CNRS Nantes University UFIP UFIP
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***  MEMBRANE PROTEIN 29-APR-19 6OR2  ***

elNémo ID: 19112212450173697

Job options:

ID        	=	 19112212450173697
JOBID     	=	 MEMBRANE PROTEIN 29-APR-19 6OR2
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    MEMBRANE PROTEIN                        29-APR-19   6OR2              
TITLE     MMPL3 IS A LIPID TRANSPORTER THAT BINDS TREHALOSE MONOMYCOLATE AND    
TITLE    2 PHOSPHATIDYLETHANOLAMINE                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MEMBRANE PROTEIN, MMPL FAMILY PROTEIN;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MMPL3;                                                      
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS (STRAIN ATCC 700084 /   
SOURCE   3 MC(2)155);                                                           
SOURCE   4 ORGANISM_TAXID: 246196;                                              
SOURCE   5 STRAIN: ATCC 700084 / MC(2)155;                                      
SOURCE   6 VARIANT: ATCC 700084 / MC(2)155;                                     
SOURCE   7 GENE: MSMEG_0250;                                                    
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSPORTER, MEMBRANE PROTEIN                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.-C.SU                                                               
REVDAT   3   12-JUN-19 6OR2    1       JRNL                                     
REVDAT   2   05-JUN-19 6OR2    1       JRNL                                     
REVDAT   1   29-MAY-19 6OR2    0                                                
SPRSDE     29-MAY-19 6OR2      6N3T                                             
JRNL        AUTH   C.C.SU,P.A.KLENOTIC,J.R.BOLLA,G.E.PURDY,C.V.ROBINSON,E.W.YU  
JRNL        TITL   MMPL3 IS A LIPID TRANSPORTER THAT BINDS TREHALOSE            
JRNL        TITL 2 MONOMYCOLATE AND PHOSPHATIDYLETHANOLAMINE.                   
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 116 11241 2019              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   31113875                                                     
JRNL        DOI    10.1073/PNAS.1901346116                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.59 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_3318: ???)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.59                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 99.25                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 90546                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.251                           
REMARK   3   R VALUE            (WORKING SET) : 0.249                           
REMARK   3   FREE R VALUE                     : 0.290                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.870                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3506                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 99.3249 -  7.5722    0.92     3441   136  0.2373 0.2945        
REMARK   3     2  7.5722 -  6.0105    0.92     3438   135  0.2481 0.2767        
REMARK   3     3  6.0105 -  5.2508    0.95     3551   141  0.2379 0.2767        
REMARK   3     4  5.2508 -  4.7707    0.93     3492   144  0.1905 0.2283        
REMARK   3     5  4.7707 -  4.4288    0.94     3524   140  0.1876 0.2419        
REMARK   3     6  4.4288 -  4.1676    0.96     3576   146  0.2001 0.2358        
REMARK   3     7  4.1676 -  3.9589    0.96     3635   147  0.2134 0.2464        
REMARK   3     8  3.9589 -  3.7866    0.96     3583   147  0.2153 0.2479        
REMARK   3     9  3.7866 -  3.6408    0.92     3435   135  0.2289 0.2377        
REMARK   3    10  3.6408 -  3.5152    0.95     3569   147  0.2511 0.3502        
REMARK   3    11  3.5152 -  3.4052    0.96     3630   149  0.2681 0.3169        
REMARK   3    12  3.4052 -  3.3079    0.96     3606   146  0.2740 0.3029        
REMARK   3    13  3.3079 -  3.2208    0.97     3607   150  0.2981 0.3579        
REMARK   3    14  3.2208 -  3.1422    0.97     3643   148  0.3139 0.3703        
REMARK   3    15  3.1422 -  3.0708    0.96     3610   145  0.3227 0.3382        
REMARK   3    16  3.0708 -  3.0054    0.93     3442   142  0.3369 0.3579        
REMARK   3    17  3.0054 -  2.9453    0.94     3590   148  0.3554 0.3727        
REMARK   3    18  2.9453 -  2.8897    0.96     3564   148  0.3560 0.3793        
REMARK   3    19  2.8897 -  2.8381    0.95     3602   141  0.3656 0.3644        
REMARK   3    20  2.8381 -  2.7900    0.95     3551   145  0.3831 0.4059        
REMARK   3    21  2.7900 -  2.7450    0.94     3548   137  0.3821 0.3437        
REMARK   3    22  2.7450 -  2.7028    0.89     3359   132  0.4019 0.4111        
REMARK   3    23  2.7028 -  2.6630    0.88     3282   131  0.4302 0.4660        
REMARK   3    24  2.6630 -  2.6255    0.79     2953   111  0.4515 0.4064        
REMARK   3    25  2.6255 -  2.5900    0.76     2809   115  0.4452 0.4669        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.510            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.890           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           5785                                  
REMARK   3   ANGLE     :  0.523           7857                                  
REMARK   3   CHIRALITY :  0.038            938                                  
REMARK   3   PLANARITY :  0.004            982                                  
REMARK   3   DIHEDRAL  : 14.564           3464                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 207 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): 134.2214  73.6620  55.2477              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9781 T22:   0.7198                                     
REMARK   3      T33:   0.6637 T12:   0.0105                                     
REMARK   3      T13:   0.0217 T23:   0.0572                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2754 L22:   2.9095                                     
REMARK   3      L33:   4.5330 L12:  -1.0402                                     
REMARK   3      L13:  -0.6572 L23:   1.8000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0302 S12:  -0.0008 S13:   0.0573                       
REMARK   3      S21:  -0.4234 S22:  -0.2859 S23:   0.1893                       
REMARK   3      S31:  -0.3718 S32:  -0.5750 S33:   0.3061                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 208 THROUGH 330 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 139.1129  53.4394  32.0505              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8491 T22:   0.4125                                     
REMARK   3      T33:   0.6567 T12:  -0.0487                                     
REMARK   3      T13:   0.0523 T23:   0.0328                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2657 L22:   1.8868                                     
REMARK   3      L33:   4.3782 L12:   0.5733                                     
REMARK   3      L13:   0.1042 L23:   0.7467                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0084 S12:   0.0327 S13:   0.0251                       
REMARK   3      S21:   0.3934 S22:  -0.0216 S23:   0.1568                       
REMARK   3      S31:   0.8100 S32:  -0.0046 S33:   0.1999                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 331 THROUGH 400 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 131.5956  55.2519  12.2247              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6891 T22:   1.1760                                     
REMARK   3      T33:   0.8933 T12:  -0.1845                                     
REMARK   3      T13:  -0.1775 T23:  -0.2584                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8540 L22:   3.1583                                     
REMARK   3      L33:   2.9180 L12:   2.4974                                     
REMARK   3      L13:  -2.6546 L23:  -1.2959                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5766 S12:   1.8924 S13:  -0.1998                       
REMARK   3      S21:  -1.6781 S22:   0.9354 S23:   0.6317                       
REMARK   3      S31:   0.3402 S32:  -1.4829 S33:  -0.1412                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 401 THROUGH 501 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 154.4924  84.8673  51.7131              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9724 T22:   0.6200                                     
REMARK   3      T33:   0.7601 T12:  -0.1284                                     
REMARK   3      T13:   0.0718 T23:   0.0117                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1746 L22:   1.5199                                     
REMARK   3      L33:   5.1589 L12:  -0.3479                                     
REMARK   3      L13:  -0.6254 L23:   0.5297                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3472 S12:  -0.3787 S13:   0.3631                       
REMARK   3      S21:   0.0032 S22:  -0.0201 S23:  -0.5003                       
REMARK   3      S31:  -1.4807 S32:   0.4836 S33:  -0.3053                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 502 THROUGH 582 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 160.4725  74.1595  51.3051              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5848 T22:   0.9054                                     
REMARK   3      T33:   0.6017 T12:  -0.0005                                     
REMARK   3      T13:  -0.0031 T23:   0.0405                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3909 L22:   4.2357                                     
REMARK   3      L33:   6.1524 L12:   1.1242                                     
REMARK   3      L13:   0.5217 L23:   3.1991                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1752 S12:  -0.3987 S13:   0.0361                       
REMARK   3      S21:  -0.2073 S22:   0.4625 S23:  -0.7000                       
REMARK   3      S31:  -1.0550 S32:   1.4035 S33:  -0.3056                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 583 THROUGH 757 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 147.2222  63.2642  21.3636              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6625 T22:   0.5186                                     
REMARK   3      T33:   0.5330 T12:  -0.0576                                     
REMARK   3      T13:  -0.1179 T23:   0.0221                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1226 L22:   1.9884                                     
REMARK   3      L33:   7.8949 L12:  -0.7247                                     
REMARK   3      L13:  -1.6245 L23:   1.5515                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0192 S12:   0.2289 S13:   0.0129                       
REMARK   3      S21:  -0.3943 S22:  -0.1152 S23:  -0.0086                       
REMARK   3      S31:  -0.7906 S32:  -0.0451 S33:   0.0787                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 758 THROUGH 761 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 136.5644  34.8616   8.3098              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.6235 T22:   1.5734                                     
REMARK   3      T33:   1.6751 T12:   0.8053                                     
REMARK   3      T13:   0.3055 T23:  -0.4339                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0306 L22:   0.1587                                     
REMARK   3      L33:   0.2801 L12:  -0.0697                                     
REMARK   3      L13:   0.0926 L23:  -0.2108                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1581 S12:   1.0372 S13:  -1.1767                       
REMARK   3      S21:   0.1803 S22:  -0.1987 S23:  -0.6933                       
REMARK   3      S31:   0.9437 S32:   0.7011 S33:  -0.0021                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6OR2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000241209.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-AUG-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
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-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51822                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.560                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 5.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.56                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.65                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.23700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 74.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG400, 0.05M MG(AC)2, 0.1M          
REMARK 280  NAAC(5.0), AND 3% GLYCEROL, PH 7.5, VAPOR DIFFUSION, TEMPERATURE    
REMARK 280  298.0K                                                              
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       40.40700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       77.29550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       64.72850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       77.29550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.40700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       64.72850            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU A   353                                                      
REMARK 465     LEU A   354                                                      
REMARK 465     LYS A   355                                                      
REMARK 465     ILE A   356                                                      
REMARK 465     PRO A   357                                                      
REMARK 465     PHE A   358                                                      
REMARK 465     LEU A   359                                                      
REMARK 465     ALA A   360                                                      
REMARK 465     ASN A   361                                                      
REMARK 465     TRP A   362                                                      
REMARK 465     GLN A   363                                                      
REMARK 465     PHE A   364                                                      
REMARK 465     SER A   365                                                      
REMARK 465     ARG A   366                                                      
REMARK 465     ARG A   367                                                      
REMARK 465     ILE A   368                                                      
REMARK 465     ILE A   369                                                      
REMARK 465     ASP A   370                                                      
REMARK 465     TRP A   371                                                      
REMARK 465     PHE A   372                                                      
REMARK 465     ALA A   373                                                      
REMARK 465     GLU A   374                                                      
REMARK 465     LYS A   375                                                      
REMARK 465     THR A   376                                                      
REMARK 465     GLN A   377                                                      
REMARK 465     LYS A   378                                                      
REMARK 465     THR A   379                                                      
REMARK 465     LYS A   380                                                      
REMARK 465     THR A   381                                                      
REMARK 465     ARG A   762                                                      
REMARK 465     PRO A   763                                                      
REMARK 465     THR A   764                                                      
REMARK 465     VAL A   765                                                      
REMARK 465     ARG A   766                                                      
REMARK 465     GLU A   767                                                      
REMARK 465     SER A   768                                                      
REMARK 465     GLU A   769                                                      
REMARK 465     THR A   770                                                      
REMARK 465     ASP A   771                                                      
REMARK 465     GLN A   772                                                      
REMARK 465     ARG A   773                                                      
REMARK 465     HIS A   774                                                      
REMARK 465     HIS A   775                                                      
REMARK 465     HIS A   776                                                      
REMARK 465     HIS A   777                                                      
REMARK 465     HIS A   778                                                      
REMARK 465     HIS A   779                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A 758    CG   OD1  OD2                                       
REMARK 470     ARG A 760    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 761    CG   CD   CE   NZ                                   
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    PRO A 757   C   -  N   -  CA  ANGL. DEV. =  13.6 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    ALA A 114       75.06   -157.47                                   
REMARK 500    THR A 285      -73.07   -114.29                                   
REMARK 500    THR A 332      -78.74   -124.05                                   
REMARK 500    LEU A 348      -71.99    -68.53                                   
REMARK 500    GLN A 421       42.86    -93.42                                   
REMARK 500    ASP A 493      119.51   -166.32                                   
REMARK 500    LYS A 509       76.04    -68.95                                   
REMARK 500    HIS A 540      -49.60    -27.73                                   
REMARK 500    ASN A 621       73.10     59.93                                   
REMARK 500    THR A 717      -71.63   -124.95                                   
REMARK 500    PHE A 722      -54.73   -127.14                                   
REMARK 500    GLU A 753       41.85    -88.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     L9Q A  801                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue L9Q A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMT A 802                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6N40   RELATED DB: PDB                                   
DBREF  6OR2 A    1   773  UNP    A0QP27   A0QP27_MYCS2     1    773             
SEQADV 6OR2 HIS A  774  UNP  A0QP27              EXPRESSION TAG                 
SEQADV 6OR2 HIS A  775  UNP  A0QP27              EXPRESSION TAG                 
SEQADV 6OR2 HIS A  776  UNP  A0QP27              EXPRESSION TAG                 
SEQADV 6OR2 HIS A  777  UNP  A0QP27              EXPRESSION TAG                 
SEQADV 6OR2 HIS A  778  UNP  A0QP27              EXPRESSION TAG                 
SEQADV 6OR2 HIS A  779  UNP  A0QP27              EXPRESSION TAG                 
SEQRES   1 A  779  MET PHE ALA TRP TRP GLY ARG THR VAL TYR GLN PHE ARG          
SEQRES   2 A  779  TYR ILE VAL ILE GLY VAL MET VAL ALA LEU CYS LEU GLY          
SEQRES   3 A  779  GLY GLY VAL TYR GLY ILE SER LEU GLY ASN HIS VAL THR          
SEQRES   4 A  779  GLN SER GLY PHE TYR ASP GLU GLY SER GLN SER VAL ALA          
SEQRES   5 A  779  ALA SER LEU ILE GLY ASP GLU VAL TYR GLY ARG ASP ARG          
SEQRES   6 A  779  THR SER HIS VAL VAL ALA ILE LEU THR PRO PRO ASP ASP          
SEQRES   7 A  779  LYS LYS VAL THR ASP LYS ALA TRP GLN LYS LYS VAL THR          
SEQRES   8 A  779  GLU GLU LEU ASP GLN VAL VAL LYS ASP HIS GLU ASP GLN          
SEQRES   9 A  779  ILE VAL GLY TRP VAL GLY TRP LEU LYS ALA PRO ASP THR          
SEQRES  10 A  779  THR ASP PRO THR VAL SER ALA MET LYS THR GLN ASP LEU          
SEQRES  11 A  779  ARG HIS THR PHE ILE SER ILE PRO LEU GLN GLY ASP ASP          
SEQRES  12 A  779  ASP ASP GLU ILE LEU LYS ASN TYR GLN VAL VAL GLU PRO          
SEQRES  13 A  779  GLU LEU GLN GLN VAL ASN GLY GLY ASP ILE ARG LEU ALA          
SEQRES  14 A  779  GLY LEU ASN PRO LEU ALA SER GLU LEU THR GLY THR ILE          
SEQRES  15 A  779  GLY GLU ASP GLN LYS ARG ALA GLU VAL ALA ALA ILE PRO          
SEQRES  16 A  779  LEU VAL ALA VAL VAL LEU PHE PHE VAL PHE GLY THR VAL          
SEQRES  17 A  779  ILE ALA ALA ALA LEU PRO ALA ILE ILE GLY GLY LEU ALA          
SEQRES  18 A  779  ILE ALA GLY ALA LEU GLY ILE MET ARG LEU VAL ALA GLU          
SEQRES  19 A  779  PHE THR PRO VAL HIS PHE PHE ALA GLN PRO VAL VAL THR          
SEQRES  20 A  779  LEU ILE GLY LEU GLY ILE ALA ILE ASP TYR GLY LEU PHE          
SEQRES  21 A  779  ILE VAL SER ARG PHE ARG GLU GLU ILE ALA GLU GLY TYR          
SEQRES  22 A  779  ASP THR GLU ALA ALA VAL ARG ARG THR VAL MET THR SER          
SEQRES  23 A  779  GLY ARG THR VAL VAL PHE SER ALA VAL ILE ILE VAL ALA          
SEQRES  24 A  779  SER SER VAL PRO LEU LEU LEU PHE PRO GLN GLY PHE LEU          
SEQRES  25 A  779  LYS SER ILE THR TYR ALA ILE ILE ALA SER VAL MET LEU          
SEQRES  26 A  779  ALA ALA ILE LEU SER ILE THR VAL LEU ALA ALA ALA LEU          
SEQRES  27 A  779  ALA ILE LEU GLY PRO ARG VAL ASP ALA LEU GLY VAL THR          
SEQRES  28 A  779  THR LEU LEU LYS ILE PRO PHE LEU ALA ASN TRP GLN PHE          
SEQRES  29 A  779  SER ARG ARG ILE ILE ASP TRP PHE ALA GLU LYS THR GLN          
SEQRES  30 A  779  LYS THR LYS THR ARG GLU GLU VAL GLU ARG GLY PHE TRP          
SEQRES  31 A  779  GLY ARG LEU VAL ASN VAL VAL MET LYS ARG PRO ILE ALA          
SEQRES  32 A  779  PHE ALA ALA PRO ILE LEU VAL VAL MET VAL LEU LEU ILE          
SEQRES  33 A  779  ILE PRO LEU GLY GLN LEU SER LEU GLY GLY ILE SER GLU          
SEQRES  34 A  779  LYS TYR LEU PRO PRO ASP ASN ALA VAL ARG GLN SER GLN          
SEQRES  35 A  779  GLU GLN PHE ASP LYS LEU PHE PRO GLY PHE ARG THR GLU          
SEQRES  36 A  779  PRO LEU THR LEU VAL MET LYS ARG GLU ASP GLY GLU PRO          
SEQRES  37 A  779  ILE THR ASP ALA GLN ILE ALA ASP MET ARG ALA LYS ALA          
SEQRES  38 A  779  LEU THR VAL SER GLY PHE THR ASP PRO ASP ASN ASP PRO          
SEQRES  39 A  779  GLU LYS MET TRP LYS GLU ARG PRO ALA ASN ASP SER GLY          
SEQRES  40 A  779  SER LYS ASP PRO SER VAL ARG VAL ILE GLN ASN GLY LEU          
SEQRES  41 A  779  GLU ASN ARG ASN ASP ALA ALA LYS LYS ILE ASP GLU LEU          
SEQRES  42 A  779  ARG ALA LEU GLN PRO PRO HIS GLY ILE GLU VAL PHE VAL          
SEQRES  43 A  779  GLY GLY THR PRO ALA LEU GLU GLN ASP SER ILE HIS SER          
SEQRES  44 A  779  LEU PHE ASP LYS LEU PRO LEU MET ALA LEU ILE LEU ILE          
SEQRES  45 A  779  VAL THR THR THR VAL LEU MET PHE LEU ALA PHE GLY SER          
SEQRES  46 A  779  VAL VAL LEU PRO ILE LYS ALA ALA LEU MET SER ALA LEU          
SEQRES  47 A  779  THR LEU GLY SER THR MET GLY ILE LEU THR TRP MET PHE          
SEQRES  48 A  779  VAL ASP GLY HIS GLY SER GLY LEU MET ASN TYR THR PRO          
SEQRES  49 A  779  GLN PRO LEU MET ALA PRO MET ILE GLY LEU ILE ILE ALA          
SEQRES  50 A  779  VAL ILE TRP GLY LEU SER THR ASP TYR GLU VAL PHE LEU          
SEQRES  51 A  779  VAL SER ARG MET VAL GLU ALA ARG GLU ARG GLY MET SER          
SEQRES  52 A  779  THR ALA GLU ALA ILE ARG ILE GLY THR ALA THR THR GLY          
SEQRES  53 A  779  ARG LEU ILE THR GLY ALA ALA LEU ILE LEU ALA VAL VAL          
SEQRES  54 A  779  ALA GLY ALA PHE VAL PHE SER ASP LEU VAL MET MET LYS          
SEQRES  55 A  779  TYR LEU ALA PHE GLY LEU LEU ILE ALA LEU LEU LEU ASP          
SEQRES  56 A  779  ALA THR ILE ILE ARG MET PHE LEU VAL PRO ALA VAL MET          
SEQRES  57 A  779  LYS LEU LEU GLY ASP ASP CYS TRP TRP ALA PRO ARG TRP          
SEQRES  58 A  779  MET LYS ARG VAL GLN GLU LYS LEU GLY LEU GLY GLU THR          
SEQRES  59 A  779  GLU LEU PRO ASP GLU ARG LYS ARG PRO THR VAL ARG GLU          
SEQRES  60 A  779  SER GLU THR ASP GLN ARG HIS HIS HIS HIS HIS HIS              
HET    L9Q  A 801      50                                                       
HET    LMT  A 802      35                                                       
HETNAM     L9Q (1S)-2-{[(S)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-          
HETNAM   2 L9Q  [(OCTADECANOYLOXY)METHYL]ETHYL (9Z)-OCTADEC-9-ENOATE            
HETNAM     LMT DODECYL-BETA-D-MALTOSIDE                                         
HETSYN     L9Q 1-STEAROYL-2-OLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE             
FORMUL   2  L9Q    C41 H80 N O8 P                                               
FORMUL   3  LMT    C24 H46 O11                                                  
FORMUL   4  HOH   *11(H2 O)                                                     
HELIX    1 AA1 MET A    1  PHE A   12  1                                  12    
HELIX    2 AA2 PHE A   12  ILE A   32  1                                  21    
HELIX    3 AA3 SER A   33  HIS A   37  5                                   5    
HELIX    4 AA4 SER A   48  GLY A   62  1                                  15    
HELIX    5 AA5 ASP A   83  HIS A  101  1                                  19    
HELIX    6 AA6 LEU A  112  ALA A  114  5                                   3    
HELIX    7 AA7 ASP A  119  ALA A  124  1                                   6    
HELIX    8 AA8 ASP A  143  GLN A  160  1                                  18    
HELIX    9 AA9 VAL A  161  GLY A  164  5                                   4    
HELIX   10 AB1 GLY A  170  ALA A  192  1                                  23    
HELIX   11 AB2 ALA A  192  GLY A  206  1                                  15    
HELIX   12 AB3 THR A  207  ALA A  233  1                                  27    
HELIX   13 AB4 PHE A  241  ILE A  249  1                                   9    
HELIX   14 AB5 ILE A  249  GLY A  272  1                                  24    
HELIX   15 AB6 ASP A  274  VAL A  302  1                                  29    
HELIX   16 AB7 PRO A  303  PHE A  307  5                                   5    
HELIX   17 AB8 GLN A  309  ILE A  331  1                                  23    
HELIX   18 AB9 THR A  332  GLY A  342  1                                  11    
HELIX   19 AC1 PRO A  343  ALA A  347  5                                   5    
HELIX   20 AC2 GLU A  383  ARG A  400  1                                  18    
HELIX   21 AC3 PRO A  401  LEU A  415  1                                  15    
HELIX   22 AC4 ILE A  416  LEU A  422  5                                   7    
HELIX   23 AC5 SER A  428  LEU A  432  5                                   5    
HELIX   24 AC6 ASN A  436  PHE A  449  1                                  14    
HELIX   25 AC7 THR A  470  LEU A  482  1                                  13    
HELIX   26 AC8 ASP A  493  MET A  497  5                                   5    
HELIX   27 AC9 ASN A  522  ASN A  524  5                                   3    
HELIX   28 AD1 ASP A  525  ALA A  535  1                                  11    
HELIX   29 AD2 GLY A  548  PHE A  583  1                                  36    
HELIX   30 AD3 VAL A  586  VAL A  612  1                                  27    
HELIX   31 AD4 GLY A  616  ASN A  621  1                                   6    
HELIX   32 AD5 ALA A  629  GLU A  659  1                                  31    
HELIX   33 AD6 SER A  663  THR A  675  1                                  13    
HELIX   34 AD7 THR A  675  VAL A  694  1                                  20    
HELIX   35 AD8 LEU A  698  THR A  717  1                                  20    
HELIX   36 AD9 THR A  717  PHE A  722  1                                   6    
HELIX   37 AE1 PHE A  722  GLY A  732  1                                  11    
HELIX   38 AE2 ASP A  733  TRP A  737  5                                   5    
HELIX   39 AE3 PRO A  739  GLY A  750  1                                  12    
SHEET    1 AA1 4 VAL A 109  GLY A 110  0                                        
SHEET    2 AA1 4 THR A 133  SER A 136 -1  O  SER A 136   N  VAL A 109           
SHEET    3 AA1 4 VAL A  70  LEU A  73 -1  N  LEU A  73   O  THR A 133           
SHEET    4 AA1 4 ILE A 166  ALA A 169 -1  O  ALA A 169   N  VAL A  70           
SHEET    1 AA2 2 LEU A 424  GLY A 425  0                                        
SHEET    2 AA2 2 LEU A 627  MET A 628  1  O  LEU A 627   N  GLY A 425           
SHEET    1 AA3 4 LYS A 499  GLU A 500  0                                        
SHEET    2 AA3 4 VAL A 513  GLY A 519 -1  O  GLN A 517   N  LYS A 499           
SHEET    3 AA3 4 PRO A 456  ARG A 463 -1  N  LEU A 459   O  ILE A 516           
SHEET    4 AA3 4 ILE A 542  GLY A 547 -1  O  PHE A 545   N  VAL A 460           
SITE     1 AC1 14 GLN A  40  PHE A  43  ASP A  64  VAL A  70                    
SITE     2 AC1 14 LEU A 171  LEU A 174  PHE A 452  ARG A 453                    
SITE     3 AC1 14 THR A 454  ARG A 501  PRO A 502  ASN A 504                    
SITE     4 AC1 14 GLN A 517  THR A 549                                          
SITE     1 AC2  5 LEU A 424  GLN A 554  ILE A 557  PHE A 561                    
SITE     2 AC2  5 LEU A 564                                                     
CRYST1   80.814  129.457  154.591  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      0.012374  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007725  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006469        0.00000                         
ATOM      1  N   MET A   1     146.554  36.490  22.472  1.00124.07           N  
ANISOU    1  N   MET A   1    26323  10650  10170   2461   1483  -1297       N  
ATOM      2  CA  MET A   1     146.198  36.967  23.805  1.00127.28           C  
ANISOU    2  CA  MET A   1    26390  11120  10849   2206   1475  -1172       C  
ATOM      3  C   MET A   1     144.838  37.659  23.791  1.00121.58           C  
ANISOU    3  C   MET A   1    25420  10535  10241   1853   1250  -1299       C  
ATOM      4  O   MET A   1     143.922  37.257  24.508  1.00110.63           O  
ANISOU    4  O   MET A   1    24003   9018   9012   1513   1165  -1410       O  
ATOM      5  CB  MET A   1     147.273  37.914  24.339  1.00129.38           C  
ANISOU    5  CB  MET A   1    26326  11638  11196   2421   1642   -894       C  
ATOM      6  CG  MET A   1     146.911  38.588  25.650  1.00128.35           C  
ANISOU    6  CG  MET A   1    25820  11615  11332   2178   1619   -762       C  
ATOM      7  SD  MET A   1     148.291  39.495  26.369  1.00123.01           S  
ANISOU    7  SD  MET A   1    24790  11197  10751   2434   1823   -473       S  
ATOM      8  CE  MET A   1     149.398  38.149  26.779  1.00128.05           C  
ANISOU    8  CE  MET A   1    25748  11600  11306   2744   1991   -446       C  
ATOM      9  N   PHE A   2     144.713  38.711  22.977  1.00124.17           N  
ANISOU    9  N   PHE A   2    25577  11126  10475   1946   1163  -1287       N  
ATOM     10  CA  PHE A   2     143.406  39.328  22.780  1.00118.77           C  
ANISOU   10  CA  PHE A   2    24694  10586   9846   1682    916  -1447       C  
ATOM     11  C   PHE A   2     142.515  38.466  21.897  1.00126.61           C  
ANISOU   11  C   PHE A   2    25976  11431  10700   1563    725  -1782       C  
ATOM     12  O   PHE A   2     141.287  38.504  22.033  1.00127.02           O  
ANISOU   12  O   PHE A   2    25884  11523  10854   1252    518  -1992       O  
ATOM     13  CB  PHE A   2     143.561  40.725  22.179  1.00108.39           C  
ANISOU   13  CB  PHE A   2    23166   9575   8443   1857    882  -1325       C  
ATOM     14  CG  PHE A   2     144.152  41.729  23.124  1.00110.72           C  
ANISOU   14  CG  PHE A   2    23112  10039   8918   1874   1026  -1043       C  
ATOM     15  CD1 PHE A   2     145.522  41.916  23.192  1.00112.86           C  
ANISOU   15  CD1 PHE A   2    23385  10348   9150   2141   1279   -822       C  
ATOM     16  CD2 PHE A   2     143.336  42.487  23.947  1.00112.02           C  
ANISOU   16  CD2 PHE A   2    22933  10340   9291   1622    908  -1022       C  
ATOM     17  CE1 PHE A   2     146.067  42.842  24.062  1.00108.43           C  
ANISOU   17  CE1 PHE A   2    22488   9950   8760   2137   1403   -594       C  
ATOM     18  CE2 PHE A   2     143.875  43.412  24.820  1.00111.97           C  
ANISOU   18  CE2 PHE A   2    22620  10479   9444   1634   1033   -778       C  
ATOM     19  CZ  PHE A   2     145.241  43.591  24.876  1.00109.64           C  
ANISOU   19  CZ  PHE A   2    22330  10214   9113   1883   1277   -568       C  
ATOM     20  N   ALA A   3     143.110  37.691  20.987  1.00132.62           N  
ANISOU   20  N   ALA A   3    27128  12033  11227   1806    789  -1856       N  
ATOM     21  CA  ALA A   3     142.331  36.729  20.216  1.00130.86           C  
ANISOU   21  CA  ALA A   3    27218  11628  10875   1681    619  -2193       C  
ATOM     22  C   ALA A   3     141.730  35.667  21.124  1.00124.86           C  
ANISOU   22  C   ALA A   3    26555  10582  10305   1316    628  -2334       C  
ATOM     23  O   ALA A   3     140.567  35.279  20.958  1.00121.99           O  
ANISOU   23  O   ALA A   3    26198  10167   9986    994    436  -2636       O  
ATOM     24  CB  ALA A   3     143.205  36.085  19.141  1.00131.79           C  
ANISOU   24  CB  ALA A   3    27761  11612  10700   2040    718  -2222       C  
ATOM     25  N   TRP A   4     142.510  35.188  22.095  1.00121.67           N  
ANISOU   25  N   TRP A   4    26230   9992  10007   1361    857  -2130       N  
ATOM     26  CA  TRP A   4     141.993  34.221  23.055  1.00124.88           C  
ANISOU   26  CA  TRP A   4    26771  10097  10579   1021    908  -2223       C  
ATOM     27  C   TRP A   4     140.890  34.833  23.908  1.00123.06           C  
ANISOU   27  C   TRP A   4    26130  10021  10607    610    797  -2269       C  
ATOM     28  O   TRP A   4     139.814  34.247  24.068  1.00124.24           O  
ANISOU   28  O   TRP A   4    26322  10033  10850    214    704  -2534       O  
ATOM     29  CB  TRP A   4     143.129  33.701  23.935  1.00131.49           C  
ANISOU   29  CB  TRP A   4    27785  10732  11443   1232   1166  -1967       C  
ATOM     30  CG  TRP A   4     142.645  32.945  25.130  1.00136.99           C  
ANISOU   30  CG  TRP A   4    28588  11143  12317    898   1248  -1987       C  
ATOM     31  CD1 TRP A   4     142.290  31.630  25.178  1.00148.55           C  
ANISOU   31  CD1 TRP A   4    30505  12196  13740    709   1297  -2178       C  
ATOM     32  CD2 TRP A   4     142.455  33.461  26.453  1.00139.13           C  
ANISOU   32  CD2 TRP A   4    28543  11498  12823    705   1310  -1811       C  
ATOM     33  NE1 TRP A   4     141.892  31.293  26.448  1.00147.25           N  
ANISOU   33  NE1 TRP A   4    30341  11845  13762    405   1403  -2121       N  
ATOM     34  CE2 TRP A   4     141.984  32.400  27.250  1.00135.19           C  
ANISOU   34  CE2 TRP A   4    28338  10625  12403    407   1408  -1897       C  
ATOM     35  CE3 TRP A   4     142.639  34.717  27.040  1.00143.93           C  
ANISOU   35  CE3 TRP A   4    28671  12446  13570    753   1302  -1592       C  
ATOM     36  CZ2 TRP A   4     141.694  32.554  28.603  1.00118.52           C  
ANISOU   36  CZ2 TRP A   4    26059   8482  10493    171   1499  -1765       C  
ATOM     37  CZ3 TRP A   4     142.350  34.869  28.385  1.00138.64           C  
ANISOU   37  CZ3 TRP A   4    27816  11751  13108    524   1374  -1473       C  
ATOM     38  CH2 TRP A   4     141.883  33.793  29.151  1.00131.66           C  
ANISOU   38  CH2 TRP A   4    27234  10503  12287    243   1473  -1556       C  
ATOM     39  N   TRP A   5     141.140  36.020  24.466  1.00115.00           N  
ANISOU   39  N   TRP A   5    24702   9289   9704    688    818  -2028       N  
ATOM     40  CA  TRP A   5     140.132  36.678  25.288  1.00113.46           C  
ANISOU   40  CA  TRP A   5    24101   9263   9744    336    718  -2062       C  
ATOM     41  C   TRP A   5     138.911  37.094  24.480  1.00119.31           C  
ANISOU   41  C   TRP A   5    24660  10213  10459    152    437  -2363       C  
ATOM     42  O   TRP A   5     137.822  37.231  25.048  1.00115.08           O  
ANISOU   42  O   TRP A   5    23861   9753  10109   -216    335  -2518       O  
ATOM     43  CB  TRP A   5     140.734  37.895  25.992  1.00109.56           C  
ANISOU   43  CB  TRP A   5    23238   9030   9360    496    796  -1742       C  
ATOM     44  CG  TRP A   5     139.761  38.597  26.884  1.00108.35           C  
ANISOU   44  CG  TRP A   5    22678   9052   9440    170    707  -1761       C  
ATOM     45  CD1 TRP A   5     139.198  39.823  26.679  1.00108.94           C  
ANISOU   45  CD1 TRP A   5    22379   9457   9555    159    539  -1771       C  
ATOM     46  CD2 TRP A   5     139.218  38.106  28.116  1.00116.15           C  
ANISOU   46  CD2 TRP A   5    23613   9883  10636   -180    791  -1778       C  
ATOM     47  NE1 TRP A   5     138.346  40.130  27.712  1.00117.84           N  
ANISOU   47  NE1 TRP A   5    23197  10666  10913   -168    505  -1801       N  
ATOM     48  CE2 TRP A   5     138.340  39.092  28.607  1.00116.93           C  
ANISOU   48  CE2 TRP A   5    23266  10257  10905   -392    668  -1805       C  
ATOM     49  CE3 TRP A   5     139.395  36.932  28.855  1.00115.87           C  
ANISOU   49  CE3 TRP A   5    23895   9489  10642   -319    970  -1769       C  
ATOM     50  CZ2 TRP A   5     137.639  38.939  29.801  1.00116.18           C  
ANISOU   50  CZ2 TRP A   5    23008  10108  11026   -753    730  -1829       C  
ATOM     51  CZ3 TRP A   5     138.697  36.781  30.040  1.00109.34           C  
ANISOU   51  CZ3 TRP A   5    22939   8586  10019   -683   1039  -1781       C  
ATOM     52  CH2 TRP A   5     137.830  37.779  30.501  1.00107.63           C  
ANISOU   52  CH2 TRP A   5    22251   8668   9977   -904    924  -1813       C  
ATOM     53  N   GLY A   6     139.063  37.292  23.170  1.00136.79           N  
ANISOU   53  N   GLY A   6    27008  12531  12434    415    309  -2460       N  
ATOM     54  CA  GLY A   6     137.922  37.674  22.356  1.00138.66           C  
ANISOU   54  CA  GLY A   6    27093  12980  12611    298     11  -2765       C  
ATOM     55  C   GLY A   6     136.837  36.614  22.323  1.00135.95           C  
ANISOU   55  C   GLY A   6    26858  12460  12337   -108   -105  -3155       C  
ATOM     56  O   GLY A   6     135.645  36.934  22.313  1.00133.90           O  
ANISOU   56  O   GLY A   6    26299  12399  12177   -376   -324  -3416       O  
ATOM     57  N   ARG A   7     137.230  35.339  22.310  1.00138.90           N  
ANISOU   57  N   ARG A   7    27659  12459  12657   -160     46  -3217       N  
ATOM     58  CA  ARG A   7     136.259  34.251  22.288  1.00145.74           C  
ANISOU   58  CA  ARG A   7    28683  13103  13590   -582    -22  -3595       C  
ATOM     59  C   ARG A   7     135.847  33.786  23.678  1.00139.78           C  
ANISOU   59  C   ARG A   7    27845  12154  13110  -1009    157  -3565       C  
ATOM     60  O   ARG A   7     134.744  33.252  23.837  1.00138.74           O  
ANISOU   60  O   ARG A   7    27653  11956  13107  -1465     85  -3897       O  
ATOM     61  CB  ARG A   7     136.806  33.061  21.493  1.00157.87           C  
ANISOU   61  CB  ARG A   7    30786  14292  14905   -438     46  -3714       C  
ATOM     62  CG  ARG A   7     138.289  32.789  21.682  1.00161.02           C  
ANISOU   62  CG  ARG A   7    31503  14487  15190    -39    313  -3357       C  
ATOM     63  CD  ARG A   7     138.703  31.503  20.978  1.00165.52           C  
ANISOU   63  CD  ARG A   7    32652  14684  15553     69    381  -3513       C  
ATOM     64  NE  ARG A   7     140.149  31.411  20.791  1.00173.19           N  
ANISOU   64  NE  ARG A   7    33888  15568  16349    567    577  -3217       N  
ATOM     65  CZ  ARG A   7     140.776  31.720  19.660  1.00182.93           C  
ANISOU   65  CZ  ARG A   7    35235  16942  17327    976    529  -3191       C  
ATOM     66  NH1 ARG A   7     140.086  32.141  18.608  1.00186.32           N  
ANISOU   66  NH1 ARG A   7    35578  17590  17627    971    274  -3431       N  
ATOM     67  NH2 ARG A   7     142.095  31.605  19.578  1.00183.70           N  
ANISOU   67  NH2 ARG A   7    35536  16974  17289   1402    737  -2936       N  
ATOM     68  N   THR A   8     136.698  33.974  24.691  1.00140.39           N  
ANISOU   68  N   THR A   8    27919  12147  13275   -880    395  -3191       N  
ATOM     69  CA  THR A   8     136.320  33.572  26.043  1.00129.93           C  
ANISOU   69  CA  THR A   8    26547  10637  12185  -1259    575  -3142       C  
ATOM     70  C   THR A   8     135.286  34.516  26.645  1.00131.54           C  
ANISOU   70  C   THR A   8    26190  11178  12612  -1555    453  -3212       C  
ATOM     71  O   THR A   8     134.424  34.076  27.413  1.00124.18           O  
ANISOU   71  O   THR A   8    25179  10137  11868  -2016    522  -3371       O  
ATOM     72  CB  THR A   8     137.553  33.497  26.946  1.00121.96           C  
ANISOU   72  CB  THR A   8    25707   9455  11177   -988    839  -2735       C  
ATOM     73  OG1 THR A   8     138.188  34.779  26.998  1.00135.43           O  
ANISOU   73  OG1 THR A   8    27063  11512  12881   -651    801  -2455       O  
ATOM     74  CG2 THR A   8     138.540  32.469  26.419  1.00131.79           C  
ANISOU   74  CG2 THR A   8    27516  10357  12203   -689    967  -2690       C  
ATOM     75  N   VAL A   9     135.353  35.809  26.314  1.00138.06           N  
ANISOU   75  N   VAL A   9    26641  12403  13412  -1299    288  -3099       N  
ATOM     76  CA  VAL A   9     134.358  36.755  26.809  1.00129.14           C  
ANISOU   76  CA  VAL A   9    24984  11612  12472  -1529    148  -3180       C  
ATOM     77  C   VAL A   9     132.992  36.501  26.184  1.00129.58           C  
ANISOU   77  C   VAL A   9    24880  11797  12557  -1862    -95  -3657       C  
ATOM     78  O   VAL A   9     131.973  36.961  26.715  1.00130.59           O  
ANISOU   78  O   VAL A   9    24589  12153  12874  -2163   -185  -3814       O  
ATOM     79  CB  VAL A   9     134.817  38.207  26.560  1.00132.68           C  
ANISOU   79  CB  VAL A   9    25134  12420  12857  -1140     38  -2936       C  
ATOM     80  CG1 VAL A   9     134.656  38.580  25.094  1.00139.10           C  
ANISOU   80  CG1 VAL A   9    25983  13431  13439   -879   -222  -3119       C  
ATOM     81  CG2 VAL A   9     134.057  39.178  27.455  1.00133.29           C  
ANISOU   81  CG2 VAL A   9    24709  12782  13153  -1336    -22  -2910       C  
ATOM     82  N   TYR A  10     132.943  35.775  25.064  1.00133.61           N  
ANISOU   82  N   TYR A  10    25701  12183  12882  -1809   -210  -3912       N  
ATOM     83  CA  TYR A  10     131.690  35.345  24.454  1.00136.94           C  
ANISOU   83  CA  TYR A  10    26011  12695  13325  -2147   -438  -4414       C  
ATOM     84  C   TYR A  10     131.160  34.054  25.067  1.00143.40           C  
ANISOU   84  C   TYR A  10    27036  13150  14301  -2681   -249  -4640       C  
ATOM     85  O   TYR A  10     129.944  33.888  25.196  1.00140.38           O  
ANISOU   85  O   TYR A  10    26369  12891  14077  -3127   -353  -5018       O  
ATOM     86  CB  TYR A  10     131.867  35.155  22.943  1.00137.18           C  
ANISOU   86  CB  TYR A  10    26301  12756  13065  -1843   -659  -4607       C  
ATOM     87  CG  TYR A  10     130.621  34.645  22.240  1.00136.76           C  
ANISOU   87  CG  TYR A  10    26150  12798  13013  -2170   -920  -5164       C  
ATOM     88  CD1 TYR A  10     129.633  35.523  21.816  1.00141.86           C  
ANISOU   88  CD1 TYR A  10    26327  13902  13669  -2167  -1254  -5427       C  
ATOM     89  CD2 TYR A  10     130.430  33.286  22.008  1.00140.79           C  
ANISOU   89  CD2 TYR A  10    27039  12945  13510  -2476   -839  -5446       C  
ATOM     90  CE1 TYR A  10     128.491  35.066  21.182  1.00147.08           C  
ANISOU   90  CE1 TYR A  10    26855  14693  14334  -2456  -1514  -5972       C  
ATOM     91  CE2 TYR A  10     129.292  32.822  21.376  1.00145.47           C  
ANISOU   91  CE2 TYR A  10    27516  13639  14116  -2804  -1079  -5989       C  
ATOM     92  CZ  TYR A  10     128.326  33.716  20.964  1.00146.20           C  
ANISOU   92  CZ  TYR A  10    27097  14227  14226  -2791  -1424  -6259       C  
ATOM     93  OH  TYR A  10     127.191  33.258  20.334  1.00151.19           O  
ANISOU   93  OH  TYR A  10    27573  15000  14873  -3106  -1685  -6835       O  
ATOM     94  N   GLN A  11     132.048  33.131  25.444  1.00143.44           N  
ANISOU   94  N   GLN A  11    27540  12706  14256  -2643     37  -4430       N  
ATOM     95  CA  GLN A  11     131.600  31.865  26.014  1.00147.70           C  
ANISOU   95  CA  GLN A  11    28373  12835  14913  -3138    250  -4624       C  
ATOM     96  C   GLN A  11     131.146  32.016  27.459  1.00142.03           C  
ANISOU   96  C   GLN A  11    27405  12100  14460  -3512    461  -4509       C  
ATOM     97  O   GLN A  11     130.330  31.219  27.933  1.00149.04           O  
ANISOU   97  O   GLN A  11    28357  12777  15496  -4050    594  -4771       O  
ATOM     98  CB  GLN A  11     132.714  30.820  25.915  1.00146.07           C  
ANISOU   98  CB  GLN A  11    28837  12134  14530  -2917    477  -4435       C  
ATOM     99  CG  GLN A  11     133.126  30.492  24.485  1.00153.98           C  
ANISOU   99  CG  GLN A  11    30147  13101  15259  -2587    302  -4585       C  
ATOM    100  CD  GLN A  11     134.331  29.573  24.411  1.00156.59           C  
ANISOU  100  CD  GLN A  11    31111  12982  15403  -2286    529  -4364       C  
ATOM    101  OE1 GLN A  11     134.928  29.224  25.430  1.00157.44           O  
ANISOU  101  OE1 GLN A  11    31432  12818  15572  -2273    802  -4077       O  
ATOM    102  NE2 GLN A  11     134.697  29.177  23.196  1.00154.05           N  
ANISOU  102  NE2 GLN A  11    31083  12606  14845  -2009    406  -4495       N  
ATOM    103  N   PHE A  12     131.658  33.017  28.170  1.00131.07           N  
ANISOU  103  N   PHE A  12    25749  10922  13129  -3252    509  -4134       N  
ATOM    104  CA  PHE A  12     131.282  33.294  29.551  1.00129.67           C  
ANISOU  104  CA  PHE A  12    25318  10767  13182  -3547    696  -3997       C  
ATOM    105  C   PHE A  12     130.645  34.673  29.665  1.00131.07           C  
ANISOU  105  C   PHE A  12    24840  11479  13481  -3511    478  -4019       C  
ATOM    106  O   PHE A  12     130.846  35.394  30.644  1.00124.03           O  
ANISOU  106  O   PHE A  12    23713  10710  12703  -3454    581  -3737       O  
ATOM    107  CB  PHE A  12     132.490  33.184  30.479  1.00132.44           C  
ANISOU  107  CB  PHE A  12    25974  10853  13495  -3274    971  -3525       C  
ATOM    108  CG  PHE A  12     133.173  31.847  30.432  1.00146.53           C  
ANISOU  108  CG  PHE A  12    28434  12103  15139  -3243   1188  -3480       C  
ATOM    109  CD1 PHE A  12     134.167  31.594  29.500  1.00152.81           C  
ANISOU  109  CD1 PHE A  12    29571  12792  15698  -2785   1129  -3386       C  
ATOM    110  CD2 PHE A  12     132.827  30.845  31.323  1.00151.57           C  
ANISOU  110  CD2 PHE A  12    29391  12331  15866  -3661   1465  -3530       C  
ATOM    111  CE1 PHE A  12     134.799  30.366  29.454  1.00159.55           C  
ANISOU  111  CE1 PHE A  12    31058  13154  16409  -2719   1321  -3352       C  
ATOM    112  CE2 PHE A  12     133.457  29.613  31.283  1.00156.38           C  
ANISOU  112  CE2 PHE A  12    30674  12418  16324  -3602   1664  -3484       C  
ATOM    113  CZ  PHE A  12     134.444  29.374  30.347  1.00160.80           C  
ANISOU  113  CZ  PHE A  12    31556  12890  16650  -3118   1581  -3399       C  
ATOM    114  N   ARG A  13     129.855  35.048  28.655  1.00139.12           N  
ANISOU  114  N   ARG A  13    25576  12822  14462  -3526    162  -4368       N  
ATOM    115  CA  ARG A  13     129.344  36.413  28.568  1.00133.37           C  
ANISOU  115  CA  ARG A  13    24281  12606  13787  -3374    -87  -4384       C  
ATOM    116  C   ARG A  13     128.336  36.726  29.668  1.00132.00           C  
ANISOU  116  C   ARG A  13    23659  12609  13885  -3803    -14  -4496       C  
ATOM    117  O   ARG A  13     128.280  37.867  30.143  1.00127.86           O  
ANISOU  117  O   ARG A  13    22750  12397  13432  -3638    -81  -4316       O  
ATOM    118  CB  ARG A  13     128.719  36.645  27.191  1.00130.76           C  
ANISOU  118  CB  ARG A  13    23806  12562  13316  -3256   -459  -4760       C  
ATOM    119  CG  ARG A  13     127.715  35.582  26.781  1.00134.80           C  
ANISOU  119  CG  ARG A  13    24364  12970  13884  -3732   -520  -5279       C  
ATOM    120  CD  ARG A  13     127.350  35.694  25.311  1.00141.51           C  
ANISOU  120  CD  ARG A  13    25187  14051  14528  -3518   -894  -5621       C  
ATOM    121  NE  ARG A  13     127.253  34.378  24.684  1.00160.85           N  
ANISOU  121  NE  ARG A  13    28049  16167  16899  -3755   -863  -5929       N  
ATOM    122  CZ  ARG A  13     126.125  33.686  24.560  1.00161.11           C  
ANISOU  122  CZ  ARG A  13    27936  16220  17059  -4268   -937  -6441       C  
ATOM    123  NH1 ARG A  13     124.985  34.187  25.014  1.00156.12           N  
ANISOU  123  NH1 ARG A  13    26721  15955  16642  -4586  -1049  -6712       N  
ATOM    124  NH2 ARG A  13     126.136  32.495  23.978  1.00171.26           N  
ANISOU  124  NH2 ARG A  13    29648  17163  18258  -4465   -895  -6700       N  
ATOM    125  N   TYR A  14     127.539  35.741  30.087  1.00135.71           N  
ANISOU  125  N   TYR A  14    24180  12879  14505  -4361    139  -4794       N  
ATOM    126  CA  TYR A  14     126.507  36.012  31.083  1.00140.70           C  
ANISOU  126  CA  TYR A  14    24364  13702  15394  -4800    226  -4943       C  
ATOM    127  C   TYR A  14     127.097  36.236  32.470  1.00143.30           C  
ANISOU  127  C   TYR A  14    24761  13868  15820  -4787    538  -4506       C  
ATOM    128  O   TYR A  14     126.563  37.040  33.243  1.00137.13           O  
ANISOU  128  O   TYR A  14    23533  13373  15196  -4887    541  -4474       O  
ATOM    129  CB  TYR A  14     125.492  34.870  31.122  1.00137.36           C  
ANISOU  129  CB  TYR A  14    23987  13100  15105  -5441    339  -5405       C  
ATOM    130  CG  TYR A  14     124.484  34.909  29.997  1.00141.14           C  
ANISOU  130  CG  TYR A  14    24141  13916  15571  -5561    -16  -5946       C  
ATOM    131  CD1 TYR A  14     123.426  35.808  30.019  1.00141.76           C  
ANISOU  131  CD1 TYR A  14    23552  14530  15782  -5646   -255  -6221       C  
ATOM    132  CD2 TYR A  14     124.585  34.042  28.918  1.00144.36           C  
ANISOU  132  CD2 TYR A  14    24911  14116  15822  -5566   -124  -6200       C  
ATOM    133  CE1 TYR A  14     122.501  35.846  28.996  1.00145.79           C  
ANISOU  133  CE1 TYR A  14    23750  15378  16265  -5718   -608  -6740       C  
ATOM    134  CE2 TYR A  14     123.663  34.071  27.891  1.00148.09           C  
ANISOU  134  CE2 TYR A  14    25085  14913  16268  -5659   -471  -6717       C  
ATOM    135  CZ  TYR A  14     122.624  34.976  27.934  1.00148.72           C  
ANISOU  135  CZ  TYR A  14    24487  15542  16478  -5728   -719  -6990       C  
ATOM    136  OH  TYR A  14     121.704  35.011  26.912  1.00152.76           O  
ANISOU  136  OH  TYR A  14    24687  16405  16949  -5783  -1093  -7528       O  
ATOM    137  N   ILE A  15     128.186  35.549  32.806  1.00149.04           N  
ANISOU  137  N   ILE A  15    26038  14149  16441  -4641    788  -4181       N  
ATOM    138  CA  ILE A  15     128.736  35.658  34.151  1.00144.07           C  
ANISOU  138  CA  ILE A  15    25509  13348  15884  -4628   1079  -3794       C  
ATOM    139  C   ILE A  15     129.674  36.855  34.296  1.00125.93           C  
ANISOU  139  C   ILE A  15    23048  11284  13514  -4080    979  -3389       C  
ATOM    140  O   ILE A  15     129.732  37.463  35.370  1.00118.72           O  
ANISOU  140  O   ILE A  15    21929  10467  12711  -4083   1097  -3162       O  
ATOM    141  CB  ILE A  15     129.435  34.346  34.551  1.00152.54           C  
ANISOU  141  CB  ILE A  15    27257  13832  16869  -4715   1397  -3645       C  
ATOM    142  CG1 ILE A  15     130.561  33.999  33.573  1.00162.10           C  
ANISOU  142  CG1 ILE A  15    28897  14855  17837  -4245   1310  -3507       C  
ATOM    143  CG2 ILE A  15     128.427  33.212  34.624  1.00149.08           C  
ANISOU  143  CG2 ILE A  15    26978  13133  16533  -5345   1558  -4036       C  
ATOM    144  CD1 ILE A  15     131.947  34.294  34.109  1.00168.15           C  
ANISOU  144  CD1 ILE A  15    29891  15508  18493  -3755   1431  -3019       C  
ATOM    145  N   VAL A  16     130.411  37.218  33.242  1.00129.93           N  
ANISOU  145  N   VAL A  16    23649  11882  13836  -3620    779  -3302       N  
ATOM    146  CA  VAL A  16     131.278  38.389  33.338  1.00125.82           C  
ANISOU  146  CA  VAL A  16    22962  11587  13255  -3142    704  -2944       C  
ATOM    147  C   VAL A  16     130.448  39.665  33.388  1.00112.29           C  
ANISOU  147  C   VAL A  16    20663  10350  11653  -3149    485  -3045       C  
ATOM    148  O   VAL A  16     130.893  40.683  33.932  1.00114.30           O  
ANISOU  148  O   VAL A  16    20709  10784  11937  -2907    488  -2761       O  
ATOM    149  CB  VAL A  16     132.294  38.418  32.182  1.00135.87           C  
ANISOU  149  CB  VAL A  16    24514  12819  14293  -2671    589  -2830       C  
ATOM    150  CG1 VAL A  16     133.228  37.221  32.265  1.00137.26           C  
ANISOU  150  CG1 VAL A  16    25266  12532  14354  -2597    819  -2690       C  
ATOM    151  CG2 VAL A  16     131.582  38.441  30.849  1.00146.23           C  
ANISOU  151  CG2 VAL A  16    25730  14320  15509  -2677    302  -3195       C  
ATOM    152  N   ILE A  17     129.237  39.639  32.828  1.00118.06           N  
ANISOU  152  N   ILE A  17    21117  11299  12441  -3413    287  -3463       N  
ATOM    153  CA  ILE A  17     128.316  40.756  33.013  1.00123.95           C  
ANISOU  153  CA  ILE A  17    21296  12494  13305  -3449     92  -3598       C  
ATOM    154  C   ILE A  17     127.801  40.779  34.447  1.00132.38           C  
ANISOU  154  C   ILE A  17    22144  13557  14598  -3812    321  -3551       C  
ATOM    155  O   ILE A  17     127.781  41.827  35.100  1.00127.14           O  
ANISOU  155  O   ILE A  17    21165  13134  14009  -3678    299  -3371       O  
ATOM    156  CB  ILE A  17     127.161  40.681  31.999  1.00126.71           C  
ANISOU  156  CB  ILE A  17    21394  13109  13642  -3602   -205  -4097       C  
ATOM    157  CG1 ILE A  17     127.626  41.161  30.625  1.00136.86           C  
ANISOU  157  CG1 ILE A  17    22793  14529  14678  -3121   -490  -4091       C  
ATOM    158  CG2 ILE A  17     125.970  41.503  32.475  1.00124.14           C  
ANISOU  158  CG2 ILE A  17    20469  13206  13492  -3787   -340  -4320       C  
ATOM    159  CD1 ILE A  17     126.494  41.433  29.666  1.00149.17           C  
ANISOU  159  CD1 ILE A  17    24031  16451  16196  -3149   -850  -4553       C  
ATOM    160  N   GLY A  18     127.395  39.618  34.964  1.00135.62           N  
ANISOU  160  N   GLY A  18    22751  13672  15108  -4278    561  -3708       N  
ATOM    161  CA  GLY A  18     126.838  39.576  36.305  1.00131.47           C  
ANISOU  161  CA  GLY A  18    22046  13127  14780  -4656    808  -3686       C  
ATOM    162  C   GLY A  18     127.857  39.891  37.385  1.00120.82           C  
ANISOU  162  C   GLY A  18    20882  11608  13416  -4427   1028  -3202       C  
ATOM    163  O   GLY A  18     127.558  40.619  38.336  1.00117.84           O  
ANISOU  163  O   GLY A  18    20191  11421  13161  -4481   1090  -3096       O  
ATOM    164  N   VAL A  19     129.072  39.359  37.253  1.00121.07           N  
ANISOU  164  N   VAL A  19    21413  11296  13291  -4152   1139  -2920       N  
ATOM    165  CA  VAL A  19     130.069  39.507  38.310  1.00117.38           C  
ANISOU  165  CA  VAL A  19    21147  10650  12800  -3941   1351  -2495       C  
ATOM    166  C   VAL A  19     130.685  40.902  38.293  1.00110.44           C  
ANISOU  166  C   VAL A  19    19975  10096  11892  -3490   1177  -2236       C  
ATOM    167  O   VAL A  19     130.721  41.589  39.320  1.00106.02           O  
ANISOU  167  O   VAL A  19    19204   9655  11423  -3471   1257  -2048       O  
ATOM    168  CB  VAL A  19     131.144  38.412  38.192  1.00116.89           C  
ANISOU  168  CB  VAL A  19    21713  10125  12576  -3784   1526  -2314       C  
ATOM    169  CG1 VAL A  19     132.293  38.695  39.146  1.00113.86           C  
ANISOU  169  CG1 VAL A  19    21494   9628  12139  -3457   1677  -1885       C  
ATOM    170  CG2 VAL A  19     130.540  37.048  38.482  1.00114.66           C  
ANISOU  170  CG2 VAL A  19    21778   9458  12329  -4267   1763  -2527       C  
ATOM    171  N   MET A  20     131.183  41.343  37.135  1.00115.01           N  
ANISOU  171  N   MET A  20    20557  10807  12335  -3129    953  -2225       N  
ATOM    172  CA  MET A  20     131.886  42.622  37.080  1.00107.65           C  
ANISOU  172  CA  MET A  20    19420  10126  11357  -2708    829  -1963       C  
ATOM    173  C   MET A  20     130.956  43.802  37.339  1.00107.71           C  
ANISOU  173  C   MET A  20    18900  10534  11489  -2772    666  -2070       C  
ATOM    174  O   MET A  20     131.378  44.795  37.943  1.00108.23           O  
ANISOU  174  O   MET A  20    18786  10747  11588  -2568    671  -1825       O  
ATOM    175  CB  MET A  20     132.586  42.781  35.734  1.00 99.83           C  
ANISOU  175  CB  MET A  20    18592   9164  10175  -2334    661  -1941       C  
ATOM    176  CG  MET A  20     133.885  42.001  35.611  1.00 99.46           C  
ANISOU  176  CG  MET A  20    19016   8786   9988  -2101    826  -1717       C  
ATOM    177  SD  MET A  20     135.096  42.499  36.848  1.00 95.85           S  
ANISOU  177  SD  MET A  20    18579   8278   9562  -1851   1021  -1283       S  
ATOM    178  CE  MET A  20     135.173  44.262  36.549  1.00 99.69           C  
ANISOU  178  CE  MET A  20    18624   9190  10063  -1580    820  -1175       C  
ATOM    179  N   VAL A  21     129.697  43.719  36.903  1.00107.49           N  
ANISOU  179  N   VAL A  21    18616  10694  11530  -3043    517  -2448       N  
ATOM    180  CA  VAL A  21     128.746  44.780  37.224  1.00112.91           C  
ANISOU  180  CA  VAL A  21    18794  11771  12337  -3099    367  -2577       C  
ATOM    181  C   VAL A  21     128.448  44.785  38.718  1.00118.55           C  
ANISOU  181  C   VAL A  21    19371  12449  13225  -3375    606  -2477       C  
ATOM    182  O   VAL A  21     128.272  45.848  39.327  1.00106.91           O  
ANISOU  182  O   VAL A  21    17578  11221  11822  -3271    560  -2373       O  
ATOM    183  CB  VAL A  21     127.462  44.632  36.383  1.00105.50           C  
ANISOU  183  CB  VAL A  21    17587  11073  11425  -3308    135  -3049       C  
ATOM    184  CG1 VAL A  21     126.348  45.532  36.912  1.00105.87           C  
ANISOU  184  CG1 VAL A  21    17090  11513  11621  -3430     21  -3229       C  
ATOM    185  CG2 VAL A  21     127.742  44.957  34.924  1.00110.01           C  
ANISOU  185  CG2 VAL A  21    18251  11756  11793  -2939   -150  -3119       C  
ATOM    186  N   ALA A  22     128.404  43.601  39.336  1.00126.76           N  
ANISOU  186  N   ALA A  22    20686  13161  14317  -3719    877  -2501       N  
ATOM    187  CA  ALA A  22     128.137  43.519  40.770  1.00121.47           C  
ANISOU  187  CA  ALA A  22    19953  12419  13781  -3986   1137  -2398       C  
ATOM    188  C   ALA A  22     129.248  44.176  41.582  1.00122.06           C  
ANISOU  188  C   ALA A  22    20126  12441  13811  -3645   1224  -1967       C  
ATOM    189  O   ALA A  22     128.977  44.876  42.565  1.00116.53           O  
ANISOU  189  O   ALA A  22    19167  11901  13210  -3685   1284  -1875       O  
ATOM    190  CB  ALA A  22     127.957  42.060  41.188  1.00115.55           C  
ANISOU  190  CB  ALA A  22    19582  11268  13055  -4398   1430  -2492       C  
ATOM    191  N   LEU A  23     130.506  43.957  41.189  1.00123.33           N  
ANISOU  191  N   LEU A  23    20645  12392  13822  -3307   1233  -1719       N  
ATOM    192  CA  LEU A  23     131.616  44.624  41.863  1.00116.22           C  
ANISOU  192  CA  LEU A  23    19796  11483  12880  -2966   1288  -1345       C  
ATOM    193  C   LEU A  23     131.543  46.135  41.676  1.00110.81           C  
ANISOU  193  C   LEU A  23    18699  11178  12224  -2718   1069  -1295       C  
ATOM    194  O   LEU A  23     131.766  46.898  42.622  1.00 96.06           O  
ANISOU  194  O   LEU A  23    16671   9413  10415  -2634   1121  -1105       O  
ATOM    195  CB  LEU A  23     132.949  44.087  41.342  1.00111.99           C  
ANISOU  195  CB  LEU A  23    19679  10693  12179  -2647   1325  -1143       C  
ATOM    196  CG  LEU A  23     133.188  42.579  41.422  1.00117.80           C  
ANISOU  196  CG  LEU A  23    20907  11010  12843  -2805   1529  -1168       C  
ATOM    197  CD1 LEU A  23     134.476  42.208  40.703  1.00125.38           C  
ANISOU  197  CD1 LEU A  23    22213  11796  13629  -2421   1513  -1004       C  
ATOM    198  CD2 LEU A  23     133.228  42.115  42.869  1.00114.21           C  
ANISOU  198  CD2 LEU A  23    20622  10340  12432  -2975   1794  -1018       C  
ATOM    199  N   CYS A  24     131.229  46.584  40.457  1.00124.23           N  
ANISOU  199  N   CYS A  24    20256  13077  13866  -2587    824  -1466       N  
ATOM    200  CA  CYS A  24     131.126  48.016  40.195  1.00119.82           C  
ANISOU  200  CA  CYS A  24    19370  12850  13307  -2333    616  -1425       C  
ATOM    201  C   CYS A  24     129.947  48.637  40.934  1.00123.42           C  
ANISOU  201  C   CYS A  24    19409  13570  13916  -2549    576  -1585       C  
