM   7206  CA  GLY A 882      28.174 -20.798  44.767  1.00 42.52           C  
ANISOU 7206  CA  GLY A 882     4865   6914   4378   -395   -325   -200       C  
ATOM   7207  C   GLY A 882      27.459 -21.645  45.806  1.00 41.77           C  
ANISOU 7207  C   GLY A 882     4799   6815   4255   -294   -304   -145       C  
ATOM   7208  O   GLY A 882      27.518 -21.337  46.994  1.00 41.41           O  
ANISOU 7208  O   GLY A 882     4788   6822   4122   -279   -349   -142       O  
ATOM   7209  N   PHE A 883      26.792 -22.718  45.372  1.00 41.32           N  
ANISOU 7209  N   PHE A 883     4729   6702   4267   -231   -236   -100       N  
ATOM   7210  CA  PHE A 883      26.094 -23.588  46.327  1.00 41.25           C  
ANISOU 7210  CA  PHE A 883     4744   6688   4241   -145   -212    -29       C  
ATOM   7211  C   PHE A 883      27.076 -24.212  47.304  1.00 40.74           C  
ANISOU 7211  C   PHE A 883     4622   6715   4142    -94   -264     32       C  
ATOM   7212  O   PHE A 883      26.851 -24.190  48.503  1.00 41.97           O  
ANISOU 7212  O   PHE A 883     4812   6922   4211    -61   -288     70       O  
ATOM   7213  CB  PHE A 883      25.323 -24.729  45.654  1.00 40.91           C  
ANISOU 7213  CB  PHE A 883     4691   6560   4293   -102   -139     14       C  
ATOM   7214  CG  PHE A 883      24.412 -24.305  44.548  1.00 41.55           C  
ANISOU 7214  CG  PHE A 883     4808   6565   4415   -151    -93    -35       C  
ATOM   7215  CD1 PHE A 883      23.884 -23.015  44.495  1.00 43.40           C  
ANISOU 7215  CD1 PHE A 883     5103   6790   4596   -201   -103    -87       C  
ATOM   7216  CD2 PHE A 883      24.038 -25.229  43.570  1.00 38.86           C  
ANISOU 7216  CD2 PHE A 883     4443   6157   4166   -143    -41    -28       C  
ATOM   7217  CE1 PHE A 883      23.033 -22.638  43.459  1.00 41.87           C  
ANISOU 7217  CE1 PHE A 883     4935   6533   4440   -239    -66   -116       C  
ATOM   7218  CE2 PHE A 883      23.183 -24.864  42.534  1.00 40.89           C  
ANISOU 7218  CE2 PHE A 883     4726   6359   4450   -192     -6    -67       C  
ATOM   7219  CZ  PHE A 883      22.679 -23.567  42.476  1.00 40.04           C  
ANISOU 7219  CZ  PHE A 883     4670   6256   4290   -238    -20   -103       C  
ATOM   7220  N   THR A 884      28.166 -24.763  46.774  1.00 42.18           N  
ANISOU 7220  N   THR A 884     4711   6928   4388    -83   -279     42       N  
ATOM   7221  CA  THR A 884      29.098 -25.551  47.573  1.00 43.05           C  
ANISOU 7221  CA  THR A 884     4748   7120   4490    -14   -325    118       C  
ATOM   7222  C   THR A 884      29.905 -24.700  48.555  1.00 44.62           C  
ANISOU 7222  C   THR A 884     4933   7447   4573    -55   -418    105       C  
ATOM   7223  O   THR A 884      30.159 -25.122  49.684  1.00 43.24           O  
ANISOU 7223  O   THR A 884     4745   7349   4336     -1   -463    177       O  
ATOM   7224  CB  THR A 884      30.035 -26.390  46.692  1.00 43.29           C  
ANISOU 7224  CB  THR A 884     4673   7149   4627     26   -308    128       C  
ATOM   7225  OG1 THR A 884      30.831 -25.524  45.878  1.00 43.57           O  
ANISOU 7225  OG1 THR A 884     4655   7236   4661    -59   -329     50       O  
ATOM   7226  CG2 THR A 884      29.233 -27.350  45.797  1.00 42.88           C  
ANISOU 7226  CG2 THR A 884     4644   6964   4684     68   -221    132       C  
ATOM   7227  N   SER A 885      30.283 -23.498  48.126  1.00 46.15           N  
ANISOU 7227  N   SER A 885     5135   7662   4737   -159   -452     16       N  
ATOM   7228  CA  SER A 885      31.019 -22.564  48.984  1.00 48.94           C  
ANISOU 7228  CA  SER A 885     5486   8124   4983   -225   -548    -18       C  
ATOM   7229  C   SER A 885      30.159 -22.110  50.162  1.00 48.11           C  
ANISOU 7229  C   SER A 885     5495   8024   4761   -213   -563    -29       C  
ATOM   7230  O   SER A 885      30.653 -21.962  51.282  1.00 48.28           O  
ANISOU 7230  O   SER A 885     5511   8156   4676   -211   -638    -14       O  
ATOM   7231  CB  SER A 885      31.490 -21.347  48.187  1.00 48.86           C  
ANISOU 7231  CB  SER A 885     5476   8107   4981   -353   -575   -109       C  
ATOM   7232  OG  SER A 885      30.374 -20.622  47.701  1.00 55.60           O  
ANISOU 7232  OG  SER A 885     6442   8841   5842   -390   -525   -167       O  
ATOM   7233  N   ALA A 886      28.877 -21.884  49.892  1.00 46.61           N  
ANISOU 7233  N   ALA A 886     5400   7727   4583   -202   -491    -56       N  
ATOM   7234  CA  ALA A 886      27.916 -21.524  50.923  1.00 46.83           C  
ANISOU 7234  CA  ALA A 886     5530   7760   4505   -173   -481    -67       C  
ATOM   7235  C   ALA A 886      27.759 -22.671  51.913  1.00 47.99           C  
ANISOU 7235  C   ALA A 886     5652   7974   4609    -76   -473     47       C  
ATOM   7236  O   ALA A 886      27.692 -22.454  53.120  1.00 48.34           O  
ANISOU 7236  O   ALA A 886     5736   8110   4522    -59   -510     55       O  
ATOM   7237  CB  ALA A 886      26.575 -21.184  50.290  1.00 46.10           C  
ANISOU 7237  CB  ALA A 886     5516   7546   4456   -169   -397   -104       C  
ATOM   7238  N   ALA A 887      27.716 -23.895  51.396  1.00 47.78           N  
ANISOU 7238  N   ALA A 887     5563   7899   4691    -16   -425    137       N  
ATOM   7239  CA  ALA A 887      27.490 -25.068  52.239  1.00 48.59           C  
ANISOU 7239  CA  ALA A 887     5649   8038   4777     75   -411    266       C  
ATOM   7240  C   ALA A 887      28.773 -25.655  52.865  1.00 49.69           C  
ANISOU 7240  C   ALA A 887     5696   8291   4892    114   -492    345       C  
ATOM   7241  O   ALA A 887      28.713 -26.623  53.634  1.00 50.79           O  
ANISOU 7241  O   ALA A 887     5818   8467   5014    192   -494    470       O  
ATOM   7242  CB  ALA A 887      26.728 -26.123  51.462  1.00 45.67           C  
ANISOU 7242  CB  ALA A 887     5271   7541   4540    120   -323    327       C  
ATOM   7243  N   LYS A 888      29.914 -25.037  52.563  1.00 49.06           N  
ANISOU 7243  N   LYS A 888     5555   8275   4809     56   -563    280       N  
ATOM   7244  CA  LYS A 888      31.235 -25.490  53.022  1.00 52.96           C  
ANISOU 7244  CA  LYS A 888     5939   8894   5290     87   -648    347       C  
ATOM   7245  C   LYS A 888      31.555 -26.883  52.476  1.00 54.52           C  
ANISOU 7245  C   LYS A 888     6051   9032   5631    187   -608    449       C  
ATOM   7246  O   LYS A 888      31.977 -27.774  53.223  1.00 54.98           O  
ANISOU 7246  O   LYS A 888     6057   9152   5679    274   -644    572       O  
ATOM   7247  CB  LYS A 888      31.370 -25.480  54.562  1.00 55.22           C  
ANISOU 7247  CB  LYS A 888     6244   9324   5415    112   -722    412       C  
ATOM   7248  CG  LYS A 888      30.634 -24.373  55.324  1.00 57.89           C  
ANISOU 7248  CG  LYS A 888     6702   9696   5597     50   -732    321       C  
ATOM   7249  CD  LYS A 888      31.291 -23.007  55.214  1.00 60.06           C  
ANISOU 7249  CD  LYS A 888     6990  10019   5813    -70   -808    180       C  
ATOM   7250  CE  LYS A 888      31.073 -22.206  56.497  1.00 62.78           C  
ANISOU 7250  CE  LYS A 888     7423  10468   5961   -103   -867    122       C  
ATOM   7251  NZ  LYS A 888      31.130 -20.738  56.242  1.00 67.51           N  
ANISOU 7251  NZ  LYS A 888     8097  11029   6524   -222   -902    -45       N  
ATOM   7252  N   LEU A 889      31.344 -27.056  51.172  1.00 54.25           N  
ANISOU 7252  N   LEU A 889     6008   8877   5727    177   -535    396       N  
ATOM   7253  CA  LEU A 889      31.614 -28.315  50.489  1.00 55.69           C  
ANISOU 7253  CA  LEU A 889     6124   8981   6055    269   -488    458       C  
ATOM   7254  C   LEU A 889      32.465 -28.088  49.244  1.00 55.59           C  
ANISOU 7254  C   LEU A 889     6024   8968   6129    236   -476    375       C  
ATOM   7255  O   LEU A 889      32.578 -26.959  48.747  1.00 55.69           O  
ANISOU 7255  O   LEU A 889     6048   9009   6103    128   -487    274       O  
ATOM   7256  CB  LEU A 889      30.303 -29.008  50.084  1.00 56.76           C  
ANISOU 7256  CB  LEU A 889     6345   8955   6268    298   -393    480       C  
ATOM   7257  CG  LEU A 889      29.591 -29.939  51.064  1.00 60.04           C  
ANISOU 7257  CG  LEU A 889     6807   9338   6668    371   -379    615       C  
ATOM   7258  CD1 LEU A 889      28.640 -29.166  51.926  1.00 63.66           C  
ANISOU 7258  CD1 LEU A 889     7356   9844   6986    320   -378    607       C  
ATOM   7259  CD2 LEU A 889      28.805 -30.983  50.305  1.00 63.06           C  
ANISOU 7259  CD2 LEU A 889     7220   9547   7191    409   -293    642       C  
ATOM   7260  N   ASP A 890      33.046 -29.172  48.735  1.00 53.75           N  
ANISOU 7260  N   ASP A 890     5708   8701   6014    333   -449    419       N  
ATOM   7261  CA  ASP A 890      33.789 -29.133  47.487  1.00 54.06           C  
ANISOU 7261  CA  ASP A 890     5660   8744   6138    321   -416    342       C  
ATOM   7262  C   ASP A 890      33.187 -30.086  46.470  1.00 52.41           C  
ANISOU 7262  C   ASP A 890     5484   8373   6057    379   -318    320       C  
ATOM   7263  O   ASP A 890      32.919 -31.246  46.781  1.00 53.02           O  
ANISOU 7263  O   ASP A 890     5577   8361   6206    484   -296    401       O  
ATOM   7264  CB  ASP A 890      35.256 -29.488  47.737  1.00 56.02           C  
ANISOU 7264  CB  ASP A 890     5753   9127   6404    390   -476    394       C  
ATOM   7265  CG  ASP A 890      36.015 -28.366  48.422  1.00 59.73           C  
ANISOU 7265  CG  ASP A 890     6172   9773   6750    294   -578    381       C  
ATOM   7266  OD1 ASP A 890      35.973 -27.222  47.913  1.00 58.73           O  
ANISOU 7266  OD1 ASP A 890     6070   9668   6578    161   -581    283       O  
ATOM   7267  OD2 ASP A 890      36.650 -28.628  49.468  1.00 63.41           O  
ANISOU 7267  OD2 ASP A 890     6575  10353   7164    347   -660    472       O  
ATOM   7268  N   TYR A 891      32.977 -29.600  45.253  1.00 50.88           N  
ANISOU 7268  N   TYR A 891     5301   8140   5890    304   -263    213       N  
ATOM   7269  CA  TYR A 891      32.453 -30.464  44.200  1.00 51.52           C  
ANISOU 7269  CA  TYR A 891     5412   8082   6082    347   -174    172       C  
ATOM   7270  C   TYR A 891      33.534 -31.354  43.581  1.00 54.70           C  
ANISOU 7270  C   TYR A 891     5701   8500   6584    454   -147    161       C  
ATOM   7271  O   TYR A 891      33.228 -32.402  43.011  1.00 56.94           O  
ANISOU 7271  O   TYR A 891     6009   8655   6971    531    -85    147       O  
ATOM   7272  CB  TYR A 891      31.659 -29.678  43.148  1.00 46.83           C  
ANISOU 7272  CB  TYR A 891     4885   7440   5469    232   -125     69       C  
ATOM   7273  CG  TYR A 891      32.420 -28.567  42.476  1.00 44.45           C  
ANISOU 7273  CG  TYR A 891     4520   7255   5116    136   -141     -4       C  
ATOM   7274  CD1 TYR A 891      32.461 -27.288  43.025  1.00 39.38           C  
ANISOU 7274  CD1 TYR A 891     3900   6691   4372     34   -204     -9       C  
ATOM   7275  CD2 TYR A 891      33.096 -28.792  41.277  1.00 43.70           C  
ANISOU 7275  CD2 TYR A 891     4344   7188   5073    144    -90    -69       C  
ATOM   7276  CE1 TYR A 891      33.170 -26.265  42.404  1.00 38.82           C  
ANISOU 7276  CE1 TYR A 891     3773   6713   4263    -69   -222    -65       C  
ATOM   7277  CE2 TYR A 891      33.801 -27.780  40.652  1.00 40.46           C  
ANISOU 7277  CE2 TYR A 891     3867   6893   4612     45   -101   -120       C  
ATOM   7278  CZ  TYR A 891      33.834 -26.522  41.218  1.00 40.22           C  
ANISOU 7278  CZ  TYR A 891     3861   6928   4492    -66   -170   -111       C  
ATOM   7279  OH  TYR A 891      34.535 -25.523  40.588  1.00 43.79           O  
ANISOU 7279  OH  TYR A 891     4252   7482   4905   -178   -184   -151       O  
ATOM   7280  N   GLU A 892      34.789 -30.930  43.707  1.00 57.17           N  
ANISOU 7280  N   GLU A 892     5887   8971   6864    458   -195    166       N  
ATOM   7281  CA  GLU A 892      35.945 -31.736  43.304  1.00 61.22           C  
ANISOU 7281  CA  GLU A 892     6265   9533   7462    579   -176    171       C  
ATOM   7282  C   GLU A 892      36.799 -32.013  44.527  1.00 63.03           C  
ANISOU 7282  C   GLU A 892     6406   9870   7673    664   -263    290       C  
ATOM   7283  O   GLU A 892      36.965 -31.137  45.376  1.00 61.62           O  
ANISOU 7283  O   GLU A 892     6220   9807   7385    582   -346    326       O  
ATOM   7284  CB  GLU A 892      36.805 -30.994  42.275  1.00 62.88           C  
ANISOU 7284  CB  GLU A 892     6368   9874   7650    508   -152     79       C  
ATOM   7285  CG  GLU A 892      36.181 -30.799  40.900  1.00 65.27           C  
ANISOU 7285  CG  GLU A 892     6730  10100   7968    438    -63    -37       C  
ATOM   7286  CD  GLU A 892      37.116 -30.083  39.941  1.00 70.05           C  
ANISOU 7286  CD  GLU A 892     7217  10857   8540    367    -39   -106       C  
ATOM   7287  OE1 GLU A 892      37.634 -30.745  39.017  1.00 74.07           O  
ANISOU 7287  OE1 GLU A 892     7652  11380   9113    448     35   -163       O  
ATOM   7288  OE2 GLU A 892      37.349 -28.865  40.116  1.00 70.03           O  
ANISOU 7288  OE2 GLU A 892     7196  10962   8450    231    -93   -103       O  
ATOM   7289  N   LYS A 893      37.352 -33.219  44.611  1.00 67.69           N  
ANISOU 7289  N   LYS A 893     6928  10421   8369    830   -249    349       N  
ATOM   7290  CA  LYS A 893      38.263 -33.566  45.703  1.00 72.89           C  
ANISOU 7290  CA  LYS A 893     7483  11195   9018    930   -336    477       C  
ATOM   7291  C   LYS A 893      39.493 -32.659  45.667  1.00 74.87           C  
ANISOU 7291  C   LYS A 893     7572  11677   9198    869   -394    455       C  
ATOM   7292  O   LYS A 893      40.238 -32.644  44.686  1.00 74.67           O  
ANISOU 7292  O   LYS A 893     7436  11716   9221    887   -343    382       O  
ATOM   7293  CB  LYS A 893      38.660 -35.047  45.646  1.00 75.46           C  
ANISOU 7293  CB  LYS A 893     7761  11419   9491   1134   -302    541       C  
ATOM   7294  CG  LYS A 893      39.083 -35.620  46.996  1.00 80.61           C  
ANISOU 7294  CG  LYS A 893     8369  12120  10138   1245   -394    715       C  
ATOM   7295  CD  LYS A 893      38.690 -37.090  47.145  1.00 84.52           C  
ANISOU 7295  CD  LYS A 893     8931  12407  10777   1408   -356    801       C  
ATOM   7296  CE  LYS A 893      38.570 -37.486  48.619  1.00 86.11           C  
ANISOU 7296  CE  LYS A 893     9156  12626  10934   1462   -447    992       C  
ATOM   7297  NZ  LYS A 893      37.977 -38.842  48.813  1.00 86.20           N  
ANISOU 7297  NZ  LYS A 893     9264  12407  11082   1588   -412   1091       N  
ATOM   7298  N   LYS A 894      39.673 -31.886  46.736  1.00 77.82           N  
ANISOU 7298  N   LYS A 894     7937  12182   9450    786   -499    514       N  
ATOM   7299  CA  LYS A 894      40.736 -30.883  46.820  1.00 80.77           C  
ANISOU 7299  CA  LYS A 894     8174  12774   9742    687   -572    494       C  
ATOM   7300  C   LYS A 894      42.095 -31.505  47.168  1.00 83.56           C  
ANISOU 7300  C   LYS A 894     8326  13282  10139    822   -625    585       C  
ATOM   7301  O   LYS A 894      42.173 -32.430  47.982  1.00 85.01           O  
ANISOU 7301  O   LYS A 894     8500  13442  10360    966   -662    705       O  
ATOM   7302  CB  LYS A 894      40.362 -29.790  47.830  1.00 81.37           C  
ANISOU 7302  CB  LYS A 894     8331  12920   9666    539   -669    504       C  
ATOM   7303  CG  LYS A 894      40.020 -30.314  49.231  1.00 86.45           C  
ANISOU 7303  CG  LYS A 894     9032  13559  10256    615   -740    629       C  
ATOM   7304  CD  LYS A 894      39.691 -29.185  50.209  1.00 88.44           C  
ANISOU 7304  CD  LYS A 894     9365  13897  10342    470   -831    616       C  
ATOM   7305  CE  LYS A 894      39.714 -29.659  51.666  1.00 89.65           C  
ANISOU 7305  CE  LYS A 894     9527  14123  10414    544   -920    751       C  
ATOM   7306  NZ  LYS A 894      38.853 -30.847  51.948  1.00 89.28           N  
ANISOU 7306  NZ  LYS A 894     9572  13916  10434    679   -862    849       N  
ATOM   7307  N   ALA A 895      43.154 -30.987  46.542  1.00 83.85           N  
ANISOU 7307  N   ALA A 895     8198  13485  10175    774   -628    536       N  
ATOM   7308  CA  ALA A 895      44.519 -31.479  46.741  1.00 84.80           C  
ANISOU 7308  CA  ALA A 895     8098  13783  10341    896   -672    614       C  
ATOM   7309  C   ALA A 895      45.180 -30.870  47.985  1.00 84.67           C  
ANISOU 7309  C   ALA A 895     7995  13970  10206    825   -827    705       C  
ATOM   7310  O   ALA A 895      46.157 -31.404  48.520  1.00 83.20           O  
ANISOU 7310  O   ALA A 895     7642  13927  10043    946   -893    810       O  
ATOM   7311  CB  ALA A 895      45.362 -31.208  45.489  1.00 85.47           C  
ANISOU 7311  CB  ALA A 895     8028  13977  10471    873   -598    525       C  
TER    7312      ALA A 895                                                      
ATOM   7313  P    DC T   3      -1.915  -1.076  30.096  1.00 97.77           P  
ANISOU 7313  P    DC T   3    11764  12677  12707  -1373   -877   1454       P  
ATOM   7314  OP1  DC T   3      -2.732  -1.602  28.974  1.00 97.06           O  
ANISOU 7314  OP1  DC T   3    11686  12673  12519  -1486   -888   1583       O  
ATOM   7315  OP2  DC T   3      -0.529  -1.553  30.338  1.00 93.35           O  
ANISOU 7315  OP2  DC T   3    11260  12171  12036  -1350   -816   1354       O  
ATOM   7316  O5'  DC T   3      -2.760  -1.263  31.440  1.00 91.66           O  
ANISOU 7316  O5'  DC T   3    10999  11835  11991  -1234   -841   1322       O  
ATOM   7317  C5'  DC T   3      -2.716  -2.497  32.144  1.00 82.32           C  
ANISOU 7317  C5'  DC T   3     9905  10719  10652  -1163   -743   1199       C  
ATOM   7318  C4'  DC T   3      -2.597  -2.291  33.650  1.00 73.76           C  
ANISOU 7318  C4'  DC T   3     8813   9581   9633  -1025   -714   1042       C  
ATOM   7319  O4'  DC T   3      -2.102  -0.978  34.021  1.00 73.97           O  
ANISOU 7319  O4'  DC T   3     8756   9511   9840   -996   -776   1014       O  
ATOM   7320  C3'  DC T   3      -3.889  -2.427  34.432  1.00 65.74           C  
ANISOU 7320  C3'  DC T   3     7782   8534   8662   -953   -698    994       C  
ATOM   7321  O3'  DC T   3      -3.527  -2.905  35.707  1.00 50.78           O  
ANISOU 7321  O3'  DC T   3     5920   6671   6704   -847   -633    844       O  
ATOM   7322  C2'  DC T   3      -4.423  -1.001  34.505  1.00 70.07           C  
ANISOU 7322  C2'  DC T   3     8219   8959   9447   -947   -784   1022       C  
ATOM   7323  C1'  DC T   3      -3.171  -0.127  34.394  1.00 75.38           C  
ANISOU 7323  C1'  DC T   3     8849   9590  10203   -962   -827   1014       C  
ATOM   7324  N1   DC T   3      -3.279   0.974  33.356  1.00 83.52           N  
ANISOU 7324  N1   DC T   3     9790  10541  11402  -1056   -929   1171       N  
ATOM   7325  C2   DC T   3      -2.119   1.617  32.842  1.00 86.74           C  
ANISOU 7325  C2   DC T   3    10167  10934  11856  -1109   -973   1222       C  
ATOM   7326  O2   DC T   3      -0.974   1.307  33.226  1.00 85.26           O  
ANISOU 7326  O2   DC T   3    10029  10792  11574  -1076   -927   1129       O  
ATOM   7327  N3   DC T   3      -2.282   2.600  31.911  1.00 89.89           N  
ANISOU 7327  N3   DC T   3    10474  11266  12414  -1200  -1072   1387       N  
ATOM   7328  C4   DC T   3      -3.507   2.948  31.486  1.00 91.68           C  
ANISOU 7328  C4   DC T   3    10639  11441  12755  -1239  -1128   1499       C  
ATOM   7329  N4   DC T   3      -3.586   3.922  30.569  1.00 93.14           N  
ANISOU 7329  N4   DC T   3    10722  11563  13103  -1335  -1233   1680       N  
ATOM   7330  C5   DC T   3      -4.692   2.313  31.987  1.00 89.81           C  
ANISOU 7330  C5   DC T   3    10434  11213  12475  -1184  -1084   1441       C  
ATOM   7331  C6   DC T   3      -4.528   1.347  32.906  1.00 86.32           C  
ANISOU 7331  C6   DC T   3    10085  10841  11873  -1095   -984   1278       C  
HETATM 7332  P   2PR T   4      -3.959  -4.353  36.188  1.00 40.77           P  
ANISOU 7332  P   2PR T   4     4730   5492   5267   -805   -546    802       P  
HETATM 7333  OP1 2PR T   4      -5.728  -4.093  35.902  1.00 47.48           O  
ANISOU 7333  OP1 2PR T   4     5536   6291   6212   -823   -580    876       O  
HETATM 7334  OP2 2PR T   4      -3.008  -5.396  35.007  1.00 46.22           O  
ANISOU 7334  OP2 2PR T   4     5499   6267   5795   -902   -509    874       O  
HETATM 7335  O5' 2PR T   4      -3.275  -3.948  37.689  1.00 45.00           O  
ANISOU 7335  O5' 2PR T   4     5238   6026   5833   -694   -526    643       O  
HETATM 7336  C5' 2PR T   4      -2.051  -4.539  38.084  1.00 37.49           C  
ANISOU 7336  C5' 2PR T   4     4335   5138   4772   -669   -482    585       C  
HETATM 7337  C4' 2PR T   4      -1.949  -4.192  39.556  1.00 38.59           C  
ANISOU 7337  C4' 2PR T   4     4434   5292   4935   -569   -467    445       C  
HETATM 7338  O4' 2PR T   4      -2.585  -5.188  40.376  1.00 37.76           O  
ANISOU 7338  O4' 2PR T   4     4361   5267   4720   -516   -405    410       O  
HETATM 7339  C3' 2PR T   4      -0.506  -4.121  40.002  1.00 36.78           C  
ANISOU 7339  C3' 2PR T   4     4214   5092   4668   -544   -459    376       C  
HETATM 7340  O3' 2PR T   4       0.070  -2.832  39.743  1.00 42.69           O  
ANISOU 7340  O3' 2PR T   4     4900   5758   5563   -562   -524    359       O  
HETATM 7341  C2' 2PR T   4      -0.628  -4.445  41.471  1.00 32.36           C  
ANISOU 7341  C2' 2PR T   4     3642   4610   4045   -455   -417    260       C  
HETATM 7342  C1' 2PR T   4      -1.720  -5.503  41.470  1.00 35.54           C  
ANISOU 7342  C1' 2PR T   4     4085   5060   4358   -453   -370    315       C  
HETATM 7343  N9  2PR T   4      -1.054  -6.824  41.307  1.00 37.65           N  
ANISOU 7343  N9  2PR T   4     4425   5396   4485   -465   -320    363       N  
HETATM 7344  C8  2PR T   4      -1.011  -7.615  40.219  1.00 35.78           C  
ANISOU 7344  C8  2PR T   4     4242   5152   4201   -531   -303    459       C  
HETATM 7345  N7  2PR T   4      -0.284  -8.720  40.508  1.00 37.85           N  
ANISOU 7345  N7  2PR T   4     4544   5475   4362   -516   -253    459       N  
HETATM 7346  C5  2PR T   4       0.131  -8.611  41.791  1.00 38.53           C  
ANISOU 7346  C5  2PR T   4     4604   5615   4421   -443   -245    379       C  
HETATM 7347  C6  2PR T   4       0.895  -9.411  42.635  1.00 38.71           C  
ANISOU 7347  C6  2PR T   4     4636   5712   4359   -401   -211    357       C  
HETATM 7348  N1  2PR T   4       1.132  -8.998  43.890  1.00 35.85           N  
ANISOU 7348  N1  2PR T   4     4231   5414   3976   -339   -217    274       N  
HETATM 7349  C2  2PR T   4       0.647  -7.822  44.346  1.00 34.23           C  
ANISOU 7349  C2  2PR T   4     3971   5195   3840   -315   -250    190       C  
HETATM 7350  N2  2PR T   4       0.885  -7.413  45.612  1.00 33.19           N  
ANISOU 7350  N2  2PR T   4     3788   5144   3679   -260   -252     87       N  
HETATM 7351  N3  2PR T   4      -0.097  -7.042  43.550  1.00 34.43           N  
ANISOU 7351  N3  2PR T   4     3982   5128   3971   -349   -283    207       N  
HETATM 7352  C4  2PR T   4      -0.361  -7.418  42.280  1.00 37.09           C  
ANISOU 7352  C4  2PR T   4     4363   5405   4323   -414   -284    310       C  
ATOM   7353  P    DT T   5       1.647  -2.641  39.501  1.00 37.59           P  
ANISOU 7353  P    DT T   5     4267   5113   4902   -583   -535    349       P  
ATOM   7354  OP1  DT T   5       1.844  -1.249  39.064  1.00 44.02           O  
ANISOU 7354  OP1  DT T   5     5003   5822   5899   -613   -611    364       O  
ATOM   7355  OP2  DT T   5       2.173  -3.739  38.663  1.00 42.53           O  
ANISOU 7355  OP2  DT T   5     4973   5792   5392   -641   -496    434       O  
ATOM   7356  O5'  DT T   5       2.220  -2.843  40.980  1.00 38.05           O  
ANISOU 7356  O5'  DT T   5     4318   5241   4896   -491   -499    205       O  
ATOM   7357  C5'  DT T   5       1.834  -1.919  42.009  1.00 36.80           C  
ANISOU 7357  C5'  DT T   5     4078   5064   4840   -428   -520     80       C  
ATOM   7358  C4'  DT T   5       2.397  -2.352  43.343  1.00 36.72           C  
ANISOU 7358  C4'  DT T   5     4070   5164   4718   -358   -478    -40       C  
ATOM   7359  O4'  DT T   5       1.932  -3.691  43.639  1.00 36.86           O  
ANISOU 7359  O4'  DT T   5     4150   5280   4574   -344   -418      5       O  
ATOM   7360  C3'  DT T   5       3.912  -2.446  43.385  1.00 37.74           C  
ANISOU 7360  C3'  DT T   5     4222   5316   4802   -360   -481    -56       C  
ATOM   7361  O3'  DT T   5       4.469  -1.170  43.704  1.00 39.31           O  
ANISOU 7361  O3'  DT T   5     4341   5454   5139   -344   -530   -156       O  
ATOM   7362  C2'  DT T   5       4.111  -3.465  44.495  1.00 36.07           C  
ANISOU 7362  C2'  DT T   5     4039   5241   4426   -308   -427   -103       C  
ATOM   7363  C1'  DT T   5       2.938  -4.424  44.313  1.00 34.84           C  
ANISOU 7363  C1'  DT T   5     3925   5119   4193   -316   -386    -23       C  
ATOM   7364  N1   DT T   5       3.310  -5.674  43.545  1.00 38.05           N  
ANISOU 7364  N1   DT T   5     4414   5541   4502   -356   -351     96       N  
ATOM   7365  C2   DT T   5       3.997  -6.683  44.195  1.00 37.13           C  
ANISOU 7365  C2   DT T   5     4325   5515   4267   -328   -313     98       C  
ATOM   7366  O2   DT T   5       4.320  -6.636  45.364  1.00 39.90           O  
ANISOU 7366  O2   DT T   5     4642   5950   4569   -277   -309     21       O  
ATOM   7367  N3   DT T   5       4.297  -7.770  43.411  1.00 38.51           N  
ANISOU 7367  N3   DT T   5     4560   5683   4391   -368   -281    194       N  
ATOM   7368  C4   DT T   5       3.992  -7.949  42.066  1.00 37.75           C  
ANISOU 7368  C4   DT T   5     4499   5518   4325   -437   -279    276       C  
ATOM   7369  O4   DT T   5       4.308  -8.975  41.459  1.00 39.86           O  
ANISOU 7369  O4   DT T   5     4808   5791   4544   -473   -242    336       O  
ATOM   7370  C5   DT T   5       3.279  -6.856  41.437  1.00 35.45           C  
ANISOU 7370  C5   DT T   5     4181   5153   4137   -470   -324    283       C  
ATOM   7371  C7   DT T   5       2.882  -6.926  39.984  1.00 33.52           C  
ANISOU 7371  C7   DT T   5     3964   4855   3919   -556   -333    381       C  
ATOM   7372  C6   DT T   5       2.985  -5.793  42.197  1.00 35.31           C  
ANISOU 7372  C6   DT T   5     4102   5121   4192   -425   -359    199       C  
ATOM   7373  P    DA T   6       6.042  -0.895  43.558  1.00 40.46           P  
ANISOU 7373  P    DA T   6     4492   5586   5295   -355   -552   -171       P  
ATOM   7374  OP1  DA T   6       6.271   0.544  43.793  1.00 44.41           O  
ANISOU 7374  OP1  DA T   6     4894   5999   5981   -342   -609   -269       O  
ATOM   7375  OP2  DA T   6       6.492  -1.534  42.313  1.00 41.06           O  
ANISOU 7375  OP2  DA T   6     4642   5638   5322   -424   -544    -27       O  
ATOM   7376  O5'  DA T   6       6.734  -1.683  44.761  1.00 42.34           O  
ANISOU 7376  O5'  DA T   6     4752   5960   5374   -300   -509   -252       O  
ATOM   7377  C5'  DA T   6       6.463  -1.375  46.125  1.00 37.70           C  
ANISOU 7377  C5'  DA T   6     4102   5458   4765   -238   -501   -397       C  
ATOM   7378  C4'  DA T   6       7.325  -2.259  47.015  1.00 38.47           C  
ANISOU 7378  C4'  DA T   6     4228   5692   4696   -208   -468   -420       C  
ATOM   7379  O4'  DA T   6       7.095  -3.663  46.727  1.00 36.93           O  
ANISOU 7379  O4'  DA T   6     4113   5550   4368   -222   -422   -293       O  
ATOM   7380  C3'  DA T   6       8.831  -2.067  46.890  1.00 39.90           C  
ANISOU 7380  C3'  DA T   6     4415   5854   4890   -216   -492   -430       C  
ATOM   7381  O3'  DA T   6       9.361  -2.227  48.188  1.00 42.24           O  
ANISOU 7381  O3'  DA T   6     4678   6285   5088   -172   -484   -529       O  
ATOM   7382  C2'  DA T   6       9.267  -3.190  45.959  1.00 38.28           C  
ANISOU 7382  C2'  DA T   6     4300   5633   4611   -257   -465   -280       C  
ATOM   7383  C1'  DA T   6       8.297  -4.301  46.362  1.00 37.66           C  
ANISOU 7383  C1'  DA T   6     4254   5645   4411   -241   -416   -228       C  
ATOM   7384  N9   DA T   6       8.042  -5.211  45.252  1.00 37.81           N  
ANISOU 7384  N9   DA T   6     4344   5616   4405   -288   -388    -93       N  
ATOM   7385  C8   DA T   6       7.481  -4.883  44.045  1.00 35.73           C  
ANISOU 7385  C8   DA T   6     4099   5254   4223   -341   -400    -27       C  
ATOM   7386  N7   DA T   6       7.390  -5.892  43.216  1.00 34.81           N  
ANISOU 7386  N7   DA T   6     4042   5130   4052   -383   -365     76       N  
ATOM   7387  C5   DA T   6       7.923  -6.958  43.928  1.00 35.45           C  
ANISOU 7387  C5   DA T   6     4143   5296   4031   -351   -328     81       C  
ATOM   7388  C6   DA T   6       8.119  -8.322  43.611  1.00 33.05           C  
ANISOU 7388  C6   DA T   6     3884   5016   3658   -369   -281    161       C  
ATOM   7389  N6   DA T   6       7.773  -8.865  42.436  1.00 28.77           N  
ANISOU 7389  N6   DA T   6     3382   4425   3125   -428   -256    235       N  
ATOM   7390  N1   DA T   6       8.690  -9.113  44.554  1.00 33.24           N  
ANISOU 7390  N1   DA T   6     3899   5119   3612   -328   -262    159       N  
ATOM   7391  C2   DA T   6       9.037  -8.585  45.736  1.00 31.72           C  
ANISOU 7391  C2   DA T   6     3661   4998   3393   -278   -287     83       C  
ATOM   7392  N3   DA T   6       8.901  -7.323  46.134  1.00 37.10           N  
ANISOU 7392  N3   DA T   6     4299   5675   4122   -259   -326    -15       N  
ATOM   7393  C4   DA T   6       8.336  -6.554  45.186  1.00 36.18           C  
ANISOU 7393  C4   DA T   6     4188   5459   4098   -295   -345    -11       C  
ATOM   7394  P    DA T   7      10.896  -1.973  48.527  1.00 42.93           P  
ANISOU 7394  P    DA T   7     4748   6390   5172   -164   -510   -581       P  
ATOM   7395  OP1  DA T   7      10.917  -1.472  49.913  1.00 42.92           O  
ANISOU 7395  OP1  DA T   7     4665   6511   5131   -122   -517   -743       O  
ATOM   7396  OP2  DA T   7      11.496  -1.155  47.453  1.00 44.83           O  
ANISOU 7396  OP2  DA T   7     4987   6478   5567   -200   -548   -557       O  
ATOM   7397  O5'  DA T   7      11.549  -3.440  48.482  1.00 41.54           O  
ANISOU 7397  O5'  DA T   7     4646   6286   4852   -172   -475   -457       O  
ATOM   7398  C5'  DA T   7      11.083  -4.459  49.383  1.00 39.75           C  
ANISOU 7398  C5'  DA T   7     4424   6203   4474   -148   -439   -428       C  
ATOM   7399  C4'  DA T   7      11.992  -5.682  49.429  1.00 41.21           C  
ANISOU 7399  C4'  DA T   7     4651   6437   4568   -153   -421   -321       C  
ATOM   7400  O4'  DA T   7      11.681  -6.574  48.325  1.00 39.20           O  
ANISOU 7400  O4'  DA T   7     4467   6100   4327   -188   -388   -189       O  
ATOM   7401  C3'  DA T   7      13.497  -5.440  49.346  1.00 38.33           C  
ANISOU 7401  C3'  DA T   7     4282   6043   4240   -159   -449   -341       C  
ATOM   7402  O3'  DA T   7      14.192  -6.294  50.273  1.00 36.54           O  
ANISOU 7402  O3'  DA T   7     4039   5941   3902   -140   -446   -307       O  
ATOM   7403  C2'  DA T   7      13.844  -5.743  47.880  1.00 37.66           C  
ANISOU 7403  C2'  DA T   7     4259   5815   4234   -205   -436   -243       C  
ATOM   7404  C1'  DA T   7      12.809  -6.797  47.503  1.00 36.63           C  
ANISOU 7404  C1'  DA T   7     4174   5693   4051   -218   -390   -140       C  
ATOM   7405  N9   DA T   7      12.346  -6.748  46.111  1.00 37.74           N  
ANISOU 7405  N9   DA T   7     4360   5715   4264   -267   -377    -80       N  
ATOM   7406  C8   DA T   7      11.969  -5.646  45.410  1.00 38.32           C  
ANISOU 7406  C8   DA T   7     4424   5699   4437   -293   -405   -112       C  
ATOM   7407  N7   DA T   7      11.592  -5.892  44.181  1.00 40.00           N  
ANISOU 7407  N7   DA T   7     4678   5837   4682   -347   -389    -30       N  
ATOM   7408  C5   DA T   7      11.718  -7.255  44.059  1.00 37.94           C  
ANISOU 7408  C5   DA T   7     4458   5613   4345   -355   -341     44       C  
ATOM   7409  C6   DA T   7      11.467  -8.144  42.988  1.00 39.84           C  
ANISOU 7409  C6   DA T   7     4745   5817   4575   -408   -300    129       C  
ATOM   7410  N6   DA T   7      11.008  -7.764  41.787  1.00 37.93           N  
ANISOU 7410  N6   DA T   7     4522   5510   4380   -471   -304    167       N  
ATOM   7411  N1   DA T   7      11.694  -9.458  43.209  1.00 40.46           N  
ANISOU 7411  N1   DA T   7     4839   5935   4599   -399   -257    176       N  
ATOM   7412  C2   DA T   7      12.145  -9.848  44.408  1.00 37.42           C  
ANISOU 7412  C2   DA T   7     4427   5625   4167   -344   -260    161       C  
ATOM   7413  N3   DA T   7      12.405  -9.100  45.478  1.00 37.37           N  
ANISOU 7413  N3   DA T   7     4380   5678   4142   -298   -299     90       N  
ATOM   7414  C4   DA T   7      12.179  -7.801  45.240  1.00 36.45           C  
ANISOU 7414  C4   DA T   7     4248   5516   4085   -305   -335     22       C  
ATOM   7415  P    DT T   8      15.790  -6.198  50.430  1.00 38.03           P  
ANISOU 7415  P    DT T   8     4212   6126   4110   -140   -476   -322       P  
ATOM   7416  OP1  DT T   8      16.157  -6.892  51.675  1.00 44.74           O  
ANISOU 7416  OP1  DT T   8     5021   7143   4835   -118   -483   -300       O  
ATOM   7417  OP2  DT T   8      16.216  -4.798  50.215  1.00 43.39           O  
ANISOU 7417  OP2  DT T   8     4859   6729   4896   -141   -514   -445       O  
ATOM   7418  O5'  DT T   8      16.351  -7.026  49.190  1.00 44.11           O  
ANISOU 7418  O5'  DT T   8     5047   6774   4940   -175   -449   -200       O  
ATOM   7419  C5'  DT T   8      16.207  -8.435  49.219  1.00 46.70           C  
ANISOU 7419  C5'  DT T   8     5398   7137   5210   -179   -413    -79       C  
ATOM   7420  C4'  DT T   8      16.611  -9.079  47.911  1.00 45.02           C  
ANISOU 7420  C4'  DT T   8     5235   6796   5073   -220   -380      0       C  
ATOM   7421  O4'  DT T   8      15.701  -8.685  46.861  1.00 46.12           O  
ANISOU 7421  O4'  DT T   8     5414   6848   5259   -252   -362     -1       O  
ATOM   7422  C3'  DT T   8      17.968  -8.696  47.351  1.00 43.45           C  