ATOM    202  O   CYS A  24     130.027  49.792  41.368  1.00124.51           O  
ANISOU  202  O   CYS A  24    19320  13904  14084  -2369    512  -1450       O  
ATOM    203  CB  CYS A  24     131.009  48.267  38.690  1.00 95.19           C  
ANISOU  203  CB  CYS A  24    16255   9858  10054  -2130    367  -1584       C  
ATOM    204  SG  CYS A  24     132.483  47.818  37.754  1.00 89.55           S  
ANISOU  204  SG  CYS A  24    15989   8894   9140  -1800    409  -1373       S  
ATOM    205  N   LEU A  25     128.850  47.893  41.084  1.00120.29           N  
ANISOU  205  N   LEU A  25    18903  13183  13617  -2940    624  -1885       N  
ATOM    206  CA  LEU A  25     127.708  48.396  41.839  1.00120.65           C  
ANISOU  206  CA  LEU A  25    18533  13492  13817  -3171    620  -2061       C  
ATOM    207  C   LEU A  25     127.941  48.321  43.341  1.00119.17           C  
ANISOU  207  C   LEU A  25    18389  13172  13719  -3316    897  -1843       C  
ATOM    208  O   LEU A  25     127.439  49.172  44.084  1.00109.42           O  
ANISOU  208  O   LEU A  25    16831  12169  12575  -3328    885  -1841       O  
ATOM    209  CB  LEU A  25     126.445  47.619  41.462  1.00122.18           C  
ANISOU  209  CB  LEU A  25    18561  13767  14094  -3569    592  -2493       C  
ATOM    210  CG  LEU A  25     125.427  48.354  40.586  1.00115.28           C  
ANISOU  210  CG  LEU A  25    17272  13306  13224  -3484    263  -2829       C  
ATOM    211  CD1 LEU A  25     126.122  49.163  39.506  1.00114.29           C  
ANISOU  211  CD1 LEU A  25    17246  13262  12916  -2988      0  -2692       C  
ATOM    212  CD2 LEU A  25     124.455  47.366  39.966  1.00112.58           C  
ANISOU  212  CD2 LEU A  25    16854  12992  12931  -3850    222  -3266       C  
ATOM    213  N   GLY A  26     128.692  47.320  43.805  1.00125.65           N  
ANISOU  213  N   GLY A  26    19623  13621  14497  -3402   1139  -1663       N  
ATOM    214  CA  GLY A  26     128.995  47.235  45.224  1.00122.85           C  
ANISOU  214  CA  GLY A  26    19365  13125  14187  -3487   1392  -1439       C  
ATOM    215  C   GLY A  26     129.894  48.362  45.696  1.00113.33           C  
ANISOU  215  C   GLY A  26    18089  12025  12946  -3106   1327  -1129       C  
ATOM    216  O   GLY A  26     129.710  48.896  46.793  1.00119.97           O  
ANISOU  216  O   GLY A  26    18769  12958  13856  -3148   1418  -1036       O  
ATOM    217  N   GLY A  27     130.879  48.738  44.878  1.00 96.42           N  
ANISOU  217  N   GLY A  27    16070   9871  10693  -2744   1183   -978       N  
ATOM    218  CA  GLY A  27     131.733  49.865  45.209  1.00 98.51           C  
ANISOU  218  CA  GLY A  27    16247  10249  10933  -2408   1118   -719       C  
ATOM    219  C   GLY A  27     131.026  51.203  45.171  1.00103.92           C  
ANISOU  219  C   GLY A  27    16519  11281  11684  -2331    933   -807       C  
ATOM    220  O   GLY A  27     131.517  52.168  45.767  1.00 95.77           O  
ANISOU  220  O   GLY A  27    15384  10341  10663  -2139    921   -615       O  
ATOM    221  N   GLY A  28     129.886  51.285  44.483  1.00115.06           N  
ANISOU  221  N   GLY A  28    17696  12890  13131  -2465    779  -1108       N  
ATOM    222  CA  GLY A  28     129.141  52.534  44.452  1.00117.28           C  
ANISOU  222  CA  GLY A  28    17594  13508  13457  -2359    590  -1213       C  
ATOM    223  C   GLY A  28     128.522  52.874  45.796  1.00122.02           C  
ANISOU  223  C   GLY A  28    17955  14221  14185  -2541    717  -1218       C  
ATOM    224  O   GLY A  28     128.706  53.978  46.316  1.00122.62           O  
ANISOU  224  O   GLY A  28    17881  14434  14275  -2348    667  -1080       O  
ATOM    225  N   VAL A  29     127.777  51.929  46.376  1.00128.22           N  
ANISOU  225  N   VAL A  29    18719  14939  15060  -2926    899  -1383       N  
ATOM    226  CA  VAL A  29     127.175  52.170  47.684  1.00129.42           C  
ANISOU  226  CA  VAL A  29    18667  15186  15321  -3121   1060  -1391       C  
ATOM    227  C   VAL A  29     128.246  52.248  48.764  1.00126.70           C  
ANISOU  227  C   VAL A  29    18568  14633  14938  -2998   1241  -1039       C  
ATOM    228  O   VAL A  29     128.108  53.008  49.730  1.00123.77           O  
ANISOU  228  O   VAL A  29    18024  14390  14613  -2957   1282   -955       O  
ATOM    229  CB  VAL A  29     126.121  51.091  48.000  1.00126.26           C  
ANISOU  229  CB  VAL A  29    18209  14746  15019  -3599   1251  -1665       C  
ATOM    230  CG1 VAL A  29     124.937  51.217  47.054  1.00126.84           C  
ANISOU  230  CG1 VAL A  29    17920  15122  15150  -3709   1038  -2066       C  
ATOM    231  CG2 VAL A  29     126.728  49.701  47.908  1.00126.47           C  
ANISOU  231  CG2 VAL A  29    18698  14370  14983  -3768   1453  -1584       C  
ATOM    232  N   TYR A  30     129.327  51.475  48.625  1.00124.66           N  
ANISOU  232  N   TYR A  30    18712  14067  14587  -2916   1338   -843       N  
ATOM    233  CA  TYR A  30     130.455  51.606  49.537  1.00116.55           C  
ANISOU  233  CA  TYR A  30    17904  12878  13503  -2727   1458   -525       C  
ATOM    234  C   TYR A  30     131.225  52.897  49.300  1.00110.08           C  
ANISOU  234  C   TYR A  30    16961  12213  12651  -2353   1272   -359       C  
ATOM    235  O   TYR A  30     131.917  53.371  50.207  1.00112.39           O  
ANISOU  235  O   TYR A  30    17288  12484  12933  -2210   1333   -149       O  
ATOM    236  CB  TYR A  30     131.385  50.397  49.401  1.00111.67           C  
ANISOU  236  CB  TYR A  30    17742  11907  12782  -2708   1598   -391       C  
ATOM    237  CG  TYR A  30     132.571  50.413  50.343  1.00113.94           C  
ANISOU  237  CG  TYR A  30    18261  12037  12993  -2488   1708    -92       C  
ATOM    238  CD1 TYR A  30     132.399  50.255  51.712  1.00114.71           C  
ANISOU  238  CD1 TYR A  30    18417  12066  13100  -2611   1898     -7       C  
ATOM    239  CD2 TYR A  30     133.864  50.577  49.861  1.00110.96           C  
ANISOU  239  CD2 TYR A  30    18038  11595  12527  -2152   1623     89       C  
ATOM    240  CE1 TYR A  30     133.480  50.269  52.576  1.00108.33           C  
ANISOU  240  CE1 TYR A  30    17821  11136  12205  -2379   1970    245       C  
ATOM    241  CE2 TYR A  30     134.951  50.587  50.718  1.00103.28           C  
ANISOU  241  CE2 TYR A  30    17237  10517  11487  -1938   1701    325       C  
ATOM    242  CZ  TYR A  30     134.753  50.436  52.073  1.00 99.50           C  
ANISOU  242  CZ  TYR A  30    16818   9978  11009  -2040   1859    400       C  
ATOM    243  OH  TYR A  30     135.831  50.448  52.929  1.00 93.50           O  
ANISOU  243  OH  TYR A  30    16228   9135  10164  -1797   1910    614       O  
ATOM    244  N   GLY A  31     131.109  53.480  48.106  1.00114.74           N  
ANISOU  244  N   GLY A  31    17425  12953  13217  -2197   1052   -457       N  
ATOM    245  CA  GLY A  31     131.757  54.734  47.781  1.00114.33           C  
ANISOU  245  CA  GLY A  31    17284  13029  13126  -1872    896   -317       C  
ATOM    246  C   GLY A  31     130.934  55.975  48.028  1.00107.85           C  
ANISOU  246  C   GLY A  31    16122  12490  12367  -1822    762   -411       C  
ATOM    247  O   GLY A  31     131.455  57.085  47.895  1.00 99.49           O  
ANISOU  247  O   GLY A  31    15015  11510  11276  -1568    657   -285       O  
ATOM    248  N   ILE A  32     129.653  55.820  48.373  1.00117.61           N  
ANISOU  248  N   ILE A  32    17119  13879  13688  -2059    772   -642       N  
ATOM    249  CA  ILE A  32     128.842  56.975  48.753  1.00115.70           C  
ANISOU  249  CA  ILE A  32    16542  13915  13502  -1994    659   -739       C  
ATOM    250  C   ILE A  32     129.430  57.645  49.989  1.00108.86           C  
ANISOU  250  C   ILE A  32    15682  13022  12658  -1904    764   -512       C  
ATOM    251  O   ILE A  32     129.405  58.875  50.122  1.00100.41           O  
ANISOU  251  O   ILE A  32    14461  12105  11586  -1700    643   -472       O  
ATOM    252  CB  ILE A  32     127.377  56.550  48.972  1.00112.70           C  
ANISOU  252  CB  ILE A  32    15880  13720  13219  -2294    685  -1054       C  
ATOM    253  CG1 ILE A  32     126.715  56.201  47.637  1.00112.14           C  
ANISOU  253  CG1 ILE A  32    15729  13758  13121  -2320    500  -1327       C  
ATOM    254  CG2 ILE A  32     126.587  57.644  49.676  1.00114.95           C  
ANISOU  254  CG2 ILE A  32    15824  14283  13568  -2236    624  -1137       C  
ATOM    255  CD1 ILE A  32     126.629  57.368  46.674  1.00113.42           C  
ANISOU  255  CD1 ILE A  32    15777  14119  13196  -1963    205  -1370       C  
ATOM    256  N   SER A  33     129.991  56.849  50.898  1.00117.47           N  
ANISOU  256  N   SER A  33    16976  13905  13752  -2036    984   -365       N  
ATOM    257  CA  SER A  33     130.603  57.349  52.122  1.00114.43           C  
ANISOU  257  CA  SER A  33    16625  13484  13370  -1949   1083   -160       C  
ATOM    258  C   SER A  33     132.012  57.895  51.910  1.00110.85           C  
ANISOU  258  C   SER A  33    16335  12933  12849  -1661   1021     75       C  
ATOM    259  O   SER A  33     132.681  58.227  52.894  1.00102.99           O  
ANISOU  259  O   SER A  33    15388  11897  11848  -1578   1093    239       O  
ATOM    260  CB  SER A  33     130.637  56.240  53.178  1.00106.62           C  
ANISOU  260  CB  SER A  33    15825  12306  12379  -2177   1340   -103       C  
ATOM    261  OG  SER A  33     131.363  55.117  52.709  1.00 98.35           O  
ANISOU  261  OG  SER A  33    15104  11003  11264  -2197   1418    -27       O  
ATOM    262  N   LEU A  34     132.477  57.996  50.661  1.00106.86           N  
ANISOU  262  N   LEU A  34    15911  12400  12290  -1512    896     80       N  
ATOM    263  CA  LEU A  34     133.827  58.494  50.414  1.00102.05           C  
ANISOU  263  CA  LEU A  34    15439  11709  11625  -1270    870    282       C  
ATOM    264  C   LEU A  34     133.966  59.964  50.789  1.00103.46           C  
ANISOU  264  C   LEU A  34    15456  12027  11828  -1109    781    346       C  
ATOM    265  O   LEU A  34     135.033  60.386  51.248  1.00 98.75           O  
ANISOU  265  O   LEU A  34    14924  11374  11221   -984    822    513       O  
ATOM    266  CB  LEU A  34     134.206  58.284  48.947  1.00 96.50           C  
ANISOU  266  CB  LEU A  34    14868  10951  10847  -1161    780    259       C  
ATOM    267  CG  LEU A  34     135.516  58.922  48.473  1.00 91.35           C  
ANISOU  267  CG  LEU A  34    14325  10247  10138   -924    761    433       C  
ATOM    268  CD1 LEU A  34     136.711  58.320  49.193  1.00 87.33           C  
ANISOU  268  CD1 LEU A  34    13969   9592   9621   -887    906    600       C  
ATOM    269  CD2 LEU A  34     135.671  58.786  46.967  1.00103.84           C  
ANISOU  269  CD2 LEU A  34    16030  11796  11629   -823    677    385       C  
ATOM    270  N   GLY A  35     132.906  60.754  50.609  1.00113.93           N  
ANISOU  270  N   GLY A  35    16571  13538  13181  -1102    658    201       N  
ATOM    271  CA  GLY A  35     132.962  62.169  50.942  1.00111.09           C  
ANISOU  271  CA  GLY A  35    16092  13286  12830   -940    573    251       C  
ATOM    272  C   GLY A  35     133.134  62.458  52.419  1.00102.36           C  
ANISOU  272  C   GLY A  35    14921  12194  11779   -982    675    336       C  
ATOM    273  O   GLY A  35     133.429  63.604  52.779  1.00 85.78           O  
ANISOU  273  O   GLY A  35    12765  10143   9683   -847    623    401       O  
ATOM    274  N   ASN A  36     132.959  61.457  53.280  1.00117.87           N  
ANISOU  274  N   ASN A  36    16918  14100  13768  -1165    824    333       N  
ATOM    275  CA  ASN A  36     133.100  61.621  54.721  1.00112.89           C  
ANISOU  275  CA  ASN A  36    16261  13474  13160  -1197    930    413       C  
ATOM    276  C   ASN A  36     134.477  61.206  55.229  1.00107.02           C  
ANISOU  276  C   ASN A  36    15726  12566  12372  -1117   1018    603       C  
ATOM    277  O   ASN A  36     134.701  61.198  56.444  1.00105.16           O  
ANISOU  277  O   ASN A  36    15512  12317  12128  -1123   1103    674       O  
ATOM    278  CB  ASN A  36     132.018  60.822  55.453  1.00118.03           C  
ANISOU  278  CB  ASN A  36    16844  14159  13842  -1440   1064    292       C  
ATOM    279  CG  ASN A  36     130.617  61.205  55.024  1.00126.22           C  
ANISOU  279  CG  ASN A  36    17615  15409  14933  -1520    975     61       C  
ATOM    280  OD1 ASN A  36     130.370  62.337  54.610  1.00124.96           O  
ANISOU  280  OD1 ASN A  36    17308  15394  14778  -1349    809     12       O  
ATOM    281  ND2 ASN A  36     129.688  60.257  55.119  1.00133.51           N  
ANISOU  281  ND2 ASN A  36    18482  16354  15893  -1779   1088    -96       N  
ATOM    282  N   HIS A  37     135.399  60.856  54.334  1.00105.67           N  
ANISOU  282  N   HIS A  37    15703  12285  12162  -1025    996    675       N  
ATOM    283  CA  HIS A  37     136.721  60.369  54.723  1.00 98.80           C  
ANISOU  283  CA  HIS A  37    15008  11287  11245   -924   1069    825       C  
ATOM    284  C   HIS A  37     137.796  60.968  53.822  1.00 91.45           C  
ANISOU  284  C   HIS A  37    14094  10349  10303   -754    995    893       C  
ATOM    285  O   HIS A  37     138.701  60.280  53.349  1.00 80.86           O  
ANISOU  285  O   HIS A  37    12901   8906   8917   -682   1037    955       O  
ATOM    286  CB  HIS A  37     136.777  58.841  54.684  1.00 97.19           C  
ANISOU  286  CB  HIS A  37    15028  10914  10986  -1018   1189    834       C  
ATOM    287  CG  HIS A  37     135.943  58.176  55.733  1.00108.87           C  
ANISOU  287  CG  HIS A  37    16552  12354  12459  -1199   1320    796       C  
ATOM    288  ND1 HIS A  37     134.571  58.083  55.647  1.00113.85           N  
ANISOU  288  ND1 HIS A  37    17053  13062  13143  -1415   1344    637       N  
ATOM    289  CD2 HIS A  37     136.290  57.570  56.894  1.00107.94           C  
ANISOU  289  CD2 HIS A  37    16604  12131  12276  -1195   1448    889       C  
ATOM    290  CE1 HIS A  37     134.108  57.448  56.709  1.00116.32           C  
ANISOU  290  CE1 HIS A  37    17451  13310  13434  -1568   1508    638       C  
ATOM    291  NE2 HIS A  37     135.130  57.126  57.481  1.00115.36           N  
ANISOU  291  NE2 HIS A  37    17538  13063  13228  -1428   1573    801       N  
ATOM    292  N   VAL A  38     137.706  62.272  53.576  1.00105.01           N  
ANISOU  292  N   VAL A  38    15674  12170  12056   -685    901    877       N  
ATOM    293  CA  VAL A  38     138.657  62.967  52.718  1.00108.34           C  
ANISOU  293  CA  VAL A  38    16124  12576  12465   -557    865    936       C  
ATOM    294  C   VAL A  38     139.338  64.070  53.515  1.00111.25           C  
ANISOU  294  C   VAL A  38    16398  12999  12876   -489    857    993       C  
ATOM    295  O   VAL A  38     138.778  64.615  54.471  1.00120.21           O  
ANISOU  295  O   VAL A  38    17427  14205  14042   -518    831    965       O  
ATOM    296  CB  VAL A  38     137.983  63.542  51.454  1.00100.88           C  
ANISOU  296  CB  VAL A  38    15175  11662  11494   -529    769    862       C  
ATOM    297  CG1 VAL A  38     138.484  62.814  50.225  1.00 99.26           C  
ANISOU  297  CG1 VAL A  38    15126  11364  11223   -491    792    876       C  
ATOM    298  CG2 VAL A  38     136.473  63.427  51.559  1.00105.61           C  
ANISOU  298  CG2 VAL A  38    15668  12352  12107   -625    702    721       C  
ATOM    299  N   THR A  39     140.563  64.395  53.109  1.00 92.39           N  
ANISOU  299  N   THR A  39    14039  10579  10485   -407    887   1057       N  
ATOM    300  CA  THR A  39     141.388  65.385  53.780  1.00 93.68           C  
ANISOU  300  CA  THR A  39    14110  10789  10697   -366    891   1089       C  
ATOM    301  C   THR A  39     141.697  66.535  52.830  1.00 88.91           C  
ANISOU  301  C   THR A  39    13522  10163  10099   -341    885   1095       C  
ATOM    302  O   THR A  39     141.553  66.418  51.610  1.00 77.40           O  
ANISOU  302  O   THR A  39    12170   8650   8589   -321    891   1096       O  
ATOM    303  CB  THR A  39     142.696  64.767  54.289  1.00 81.87           C  
ANISOU  303  CB  THR A  39    12611   9295   9201   -303    952   1134       C  
ATOM    304  OG1 THR A  39     143.433  65.749  55.027  1.00 77.80           O  
ANISOU  304  OG1 THR A  39    11970   8850   8740   -283    940   1127       O  
ATOM    305  CG2 THR A  39     143.542  64.281  53.119  1.00 75.82           C  
ANISOU  305  CG2 THR A  39    11927   8477   8403   -251   1014   1160       C  
ATOM    306  N   GLN A  40     142.134  67.655  53.407  1.00 92.36           N  
ANISOU  306  N   GLN A  40    13880  10628  10587   -345    883   1094       N  
ATOM    307  CA  GLN A  40     142.388  68.867  52.643  1.00 83.68           C  
ANISOU  307  CA  GLN A  40    12836   9472   9486   -342    904   1102       C  
ATOM    308  C   GLN A  40     143.860  69.239  52.553  1.00 74.14           C  
ANISOU  308  C   GLN A  40    11593   8254   8325   -370   1012   1123       C  
ATOM    309  O   GLN A  40     144.196  70.165  51.808  1.00 61.59           O  
ANISOU  309  O   GLN A  40    10088   6588   6727   -397   1078   1136       O  
ATOM    310  CB  GLN A  40     141.614  70.048  53.248  1.00 91.47           C  
ANISOU  310  CB  GLN A  40    13792  10472  10489   -341    828   1064       C  
ATOM    311  CG  GLN A  40     142.161  70.514  54.585  1.00101.83           C  
ANISOU  311  CG  GLN A  40    14975  11842  11875   -376    829   1043       C  
ATOM    312  CD  GLN A  40     141.374  71.667  55.169  1.00 98.66           C  
ANISOU  312  CD  GLN A  40    14564  11443  11480   -361    756    999       C  
ATOM    313  OE1 GLN A  40     140.153  71.595  55.300  1.00 87.99           O  
ANISOU  313  OE1 GLN A  40    13204  10134  10093   -319    678    964       O  
ATOM    314  NE2 GLN A  40     142.071  72.744  55.516  1.00100.63           N  
ANISOU  314  NE2 GLN A  40    14808  11653  11774   -400    787    982       N  
ATOM    315  N   SER A  41     144.740  68.565  53.285  1.00 89.44           N  
ANISOU  315  N   SER A  41    13413  10267  10302   -362   1040   1114       N  
ATOM    316  CA  SER A  41     146.159  68.883  53.250  1.00103.35           C  
ANISOU  316  CA  SER A  41    15080  12067  12120   -388   1136   1093       C  
ATOM    317  C   SER A  41     146.912  67.855  52.414  1.00 81.79           C  
ANISOU  317  C   SER A  41    12383   9341   9354   -332   1220   1115       C  
ATOM    318  O   SER A  41     146.488  66.708  52.254  1.00 72.71           O  
ANISOU  318  O   SER A  41    11313   8173   8141   -260   1187   1144       O  
ATOM    319  CB  SER A  41     146.747  68.952  54.664  1.00113.86           C  
ANISOU  319  CB  SER A  41    16231  13518  13514   -378   1086   1033       C  
ATOM    320  OG  SER A  41     146.822  67.670  55.258  1.00116.31           O  
ANISOU  320  OG  SER A  41    16524  13888  13778   -271   1041   1044       O  
ATOM    321  N   GLY A  42     148.049  68.290  51.879  1.00 95.42           N  
ANISOU  321  N   GLY A  42    14049  11086  11119   -376   1345   1091       N  
ATOM    322  CA  GLY A  42     148.857  67.462  51.008  1.00 94.33           C  
ANISOU  322  CA  GLY A  42    13932  10965  10945   -316   1449   1101       C  
ATOM    323  C   GLY A  42     149.545  68.278  49.934  1.00 84.27           C  
ANISOU  323  C   GLY A  42    12697   9640   9680   -412   1623   1099       C  
ATOM    324  O   GLY A  42     150.084  67.729  48.969  1.00 91.95           O  
ANISOU  324  O   GLY A  42    13729  10605  10604   -369   1735   1115       O  
ATOM    325  N   PHE A  43     149.529  69.601  50.094  1.00 76.94           N  
ANISOU  325  N   PHE A  43    11765   8663   8807   -543   1663   1080       N  
ATOM    326  CA  PHE A  43     150.160  70.506  49.144  1.00 77.42           C  
ANISOU  326  CA  PHE A  43    11908   8639   8870   -669   1863   1082       C  
ATOM    327  C   PHE A  43     151.622  70.788  49.464  1.00 83.45           C  
ANISOU  327  C   PHE A  43    12416   9537   9753   -782   2007    970       C  
ATOM    328  O   PHE A  43     152.308  71.411  48.645  1.00 74.12           O  
ANISOU  328  O   PHE A  43    11282   8298   8582   -914   2222    957       O  
ATOM    329  CB  PHE A  43     149.399  71.833  49.091  1.00 83.53           C  
ANISOU  329  CB  PHE A  43    12861   9252   9625   -755   1854   1114       C  
ATOM    330  CG  PHE A  43     147.937  71.682  48.801  1.00 90.90           C  
ANISOU  330  CG  PHE A  43    14003  10092  10445   -632   1698   1187       C  
ATOM    331  CD1 PHE A  43     147.490  71.508  47.504  1.00 92.71           C  
ANISOU  331  CD1 PHE A  43    14481  10208  10537   -557   1737   1257       C  
ATOM    332  CD2 PHE A  43     147.008  71.719  49.825  1.00 90.55           C  
ANISOU  332  CD2 PHE A  43    13892  10088  10423   -586   1512   1167       C  
ATOM    333  CE1 PHE A  43     146.143  71.372  47.232  1.00 89.99           C  
ANISOU  333  CE1 PHE A  43    14289   9813  10091   -436   1573   1286       C  
ATOM    334  CE2 PHE A  43     145.660  71.583  49.558  1.00 91.67           C  
ANISOU  334  CE2 PHE A  43    14178  10181  10474   -482   1374   1201       C  
ATOM    335  CZ  PHE A  43     145.229  71.411  48.260  1.00 87.92           C  
ANISOU  335  CZ  PHE A  43    13922   9612   9872   -406   1394   1251       C  
ATOM    336  N   TYR A  44     152.111  70.350  50.619  1.00 93.92           N  
ANISOU  336  N   TYR A  44    13478  11046  11162   -731   1899    877       N  
ATOM    337  CA  TYR A  44     153.459  70.654  51.072  1.00 96.03           C  
ANISOU  337  CA  TYR A  44    13446  11489  11551   -826   1992    725       C  
ATOM    338  C   TYR A  44     154.305  69.389  51.129  1.00 91.64           C  
ANISOU  338  C   TYR A  44    12704  11129  10985   -650   1977    666       C  
ATOM    339  O   TYR A  44     153.793  68.272  51.248  1.00 86.05           O  
ANISOU  339  O   TYR A  44    12091  10418  10186   -450   1849    738       O  
ATOM    340  CB  TYR A  44     153.430  71.323  52.452  1.00 88.21           C  
ANISOU  340  CB  TYR A  44    12288  10576  10651   -884   1856    628       C  
ATOM    341  CG  TYR A  44     152.534  72.538  52.522  1.00 86.47           C  
ANISOU  341  CG  TYR A  44    12266  10160  10429  -1018   1847    679       C  
ATOM    342  CD1 TYR A  44     152.551  73.497  51.517  1.00 90.61           C  
ANISOU  342  CD1 TYR A  44    12988  10497  10941  -1185   2042    720       C  
ATOM    343  CD2 TYR A  44     151.661  72.720  53.588  1.00 80.74           C  
ANISOU  343  CD2 TYR A  44    11558   9426   9695   -956   1651    688       C  
ATOM    344  CE1 TYR A  44     151.730  74.609  51.574  1.00 95.03           C  
ANISOU  344  CE1 TYR A  44    13769  10862  11476  -1265   2026    767       C  
ATOM    345  CE2 TYR A  44     150.835  73.828  53.654  1.00 98.79           C  
ANISOU  345  CE2 TYR A  44    14027  11541  11969  -1043   1636    725       C  
ATOM    346  CZ  TYR A  44     150.874  74.769  52.644  1.00104.74           C  
ANISOU  346  CZ  TYR A  44    14986  12105  12706  -1186   1815    763       C  
ATOM    347  OH  TYR A  44     150.055  75.872  52.704  1.00109.67           O  
ANISOU  347  OH  TYR A  44    15829  12543  13296  -1233   1793    799       O  
ATOM    348  N   ASP A  45     155.618  69.582  51.041  1.00 93.22           N  
ANISOU  348  N   ASP A  45    12640  11501  11279   -727   2118    521       N  
ATOM    349  CA  ASP A  45     156.580  68.490  51.180  1.00 90.65           C  
ANISOU  349  CA  ASP A  45    12089  11405  10950   -532   2098    424       C  
ATOM    350  C   ASP A  45     156.638  68.087  52.647  1.00 85.45           C  
ANISOU  350  C   ASP A  45    11252  10909  10306   -367   1855    341       C  
ATOM    351  O   ASP A  45     157.243  68.776  53.470  1.00 91.24           O  
ANISOU  351  O   ASP A  45    11725  11796  11147   -460   1818    182       O  
ATOM    352  CB  ASP A  45     157.948  68.924  50.665  1.00 85.06           C  
ANISOU  352  CB  ASP A  45    11110  10862  10347   -678   2329    260       C  
ATOM    353  CG  ASP A  45     158.959  67.790  50.648  1.00 87.57           C  
ANISOU  353  CG  ASP A  45    11192  11433  10647   -441   2320    149       C  
ATOM    354  OD1 ASP A  45     158.596  66.647  50.999  1.00 88.25           O  
ANISOU  354  OD1 ASP A  45    11377  11529  10625   -156   2139    217       O  
ATOM    355  OD2 ASP A  45     160.124  68.045  50.278  1.00 87.52           O  
ANISOU  355  OD2 ASP A  45    10907  11614  10731   -540   2506    -17       O  
ATOM    356  N   GLU A  46     156.009  66.956  52.980  1.00 90.96           N  
ANISOU  356  N   GLU A  46    12111  11567  10884   -124   1695    443       N  
ATOM    357  CA  GLU A  46     155.876  66.548  54.374  1.00 95.17           C  
ANISOU  357  CA  GLU A  46    12573  12201  11388     48   1473    402       C  
ATOM    358  C   GLU A  46     157.213  66.191  55.013  1.00 96.29           C  
ANISOU  358  C   GLU A  46    12380  12643  11563    215   1415    205       C  
ATOM    359  O   GLU A  46     157.309  66.162  56.245  1.00100.03           O  
ANISOU  359  O   GLU A  46    12746  13238  12024    335   1234    126       O  
ATOM    360  CB  GLU A  46     154.907  65.368  54.479  1.00 89.01           C  
ANISOU  360  CB  GLU A  46    12086  11275  10458    244   1364    559       C  
ATOM    361  CG  GLU A  46     154.341  65.139  55.871  1.00107.88           C  
ANISOU  361  CG  GLU A  46    14522  13675  12794    358   1171    574       C  
ATOM    362  CD  GLU A  46     153.228  64.110  55.882  1.00118.99           C  
ANISOU  362  CD  GLU A  46    16250  14894  14068    464   1118    732       C  
ATOM    363  OE1 GLU A  46     152.687  63.809  54.797  1.00117.08           O  
ANISOU  363  OE1 GLU A  46    16193  14497  13796    401   1211    827       O  
ATOM    364  OE2 GLU A  46     152.895  63.601  56.974  1.00120.11           O  
ANISOU  364  OE2 GLU A  46    16468  15039  14128    603    992    751       O  
ATOM    365  N   GLY A  47     158.243  65.930  54.213  1.00 95.11           N  
ANISOU  365  N   GLY A  47    12060  12631  11446    243   1559    110       N  
ATOM    366  CA  GLY A  47     159.557  65.635  54.751  1.00 92.93           C  
ANISOU  366  CA  GLY A  47    11418  12683  11210    415   1502   -115       C  
ATOM    367  C   GLY A  47     160.532  66.783  54.590  1.00100.65           C  
ANISOU  367  C   GLY A  47    12029  13844  12368    140   1652   -329       C  
ATOM    368  O   GLY A  47     161.723  66.566  54.348  1.00 88.40           O  
ANISOU  368  O   GLY A  47    10158  12558  10872    207   1729   -521       O  
ATOM    369  N   SER A  48     160.039  68.009  54.726  1.00126.48           N  
ANISOU  369  N   SER A  48    15346  16977  15735   -172   1704   -313       N  
ATOM    370  CA  SER A  48     160.837  69.213  54.549  1.00124.24           C  
ANISOU  370  CA  SER A  48    14782  16797  15626   -501   1881   -505       C  
ATOM    371  C   SER A  48     161.075  69.890  55.896  1.00120.37           C  
ANISOU  371  C   SER A  48    14051  16464  15219   -551   1698   -692       C  
ATOM    372  O   SER A  48     160.586  69.451  56.942  1.00119.80           O  
ANISOU  372  O   SER A  48    14051  16413  15055   -321   1441   -655       O  
ATOM    373  CB  SER A  48     160.157  70.169  53.567  1.00122.58           C  
ANISOU  373  CB  SER A  48    14860  16271  15443   -827   2111   -350       C  
ATOM    374  OG  SER A  48     158.893  70.586  54.052  1.00117.98           O  
ANISOU  374  OG  SER A  48    14572  15448  14806   -855   1974   -190       O  
ATOM    375  N   GLN A  49     161.839  70.983  55.856  1.00110.90           N  
ANISOU  375  N   GLN A  49    12577  15368  14190   -871   1848   -904       N  
ATOM    376  CA  GLN A  49     162.163  71.723  57.070  1.00104.28           C  
ANISOU  376  CA  GLN A  49    11484  14691  13446   -958   1689  -1124       C  
ATOM    377  C   GLN A  49     161.008  72.612  57.516  1.00 99.18           C  
ANISOU  377  C   GLN A  49    11152  13748  12786  -1121   1630   -979       C  
ATOM    378  O   GLN A  49     160.725  72.711  58.715  1.00 90.35           O  
ANISOU  378  O   GLN A  49    10000  12693  11635  -1005   1387  -1036       O  
ATOM    379  CB  GLN A  49     163.427  72.555  56.848  1.00 91.63           C  
ANISOU  379  CB  GLN A  49     9460  13311  12044  -1275   1888  -1436       C  
ATOM    380  CG  GLN A  49     163.755  73.514  57.977  1.00 94.44           C  
ANISOU  380  CG  GLN A  49     9563  13801  12519  -1450   1758  -1691       C  
ATOM    381  CD  GLN A  49     165.042  74.277  57.736  1.00104.09           C  
ANISOU  381  CD  GLN A  49    10337  15260  13953  -1795   1973  -2035       C  
ATOM    382  OE1 GLN A  49     165.169  75.441  58.119  1.00 99.29           O  
ANISOU  382  OE1 GLN A  49     9648  14599  13477  -2140   2033  -2194       O  
ATOM    383  NE2 GLN A  49     166.004  73.624  57.096  1.00102.98           N  
ANISOU  383  NE2 GLN A  49     9899  15381  13846  -1713   2101  -2164       N  
ATOM    384  N   SER A  50     160.331  73.265  56.566  1.00 99.40           N  
ANISOU  384  N   SER A  50    11496  13453  12818  -1363   1846   -797       N  
ATOM    385  CA  SER A  50     159.215  74.139  56.918  1.00 93.24           C  
ANISOU  385  CA  SER A  50    11022  12392  12014  -1489   1794   -666       C  
ATOM    386  C   SER A  50     158.075  73.364  57.566  1.00 92.12           C  
ANISOU  386  C   SER A  50    11117  12171  11714  -1181   1541   -474       C  
ATOM    387  O   SER A  50     157.361  73.908  58.417  1.00 82.28           O  
ANISOU  387  O   SER A  50     9979  10834  10448  -1193   1401   -455       O  
ATOM    388  CB  SER A  50     158.718  74.880  55.676  1.00 95.61           C  
ANISOU  388  CB  SER A  50    11648  12366  12312  -1741   2065   -502       C  
ATOM    389  OG  SER A  50     158.295  73.974  54.674  1.00 81.67           O  
ANISOU  389  OG  SER A  50    10102  10504  10426  -1572   2129   -295       O  
ATOM    390  N   VAL A  51     157.882  72.102  57.176  1.00 98.74           N  
ANISOU  390  N   VAL A  51    12049  13033  12435   -916   1498   -339       N  
ATOM    391  CA  VAL A  51     156.883  71.269  57.838  1.00 96.41           C  
ANISOU  391  CA  VAL A  51    11966  12674  11993   -644   1285   -180       C  
ATOM    392  C   VAL A  51     157.379  70.843  59.213  1.00 89.44           C  
ANISOU  392  C   VAL A  51    10860  12043  11079   -422   1050   -335       C  
ATOM    393  O   VAL A  51     156.619  70.840  60.189  1.00 85.30           O  
ANISOU  393  O   VAL A  51    10464  11469  10477   -319    879   -280       O  
ATOM    394  CB  VAL A  51     156.529  70.058  56.957  1.00 84.73           C  
ANISOU  394  CB  VAL A  51    10687  11110  10396   -458   1331      0       C  
ATOM    395  CG1 VAL A  51     155.636  69.088  57.715  1.00 90.46           C  
ANISOU  395  CG1 VAL A  51    11608  11787  10974   -196   1133    131       C  
ATOM    396  CG2 VAL A  51     155.845  70.522  55.688  1.00 77.07           C  
ANISOU  396  CG2 VAL A  51     9985   9877   9420   -644   1521    160       C  
ATOM    397  N   ALA A  52     158.660  70.477  59.313  1.00 91.71           N  
ANISOU  397  N   ALA A  52    10812  12619  11414   -327   1037   -541       N  
ATOM    398  CA  ALA A  52     159.246  70.178  60.614  1.00 90.42           C  
ANISOU  398  CA  ALA A  52    10417  12727  11212    -96    796   -727       C  
ATOM    399  C   ALA A  52     159.147  71.378  61.545  1.00 91.26           C  
ANISOU  399  C   ALA A  52    10426  12849  11400   -288    710   -868       C  
ATOM    400  O   ALA A  52     158.858  71.228  62.738  1.00 92.17           O  
ANISOU  400  O   ALA A  52    10573  13029  11418    -97    486   -895       O  
ATOM    401  CB  ALA A  52     160.702  69.745  60.448  1.00 83.77           C  
ANISOU  401  CB  ALA A  52     9179  12223  10425     20    806   -971       C  
ATOM    402  N   ALA A  53     159.376  72.581  61.013  1.00 96.92           N  
ANISOU  402  N   ALA A  53    11056  13486  12282   -665    897   -958       N  
ATOM    403  CA  ALA A  53     159.232  73.790  61.816  1.00 95.62           C  
ANISOU  403  CA  ALA A  53    10846  13289  12197   -876    836  -1089       C  
ATOM    404  C   ALA A  53     157.792  73.991  62.269  1.00 92.43           C  
ANISOU  404  C   ALA A  53    10822  12617  11682   -827    747   -865       C  
ATOM    405  O   ALA A  53     157.548  74.629  63.299  1.00 84.43           O  
ANISOU  405  O   ALA A  53     9799  11616  10665   -848    605   -958       O  
ATOM    406  CB  ALA A  53     159.717  75.005  61.025  1.00 91.98           C  
ANISOU  406  CB  ALA A  53    10294  12734  11921  -1308   1100  -1205       C  
ATOM    407  N   SER A  54     156.829  73.458  61.517  1.00100.32           N  
ANISOU  407  N   SER A  54    12140  13388  12588   -760    826   -591       N  
ATOM    408  CA  SER A  54     155.431  73.553  61.920  1.00104.74           C  
ANISOU  408  CA  SER A  54    13022  13732  13044   -700    745   -397       C  
ATOM    409  C   SER A  54     155.078  72.493  62.957  1.00103.03           C  
ANISOU  409  C   SER A  54    12860  13621  12667   -366    532   -344       C  
ATOM    410  O   SER A  54     154.304  72.761  63.882  1.00100.36           O  
ANISOU  410  O   SER A  54    12648  13225  12257   -312    412   -310       O  
ATOM    411  CB  SER A  54     154.524  73.430  60.695  1.00103.35           C  
ANISOU  411  CB  SER A  54    13143  13293  12833   -768    905   -159       C  
ATOM    412  OG  SER A  54     154.831  74.426  59.733  1.00104.60           O  
ANISOU  412  OG  SER A  54    13314  13323  13104  -1057   1116   -191       O  
ATOM    413  N   LEU A  55     155.635  71.287  62.818  1.00102.15           N  
ANISOU  413  N   LEU A  55    12682  13650  12482   -132    496   -335       N  
ATOM    414  CA  LEU A  55     155.377  70.235  63.796  1.00104.62           C  
ANISOU  414  CA  LEU A  55    13097  14036  12617    200    314   -281       C  
ATOM    415  C   LEU A  55     156.005  70.571  65.144  1.00103.07           C  
ANISOU  415  C   LEU A  55    12697  14069  12396    319    112   -499       C  
ATOM    416  O   LEU A  55     155.374  70.391  66.192  1.00 94.17           O  
ANISOU  416  O   LEU A  55    11731  12916  11132    476    -26   -447       O  
ATOM    417  CB  LEU A  55     155.900  68.895  63.276  1.00 98.27           C  
ANISOU  417  CB  LEU A  55    12302  13307  11729    439    330   -231       C  
ATOM    418  CG  LEU A  55     155.302  68.389  61.961  1.00 94.10           C  
ANISOU  418  CG  LEU A  55    11993  12564  11198    362    508    -27       C  
ATOM    419  CD1 LEU A  55     155.957  67.083  61.543  1.00 95.22           C  
ANISOU  419  CD1 LEU A  55    12134  12796  11251    620    511    -12       C  
ATOM    420  CD2 LEU A  55     153.797  68.223  62.083  1.00 84.71           C  
ANISOU  420  CD2 LEU A  55    11142  11126   9917    338    511    188       C  
ATOM    421  N   ILE A  56     157.248  71.059  65.134  1.00 99.05           N  
ANISOU  421  N   ILE A  56    11828  13795  12012    241     97   -758       N  
ATOM    422  CA  ILE A  56     157.906  71.444  66.378  1.00 89.26           C  
ANISOU  422  CA  ILE A  56    10357  12802  10757    344   -114  -1010       C  
ATOM    423  C   ILE A  56     157.203  72.639  67.007  1.00 89.98           C  
ANISOU  423  C   ILE A  56    10540  12758  10891    131   -140  -1031       C  
ATOM    424  O   ILE A  56     156.987  72.679  68.224  1.00 89.46           O  
ANISOU  424  O   ILE A  56    10520  12764  10707    301   -332  -1089       O  
ATOM    425  CB  ILE A  56     159.396  71.738  66.123  1.00 92.07           C  
ANISOU  425  CB  ILE A  56    10259  13460  11265    265   -106  -1321       C  
ATOM    426  CG1 ILE A  56     160.106  70.503  65.570  1.00 85.13           C  
ANISOU  426  CG1 ILE A  56     9285  12740  10321    536    -98  -1314       C  
ATOM    427  CG2 ILE A  56     160.071  72.213  67.402  1.00 96.35           C  
ANISOU  427  CG2 ILE A  56    10533  14277  11798    355   -344  -1622       C  
ATOM    428  CD1 ILE A  56     161.554  70.751  65.200  1.00 88.62           C  
ANISOU  428  CD1 ILE A  56     9245  13504  10922    452    -58  -1630       C  
ATOM    429  N   GLY A  57     156.830  73.627  66.190  1.00 89.86           N  
ANISOU  429  N   GLY A  57    10582  12534  11025   -222     55   -984       N  
ATOM    430  CA  GLY A  57     156.203  74.824  66.728  1.00 78.73           C  
ANISOU  430  CA  GLY A  57     9275  10983   9657   -416     39  -1017       C  
ATOM    431  C   GLY A  57     154.850  74.552  67.356  1.00 77.36           C  
ANISOU  431  C   GLY A  57     9434  10641   9317   -253    -39   -802       C  
ATOM    432  O   GLY A  57     154.520  75.105  68.408  1.00 77.52           O  
ANISOU  432  O   GLY A  57     9494  10675   9285   -223   -168   -879       O  
ATOM    433  N   ASP A  58     154.044  73.700  66.717  1.00 86.61           N  
ANISOU  433  N   ASP A  58    10842  11659  10405   -158     47   -547       N  
ATOM    434  CA  ASP A  58     152.753  73.342  67.296  1.00 99.63           C  
ANISOU  434  CA  ASP A  58    12780  13172  11903    -20     -2   -360       C  
ATOM    435  C   ASP A  58     152.917  72.486  68.545  1.00103.47           C  
ANISOU  435  C   ASP A  58    13285  13822  12206    298   -187   -393       C  
ATOM    436  O   ASP A  58     152.076  72.546  69.450  1.00 98.38           O  
ANISOU  436  O   ASP A  58    12818  13121  11440    387   -254   -332       O  
ATOM    437  CB  ASP A  58     151.893  72.610  66.265  1.00104.74           C  
ANISOU  437  CB  ASP A  58    13649  13632  12517    -23    140   -114       C  
ATOM    438  CG  ASP A  58     151.331  73.540  65.209  1.00 99.39           C  
ANISOU  438  CG  ASP A  58    13058  12749  11957   -287    297    -46       C  
ATOM    439  OD1 ASP A  58     151.832  74.677  65.084  1.00102.84           O  
ANISOU  439  OD1 ASP A  58    13380  13176  12518   -489    337   -186       O  
ATOM    440  OD2 ASP A  58     150.378  73.136  64.511  1.00 91.44           O  
ANISOU  440  OD2 ASP A  58    12250  11583  10908   -288    381    137       O  
ATOM    441  N   GLU A  59     153.985  71.691  68.615  1.00114.60           N  
ANISOU  441  N   GLU A  59    14532  15436  13577    493   -267   -491       N  
ATOM    442  CA  GLU A  59     154.202  70.850  69.787  1.00119.10           C  
ANISOU  442  CA  GLU A  59    15163  16153  13937    844   -453   -522       C  
ATOM    443  C   GLU A  59     154.599  71.685  70.999  1.00116.95           C  
ANISOU  443  C   GLU A  59    14744  16048  13644    880   -638   -751       C  
ATOM    444  O   GLU A  59     154.215  71.370  72.131  1.00127.48           O  
ANISOU  444  O   GLU A  59    16250  17406  14780   1110   -767   -726       O  
ATOM    445  CB  GLU A  59     155.272  69.802  69.483  1.00126.13           C  
ANISOU  445  CB  GLU A  59    15922  17223  14779   1084   -502   -583       C  
ATOM    446  CG  GLU A  59     155.280  68.614  70.431  1.00134.79           C  
ANISOU  446  CG  GLU A  59    17224  18381  15607   1499   -649   -522       C  
ATOM    447  CD  GLU A  59     156.430  67.665  70.157  1.00146.20           C  
ANISOU  447  CD  GLU A  59    18527  20025  16997   1777   -723   -616       C  
ATOM    448  OE1 GLU A  59     157.571  67.983  70.555  1.00150.22           O  
ANISOU  448  OE1 GLU A  59    18702  20830  17542   1882   -883   -892       O  
ATOM    449  OE2 GLU A  59     156.197  66.609  69.533  1.00147.57           O  
ANISOU  449  OE2 GLU A  59    18912  20066  17092   1893   -623   -433       O  
ATOM    450  N   VAL A  60     155.357  72.756  70.781  1.00 99.15           N  
ANISOU  450  N   VAL A  60    12191  13899  11582    643   -640   -982       N  
ATOM    451  CA  VAL A  60     155.883  73.562  71.878  1.00 85.04           C  
ANISOU  451  CA  VAL A  60    10224  12294   9792    657   -828  -1250       C  
ATOM    452  C   VAL A  60     154.951  74.715  72.222  1.00 90.91           C  
ANISOU  452  C   VAL A  60    11121  12843  10578    434   -785  -1222       C  
ATOM    453  O   VAL A  60     154.568  74.892  73.381  1.00 99.11           O  
ANISOU  453  O   VAL A  60    12274  13912  11473    582   -929  -1262       O  
ATOM    454  CB  VAL A  60     157.297  74.069  71.525  1.00 84.38           C  
ANISOU  454  CB  VAL A  60     9706  12457   9899    507   -854  -1564       C  
ATOM    455  CG1 VAL A  60     157.827  74.972  72.630  1.00 96.57           C  
ANISOU  455  CG1 VAL A  60    11047  14188  11457    480  -1051  -1876       C  
ATOM    456  CG2 VAL A  60     158.235  72.896  71.286  1.00 85.93           C  
ANISOU  456  CG2 VAL A  60     9734  12886  10031    790   -922  -1616       C  
ATOM    457  N   TYR A  61     154.569  75.514  71.228  1.00 88.26           N  
ANISOU  457  N   TYR A  61    10815  12298  10420    101   -586  -1155       N  
ATOM    458  CA  TYR A  61     153.763  76.703  71.471  1.00 90.89           C  
ANISOU  458  CA  TYR A  61    11294  12441  10799   -100   -544  -1152       C  
ATOM    459  C   TYR A  61     152.264  76.453  71.367  1.00 87.13           C  
ANISOU  459  C   TYR A  61    11159  11731  10216    -42   -455   -866       C  
ATOM    460  O   TYR A  61     151.482  77.290  71.831  1.00 74.96           O  
ANISOU  460  O   TYR A  61     9760  10066   8657   -110   -460   -862       O  
ATOM    461  CB  TYR A  61     154.171  77.819  70.502  1.00 81.13           C  
ANISOU  461  CB  TYR A  61     9943  11088   9793   -480   -377  -1254       C  
ATOM    462  CG  TYR A  61     155.476  78.486  70.874  1.00 82.42           C  
ANISOU  462  CG  TYR A  61     9769  11465  10085   -624   -459  -1603       C  
ATOM    463  CD1 TYR A  61     156.695  77.919  70.524  1.00 84.27           C  
ANISOU  463  CD1 TYR A  61     9681  11946  10390   -598   -473  -1758       C  
ATOM    464  CD2 TYR A  61     155.489  79.676  71.589  1.00 83.83           C  
ANISOU  464  CD2 TYR A  61     9935  11608  10311   -784   -526  -1801       C  
ATOM    465  CE1 TYR A  61     157.893  78.524  70.872  1.00 87.73           C  
ANISOU  465  CE1 TYR A  61     9760  12617  10957   -745   -549  -2117       C  
ATOM    466  CE2 TYR A  61     156.678  80.288  71.939  1.00 87.24           C  
ANISOU  466  CE2 TYR A  61    10036  12242  10868   -946   -601  -2153       C  
ATOM    467  CZ  TYR A  61     157.876  79.709  71.578  1.00 89.23           C  
ANISOU  467  CZ  TYR A  61     9938  12763  11202   -934   -612  -2318       C  
ATOM    468  OH  TYR A  61     159.059  80.317  71.926  1.00 92.98           O  
ANISOU  468  OH  TYR A  61    10039  13475  11815  -1111   -686  -2705       O  
ATOM    469  N   GLY A  62     151.845  75.338  70.787  1.00 92.57           N  
ANISOU  469  N   GLY A  62    11973  12365  10834     79   -375   -649       N  
ATOM    470  CA  GLY A  62     150.421  75.049  70.708  1.00 94.93           C  
ANISOU  470  CA  GLY A  62    12555  12475  11039    117   -290   -412       C  
ATOM    471  C   GLY A  62     149.796  75.543  69.419  1.00 94.95           C  
ANISOU  471  C   GLY A  62    12643  12265  11170   -110   -111   -289       C  
ATOM    472  O   GLY A  62     150.220  76.531  68.820  1.00 96.00           O  
ANISOU  472  O   GLY A  62    12690  12333  11452   -332    -45   -386       O  
ATOM    473  N   ARG A  63     148.755  74.834  68.989  1.00 92.93           N  
ANISOU  473  N   ARG A  63    12576  11892  10843    -53    -26    -79       N  
ATOM    474  CA  ARG A  63     148.059  75.183  67.759  1.00 83.11           C  
ANISOU  474  CA  ARG A  63    11432  10461   9684   -214    119     40       C  
ATOM    475  C   ARG A  63     147.310  76.500  67.923  1.00 87.70           C  
ANISOU  475  C   ARG A  63    12105  10917  10302   -325    127      3       C  
ATOM    476  O   ARG A  63     146.687  76.755  68.958  1.00 81.42           O  
ANISOU  476  O   ARG A  63    11373  10144   9418   -235     51    -23       O  
ATOM    477  CB  ARG A  63     147.089  74.068  67.366  1.00 80.33           C  
ANISOU  477  CB  ARG A  63    11237  10044   9240   -119    184    236       C  
ATOM    478  CG  ARG A  63     146.278  74.351  66.110  1.00114.17           C  
ANISOU  478  CG  ARG A  63    15628  14163  13589   -245    302    345       C  
ATOM    479  CD  ARG A  63     145.255  73.255  65.845  1.00130.03           C  
ANISOU  479  CD  ARG A  63    17765  16130  15509   -169    352    497       C  
ATOM    480  NE  ARG A  63     145.880  71.965  65.564  1.00138.04           N  
ANISOU  480  NE  ARG A  63    18772  17193  16483    -86    373    552       N  
ATOM    481  CZ  ARG A  63     146.228  71.550  64.350  1.00140.93           C  
ANISOU  481  CZ  ARG A  63    19136  17508  16903   -138    451    605       C  
ATOM    482  NH1 ARG A  63     146.015  72.326  63.295  1.00142.55           N  
ANISOU  482  NH1 ARG A  63    19359  17609  17195   -274    517    617       N  
ATOM    483  NH2 ARG A  63     146.791  70.360  64.189  1.00139.55           N  
ANISOU  483  NH2 ARG A  63    18970  17376  16676    -34    463    647       N  
ATOM    484  N   ASP A  64     147.377  77.342  66.893  1.00 95.30           N  
ANISOU  484  N   ASP A  64    13099  11733  11377   -506    228      1       N  
ATOM    485  CA  ASP A  64     146.700  78.633  66.903  1.00 86.46           C  
ANISOU  485  CA  ASP A  64    12113  10457  10281   -594    246    -30       C  
ATOM    486  C   ASP A  64     145.292  78.470  66.347  1.00 86.25           C  
ANISOU  486  C   ASP A  64    12265  10317  10190   -521    293    132       C  
ATOM    487  O   ASP A  64     145.118  78.107  65.179  1.00 87.72           O  
ANISOU  487  O   ASP A  64    12508  10424  10397   -555    382    240       O  
ATOM    488  CB  ASP A  64     147.480  79.665  66.092  1.00 90.32           C  
ANISOU  488  CB  ASP A  64    12600  10817  10900   -820    347   -116       C  
ATOM    489  CG  ASP A  64     146.738  80.982  65.959  1.00 93.62           C  
ANISOU  489  CG  ASP A  64    13232  11021  11320   -887    381   -125       C  
ATOM    490  OD1 ASP A  64     146.251  81.500  66.986  1.00 81.46           O  
ANISOU  490  OD1 ASP A  64    11733   9494   9726   -812    283   -196       O  
ATOM    491  OD2 ASP A  64     146.646  81.503  64.826  1.00 96.91           O  
ANISOU  491  OD2 ASP A  64    13799  11249  11775   -995    508    -61       O  
ATOM    492  N   ARG A  65     144.291  78.740  67.184  1.00 93.25           N  
ANISOU  492  N   ARG A  65    13226  11211  10992   -414    231    129       N  
ATOM    493  CA  ARG A  65     142.892  78.669  66.785  1.00 85.92           C  
ANISOU  493  CA  ARG A  65    12421  10219  10005   -337    261    235       C  
ATOM    494  C   ARG A  65     142.242  80.044  66.688  1.00 83.27           C  
ANISOU  494  C   ARG A  65    12225   9740   9672   -341    254    185       C  
ATOM    495  O   ARG A  65     141.016  80.132  66.558  1.00 73.59           O  
ANISOU  495  O   ARG A  65    11077   8498   8386   -237    250    231       O  
ATOM    496  CB  ARG A  65     142.112  77.786  67.761  1.00 79.53           C  
ANISOU  496  CB  ARG A  65    11587   9545   9086   -199    225    272       C  
ATOM    497  CG  ARG A  65     142.982  77.038  68.756  1.00 94.58           C  
ANISOU  497  CG  ARG A  65    13402  11591  10942   -143    170    232       C  
ATOM    498  CD  ARG A  65     142.148  76.124  69.641  1.00111.32           C  
ANISOU  498  CD  ARG A  65    15567  13802  12929    -15    177    294       C  
ATOM    499  NE  ARG A  65     141.701  74.931  68.928  1.00117.53           N  
ANISOU  499  NE  ARG A  65    16382  14577  13698    -20    265    425       N  
ATOM    500  CZ  ARG A  65     142.303  73.749  69.005  1.00110.73           C  
ANISOU  500  CZ  ARG A  65    15523  13761  12787     27    280    482       C  
ATOM    501  NH1 ARG A  65     143.376  73.600  69.770  1.00119.27           N  
ANISOU  501  NH1 ARG A  65    16561  14929  13825    110    198    416       N  
ATOM    502  NH2 ARG A  65     141.832  72.714  68.321  1.00 82.19           N  
ANISOU  502  NH2 ARG A  65    11961  10108   9158      6    369    591       N  
ATOM    503  N   THR A  66     143.034  81.118  66.743  1.00 85.20           N  
ANISOU  503  N   THR A  66    12507   9882   9983   -457    257     78       N  
ATOM    504  CA  THR A  66     142.480  82.466  66.673  1.00 94.24           C  
ANISOU  504  CA  THR A  66    13840  10851  11115   -452    257     28       C  
ATOM    505  C   THR A  66     142.046  82.848  65.263  1.00 96.57           C  
ANISOU  505  C   THR A  66    14320  10961  11412   -463    342    125       C  
ATOM    506  O   THR A  66     141.177  83.712  65.103  1.00 93.46           O  
ANISOU  506  O   THR A  66    14113  10440  10958   -361    325    122       O  
ATOM    507  CB  THR A  66     143.497  83.486  67.190  1.00 91.20           C  
ANISOU  507  CB  THR A  66    13464  10388  10799   -604    250   -133       C  
ATOM    508  OG1 THR A  66     144.747  83.306  66.510  1.00 88.41           O  
ANISOU  508  OG1 THR A  66    13019  10019  10554   -799    336   -155       O  
ATOM    509  CG2 THR A  66     143.710  83.321  68.690  1.00 84.66           C  
ANISOU  509  CG2 THR A  66    12499   9738   9929   -537    130   -252       C  
ATOM    510  N   SER A  67     142.630  82.227  64.240  1.00104.04           N  
ANISOU  510  N   SER A  67    15234  11891  12406   -555    426    205       N  
ATOM    511  CA  SER A  67     142.306  82.523  62.853  1.00 91.49           C  
ANISOU  511  CA  SER A  67    13840  10126  10794   -554    509    301       C  
ATOM    512  C   SER A  67     141.275  81.566  62.270  1.00 78.72           C  
ANISOU  512  C   SER A  67    12201   8602   9107   -400    475    411       C  
ATOM    513  O   SER A  67     140.996  81.635  61.070  1.00 73.11           O  
ANISOU  513  O   SER A  67    11640   7779   8360   -371    523    488       O  
ATOM    514  CB  SER A  67     143.576  82.501  62.000  1.00 98.56           C  
ANISOU  514  CB  SER A  67    14736  10938  11776   -758    645    310       C  
ATOM    515  OG  SER A  67     144.235  81.250  62.097  1.00112.03           O  
ANISOU  515  OG  SER A  67    16201  12838  13528   -790    644    328       O  
ATOM    516  N   HIS A  68     140.706  80.677  63.091  1.00 79.82           N  
ANISOU  516  N   HIS A  68    12171   8940   9219   -309    402    409       N  
ATOM    517  CA  HIS A  68     139.705  79.733  62.602  1.00 73.58           C  
ANISOU  517  CA  HIS A  68    11338   8243   8374   -204    384    483       C  
ATOM    518  C   HIS A  68     138.499  80.462  62.022  1.00 73.52           C  
ANISOU  518  C   HIS A  68    11478   8163   8292    -53    339    478       C  
ATOM    519  O   HIS A  68     138.112  80.237  60.869  1.00 78.33           O  
ANISOU  519  O   HIS A  68    12167   8730   8867     -5    348    536       O  
ATOM    520  CB  HIS A  68     139.270  78.794  63.729  1.00 84.23           C  
ANISOU  520  CB  HIS A  68    12516   9789   9697   -158    346    467       C  
ATOM    521  CG  HIS A  68     140.276  77.737  64.063  1.00 83.40           C  
ANISOU  521  CG  HIS A  68    12293   9769   9626   -239    377    497       C  
ATOM    522  ND1 HIS A  68     140.024  76.733  64.974  1.00 80.23           N  
ANISOU  522  ND1 HIS A  68    11798   9509   9177   -197    368    508       N  
ATOM    523  CD2 HIS A  68     141.534  77.525  63.608  1.00 87.00           C  
ANISOU  523  CD2 HIS A  68    12720  10190  10144   -341    422    510       C  
ATOM    524  CE1 HIS A  68     141.083  75.948  65.065  1.00 82.68           C  
ANISOU  524  CE1 HIS A  68    12048   9859   9507   -239    387    532       C  
ATOM    525  NE2 HIS A  68     142.013  76.407  64.247  1.00 84.89           N  
ANISOU  525  NE2 HIS A  68    12340  10052   9861   -325    415    524       N  
ATOM    526  N   VAL A  69     137.884  81.338  62.815  1.00 84.05           N  
ANISOU  526  N   VAL A  69    12854   9495   9586     49    278    398       N  
ATOM    527  CA  VAL A  69     136.733  82.125  62.387  1.00 82.05           C  
ANISOU  527  CA  VAL A  69    12739   9190   9246    243    215    368       C  
ATOM    528  C   VAL A  69     136.903  83.548  62.900  1.00 79.83           C  
ANISOU  528  C   VAL A  69    12645   8744   8942    281    199    296       C  
ATOM    529  O   VAL A  69     137.214  83.754  64.078  1.00 84.72           O  
ANISOU  529  O   VAL A  69    13187   9414   9589    233    186    226       O  
ATOM    530  CB  VAL A  69     135.401  81.539  62.899  1.00 78.92           C  
ANISOU  530  CB  VAL A  69    12161   9020   8803    383    152    317       C  
ATOM    531  CG1 VAL A  69     134.228  82.354  62.373  1.00 82.27           C  
ANISOU  531  CG1 VAL A  69    12699   9426   9134    620     66    259       C  
ATOM    532  CG2 VAL A  69     135.256  80.073  62.505  1.00 77.46           C  
ANISOU  532  CG2 VAL A  69    11803   8981   8647    304    186    373       C  
ATOM    533  N   VAL A  70     136.704  84.528  62.021  1.00 74.37           N  
ANISOU  533  N   VAL A  70    12231   7843   8185    379    199    311       N  
ATOM    534  CA  VAL A  70     136.598  85.931  62.408  1.00 80.68           C  
ANISOU  534  CA  VAL A  70    13270   8454   8930    464    179    239       C  
ATOM    535  C   VAL A  70     135.257  86.450  61.903  1.00 79.20           C  
ANISOU  535  C   VAL A  70    13227   8260   8606    779     80    217       C  
ATOM    536  O   VAL A  70     134.966  86.376  60.703  1.00 76.42           O  
ANISOU  536  O   VAL A  70    13010   7840   8185    879     72    282       O  
ATOM    537  CB  VAL A  70     137.768  86.776  61.875  1.00 79.36           C  
ANISOU  537  CB  VAL A  70    13372   7984   8797    277    298    265       C  
ATOM    538  CG1 VAL A  70     139.009  86.527  62.710  1.00 77.19           C  
ANISOU  538  CG1 VAL A  70    12915   7756   8656      3    360    213       C  
ATOM    539  CG2 VAL A  70     138.050  86.462  60.418  1.00 89.49           C  
ANISOU  539  CG2 VAL A  70    14791   9156  10056    240    379    382       C  
ATOM    540  N   ALA A  71     134.437  86.955  62.821  1.00 86.55           N  
ANISOU  540  N   ALA A  71    14123   9278   9485    957     -4    113       N  
ATOM    541  CA  ALA A  71     133.074  87.376  62.523  1.00 88.72           C  
ANISOU  541  CA  ALA A  71    14458   9621   9630   1294   -119     52       C  
ATOM    542  C   ALA A  71     132.969  88.885  62.683  1.00 88.96           C  
ANISOU  542  C   ALA A  71    14848   9393   9560   1465   -145     -3       C  
ATOM    543  O   ALA A  71     133.207  89.414  63.773  1.00 95.67           O  
ANISOU  543  O   ALA A  71    15707  10210  10435   1416   -136    -79       O  
ATOM    544  CB  ALA A  71     132.074  86.666  63.435  1.00 83.01           C  
ANISOU  544  CB  ALA A  71    13379   9243   8918   1386   -179    -42       C  
ATOM    545  N   ILE A  72     132.603  89.572  61.605  1.00 91.53           N  
ANISOU  545  N   ILE A  72    15499   9525   9754   1681   -182     30       N  
ATOM    546  CA  ILE A  72     132.477  91.025  61.609  1.00 85.30           C  
ANISOU  546  CA  ILE A  72    15136   8437   8838   1874   -199     -9       C  
ATOM    547  C   ILE A  72     131.040  91.373  61.981  1.00 92.18           C  
ANISOU  547  C   ILE A  72    15941   9499   9583   2283   -361   -137       C  
ATOM    548  O   ILE A  72     130.106  91.081  61.230  1.00 97.34           O  
ANISOU  548  O   ILE A  72    16532  10311  10143   2550   -472   -155       O  
ATOM    549  CB  ILE A  72     132.864  91.625  60.253  1.00 95.23           C  
ANISOU  549  CB  ILE A  72    16848   9351   9985   1919   -137    102       C  
ATOM    550  CG1 ILE A  72     134.299  91.234  59.889  1.00 98.44           C  
ANISOU  550  CG1 ILE A  72    17272   9605  10528   1495     49    210       C  
ATOM    551  CG2 ILE A  72     132.698  93.139  60.275  1.00 86.28           C  
ANISOU  551  CG2 ILE A  72    16218   7868   8697   2133   -141     66       C  
ATOM    552  CD1 ILE A  72     134.759  91.769  58.548  1.00 99.75           C  
ANISOU  552  CD1 ILE A  72    17892   9425  10582   1495    158    329       C  
ATOM    553  N   LEU A  73     130.864  92.002  63.140  1.00101.73           N  
ANISOU  553  N   LEU A  73    17152  10713  10790   2340   -380   -244       N  
ATOM    554  CA  LEU A  73     129.550  92.377  63.647  1.00 98.29           C  
ANISOU  554  CA  LEU A  73    16627  10477  10241   2724   -515   -387       C  
ATOM    555  C   LEU A  73     129.320  93.867  63.431  1.00100.70           C  
ANISOU  555  C   LEU A  73    17444  10448  10369   3028   -564   -425       C  
ATOM    556  O   LEU A  73     130.176  94.690  63.774  1.00 99.73           O  
ANISOU  556  O   LEU A  73    17643   9992  10258   2864   -471   -405       O  
ATOM    557  CB  LEU A  73     129.422  92.024  65.130  1.00 92.34           C  
ANISOU  557  CB  LEU A  73    15535   9972   9577   2617   -496   -488       C  
ATOM    558  CG  LEU A  73     129.508  90.529  65.449  1.00 79.42           C  
ANISOU  558  CG  LEU A  73    13426   8665   8084   2360   -443   -457       C  
ATOM    559  CD1 LEU A  73     129.730  90.302  66.926  1.00 83.44           C  
ANISOU  559  CD1 LEU A  73    13729   9315   8661   2210   -390   -521       C  
ATOM    560  CD2 LEU A  73     128.250  89.808  64.988  1.00 80.19           C  
ANISOU  560  CD2 LEU A  73    13224   9099   8144   2574   -527   -521       C  
ATOM    561  N   THR A  74     128.163  94.208  62.865  1.00110.69           N  
ANISOU  561  N   THR A  74    18789  11804  11465   3476   -712   -494       N  
ATOM    562  CA  THR A  74     127.819  95.589  62.535  1.00111.12           C  
ANISOU  562  CA  THR A  74    19375  11539  11308   3850   -778   -526       C  
ATOM    563  C   THR A  74     126.445  95.904  63.110  1.00114.35           C  
ANISOU  563  C   THR A  74    19610  12235  11601   4307   -943   -716       C  
ATOM    564  O   THR A  74     125.464  95.202  62.786  1.00118.95           O  
ANISOU  564  O   THR A  74    19823  13205  12165   4517  -1063   -799       O  
ATOM    565  CB  THR A  74     127.839  95.814  61.021  1.00 93.09           C  
ANISOU  565  CB  THR A  74    17471   9025   8873   4024   -807   -413       C  
ATOM    566  OG1 THR A  74     129.195  95.862  60.560  1.00 92.23           O  
ANISOU  566  OG1 THR A  74    17639   8560   8844   3614   -614   -248       O  
ATOM    567  CG2 THR A  74     127.139  97.111  60.665  1.00 97.01           C  
ANISOU  567  CG2 THR A  74    18483   9274   9102   4540   -922   -469       C  
ATOM    568  N   PRO A  75     126.314  96.927  63.949  1.00122.12           N  
ANISOU  568  N   PRO A  75    20830  13061  12507   4471   -952   -809       N  
ATOM    569  CA  PRO A  75     125.014  97.234  64.557  1.00123.01           C  
ANISOU  569  CA  PRO A  75    20756  13471  12510   4917  -1096  -1006       C  
ATOM    570  C   PRO A  75     124.078  97.878  63.550  1.00119.00           C  
ANISOU  570  C   PRO A  75    20534  12922  11759   5481  -1274  -1060       C  
ATOM    571  O   PRO A  75     124.508  98.693  62.719  1.00111.70           O  
ANISOU  571  O   PRO A  75    20198  11557  10687   5597  -1267   -952       O  
ATOM    572  CB  PRO A  75     125.370  98.211  65.690  1.00118.66           C  
ANISOU  572  CB  PRO A  75    20468  12680  11939   4893  -1036  -1070       C  
ATOM    573  CG  PRO A  75     126.867  98.116  65.849  1.00115.34           C  
ANISOU  573  CG  PRO A  75    20198  11949  11675   4344   -857   -929       C  
ATOM    574  CD  PRO A  75     127.387  97.772  64.493  1.00119.67           C  
ANISOU  574  CD  PRO A  75    20914  12327  12229   4212   -817   -762       C  
ATOM    575  N   PRO A  76     122.792  97.543  63.593  1.00116.59           N  
ANISOU  575  N   PRO A  76    19835  13069  11396   5851  -1432  -1237       N  
ATOM    576  CA  PRO A  76     121.838  98.156  62.664  1.00122.05           C  
ANISOU  576  CA  PRO A  76    20765  13772  11835   6453  -1640  -1324       C  
ATOM    577  C   PRO A  76     121.519  99.594  63.046  1.00125.35           C  
ANISOU  577  C   PRO A  76    21687  13904  12036   6895  -1707  -1407       C  
ATOM    578  O   PRO A  76     121.807 100.056  64.152  1.00122.12           O  
ANISOU  578  O   PRO A  76    21335  13385  11681   6767  -1611  -1446       O  
ATOM    579  CB  PRO A  76     120.601  97.260  62.789  1.00124.50           C  
ANISOU  579  CB  PRO A  76    20387  14721  12196   6640  -1770  -1534       C  
ATOM    580  CG  PRO A  76     120.690  96.705  64.168  1.00125.17           C  
ANISOU  580  CG  PRO A  76    20020  15055  12486   6288  -1623  -1595       C  
ATOM    581  CD  PRO A  76     122.159  96.515  64.439  1.00123.76           C  
ANISOU  581  CD  PRO A  76    20045  14515  12463   5720  -1418  -1374       C  
ATOM    582  N   ASP A  77     120.911 100.303  62.090  1.00132.29           N  
ANISOU  582  N   ASP A  77    22961  14653  12648   7446  -1882  -1439       N  
ATOM    583  CA  ASP A  77     120.474 101.691  62.264  1.00140.11           C  
ANISOU  583  CA  ASP A  77    24496  15361  13378   7977  -1978  -1525       C  
ATOM    584  C   ASP A  77     121.631 102.619  62.627  1.00144.63           C  
ANISOU  584  C   ASP A  77    25710  15299  13944   7691  -1783  -1371       C  
ATOM    585  O   ASP A  77     121.461 103.556  63.411  1.00150.57           O  
ANISOU  585  O   ASP A  77    26732  15876  14600   7901  -1785  -1467       O  
ATOM    586  CB  ASP A  77     119.358 101.797  63.307  1.00146.87           C  
ANISOU  586  CB  ASP A  77    24918  16664  14222   8318  -2087  -1793       C  