ANISOU 7422  C3'  DT T   8     5037   6519   4953   -241   -396    -27       C  
ATOM   7423  O3'  DT T   8      18.987  -9.487  47.954  1.00 45.29           O  
ANISOU 7423  O3'  DT T   8     5242   6797   5168   -225   -400     17       O  
ATOM   7424  C2'  DT T   8      17.789  -9.094  45.890  1.00 44.06           C  
ANISOU 7424  C2'  DT T   8     5165   6484   5092   -295   -353     27       C  
ATOM   7425  C1'  DT T   8      16.286  -9.215  45.697  1.00 39.30           C  
ANISOU 7425  C1'  DT T   8     4586   5892   4455   -299   -332     52       C  
ATOM   7426  N1   DT T   8      15.810  -8.510  44.496  1.00 36.39           N  
ANISOU 7426  N1   DT T   8     4247   5435   4145   -348   -330     43       N  
ATOM   7427  C2   DT T   8      15.610  -9.272  43.360  1.00 38.26           C  
ANISOU 7427  C2   DT T   8     4521   5619   4397   -401   -284    107       C  
ATOM   7428  O2   DT T   8      15.799 -10.474  43.301  1.00 41.26           O  
ANISOU 7428  O2   DT T   8     4907   6006   4762   -406   -243    157       O  
ATOM   7429  N3   DT T   8      15.165  -8.569  42.272  1.00 36.87           N  
ANISOU 7429  N3   DT T   8     4364   5382   4262   -456   -290    110       N  
ATOM   7430  C4   DT T   8      14.918  -7.215  42.197  1.00 35.49           C  
ANISOU 7430  C4   DT T   8     4170   5177   4137   -458   -340     68       C  
ATOM   7431  O4   DT T   8      14.523  -6.707  41.154  1.00 39.86           O  
ANISOU 7431  O4   DT T   8     4735   5678   4733   -516   -347     99       O  
ATOM   7432  C5   DT T   8      15.156  -6.468  43.418  1.00 33.06           C  
ANISOU 7432  C5   DT T   8     3819   4908   3835   -394   -383    -11       C  
ATOM   7433  C7   DT T   8      14.916  -4.987  43.449  1.00 29.11           C  
ANISOU 7433  C7   DT T   8     3279   4363   3419   -391   -437    -75       C  
ATOM   7434  C6   DT T   8      15.584  -7.145  44.497  1.00 31.60           C  
ANISOU 7434  C6   DT T   8     3620   4801   3585   -345   -374    -25       C  
ATOM   7435  P    DT T   9      20.530  -9.376  47.525  1.00 44.27           P  
ANISOU 7435  P    DT T   9     5105   6598   5118   -243   -412      3       P  
ATOM   7436  OP1  DT T   9      21.320  -9.793  48.703  1.00 42.04           O  
ANISOU 7436  OP1  DT T   9     4770   6411   4792   -210   -443     23       O  
ATOM   7437  OP2  DT T   9      20.746  -8.046  46.902  1.00 45.76           O  
ANISOU 7437  OP2  DT T   9     5303   6715   5370   -261   -435    -84       O  
ATOM   7438  O5'  DT T   9      20.727 -10.448  46.365  1.00 43.09           O  
ANISOU 7438  O5'  DT T   9     4987   6352   5032   -286   -354     79       O  
ATOM   7439  C5'  DT T   9      20.548 -11.838  46.587  1.00 43.97           C  
ANISOU 7439  C5'  DT T   9     5087   6483   5136   -281   -321    172       C  
ATOM   7440  C4'  DT T   9      20.336 -12.521  45.245  1.00 47.28           C  
ANISOU 7440  C4'  DT T   9     5540   6802   5621   -333   -260    199       C  
ATOM   7441  O4'  DT T   9      19.236 -11.898  44.522  1.00 47.86           O  
ANISOU 7441  O4'  DT T   9     5660   6857   5670   -360   -248    173       O  
ATOM   7442  C3'  DT T   9      21.545 -12.469  44.314  1.00 46.03           C  
ANISOU 7442  C3'  DT T   9     5380   6557   5552   -375   -240    166       C  
ATOM   7443  O3'  DT T   9      22.287 -13.668  44.472  1.00 48.54           O  
ANISOU 7443  O3'  DT T   9     5657   6850   5935   -371   -215    217       O  
ATOM   7444  C2'  DT T   9      20.960 -12.371  42.912  1.00 45.37           C  
ANISOU 7444  C2'  DT T   9     5340   6412   5485   -439   -194    149       C  
ATOM   7445  C1'  DT T   9      19.512 -11.940  43.127  1.00 49.25           C  
ANISOU 7445  C1'  DT T   9     5861   6947   5904   -425   -208    159       C  
ATOM   7446  N1   DT T   9      19.145 -10.625  42.500  1.00 49.00           N  
ANISOU 7446  N1   DT T   9     5856   6894   5869   -455   -234    113       N  
ATOM   7447  C2   DT T   9      18.488 -10.654  41.295  1.00 49.20           C  
ANISOU 7447  C2   DT T   9     5913   6882   5899   -519   -201    129       C  
ATOM   7448  O2   DT T   9      18.200 -11.678  40.712  1.00 54.98           O  
ANISOU 7448  O2   DT T   9     6655   7602   6634   -552   -148    160       O  
ATOM   7449  N3   DT T   9      18.164  -9.432  40.783  1.00 47.22           N  
ANISOU 7449  N3   DT T   9     5672   6611   5658   -547   -236    109       N  
ATOM   7450  C4   DT T   9      18.421  -8.203  41.339  1.00 44.76           C  
ANISOU 7450  C4   DT T   9     5339   6298   5370   -516   -296     64       C  
ATOM   7451  O4   DT T   9      18.069  -7.180  40.762  1.00 47.57           O  
ANISOU 7451  O4   DT T   9     5694   6620   5760   -549   -326     59       O  
ATOM   7452  C5   DT T   9      19.117  -8.228  42.610  1.00 45.48           C  
ANISOU 7452  C5   DT T   9     5399   6432   5450   -448   -323     26       C  
ATOM   7453  C7   DT T   9      19.469  -6.955  43.328  1.00 40.75           C  
ANISOU 7453  C7   DT T   9     4764   5840   4879   -411   -385    -46       C  
ATOM   7454  C6   DT T   9      19.443  -9.426  43.122  1.00 46.54           C  
ANISOU 7454  C6   DT T   9     5526   6600   5558   -423   -293     59       C  
ATOM   7455  P    DA T  10      23.773 -13.779  43.920  1.00 44.97           P  
ANISOU 7455  P    DA T  10     5178   6324   5583   -399   -201    184       P  
ATOM   7456  OP1  DA T  10      24.403 -15.025  44.382  1.00 49.13           O  
ANISOU 7456  OP1  DA T  10     5644   6831   6190   -382   -188    248       O  
ATOM   7457  OP2  DA T  10      24.419 -12.472  44.158  1.00 45.37           O  
ANISOU 7457  OP2  DA T  10     5234   6391   5612   -389   -253    121       O  
ATOM   7458  O5'  DA T  10      23.513 -13.940  42.353  1.00 50.10           O  
ANISOU 7458  O5'  DA T  10     5861   6903   6272   -475   -133    146       O  
ATOM   7459  C5'  DA T  10      22.970 -15.141  41.815  1.00 51.34           C  
ANISOU 7459  C5'  DA T  10     6010   7027   6470   -502    -71    175       C  
ATOM   7460  C4'  DA T  10      22.940 -15.036  40.301  1.00 49.21           C  
ANISOU 7460  C4'  DA T  10     5765   6715   6219   -586    -13    115       C  
ATOM   7461  O4'  DA T  10      22.135 -13.886  39.950  1.00 46.50           O  
ANISOU 7461  O4'  DA T  10     5476   6407   5785   -606    -41    103       O  
ATOM   7462  C3'  DA T  10      24.315 -14.804  39.679  1.00 50.35           C  
ANISOU 7462  C3'  DA T  10     5883   6814   6431   -627      5     55       C  
ATOM   7463  O3'  DA T  10      24.499 -15.666  38.558  1.00 51.38           O  
ANISOU 7463  O3'  DA T  10     5991   6903   6628   -698     87     10       O  
ATOM   7464  C2'  DA T  10      24.322 -13.318  39.296  1.00 48.45           C  
ANISOU 7464  C2'  DA T  10     5685   6599   6125   -652    -36     25       C  
ATOM   7465  C1'  DA T  10      22.841 -13.037  39.062  1.00 46.73           C  
ANISOU 7465  C1'  DA T  10     5513   6418   5824   -664    -40     53       C  
ATOM   7466  N9   DA T  10      22.432 -11.651  39.310  1.00 44.67           N  
ANISOU 7466  N9   DA T  10     5281   6183   5509   -648   -105     54       N  
ATOM   7467  C8   DA T  10      22.620 -10.934  40.461  1.00 43.46           C  
ANISOU 7467  C8   DA T  10     5118   6053   5342   -578   -171     50       C  
ATOM   7468  N7   DA T  10      22.153  -9.705  40.411  1.00 43.49           N  
ANISOU 7468  N7   DA T  10     5137   6064   5322   -580   -217     37       N  
ATOM   7469  C5   DA T  10      21.621  -9.602  39.135  1.00 44.32           C  
ANISOU 7469  C5   DA T  10     5266   6153   5419   -659   -186     52       C  
ATOM   7470  C6   DA T  10      20.972  -8.551  38.444  1.00 44.13           C  
ANISOU 7470  C6   DA T  10     5258   6124   5387   -705   -215     66       C  
ATOM   7471  N6   DA T  10      20.741  -7.352  38.979  1.00 45.99           N  
ANISOU 7471  N6   DA T  10     5482   6352   5641   -669   -281     53       N  
ATOM   7472  N1   DA T  10      20.568  -8.770  37.171  1.00 43.10           N  
ANISOU 7472  N1   DA T  10     5142   5998   5236   -794   -176     94       N  
ATOM   7473  C2   DA T  10      20.798  -9.966  36.619  1.00 41.85           C  
ANISOU 7473  C2   DA T  10     4983   5848   5069   -833   -104     84       C  
ATOM   7474  N3   DA T  10      21.388 -11.030  37.171  1.00 46.57           N  
ANISOU 7474  N3   DA T  10     5563   6433   5696   -792    -68     61       N  
ATOM   7475  C4   DA T  10      21.785 -10.791  38.440  1.00 44.33           C  
ANISOU 7475  C4   DA T  10     5266   6146   5431   -705   -115     56       C  
ATOM   7476  P    DA T  11      25.963 -15.874  37.941  1.00 49.92           P  
ANISOU 7476  P    DA T  11     5756   6667   6544   -742    128    -60       P  
ATOM   7477  OP1  DA T  11      26.170 -17.320  37.743  1.00 55.23           O  
ANISOU 7477  OP1  DA T  11     6364   7282   7339   -754    195    -80       O  
ATOM   7478  OP2  DA T  11      26.936 -15.100  38.742  1.00 51.00           O  
ANISOU 7478  OP2  DA T  11     5885   6803   6691   -692     63    -50       O  
ATOM   7479  O5'  DA T  11      25.836 -15.195  36.503  1.00 50.08           O  
ANISOU 7479  O5'  DA T  11     5808   6719   6502   -845    166   -121       O  
ATOM   7480  C5'  DA T  11      24.687 -15.402  35.688  1.00 48.64           C  
ANISOU 7480  C5'  DA T  11     5655   6574   6254   -903    203   -124       C  
ATOM   7481  C4'  DA T  11      24.667 -14.359  34.590  1.00 49.34           C  
ANISOU 7481  C4'  DA T  11     5772   6715   6261   -992    203   -145       C  
ATOM   7482  O4'  DA T  11      24.099 -13.124  35.088  1.00 46.38           O  
ANISOU 7482  O4'  DA T  11     5445   6364   5814   -954    119    -82       O  
ATOM   7483  C3'  DA T  11      26.043 -13.999  34.040  1.00 51.60           C  
ANISOU 7483  C3'  DA T  11     6023   6991   6591  -1042    223   -203       C  
ATOM   7484  O3'  DA T  11      25.934 -14.009  32.639  1.00 54.99           O  
ANISOU 7484  O3'  DA T  11     6444   7478   6971  -1163    283   -250       O  
ATOM   7485  C2'  DA T  11      26.294 -12.584  34.540  1.00 50.51           C  
ANISOU 7485  C2'  DA T  11     5915   6859   6418  -1006    135   -156       C  
ATOM   7486  C1'  DA T  11      24.869 -12.040  34.633  1.00 49.14           C  
ANISOU 7486  C1'  DA T  11     5792   6723   6156   -996     91    -92       C  
ATOM   7487  N9   DA T  11      24.731 -10.925  35.566  1.00 52.12           N  
ANISOU 7487  N9   DA T  11     6191   7091   6521   -923      2    -49       N  
ATOM   7488  C8   DA T  11      25.222 -10.852  36.846  1.00 52.50           C  
ANISOU 7488  C8   DA T  11     6227   7111   6607   -827    -44    -48       C  
ATOM   7489  N7   DA T  11      24.965  -9.721  37.462  1.00 52.67           N  
ANISOU 7489  N7   DA T  11     6264   7139   6610   -783   -118    -30       N  
ATOM   7490  C5   DA T  11      24.253  -8.993  36.516  1.00 54.08           C  
ANISOU 7490  C5   DA T  11     6463   7336   6751   -852   -126     -4       C  
ATOM   7491  C6   DA T  11      23.688  -7.699  36.544  1.00 53.91           C  
ANISOU 7491  C6   DA T  11     6449   7313   6722   -851   -192     26       C  
ATOM   7492  N6   DA T  11      23.761  -6.905  37.617  1.00 55.14           N  
ANISOU 7492  N6   DA T  11     6594   7451   6906   -773   -259     10       N  
ATOM   7493  N1   DA T  11      23.044  -7.254  35.438  1.00 53.28           N  
ANISOU 7493  N1   DA T  11     6378   7252   6613   -937   -190     70       N  
ATOM   7494  C2   DA T  11      22.973  -8.067  34.371  1.00 56.02           C  
ANISOU 7494  C2   DA T  11     6730   7636   6920  -1023   -120     71       C  
ATOM   7495  N3   DA T  11      23.467  -9.307  34.223  1.00 55.61           N  
ANISOU 7495  N3   DA T  11     6669   7590   6870  -1034    -46     23       N  
ATOM   7496  C4   DA T  11      24.102  -9.717  35.340  1.00 54.21           C  
ANISOU 7496  C4   DA T  11     6480   7375   6742   -942    -54     -8       C  
ATOM   7497  P    DT T  12      27.151 -14.416  31.696  1.00 53.46           P  
ANISOU 7497  P    DT T  12     6188   7292   6833  -1250    363   -353       P  
ATOM   7498  OP1  DT T  12      26.571 -15.352  30.711  1.00 54.50           O  
ANISOU 7498  OP1  DT T  12     6294   7470   6944  -1338    450   -421       O  
ATOM   7499  OP2  DT T  12      28.316 -14.814  32.527  1.00 54.77           O  
ANISOU 7499  OP2  DT T  12     6311   7373   7126  -1176    359   -379       O  
ATOM   7500  O5'  DT T  12      27.510 -13.033  30.965  1.00 53.90           O  
ANISOU 7500  O5'  DT T  12     6260   7412   6807  -1326    326   -324       O  
ATOM   7501  C5'  DT T  12      26.482 -12.353  30.235  1.00 53.84           C  
ANISOU 7501  C5'  DT T  12     6289   7486   6681  -1397    303   -264       C  
ATOM   7502  C4'  DT T  12      26.583 -10.839  30.335  1.00 52.71           C  
ANISOU 7502  C4'  DT T  12     6169   7352   6506  -1395    213   -178       C  
ATOM   7503  O4'  DT T  12      26.298 -10.356  31.674  1.00 52.08           O  
ANISOU 7503  O4'  DT T  12     6123   7200   6465  -1266    131   -126       O  
ATOM   7504  C3'  DT T  12      27.950 -10.260  29.982  1.00 51.87           C  
ANISOU 7504  C3'  DT T  12     6025   7247   6437  -1437    216   -205       C  
ATOM   7505  O3'  DT T  12      27.916  -9.755  28.649  1.00 48.53           O  
ANISOU 7505  O3'  DT T  12     5583   6928   5930  -1577    236   -184       O  
ATOM   7506  C2'  DT T  12      28.166  -9.158  31.023  1.00 51.96           C  
ANISOU 7506  C2'  DT T  12     6057   7189   6495  -1339    114   -142       C  
ATOM   7507  C1'  DT T  12      26.803  -9.037  31.687  1.00 51.78           C  
ANISOU 7507  C1'  DT T  12     6081   7154   6438  -1272     63    -82       C  
ATOM   7508  N1   DT T  12      26.855  -8.459  33.076  1.00 53.17           N  
ANISOU 7508  N1   DT T  12     6273   7261   6668  -1146    -17    -60       N  
ATOM   7509  C2   DT T  12      26.184  -7.272  33.333  1.00 54.57           C  
ANISOU 7509  C2   DT T  12     6466   7430   6837  -1125    -99      4       C  
ATOM   7510  O2   DT T  12      25.534  -6.672  32.489  1.00 56.68           O  
ANISOU 7510  O2   DT T  12     6736   7736   7063  -1202   -115     63       O  
ATOM   7511  N3   DT T  12      26.289  -6.815  34.630  1.00 52.14           N  
ANISOU 7511  N3   DT T  12     6162   7071   6577  -1014   -162     -5       N  
ATOM   7512  C4   DT T  12      26.991  -7.411  35.670  1.00 52.58           C  
ANISOU 7512  C4   DT T  12     6209   7098   6673   -929   -157    -53       C  
ATOM   7513  O4   DT T  12      27.019  -6.917  36.799  1.00 52.89           O  
ANISOU 7513  O4   DT T  12     6245   7115   6736   -843   -218    -61       O  
ATOM   7514  C5   DT T  12      27.675  -8.649  35.333  1.00 50.20           C  
ANISOU 7514  C5   DT T  12     5889   6796   6388   -955    -78    -96       C  
ATOM   7515  C7   DT T  12      28.475  -9.402  36.358  1.00 50.58           C  
ANISOU 7515  C7   DT T  12     5913   6808   6496   -875    -73   -130       C  
ATOM   7516  C6   DT T  12      27.575  -9.102  34.076  1.00 50.64           C  
ANISOU 7516  C6   DT T  12     5939   6890   6411  -1058    -10   -107       C  
ATOM   7517  P    DT T  13      29.172  -9.043  27.960  1.00 51.29           P  
ANISOU 7517  P    DT T  13     5885   7314   6289  -1659    243   -193       P  
ATOM   7518  OP1  DT T  13      29.125  -9.391  26.524  1.00 54.97           O  
ANISOU 7518  OP1  DT T  13     6313   7916   6657  -1818    321   -229       O  
ATOM   7519  OP2  DT T  13      30.392  -9.323  28.738  1.00 52.96           O  
ANISOU 7519  OP2  DT T  13     6074   7434   6613  -1577    253   -262       O  
ATOM   7520  O5'  DT T  13      28.873  -7.488  28.153  1.00 51.72           O  
ANISOU 7520  O5'  DT T  13     5959   7354   6340  -1646    129    -62       O  
ATOM   7521  C5'  DT T  13      27.830  -6.849  27.425  1.00 56.95           C  
ANISOU 7521  C5'  DT T  13     6629   8091   6917  -1727     90     42       C  
ATOM   7522  C4'  DT T  13      27.979  -5.345  27.541  1.00 58.30           C  
ANISOU 7522  C4'  DT T  13     6787   8229   7137  -1723    -12    153       C  
ATOM   7523  O4'  DT T  13      27.836  -4.970  28.932  1.00 57.46           O  
ANISOU 7523  O4'  DT T  13     6710   7997   7124  -1571    -81    151       O  
ATOM   7524  C3'  DT T  13      29.323  -4.789  27.092  1.00 60.34           C  
ANISOU 7524  C3'  DT T  13     6994   8501   7431  -1781     -7    149       C  
ATOM   7525  O3'  DT T  13      29.094  -3.575  26.377  1.00 61.30           O  
ANISOU 7525  O3'  DT T  13     7082   8669   7539  -1870    -76    285       O  
ATOM   7526  C2'  DT T  13      30.101  -4.590  28.400  1.00 59.89           C  
ANISOU 7526  C2'  DT T  13     6947   8311   7496  -1638    -46     97       C  
ATOM   7527  C1'  DT T  13      28.980  -4.275  29.385  1.00 59.02           C  
ANISOU 7527  C1'  DT T  13     6881   8131   7414  -1530   -118    138       C  
ATOM   7528  N1   DT T  13      29.205  -4.656  30.829  1.00 58.89           N  
ANISOU 7528  N1   DT T  13     6890   8020   7467  -1381   -134     65       N  
ATOM   7529  C2   DT T  13      28.759  -3.789  31.815  1.00 57.93           C  
ANISOU 7529  C2   DT T  13     6778   7827   7406  -1286   -223     95       C  
ATOM   7530  O2   DT T  13      28.204  -2.728  31.585  1.00 57.72           O  
ANISOU 7530  O2   DT T  13     6737   7790   7404  -1311   -290    175       O  
ATOM   7531  N3   DT T  13      28.994  -4.210  33.101  1.00 57.35           N  
ANISOU 7531  N3   DT T  13     6722   7698   7372  -1165   -232     27       N  
ATOM   7532  C4   DT T  13      29.602  -5.387  33.503  1.00 57.41           C  
ANISOU 7532  C4   DT T  13     6734   7702   7379  -1126   -170    -46       C  
ATOM   7533  O4   DT T  13      29.758  -5.667  34.688  1.00 59.31           O  
ANISOU 7533  O4   DT T  13     6981   7902   7652  -1023   -192    -83       O  
ATOM   7534  C5   DT T  13      30.039  -6.251  32.434  1.00 57.66           C  
ANISOU 7534  C5   DT T  13     6750   7784   7374  -1222    -79    -77       C  
ATOM   7535  C7   DT T  13      30.720  -7.550  32.757  1.00 58.94           C  
ANISOU 7535  C7   DT T  13     6899   7926   7568  -1189     -8   -159       C  
ATOM   7536  C6   DT T  13      29.821  -5.855  31.165  1.00 58.76           C  
ANISOU 7536  C6   DT T  13     6876   7992   7458  -1344    -61    -31       C  
ATOM   7537  P    DA T  14      30.304  -2.716  25.766  1.00 64.87           P  
ANISOU 7537  P    DA T  14     7471   9150   8027  -1952    -92    329       P  
ATOM   7538  OP1  DA T  14      29.721  -1.911  24.668  1.00 66.36           O  
ANISOU 7538  OP1  DA T  14     7619   9443   8151  -2091   -137    483       O  
ATOM   7539  OP2  DA T  14      31.451  -3.611  25.495  1.00 65.19           O  
ANISOU 7539  OP2  DA T  14     7493   9230   8049  -1983     10    200       O  
ATOM   7540  O5'  DA T  14      30.723  -1.750  26.973  1.00 64.43           O  
ANISOU 7540  O5'  DA T  14     7416   8935   8127  -1817   -187    345       O  
ATOM   7541  C5'  DA T  14      29.750  -0.853  27.517  1.00 67.18           C  
ANISOU 7541  C5'  DA T  14     7775   9210   8542  -1756   -286    434       C  
ATOM   7542  C4'  DA T  14      30.363   0.214  28.410  1.00 69.70           C  
ANISOU 7542  C4'  DA T  14     8066   9401   9016  -1664   -371    439       C  
ATOM   7543  O4'  DA T  14      30.463  -0.276  29.773  1.00 69.74           O  
ANISOU 7543  O4'  DA T  14     8114   9318   9066  -1514   -367    321       O  
ATOM   7544  C3'  DA T  14      31.753   0.715  28.023  1.00 70.14           C  
ANISOU 7544  C3'  DA T  14     8068   9457   9126  -1714   -369    444       C  
ATOM   7545  O3'  DA T  14      31.745   2.131  28.167  1.00 71.20           O  
ANISOU 7545  O3'  DA T  14     8148   9513   9393  -1706   -475    543       O  
ATOM   7546  C2'  DA T  14      32.689   0.019  29.016  1.00 70.35           C  
ANISOU 7546  C2'  DA T  14     8121   9419   9191  -1604   -327    297       C  
ATOM   7547  C1'  DA T  14      31.798  -0.219  30.236  1.00 69.35           C  
ANISOU 7547  C1'  DA T  14     8044   9219   9085  -1470   -360    248       C  
ATOM   7548  N9   DA T  14      32.077  -1.472  30.946  1.00 68.28           N  
ANISOU 7548  N9   DA T  14     7952   9078   8915  -1392   -293    130       N  
ATOM   7549  C8   DA T  14      32.427  -2.675  30.391  1.00 67.62           C  
ANISOU 7549  C8   DA T  14     7878   9061   8754  -1444   -193     70       C  
ATOM   7550  N7   DA T  14      32.622  -3.633  31.264  1.00 65.71           N  
ANISOU 7550  N7   DA T  14     7662   8781   8524  -1352   -158    -19       N  
ATOM   7551  C5   DA T  14      32.376  -3.019  32.476  1.00 64.69           C  
ANISOU 7551  C5   DA T  14     7545   8575   8459  -1237   -240    -18       C  
ATOM   7552  C6   DA T  14      32.411  -3.506  33.796  1.00 65.30           C  
ANISOU 7552  C6   DA T  14     7643   8604   8564  -1115   -255    -79       C  
ATOM   7553  N6   DA T  14      32.727  -4.774  34.078  1.00 66.43           N  
ANISOU 7553  N6   DA T  14     7795   8754   8691  -1087   -190   -138       N  
ATOM   7554  N1   DA T  14      32.115  -2.642  34.801  1.00 64.38           N  
ANISOU 7554  N1   DA T  14     7525   8438   8499  -1029   -340    -76       N  
ATOM   7555  C2   DA T  14      31.808  -1.371  34.487  1.00 63.74           C  
ANISOU 7555  C2   DA T  14     7419   8334   8465  -1059   -405    -19       C  
ATOM   7556  N3   DA T  14      31.741  -0.801  33.279  1.00 62.76           N  
ANISOU 7556  N3   DA T  14     7271   8237   8339  -1169   -406     61       N  
ATOM   7557  C4   DA T  14      32.039  -1.687  32.308  1.00 64.77           C  
ANISOU 7557  C4   DA T  14     7532   8562   8515  -1257   -320     60       C  
ATOM   7558  P    DA T  15      33.040   3.055  27.950  1.00 71.39           P  
ANISOU 7558  P    DA T  15     8101   9499   9526  -1740   -511    578       P  
ATOM   7559  OP1  DA T  15      32.547   4.435  27.710  1.00 69.20           O  
ANISOU 7559  OP1  DA T  15     7756   9166   9369  -1774   -619    726       O  
ATOM   7560  OP2  DA T  15      33.951   2.396  26.983  1.00 70.27           O  
ANISOU 7560  OP2  DA T  15     7946   9475   9279  -1852   -419    557       O  
ATOM   7561  O5'  DA T  15      33.732   2.995  29.384  1.00 70.94           O  
ANISOU 7561  O5'  DA T  15     8066   9318   9570  -1583   -525    437       O  
ATOM   7562  C5'  DA T  15      33.156   3.712  30.474  1.00 72.65           C  
ANISOU 7562  C5'  DA T  15     8280   9421   9904  -1468   -610    419       C  
ATOM   7563  C4'  DA T  15      34.049   3.640  31.701  1.00 73.07           C  
ANISOU 7563  C4'  DA T  15     8340   9393  10030  -1345   -618    285       C  
ATOM   7564  O4'  DA T  15      33.980   2.306  32.273  1.00 70.61           O  
ANISOU 7564  O4'  DA T  15     8098   9120   9612  -1283   -545    180       O  
ATOM   7565  C3'  DA T  15      35.534   3.937  31.467  1.00 75.12           C  
ANISOU 7565  C3'  DA T  15     8554   9635  10352  -1375   -610    270       C  
ATOM   7566  O3'  DA T  15      36.013   4.687  32.572  1.00 80.07           O  
ANISOU 7566  O3'  DA T  15     9151  10154  11120  -1270   -680    201       O  
ATOM   7567  C2'  DA T  15      36.142   2.540  31.440  1.00 73.03           C  
ANISOU 7567  C2'  DA T  15     8339   9437   9974  -1373   -507    177       C  
ATOM   7568  C1'  DA T  15      35.305   1.912  32.546  1.00 70.46           C  
ANISOU 7568  C1'  DA T  15     8071   9088   9612  -1259   -509    101       C  
ATOM   7569  N9   DA T  15      35.408   0.466  32.629  1.00 66.46           N  
ANISOU 7569  N9   DA T  15     7613   8636   9003  -1246   -419     29       N  
ATOM   7570  C8   DA T  15      35.589  -0.416  31.603  1.00 67.32           C  
ANISOU 7570  C8   DA T  15     7730   8830   9021  -1342   -328     31       C  
ATOM   7571  N7   DA T  15      35.655  -1.665  31.993  1.00 66.48           N  
ANISOU 7571  N7   DA T  15     7656   8736   8867  -1299   -261    -51       N  
ATOM   7572  C5   DA T  15      35.513  -1.586  33.364  1.00 65.21           C  
ANISOU 7572  C5   DA T  15     7514   8507   8756  -1170   -317    -93       C  
ATOM   7573  C6   DA T  15      35.502  -2.571  34.364  1.00 66.44           C  
ANISOU 7573  C6   DA T  15     7698   8648   8900  -1077   -296   -161       C  
ATOM   7574  N6   DA T  15      35.634  -3.871  34.078  1.00 68.61           N  
ANISOU 7574  N6   DA T  15     7983   8955   9132  -1098   -210   -201       N  
ATOM   7575  N1   DA T  15      35.339  -2.169  35.648  1.00 65.62           N  
ANISOU 7575  N1   DA T  15     7598   8501   8835   -969   -366   -187       N  
ATOM   7576  C2   DA T  15      35.201  -0.857  35.909  1.00 64.85           C  
ANISOU 7576  C2   DA T  15     7477   8364   8801   -951   -448   -166       C  
ATOM   7577  N3   DA T  15      35.199   0.160  35.049  1.00 64.30           N  
ANISOU 7577  N3   DA T  15     7376   8282   8776  -1025   -478   -102       N  
ATOM   7578  C4   DA T  15      35.361  -0.279  33.782  1.00 65.77           C  
ANISOU 7578  C4   DA T  15     7561   8523   8905  -1136   -410    -58       C  
ATOM   7579  P    DT T  16      37.459   5.379  32.655  1.00 83.21           P  
ANISOU 7579  P    DT T  16     9486  10491  11640  -1270   -709    181       P  
ATOM   7580  OP1  DT T  16      37.409   6.588  31.809  1.00 84.85           O  
ANISOU 7580  OP1  DT T  16     9615  10670  11953  -1358   -771    317       O  
ATOM   7581  OP2  DT T  16      38.546   4.391  32.457  1.00 83.06           O  
ANISOU 7581  OP2  DT T  16     9491  10525  11545  -1288   -624    117       O  
ATOM   7582  O5'  DT T  16      37.472   5.787  34.207  1.00 86.44           O  
ANISOU 7582  O5'  DT T  16     9889  10807  12149  -1125   -773     61       O  
ATOM   7583  C5'  DT T  16      36.597   5.137  35.158  1.00 87.17           C  
ANISOU 7583  C5'  DT T  16    10039  10917  12166  -1035   -764    -18       C  
ATOM   7584  C4'  DT T  16      37.312   4.190  36.121  1.00 87.47           C  
ANISOU 7584  C4'  DT T  16    10114  10976  12146   -953   -726   -135       C  
ATOM   7585  O4'  DT T  16      37.239   2.807  35.667  1.00 87.46           O  
ANISOU 7585  O4'  DT T  16    10173  11055  12003   -987   -633   -129       O  
ATOM   7586  C3'  DT T  16      38.795   4.450  36.381  1.00 87.62           C  
ANISOU 7586  C3'  DT T  16    10091  10952  12247   -937   -738   -186       C  
ATOM   7587  O3'  DT T  16      39.018   4.342  37.774  1.00 88.05           O  
ANISOU 7587  O3'  DT T  16    10148  10992  12317   -827   -771   -298       O  
ATOM   7588  C2'  DT T  16      39.493   3.313  35.640  1.00 86.50           C  
ANISOU 7588  C2'  DT T  16     9981  10873  12014   -998   -643   -174       C  
ATOM   7589  C1'  DT T  16      38.492   2.205  35.937  1.00 85.27           C  
ANISOU 7589  C1'  DT T  16     9892  10777  11732   -967   -597   -192       C  
ATOM   7590  N1   DT T  16      38.649   0.944  35.143  1.00 83.68           N  
ANISOU 7590  N1   DT T  16     9723  10642  11430  -1031   -496   -182       N  
ATOM   7591  C2   DT T  16      38.594  -0.272  35.805  1.00 81.97           C  
ANISOU 7591  C2   DT T  16     9544  10448  11153   -971   -451   -241       C  
ATOM   7592  O2   DT T  16      38.424  -0.380  37.008  1.00 81.43           O  
ANISOU 7592  O2   DT T  16     9485  10364  11090   -874   -492   -288       O  
ATOM   7593  N3   DT T  16      38.745  -1.376  35.001  1.00 81.18           N  
ANISOU 7593  N3   DT T  16     9458  10397  10991  -1036   -357   -243       N  
ATOM   7594  C4   DT T  16      38.945  -1.388  33.628  1.00 82.33           C  
ANISOU 7594  C4   DT T  16     9586  10589  11106  -1157   -299   -204       C  
ATOM   7595  O4   DT T  16      39.065  -2.438  32.999  1.00 81.49           O  
ANISOU 7595  O4   DT T  16     9484  10531  10947  -1211   -209   -233       O  
ATOM   7596  C5   DT T  16      38.994  -0.086  32.996  1.00 83.44           C  
ANISOU 7596  C5   DT T  16     9692  10723  11289  -1220   -352   -129       C  
ATOM   7597  C7   DT T  16      39.203   0.035  31.512  1.00 86.26           C  
ANISOU 7597  C7   DT T  16    10019  11155  11601  -1365   -300    -68       C  
ATOM   7598  C6   DT T  16      38.843   1.003  33.771  1.00 83.70           C  
ANISOU 7598  C6   DT T  16     9708  10688  11406  -1152   -448   -117       C  
ATOM   7599  P    DT T  17      39.898   5.414  38.568  1.00 89.20           P  
ANISOU 7599  P    DT T  17    10222  11061  12609   -772   -850   -373       P  
ATOM   7600  OP1  DT T  17      38.953   6.251  39.337  1.00 88.46           O  
ANISOU 7600  OP1  DT T  17    10099  10936  12576   -714   -919   -422       O  
ATOM   7601  OP2  DT T  17      40.871   6.048  37.645  1.00 88.75           O  
ANISOU 7601  OP2  DT T  17    10114  10956  12651   -846   -854   -313       O  
ATOM   7602  O5'  DT T  17      40.728   4.475  39.565  1.00 85.00           O  
ANISOU 7602  O5'  DT T  17     9712  10569  12016   -701   -828   -463       O  
ATOM   7603  C5'  DT T  17      40.052   3.520  40.382  1.00 79.47           C  
ANISOU 7603  C5'  DT T  17     9061   9937  11196   -642   -807   -500       C  
ATOM   7604  C4'  DT T  17      40.774   2.183  40.418  1.00 75.16           C  
ANISOU 7604  C4'  DT T  17     8546   9433  10576   -640   -742   -499       C  
ATOM   7605  O4'  DT T  17      40.639   1.494  39.165  1.00 75.43           O  
ANISOU 7605  O4'  DT T  17     8613   9484  10562   -724   -661   -426       O  
ATOM   7606  C3'  DT T  17      42.287   2.212  40.574  1.00 72.41           C  
ANISOU 7606  C3'  DT T  17     8157   9051  10305   -635   -749   -534       C  
ATOM   7607  O3'  DT T  17      42.593   2.434  41.934  1.00 66.64           O  
ANISOU 7607  O3'  DT T  17     7398   8335   9589   -551   -813   -615       O  
ATOM   7608  C2'  DT T  17      42.712   0.821  40.095  1.00 72.11           C  
ANISOU 7608  C2'  DT T  17     8149   9042  10209   -666   -663   -504       C  
ATOM   7609  C1'  DT T  17      41.498   0.377  39.282  1.00 74.95           C  
ANISOU 7609  C1'  DT T  17     8558   9439  10480   -717   -609   -445       C  
ATOM   7610  N1   DT T  17      41.780  -0.193  37.918  1.00 75.70           N  
ANISOU 7610  N1   DT T  17     8660   9543  10558   -815   -522   -401       N  
ATOM   7611  C2   DT T  17      41.824  -1.570  37.771  1.00 77.42           C  
ANISOU 7611  C2   DT T  17     8900   9793  10724   -823   -444   -408       C  
ATOM   7612  O2   DT T  17      41.666  -2.365  38.687  1.00 77.54           O  
ANISOU 7612  O2   DT T  17     8927   9821  10712   -755   -448   -429       O  
ATOM   7613  N3   DT T  17      42.073  -1.993  36.485  1.00 79.08           N  
ANISOU 7613  N3   DT T  17     9105  10021  10920   -922   -362   -390       N  
ATOM   7614  C4   DT T  17      42.275  -1.200  35.364  1.00 79.14           C  
ANISOU 7614  C4   DT T  17     9091  10037  10942  -1016   -351   -350       C  
ATOM   7615  O4   DT T  17      42.494  -1.687  34.261  1.00 82.37           O  
ANISOU 7615  O4   DT T  17     9490  10487  11319  -1110   -271   -343       O  
ATOM   7616  C5   DT T  17      42.213   0.227  35.583  1.00 78.32           C  
ANISOU 7616  C5   DT T  17     8965   9895  10899  -1002   -442   -319       C  
ATOM   7617  C7   DT T  17      42.417   1.186  34.442  1.00 76.89           C  
ANISOU 7617  C7   DT T  17     8746   9717  10750  -1104   -447   -249       C  
ATOM   7618  C6   DT T  17      41.968   0.651  36.835  1.00 76.71           C  
ANISOU 7618  C6   DT T  17     8764   9657  10726   -901   -520   -353       C  
ATOM   7619  P    DG T  18      43.995   3.058  42.369  1.00 65.53           P  
ANISOU 7619  P    DG T  18     7194   8146   9558   -530   -863   -672       P  
ATOM   7620  OP1  DG T  18      44.935   1.918  42.465  1.00 66.49           O  
ANISOU 7620  OP1  DG T  18     7322   8286   9656   -526   -818   -661       O  
ATOM   7621  OP2  DG T  18      43.739   3.907  43.553  1.00 66.34           O  
ANISOU 7621  OP2  DG T  18     7257   8264   9686   -462   -946   -764       O  
ATOM   7622  O5'  DG T  18      44.452   4.013  41.169  1.00 61.94           O  
ANISOU 7622  O5'  DG T  18     6706   7609   9218   -605   -861   -628       O  
ATOM   7623  C5'  DG T  18      45.828   4.364  41.016  1.00 58.15           C  
ANISOU 7623  C5'  DG T  18     6178   7077   8840   -619   -873   -645       C  
ATOM   7624  C4'  DG T  18      46.269   4.262  39.559  1.00 53.75           C  
ANISOU 7624  C4'  DG T  18     5621   6496   8307   -719   -808   -562       C  
ATOM   7625  O4'  DG T  18      47.575   4.866  39.374  1.00 51.08           O  
ANISOU 7625  O4'  DG T  18     5223   6097   8088   -737   -829   -576       O  
ATOM   7626  C3'  DG T  18      46.416   2.850  39.014  1.00 53.22           C  
ANISOU 7626  C3'  DG T  18     5597   6477   8147   -755   -711   -534       C  
ATOM   7627  O3'  DG T  18      46.081   2.868  37.631  1.00 52.02           O  
ANISOU 7627  O3'  DG T  18     5456   6342   7969   -857   -652   -458       O  
ATOM   7628  C2'  DG T  18      47.897   2.542  39.252  1.00 51.27           C  
ANISOU 7628  C2'  DG T  18     5310   6199   7971   -742   -703   -574       C  
ATOM   7629  C1'  DG T  18      48.527   3.901  38.951  1.00 49.91           C  
ANISOU 7629  C1'  DG T  18     5079   5961   7922   -768   -757   -571       C  
ATOM   7630  N9   DG T  18      49.832   4.208  39.559  1.00 46.04           N  
ANISOU 7630  N9   DG T  18     4536   5424   7535   -730   -799   -628       N  
ATOM   7631  C8   DG T  18      50.952   4.623  38.871  1.00 48.55           C  
ANISOU 7631  C8   DG T  18     4804   5692   7949   -783   -785   -612       C  
ATOM   7632  N7   DG T  18      51.999   4.847  39.625  1.00 49.46           N  
ANISOU 7632  N7   DG T  18     4876   5767   8150   -733   -832   -672       N  
ATOM   7633  C5   DG T  18      51.547   4.566  40.909  1.00 48.94           C  
ANISOU 7633  C5   DG T  18     4829   5737   8031   -644   -882   -730       C  
ATOM   7634  C6   DG T  18      52.236   4.635  42.152  1.00 49.49           C  
ANISOU 7634  C6   DG T  18     4862   5807   8136   -569   -949   -806       C  
ATOM   7635  O6   DG T  18      53.419   4.965  42.345  1.00 52.20           O  
ANISOU 7635  O6   DG T  18     5151   6103   8578   -561   -978   -838       O  
ATOM   7636  N1   DG T  18      51.423   4.279  43.235  1.00 44.98           N  
ANISOU 7636  N1   DG T  18     4317   5307   7467   -503   -984   -842       N  
ATOM   7637  C2   DG T  18      50.102   3.899  43.114  1.00 47.87           C  
ANISOU 7637  C2   DG T  18     4739   5725   7724   -506   -956   -810       C  
ATOM   7638  N2   DG T  18      49.455   3.587  44.250  1.00 46.32           N  