ATOM    587  CG  ASP A  77     118.158 100.942  62.961  1.00143.01           C  
ANISOU  587  CG  ASP A  77    23775  16820  13743   8599  -2270  -1990       C  
ATOM    588  OD1 ASP A  77     118.138 100.366  61.851  1.00137.33           O  
ANISOU  588  OD1 ASP A  77    23000  16174  13005   8598  -2349  -1925       O  
ATOM    589  OD2 ASP A  77     117.240 100.842  63.802  1.00146.68           O  
ANISOU  589  OD2 ASP A  77    23773  17723  14233   8806  -2326  -2223       O  
ATOM    590  N   ASP A  78     122.813 102.356  62.064  1.00134.66           N  
ANISOU  590  N   ASP A  78    24677  13700  12786   7199  -1607  -1150       N  
ATOM    591  CA  ASP A  78     124.003 103.191  62.263  1.00135.91           C  
ANISOU  591  CA  ASP A  78    25434  13249  12956   6859  -1398  -1014       C  
ATOM    592  C   ASP A  78     124.333 103.375  63.744  1.00138.95           C  
ANISOU  592  C   ASP A  78    25628  13664  13504   6580  -1301  -1114       C  
ATOM    593  O   ASP A  78     124.933 104.376  64.144  1.00145.83           O  
ANISOU  593  O   ASP A  78    27018  14069  14322   6489  -1193  -1101       O  
ATOM    594  CB  ASP A  78     123.850 104.552  61.576  1.00143.64           C  
ANISOU  594  CB  ASP A  78    27276  13695  13605   7328  -1440   -976       C  
ATOM    595  CG  ASP A  78     125.190 105.188  61.234  1.00137.84           C  
ANISOU  595  CG  ASP A  78    27195  12297  12880   6896  -1183   -785       C  
ATOM    596  OD1 ASP A  78     125.787 104.799  60.208  1.00130.00           O  
ANISOU  596  OD1 ASP A  78    26347  11149  11897   6669  -1085   -611       O  
ATOM    597  OD2 ASP A  78     125.650 106.069  61.993  1.00137.22           O  
ANISOU  597  OD2 ASP A  78    27477  11859  12802   6767  -1069   -823       O  
ATOM    598  N   LYS A  79     123.949 102.408  64.570  1.00133.95           N  
ANISOU  598  N   LYS A  79    24269  13567  13058   6434  -1330  -1221       N  
ATOM    599  CA  LYS A  79     124.298 102.450  65.979  1.00127.24           C  
ANISOU  599  CA  LYS A  79    23211  12778  12355   6153  -1237  -1308       C  
ATOM    600  C   LYS A  79     125.762 102.076  66.164  1.00123.41           C  
ANISOU  600  C   LYS A  79    22738  12060  12092   5473  -1031  -1164       C  
ATOM    601  O   LYS A  79     126.313 101.252  65.429  1.00126.46           O  
ANISOU  601  O   LYS A  79    22962  12488  12597   5163   -965  -1023       O  
ATOM    602  CB  LYS A  79     123.404 101.506  66.785  1.00129.02           C  
ANISOU  602  CB  LYS A  79    22691  13645  12688   6219  -1308  -1461       C  
ATOM    603  CG  LYS A  79     121.941 101.926  66.842  1.00126.74           C  
ANISOU  603  CG  LYS A  79    22310  13647  12200   6881  -1500  -1663       C  
ATOM    604  CD  LYS A  79     121.100 100.891  67.575  1.00127.94           C  
ANISOU  604  CD  LYS A  79    21686  14444  12480   6865  -1521  -1816       C  
ATOM    605  CE  LYS A  79     119.642 101.312  67.657  1.00135.77           C  
ANISOU  605  CE  LYS A  79    22528  15771  13287   7517  -1702  -2052       C  
ATOM    606  NZ  LYS A  79     119.457 102.539  68.482  1.00143.12           N  
ANISOU  606  NZ  LYS A  79    23848  16473  14060   7837  -1720  -2167       N  
ATOM    607  N   LYS A  80     126.396 102.704  67.146  1.00120.42           N  
ANISOU  607  N   LYS A  80    22551  11442  11762   5255   -938  -1219       N  
ATOM    608  CA  LYS A  80     127.792 102.419  67.427  1.00116.96           C  
ANISOU  608  CA  LYS A  80    22093  10813  11532   4629   -761  -1131       C  
ATOM    609  C   LYS A  80     127.913 101.173  68.299  1.00116.26           C  
ANISOU  609  C   LYS A  80    21306  11210  11658   4321   -745  -1164       C  
ATOM    610  O   LYS A  80     126.990 100.798  69.026  1.00118.17           O  
ANISOU  610  O   LYS A  80    21160  11857  11881   4554   -833  -1284       O  
ATOM    611  CB  LYS A  80     128.457 103.616  68.105  1.00124.06           C  
ANISOU  611  CB  LYS A  80    23490  11254  12394   4507   -677  -1204       C  
ATOM    612  CG  LYS A  80     128.418 104.884  67.267  1.00136.30           C  
ANISOU  612  CG  LYS A  80    25819  12250  13719   4778   -656  -1160       C  
ATOM    613  CD  LYS A  80     128.914 106.093  68.044  1.00144.95           C  
ANISOU  613  CD  LYS A  80    27405  12903  14765   4691   -579  -1269       C  
ATOM    614  CE  LYS A  80     128.794 107.360  67.210  1.00148.94           C  
ANISOU  614  CE  LYS A  80    28747  12826  15016   4995   -546  -1221       C  
ATOM    615  NZ  LYS A  80     129.232 108.570  67.956  1.00151.36           N  
ANISOU  615  NZ  LYS A  80    29575  12669  15265   4912   -464  -1342       N  
ATOM    616  N   VAL A  81     129.078 100.524  68.215  1.00120.54           N  
ANISOU  616  N   VAL A  81    21703  11704  12394   3797   -617  -1058       N  
ATOM    617  CA  VAL A  81     129.316  99.307  68.985  1.00112.36           C  
ANISOU  617  CA  VAL A  81    20068  11081  11544   3499   -593  -1068       C  
ATOM    618  C   VAL A  81     129.327  99.547  70.485  1.00110.20           C  
ANISOU  618  C   VAL A  81    19668  10915  11287   3466   -602  -1220       C  
ATOM    619  O   VAL A  81     129.267  98.581  71.257  1.00101.91           O  
ANISOU  619  O   VAL A  81    18145  10239  10336   3328   -595  -1246       O  
ATOM    620  CB  VAL A  81     130.644  98.644  68.568  1.00 99.85           C  
ANISOU  620  CB  VAL A  81    18396   9396  10146   2978   -463   -936       C  
ATOM    621  CG1 VAL A  81     130.563  98.164  67.130  1.00 92.90           C  
ANISOU  621  CG1 VAL A  81    17553   8495   9252   3010   -451   -783       C  
ATOM    622  CG2 VAL A  81     131.800  99.615  68.743  1.00103.02           C  
ANISOU  622  CG2 VAL A  81    19222   9339  10580   2687   -353   -959       C  
ATOM    623  N   THR A  82     129.406 100.804  70.919  1.00120.24           N  
ANISOU  623  N   THR A  82    21383  11853  12449   3595   -610  -1323       N  
ATOM    624  CA  THR A  82     129.308 101.147  72.330  1.00112.52           C  
ANISOU  624  CA  THR A  82    20338  10966  11450   3629   -635  -1487       C  
ATOM    625  C   THR A  82     127.876 101.123  72.845  1.00116.58           C  
ANISOU  625  C   THR A  82    20640  11827  11826   4110   -738  -1603       C  
ATOM    626  O   THR A  82     127.663 101.334  74.044  1.00122.29           O  
ANISOU  626  O   THR A  82    21277  12675  12512   4179   -753  -1742       O  
ATOM    627  CB  THR A  82     129.917 102.528  72.582  1.00106.06           C  
ANISOU  627  CB  THR A  82    20097   9641  10562   3582   -601  -1573       C  
ATOM    628  OG1 THR A  82     129.375 103.469  71.646  1.00105.38           O  
ANISOU  628  OG1 THR A  82    20517   9226  10298   3939   -630  -1541       O  
ATOM    629  CG2 THR A  82     131.428 102.478  72.433  1.00102.58           C  
ANISOU  629  CG2 THR A  82    19744   8937  10293   3023   -478  -1521       C  
ATOM    630  N   ASP A  83     126.896 100.888  71.973  1.00118.13           N  
ANISOU  630  N   ASP A  83    20748  12194  11941   4447   -809  -1567       N  
ATOM    631  CA  ASP A  83     125.508 100.746  72.394  1.00119.38           C  
ANISOU  631  CA  ASP A  83    20614  12754  11992   4884   -899  -1701       C  
ATOM    632  C   ASP A  83     125.381  99.560  73.341  1.00115.19           C  
ANISOU  632  C   ASP A  83    19492  12688  11587   4663   -837  -1732       C  
ATOM    633  O   ASP A  83     125.445  98.405  72.909  1.00114.19           O  
ANISOU  633  O   ASP A  83    18996  12807  11585   4446   -797  -1632       O  
ATOM    634  CB  ASP A  83     124.598 100.583  71.171  1.00111.55           C  
ANISOU  634  CB  ASP A  83    19581  11891  10913   5235   -997  -1670       C  
ATOM    635  CG  ASP A  83     123.123 100.582  71.529  1.00113.81           C  
ANISOU  635  CG  ASP A  83    19573  12593  11078   5726  -1099  -1851       C  
ATOM    636  OD1 ASP A  83     122.634  99.555  72.045  1.00118.19           O  
ANISOU  636  OD1 ASP A  83    19563  13614  11729   5628  -1059  -1903       O  
ATOM    637  OD2 ASP A  83     122.453 101.612  71.300  1.00119.80           O  
ANISOU  637  OD2 ASP A  83    20673  13208  11638   6213  -1209  -1950       O  
ATOM    638  N   LYS A  84     125.215  99.839  74.637  1.00123.34           N  
ANISOU  638  N   LYS A  84    20470  13822  12572   4720   -819  -1868       N  
ATOM    639  CA  LYS A  84     125.190  98.774  75.636  1.00125.81           C  
ANISOU  639  CA  LYS A  84    20306  14522  12974   4501   -736  -1888       C  
ATOM    640  C   LYS A  84     124.046  97.797  75.398  1.00121.42           C  
ANISOU  640  C   LYS A  84    19258  14446  12431   4656   -723  -1911       C  
ATOM    641  O   LYS A  84     124.193  96.597  75.655  1.00117.09           O  
ANISOU  641  O   LYS A  84    18325  14166  11998   4368   -629  -1844       O  
ATOM    642  CB  LYS A  84     125.086  99.372  77.040  1.00129.81           C  
ANISOU  642  CB  LYS A  84    20896  15045  13381   4611   -725  -2046       C  
ATOM    643  CG  LYS A  84     125.998 100.571  77.293  1.00132.35           C  
ANISOU  643  CG  LYS A  84    21746  14881  13659   4537   -757  -2088       C  
ATOM    644  CD  LYS A  84     127.460 100.222  77.069  1.00128.76           C  
ANISOU  644  CD  LYS A  84    21355  14199  13370   4025   -708  -1964       C  
ATOM    645  CE  LYS A  84     127.950  99.176  78.058  1.00124.61           C  
ANISOU  645  CE  LYS A  84    20448  13964  12934   3723   -647  -1956       C  
ATOM    646  NZ  LYS A  84     129.391  98.854  77.851  1.00115.17           N  
ANISOU  646  NZ  LYS A  84    19289  12577  11894   3260   -617  -1865       N  
ATOM    647  N   ALA A  85     122.905  98.286  74.908  1.00122.62           N  
ANISOU  647  N   ALA A  85    19418  14712  12460   5109   -814  -2018       N  
ATOM    648  CA  ALA A  85     121.779  97.398  74.640  1.00114.90           C  
ANISOU  648  CA  ALA A  85    17940  14213  11503   5250   -807  -2083       C  
ATOM    649  C   ALA A  85     122.091  96.444  73.497  1.00122.94           C  
ANISOU  649  C   ALA A  85    18790  15268  12654   4997   -804  -1928       C  
ATOM    650  O   ALA A  85     121.694  95.274  73.532  1.00119.46           O  
ANISOU  650  O   ALA A  85    17887  15191  12311   4829   -726  -1926       O  
ATOM    651  CB  ALA A  85     120.526  98.214  74.328  1.00113.55           C  
ANISOU  651  CB  ALA A  85    17815  14165  11162   5831   -936  -2264       C  
ATOM    652  N   TRP A  86     122.796  96.926  72.471  1.00125.64           N  
ANISOU  652  N   TRP A  86    19522  15222  12992   4960   -873  -1800       N  
ATOM    653  CA  TRP A  86     123.146  96.066  71.346  1.00109.62           C  
ANISOU  653  CA  TRP A  86    17373  13203  11073   4732   -869  -1651       C  
ATOM    654  C   TRP A  86     124.199  95.038  71.740  1.00102.91           C  
ANISOU  654  C   TRP A  86    16337  12362  10401   4199   -731  -1511       C  
ATOM    655  O   TRP A  86     124.152  93.888  71.285  1.00 90.24           O  
ANISOU  655  O   TRP A  86    14407  10976   8904   3996   -687  -1440       O  
ATOM    656  CB  TRP A  86     123.634  96.913  70.171  1.00116.35           C  
ANISOU  656  CB  TRP A  86    18739  13621  11848   4846   -953  -1550       C  
ATOM    657  CG  TRP A  86     124.192  96.103  69.044  1.00114.01           C  
ANISOU  657  CG  TRP A  86    18387  13276  11657   4579   -932  -1382       C  
ATOM    658  CD1 TRP A  86     123.486  95.429  68.091  1.00111.99           C  
ANISOU  658  CD1 TRP A  86    17881  13272  11398   4711  -1005  -1388       C  
ATOM    659  CD2 TRP A  86     125.576  95.883  68.749  1.00112.12           C  
ANISOU  659  CD2 TRP A  86    18334  12731  11537   4141   -831  -1204       C  
ATOM    660  NE1 TRP A  86     124.345  94.800  67.223  1.00116.84           N  
ANISOU  660  NE1 TRP A  86    18543  13738  12114   4388   -953  -1210       N  
ATOM    661  CE2 TRP A  86     125.634  95.064  67.604  1.00112.30           C  
ANISOU  661  CE2 TRP A  86    18226  12827  11617   4039   -839  -1094       C  
ATOM    662  CE3 TRP A  86     126.772  96.298  69.343  1.00114.49           C  
ANISOU  662  CE3 TRP A  86    18879  12721  11902   3826   -737  -1150       C  
ATOM    663  CZ2 TRP A  86     126.841  94.653  67.041  1.00108.90           C  
ANISOU  663  CZ2 TRP A  86    17907  12169  11300   3647   -745   -921       C  
ATOM    664  CZ3 TRP A  86     127.969  95.890  68.782  1.00110.46           C  
ANISOU  664  CZ3 TRP A  86    18448  12005  11516   3428   -648   -994       C  
ATOM    665  CH2 TRP A  86     127.994  95.076  67.643  1.00107.84           C  
ANISOU  665  CH2 TRP A  86    17989  11753  11235   3348   -646   -876       C  
ATOM    666  N   GLN A  87     125.161  95.433  72.580  1.00112.17           N  
ANISOU  666  N   GLN A  87    17722  13301  11598   3981   -673  -1484       N  
ATOM    667  CA  GLN A  87     126.175  94.490  73.042  1.00108.05           C  
ANISOU  667  CA  GLN A  87    17025  12808  11221   3526   -565  -1375       C  
ATOM    668  C   GLN A  87     125.542  93.328  73.794  1.00110.38           C  
ANISOU  668  C   GLN A  87    16845  13541  11556   3453   -476  -1415       C  
ATOM    669  O   GLN A  87     125.905  92.166  73.578  1.00 98.45           O  
ANISOU  669  O   GLN A  87    15093  12156  10158   3165   -402  -1306       O  
ATOM    670  CB  GLN A  87     127.192  95.202  73.933  1.00101.56           C  
ANISOU  670  CB  GLN A  87    16485  11709  10396   3363   -545  -1398       C  
ATOM    671  CG  GLN A  87     127.987  96.292  73.243  1.00108.68           C  
ANISOU  671  CG  GLN A  87    17874  12140  11281   3332   -584  -1358       C  
ATOM    672  CD  GLN A  87     128.972  96.962  74.180  1.00114.42           C  
ANISOU  672  CD  GLN A  87    18833  12622  12018   3136   -563  -1422       C  
ATOM    673  OE1 GLN A  87     129.045  96.630  75.362  1.00108.68           O  
ANISOU  673  OE1 GLN A  87    17912  12088  11292   3064   -541  -1496       O  
ATOM    674  NE2 GLN A  87     129.735  97.913  73.655  1.00134.50           N  
ANISOU  674  NE2 GLN A  87    21805  14736  14561   3044   -562  -1405       N  
ATOM    675  N   LYS A  88     124.590  93.624  74.681  1.00129.40           N  
ANISOU  675  N   LYS A  88    19132  16173  13862   3710   -465  -1573       N  
ATOM    676  CA  LYS A  88     123.929  92.572  75.444  1.00136.65           C  
ANISOU  676  CA  LYS A  88    19625  17495  14800   3632   -339  -1622       C  
ATOM    677  C   LYS A  88     123.136  91.632  74.543  1.00126.75           C  
ANISOU  677  C   LYS A  88    18023  16521  13616   3627   -320  -1616       C  
ATOM    678  O   LYS A  88     123.020  90.440  74.845  1.00126.76           O  
ANISOU  678  O   LYS A  88    17711  16761  13691   3384   -186  -1579       O  
ATOM    679  CB  LYS A  88     123.019  93.198  76.501  1.00142.73           C  
ANISOU  679  CB  LYS A  88    20353  18445  15434   3937   -318  -1811       C  
ATOM    680  CG  LYS A  88     122.282  92.201  77.377  1.00147.06           C  
ANISOU  680  CG  LYS A  88    20492  19402  15981   3857   -147  -1876       C  
ATOM    681  CD  LYS A  88     121.219  92.894  78.210  1.00156.08           C  
ANISOU  681  CD  LYS A  88    21570  20751  16981   4215   -125  -2085       C  
ATOM    682  CE  LYS A  88     120.320  91.889  78.906  1.00161.00           C  
ANISOU  682  CE  LYS A  88    21757  21809  17605   4137     79  -2167       C  
ATOM    683  NZ  LYS A  88     119.158  92.553  79.560  1.00166.43           N  
ANISOU  683  NZ  LYS A  88    22326  22748  18161   4512    109  -2396       N  
ATOM    684  N   LYS A  89     122.598  92.139  73.432  1.00118.09           N  
ANISOU  684  N   LYS A  89    16999  15387  12485   3892   -453  -1658       N  
ATOM    685  CA  LYS A  89     121.789  91.297  72.557  1.00110.76           C  
ANISOU  685  CA  LYS A  89    15725  14747  11612   3912   -463  -1691       C  
ATOM    686  C   LYS A  89     122.649  90.305  71.783  1.00102.26           C  
ANISOU  686  C   LYS A  89    14620  13564  10670   3540   -424  -1501       C  
ATOM    687  O   LYS A  89     122.297  89.124  71.677  1.00 98.63           O  
ANISOU  687  O   LYS A  89    13810  13366  10297   3342   -330  -1498       O  
ATOM    688  CB  LYS A  89     120.972  92.166  71.600  1.00113.43           C  
ANISOU  688  CB  LYS A  89    16172  15084  11841   4359   -647  -1807       C  
ATOM    689  CG  LYS A  89     120.149  91.383  70.584  1.00116.06           C  
ANISOU  689  CG  LYS A  89    16159  15716  12221   4412   -700  -1873       C  
ATOM    690  CD  LYS A  89     119.215  92.299  69.806  1.00120.13           C  
ANISOU  690  CD  LYS A  89    16763  16289  12590   4938   -905  -2031       C  
ATOM    691  CE  LYS A  89     118.518  91.556  68.675  1.00122.53           C  
ANISOU  691  CE  LYS A  89    16755  16867  12933   4993   -996  -2104       C  
ATOM    692  NZ  LYS A  89     119.475  91.135  67.614  1.00124.40           N  
ANISOU  692  NZ  LYS A  89    17214  16819  13233   4743  -1021  -1886       N  
ATOM    693  N   VAL A  90     123.780  90.759  71.239  1.00105.94           N  
ANISOU  693  N   VAL A  90    15455  13643  11154   3429   -479  -1351       N  
ATOM    694  CA  VAL A  90     124.594  89.875  70.410  1.00106.85           C  
ANISOU  694  CA  VAL A  90    15551  13659  11387   3111   -446  -1180       C  
ATOM    695  C   VAL A  90     125.455  88.946  71.262  1.00101.76           C  
ANISOU  695  C   VAL A  90    14790  13035  10839   2727   -301  -1078       C  
ATOM    696  O   VAL A  90     125.768  87.829  70.835  1.00 93.90           O  
ANISOU  696  O   VAL A  90    13627  12110   9941   2474   -236   -977       O  
ATOM    697  CB  VAL A  90     125.453  90.694  69.430  1.00105.15           C  
ANISOU  697  CB  VAL A  90    15765  13038  11150   3135   -534  -1068       C  
ATOM    698  CG1 VAL A  90     124.565  91.473  68.475  1.00 95.63           C  
ANISOU  698  CG1 VAL A  90    14703  11814   9818   3546   -682  -1153       C  
ATOM    699  CG2 VAL A  90     126.380  91.633  70.183  1.00118.49           C  
ANISOU  699  CG2 VAL A  90    17791  14415  12814   3067   -514  -1048       C  
ATOM    700  N   THR A  91     125.852  89.375  72.464  1.00106.10           N  
ANISOU  700  N   THR A  91    15442  13521  11348   2699   -257  -1109       N  
ATOM    701  CA  THR A  91     126.642  88.500  73.328  1.00 99.83           C  
ANISOU  701  CA  THR A  91    14555  12764  10611   2389   -141  -1025       C  
ATOM    702  C   THR A  91     125.827  87.296  73.782  1.00 89.39           C  
ANISOU  702  C   THR A  91    12869  11791   9304   2305     -4  -1055       C  
ATOM    703  O   THR A  91     126.350  86.177  73.853  1.00 83.63           O  
ANISOU  703  O   THR A  91    12034  11098   8642   2033     92   -943       O  
ATOM    704  CB  THR A  91     127.172  89.273  74.537  1.00 98.49           C  
ANISOU  704  CB  THR A  91    14582  12471  10370   2415   -145  -1081       C  
ATOM    705  OG1 THR A  91     126.115  90.049  75.115  1.00 98.81           O  
ANISOU  705  OG1 THR A  91    14615  12635  10292   2730   -165  -1244       O  
ATOM    706  CG2 THR A  91     128.318  90.190  74.129  1.00 96.90           C  
ANISOU  706  CG2 THR A  91    14730  11893  10194   2346   -234  -1032       C  
ATOM    707  N   GLU A  92     124.545  87.503  74.090  1.00 93.93           N  
ANISOU  707  N   GLU A  92    13257  12621   9811   2535     19  -1214       N  
ATOM    708  CA  GLU A  92     123.678  86.379  74.426  1.00 99.53           C  
ANISOU  708  CA  GLU A  92    13607  13666  10544   2427    180  -1266       C  
ATOM    709  C   GLU A  92     123.518  85.438  73.241  1.00 92.70           C  
ANISOU  709  C   GLU A  92    12563  12872   9787   2275    180  -1210       C  
ATOM    710  O   GLU A  92     123.515  84.214  73.408  1.00 92.79           O  
ANISOU  710  O   GLU A  92    12394  13006   9856   2012    331  -1154       O  
ATOM    711  CB  GLU A  92     122.315  86.886  74.898  1.00113.85           C  
ANISOU  711  CB  GLU A  92    15227  15760  12272   2715    203  -1482       C  
ATOM    712  CG  GLU A  92     122.366  87.682  76.189  1.00124.11           C  
ANISOU  712  CG  GLU A  92    16679  17026  13449   2862    234  -1552       C  
ATOM    713  CD  GLU A  92     121.021  88.267  76.565  1.00130.82           C  
ANISOU  713  CD  GLU A  92    17341  18155  14209   3187    249  -1778       C  
ATOM    714  OE1 GLU A  92     120.668  88.227  77.763  1.00132.01           O  
ANISOU  714  OE1 GLU A  92    17422  18461  14277   3206    394  -1855       O  
ATOM    715  OE2 GLU A  92     120.313  88.763  75.662  1.00131.89           O  
ANISOU  715  OE2 GLU A  92    17403  18366  14345   3443    115  -1887       O  
ATOM    716  N   GLU A  93     123.387  85.992  72.032  1.00106.14           N  
ANISOU  716  N   GLU A  93    14345  14482  11501   2445     14  -1226       N  
ATOM    717  CA  GLU A  93     123.292  85.154  70.840  1.00107.51           C  
ANISOU  717  CA  GLU A  93    14380  14707  11764   2319     -9  -1178       C  
ATOM    718  C   GLU A  93     124.572  84.353  70.630  1.00 95.08           C  
ANISOU  718  C   GLU A  93    12935  12918  10272   1987     49   -968       C  
ATOM    719  O   GLU A  93     124.524  83.184  70.231  1.00 85.62           O  
ANISOU  719  O   GLU A  93    11561  11820   9151   1767    132   -920       O  
ATOM    720  CB  GLU A  93     122.987  86.019  69.616  1.00106.19           C  
ANISOU  720  CB  GLU A  93    14346  14449  11552   2612   -212  -1228       C  
ATOM    721  CG  GLU A  93     121.638  86.725  69.677  1.00104.19           C  
ANISOU  721  CG  GLU A  93    13931  14449  11207   2993   -297  -1460       C  
ATOM    722  CD  GLU A  93     121.470  87.773  68.592  1.00106.64           C  
ANISOU  722  CD  GLU A  93    14490  14604  11423   3351   -516  -1492       C  
ATOM    723  OE1 GLU A  93     122.484  88.174  67.983  1.00107.07           O  
ANISOU  723  OE1 GLU A  93    14909  14300  11471   3297   -573  -1326       O  
ATOM    724  OE2 GLU A  93     120.320  88.196  68.348  1.00108.89           O  
ANISOU  724  OE2 GLU A  93    14612  15129  11631   3697   -623  -1693       O  
ATOM    725  N   LEU A  94     125.727  84.968  70.895  1.00 92.01           N  
ANISOU  725  N   LEU A  94    12848  12240   9869   1947      9   -859       N  
ATOM    726  CA  LEU A  94     126.991  84.244  70.813  1.00 92.50           C  
ANISOU  726  CA  LEU A  94    13008  12132  10006   1655     61   -685       C  
ATOM    727  C   LEU A  94     127.109  83.222  71.936  1.00103.97           C  
ANISOU  727  C   LEU A  94    14323  13723  11458   1456    224   -653       C  
ATOM    728  O   LEU A  94     127.466  82.061  71.700  1.00101.28           O  
ANISOU  728  O   LEU A  94    13904  13402  11177   1234    309   -554       O  
ATOM    729  CB  LEU A  94     128.160  85.228  70.854  1.00 81.79           C  
ANISOU  729  CB  LEU A  94    11972  10464   8640   1658    -20   -621       C  
ATOM    730  CG  LEU A  94     128.270  86.173  69.662  1.00 76.62           C  
ANISOU  730  CG  LEU A  94    11543   9593   7974   1806   -144   -610       C  
ATOM    731  CD1 LEU A  94     129.271  87.273  69.966  1.00 78.01           C  
ANISOU  731  CD1 LEU A  94    12039   9470   8132   1796   -185   -592       C  
ATOM    732  CD2 LEU A  94     128.669  85.397  68.416  1.00 75.38           C  
ANISOU  732  CD2 LEU A  94    11363   9384   7895   1655   -143   -493       C  
ATOM    733  N   ASP A  95     126.815  83.638  73.170  1.00113.71           N  
ANISOU  733  N   ASP A  95    15562  15038  12605   1550    274   -736       N  
ATOM    734  CA  ASP A  95     126.790  82.702  74.287  1.00104.55           C  
ANISOU  734  CA  ASP A  95    14307  14013  11403   1400    445   -711       C  
ATOM    735  C   ASP A  95     125.776  81.585  74.078  1.00 97.77           C  
ANISOU  735  C   ASP A  95    13172  13397  10578   1286    599   -749       C  
ATOM    736  O   ASP A  95     125.941  80.501  74.648  1.00 98.91           O  
ANISOU  736  O   ASP A  95    13285  13589  10709   1086    764   -675       O  
ATOM    737  CB  ASP A  95     126.483  83.448  75.588  1.00100.75           C  
ANISOU  737  CB  ASP A  95    13885  13595  10801   1562    473   -816       C  
ATOM    738  CG  ASP A  95     127.611  84.371  76.018  1.00 89.13           C  
ANISOU  738  CG  ASP A  95    12690  11881   9293   1609    347   -789       C  
ATOM    739  OD1 ASP A  95     128.686  84.337  75.380  1.00 82.43           O  
ANISOU  739  OD1 ASP A  95    11966  10832   8522   1484    264   -686       O  
ATOM    740  OD2 ASP A  95     127.421  85.124  77.000  1.00 83.52           O  
ANISOU  740  OD2 ASP A  95    12065  11191   8479   1762    339   -887       O  
ATOM    741  N   GLN A  96     124.740  81.820  73.269  1.00 94.47           N  
ANISOU  741  N   GLN A  96    12567  13131  10197   1411    549   -873       N  
ATOM    742  CA  GLN A  96     123.724  80.802  73.025  1.00 99.16           C  
ANISOU  742  CA  GLN A  96    12859  13978  10839   1281    691   -955       C  
ATOM    743  C   GLN A  96     124.225  79.714  72.084  1.00 92.13           C  
ANISOU  743  C   GLN A  96    11962  12999  10046   1039    707   -832       C  
ATOM    744  O   GLN A  96     123.990  78.527  72.332  1.00 92.37           O  
ANISOU  744  O   GLN A  96    11876  13122  10100    802    895   -810       O  
ATOM    745  CB  GLN A  96     122.458  81.444  72.457  1.00107.46           C  
ANISOU  745  CB  GLN A  96    13681  15256  11892   1524    600  -1167       C  
ATOM    746  CG  GLN A  96     121.326  80.466  72.163  1.00118.26           C  
ANISOU  746  CG  GLN A  96    14680  16928  13325   1383    736  -1309       C  
ATOM    747  CD  GLN A  96     120.813  79.773  73.409  1.00127.18           C  
ANISOU  747  CD  GLN A  96    15666  18238  14419   1205   1018  -1359       C  
ATOM    748  OE1 GLN A  96     120.905  80.308  74.513  1.00125.83           O  
ANISOU  748  OE1 GLN A  96    15607  18055  14147   1308   1080  -1360       O  
ATOM    749  NE2 GLN A  96     120.274  78.571  73.239  1.00132.96           N  
ANISOU  749  NE2 GLN A  96    16174  19123  15222    928   1205  -1404       N  
ATOM    750  N   VAL A  97     124.905  80.092  70.999  1.00 92.18           N  
ANISOU  750  N   VAL A  97    12113  12813  10097   1092    530   -752       N  
ATOM    751  CA  VAL A  97     125.376  79.082  70.056  1.00 99.47           C  
ANISOU  751  CA  VAL A  97    13035  13656  11104    884    542   -643       C  
ATOM    752  C   VAL A  97     126.563  78.320  70.631  1.00 89.09           C  
ANISOU  752  C   VAL A  97    11896  12169   9786    674    641   -462       C  
ATOM    753  O   VAL A  97     126.780  77.151  70.293  1.00 92.29           O  
ANISOU  753  O   VAL A  97    12274  12557  10237    465    735   -383       O  
ATOM    754  CB  VAL A  97     125.711  79.718  68.691  1.00102.08           C  
ANISOU  754  CB  VAL A  97    13481  13840  11464   1017    341   -615       C  
ATOM    755  CG1 VAL A  97     124.497  80.445  68.132  1.00 99.83           C  
ANISOU  755  CG1 VAL A  97    13042  13739  11151   1281    222   -806       C  
ATOM    756  CG2 VAL A  97     126.898  80.662  68.804  1.00111.67           C  
ANISOU  756  CG2 VAL A  97    15000  14778  12651   1091    245   -502       C  
ATOM    757  N   VAL A  98     127.349  78.955  71.505  1.00 90.49           N  
ANISOU  757  N   VAL A  98    12259  12222   9902    740    613   -407       N  
ATOM    758  CA  VAL A  98     128.419  78.235  72.187  1.00 91.51           C  
ANISOU  758  CA  VAL A  98    12533  12233  10003    587    690   -267       C  
ATOM    759  C   VAL A  98     127.834  77.271  73.212  1.00 85.71           C  
ANISOU  759  C   VAL A  98    11725  11644   9198    472    908   -278       C  
ATOM    760  O   VAL A  98     128.338  76.157  73.398  1.00 88.05           O  
ANISOU  760  O   VAL A  98    12096  11879   9478    306   1019   -164       O  
ATOM    761  CB  VAL A  98     129.406  79.225  72.831  1.00 93.89           C  
ANISOU  761  CB  VAL A  98    13033  12385  10256    695    579   -245       C  
ATOM    762  CG1 VAL A  98     130.485  78.481  73.601  1.00 94.28           C  
ANISOU  762  CG1 VAL A  98    13207  12357  10257    581    633   -132       C  
ATOM    763  CG2 VAL A  98     130.030  80.117  71.770  1.00 95.14           C  
ANISOU  763  CG2 VAL A  98    13299  12366  10486    759    410   -227       C  
ATOM    764  N   LYS A  99     126.758  77.682  73.887  1.00 89.69           N  
ANISOU  764  N   LYS A  99    12099  12334   9647    567    987   -416       N  
ATOM    765  CA  LYS A  99     126.078  76.796  74.826  1.00 81.47           C  
ANISOU  765  CA  LYS A  99    10986  11436   8534    438   1238   -440       C  
ATOM    766  C   LYS A  99     125.509  75.573  74.117  1.00 85.62           C  
ANISOU  766  C   LYS A  99    11359  12033   9140    206   1381   -443       C  
ATOM    767  O   LYS A  99     125.603  74.450  74.625  1.00 75.74           O  
ANISOU  767  O   LYS A  99    10188  10749   7840     11   1586   -360       O  
ATOM    768  CB  LYS A  99     124.972  77.564  75.550  1.00 77.86           C  
ANISOU  768  CB  LYS A  99    10380  11189   8013    593   1297   -615       C  
ATOM    769  CG  LYS A  99     124.042  76.706  76.388  1.00 88.29           C  
ANISOU  769  CG  LYS A  99    11579  12697   9272    440   1596   -676       C  
ATOM    770  CD  LYS A  99     122.964  77.559  77.039  1.00103.11           C  
ANISOU  770  CD  LYS A  99    13282  14805  11091    620   1647   -870       C  
ATOM    771  CE  LYS A  99     122.044  76.724  77.911  1.00122.06           C  
ANISOU  771  CE  LYS A  99    15557  17394  13425    442   1986   -940       C  
ATOM    772  NZ  LYS A  99     121.323  75.686  77.125  1.00128.48           N  
ANISOU  772  NZ  LYS A  99    16130  18327  14361    179   2133  -1004       N  
ATOM    773  N   ASP A 100     124.921  75.771  72.936  1.00 96.16           N  
ANISOU  773  N   ASP A 100    12499  13454  10586    230   1273   -543       N  
ATOM    774  CA  ASP A 100     124.329  74.678  72.177  1.00 97.75           C  
ANISOU  774  CA  ASP A 100    12531  13736  10872      9   1383   -585       C  
ATOM    775  C   ASP A 100     125.358  73.851  71.417  1.00 92.30           C  
ANISOU  775  C   ASP A 100    12017  12825  10229   -133   1341   -413       C  
ATOM    776  O   ASP A 100     125.017  72.769  70.928  1.00 85.48           O  
ANISOU  776  O   ASP A 100    11077  11982   9418   -350   1461   -424       O  
ATOM    777  CB  ASP A 100     123.293  75.224  71.190  1.00 90.21           C  
ANISOU  777  CB  ASP A 100    11291  12985  10000    127   1252   -786       C  
ATOM    778  CG  ASP A 100     122.240  76.083  71.864  1.00103.01           C  
ANISOU  778  CG  ASP A 100    12713  14852  11575    312   1275   -982       C  
ATOM    779  OD1 ASP A 100     121.911  75.813  73.038  1.00110.73           O  
ANISOU  779  OD1 ASP A 100    13676  15915  12482    229   1495  -1003       O  
ATOM    780  OD2 ASP A 100     121.743  77.031  71.219  1.00106.49           O  
ANISOU  780  OD2 ASP A 100    13031  15396  12033    560   1079  -1115       O  
ATOM    781  N   HIS A 101     126.597  74.323  71.306  1.00 98.84           N  
ANISOU  781  N   HIS A 101    13069  13448  11039    -26   1183   -271       N  
ATOM    782  CA  HIS A 101     127.622  73.650  70.512  1.00 95.77           C  
ANISOU  782  CA  HIS A 101    12827  12866  10695   -125   1128   -123       C  
ATOM    783  C   HIS A 101     128.960  73.664  71.247  1.00 95.98           C  
ANISOU  783  C   HIS A 101    13103  12716  10648    -87   1103     30       C  
ATOM    784  O   HIS A 101     130.000  74.012  70.685  1.00 72.04           O  
ANISOU  784  O   HIS A 101    10180   9541   7652    -30    954    109       O  
ATOM    785  CB  HIS A 101     127.755  74.297  69.134  1.00 99.85           C  
ANISOU  785  CB  HIS A 101    13302  13340  11296    -20    920   -149       C  
ATOM    786  CG  HIS A 101     126.503  74.245  68.314  1.00105.42           C  
ANISOU  786  CG  HIS A 101    13761  14234  12060    -22    902   -316       C  
ATOM    787  ND1 HIS A 101     126.152  73.144  67.562  1.00104.91           N  
ANISOU  787  ND1 HIS A 101    13602  14203  12055   -212    973   -340       N  
ATOM    788  CD2 HIS A 101     125.525  75.160  68.120  1.00110.42           C  
ANISOU  788  CD2 HIS A 101    14217  15043  12694    162    805   -488       C  
ATOM    789  CE1 HIS A 101     125.008  73.382  66.945  1.00107.53           C  
ANISOU  789  CE1 HIS A 101    13685  14743  12429   -157    914   -532       C  
ATOM    790  NE2 HIS A 101     124.606  74.599  67.267  1.00112.92           N  
ANISOU  790  NE2 HIS A 101    14311  15522  13072     86    808   -624       N  
ATOM    791  N   GLU A 102     128.945  73.274  72.527  1.00109.07           N  
ANISOU  791  N   GLU A 102    14853  14396  12192   -114   1255     59       N  
ATOM    792  CA  GLU A 102     130.186  73.216  73.295  1.00 99.31           C  
ANISOU  792  CA  GLU A 102    13846  13024  10864    -50   1214    179       C  
ATOM    793  C   GLU A 102     131.172  72.220  72.697  1.00101.50           C  
ANISOU  793  C   GLU A 102    14254  13149  11163   -142   1205    316       C  
ATOM    794  O   GLU A 102     132.387  72.379  72.857  1.00 96.33           O  
ANISOU  794  O   GLU A 102    13729  12391  10482    -58   1088    390       O  
ATOM    795  CB  GLU A 102     129.895  72.852  74.753  1.00106.23           C  
ANISOU  795  CB  GLU A 102    14830  13953  11579    -46   1393    187       C  
ATOM    796  CG  GLU A 102     129.186  73.937  75.550  1.00115.52           C  
ANISOU  796  CG  GLU A 102    15921  15269  12703     92   1386     59       C  
ATOM    797  CD  GLU A 102     128.988  73.559  77.008  1.00113.77           C  
ANISOU  797  CD  GLU A 102    15844  15087  12298    107   1573     78       C  
ATOM    798  OE1 GLU A 102     129.368  72.431  77.389  1.00110.58           O  
ANISOU  798  OE1 GLU A 102    15626  14591  11798     11   1713    197       O  
ATOM    799  OE2 GLU A 102     128.452  74.390  77.772  1.00112.41           O  
ANISOU  799  OE2 GLU A 102    15625  15027  12057    230   1584    -25       O  
ATOM    800  N   ASP A 103     130.672  71.196  72.004  1.00 99.45           N  
ANISOU  800  N   ASP A 103    13951  12883  10954   -311   1324    332       N  
ATOM    801  CA  ASP A 103     131.527  70.164  71.430  1.00 93.83           C  
ANISOU  801  CA  ASP A 103    13380  12020  10250   -390   1333    455       C  
ATOM    802  C   ASP A 103     132.160  70.575  70.106  1.00 95.77           C  
ANISOU  802  C   ASP A 103    13569  12202  10619   -355   1148    468       C  
ATOM    803  O   ASP A 103     133.079  69.891  69.643  1.00 91.65           O  
ANISOU  803  O   ASP A 103    13162  11559  10101   -378   1127    568       O  
ATOM    804  CB  ASP A 103     130.728  68.871  71.245  1.00 89.77           C  
ANISOU  804  CB  ASP A 103    12878  11500   9732   -605   1552    457       C  
ATOM    805  CG  ASP A 103     130.320  68.245  72.568  1.00102.28           C  
ANISOU  805  CG  ASP A 103    14608  13088  11166   -665   1785    484       C  
ATOM    806  OD1 ASP A 103     131.104  68.334  73.537  1.00 97.45           O  
ANISOU  806  OD1 ASP A 103    14193  12416  10419   -524   1763    568       O  
ATOM    807  OD2 ASP A 103     129.215  67.666  72.640  1.00106.71           O  
ANISOU  807  OD2 ASP A 103    15091  13718  11737   -856   1997    409       O  
ATOM    808  N   GLN A 104     131.701  71.665  69.490  1.00105.04           N  
ANISOU  808  N   GLN A 104    14589  13447  11874   -284   1024    371       N  
ATOM    809  CA  GLN A 104     132.308  72.187  68.272  1.00 80.64           C  
ANISOU  809  CA  GLN A 104    11489  10276   8873   -237    866    389       C  
ATOM    810  C   GLN A 104     133.058  73.494  68.476  1.00 77.05           C  
ANISOU  810  C   GLN A 104    11080   9773   8424    -94    720    379       C  
ATOM    811  O   GLN A 104     134.035  73.745  67.768  1.00 65.10           O  
ANISOU  811  O   GLN A 104     9628   8148   6960    -83    631    432       O  
ATOM    812  CB  GLN A 104     131.247  72.402  67.183  1.00 69.37           C  
ANISOU  812  CB  GLN A 104     9905   8934   7519   -252    828    287       C  
ATOM    813  CG  GLN A 104     130.594  71.126  66.674  1.00 79.87           C  
ANISOU  813  CG  GLN A 104    11175  10300   8874   -427    949    269       C  
ATOM    814  CD  GLN A 104     129.496  70.621  67.588  1.00 84.00           C  
ANISOU  814  CD  GLN A 104    11596  10961   9358   -535   1129    182       C  
ATOM    815  OE1 GLN A 104     128.764  71.405  68.190  1.00 86.20           O  
ANISOU  815  OE1 GLN A 104    11755  11380   9618   -450   1127     76       O  
ATOM    816  NE2 GLN A 104     129.376  69.304  67.695  1.00101.91           N  
ANISOU  816  NE2 GLN A 104    13930  13182  11609   -728   1302    221       N  
ATOM    817  N   ILE A 105     132.629  74.328  69.420  1.00 98.26           N  
ANISOU  817  N   ILE A 105    13742  12533  11059      2    707    303       N  
ATOM    818  CA  ILE A 105     133.232  75.632  69.662  1.00 93.13           C  
ANISOU  818  CA  ILE A 105    13150  11824  10413    122    576    268       C  
ATOM    819  C   ILE A 105     133.878  75.626  71.040  1.00 89.79           C  
ANISOU  819  C   ILE A 105    12812  11407   9897    161    590    279       C  
ATOM    820  O   ILE A 105     133.237  75.261  72.033  1.00 95.20           O  
ANISOU  820  O   ILE A 105    13493  12189  10489    173    694    257       O  
ATOM    821  CB  ILE A 105     132.195  76.764  69.557  1.00 93.03           C  
ANISOU  821  CB  ILE A 105    13065  11880  10402    246    519    146       C  
ATOM    822  CG1 ILE A 105     131.447  76.691  68.224  1.00 83.38           C  
ANISOU  822  CG1 ILE A 105    11754  10685   9241    247    489    116       C  
ATOM    823  CG2 ILE A 105     132.867  78.123  69.721  1.00 93.19           C  
ANISOU  823  CG2 ILE A 105    13196  11787  10423    352    396    112       C  
ATOM    824  CD1 ILE A 105     130.372  77.750  68.069  1.00 73.63           C  
ANISOU  824  CD1 ILE A 105    10449   9539   7989    420    414    -18       C  
ATOM    825  N   VAL A 106     135.150  76.025  71.097  1.00 85.62           N  
ANISOU  825  N   VAL A 106    12360  10785   9388    179    491    300       N  
ATOM    826  CA  VAL A 106     135.770  76.359  72.378  1.00 80.43           C  
ANISOU  826  CA  VAL A 106    11770  10148   8641    255    448    262       C  
ATOM    827  C   VAL A 106     135.042  77.540  73.010  1.00 75.83           C  
ANISOU  827  C   VAL A 106    11183   9607   8020    359    412    148       C  
ATOM    828  O   VAL A 106     134.511  77.451  74.123  1.00 74.80           O  
ANISOU  828  O   VAL A 106    11074   9571   7776    426    473    112       O  
ATOM    829  CB  VAL A 106     137.266  76.664  72.185  1.00 76.88           C  
ANISOU  829  CB  VAL A 106    11351   9615   8245    238    334    260       C  
ATOM    830  CG1 VAL A 106     137.941  76.888  73.530  1.00 80.26           C  
ANISOU  830  CG1 VAL A 106    11832  10093   8569    327    266    196       C  
ATOM    831  CG2 VAL A 106     137.944  75.538  71.403  1.00 63.63           C  
ANISOU  831  CG2 VAL A 106     9666   7901   6609    160    369    364       C  
ATOM    832  N   GLY A 107     135.007  78.657  72.295  1.00 87.35           N  
ANISOU  832  N   GLY A 107    12644  10984   9560    384    325     91       N  
ATOM    833  CA  GLY A 107     134.306  79.842  72.745  1.00 71.50           C  
ANISOU  833  CA  GLY A 107    10661   8991   7516    509    282    -22       C  
ATOM    834  C   GLY A 107     134.516  80.957  71.745  1.00 72.12           C  
ANISOU  834  C   GLY A 107    10810   8914   7677    526    191    -54       C  
ATOM    835  O   GLY A 107     135.108  80.753  70.684  1.00 65.81           O  
ANISOU  835  O   GLY A 107    10026   8016   6962    432    181     15       O  
ATOM    836  N   TRP A 108     134.026  82.145  72.085  1.00 82.86           N  
ANISOU  836  N   TRP A 108    12243  10240   8998    657    137   -157       N  
ATOM    837  CA  TRP A 108     134.293  83.324  71.278  1.00 76.99           C  
ANISOU  837  CA  TRP A 108    11645   9302   8304    686     62   -190       C  
ATOM    838  C   TRP A 108     135.099  84.333  72.088  1.00 81.93           C  
ANISOU  838  C   TRP A 108    12405   9811   8914    680     -2   -283       C  
ATOM    839  O   TRP A 108     135.023  84.378  73.320  1.00 70.50           O  
ANISOU  839  O   TRP A 108    10939   8460   7386    739    -13   -353       O  
ATOM    840  CB  TRP A 108     132.998  83.955  70.743  1.00 74.42           C  
ANISOU  840  CB  TRP A 108    11340   8997   7940    874     40   -243       C  
ATOM    841  CG  TRP A 108     132.069  84.487  71.781  1.00 81.46           C  
ANISOU  841  CG  TRP A 108    12210  10008   8734   1053     34   -360       C  
ATOM    842  CD1 TRP A 108     131.153  83.779  72.500  1.00 86.52           C  
ANISOU  842  CD1 TRP A 108    12672  10884   9317   1100    113   -392       C  
ATOM    843  CD2 TRP A 108     131.938  85.852  72.195  1.00 82.91           C  
ANISOU  843  CD2 TRP A 108    12570  10073   8858   1210    -38   -468       C  
ATOM    844  NE1 TRP A 108     130.470  84.616  73.349  1.00 88.79           N  
ANISOU  844  NE1 TRP A 108    12992  11230   9513   1285     96   -515       N  
ATOM    845  CE2 TRP A 108     130.933  85.894  73.181  1.00 81.63           C  
ANISOU  845  CE2 TRP A 108    12308  10105   8601   1369     -8   -564       C  
ATOM    846  CE3 TRP A 108     132.579  87.041  71.834  1.00 81.83           C  
ANISOU  846  CE3 TRP A 108    12685   9672   8736   1221   -106   -498       C  
ATOM    847  CZ2 TRP A 108     130.552  87.076  73.809  1.00 80.83           C  
ANISOU  847  CZ2 TRP A 108    12346   9952   8414   1565    -63   -689       C  
ATOM    848  CZ3 TRP A 108     132.198  88.216  72.459  1.00 83.30           C  
ANISOU  848  CZ3 TRP A 108    13033   9780   8838   1400   -159   -620       C  
ATOM    849  CH2 TRP A 108     131.194  88.224  73.436  1.00 85.03           C  
ANISOU  849  CH2 TRP A 108    13143  10207   8958   1584   -147   -715       C  
ATOM    850  N   VAL A 109     135.885  85.132  71.373  1.00 94.32           N  
ANISOU  850  N   VAL A 109    14119  11164  10553    596    -34   -291       N  
ATOM    851  CA  VAL A 109     136.874  86.023  71.967  1.00 77.89           C  
ANISOU  851  CA  VAL A 109    12153   8949   8491    513    -83   -394       C  
ATOM    852  C   VAL A 109     136.838  87.345  71.219  1.00 78.76           C  
ANISOU  852  C   VAL A 109    12511   8795   8618    533    -92   -433       C  
ATOM    853  O   VAL A 109     136.859  87.362  69.984  1.00 88.50           O  
ANISOU  853  O   VAL A 109    13823   9907   9896    494    -50   -346       O  
ATOM    854  CB  VAL A 109     138.287  85.408  71.909  1.00 74.93           C  
ANISOU  854  CB  VAL A 109    11681   8583   8207    301    -76   -373       C  
ATOM    855  CG1 VAL A 109     139.354  86.480  72.076  1.00 92.88           C  
ANISOU  855  CG1 VAL A 109    14069  10681  10541    161   -111   -501       C  
ATOM    856  CG2 VAL A 109     138.440  84.333  72.967  1.00 75.65           C  
ANISOU  856  CG2 VAL A 109    11607   8899   8235    329    -92   -367       C  
ATOM    857  N   GLY A 110     136.789  88.450  71.954  1.00 86.77           N  
ANISOU  857  N   GLY A 110    13685   9704   9581    601   -140   -562       N  
ATOM    858  CA  GLY A 110     136.830  89.741  71.300  1.00 87.55           C  
ANISOU  858  CA  GLY A 110    14082   9505   9680    614   -134   -601       C  
ATOM    859  C   GLY A 110     136.544  90.884  72.249  1.00 82.26           C  
ANISOU  859  C   GLY A 110    13594   8736   8925    739   -192   -753       C  
ATOM    860  O   GLY A 110     136.344  90.703  73.454  1.00 77.28           O  
ANISOU  860  O   GLY A 110    12847   8282   8235    815   -241   -837       O  
ATOM    861  N   TRP A 111     136.523  92.082  71.656  1.00 95.53           N  
ANISOU  861  N   TRP A 111    15602  10110  10586    769   -176   -785       N  
ATOM    862  CA  TRP A 111     136.288  93.312  72.406  1.00 93.14           C  
ANISOU  862  CA  TRP A 111    15549   9643  10199    888   -223   -934       C  
ATOM    863  C   TRP A 111     134.910  93.327  73.054  1.00103.33           C  
ANISOU  863  C   TRP A 111    16784  11125  11350   1235   -287   -973       C  
ATOM    864  O   TRP A 111     134.710  94.011  74.064  1.00100.25           O  
ANISOU  864  O   TRP A 111    16494  10716  10881   1346   -337  -1111       O  
ATOM    865  CB  TRP A 111     136.464  94.510  71.470  1.00 89.85           C  
ANISOU  865  CB  TRP A 111    15547   8822   9768    868   -169   -932       C  
ATOM    866  CG  TRP A 111     136.106  95.842  72.055  1.00100.31           C  
ANISOU  866  CG  TRP A 111    17207   9920  10986   1027   -209  -1073       C  
ATOM    867  CD1 TRP A 111     136.934  96.690  72.733  1.00107.43           C  
ANISOU  867  CD1 TRP A 111    18282  10618  11919    836   -203  -1230       C  
ATOM    868  CD2 TRP A 111     134.832  96.494  71.987  1.00103.81           C  
ANISOU  868  CD2 TRP A 111    17860  10314  11270   1419   -265  -1088       C  
ATOM    869  NE1 TRP A 111     136.250  97.824  73.103  1.00104.11           N  
ANISOU  869  NE1 TRP A 111    18196   9998  11364   1082   -244  -1330       N  
ATOM    870  CE2 TRP A 111     134.958  97.728  72.656  1.00107.08           C  
ANISOU  870  CE2 TRP A 111    18599  10470  11615   1459   -285  -1243       C  
ATOM    871  CE3 TRP A 111     133.596  96.150  71.432  1.00103.32           C  
ANISOU  871  CE3 TRP A 111    17727  10416  11113   1750   -307  -1008       C  
ATOM    872  CZ2 TRP A 111     133.894  98.620  72.784  1.00111.85           C  
ANISOU  872  CZ2 TRP A 111    19480  10967  12052   1843   -343  -1304       C  
ATOM    873  CZ3 TRP A 111     132.541  97.037  71.559  1.00107.46           C  
ANISOU  873  CZ3 TRP A 111    18488  10865  11477   2132   -375  -1085       C  
ATOM    874  CH2 TRP A 111     132.697  98.257  72.230  1.00114.97           C  
ANISOU  874  CH2 TRP A 111    19781  11548  12353   2189   -391  -1224       C  
ATOM    875  N   LEU A 112     133.950  92.588  72.493  1.00119.40           N  
ANISOU  875  N   LEU A 112    18654  13358  13356   1405   -281   -872       N  
ATOM    876  CA  LEU A 112     132.629  92.506  73.109  1.00124.15           C  
ANISOU  876  CA  LEU A 112    19137  14193  13841   1710   -320   -931       C  
ATOM    877  C   LEU A 112     132.694  91.830  74.472  1.00119.40           C  
ANISOU  877  C   LEU A 112    18294  13853  13221   1661   -313   -988       C  
ATOM    878  O   LEU A 112     131.953  92.196  75.392  1.00118.54           O  
ANISOU  878  O   LEU A 112    18184  13853  13001   1869   -335  -1096       O  
ATOM    879  CB  LEU A 112     131.663  91.758  72.191  1.00118.13           C  
ANISOU  879  CB  LEU A 112    18197  13616  13072   1850   -310   -839       C  
ATOM    880  CG  LEU A 112     131.047  92.555  71.044  1.00112.24           C  
ANISOU  880  CG  LEU A 112    17703  12685  12258   2082   -354   -824       C  
ATOM    881  CD1 LEU A 112     130.147  91.661  70.216  1.00110.62           C  
ANISOU  881  CD1 LEU A 112    17256  12722  12054   2199   -364   -763       C  
ATOM    882  CD2 LEU A 112     130.271  93.739  71.591  1.00117.44           C  
ANISOU  882  CD2 LEU A 112    18581  13265  12776   2405   -420   -965       C  
ATOM    883  N   LYS A 113     133.577  90.841  74.621  1.00114.67           N  
ANISOU  883  N   LYS A 113    17506  13354  12710   1409   -280   -919       N  
ATOM    884  CA  LYS A 113     133.716  90.137  75.889  1.00108.92           C  
ANISOU  884  CA  LYS A 113    16596  12855  11936   1380   -274   -957       C  
ATOM    885  C   LYS A 113     134.334  91.005  76.977  1.00108.13           C  
ANISOU  885  C   LYS A 113    16651  12651  11783   1368   -342  -1113       C  
ATOM    886  O   LYS A 113     134.323  90.603  78.146  1.00111.88           O  
ANISOU  886  O   LYS A 113    17029  13308  12173   1409   -351  -1168       O  
ATOM    887  CB  LYS A 113     134.550  88.872  75.691  1.00 99.33           C  
ANISOU  887  CB  LYS A 113    15181  11749  10810   1152   -236   -843       C  
ATOM    888  CG  LYS A 113     133.979  87.646  76.376  1.00102.17           C  
ANISOU  888  CG  LYS A 113    15320  12397  11102   1200   -171   -789       C  
ATOM    889  CD  LYS A 113     134.646  86.378  75.878  1.00104.23           C  
ANISOU  889  CD  LYS A 113    15429  12728  11446   1012   -126   -655       C  
ATOM    890  CE  LYS A 113     134.030  85.147  76.520  1.00109.25           C  
ANISOU  890  CE  LYS A 113    15902  13606  12000   1049    -32   -592       C  
ATOM    891  NZ  LYS A 113     132.555  85.083  76.308  1.00106.98           N  
ANISOU  891  NZ  LYS A 113    15531  13445  11672   1192     46   -598       N  
ATOM    892  N   ALA A 114     134.864  92.173  76.623  1.00103.16           N  
ANISOU  892  N   ALA A 114    16281  11725  11189   1308   -382  -1190       N  
ATOM    893  CA  ALA A 114     135.436  93.112  77.578  1.00 97.17           C  
ANISOU  893  CA  ALA A 114    15695  10837  10388   1279   -450  -1368       C  
ATOM    894  C   ALA A 114     135.435  94.514  76.978  1.00 97.26           C  
ANISOU  894  C   ALA A 114    16063  10489  10404   1304   -456  -1436       C  
ATOM    895  O   ALA A 114     136.490  95.009  76.562  1.00 85.66           O  
ANISOU  895  O   ALA A 114    14730   8778   9037   1049   -443  -1476       O  
ATOM    896  CB  ALA A 114     136.855  92.693  77.965  1.00 93.01           C  
ANISOU  896  CB  ALA A 114    15049  10338   9952    996   -487  -1416       C  
ATOM    897  N   PRO A 115     134.276  95.179  76.909  1.00 98.18           N  
ANISOU  897  N   PRO A 115    16346  10555  10404   1610   -464  -1459       N  
ATOM    898  CA  PRO A 115     134.232  96.500  76.255  1.00101.56           C  
ANISOU  898  CA  PRO A 115    17178  10603  10807   1673   -463  -1505       C  
ATOM    899  C   PRO A 115     135.144  97.526  76.901  1.00117.89           C  
ANISOU  899  C   PRO A 115    19503  12405  12885   1502   -492  -1680       C  
ATOM    900  O   PRO A 115     135.719  98.369  76.202  1.00105.94           O  
ANISOU  900  O   PRO A 115    18299  10530  11423   1347   -446  -1697       O  
ATOM    901  CB  PRO A 115     132.753  96.899  76.376  1.00101.41           C  
ANISOU  901  CB  PRO A 115    17233  10669  10630   2099   -494  -1534       C  
ATOM    902  CG  PRO A 115     132.020  95.609  76.563  1.00107.71           C  
ANISOU  902  CG  PRO A 115    17619  11882  11422   2187   -472  -1451       C  
ATOM    903  CD  PRO A 115     132.944  94.739  77.359  1.00107.20           C  
ANISOU  903  CD  PRO A 115    17320  11985  11428   1916   -461  -1449       C  
ATOM    904  N   ASP A 116     135.290  97.477  78.222  1.00142.87           N  
ANISOU  904  N   ASP A 116    22562  15731  15994   1519   -558  -1821       N  
ATOM    905  CA  ASP A 116     136.169  98.381  78.961  1.00145.17           C  
ANISOU  905  CA  ASP A 116    23054  15812  16292   1348   -607  -2025       C  
ATOM    906  C   ASP A 116     137.466  97.626  79.234  1.00141.35           C  
ANISOU  906  C   ASP A 116    22296  15470  15943   1002   -629  -2058       C  
ATOM    907  O   ASP A 116     137.612  96.952  80.254  1.00144.35           O  
ANISOU  907  O   ASP A 116    22437  16136  16272   1033   -700  -2113       O  
ATOM    908  CB  ASP A 116     135.500  98.851  80.246  1.00143.85           C  
ANISOU  908  CB  ASP A 116    22963  15740  15953   1621   -685  -2182       C  
ATOM    909  CG  ASP A 116     134.144  99.481  79.999  1.00147.43           C  
ANISOU  909  CG  ASP A 116    23630  16123  16265   2015   -671  -2159       C  
ATOM    910  OD1 ASP A 116     134.098 100.608  79.463  1.00150.64           O  
ANISOU  910  OD1 ASP A 116    24430  16159  16648   2063   -658  -2205       O  
ATOM    911  OD2 ASP A 116     133.122  98.839  80.325  1.00146.27           O  
ANISOU  911  OD2 ASP A 116    23260  16290  16026   2279   -665  -2103       O  
ATOM    912  N   THR A 117     138.414  97.737  78.306  1.00137.23           N  
ANISOU  912  N   THR A 117    21816  14748  15579    687   -560  -2027       N  
ATOM    913  CA  THR A 117     139.681  97.030  78.411  1.00132.31           C  
ANISOU  913  CA  THR A 117    20907  14268  15095    366   -577  -2069       C  
ATOM    914  C   THR A 117     140.817  97.952  77.990  1.00136.74           C  
ANISOU  914  C   THR A 117    21658  14503  15792      3   -520  -2216       C  
ATOM    915  O   THR A 117     140.619  98.924  77.256  1.00134.00           O  
ANISOU  915  O   THR A 117    21676  13792  15447    -27   -423  -2201       O  
ATOM    916  CB  THR A 117     139.695  95.755  77.554  1.00123.20           C  
ANISOU  916  CB  THR A 117    19472  13316  14021    326   -514  -1845       C  
ATOM    917  OG1 THR A 117     140.960  95.096  77.695  1.00119.75           O  
ANISOU  917  OG1 THR A 117    18764  13027  13708     49   -540  -1905       O  
ATOM    918  CG2 THR A 117     139.470  96.094  76.090  1.00127.09           C  
ANISOU  918  CG2 THR A 117    20171  13544  14572    280   -387  -1693       C  
ATOM    919  N   THR A 118     142.018  97.632  78.470  1.00143.51           N  
ANISOU  919  N   THR A 118    22270  15500  16757   -270   -576  -2370       N  
ATOM    920  CA  THR A 118     143.220  98.391  78.157  1.00144.89           C  
ANISOU  920  CA  THR A 118    22535  15428  17088   -674   -512  -2553       C  
ATOM    921  C   THR A 118     144.158  97.647  77.219  1.00149.15           C  
ANISOU  921  C   THR A 118    22816  16048  17806   -964   -413  -2469       C  
ATOM    922  O   THR A 118     145.247  98.152  76.923  1.00148.55           O  
ANISOU  922  O   THR A 118    22745  15817  17882  -1341   -334  -2633       O  
ATOM    923  CB  THR A 118     143.967  98.759  79.444  1.00139.20           C  
ANISOU  923  CB  THR A 118    21718  14808  16363   -789   -663  -2869       C  
ATOM    924  OG1 THR A 118     144.219  97.573  80.209  1.00138.68           O  
ANISOU  924  OG1 THR A 118    21250  15181  16260   -674   -808  -2872       O  
ATOM    925  CG2 THR A 118     143.148  99.734  80.274  1.00127.82           C  
ANISOU  925  CG2 THR A 118    20610  13203  14752   -549   -733  -2984       C  
ATOM    926  N   ASP A 119     143.771  96.468  76.752  1.00151.02           N  
ANISOU  926  N   ASP A 119    22825  16525  18031   -810   -403  -2236       N  
ATOM    927  CA  ASP A 119     144.599  95.706  75.825  1.00146.82           C  
ANISOU  927  CA  ASP A 119    22057  16075  17652  -1046   -306  -2143       C  
ATOM    928  C   ASP A 119     144.545  96.351  74.445  1.00158.17           C  
ANISOU  928  C   ASP A 119    23802  17143  19152  -1199   -100  -2021       C  
ATOM    929  O   ASP A 119     143.450  96.516  73.891  1.00157.45           O  
ANISOU  929  O   ASP A 119    23959  16913  18952   -949    -57  -1835       O  
ATOM    930  CB  ASP A 119     144.121  94.255  75.768  1.00138.16           C  
ANISOU  930  CB  ASP A 119    20674  15319  16502   -816   -356  -1931       C  
ATOM    931  CG  ASP A 119     145.178  93.305  75.226  1.00134.79           C  
ANISOU  931  CG  ASP A 119    19923  15073  16217  -1029   -317  -1902       C  
ATOM    932  OD1 ASP A 119     145.922  93.691  74.299  1.00133.66           O  
ANISOU  932  OD1 ASP A 119    19829  14740  16214  -1323   -174  -1924       O  
ATOM    933  OD2 ASP A 119     145.264  92.166  75.731  1.00130.38           O  
ANISOU  933  OD2 ASP A 119    19079  14841  15617   -895   -418  -1858       O  
ATOM    934  N   PRO A 120     145.685  96.742  73.863  1.00169.57           N  
ANISOU  934  N   PRO A 120    25247  18424  20759  -1595     36  -2129       N  
ATOM    935  CA  PRO A 120     145.678  97.411  72.553  1.00171.43           C  
ANISOU  935  CA  PRO A 120    25837  18269  21030  -1753    262  -2011       C  
ATOM    936  C   PRO A 120     145.146  96.544  71.422  1.00160.20           C  
ANISOU  936  C   PRO A 120    24380  16911  19578  -1595    338  -1713       C  
ATOM    937  O   PRO A 120     144.300  96.985  70.635  1.00162.53           O  
ANISOU  937  O   PRO A 120    25035  16950  19768  -1421    419  -1546       O  
ATOM    938  CB  PRO A 120     147.158  97.742  72.329  1.00178.30           C  
ANISOU  938  CB  PRO A 120    26589  19060  22099  -2249    397  -2219       C  
ATOM    939  CG  PRO A 120     147.746  97.791  73.694  1.00180.79           C  
ANISOU  939  CG  PRO A 120    26633  19608  22450  -2320    210  -2513       C  
ATOM    940  CD  PRO A 120     147.029  96.725  74.460  1.00177.78           C  
ANISOU  940  CD  PRO A 120    25990  19615  21942  -1918    -10  -2405       C  
ATOM    941  N   THR A 121     145.652  95.311  71.324  1.00146.21           N  
ANISOU  941  N   THR A 121    22187  15479  17888  -1638    305  -1657       N  
ATOM    942  CA  THR A 121     145.201  94.420  70.258  1.00134.57           C  
ANISOU  942  CA  THR A 121    20664  14075  16391  -1506    372  -1393       C  
ATOM    943  C   THR A 121     143.716  94.109  70.384  1.00121.19           C  
ANISOU  943  C   THR A 121    19060  12460  14525  -1080    261  -1225       C  
ATOM    944  O   THR A 121     143.024  93.964  69.370  1.00126.11           O  
ANISOU  944  O   THR A 121    19848  12982  15087   -936    330  -1030       O  
ATOM    945  CB  THR A 121     146.011  93.119  70.256  1.00131.02           C  
ANISOU  945  CB  THR A 121    19753  13981  16046  -1603    341  -1383       C  
ATOM    946  OG1 THR A 121     145.773  92.398  71.472  1.00134.71           O  
ANISOU  946  OG1 THR A 121    19947  14785  16452  -1395    135  -1441       O  
ATOM    947  CG2 THR A 121     147.503  93.408  70.120  1.00130.88           C  
ANISOU  947  CG2 THR A 121    19584  13937  16209  -2021    450  -1583       C  
ATOM    948  N   VAL A 122     143.207  94.017  71.615  1.00107.20           N  
ANISOU  948  N   VAL A 122    17182  10880  12671   -875     94  -1314       N  
ATOM    949  CA  VAL A 122     141.774  93.818  71.805  1.00101.42           C  
ANISOU  949  CA  VAL A 122    16522  10232  11782   -492     12  -1193       C  
ATOM    950  C   VAL A 122     141.013  95.099  71.492  1.00100.42           C  
ANISOU  950  C   VAL A 122    16844   9759  11550   -347     49  -1198       C  
ATOM    951  O   VAL A 122     139.894  95.053  70.966  1.00 95.38           O  
ANISOU  951  O   VAL A 122    16335   9105  10802    -60     40  -1060       O  
ATOM    952  CB  VAL A 122     141.488  93.320  73.233  1.00 94.68           C  
ANISOU  952  CB  VAL A 122    15432   9686  10857   -325   -147  -1287       C  
ATOM    953  CG1 VAL A 122     139.994  93.089  73.430  1.00 82.14           C  
ANISOU  953  CG1 VAL A 122    13883   8209   9116     44   -199  -1179       C  
ATOM    954  CG2 VAL A 122     142.269  92.046  73.515  1.00 85.06           C  
ANISOU  954  CG2 VAL A 122    13824   8782   9713   -432   -187  -1274       C  
ATOM    955  N   SER A 123     141.599  96.258  71.801  1.00118.30           N  
ANISOU  955  N   SER A 123    19362  11745  13842   -532     89  -1372       N  
ATOM    956  CA  SER A 123     140.981  97.526  71.432  1.00114.46           C  
ANISOU  956  CA  SER A 123    19374  10871  13246   -402    144  -1375       C  
ATOM    957  C   SER A 123     141.080  97.797  69.937  1.00119.88           C  
ANISOU  957  C   SER A 123    20352  11259  13937   -488    317  -1216       C  
ATOM    958  O   SER A 123     140.303  98.601  69.413  1.00122.48           O  
ANISOU  958  O   SER A 123    21105  11305  14128   -262    347  -1150       O  
ATOM    959  CB  SER A 123     141.621  98.673  72.216  1.00108.33           C  
ANISOU  959  CB  SER A 123    18813   9853  12495   -606    150  -1619       C  
ATOM    960  OG  SER A 123     140.999  99.908  71.909  1.00119.53           O  
ANISOU  960  OG  SER A 123    20763  10868  13786   -453    204  -1622       O  
ATOM    961  N   ALA A 124     142.018  97.149  69.244  1.00125.10           N  
ANISOU  961  N   ALA A 124    20813  11979  14738   -784    431  -1157       N  
ATOM    962  CA  ALA A 124     142.103  97.242  67.793  1.00115.44           C  
ANISOU  962  CA  ALA A 124    19844  10513  13505   -850    605   -987       C  
ATOM    963  C   ALA A 124     141.073  96.370  67.090  1.00106.42           C  
ANISOU  963  C   ALA A 124    18610   9562  12262   -512    536   -773       C  
ATOM    964  O   ALA A 124     140.933  96.471  65.865  1.00110.98           O  
ANISOU  964  O   ALA A 124    19441   9942  12783   -478    648   -623       O  
ATOM    965  CB  ALA A 124     143.507  96.861  67.318  1.00116.54           C  
ANISOU  965  CB  ALA A 124    19782  10666  13830  -1294    767  -1021       C  
ATOM    966  N   MET A 125     140.355  95.522  67.831  1.00102.64           N  
ANISOU  966  N   MET A 125    17787   9458  11752   -271    362   -765       N  
ATOM    967  CA  MET A 125     139.269  94.707  67.293  1.00100.62           C  
ANISOU  967  CA  MET A 125    17416   9409  11406     44    287   -604       C  
ATOM    968  C   MET A 125     138.003  95.514  67.054  1.00 97.64           C  
ANISOU  968  C   MET A 125    17384   8872  10842    430    223   -579       C  
ATOM    969  O   MET A 125     136.924  94.939  66.876  1.00 84.70           O  
ANISOU  969  O   MET A 125    15606   7457   9118    735    123   -508       O  
ATOM    970  CB  MET A 125     138.977  93.533  68.231  1.00 98.77           C  
ANISOU  970  CB  MET A 125    16709   9613  11205    126    160   -622       C  
ATOM    971  CG  MET A 125     140.204  92.706  68.597  1.00 82.78           C  
ANISOU  971  CG  MET A 125    14344   7772   9336   -188    188   -664       C  
ATOM    972  SD  MET A 125     139.850  91.331  69.703  1.00 78.14           S  
ANISOU  972  SD  MET A 125    13299   7647   8742    -61     55   -666       S  
ATOM    973  CE  MET A 125     139.034  90.209  68.577  1.00 91.29           C  
ANISOU  973  CE  MET A 125    14850   9457  10378     92     80   -455       C  
ATOM    974  N   LYS A 126     138.142  96.839  67.060  1.00104.50           N  
ANISOU  974  N   LYS A 126    18700   9359  11646    418    281   -655       N  
ATOM    975  CA  LYS A 126     137.056  97.764  66.776  1.00111.87           C  
ANISOU  975  CA  LYS A 126    20046  10079  12382    804    227   -642       C  
ATOM    976  C   LYS A 126     137.594  98.885  65.897  1.00106.35           C  
ANISOU  976  C   LYS A 126    19921   8861  11626    674    396   -609       C  
ATOM    977  O   LYS A 126     138.754  99.287  66.019  1.00102.27           O  
ANISOU  977  O   LYS A 126    19495   8133  11231    267    544   -683       O  
ATOM    978  CB  LYS A 126     136.446  98.327  68.070  1.00120.33           C  
ANISOU  978  CB  LYS A 126    21120  11220  13382   1015     99   -805       C  
ATOM    979  CG  LYS A 126     136.536  99.838  68.210  1.00136.67           C  
ANISOU  979  CG  LYS A 126    23742  12834  15351   1048    149   -906       C  
ATOM    980  CD  LYS A 126     136.170 100.288  69.612  1.00142.85           C  
ANISOU  980  CD  LYS A 126    24472  13712  16092   1184     32  -1090       C  
ATOM    981  CE  LYS A 126     137.217  99.848  70.621  1.00145.81           C  
ANISOU  981  CE  LYS A 126    24494  14265  16641    803     35  -1218       C  
ATOM    982  NZ  LYS A 126     138.551 100.444  70.329  1.00149.24           N  
ANISOU  982  NZ  LYS A 126    25143  14362  17199    349    195  -1284       N  
ATOM    983  N   THR A 127     136.745  99.377  65.000  1.00112.97           N  
ANISOU  983  N   THR A 127    21151   9500  12271   1022    381   -508       N  
ATOM    984  CA  THR A 127     137.161 100.413  64.069  1.00114.91           C  
ANISOU  984  CA  THR A 127    22019   9223  12420    943    560   -446       C  
ATOM    985  C   THR A 127     137.129 101.786  64.739  1.00113.00           C  
ANISOU  985  C   THR A 127    22237   8610  12089    988    580   -586       C  
ATOM    986  O   THR A 127     136.442 102.004  65.740  1.00110.59           O  
ANISOU  986  O   THR A 127    21829   8458  11734   1239    417   -709       O  
ATOM    987  CB  THR A 127     136.271 100.407  62.827  1.00 99.03           C  
ANISOU  987  CB  THR A 127    20295   7132  10200   1342    519   -283       C  
ATOM    988  OG1 THR A 127     134.914 100.663  63.208  1.00100.97           O  
ANISOU  988  OG1 THR A 127    20567   7523  10273   1873    301   -338       O  
ATOM    989  CG2 THR A 127     136.350  99.058  62.135  1.00 95.90           C  
ANISOU  989  CG2 THR A 127    19467   7078   9893   1270    506   -158       C  
ATOM    990  N   GLN A 128     137.891 102.721  64.161  1.00123.60           N  
ANISOU  990  N   GLN A 128    24112   9443  13405    732    804   -572       N  
ATOM    991  CA  GLN A 128     138.048 104.046  64.755  1.00122.17           C  
ANISOU  991  CA  GLN A 128    24414   8846  13159    684    866   -716       C  
ATOM    992  C   GLN A 128     136.742 104.829  64.803  1.00119.25           C  
ANISOU  992  C   GLN A 128    24465   8329  12517   1283    711   -715       C  
ATOM    993  O   GLN A 128     136.615 105.746  65.621  1.00112.92           O  
ANISOU  993  O   GLN A 128    23930   7317  11657   1348    681   -867       O  
ATOM    994  CB  GLN A 128     139.102 104.848  63.985  1.00141.52           C  
ANISOU  994  CB  GLN A 128    27390  10753  15628    264   1180   -687       C  
ATOM    995  CG  GLN A 128     140.524 104.295  64.074  1.00158.56           C  
ANISOU  995  CG  GLN A 128    29150  13025  18070   -372   1356   -756       C  
ATOM    996  CD  GLN A 128     140.783 103.143  63.114  1.00167.03           C  
ANISOU  996  CD  GLN A 128    29888  14362  19214   -452   1410   -578       C  
ATOM    997  OE1 GLN A 128     139.879 102.376  62.782  1.00164.28           O  
ANISOU  997  OE1 GLN A 128    29329  14317  18773    -59   1232   -449       O  
ATOM    998  NE2 GLN A 128     142.025 103.023  62.659  1.00169.31           N  
ANISOU  998  NE2 GLN A 128    30120  14540  19670   -972   1663   -590       N  
ATOM    999  N   ASP A 129     135.774 104.498  63.950  1.00127.46           N  
ANISOU  999  N   ASP A 129    25566   9481  13381   1734    602   -567       N  
ATOM   1000  CA  ASP A 129     134.477 105.159  63.949  1.00123.33           C  
ANISOU 1000  CA  ASP A 129    25382   8889  12591   2362    426   -584       C  
ATOM   1001  C   ASP A 129     133.438 104.407  64.773  1.00125.65           C  
ANISOU 1001  C   ASP A 129    25080   9761  12901   2709    163   -671       C  
ATOM   1002  O   ASP A 129     132.262 104.785  64.761  1.00121.84           O  
ANISOU 1002  O   ASP A 129    24753   9333  12209   3265     -6   -703       O  
ATOM   1003  CB  ASP A 129     133.977 105.347  62.515  1.00123.09           C  
ANISOU 1003  CB  ASP A 129    25810   8634  12325   2703    446   -402       C  
ATOM   1004  CG  ASP A 129     133.895 104.042  61.748  1.00112.15           C  
ANISOU 1004  CG  ASP A 129    23944   7651  11018   2680    399   -269       C  
ATOM   1005  OD1 ASP A 129     134.730 103.148  62.000  1.00107.37           O  
ANISOU 1005  OD1 ASP A 129    22835   7292  10668   2217    479   -267       O  
ATOM   1006  OD2 ASP A 129     132.996 103.912  60.891  1.00112.56           O  
ANISOU 1006  OD2 ASP A 129    24128   7772  10866   3142    272   -180       O  
ATOM   1007  N   LEU A 130     133.847 103.347  65.476  1.00134.82           N  
ANISOU 1007  N   LEU A 130    25573  11355  14296   2400    134   -716       N  
ATOM   1008  CA  LEU A 130     132.977 102.594  66.384  1.00129.12           C  
ANISOU 1008  CA  LEU A 130    24285  11170  13607   2644    -65   -805       C  
ATOM   1009  C   LEU A 130     131.785 101.977  65.659  1.00123.35           C  
ANISOU 1009  C   LEU A 130    23370  10747  12749   3097   -216   -726       C  
ATOM   1010  O   LEU A 130     130.731 101.749  66.258  1.00113.59           O  
ANISOU 1010  O   LEU A 130    21847   9859  11453   3451   -380   -822       O  
ATOM   1011  CB  LEU A 130     132.498 103.467  67.549  1.00129.65           C  
ANISOU 1011  CB  LEU A 130    24502  11175  13583   2868   -154   -989       C  
ATOM   1012  CG  LEU A 130     133.365 103.537  68.809  1.00127.30           C  
ANISOU 1012  CG  LEU A 130    24014  10901  13452   2472   -108  -1139       C  
ATOM   1013  CD1 LEU A 130     134.808 103.895  68.488  1.00126.14           C  
ANISOU 1013  CD1 LEU A 130    24108  10376  13444   1923     98  -1126       C  
ATOM   1014  CD2 LEU A 130     132.777 104.542  69.783  1.00133.21           C  
ANISOU 1014  CD2 LEU A 130    25026  11527  14060   2768   -196  -1314       C  
ATOM   1015  N   ARG A 131     131.941 101.691  64.366  1.00136.03           N  
ANISOU 1015  N   ARG A 131    25127  12244  14316   3083   -156   -566       N  
ATOM   1016  CA  ARG A 131     130.863 101.121  63.569  1.00124.52           C  
ANISOU 1016  CA  ARG A 131    23513  11067  12732   3502   -309   -509       C  
ATOM   1017  C   ARG A 131     131.014  99.629  63.312  1.00103.73           C  
ANISOU 1017  C   ARG A 131    20275   8860  10277   3269   -316   -437       C  
ATOM   1018  O   ARG A 131     130.043  98.989  62.894  1.00 97.28           O  
ANISOU 1018  O   ARG A 131    19189   8379   9396   3580   -462   -438       O  
ATOM   1019  CB  ARG A 131     130.755 101.851  62.226  1.00121.80           C  
ANISOU 1019  CB  ARG A 131    23809  10309  12159   3751   -271   -387       C  
ATOM   1020  CG  ARG A 131     129.812 103.039  62.257  1.00134.84           C  
ANISOU 1020  CG  ARG A 131    25965  11734  13534   4315   -394   -468       C  
ATOM   1021  CD  ARG A 131     128.379 102.572  62.441  1.00151.49           C  
ANISOU 1021  CD  ARG A 131    27660  14349  15552   4838   -654   -580       C  
ATOM   1022  NE  ARG A 131     127.862 101.926  61.237  1.00166.74           N  
ANISOU 1022  NE  ARG A 131    29499  16465  17389   5072   -752   -492       N  
ATOM   1023  CZ  ARG A 131     126.837 101.079  61.222  1.00170.84           C  
ANISOU 1023  CZ  ARG A 131    29477  17518  17915   5345   -943   -580       C  
ATOM   1024  NH1 ARG A 131     126.221 100.758  62.351  1.00174.86           N  
ANISOU 1024  NH1 ARG A 131    29490  18427  18522   5408  -1030   -744       N  
ATOM   1025  NH2 ARG A 131     126.435 100.545  60.077  1.00162.96           N  
ANISOU 1025  NH2 ARG A 131    28435  16656  16825   5540  -1035   -515       N  
ATOM   1026  N   HIS A 132     132.195  99.063  63.550  1.00100.37           N  
ANISOU 1026  N   HIS A 132    19630   8436  10068   2742   -167   -392       N  
ATOM   1027  CA  HIS A 132     132.432  97.649  63.312  1.00 98.68           C  
ANISOU 1027  CA  HIS A 132    18891   8587  10016   2516   -161   -318       C  
ATOM   1028  C   HIS A 132     133.336  97.093  64.400  1.00 95.87           C  
ANISOU 1028  C   HIS A 132    18151   8393   9883   2087    -90   -377       C  
ATOM   1029  O   HIS A 132     134.186  97.801  64.947  1.00 92.79           O  
ANISOU 1029  O   HIS A 132    17963   7742   9551   1834      8   -438       O  
ATOM   1030  CB  HIS A 132     133.072  97.398  61.938  1.00107.52           C  
ANISOU 1030  CB  HIS A 132    20220   9504  11128   2351    -37   -152       C  
ATOM   1031  CG  HIS A 132     132.390  98.107  60.810  1.00115.04           C  
ANISOU 1031  CG  HIS A 132    21678  10205  11827   2759    -86    -85       C  
ATOM   1032  ND1 HIS A 132     131.219  97.652  60.243  1.00115.37           N  
ANISOU 1032  ND1 HIS A 132    21572  10525  11737   3183   -273    -88       N  
ATOM   1033  CD2 HIS A 132     132.715  99.240  60.144  1.00117.10           C  
ANISOU 1033  CD2 HIS A 132    22610   9957  11926   2816     28    -21       C  
ATOM   1034  CE1 HIS A 132     130.852  98.476  59.277  1.00119.27           C  
ANISOU 1034  CE1 HIS A 132    22622  10709  11987   3523   -297    -31       C  
ATOM   1035  NE2 HIS A 132     131.743  99.448  59.197  1.00120.79           N  
ANISOU 1035  NE2 HIS A 132    23345  10401  12148   3310   -105     24       N  
ATOM   1036  N   THR A 133     133.137  95.814  64.710  1.00 99.77           N  
ANISOU 1036  N   THR A 133    18103   9316  10491   2016   -144   -368       N  
ATOM   1037  CA  THR A 133     134.015  95.081  65.609  1.00101.10           C  
ANISOU 1037  CA  THR A 133    17897   9667  10849   1642    -89   -401       C  
ATOM   1038  C   THR A 133     133.960  93.610  65.227  1.00 95.41           C  
ANISOU 1038  C   THR A 133    16744   9285  10221   1548    -97   -310       C  
ATOM   1039  O   THR A 133     132.925  93.111  64.775  1.00 91.90           O  
ANISOU 1039  O   THR A 133    16160   9054   9704   1813   -188   -288       O  
ATOM   1040  CB  THR A 133     133.632  95.271  67.086  1.00 93.14           C  
ANISOU 1040  CB  THR A 133    16714   8835   9839   1728   -169   -553       C  
ATOM   1041  OG1 THR A 133     134.570  94.576  67.918  1.00 89.53           O  
ANISOU 1041  OG1 THR A 133    15940   8536   9540   1384   -124   -583       O  
ATOM   1042  CG2 THR A 133     132.230  94.740  67.362  1.00 84.68           C  
ANISOU 1042  CG2 THR A 133    15361   8129   8685   2082   -295   -594       C  
ATOM   1043  N   PHE A 134     135.086  92.921  65.389  1.00 98.74           N  
ANISOU 1043  N   PHE A 134    16958   9757  10803   1175     -4   -274       N  
ATOM   1044  CA  PHE A 134     135.171  91.515  65.030  1.00 91.54           C  
ANISOU 1044  CA  PHE A 134    15679   9124   9978   1066      3   -185       C  
ATOM   1045  C   PHE A 134     135.532  90.676  66.248  1.00 88.01           C  
ANISOU 1045  C   PHE A 134    14847   8956   9638    901    -11   -243       C  
ATOM   1046  O   PHE A 134     136.141  91.162  67.205  1.00 86.37           O  
ANISOU 1046  O   PHE A 134    14659   8688   9469    773     -4   -342       O  
ATOM   1047  CB  PHE A 134     136.186  91.277  63.892  1.00 86.56           C  
ANISOU 1047  CB  PHE A 134    15161   8313   9414    816    133    -67       C  
ATOM   1048  CG  PHE A 134     137.617  91.143  64.348  1.00 77.55           C  
ANISOU 1048  CG  PHE A 134    13914   7123   8428    431    240    -98       C  
ATOM   1049  CD1 PHE A 134     138.152  89.899  64.652  1.00 75.45           C  
ANISOU 1049  CD1 PHE A 134    13260   7129   8280    257    246    -75       C  
ATOM   1050  CD2 PHE A 134     138.437  92.256  64.435  1.00 83.15           C  
ANISOU 1050  CD2 PHE A 134    14918   7516   9161    246    338   -165       C  
ATOM   1051  CE1 PHE A 134     139.465  89.772  65.059  1.00 76.54           C  
ANISOU 1051  CE1 PHE A 134    13275   7258   8550    -56    321   -130       C  
ATOM   1052  CE2 PHE A 134     139.755  92.134  64.839  1.00 80.31           C  
ANISOU 1052  CE2 PHE A 134    14412   7150   8953   -113    428   -232       C  
ATOM   1053  CZ  PHE A 134     140.268  90.890  65.152  1.00 79.75           C  
ANISOU 1053  CZ  PHE A 134    13922   7385   8992   -246    407   -219       C  
ATOM   1054  N   ILE A 135     135.138  89.408  66.195  1.00 95.58           N  
ANISOU 1054  N   ILE A 135    15478  10210  10629    912    -33   -188       N  
ATOM   1055  CA  ILE A 135     135.424  88.431  67.234  1.00 87.98           C  
ANISOU 1055  CA  ILE A 135    14182   9508   9737    782    -34   -213       C  
ATOM   1056  C   ILE A 135     136.124  87.242  66.594  1.00 81.51           C  
ANISOU 1056  C   ILE A 135    13182   8774   9013    579     30   -102       C  
ATOM   1057  O   ILE A 135     135.972  86.975  65.398  1.00 83.65           O  
ANISOU 1057  O   ILE A 135    13514   8990   9278    599     55    -11       O  
ATOM   1058  CB  ILE A 135     134.141  87.975  67.961  1.00 80.88           C  
ANISOU 1058  CB  ILE A 135    13074   8891   8766   1003    -96   -266       C  
ATOM   1059  CG1 ILE A 135     133.143  87.412  66.948  1.00 77.24           C  
ANISOU 1059  CG1 ILE A 135    12529   8549   8268   1157   -118   -211       C  
ATOM   1060  CG2 ILE A 135     133.530  89.125  68.745  1.00 82.75           C  
ANISOU 1060  CG2 ILE A 135    13469   9066   8906   1213   -155   -393       C  
ATOM   1061  CD1 ILE A 135     131.857  86.928  67.556  1.00 80.93           C  
ANISOU 1061  CD1 ILE A 135    12755   9314   8682   1337   -152   -286       C  
ATOM   1062  N   SER A 136     136.899  86.526  67.401  1.00 84.41           N  
ANISOU 1062  N   SER A 136    13344   9277   9452    410     47   -117       N  
ATOM   1063  CA  SER A 136     137.531  85.282  66.989  1.00 68.53           C  
ANISOU 1063  CA  SER A 136    11143   7379   7516    254     97    -24       C  
ATOM   1064  C   SER A 136     136.803  84.125  67.657  1.00 70.62           C  
ANISOU 1064  C   SER A 136    11172   7916   7746    334     78     -6       C  
ATOM   1065  O   SER A 136     136.535  84.168  68.861  1.00 67.67           O  
ANISOU 1065  O   SER A 136    10731   7657   7324    396     47    -80       O  
ATOM   1066  CB  SER A 136     139.017  85.267  67.353  1.00 68.71           C  
ANISOU 1066  CB  SER A 136    11115   7358   7632     23    130    -65       C  
ATOM   1067  OG  SER A 136     139.616  84.033  66.997  1.00 83.80           O  
ANISOU 1067  OG  SER A 136    12845   9393   9601    -84    170     17       O  
ATOM   1068  N   ILE A 137     136.483  83.099  66.876  1.00 82.96           N  
ANISOU 1068  N   ILE A 137    12631   9567   9321    322    112     88       N  
ATOM   1069  CA  ILE A 137     135.708  81.964  67.372  1.00 76.91           C  
ANISOU 1069  CA  ILE A 137    11670   9029   8523    365    128    105       C  
ATOM   1070  C   ILE A 137     136.534  80.692  67.215  1.00 75.21           C  
ANISOU 1070  C   ILE A 137    11347   8871   8360    213    183    194       C  
ATOM   1071  O   ILE A 137     136.369  79.967  66.223  1.00 63.51           O  
ANISOU 1071  O   ILE A 137     9835   7396   6902    178    216    269       O  
ATOM   1072  CB  ILE A 137     134.360  81.854  66.640  1.00 67.86           C  
ANISOU 1072  CB  ILE A 137    10489   7959   7335    507    113    100       C  
ATOM   1073  CG1 ILE A 137     133.644  83.205  66.637  1.00 67.21           C  
ANISOU 1073  CG1 ILE A 137    10551   7799   7188    705     41     10       C  
ATOM   1074  CG2 ILE A 137     133.476  80.806  67.290  1.00 65.43           C  
ANISOU 1074  CG2 ILE A 137     9975   7886   6998    517    159     82       C  
ATOM   1075  CD1 ILE A 137     132.289  83.171  65.972  1.00 72.16           C  
ANISOU 1075  CD1 ILE A 137    11117   8541   7760    893     -5    -33       C  
ATOM   1076  N   PRO A 138     137.433  80.387  68.151  1.00 94.31           N  
ANISOU 1076  N   PRO A 138    13716  11333  10784    142    183    177       N  
ATOM   1077  CA  PRO A 138     138.228  79.157  68.038  1.00 85.45           C  
ANISOU 1077  CA  PRO A 138    12509  10268   9690     45    224    255       C  
ATOM   1078  C   PRO A 138     137.344  77.919  68.065  1.00 84.73           C  
ANISOU 1078  C   PRO A 138    12341  10302   9551     70    286    320       C  
ATOM   1079  O   PRO A 138     136.355  77.853  68.799  1.00 76.52           O  
ANISOU 1079  O   PRO A 138    11268   9364   8443    143    306    283       O  
ATOM   1080  CB  PRO A 138     139.151  79.218  69.260  1.00 91.37           C  
ANISOU 1080  CB  PRO A 138    13229  11072  10416     36    179    188       C  
ATOM   1081  CG  PRO A 138     139.208  80.669  69.624  1.00 89.22           C  
ANISOU 1081  CG  PRO A 138    13043  10706  10152     55    120     74       C  
ATOM   1082  CD  PRO A 138     137.853  81.215  69.295  1.00 88.16           C  
ANISOU 1082  CD  PRO A 138    12975  10543   9977    166    129     73       C  
ATOM   1083  N   LEU A 139     137.713  76.930  67.255  1.00 83.07           N  
ANISOU 1083  N   LEU A 139    12108  10080   9376     -6    332    407       N  
ATOM   1084  CA  LEU A 139     136.919  75.725  67.068  1.00 76.68           C  
ANISOU 1084  CA  LEU A 139    11250   9350   8535    -23    405    462       C  
ATOM   1085  C   LEU A 139     137.641  74.502  67.620  1.00 76.68           C  
ANISOU 1085  C   LEU A 139    11257   9384   8495    -59    455    527       C  
ATOM   1086  O   LEU A 139     138.868  74.474  67.745  1.00 73.72           O  
ANISOU 1086  O   LEU A 139    10895   8980   8137    -64    417    537       O  
ATOM   1087  CB  LEU A 139     136.599  75.505  65.587  1.00 85.54           C  
ANISOU 1087  CB  LEU A 139    12378  10416   9708    -60    415    502       C  
ATOM   1088  CG  LEU A 139     135.911  76.654  64.851  1.00 84.03           C  
ANISOU 1088  CG  LEU A 139    12226  10175   9528     20    353    447       C  
ATOM   1089  CD1 LEU A 139     135.739  76.300  63.389  1.00 80.48           C  
ANISOU 1089  CD1 LEU A 139    11806   9672   9100      1    353    491       C  
ATOM   1090  CD2 LEU A 139     134.568  76.987  65.486  1.00 83.32           C  
ANISOU 1090  CD2 LEU A 139    12063  10209   9387    119    340    356       C  
ATOM   1091  N   GLN A 140     136.851  73.481  67.943  1.00 76.78           N  
ANISOU 1091  N   GLN A 140    11266   9460   8448    -79    547    560       N  
ATOM   1092  CA  GLN A 140     137.387  72.220  68.430  1.00 85.31           C  
ANISOU 1092  CA  GLN A 140    12415  10539   9459    -92    613    636       C  
ATOM   1093  C   GLN A 140     137.911  71.378  67.272  1.00 84.87           C  
ANISOU 1093  C   GLN A 140    12383  10409   9456   -154    635    709       C  
ATOM   1094  O   GLN A 140     137.446  71.488  66.133  1.00 78.78           O  
ANISOU 1094  O   GLN A 140    11572   9606   8754   -211    636    706       O  
ATOM   1095  CB  GLN A 140     136.314  71.438  69.191  1.00 90.33           C  
ANISOU 1095  CB  GLN A 140    13083  11234  10002   -121    744    644       C  
ATOM   1096  CG  GLN A 140     135.717  72.168  70.385  1.00 87.27           C  
ANISOU 1096  CG  GLN A 140    12680  10934   9543    -51    750    571       C  
ATOM   1097  CD  GLN A 140     136.585  72.084  71.623  1.00 83.92           C  
ANISOU 1097  CD  GLN A 140    12366  10518   9000     55    719    587       C  
ATOM   1098  OE1 GLN A 140     137.700  71.564  71.583  1.00 84.98           O  
ANISOU 1098  OE1 GLN A 140    12568  10607   9115     94    671    639       O  
ATOM   1099  NE2 GLN A 140     136.074  72.593  72.736  1.00 98.72           N  
ANISOU 1099  NE2 GLN A 140    14258  12465  10784    124    738    528       N  
ATOM   1100  N   GLY A 141     138.883  70.530  67.574  1.00 80.08           N  
ANISOU 1100  N   GLY A 141    11851   9779   8797   -117    645    768       N  
ATOM   1101  CA  GLY A 141     139.451  69.616  66.598  1.00 72.74           C  
ANISOU 1101  CA  GLY A 141    10963   8780   7895   -149    674    836       C  
ATOM   1102  C   GLY A 141     140.941  69.404  66.785  1.00 70.47           C  
ANISOU 1102  C   GLY A 141    10687   8498   7591    -55    611    847       C  
ATOM   1103  O   GLY A 141     141.670  70.281  67.252  1.00 65.13           O  
ANISOU 1103  O   GLY A 141     9933   7875   6938     -4    518    777       O  
ATOM   1104  N   ASP A 142     141.408  68.213  66.407  1.00 91.01           N  
ANISOU 1104  N   ASP A 142    13378  11050  10151    -27    658    918       N  
ATOM   1105  CA  ASP A 142     142.818  67.866  66.514  1.00 99.68           C  
ANISOU 1105  CA  ASP A 142    14471  12179  11224     96    595    914       C  
ATOM   1106  C   ASP A 142     143.582  68.035  65.207  1.00 97.81           C  
ANISOU 1106  C   ASP A 142    14140  11921  11102     48    585    905       C  
ATOM   1107  O   ASP A 142     144.806  68.203  65.243  1.00 99.42           O  
ANISOU 1107  O   ASP A 142    14251  12195  11331    123    523    852       O  
ATOM   1108  CB  ASP A 142     142.970  66.422  67.010  1.00110.80           C  
ANISOU 1108  CB  ASP A 142    16075  13540  12483    209    653    994       C  
ATOM   1109  CG  ASP A 142     142.355  66.213  68.382  1.00110.27           C  
ANISOU 1109  CG  ASP A 142    16143  13483  12270    270    688   1011       C  
ATOM   1110  OD1 ASP A 142     142.395  67.156  69.200  1.00103.06           O  
ANISOU 1110  OD1 ASP A 142    15145  12662  11351    310    608    938       O  
ATOM   1111  OD2 ASP A 142     141.828  65.110  68.641  1.00110.79           O  
ANISOU 1111  OD2 ASP A 142    16422  13453  12222    269    808   1094       O  
ATOM   1112  N   ASP A 143     142.899  67.998  64.065  1.00 93.32           N  
ANISOU 1112  N   ASP A 143    13589  11273  10597    -69    648    942       N  
ATOM   1113  CA  ASP A 143     143.507  68.271  62.771  1.00 94.67           C  
ANISOU 1113  CA  ASP A 143    13701  11411  10859   -119    657    939       C  
ATOM   1114  C   ASP A 143     142.615  69.225  61.987  1.00 85.36           C  
ANISOU 1114  C   ASP A 143    12502  10182   9749   -229    663    924       C  
ATOM   1115  O   ASP A 143     141.461  69.473  62.349  1.00 67.76           O  
ANISOU 1115  O   ASP A 143    10288   7957   7500   -257    659    912       O  
ATOM   1116  CB  ASP A 143     143.747  66.982  61.971  1.00 92.40           C  
ANISOU 1116  CB  ASP A 143    13515  11058  10533    -92    721   1008       C  
ATOM   1117  CG  ASP A 143     142.480  66.181  61.761  1.00 88.77           C  
ANISOU 1117  CG  ASP A 143    13184  10518  10026   -161    788   1057       C  
ATOM   1118  OD1 ASP A 143     141.885  65.735  62.763  1.00 94.98           O  
ANISOU 1118  OD1 ASP A 143    14046  11306  10734   -150    815   1071       O  
ATOM   1119  OD2 ASP A 143     142.076  66.005  60.594  1.00 92.28           O  
ANISOU 1119  OD2 ASP A 143    13656  10901  10505   -235    821   1070       O  
ATOM   1120  N   ASP A 144     143.167  69.761  60.894  1.00 91.78           N  
ANISOU 1120  N   ASP A 144    13290  10951  10631   -275    680    918       N  
ATOM   1121  CA  ASP A 144     142.456  70.760  60.102  1.00 82.22           C  
ANISOU 1121  CA  ASP A 144    12107   9675   9457   -336    677    907       C  
ATOM   1122  C   ASP A 144     141.159  70.226  59.508  1.00 75.20           C  
ANISOU 1122  C   ASP A 144    11287   8757   8528   -347    683    933       C  
ATOM   1123  O   ASP A 144     140.274  71.020  59.171  1.00 72.91           O  
ANISOU 1123  O   ASP A 144    11011   8451   8241   -349    647    902       O  
ATOM   1124  CB  ASP A 144     143.359  71.289  58.985  1.00 90.48           C  
ANISOU 1124  CB  ASP A 144    13166  10655  10556   -384    727    911       C  
ATOM   1125  CG  ASP A 144     144.472  72.180  59.505  1.00 89.73           C  
ANISOU 1125  CG  ASP A 144    12974  10592  10527   -425    728    839       C  
ATOM   1126  OD1 ASP A 144     144.233  72.925  60.478  1.00 91.94           O  
ANISOU 1126  OD1 ASP A 144    13216  10901  10816   -424    668    781       O  
ATOM   1127  OD2 ASP A 144     145.586  72.138  58.940  1.00 90.21           O  
ANISOU 1127  OD2 ASP A 144    12986  10656  10633   -465    795    825       O  
ATOM   1128  N   ASP A 145     141.021  68.906  59.374  1.00 87.02           N  
ANISOU 1128  N   ASP A 145    12830  10249   9983   -348    725    973       N  
ATOM   1129  CA  ASP A 145     139.793  68.346  58.818  1.00 85.45           C  
ANISOU 1129  CA  ASP A 145    12673  10037   9758   -391    734    964       C  
ATOM   1130  C   ASP A 145     138.675  68.304  59.853  1.00 83.83           C  
ANISOU 1130  C   ASP A 145    12419   9902   9530   -417    732    918       C  
ATOM   1131  O   ASP A 145     137.521  68.607  59.532  1.00 69.07           O  
ANISOU 1131  O   ASP A 145    10503   8074   7666   -444    705    855       O  
ATOM   1132  CB  ASP A 145     140.058  66.949  58.258  1.00 88.55           C  
ANISOU 1132  CB  ASP A 145    13158  10372  10114   -407    796   1009       C  
ATOM   1133  CG  ASP A 145     141.122  66.946  57.178  1.00 87.23           C  
ANISOU 1133  CG  ASP A 145    13033  10149   9960   -373    814   1046       C  
ATOM   1134  OD1 ASP A 145     141.119  67.867  56.332  1.00 89.44           O  
ANISOU 1134  OD1 ASP A 145    13313  10406  10265   -375    793   1034       O  
ATOM   1135  OD2 ASP A 145     141.965  66.027  57.183  1.00 87.13           O  
ANISOU 1135  OD2 ASP A 145    13070  10113   9922   -331    860   1085       O  
ATOM   1136  N   GLU A 146     138.993  67.924  61.095  1.00 99.63           N  
ANISOU 1136  N   GLU A 146    14429  11932  11494   -397    764    937       N  
ATOM   1137  CA  GLU A 146     137.983  67.927  62.150  1.00 94.34           C  
ANISOU 1137  CA  GLU A 146    13726  11329  10789   -425    792    897       C  
ATOM   1138  C   GLU A 146     137.530  69.341  62.486  1.00 79.66           C  
ANISOU 1138  C   GLU A 146    11767   9538   8962   -385    717    827       C  
ATOM   1139  O   GLU A 146     136.363  69.552  62.837  1.00 64.14           O  
ANISOU 1139  O   GLU A 146     9737   7647   6988   -410    728    761       O  
ATOM   1140  CB  GLU A 146     138.523  67.241  63.406  1.00118.98           C  
ANISOU 1140  CB  GLU A 146    16932  14447  13829   -379    844    944       C  
ATOM   1141  CG  GLU A 146     138.733  65.745  63.275  1.00129.63           C  
ANISOU 1141  CG  GLU A 146    18435  15706  15112   -402    938   1011       C  
ATOM   1142  CD  GLU A 146     139.265  65.128  64.554  1.00122.49           C  
ANISOU 1142  CD  GLU A 146    17664  14786  14090   -307    979   1064       C  
ATOM   1143  OE1 GLU A 146     139.250  65.816  65.597  1.00118.84           O  
ANISOU 1143  OE1 GLU A 146    17158  14400  13596   -248    943   1036       O  
ATOM   1144  OE2 GLU A 146     139.703  63.959  64.515  1.00121.03           O  
ANISOU 1144  OE2 GLU A 146    17652  14505  13828   -271   1042   1129       O  
ATOM   1145  N   ILE A 147     138.436  70.315  62.388  1.00 83.21           N  
ANISOU 1145  N   ILE A 147    12205   9963   9448   -329    651    828       N  
ATOM   1146  CA  ILE A 147     138.080  71.704  62.657  1.00 80.73           C  
ANISOU 1146  CA  ILE A 147    11845   9673   9156   -287    583    762       C  
ATOM   1147  C   ILE A 147     137.079  72.206  61.624  1.00 80.40           C  
ANISOU 1147  C   ILE A 147    11795   9624   9127   -274    546    721       C  
ATOM   1148  O   ILE A 147     136.070  72.834  61.968  1.00 75.40           O  
ANISOU 1148  O   ILE A 147    11110   9060   8480   -225    509    646       O  
ATOM   1149  CB  ILE A 147     139.347  72.578  62.690  1.00 81.92           C  
ANISOU 1149  CB  ILE A 147    12005   9771   9348   -270    544    760       C  
ATOM   1150  CG1 ILE A 147     140.292  72.103  63.797  1.00 72.76           C  
ANISOU 1150  CG1 ILE A 147    10822   8662   8160   -244    545    765       C  
ATOM   1151  CG2 ILE A 147     138.983  74.046  62.864  1.00 95.03           C  
ANISOU 1151  CG2 ILE A 147    13671  11410  11025   -234    485    692       C  
ATOM   1152  CD1 ILE A 147     141.678  72.707  63.717  1.00 77.11           C  
ANISOU 1152  CD1 ILE A 147    11335   9195   8769   -254    514    733       C  
ATOM   1153  N   LEU A 148     137.338  71.929  60.342  1.00 91.93           N  
ANISOU 1153  N   LEU A 148    13313  11014  10602   -291    548    758       N  
ATOM   1154  CA  LEU A 148     136.437  72.384  59.287  1.00 84.08           C  
ANISOU 1154  CA  LEU A 148    12338  10017   9593   -240    490    712       C  
ATOM   1155  C   LEU A 148     135.066  71.728  59.403  1.00 68.46           C  
ANISOU 1155  C   LEU A 148    10252   8164   7596   -261    486    630       C  
ATOM   1156  O   LEU A 148     134.039  72.380  59.182  1.00 69.86           O  
ANISOU 1156  O   LEU A 148    10372   8417   7755   -177    411    537       O  
ATOM   1157  CB  LEU A 148     137.049  72.102  57.915  1.00 95.13           C  
ANISOU 1157  CB  LEU A 148    13843  11316  10987   -249    503    770       C  
ATOM   1158  CG  LEU A 148     136.165  72.389  56.701  1.00102.37           C  
ANISOU 1158  CG  LEU A 148    14811  12228  11855   -169    430    724       C  
ATOM   1159  CD1 LEU A 148     135.716  73.841  56.694  1.00105.98           C  
ANISOU 1159  CD1 LEU A 148    15323  12663  12280    -40    350    678       C  
ATOM   1160  CD2 LEU A 148     136.899  72.047  55.413  1.00110.80           C  
ANISOU 1160  CD2 LEU A 148    16012  13188  12900   -177    463    793       C  
ATOM   1161  N   LYS A 149     135.028  70.439  59.750  1.00 76.64           N  
ANISOU 1161  N   LYS A 149    11263   9223   8632   -370    573    650       N  
ATOM   1162  CA  LYS A 149     133.750  69.755  59.909  1.00 80.19           C  
ANISOU 1162  CA  LYS A 149    11603   9787   9077   -446    608    554       C  
ATOM   1163  C   LYS A 149     132.955  70.281  61.097  1.00 82.95           C  
ANISOU 1163  C   LYS A 149    11837  10261   9420   -427    625    477       C  
ATOM   1164  O   LYS A 149     131.736  70.083  61.144  1.00 70.57           O  
ANISOU 1164  O   LYS A 149    10129   8827   7857   -469    641    356       O  
ATOM   1165  CB  LYS A 149     133.964  68.246  60.048  1.00 89.98           C  
ANISOU 1165  CB  LYS A 149    12903  10976  10309   -588    730    602       C  
ATOM   1166  CG  LYS A 149     134.513  67.588  58.793  1.00104.25           C  
ANISOU 1166  CG  LYS A 149    14813  12682  12116   -606    718    649       C  
ATOM   1167  CD  LYS A 149     133.859  66.240  58.525  1.00114.14           C  
ANISOU 1167  CD  LYS A 149    16075  13930  13364   -758    804    598       C  
ATOM   1168  CE  LYS A 149     134.295  65.192  59.531  1.00132.78           C  
ANISOU 1168  CE  LYS A 149    18552  16210  15690   -845    950    679       C  
ATOM   1169  NZ  LYS A 149     133.701  63.861  59.226  1.00144.70           N  
ANISOU 1169  NZ  LYS A 149    20122  17667  17190  -1018   1058    631       N  
ATOM   1170  N   ASN A 150     133.611  70.944  62.053  1.00 92.07           N  
ANISOU 1170  N   ASN A 150    13034  11387  10561   -366    623    526       N  
ATOM   1171  CA  ASN A 150     132.888  71.560  63.160  1.00 85.65           C  
ANISOU 1171  CA  ASN A 150    12130  10687   9727   -321    633    450       C  
ATOM   1172  C   ASN A 150     132.350  72.939  62.795  1.00 86.73           C  
ANISOU 1172  C   ASN A 150    12222  10867   9866   -167    508    364       C  
ATOM   1173  O   ASN A 150     131.296  73.338  63.303  1.00 96.10           O  
ANISOU 1173  O   ASN A 150    13284  12194  11036   -114    503    251       O  
ATOM   1174  CB  ASN A 150     133.786  71.654  64.396  1.00 95.34           C  
ANISOU 1174  CB  ASN A 150    13437  11870  10918   -305    673    521       C  
ATOM   1175  CG  ASN A 150     133.976  70.314  65.087  1.00 89.71           C  
ANISOU 1175  CG  ASN A 150    12788  11139  10157   -410    809    585       C  
ATOM   1176  OD1 ASN A 150     133.110  69.441  65.029  1.00 67.97           O  
ANISOU 1176  OD1 ASN A 150     9996   8431   7397   -525    913    548       O  
ATOM   1177  ND2 ASN A 150     135.115  70.148  65.750  1.00107.55           N  
ANISOU 1177  ND2 ASN A 150    15158  13331  12375   -367    810    668       N  
ATOM   1178  N   TYR A 151     133.048  73.678  61.926  1.00 79.39           N  
ANISOU 1178  N   TYR A 151    11407   9813   8943    -87    420    411       N  
ATOM   1179  CA  TYR A 151     132.543  74.977  61.487  1.00 77.98           C  
ANISOU 1179  CA  TYR A 151    11257   9633   8740     82    306    341       C  
ATOM   1180  C   TYR A 151     131.246  74.838  60.703  1.00 79.21           C  
ANISOU 1180  C   TYR A 151    11296   9926   8875    156    239    221       C  
ATOM   1181  O   TYR A 151     130.364  75.700  60.801  1.00 87.67           O  
ANISOU 1181  O   TYR A 151    12310  11092   9909    320    155    110       O  
ATOM   1182  CB  TYR A 151     133.594  75.697  60.638  1.00 77.00           C  
ANISOU 1182  CB  TYR A 151    11328   9315   8615    122    266    427       C  
ATOM   1183  CG  TYR A 151     133.068  76.918  59.913  1.00 81.56           C  
ANISOU 1183  CG  TYR A 151    12015   9840   9135    310    158    374       C  
ATOM   1184  CD1 TYR A 151     132.818  78.104  60.595  1.00 72.14           C  
ANISOU 1184  CD1 TYR A 151    10871   8628   7912    435    112    319       C  
ATOM   1185  CD2 TYR A 151     132.823  76.884  58.544  1.00 77.87           C  
ANISOU 1185  CD2 TYR A 151    11635   9330   8622    387     99    378       C  
ATOM   1186  CE1 TYR A 151     132.335  79.221  59.931  1.00 82.61           C  
ANISOU 1186  CE1 TYR A 151    12348   9879   9160    641     14    275       C  
ATOM   1187  CE2 TYR A 151     132.341  77.994  57.874  1.00 75.74           C  
ANISOU 1187  CE2 TYR A 151    11515   8997   8265    601     -5    336       C  
ATOM   1188  CZ  TYR A 151     132.099  79.158  58.570  1.00 86.92           C  
ANISOU 1188  CZ  TYR A 151    12996  10380   9649    732    -45    288       C  
ATOM   1189  OH  TYR A 151     131.619  80.260  57.898  1.00 85.59           O  
ANISOU 1189  OH  TYR A 151    13026  10123   9370    976   -148    250       O  
ATOM   1190  N   GLN A 152     131.111  73.763  59.925  1.00 83.48           N  
ANISOU 1190  N   GLN A 152    11796  10489   9433     52    264    223       N  
ATOM   1191  CA  GLN A 152     129.937  73.570  59.084  1.00 89.37           C  
ANISOU 1191  CA  GLN A 152    12414  11382  10161    114    180     81       C  
ATOM   1192  C   GLN A 152     128.701  73.160  59.875  1.00 85.85           C  
ANISOU 1192  C   GLN A 152    11710  11168   9739     52    232    -79       C  
ATOM   1193  O   GLN A 152     127.586  73.258  59.351  1.00 85.35           O  
ANISOU 1193  O   GLN A 152    11481  11285   9664    139    140   -250       O  
ATOM   1194  CB  GLN A 152     130.244  72.529  58.006  1.00 91.58           C  
ANISOU 1194  CB  GLN A 152    12746  11601  10451      5    194    120       C  
ATOM   1195  CG  GLN A 152     131.472  72.875  57.176  1.00 95.30           C  
ANISOU 1195  CG  GLN A 152    13460  11856  10894     54    174    270       C  
ATOM   1196  CD  GLN A 152     131.741  71.880  56.070  1.00 97.76           C  
ANISOU 1196  CD  GLN A 152    13832  12114  11198    -26    185    299       C  
ATOM   1197  OE1 GLN A 152     131.115  70.822  56.002  1.00 95.92           O  
ANISOU 1197  OE1 GLN A 152    13474  11981  10991   -149    217    217       O  
ATOM   1198  NE2 GLN A 152     132.677  72.216  55.191  1.00108.41           N  
ANISOU 1198  NE2 GLN A 152    15385  13296  12509     33    174    409       N  
ATOM   1199  N   VAL A 153     128.872  72.713  61.120  1.00 86.64           N  
ANISOU 1199  N   VAL A 153    11774  11281   9865    -89    379    -38       N  
ATOM   1200  CA  VAL A 153     127.725  72.408  61.969  1.00 90.21           C  
ANISOU 1200  CA  VAL A 153    11998  11945  10331   -162    470   -186       C  
ATOM   1201  C   VAL A 153     127.131  73.683  62.559  1.00 95.06           C  
ANISOU 1201  C   VAL A 153    12534  12677  10909     51    392   -283       C  
ATOM   1202  O   VAL A 153     125.921  73.752  62.809  1.00 90.18           O  
ANISOU 1202  O   VAL A 153    11678  12292  10296     81    400   -468       O  
ATOM   1203  CB  VAL A 153     128.134  71.423  63.079  1.00 91.26           C  
ANISOU 1203  CB  VAL A 153    12180  12023  10471   -377    677    -93       C  
ATOM   1204  CG1 VAL A 153     126.919  70.981  63.885  1.00 97.95           C  
ANISOU 1204  CG1 VAL A 153    12809  13078  11328   -500    823   -246       C  
ATOM   1205  CG2 VAL A 153     128.849  70.220  62.492  1.00 78.50           C  
ANISOU 1205  CG2 VAL A 153    10697  10256   8873   -544    744     17       C  
ATOM   1206  N   VAL A 154     127.952  74.710  62.773  1.00 99.86           N  
ANISOU 1206  N   VAL A 154    13332  13129  11480    197    321   -179       N  
ATOM   1207  CA  VAL A 154     127.526  75.918  63.473  1.00 90.09           C  
ANISOU 1207  CA  VAL A 154    12076  11957  10198    396    262   -257       C  
ATOM   1208  C   VAL A 154     127.306  77.106  62.547  1.00100.52           C  
ANISOU 1208  C   VAL A 154    13492  13236  11465    667     73   -307       C  
ATOM   1209  O   VAL A 154     126.695  78.097  62.980  1.00100.13           O  
ANISOU 1209  O   VAL A 154    13414  13267  11365    874      6   -410       O  
ATOM   1210  CB  VAL A 154     128.526  76.299  64.585  1.00 90.48           C  
ANISOU 1210  CB  VAL A 154    12286  11861  10229    367    326   -135       C  
ATOM   1211  CG1 VAL A 154     128.604  75.196  65.621  1.00 89.73           C  
ANISOU 1211  CG1 VAL A 154    12130  11820  10144    160    508    -96       C  
ATOM   1212  CG2 VAL A 154     129.900  76.566  63.995  1.00 83.83           C  
ANISOU 1212  CG2 VAL A 154    11682  10772   9400    352    275     20       C  
ATOM   1213  N   GLU A 155     127.772  77.046  61.298  1.00109.14           N  
ANISOU 1213  N   GLU A 155    14725  14195  12547    692     -8   -239       N  
ATOM   1214  CA  GLU A 155     127.664  78.198  60.405  1.00100.85           C  
ANISOU 1214  CA  GLU A 155    13850  13056  11412    964   -172   -260       C  
ATOM   1215  C   GLU A 155     126.236  78.706  60.223  1.00 89.56           C  
ANISOU 1215  C   GLU A 155    12242  11866   9920   1221   -304   -474       C  
ATOM   1216  O   GLU A 155     126.047  79.935  60.246  1.00 78.08           O  
ANISOU 1216  O   GLU A 155    10934  10353   8379   1490   -408   -507       O  
ATOM   1217  CB  GLU A 155     128.304  77.862  59.049  1.00106.49           C  
ANISOU 1217  CB  GLU A 155    14738  13614  12111    934   -212   -159       C  
ATOM   1218  CG  GLU A 155     128.471  79.053  58.110  1.00110.23           C  
ANISOU 1218  CG  GLU A 155    15499  13912  12471   1194   -340   -128       C  
ATOM   1219  CD  GLU A 155     127.405  79.109  57.030  1.00116.34           C  
ANISOU 1219  CD  GLU A 155    16219  14835  13151   1432   -509   -270       C  
ATOM   1220  OE1 GLU A 155     126.695  78.099  56.838  1.00115.25           O  
ANISOU 1220  OE1 GLU A 155    15808  14922  13059   1340   -521   -389       O  
ATOM   1221  OE2 GLU A 155     127.276  80.164  56.371  1.00118.00           O  
ANISOU 1221  OE2 GLU A 155    16672  14931  13230   1716   -632   -274       O  
ATOM   1222  N   PRO A 156     125.210  77.864  60.038  1.00 89.23           N  
ANISOU 1222  N   PRO A 156    11894  12096   9915   1166   -309   -639       N  
ATOM   1223  CA  PRO A 156     123.849  78.423  59.902  1.00 98.68           C  
ANISOU 1223  CA  PRO A 156    12878  13563  11051   1440   -450   -880       C  
ATOM   1224  C   PRO A 156     123.375  79.187  61.128  1.00 92.16           C  
ANISOU 1224  C   PRO A 156    11964  12843  10209   1561   -412   -962       C  
ATOM   1225  O   PRO A 156     122.865  80.307  60.993  1.00 93.35           O  
ANISOU 1225  O   PRO A 156    12180  13029  10259   1904   -561  -1057       O  
ATOM   1226  CB  PRO A 156     122.988  77.180  59.620  1.00106.31           C  
ANISOU 1226  CB  PRO A 156    13493  14805  12096   1252   -412  -1051       C  
ATOM   1227  CG  PRO A 156     123.823  76.011  60.032  1.00 89.13           C  
ANISOU 1227  CG  PRO A 156    11356  12491  10017    866   -203   -889       C  
ATOM   1228  CD  PRO A 156     125.227  76.418  59.751  1.00 73.12           C  
ANISOU 1228  CD  PRO A 156     9704  10120   7958    876   -208   -637       C  
ATOM   1229  N   GLU A 157     123.524  78.614  62.325  1.00108.09           N  
ANISOU 1229  N   GLU A 157    13862  14905  12303   1310   -215   -928       N  
ATOM   1230  CA  GLU A 157     123.134  79.334  63.536  1.00103.48           C  
ANISOU 1230  CA  GLU A 157    13219  14411  11688   1424   -166   -999       C  
ATOM   1231  C   GLU A 157     124.039  80.532  63.790  1.00 89.78           C  
ANISOU 1231  C   GLU A 157    11842  12388   9883   1587   -227   -858       C  
ATOM   1232  O   GLU A 157     123.582  81.554  64.317  1.00 88.52           O  
ANISOU 1232  O   GLU A 157    11709  12273   9651   1835   -287   -950       O  
ATOM   1233  CB  GLU A 157     123.151  78.392  64.739  1.00 96.87           C  
ANISOU 1233  CB  GLU A 157    12224  13661  10921   1117     74   -979       C  
ATOM   1234  CG  GLU A 157     121.956  77.455  64.813  1.00109.98           C  
ANISOU 1234  CG  GLU A 157    13496  15650  12642    970    176  -1184       C  
ATOM   1235  CD  GLU A 157     122.085  76.436  65.927  1.00118.29           C  
ANISOU 1235  CD  GLU A 157    14481  16722  13743    638    450  -1127       C  
ATOM   1236  OE1 GLU A 157     122.918  75.514  65.798  1.00119.40           O  
ANISOU 1236  OE1 GLU A 157    14769  16676  13921    391    545   -959       O  
ATOM   1237  OE2 GLU A 157     121.361  76.561  66.937  1.00123.95           O  
ANISOU 1237  OE2 GLU A 157    15021  17631  14443    641    577  -1248       O  
ATOM   1238  N   LEU A 158     125.316  80.426  63.422  1.00 83.71           N  
ANISOU 1238  N   LEU A 158    11345  11327   9136   1444   -206   -651       N  
ATOM   1239  CA  LEU A 158     126.234  81.548  63.581  1.00 82.83           C  
ANISOU 1239  CA  LEU A 158    11569  10931   8973   1548   -247   -535       C  
ATOM   1240  C   LEU A 158     125.900  82.674  62.609  1.00 96.89           C  
ANISOU 1240  C   LEU A 158    13558  12614  10643   1882   -425   -583       C  
ATOM   1241  O   LEU A 158     126.047  83.856  62.943  1.00 95.93           O  
ANISOU 1241  O   LEU A 158    13664  12340  10447   2070   -473   -584       O  
ATOM   1242  CB  LEU A 158     127.670  81.064  63.385  1.00 78.50           C  
ANISOU 1242  CB  LEU A 158    11205  10135   8487   1290   -164   -333       C  
ATOM   1243  CG  LEU A 158     128.820  81.872  63.980  1.00 95.72           C  
ANISOU 1243  CG  LEU A 158    13643  12062  10664   1249   -134   -227       C  
ATOM   1244  CD1 LEU A 158     128.642  82.026  65.480  1.00 99.20           C  
ANISOU 1244  CD1 LEU A 158    13986  12605  11101   1234    -67   -288       C  
ATOM   1245  CD2 LEU A 158     130.139  81.186  63.664  1.00 92.16           C  
ANISOU 1245  CD2 LEU A 158    13285  11445  10287    994    -54    -66       C  
ATOM   1246  N   GLN A 159     125.440  82.326  61.405  1.00107.04           N  
ANISOU 1246  N   GLN A 159    14799  13974  11899   1972   -526   -627       N  
ATOM   1247  CA  GLN A 159     125.068  83.321  60.405  1.00103.22           C  
ANISOU 1247  CA  GLN A 159    14544  13402  11273   2330   -706   -672       C  
ATOM   1248  C   GLN A 159     123.753  84.019  60.730  1.00103.67           C  
ANISOU 1248  C   GLN A 159    14443  13705  11240   2685   -834   -896       C  
ATOM   1249  O   GLN A 159     123.459  85.058  60.129  1.00105.54           O  
ANISOU 1249  O   GLN A 159    14931  13840  11329   3048   -988   -935       O  
ATOM   1250  CB  GLN A 159     124.984  82.658  59.026  1.00 97.71           C  
ANISOU 1250  CB  GLN A 159    13842  12729  10553   2332   -786   -663       C  
ATOM   1251  CG  GLN A 159     124.954  83.619  57.848  1.00 94.61           C  
ANISOU 1251  CG  GLN A 159    13811  12152   9987   2674   -949   -642       C  
ATOM   1252  CD  GLN A 159     126.234  84.417  57.712  1.00 89.29           C  
ANISOU 1252  CD  GLN A 159    13598  11053   9276   2611   -864   -427       C  
ATOM   1253  OE1 GLN A 159     127.271  83.888  57.308  1.00 76.21           O  
ANISOU 1253  OE1 GLN A 159    12054   9220   7685   2343   -751   -266       O  
ATOM   1254  NE2 GLN A 159     126.169  85.700  58.050  1.00 94.03           N  
ANISOU 1254  NE2 GLN A 159    14467  11488   9771   2853   -907   -440       N  
ATOM   1255  N   GLN A 160     122.964  83.487  61.663  1.00103.80           N  
ANISOU 1255  N   GLN A 160    14071  14037  11332   2603   -762  -1047       N  
ATOM   1256  CA  GLN A 160     121.675  84.071  62.008  1.00100.88           C  
ANISOU 1256  CA  GLN A 160    13487  13954  10887   2933   -866  -1289       C  
ATOM   1257  C   GLN A 160     121.756  85.103  63.124  1.00 97.39           C  
ANISOU 1257  C   GLN A 160    13192  13417  10393   3075   -829  -1292       C  
ATOM   1258  O   GLN A 160     120.753  85.771  63.398  1.00 95.19           O  
ANISOU 1258  O   GLN A 160    12795  13344  10030   3407   -926  -1488       O  
ATOM   1259  CB  GLN A 160     120.684  82.970  62.405  1.00 96.79           C  
ANISOU 1259  CB  GLN A 160    12446  13854  10475   2760   -783  -1485       C  
ATOM   1260  CG  GLN A 160     119.940  82.360  61.228  1.00112.76           C  
ANISOU 1260  CG  GLN A 160    14243  16106  12495   2831   -920  -1640       C  
ATOM   1261  CD  GLN A 160     119.044  83.366  60.524  1.00133.69           C  
ANISOU 1261  CD  GLN A 160    16922  18891  14984   3353  -1183  -1830       C  
ATOM   1262  OE1 GLN A 160     118.355  84.157  61.169  1.00137.78           O  
ANISOU 1262  OE1 GLN A 160    17355  19558  15436   3632  -1229  -1979       O  
ATOM   1263  NE2 GLN A 160     119.058  83.347  59.196  1.00137.39           N  
ANISOU 1263  NE2 GLN A 160    17532  19302  15368   3515  -1362  -1828       N  
ATOM   1264  N   VAL A 161     122.913  85.259  63.770  1.00102.51           N  
ANISOU 1264  N   VAL A 161    14087  13776  11085   2847   -702  -1101       N  
ATOM   1265  CA  VAL A 161     123.011  86.236  64.848  1.00110.77           C  
ANISOU 1265  CA  VAL A 161    15284  14727  12078   2971   -674  -1120       C  
ATOM   1266  C   VAL A 161     123.060  87.646  64.269  1.00101.05           C  
ANISOU 1266  C   VAL A 161    14464  13237  10692   3343   -831  -1117       C  
ATOM   1267  O   VAL A 161     123.379  87.863  63.093  1.00 91.22           O  
ANISOU 1267  O   VAL A 161    13474  11799   9388   3433   -923  -1033       O  
ATOM   1268  CB  VAL A 161     124.231  85.960  65.743  1.00116.94           C  
ANISOU 1268  CB  VAL A 161    16184  15302  12946   2621   -509   -949       C  
ATOM   1269  CG1 VAL A 161     124.281  84.492  66.148  1.00113.70           C  
ANISOU 1269  CG1 VAL A 161    15453  15088  12659   2268   -352   -920       C  
ATOM   1270  CG2 VAL A 161     125.510  86.375  65.044  1.00119.81           C  
ANISOU 1270  CG2 VAL A 161    16942  15271  13308   2522   -525   -759       C  
ATOM   1271  N   ASN A 162     122.728  88.620  65.120  1.00109.80           N  
ANISOU 1271  N   ASN A 162    15670  14329  11719   3572   -851  -1209       N  
ATOM   1272  CA  ASN A 162     122.699  90.034  64.741  1.00107.36           C  
ANISOU 1272  CA  ASN A 162    15793  13754  11244   3952   -985  -1222       C  
ATOM   1273  C   ASN A 162     121.767  90.267  63.553  1.00108.80           C  
ANISOU 1273  C   ASN A 162    15982  14063  11295   4353  -1184  -1335       C  
ATOM   1274  O   ASN A 162     122.082  91.019  62.628  1.00 98.40           O  
ANISOU 1274  O   ASN A 162    15099  12443   9846   4562  -1283  -1252       O  
ATOM   1275  CB  ASN A 162     124.108  90.556  64.448  1.00 97.91           C  
ANISOU 1275  CB  ASN A 162    15075  12074  10051   3755   -924  -1006       C  
ATOM   1276  CG  ASN A 162     124.187  92.071  64.467  1.00102.49           C  
ANISOU 1276  CG  ASN A 162    16143  12329  10471   4068   -996  -1020       C  
ATOM   1277  OD1 ASN A 162     123.419  92.737  65.162  1.00 96.56           O  
ANISOU 1277  OD1 ASN A 162    15368  11689   9630   4364  -1055  -1174       O  
ATOM   1278  ND2 ASN A 162     125.119  92.623  63.699  1.00106.97           N  
ANISOU 1278  ND2 ASN A 162    17171  12479  10994   3999   -975   -863       N  
ATOM   1279  N   GLY A 163     120.607  89.613  63.579  1.00114.77           N  
ANISOU 1279  N   GLY A 163    16257  15274  12077   4460  -1238  -1539       N  
ATOM   1280  CA  GLY A 163     119.653  89.731  62.489  1.00107.15           C  
ANISOU 1280  CA  GLY A 163    15218  14504  10990   4851  -1453  -1693       C  
ATOM   1281  C   GLY A 163     120.179  89.238  61.161  1.00106.82           C  
ANISOU 1281  C   GLY A 163    15340  14306  10942   4745  -1507  -1555       C  
ATOM   1282  O   GLY A 163     119.744  89.720  60.110  1.00100.16           O  
ANISOU 1282  O   GLY A 163    14689  13438   9930   5131  -1706  -1611       O  
ATOM   1283  N   GLY A 164     121.108  88.282  61.180  1.00110.87           N  
ANISOU 1283  N   GLY A 164    15796  14713  11617   4255  -1340  -1378       N  
ATOM   1284  CA  GLY A 164     121.749  87.806  59.976  1.00100.30           C  
ANISOU 1284  CA  GLY A 164    14639  13195  10276   4122  -1361  -1229       C  
ATOM   1285  C   GLY A 164     122.918  88.639  59.502  1.00 93.59           C  
ANISOU 1285  C   GLY A 164    14382  11837   9342   4111  -1322   -998       C  
ATOM   1286  O   GLY A 164     123.660  88.188  58.619  1.00 96.21           O  
ANISOU 1286  O   GLY A 164    14874  11990   9691   3923  -1282   -844       O  
ATOM   1287  N   ASP A 165     123.117  89.833  60.062  1.00 99.42           N  
ANISOU 1287  N   ASP A 165    15454  12331   9989   4287  -1314   -978       N  
ATOM   1288  CA  ASP A 165     124.175  90.744  59.623  1.00110.22           C  
ANISOU 1288  CA  ASP A 165    17416  13194  11270   4270  -1257   -785       C  
ATOM   1289  C   ASP A 165     125.462  90.395  60.365  1.00103.60           C  
ANISOU 1289  C   ASP A 165    16582  12166  10616   3760  -1037   -627       C  
ATOM   1290  O   ASP A 165     125.843  91.023  61.356  1.00 98.64           O  
ANISOU 1290  O   ASP A 165    16067  11396  10015   3688   -960   -627       O  
ATOM   1291  CB  ASP A 165     123.759  92.193  59.852  1.00126.24           C  
ANISOU 1291  CB  ASP A 165    19830  15031  13105   4699  -1352   -856       C  
ATOM   1292  CG  ASP A 165     124.643  93.185  59.112  1.00132.12           C  
ANISOU 1292  CG  ASP A 165    21251  15238  13709   4748  -1304   -679       C  
ATOM   1293  OD1 ASP A 165     125.870  92.963  59.032  1.00130.94           O  
ANISOU 1293  OD1 ASP A 165    21253  14824  13675   4327  -1124   -501       O  
ATOM   1294  OD2 ASP A 165     124.105  94.193  58.609  1.00138.33           O  
ANISOU 1294  OD2 ASP A 165    22430  15868  14262   5216  -1439   -726       O  
ATOM   1295  N   ILE A 166     126.146  89.370  59.861  1.00102.86           N  
ANISOU 1295  N   ILE A 166    16362  12078  10641   3421   -946   -507       N  
ATOM   1296  CA  ILE A 166     127.434  88.957  60.404  1.00 99.21           C  
ANISOU 1296  CA  ILE A 166    15898  11454  10344   2964   -756   -363       C  
ATOM   1297  C   ILE A 166     128.265  88.336  59.288  1.00 95.20           C  
ANISOU 1297  C   ILE A 166    15503  10799   9868   2749   -690   -207       C  
ATOM   1298  O   ILE A 166     127.834  87.380  58.633  1.00106.02           O  
ANISOU 1298  O   ILE A 166    16637  12388  11257   2744   -742   -228       O  
ATOM   1299  CB  ILE A 166     127.261  87.986  61.588  1.00 96.86           C  
ANISOU 1299  CB  ILE A 166    15123  11473  10205   2725   -684   -430       C  
ATOM   1300  CG1 ILE A 166     128.596  87.329  61.942  1.00 98.39           C  
ANISOU 1300  CG1 ILE A 166    15290  11541  10553   2286   -519   -284       C  
ATOM   1301  CG2 ILE A 166     126.190  86.942  61.288  1.00101.19           C  
ANISOU 1301  CG2 ILE A 166    15255  12415  10779   2787   -755   -547       C  
ATOM   1302  CD1 ILE A 166     128.504  86.326  63.072  1.00 86.30           C  
ANISOU 1302  CD1 ILE A 166    13362  10282   9146   2065   -438   -326       C  
ATOM   1303  N   ARG A 167     129.455  88.883  59.058  1.00 93.38           N  
ANISOU 1303  N   ARG A 167    15633  10202   9646   2564   -565    -66       N  
ATOM   1304  CA  ARG A 167     130.332  88.443  57.979  1.00 89.71           C  
ANISOU 1304  CA  ARG A 167    15325   9564   9197   2369   -473     84       C  
ATOM   1305  C   ARG A 167     131.327  87.430  58.528  1.00 90.72           C  
ANISOU 1305  C   ARG A 167    15170   9769   9532   1935   -328    152       C  
ATOM   1306  O   ARG A 167     132.127  87.756  59.413  1.00 78.39           O  
ANISOU 1306  O   ARG A 167    13629   8094   8062   1723   -227    165       O  
ATOM   1307  CB  ARG A 167     131.063  89.633  57.359  1.00 91.01           C  
ANISOU 1307  CB  ARG A 167    16054   9281   9245   2403   -389    187       C  
ATOM   1308  CG  ARG A 167     130.153  90.787  56.970  1.00105.51           C  
ANISOU 1308  CG  ARG A 167    18257  10983  10849   2867   -527    124       C  
ATOM   1309  CD  ARG A 167     129.253  90.420  55.804  1.00133.75           C  
ANISOU 1309  CD  ARG A 167    21838  14713  14269   3195   -690     98       C  
ATOM   1310  NE  ARG A 167     130.025  90.138  54.597  1.00155.61           N  
ANISOU 1310  NE  ARG A 167    24860  17271  16992   3059   -589    254       N  
ATOM   1311  CZ  ARG A 167     130.451  91.068  53.749  1.00161.40           C  
ANISOU 1311  CZ  ARG A 167    26175  17606  17546   3176   -517    365       C  
ATOM   1312  NH1 ARG A 167     130.182  92.348  53.975  1.00157.15           N  
ANISOU 1312  NH1 ARG A 167    26043  16813  16853   3436   -544    338       N  
ATOM   1313  NH2 ARG A 167     131.149  90.720  52.677  1.00162.62           N  
ANISOU 1313  NH2 ARG A 167    26529  17598  17660   3034   -402    504       N  
ATOM   1314  N   LEU A 168     131.282  86.209  58.003  1.00 95.06           N  
ANISOU 1314  N   LEU A 168    15468  10509  10140   1823   -327    183       N  
ATOM   1315  CA  LEU A 168     132.152  85.129  58.451  1.00 94.91           C  
ANISOU 1315  CA  LEU A 168    15191  10578  10293   1464   -206    245       C  
ATOM   1316  C   LEU A 168     133.360  85.037  57.527  1.00 96.12           C  
ANISOU 1316  C   LEU A 168    15565  10491  10465   1266    -78    387       C  
ATOM   1317  O   LEU A 168     133.207  84.857  56.314  1.00106.82           O  
ANISOU 1317  O   LEU A 168    17064  11794  11730   1366   -103    438       O  
ATOM   1318  CB  LEU A 168     131.395  83.801  58.486  1.00 90.93           C  
ANISOU 1318  CB  LEU A 168    14299  10409   9843   1440   -258    186       C  
ATOM   1319  CG  LEU A 168     130.264  83.719  59.513  1.00 88.00           C  
ANISOU 1319  CG  LEU A 168    13643  10313   9479   1564   -332     35       C  
ATOM   1320  CD1 LEU A 168     129.556  82.376  59.442  1.00 84.42           C  
ANISOU 1320  CD1 LEU A 168    12830  10161   9084   1487   -345    -30       C  
ATOM   1321  CD2 LEU A 168     130.799  83.971  60.914  1.00 84.05           C  
ANISOU 1321  CD2 LEU A 168    13088   9790   9057   1415   -248     31       C  
ATOM   1322  N   ALA A 169     134.556  85.161  58.103  1.00 78.63           N  
ANISOU 1322  N   ALA A 169    13367   8146   8362    992     57    435       N  
ATOM   1323  CA  ALA A 169     135.804  85.069  57.359  1.00 78.22           C  
ANISOU 1323  CA  ALA A 169    13471   7896   8353    766    209    545       C  
ATOM   1324  C   ALA A 169     136.797  84.249  58.173  1.00 82.12           C  
ANISOU 1324  C   ALA A 169    13678   8508   9017    469    297    550       C  
ATOM   1325  O   ALA A 169     136.498  83.800  59.284  1.00 72.79           O  
ANISOU 1325  O   ALA A 169    12231   7529   7896    453    241    483       O  
ATOM   1326  CB  ALA A 169     136.358  86.460  57.033  1.00 77.19           C  
ANISOU 1326  CB  ALA A 169    13767   7410   8151    760    302    574       C  
ATOM   1327  N   GLY A 170     137.988  84.051  57.615  1.00101.75           N  
ANISOU 1327  N   GLY A 170    16225  10872  11564    250    439    623       N  
ATOM   1328  CA  GLY A 170     139.012  83.273  58.282  1.00 95.21           C  
ANISOU 1328  CA  GLY A 170    15132  10163  10881      6    509    616       C  
ATOM   1329  C   GLY A 170     139.390  82.007  57.540  1.00 86.33           C  
ANISOU 1329  C   GLY A 170    13870   9144   9789    -72    557    692       C  
ATOM   1330  O   GLY A 170     139.101  81.856  56.349  1.00 85.99           O  
ANISOU 1330  O   GLY A 170    13979   9033   9662     13    569    759       O  
ATOM   1331  N   LEU A 171     140.036  81.081  58.250  1.00 96.25           N  
ANISOU 1331  N   LEU A 171    14856  10564  11149   -209    576    677       N  
ATOM   1332  CA  LEU A 171     140.534  79.865  57.614  1.00 92.08           C  
ANISOU 1332  CA  LEU A 171    14214  10121  10652   -283    631    743       C  
ATOM   1333  C   LEU A 171     139.397  78.938  57.198  1.00 90.54           C  
ANISOU 1333  C   LEU A 171    13954  10056  10390   -139    540    768       C  
ATOM   1334  O   LEU A 171     139.444  78.339  56.118  1.00 92.53           O  
ANISOU 1334  O   LEU A 171    14264  10288  10607   -131    572    828       O  
ATOM   1335  CB  LEU A 171     141.491  79.133  58.556  1.00 89.41           C  
ANISOU 1335  CB  LEU A 171    13629   9923  10418   -419    656    710       C  
ATOM   1336  CG  LEU A 171     142.989  79.441  58.486  1.00101.77           C  
ANISOU 1336  CG  LEU A 171    15170  11423  12074   -611    778    682       C  
ATOM   1337  CD1 LEU A 171     143.265  80.931  58.555  1.00111.15           C  
ANISOU 1337  CD1 LEU A 171    16541  12418  13274   -692    834    625       C  
ATOM   1338  CD2 LEU A 171     143.722  78.715  59.603  1.00108.49           C  
ANISOU 1338  CD2 LEU A 171    15758  12463  12999   -665    742    618       C  
ATOM   1339  N   ASN A 172     138.371  78.805  58.037  1.00 81.30           N  
ANISOU 1339  N   ASN A 172    12660   9027   9203    -37    436    706       N  
ATOM   1340  CA  ASN A 172     137.331  77.804  57.817  1.00 72.46           C  
ANISOU 1340  CA  ASN A 172    11418   8066   8048     43    369    694       C  
ATOM   1341  C   ASN A 172     136.180  78.291  56.938  1.00 74.02           C  
ANISOU 1341  C   ASN A 172    11734   8249   8141    236    274    660       C  
ATOM   1342  O   ASN A 172     135.657  77.499  56.143  1.00 75.59           O  
ANISOU 1342  O   ASN A 172    11895   8522   8305    274    239    659       O  
ATOM   1343  CB  ASN A 172     136.795  77.302  59.158  1.00 73.12           C  
ANISOU 1343  CB  ASN A 172    11292   8327   8163     33    337    634       C  
ATOM   1344  CG  ASN A 172     137.825  76.505  59.927  1.00 72.68           C  
ANISOU 1344  CG  ASN A 172    11125   8315   8174   -108    407    669       C  
ATOM   1345  OD1 ASN A 172     137.974  75.302  59.720  1.00 69.47           O  
ANISOU 1345  OD1 ASN A 172    10650   7968   7779   -165    445    711       O  
ATOM   1346  ND2 ASN A 172     138.552  77.174  60.815  1.00 97.15           N  
ANISOU 1346  ND2 ASN A 172    14222  11383  11309   -149    416    640       N  
ATOM   1347  N   PRO A 173     135.729  79.549  57.047  1.00 92.65           N  
ANISOU 1347  N   PRO A 173    14242  10522  10438    380    217    616       N  
ATOM   1348  CA  PRO A 173     134.742  80.030  56.063  1.00 88.87           C  
ANISOU 1348  CA  PRO A 173    13916  10022   9831    614    111    583       C  
ATOM   1349  C   PRO A 173     135.224  79.920  54.626  1.00 84.19           C  
ANISOU 1349  C   PRO A 173    13542   9280   9167    621    155    671       C  
ATOM   1350  O   PRO A 173     134.425  79.614  53.732  1.00 77.52           O  
ANISOU 1350  O   PRO A 173    12725   8504   8227    780     57    639       O  
ATOM   1351  CB  PRO A 173     134.515  81.487  56.486  1.00 86.46           C  
ANISOU 1351  CB  PRO A 173    13802   9584   9463    759     73    543       C  
ATOM   1352  CG  PRO A 173     134.745  81.473  57.948  1.00 85.60           C  
ANISOU 1352  CG  PRO A 173    13504   9564   9456    638    103    497       C  
ATOM   1353  CD  PRO A 173     135.875  80.501  58.166  1.00 87.84           C  
ANISOU 1353  CD  PRO A 173    13652   9869   9854    380    216    568       C  
ATOM   1354  N   LEU A 174     136.517  80.152  54.381  1.00 92.48           N  
ANISOU 1354  N   LEU A 174    14739  10142  10257    452    304    766       N  
ATOM   1355  CA  LEU A 174     137.069  80.014  53.037  1.00 89.59           C  
ANISOU 1355  CA  LEU A 174    14588   9633   9821    439    385    856       C  
ATOM   1356  C   LEU A 174     137.213  78.550  52.641  1.00 88.66           C  
ANISOU 1356  C   LEU A 174    14277   9662   9748    348    397    876       C  
ATOM   1357  O   LEU A 174     136.841  78.161  51.528  1.00 90.29           O  