ANISOU 7638  N2   DG T  18     4556   5606   7438   -442   -994   -850       N  
ATOM   7639  N3   DG T  18      49.450   3.833  41.951  1.00 45.69           N  
ANISOU 7639  N3   DG T  18     4499   5437   7423   -572   -895   -742       N  
ATOM   7640  C4   DG T  18      50.218   4.176  40.887  1.00 45.81           C  
ANISOU 7640  C4   DG T  18     4488   5395   7522   -641   -861   -704       C  
TER    7641       DG T  18                                                      
ATOM   7642  O5'  DA P 103      41.027 -14.509  36.059  1.00148.79           O  
ANISOU 7642  O5'  DA P 103    17730  18720  20082   -918    261   -614       O  
ATOM   7643  C5'  DA P 103      40.011 -14.165  36.993  1.00148.30           C  
ANISOU 7643  C5'  DA P 103    17735  18698  19913   -847    176   -513       C  
ATOM   7644  C4'  DA P 103      40.509 -13.102  37.961  1.00147.71           C  
ANISOU 7644  C4'  DA P 103    17686  18635  19803   -782     70   -458       C  
ATOM   7645  O4'  DA P 103      41.025 -11.961  37.222  1.00147.14           O  
ANISOU 7645  O4'  DA P 103    17635  18588  19683   -838     72   -502       O  
ATOM   7646  C3'  DA P 103      39.456 -12.537  38.918  1.00147.08           C  
ANISOU 7646  C3'  DA P 103    17673  18616  19595   -715    -18   -376       C  
ATOM   7647  O3'  DA P 103      40.010 -12.422  40.235  1.00147.13           O  
ANISOU 7647  O3'  DA P 103    17653  18615  19636   -634   -105   -322       O  
ATOM   7648  C2'  DA P 103      39.152 -11.168  38.312  1.00145.80           C  
ANISOU 7648  C2'  DA P 103    17572  18505  19320   -758    -38   -394       C  
ATOM   7649  C1'  DA P 103      40.558 -10.796  37.870  1.00145.53           C  
ANISOU 7649  C1'  DA P 103    17491  18429  19374   -793    -22   -448       C  
ATOM   7650  N9   DA P 103      40.619  -9.634  36.989  1.00143.75           N  
ANISOU 7650  N9   DA P 103    17295  18237  19086   -859    -20   -469       N  
ATOM   7651  C8   DA P 103      40.324  -9.576  35.654  1.00143.22           C  
ANISOU 7651  C8   DA P 103    17237  18210  18971   -962     54   -502       C  
ATOM   7652  N7   DA P 103      40.474  -8.381  35.133  1.00142.43           N  
ANISOU 7652  N7   DA P 103    17154  18139  18825  -1008     26   -490       N  
ATOM   7653  C5   DA P 103      40.896  -7.604  36.200  1.00141.65           C  
ANISOU 7653  C5   DA P 103    17056  18006  18757   -926    -69   -463       C  
ATOM   7654  C6   DA P 103      41.231  -6.237  36.314  1.00140.73           C  
ANISOU 7654  C6   DA P 103    16945  17885  18640   -921   -141   -444       C  
ATOM   7655  N6   DA P 103      41.185  -5.386  35.284  1.00140.14           N  
ANISOU 7655  N6   DA P 103    16873  17840  18534  -1007   -130   -429       N  
ATOM   7656  N1   DA P 103      41.611  -5.777  37.531  1.00140.51           N  
ANISOU 7656  N1   DA P 103    16909  17828  18650   -831   -226   -440       N  
ATOM   7657  C2   DA P 103      41.660  -6.629  38.567  1.00140.65           C  
ANISOU 7657  C2   DA P 103    16916  17834  18690   -755   -243   -437       C  
ATOM   7658  N3   DA P 103      41.368  -7.932  38.579  1.00141.22           N  
ANISOU 7658  N3   DA P 103    16981  17905  18772   -751   -186   -433       N  
ATOM   7659  C4   DA P 103      40.991  -8.361  37.356  1.00142.18           C  
ANISOU 7659  C4   DA P 103    17110  18041  18870   -836    -98   -453       C  
ATOM   7660  P    DA P 104      39.108 -12.135  41.533  1.00146.70           P  
ANISOU 7660  P    DA P 104    17635  18632  19473   -556   -196   -242       P  
ATOM   7661  OP1  DA P 104      39.194 -13.344  42.381  1.00147.18           O  
ANISOU 7661  OP1  DA P 104    17635  18673  19612   -510   -209   -170       O  
ATOM   7662  OP2  DA P 104      37.775 -11.646  41.113  1.00146.06           O  
ANISOU 7662  OP2  DA P 104    17629  18606  19261   -577   -186   -242       O  
ATOM   7663  O5'  DA P 104      39.875 -10.928  42.264  1.00145.68           O  
ANISOU 7663  O5'  DA P 104    17506  18527  19320   -519   -285   -252       O  
ATOM   7664  C5'  DA P 104      40.233  -9.731  41.563  1.00143.60           C  
ANISOU 7664  C5'  DA P 104    17269  18256  19036   -559   -287   -312       C  
ATOM   7665  C4'  DA P 104      39.548  -8.485  42.116  1.00142.14           C  
ANISOU 7665  C4'  DA P 104    17131  18133  18744   -527   -363   -312       C  
ATOM   7666  O4'  DA P 104      39.589  -7.437  41.110  1.00141.64           O  
ANISOU 7666  O4'  DA P 104    17093  18052  18672   -585   -348   -353       O  
ATOM   7667  C3'  DA P 104      38.074  -8.618  42.500  1.00141.14           C  
ANISOU 7667  C3'  DA P 104    17050  18070  18508   -502   -374   -275       C  
ATOM   7668  O3'  DA P 104      37.771  -7.778  43.618  1.00140.87           O  
ANISOU 7668  O3'  DA P 104    17020  18099  18404   -444   -460   -279       O  
ATOM   7669  C2'  DA P 104      37.356  -8.155  41.236  1.00140.73           C  
ANISOU 7669  C2'  DA P 104    17045  18009  18416   -571   -323   -295       C  
ATOM   7670  C1'  DA P 104      38.271  -7.019  40.795  1.00141.13           C  
ANISOU 7670  C1'  DA P 104    17082  18027  18514   -601   -347   -337       C  
ATOM   7671  N9   DA P 104      38.183  -6.694  39.369  1.00140.95           N  
ANISOU 7671  N9   DA P 104    17076  17989  18491   -691   -290   -349       N  
ATOM   7672  C8   DA P 104      37.904  -7.546  38.332  1.00140.49           C  
ANISOU 7672  C8   DA P 104    17024  17933  18425   -760   -201   -350       C  
ATOM   7673  N7   DA P 104      37.887  -6.970  37.153  1.00139.74           N  
ANISOU 7673  N7   DA P 104    16936  17848  18311   -846   -168   -357       N  
ATOM   7674  C5   DA P 104      38.177  -5.645  37.434  1.00139.79           C  
ANISOU 7674  C5   DA P 104    16939  17842  18331   -829   -244   -350       C  
ATOM   7675  C6   DA P 104      38.313  -4.507  36.612  1.00139.32           C  
ANISOU 7675  C6   DA P 104    16875  17784  18278   -894   -262   -334       C  
ATOM   7676  N6   DA P 104      38.167  -4.544  35.286  1.00138.93           N  
ANISOU 7676  N6   DA P 104    16824  17768  18195  -1000   -201   -316       N  
ATOM   7677  N1   DA P 104      38.610  -3.328  37.203  1.00139.61           N  
ANISOU 7677  N1   DA P 104    16895  17789  18359   -853   -346   -334       N  
ATOM   7678  C2   DA P 104      38.759  -3.291  38.535  1.00140.08           C  
ANISOU 7678  C2   DA P 104    16949  17837  18438   -755   -405   -362       C  
ATOM   7679  N3   DA P 104      38.658  -4.292  39.412  1.00140.42           N  
ANISOU 7679  N3   DA P 104    16997  17898  18458   -693   -398   -371       N  
ATOM   7680  C4   DA P 104      38.362  -5.454  38.794  1.00140.50           C  
ANISOU 7680  C4   DA P 104    17021  17922  18441   -732   -317   -357       C  
ATOM   7681  P    DT P 105      36.310  -7.729  44.285  1.00140.85           P  
ANISOU 7681  P    DT P 105    17054  18178  18283   -408   -486   -253       P  
ATOM   7682  OP1  DT P 105      36.487  -7.286  45.688  1.00141.59           O  
ANISOU 7682  OP1  DT P 105    17117  18350  18332   -347   -569   -264       O  
ATOM   7683  OP2  DT P 105      35.615  -9.006  44.005  1.00141.02           O  
ANISOU 7683  OP2  DT P 105    17088  18200  18295   -420   -426   -194       O  
ATOM   7684  O5'  DT P 105      35.557  -6.583  43.456  1.00138.22           O  
ANISOU 7684  O5'  DT P 105    16768  17831  17920   -446   -483   -291       O  
ATOM   7685  C5'  DT P 105      34.701  -5.641  44.100  1.00134.86           C  
ANISOU 7685  C5'  DT P 105    16355  17456  17429   -412   -539   -319       C  
ATOM   7686  C4'  DT P 105      35.103  -4.223  43.740  1.00132.54           C  
ANISOU 7686  C4'  DT P 105    16049  17118  17191   -430   -579   -376       C  
ATOM   7687  O4'  DT P 105      36.070  -4.247  42.655  1.00131.87           O  
ANISOU 7687  O4'  DT P 105    15956  16961  17187   -489   -538   -370       O  
ATOM   7688  C3'  DT P 105      33.969  -3.346  43.224  1.00130.94           C  
ANISOU 7688  C3'  DT P 105    15874  16906  16971   -453   -587   -382       C  
ATOM   7689  O3'  DT P 105      33.196  -2.772  44.299  1.00128.72           O  
ANISOU 7689  O3'  DT P 105    15581  16684  16644   -396   -642   -427       O  
ATOM   7690  C2'  DT P 105      34.726  -2.326  42.375  1.00131.26           C  
ANISOU 7690  C2'  DT P 105    15893  16872  17108   -501   -600   -399       C  
ATOM   7691  C1'  DT P 105      35.821  -3.183  41.750  1.00131.07           C  
ANISOU 7691  C1'  DT P 105    15863  16818  17117   -539   -545   -375       C  
ATOM   7692  N1   DT P 105      35.477  -3.702  40.371  1.00129.38           N  
ANISOU 7692  N1   DT P 105    15680  16590  16889   -622   -468   -327       N  
ATOM   7693  C2   DT P 105      35.486  -2.834  39.289  1.00128.40           C  
ANISOU 7693  C2   DT P 105    15553  16435  16799   -694   -466   -309       C  
ATOM   7694  O2   DT P 105      35.758  -1.648  39.357  1.00128.08           O  
ANISOU 7694  O2   DT P 105    15484  16361  16820   -692   -524   -323       O  
ATOM   7695  N3   DT P 105      35.164  -3.413  38.088  1.00127.92           N  
ANISOU 7695  N3   DT P 105    15513  16389  16701   -777   -394   -269       N  
ATOM   7696  C4   DT P 105      34.839  -4.737  37.852  1.00128.57           C  
ANISOU 7696  C4   DT P 105    15618  16500  16732   -790   -322   -262       C  
ATOM   7697  O4   DT P 105      34.563  -5.143  36.727  1.00128.48           O  
ANISOU 7697  O4   DT P 105    15617  16510  16689   -873   -258   -243       O  
ATOM   7698  C5   DT P 105      34.842  -5.592  39.018  1.00128.86           C  
ANISOU 7698  C5   DT P 105    15654  16547  16760   -707   -329   -277       C  
ATOM   7699  C7   DT P 105      34.502  -7.050  38.901  1.00128.63           C  
ANISOU 7699  C7   DT P 105    15634  16532  16707   -712   -260   -264       C  
ATOM   7700  C6   DT P 105      35.159  -5.040  40.200  1.00129.04           C  
ANISOU 7700  C6   DT P 105    15658  16570  16802   -631   -403   -301       C  
ATOM   7701  P    DT P 106      33.620  -1.476  45.152  1.00128.14           P  
ANISOU 7701  P    DT P 106    15452  16614  16622   -356   -721   -524       P  
ATOM   7702  OP1  DT P 106      34.910  -1.763  45.823  1.00127.89           O  
ANISOU 7702  OP1  DT P 106    15383  16602  16606   -330   -743   -547       O  
ATOM   7703  OP2  DT P 106      32.439  -1.095  45.964  1.00128.03           O  
ANISOU 7703  OP2  DT P 106    15431  16666  16547   -316   -749   -571       O  
ATOM   7704  O5'  DT P 106      33.865  -0.336  44.046  1.00123.51           O  
ANISOU 7704  O5'  DT P 106    14853  15923  16151   -409   -732   -527       O  
ATOM   7705  C5'  DT P 106      33.189   0.919  44.080  1.00115.24           C  
ANISOU 7705  C5'  DT P 106    13776  14842  15168   -404   -779   -574       C  
ATOM   7706  C4'  DT P 106      32.424   1.196  42.794  1.00107.80           C  
ANISOU 7706  C4'  DT P 106    12860  13842  14258   -471   -754   -496       C  
ATOM   7707  O4'  DT P 106      32.746   0.245  41.745  1.00103.64           O  
ANISOU 7707  O4'  DT P 106    12378  13312  13690   -532   -686   -410       O  
ATOM   7708  C3'  DT P 106      30.904   1.154  42.936  1.00103.93           C  
ANISOU 7708  C3'  DT P 106    12392  13383  13713   -458   -750   -485       C  
ATOM   7709  O3'  DT P 106      30.402   2.479  42.762  1.00101.13           O  
ANISOU 7709  O3'  DT P 106    11988  12962  13473   -466   -802   -511       O  
ATOM   7710  C2'  DT P 106      30.441   0.204  41.829  1.00101.30           C  
ANISOU 7710  C2'  DT P 106    12120  13057  13311   -520   -681   -379       C  
ATOM   7711  C1'  DT P 106      31.633   0.218  40.881  1.00 99.76           C  
ANISOU 7711  C1'  DT P 106    11917  12815  13170   -582   -661   -342       C  
ATOM   7712  N1   DT P 106      31.713  -0.968  39.968  1.00 95.73           N  
ANISOU 7712  N1   DT P 106    11453  12330  12589   -640   -581   -276       N  
ATOM   7713  C2   DT P 106      31.828  -0.783  38.599  1.00 92.88           C  
ANISOU 7713  C2   DT P 106    11095  11947  12249   -734   -552   -211       C  
ATOM   7714  O2   DT P 106      31.876   0.307  38.058  1.00 92.83           O  
ANISOU 7714  O2   DT P 106    11055  11897  12320   -776   -593   -182       O  
ATOM   7715  N3   DT P 106      31.889  -1.945  37.870  1.00 90.63           N  
ANISOU 7715  N3   DT P 106    10843  11698  11894   -786   -473   -180       N  
ATOM   7716  C4   DT P 106      31.847  -3.243  38.356  1.00 91.85           C  
ANISOU 7716  C4   DT P 106    11024  11889  11988   -748   -424   -199       C  
ATOM   7717  O4   DT P 106      31.908  -4.218  37.612  1.00 90.41           O  
ANISOU 7717  O4   DT P 106    10857  11726  11769   -801   -351   -182       O  
ATOM   7718  C5   DT P 106      31.724  -3.365  39.792  1.00 93.20           C  
ANISOU 7718  C5   DT P 106    11190  12077  12146   -649   -465   -242       C  
ATOM   7719  C7   DT P 106      31.660  -4.710  40.456  1.00 94.08           C  
ANISOU 7719  C7   DT P 106    11315  12227  12203   -605   -427   -241       C  
ATOM   7720  C6   DT P 106      31.663  -2.238  40.513  1.00 94.51           C  
ANISOU 7720  C6   DT P 106    11328  12227  12355   -603   -538   -282       C  
ATOM   7721  P    DA P 107      28.836   2.822  42.795  1.00 98.47           P  
ANISOU 7721  P    DA P 107    11653  12627  13136   -459   -812   -507       P  
ATOM   7722  OP1  DA P 107      28.710   4.239  43.204  1.00 99.49           O  
ANISOU 7722  OP1  DA P 107    11697  12689  13417   -436   -881   -592       O  
ATOM   7723  OP2  DA P 107      28.124   1.763  43.548  1.00 98.04           O  
ANISOU 7723  OP2  DA P 107    11643  12673  12934   -417   -775   -520       O  
ATOM   7724  O5'  DA P 107      28.408   2.699  41.259  1.00 95.06           O  
ANISOU 7724  O5'  DA P 107    11255  12151  12714   -549   -782   -370       O  
ATOM   7725  C5'  DA P 107      28.992   3.563  40.278  1.00 89.60           C  
ANISOU 7725  C5'  DA P 107    10524  11378  12144   -615   -810   -311       C  
ATOM   7726  C4'  DA P 107      28.266   3.466  38.945  1.00 83.52           C  
ANISOU 7726  C4'  DA P 107     9778  10599  11356   -704   -788   -179       C  
ATOM   7727  O4'  DA P 107      28.642   2.243  38.269  1.00 79.55           O  
ANISOU 7727  O4'  DA P 107     9339  10160  10726   -753   -712   -125       O  
ATOM   7728  C3'  DA P 107      26.745   3.431  39.016  1.00 82.28           C  
ANISOU 7728  C3'  DA P 107     9635  10455  11171   -695   -791   -156       C  
ATOM   7729  O3'  DA P 107      26.239   4.085  37.877  1.00 82.44           O  
ANISOU 7729  O3'  DA P 107     9628  10429  11266   -778   -816    -40       O  
ATOM   7730  C2'  DA P 107      26.420   1.943  38.961  1.00 78.35           C  
ANISOU 7730  C2'  DA P 107     9221  10048  10500   -696   -713   -136       C  
ATOM   7731  C1'  DA P 107      27.485   1.482  37.977  1.00 75.93           C  
ANISOU 7731  C1'  DA P 107     8932   9753  10166   -770   -671    -79       C  
ATOM   7732  N9   DA P 107      27.849   0.073  38.067  1.00 70.72           N  
ANISOU 7732  N9   DA P 107     8328   9159   9385   -762   -597    -94       N  
ATOM   7733  C8   DA P 107      27.989  -0.692  39.194  1.00 70.68           C  
ANISOU 7733  C8   DA P 107     8342   9192   9322   -681   -581   -164       C  
ATOM   7734  N7   DA P 107      28.338  -1.935  38.949  1.00 68.98           N  
ANISOU 7734  N7   DA P 107     8162   9016   9030   -698   -514   -150       N  
ATOM   7735  C5   DA P 107      28.441  -1.979  37.566  1.00 65.91           C  
ANISOU 7735  C5   DA P 107     7780   8624   8640   -798   -478    -85       C  
ATOM   7736  C6   DA P 107      28.777  -3.010  36.666  1.00 63.50           C  
ANISOU 7736  C6   DA P 107     7497   8353   8278   -866   -400    -62       C  
ATOM   7737  N6   DA P 107      29.082  -4.246  37.058  1.00 58.75           N  
ANISOU 7737  N6   DA P 107     6912   7773   7636   -834   -346    -96       N  
ATOM   7738  N1   DA P 107      28.782  -2.722  35.344  1.00 65.53           N  
ANISOU 7738  N1   DA P 107     7746   8624   8530   -973   -380     -3       N  
ATOM   7739  C2   DA P 107      28.472  -1.479  34.943  1.00 64.92           C  
ANISOU 7739  C2   DA P 107     7639   8519   8510  -1009   -442     53       C  
ATOM   7740  N3   DA P 107      28.143  -0.431  35.698  1.00 66.64           N  
ANISOU 7740  N3   DA P 107     7829   8681   8810   -947   -521     42       N  
ATOM   7741  C4   DA P 107      28.144  -0.750  37.007  1.00 66.80           C  
ANISOU 7741  C4   DA P 107     7861   8698   8824   -842   -531    -40       C  
ATOM   7742  P    DA P 108      24.853   4.871  37.928  1.00 82.74           P  
ANISOU 7742  P    DA P 108     9624  10415  11399   -771   -867    -16       P  
ATOM   7743  OP1  DA P 108      25.210   6.308  37.885  1.00 82.68           O  
ANISOU 7743  OP1  DA P 108     9515  10298  11602   -777   -946    -17       O  
ATOM   7744  OP2  DA P 108      24.023   4.340  39.035  1.00 80.90           O  
ANISOU 7744  OP2  DA P 108     9422  10230  11088   -686   -846   -115       O  
ATOM   7745  O5'  DA P 108      24.148   4.443  36.554  1.00 81.89           O  
ANISOU 7745  O5'  DA P 108     9553  10345  11218   -875   -839    141       O  
ATOM   7746  C5'  DA P 108      24.916   4.161  35.372  1.00 81.25           C  
ANISOU 7746  C5'  DA P 108     9485  10301  11085   -976   -810    240       C  