ANISOU 1357  O   LEU A 174    14586   9866   9854    453    355    891       O  
ATOM   1358  CB  LEU A 174     138.422  80.723  52.949  1.00 88.77           C  
ANISOU 1358  CB  LEU A 174    14670   9300   9759    255    573    929       C  
ATOM   1359  CG  LEU A 174     138.431  82.242  53.120  1.00100.81           C  
ANISOU 1359  CG  LEU A 174    16484  10598  11221    313    603    920       C  
ATOM   1360  CD1 LEU A 174     139.857  82.755  53.216  1.00108.32           C  
ANISOU 1360  CD1 LEU A 174    17531  11364  12263     44    815    955       C  
ATOM   1361  CD2 LEU A 174     137.699  82.917  51.971  1.00102.09           C  
ANISOU 1361  CD2 LEU A 174    17015  10600  11174    577    547    956       C  
ATOM   1362  N   ALA A 175     137.758  77.726  53.541  1.00 82.78           N  
ANISOU 1362  N   ALA A 175    13279   9036   9139    169    450    872       N  
ATOM   1363  CA  ALA A 175     137.948  76.311  53.239  1.00 72.41           C  
ANISOU 1363  CA  ALA A 175    11818   7833   7862     86    473    893       C  
ATOM   1364  C   ALA A 175     136.622  75.628  52.933  1.00 79.73           C  
ANISOU 1364  C   ALA A 175    12649   8913   8733    205    338    816       C  
ATOM   1365  O   ALA A 175     136.552  74.752  52.063  1.00 78.92           O  
ANISOU 1365  O   ALA A 175    12558   8835   8594    202    335    826       O  
ATOM   1366  CB  ALA A 175     138.653  75.615  54.403  1.00 75.48           C  
ANISOU 1366  CB  ALA A 175    11985   8316   8376    -74    534    893       C  
ATOM   1367  N   SER A 176     135.560  76.011  53.645  1.00 81.71           N  
ANISOU 1367  N   SER A 176    12789   9281   8978    303    230    720       N  
ATOM   1368  CA  SER A 176     134.235  75.486  53.334  1.00 74.48           C  
ANISOU 1368  CA  SER A 176    11746   8538   8014    411    101    606       C  
ATOM   1369  C   SER A 176     133.788  75.928  51.948  1.00 75.70           C  
ANISOU 1369  C   SER A 176    12108   8631   8022    613      3    589       C  
ATOM   1370  O   SER A 176     133.171  75.153  51.207  1.00 72.85           O  
ANISOU 1370  O   SER A 176    11686   8377   7618    654    -75    520       O  
ATOM   1371  CB  SER A 176     133.231  75.940  54.394  1.00 66.24           C  
ANISOU 1371  CB  SER A 176    10531   7645   6991    487     23    491       C  
ATOM   1372  OG  SER A 176     131.935  75.437  54.124  1.00 67.67           O  
ANISOU 1372  OG  SER A 176    10540   8030   7142    572    -91    346       O  
ATOM   1373  N   GLU A 177     134.097  77.173  51.579  1.00 83.55           N  
ANISOU 1373  N   GLU A 177    13376   9443   8927    745      8    646       N  
ATOM   1374  CA  GLU A 177     133.699  77.680  50.272  1.00 81.96           C  
ANISOU 1374  CA  GLU A 177    13441   9153   8545    978    -83    644       C  
ATOM   1375  C   GLU A 177     134.574  77.106  49.163  1.00 85.01           C  
ANISOU 1375  C   GLU A 177    13999   9413   8888    894     23    751       C  
ATOM   1376  O   GLU A 177     134.100  76.915  48.037  1.00 69.24           O  
ANISOU 1376  O   GLU A 177    12133   7426   6748   1059    -72    721       O  
ATOM   1377  CB  GLU A 177     133.755  79.210  50.271  1.00 69.65           C  
ANISOU 1377  CB  GLU A 177    12183   7399   6884   1149    -86    681       C  
ATOM   1378  CG  GLU A 177     132.981  79.871  49.142  1.00 72.02           C  
ANISOU 1378  CG  GLU A 177    12767   7641   6957   1487   -232    645       C  
ATOM   1379  CD  GLU A 177     131.488  79.949  49.414  1.00 77.16           C  
ANISOU 1379  CD  GLU A 177    13212   8547   7557   1741   -465    457       C  
ATOM   1380  OE1 GLU A 177     131.041  79.445  50.468  1.00 72.10           O  
ANISOU 1380  OE1 GLU A 177    12205   8124   7065   1620   -484    359       O  
ATOM   1381  OE2 GLU A 177     130.762  80.520  48.572  1.00 79.39           O  
ANISOU 1381  OE2 GLU A 177    13703   8820   7640   2073   -624    398       O  
ATOM   1382  N   LEU A 178     135.846  76.826  49.460  1.00 85.00           N  
ANISOU 1382  N   LEU A 178    13992   9308   8997    657    211    859       N  
ATOM   1383  CA  LEU A 178     136.735  76.249  48.454  1.00 83.55           C  
ANISOU 1383  CA  LEU A 178    13947   9022   8778    574    333    952       C  
ATOM   1384  C   LEU A 178     136.379  74.793  48.179  1.00 87.31           C  
ANISOU 1384  C   LEU A 178    14225   9665   9283    526    275    896       C  
ATOM   1385  O   LEU A 178     136.144  74.407  47.028  1.00 82.55           O  
ANISOU 1385  O   LEU A 178    13756   9050   8558    628    227    887       O  
ATOM   1386  CB  LEU A 178     138.191  76.378  48.904  1.00 73.56           C  
ANISOU 1386  CB  LEU A 178    12683   7637   7630    345    546   1049       C  
ATOM   1387  CG  LEU A 178     138.789  77.787  48.932  1.00 83.81           C  
ANISOU 1387  CG  LEU A 178    14232   8715   8896    331    659   1107       C  
ATOM   1388  CD1 LEU A 178     140.148  77.770  49.609  1.00 80.12           C  
ANISOU 1388  CD1 LEU A 178    13645   8210   8587     72    844   1143       C  
ATOM   1389  CD2 LEU A 178     138.902  78.364  47.529  1.00 81.11           C  
ANISOU 1389  CD2 LEU A 178    14286   8168   8364    458    723   1183       C  
ATOM   1390  N   THR A 179     136.329  73.968  49.228  1.00 87.96           N  
ANISOU 1390  N   THR A 179    14018   9890   9513    371    284    853       N  
ATOM   1391  CA  THR A 179     135.928  72.576  49.058  1.00 82.22           C  
ANISOU 1391  CA  THR A 179    13131   9294   8815    302    246    791       C  
ATOM   1392  C   THR A 179     134.475  72.445  48.621  1.00 82.72           C  
ANISOU 1392  C   THR A 179    13122   9509   8799    450     56    637       C  
ATOM   1393  O   THR A 179     134.096  71.403  48.076  1.00 89.58           O  
ANISOU 1393  O   THR A 179    13928  10456   9653    414     12    566       O  
ATOM   1394  CB  THR A 179     136.148  71.795  50.356  1.00 74.39           C  
ANISOU 1394  CB  THR A 179    11898   8393   7972    118    313    785       C  
ATOM   1395  OG1 THR A 179     135.375  72.385  51.408  1.00 75.22           O  
ANISOU 1395  OG1 THR A 179    11859   8600   8121    147    245    710       O  
ATOM   1396  CG2 THR A 179     137.619  71.805  50.745  1.00 64.38           C  
ANISOU 1396  CG2 THR A 179    10667   7017   6777     -3    474    904       C  
ATOM   1397  N   GLY A 180     133.656  73.473  48.852  1.00 84.13           N  
ANISOU 1397  N   GLY A 180    13303   9739   8925    621    -64    565       N  
ATOM   1398  CA  GLY A 180     132.279  73.444  48.394  1.00 87.21           C  
ANISOU 1398  CA  GLY A 180    13599  10306   9230    800   -264    388       C  
ATOM   1399  C   GLY A 180     132.129  73.592  46.896  1.00 84.16           C  
ANISOU 1399  C   GLY A 180    13460   9860   8656   1008   -366    376       C  
ATOM   1400  O   GLY A 180     131.074  73.247  46.353  1.00 74.95           O  
ANISOU 1400  O   GLY A 180    12190   8869   7418   1137   -545    204       O  
ATOM   1401  N   THR A 181     133.157  74.106  46.216  1.00 84.44           N  
ANISOU 1401  N   THR A 181    13821   9658   8602   1043   -252    542       N  
ATOM   1402  CA  THR A 181     133.122  74.174  44.761  1.00 85.89           C  
ANISOU 1402  CA  THR A 181    14290   9761   8583   1236   -318    552       C  
ATOM   1403  C   THR A 181     133.081  72.790  44.131  1.00 83.13           C  
ANISOU 1403  C   THR A 181    13839   9502   8245   1133   -336    489       C  
ATOM   1404  O   THR A 181     132.649  72.655  42.982  1.00 76.03           O  
ANISOU 1404  O   THR A 181    13092   8623   7174   1318   -464    421       O  
ATOM   1405  CB  THR A 181     134.334  74.948  44.234  1.00 84.30           C  
ANISOU 1405  CB  THR A 181    14462   9273   8296   1238   -129    751       C  
ATOM   1406  OG1 THR A 181     135.540  74.274  44.617  1.00 69.56           O  
ANISOU 1406  OG1 THR A 181    12509   7337   6584    951     89    862       O  
ATOM   1407  CG2 THR A 181     134.347  76.364  44.793  1.00 81.52           C  
ANISOU 1407  CG2 THR A 181    14260   8794   7918   1336   -108    801       C  
ATOM   1408  N   ILE A 182     133.522  71.763  44.862  1.00 91.79           N  
ANISOU 1408  N   ILE A 182    14711  10643   9524    857   -215    505       N  
ATOM   1409  CA  ILE A 182     133.463  70.393  44.358  1.00 92.47           C  
ANISOU 1409  CA  ILE A 182    14717  10792   9627    742   -221    437       C  
ATOM   1410  C   ILE A 182     132.021  70.000  44.061  1.00 93.39           C  
ANISOU 1410  C   ILE A 182    14650  11134   9701    836   -448    197       C  
ATOM   1411  O   ILE A 182     131.694  69.561  42.952  1.00 97.02           O  
ANISOU 1411  O   ILE A 182    15207  11624  10031    941   -559    107       O  
ATOM   1412  CB  ILE A 182     134.114  69.427  45.365  1.00 90.21           C  
ANISOU 1412  CB  ILE A 182    14245  10499   9531    457    -54    495       C  
ATOM   1413  CG1 ILE A 182     135.566  69.831  45.629  1.00 95.12           C  
ANISOU 1413  CG1 ILE A 182    15007  10941  10195    383    149    694       C  
ATOM   1414  CG2 ILE A 182     134.024  67.995  44.874  1.00 94.68           C  
ANISOU 1414  CG2 ILE A 182    14769  11099  10106    340    -51    421       C  
ATOM   1415  CD1 ILE A 182     136.372  70.108  44.375  1.00 90.30           C  
ANISOU 1415  CD1 ILE A 182    14700  10168   9441    483    225    799       C  
ATOM   1416  N   GLY A 183     131.139  70.152  45.050  1.00 89.10           N  
ANISOU 1416  N   GLY A 183    13824  10768   9264    796   -517     71       N  
ATOM   1417  CA  GLY A 183     129.739  69.826  44.842  1.00 86.20           C  
ANISOU 1417  CA  GLY A 183    13221  10655   8875    866   -723   -194       C  
ATOM   1418  C   GLY A 183     129.070  70.706  43.805  1.00 97.62           C  
ANISOU 1418  C   GLY A 183    14821  12162  10106   1234   -954   -294       C  
ATOM   1419  O   GLY A 183     128.183  70.250  43.078  1.00102.15           O  
ANISOU 1419  O   GLY A 183    15291  12916  10603   1330  -1143   -512       O  
ATOM   1420  N   GLU A 184     129.478  71.975  43.723  1.00107.62           N  
ANISOU 1420  N   GLU A 184    16353  13277  11262   1451   -944   -149       N  
ATOM   1421  CA  GLU A 184     128.970  72.843  42.666  1.00109.05           C  
ANISOU 1421  CA  GLU A 184    16783  13459  11192   1841  -1147   -207       C  
ATOM   1422  C   GLU A 184     129.375  72.331  41.291  1.00104.97           C  
ANISOU 1422  C   GLU A 184    16539  12840  10507   1918  -1169   -174       C  
ATOM   1423  O   GLU A 184     128.622  72.484  40.323  1.00107.79           O  
ANISOU 1423  O   GLU A 184    16988  13305  10662   2211  -1401   -326       O  
ATOM   1424  CB  GLU A 184     129.475  74.274  42.860  1.00111.65           C  
ANISOU 1424  CB  GLU A 184    17422  13572  11428   2022  -1079    -27       C  
ATOM   1425  CG  GLU A 184     128.955  74.974  44.102  1.00109.79           C  
ANISOU 1425  CG  GLU A 184    16970  13439  11306   2033  -1100    -82       C  
ATOM   1426  CD  GLU A 184     129.420  76.414  44.187  1.00115.96           C  
ANISOU 1426  CD  GLU A 184    18108  13978  11972   2225  -1043     79       C  
ATOM   1427  OE1 GLU A 184     130.113  76.871  43.253  1.00117.59           O  
ANISOU 1427  OE1 GLU A 184    18737  13936  12006   2340   -975    231       O  
ATOM   1428  OE2 GLU A 184     129.093  77.090  45.185  1.00122.50           O  
ANISOU 1428  OE2 GLU A 184    18816  14852  12876   2253  -1050     49       O  
ATOM   1429  N   ASP A 185     130.557  71.721  41.188  1.00 97.28           N  
ANISOU 1429  N   ASP A 185    15692  11670   9600   1680   -938     10       N  
ATOM   1430  CA  ASP A 185     131.032  71.213  39.908  1.00100.16           C  
ANISOU 1430  CA  ASP A 185    16327  11925   9803   1743   -927     52       C  
ATOM   1431  C   ASP A 185     130.397  69.877  39.550  1.00111.75           C  
ANISOU 1431  C   ASP A 185    17562  13583  11314   1630  -1047   -162       C  
ATOM   1432  O   ASP A 185     130.175  69.599  38.366  1.00111.76           O  
ANISOU 1432  O   ASP A 185    17738  13600  11124   1804  -1179   -246       O  
ATOM   1433  CB  ASP A 185     132.554  71.082  39.933  1.00 96.86           C  
ANISOU 1433  CB  ASP A 185    16114  11247   9440   1544   -625    310       C  
ATOM   1434  CG  ASP A 185     133.252  72.415  40.113  1.00 97.25           C  
ANISOU 1434  CG  ASP A 185    16434  11084   9432   1630   -486    505       C  
ATOM   1435  OD1 ASP A 185     132.577  73.462  40.009  1.00 88.76           O  
ANISOU 1435  OD1 ASP A 185    15485  10017   8221   1895   -630    463       O  
ATOM   1436  OD2 ASP A 185     134.474  72.415  40.370  1.00 99.20           O  
ANISOU 1436  OD2 ASP A 185    16766  11158   9769   1432   -231    685       O  
ATOM   1437  N   GLN A 186     130.104  69.040  40.548  1.00118.37           N  
ANISOU 1437  N   GLN A 186    18036  14553  12388   1337   -995   -256       N  
ATOM   1438  CA  GLN A 186     129.468  67.756  40.274  1.00122.66           C  
ANISOU 1438  CA  GLN A 186    18365  15254  12985   1183  -1084   -476       C  
ATOM   1439  C   GLN A 186     128.027  67.945  39.815  1.00123.75           C  
ANISOU 1439  C   GLN A 186    18317  15677  13026   1398  -1392   -785       C  
ATOM   1440  O   GLN A 186     127.608  67.370  38.804  1.00123.66           O  
ANISOU 1440  O   GLN A 186    18343  15751  12893   1481  -1551   -957       O  
ATOM   1441  CB  GLN A 186     129.526  66.866  41.516  1.00125.53           C  
ANISOU 1441  CB  GLN A 186    18435  15653  13609    809   -916   -485       C  
ATOM   1442  CG  GLN A 186     130.933  66.469  41.936  1.00129.54           C  
ANISOU 1442  CG  GLN A 186    19098  15916  14205    614   -641   -222       C  
ATOM   1443  CD  GLN A 186     131.573  65.478  40.982  1.00132.13           C  
ANISOU 1443  CD  GLN A 186    19627  16116  14460    562   -580   -189       C  
ATOM   1444  OE1 GLN A 186     130.889  64.835  40.185  1.00130.25           O  
ANISOU 1444  OE1 GLN A 186    19367  15976  14145    588   -728   -386       O  
ATOM   1445  NE2 GLN A 186     132.892  65.350  41.061  1.00136.40           N  
ANISOU 1445  NE2 GLN A 186    20353  16452  15022    492   -364     40       N  
ATOM   1446  N   LYS A 187     127.254  68.750  40.550  1.00125.77           N  
ANISOU 1446  N   LYS A 187    18359  16100  13327   1504  -1490   -878       N  
ATOM   1447  CA  LYS A 187     125.866  68.995  40.170  1.00122.93           C  
ANISOU 1447  CA  LYS A 187    17778  16054  12877   1742  -1797  -1200       C  
ATOM   1448  C   LYS A 187     125.773  69.661  38.804  1.00113.21           C  
ANISOU 1448  C   LYS A 187    16895  14789  11331   2179  -2015  -1216       C  
ATOM   1449  O   LYS A 187     124.814  69.425  38.062  1.00113.49           O  
ANISOU 1449  O   LYS A 187    16806  15066  11248   2364  -2288  -1505       O  
ATOM   1450  CB  LYS A 187     125.176  69.850  41.236  1.00124.81           C  
ANISOU 1450  CB  LYS A 187    17759  16457  13206   1816  -1838  -1269       C  
ATOM   1451  CG  LYS A 187     123.689  69.558  41.428  1.00132.64           C  
ANISOU 1451  CG  LYS A 187    18282  17853  14261   1832  -2055  -1661       C  
ATOM   1452  CD  LYS A 187     122.823  70.259  40.392  1.00147.94           C  
ANISOU 1452  CD  LYS A 187    20275  19990  15943   2314  -2407  -1879       C  
ATOM   1453  CE  LYS A 187     122.913  71.773  40.521  1.00153.96           C  
ANISOU 1453  CE  LYS A 187    21296  20657  16547   2711  -2470  -1729       C  
ATOM   1454  NZ  LYS A 187     122.063  72.470  39.512  1.00153.21           N  
ANISOU 1454  NZ  LYS A 187    21302  20745  16166   3238  -2827  -1938       N  
ATOM   1455  N   ARG A 188     126.761  70.488  38.453  1.00115.12           N  
ANISOU 1455  N   ARG A 188    17582  14733  11425   2344  -1893   -921       N  
ATOM   1456  CA  ARG A 188     126.767  71.114  37.135  1.00116.71           C  
ANISOU 1456  CA  ARG A 188    18197  14850  11295   2757  -2057   -901       C  
ATOM   1457  C   ARG A 188     127.021  70.092  36.033  1.00109.80           C  
ANISOU 1457  C   ARG A 188    17457  13945  10317   2710  -2086   -956       C  
ATOM   1458  O   ARG A 188     126.502  70.239  34.921  1.00 96.72           O  
ANISOU 1458  O   ARG A 188    15978  12374   8396   3049  -2333  -1101       O  
ATOM   1459  CB  ARG A 188     127.812  72.230  37.093  1.00120.13           C  
ANISOU 1459  CB  ARG A 188    19091  14941  11610   2882  -1859   -565       C  
ATOM   1460  CG  ARG A 188     127.867  72.998  35.781  1.00122.44           C  
ANISOU 1460  CG  ARG A 188    19896  15095  11531   3319  -1983   -506       C  
ATOM   1461  CD  ARG A 188     128.586  74.334  35.934  1.00131.26           C  
ANISOU 1461  CD  ARG A 188    21432  15902  12537   3461  -1807   -228       C  
ATOM   1462  NE  ARG A 188     129.910  74.195  36.536  1.00134.87           N  
ANISOU 1462  NE  ARG A 188    21941  16108  13194   3074  -1436     38       N  
ATOM   1463  CZ  ARG A 188     130.217  74.593  37.766  1.00128.58           C  
ANISOU 1463  CZ  ARG A 188    20965  15266  12623   2859  -1280    130       C  
ATOM   1464  NH1 ARG A 188     129.297  75.164  38.531  1.00130.48           N  
ANISOU 1464  NH1 ARG A 188    20978  15680  12917   2987  -1444     -8       N  
ATOM   1465  NH2 ARG A 188     131.447  74.425  38.231  1.00122.96           N  
ANISOU 1465  NH2 ARG A 188    20293  14352  12074   2532   -968    343       N  
ATOM   1466  N   ALA A 189     127.802  69.049  36.322  1.00113.61           N  
ANISOU 1466  N   ALA A 189    17871  14309  10985   2320  -1849   -854       N  
ATOM   1467  CA  ALA A 189     128.023  67.995  35.339  1.00103.48           C  
ANISOU 1467  CA  ALA A 189    16703  12997   9617   2258  -1870   -924       C  
ATOM   1468  C   ALA A 189     126.842  67.036  35.254  1.00109.17           C  
ANISOU 1468  C   ALA A 189    17033  14030  10416   2157  -2099  -1303       C  
ATOM   1469  O   ALA A 189     126.626  66.420  34.205  1.00105.82           O  
ANISOU 1469  O   ALA A 189    16711  13656   9840   2247  -2247  -1459       O  
ATOM   1470  CB  ALA A 189     129.302  67.226  35.670  1.00 90.28           C  
ANISOU 1470  CB  ALA A 189    15119  11081   8102   1911  -1536   -687       C  
ATOM   1471  N   GLU A 190     126.070  66.898  36.334  1.00120.33           N  
ANISOU 1471  N   GLU A 190    18002  15658  12061   1960  -2122  -1468       N  
ATOM   1472  CA  GLU A 190     124.929  65.990  36.339  1.00120.35           C  
ANISOU 1472  CA  GLU A 190    17595  15967  12167   1803  -2300  -1852       C  
ATOM   1473  C   GLU A 190     123.700  66.578  35.660  1.00124.26           C  
ANISOU 1473  C   GLU A 190    17961  16781  12471   2196  -2686  -2174       C  
ATOM   1474  O   GLU A 190     122.768  65.830  35.345  1.00131.38           O  
ANISOU 1474  O   GLU A 190    18556  17956  13408   2114  -2878  -2537       O  
ATOM   1475  CB  GLU A 190     124.573  65.594  37.775  1.00115.89           C  
ANISOU 1475  CB  GLU A 190    16607  15509  11917   1420  -2139  -1912       C  
ATOM   1476  CG  GLU A 190     125.673  64.849  38.511  1.00117.90           C  
ANISOU 1476  CG  GLU A 190    16954  15485  12358   1035  -1787  -1645       C  
ATOM   1477  CD  GLU A 190     125.300  64.528  39.946  1.00121.36           C  
ANISOU 1477  CD  GLU A 190    17028  16016  13066    697  -1627  -1692       C  
ATOM   1478  OE1 GLU A 190     124.103  64.635  40.286  1.00125.91           O  
ANISOU 1478  OE1 GLU A 190    17231  16897  13710    689  -1775  -1982       O  
ATOM   1479  OE2 GLU A 190     126.203  64.174  40.733  1.00119.06           O  
ANISOU 1479  OE2 GLU A 190    16824  15505  12908    453  -1352  -1448       O  
ATOM   1480  N   VAL A 191     123.668  67.889  35.434  1.00121.06           N  
ANISOU 1480  N   VAL A 191    17785  16351  11861   2624  -2805  -2066       N  
ATOM   1481  CA  VAL A 191     122.520  68.537  34.808  1.00125.16           C  
ANISOU 1481  CA  VAL A 191    18215  17174  12165   3075  -3191  -2364       C  
ATOM   1482  C   VAL A 191     122.864  69.215  33.492  1.00125.42           C  
ANISOU 1482  C   VAL A 191    18795  17050  11808   3559  -3346  -2250       C  
ATOM   1483  O   VAL A 191     121.943  69.558  32.735  1.00126.12           O  
ANISOU 1483  O   VAL A 191    18864  17391  11665   3973  -3705  -2525       O  
ATOM   1484  CB  VAL A 191     121.853  69.553  35.760  1.00121.34           C  
ANISOU 1484  CB  VAL A 191    17486  16865  11753   3233  -3256  -2417       C  
ATOM   1485  CG1 VAL A 191     121.573  68.916  37.113  1.00118.87           C  
ANISOU 1485  CG1 VAL A 191    16673  16682  11809   2748  -3061  -2500       C  
ATOM   1486  CG2 VAL A 191     122.720  70.793  35.908  1.00113.67           C  
ANISOU 1486  CG2 VAL A 191    16980  15564  10646   3469  -3109  -2033       C  
ATOM   1487  N   ALA A 192     124.142  69.424  33.187  1.00121.90           N  
ANISOU 1487  N   ALA A 192    18837  16209  11269   3535  -3086  -1870       N  
ATOM   1488  CA  ALA A 192     124.541  70.087  31.954  1.00119.21           C  
ANISOU 1488  CA  ALA A 192    19071  15679  10544   3971  -3174  -1730       C  
ATOM   1489  C   ALA A 192     125.508  69.281  31.102  1.00120.35           C  
ANISOU 1489  C   ALA A 192    19540  15584  10602   3825  -3004  -1580       C  
ATOM   1490  O   ALA A 192     125.491  69.427  29.879  1.00121.94           O  
ANISOU 1490  O   ALA A 192    20115  15744  10470   4174  -3164  -1610       O  
ATOM   1491  CB  ALA A 192     125.173  71.454  32.260  1.00115.05           C  
ANISOU 1491  CB  ALA A 192    18933  14871   9909   4176  -3009  -1398       C  
ATOM   1492  N   ALA A 193     126.344  68.436  31.705  1.00119.46           N  
ANISOU 1492  N   ALA A 193    19313  15316  10761   3349  -2690  -1424       N  
ATOM   1493  CA  ALA A 193     127.320  67.668  30.941  1.00110.25           C  
ANISOU 1493  CA  ALA A 193    18450  13921   9517   3221  -2510  -1278       C  
ATOM   1494  C   ALA A 193     126.779  66.306  30.520  1.00113.18           C  
ANISOU 1494  C   ALA A 193    18572  14482   9950   3040  -2659  -1586       C  
ATOM   1495  O   ALA A 193     126.843  65.950  29.340  1.00118.01           O  
ANISOU 1495  O   ALA A 193    19458  15066  10314   3228  -2777  -1659       O  
ATOM   1496  CB  ALA A 193     128.610  67.500  31.749  1.00112.95           C  
ANISOU 1496  CB  ALA A 193    18843  13985  10089   2852  -2093   -944       C  
ATOM   1497  N   ILE A 194     126.239  65.537  31.462  1.00131.63           N  
ANISOU 1497  N   ILE A 194    20415  16998  12601   2671  -2646  -1775       N  
ATOM   1498  CA  ILE A 194     125.738  64.197  31.160  1.00134.83           C  
ANISOU 1498  CA  ILE A 194    20583  17551  13094   2428  -2747  -2076       C  
ATOM   1499  C   ILE A 194     124.503  64.222  30.257  1.00138.98           C  
ANISOU 1499  C   ILE A 194    20987  18404  13414   2738  -3174  -2483       C  
ATOM   1500  O   ILE A 194     124.224  63.201  29.611  1.00144.17           O  
ANISOU 1500  O   ILE A 194    21591  19141  14046   2625  -3286  -2726       O  
ATOM   1501  CB  ILE A 194     125.475  63.391  32.448  1.00128.14           C  
ANISOU 1501  CB  ILE A 194    19276  16784  12629   1931  -2584  -2166       C  
ATOM   1502  CG1 ILE A 194     124.360  64.004  33.297  1.00136.29           C  
ANISOU 1502  CG1 ILE A 194    19873  18120  13790   1961  -2738  -2372       C  
ATOM   1503  CG2 ILE A 194     126.752  63.265  33.268  1.00115.21           C  
ANISOU 1503  CG2 ILE A 194    17782  14829  11163   1660  -2189  -1782       C  
ATOM   1504  CD1 ILE A 194     123.022  63.304  33.157  1.00146.80           C  
ANISOU 1504  CD1 ILE A 194    20761  19821  15196   1854  -2999  -2857       C  
ATOM   1505  N   PRO A 195     123.717  65.328  30.154  1.00135.30           N  
ANISOU 1505  N   PRO A 195    20475  18145  12787   3148  -3440  -2596       N  
ATOM   1506  CA  PRO A 195     122.723  65.373  29.071  1.00134.03           C  
ANISOU 1506  CA  PRO A 195    20297  18272  12354   3535  -3866  -2964       C  
ATOM   1507  C   PRO A 195     123.351  65.705  27.726  1.00131.65           C  
ANISOU 1507  C   PRO A 195    20614  17757  11650   3938  -3927  -2799       C  
ATOM   1508  O   PRO A 195     122.900  65.211  26.687  1.00134.83           O  
ANISOU 1508  O   PRO A 195    21082  18304  11844   4121  -4193  -3067       O  
ATOM   1509  CB  PRO A 195     121.750  66.469  29.525  1.00135.96           C  
ANISOU 1509  CB  PRO A 195    20298  18796  12564   3858  -4105  -3116       C  
ATOM   1510  CG  PRO A 195     122.559  67.342  30.382  1.00135.12           C  
ANISOU 1510  CG  PRO A 195    20382  18412  12547   3816  -3802  -2703       C  
ATOM   1511  CD  PRO A 195     123.474  66.419  31.120  1.00129.02           C  
ANISOU 1511  CD  PRO A 195    19535  17404  12084   3248  -3409  -2491       C  
ATOM   1512  N   LEU A 196     124.392  66.541  27.732  1.00131.57           N  
ANISOU 1512  N   LEU A 196    21067  17403  11522   4069  -3670  -2369       N  
ATOM   1513  CA  LEU A 196     125.067  66.884  26.483  1.00123.91           C  
ANISOU 1513  CA  LEU A 196    20723  16195  10162   4424  -3662  -2180       C  
ATOM   1514  C   LEU A 196     125.787  65.678  25.894  1.00129.58           C  
ANISOU 1514  C   LEU A 196    21583  16757  10893   4159  -3502  -2150       C  
ATOM   1515  O   LEU A 196     125.713  65.438  24.683  1.00130.71           O  
ANISOU 1515  O   LEU A 196    22030  16910  10725   4434  -3680  -2263       O  
ATOM   1516  CB  LEU A 196     126.046  68.036  26.706  1.00118.04           C  
ANISOU 1516  CB  LEU A 196    20419  15107   9326   4550  -3370  -1736       C  
ATOM   1517  CG  LEU A 196     125.485  69.459  26.642  1.00127.65           C  
ANISOU 1517  CG  LEU A 196    21832  16368  10299   5044  -3567  -1718       C  
ATOM   1518  CD1 LEU A 196     126.577  70.475  26.938  1.00135.73           C  
ANISOU 1518  CD1 LEU A 196    23293  17000  11278   5052  -3208  -1272       C  
ATOM   1519  CD2 LEU A 196     124.856  69.731  25.285  1.00123.28           C  
ANISOU 1519  CD2 LEU A 196    21618  15933   9289   5610  -3938  -1914       C  
ATOM   1520  N   VAL A 197     126.485  64.903  26.728  1.00128.56           N  
ANISOU 1520  N   VAL A 197    21260  16485  11103   3652  -3174  -2006       N  
ATOM   1521  CA  VAL A 197     127.144  63.696  26.240  1.00127.72           C  
ANISOU 1521  CA  VAL A 197    21273  16233  11022   3404  -3022  -1995       C  
ATOM   1522  C   VAL A 197     126.151  62.615  25.848  1.00137.21           C  
ANISOU 1522  C   VAL A 197    22168  17709  12257   3300  -3315  -2444       C  
ATOM   1523  O   VAL A 197     126.543  61.625  25.221  1.00145.57           O  
ANISOU 1523  O   VAL A 197    23378  18664  13268   3173  -3260  -2495       O  
ATOM   1524  CB  VAL A 197     128.132  63.132  27.283  1.00110.67           C  
ANISOU 1524  CB  VAL A 197    18990  13854   9204   2923  -2611  -1737       C  
ATOM   1525  CG1 VAL A 197     129.084  64.221  27.759  1.00100.36           C  
ANISOU 1525  CG1 VAL A 197    17924  12311   7899   2987  -2329  -1335       C  
ATOM   1526  CG2 VAL A 197     127.386  62.507  28.447  1.00117.14           C  
ANISOU 1526  CG2 VAL A 197    19243  14875  10390   2536  -2638  -1955       C  
ATOM   1527  N   ALA A 198     124.874  62.778  26.201  1.00135.11           N  
ANISOU 1527  N   ALA A 198    21465  17795  12074   3346  -3618  -2790       N  
ATOM   1528  CA  ALA A 198     123.854  61.835  25.760  1.00123.66           C  
ANISOU 1528  CA  ALA A 198    19702  16641  10643   3258  -3920  -3269       C  
ATOM   1529  C   ALA A 198     123.463  62.081  24.308  1.00130.83           C  
ANISOU 1529  C   ALA A 198    20924  17665  11119   3768  -4278  -3464       C  
ATOM   1530  O   ALA A 198     123.250  61.127  23.551  1.00133.30           O  
ANISOU 1530  O   ALA A 198    21250  18043  11354   3703  -4420  -3727       O  
ATOM   1531  CB  ALA A 198     122.627  61.920  26.667  1.00121.70           C  
ANISOU 1531  CB  ALA A 198    18832  16762  10646   3109  -4099  -3599       C  
ATOM   1532  N   VAL A 199     123.364  63.349  23.900  1.00135.82           N  
ANISOU 1532  N   VAL A 199    21842  18311  11450   4290  -4429  -3344       N  
ATOM   1533  CA  VAL A 199     123.038  63.651  22.510  1.00145.83           C  
ANISOU 1533  CA  VAL A 199    23485  19666  12259   4833  -4766  -3499       C  
ATOM   1534  C   VAL A 199     124.263  63.564  21.609  1.00139.39           C  
ANISOU 1534  C   VAL A 199    23323  18463  11174   4947  -4522  -3157       C  
ATOM   1535  O   VAL A 199     124.117  63.398  20.392  1.00133.53           O  
ANISOU 1535  O   VAL A 199    22902  17759  10073   5286  -4753  -3306       O  
ATOM   1536  CB  VAL A 199     122.379  65.035  22.381  1.00153.05           C  
ANISOU 1536  CB  VAL A 199    24496  20743  12912   5400  -5043  -3526       C  
ATOM   1537  CG1 VAL A 199     121.208  65.158  23.346  1.00152.20           C  
ANISOU 1537  CG1 VAL A 199    23712  21032  13086   5286  -5251  -3857       C  
ATOM   1538  CG2 VAL A 199     123.391  66.145  22.615  1.00155.92           C  
ANISOU 1538  CG2 VAL A 199    25348  20726  13169   5550  -4715  -3003       C  
ATOM   1539  N   VAL A 200     125.469  63.674  22.170  1.00143.61           N  
ANISOU 1539  N   VAL A 200    24055  18643  11866   4681  -4063  -2719       N  
ATOM   1540  CA  VAL A 200     126.673  63.439  21.381  1.00137.25           C  
ANISOU 1540  CA  VAL A 200    23796  17495  10857   4714  -3787  -2423       C  
ATOM   1541  C   VAL A 200     126.827  61.952  21.087  1.00132.77           C  
ANISOU 1541  C   VAL A 200    23112  16925  10410   4381  -3754  -2611       C  
ATOM   1542  O   VAL A 200     127.229  61.560  19.985  1.00136.34           O  
ANISOU 1542  O   VAL A 200    23964  17264  10574   4559  -3769  -2611       O  
ATOM   1543  CB  VAL A 200     127.907  64.008  22.108  1.00132.36           C  
ANISOU 1543  CB  VAL A 200    23365  16538  10389   4519  -3312  -1938       C  
ATOM   1544  CG1 VAL A 200     129.182  63.655  21.356  1.00131.84           C  
ANISOU 1544  CG1 VAL A 200    23788  16150  10156   4498  -2993  -1663       C  
ATOM   1545  CG2 VAL A 200     127.783  65.514  22.266  1.00128.78           C  
ANISOU 1545  CG2 VAL A 200    23120  16041   9769   4873  -3341  -1754       C  
ATOM   1546  N   LEU A 201     126.498  61.101  22.062  1.00126.95           N  
ANISOU 1546  N   LEU A 201    21855  16299  10084   3897  -3700  -2777       N  
ATOM   1547  CA  LEU A 201     126.589  59.659  21.858  1.00116.80           C  
ANISOU 1547  CA  LEU A 201    20468  14985   8925   3555  -3661  -2971       C  
ATOM   1548  C   LEU A 201     125.583  59.180  20.821  1.00132.19           C  
ANISOU 1548  C   LEU A 201    22379  17204  10643   3772  -4098  -3437       C  
ATOM   1549  O   LEU A 201     125.870  58.253  20.054  1.00131.92           O  
ANISOU 1549  O   LEU A 201    22551  17076  10496   3716  -4099  -3541       O  
ATOM   1550  CB  LEU A 201     126.374  58.927  23.182  1.00117.35           C  
ANISOU 1550  CB  LEU A 201    20020  15100   9466   2999  -3501  -3049       C  
ATOM   1551  CG  LEU A 201     127.609  58.712  24.054  1.00111.75           C  
ANISOU 1551  CG  LEU A 201    19390  14069   9000   2670  -3030  -2641       C  
ATOM   1552  CD1 LEU A 201     127.207  58.277  25.452  1.00107.10           C  
ANISOU 1552  CD1 LEU A 201    18297  13563   8832   2211  -2920  -2720       C  
ATOM   1553  CD2 LEU A 201     128.523  57.681  23.411  1.00113.88           C  
ANISOU 1553  CD2 LEU A 201    19986  14088   9194   2558  -2836  -2557       C  
ATOM   1554  N   PHE A 202     124.399  59.792  20.781  1.00140.64           N  
ANISOU 1554  N   PHE A 202    23178  18624  11635   4034  -4485  -3741       N  
ATOM   1555  CA  PHE A 202     123.386  59.337  19.840  1.00140.02           C  
ANISOU 1555  CA  PHE A 202    23000  18853  11350   4241  -4935  -4236       C  
ATOM   1556  C   PHE A 202     123.695  59.750  18.408  1.00144.32           C  
ANISOU 1556  C   PHE A 202    24154  19310  11370   4803  -5101  -4173       C  
ATOM   1557  O   PHE A 202     123.237  59.084  17.474  1.00156.84           O  
ANISOU 1557  O   PHE A 202    25792  21042  12760   4921  -5388  -4522       O  
ATOM   1558  CB  PHE A 202     122.007  59.858  20.240  1.00144.25           C  
ANISOU 1558  CB  PHE A 202    23017  19833  11959   4376  -5314  -4618       C  
ATOM   1559  CG  PHE A 202     120.883  59.143  19.559  1.00155.95           C  
ANISOU 1559  CG  PHE A 202    24201  21689  13364   4417  -5753  -5214       C  
ATOM   1560  CD1 PHE A 202     120.420  57.937  20.054  1.00165.78           C  
ANISOU 1560  CD1 PHE A 202    24971  23052  14965   3847  -5720  -5546       C  
ATOM   1561  CD2 PHE A 202     120.306  59.659  18.412  1.00167.72           C  
ANISOU 1561  CD2 PHE A 202    25874  23382  14470   4994  -6149  -5412       C  
ATOM   1562  CE1 PHE A 202     119.395  57.265  19.425  1.00175.65           C  
ANISOU 1562  CE1 PHE A 202    25930  24649  16160   3843  -6114  -6125       C  
ATOM   1563  CE2 PHE A 202     119.279  58.989  17.779  1.00178.27           C  
ANISOU 1563  CE2 PHE A 202    26837  25037  15862   4970  -6464  -5893       C  
ATOM   1564  CZ  PHE A 202     118.826  57.789  18.288  1.00179.89           C  
ANISOU 1564  CZ  PHE A 202    26584  25399  16367   4401  -6485  -6294       C  
ATOM   1565  N   PHE A 203     124.459  60.822  18.210  1.00138.58           N  
ANISOU 1565  N   PHE A 203    23908  18341  10405   5139  -4917  -3745       N  
ATOM   1566  CA  PHE A 203     124.788  61.256  16.858  1.00157.66           C  
ANISOU 1566  CA  PHE A 203    26918  20627  12360   5649  -4995  -3626       C  
ATOM   1567  C   PHE A 203     125.971  60.502  16.266  1.00157.73           C  
ANISOU 1567  C   PHE A 203    27375  20302  12253   5508  -4679  -3404       C  
ATOM   1568  O   PHE A 203     126.405  60.837  15.158  1.00157.72           O  
ANISOU 1568  O   PHE A 203    27811  20119  11996   5843  -4606  -3208       O  
ATOM   1569  CB  PHE A 203     125.064  62.763  16.831  1.00169.48           C  
ANISOU 1569  CB  PHE A 203    28728  21963  13704   6042  -4875  -3248       C  
ATOM   1570  CG  PHE A 203     123.820  63.612  16.886  1.00193.32           C  
ANISOU 1570  CG  PHE A 203    31432  25292  16729   6388  -5240  -3476       C  
ATOM   1571  CD1 PHE A 203     122.631  63.102  17.387  1.00202.36           C  
ANISOU 1571  CD1 PHE A 203    31933  26861  18092   6226  -5580  -3954       C  
ATOM   1572  CD2 PHE A 203     123.837  64.915  16.422  1.00203.28           C  
ANISOU 1572  CD2 PHE A 203    33042  26409  17787   6874  -5223  -3229       C  
ATOM   1573  CE1 PHE A 203     121.490  63.880  17.435  1.00206.41           C  
ANISOU 1573  CE1 PHE A 203    32129  27679  18619   6561  -5899  -4174       C  
ATOM   1574  CE2 PHE A 203     122.697  65.698  16.465  1.00208.29           C  
ANISOU 1574  CE2 PHE A 203    33409  27314  18418   7231  -5552  -3446       C  
ATOM   1575  CZ  PHE A 203     121.522  65.178  16.973  1.00208.61           C  
ANISOU 1575  CZ  PHE A 203    32779  27808  18676   7086  -5895  -3918       C  
ATOM   1576  N   VAL A 204     126.500  59.502  16.968  1.00154.99           N  
ANISOU 1576  N   VAL A 204    26805  19829  12257   4966  -4397  -3361       N  
ATOM   1577  CA  VAL A 204     127.525  58.631  16.411  1.00146.96           C  
ANISOU 1577  CA  VAL A 204    26135  18531  11171   4820  -4120  -3209       C  
ATOM   1578  C   VAL A 204     127.019  57.211  16.185  1.00138.98           C  
ANISOU 1578  C   VAL A 204    24874  17645  10287   4531  -4296  -3625       C  
ATOM   1579  O   VAL A 204     127.651  56.462  15.424  1.00145.26           O  
ANISOU 1579  O   VAL A 204    26012  18259  10923   4531  -4185  -3601       O  
ATOM   1580  CB  VAL A 204     128.791  58.610  17.295  1.00122.45           C  
ANISOU 1580  CB  VAL A 204    23066  15106   8354   4462  -3581  -2757       C  
ATOM   1581  CG1 VAL A 204     129.097  60.003  17.827  1.00120.57           C  
ANISOU 1581  CG1 VAL A 204    22920  14786   8103   4630  -3422  -2413       C  
ATOM   1582  CG2 VAL A 204     128.636  57.616  18.431  1.00119.98           C  
ANISOU 1582  CG2 VAL A 204    22230  14829   8529   3891  -3468  -2882       C  
ATOM   1583  N   PHE A 205     125.908  56.820  16.806  1.00130.20           N  
ANISOU 1583  N   PHE A 205    23190  16831   9451   4280  -4553  -4014       N  
ATOM   1584  CA  PHE A 205     125.371  55.472  16.695  1.00141.37           C  
ANISOU 1584  CA  PHE A 205    24336  18352  11024   3934  -4696  -4433       C  
ATOM   1585  C   PHE A 205     123.985  55.411  16.071  1.00145.42           C  
ANISOU 1585  C   PHE A 205    24590  19283  11381   4150  -5244  -4998       C  
ATOM   1586  O   PHE A 205     123.656  54.403  15.442  1.00140.23           O  
ANISOU 1586  O   PHE A 205    23922  18689  10669   4036  -5419  -5356       O  
ATOM   1587  CB  PHE A 205     125.328  54.803  18.079  1.00132.48           C  
ANISOU 1587  CB  PHE A 205    22726  17187  10424   3311  -4445  -4434       C  
ATOM   1588  CG  PHE A 205     126.686  54.489  18.645  1.00124.61           C  
ANISOU 1588  CG  PHE A 205    21956  15793   9598   3047  -3935  -3972       C  
ATOM   1589  CD1 PHE A 205     127.638  53.840  17.877  1.00129.45           C  
ANISOU 1589  CD1 PHE A 205    23025  16132  10027   3094  -3749  -3830       C  
ATOM   1590  CD2 PHE A 205     127.014  54.850  19.940  1.00120.68           C  
ANISOU 1590  CD2 PHE A 205    21209  15214   9431   2776  -3650  -3696       C  
ATOM   1591  CE1 PHE A 205     128.889  53.549  18.393  1.00120.85           C  
ANISOU 1591  CE1 PHE A 205    22113  14714   9090   2882  -3296  -3433       C  
ATOM   1592  CE2 PHE A 205     128.263  54.563  20.460  1.00121.43           C  
ANISOU 1592  CE2 PHE A 205    21490  14976   9671   2564  -3209  -3301       C  
ATOM   1593  CZ  PHE A 205     129.201  53.912  19.683  1.00117.07           C  
ANISOU 1593  CZ  PHE A 205    21367  14172   8940   2622  -3035  -3175       C  
ATOM   1594  N   GLY A 206     123.166  56.452  16.228  1.00145.26           N  
ANISOU 1594  N   GLY A 206    24354  19556  11283   4466  -5527  -5107       N  
ATOM   1595  CA  GLY A 206     121.841  56.486  15.645  1.00156.04           C  
ANISOU 1595  CA  GLY A 206    25332  21325  12632   4659  -5963  -5552       C  
ATOM   1596  C   GLY A 206     120.800  55.641  16.345  1.00167.64           C  
ANISOU 1596  C   GLY A 206    26138  23111  14447   4184  -6146  -6076       C  
ATOM   1597  O   GLY A 206     119.624  55.698  15.965  1.00170.76           O  
ANISOU 1597  O   GLY A 206    26117  23883  14882   4306  -6488  -6462       O  
ATOM   1598  N   THR A 207     121.187  54.858  17.349  1.00175.50           N  
ANISOU 1598  N   THR A 207    26966  23935  15782   3603  -5843  -6034       N  
ATOM   1599  CA  THR A 207     120.262  54.016  18.091  1.00175.18           C  
ANISOU 1599  CA  THR A 207    26291  24129  16139   3059  -5903  -6470       C  
ATOM   1600  C   THR A 207     120.585  54.129  19.574  1.00163.14           C  
ANISOU 1600  C   THR A 207    24495  22455  15036   2624  -5496  -6159       C  
ATOM   1601  O   THR A 207     121.743  54.307  19.958  1.00148.10           O  
ANISOU 1601  O   THR A 207    22933  20172  13168   2577  -5102  -5637       O  
ATOM   1602  CB  THR A 207     120.337  52.557  17.624  1.00171.64           C  
ANISOU 1602  CB  THR A 207    25914  23550  15751   2677  -5869  -6744       C  
ATOM   1603  OG1 THR A 207     119.734  51.702  18.604  1.00168.81           O  
ANISOU 1603  OG1 THR A 207    25021  23275  15843   2024  -5745  -7024       O  
ATOM   1604  CG2 THR A 207     121.783  52.150  17.403  1.00166.21           C  
ANISOU 1604  CG2 THR A 207    25822  22353  14977   2636  -5464  -6260       C  
ATOM   1605  N   VAL A 208     119.545  54.023  20.405  1.00108.51           N  
ANISOU 1605  N   VAL A 208    12079  14725  14423  -2760    200   -166       N  
ATOM   1606  CA  VAL A 208     119.691  54.368  21.817  1.00112.92           C  
ANISOU 1606  CA  VAL A 208    12696  15118  15092  -2672    375   -191       C  
ATOM   1607  C   VAL A 208     120.574  53.357  22.543  1.00116.63           C  
ANISOU 1607  C   VAL A 208    13618  15253  15444  -2835    527   -222       C  
ATOM   1608  O   VAL A 208     121.390  53.731  23.393  1.00113.31           O  
ANISOU 1608  O   VAL A 208    13385  14584  15086  -2661    605   -170       O  
ATOM   1609  CB  VAL A 208     118.307  54.504  22.485  1.00107.71           C  
ANISOU 1609  CB  VAL A 208    11673  14755  14497  -2792    477   -324       C  
ATOM   1610  CG1 VAL A 208     117.492  55.594  21.809  1.00100.91           C  
ANISOU 1610  CG1 VAL A 208    10359  14214  13769  -2554    307   -285       C  
ATOM   1611  CG2 VAL A 208     117.551  53.189  22.458  1.00100.50           C  
ANISOU 1611  CG2 VAL A 208    10779  13990  13415  -3247    569   -473       C  
ATOM   1612  N   ILE A 209     120.438  52.069  22.219  1.00116.79           N  
ANISOU 1612  N   ILE A 209    13832  15254  15290  -3165    563   -307       N  
ATOM   1613  CA  ILE A 209     121.162  51.043  22.965  1.00111.45           C  
ANISOU 1613  CA  ILE A 209    13600  14249  14497  -3319    706   -339       C  
ATOM   1614  C   ILE A 209     122.658  51.131  22.688  1.00106.43           C  
ANISOU 1614  C   ILE A 209    13274  13317  13847  -3069    636   -228       C  
ATOM   1615  O   ILE A 209     123.478  51.035  23.609  1.00108.07           O  
ANISOU 1615  O   ILE A 209    13748  13257  14057  -2974    728   -197       O  
ATOM   1616  CB  ILE A 209     120.591  49.648  22.646  1.00112.73           C  
ANISOU 1616  CB  ILE A 209    13913  14441  14477  -3743    757   -465       C  
ATOM   1617  CG1 ILE A 209     121.647  48.558  22.858  1.00110.67           C  
ANISOU 1617  CG1 ILE A 209    14185  13786  14078  -3817    817   -461       C  
ATOM   1618  CG2 ILE A 209     120.012  49.608  21.239  1.00123.76           C  
ANISOU 1618  CG2 ILE A 209    15073  16125  15825  -3831    589   -494       C  
ATOM   1619  CD1 ILE A 209     121.952  48.266  24.313  1.00121.18           C  
ANISOU 1619  CD1 ILE A 209    15779  14867  15397  -3851    994   -458       C  
ATOM   1620  N   ALA A 210     123.039  51.325  21.424  1.00116.07           N  
ANISOU 1620  N   ALA A 210    14453  14606  15043  -2960    471   -168       N  
ATOM   1621  CA  ALA A 210     124.454  51.487  21.107  1.00121.47           C  
ANISOU 1621  CA  ALA A 210    15379  15061  15711  -2723    411    -71       C  
ATOM   1622  C   ALA A 210     125.035  52.731  21.763  1.00122.97           C  
ANISOU 1622  C   ALA A 210    15486  15173  16064  -2410    412     39       C  
ATOM   1623  O   ALA A 210     126.221  52.754  22.110  1.00120.61           O  
ANISOU 1623  O   ALA A 210    15428  14641  15759  -2255    432     91       O  
ATOM   1624  CB  ALA A 210     124.654  51.541  19.593  1.00117.83           C  
ANISOU 1624  CB  ALA A 210    14854  14740  15177  -2687    244    -31       C  
ATOM   1625  N   ALA A 211     124.216  53.768  21.952  1.00128.70           N  
ANISOU 1625  N   ALA A 211    15873  16091  16937  -2311    388     63       N  
ATOM   1626  CA  ALA A 211     124.692  54.994  22.581  1.00126.99           C  
ANISOU 1626  CA  ALA A 211    15587  15783  16881  -2027    390    151       C  
ATOM   1627  C   ALA A 211     124.697  54.898  24.101  1.00125.14           C  
ANISOU 1627  C   ALA A 211    15461  15404  16681  -2055    567     85       C  
ATOM   1628  O   ALA A 211     125.523  55.546  24.754  1.00122.66           O  
ANISOU 1628  O   ALA A 211    15248  14918  16441  -1859    591    140       O  
ATOM   1629  CB  ALA A 211     123.835  56.180  22.136  1.00121.26           C  
ANISOU 1629  CB  ALA A 211    14478  15293  16301  -1870    283    202       C  
ATOM   1630  N   ALA A 212     123.796  54.103  24.681  1.00118.97           N  
ANISOU 1630  N   ALA A 212    14667  14702  15834  -2317    692    -35       N  
ATOM   1631  CA  ALA A 212     123.709  53.998  26.131  1.00108.93           C  
ANISOU 1631  CA  ALA A 212    13498  13323  14568  -2373    869    -96       C  
ATOM   1632  C   ALA A 212     124.805  53.130  26.731  1.00112.82           C  
ANISOU 1632  C   ALA A 212    14427  13509  14932  -2417    936    -80       C  
ATOM   1633  O   ALA A 212     125.135  53.303  27.909  1.00115.32           O  
ANISOU 1633  O   ALA A 212    14867  13692  15257  -2365   1042    -86       O  
ATOM   1634  CB  ALA A 212     122.341  53.448  26.539  1.00103.04           C  
ANISOU 1634  CB  ALA A 212    12582  12793  13777  -2670    992   -228       C  
ATOM   1635  N   LEU A 213     125.376  52.208  25.956  1.00106.62           N  
ANISOU 1635  N   LEU A 213    13878  12613  14020  -2496    870    -65       N  
ATOM   1636  CA  LEU A 213     126.394  51.310  26.499  1.00104.10           C  
ANISOU 1636  CA  LEU A 213    13979  11999  13575  -2509    921    -54       C  
ATOM   1637  C   LEU A 213     127.656  52.038  26.949  1.00 96.45           C  
ANISOU 1637  C   LEU A 213    13107  10872  12670  -2206    884     32       C  
ATOM   1638  O   LEU A 213     128.151  51.736  28.049  1.00 99.10           O  
ANISOU 1638  O   LEU A 213    13676  11027  12951  -2192    969     32       O  
ATOM   1639  CB  LEU A 213     126.710  50.212  25.477  1.00108.58           C  
ANISOU 1639  CB  LEU A 213    14762  12489  14004  -2626    854    -78       C  
ATOM   1640  CG  LEU A 213     125.622  49.157  25.269  1.00114.77           C  
ANISOU 1640  CG  LEU A 213    15585  13348  14676  -2996    918   -185       C  
ATOM   1641  CD1 LEU A 213     126.005  48.208  24.147  1.00122.33           C  
ANISOU 1641  CD1 LEU A 213    16751  14224  15506  -3078    835   -220       C  
ATOM   1642  CD2 LEU A 213     125.367  48.389  26.557  1.00109.78           C  
ANISOU 1642  CD2 LEU A 213    15210  12549  13953  -3204   1085   -227       C  
ATOM   1643  N   PRO A 214     128.232  52.974  26.183  1.00 93.76           N  
ANISOU 1643  N   PRO A 214    12609  10589  12426  -1976    759    110       N  
ATOM   1644  CA  PRO A 214     129.412  53.690  26.701  1.00101.17           C  
ANISOU 1644  CA  PRO A 214    13627  11392  13420  -1730    736    179       C  
ATOM   1645  C   PRO A 214     129.120  54.517  27.939  1.00106.76           C  
ANISOU 1645  C   PRO A 214    14240  12096  14228  -1671    827    164       C  
ATOM   1646  O   PRO A 214     130.016  54.706  28.772  1.00107.99           O  
ANISOU 1646  O   PRO A 214    14554  12105  14372  -1553    851    184       O  
ATOM   1647  CB  PRO A 214     129.834  54.575  25.519  1.00 82.70           C  
ANISOU 1647  CB  PRO A 214    11105   9155  11162  -1562    595    265       C  
ATOM   1648  CG  PRO A 214     129.266  53.905  24.323  1.00 86.89           C  
ANISOU 1648  CG  PRO A 214    11589   9814  11613  -1709    533    241       C  
ATOM   1649  CD  PRO A 214     127.962  53.334  24.779  1.00 82.09           C  
ANISOU 1649  CD  PRO A 214    10917   9293  10982  -1949    628    146       C  
ATOM   1650  N   ALA A 215     127.892  55.021  28.086  1.00103.19           N  
ANISOU 1650  N   ALA A 215    13521  11818  13867  -1743    876    116       N  
ATOM   1651  CA  ALA A 215     127.540  55.766  29.290  1.00 98.50           C  
ANISOU 1651  CA  ALA A 215    12837  11231  13359  -1690    982     70       C  
ATOM   1652  C   ALA A 215     127.399  54.838  30.489  1.00 99.64           C  
ANISOU 1652  C   ALA A 215    13215  11281  13363  -1879   1137      2       C  
ATOM   1653  O   ALA A 215     127.804  55.189  31.604  1.00 98.92           O  
ANISOU 1653  O   ALA A 215    13223  11095  13269  -1807   1209    -11       O  
ATOM   1654  CB  ALA A 215     126.251  56.555  29.062  1.00 94.39           C  
ANISOU 1654  CB  ALA A 215    11943  10944  12976  -1684    990     23       C  
ATOM   1655  N   ILE A 216     126.826  53.649  30.279  1.00102.45           N  
ANISOU 1655  N   ILE A 216    13679  11657  13589  -2136   1186    -41       N  
ATOM   1656  CA  ILE A 216     126.729  52.665  31.354  1.00 93.44           C  
ANISOU 1656  CA  ILE A 216    12820  10394  12288  -2344   1328    -83       C  
ATOM   1657  C   ILE A 216     128.117  52.243  31.812  1.00 95.67           C  
ANISOU 1657  C   ILE A 216    13468  10410  12470  -2211   1287    -12       C  
ATOM   1658  O   ILE A 216     128.390  52.154  33.015  1.00 93.40           O  
ANISOU 1658  O   ILE A 216    13360  10019  12107  -2218   1375    -15       O  
ATOM   1659  CB  ILE A 216     125.890  51.456  30.896  1.00 86.03           C  
ANISOU 1659  CB  ILE A 216    11956   9504  11227  -2669   1376   -137       C  
ATOM   1660  CG1 ILE A 216     124.436  51.870  30.663  1.00 88.98           C  
ANISOU 1660  CG1 ILE A 216    11932  10191  11685  -2819   1432   -226       C  
ATOM   1661  CG2 ILE A 216     125.971  50.330  31.915  1.00 83.09           C  
ANISOU 1661  CG2 ILE A 216    11967   8939  10664  -2888   1505   -148       C  
ATOM   1662  CD1 ILE A 216     123.568  50.764  30.104  1.00 94.06           C  
ANISOU 1662  CD1 ILE A 216    12599  10927  12212  -3167   1467   -292       C  
ATOM   1663  N   ILE A 217     129.018  51.983  30.862  1.00103.55           N  
ANISOU 1663  N   ILE A 217    14570  11318  13458  -2080   1152     46       N  
ATOM   1664  CA  ILE A 217     130.394  51.637  31.210  1.00105.39           C  
ANISOU 1664  CA  ILE A 217    15100  11337  13606  -1910   1095    103       C  
ATOM   1665  C   ILE A 217     131.051  52.775  31.979  1.00 91.47           C  
ANISOU 1665  C   ILE A 217    13246   9577  11932  -1697   1084    130       C  
ATOM   1666  O   ILE A 217     131.769  52.548  32.961  1.00 82.28           O  
ANISOU 1666  O   ILE A 217    12309   8277  10675  -1635   1105    148       O  
ATOM   1667  CB  ILE A 217     131.189  51.271  29.941  1.00104.00           C  
ANISOU 1667  CB  ILE A 217    14981  11119  13414  -1795    961    137       C  
ATOM   1668  CG1 ILE A 217     130.637  49.984  29.325  1.00 99.31           C  
ANISOU 1668  CG1 ILE A 217    14560  10472  12701  -2022    980     90       C  
ATOM   1669  CG2 ILE A 217     132.677  51.131  30.249  1.00105.50           C  
ANISOU 1669  CG2 ILE A 217    15392  11148  13546  -1565    890    186       C  
ATOM   1670  CD1 ILE A 217     130.569  48.826  30.297  1.00 93.22           C  
ANISOU 1670  CD1 ILE A 217    14164   9489  11768  -2184   1076     75       C  
ATOM   1671  N   GLY A 218     130.806  54.018  31.554  1.00 91.66           N  
ANISOU 1671  N   GLY A 218    12952   9749  12128  -1585   1044    134       N  
ATOM   1672  CA  GLY A 218     131.347  55.160  32.270  1.00 88.58           C  
ANISOU 1672  CA  GLY A 218    12481   9349  11829  -1410   1040    143       C  
ATOM   1673  C   GLY A 218     130.757  55.329  33.655  1.00 91.29           C  
ANISOU 1673  C   GLY A 218    12846   9698  12142  -1499   1184     73       C  
ATOM   1674  O   GLY A 218     131.449  55.769  34.579  1.00 75.04           O  
ANISOU 1674  O   GLY A 218    10881   7567  10063  -1397   1196     70       O  
ATOM   1675  N   GLY A 219     129.478  54.988  33.823  1.00 99.75           N  
ANISOU 1675  N   GLY A 219    13822  10879  13198  -1701   1300      6       N  
ATOM   1676  CA  GLY A 219     128.884  55.028  35.148  1.00 98.23           C  
ANISOU 1676  CA  GLY A 219    13663  10717  12945  -1819   1462    -71       C  
ATOM   1677  C   GLY A 219     129.383  53.909  36.042  1.00 95.56           C  
ANISOU 1677  C   GLY A 219    13712  10212  12384  -1938   1516    -43       C  
ATOM   1678  O   GLY A 219     129.673  54.127  37.221  1.00 92.69           O  
ANISOU 1678  O   GLY A 219    13468   9803  11945  -1918   1584    -62       O  
ATOM   1679  N   LEU A 220     129.487  52.694  35.496  1.00100.72           N  
ANISOU 1679  N   LEU A 220    14584  10762  12921  -2059   1481      2       N  
ATOM   1680  CA  LEU A 220     130.053  51.586  36.256  1.00 90.62           C  
ANISOU 1680  CA  LEU A 220    13723   9280  11430  -2135   1504     50       C  
ATOM   1681  C   LEU A 220     131.504  51.850  36.630  1.00 87.17           C  
ANISOU 1681  C   LEU A 220    13444   8712  10965  -1867   1386    115       C  
ATOM   1682  O   LEU A 220     131.970  51.389  37.678  1.00 84.01           O  
ANISOU 1682  O   LEU A 220    13327   8190  10404  -1874   1412    147       O  
ATOM   1683  CB  LEU A 220     129.951  50.287  35.455  1.00 96.88           C  
ANISOU 1683  CB  LEU A 220    14732   9954  12125  -2282   1471     78       C  
ATOM   1684  CG  LEU A 220     128.567  49.774  35.056  1.00102.26           C  
ANISOU 1684  CG  LEU A 220    15304  10757  12792  -2603   1579     10       C  
ATOM   1685  CD1 LEU A 220     128.697  48.535  34.184  1.00106.14           C  
ANISOU 1685  CD1 LEU A 220    16048  11093  13188  -2718   1519     31       C  
ATOM   1686  CD2 LEU A 220     127.726  49.481  36.282  1.00 99.82           C  
ANISOU 1686  CD2 LEU A 220    15086  10485  12358  -2870   1769    -31       C  
ATOM   1687  N   ALA A 221     132.233  52.585  35.787  1.00 95.61           N  
ANISOU 1687  N   ALA A 221    14333   9820  12175  -1642   1254    137       N  
ATOM   1688  CA  ALA A 221     133.642  52.849  36.057  1.00 94.06           C  
ANISOU 1688  CA  ALA A 221    14245   9541  11954  -1404   1138    185       C  
ATOM   1689  C   ALA A 221     133.811  53.754  37.271  1.00 97.15           C  
ANISOU 1689  C   ALA A 221    14590   9975  12348  -1351   1188    151       C  
ATOM   1690  O   ALA A 221     134.593  53.449  38.179  1.00 91.99           O  
ANISOU 1690  O   ALA A 221    14167   9233  11553  -1286   1160    179       O  
ATOM   1691  CB  ALA A 221     134.307  53.466  34.827  1.00 90.07           C  
ANISOU 1691  CB  ALA A 221    13536   9098  11590  -1223   1005    211       C  
ATOM   1692  N   ILE A 222     133.085  54.873  37.308  1.00 95.76           N  
ANISOU 1692  N   ILE A 222    14123   9934  12326  -1368   1255     84       N  
ATOM   1693  CA  ILE A 222     133.211  55.777  38.447  1.00 95.75           C  
ANISOU 1693  CA  ILE A 222    14082   9966  12330  -1322   1311     25       C  
ATOM   1694  C   ILE A 222     132.576  55.169  39.692  1.00 93.65           C  
ANISOU 1694  C   ILE A 222    14006   9692  11885  -1510   1463    -14       C  
ATOM   1695  O   ILE A 222     133.008  55.452  40.817  1.00 81.06           O  
ANISOU 1695  O   ILE A 222    12527   8082  10189  -1481   1489    -39       O  
ATOM   1696  CB  ILE A 222     132.610  57.158  38.117  1.00 95.75           C  
ANISOU 1696  CB  ILE A 222    13742  10085  12554  -1259   1339    -45       C  
ATOM   1697  CG1 ILE A 222     131.098  57.063  37.911  1.00 96.12           C  
ANISOU 1697  CG1 ILE A 222    13608  10255  12659  -1421   1467   -109       C  
ATOM   1698  CG2 ILE A 222     133.276  57.750  36.883  1.00 90.91           C  
ANISOU 1698  CG2 ILE A 222    12980   9470  12093  -1097   1188     18       C  
ATOM   1699  CD1 ILE A 222     130.442  58.397  37.638  1.00 88.33           C  
ANISOU 1699  CD1 ILE A 222    12292   9378  11890  -1321   1488   -181       C  
ATOM   1700  N   ALA A 223     131.555  54.323  39.523  1.00 97.48           N  
ANISOU 1700  N   ALA A 223    14532  10198  12308  -1729   1566    -21       N  
ATOM   1701  CA  ALA A 223     130.947  53.662  40.673  1.00 96.11           C  
ANISOU 1701  CA  ALA A 223    14563  10019  11937  -1952   1723    -46       C  
ATOM   1702  C   ALA A 223     131.940  52.731  41.355  1.00 97.23           C  
ANISOU 1702  C   ALA A 223    15119   9972  11850  -1923   1654     54       C  
ATOM   1703  O   ALA A 223     132.056  52.726  42.587  1.00 98.64           O  
ANISOU 1703  O   ALA A 223    15468  10143  11868  -1973   1722     46       O  
ATOM   1704  CB  ALA A 223     129.697  52.895  40.238  1.00 94.90           C  
ANISOU 1704  CB  ALA A 223    14368   9930  11760  -2224   1841    -72       C  
ATOM   1705  N   GLY A 224     132.673  51.939  40.569  1.00 96.41           N  
ANISOU 1705  N   GLY A 224    15187   9724  11723  -1828   1514    145       N  
ATOM   1706  CA  GLY A 224     133.713  51.095  41.125  1.00 86.74           C  
ANISOU 1706  CA  GLY A 224    14341   8316  10301  -1731   1416    241       C  
ATOM   1707  C   GLY A 224     134.972  51.834  41.517  1.00 85.15           C  
ANISOU 1707  C   GLY A 224    14104   8136  10113  -1462   1281    252       C  
ATOM   1708  O   GLY A 224     135.730  51.336  42.355  1.00 77.15           O  
ANISOU 1708  O   GLY A 224    13376   7027   8912  -1387   1216    316       O  
ATOM   1709  N   ALA A 225     135.207  53.018  40.942  1.00 87.54           N  
ANISOU 1709  N   ALA A 225    14070   8566  10625  -1326   1232    194       N  
ATOM   1710  CA  ALA A 225     136.401  53.787  41.277  1.00 83.26           C  
ANISOU 1710  CA  ALA A 225    13473   8062  10101  -1110   1108    191       C  
ATOM   1711  C   ALA A 225     136.243  54.535  42.594  1.00 93.14           C  
ANISOU 1711  C   ALA A 225    14715   9389  11284  -1164   1194    119       C  
ATOM   1712  O   ALA A 225     137.213  54.672  43.346  1.00 91.14           O  
ANISOU 1712  O   ALA A 225    14578   9136  10915  -1050   1103    132       O  
ATOM   1713  CB  ALA A 225     136.737  54.763  40.152  1.00 78.63           C  
ANISOU 1713  CB  ALA A 225    12566   7562   9749   -977   1028    165       C  
ATOM   1714  N   LEU A 226     135.039  55.034  42.888  1.00102.20           N  
ANISOU 1714  N   LEU A 226    15714  10623  12494  -1332   1366     29       N  
ATOM   1715  CA  LEU A 226     134.808  55.671  44.181  1.00 94.32           C  
ANISOU 1715  CA  LEU A 226    14727   9701  11408  -1396   1473    -61       C  
ATOM   1716  C   LEU A 226     134.895  54.667  45.322  1.00 94.75           C  
ANISOU 1716  C   LEU A 226    15148   9691  11162  -1512   1513     -1       C  
ATOM   1717  O   LEU A 226     135.197  55.048  46.459  1.00105.37           O  
ANISOU 1717  O   LEU A 226    16583  11086  12369  -1514   1534    -45       O  
ATOM   1718  CB  LEU A 226     133.448  56.370  44.193  1.00 91.29           C  
ANISOU 1718  CB  LEU A 226    14085   9440  11160  -1530   1659   -186       C  
ATOM   1719  CG  LEU A 226     133.276  57.569  43.257  1.00 96.41           C  
ANISOU 1719  CG  LEU A 226    14381  10149  12100  -1399   1623   -251       C  
ATOM   1720  CD1 LEU A 226     131.898  58.193  43.421  1.00100.16           C  
ANISOU 1720  CD1 LEU A 226    14615  10753  12686  -1501   1806   -384       C  
ATOM   1721  CD2 LEU A 226     134.367  58.601  43.495  1.00 90.23           C  
ANISOU 1721  CD2 LEU A 226    13553   9351  11380  -1220   1509   -283       C  
ATOM   1722  N   GLY A 227     134.637  53.390  45.043  1.00 88.56           N  
ANISOU 1722  N   GLY A 227    14598   8789  10262  -1618   1519    101       N  
ATOM   1723  CA  GLY A 227     134.746  52.353  46.049  1.00 88.92           C  
ANISOU 1723  CA  GLY A 227    15045   8731  10010  -1728   1542    191       C  
ATOM   1724  C   GLY A 227     136.182  51.950  46.305  1.00 90.46           C  
ANISOU 1724  C   GLY A 227    15475   8822  10075  -1492   1328    295       C  
ATOM   1725  O   GLY A 227     136.552  51.628  47.438  1.00 79.29           O  
ANISOU 1725  O   GLY A 227    14329   7382   8417  -1505   1309    345       O  
ATOM   1726  N   ILE A 228     137.003  51.963  45.251  1.00 95.96           N  
ANISOU 1726  N   ILE A 228    16062   9479  10920  -1271   1163    326       N  
ATOM   1727  CA  ILE A 228     138.423  51.660  45.412  1.00 87.68           C  
ANISOU 1727  CA  ILE A 228    15166   8379   9770  -1013    951    403       C  
ATOM   1728  C   ILE A 228     139.092  52.710  46.286  1.00 86.18           C  
ANISOU 1728  C   ILE A 228    14853   8343   9547   -923    898    333       C  
ATOM   1729  O   ILE A 228     139.869  52.384  47.192  1.00 76.39           O  
ANISOU 1729  O   ILE A 228    13836   7096   8092   -829    790    390       O  
ATOM   1730  CB  ILE A 228     139.105  51.553  44.036  1.00 86.96           C  
ANISOU 1730  CB  ILE A 228    14926   8259   9855   -811    813    421       C  
ATOM   1731  CG1 ILE A 228     138.582  50.337  43.272  1.00 80.42           C  
ANISOU 1731  CG1 ILE A 228    14297   7252   9008   -890    843    488       C  
ATOM   1732  CG2 ILE A 228     140.617  51.481  44.189  1.00 90.03           C  
ANISOU 1732  CG2 ILE A 228    15369   8670  10168   -523    599    463       C  
ATOM   1733  CD1 ILE A 228     139.052  50.279  41.836  1.00 78.53           C  
ANISOU 1733  CD1 ILE A 228    13885   7008   8944   -730    744    480       C  
ATOM   1734  N   MET A 229     138.788  53.988  46.040  1.00 94.38           N  
ANISOU 1734  N   MET A 229    15549   9519  10791   -953    967    207       N  
ATOM   1735  CA  MET A 229     139.410  55.059  46.812  1.00 96.40           C  
ANISOU 1735  CA  MET A 229    15688   9908  11031   -890    922    118       C  
ATOM   1736  C   MET A 229     138.898  55.093  48.249  1.00 87.83           C  
ANISOU 1736  C   MET A 229    14781   8865   9724  -1054   1045     75       C  
ATOM   1737  O   MET A 229     139.631  55.507  49.154  1.00 74.97           O  
ANISOU 1737  O   MET A 229    13207   7321   7959   -995    966     40       O  
ATOM   1738  CB  MET A 229     139.176  56.404  46.124  1.00 83.71           C  
ANISOU 1738  CB  MET A 229    13710   8389   9708   -882    967     -2       C  
ATOM   1739  CG  MET A 229     139.564  56.426  44.650  1.00 72.12           C  
ANISOU 1739  CG  MET A 229    12059   6897   8448   -757    868     43       C  
ATOM   1740  SD  MET A 229     141.233  55.822  44.348  1.00 57.65           S  
ANISOU 1740  SD  MET A 229    10318   5068   6519   -513    623    136       S  
ATOM   1741  CE  MET A 229     142.170  56.990  45.320  1.00 58.14           C  
ANISOU 1741  CE  MET A 229    10275   5283   6533   -466    543     37       C  
ATOM   1742  N   ARG A 230     137.652  54.670  48.478  1.00 90.30           N  