ATOM   7747  C4'  DA P 108      24.367   2.972  34.591  1.00 79.08           C  
ANISOU 7747  C4'  DA P 108     9284  10125  10639  -1039   -737    303       C  
ATOM   7748  O4'  DA P 108      24.997   1.740  35.023  1.00 76.43           O  
ANISOU 7748  O4'  DA P 108     9011   9851  10177  -1000   -662    219       O  
ATOM   7749  C3'  DA P 108      22.867   2.747  34.731  1.00 78.67           C  
ANISOU 7749  C3'  DA P 108     9255  10085  10551  -1021   -739    326       C  
ATOM   7750  O3'  DA P 108      22.253   3.072  33.487  1.00 82.69           O  
ANISOU 7750  O3'  DA P 108     9742  10610  11065  -1132   -760    472       O  
ATOM   7751  C2'  DA P 108      22.714   1.272  35.108  1.00 75.97           C  
ANISOU 7751  C2'  DA P 108     8996   9825  10044   -984   -656    263       C  
ATOM   7752  C1'  DA P 108      24.090   0.680  34.835  1.00 72.56           C  
ANISOU 7752  C1'  DA P 108     8581   9428   9561  -1011   -606    235       C  
ATOM   7753  N9   DA P 108      24.440  -0.406  35.749  1.00 68.48           N  
ANISOU 7753  N9   DA P 108     8110   8945   8965   -932   -552    137       N  
ATOM   7754  C8   DA P 108      24.444  -0.367  37.117  1.00 66.25           C  
ANISOU 7754  C8   DA P 108     7825   8646   8703   -823   -574     45       C  
ATOM   7755  N7   DA P 108      24.798  -1.491  37.689  1.00 62.85           N  
ANISOU 7755  N7   DA P 108     7431   8260   8190   -779   -523     -5       N  
ATOM   7756  C5   DA P 108      25.047  -2.331  36.622  1.00 64.61           C  
ANISOU 7756  C5   DA P 108     7681   8518   8349   -860   -458     43       C  
ATOM   7757  C6   DA P 108      25.457  -3.681  36.550  1.00 64.61           C  
ANISOU 7757  C6   DA P 108     7712   8559   8277   -864   -383     21       C  
ATOM   7758  N6   DA P 108      25.706  -4.430  37.626  1.00 64.43           N  
ANISOU 7758  N6   DA P 108     7698   8547   8234   -782   -370    -32       N  
ATOM   7759  N1   DA P 108      25.611  -4.229  35.324  1.00 64.55           N  
ANISOU 7759  N1   DA P 108     7713   8585   8228   -961   -325     57       N  
ATOM   7760  C2   DA P 108      25.364  -3.476  34.242  1.00 65.07           C  
ANISOU 7760  C2   DA P 108     7762   8660   8301  -1054   -344    126       C  
ATOM   7761  N3   DA P 108      24.972  -2.202  34.184  1.00 65.24           N  
ANISOU 7761  N3   DA P 108     7754   8645   8391  -1062   -419    177       N  
ATOM   7762  C4   DA P 108      24.829  -1.682  35.417  1.00 66.16           C  
ANISOU 7762  C4   DA P 108     7860   8710   8569   -958   -473    125       C  
ATOM   7763  P    DT P 109      20.677   2.886  33.248  1.00 85.34           P  
ANISOU 7763  P    DT P 109    10095  10964  11367  -1149   -766    535       P  
ATOM   7764  OP1  DT P 109      20.276   3.875  32.223  1.00 85.39           O  
ANISOU 7764  OP1  DT P 109    10030  10941  11474  -1248   -835    691       O  
ATOM   7765  OP2  DT P 109      19.970   2.844  34.553  1.00 82.43           O  
ANISOU 7765  OP2  DT P 109     9736  10556  11028  -1028   -773    424       O  
ATOM   7766  O5'  DT P 109      20.612   1.416  32.608  1.00 81.90           O  
ANISOU 7766  O5'  DT P 109     9740  10649  10729  -1204   -671    545       O  
ATOM   7767  C5'  DT P 109      21.494   1.046  31.536  1.00 75.17           C  
ANISOU 7767  C5'  DT P 109     8891   9871   9799  -1310   -629    593       C  
ATOM   7768  C4'  DT P 109      21.267  -0.397  31.114  1.00 67.83           C  
ANISOU 7768  C4'  DT P 109     8028   9044   8700  -1345   -535    564       C  
ATOM   7769  O4'  DT P 109      21.852  -1.294  32.092  1.00 63.58           O  
ANISOU 7769  O4'  DT P 109     7534   8498   8127  -1248   -479    434       O  
ATOM   7770  C3'  DT P 109      19.806  -0.819  30.978  1.00 64.92           C  
ANISOU 7770  C3'  DT P 109     7689   8705   8272  -1353   -529    605       C  
ATOM   7771  O3'  DT P 109      19.607  -1.391  29.670  1.00 59.93           O  
ANISOU 7771  O3'  DT P 109     7065   8183   7522  -1484   -484    674       O  
ATOM   7772  C2'  DT P 109      19.588  -1.791  32.151  1.00 59.98           C  
ANISOU 7772  C2'  DT P 109     7121   8067   7604  -1233   -480    485       C  
ATOM   7773  C1'  DT P 109      20.982  -2.382  32.323  1.00 58.06           C  
ANISOU 7773  C1'  DT P 109     6888   7839   7335  -1219   -427    403       C  
ATOM   7774  N1   DT P 109      21.349  -2.966  33.669  1.00 54.95           N  
ANISOU 7774  N1   DT P 109     6519   7413   6946  -1094   -405    293       N  
ATOM   7775  C2   DT P 109      21.938  -4.225  33.736  1.00 53.56           C  
ANISOU 7775  C2   DT P 109     6372   7274   6703  -1086   -328    232       C  
ATOM   7776  O2   DT P 109      22.169  -4.930  32.763  1.00 51.98           O  
ANISOU 7776  O2   DT P 109     6178   7130   6440  -1173   -266    241       O  
ATOM   7777  N3   DT P 109      22.248  -4.652  35.007  1.00 49.79           N  
ANISOU 7777  N3   DT P 109     5906   6771   6240   -977   -324    158       N  
ATOM   7778  C4   DT P 109      22.039  -3.967  36.187  1.00 51.70           C  
ANISOU 7778  C4   DT P 109     6135   6974   6535   -882   -384    124       C  
ATOM   7779  O4   DT P 109      22.354  -4.439  37.277  1.00 55.60           O  
ANISOU 7779  O4   DT P 109     6634   7472   7020   -798   -378     64       O  
ATOM   7780  C5   DT P 109      21.430  -2.662  36.051  1.00 53.33           C  
ANISOU 7780  C5   DT P 109     6309   7139   6814   -893   -456    164       C  
ATOM   7781  C7   DT P 109      21.153  -1.826  37.269  1.00 54.62           C  
ANISOU 7781  C7   DT P 109     6442   7260   7051   -799   -517    105       C  
ATOM   7782  C6   DT P 109      21.123  -2.227  34.819  1.00 52.87           C  
ANISOU 7782  C6   DT P 109     6238   7088   6764   -995   -466    253       C  
ATOM   7783  P    DT P 110      18.169  -1.937  29.215  1.00 61.20           P  
ANISOU 7783  P    DT P 110     7252   8400   7599  -1526   -469    728       P  
ATOM   7784  OP1  DT P 110      18.147  -1.926  27.732  1.00 61.04           O  
ANISOU 7784  OP1  DT P 110     7204   8495   7492  -1689   -460    831       O  
ATOM   7785  OP2  DT P 110      17.121  -1.239  30.004  1.00 53.08           O  
ANISOU 7785  OP2  DT P 110     6214   7282   6673  -1442   -540    753       O  
ATOM   7786  O5'  DT P 110      18.186  -3.461  29.703  1.00 58.04           O  
ANISOU 7786  O5'  DT P 110     6919   8034   7101  -1467   -372    604       O  
ATOM   7787  C5'  DT P 110      19.141  -4.381  29.180  1.00 55.53           C  
ANISOU 7787  C5'  DT P 110     6610   7786   6705  -1521   -288    537       C  
ATOM   7788  C4'  DT P 110      18.855  -5.781  29.683  1.00 54.28           C  
ANISOU 7788  C4'  DT P 110     6499   7636   6489  -1461   -210    440       C  
ATOM   7789  O4'  DT P 110      19.335  -5.906  31.039  1.00 56.35           O  
ANISOU 7789  O4'  DT P 110     6776   7815   6818  -1325   -216    364       O  
ATOM   7790  C3'  DT P 110      17.381  -6.172  29.711  1.00 53.66           C  
ANISOU 7790  C3'  DT P 110     6448   7573   6368  -1452   -212    475       C  
ATOM   7791  O3'  DT P 110      17.246  -7.295  28.858  1.00 50.68           O  
ANISOU 7791  O3'  DT P 110     6079   7284   5893  -1536   -130    440       O  
ATOM   7792  C2'  DT P 110      17.073  -6.469  31.184  1.00 54.95           C  
ANISOU 7792  C2'  DT P 110     6641   7657   6580  -1302   -219    415       C  
ATOM   7793  C1'  DT P 110      18.460  -6.731  31.769  1.00 54.30           C  
ANISOU 7793  C1'  DT P 110     6553   7543   6536  -1249   -192    332       C  
ATOM   7794  N1   DT P 110      18.685  -6.410  33.223  1.00 53.75           N  
ANISOU 7794  N1   DT P 110     6487   7402   6534  -1116   -232    288       N  
ATOM   7795  C2   DT P 110      19.403  -7.307  33.993  1.00 55.49           C  
ANISOU 7795  C2   DT P 110     6715   7610   6757  -1048   -189    214       C  
ATOM   7796  O2   DT P 110      19.846  -8.353  33.562  1.00 60.94           O  
ANISOU 7796  O2   DT P 110     7407   8327   7419  -1083   -118    178       O  
ATOM   7797  N3   DT P 110      19.587  -6.952  35.307  1.00 53.14           N  
ANISOU 7797  N3   DT P 110     6413   7272   6505   -939   -231    180       N  
ATOM   7798  C4   DT P 110      19.138  -5.803  35.927  1.00 51.87           C  
ANISOU 7798  C4   DT P 110     6238   7079   6393   -890   -305    191       C  
ATOM   7799  O4   DT P 110      19.371  -5.597  37.115  1.00 49.81           O  
ANISOU 7799  O4   DT P 110     5967   6801   6159   -800   -333    141       O  
ATOM   7800  C5   DT P 110      18.398  -4.895  35.068  1.00 53.50           C  
ANISOU 7800  C5   DT P 110     6431   7277   6621   -960   -346    263       C  
ATOM   7801  C7   DT P 110      17.840  -3.604  35.599  1.00 54.78           C  
ANISOU 7801  C7   DT P 110     6558   7385   6870   -917   -427    274       C  
ATOM   7802  C6   DT P 110      18.218  -5.233  33.776  1.00 53.29           C  
ANISOU 7802  C6   DT P 110     6411   7296   6542  -1069   -312    318       C  
ATOM   7803  P    DA P 111      15.842  -7.969  28.531  1.00 53.22           P  
ANISOU 7803  P    DA P 111     6425   7650   6147  -1563   -108    465       P  
ATOM   7804  OP1  DA P 111      15.984  -8.558  27.182  1.00 52.46           O  
ANISOU 7804  OP1  DA P 111     6306   7675   5950  -1709    -46    451       O  
ATOM   7805  OP2  DA P 111      14.740  -7.025  28.823  1.00 55.69           O  
ANISOU 7805  OP2  DA P 111     6739   7922   6500  -1533   -194    564       O  
ATOM   7806  O5'  DA P 111      15.744  -9.129  29.631  1.00 50.48           O  
ANISOU 7806  O5'  DA P 111     6112   7246   5823  -1442    -55    370       O  
ATOM   7807  C5'  DA P 111      16.719 -10.164  29.631  1.00 50.77           C  
ANISOU 7807  C5'  DA P 111     6139   7288   5862  -1441     25    268       C  
ATOM   7808  C4'  DA P 111      16.638 -10.974  30.908  1.00 49.72           C  
ANISOU 7808  C4'  DA P 111     6026   7082   5781  -1310     44    218       C  
ATOM   7809  O4'  DA P 111      16.911 -10.115  32.034  1.00 48.04           O  
ANISOU 7809  O4'  DA P 111     5821   6804   5628  -1207    -25    239       O  
ATOM   7810  C3'  DA P 111      15.268 -11.593  31.177  1.00 46.66           C  
ANISOU 7810  C3'  DA P 111     5665   6696   5368  -1278     52    241       C  
ATOM   7811  O3'  DA P 111      15.363 -12.996  30.952  1.00 44.06           O  
ANISOU 7811  O3'  DA P 111     5324   6378   5040  -1295    137    169       O  
ATOM   7812  C2'  DA P 111      14.949 -11.233  32.631  1.00 46.25           C  
ANISOU 7812  C2'  DA P 111     5632   6578   5363  -1144     -2    262       C  
ATOM   7813  C1'  DA P 111      16.284 -10.699  33.147  1.00 46.43           C  
ANISOU 7813  C1'  DA P 111     5637   6566   5440  -1103    -24    230       C  
ATOM   7814  N9   DA P 111      16.191  -9.681  34.189  1.00 46.93           N  
ANISOU 7814  N9   DA P 111     5702   6587   5540  -1016   -100    251       N  
ATOM   7815  C8   DA P 111      15.645  -8.425  34.096  1.00 45.94           C  
ANISOU 7815  C8   DA P 111     5572   6450   5432  -1025   -170    303       C  
ATOM   7816  N7   DA P 111      15.721  -7.731  35.216  1.00 46.66           N  
ANISOU 7816  N7   DA P 111     5655   6502   5573   -934   -222    284       N  
ATOM   7817  C5   DA P 111      16.363  -8.586  36.099  1.00 44.04           C  
ANISOU 7817  C5   DA P 111     5326   6170   5238   -864   -188    230       C  
ATOM   7818  C6   DA P 111      16.744  -8.459  37.450  1.00 44.27           C  
ANISOU 7818  C6   DA P 111     5343   6188   5290   -764   -215    190       C  
ATOM   7819  N6   DA P 111      16.518  -7.366  38.178  1.00 44.94           N  
ANISOU 7819  N6   DA P 111     5410   6257   5409   -712   -278    174       N  
ATOM   7820  N1   DA P 111      17.367  -9.506  38.041  1.00 46.24           N  
ANISOU 7820  N1   DA P 111     5590   6448   5532   -722   -176    164       N  
ATOM   7821  C2   DA P 111      17.589 -10.616  37.319  1.00 46.43           C  
ANISOU 7821  C2   DA P 111     5618   6475   5549   -772   -109    166       C  
ATOM   7822  N3   DA P 111      17.279 -10.852  36.041  1.00 43.84           N  
ANISOU 7822  N3   DA P 111     5299   6159   5199   -866    -71    179       N  
ATOM   7823  C4   DA P 111      16.659  -9.793  35.485  1.00 45.34           C  
ANISOU 7823  C4   DA P 111     5497   6356   5374   -910   -115    216       C  
ATOM   7824  P    DA P 112      14.064 -13.932  30.975  1.00 45.88           P  
ANISOU 7824  P    DA P 112     5569   6617   5249  -1285    169    177       P  
ATOM   7825  OP1  DA P 112      14.355 -15.108  30.141  1.00 46.82           O  
ANISOU 7825  OP1  DA P 112     5652   6768   5368  -1362    259     90       O  
ATOM   7826  OP2  DA P 112      12.838 -13.134  30.743  1.00 45.64           O  
ANISOU 7826  OP2  DA P 112     5564   6613   5165  -1307    110    263       O  
ATOM   7827  O5'  DA P 112      13.974 -14.360  32.513  1.00 43.30           O  
ANISOU 7827  O5'  DA P 112     5252   6214   4986  -1142    153    184       O  
ATOM   7828  C5'  DA P 112      15.063 -14.940  33.189  1.00 43.63           C  
ANISOU 7828  C5'  DA P 112     5268   6210   5099  -1084    179    136       C  
ATOM   7829  C4'  DA P 112      14.788 -14.878  34.677  1.00 45.54           C  
ANISOU 7829  C4'  DA P 112     5522   6415   5367   -959    133    180       C  
ATOM   7830  O4'  DA P 112      14.967 -13.524  35.149  1.00 45.52           O  
ANISOU 7830  O4'  DA P 112     5536   6413   5347   -925     58    208       O  
ATOM   7831  C3'  DA P 112      13.362 -15.237  35.083  1.00 44.16           C  
ANISOU 7831  C3'  DA P 112     5367   6247   5163   -922    126    229       C  
ATOM   7832  O3'  DA P 112      13.351 -16.601  35.472  1.00 42.97           O  
ANISOU 7832  O3'  DA P 112     5188   6069   5068   -889    177    218       O  
ATOM   7833  C2'  DA P 112      13.070 -14.321  36.267  1.00 45.14           C  
ANISOU 7833  C2'  DA P 112     5509   6370   5271   -832     54    271       C  
ATOM   7834  C1'  DA P 112      14.312 -13.443  36.388  1.00 43.28           C  
ANISOU 7834  C1'  DA P 112     5262   6123   5058   -828     20    242       C  
ATOM   7835  N9   DA P 112      13.971 -12.058  36.709  1.00 44.37           N  
ANISOU 7835  N9   DA P 112     5413   6266   5180   -805    -51    263       N  
ATOM   7836  C8   DA P 112      13.309 -11.143  35.935  1.00 44.36           C  
ANISOU 7836  C8   DA P 112     5423   6271   5161   -863    -83    294       C  
ATOM   7837  N7   DA P 112      13.141  -9.976  36.523  1.00 45.35           N  
ANISOU 7837  N7   DA P 112     5542   6381   5308   -820   -149    300       N  
ATOM   7838  C5   DA P 112      13.729 -10.144  37.771  1.00 45.15           C  
ANISOU 7838  C5   DA P 112     5504   6353   5296   -731   -157    263       C  
ATOM   7839  C6   DA P 112      13.894  -9.293  38.894  1.00 42.38           C  
ANISOU 7839  C6   DA P 112     5134   6001   4966   -655   -211    232       C  
ATOM   7840  N6   DA P 112      13.458  -8.038  38.942  1.00 39.65           N  
ANISOU 7840  N6   DA P 112     4773   5635   4656   -651   -267    226       N  
ATOM   7841  N1   DA P 112      14.526  -9.783  39.980  1.00 38.97           N  
ANISOU 7841  N1   DA P 112     4687   5593   4526   -587   -206    203       N  
ATOM   7842  C2   DA P 112      14.970 -11.044  39.965  1.00 40.99           C  
ANISOU 7842  C2   DA P 112     4944   5856   4775   -588   -155    217       C  
ATOM   7843  N3   DA P 112      14.869 -11.938  38.979  1.00 43.81           N  
ANISOU 7843  N3   DA P 112     5313   6198   5135   -650    -99    237       N  
ATOM   7844  C4   DA P 112      14.239 -11.424  37.902  1.00 43.35           C  
ANISOU 7844  C4   DA P 112     5274   6133   5065   -721   -101    252       C  
ATOM   7845  P    DT P 113      12.111 -17.328  36.176  1.00 39.87           P  
ANISOU 7845  P    DT P 113     4801   5675   4674   -832    180    273       P  
ATOM   7846  OP1  DT P 113      12.072 -18.658  35.545  1.00 44.89           O  
ANISOU 7846  OP1  DT P 113     5400   6285   5372   -876    254    235       O  
ATOM   7847  OP2  DT P 113      10.898 -16.489  36.198  1.00 39.95           O  
ANISOU 7847  OP2  DT P 113     4852   5717   4609   -828    136    318       O  
ATOM   7848  O5'  DT P 113      12.661 -17.526  37.654  1.00 40.80           O  
ANISOU 7848  O5'  DT P 113     4896   5778   4830   -728    150    308       O  
ATOM   7849  C5'  DT P 113      11.856 -17.383  38.812  1.00 41.29           C  
ANISOU 7849  C5'  DT P 113     4966   5869   4853   -650    110    370       C  
ATOM   7850  C4'  DT P 113      12.774 -16.879  39.903  1.00 37.31           C  
ANISOU 7850  C4'  DT P 113     4445   5382   4348   -585     64    376       C  
ATOM   7851  O4'  DT P 113      13.150 -15.530  39.570  1.00 42.21           O  
ANISOU 7851  O4'  DT P 113     5092   6011   4934   -607     24    334       O  
ATOM   7852  C3'  DT P 113      12.171 -16.797  41.284  1.00 40.36           C  
ANISOU 7852  C3'  DT P 113     4823   5825   4687   -506     25    431       C  
ATOM   7853  O3'  DT P 113      12.587 -17.933  41.990  1.00 37.59           O  
ANISOU 7853  O3'  DT P 113     4422   5470   4391   -470     40    483       O  
ATOM   7854  C2'  DT P 113      12.801 -15.558  41.913  1.00 40.81           C  
ANISOU 7854  C2'  DT P 113     4883   5916   4705   -473    -33    395       C  
ATOM   7855  C1'  DT P 113      13.200 -14.709  40.719  1.00 39.49           C  
ANISOU 7855  C1'  DT P 113     4745   5708   4553   -539    -33    339       C  
ATOM   7856  N1   DT P 113      12.369 -13.457  40.504  1.00 44.24           N  
ANISOU 7856  N1   DT P 113     5375   6322   5113   -549    -73    324       N  
ATOM   7857  C2   DT P 113      12.458 -12.451  41.446  1.00 41.09           C  
ANISOU 7857  C2   DT P 113     4964   5954   4694   -496   -128    297       C  
ATOM   7858  O2   DT P 113      13.156 -12.530  42.437  1.00 42.27           O  
ANISOU 7858  O2   DT P 113     5086   6138   4836   -445   -146    287       O  
ATOM   7859  N3   DT P 113      11.699 -11.339  41.183  1.00 41.49           N  
ANISOU 7859  N3   DT P 113     5027   5998   4741   -508   -163    281       N  
ATOM   7860  C4   DT P 113      10.873 -11.124  40.091  1.00 43.13           C  
ANISOU 7860  C4   DT P 113     5258   6174   4954   -570   -156    306       C  
ATOM   7861  O4   DT P 113      10.241 -10.079  39.973  1.00 44.10           O  
ANISOU 7861  O4   DT P 113     5378   6284   5094   -576   -196    300       O  
ATOM   7862  C5   DT P 113      10.810 -12.209  39.128  1.00 41.50           C  
ANISOU 7862  C5   DT P 113     5068   5954   4744   -630    -99    337       C  
ATOM   7863  C7   DT P 113       9.944 -12.092  37.902  1.00 37.61           C  
ANISOU 7863  C7   DT P 113     4597   5451   4242   -710    -89    366       C  
ATOM   7864  C6   DT P 113      11.553 -13.307  39.379  1.00 42.24           C  
ANISOU 7864  C6   DT P 113     5148   6048   4851   -616    -58    335       C  
ATOM   7865  P    DT P 114      11.570 -18.625  42.992  1.00 38.42           P  
ANISOU 7865  P    DT P 114     4504   5626   4466   -420     35    571       P  
ATOM   7866  OP1  DT P 114      12.189 -19.908  43.384  1.00 35.98           O  
ANISOU 7866  OP1  DT P 114     4130   5287   4255   -404     55    634       O  
ATOM   7867  OP2  DT P 114      10.195 -18.610  42.441  1.00 37.35           O  
ANISOU 7867  OP2  DT P 114     4406   5491   4296   -443     56    574       O  
ATOM   7868  O5'  DT P 114      11.537 -17.581  44.193  1.00 37.53           O  
ANISOU 7868  O5'  DT P 114     4394   5611   4255   -365    -26    569       O  
ATOM   7869  C5'  DT P 114      12.695 -17.317  44.958  1.00 40.08           C  
ANISOU 7869  C5'  DT P 114     4684   5967   4577   -335    -62    564       C  
ATOM   7870  C4'  DT P 114      12.276 -16.428  46.100  1.00 39.07           C  
ANISOU 7870  C4'  DT P 114     4552   5952   4343   -289   -110    552       C  
ATOM   7871  O4'  DT P 114      11.939 -15.119  45.575  1.00 39.62           O  
ANISOU 7871  O4'  DT P 114     4666   6004   4385   -305   -127    461       O  
ATOM   7872  C3'  DT P 114      11.045 -16.961  46.807  1.00 36.17           C  
ANISOU 7872  C3'  DT P 114     4169   5659   3917   -264   -103    623       C  
ATOM   7873  O3'  DT P 114      11.357 -17.025  48.183  1.00 37.53           O  
ANISOU 7873  O3'  DT P 114     4287   5951   4021   -224   -140    666       O  
ATOM   7874  C2'  DT P 114       9.942 -15.960  46.457  1.00 34.55           C  
ANISOU 7874  C2'  DT P 114     4009   5458   3660   -271   -106    556       C  
ATOM   7875  C1'  DT P 114      10.701 -14.693  46.103  1.00 35.62           C  
ANISOU 7875  C1'  DT P 114     4163   5563   3806   -282   -137    457       C  
ATOM   7876  N1   DT P 114      10.025 -13.879  45.052  1.00 34.05           N  
ANISOU 7876  N1   DT P 114     4010   5297   3630   -319   -134    406       N  
ATOM   7877  C2   DT P 114       9.755 -12.538  45.268  1.00 34.80           C  
ANISOU 7877  C2   DT P 114     4105   5409   3709   -307   -172    330       C  
ATOM   7878  O2   DT P 114      10.041 -11.961  46.301  1.00 38.62           O  
ANISOU 7878  O2   DT P 114     4555   5967   4154   -267   -205    282       O  
ATOM   7879  N3   DT P 114       9.137 -11.891  44.218  1.00 32.96           N  
ANISOU 7879  N3   DT P 114     3904   5104   3516   -349   -174    311       N  
ATOM   7880  C4   DT P 114       8.771 -12.455  42.999  1.00 34.11           C  
ANISOU 7880  C4   DT P 114     4084   5185   3692   -406   -139    356       C  
ATOM   7881  O4   DT P 114       8.212 -11.805  42.115  1.00 35.18           O  
ANISOU 7881  O4   DT P 114     4239   5273   3853   -449   -150    349       O  
ATOM   7882  C5   DT P 114       9.091 -13.862  42.840  1.00 31.09           C  
ANISOU 7882  C5   DT P 114     3701   4796   3318   -416    -93    411       C  
ATOM   7883  C7   DT P 114       8.754 -14.610  41.587  1.00 32.40           C  
ANISOU 7883  C7   DT P 114     3891   4903   3516   -480    -47    439       C  
ATOM   7884  C6   DT P 114       9.697 -14.488  43.853  1.00 32.29           C  
ANISOU 7884  C6   DT P 114     3819   4997   3455   -371    -93    435       C  
HETATM 7885  P   2DA P 115      10.319 -17.535  49.296  1.00 41.14           P  
ANISOU 7885  P   2DA P 115     4705   6537   4390   -196   -144    752       P  
HETATM 7886  OP1 2DA P 115      11.076 -17.649  50.591  1.00 38.43           O  
ANISOU 7886  OP1 2DA P 115     4294   6323   3984   -171   -187    802       O  
HETATM 7887  OP2 2DA P 115       9.572 -18.754  48.816  1.00 43.15           O  
ANISOU 7887  OP2 2DA P 115     4956   6727   4711   -210   -101    847       O  
HETATM 7888  O5' 2DA P 115       9.235 -16.345  49.345  1.00 41.87           O  
ANISOU 7888  O5' 2DA P 115     4833   6675   4399   -188   -149    652       O  
HETATM 7889  C5' 2DA P 115       9.199 -15.430  50.424  1.00 44.44           C  
ANISOU 7889  C5' 2DA P 115     5127   7135   4621   -162   -184    585       C  
HETATM 7890  C4' 2DA P 115       8.385 -14.182  50.093  1.00 43.33           C  
ANISOU 7890  C4' 2DA P 115     5019   6974   4469   -161   -187    463       C  
HETATM 7891  O4' 2DA P 115       8.511 -13.729  48.744  1.00 42.14           O  
ANISOU 7891  O4' 2DA P 115     4924   6671   4415   -192   -178    418       O  
HETATM 7892  C3' 2DA P 115       6.895 -14.410  50.266  1.00 43.10           C  
ANISOU 7892  C3' 2DA P 115     4991   6987   4396   -156   -160    490       C  
HETATM 7893  C2' 2DA P 115       6.307 -13.280  49.440  1.00 42.00           C  
ANISOU 7893  C2' 2DA P 115     4891   6756   4310   -168   -163    386       C  
HETATM 7894  C1' 2DA P 115       7.444 -12.806  48.550  1.00 38.97           C  
ANISOU 7894  C1' 2DA P 115     4537   6259   4010   -191   -180    346       C  
HETATM 7895  N9  2DA P 115       6.943 -12.795  47.163  1.00 37.05           N  
ANISOU 7895  N9  2DA P 115     4348   5885   3845   -232   -160    361       N  
HETATM 7896  C8  2DA P 115       6.838 -13.838  46.329  1.00 38.22           C  
ANISOU 7896  C8  2DA P 115     4525   5965   4031   -263   -124    441       C  
HETATM 7897  N7  2DA P 115       6.311 -13.404  45.154  1.00 40.70           N  
ANISOU 7897  N7  2DA P 115     4879   6189   4397   -305   -118    424       N  
HETATM 7898  C5  2DA P 115       6.084 -12.074  45.262  1.00 40.07           C  
ANISOU 7898  C5  2DA P 115     4791   6107   4327   -298   -155    345       C  
HETATM 7899  C6  2DA P 115       5.571 -11.094  44.408  1.00 40.54           C  
ANISOU 7899  C6  2DA P 115     4865   6092   4445   -330   -176    311       C  
HETATM 7900  N6  2DA P 115       5.151 -11.377  43.149  1.00 35.40           N  
ANISOU 7900  N6  2DA P 115     4252   5368   3830   -388   -160    362       N  
HETATM 7901  N1  2DA P 115       5.481  -9.824  44.855  1.00 39.69           N  
ANISOU 7901  N1  2DA P 115     4725   5990   4366   -308   -217    227       N  
HETATM 7902  C2  2DA P 115       5.873  -9.496  46.095  1.00 37.34           C  
ANISOU 7902  C2  2DA P 115     4383   5780   4026   -258   -232    158       C  
HETATM 7903  N3  2DA P 115       6.369 -10.411  46.934  1.00 35.92           N  
ANISOU 7903  N3  2DA P 115     4191   5692   3766   -232   -214    192       N  
HETATM 7904  C4  2DA P 115       6.484 -11.704  46.540  1.00 39.43           C  
ANISOU 7904  C4  2DA P 115     4665   6122   4194   -249   -178    294       C  
TER    7905      2DA P 115                                                      
HETATM 7906  PA  TTP A 896       2.899 -15.825  50.409  1.00 57.46           P  
ANISOU 7906  PA  TTP A 896     6813   8873   6145   -150    -72    643       P  
HETATM 7907  O1A TTP A 896       3.570 -16.488  49.239  1.00 54.08           O  
ANISOU 7907  O1A TTP A 896     6428   8296   5824   -179    -59    694       O  
HETATM 7908  O2A TTP A 896       3.266 -16.471  51.724  1.00 58.53           O  
ANISOU 7908  O2A TTP A 896     6882   9172   6186   -133    -82    721       O  
HETATM 7909  O3A TTP A 896       1.318 -15.909  50.156  1.00 56.04           O  
ANISOU 7909  O3A TTP A 896     6648   8679   5964   -152    -42    655       O  
HETATM 7910  PB  TTP A 896       0.208 -15.496  51.232  1.00 53.65           P  
ANISOU 7910  PB  TTP A 896     6298   8524   5564   -129    -35    615       P  
HETATM 7911  O1B TTP A 896      -0.464 -14.234  50.760  1.00 54.61           O  
ANISOU 7911  O1B TTP A 896     6437   8580   5732   -130    -42    485       O  
HETATM 7912  O2B TTP A 896       0.740 -15.303  52.637  1.00 51.08           O  
ANISOU 7912  O2B TTP A 896     5902   8386   5119   -111    -53    589       O  
HETATM 7913  O3B TTP A 896      -0.839 -16.707  51.133  1.00 49.03           O  
ANISOU 7913  O3B TTP A 896     5713   7936   4982   -134      2    747       O  
HETATM 7914  PG  TTP A 896      -0.629 -18.131  51.854  1.00 53.28           P  
ANISOU 7914  PG  TTP A 896     6202   8561   5480   -132     12    911       P  
HETATM 7915  O1G TTP A 896       0.674 -18.198  52.612  1.00 52.91           O  
ANISOU 7915  O1G TTP A 896     6113   8604   5386   -126    -20    931       O  
HETATM 7916  O2G TTP A 896      -1.804 -18.291  52.784  1.00 48.81           O  
ANISOU 7916  O2G TTP A 896     5587   8139   4818   -121     31    943       O  
HETATM 7917  O3G TTP A 896      -0.661 -19.290  50.873  1.00 50.94           O  
ANISOU 7917  O3G TTP A 896     5935   8121   5300   -151     35   1018       O  
HETATM 7918  O5' TTP A 896       3.249 -14.260  50.396  1.00 57.44           O  
ANISOU 7918  O5' TTP A 896     6815   8863   6146   -145   -103    484       O  
HETATM 7919  C5' TTP A 896       3.214 -13.499  51.594  1.00 55.08           C  
ANISOU 7919  C5' TTP A 896     6459   8713   5757   -120   -122    394       C  
HETATM 7920  C4' TTP A 896       2.877 -12.055  51.251  1.00 52.94           C  
ANISOU 7920  C4' TTP A 896     6190   8380   5543   -118   -138    243       C  
HETATM 7921  O4' TTP A 896       3.728 -11.546  50.212  1.00 50.47           O  
ANISOU 7921  O4' TTP A 896     5921   7922   5334   -138   -161    215       O  
HETATM 7922  C3' TTP A 896       1.476 -11.909  50.688  1.00 51.89           C  
ANISOU 7922  C3' TTP A 896     6079   8182   5457   -125   -116    242       C  
HETATM 7923  O3' TTP A 896       0.486 -11.911  51.717  1.00 53.17           O  
ANISOU 7923  O3' TTP A 896     6187   8483   5532   -105    -96    213       O  
HETATM 7924  C2' TTP A 896       1.591 -10.591  49.940  1.00 49.38           C  
ANISOU 7924  C2' TTP A 896     5771   7741   5251   -135   -146    132       C  
HETATM 7925  C1' TTP A 896       3.004 -10.643  49.362  1.00 47.96           C  
ANISOU 7925  C1' TTP A 896     5622   7489   5110   -152   -168    154       C  
HETATM 7926  N1  TTP A 896       2.830 -11.141  47.982  1.00 47.24           N  
ANISOU 7926  N1  TTP A 896     5596   7261   5093   -192   -155    242       N  
HETATM 7927  C2  TTP A 896       2.456 -10.213  46.976  1.00 46.41           C  
ANISOU 7927  C2  TTP A 896     5508   7036   5088   -220   -176    205       C  
HETATM 7928  O2  TTP A 896       2.321  -9.001  47.260  1.00 46.88           O  
ANISOU 7928  O2  TTP A 896     5526   7086   5198   -207   -206    101       O  
HETATM 7929  N3  TTP A 896       2.241 -10.597  45.716  1.00 46.75           N  
ANISOU 7929  N3  TTP A 896     5601   6979   5182   -267   -166    280       N  
HETATM 7930  C4  TTP A 896       2.360 -11.874  45.342  1.00 47.75           C  
ANISOU 7930  C4  TTP A 896     5762   7103   5278   -285   -130    373       C  
HETATM 7931  O4  TTP A 896       2.153 -12.200  44.147  1.00 48.61           O  
ANISOU 7931  O4  TTP A 896     5910   7130   5429   -336   -119    423       O  
HETATM 7932  C5  TTP A 896       2.744 -12.884  46.363  1.00 48.68           C  
ANISOU 7932  C5  TTP A 896     5857   7319   5318   -250   -108    415       C  
HETATM 7933  C5M TTP A 896       2.904 -14.340  45.994  1.00 44.73           C  
ANISOU 7933  C5M TTP A 896     5376   6800   4819   -268    -70    519       C  
HETATM 7934  C6  TTP A 896       2.962 -12.447  47.671  1.00 48.62           C  
ANISOU 7934  C6  TTP A 896     5800   7427   5246   -206   -125    356       C  
HETATM 7935 CA    CA A 897       1.991 -16.791  53.741  1.00 38.90          CA  
HETATM 7936 CA    CA A 898       5.766 -17.514  52.649  1.00 72.26          CA  
HETATM 7937 CA    CA A 899      -0.292 -52.951  49.399  1.00 78.90          CA  
HETATM 7938 CA    CA A 900      -0.250 -22.538  56.207  1.00104.52          CA  
HETATM 7939 CA    CA A 901      -0.254 -25.170  12.922  1.00 73.00          CA  
HETATM 7940  O   HOH A 902      -5.140  -0.468  23.482  1.00 44.80           O  
HETATM 7941  O   HOH A 903     -25.416  19.461  43.795  1.00 33.14           O  
HETATM 7942  O   HOH A 904     -10.960 -23.164  37.759  1.00 21.84           O  
HETATM 7943  O   HOH A 905     -20.660 -25.277  26.653  1.00 27.64           O  
HETATM 7944  O   HOH A 906       2.860 -23.255  18.621  1.00 26.11           O  
HETATM 7945  O   HOH A 907      22.051  -8.501  13.004  1.00 42.31           O  
HETATM 7946  O   HOH A 908       5.637 -31.341  72.082  1.00 26.32           O  
HETATM 7947  O   HOH A 909       1.031 -16.894  36.081  1.00 31.99           O  
HETATM 7948  O   HOH A 910      -3.631 -18.595  16.047  1.00 31.45           O  
HETATM 7949  O   HOH A 911      13.861 -23.827   9.847  1.00 27.83           O  
HETATM 7950  O   HOH A 912      -0.450 -13.585  44.728  1.00 29.96           O  
HETATM 7951  O   HOH A 913      -0.681 -16.126  44.212  1.00 21.34           O  
HETATM 7952  O   HOH A 914     -17.260   8.153  47.090  1.00 42.01           O  
HETATM 7953  O   HOH A 915      -8.186   9.967  45.288  1.00 45.77           O  
HETATM 7954  O  AHOH A 916      -7.742 -24.723  20.318  0.50 18.02           O  
HETATM 7955  O  BHOH A 916      -6.052 -23.992  19.114  0.50 15.42           O  
HETATM 7956  O   HOH A 917     -11.102 -42.806  41.181  1.00 30.50           O  
HETATM 7957  O   HOH A 918     -21.861 -23.848  35.421  1.00 32.56           O  
HETATM 7958  O   HOH A 919      29.417 -18.167  56.872  1.00 23.16           O  
HETATM 7959  O   HOH A 920     -27.751   5.467  26.358  1.00 26.12           O  
HETATM 7960  O   HOH A 921      18.060 -25.682  27.446  1.00 27.90           O  
HETATM 7961  O   HOH A 922     -15.337  -5.385  31.844  1.00 38.70           O  
HETATM 7962  O   HOH A 923      15.238  -4.791  15.188  1.00 43.94           O  
HETATM 7963  O   HOH A 924       7.147 -30.403   4.979  1.00 41.03           O  
HETATM 7964  O   HOH A 925       3.938 -26.204  18.136  1.00 37.57           O  
HETATM 7965  O   HOH A 926     -14.173 -40.786  19.021  1.00 36.48           O  
HETATM 7966  O   HOH A 927     -14.800 -44.426  17.810  1.00 42.30           O  
HETATM 7967  O   HOH A 928      26.546 -25.807   7.298  1.00 49.21           O  
HETATM 7968  O   HOH A 929       8.219 -37.603  54.931  1.00 26.85           O  
HETATM 7969  O   HOH A 930      -7.754 -30.889  36.427  1.00 30.94           O  
HETATM 7970  O   HOH A 931     -13.232  -3.385   2.334  1.00 36.39           O  
HETATM 7971  O   HOH A 932     -22.811  -8.266  23.440  1.00 32.83           O  
HETATM 7972  O   HOH A 933      34.269 -26.802  22.855  1.00 23.08           O  
HETATM 7973  O   HOH A 934      27.512 -17.922  35.400  1.00 34.14           O  
HETATM 7974  O   HOH A 935     -23.264   5.432  35.299  1.00 38.66           O  
HETATM 7975  O  AHOH A 936      -3.418 -21.839  63.505  0.50  9.68           O  
HETATM 7976  O  BHOH A 936      -1.895 -22.796  64.542  0.50 14.96           O  
HETATM 7977  O   HOH A 937      -2.387 -35.494  44.678  1.00 27.97           O  
HETATM 7978  O   HOH A 938      23.096 -17.248  67.493  1.00 27.87           O  
HETATM 7979  O   HOH A 939      18.218 -37.060  60.113  1.00 37.48           O  
HETATM 7980  O   HOH A 940      -6.082 -19.920  52.993  1.00 30.57           O  
HETATM 7981  O   HOH A 941      18.519 -11.352   8.377  1.00 42.52           O  
HETATM 7982  O   HOH A 942      -3.045 -13.961  50.020  1.00 32.26           O  
HETATM 7983  O   HOH A 943      -1.488 -22.876  13.384  1.00 54.54           O  
HETATM 7984  O   HOH A 944      -5.793   7.985  69.608  1.00 15.59           O  
HETATM 7985  O   HOH A 945     -12.099 -25.093  32.422  1.00 37.86           O  
HETATM 7986  O   HOH A 946     -25.972   4.311  35.910  1.00 30.98           O  
HETATM 7987  O   HOH A 947      23.868 -13.552  53.056  1.00 28.65           O  
HETATM 7988  O   HOH A 948      -5.690 -21.265  -7.730  1.00 49.63           O  
HETATM 7989  O   HOH A 949      26.411 -41.770  23.681  1.00 34.01           O  
HETATM 7990  O   HOH A 950      -2.382 -35.044  21.378  1.00 33.63           O  
HETATM 7991  O   HOH A 951      13.106 -15.939  50.347  1.00 30.54           O  
HETATM 7992  O   HOH A 952      -2.052   1.201  69.228  1.00 27.88           O  