ANISOU 1742  N   ARG A 230    15178   9146   9986  -1274   1240     68       N  
ATOM   1743  CA  ARG A 230     137.160  54.543  49.846  1.00 89.24           C  
ANISOU 1743  CA  ARG A 230    15248   9062   9599  -1452   1372     39       C  
ATOM   1744  C   ARG A 230     137.904  53.446  50.597  1.00100.63           C  
ANISOU 1744  C   ARG A 230    17099  10409  10728  -1407   1243    197       C  
ATOM   1745  O   ARG A 230     138.090  53.544  51.816  1.00104.61           O  
ANISOU 1745  O   ARG A 230    17772  10984  10990  -1461   1254    184       O  
ATOM   1746  CB  ARG A 230     135.653  54.277  49.839  1.00 85.63           C  
ANISOU 1746  CB  ARG A 230    14765   8618   9155  -1718   1620     -4       C  
ATOM   1747  CG  ARG A 230     135.036  53.983  51.205  1.00 89.65           C  
ANISOU 1747  CG  ARG A 230    15505   9188   9372  -1949   1788    -24       C  
ATOM   1748  CD  ARG A 230     135.217  55.125  52.193  1.00 91.00           C  
ANISOU 1748  CD  ARG A 230    15563   9521   9492  -1930   1835   -182       C  
ATOM   1749  NE  ARG A 230     134.455  54.898  53.419  1.00104.31           N  
ANISOU 1749  NE  ARG A 230    17430  11298  10903  -2179   2037   -225       N  
ATOM   1750  CZ  ARG A 230     134.924  54.255  54.483  1.00123.41           C  
ANISOU 1750  CZ  ARG A 230    20215  13698  12977  -2237   1988   -122       C  
ATOM   1751  NH1 ARG A 230     136.160  53.774  54.478  1.00131.21           N  
ANISOU 1751  NH1 ARG A 230    21412  14581  13863  -2035   1731     27       N  
ATOM   1752  NH2 ARG A 230     134.157  54.092  55.555  1.00124.18           N  
ANISOU 1752  NH2 ARG A 230    20465  13899  12819  -2492   2195   -167       N  
ATOM   1753  N   LEU A 231     138.346  52.406  49.887  1.00104.97           N  
ANISOU 1753  N   LEU A 231    17819  10795  11268  -1293   1113    342       N  
ATOM   1754  CA  LEU A 231     139.188  51.388  50.505  1.00105.69           C  
ANISOU 1754  CA  LEU A 231    18301  10774  11084  -1176    949    500       C  
ATOM   1755  C   LEU A 231     140.599  51.913  50.738  1.00107.14           C  
ANISOU 1755  C   LEU A 231    18394  11068  11245   -901    718    487       C  
ATOM   1756  O   LEU A 231     141.246  51.555  51.731  1.00110.91           O  
ANISOU 1756  O   LEU A 231    19126  11561  11455   -829    600    562       O  
ATOM   1757  CB  LEU A 231     139.212  50.134  49.630  1.00 93.82           C  
ANISOU 1757  CB  LEU A 231    17012   9042   9595  -1117    884    637       C  
ATOM   1758  CG  LEU A 231     140.199  49.022  49.988  1.00 85.15           C  
ANISOU 1758  CG  LEU A 231    16311   7780   8264   -910    675    808       C  
ATOM   1759  CD1 LEU A 231     139.894  48.444  51.360  1.00 81.51           C  
ANISOU 1759  CD1 LEU A 231    16255   7260   7454  -1077    730    910       C  
ATOM   1760  CD2 LEU A 231     140.175  47.938  48.928  1.00 72.18           C  
ANISOU 1760  CD2 LEU A 231    14827   5900   6696   -838    628    897       C  
ATOM   1761  N   VAL A 232     141.094  52.762  49.834  1.00101.50           N  
ANISOU 1761  N   VAL A 232    17319  10447  10799   -758    647    394       N  
ATOM   1762  CA  VAL A 232     142.421  53.349  50.009  1.00 93.76           C  
ANISOU 1762  CA  VAL A 232    16205   9610   9810   -538    442    359       C  
ATOM   1763  C   VAL A 232     142.441  54.259  51.231  1.00 92.63           C  
ANISOU 1763  C   VAL A 232    16030   9632   9535   -645    485    248       C  
ATOM   1764  O   VAL A 232     143.438  54.324  51.961  1.00 86.04           O  
ANISOU 1764  O   VAL A 232    15267   8904   8520   -521    314    260       O  
ATOM   1765  CB  VAL A 232     142.846  54.098  48.732  1.00 89.27           C  
ANISOU 1765  CB  VAL A 232    15261   9105   9553   -420    389    284       C  
ATOM   1766  CG1 VAL A 232     144.165  54.821  48.948  1.00 92.04           C  
ANISOU 1766  CG1 VAL A 232    15438   9637   9894   -250    203    225       C  
ATOM   1767  CG2 VAL A 232     142.959  53.133  47.564  1.00 74.16           C  
ANISOU 1767  CG2 VAL A 232    13400   7048   7729   -295    330    385       C  
ATOM   1768  N   ALA A 233     141.334  54.962  51.482  1.00103.34           N  
ANISOU 1768  N   ALA A 233    17273  11022  10969   -870    711    127       N  
ATOM   1769  CA  ALA A 233     141.232  55.845  52.637  1.00100.89           C  
ANISOU 1769  CA  ALA A 233    16941  10858  10534   -986    784     -9       C  
ATOM   1770  C   ALA A 233     141.280  55.095  53.962  1.00102.69           C  
ANISOU 1770  C   ALA A 233    17544  11098  10376  -1061    770     78       C  
ATOM   1771  O   ALA A 233     141.468  55.730  55.006  1.00 88.89           O  
ANISOU 1771  O   ALA A 233    15814   9495   8467  -1125    779    -24       O  
ATOM   1772  CB  ALA A 233     139.946  56.669  52.554  1.00 97.96           C  
ANISOU 1772  CB  ALA A 233    16370  10512  10338  -1184   1044   -166       C  
ATOM   1773  N   GLU A 234     141.113  53.771  53.949  1.00103.45           N  
ANISOU 1773  N   GLU A 234    17959  11036  10311  -1063    747    264       N  
ATOM   1774  CA  GLU A 234     141.231  52.979  55.166  1.00 99.46           C  
ANISOU 1774  CA  GLU A 234    17858  10515   9418  -1121    708    386       C  
ATOM   1775  C   GLU A 234     142.677  52.810  55.612  1.00 98.40           C  
ANISOU 1775  C   GLU A 234    17825  10454   9107   -860    410    463       C  
ATOM   1776  O   GLU A 234     142.912  52.381  56.746  1.00 96.43           O  
ANISOU 1776  O   GLU A 234    17883  10241   8516   -886    344    548       O  
ATOM   1777  CB  GLU A 234     140.592  51.606  54.955  1.00 89.35           C  
ANISOU 1777  CB  GLU A 234    16919   9002   8027  -1215    774    570       C  
ATOM   1778  CG  GLU A 234     139.897  51.044  56.181  1.00107.09           C  
ANISOU 1778  CG  GLU A 234    19537  11232   9921  -1472    916    644       C  
ATOM   1779  CD  GLU A 234     138.626  51.796  56.520  1.00107.45           C  
ANISOU 1779  CD  GLU A 234    19398  11411  10018  -1781   1227    466       C  
ATOM   1780  OE1 GLU A 234     138.496  52.265  57.670  1.00106.10           O  
ANISOU 1780  OE1 GLU A 234    19291  11400   9621  -1911   1307    385       O  
ATOM   1781  OE2 GLU A 234     137.757  51.921  55.631  1.00108.10           O  
ANISOU 1781  OE2 GLU A 234    19260  11452  10359  -1886   1388    396       O  
ATOM   1782  N   PHE A 235     143.642  53.138  54.753  1.00101.86           N  
ANISOU 1782  N   PHE A 235    18006  10941   9757   -616    227    435       N  
ATOM   1783  CA  PHE A 235     145.059  52.974  55.051  1.00111.69           C  
ANISOU 1783  CA  PHE A 235    19281  12297  10860   -346    -67    493       C  
ATOM   1784  C   PHE A 235     145.821  54.289  55.010  1.00113.99           C  
ANISOU 1784  C   PHE A 235    19192  12830  11288   -298   -148    307       C  
ATOM   1785  O   PHE A 235     146.579  54.590  55.939  1.00126.76           O  
ANISOU 1785  O   PHE A 235    20842  14632  12691   -252   -295    274       O  
ATOM   1786  CB  PHE A 235     145.685  51.968  54.068  1.00111.30           C  
ANISOU 1786  CB  PHE A 235    19297  12097  10896    -73   -236    639       C  
ATOM   1787  CG  PHE A 235     144.964  50.650  54.007  1.00116.61           C  
ANISOU 1787  CG  PHE A 235    20369  12488  11450   -128   -161    816       C  
ATOM   1788  CD1 PHE A 235     145.275  49.635  54.898  1.00120.40           C  
ANISOU 1788  CD1 PHE A 235    21288  12869  11591    -45   -291    996       C  
ATOM   1789  CD2 PHE A 235     143.976  50.426  53.062  1.00113.63           C  
ANISOU 1789  CD2 PHE A 235    19941  11941  11290   -275     32    806       C  
ATOM   1790  CE1 PHE A 235     144.614  48.421  54.848  1.00114.70           C  
ANISOU 1790  CE1 PHE A 235    20972  11855  10754   -123   -218   1164       C  
ATOM   1791  CE2 PHE A 235     143.311  49.215  53.007  1.00114.36           C  
ANISOU 1791  CE2 PHE A 235    20411  11772  11269   -365    106    957       C  
ATOM   1792  CZ  PHE A 235     143.631  48.211  53.902  1.00116.38           C  
ANISOU 1792  CZ  PHE A 235    21127  11901  11190   -297    -14   1137       C  
ATOM   1793  N   THR A 236     145.644  55.081  53.960  1.00101.65           N  
ANISOU 1793  N   THR A 236    17284  11272  10066   -321    -64    190       N  
ATOM   1794  CA  THR A 236     146.294  56.370  53.787  1.00104.37           C  
ANISOU 1794  CA  THR A 236    17278  11805  10571   -314   -119     16       C  
ATOM   1795  C   THR A 236     145.245  57.420  53.461  1.00105.12           C  
ANISOU 1795  C   THR A 236    17170  11859  10912   -529    129   -142       C  
ATOM   1796  O   THR A 236     144.169  57.094  52.949  1.00104.28           O  
ANISOU 1796  O   THR A 236    17098  11596  10926   -623    308   -106       O  
ATOM   1797  CB  THR A 236     147.345  56.320  52.667  1.00103.66           C  
ANISOU 1797  CB  THR A 236    16952  11767  10667    -82   -301     45       C  
ATOM   1798  OG1 THR A 236     146.696  56.089  51.410  1.00 90.80           O  
ANISOU 1798  OG1 THR A 236    15231   9968   9300    -86   -181     83       O  
ATOM   1799  CG2 THR A 236     148.356  55.209  52.924  1.00125.52           C  
ANISOU 1799  CG2 THR A 236    19912  14572  13208    183   -550    196       C  
ATOM   1800  N   PRO A 237     145.522  58.692  53.749  1.00107.53           N  
ANISOU 1800  N   PRO A 237    17264  12298  11293   -609    140   -324       N  
ATOM   1801  CA  PRO A 237     144.547  59.746  53.442  1.00100.97           C  
ANISOU 1801  CA  PRO A 237    16250  11407  10706   -775    363   -480       C  
ATOM   1802  C   PRO A 237     144.404  59.986  51.945  1.00 93.12           C  
ANISOU 1802  C   PRO A 237    15012  10314  10056   -710    386   -457       C  
ATOM   1803  O   PRO A 237     145.301  59.704  51.147  1.00 83.83           O  
ANISOU 1803  O   PRO A 237    13732   9165   8953   -554    221   -376       O  
ATOM   1804  CB  PRO A 237     145.123  60.980  54.146  1.00 96.18           C  
ANISOU 1804  CB  PRO A 237    15522  10953  10068   -849    321   -674       C  
ATOM   1805  CG  PRO A 237     146.584  60.696  54.271  1.00 96.39           C  
ANISOU 1805  CG  PRO A 237    15532  11141   9951   -698     46   -615       C  
ATOM   1806  CD  PRO A 237     146.681  59.216  54.494  1.00105.95           C  
ANISOU 1806  CD  PRO A 237    17013  12311  10932   -565    -48   -405       C  
ATOM   1807  N   VAL A 238     143.238  60.519  51.573  1.00 97.21           N  
ANISOU 1807  N   VAL A 238    15430  10731  10773   -828    597   -534       N  
ATOM   1808  CA  VAL A 238     142.928  60.882  50.196  1.00 92.75           C  
ANISOU 1808  CA  VAL A 238    14636  10075  10531   -790    636   -520       C  
ATOM   1809  C   VAL A 238     142.340  62.288  50.177  1.00 81.59           C  
ANISOU 1809  C   VAL A 238    13038   8639   9325   -889    774   -700       C  
ATOM   1810  O   VAL A 238     141.643  62.704  51.107  1.00 83.56           O  
ANISOU 1810  O   VAL A 238    13355   8902   9494  -1003    920   -828       O  
ATOM   1811  CB  VAL A 238     141.961  59.873  49.530  1.00 91.17           C  
ANISOU 1811  CB  VAL A 238    14512   9749  10379   -800    739   -396       C  
ATOM   1812  CG1 VAL A 238     142.585  58.488  49.485  1.00 90.65           C  
ANISOU 1812  CG1 VAL A 238    14662   9658  10122   -682    595   -222       C  
ATOM   1813  CG2 VAL A 238     140.634  59.832  50.266  1.00102.35           C  
ANISOU 1813  CG2 VAL A 238    16028  11138  11721   -971    965   -463       C  
ATOM   1814  N   HIS A 239     142.618  63.018  49.099  1.00 80.73           N  
ANISOU 1814  N   HIS A 239    12708   8489   9478   -841    730   -710       N  
ATOM   1815  CA  HIS A 239     142.308  64.438  49.008  1.00 82.98           C  
ANISOU 1815  CA  HIS A 239    12838   8723   9969   -904    814   -868       C  
ATOM   1816  C   HIS A 239     140.915  64.669  48.423  1.00 82.44           C  
ANISOU 1816  C   HIS A 239    12677   8536  10111   -921    995   -886       C  
ATOM   1817  O   HIS A 239     140.328  63.790  47.788  1.00 71.98           O  
ANISOU 1817  O   HIS A 239    11355   7179   8813   -894   1031   -764       O  
ATOM   1818  CB  HIS A 239     143.358  65.147  48.153  1.00 83.87           C  
ANISOU 1818  CB  HIS A 239    12779   8847  10239   -862    668   -856       C  
ATOM   1819  CG  HIS A 239     143.600  66.569  48.546  1.00 80.14           C  
ANISOU 1819  CG  HIS A 239    12242   8350   9856   -952    687  -1034       C  
ATOM   1820  ND1 HIS A 239     142.928  67.625  47.972  1.00 85.80           N  
ANISOU 1820  ND1 HIS A 239    12851   8913  10836   -974    789  -1106       N  
ATOM   1821  CD2 HIS A 239     144.447  67.110  49.453  1.00 90.17           C  
ANISOU 1821  CD2 HIS A 239    13557   9719  10984  -1028    610  -1159       C  
ATOM   1822  CE1 HIS A 239     143.349  68.756  48.509  1.00 92.11           C  
ANISOU 1822  CE1 HIS A 239    13652   9687  11657  -1062    782  -1269       C  
ATOM   1823  NE2 HIS A 239     144.269  68.471  49.413  1.00 96.43           N  
ANISOU 1823  NE2 HIS A 239    14284  10397  11957  -1110    677  -1311       N  
ATOM   1824  N   PHE A 240     140.390  65.882  48.644  1.00 90.26           N  
ANISOU 1824  N   PHE A 240    13581   9464  11250   -962   1104  -1052       N  
ATOM   1825  CA APHE A 240     139.072  66.190  48.101  0.53 89.99           C  
ANISOU 1825  CA APHE A 240    13428   9340  11424   -946   1262  -1083       C  
ATOM   1826  CA BPHE A 240     139.082  66.252  48.103  0.47 90.36           C  
ANISOU 1826  CA BPHE A 240    13470   9383  11478   -946   1262  -1089       C  
ATOM   1827  C   PHE A 240     139.103  66.296  46.580  1.00 88.83           C  
ANISOU 1827  C   PHE A 240    13118   9115  11520   -862   1185   -951       C  
ATOM   1828  O   PHE A 240     138.127  65.917  45.923  1.00 76.08           O  
ANISOU 1828  O   PHE A 240    11421   7476  10011   -837   1263   -892       O  
ATOM   1829  CB APHE A 240     138.507  67.469  48.737  0.53 88.20           C  
ANISOU 1829  CB APHE A 240    13161   9053  11298   -970   1394  -1305       C  
ATOM   1830  CB BPHE A 240     138.649  67.617  48.645  0.47 87.77           C  
ANISOU 1830  CB BPHE A 240    13096   8986  11269   -964   1373  -1306       C  
ATOM   1831  CG APHE A 240     139.125  68.753  48.235  0.53 90.54           C  
ANISOU 1831  CG APHE A 240    13371   9230  11800   -938   1310  -1365       C  
ATOM   1832  CG BPHE A 240     138.064  67.577  50.027  0.47 79.29           C  
ANISOU 1832  CG BPHE A 240    12140   7989   9996  -1047   1530  -1470       C  
ATOM   1833  CD1APHE A 240     138.652  69.370  47.085  0.53 99.10           C  
ANISOU 1833  CD1APHE A 240    14305  10180  13169   -855   1313  -1317       C  
ATOM   1834  CD1BPHE A 240     136.711  67.345  50.215  0.47 76.24           C  
ANISOU 1834  CD1BPHE A 240    11707   7630   9631  -1060   1728  -1529       C  
ATOM   1835  CD2APHE A 240     140.144  69.369  48.941  0.53 95.56           C  
ANISOU 1835  CD2APHE A 240    14090   9886  12333  -1009   1227  -1472       C  
ATOM   1836  CD2BPHE A 240     138.858  67.804  51.138  0.47 76.52           C  
ANISOU 1836  CD2BPHE A 240    11935   7711   9429  -1123   1484  -1577       C  
ATOM   1837  CE1APHE A 240     139.206  70.553  46.631  0.53 93.46           C  
ANISOU 1837  CE1APHE A 240    13552   9329  12631   -847   1240  -1356       C  
ATOM   1838  CE1BPHE A 240     136.166  67.320  51.485  0.47 71.13           C  
ANISOU 1838  CE1BPHE A 240    11162   7080   8785  -1153   1891  -1690       C  
ATOM   1839  CE2APHE A 240     140.698  70.558  48.493  0.53 95.13           C  
ANISOU 1839  CE2APHE A 240    13979   9706  12460  -1021   1160  -1530       C  
ATOM   1840  CE2BPHE A 240     138.319  67.780  52.410  0.47 70.15           C  
ANISOU 1840  CE2BPHE A 240    11247   6991   8416  -1210   1634  -1732       C  
ATOM   1841  CZ APHE A 240     140.230  71.148  47.337  0.53 88.96           C  
ANISOU 1841  CZ APHE A 240    13075   8765  11960   -942   1169  -1465       C  
ATOM   1842  CZ BPHE A 240     136.972  67.538  52.583  0.47 69.18           C  
ANISOU 1842  CZ BPHE A 240    11082   6893   8311  -1227   1846  -1789       C  
ATOM   1843  N   PHE A 241     140.207  66.778  46.005  1.00104.41           N  
ANISOU 1843  N   PHE A 241    15038  11070  13564   -836   1032   -906       N  
ATOM   1844  CA  PHE A 241     140.324  66.972  44.565  1.00109.09           C  
ANISOU 1844  CA  PHE A 241    15485  11600  14363   -774    959   -782       C  
ATOM   1845  C   PHE A 241     140.299  65.666  43.777  1.00 99.11           C  
ANISOU 1845  C   PHE A 241    14221  10393  13043   -727    908   -610       C  
ATOM   1846  O   PHE A 241     140.130  65.711  42.554  1.00 99.18           O  
ANISOU 1846  O   PHE A 241    14110  10362  13210   -682    874   -511       O  
ATOM   1847  CB  PHE A 241     141.613  67.738  44.258  1.00117.69           C  
ANISOU 1847  CB  PHE A 241    16531  12692  15495   -798    819   -782       C  
ATOM   1848  CG  PHE A 241     141.485  68.728  43.133  1.00136.51           C  
ANISOU 1848  CG  PHE A 241    18787  14945  18134   -782    803   -743       C  
ATOM   1849  CD1 PHE A 241     141.009  70.007  43.371  1.00147.56           C  
ANISOU 1849  CD1 PHE A 241    20184  16190  19692   -799    877   -870       C  
ATOM   1850  CD2 PHE A 241     141.856  68.385  41.842  1.00131.29           C  
ANISOU 1850  CD2 PHE A 241    18030  14309  17545   -745    713   -580       C  
ATOM   1851  CE1 PHE A 241     140.895  70.925  42.342  1.00143.03           C  
ANISOU 1851  CE1 PHE A 241    19531  15470  19345   -777    850   -813       C  
ATOM   1852  CE2 PHE A 241     141.743  69.298  40.808  1.00124.90           C  
ANISOU 1852  CE2 PHE A 241    17127  13382  16946   -742    694   -524       C  
ATOM   1853  CZ  PHE A 241     141.265  70.570  41.059  1.00126.65           C  
ANISOU 1853  CZ  PHE A 241    17365  13431  17325   -756    756   -630       C  
ATOM   1854  N   ALA A 242     140.458  64.516  44.434  1.00 83.80           N  
ANISOU 1854  N   ALA A 242    12434   8533  10875   -738    899   -571       N  
ATOM   1855  CA  ALA A 242     140.461  63.234  43.740  1.00 79.46           C  
ANISOU 1855  CA  ALA A 242    11927   8003  10261   -692    851   -421       C  
ATOM   1856  C   ALA A 242     139.065  62.744  43.375  1.00 87.42           C  
ANISOU 1856  C   ALA A 242    12914   8967  11336   -731    987   -397       C  
ATOM   1857  O   ALA A 242     138.947  61.713  42.705  1.00 79.49           O  
ANISOU 1857  O   ALA A 242    11948   7958  10295   -716    958   -284       O  
ATOM   1858  CB  ALA A 242     141.167  62.173  44.587  1.00 68.62           C  
ANISOU 1858  CB  ALA A 242    10761   6698   8614   -676    777   -379       C  
ATOM   1859  N   GLN A 243     138.015  63.440  43.798  1.00 98.66           N  
ANISOU 1859  N   GLN A 243    14269  10369  12849   -782   1134   -512       N  
ATOM   1860  CA  GLN A 243     136.656  63.081  43.411  1.00105.98           C  
ANISOU 1860  CA  GLN A 243    15117  11297  13853   -824   1263   -507       C  
ATOM   1861  C   GLN A 243     136.280  63.720  42.073  1.00105.70           C  
ANISOU 1861  C   GLN A 243    14866  11220  14076   -751   1226   -462       C  
ATOM   1862  O   GLN A 243     135.739  63.025  41.204  1.00 89.73           O  
ANISOU 1862  O   GLN A 243    12787   9217  12089   -762   1225   -373       O  
ATOM   1863  CB  GLN A 243     135.659  63.474  44.504  1.00111.59           C  
ANISOU 1863  CB  GLN A 243    15829  12044  14527   -899   1447   -665       C  
ATOM   1864  CG  GLN A 243     135.903  62.795  45.841  1.00111.93           C  
ANISOU 1864  CG  GLN A 243    16104  12142  14284   -997   1496   -699       C  
ATOM   1865  CD  GLN A 243     135.117  63.433  46.968  1.00112.22           C  
ANISOU 1865  CD  GLN A 243    16130  12231  14276  -1066   1677   -886       C  
ATOM   1866  OE1 GLN A 243     134.231  62.810  47.553  1.00111.05           O  
ANISOU 1866  OE1 GLN A 243    16039  12158  13996  -1186   1831   -919       O  
ATOM   1867  NE2 GLN A 243     135.442  64.683  47.282  1.00108.45           N  
ANISOU 1867  NE2 GLN A 243    15587  11716  13903  -1004   1669  -1020       N  
ATOM   1868  N   PRO A 244     136.533  65.020  41.854  1.00107.41           N  
ANISOU 1868  N   PRO A 244    14975  11373  14465   -685   1192   -516       N  
ATOM   1869  CA  PRO A 244     136.256  65.580  40.521  1.00102.86           C  
ANISOU 1869  CA  PRO A 244    14226  10747  14109   -611   1134   -438       C  
ATOM   1870  C   PRO A 244     137.117  64.981  39.426  1.00 87.93           C  
ANISOU 1870  C   PRO A 244    12338   8877  12195   -593    991   -280       C  
ATOM   1871  O   PRO A 244     136.653  64.862  38.286  1.00 88.27           O  
ANISOU 1871  O   PRO A 244    12267   8927  12345   -564    960   -190       O  
ATOM   1872  CB  PRO A 244     136.542  67.078  40.700  1.00101.52           C  
ANISOU 1872  CB  PRO A 244    14015  10468  14090   -561   1120   -526       C  
ATOM   1873  CG  PRO A 244     136.409  67.318  42.148  1.00100.92           C  
ANISOU 1873  CG  PRO A 244    14039  10401  13907   -606   1228   -696       C  
ATOM   1874  CD  PRO A 244     136.931  66.082  42.797  1.00 92.58           C  
ANISOU 1874  CD  PRO A 244    13137   9448  12590   -686   1215   -658       C  
ATOM   1875  N   VAL A 245     138.359  64.600  39.736  1.00 80.80           N  
ANISOU 1875  N   VAL A 245    11549   8005  11145   -602    900   -252       N  
ATOM   1876  CA  VAL A 245     139.238  64.021  38.723  1.00 83.05           C  
ANISOU 1876  CA  VAL A 245    11822   8334  11399   -567    774   -125       C  
ATOM   1877  C   VAL A 245     138.651  62.722  38.183  1.00 77.82           C  
ANISOU 1877  C   VAL A 245    11198   7703  10667   -574    793    -48       C  
ATOM   1878  O   VAL A 245     138.770  62.417  36.989  1.00 76.01           O  
ANISOU 1878  O   VAL A 245    10899   7495  10486   -545    729     46       O  
ATOM   1879  CB  VAL A 245     140.652  63.814  39.300  1.00 81.29           C  
ANISOU 1879  CB  VAL A 245    11694   8173  11020   -555    676   -135       C  
ATOM   1880  CG1 VAL A 245     141.518  63.034  38.328  1.00 92.45           C  
ANISOU 1880  CG1 VAL A 245    13091   9659  12377   -495    563    -25       C  
ATOM   1881  CG2 VAL A 245     141.293  65.158  39.615  1.00 67.64           C  
ANISOU 1881  CG2 VAL A 245     9909   6418   9371   -584    645   -210       C  
ATOM   1882  N   VAL A 246     138.001  61.939  39.048  1.00 81.73           N  
ANISOU 1882  N   VAL A 246    11817   8200  11035   -632    888    -90       N  
ATOM   1883  CA  VAL A 246     137.309  60.738  38.588  1.00 77.73           C  
ANISOU 1883  CA  VAL A 246    11367   7702  10464   -681    924    -31       C  
ATOM   1884  C   VAL A 246     136.177  61.109  37.637  1.00 84.46           C  
ANISOU 1884  C   VAL A 246    12024   8572  11494   -703    970    -21       C  
ATOM   1885  O   VAL A 246     135.924  60.415  36.645  1.00 92.41           O  
ANISOU 1885  O   VAL A 246    13006   9600  12506   -720    936     52       O  
ATOM   1886  CB  VAL A 246     136.803  59.919  39.791  1.00 75.70           C  
ANISOU 1886  CB  VAL A 246    11300   7439  10025   -779   1031    -77       C  
ATOM   1887  CG1 VAL A 246     135.938  58.756  39.331  1.00 70.48           C  
ANISOU 1887  CG1 VAL A 246    10702   6771   9308   -877   1089    -28       C  
ATOM   1888  CG2 VAL A 246     137.974  59.407  40.615  1.00 76.61           C  
ANISOU 1888  CG2 VAL A 246    11626   7541   9940   -731    949    -57       C  
ATOM   1889  N   THR A 247     135.492  62.221  37.912  1.00 89.23           N  
ANISOU 1889  N   THR A 247    12488   9173  12243   -690   1040   -101       N  
ATOM   1890  CA  THR A 247     134.404  62.664  37.047  1.00 92.10           C  
ANISOU 1890  CA  THR A 247    12646   9567  12780   -675   1065    -93       C  
ATOM   1891  C   THR A 247     134.926  63.434  35.838  1.00 96.09           C  
ANISOU 1891  C   THR A 247    13039  10042  13431   -582    936      1       C  
ATOM   1892  O   THR A 247     134.428  63.254  34.720  1.00 92.38           O  
ANISOU 1892  O   THR A 247    12456   9619  13027   -575    892     77       O  
ATOM   1893  CB  THR A 247     133.420  63.524  37.845  1.00 86.54           C  
ANISOU 1893  CB  THR A 247    11837   8871  12174   -664   1193   -227       C  
ATOM   1894  OG1 THR A 247     132.861  62.747  38.912  1.00 76.77           O  
ANISOU 1894  OG1 THR A 247    10698   7691  10777   -783   1330   -310       O  
ATOM   1895  CG2 THR A 247     132.295  64.031  36.954  1.00 89.60           C  
ANISOU 1895  CG2 THR A 247    11988   9308  12747   -606   1199   -219       C  
ATOM   1896  N   LEU A 248     135.938  64.282  36.040  1.00104.26           N  
ANISOU 1896  N   LEU A 248    14108  11009  14497   -532    874     -1       N  
ATOM   1897  CA  LEU A 248     136.431  65.133  34.961  1.00105.07           C  
ANISOU 1897  CA  LEU A 248    14120  11073  14728   -475    766     91       C  
ATOM   1898  C   LEU A 248     137.246  64.353  33.936  1.00106.06           C  
ANISOU 1898  C   LEU A 248    14267  11267  14765   -488    665    209       C  
ATOM   1899  O   LEU A 248     137.245  64.705  32.751  1.00108.63           O  
ANISOU 1899  O   LEU A 248    14496  11605  15171   -466    594    307       O  
ATOM   1900  CB  LEU A 248     137.268  66.275  35.541  1.00105.73           C  
ANISOU 1900  CB  LEU A 248    14248  11065  14862   -462    743     39       C  
ATOM   1901  CG  LEU A 248     137.942  67.250  34.575  1.00105.42           C  
ANISOU 1901  CG  LEU A 248    14156  10964  14934   -446    641    135       C  
ATOM   1902  CD1 LEU A 248     136.904  67.944  33.721  1.00101.94           C  
ANISOU 1902  CD1 LEU A 248    13597  10463  14673   -375    632    196       C  
ATOM   1903  CD2 LEU A 248     138.781  68.266  35.332  1.00103.08           C  
ANISOU 1903  CD2 LEU A 248    13932  10575  14660   -479    633     57       C  
ATOM   1904  N   ILE A 249     137.940  63.297  34.359  1.00108.59           N  
ANISOU 1904  N   ILE A 249    14718  11632  14910   -511    656    199       N  
ATOM   1905  CA  ILE A 249     138.882  62.577  33.511  1.00103.84           C  
ANISOU 1905  CA  ILE A 249    14144  11095  14214   -492    565    279       C  
ATOM   1906  C   ILE A 249     138.472  61.121  33.326  1.00 89.87           C  
ANISOU 1906  C   ILE A 249    12471   9354  12321   -514    587    291       C  
ATOM   1907  O   ILE A 249     138.418  60.618  32.199  1.00 97.84           O  
ANISOU 1907  O   ILE A 249    13442  10409  13322   -514    543    354       O  
ATOM   1908  CB  ILE A 249     140.320  62.673  34.064  1.00105.38           C  
ANISOU 1908  CB  ILE A 249    14406  11320  14313   -464    504    256       C  
ATOM   1909  CG1 ILE A 249     140.747  64.140  34.164  1.00100.04           C  
ANISOU 1909  CG1 ILE A 249    13649  10605  13758   -484    483    240       C  
ATOM   1910  CG2 ILE A 249     141.277  61.875  33.193  1.00103.31           C  
ANISOU 1910  CG2 ILE A 249    14150  11153  13951   -417    420    318       C  
ATOM   1911  CD1 ILE A 249     142.059  64.349  34.878  1.00 99.35           C  
ANISOU 1911  CD1 ILE A 249    13603  10569  13576   -490    430    188       C  
ATOM   1912  N   GLY A 250     138.183  60.424  34.425  1.00 87.88           N  
ANISOU 1912  N   GLY A 250    12366   9067  11959   -548    657    230       N  
ATOM   1913  CA  GLY A 250     137.829  59.016  34.323  1.00 91.67           C  
ANISOU 1913  CA  GLY A 250    12987   9534  12309   -592    681    244       C  
ATOM   1914  C   GLY A 250     136.522  58.785  33.589  1.00 81.24           C  
ANISOU 1914  C   GLY A 250    11569   8241  11060   -683    735    253       C  
ATOM   1915  O   GLY A 250     136.422  57.884  32.752  1.00 77.27           O  
ANISOU 1915  O   GLY A 250    11110   7749  10499   -712    706    289       O  
ATOM   1916  N   LEU A 251     135.502  59.589  33.895  1.00 86.10           N  
ANISOU 1916  N   LEU A 251    12042   8876  11796   -724    812    207       N  
ATOM   1917  CA  LEU A 251     134.204  59.437  33.243  1.00 92.53           C  
ANISOU 1917  CA  LEU A 251    12718   9758  12681   -803    855    204       C  
ATOM   1918  C   LEU A 251     134.279  59.775  31.759  1.00103.94           C  
ANISOU 1918  C   LEU A 251    14016  11260  14218   -753    748    289       C  
ATOM   1919  O   LEU A 251     133.535  59.199  30.955  1.00102.81           O  
ANISOU 1919  O   LEU A 251    13812  11188  14064   -827    741    305       O  
ATOM   1920  CB  LEU A 251     133.169  60.317  33.953  1.00 99.02           C  
ANISOU 1920  CB  LEU A 251    13395  10611  13619   -814    957    120       C  
ATOM   1921  CG  LEU A 251     131.693  60.348  33.531  1.00 94.76           C  
ANISOU 1921  CG  LEU A 251    12652  10185  13166   -880   1016     85       C  
ATOM   1922  CD1 LEU A 251     131.437  61.382  32.438  1.00 96.30           C  
ANISOU 1922  CD1 LEU A 251    12626  10421  13542   -761    918    146       C  
ATOM   1923  CD2 LEU A 251     131.207  58.968  33.106  1.00 97.28           C  
ANISOU 1923  CD2 LEU A 251    13046  10558  13357  -1042   1039     96       C  
ATOM   1924  N   GLY A 252     135.167  60.692  31.379  1.00111.32           N  
ANISOU 1924  N   GLY A 252    14899  12173  15223   -650    664    342       N  
ATOM   1925  CA  GLY A 252     135.331  61.079  29.993  1.00102.81           C  
ANISOU 1925  CA  GLY A 252    13703  11151  14207   -614    563    438       C  
ATOM   1926  C   GLY A 252     135.981  60.028  29.120  1.00 94.33           C  
ANISOU 1926  C   GLY A 252    12717  10124  13000   -634    505    480       C  
ATOM   1927  O   GLY A 252     135.393  59.620  28.114  1.00 92.44           O  
ANISOU 1927  O   GLY A 252    12414   9960  12750   -682    474    513       O  
ATOM   1928  N   ILE A 253     137.178  59.569  29.494  1.00 90.55           N  
ANISOU 1928  N   ILE A 253    12380   9612  12412   -589    486    467       N  
ATOM   1929  CA  ILE A 253     137.888  58.606  28.656  1.00 88.46           C  
ANISOU 1929  CA  ILE A 253    12196   9392  12024   -570    432    488       C  
ATOM   1930  C   ILE A 253     137.325  57.194  28.780  1.00 82.51           C  
ANISOU 1930  C   ILE A 253    11603   8595  11154   -639    478    439       C  
ATOM   1931  O   ILE A 253     137.589  56.353  27.909  1.00 80.18           O  
ANISOU 1931  O   ILE A 253    11370   8325  10768   -639    442    441       O  
ATOM   1932  CB  ILE A 253     139.391  58.601  28.979  1.00 88.03           C  
ANISOU 1932  CB  ILE A 253    12210   9345  11894   -470    387    481       C  
ATOM   1933  CG1 ILE A 253     139.694  57.625  30.111  1.00 97.50           C  
ANISOU 1933  CG1 ILE A 253    13617  10461  12969   -436    419    418       C  
ATOM   1934  CG2 ILE A 253     139.866  60.001  29.352  1.00 81.48           C  
ANISOU 1934  CG2 ILE A 253    11268   8520  11172   -450    370    501       C  
ATOM   1935  CD1 ILE A 253     141.115  57.152  30.112  1.00113.65           C  
ANISOU 1935  CD1 ILE A 253    15733  12546  14902   -308    351    406       C  
ATOM   1936  N   ALA A 254     136.568  56.903  29.841  1.00 84.90           N  
ANISOU 1936  N   ALA A 254    11987   8827  11443   -713    565    387       N  
ATOM   1937  CA  ALA A 254     135.896  55.611  29.925  1.00 85.19           C  
ANISOU 1937  CA  ALA A 254    12187   8811  11370   -830    619    349       C  
ATOM   1938  C   ALA A 254     134.826  55.488  28.852  1.00 83.38           C  
ANISOU 1938  C   ALA A 254    11819   8677  11186   -946    616    353       C  
ATOM   1939  O   ALA A 254     134.663  54.422  28.249  1.00 83.91           O  
ANISOU 1939  O   ALA A 254    12002   8727  11153  -1025    610    332       O  
ATOM   1940  CB  ALA A 254     135.283  55.414  31.310  1.00 72.88           C  
ANISOU 1940  CB  ALA A 254    10736   7181   9775   -917    727    299       C  
ATOM   1941  N   ILE A 255     134.085  56.570  28.607  1.00 90.06           N  
ANISOU 1941  N   ILE A 255    12421   9621  12177   -952    614    373       N  
ATOM   1942  CA  ILE A 255     133.126  56.580  27.509  1.00101.33           C  
ANISOU 1942  CA  ILE A 255    13679  11174  13646  -1035    580    388       C  
ATOM   1943  C   ILE A 255     133.854  56.547  26.173  1.00102.22           C  
ANISOU 1943  C   ILE A 255    13772  11345  13721   -975    471    452       C  
ATOM   1944  O   ILE A 255     133.377  55.931  25.211  1.00102.11           O  
ANISOU 1944  O   ILE A 255    13739  11412  13647  -1067    438    444       O  
ATOM   1945  CB  ILE A 255     132.201  57.804  27.634  1.00 94.23           C  
ANISOU 1945  CB  ILE A 255    12526  10361  12917  -1006    589    399       C  
ATOM   1946  CG1 ILE A 255     131.404  57.725  28.937  1.00 90.16           C  
ANISOU 1946  CG1 ILE A 255    12018   9822  12415  -1083    721    308       C  
ATOM   1947  CG2 ILE A 255     131.264  57.898  26.446  1.00 99.98           C  
ANISOU 1947  CG2 ILE A 255    13055  11248  13684  -1060    522    429       C  
ATOM   1948  CD1 ILE A 255     130.536  58.931  29.198  1.00 86.66           C  
ANISOU 1948  CD1 ILE A 255    11329   9456  12142  -1016    744    289       C  
ATOM   1949  N   ASP A 256     135.019  57.193  26.091  1.00 91.41           N  
ANISOU 1949  N   ASP A 256    12406   9954  12372   -840    419    505       N  
ATOM   1950  CA  ASP A 256     135.852  57.072  24.899  1.00 84.22           C  
ANISOU 1950  CA  ASP A 256    11493   9115  11393   -794    337    553       C  
ATOM   1951  C   ASP A 256     136.262  55.622  24.667  1.00 93.06           C  
ANISOU 1951  C   ASP A 256    12817  10193  12350   -819    350    483       C  
ATOM   1952  O   ASP A 256     136.185  55.116  23.543  1.00 88.34           O  
ANISOU 1952  O   ASP A 256    12216   9674  11676   -864    310    478       O  
ATOM   1953  CB  ASP A 256     137.088  57.965  25.024  1.00 70.15           C  
ANISOU 1953  CB  ASP A 256     9680   7327   9646   -675    301    605       C  
ATOM   1954  CG  ASP A 256     136.763  59.437  24.872  1.00 75.04           C  
ANISOU 1954  CG  ASP A 256    10122   7971  10418   -654    267    689       C  
ATOM   1955  OD1 ASP A 256     135.565  59.776  24.776  1.00 71.05           O  
ANISOU 1955  OD1 ASP A 256     9507   7488  10002   -694    269    702       O  
ATOM   1956  OD2 ASP A 256     137.709  60.253  24.841  1.00 68.15           O  
ANISOU 1956  OD2 ASP A 256     9223   7096   9576   -598    236    740       O  
ATOM   1957  N   TYR A 257     136.696  54.936  25.728  1.00 85.25           N  
ANISOU 1957  N   TYR A 257    12026   9069  11298   -784    401    427       N  
ATOM   1958  CA  TYR A 257     137.096  53.540  25.591  1.00 76.50           C  
ANISOU 1958  CA  TYR A 257    11155   7872  10039   -779    408    363       C  
ATOM   1959  C   TYR A 257     135.920  52.673  25.164  1.00 90.80           C  
ANISOU 1959  C   TYR A 257    13029   9669  11800   -967    443    314       C  
ATOM   1960  O   TYR A 257     136.056  51.818  24.280  1.00 92.99           O  
ANISOU 1960  O   TYR A 257    13409   9947  11977   -993    417    269       O  
ATOM   1961  CB  TYR A 257     137.692  53.031  26.903  1.00 77.50           C  
ANISOU 1961  CB  TYR A 257    11497   7844  10105   -698    443    334       C  
ATOM   1962  CG  TYR A 257     139.055  53.604  27.224  1.00 88.40           C  
ANISOU 1962  CG  TYR A 257    12839   9260  11491   -510    392    356       C  
ATOM   1963  CD1 TYR A 257     139.722  54.419  26.317  1.00 77.34           C  
ANISOU 1963  CD1 TYR A 257    11240   8010  10135   -445    335    395       C  
ATOM   1964  CD2 TYR A 257     139.681  53.318  28.432  1.00 91.88           C  
ANISOU 1964  CD2 TYR A 257    13438   9598  11873   -414    397    340       C  
ATOM   1965  CE1 TYR A 257     140.970  54.941  26.607  1.00 84.37           C  
ANISOU 1965  CE1 TYR A 257    12075   8960  11023   -309    295    404       C  
ATOM   1966  CE2 TYR A 257     140.930  53.834  28.731  1.00 82.80           C  
ANISOU 1966  CE2 TYR A 257    12226   8515  10720   -255    341    347       C  
ATOM   1967  CZ  TYR A 257     141.570  54.643  27.815  1.00 82.27           C  
ANISOU 1967  CZ  TYR A 257    11943   8609  10706   -213    294    373       C  
ATOM   1968  OH  TYR A 257     142.811  55.158  28.109  1.00 70.91           O  
ANISOU 1968  OH  TYR A 257    10423   7263   9256    -89    245    370       O  
ATOM   1969  N   GLY A 258     134.754  52.883  25.774  1.00 97.93           N  
ANISOU 1969  N   GLY A 258    13866  10576  12768  -1109    505    307       N  
ATOM   1970  CA  GLY A 258     133.562  52.163  25.369  1.00102.82           C  
ANISOU 1970  CA  GLY A 258    14495  11227  13344  -1323    540    255       C  
ATOM   1971  C   GLY A 258     133.025  52.561  24.013  1.00 97.08           C  
ANISOU 1971  C   GLY A 258    13542  10693  12649  -1377    465    276       C  
ATOM   1972  O   GLY A 258     132.109  51.903  23.508  1.00 83.77           O  
ANISOU 1972  O   GLY A 258    11855   9065  10909  -1564    474    220       O  
ATOM   1973  N   LEU A 259     133.575  53.618  23.416  1.00100.23           N  
ANISOU 1973  N   LEU A 259    13762  11197  13123  -1233    387    358       N  
ATOM   1974  CA  LEU A 259     133.118  54.076  22.110  1.00 99.20           C  
ANISOU 1974  CA  LEU A 259    13430  11254  13006  -1270    300    404       C  
ATOM   1975  C   LEU A 259     133.776  53.277  20.990  1.00 99.53           C  
ANISOU 1975  C   LEU A 259    13592  11326  12897  -1274    253    370       C  
ATOM   1976  O   LEU A 259     133.109  52.856  20.039  1.00 94.25           O  
ANISOU 1976  O   LEU A 259    12879  10773  12158  -1406    213    338       O  
ATOM   1977  CB  LEU A 259     133.408  55.574  21.966  1.00 96.02           C  
ANISOU 1977  CB  LEU A 259    12823  10926  12736  -1130    239    521       C  
ATOM   1978  CG  LEU A 259     132.888  56.358  20.760  1.00105.82           C  
ANISOU 1978  CG  LEU A 259    13845  12350  14012  -1137    133    613       C  
ATOM   1979  CD1 LEU A 259     132.624  57.795  21.171  1.00 95.68           C  
ANISOU 1979  CD1 LEU A 259    12385  11064  12903  -1028    108    707       C  
ATOM   1980  CD2 LEU A 259     133.888  56.320  19.618  1.00119.93           C  
ANISOU 1980  CD2 LEU A 259    15674  14208  15688  -1091     66    661       C  
ATOM   1981  N   PHE A 260     135.090  53.060  21.090  1.00 99.33           N  
ANISOU 1981  N   PHE A 260    13709  11217  12815  -1127    257    362       N  
ATOM   1982  CA  PHE A 260     135.798  52.282  20.081  1.00 79.96           C  
ANISOU 1982  CA  PHE A 260    11371   8796  10216  -1101    228    304       C  
ATOM   1983  C   PHE A 260     135.399  50.812  20.093  1.00 80.26           C  
ANISOU 1983  C   PHE A 260    11657   8705  10134  -1220    273    176       C  
ATOM   1984  O   PHE A 260     135.544  50.136  19.069  1.00 77.31           O  
ANISOU 1984  O   PHE A 260    11358   8379   9637  -1259    247    104       O  
ATOM   1985  CB  PHE A 260     137.309  52.417  20.281  1.00 80.76           C  
ANISOU 1985  CB  PHE A 260    11534   8863  10291   -896    228    310       C  
ATOM   1986  CG  PHE A 260     137.827  53.806  20.049  1.00 86.49           C  
ANISOU 1986  CG  PHE A 260    12039   9721  11103   -817    185    429       C  
ATOM   1987  CD1 PHE A 260     137.799  54.749  21.061  1.00 97.25           C  
ANISOU 1987  CD1 PHE A 260    13320  11026  12604   -774    199    496       C  
ATOM   1988  CD2 PHE A 260     138.336  54.172  18.815  1.00101.14           C  
ANISOU 1988  CD2 PHE A 260    13788  11751  12888   -805    136    469       C  
ATOM   1989  CE1 PHE A 260     138.270  56.032  20.851  1.00106.34           C  
ANISOU 1989  CE1 PHE A 260    14304  12265  13835   -723    160    602       C  
ATOM   1990  CE2 PHE A 260     138.811  55.452  18.598  1.00102.27           C  
ANISOU 1990  CE2 PHE A 260    13761  11996  13101   -765    100    590       C  
ATOM   1991  CZ  PHE A 260     138.775  56.383  19.618  1.00 99.11           C  
ANISOU 1991  CZ  PHE A 260    13298  11509  12851   -726    110    657       C  
ATOM   1992  N   ILE A 261     134.893  50.307  21.218  1.00 87.50           N  
ANISOU 1992  N   ILE A 261    12719   9453  11073  -1296    342    142       N  
ATOM   1993  CA  ILE A 261     134.465  48.914  21.287  1.00 90.07           C  
ANISOU 1993  CA  ILE A 261    13319   9621  11283  -1445    390     30       C  
ATOM   1994  C   ILE A 261     133.141  48.721  20.561  1.00 91.06           C  
ANISOU 1994  C   ILE A 261    13330   9883  11386  -1708    380    -11       C  
ATOM   1995  O   ILE A 261     132.967  47.764  19.799  1.00 93.84           O  
ANISOU 1995  O   ILE A 261    13832  10210  11614  -1830    372   -111       O  
ATOM   1996  CB  ILE A 261     134.374  48.455  22.755  1.00 88.26           C  
ANISOU 1996  CB  ILE A 261    13303   9169  11062  -1463    472     25       C  
ATOM   1997  CG1 ILE A 261     135.699  48.697  23.481  1.00 94.03           C  
ANISOU 1997  CG1 ILE A 261    14120   9800  11806  -1193    459     67       C  
ATOM   1998  CG2 ILE A 261     133.982  46.987  22.831  1.00 80.49           C  
ANISOU 1998  CG2 ILE A 261    12655   7979   9947  -1633    522    -77       C  
ATOM   1999  CD1 ILE A 261     136.861  47.946  22.891  1.00 93.77           C  
ANISOU 1999  CD1 ILE A 261    14269   9694  11663  -1010    419      5       C  
ATOM   2000  N   VAL A 262     132.189  49.628  20.785  1.00 94.52           N  
ANISOU 2000  N   VAL A 262    13495  10476  11942  -1792    375     53       N  
ATOM   2001  CA  VAL A 262     130.872  49.492  20.171  1.00100.05           C  
ANISOU 2001  CA  VAL A 262    14040  11350  12626  -2036    355     11       C  
ATOM   2002  C   VAL A 262     130.934  49.821  18.683  1.00 98.01           C  
ANISOU 2002  C   VAL A 262    13619  11307  12314  -2019    241     31       C  
ATOM   2003  O   VAL A 262     130.262  49.182  17.864  1.00 89.44           O  
ANISOU 2003  O   VAL A 262    12537  10322  11124  -2217    210    -51       O  
ATOM   2004  CB  VAL A 262     129.848  50.373  20.911  1.00 96.40           C  
ANISOU 2004  CB  VAL A 262    13314  11005  12308  -2091    385     62       C  
ATOM   2005  CG1 VAL A 262     128.503  50.348  20.204  1.00 90.93           C  
ANISOU 2005  CG1 VAL A 262    12392  10554  11605  -2312    343     19       C  
ATOM   2006  CG2 VAL A 262     129.699  49.908  22.354  1.00102.84           C  
ANISOU 2006  CG2 VAL A 262    14313  11628  13135  -2159    514     25       C  
ATOM   2007  N   SER A 263     131.742  50.815  18.308  1.00102.28           N  
ANISOU 2007  N   SER A 263    14027  11926  12908  -1805    178    139       N  
ATOM   2008  CA  SER A 263     131.861  51.175  16.897  1.00101.88           C  
ANISOU 2008  CA  SER A 263    13842  12086  12784  -1794     72    178       C  
ATOM   2009  C   SER A 263     132.499  50.047  16.096  1.00100.39           C  
ANISOU 2009  C   SER A 263    13887  11849  12409  -1828     79     57       C  
ATOM   2010  O   SER A 263     132.002  49.674  15.028  1.00102.97           O  
ANISOU 2010  O   SER A 263    14179  12327  12617  -1974     21      1       O  
ATOM   2011  CB  SER A 263     132.673  52.461  16.746  1.00 93.77           C  
ANISOU 2011  CB  SER A 263    12664  11125  11841  -1582     21    327       C  
ATOM   2012  OG  SER A 263     134.051  52.218  16.965  1.00 96.53           O  
ANISOU 2012  OG  SER A 263    13185  11346  12145  -1425     66    306       O  
ATOM   2013  N   ARG A 264     133.608  49.494  16.597  1.00 97.10           N  
ANISOU 2013  N   ARG A 264    13706  11228  11959  -1682    143      6       N  
ATOM   2014  CA  ARG A 264     134.257  48.387  15.904  1.00 92.47           C  
ANISOU 2014  CA  ARG A 264    13359  10571  11204  -1671    158   -131       C  
ATOM   2015  C   ARG A 264     133.349  47.169  15.834  1.00 94.13           C  
ANISOU 2015  C   ARG A 264    13768  10676  11321  -1918    190   -274       C  
ATOM   2016  O   ARG A 264     133.440  46.379  14.887  1.00 96.06           O  
ANISOU 2016  O   ARG A 264    14146  10940  11414  -1994    176   -398       O  
ATOM   2017  CB  ARG A 264     135.572  48.031  16.596  1.00 87.75           C  
ANISOU 2017  CB  ARG A 264    12964   9772  10604  -1433    213   -160       C  
ATOM   2018  CG  ARG A 264     136.499  47.154  15.772  1.00 89.71           C  
ANISOU 2018  CG  ARG A 264    13401   9993  10694  -1329    221   -294       C  
ATOM   2019  CD  ARG A 264     136.709  47.740  14.384  1.00 93.51           C  
ANISOU 2019  CD  ARG A 264    13676  10766  11089  -1338    162   -271       C  
ATOM   2020  NE  ARG A 264     138.069  47.529  13.896  1.00 96.47           N  
ANISOU 2020  NE  ARG A 264    14109  11179  11366  -1125    184   -340       N  
ATOM   2021  CZ  ARG A 264     138.481  46.423  13.286  1.00113.27           C  
ANISOU 2021  CZ  ARG A 264    16454  13243  13341  -1089    215   -521       C  
ATOM   2022  NH1 ARG A 264     137.642  45.418  13.088  1.00122.44           N  
ANISOU 2022  NH1 ARG A 264    17823  14272  14428  -1276    223   -646       N  
ATOM   2023  NH2 ARG A 264     139.733  46.321  12.876  1.00112.26           N  
ANISOU 2023  NH2 ARG A 264    16332  13188  13132   -872    242   -590       N  
ATOM   2024  N   PHE A 265     132.467  47.002  16.821  1.00 98.28           N  
ANISOU 2024  N   PHE A 265    14320  11096  11925  -2066    242   -269       N  
ATOM   2025  CA  PHE A 265     131.538  45.878  16.805  1.00 97.95           C  
ANISOU 2025  CA  PHE A 265    14463  10961  11793  -2355    282   -400       C  
ATOM   2026  C   PHE A 265     130.495  46.045  15.708  1.00104.61           C  
ANISOU 2026  C   PHE A 265    15074  12093  12578  -2583    203   -431       C  
ATOM   2027  O   PHE A 265     130.202  45.100  14.967  1.00112.02           O  
ANISOU 2027  O   PHE A 265    16171  13023  13370  -2773    195   -573       O  
ATOM   2028  CB  PHE A 265     130.874  45.732  18.173  1.00 88.27           C  
ANISOU 2028  CB  PHE A 265    13302   9584  10654  -2475    371   -378       C  
ATOM   2029  CG  PHE A 265     129.842  44.648  18.230  1.00 94.64           C  
ANISOU 2029  CG  PHE A 265    14283  10309  11368  -2823    425   -502       C  
ATOM   2030  CD1 PHE A 265     130.216  43.316  18.177  1.00 94.79           C  
ANISOU 2030  CD1 PHE A 265    14721  10043  11252  -2892    471   -628       C  
ATOM   2031  CD2 PHE A 265     128.498  44.960  18.344  1.00 93.99           C  
ANISOU 2031  CD2 PHE A 265    13946  10435  11333  -3084    433   -500       C  
ATOM   2032  CE1 PHE A 265     129.267  42.315  18.231  1.00 92.83           C  
ANISOU 2032  CE1 PHE A 265    14662   9698  10912  -3252    526   -744       C  
ATOM   2033  CE2 PHE A 265     127.544  43.963  18.400  1.00 96.22           C  
ANISOU 2033  CE2 PHE A 265    14373  10667  11520  -3446    491   -623       C  
ATOM   2034  CZ  PHE A 265     127.929  42.638  18.343  1.00 92.39           C  
ANISOU 2034  CZ  PHE A 265    14333   9875  10894  -3549    540   -742       C  
ATOM   2035  N   ARG A 266     129.923  47.246  15.588  1.00104.44           N  
ANISOU 2035  N   ARG A 266    14686  12328  12666  -2561    134   -304       N  
ATOM   2036  CA  ARG A 266     128.985  47.512  14.502  1.00107.10           C  
ANISOU 2036  CA  ARG A 266    14775  12975  12944  -2733     29   -312       C  
ATOM   2037  C   ARG A 266     129.666  47.430  13.142  1.00 99.26           C  
ANISOU 2037  C   ARG A 266    13815  12102  11797  -2668    -51   -338       C  
ATOM   2038  O   ARG A 266     129.036  47.032  12.155  1.00 92.35           O  
ANISOU 2038  O   ARG A 266    12894  11409  10785  -2868   -120   -423       O  
ATOM   2039  CB  ARG A 266     128.342  48.885  14.690  1.00101.99           C  
ANISOU 2039  CB  ARG A 266    13745  12551  12456  -2653    -40   -155       C  
ATOM   2040  CG  ARG A 266     127.374  48.974  15.857  1.00 96.03           C  
ANISOU 2040  CG  ARG A 266    12887  11769  11830  -2767     36   -162       C  
ATOM   2041  CD  ARG A 266     127.091  50.426  16.195  1.00108.40           C  
ANISOU 2041  CD  ARG A 266    14127  13480  13578  -2580    -16     -7       C  
ATOM   2042  NE  ARG A 266     126.767  51.207  15.004  1.00125.02           N  
ANISOU 2042  NE  ARG A 266    15970  15870  15663  -2529   -176     82       N  
ATOM   2043  CZ  ARG A 266     125.546  51.631  14.696  1.00133.56           C  
ANISOU 2043  CZ  ARG A 266    16744  17222  16782  -2623   -263     95       C  
ATOM   2044  NH1 ARG A 266     124.526  51.361  15.497  1.00136.63           N  
ANISOU 2044  NH1 ARG A 266    17023  17655  17235  -2787   -187     10       N  
ATOM   2045  NH2 ARG A 266     125.346  52.335  13.590  1.00131.66           N  
ANISOU 2045  NH2 ARG A 266    16298  17224  16503  -2551   -427    196       N  
ATOM   2046  N   GLU A 267     130.948  47.799  13.072  1.00 96.26           N  
ANISOU 2046  N   GLU A 267    13504  11648  11423  -2403    -40   -276       N  
ATOM   2047  CA  GLU A 267     131.677  47.722  11.811  1.00 95.56           C  
ANISOU 2047  CA  GLU A 267    13445  11691  11172  -2340    -92   -309       C  
ATOM   2048  C   GLU A 267     131.823  46.279  11.346  1.00101.82           C  
ANISOU 2048  C   GLU A 267    14551  12350  11786  -2469    -43   -530       C  
ATOM   2049  O   GLU A 267     131.665  45.985  10.156  1.00106.26           O  
ANISOU 2049  O   GLU A 267    15105  13091  12177  -2586   -102   -614       O  
ATOM   2050  CB  GLU A 267     133.049  48.381  11.961  1.00 96.19           C  
ANISOU 2050  CB  GLU A 267    13524  11726  11298  -2048    -67   -212       C  
ATOM   2051  CG  GLU A 267     133.774  48.629  10.650  1.00116.57           C  
ANISOU 2051  CG  GLU A 267    16055  14517  13721  -1984   -118   -206       C  
ATOM   2052  CD  GLU A 267     135.180  49.160  10.853  1.00115.60           C  
ANISOU 2052  CD  GLU A 267    15934  14358  13631  -1726    -72   -138       C  
ATOM   2053  OE1 GLU A 267     136.146  48.426  10.553  1.00115.97           O  
ANISOU 2053  OE1 GLU A 267    16160  14344  13560  -1624    -10   -272       O  
ATOM   2054  OE2 GLU A 267     135.321  50.310  11.321  1.00110.84           O  
ANISOU 2054  OE2 GLU A 267    15150  13792  13172  -1627    -96     39       O  
ATOM   2055  N   GLU A 268     132.120  45.364  12.272  1.00 97.81           N  
ANISOU 2055  N   GLU A 268    14341  11518  11304  -2450     60   -628       N  
ATOM   2056  CA  GLU A 268     132.242  43.957  11.908  1.00100.16           C  
ANISOU 2056  CA  GLU A 268    14987  11627  11443  -2563    109   -843       C  
ATOM   2057  C   GLU A 268     130.889  43.345  11.574  1.00105.44           C  
ANISOU 2057  C   GLU A 268    15664  12364  12033  -2942     85   -950       C  
ATOM   2058  O   GLU A 268     130.818  42.399  10.780  1.00100.30           O  
ANISOU 2058  O   GLU A 268    15219  11679  11211  -3093     85  -1132       O  
ATOM   2059  CB  GLU A 268     132.915  43.179  13.039  1.00 99.46           C  
ANISOU 2059  CB  GLU A 268    15238  11147  11404  -2422    211   -892       C  
ATOM   2060  CG  GLU A 268     134.308  43.676  13.378  1.00 89.36           C  
ANISOU 2060  CG  GLU A 268    13948   9818  10186  -2049    229   -814       C  
ATOM   2061  CD  GLU A 268     135.249  43.606  12.195  1.00 95.70           C  
ANISOU 2061  CD  GLU A 268    14748  10766  10849  -1896    209   -900       C  
ATOM   2062  OE1 GLU A 268     135.302  42.545  11.538  1.00102.56           O  
ANISOU 2062  OE1 GLU A 268    15864  11539  11563  -1967    230  -1093       O  
ATOM   2063  OE2 GLU A 268     135.927  44.616  11.912  1.00 94.90           O  
ANISOU 2063  OE2 GLU A 268    14402  10875  10782  -1720    179   -782       O  
ATOM   2064  N   ILE A 269     129.811  43.863  12.167  1.00108.17           N  
ANISOU 2064  N   ILE A 269    15783  12819  12498  -3103     69   -856       N  
ATOM   2065  CA  ILE A 269     128.475  43.371  11.842  1.00113.86           C  
ANISOU 2065  CA  ILE A 269    16444  13673  13145  -3481     40   -958       C  
ATOM   2066  C   ILE A 269     128.101  43.745  10.413  1.00111.89           C  
ANISOU 2066  C   ILE A 269    15956  13793  12764  -3571    -95   -973       C  
ATOM   2067  O   ILE A 269     127.564  42.923   9.661  1.00114.24           O  
ANISOU 2067  O   ILE A 269    16356  14155  12894  -3843   -122  -1142       O  
ATOM   2068  CB  ILE A 269     127.447  43.908  12.854  1.00109.54           C  
ANISOU 2068  CB  ILE A 269    15663  13196  12760  -3602     63   -859       C  
ATOM   2069  CG1 ILE A 269     127.695  43.311  14.240  1.00106.62           C  
ANISOU 2069  CG1 ILE A 269    15589  12455  12466  -3593    205   -871       C  
ATOM   2070  CG2 ILE A 269     126.031  43.613  12.386  1.00113.98           C  
ANISOU 2070  CG2 ILE A 269    16050  14009  13248  -3985     12   -954       C  
ATOM   2071  CD1 ILE A 269     127.548  41.808  14.296  1.00102.57           C  
ANISOU 2071  CD1 ILE A 269    15500  11658  11813  -3850    284  -1059       C  
ATOM   2072  N   ALA A 270     128.380  44.989  10.014  1.00107.05           N  
ANISOU 2072  N   ALA A 270    15041  13423  12210  -3356   -187   -794       N  
ATOM   2073  CA  ALA A 270     128.074  45.419   8.655  1.00106.12           C  
ANISOU 2073  CA  ALA A 270    14709  13662  11949  -3421   -328   -775       C  
ATOM   2074  C   ALA A 270     128.901  44.665   7.622  1.00108.07           C  
ANISOU 2074  C   ALA A 270    15207  13880  11975  -3412   -317   -929       C  
ATOM   2075  O   ALA A 270     128.441  44.461   6.493  1.00101.59           O  
ANISOU 2075  O   ALA A 270    14325  13308  10968  -3595   -411  -1012       O  
ATOM   2076  CB  ALA A 270     128.302  46.923   8.515  1.00100.03           C  
ANISOU 2076  CB  ALA A 270    13620  13099  11287  -3177   -421   -529       C  
ATOM   2077  N   GLU A 271     130.119  44.247   7.980  1.00108.59           N  
ANISOU 2077  N   GLU A 271    15545  13665  12048  -3192   -207   -980       N  
ATOM   2078  CA  GLU A 271     130.928  43.464   7.052  1.00103.75           C  
ANISOU 2078  CA  GLU A 271    15177  13015  11229  -3157   -177  -1159       C  
ATOM   2079  C   GLU A 271     130.389  42.050   6.877  1.00110.99           C  
ANISOU 2079  C   GLU A 271    16403  13757  12011  -3439   -134  -1416       C  
ATOM   2080  O   GLU A 271     130.785  41.360   5.930  1.00122.24           O  
ANISOU 2080  O   GLU A 271    18015  15197  13235  -3476   -127  -1600       O  
ATOM   2081  CB  GLU A 271     132.385  43.416   7.521  1.00 98.40           C  
ANISOU 2081  CB  GLU A 271    14675  12107  10604  -2815    -76  -1153       C  
ATOM   2082  CG  GLU A 271     133.094  44.759   7.500  1.00111.01           C  
ANISOU 2082  CG  GLU A 271    15999  13890  12291  -2562   -111   -929       C  
ATOM   2083  CD  GLU A 271     134.551  44.653   7.914  1.00120.05           C  
ANISOU 2083  CD  GLU A 271    17291  14854  13469  -2247    -13   -950       C  
ATOM   2084  OE1 GLU A 271     135.116  43.543   7.818  1.00122.52           O  
ANISOU 2084  OE1 GLU A 271    17905  14966  13682  -2190     64  -1156       O  
ATOM   2085  OE2 GLU A 271     135.130  45.676   8.343  1.00119.23           O  
ANISOU 2085  OE2 GLU A 271    17003  14809  13492  -2053    -16   -768       O  
ATOM   2086  N   GLY A 272     129.506  41.609   7.761  1.00103.59           N  
ANISOU 2086  N   GLY A 272    15534  12656  11172  -3652    -97  -1441       N  
ATOM   2087  CA  GLY A 272     128.864  40.323   7.650  1.00106.58           C  
ANISOU 2087  CA  GLY A 272    16202  12865  11428  -3981    -57  -1670       C  
ATOM   2088  C   GLY A 272     129.327  39.248   8.619  1.00106.33           C  
ANISOU 2088  C   GLY A 272    16623  12338  11442  -3943     80  -1778       C  
ATOM   2089  O   GLY A 272     129.066  38.065   8.363  1.00 99.76           O  
ANISOU 2089  O   GLY A 272    16127  11301  10476  -4179    122  -1995       O  
ATOM   2090  N   TYR A 273     129.997  39.612   9.709  1.00110.55           N  
ANISOU 2090  N   TYR A 273    17192  12665  12148  -3662    144  -1634       N  
ATOM   2091  CA  TYR A 273     130.464  38.635  10.682  1.00110.95           C  
ANISOU 2091  CA  TYR A 273    17679  12243  12234  -3594    256  -1705       C  
ATOM   2092  C   TYR A 273     129.391  38.368  11.731  1.00115.31           C  
ANISOU 2092  C   TYR A 273    18277  12664  12873  -3896    308  -1665       C  
ATOM   2093  O   TYR A 273     128.579  39.240  12.054  1.00104.90           O  
ANISOU 2093  O   TYR A 273    16588  11609  11659  -4007    272  -1526       O  
ATOM   2094  CB  TYR A 273     131.748  39.115  11.363  1.00107.50           C  
ANISOU 2094  CB  TYR A 273    17261  11667  11917  -3145    291  -1577       C  
ATOM   2095  CG  TYR A 273     132.927  39.232  10.424  1.00112.73           C  
ANISOU 2095  CG  TYR A 273    17917  12431  12483  -2847    271  -1642       C  
ATOM   2096  CD1 TYR A 273     133.744  38.138  10.167  1.00114.08           C  
ANISOU 2096  CD1 TYR A 273    18484  12319  12542  -2702    328  -1841       C  
ATOM   2097  CD2 TYR A 273     133.220  40.433   9.793  1.00112.33           C  
ANISOU 2097  CD2 TYR A 273    17471  12761  12448  -2711    202  -1508       C  
ATOM   2098  CE1 TYR A 273     134.820  38.236   9.305  1.00114.47           C  
ANISOU 2098  CE1 TYR A 273    18501  12499  12495  -2429    326  -1922       C  
ATOM   2099  CE2 TYR A 273     134.296  40.541   8.929  1.00116.82           C  
ANISOU 2099  CE2 TYR A 273    18025  13453  12910  -2472    201  -1570       C  
ATOM   2100  CZ  TYR A 273     135.092  39.440   8.689  1.00117.37           C  
ANISOU 2100  CZ  TYR A 273    18456  13273  12865  -2331    269  -1786       C  
ATOM   2101  OH  TYR A 273     136.164  39.542   7.832  1.00108.17           O  
ANISOU 2101  OH  TYR A 273    17249  12264  11585  -2090    284  -1868       O  
ATOM   2102  N   ASP A 274     129.389  37.144  12.257  1.00128.05           N  
ANISOU 2102  N   ASP A 274    20358  13862  14431  -4029    396  -1792       N  
ATOM   2103  CA  ASP A 274     128.451  36.795  13.311  1.00132.41           C  
ANISOU 2103  CA  ASP A 274    21009  14260  15041  -4336    468  -1756       C  
ATOM   2104  C   ASP A 274     128.891  37.412  14.638  1.00134.25           C  
ANISOU 2104  C   ASP A 274    21190  14373  15447  -4075    517  -1550       C  
ATOM   2105  O   ASP A 274     129.967  38.005  14.754  1.00132.40           O  
ANISOU 2105  O   ASP A 274    20882  14138  15285  -3662    493  -1451       O  
ATOM   2106  CB  ASP A 274     128.306  35.276  13.435  1.00140.02           C  
ANISOU 2106  CB  ASP A 274    22537  14790  15875  -4590    547  -1945       C  
ATOM   2107  CG  ASP A 274     129.632  34.572  13.632  1.00142.58           C  
ANISOU 2107  CG  ASP A 274    23317  14684  16174  -4217    583  -1998       C  
ATOM   2108  OD1 ASP A 274     130.619  34.964  12.977  1.00142.07           O  
ANISOU 2108  OD1 ASP A 274    23144  14736  16101  -3851    533  -2009       O  
ATOM   2109  OD2 ASP A 274     129.685  33.620  14.440  1.00143.71           O  
ANISOU 2109  OD2 ASP A 274    23927  14379  16296  -4289    661  -2027       O  
ATOM   2110  N   THR A 275     128.034  37.260  15.652  1.00134.29           N  
ANISOU 2110  N   THR A 275    21228  14292  15502  -4343    592  -1496       N  
ATOM   2111  CA  THR A 275     128.220  37.992  16.903  1.00124.14           C  
ANISOU 2111  CA  THR A 275    19817  12979  14371  -4155    637  -1303       C  
ATOM   2112  C   THR A 275     129.520  37.605  17.600  1.00122.37           C  
ANISOU 2112  C   THR A 275    19966  12365  14162  -3783    668  -1255       C  
ATOM   2113  O   THR A 275     130.261  38.476  18.072  1.00113.52           O  
ANISOU 2113  O   THR A 275    18661  11316  13155  -3437    645  -1113       O  
ATOM   2114  CB  THR A 275     127.024  37.760  17.828  1.00113.65           C  
ANISOU 2114  CB  THR A 275    18489  11635  13058  -4553    731  -1283       C  
ATOM   2115  OG1 THR A 275     125.827  38.220  17.187  1.00100.36           O  
ANISOU 2115  OG1 THR A 275    16386  10373  11371  -4861    688  -1328       O  
ATOM   2116  CG2 THR A 275     127.209  38.513  19.135  1.00116.63           C  
ANISOU 2116  CG2 THR A 275    18747  11992  13575  -4365    786  -1101       C  
ATOM   2117  N   GLU A 276     129.818  36.305  17.676  1.00127.67           N  
ANISOU 2117  N   GLU A 276    21169  12623  14717  -3842    714  -1376       N  
ATOM   2118  CA  GLU A 276     131.038  35.870  18.352  1.00121.54           C  
ANISOU 2118  CA  GLU A 276    20760  11472  13947  -3463    727  -1332       C  
ATOM   2119  C   GLU A 276     132.282  36.352  17.615  1.00119.74           C  
ANISOU 2119  C   GLU A 276    20382  11372  13740  -3009    648  -1347       C  
ATOM   2120  O   GLU A 276     133.220  36.869  18.233  1.00113.16           O  
ANISOU 2120  O   GLU A 276    19490  10515  12992  -2639    630  -1228       O  
ATOM   2121  CB  GLU A 276     131.061  34.348  18.486  1.00125.78           C  
ANISOU 2121  CB  GLU A 276    21925  11516  14350  -3611    779  -1465       C  
ATOM   2122  CG  GLU A 276     132.362  33.821  19.072  1.00133.12           C  
ANISOU 2122  CG  GLU A 276    23253  12053  15275  -3170    768  -1434       C  
ATOM   2123  CD  GLU A 276     132.484  32.313  18.980  1.00147.45           C  
ANISOU 2123  CD  GLU A 276    25699  13372  16954  -3247    798  -1581       C  
ATOM   2124  OE1 GLU A 276     131.521  31.660  18.526  1.00150.25           O  
ANISOU 2124  OE1 GLU A 276    26104  13761  17222  -3639    835  -1674       O  
ATOM   2125  OE2 GLU A 276     133.549  31.780  19.360  1.00150.85           O  
ANISOU 2125  OE2 GLU A 276    26407  13533  17375  -2828    770  -1552       O  
ATOM   2126  N   ALA A 277     132.313  36.182  16.291  1.00117.55           N  
ANISOU 2126  N   ALA A 277    20040  11251  13371  -3048    604  -1500       N  
ATOM   2127  CA  ALA A 277     133.478  36.614  15.527  1.00110.48           C  
ANISOU 2127  CA  ALA A 277    18997  10510  12472  -2652    548  -1528       C  
ATOM   2128  C   ALA A 277     133.662  38.124  15.590  1.00103.75           C  
ANISOU 2128  C   ALA A 277    17619  10051  11749  -2486    500  -1345       C  
ATOM   2129  O   ALA A 277     134.795  38.614  15.526  1.00 98.97           O  
ANISOU 2129  O   ALA A 277    16907   9516  11181  -2113    473  -1299       O  
ATOM   2130  CB  ALA A 277     133.360  36.152  14.076  1.00110.15           C  
ANISOU 2130  CB  ALA A 277    18983  10589  12279  -2777    520  -1734       C  
ATOM   2131  N   ALA A 278     132.569  38.876  15.722  1.00103.56           N  
ANISOU 2131  N   ALA A 278    17266  10287  11796  -2756    488  -1245       N  
ATOM   2132  CA  ALA A 278     132.680  40.329  15.790  1.00 99.61           C  
ANISOU 2132  CA  ALA A 278    16299  10124  11426  -2603    439  -1070       C  
ATOM   2133  C   ALA A 278     133.330  40.772  17.097  1.00108.55           C  
ANISOU 2133  C   ALA A 278    17452  11109  12685  -2347    471   -923       C  
ATOM   2134  O   ALA A 278     134.247  41.602  17.091  1.00106.94           O  
ANISOU 2134  O   ALA A 278    17049  11034  12548  -2044    435   -834       O  
ATOM   2135  CB  ALA A 278     131.302  40.969  15.621  1.00 88.01           C  
ANISOU 2135  CB  ALA A 278    14485   8952  10001  -2929    413  -1016       C  
ATOM   2136  N   VAL A 279     132.884  40.219  18.229  1.00109.99           N  
ANISOU 2136  N   VAL A 279    17880  11025  12885  -2484    540   -897       N  
ATOM   2137  CA  VAL A 279     133.428  40.654  19.514  1.00120.99           C  
ANISOU 2137  CA  VAL A 279    19292  12301  14379  -2266    565   -757       C  
ATOM   2138  C   VAL A 279     134.896  40.264  19.647  1.00119.89           C  
ANISOU 2138  C   VAL A 279    19388  11958  14207  -1868    540   -778       C  
ATOM   2139  O   VAL A 279     135.654  40.920  20.372  1.00121.15           O  
ANISOU 2139  O   VAL A 279    19439  12143  14449  -1603    523   -665       O  
ATOM   2140  CB  VAL A 279     132.594  40.099  20.687  1.00112.98           C  
ANISOU 2140  CB  VAL A 279    18510  11058  13358  -2529    651   -724       C  
ATOM   2141  CG1 VAL A 279     131.123  40.426  20.502  1.00111.90           C  
ANISOU 2141  CG1 VAL A 279    18108  11165  13245  -2929    681   -732       C  
ATOM   2142  CG2 VAL A 279     132.800  38.604  20.847  1.00111.30           C  
ANISOU 2142  CG2 VAL A 279    18855  10424  13011  -2588    689   -830       C  
ATOM   2143  N   ARG A 280     135.328  39.205  18.957  1.00110.28           N  
ANISOU 2143  N   ARG A 280    18483  10549  12868  -1811    535   -934       N  
ATOM   2144  CA  ARG A 280     136.730  38.809  19.040  1.00105.53           C  
ANISOU 2144  CA  ARG A 280    18080   9780  12235  -1397    508   -974       C  
ATOM   2145  C   ARG A 280     137.612  39.743  18.222  1.00103.93           C  
ANISOU 2145  C   ARG A 280    17504   9922  12065  -1139    458   -968       C  
ATOM   2146  O   ARG A 280     138.739  40.056  18.623  1.00103.50           O  
ANISOU 2146  O   ARG A 280    17397   9881  12048   -793    432   -922       O  
ATOM   2147  CB  ARG A 280     136.899  37.362  18.577  1.00111.24           C  
ANISOU 2147  CB  ARG A 280    19277  10168  12821  -1397    526  -1161       C  
ATOM   2148  CG  ARG A 280     138.321  36.835  18.706  1.00122.56           C  
ANISOU 2148  CG  ARG A 280    20941  11405  14221   -934    495  -1221       C  
ATOM   2149  CD  ARG A 280     138.434  35.384  18.256  1.00127.09           C  
ANISOU 2149  CD  ARG A 280    22018  11606  14664   -921    513  -1418       C  
ATOM   2150  NE  ARG A 280     138.200  35.224  16.823  1.00132.66           N  
ANISOU 2150  NE  ARG A 280    22633  12490  15281  -1058    521  -1601       N  
ATOM   2151  CZ  ARG A 280     137.032  34.877  16.291  1.00140.63           C  
ANISOU 2151  CZ  ARG A 280    23707  13499  16226  -1495    551  -1681       C  
ATOM   2152  NH1 ARG A 280     135.984  34.654  17.071  1.00148.06           N  
ANISOU 2152  NH1 ARG A 280    24790  14279  17189  -1846    587  -1596       N  
ATOM   2153  NH2 ARG A 280     136.910  34.754  14.978  1.00135.93           N  
ANISOU 2153  NH2 ARG A 280    23024  13090  15532  -1595    546  -1851       N  
ATOM   2154  N   ARG A 281     137.113  40.201  17.071  1.00107.19           N  
ANISOU 2154  N   ARG A 281    17649  10630  12448  -1316    440  -1011       N  
ATOM   2155  CA  ARG A 281     137.896  41.108  16.238  1.00103.65           C  
ANISOU 2155  CA  ARG A 281    16860  10517  12007  -1117    400   -991       C  
ATOM   2156  C   ARG A 281     137.981  42.502  16.848  1.00100.18           C  
ANISOU 2156  C   ARG A 281    16054  10294  11714  -1053    375   -791       C  
ATOM   2157  O   ARG A 281     138.970  43.212  16.630  1.00 93.05           O  
ANISOU 2157  O   ARG A 281    14943   9575  10836   -815    352   -748       O  
ATOM   2158  CB  ARG A 281     137.303  41.157  14.831  1.00101.81           C  
ANISOU 2158  CB  ARG A 281    16484  10527  11672  -1339    379  -1083       C  
ATOM   2159  CG  ARG A 281     137.320  39.804  14.133  1.00104.67           C  
ANISOU 2159  CG  ARG A 281    17211  10683  11874  -1394    406  -1312       C  
ATOM   2160  CD  ARG A 281     136.494  39.807  12.858  1.00113.91           C  
ANISOU 2160  CD  ARG A 281    18257  12093  12931  -1690    379  -1404       C  
ATOM   2161  NE  ARG A 281     137.135  40.569  11.792  1.00121.35           N  
ANISOU 2161  NE  ARG A 281    18903  13392  13812  -1553    346  -1399       N  
ATOM   2162  CZ  ARG A 281     137.986  40.049  10.915  1.00121.01           C  
ANISOU 2162  CZ  ARG A 281    18971  13379  13629  -1384    368  -1572       C  
ATOM   2163  NH1 ARG A 281     138.300  38.761  10.977  1.00112.72           N  
ANISOU 2163  NH1 ARG A 281    18332  11997  12498  -1301    415  -1771       N  
ATOM   2164  NH2 ARG A 281     138.524  40.814   9.975  1.00128.42           N  
ANISOU 2164  NH2 ARG A 281    19622  14672  14499  -1297    348  -1550       N  
ATOM   2165  N   THR A 282     136.969  42.909  17.619  1.00106.76           N  
ANISOU 2165  N   THR A 282    16809  11111  12643  -1269    388   -680       N  
ATOM   2166  CA  THR A 282     137.052  44.186  18.322  1.00104.15           C  
ANISOU 2166  CA  THR A 282    16180  10935  12458  -1193    372   -508       C  
ATOM   2167  C   THR A 282     138.049  44.117  19.470  1.00 93.72           C  
ANISOU 2167  C   THR A 282    14998   9433  11179   -920    382   -462       C  
ATOM   2168  O   THR A 282     138.800  45.070  19.705  1.00 91.47           O  
ANISOU 2168  O   THR A 282    14485   9301  10969   -733    356   -373       O  
ATOM   2169  CB  THR A 282     135.676  44.598  18.843  1.00 96.44           C  
ANISOU 2169  CB  THR A 282    15078  10001  11566  -1480    392   -429       C  
ATOM   2170  OG1 THR A 282     135.246  43.672  19.848  1.00101.35           O  
ANISOU 2170  OG1 THR A 282    16020  10326  12163  -1596    455   -460       O  
ATOM   2171  CG2 THR A 282     134.673  44.606  17.717  1.00 87.63           C  
ANISOU 2171  CG2 THR A 282    13814   9085  10396  -1744    363   -481       C  
ATOM   2172  N   VAL A 283     138.067  42.998  20.198  1.00 92.50           N  
ANISOU 2172  N   VAL A 283    15227   8952  10967   -905    414   -517       N  
ATOM   2173  CA  VAL A 283     139.027  42.837  21.285  1.00 89.02           C  
ANISOU 2173  CA  VAL A 283    14946   8338  10541   -628    404   -471       C  
ATOM   2174  C   VAL A 283     140.447  42.771  20.736  1.00 89.31           C  
ANISOU 2174  C   VAL A 283    14945   8456  10533   -278    360   -543       C  
ATOM   2175  O   VAL A 283     141.382  43.327  21.326  1.00 88.58           O  
ANISOU 2175  O   VAL A 283    14727   8441  10488    -34    327   -479       O  
ATOM   2176  CB  VAL A 283     138.676  41.596  22.125  1.00 93.74           C  
ANISOU 2176  CB  VAL A 283    16005   8545  11065   -700    439   -501       C  
ATOM   2177  CG1 VAL A 283     139.805  41.259  23.084  1.00 96.69           C  
ANISOU 2177  CG1 VAL A 283    16588   8732  11419   -360    400   -466       C  
ATOM   2178  CG2 VAL A 283     137.383  41.831  22.891  1.00 84.70           C  
ANISOU 2178  CG2 VAL A 283    14842   7372   9968  -1038    498   -415       C  
ATOM   2179  N   MET A 284     140.631  42.105  19.593  1.00 88.63           N  
ANISOU 2179  N   MET A 284    14949   8380  10346   -256    363   -691       N  
ATOM   2180  CA  MET A 284     141.937  42.076  18.946  1.00 86.61           C  
ANISOU 2180  CA  MET A 284    14611   8260  10037     63    339   -783       C  
ATOM   2181  C   MET A 284     142.363  43.444  18.432  1.00 88.98           C  
ANISOU 2181  C   MET A 284    14457   8955  10396     87    322   -701       C  
ATOM   2182  O   MET A 284     143.563  43.679  18.257  1.00 90.51           O  
ANISOU 2182  O   MET A 284    14517   9301  10570    356    307   -735       O  
ATOM   2183  CB  MET A 284     141.934  41.079  17.787  1.00101.30           C  
ANISOU 2183  CB  MET A 284    16669  10057  11764     51    361   -979       C  
ATOM   2184  CG  MET A 284     142.238  39.650  18.187  1.00105.08           C  
ANISOU 2184  CG  MET A 284    17628  10133  12165    217    365  -1102       C  
ATOM   2185  SD  MET A 284     142.264  38.530  16.776  1.00 85.05           S  
ANISOU 2185  SD  MET A 284    15329   7518   9469    208    398  -1364       S  
ATOM   2186  CE  MET A 284     140.533  38.521  16.331  1.00 85.90           C  
ANISOU 2186  CE  MET A 284    15450   7628   9559   -341    427  -1348       C  
ATOM   2187  N   THR A 285     141.414  44.345  18.184  1.00 88.93           N  
ANISOU 2187  N   THR A 285    14214   9119  10457   -186    323   -594       N  
ATOM   2188  CA  THR A 285     141.715  45.666  17.643  1.00 83.61           C  
ANISOU 2188  CA  THR A 285    13151   8783   9834   -192    302   -498       C  
ATOM   2189  C   THR A 285     141.385  46.761  18.651  1.00 83.07           C  
ANISOU 2189  C   THR A 285    12901   8744   9917   -253    288   -325       C  
ATOM   2190  O   THR A 285     142.295  47.358  19.231  1.00 71.44           O  
ANISOU 2190  O   THR A 285    11310   7338   8497    -72    274   -269       O  
ATOM   2191  CB  THR A 285     140.964  45.882  16.328  1.00 79.67           C  
ANISOU 2191  CB  THR A 285    12519   8481   9271   -423    297   -518       C  
ATOM   2192  OG1 THR A 285     139.555  45.727  16.546  1.00 69.10           O  
ANISOU 2192  OG1 THR A 285    11245   7039   7970   -701    296   -484       O  
ATOM   2193  CG2 THR A 285     141.422  44.874  15.294  1.00 84.97           C  
ANISOU 2193  CG2 THR A 285    13356   9152   9777   -349    318   -710       C  
ATOM   2194  N   SER A 286     140.100  47.045  18.877  1.00 81.25           N  
ANISOU 2194  N   SER A 286    12637   8481   9754   -505    295   -253       N  
ATOM   2195  CA  SER A 286     139.729  48.138  19.770  1.00 92.80           C  
ANISOU 2195  CA  SER A 286    13916   9982  11361   -556    290   -109       C  
ATOM   2196  C   SER A 286     140.016  47.785  21.225  1.00102.92           C  
ANISOU 2196  C   SER A 286    15389  11038  12676   -447    311    -94       C  
ATOM   2197  O   SER A 286     140.562  48.604  21.974  1.00 97.29           O  
ANISOU 2197  O   SER A 286    14547  10375  12042   -335    297    -15       O  
ATOM   2198  CB  SER A 286     138.255  48.492  19.577  1.00 88.23           C  
ANISOU 2198  CB  SER A 286    13228   9457  10840   -831    293    -58       C  
ATOM   2199  OG  SER A 286     138.053  49.149  18.339  1.00 94.93           O  
ANISOU 2199  OG  SER A 286    13845  10552  11671   -906    248    -24       O  
ATOM   2200  N   GLY A 287     139.645  46.573  21.645  1.00104.73           N  
ANISOU 2200  N   GLY A 287    15946  11014  12834   -493    341   -167       N  
ATOM   2201  CA  GLY A 287     139.970  46.141  22.994  1.00100.13           C  
ANISOU 2201  CA  GLY A 287    15590  10206  12248   -381    351   -142       C  
ATOM   2202  C   GLY A 287     141.462  46.168  23.261  1.00 93.58           C  
ANISOU 2202  C   GLY A 287    14760   9404  11393    -49    302   -156       C  
ATOM   2203  O   GLY A 287     141.903  46.539  24.352  1.00 92.02           O  
ANISOU 2203  O   GLY A 287    14557   9173  11232     63    284    -88       O  
ATOM   2204  N   ARG A 288     142.259  45.783  22.264  1.00 88.74           N  
ANISOU 2204  N   ARG A 288    14136   8877  10706    110    280   -254       N  
ATOM   2205  CA  ARG A 288     143.705  45.912  22.383  1.00 83.55           C  
ANISOU 2205  CA  ARG A 288    13395   8325  10025    427    235   -283       C  
ATOM   2206  C   ARG A 288     144.122  47.377  22.418  1.00 87.71           C  
ANISOU 2206  C   ARG A 288    13543   9136  10647    418    219   -188       C  
ATOM   2207  O   ARG A 288     145.023  47.755  23.176  1.00 76.32           O  
ANISOU 2207  O   ARG A 288    12023   7750   9225    597    182   -159       O  
ATOM   2208  CB  ARG A 288     144.384  45.183  21.226  1.00 79.60           C  
ANISOU 2208  CB  ARG A 288    12943   7884   9417    583    235   -433       C  
ATOM   2209  CG  ARG A 288     145.889  45.097  21.340  1.00 83.95           C  
ANISOU 2209  CG  ARG A 288    13422   8549   9927    937    194   -497       C  
ATOM   2210  CD  ARG A 288     146.475  44.407  20.127  1.00 92.09           C  
ANISOU 2210  CD  ARG A 288    14478   9665  10847   1082    214   -667       C  
ATOM   2211  NE  ARG A 288     147.418  45.270  19.426  1.00104.51           N  
ANISOU 2211  NE  ARG A 288    15680  11618  12411   1167    221   -686       N  
ATOM   2212  CZ  ARG A 288     148.729  45.261  19.633  1.00 98.29           C  
ANISOU 2212  CZ  ARG A 288    14771  10981  11593   1471    193   -750       C  
ATOM   2213  NH1 ARG A 288     149.257  44.428  20.517  1.00 98.38           N  
ANISOU 2213  NH1 ARG A 288    15010  10785  11584   1754    139   -796       N  
ATOM   2214  NH2 ARG A 288     149.514  46.079  18.952  1.00 90.54           N  
ANISOU 2214  NH2 ARG A 288    13440  10368  10593   1488    217   -767       N  
ATOM   2215  N   THR A 289     143.471  48.216  21.608  1.00 99.19           N  
ANISOU 2215  N   THR A 289    14770  10766  12153    206    239   -136       N  
ATOM   2216  CA  THR A 289     143.785  49.642  21.601  1.00 87.12           C  
ANISOU 2216  CA  THR A 289    12921   9464  10717    173    224    -34       C  
ATOM   2217  C   THR A 289     143.430  50.291  22.933  1.00 84.61           C  
ANISOU 2217  C   THR A 289    12590   9051  10507    124    222     63       C  
ATOM   2218  O   THR A 289     144.169  51.147  23.434  1.00 68.56           O  
ANISOU 2218  O   THR A 289    10395   7129   8526    203    199    109       O  
ATOM   2219  CB  THR A 289     143.046  50.331  20.451  1.00 82.96           C  
ANISOU 2219  CB  THR A 289    12204   9105  10212    -37    232     18       C  
ATOM   2220  OG1 THR A 289     143.531  49.828  19.198  1.00 77.74           O  
ANISOU 2220  OG1 THR A 289    11535   8577   9427     12    238    -78       O  
ATOM   2221  CG2 THR A 289     143.238  51.846  20.501  1.00 65.29           C  
ANISOU 2221  CG2 THR A 289     9685   7041   8079    -93    215    144       C  
ATOM   2222  N   VAL A 290     142.308  49.882  23.530  1.00 93.19           N  
ANISOU 2222  N   VAL A 290    13847   9944  11618    -21    253     81       N  
ATOM   2223  CA  VAL A 290     141.853  50.496  24.774  1.00 84.40           C  
ANISOU 2223  CA  VAL A 290    12718   8754  10594    -87    269    158       C  
ATOM   2224  C   VAL A 290     142.760  50.103  25.935  1.00 85.02           C  
ANISOU 2224  C   VAL A 290    12954   8727  10622    111    241    144       C  
ATOM   2225  O   VAL A 290     143.108  50.940  26.777  1.00 83.21           O  
ANISOU 2225  O   VAL A 290    12612   8552  10451    144    226    194       O  
ATOM   2226  CB  VAL A 290     140.384  50.121  25.041  1.00 82.09           C  
ANISOU 2226  CB  VAL A 290    12544   8323  10322   -316    325    167       C  
ATOM   2227  CG1 VAL A 290     140.040  50.301  26.506  1.00 84.31           C  
ANISOU 2227  CG1 VAL A 290    12913   8481  10639   -350    360    208       C  
ATOM   2228  CG2 VAL A 290     139.461  50.962  24.172  1.00 79.50           C  
ANISOU 2228  CG2 VAL A 290    11968   8155  10081   -496    331    211       C  
ATOM   2229  N   VAL A 291     143.156  48.829  26.001  1.00 89.63           N  
ANISOU 2229  N   VAL A 291    13810   9153  11090    250    224     75       N  
ATOM   2230  CA  VAL A 291     144.045  48.381  27.072  1.00 84.01           C  
ANISOU 2230  CA  VAL A 291    13264   8343  10314    474    172     71       C  
ATOM   2231  C   VAL A 291     145.377  49.117  26.999  1.00 84.97           C  
ANISOU 2231  C   VAL A 291    13130   8706  10449    673    111     60       C  
ATOM   2232  O   VAL A 291     145.897  49.600  28.012  1.00 82.73           O  
ANISOU 2232  O   VAL A 291    12798   8460  10175    752     70     98       O  
ATOM   2233  CB  VAL A 291     144.234  46.854  27.013  1.00 85.02           C  
ANISOU 2233  CB  VAL A 291    13754   8235  10316    615    155      0       C  
ATOM   2234  CG1 VAL A 291     145.361  46.421  27.938  1.00 75.06           C  
ANISOU 2234  CG1 VAL A 291    12630   6912   8977    918     70     -3       C  
ATOM   2235  CG2 VAL A 291     142.937  46.148  27.383  1.00 87.12           C  
ANISOU 2235  CG2 VAL A 291    14303   8242  10555    376    220     22       C  
ATOM   2236  N   PHE A 292     145.946  49.219  25.794  1.00 79.60           N  
ANISOU 2236  N   PHE A 292    12276   8214   9756    736    107      1       N  
ATOM   2237  CA  PHE A 292     147.164  50.004  25.616  1.00 77.73           C  
ANISOU 2237  CA  PHE A 292    11755   8250   9528    868     67    -13       C  
ATOM   2238  C   PHE A 292     146.943  51.460  26.005  1.00 84.14           C  
ANISOU 2238  C   PHE A 292    12330   9183  10456    689     78     81       C  
ATOM   2239  O   PHE A 292     147.783  52.065  26.681  1.00 66.19           O  
ANISOU 2239  O   PHE A 292     9926   7030   8193    771     35     90       O  
ATOM   2240  CB  PHE A 292     147.645  49.914  24.167  1.00 74.39           C  
ANISOU 2240  CB  PHE A 292    11183   8025   9059    906     87    -90       C  
ATOM   2241  CG  PHE A 292     148.534  48.738  23.894  1.00 75.51           C  
ANISOU 2241  CG  PHE A 292    11458   8150   9083   1196     58   -220       C  
ATOM   2242  CD1 PHE A 292     149.842  48.724  24.351  1.00 69.76           C  
ANISOU 2242  CD1 PHE A 292    10620   7573   8311   1461     -4   -272       C  
ATOM   2243  CD2 PHE A 292     148.072  47.656  23.161  1.00 68.72           C  
ANISOU 2243  CD2 PHE A 292    10826   7133   8153   1210     88   -304       C  
ATOM   2244  CE1 PHE A 292     150.667  47.644  24.098  1.00 70.50           C  
ANISOU 2244  CE1 PHE A 292    10826   7659   8303   1771    -38   -403       C  
ATOM   2245  CE2 PHE A 292     148.894  46.574  22.904  1.00 85.86           C  
ANISOU 2245  CE2 PHE A 292    13139   9263  10220   1504     63   -440       C  
ATOM   2246  CZ  PHE A 292     150.194  46.568  23.373  1.00 78.87           C  
ANISOU 2246  CZ  PHE A 292    12137   8528   9301   1803     -1   -488       C  
ATOM   2247  N   SER A 293     145.816  52.040  25.587  1.00 93.87           N  
ANISOU 2247  N   SER A 293    13506  10385  11774    450    130    146       N  
ATOM   2248  CA  SER A 293     145.537  53.434  25.910  1.00 91.77           C  
ANISOU 2248  CA  SER A 293    13042  10197  11629    298    140    231       C  
ATOM   2249  C   SER A 293     145.388  53.646  27.412  1.00 91.60           C  
ANISOU 2249  C   SER A 293    13115  10051  11638    303    133    255       C  
ATOM   2250  O   SER A 293     145.768  54.701  27.930  1.00 73.25           O  
ANISOU 2250  O   SER A 293    10639   7815   9378    271    119    284       O  
ATOM   2251  CB  SER A 293     144.281  53.898  25.171  1.00 79.37           C  
ANISOU 2251  CB  SER A 293    11411   8606  10140     84    184    292       C  
ATOM   2252  OG  SER A 293     144.422  53.713  23.773  1.00 77.95           O  
ANISOU 2252  OG  SER A 293    11153   8559   9907     67    183    274       O  
ATOM   2253  N   ALA A 294     144.853  52.656  28.129  1.00 99.72           N  
ANISOU 2253  N   ALA A 294    14409  10873  12607    327    146    239       N  
ATOM   2254  CA  ALA A 294     144.704  52.799  29.574  1.00 83.11           C  
ANISOU 2254  CA  ALA A 294    12416   8663  10500    322    146    262       C  
ATOM   2255  C   ALA A 294     146.044  52.652  30.286  1.00 73.06           C  
ANISOU 2255  C   ALA A 294    11153   7465   9141    541     59    232       C  
ATOM   2256  O   ALA A 294     146.350  53.418  31.207  1.00 64.37           O  
ANISOU 2256  O   ALA A 294     9975   6420   8061    527     38    246       O  
ATOM   2257  CB  ALA A 294     143.699  51.778  30.103  1.00 80.87           C  
ANISOU 2257  CB  ALA A 294    12428   8143  10158    246    195    267       C  
ATOM   2258  N   VAL A 295     146.853  51.670  29.878  1.00 75.42           N  
ANISOU 2258  N   VAL A 295    11541   7776   9338    755      5    178       N  
ATOM   2259  CA  VAL A 295     148.163  51.474  30.496  1.00 63.75           C  
ANISOU 2259  CA  VAL A 295    10044   6406   7773   1001    -95    141       C  
ATOM   2260  C   VAL A 295     149.069  52.670  30.230  1.00 73.19           C  
ANISOU 2260  C   VAL A 295    10888   7895   9025    985   -121    123       C  
ATOM   2261  O   VAL A 295     149.946  52.992  31.043  1.00 70.16           O  
ANISOU 2261  O   VAL A 295    10423   7635   8600   1088   -196    105       O  
ATOM   2262  CB  VAL A 295     148.787  50.154  29.996  1.00 71.98           C  
ANISOU 2262  CB  VAL A 295    11249   7396   8705   1262   -145     73       C  
ATOM   2263  CG1 VAL A 295     150.205  49.982  30.518  1.00 81.10           C  
ANISOU 2263  CG1 VAL A 295    12327   8713   9773   1557   -262     24       C  
ATOM   2264  CG2 VAL A 295     147.925  48.974  30.417  1.00 74.11           C  
ANISOU 2264  CG2 VAL A 295    11917   7333   8907   1253   -124     99       C  
ATOM   2265  N   ILE A 296     148.864  53.358  29.105  1.00 93.03           N  
ANISOU 2265  N   ILE A 296    13198  10529  11622    837    -64    132       N  
ATOM   2266  CA  ILE A 296     149.672  54.533  28.793  1.00 92.97           C  
ANISOU 2266  CA  ILE A 296    12881  10781  11661    772    -75    128       C  
ATOM   2267  C   ILE A 296     149.369  55.666  29.764  1.00 85.84           C  
ANISOU 2267  C   ILE A 296    11926   9848  10843    608    -70    176       C  
ATOM   2268  O   ILE A 296     150.281  56.336  30.263  1.00 72.66           O  
ANISOU 2268  O   ILE A 296    10100   8345   9162    619   -119    148       O  
ATOM   2269  CB  ILE A 296     149.447  54.960  27.332  1.00 93.51           C  
ANISOU 2269  CB  ILE A 296    12793  10960  11777    638    -14    147       C  
ATOM   2270  CG1 ILE A 296     150.174  54.004  26.384  1.00 93.96           C  
ANISOU 2270  CG1 ILE A 296    12833  11142  11726    824    -23     60       C  
ATOM   2271  CG2 ILE A 296     149.916  56.386  27.113  1.00 97.52           C  
ANISOU 2271  CG2 ILE A 296    13038  11659  12357    475     -6    184       C  
ATOM   2272  CD1 ILE A 296     149.808  54.187  24.937  1.00 92.90           C  
ANISOU 2272  CD1 ILE A 296    12605  11093  11601    693     39     75       C  
ATOM   2273  N   ILE A 297     148.086  55.898  30.049  1.00 84.41           N  
ANISOU 2273  N   ILE A 297    11865   9464  10742    450     -7    232       N  
ATOM   2274  CA  ILE A 297     147.716  56.931  31.011  1.00 79.66           C  
ANISOU 2274  CA  ILE A 297    11236   8813  10220    313     10    256       C  
ATOM   2275  C   ILE A 297     148.243  56.583  32.398  1.00 77.52           C  
ANISOU 2275  C   ILE A 297    11084   8524   9848    429    -51    218       C  
ATOM   2276  O   ILE A 297     148.682  57.463  33.149  1.00 59.96           O  
ANISOU 2276  O   ILE A 297     8765   6378   7640    373    -78    197       O  
ATOM   2277  CB  ILE A 297     146.191  57.141  31.004  1.00 75.66           C  
ANISOU 2277  CB  ILE A 297    10818   8117   9814    153     96    305       C  
ATOM   2278  CG1 ILE A 297     145.800  58.026  29.818  1.00 77.33           C  
ANISOU 2278  CG1 ILE A 297    10851   8387  10143     19    130    358       C  
ATOM   2279  CG2 ILE A 297     145.715  57.731  32.321  1.00 69.37           C  
ANISOU 2279  CG2 ILE A 297    10085   7222   9052     75    124    297       C  
ATOM   2280  CD1 ILE A 297     144.397  58.576  29.888  1.00 76.64           C  
ANISOU 2280  CD1 ILE A 297    10779   8161  10178   -124    196    401       C  
ATOM   2281  N   VAL A 298     148.228  55.294  32.753  1.00 81.74           N  
ANISOU 2281  N   VAL A 298    11844   8948  10264    588    -83    210       N  
ATOM   2282  CA  VAL A 298     148.854  54.859  34.001  1.00 67.87           C  
ANISOU 2282  CA  VAL A 298    10217   7190   8381    734   -167    190       C  
ATOM   2283  C   VAL A 298     150.339  55.196  33.992  1.00 74.45           C  
ANISOU 2283  C   VAL A 298    10827   8297   9164    872   -272    132       C  
ATOM   2284  O   VAL A 298     150.874  55.748  34.960  1.00 70.78           O  
ANISOU 2284  O   VAL A 298    10304   7932   8657    865   -332    108       O  
ATOM   2285  CB  VAL A 298     148.620  53.355  34.231  1.00 71.48           C  
ANISOU 2285  CB  VAL A 298    10989   7457   8715    895   -191    208       C  
ATOM   2286  CG1 VAL A 298     149.518  52.846  35.349  1.00 74.53           C  
ANISOU 2286  CG1 VAL A 298    11495   7876   8946   1107   -316    199       C  
ATOM   2287  CG2 VAL A 298     147.169  53.101  34.569  1.00 78.72           C  
ANISOU 2287  CG2 VAL A 298    12124   8130   9656    709    -85    257       C  
ATOM   2288  N   ALA A 299     151.025  54.874  32.891  1.00 85.77           N  
ANISOU 2288  N   ALA A 299    12119   9880  10590    988   -291     97       N  
ATOM   2289  CA  ALA A 299     152.429  55.245  32.754  1.00 85.00           C  
ANISOU 2289  CA  ALA A 299    11753  10094  10447   1093   -372     28       C  
ATOM   2290  C   ALA A 299     152.628  56.752  32.800  1.00 79.34           C  
ANISOU 2290  C   ALA A 299    10795   9528   9824    848   -343     25       C  
ATOM   2291  O   ALA A 299     153.730  57.213  33.118  1.00 70.07           O  
ANISOU 2291  O   ALA A 299     9417   8605   8602    876   -416    -35       O  
ATOM   2292  CB  ALA A 299     152.999  54.687  31.449  1.00 77.09           C  
ANISOU 2292  CB  ALA A 299    10629   9237   9423   1229   -363    -20       C  
ATOM   2293  N   SER A 300     151.589  57.525  32.490  1.00 75.11           N  
ANISOU 2293  N   SER A 300    10279   8841   9418    611   -243     85       N  
ATOM   2294  CA  SER A 300     151.663  58.975  32.569  1.00 76.10           C  
ANISOU 2294  CA  SER A 300    10234   9038   9643    378   -214     89       C  
ATOM   2295  C   SER A 300     151.419  59.506  33.974  1.00 85.15           C  
ANISOU 2295  C   SER A 300    11476  10090  10786    303   -232     69       C  
ATOM   2296  O   SER A 300     151.717  60.676  34.233  1.00 74.55           O  
ANISOU 2296  O   SER A 300    10004   8819   9501    132   -229     43       O  
ATOM   2297  CB  SER A 300     150.659  59.607  31.600  1.00 81.02           C  
ANISOU 2297  CB  SER A 300    10844   9532  10406    190   -113    165       C  
ATOM   2298  OG  SER A 300     150.935  59.235  30.260  1.00 71.86           O  
ANISOU 2298  OG  SER A 300     9583   8489   9229    227    -94    180       O  
ATOM   2299  N   SER A 301     150.906  58.679  34.886  1.00 99.17           N  
ANISOU 2299  N   SER A 301    13489  11708  12485    412   -248     77       N  
ATOM   2300  CA  SER A 301     150.504  59.134  36.210  1.00 85.77           C  
ANISOU 2300  CA  SER A 301    11909   9912  10769    326   -244     57       C  
ATOM   2301  C   SER A 301     151.392  58.636  37.341  1.00 79.77           C  
ANISOU 2301  C   SER A 301    11206   9270   9832    482   -369     11       C  
ATOM   2302  O   SER A 301     151.504  59.322  38.359  1.00 74.63           O  
ANISOU 2302  O   SER A 301    10558   8648   9149    384   -390    -36       O  
ATOM   2303  CB  SER A 301     149.057  58.714  36.495  1.00 71.54           C  
ANISOU 2303  CB  SER A 301    10342   7840   9000    274   -145    107       C  
ATOM   2304  OG  SER A 301     148.165  59.321  35.576  1.00 59.14           O  
ANISOU 2304  OG  SER A 301     8699   6177   7595    126    -44    145       O  
ATOM   2305  N   VAL A 302     152.029  57.478  37.194  1.00 86.48           N  
ANISOU 2305  N   VAL A 302    12108  10189  10562    731   -459     17       N  
ATOM   2306  CA  VAL A 302     152.872  56.924  38.254  1.00 82.81           C  
ANISOU 2306  CA  VAL A 302    11710   9836   9916    923   -603    -11       C  
ATOM   2307  C   VAL A 302     154.119  57.762  38.543  1.00 79.77           C  
ANISOU 2307  C   VAL A 302    11039   9774   9495    896   -703    -99       C  
ATOM   2308  O   VAL A 302     154.566  57.768  39.699  1.00 82.08           O  
ANISOU 2308  O   VAL A 302    11380  10153   9654    946   -808   -130       O  
ATOM   2309  CB  VAL A 302     153.266  55.463  37.957  1.00 84.62           C  
ANISOU 2309  CB  VAL A 302    12077  10040  10035   1236   -685     17       C  
ATOM   2310  CG1 VAL A 302     152.159  54.522  38.398  1.00 71.30           C  
ANISOU 2310  CG1 VAL A 302    10770   8025   8297   1257   -632    101       C  
ATOM   2311  CG2 VAL A 302     153.578  55.251  36.484  1.00 96.07           C  
ANISOU 2311  CG2 VAL A 302    13352  11581  11569   1301   -647     -4       C  
ATOM   2312  N   PRO A 303     154.734  58.470  37.582  1.00 86.98           N  
ANISOU 2312  N   PRO A 303    11657  10890  10501    800   -680   -143       N  
ATOM   2313  CA  PRO A 303     155.896  59.297  37.953  1.00 92.06           C  
ANISOU 2313  CA  PRO A 303    12031  11850  11097    724   -769   -237       C  
ATOM   2314  C   PRO A 303     155.558  60.411  38.925  1.00 87.48           C  
ANISOU 2314  C   PRO A 303    11491  11207  10542    468   -745   -274       C  
ATOM   2315  O   PRO A 303     156.467  60.929  39.587  1.00 80.81           O  
ANISOU 2315  O   PRO A 303    10491  10601   9611    416   -844   -361       O  
ATOM   2316  CB  PRO A 303     156.380  59.855  36.607  1.00 96.40           C  
ANISOU 2316  CB  PRO A 303    12301  12577  11751    610   -706   -257       C  
ATOM   2317  CG  PRO A 303     155.879  58.902  35.606  1.00 90.80           C  
ANISOU 2317  CG  PRO A 303    11693  11732  11074    767   -646   -194       C  
ATOM   2318  CD  PRO A 303     154.540  58.493  36.119  1.00 86.68           C  
ANISOU 2318  CD  PRO A 303    11507  10846  10582    757   -585   -116       C  
ATOM   2319  N   LEU A 304     154.284  60.798  39.031  1.00 85.37           N  
ANISOU 2319  N   LEU A 304    11414  10636  10384    310   -616   -226       N  
ATOM   2320  CA  LEU A 304     153.880  61.778  40.032  1.00 87.58           C  
ANISOU 2320  CA  LEU A 304    11766  10829  10681    101   -583   -280       C  
ATOM   2321  C   LEU A 304     154.125  61.283  41.450  1.00 84.89           C  
ANISOU 2321  C   LEU A 304    11576  10538  10141    212   -691   -314       C  
ATOM   2322  O   LEU A 304     154.209  62.099  42.375  1.00 87.37           O  
ANISOU 2322  O   LEU A 304    11894  10886  10415     53   -705   -397       O  
ATOM   2323  CB  LEU A 304     152.404  62.136  39.854  1.00 75.36           C  
ANISOU 2323  CB  LEU A 304    10389   8960   9284    -32   -422   -228       C  
ATOM   2324  CG  LEU A 304     152.011  62.914  38.598  1.00 77.36           C  
ANISOU 2324  CG  LEU A 304    10519   9136   9738   -183   -319   -188       C  
ATOM   2325  CD1 LEU A 304     150.496  62.968  38.450  1.00 59.58           C  
ANISOU 2325  CD1 LEU A 304     8436   6589   7611   -237   -186   -130       C  
ATOM   2326  CD2 LEU A 304     152.597  64.316  38.645  1.00 72.66           C  
ANISOU 2326  CD2 LEU A 304     9761   8635   9211   -413   -322   -263       C  
ATOM   2327  N   LEU A 305     154.238  59.967  41.643  1.00 77.77           N  
ANISOU 2327  N   LEU A 305    10819   9629   9104    479   -772   -252       N  
ATOM   2328  CA  LEU A 305     154.580  59.419  42.949  1.00 77.31           C  
ANISOU 2328  CA  LEU A 305    10915   9634   8826    611   -902   -261       C  
ATOM   2329  C   LEU A 305     156.016  59.725  43.353  1.00 79.90           C  
ANISOU 2329  C   LEU A 305    10996  10331   9032    666  -1079   -355       C  
ATOM   2330  O   LEU A 305     156.366  59.530  44.522  1.00 78.02           O  
ANISOU 2330  O   LEU A 305    10852  10189   8603    732  -1202   -379       O  
ATOM   2331  CB  LEU A 305     154.340  57.909  42.959  1.00 79.87           C  
ANISOU 2331  CB  LEU A 305    11489   9819   9040    890   -949   -153       C  
ATOM   2332  CG  LEU A 305     152.909  57.476  42.623  1.00 78.26           C  
ANISOU 2332  CG  LEU A 305    11538   9270   8929    819   -781    -66       C  
ATOM   2333  CD1 LEU A 305     152.753  55.968  42.738  1.00 67.72           C  
ANISOU 2333  CD1 LEU A 305    10487   7783   7460   1068   -838     35       C  
ATOM   2334  CD2 LEU A 305     151.906  58.191  43.517  1.00 75.76           C  
ANISOU 2334  CD2 LEU A 305    11361   8801   8623    576   -663    -90       C  
ATOM   2335  N   LEU A 306     156.855  60.184  42.420  1.00 90.52           N  
ANISOU 2335  N   LEU A 306    12020  11907  10465    629  -1095   -410       N  
ATOM   2336  CA  LEU A 306     158.155  60.722  42.803  1.00 97.26           C  
ANISOU 2336  CA  LEU A 306    12591  13142  11220    594  -1238   -525       C  
ATOM   2337  C   LEU A 306     158.001  62.001  43.614  1.00 89.08           C  
ANISOU 2337  C   LEU A 306    11550  12101  10195    268  -1203   -620       C  
ATOM   2338  O   LEU A 306     158.840  62.295  44.473  1.00 96.86           O  
ANISOU 2338  O   LEU A 306    12423  13349  11029    237  -1343   -716       O  
ATOM   2339  CB  LEU A 306     159.009  60.990  41.562  1.00102.38           C  
ANISOU 2339  CB  LEU A 306    12892  14044  11964    574  -1228   -567       C  
ATOM   2340  CG  LEU A 306     159.386  59.815  40.657  1.00 99.17           C  
ANISOU 2340  CG  LEU A 306    12426  13713  11542    900  -1265   -517       C  
ATOM   2341  CD1 LEU A 306     159.979  60.329  39.358  1.00103.12           C  
ANISOU 2341  CD1 LEU A 306    12599  14428  12155    782  -1192   -563       C  
ATOM   2342  CD2 LEU A 306     160.364  58.888  41.357  1.00 94.77           C  
ANISOU 2342  CD2 LEU A 306    11822  13410  10777   1243  -1480   -547       C  
ATOM   2343  N   PHE A 307     156.935  62.767  43.360  1.00 85.65           N  
ANISOU 2343  N   PHE A 307    11237  11373   9933     32  -1023   -605       N  
ATOM   2344  CA  PHE A 307     156.664  64.009  44.068  1.00 88.13           C  
ANISOU 2344  CA  PHE A 307    11584  11620  10281   -267   -966   -707       C  
ATOM   2345  C   PHE A 307     156.099  63.714  45.458  1.00 85.92           C  
ANISOU 2345  C   PHE A 307    11578  11225   9841   -227   -990   -722       C  
ATOM   2346  O   PHE A 307     155.236  62.845  45.607  1.00 78.97           O  
ANISOU 2346  O   PHE A 307    10941  10132   8933    -77   -938   -621       O  
ATOM   2347  CB  PHE A 307     155.680  64.871  43.278  1.00 85.74           C  
ANISOU 2347  CB  PHE A 307    11329  11027  10223   -477   -773   -680       C  
ATOM   2348  CG  PHE A 307     156.193  65.299  41.932  1.00 89.25           C  
ANISOU 2348  CG  PHE A 307    11531  11574  10807   -566   -739   -657       C  
ATOM   2349  CD1 PHE A 307     157.530  65.618  41.755  1.00 96.47           C  
ANISOU 2349  CD1 PHE A 307    12159  12842  11652   -636   -844   -736       C  
ATOM   2350  CD2 PHE A 307     155.341  65.374  40.843  1.00 83.30           C  
ANISOU 2350  CD2 PHE A 307    10825  10588  10238   -590   -602   -556       C  
ATOM   2351  CE1 PHE A 307     158.006  66.011  40.519  1.00 99.16           C  
ANISOU 2351  CE1 PHE A 307    12279  13296  12100   -746   -797   -714       C  
ATOM   2352  CE2 PHE A 307     155.810  65.765  39.604  1.00 84.36           C  
ANISOU 2352  CE2 PHE A 307    10754  10824  10473   -684   -570   -524       C  
ATOM   2353  CZ  PHE A 307     157.145  66.084  39.441  1.00 98.73           C  
ANISOU 2353  CZ  PHE A 307    12303  12992  12217   -770   -659   -602       C  
ATOM   2354  N   PRO A 308     156.564  64.426  46.487  1.00 99.29           N  
ANISOU 2354  N   PRO A 308    13246  13065  11414   -384  -1063   -852       N  
ATOM   2355  CA  PRO A 308     156.130  64.137  47.860  1.00 96.40           C  
ANISOU 2355  CA  PRO A 308    13136  12639  10852   -354  -1095   -875       C  
ATOM   2356  C   PRO A 308     154.809  64.775  48.263  1.00 85.67           C  
ANISOU 2356  C   PRO A 308    12004  10956   9591   -539   -899   -910       C  
ATOM   2357  O   PRO A 308     154.369  64.566  49.399  1.00 70.28           O  
ANISOU 2357  O   PRO A 308    10274   8959   7472   -538   -897   -937       O  
ATOM   2358  CB  PRO A 308     157.283  64.707  48.696  1.00 97.91           C  
ANISOU 2358  CB  PRO A 308    13163  13169  10869   -463  -1264  -1022       C  
ATOM   2359  CG  PRO A 308     157.762  65.867  47.889  1.00 99.09           C  
ANISOU 2359  CG  PRO A 308    13053  13391  11205   -718  -1211  -1117       C  
ATOM   2360  CD  PRO A 308     157.604  65.470  46.442  1.00101.01           C  
ANISOU 2360  CD  PRO A 308    13193  13546  11641   -607  -1130   -991       C  
ATOM   2361  N   GLN A 309     154.166  65.547  47.391  1.00 97.43           N  
ANISOU 2361  N   GLN A 309    13448  12236  11337   -687   -736   -914       N  
ATOM   2362  CA  GLN A 309     152.882  66.150  47.729  1.00 87.05           C  
ANISOU 2362  CA  GLN A 309    12323  10623  10129   -821   -550   -958       C  
ATOM   2363  C   GLN A 309     151.809  65.070  47.791  1.00 78.94           C  
ANISOU 2363  C   GLN A 309    11512   9411   9071   -654   -464   -831       C  
ATOM   2364  O   GLN A 309     151.565  64.370  46.803  1.00 81.64           O  
ANISOU 2364  O   GLN A 309    11828   9681   9512   -521   -440   -700       O  
ATOM   2365  CB  GLN A 309     152.503  67.222  46.708  1.00 92.20           C  
ANISOU 2365  CB  GLN A 309    12869  11098  11064   -986   -423   -976       C  
ATOM   2366  CG  GLN A 309     153.383  68.466  46.728  1.00 98.21           C  
ANISOU 2366  CG  GLN A 309    13474  11974  11866  -1224   -471  -1115       C  
ATOM   2367  CD  GLN A 309     154.708  68.264  46.018  1.00101.35           C  
ANISOU 2367  CD  GLN A 309    13608  12672  12230  -1206   -613  -1082       C  
ATOM   2368  OE1 GLN A 309     154.953  67.216  45.422  1.00 90.75           O  
ANISOU 2368  OE1 GLN A 309    12194  11434  10851   -989   -670   -958       O  
ATOM   2369  NE2 GLN A 309     155.570  69.272  46.078  1.00112.04           N  
ANISOU 2369  NE2 GLN A 309    14812  14170  13589  -1444   -663  -1206       N  
ATOM   2370  N   GLY A 310     151.172  64.928  48.956  1.00 84.72           N  
ANISOU 2370  N   GLY A 310    12464  10075   9650   -683   -412   -878       N  
ATOM   2371  CA  GLY A 310     150.104  63.952  49.092  1.00 83.47           C  
ANISOU 2371  CA  GLY A 310    12523   9745   9447   -579   -310   -767       C  
ATOM   2372  C   GLY A 310     148.890  64.283  48.251  1.00 82.23           C  
ANISOU 2372  C   GLY A 310    12357   9339   9546   -637   -114   -741       C  
ATOM   2373  O   GLY A 310     148.133  63.385  47.867  1.00 69.20           O  
ANISOU 2373  O   GLY A 310    10810   7568   7914   -545    -45   -622       O  
ATOM   2374  N   PHE A 311     148.681  65.570  47.964  1.00 97.31           N  
ANISOU 2374  N   PHE A 311    14153  11167  11652   -790    -30   -852       N  
ATOM   2375  CA  PHE A 311     147.631  65.976  47.035  1.00 93.29           C  
ANISOU 2375  CA  PHE A 311    13601  10441  11404   -817    125   -818       C  
ATOM   2376  C   PHE A 311     147.788  65.274  45.691  1.00 91.58           C  
ANISOU 2376  C   PHE A 311    13278  10225  11293   -696     81   -657       C  
ATOM   2377  O   PHE A 311     146.804  64.802  45.110  1.00 73.73           O  
ANISOU 2377  O   PHE A 311    11058   7825   9130   -647    182   -573       O  
ATOM   2378  CB  PHE A 311     147.660  67.498  46.876  1.00 96.14           C  
ANISOU 2378  CB  PHE A 311    13866  10715  11948   -977    176   -949       C  
ATOM   2379  CG  PHE A 311     146.992  68.007  45.632  1.00 88.09           C  
ANISOU 2379  CG  PHE A 311    12751   9514  11207   -979    265   -883       C  
ATOM   2380  CD1 PHE A 311     145.614  68.124  45.564  1.00 93.51           C  
ANISOU 2380  CD1 PHE A 311    13499  10010  12019   -956    424   -889       C  
ATOM   2381  CD2 PHE A 311     147.748  68.408  44.542  1.00 81.45           C  
ANISOU 2381  CD2 PHE A 311    11748   8711  10488  -1011    189   -819       C  
ATOM   2382  CE1 PHE A 311     145.001  68.610  44.423  1.00 91.16           C  
ANISOU 2382  CE1 PHE A 311    13110   9560  11966   -941    484   -822       C  
ATOM   2383  CE2 PHE A 311     147.141  68.892  43.399  1.00 89.41           C  
ANISOU 2383  CE2 PHE A 311    12688   9554  11728  -1016    258   -743       C  
ATOM   2384  CZ  PHE A 311     145.766  68.993  43.339  1.00 90.05           C  
ANISOU 2384  CZ  PHE A 311    12837   9441  11935   -969    395   -740       C  
ATOM   2385  N   LEU A 312     149.023  65.173  45.195  1.00 94.98           N  
ANISOU 2385  N   LEU A 312    13562  10834  11691   -653    -66   -625       N  
ATOM   2386  CA  LEU A 312     149.257  64.489  43.928  1.00 79.58           C  
ANISOU 2386  CA  LEU A 312    11508   8911   9819   -532   -105   -493       C  
ATOM   2387  C   LEU A 312     149.071  62.985  44.070  1.00 81.41           C  
ANISOU 2387  C   LEU A 312    11892   9141   9898   -346   -140   -387       C  
ATOM   2388  O   LEU A 312     148.413  62.353  43.236  1.00 81.89           O  
ANISOU 2388  O   LEU A 312    11984   9085  10044   -279    -78   -290       O  
ATOM   2389  CB  LEU A 312     150.657  64.809  43.407  1.00 69.86           C  
ANISOU 2389  CB  LEU A 312    10059   7906   8579   -542   -239   -510       C  
ATOM   2390  CG  LEU A 312     150.885  66.268  43.020  1.00 69.87           C  
ANISOU 2390  CG  LEU A 312     9921   7883   8744   -756   -201   -588       C  
ATOM   2391  CD1 LEU A 312     152.277  66.465  42.436  1.00 70.28           C  
ANISOU 2391  CD1 LEU A 312     9742   8194   8768   -791   -321   -597       C  
ATOM   2392  CD2 LEU A 312     149.812  66.710  42.043  1.00 67.68           C  
ANISOU 2392  CD2 LEU A 312     9653   7364   8697   -799    -65   -518       C  
ATOM   2393  N   LYS A 313     149.643  62.394  45.123  1.00 97.49           N  
ANISOU 2393  N   LYS A 313    14043  11299  11700   -265   -248   -403       N  
ATOM   2394  CA  LYS A 313     149.602  60.942  45.284  1.00 88.67           C  
ANISOU 2394  CA  LYS A 313    13110  10162  10421    -76   -305   -291       C  
ATOM   2395  C   LYS A 313     148.169  60.422  45.266  1.00 74.69           C  
ANISOU 2395  C   LYS A 313    11536   8153   8690   -117   -142   -229       C  
ATOM   2396  O   LYS A 313     147.865  59.432  44.590  1.00 64.28           O  
ANISOU 2396  O   LYS A 313    10297   6742   7383    -11   -132   -124       O  
ATOM   2397  CB  LYS A 313     150.309  60.537  46.580  1.00 85.84           C  
ANISOU 2397  CB  LYS A 313    12877   9948   9788      0   -444   -314       C  
ATOM   2398  CG  LYS A 313     151.780  60.919  46.623  1.00 93.13           C  
ANISOU 2398  CG  LYS A 313    13580  11158  10648     53   -627   -380       C  
ATOM   2399  CD  LYS A 313     152.571  59.997  47.533  1.00 86.01           C  
ANISOU 2399  CD  LYS A 313    12802  10414   9466    250   -816   -341       C  
ATOM   2400  CE  LYS A 313     154.065  60.243  47.394  1.00101.64           C  
ANISOU 2400  CE  LYS A 313    14505  12721  11392    339  -1009   -405       C  
ATOM   2401  NZ  LYS A 313     154.874  59.187  48.063  1.00123.66           N  
ANISOU 2401  NZ  LYS A 313    17391  15670  13924    609  -1220   -344       N  
ATOM   2402  N   SER A 314     147.270  61.088  45.994  1.00 89.10           N  
ANISOU 2402  N   SER A 314    13433   9887  10532   -280     -6   -308       N  
ATOM   2403  CA  SER A 314     145.876  60.657  46.028  1.00 81.54           C  
ANISOU 2403  CA  SER A 314    12625   8749   9608   -343    162   -270       C  
ATOM   2404  C   SER A 314     145.223  60.748  44.654  1.00 80.44           C  
ANISOU 2404  C   SER A 314    12348   8503   9710   -352    245   -220       C  
ATOM   2405  O   SER A 314     144.334  59.950  44.337  1.00 64.95           O  
ANISOU 2405  O   SER A 314    10494   6428   7756   -354    330   -148       O  
ATOM   2406  CB  SER A 314     145.095  61.497  47.040  1.00 72.69           C  
ANISOU 2406  CB  SER A 314    11556   7592   8472   -506    300   -398       C  
ATOM   2407  OG  SER A 314     145.828  61.659  48.241  1.00 90.65           O  
ANISOU 2407  OG  SER A 314    13918   9996  10529   -520    210   -468       O  
ATOM   2408  N   ILE A 315     145.649  61.704  43.827  1.00 97.01           N  
ANISOU 2408  N   ILE A 315    14222  10643  11994   -375    218   -254       N  
ATOM   2409  CA  ILE A 315     145.020  61.899  42.524  1.00 92.41           C  
ANISOU 2409  CA  ILE A 315    13512   9971  11629   -389    287   -200       C  
ATOM   2410  C   ILE A 315     145.484  60.841  41.528  1.00 78.98           C  
ANISOU 2410  C   ILE A 315    11802   8304   9904   -256    204    -88       C  
ATOM   2411  O   ILE A 315     144.685  60.339  40.729  1.00 71.50           O  
ANISOU 2411  O   ILE A 315    10868   7261   9036   -254    271    -23       O  
ATOM   2412  CB  ILE A 315     145.291  63.328  42.019  1.00102.75           C  
ANISOU 2412  CB  ILE A 315    14623  11289  13128   -475    289   -261       C  
ATOM   2413  CG1 ILE A 315     144.533  64.339  42.881  1.00 98.80           C  
ANISOU 2413  CG1 ILE A 315    14158  10696  12687   -590    403   -384       C  
ATOM   2414  CG2 ILE A 315     144.897  63.473  40.556  1.00112.96           C  
ANISOU 2414  CG2 ILE A 315    15783  12523  14613   -467    316   -177       C  
ATOM   2415  CD1 ILE A 315     144.656  65.764  42.402  1.00111.06           C  
ANISOU 2415  CD1 ILE A 315    15570  12191  14438   -675    415   -441       C  
ATOM   2416  N   THR A 316     146.771  60.477  41.559  1.00 76.95           N  
ANISOU 2416  N   THR A 316    11513   8195   9530   -138     56    -77       N  
ATOM   2417  CA  THR A 316     147.258  59.427  40.666  1.00 81.09           C  
ANISOU 2417  CA  THR A 316    12038   8753  10018     20    -19      6       C  
ATOM   2418  C   THR A 316     146.533  58.112  40.916  1.00 81.04           C  
ANISOU 2418  C   THR A 316    12293   8598   9899     83     18     76       C  
ATOM   2419  O   THR A 316     146.221  57.379  39.970  1.00 82.35           O  
ANISOU 2419  O   THR A 316    12487   8691  10109    134     38    136       O  
ATOM   2420  CB  THR A 316     148.767  59.233  40.828  1.00 72.43           C  
ANISOU 2420  CB  THR A 316    10855   7868   8798    165   -186    -15       C  
ATOM   2421  OG1 THR A 316     149.030  58.459  42.005  1.00 91.17           O  
ANISOU 2421  OG1 THR A 316    13438  10249  10954    270   -265     -7       O  
ATOM   2422  CG2 THR A 316     149.462  60.570  40.953  1.00 70.95           C  
ANISOU 2422  CG2 THR A 316    10450   7831   8679     42   -217   -104       C  
ATOM   2423  N   TYR A 317     146.259  57.793  42.185  1.00 81.36           N  
ANISOU 2423  N   TYR A 317    12543   8591   9778     58     31     68       N  
ATOM   2424  CA  TYR A 317     145.521  56.572  42.495  1.00 80.47           C  
ANISOU 2424  CA  TYR A 317    12714   8318   9542     71     81    144       C  
ATOM   2425  C   TYR A 317     144.122  56.611  41.890  1.00 80.00           C  
ANISOU 2425  C   TYR A 317    12644   8126   9628    -87    250    153       C  
ATOM   2426  O   TYR A 317     143.598  55.581  41.451  1.00 77.28           O  
ANISOU 2426  O   TYR A 317    12452   7660   9252    -81    284    219       O  
ATOM   2427  CB  TYR A 317     145.437  56.366  44.009  1.00 70.92           C  
ANISOU 2427  CB  TYR A 317    11730   7098   8118     33     79    137       C  
ATOM   2428  CG  TYR A 317     146.766  56.256  44.728  1.00 74.70           C  
ANISOU 2428  CG  TYR A 317    12234   7728   8420    195   -107    132       C  
ATOM   2429  CD1 TYR A 317     147.926  55.904  44.050  1.00 78.81           C  
ANISOU 2429  CD1 TYR A 317    12641   8361   8943    407   -265    154       C  
ATOM   2430  CD2 TYR A 317     146.856  56.502  46.094  1.00 79.12           C  
ANISOU 2430  CD2 TYR A 317    12919   8346   8798    137   -126     96       C  
ATOM   2431  CE1 TYR A 317     149.140  55.804  44.714  1.00 87.62           C  
ANISOU 2431  CE1 TYR A 317    13744   9654   9895    568   -446    141       C  
ATOM   2432  CE2 TYR A 317     148.063  56.404  46.764  1.00 77.23           C  
ANISOU 2432  CE2 TYR A 317    12688   8273   8383    285   -315     91       C  
ATOM   2433  CZ  TYR A 317     149.201  56.054  46.071  1.00 81.64           C  
ANISOU 2433  CZ  TYR A 317    13111   8952   8957    506   -479    114       C  
ATOM   2434  OH  TYR A 317     150.402  55.957  46.737  1.00 67.37           O  
ANISOU 2434  OH  TYR A 317    11277   7347   6973    667   -678    101       O  
ATOM   2435  N   ALA A 318     143.505  57.795  41.855  1.00 88.65           N  
ANISOU 2435  N   ALA A 318    13560   9242  10882   -225    351     80       N  
ATOM   2436  CA  ALA A 318     142.172  57.919  41.275  1.00 89.09           C  
ANISOU 2436  CA  ALA A 318    13559   9208  11082   -353    496     79       C  
ATOM   2437  C   ALA A 318     142.210  57.827  39.757  1.00 77.45           C  
ANISOU 2437  C   ALA A 318    11935   7736   9758   -306    464    129       C  
ATOM   2438  O   ALA A 318     141.272  57.304  39.145  1.00 67.29           O  
ANISOU 2438  O   ALA A 318    10672   6376   8519   -371    540    162       O  
ATOM   2439  CB  ALA A 318     141.529  59.235  41.712  1.00 85.04           C  
ANISOU 2439  CB  ALA A 318    12903   8712  10695   -470    601    -21       C  
ATOM   2440  N   ILE A 319     143.277  58.332  39.135  1.00 84.14           N  
ANISOU 2440  N   ILE A 319    12619   8685  10664   -213    356    130       N  
ATOM   2441  CA  ILE A 319     143.424  58.209  37.689  1.00 81.73           C  
ANISOU 2441  CA  ILE A 319    12182   8407  10466   -169    324    178       C  
ATOM   2442  C   ILE A 319     143.731  56.766  37.308  1.00 84.87           C  
ANISOU 2442  C   ILE A 319    12747   8765  10736    -51    269    231       C  
ATOM   2443  O   ILE A 319     143.186  56.237  36.332  1.00 83.67           O  
ANISOU 2443  O   ILE A 319    12598   8561  10633    -72    302    264       O  
ATOM   2444  CB  ILE A 319     144.508  59.179  37.183  1.00 78.28           C  
ANISOU 2444  CB  ILE A 319    11527   8108  10106   -133    240    160       C  
ATOM   2445  CG1 ILE A 319     144.042  60.627  37.358  1.00 75.93           C  
ANISOU 2445  CG1 ILE A 319    11097   7790   9964   -262    304    115       C  
ATOM   2446  CG2 ILE A 319     144.858  58.892  35.735  1.00 79.14           C  
ANISOU 2446  CG2 ILE A 319    11522   8278  10269    -77    200    212       C  
ATOM   2447  CD1 ILE A 319     145.050  61.661  36.909  1.00 77.65           C  
ANISOU 2447  CD1 ILE A 319    11132   8117  10255   -280    235    100       C  
ATOM   2448  N   ILE A 320     144.596  56.104  38.080  1.00 80.90           N  
ANISOU 2448  N   ILE A 320    12397   8279  10061     81    178    234       N  
ATOM   2449  CA  ILE A 320     144.939  54.711  37.802  1.00 82.18           C  
ANISOU 2449  CA  ILE A 320    12758   8369  10098    230    116    279       C  
ATOM   2450  C   ILE A 320     143.709  53.820  37.932  1.00 79.50           C  
ANISOU 2450  C   ILE A 320    12660   7832   9713    111    220    317       C  
ATOM   2451  O   ILE A 320     143.429  52.986  37.063  1.00 73.92           O  
ANISOU 2451  O   ILE A 320    12035   7039   9012    127    231    341       O  
ATOM   2452  CB  ILE A 320     146.071  54.244  38.734  1.00 80.34           C  
ANISOU 2452  CB  ILE A 320    12650   8190   9684    417    -18    282       C  
ATOM   2453  CG1 ILE A 320     147.386  54.929  38.362  1.00 81.26           C  
ANISOU 2453  CG1 ILE A 320    12498   8540   9838    539   -130    234       C  
ATOM   2454  CG2 ILE A 320     146.215  52.734  38.683  1.00 73.67           C  
ANISOU 2454  CG2 ILE A 320    12096   7198   8697    577    -73    337       C  
ATOM   2455  CD1 ILE A 320     148.531  54.572  39.279  1.00 81.19           C  
ANISOU 2455  CD1 ILE A 320    12555   8639   9654    731   -280    225       C  
ATOM   2456  N   ALA A 321     142.956  53.984  39.022  1.00 81.34           N  
ANISOU 2456  N   ALA A 321    13010   8004   9890    -30    307    312       N  
ATOM   2457  CA  ALA A 321     141.799  53.130  39.262  1.00 78.59           C  
ANISOU 2457  CA  ALA A 321    12893   7495   9475   -182    419    344       C  
ATOM   2458  C   ALA A 321     140.660  53.404  38.291  1.00 80.00           C  
ANISOU 2458  C   ALA A 321    12906   7669   9819   -346    532    323       C  
ATOM   2459  O   ALA A 321     139.836  52.514  38.056  1.00 78.92           O  
ANISOU 2459  O   ALA A 321    12930   7417   9639   -463    602    346       O  
ATOM   2460  CB  ALA A 321     141.307  53.301  40.701  1.00 81.14           C  
ANISOU 2460  CB  ALA A 321    13358   7795   9678   -306    497    334       C  
ATOM   2461  N   SER A 322     140.591  54.609  37.722  1.00 91.68           N  
ANISOU 2461  N   SER A 322    14081   9273  11481   -365    543    284       N  
ATOM   2462  CA  SER A 322     139.492  54.933  36.819  1.00 91.55           C  
ANISOU 2462  CA  SER A 322    13896   9272  11618   -498    629    272       C  
ATOM   2463  C   SER A 322     139.768  54.468  35.392  1.00 89.05           C  
ANISOU 2463  C   SER A 322    13521   8967  11347   -433    563    303       C  
ATOM   2464  O   SER A 322     138.877  53.917  34.737  1.00 78.68           O  
ANISOU 2464  O   SER A 322    12231   7613  10053   -546    618    308       O  
ATOM   2465  CB  SER A 322     139.217  56.437  36.847  1.00 77.05           C  
ANISOU 2465  CB  SER A 322    11793   7532   9952   -534    665    227       C  
ATOM   2466  OG  SER A 322     140.405  57.175  36.631  1.00 81.72           O  
ANISOU 2466  OG  SER A 322    12262   8203  10587   -407    559    228       O  
ATOM   2467  N   VAL A 323     140.989  54.675  34.895  1.00 89.06           N  
ANISOU 2467  N   VAL A 323    13439   9045  11354   -267    451    312       N  
ATOM   2468  CA  VAL A 323     141.283  54.312  33.512  1.00 95.62           C  
ANISOU 2468  CA  VAL A 323    14198   9917  12218   -209    401    327       C  
ATOM   2469  C   VAL A 323     141.449  52.802  33.360  1.00100.89           C  
ANISOU 2469  C   VAL A 323    15138  10457  12740   -141    376    331       C  
ATOM   2470  O   VAL A 323     141.114  52.244  32.308  1.00111.71           O  
ANISOU 2470  O   VAL A 323    16519  11806  14122   -174    384    326       O  
ATOM   2471  CB  VAL A 323     142.522  55.074  33.005  1.00 93.87           C  
ANISOU 2471  CB  VAL A 323    13775   9850  12042    -77    309    325       C  
ATOM   2472  CG1 VAL A 323     142.384  56.556  33.298  1.00 92.38           C  
ANISOU 2472  CG1 VAL A 323    13380   9735  11986   -157    333    320       C  
ATOM   2473  CG2 VAL A 323     143.804  54.525  33.619  1.00 98.61           C  
ANISOU 2473  CG2 VAL A 323    14490  10474  12504    114    215    309       C  
ATOM   2474  N   MET A 324     141.950  52.115  34.389  1.00 92.89           N  
ANISOU 2474  N   MET A 324    14366   9345  11582    -45    341    341       N  
ATOM   2475  CA  MET A 324     142.132  50.671  34.284  1.00 93.05           C  
ANISOU 2475  CA  MET A 324    14692   9199  11464     42    308    352       C  
ATOM   2476  C   MET A 324     140.808  49.935  34.420  1.00 93.73           C  
ANISOU 2476  C   MET A 324    14986   9115  11511   -187    419    364       C  
ATOM   2477  O   MET A 324     140.547  48.984  33.676  1.00 98.64           O  
ANISOU 2477  O   MET A 324    15761   9622  12095   -213    426    352       O  
ATOM   2478  CB  MET A 324     143.129  50.182  35.334  1.00 88.68           C  
ANISOU 2478  CB  MET A 324    14344   8591  10759    243    212    376       C  
ATOM   2479  CG  MET A 324     144.544  50.687  35.110  1.00 88.59           C  
ANISOU 2479  CG  MET A 324    14125   8772  10762    481     89    348       C  
ATOM   2480  SD  MET A 324     145.080  50.510  33.397  1.00 67.34           S  
ANISOU 2480  SD  MET A 324    11253   6188   8145    594     57    297       S  
ATOM   2481  CE  MET A 324     145.098  48.729  33.226  1.00 85.49           C  
ANISOU 2481  CE  MET A 324    13956   8227  10298    737     27    293       C  
ATOM   2482  N   LEU A 325     139.962  50.363  35.358  1.00 91.23           N  
ANISOU 2482  N   LEU A 325    14674   8793  11196   -368    515    374       N  
ATOM   2483  CA  LEU A 325     138.621  49.800  35.446  1.00 92.96           C  
ANISOU 2483  CA  LEU A 325    15024   8910  11387   -629    641    372       C  
ATOM   2484  C   LEU A 325     137.823  50.086  34.181  1.00 91.04           C  
ANISOU 2484  C   LEU A 325    14545   8762  11284   -757    682    334       C  
ATOM   2485  O   LEU A 325     136.987  49.270  33.777  1.00 76.19           O  
ANISOU 2485  O   LEU A 325    12791   6794   9364   -934    743    320       O  
ATOM   2486  CB  LEU A 325     137.898  50.357  36.673  1.00 80.53           C  
ANISOU 2486  CB  LEU A 325    13436   7369   9791   -790    748    370       C  
ATOM   2487  CG  LEU A 325     136.629  49.628  37.111  1.00 83.92           C  
ANISOU 2487  CG  LEU A 325    14053   7699  10133  -1073    891    370       C  
ATOM   2488  CD1 LEU A 325     136.963  48.220  37.575  1.00 87.76           C  
ANISOU 2488  CD1 LEU A 325    14992   7942  10411  -1063    861    433       C  
ATOM   2489  CD2 LEU A 325     135.913  50.402  38.205  1.00 88.35           C  
ANISOU 2489  CD2 LEU A 325    14512   8362  10695  -1221   1013    339       C  
ATOM   2490  N   ALA A 326     138.074  51.231  33.542  1.00 98.40           N  
ANISOU 2490  N   ALA A 326    15146   9873  12369   -682    644    321       N  
ATOM   2491  CA  ALA A 326     137.410  51.547  32.282  1.00 98.13           C  
ANISOU 2491  CA  ALA A 326    14888   9944  12453   -775    655    303       C  
ATOM   2492  C   ALA A 326     137.788  50.546  31.198  1.00 93.70           C  
ANISOU 2492  C   ALA A 326    14454   9322  11826   -721    597    290       C  
ATOM   2493  O   ALA A 326     136.918  50.002  30.506  1.00 98.54           O  
ANISOU 2493  O   ALA A 326    15090   9917  12432   -887    637    263       O  
ATOM   2494  CB  ALA A 326     137.767  52.968  31.850  1.00 92.17           C  
ANISOU 2494  CB  ALA A 326    13806   9361  11853   -685    610    314       C  
ATOM   2495  N   ALA A 327     139.088  50.290  31.036  1.00 89.36           N  
ANISOU 2495  N   ALA A 327    13977   8755  11220   -489    502    293       N  
ATOM   2496  CA  ALA A 327     139.536  49.325  30.038  1.00 89.76           C  
ANISOU 2496  CA  ALA A 327    14158   8747  11200   -403    452    257       C  
ATOM   2497  C   ALA A 327     139.049  47.922  30.370  1.00 85.57           C  
ANISOU 2497  C   ALA A 327    14006   7969  10536   -498    493    240       C  
ATOM   2498  O   ALA A 327     138.674  47.158  29.471  1.00 89.17           O  
ANISOU 2498  O   ALA A 327    14562   8362  10958   -581    503    192       O  
ATOM   2499  CB  ALA A 327     141.059  49.350  29.928  1.00 94.36           C  
ANISOU 2499  CB  ALA A 327    14722   9387  11746   -112    350    248       C  
ATOM   2500  N   ILE A 328     139.048  47.563  31.655  1.00 84.46           N  
ANISOU 2500  N   ILE A 328    14100   7682  10307   -503    515    280       N  
ATOM   2501  CA  ILE A 328     138.580  46.239  32.058  1.00 87.15           C  
ANISOU 2501  CA  ILE A 328    14847   7758  10507   -620    558    285       C  
ATOM   2502  C   ILE A 328     137.102  46.078  31.725  1.00 88.70           C  
ANISOU 2502  C   ILE A 328    15012   7958  10730   -971    675    256       C  
ATOM   2503  O   ILE A 328     136.681  45.056  31.171  1.00 78.64           O  
ANISOU 2503  O   ILE A 328    13960   6534   9386  -1099    698    215       O  
ATOM   2504  CB  ILE A 328     138.855  46.004  33.554  1.00 91.67           C  
ANISOU 2504  CB  ILE A 328    15672   8196  10962   -571    558    355       C  
ATOM   2505  CG1 ILE A 328     140.356  45.830  33.794  1.00 86.69           C  
ANISOU 2505  CG1 ILE A 328    15129   7540  10271   -205    416    374       C  
ATOM   2506  CG2 ILE A 328     138.088  44.792  34.061  1.00 87.40           C  
ANISOU 2506  CG2 ILE A 328    15548   7383  10275   -785    634    381       C  
ATOM   2507  CD1 ILE A 328     140.724  45.649  35.247  1.00 88.29           C  
ANISOU 2507  CD1 ILE A 328    15566   7639  10340   -129    385    451       C  
ATOM   2508  N   LEU A 329     136.294  47.092  32.046  1.00 94.49           N  
ANISOU 2508  N   LEU A 329    15461   8874  11566  -1129    750    262       N  
ATOM   2509  CA  LEU A 329     134.875  47.039  31.707  1.00106.05           C  
ANISOU 2509  CA  LEU A 329    16822  10407  13066  -1447    854    223       C  
ATOM   2510  C   LEU A 329     134.654  47.024  30.200  1.00100.01           C  
ANISOU 2510  C   LEU A 329    15879   9751  12367  -1478    809    169       C  
ATOM   2511  O   LEU A 329     133.671  46.444  29.723  1.00 92.11           O  
ANISOU 2511  O   LEU A 329    14917   8743  11336  -1733    865    120       O  
ATOM   2512  CB  LEU A 329     134.140  48.224  32.334  1.00104.57           C  