HETATM 7993  O   HOH A 953     -21.100 -16.274   3.272  1.00 42.24           O  
HETATM 7994  O   HOH A 954       8.501 -34.764  21.855  1.00 44.08           O  
HETATM 7995  O   HOH A 955     -15.881  18.491  44.066  1.00 34.88           O  
HETATM 7996  O   HOH A 956       6.214 -37.235  28.805  1.00 48.01           O  
HETATM 7997  O   HOH A 957      24.524 -18.422  40.501  1.00 42.62           O  
HETATM 7998  O   HOH A 958       2.307 -44.676  17.567  1.00 32.55           O  
HETATM 7999  O   HOH A 959      -8.465 -46.688  11.448  1.00 28.12           O  
HETATM 8000  O   HOH A 960     -19.770   1.107  28.844  1.00 38.08           O  
HETATM 8001  O   HOH A 961       7.134 -43.878  53.603  1.00 37.00           O  
HETATM 8002  O   HOH A 962      -0.174 -33.916   0.315  1.00 16.41           O  
HETATM 8003  O   HOH A 963     -20.896 -28.000  26.385  1.00 46.31           O  
HETATM 8004  O   HOH A 964     -11.226 -19.221  -4.029  1.00 26.56           O  
HETATM 8005  O   HOH A 965       6.040   1.509  75.854  1.00 24.51           O  
HETATM 8006  O   HOH A 966     -12.866 -10.294  58.876  1.00 30.18           O  
HETATM 8007  O   HOH A 967       3.351 -28.764  62.822  1.00 18.02           O  
HETATM 8008  O   HOH A 968     -18.300 -11.395  28.286  1.00 38.73           O  
HETATM 8009  O   HOH A 969       2.579   3.497  75.897  1.00 42.54           O  
HETATM 8010  O   HOH A 970     -18.504  -8.724  27.440  1.00 27.34           O  
HETATM 8011  O   HOH A 971     -15.572 -30.913  -2.031  1.00 39.63           O  
HETATM 8012  O   HOH A 972      18.456 -14.277  70.333  1.00 42.24           O  
HETATM 8013  O   HOH A 973      19.600 -24.447  67.015  1.00 33.66           O  
HETATM 8014  O   HOH A 974      -7.857 -19.258  58.137  1.00 25.50           O  
HETATM 8015  O   HOH A 975      -7.456   3.403  49.630  1.00 18.55           O  
HETATM 8016  O   HOH A 976       0.201 -12.741   4.826  1.00 32.45           O  
HETATM 8017  O   HOH A 977      -1.895 -13.823  22.056  1.00 39.85           O  
HETATM 8018  O   HOH A 978      -9.448  -5.011  70.433  1.00 29.30           O  
HETATM 8019  O   HOH A 979       5.440 -36.393   8.960  1.00 52.38           O  
HETATM 8020  O   HOH A 980      -1.845 -20.994   1.686  1.00 31.37           O  
HETATM 8021  O   HOH A 981       6.250 -38.587  47.861  1.00 26.35           O  
HETATM 8022  O   HOH A 982      14.003 -36.929  46.985  1.00 21.89           O  
HETATM 8023  O   HOH A 983       4.175   5.016  69.265  1.00 23.56           O  
HETATM 8024  O   HOH A 984     -15.217   1.144  42.273  1.00 34.15           O  
HETATM 8025  O   HOH A 985      10.289   4.631  71.002  1.00 23.35           O  
HETATM 8026  O   HOH A 986      -7.206 -13.026  55.210  1.00 37.14           O  
HETATM 8027  O   HOH A 987      -5.456   7.317  72.422  1.00 28.25           O  
HETATM 8028  O   HOH A 988      -7.259 -47.141  58.058  1.00 40.59           O  
HETATM 8029  O   HOH A 989      19.264  -8.537  58.414  1.00 23.78           O  
HETATM 8030  O   HOH A 990     -19.001 -26.760  29.026  1.00 44.54           O  
HETATM 8031  O   HOH A 991      -3.190   8.550  69.009  1.00 21.38           O  
HETATM 8032  O   HOH A 992      24.869 -20.587  60.196  1.00 27.26           O  
HETATM 8033  O   HOH A 993     -11.738  -5.526  59.305  1.00 30.32           O  
HETATM 8034  O   HOH A 994      -6.688 -12.754  25.080  1.00 38.72           O  
HETATM 8035  O   HOH A 995     -28.135 -15.866  37.669  1.00 46.51           O  
HETATM 8036  O   HOH A 996      -7.776 -29.926  53.802  1.00 40.30           O  
HETATM 8037  O   HOH A 997     -25.263 -25.637  18.582  1.00 27.73           O  
HETATM 8038  O   HOH A 998      -8.720 -40.538  58.390  1.00 36.74           O  
HETATM 8039  O   HOH A 999       5.186 -44.733  57.634  1.00 27.19           O  
HETATM 8040  O   HOH A1000      22.002 -12.715  28.556  1.00 29.36           O  
HETATM 8041  O   HOH A1001       1.479 -21.729  54.025  1.00 54.02           O  
HETATM 8042  O   HOH A1002     -31.921  -5.293  30.368  1.00 38.71           O  
HETATM 8043  O   HOH A1003     -16.130 -17.203  42.712  1.00 38.25           O  
HETATM 8044  O   HOH A1004     -15.816 -47.891  51.513  1.00 31.50           O  
HETATM 8045  O   HOH A1005      30.199 -13.933   9.839  1.00 27.53           O  
HETATM 8046  O   HOH A1006      -5.352   1.371  78.141  1.00 39.20           O  
HETATM 8047  O   HOH A1007      27.057 -44.855  43.192  1.00 29.93           O  
HETATM 8048  O   HOH A1008      26.133 -18.276  42.513  1.00 34.86           O  
HETATM 8049  O   HOH A1009       5.194   4.540  77.240  1.00 35.83           O  
HETATM 8050  O   HOH A1010      -2.828   8.529  36.696  1.00 37.29           O  
HETATM 8051  O   HOH A1011      -7.497 -19.958  61.326  1.00 32.27           O  
HETATM 8052  O   HOH A1012      21.162 -33.901  32.598  1.00 27.46           O  
HETATM 8053  O   HOH A1013      17.094 -32.892  29.425  1.00 19.41           O  
HETATM 8054  O   HOH A1014       2.135 -26.275   3.692  1.00 21.46           O  
HETATM 8055  O  AHOH A1015       7.834  -7.954  55.616  0.50  2.00           O  
HETATM 8056  O  BHOH A1015       5.833  -6.578  54.845  0.50  2.00           O  
HETATM 8057  O   HOH A1016     -10.596 -29.199  43.683  1.00 24.41           O  
HETATM 8058  O   HOH A1017     -23.579  20.828  37.014  1.00 46.87           O  
HETATM 8059  O   HOH A1018      17.187 -14.319  64.449  1.00 22.78           O  
HETATM 8060  O   HOH A1019      -2.313  -9.524  74.704  1.00 31.56           O  
HETATM 8061  O   HOH A1020     -17.059 -46.621  18.478  1.00 28.40           O  
HETATM 8062  O   HOH A1021     -13.934 -33.680  23.422  1.00 35.60           O  
HETATM 8063  O   HOH A1022     -14.842 -37.072  25.161  1.00 40.79           O  
HETATM 8064  O   HOH A1023      12.340 -33.441  44.694  1.00 16.91           O  
HETATM 8065  O   HOH A1024       6.547 -34.297  75.835  1.00 56.42           O  
HETATM 8066  O   HOH A1025      43.348 -27.509  49.269  1.00 45.50           O  
HETATM 8067  O   HOH A1026      -6.040   9.784  48.145  1.00 31.43           O  
HETATM 8068  O   HOH A1027       2.807 -20.172  52.071  1.00 38.15           O  
HETATM 8069  O   HOH A1028      -8.998 -32.912  35.290  1.00 26.26           O  
HETATM 8070  O   HOH A1029      -5.709 -37.787  53.217  1.00 28.84           O  
HETATM 8071  O   HOH A1030     -19.969  -8.097  45.337  1.00 45.07           O  
HETATM 8072  O   HOH A1031      -2.998 -24.998  38.103  1.00 20.77           O  
HETATM 8073  O   HOH A1032      -3.980 -15.950  -3.034  1.00 25.56           O  
HETATM 8074  O  AHOH A1033       2.576 -26.859   1.111  0.50  2.31           O  
HETATM 8075  O  BHOH A1033       0.353 -26.527  -0.374  0.50 14.79           O  
HETATM 8076  O   HOH A1034      16.703 -19.502  78.716  1.00 30.39           O  
HETATM 8077  O   HOH A1035      15.588 -21.845  80.083  1.00 31.64           O  
HETATM 8078  O   HOH A1036       7.809  -9.303  49.337  1.00 21.49           O  
HETATM 8079  O   HOH A1037      -2.307 -14.406  59.050  1.00 22.45           O  
HETATM 8080  O   HOH A1038       8.287   0.858   6.733  1.00 23.47           O  
HETATM 8081  O   HOH A1039       2.269 -27.483  13.100  1.00 46.74           O  
HETATM 8082  O   HOH A1040      -8.501 -32.352  -7.118  1.00 32.31           O  
HETATM 8083  O   HOH A1041      33.630 -30.080  28.308  1.00 39.54           O  
HETATM 8084  O   HOH A1042      35.807 -32.560  29.037  1.00 44.26           O  
HETATM 8085  O   HOH A1043     -18.570 -30.772  42.115  1.00 37.60           O  
HETATM 8086  O   HOH A1044      23.490 -15.339  69.526  1.00 21.28           O  
HETATM 8087  O   HOH A1045      21.835 -17.485  62.253  1.00 27.16           O  
HETATM 8088  O   HOH A1046      26.184 -22.607  64.249  1.00 42.21           O  
HETATM 8089  O   HOH A1047      24.486 -24.529  60.613  1.00 21.03           O  
HETATM 8090  O   HOH A1048      33.597 -29.202  56.380  1.00 42.11           O  
HETATM 8091  O   HOH A1049      47.212 -27.537  50.580  1.00 51.69           O  
HETATM 8092  O   HOH A1050      34.351 -30.240  53.771  1.00 34.75           O  
HETATM 8093  O   HOH A1051      -2.114  -7.871  36.423  1.00 33.28           O  
HETATM 8094  O   HOH A1052      -2.364 -59.612  37.580  1.00 34.30           O  
HETATM 8095  O   HOH T  19      22.053 -11.998  49.900  1.00 31.65           O  
HETATM 8096  O   HOH T  26       8.687   1.054  44.761  1.00 27.45           O  
HETATM 8097  O   HOH T  36      42.977   3.244  37.354  1.00 46.00           O  
HETATM 8098  O   HOH T  84      23.971 -18.413  37.002  1.00 44.40           O  
HETATM 8099  O   HOH T  86       0.389   0.964  28.666  1.00 38.44           O  
HETATM 8100  O   HOH T  88      -4.349   3.492  28.107  1.00 38.48           O  
HETATM 8101  O   HOH T  90      10.513  -8.921  48.852  1.00 23.82           O  
HETATM 8102  O   HOH T  92       8.136  -6.629  48.924  1.00 23.28           O  
HETATM 8103  O   HOH T  96      -0.219  -4.987  34.259  1.00 20.58           O  
HETATM 8104  O   HOH P  30      13.824  -7.544  31.345  1.00 31.18           O  
HETATM 8105  O   HOH P  55      11.111 -22.202  42.926  1.00 24.79           O  
CONECT  980 7939                                                                
CONECT  981 7939                                                                
CONECT 3417 7935                                                                
CONECT 3418 7935 7936                                                           
CONECT 3422 7935                                                                
CONECT 4166 7937                                                                
CONECT 4184 7937                                                                
CONECT 4384 7937                                                                
CONECT 5119 7935                                                                
CONECT 5120 7936                                                                
CONECT 7321 7332                                                                
CONECT 7332 7321 7333 7334 7335                                                 
CONECT 7333 7332                                                                
CONECT 7334 7332                                                                
CONECT 7335 7332 7336                                                           
CONECT 7336 7335 7337                                                           
CONECT 7337 7336 7338 7339                                                      
CONECT 7338 7337 7342                                                           
CONECT 7339 7337 7340 7341                                                      
CONECT 7340 7339 7353                                                           
CONECT 7341 7339 7342                                                           
CONECT 7342 7338 7341 7343                                                      
CONECT 7343 7342 7344 7352                                                      
CONECT 7344 7343 7345                                                           
CONECT 7345 7344 7346                                                           
CONECT 7346 7345 7347 7352                                                      
CONECT 7347 7346 7348                                                           
CONECT 7348 7347 7349                                                           
CONECT 7349 7348 7350 7351                                                      
CONECT 7350 7349                                                                
CONECT 7351 7349 7352                                                           
CONECT 7352 7343 7346 7351                                                      
CONECT 7353 7340                                                                
CONECT 7873 7885                                                                
CONECT 7885 7873 7886 7887 7888                                                 
CONECT 7886 7885                                                                
CONECT 7887 7885                                                                
CONECT 7888 7885 7889                                                           
CONECT 7889 7888 7890                                                           
CONECT 7890 7889 7891 7892                                                      
CONECT 7891 7890 7894                                                           
CONECT 7892 7890 7893                                                           
CONECT 7893 7892 7894                                                           
CONECT 7894 7891 7893 7895                                                      
CONECT 7895 7894 7896 7904                                                      
CONECT 7896 7895 7897                                                           
CONECT 7897 7896 7898                                                           
CONECT 7898 7897 7899 7904                                                      
CONECT 7899 7898 7900 7901                                                      
CONECT 7900 7899                                                                
CONECT 7901 7899 7902                                                           
CONECT 7902 7901 7903                                                           
CONECT 7903 7902 7904                                                           
CONECT 7904 7895 7898 7903                                                      
CONECT 7906 7907 7908 7909 7918                                                 
CONECT 7907 7906                                                                
CONECT 7908 7906 7935 7936                                                      
CONECT 7909 7906 7910                                                           
CONECT 7910 7909 7911 7912 7913                                                 
CONECT 7911 7910                                                                
CONECT 7912 7910 7935                                                           
CONECT 7913 7910 7914                                                           
CONECT 7914 7913 7915 7916 7917                                                 
CONECT 7915 7914 7935                                                           
CONECT 7916 7914                                                                
CONECT 7917 7914                                                                
CONECT 7918 7906 7919                                                           
CONECT 7919 7918 7920                                                           
CONECT 7920 7919 7921 7922                                                      
CONECT 7921 7920 7925                                                           
CONECT 7922 7920 7923 7924                                                      
CONECT 7923 7922                                                                
CONECT 7924 7922 7925                                                           
CONECT 7925 7921 7924 7926                                                      
CONECT 7926 7925 7927 7934                                                      
CONECT 7927 7926 7928 7929                                                      
CONECT 7928 7927                                                                
CONECT 7929 7927 7930                                                           
CONECT 7930 7929 7931 7932                                                      
CONECT 7931 7930                                                                
CONECT 7932 7930 7933 7934                                                      
CONECT 7933 7932                                                                
CONECT 7934 7926 7932                                                           
CONECT 7935 3417 3418 3422 5119                                                 
CONECT 7935 7908 7912 7915                                                      
CONECT 7936 3418 5120 7908                                                      
CONECT 7937 4166 4184 4384                                                      
CONECT 7938 8041                                                                
CONECT 7939  980  981 7983                                                      
CONECT 7983 7939                                                                
CONECT 8041 7938                                                                
MASTER      523    0    8   36   36    0   10    6 8083    3   91   72          
END

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Related entries of code: 3sun

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
3sq2	RCSB PDB PDBbind	13aa, >3SQ2_3\|Chain... at 92%
3suq	RCSB PDB PDBbind	13aa, >3SUQ_3\|Chain... at 92%
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
3sq2	RCSB PDB PDBbind	dTTP Opposite 2AP (AT rich sequence) DNA

Entry Information

PDB ID	3sun
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	RB69 DNA Polymerase (Y567A) mutant
Ligand Name	dTTP Opposite 2AP (AT rich sequence) DNA
EC.Number	E.C.2.7.7.7
Resolution	2.42(Å)
Affinity (Kd/Ki/IC50)	Kd=9.2uM
Release Year	2011
Protein/NA Sequence	Check fasta file
Primary Reference	(2011) Biochemistry Vol. 50: pp. 10136-10149

Links to External Databases

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

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