ANISOU 2512  CB  LEU A 329    16329  10415  12987  -1545    932    227       C  
ATOM   2513  CG  LEU A 329     134.042  48.236  33.858  1.00 95.00           C  
ANISOU 2513  CG  LEU A 329    15279   9129  11687  -1599   1013    259       C  
ATOM   2514  CD1 LEU A 329     133.406  49.530  34.334  1.00100.65           C  
ANISOU 2514  CD1 LEU A 329    15654  10057  12530  -1648   1086    233       C  
ATOM   2515  CD2 LEU A 329     133.260  47.032  34.352  1.00 90.71           C  
ANISOU 2515  CD2 LEU A 329    15068   8414  10984  -1876   1117    258       C  
ATOM   2516  N   SER A 330     135.551  47.653  29.437  1.00 92.79           N  
ANISOU 2516  N   SER A 330    14770   8956  11528  -1242    710    175       N  
ATOM   2517  CA  SER A 330     135.387  47.701  27.988  1.00 93.03           C  
ANISOU 2517  CA  SER A 330    14632   9115  11601  -1269    664    131       C  
ATOM   2518  C   SER A 330     135.503  46.313  27.368  1.00 95.16           C  
ANISOU 2518  C   SER A 330    15216   9200  11739  -1311    652     64       C  
ATOM   2519  O   SER A 330     134.773  45.987  26.424  1.00 96.14           O  
ANISOU 2519  O   SER A 330    15292   9385  11853  -1495    662      5       O  
ATOM   2520  CB  SER A 330     136.417  48.651  27.376  1.00 81.40           C  
ANISOU 2520  CB  SER A 330    12915   7805  10209  -1022    573    160       C  
ATOM   2521  OG  SER A 330     136.184  49.987  27.784  1.00 78.46           O  
ANISOU 2521  OG  SER A 330    12254   7587   9969  -1015    583    213       O  
ATOM   2522  N   ILE A 331     136.407  45.480  27.885  1.00 93.95           N  
ANISOU 2522  N   ILE A 331    13499   8091  14106   -463    800  -2112       N  
ATOM   2523  CA  ILE A 331     136.649  44.157  27.324  1.00 93.11           C  
ANISOU 2523  CA  ILE A 331    13461   7524  14393   -614    999  -2231       C  
ATOM   2524  C   ILE A 331     136.016  43.052  28.166  1.00101.15           C  
ANISOU 2524  C   ILE A 331    14138   8465  15828   -692   1000  -1946       C  
ATOM   2525  O   ILE A 331     136.281  41.870  27.929  1.00 91.85           O  
ANISOU 2525  O   ILE A 331    12946   6855  15097   -796   1226  -1973       O  
ATOM   2526  CB  ILE A 331     138.154  43.908  27.130  1.00 99.61           C  
ANISOU 2526  CB  ILE A 331    14374   8043  15431   -505   1328  -2247       C  
ATOM   2527  CG1 ILE A 331     138.862  43.787  28.480  1.00101.76           C  
ANISOU 2527  CG1 ILE A 331    14265   8454  15945   -320   1418  -1773       C  
ATOM   2528  CG2 ILE A 331     138.775  45.036  26.319  1.00 95.36           C  
ANISOU 2528  CG2 ILE A 331    14168   7593  14470   -438   1334  -2516       C  
ATOM   2529  CD1 ILE A 331     140.346  43.503  28.368  1.00 88.17           C  
ANISOU 2529  CD1 ILE A 331    12552   6458  14490   -198   1734  -1710       C  
ATOM   2530  N   THR A 332     135.183  43.408  29.145  1.00106.47           N  
ANISOU 2530  N   THR A 332    14533   9528  16394   -651    785  -1676       N  
ATOM   2531  CA  THR A 332     134.457  42.414  29.930  1.00 96.70           C  
ANISOU 2531  CA  THR A 332    12969   8259  15514   -745    764  -1393       C  
ATOM   2532  C   THR A 332     132.956  42.672  29.870  1.00 92.39           C  
ANISOU 2532  C   THR A 332    12368   7976  14762   -880    474  -1468       C  
ATOM   2533  O   THR A 332     132.238  41.999  29.125  1.00 91.08           O  
ANISOU 2533  O   THR A 332    12298   7599  14708  -1106    425  -1687       O  
ATOM   2534  CB  THR A 332     134.929  42.406  31.387  1.00 86.57           C  
ANISOU 2534  CB  THR A 332    11305   7233  14354   -589    818   -896       C  
ATOM   2535  OG1 THR A 332     134.842  43.729  31.932  1.00 76.71           O  
ANISOU 2535  OG1 THR A 332    10021   6481  12645   -472    664   -864       O  
ATOM   2536  CG2 THR A 332     136.364  41.908  31.486  1.00 88.49           C  
ANISOU 2536  CG2 THR A 332    11511   7198  14912   -473   1104   -727       C  
ATOM   2537  N   VAL A 333     132.476  43.644  30.651  1.00 90.34           N  
ANISOU 2537  N   VAL A 333    11938   8178  14211   -761    302  -1299       N  
ATOM   2538  CA  VAL A 333     131.045  43.946  30.679  1.00 98.65           C  
ANISOU 2538  CA  VAL A 333    12879   9494  15109   -852     47  -1320       C  
ATOM   2539  C   VAL A 333     130.562  44.370  29.298  1.00100.05           C  
ANISOU 2539  C   VAL A 333    13367   9623  15026   -962   -113  -1691       C  
ATOM   2540  O   VAL A 333     129.595  43.816  28.762  1.00 96.37           O  
ANISOU 2540  O   VAL A 333    12889   9110  14619  -1183   -257  -1805       O  
ATOM   2541  CB  VAL A 333     130.742  45.027  31.732  1.00 98.94           C  
ANISOU 2541  CB  VAL A 333    12698  10002  14894   -688    -32  -1118       C  
ATOM   2542  CG1 VAL A 333     129.315  45.532  31.577  1.00 93.09           C  
ANISOU 2542  CG1 VAL A 333    11866   9508  13997   -740   -270  -1171       C  
ATOM   2543  CG2 VAL A 333     130.958  44.480  33.125  1.00 94.64           C  
ANISOU 2543  CG2 VAL A 333    11796   9605  14558   -666     78   -724       C  
ATOM   2544  N   LEU A 334     131.228  45.361  28.703  1.00 97.27           N  
ANISOU 2544  N   LEU A 334    13282   9312  14365   -834    -95  -1865       N  
ATOM   2545  CA  LEU A 334     130.784  45.881  27.414  1.00 96.01           C  
ANISOU 2545  CA  LEU A 334    13395   9183  13902   -933   -266  -2147       C  
ATOM   2546  C   LEU A 334     130.948  44.843  26.311  1.00103.53           C  
ANISOU 2546  C   LEU A 334    14587   9787  14962  -1208   -194  -2445       C  
ATOM   2547  O   LEU A 334     130.038  44.638  25.500  1.00102.23           O  
ANISOU 2547  O   LEU A 334    14486   9690  14666  -1448   -392  -2614       O  
ATOM   2548  CB  LEU A 334     131.550  47.155  27.070  1.00 94.47           C  
ANISOU 2548  CB  LEU A 334    13426   9083  13386   -731   -223  -2229       C  
ATOM   2549  CG  LEU A 334     131.144  47.790  25.742  1.00 96.58           C  
ANISOU 2549  CG  LEU A 334    13960   9427  13310   -816   -405  -2442       C  
ATOM   2550  CD1 LEU A 334     129.649  48.064  25.721  1.00 95.55           C  
ANISOU 2550  CD1 LEU A 334    13615   9595  13096   -881   -707  -2320       C  
ATOM   2551  CD2 LEU A 334     131.925  49.063  25.507  1.00 95.73           C  
ANISOU 2551  CD2 LEU A 334    14049   9386  12937   -598   -329  -2473       C  
ATOM   2552  N   ALA A 335     132.105  44.177  26.265  1.00106.28           N  
ANISOU 2552  N   ALA A 335    15055   9771  15556  -1196    105  -2520       N  
ATOM   2553  CA  ALA A 335     132.341  43.173  25.232  1.00100.41           C  
ANISOU 2553  CA  ALA A 335    14552   8638  14961  -1469    263  -2859       C  
ATOM   2554  C   ALA A 335     131.331  42.036  25.324  1.00104.62           C  
ANISOU 2554  C   ALA A 335    14907   9054  15789  -1747    209  -2872       C  
ATOM   2555  O   ALA A 335     130.892  41.502  24.299  1.00105.89           O  
ANISOU 2555  O   ALA A 335    15257   9093  15885  -2078    182  -3220       O  
ATOM   2556  CB  ALA A 335     133.767  42.634  25.336  1.00106.76           C  
ANISOU 2556  CB  ALA A 335    15440   9035  16088  -1360    649  -2874       C  
ATOM   2557  N   ALA A 336     130.946  41.655  26.544  1.00109.97           N  
ANISOU 2557  N   ALA A 336    15217   9793  16774  -1651    198  -2504       N  
ATOM   2558  CA  ALA A 336     129.948  40.603  26.705  1.00104.05           C  
ANISOU 2558  CA  ALA A 336    14270   8936  16328  -1913    151  -2482       C  
ATOM   2559  C   ALA A 336     128.541  41.117  26.433  1.00100.24           C  
ANISOU 2559  C   ALA A 336    13699   8872  15516  -2059   -231  -2516       C  
ATOM   2560  O   ALA A 336     127.699  40.376  25.915  1.00 96.95           O  
ANISOU 2560  O   ALA A 336    13268   8387  15181  -2397   -317  -2702       O  
ATOM   2561  CB  ALA A 336     130.030  40.004  28.106  1.00 88.96           C  
ANISOU 2561  CB  ALA A 336    11980   6966  14855  -1768    279  -2029       C  
ATOM   2562  N   ALA A 337     128.264  42.376  26.786  1.00101.04           N  
ANISOU 2562  N   ALA A 337    13717   9400  15274  -1819   -444  -2334       N  
ATOM   2563  CA  ALA A 337     126.976  42.968  26.441  1.00109.97           C  
ANISOU 2563  CA  ALA A 337    14745  10923  16115  -1917   -795  -2330       C  
ATOM   2564  C   ALA A 337     126.772  42.980  24.932  1.00120.05           C  
ANISOU 2564  C   ALA A 337    16325  12209  17078  -2206   -933  -2701       C  
ATOM   2565  O   ALA A 337     125.674  42.692  24.442  1.00114.57           O  
ANISOU 2565  O   ALA A 337    15537  11698  16298  -2493  -1175  -2778       O  
ATOM   2566  CB  ALA A 337     126.875  44.383  27.012  1.00101.96           C  
ANISOU 2566  CB  ALA A 337    13616  10282  14843  -1580   -913  -2094       C  
ATOM   2567  N   LEU A 338     127.826  43.299  24.178  1.00122.97           N  
ANISOU 2567  N   LEU A 338    17049  12420  17255  -2162   -783  -2931       N  
ATOM   2568  CA  LEU A 338     127.753  43.214  22.725  1.00109.16           C  
ANISOU 2568  CA  LEU A 338    15614  10687  15176  -2486   -870  -3309       C  
ATOM   2569  C   LEU A 338     127.596  41.773  22.256  1.00111.07           C  
ANISOU 2569  C   LEU A 338    15928  10596  15679  -2917   -715  -3637       C  
ATOM   2570  O   LEU A 338     127.046  41.531  21.176  1.00115.59           O  
ANISOU 2570  O   LEU A 338    16650  11299  15971  -3315   -866  -3944       O  
ATOM   2571  CB  LEU A 338     128.998  43.843  22.103  1.00 94.56           C  
ANISOU 2571  CB  LEU A 338    14122   8719  13089  -2338   -688  -3476       C  
ATOM   2572  CG  LEU A 338     129.216  45.317  22.441  1.00 95.10           C  
ANISOU 2572  CG  LEU A 338    14160   9074  12900  -1949   -802  -3206       C  
ATOM   2573  CD1 LEU A 338     130.556  45.802  21.911  1.00104.96           C  
ANISOU 2573  CD1 LEU A 338    15752  10144  13985  -1817   -569  -3373       C  
ATOM   2574  CD2 LEU A 338     128.077  46.159  21.890  1.00 96.65           C  
ANISOU 2574  CD2 LEU A 338    14271   9729  12723  -2007  -1194  -3089       C  
ATOM   2575  N   ALA A 339     128.066  40.808  23.049  1.00108.35           N  
ANISOU 2575  N   ALA A 339    15466   9829  15871  -2866   -403  -3569       N  
ATOM   2576  CA  ALA A 339     127.929  39.404  22.676  1.00114.07           C  
ANISOU 2576  CA  ALA A 339    16241  10149  16950  -3263   -184  -3875       C  
ATOM   2577  C   ALA A 339     126.520  38.887  22.944  1.00120.19           C  
ANISOU 2577  C   ALA A 339    16719  11117  17831  -3532   -431  -3790       C  
ATOM   2578  O   ALA A 339     125.989  38.092  22.161  1.00108.49           O  
ANISOU 2578  O   ALA A 339    15330   9539  16352  -4004   -430  -4156       O  
ATOM   2579  CB  ALA A 339     128.960  38.559  23.424  1.00116.00           C  
ANISOU 2579  CB  ALA A 339    16431   9841  17804  -3083    263  -3761       C  
ATOM   2580  N   ILE A 340     125.903  39.320  24.045  1.00120.18           N  
ANISOU 2580  N   ILE A 340    16355  11398  17912  -3268   -625  -3333       N  
ATOM   2581  CA  ILE A 340     124.535  38.906  24.343  1.00127.48           C  
ANISOU 2581  CA  ILE A 340    16962  12540  18936  -3500   -865  -3217       C  
ATOM   2582  C   ILE A 340     123.555  39.613  23.418  1.00124.82           C  
ANISOU 2582  C   ILE A 340    16643  12717  18065  -3716  -1286  -3334       C  
ATOM   2583  O   ILE A 340     122.693  38.981  22.794  1.00130.94           O  
ANISOU 2583  O   ILE A 340    17379  13579  18793  -4171  -1433  -3562       O  
ATOM   2584  CB  ILE A 340     124.203  39.169  25.823  1.00124.61           C  
ANISOU 2584  CB  ILE A 340    16198  12336  18812  -3156   -904  -2696       C  
ATOM   2585  CG1 ILE A 340     124.764  38.048  26.697  1.00132.07           C  
ANISOU 2585  CG1 ILE A 340    17016  12805  20359  -3119   -540  -2538       C  
ATOM   2586  CG2 ILE A 340     122.699  39.305  26.025  1.00113.53           C  
ANISOU 2586  CG2 ILE A 340    14462  11350  17325  -3304  -1250  -2534       C  
ATOM   2587  CD1 ILE A 340     125.709  38.526  27.772  1.00128.51           C  
ANISOU 2587  CD1 ILE A 340    16466  12350  20010  -2670   -374  -2162       C  
ATOM   2588  N   LEU A 341     123.671  40.936  23.315  1.00120.81           N  
ANISOU 2588  N   LEU A 341    16173  12568  17162  -3407  -1482  -3158       N  
ATOM   2589  CA  LEU A 341     122.778  41.695  22.448  1.00122.38           C  
ANISOU 2589  CA  LEU A 341    16346  13275  16877  -3560  -1888  -3165       C  
ATOM   2590  C   LEU A 341     122.996  41.333  20.984  1.00123.34           C  
ANISOU 2590  C   LEU A 341    16828  13383  16651  -4011  -1908  -3637       C  
ATOM   2591  O   LEU A 341     122.086  40.843  20.308  1.00112.76           O  
ANISOU 2591  O   LEU A 341    15422  12269  15155  -4476  -2130  -3817       O  
ATOM   2592  CB  LEU A 341     122.983  43.193  22.675  1.00111.74           C  
ANISOU 2592  CB  LEU A 341    14971  12221  15264  -3099  -2014  -2857       C  
ATOM   2593  CG  LEU A 341     122.504  43.742  24.020  1.00107.88           C  
ANISOU 2593  CG  LEU A 341    14096  11883  15012  -2718  -2043  -2422       C  
ATOM   2594  CD1 LEU A 341     123.349  44.929  24.460  1.00106.63           C  
ANISOU 2594  CD1 LEU A 341    14031  11736  14746  -2253  -1914  -2254       C  
ATOM   2595  CD2 LEU A 341     121.039  44.135  23.928  1.00102.07           C  
ANISOU 2595  CD2 LEU A 341    13007  11609  14165  -2806  -2419  -2195       C  
ATOM   2596  N   GLY A 342     124.203  41.568  20.477  1.00127.89           N  
ANISOU 2596  N   GLY A 342    17781  13727  17084  -3911  -1668  -3854       N  
ATOM   2597  CA  GLY A 342     124.508  41.303  19.094  1.00125.90           C  
ANISOU 2597  CA  GLY A 342    17897  13482  16456  -4334  -1641  -4321       C  
ATOM   2598  C   GLY A 342     124.067  42.456  18.220  1.00126.55           C  
ANISOU 2598  C   GLY A 342    18022  14149  15911  -4353  -2039  -4197       C  
ATOM   2599  O   GLY A 342     124.172  43.626  18.605  1.00122.00           O  
ANISOU 2599  O   GLY A 342    17352  13773  15230  -3901  -2161  -3816       O  
ATOM   2600  N   PRO A 343     123.547  42.150  17.028  1.00130.56           N  
ANISOU 2600  N   PRO A 343    18655  14957  15994  -4898  -2240  -4503       N  
ATOM   2601  CA  PRO A 343     123.133  43.222  16.112  1.00130.42           C  
ANISOU 2601  CA  PRO A 343    18658  15545  15351  -4947  -2639  -4324       C  
ATOM   2602  C   PRO A 343     121.832  43.918  16.504  1.00129.23           C  
ANISOU 2602  C   PRO A 343    18033  15909  15158  -4795  -3097  -3796       C  
ATOM   2603  O   PRO A 343     121.486  44.922  15.863  1.00124.41           O  
ANISOU 2603  O   PRO A 343    17372  15786  14111  -4739  -3424  -3521       O  
ATOM   2604  CB  PRO A 343     123.003  42.499  14.766  1.00124.46           C  
ANISOU 2604  CB  PRO A 343    18169  14967  14155  -5660  -2681  -4850       C  
ATOM   2605  CG  PRO A 343     122.721  41.109  15.127  1.00126.86           C  
ANISOU 2605  CG  PRO A 343    18406  14896  14900  -6012  -2460  -5192       C  
ATOM   2606  CD  PRO A 343     123.508  40.834  16.375  1.00123.69           C  
ANISOU 2606  CD  PRO A 343    17968  13857  15171  -5513  -2050  -5065       C  
ATOM   2607  N   ARG A 344     121.112  43.455  17.537  1.00133.14           N  
ANISOU 2607  N   ARG A 344    18161  16310  16115  -4706  -3115  -3608       N  
ATOM   2608  CA  ARG A 344     120.004  44.247  18.062  1.00142.58           C  
ANISOU 2608  CA  ARG A 344    18890  17931  17351  -4448  -3471  -3071       C  
ATOM   2609  C   ARG A 344     120.483  45.366  18.986  1.00131.54           C  
ANISOU 2609  C   ARG A 344    17412  16410  16156  -3766  -3338  -2680       C  
ATOM   2610  O   ARG A 344     119.696  45.915  19.769  1.00128.58           O  
ANISOU 2610  O   ARG A 344    16639  16224  15992  -3474  -3480  -2268       O  
ATOM   2611  CB  ARG A 344     118.967  43.357  18.761  1.00152.74           C  
ANISOU 2611  CB  ARG A 344    19797  19221  19017  -4654  -3547  -3022       C  
ATOM   2612  CG  ARG A 344     119.465  42.513  19.912  1.00158.85           C  
ANISOU 2612  CG  ARG A 344    20563  19420  20373  -4497  -3142  -3116       C  
ATOM   2613  CD  ARG A 344     118.508  41.353  20.183  1.00172.41           C  
ANISOU 2613  CD  ARG A 344    22011  21117  22380  -4912  -3198  -3218       C  
ATOM   2614  NE  ARG A 344     117.126  41.808  20.305  1.00188.54           N  
ANISOU 2614  NE  ARG A 344    23588  23703  24345  -4937  -3620  -2841       N  
ATOM   2615  CZ  ARG A 344     116.081  41.018  20.535  1.00200.74           C  
ANISOU 2615  CZ  ARG A 344    24811  25364  26098  -5280  -3755  -2837       C  
ATOM   2616  NH1 ARG A 344     116.239  39.707  20.677  1.00206.48           N  
ANISOU 2616  NH1 ARG A 344    25641  25672  27141  -5640  -3490  -3198       N  
ATOM   2617  NH2 ARG A 344     114.870  41.548  20.624  1.00202.69           N  
ANISOU 2617  NH2 ARG A 344    24609  26129  26273  -5257  -4137  -2454       N  
ATOM   2618  N   VAL A 345     121.769  45.712  18.886  1.00120.53           N  
ANISOU 2618  N   VAL A 345    16388  14706  14700  -3538  -3044  -2830       N  
ATOM   2619  CA  VAL A 345     122.275  46.977  19.399  1.00110.19           C  
ANISOU 2619  CA  VAL A 345    15071  13376  13421  -2980  -2959  -2511       C  
ATOM   2620  C   VAL A 345     121.885  48.141  18.501  1.00116.67           C  
ANISOU 2620  C   VAL A 345    15868  14648  13815  -2918  -3274  -2238       C  
ATOM   2621  O   VAL A 345     122.116  49.302  18.861  1.00108.96           O  
ANISOU 2621  O   VAL A 345    14835  13682  12881  -2465  -3226  -1932       O  
ATOM   2622  CB  VAL A 345     123.810  46.894  19.541  1.00100.61           C  
ANISOU 2622  CB  VAL A 345    14251  11693  12284  -2806  -2541  -2774       C  
ATOM   2623  CG1 VAL A 345     124.488  47.040  18.185  1.00106.50           C  
ANISOU 2623  CG1 VAL A 345    15412  12490  12561  -3046  -2538  -3056       C  
ATOM   2624  CG2 VAL A 345     124.338  47.927  20.521  1.00 98.25           C  
ANISOU 2624  CG2 VAL A 345    13874  11282  12176  -2249  -2367  -2486       C  
ATOM   2625  N   ASP A 346     121.314  47.851  17.328  1.00122.32           N  
ANISOU 2625  N   ASP A 346    16617  15743  14116  -3386  -3583  -2336       N  
ATOM   2626  CA  ASP A 346     120.844  48.856  16.382  1.00119.18           C  
ANISOU 2626  CA  ASP A 346    16146  15855  13280  -3393  -3936  -2007       C  
ATOM   2627  C   ASP A 346     119.335  48.760  16.185  1.00123.43           C  
ANISOU 2627  C   ASP A 346    16218  16922  13757  -3635  -4385  -1703       C  
ATOM   2628  O   ASP A 346     118.822  49.083  15.112  1.00131.25           O  
ANISOU 2628  O   ASP A 346    17150  18433  14285  -3912  -4748  -1537       O  
ATOM   2629  CB  ASP A 346     121.552  48.714  15.034  1.00118.39           C  
ANISOU 2629  CB  ASP A 346    16491  15867  12626  -3776  -3940  -2341       C  
ATOM   2630  CG  ASP A 346     123.060  48.677  15.160  1.00116.86           C  
ANISOU 2630  CG  ASP A 346    16751  15146  12507  -3588  -3480  -2679       C  
ATOM   2631  OD1 ASP A 346     123.601  49.356  16.058  1.00108.16           O  
ANISOU 2631  OD1 ASP A 346    15618  13746  11730  -3061  -3252  -2482       O  
ATOM   2632  OD2 ASP A 346     123.703  47.968  14.358  1.00115.19           O  
ANISOU 2632  OD2 ASP A 346    16913  14827  12027  -3989  -3329  -3155       O  
ATOM   2633  N   ALA A 347     118.608  48.328  17.216  1.00124.42           N  
ANISOU 2633  N   ALA A 347    15983  16957  14335  -3544  -4372  -1596       N  
ATOM   2634  CA  ALA A 347     117.213  47.937  17.050  1.00138.59           C  
ANISOU 2634  CA  ALA A 347    17342  19208  16108  -3872  -4761  -1408       C  
ATOM   2635  C   ALA A 347     116.230  49.075  17.314  1.00155.80           C  
ANISOU 2635  C   ALA A 347    19020  21764  18412  -3491  -5033   -749       C  
ATOM   2636  O   ALA A 347     115.362  49.351  16.479  1.00162.09           O  
ANISOU 2636  O   ALA A 347    19558  23129  18901  -3727  -5460   -453       O  
ATOM   2637  CB  ALA A 347     116.897  46.752  17.968  1.00131.83           C  
ANISOU 2637  CB  ALA A 347    16346  18054  15688  -4036  -4592  -1651       C  
ATOM   2638  N   LEU A 348     116.348  49.740  18.463  1.00161.40           N  
ANISOU 2638  N   LEU A 348    19569  22178  19576  -2920  -4777   -510       N  
ATOM   2639  CA  LEU A 348     115.294  50.629  18.941  1.00158.61           C  
ANISOU 2639  CA  LEU A 348    18677  22088  19498  -2567  -4941     61       C  
ATOM   2640  C   LEU A 348     115.145  51.878  18.079  1.00153.01           C  
ANISOU 2640  C   LEU A 348    17883  21717  18538  -2364  -5171    521       C  
ATOM   2641  O   LEU A 348     114.159  52.013  17.348  1.00166.07           O  
ANISOU 2641  O   LEU A 348    19194  23913  19993  -2581  -5599    874       O  
ATOM   2642  CB  LEU A 348     115.548  51.014  20.401  1.00149.20           C  
ANISOU 2642  CB  LEU A 348    17381  20476  18832  -2052  -4537    119       C  
ATOM   2643  CG  LEU A 348     115.128  49.981  21.455  1.00154.45           C  
ANISOU 2643  CG  LEU A 348    17850  20976  19858  -2177  -4406    -55       C  
ATOM   2644  CD1 LEU A 348     116.047  48.765  21.467  1.00155.16           C  
ANISOU 2644  CD1 LEU A 348    18366  20708  19879  -2502  -4195   -595       C  
ATOM   2645  CD2 LEU A 348     115.054  50.609  22.839  1.00156.21           C  
ANISOU 2645  CD2 LEU A 348    17833  20979  20540  -1676  -4088    142       C  
ATOM   2646  N   GLY A 349     116.099  52.799  18.163  1.00135.81           N  
ANISOU 2646  N   GLY A 349    15982  19242  16378  -1958  -4893    558       N  
ATOM   2647  CA  GLY A 349     116.042  54.024  17.387  1.00133.99           C  
ANISOU 2647  CA  GLY A 349    15683  19260  15967  -1728  -5054   1026       C  
ATOM   2648  C   GLY A 349     115.597  55.217  18.216  1.00137.03           C  
ANISOU 2648  C   GLY A 349    15683  19512  16870  -1121  -4881   1508       C  
ATOM   2649  O   GLY A 349     115.273  55.118  19.403  1.00136.10           O  
ANISOU 2649  O   GLY A 349    15335  19162  17216   -896  -4648   1472       O  
ATOM   2650  N   VAL A 350     115.575  56.375  17.549  1.00140.05           N  
ANISOU 2650  N   VAL A 350    15989  20049  17175   -868  -4976   1977       N  
ATOM   2651  CA  VAL A 350     115.298  57.629  18.244  1.00141.75           C  
ANISOU 2651  CA  VAL A 350    15891  20048  17920   -268  -4724   2410       C  
ATOM   2652  C   VAL A 350     113.832  57.728  18.649  1.00155.07           C  
ANISOU 2652  C   VAL A 350    16900  22022  19999   -164  -4922   2872       C  
ATOM   2653  O   VAL A 350     113.501  58.390  19.641  1.00151.02           O  
ANISOU 2653  O   VAL A 350    16097  21239  20046    278  -4605   3044       O  
ATOM   2654  CB  VAL A 350     115.725  58.828  17.373  1.00146.35           C  
ANISOU 2654  CB  VAL A 350    16585  20666  18357    -27  -4738   2809       C  
ATOM   2655  CG1 VAL A 350     114.850  58.944  16.130  1.00156.85           C  
ANISOU 2655  CG1 VAL A 350    17599  22654  19343   -278  -5297   3363       C  
ATOM   2656  CG2 VAL A 350     115.706  60.118  18.183  1.00142.56           C  
ANISOU 2656  CG2 VAL A 350    15891  19791  18485    600  -4329   3117       C  
ATOM   2657  N   THR A 351     112.933  57.078  17.905  1.00170.43           N  
ANISOU 2657  N   THR A 351    18569  24524  21660   -589  -5424   3061       N  
ATOM   2658  CA  THR A 351     111.509  57.182  18.210  1.00180.10           C  
ANISOU 2658  CA  THR A 351    19103  26072  23255   -505  -5644   3550       C  
ATOM   2659  C   THR A 351     111.188  56.606  19.582  1.00181.30           C  
ANISOU 2659  C   THR A 351    19096  25928  23863   -419  -5349   3247       C  
ATOM   2660  O   THR A 351     110.241  57.054  20.238  1.00184.33           O  
ANISOU 2660  O   THR A 351    18940  26344  24753   -120  -5281   3623       O  
ATOM   2661  CB  THR A 351     110.685  56.472  17.137  1.00184.09           C  
ANISOU 2661  CB  THR A 351    19372  27279  23295  -1074  -6258   3740       C  
ATOM   2662  OG1 THR A 351     110.656  55.065  17.408  1.00181.50           O  
ANISOU 2662  OG1 THR A 351    19205  26956  22800  -1572  -6308   3159       O  
ATOM   2663  CG2 THR A 351     111.297  56.699  15.763  1.00185.75           C  
ANISOU 2663  CG2 THR A 351    19924  27791  22861  -1334  -6523   3814       C  
ATOM   2664  N   THR A 352     111.965  55.626  20.032  1.00178.79           N  
ANISOU 2664  N   THR A 352    19220  25320  23393   -671  -5152   2600       N  
ATOM   2665  CA  THR A 352     111.742  54.992  21.324  1.00175.78           C  
ANISOU 2665  CA  THR A 352    18716  24683  23389   -633  -4877   2322       C  
ATOM   2666  C   THR A 352     111.998  55.969  22.468  1.00169.69           C  
ANISOU 2666  C   THR A 352    17870  23489  23116    -60  -4367   2387       C  
ATOM   2667  O   THR A 352     111.140  56.174  23.326  1.00168.77           O  
ANISOU 2667  O   THR A 352    17295  23378  23452    153  -4234   2592       O  
ATOM   2668  CB  THR A 352     112.645  53.759  21.503  1.00170.86           C  
ANISOU 2668  CB  THR A 352    18596  23812  22511  -1008  -4753   1668       C  
ATOM   2669  OG1 THR A 352     113.008  53.241  20.218  1.00174.07           O  
ANISOU 2669  OG1 THR A 352    19322  24455  22362  -1461  -5070   1497       O  
ATOM   2670  CG2 THR A 352     111.918  52.678  22.286  1.00170.54           C  
ANISOU 2670  CG2 THR A 352    18288  23810  22701  -1254  -4770   1516       C  
ATOM   2671  N   ARG A 382     124.524  59.365   5.215  1.00207.80           N  
ANISOU 2671  N   ARG A 382    28986  30404  19563  -3128  -5220   1539       N  
ATOM   2672  CA  ARG A 382     125.456  60.485   5.285  1.00207.94           C  
ANISOU 2672  CA  ARG A 382    29207  30004  19797  -2642  -4875   1780       C  
ATOM   2673  C   ARG A 382     126.695  60.121   6.101  1.00203.48           C  
ANISOU 2673  C   ARG A 382    29066  28654  19593  -2442  -4301   1057       C  
ATOM   2674  O   ARG A 382     127.623  60.919   6.225  1.00198.32           O  
ANISOU 2674  O   ARG A 382    28636  27598  19119  -2090  -3955   1112       O  
ATOM   2675  CB  ARG A 382     124.775  61.715   5.888  1.00204.47           C  
ANISOU 2675  CB  ARG A 382    28275  29433  19982  -2002  -4933   2595       C  
ATOM   2676  CG  ARG A 382     124.788  62.947   4.992  1.00200.88           C  
ANISOU 2676  CG  ARG A 382    27731  29289  19303  -1843  -5071   3387       C  
ATOM   2677  CD  ARG A 382     123.822  62.806   3.825  1.00199.83           C  
ANISOU 2677  CD  ARG A 382    27313  30113  18499  -2328  -5683   3909       C  
ATOM   2678  NE  ARG A 382     123.732  64.036   3.042  1.00198.98           N  
ANISOU 2678  NE  ARG A 382    27030  30318  18254  -2122  -5837   4809       N  
ATOM   2679  CZ  ARG A 382     122.873  64.228   2.046  1.00203.45           C  
ANISOU 2679  CZ  ARG A 382    27250  31746  18306  -2430  -6382   5513       C  
ATOM   2680  NH1 ARG A 382     122.863  65.381   1.390  1.00205.55           N  
ANISOU 2680  NH1 ARG A 382    27349  32236  18513  -2194  -6479   6384       N  
ATOM   2681  NH2 ARG A 382     122.022  63.270   1.706  1.00206.37           N  
ANISOU 2681  NH2 ARG A 382    27419  32766  18225  -2989  -6832   5370       N  
ATOM   2682  N   GLU A 383     126.701  58.911   6.666  1.00200.94           N  
ANISOU 2682  N   GLU A 383    28827  28123  19398  -2674  -4198    408       N  
ATOM   2683  CA  GLU A 383     127.874  58.456   7.405  1.00183.72           C  
ANISOU 2683  CA  GLU A 383    27010  25252  17542  -2525  -3679   -243       C  
ATOM   2684  C   GLU A 383     129.054  58.197   6.478  1.00178.79           C  
ANISOU 2684  C   GLU A 383    26923  24609  16399  -2856  -3435   -687       C  
ATOM   2685  O   GLU A 383     130.210  58.283   6.909  1.00167.07           O  
ANISOU 2685  O   GLU A 383    25735  22579  15164  -2622  -2985  -1021       O  
ATOM   2686  CB  GLU A 383     127.542  57.195   8.203  1.00178.92           C  
ANISOU 2686  CB  GLU A 383    26319  24438  17224  -2698  -3635   -751       C  
ATOM   2687  CG  GLU A 383     126.936  57.467   9.570  1.00177.01           C  
ANISOU 2687  CG  GLU A 383    25671  23889  17697  -2212  -3600   -506       C  
ATOM   2688  CD  GLU A 383     126.618  56.194  10.331  1.00173.97           C  
ANISOU 2688  CD  GLU A 383    25202  23321  17578  -2405  -3557   -970       C  
ATOM   2689  OE1 GLU A 383     125.564  55.582  10.056  1.00178.18           O  
ANISOU 2689  OE1 GLU A 383    25485  24270  17944  -2754  -3916   -914       O  
ATOM   2690  OE2 GLU A 383     127.426  55.800  11.199  1.00166.07           O  
ANISOU 2690  OE2 GLU A 383    24369  21776  16956  -2221  -3165  -1365       O  
ATOM   2691  N   GLU A 384     128.787  57.884   5.211  1.00182.49           N  
ANISOU 2691  N   GLU A 384    27508  25695  16133  -3418  -3716   -698       N  
ATOM   2692  CA  GLU A 384     129.838  57.614   4.242  1.00170.13           C  
ANISOU 2692  CA  GLU A 384    26450  24177  14014  -3795  -3477  -1139       C  
ATOM   2693  C   GLU A 384     130.349  58.869   3.544  1.00172.15           C  
ANISOU 2693  C   GLU A 384    26825  24587  13998  -3596  -3454   -630       C  
ATOM   2694  O   GLU A 384     131.395  58.807   2.889  1.00166.25           O  
ANISOU 2694  O   GLU A 384    26511  23766  12889  -3796  -3164   -977       O  
ATOM   2695  CB  GLU A 384     129.342  56.616   3.188  1.00166.87           C  
ANISOU 2695  CB  GLU A 384    26138  24386  12880  -4585  -3746  -1482       C  
ATOM   2696  CG  GLU A 384     128.943  55.254   3.741  1.00160.66           C  
ANISOU 2696  CG  GLU A 384    25299  23413  12332  -4877  -3705  -2080       C  
ATOM   2697  CD  GLU A 384     130.109  54.502   4.355  1.00148.02           C  
ANISOU 2697  CD  GLU A 384    24052  21044  11143  -4779  -3118  -2805       C  
ATOM   2698  OE1 GLU A 384     130.354  54.664   5.569  1.00139.09           O  
ANISOU 2698  OE1 GLU A 384    22786  19337  10724  -4235  -2900  -2748       O  
ATOM   2699  OE2 GLU A 384     130.784  53.750   3.621  1.00149.13           O  
ANISOU 2699  OE2 GLU A 384    24590  21175  10898  -5258  -2860  -3420       O  
ATOM   2700  N   VAL A 385     129.653  59.998   3.666  1.00178.97           N  
ANISOU 2700  N   VAL A 385    27308  25634  15060  -3203  -3719    188       N  
ATOM   2701  CA  VAL A 385     130.090  61.206   2.975  1.00185.48           C  
ANISOU 2701  CA  VAL A 385    28219  26594  15661  -3015  -3693    738       C  
ATOM   2702  C   VAL A 385     131.124  61.982   3.790  1.00174.53           C  
ANISOU 2702  C   VAL A 385    26988  24444  14880  -2427  -3191    693       C  
ATOM   2703  O   VAL A 385     131.953  62.695   3.215  1.00178.77           O  
ANISOU 2703  O   VAL A 385    27786  24929  15210  -2361  -2989    834       O  
ATOM   2704  CB  VAL A 385     128.884  62.093   2.614  1.00189.74           C  
ANISOU 2704  CB  VAL A 385    28256  27690  16146  -2881  -4189   1703       C  
ATOM   2705  CG1 VAL A 385     127.780  61.255   1.984  1.00193.73           C  
ANISOU 2705  CG1 VAL A 385    28534  28964  16110  -3472  -4712   1727       C  
ATOM   2706  CG2 VAL A 385     128.369  62.850   3.829  1.00184.39           C  
ANISOU 2706  CG2 VAL A 385    27159  26543  16358  -2195  -4117   2139       C  
ATOM   2707  N   GLU A 386     131.101  61.860   5.120  1.00164.75           N  
ANISOU 2707  N   GLU A 386    25591  22643  14365  -2028  -2980    497       N  
ATOM   2708  CA  GLU A 386     132.143  62.482   5.929  1.00154.83           C  
ANISOU 2708  CA  GLU A 386    24497  20700  13631  -1558  -2490    354       C  
ATOM   2709  C   GLU A 386     133.425  61.662   5.889  1.00146.46           C  
ANISOU 2709  C   GLU A 386    23906  19313  12428  -1785  -2093   -423       C  
ATOM   2710  O   GLU A 386     134.527  62.222   5.892  1.00136.23           O  
ANISOU 2710  O   GLU A 386    22872  17670  11217  -1594  -1725   -515       O  
ATOM   2711  CB  GLU A 386     131.673  62.652   7.374  1.00147.25           C  
ANISOU 2711  CB  GLU A 386    23191  19317  13441  -1098  -2398    415       C  
ATOM   2712  CG  GLU A 386     132.621  63.481   8.232  1.00143.52           C  
ANISOU 2712  CG  GLU A 386    22819  18214  13499   -622  -1924    354       C  
ATOM   2713  CD  GLU A 386     132.503  63.169   9.712  1.00137.14           C  
ANISOU 2713  CD  GLU A 386    21811  16980  13315   -347  -1739     81       C  
ATOM   2714  OE1 GLU A 386     133.457  62.590  10.276  1.00127.46           O  
ANISOU 2714  OE1 GLU A 386    20820  15392  12217   -370  -1417   -474       O  
ATOM   2715  OE2 GLU A 386     131.457  63.497  10.311  1.00136.10           O  
ANISOU 2715  OE2 GLU A 386    21268  16897  13545   -115  -1909    445       O  
ATOM   2716  N   ARG A 387     133.294  60.333   5.854  1.00144.33           N  
ANISOU 2716  N   ARG A 387    23727  19130  11982  -2191  -2141   -976       N  
ATOM   2717  CA  ARG A 387     134.462  59.470   5.726  1.00135.18           C  
ANISOU 2717  CA  ARG A 387    22985  17663  10713  -2431  -1746  -1699       C  
ATOM   2718  C   ARG A 387     135.206  59.734   4.422  1.00128.45           C  
ANISOU 2718  C   ARG A 387    22514  17073   9219  -2743  -1645  -1755       C  
ATOM   2719  O   ARG A 387     136.420  59.517   4.344  1.00126.89           O  
ANISOU 2719  O   ARG A 387    22661  16524   9028  -2768  -1217  -2202       O  
ATOM   2720  CB  ARG A 387     134.031  58.006   5.829  1.00137.11           C  
ANISOU 2720  CB  ARG A 387    23221  17968  10905  -2842  -1821  -2229       C  
ATOM   2721  CG  ARG A 387     135.172  57.009   5.858  1.00145.37           C  
ANISOU 2721  CG  ARG A 387    24632  18598  12005  -3042  -1363  -2973       C  
ATOM   2722  CD  ARG A 387     135.101  56.091   4.657  1.00163.04           C  
ANISOU 2722  CD  ARG A 387    27133  21222  13591  -3722  -1414  -3407       C  
ATOM   2723  NE  ARG A 387     136.411  55.889   4.051  1.00174.25           N  
ANISOU 2723  NE  ARG A 387    28994  22416  14796  -3889   -960  -3870       N  
ATOM   2724  CZ  ARG A 387     136.593  55.460   2.808  1.00192.17           C  
ANISOU 2724  CZ  ARG A 387    31303  25036  16676  -4290   -895  -4055       C  
ATOM   2725  NH1 ARG A 387     137.820  55.303   2.330  1.00197.18           N  
ANISOU 2725  NH1 ARG A 387    32044  25415  17461  -4234   -434  -4312       N  
ATOM   2726  NH2 ARG A 387     135.545  55.194   2.040  1.00203.27           N  
ANISOU 2726  NH2 ARG A 387    32611  27069  17552  -4749  -1302  -3960       N  
ATOM   2727  N   GLY A 388     134.498  60.208   3.393  1.00131.99           N  
ANISOU 2727  N   GLY A 388    22882  18164   9104  -2987  -2032  -1275       N  
ATOM   2728  CA  GLY A 388     135.165  60.632   2.175  1.00132.80           C  
ANISOU 2728  CA  GLY A 388    23314  18566   8578  -3253  -1950  -1213       C  
ATOM   2729  C   GLY A 388     135.814  61.995   2.288  1.00143.41           C  
ANISOU 2729  C   GLY A 388    24686  19632  10170  -2768  -1743   -736       C  
ATOM   2730  O   GLY A 388     136.852  62.239   1.666  1.00128.63           O  
ANISOU 2730  O   GLY A 388    23170  17690   8013  -2870  -1443   -901       O  
ATOM   2731  N   PHE A 389     135.217  62.899   3.072  1.00153.65           N  
ANISOU 2731  N   PHE A 389    25609  20752  12018  -2253  -1865   -158       N  
ATOM   2732  CA  PHE A 389     135.844  64.194   3.321  1.00156.32           C  
ANISOU 2732  CA  PHE A 389    25963  20720  12711  -1776  -1598    238       C  
ATOM   2733  C   PHE A 389     137.172  64.038   4.048  1.00142.28           C  
ANISOU 2733  C   PHE A 389    24464  18274  11320  -1581  -1055   -347       C  
ATOM   2734  O   PHE A 389     138.109  64.809   3.805  1.00139.10           O  
ANISOU 2734  O   PHE A 389    24275  17650  10927  -1432   -751   -265       O  
ATOM   2735  CB  PHE A 389     134.900  65.091   4.124  1.00159.54           C  
ANISOU 2735  CB  PHE A 389    25897  21002  13716  -1278  -1769    878       C  
ATOM   2736  CG  PHE A 389     135.599  66.183   4.888  1.00156.87           C  
ANISOU 2736  CG  PHE A 389    25561  20049  13995   -748  -1361   1027       C  
ATOM   2737  CD1 PHE A 389     136.153  67.268   4.228  1.00161.85           C  
ANISOU 2737  CD1 PHE A 389    26329  20655  14512   -627  -1208   1444       C  
ATOM   2738  CD2 PHE A 389     135.695  66.127   6.270  1.00143.91           C  
ANISOU 2738  CD2 PHE A 389    23776  17874  13030   -404  -1122    747       C  
ATOM   2739  CE1 PHE A 389     136.795  68.271   4.931  1.00154.13           C  
ANISOU 2739  CE1 PHE A 389    25354  19093  14115   -180   -806   1540       C  
ATOM   2740  CE2 PHE A 389     136.334  67.128   6.978  1.00135.80           C  
ANISOU 2740  CE2 PHE A 389    22750  16315  12533     18   -734    831       C  
ATOM   2741  CZ  PHE A 389     136.885  68.200   6.308  1.00141.22           C  
ANISOU 2741  CZ  PHE A 389    23581  16944  13131    127   -567   1210       C  
ATOM   2742  N   TRP A 390     137.273  63.052   4.942  1.00132.13           N  
ANISOU 2742  N   TRP A 390    23157  16681  10367  -1586   -929   -903       N  
ATOM   2743  CA  TRP A 390     138.545  62.792   5.605  1.00121.23           C  
ANISOU 2743  CA  TRP A 390    22003  14732   9325  -1442   -441  -1435       C  
ATOM   2744  C   TRP A 390     139.596  62.317   4.611  1.00117.77           C  
ANISOU 2744  C   TRP A 390    22003  14357   8388  -1819   -183  -1868       C  
ATOM   2745  O   TRP A 390     140.752  62.750   4.668  1.00110.37           O  
ANISOU 2745  O   TRP A 390    21279  13081   7577  -1668    206  -2007       O  
ATOM   2746  CB  TRP A 390     138.353  61.770   6.725  1.00116.78           C  
ANISOU 2746  CB  TRP A 390    21281  13889   9201  -1393   -396  -1859       C  
ATOM   2747  CG  TRP A 390     137.660  62.342   7.918  1.00108.88           C  
ANISOU 2747  CG  TRP A 390    19891  12693   8785   -960   -488  -1526       C  
ATOM   2748  CD1 TRP A 390     136.382  62.094   8.325  1.00112.30           C  
ANISOU 2748  CD1 TRP A 390    19974  13337   9359   -936   -838  -1301       C  
ATOM   2749  CD2 TRP A 390     138.206  63.276   8.853  1.00102.08           C  
ANISOU 2749  CD2 TRP A 390    18948  11397   8440   -516   -196  -1405       C  
ATOM   2750  NE1 TRP A 390     136.101  62.811   9.464  1.00107.07           N  
ANISOU 2750  NE1 TRP A 390    19021  12384   9277   -492   -759  -1056       N  
ATOM   2751  CE2 TRP A 390     137.205  63.546   9.808  1.00 99.85           C  
ANISOU 2751  CE2 TRP A 390    18272  11076   8589   -245   -364  -1133       C  
ATOM   2752  CE3 TRP A 390     139.446  63.909   8.979  1.00 99.85           C  
ANISOU 2752  CE3 TRP A 390    18880  10767   8292   -351    206  -1524       C  
ATOM   2753  CZ2 TRP A 390     137.406  64.420  10.873  1.00102.94           C  
ANISOU 2753  CZ2 TRP A 390    18499  11095   9519    160   -121  -1014       C  
ATOM   2754  CZ3 TRP A 390     139.643  64.775  10.035  1.00102.62           C  
ANISOU 2754  CZ3 TRP A 390    19058  10760   9172     40    420  -1395       C  
ATOM   2755  CH2 TRP A 390     138.629  65.024  10.969  1.00101.68           C  
ANISOU 2755  CH2 TRP A 390    18566  10612   9457    282    267  -1160       C  
ATOM   2756  N   GLY A 391     139.211  61.436   3.687  1.00128.24           N  
ANISOU 2756  N   GLY A 391    23462  16123   9142  -2335   -374  -2103       N  
ATOM   2757  CA  GLY A 391     140.146  60.999   2.665  1.00130.97           C  
ANISOU 2757  CA  GLY A 391    24227  16564   8971  -2738   -102  -2534       C  
ATOM   2758  C   GLY A 391     140.614  62.134   1.773  1.00131.73           C  
ANISOU 2758  C   GLY A 391    24496  16871   8687  -2715    -51  -2109       C  
ATOM   2759  O   GLY A 391     141.788  62.199   1.402  1.00143.02           O  
ANISOU 2759  O   GLY A 391    26242  18093  10004  -2775    352  -2401       O  
ATOM   2760  N   ARG A 392     139.705  63.050   1.426  1.00126.41           N  
ANISOU 2760  N   ARG A 392    23589  16599   7841  -2617   -443  -1376       N  
ATOM   2761  CA  ARG A 392     140.073  64.155   0.545  1.00136.09           C  
ANISOU 2761  CA  ARG A 392    24946  18048   8715  -2597   -414   -874       C  
ATOM   2762  C   ARG A 392     141.028  65.124   1.231  1.00133.79           C  
ANISOU 2762  C   ARG A 392    24693  17140   9001  -2091     -8   -762       C  
ATOM   2763  O   ARG A 392     141.960  65.633   0.600  1.00124.34           O  
ANISOU 2763  O   ARG A 392    23773  15902   7570  -2143    272   -745       O  
ATOM   2764  CB  ARG A 392     138.823  64.893   0.065  1.00147.71           C  
ANISOU 2764  CB  ARG A 392    26092  20081   9949  -2579   -935    -34       C  
ATOM   2765  CG  ARG A 392     137.870  64.044  -0.756  1.00166.82           C  
ANISOU 2765  CG  ARG A 392    28458  23238  11689  -3150  -1381    -77       C  
ATOM   2766  CD  ARG A 392     137.157  64.875  -1.813  1.00182.18           C  
ANISOU 2766  CD  ARG A 392    30245  25902  13074  -3303  -1799    765       C  
ATOM   2767  NE  ARG A 392     136.629  66.124  -1.272  1.00190.55           N  
ANISOU 2767  NE  ARG A 392    30919  26769  14713  -2711  -1926   1604       N  
ATOM   2768  CZ  ARG A 392     135.429  66.251  -0.715  1.00197.75           C  
ANISOU 2768  CZ  ARG A 392    31365  27786  15984  -2487  -2291   2043       C  
ATOM   2769  NH1 ARG A 392     134.624  65.200  -0.619  1.00199.26           N  
ANISOU 2769  NH1 ARG A 392    31417  28299  15993  -2816  -2599   1734       N  
ATOM   2770  NH2 ARG A 392     135.032  67.428  -0.252  1.00201.50           N  
ANISOU 2770  NH2 ARG A 392    31506  28020  17034  -1940  -2317   2780       N  
ATOM   2771  N   LEU A 393     140.813  65.393   2.521  1.00135.91           N  
ANISOU 2771  N   LEU A 393    24686  16946  10007  -1632     43   -701       N  
ATOM   2772  CA  LEU A 393     141.668  66.341   3.228  1.00131.28           C  
ANISOU 2772  CA  LEU A 393    24113  15800   9967  -1195    428   -619       C  
ATOM   2773  C   LEU A 393     143.081  65.795   3.395  1.00126.32           C  
ANISOU 2773  C   LEU A 393    23802  14795   9400  -1281    902  -1290       C  
ATOM   2774  O   LEU A 393     144.061  66.532   3.240  1.00117.75           O  
ANISOU 2774  O   LEU A 393    22892  13468   8380  -1159   1236  -1247       O  
ATOM   2775  CB  LEU A 393     141.052  66.688   4.584  1.00120.10           C  
ANISOU 2775  CB  LEU A 393    22322  14037   9275   -753    378   -456       C  
ATOM   2776  CG  LEU A 393     141.654  67.845   5.388  1.00127.93           C  
ANISOU 2776  CG  LEU A 393    23246  14499  10860   -306    727   -286       C  
ATOM   2777  CD1 LEU A 393     140.573  68.527   6.208  1.00131.89           C  
ANISOU 2777  CD1 LEU A 393    23335  14898  11880     60    553    174       C  
ATOM   2778  CD2 LEU A 393     142.772  67.365   6.301  1.00130.75           C  
ANISOU 2778  CD2 LEU A 393    23728  14391  11559   -238   1127   -921       C  
ATOM   2779  N   VAL A 394     143.205  64.504   3.707  1.00130.25           N  
ANISOU 2779  N   VAL A 394    24353  15225   9911  -1488    954  -1891       N  
ATOM   2780  CA  VAL A 394     144.520  63.913   3.929  1.00127.25           C  
ANISOU 2780  CA  VAL A 394    24210  14464   9675  -1539   1416  -2493       C  
ATOM   2781  C   VAL A 394     145.316  63.873   2.632  1.00126.91           C  
ANISOU 2781  C   VAL A 394    24550  14631   9040  -1894   1629  -2658       C  
ATOM   2782  O   VAL A 394     146.539  64.064   2.630  1.00114.34           O  
ANISOU 2782  O   VAL A 394    22885  12759   7800  -1783   1991  -2782       O  
ATOM   2783  CB  VAL A 394     144.366  62.517   4.554  1.00127.98           C  
ANISOU 2783  CB  VAL A 394    24157  14432  10037  -1653   1410  -2994       C  
ATOM   2784  CG1 VAL A 394     145.720  61.871   4.769  1.00134.30           C  
ANISOU 2784  CG1 VAL A 394    24597  14963  11469  -1584   1770  -3271       C  
ATOM   2785  CG2 VAL A 394     143.627  62.634   5.862  1.00123.66           C  
ANISOU 2785  CG2 VAL A 394    23300  13685  10000  -1314   1235  -2833       C  
ATOM   2786  N   ASN A 395     144.639  63.632   1.507  1.00138.86           N  
ANISOU 2786  N   ASN A 395    26166  16710   9884  -2297   1343  -2537       N  
ATOM   2787  CA  ASN A 395     145.322  63.663   0.218  1.00141.88           C  
ANISOU 2787  CA  ASN A 395    26713  17376   9821  -2622   1501  -2593       C  
ATOM   2788  C   ASN A 395     145.824  65.061  -0.116  1.00144.70           C  
ANISOU 2788  C   ASN A 395    27330  17696   9954  -2445   1654  -2126       C  
ATOM   2789  O   ASN A 395     146.855  65.202  -0.782  1.00149.62           O  
ANISOU 2789  O   ASN A 395    28042  18282  10523  -2550   1962  -2254       O  
ATOM   2790  CB  ASN A 395     144.396  63.148  -0.883  1.00140.81           C  
ANISOU 2790  CB  ASN A 395    26589  17930   8982  -3121   1129  -2532       C  
ATOM   2791  CG  ASN A 395     144.138  61.658  -0.777  1.00141.01           C  
ANISOU 2791  CG  ASN A 395    26341  17953   9284  -3342   1100  -3069       C  
ATOM   2792  OD1 ASN A 395     143.001  61.200  -0.892  1.00139.55           O  
ANISOU 2792  OD1 ASN A 395    26075  18146   8801  -3581    717  -3021       O  
ATOM   2793  ND2 ASN A 395     145.199  60.891  -0.552  1.00138.20           N  
ANISOU 2793  ND2 ASN A 395    25813  17176   9522  -3253   1500  -3521       N  
ATOM   2794  N   VAL A 396     145.118  66.102   0.334  1.00137.30           N  
ANISOU 2794  N   VAL A 396    26103  16740   9326  -2074   1400  -1464       N  
ATOM   2795  CA  VAL A 396     145.619  67.461   0.158  1.00132.34           C  
ANISOU 2795  CA  VAL A 396    25505  15956   8821  -1807   1574   -959       C  
ATOM   2796  C   VAL A 396     146.820  67.702   1.061  1.00126.49           C  
ANISOU 2796  C   VAL A 396    24822  14557   8680  -1503   2063  -1309       C  
ATOM   2797  O   VAL A 396     147.810  68.322   0.651  1.00125.41           O  
ANISOU 2797  O   VAL A 396    24894  14274   8480  -1492   2400  -1278       O  
ATOM   2798  CB  VAL A 396     144.501  68.487   0.422  1.00133.72           C  
ANISOU 2798  CB  VAL A 396    25325  16230   9252  -1482   1219   -160       C  
ATOM   2799  CG1 VAL A 396     145.033  69.902   0.266  1.00140.09           C  
ANISOU 2799  CG1 VAL A 396    26159  16798  10273  -1198   1457    359       C  
ATOM   2800  CG2 VAL A 396     143.335  68.256  -0.520  1.00145.76           C  
ANISOU 2800  CG2 VAL A 396    26750  18480  10152  -1807    707    247       C  
ATOM   2801  N   VAL A 397     146.756  67.215   2.302  1.00119.13           N  
ANISOU 2801  N   VAL A 397    23689  13257   8319  -1274   2102  -1629       N  
ATOM   2802  CA  VAL A 397     147.874  67.379   3.227  1.00109.47           C  
ANISOU 2802  CA  VAL A 397    22473  11481   7641  -1024   2528  -1956       C  
ATOM   2803  C   VAL A 397     149.099  66.632   2.715  1.00120.73           C  
ANISOU 2803  C   VAL A 397    23953  12869   9051  -1271   2824  -2413       C  
ATOM   2804  O   VAL A 397     150.192  67.198   2.613  1.00128.25           O  
ANISOU 2804  O   VAL A 397    24899  13611  10220  -1196   3130  -2393       O  
ATOM   2805  CB  VAL A 397     147.475  66.916   4.640  1.00111.52           C  
ANISOU 2805  CB  VAL A 397    22429  11461   8482   -778   2451  -2155       C  
ATOM   2806  CG1 VAL A 397     148.666  66.999   5.576  1.00110.21           C  
ANISOU 2806  CG1 VAL A 397    22052  10871   8951   -581   2797  -2399       C  
ATOM   2807  CG2 VAL A 397     146.327  67.760   5.168  1.00105.75           C  
ANISOU 2807  CG2 VAL A 397    21386  10758   8037   -488   2152  -1608       C  
ATOM   2808  N   MET A 398     148.932  65.354   2.366  1.00125.13           N  
ANISOU 2808  N   MET A 398    24304  13659   9583  -1543   2675  -2712       N  
ATOM   2809  CA  MET A 398     150.065  64.567   1.888  1.00118.11           C  
ANISOU 2809  CA  MET A 398    23188  12752   8935  -1708   2899  -3012       C  
ATOM   2810  C   MET A 398     150.588  65.052   0.542  1.00122.36           C  
ANISOU 2810  C   MET A 398    24049  13520   8920  -1967   3054  -2942       C  
ATOM   2811  O   MET A 398     151.710  64.698   0.165  1.00125.23           O  
ANISOU 2811  O   MET A 398    24286  13794   9501  -2044   3315  -3143       O  
ATOM   2812  CB  MET A 398     149.685  63.085   1.798  1.00119.08           C  
ANISOU 2812  CB  MET A 398    23066  13036   9141  -1917   2759  -3340       C  
ATOM   2813  CG  MET A 398     149.526  62.401   3.151  1.00106.37           C  
ANISOU 2813  CG  MET A 398    21032  11183   8199  -1662   2681  -3430       C  
ATOM   2814  SD  MET A 398     149.325  60.618   3.029  1.00104.56           S  
ANISOU 2814  SD  MET A 398    20530  11053   8145  -1875   2629  -3807       S  
ATOM   2815  CE  MET A 398     147.766  60.521   2.159  1.00109.51           C  
ANISOU 2815  CE  MET A 398    21496  12127   7986  -2243   2280  -3813       C  
ATOM   2816  N   LYS A 399     149.810  65.855  -0.186  1.00139.66           N  
ANISOU 2816  N   LYS A 399    26632  16049  10385  -2099   2887  -2596       N  
ATOM   2817  CA  LYS A 399     150.256  66.348  -1.485  1.00152.93           C  
ANISOU 2817  CA  LYS A 399    28575  18036  11496  -2363   3003  -2443       C  
ATOM   2818  C   LYS A 399     151.226  67.513  -1.335  1.00149.42           C  
ANISOU 2818  C   LYS A 399    28272  17250  11252  -2119   3345  -2224       C  
ATOM   2819  O   LYS A 399     152.224  67.592  -2.061  1.00143.39           O  
ANISOU 2819  O   LYS A 399    27545  16496  10440  -2263   3602  -2325       O  
ATOM   2820  CB  LYS A 399     149.052  66.764  -2.327  1.00154.92           C  
ANISOU 2820  CB  LYS A 399    29079  18893  10889  -2611   2627  -1987       C  
ATOM   2821  CG  LYS A 399     149.303  66.789  -3.821  1.00166.85           C  
ANISOU 2821  CG  LYS A 399    30714  20925  11756  -3026   2629  -1908       C  
ATOM   2822  CD  LYS A 399     148.248  65.970  -4.545  1.00180.71           C  
ANISOU 2822  CD  LYS A 399    32386  23306  12968  -3441   2225  -1957       C  
ATOM   2823  CE  LYS A 399     146.848  66.352  -4.089  1.00184.38           C  
ANISOU 2823  CE  LYS A 399    32852  24018  13186  -3349   1757  -1445       C  
ATOM   2824  NZ  LYS A 399     145.809  65.449  -4.653  1.00195.32           N  
ANISOU 2824  NZ  LYS A 399    34074  25993  14145  -3758   1343  -1547       N  
ATOM   2825  N   ARG A 400     150.945  68.425  -0.407  1.00142.66           N  
ANISOU 2825  N   ARG A 400    27499  16080  10627  -1753   3380  -1935       N  
ATOM   2826  CA  ARG A 400     151.823  69.554  -0.100  1.00139.53           C  
ANISOU 2826  CA  ARG A 400    27208  15291  10518  -1495   3744  -1752       C  
ATOM   2827  C   ARG A 400     152.028  69.594   1.409  1.00143.10           C  
ANISOU 2827  C   ARG A 400    27351  15239  11780  -1130   3829  -1927       C  
ATOM   2828  O   ARG A 400     151.521  70.484   2.101  1.00137.12           O  
ANISOU 2828  O   ARG A 400    26574  14271  11254   -825   3811  -1609       O  
ATOM   2829  CB  ARG A 400     151.232  70.861  -0.628  1.00142.45           C  
ANISOU 2829  CB  ARG A 400    27690  15833  10600  -1393   3628  -1000       C  
ATOM   2830  CG  ARG A 400     152.236  71.988  -0.791  1.00146.68           C  
ANISOU 2830  CG  ARG A 400    28343  16068  11320  -1260   4028   -780       C  
ATOM   2831  CD  ARG A 400     151.760  73.020  -1.810  1.00160.59           C  
ANISOU 2831  CD  ARG A 400    30149  18157  12713  -1302   3872      2       C  
ATOM   2832  NE  ARG A 400     150.328  73.294  -1.706  1.00173.43           N  
ANISOU 2832  NE  ARG A 400    31492  20023  14381  -1157   3386    573       N  
ATOM   2833  CZ  ARG A 400     149.418  72.870  -2.579  1.00187.05           C  
ANISOU 2833  CZ  ARG A 400    33216  22383  15471  -1441   2967    846       C  
ATOM   2834  NH1 ARG A 400     149.788  72.150  -3.630  1.00190.97           N  
ANISOU 2834  NH1 ARG A 400    34011  23340  15210  -1915   2995    555       N  
ATOM   2835  NH2 ARG A 400     148.137  73.165  -2.402  1.00191.45           N  
ANISOU 2835  NH2 ARG A 400    33461  23133  16148  -1274   2535   1400       N  
ATOM   2836  N   PRO A 401     152.778  68.630   1.953  1.00122.34           N  
ANISOU 2836  N   PRO A 401    20073  14358  12055   4504   2449   1396       N  
ATOM   2837  CA  PRO A 401     152.826  68.488   3.419  1.00111.06           C  
ANISOU 2837  CA  PRO A 401    18347  12908  10944   4290   2352   1377       C  
ATOM   2838  C   PRO A 401     153.647  69.555   4.117  1.00109.28           C  
ANISOU 2838  C   PRO A 401    18087  12543  10891   4152   2581   1515       C  
ATOM   2839  O   PRO A 401     153.264  70.001   5.206  1.00 96.30           O  
ANISOU 2839  O   PRO A 401    16306  10884   9399   4050   2483   1541       O  
ATOM   2840  CB  PRO A 401     153.423  67.086   3.608  1.00102.30           C  
ANISOU 2840  CB  PRO A 401    17061  11811   9996   4184   2315   1245       C  
ATOM   2841  CG  PRO A 401     154.206  66.840   2.363  1.00 98.06           C  
ANISOU 2841  CG  PRO A 401    16717  11248   9293   4303   2525   1243       C  
ATOM   2842  CD  PRO A 401     153.516  67.561   1.256  1.00111.08           C  
ANISOU 2842  CD  PRO A 401    18660  12936  10609   4512   2532   1300       C  
ATOM   2843  N   ILE A 402     154.770  69.977   3.531  1.00127.86           N  
ANISOU 2843  N   ILE A 402    20562  14803  13217   4126   2890   1595       N  
ATOM   2844  CA  ILE A 402     155.589  71.009   4.163  1.00121.46           C  
ANISOU 2844  CA  ILE A 402    19727  13867  12555   3946   3123   1712       C  
ATOM   2845  C   ILE A 402     154.809  72.311   4.289  1.00105.14           C  
ANISOU 2845  C   ILE A 402    17885  11709  10355   4021   3113   1828       C  
ATOM   2846  O   ILE A 402     155.060  73.111   5.199  1.00105.87           O  
ANISOU 2846  O   ILE A 402    17928  11698  10599   3857   3191   1895       O  
ATOM   2847  CB  ILE A 402     156.905  71.196   3.381  1.00118.49           C  
ANISOU 2847  CB  ILE A 402    19444  13441  12134   3892   3470   1767       C  
ATOM   2848  CG1 ILE A 402     157.685  69.881   3.335  1.00106.75           C  
ANISOU 2848  CG1 ILE A 402    17722  12060  10780   3859   3474   1647       C  
ATOM   2849  CG2 ILE A 402     157.765  72.284   4.010  1.00106.76           C  
ANISOU 2849  CG2 ILE A 402    17935  11841  10787   3653   3722   1875       C  
ATOM   2850  CD1 ILE A 402     159.023  69.990   2.635  1.00107.28           C  
ANISOU 2850  CD1 ILE A 402    17817  12132  10813   3809   3818   1686       C  
ATOM   2851  N   ALA A 403     153.834  72.535   3.405  1.00107.53           N  
ANISOU 2851  N   ALA A 403    18443  12054  10360   4286   3009   1847       N  
ATOM   2852  CA  ALA A 403     152.996  73.724   3.509  1.00114.04           C  
ANISOU 2852  CA  ALA A 403    19496  12807  11026   4427   2977   1955       C  
ATOM   2853  C   ALA A 403     152.061  73.673   4.711  1.00109.00           C  
ANISOU 2853  C   ALA A 403    18630  12252  10535   4398   2702   1901       C  
ATOM   2854  O   ALA A 403     151.514  74.712   5.097  1.00107.20           O  
ANISOU 2854  O   ALA A 403    18548  11947  10238   4481   2696   1989       O  
ATOM   2855  CB  ALA A 403     152.185  73.915   2.227  1.00112.84           C  
ANISOU 2855  CB  ALA A 403    19657  12723  10492   4759   2917   1983       C  
ATOM   2856  N   PHE A 404     151.861  72.499   5.305  1.00117.34           N  
ANISOU 2856  N   PHE A 404    19356  13453  11775   4289   2486   1760       N  
ATOM   2857  CA  PHE A 404     151.057  72.347   6.514  1.00113.80           C  
ANISOU 2857  CA  PHE A 404    18661  13093  11483   4219   2242   1703       C  
ATOM   2858  C   PHE A 404     151.890  72.125   7.766  1.00106.79           C  
ANISOU 2858  C   PHE A 404    17504  12130  10941   3925   2297   1685       C  
ATOM   2859  O   PHE A 404     151.562  72.670   8.822  1.00100.59           O  
ANISOU 2859  O   PHE A 404    16625  11316  10277   3846   2234   1711       O  
ATOM   2860  CB  PHE A 404     150.074  71.179   6.358  1.00112.66           C  
ANISOU 2860  CB  PHE A 404    18355  13178  11274   4291   1938   1552       C  
ATOM   2861  CG  PHE A 404     148.968  71.442   5.378  1.00108.79           C  
ANISOU 2861  CG  PHE A 404    18059  12838  10438   4585   1805   1549       C  
ATOM   2862  CD1 PHE A 404     149.127  71.140   4.035  1.00114.37           C  
ANISOU 2862  CD1 PHE A 404    18973  13574  10910   4735   1868   1534       C  
ATOM   2863  CD2 PHE A 404     147.766  71.987   5.801  1.00 96.26           C  
ANISOU 2863  CD2 PHE A 404    16440  11389   8746   4729   1614   1557       C  
ATOM   2864  CE1 PHE A 404     148.109  71.380   3.129  1.00109.58           C  
ANISOU 2864  CE1 PHE A 404    18539  13133   9965   5019   1731   1526       C  
ATOM   2865  CE2 PHE A 404     146.744  72.230   4.900  1.00108.88           C  
ANISOU 2865  CE2 PHE A 404    18191  13172  10006   5028   1478   1549       C  
ATOM   2866  CZ  PHE A 404     146.917  71.926   3.562  1.00108.60           C  
ANISOU 2866  CZ  PHE A 404    18362  13166   9734   5170   1531   1534       C  
ATOM   2867  N   ALA A 405     152.964  71.339   7.671  1.00105.58           N  
ANISOU 2867  N   ALA A 405    17223  11958  10935   3780   2411   1638       N  
ATOM   2868  CA  ALA A 405     153.773  71.039   8.847  1.00101.48           C  
ANISOU 2868  CA  ALA A 405    16425  11407  10726   3528   2443   1613       C  
ATOM   2869  C   ALA A 405     154.534  72.269   9.326  1.00115.66           C  
ANISOU 2869  C   ALA A 405    18284  13053  12607   3378   2680   1726       C  
ATOM   2870  O   ALA A 405     154.508  72.601  10.516  1.00117.43           O  
ANISOU 2870  O   ALA A 405    18356  13251  13013   3226   2625   1731       O  
ATOM   2871  CB  ALA A 405     154.740  69.896   8.539  1.00 97.40           C  
ANISOU 2871  CB  ALA A 405    15771  10929  10307   3468   2511   1535       C  
ATOM   2872  N   ALA A 406     155.213  72.961   8.409  1.00123.53           N  
ANISOU 2872  N   ALA A 406    19523  13950  13464   3400   2952   1813       N  
ATOM   2873  CA  ALA A 406     156.062  74.085   8.804  1.00118.50           C  
ANISOU 2873  CA  ALA A 406    18963  13162  12901   3198   3210   1909       C  
ATOM   2874  C   ALA A 406     155.291  75.212   9.483  1.00112.55           C  
ANISOU 2874  C   ALA A 406    18366  12287  12110   3212   3158   1979       C  
ATOM   2875  O   ALA A 406     155.704  75.632  10.577  1.00109.01           O  
ANISOU 2875  O   ALA A 406    17781  11780  11857   2984   3195   1982       O  
ATOM   2876  CB  ALA A 406     156.847  74.590   7.588  1.00113.08           C  
ANISOU 2876  CB  ALA A 406    18545  12391  12032   3216   3523   1991       C  
ATOM   2877  N   PRO A 407     154.194  75.743   8.926  1.00111.34           N  
ANISOU 2877  N   PRO A 407    18496  12103  11707   3480   3070   2032       N  
ATOM   2878  CA  PRO A 407     153.498  76.836   9.629  1.00106.92           C  
ANISOU 2878  CA  PRO A 407    18094  11425  11107   3524   3032   2097       C  
ATOM   2879  C   PRO A 407     152.890  76.411  10.953  1.00106.23           C  
ANISOU 2879  C   PRO A 407    17690  11451  11223   3453   2773   2012       C  
ATOM   2880  O   PRO A 407     152.823  77.222  11.884  1.00104.87           O  
ANISOU 2880  O   PRO A 407    17550  11166  11131   3354   2798   2047       O  
ATOM   2881  CB  PRO A 407     152.414  77.270   8.630  1.00 97.35           C  
ANISOU 2881  CB  PRO A 407    17213  10222   9553   3896   2961   2158       C  
ATOM   2882  CG  PRO A 407     152.856  76.729   7.313  1.00111.44           C  
ANISOU 2882  CG  PRO A 407    19099  12053  11189   3981   3066   2157       C  
ATOM   2883  CD  PRO A 407     153.552  75.448   7.632  1.00102.97           C  
ANISOU 2883  CD  PRO A 407    17639  11119  10365   3776   3010   2036       C  
ATOM   2884  N   ILE A 408     152.452  75.158  11.067  1.00112.18           N  
ANISOU 2884  N   ILE A 408    18157  12413  12052   3490   2535   1899       N  
ATOM   2885  CA  ILE A 408     151.795  74.705  12.289  1.00109.14           C  
ANISOU 2885  CA  ILE A 408    17487  12145  11835   3423   2290   1821       C  
ATOM   2886  C   ILE A 408     152.802  74.575  13.425  1.00 99.76           C  
ANISOU 2886  C   ILE A 408    16057  10904  10945   3110   2363   1798       C  
ATOM   2887  O   ILE A 408     152.559  75.037  14.546  1.00101.97           O  
ANISOU 2887  O   ILE A 408    16255  11152  11338   3013   2302   1800       O  
ATOM   2888  CB  ILE A 408     151.050  73.382  12.033  1.00101.91           C  
ANISOU 2888  CB  ILE A 408    16375  11452  10894   3518   2032   1705       C  
ATOM   2889  CG1 ILE A 408     149.662  73.663  11.450  1.00 99.07           C  
ANISOU 2889  CG1 ILE A 408    16162  11220  10260   3813   1865   1707       C  
ATOM   2890  CG2 ILE A 408     150.962  72.549  13.306  1.00 83.25           C  
ANISOU 2890  CG2 ILE A 408    13668   9182   8782   3327   1854   1615       C  
ATOM   2891  CD1 ILE A 408     148.924  72.423  11.005  1.00 95.47           C  
ANISOU 2891  CD1 ILE A 408    15552  10991   9729   3883   1631   1583       C  
ATOM   2892  N   LEU A 409     153.955  73.956  13.155  1.00 84.96           N  
ANISOU 2892  N   LEU A 409    14059   9035   9185   2963   2495   1771       N  
ATOM   2893  CA  LEU A 409     154.903  73.706  14.234  1.00101.37           C  
ANISOU 2893  CA  LEU A 409    15863  11122  11533   2693   2535   1736       C  
ATOM   2894  C   LEU A 409     155.637  74.970  14.672  1.00113.35           C  
ANISOU 2894  C   LEU A 409    17492  12480  13095   2495   2763   1810       C  
ATOM   2895  O   LEU A 409     156.109  75.026  15.811  1.00120.79           O  
ANISOU 2895  O   LEU A 409    18224  13434  14237   2280   2747   1779       O  
ATOM   2896  CB  LEU A 409     155.897  72.611  13.829  1.00102.07           C  
ANISOU 2896  CB  LEU A 409    15765  11302  11714   2637   2595   1677       C  
ATOM   2897  CG  LEU A 409     156.893  72.817  12.686  1.00110.81           C  
ANISOU 2897  CG  LEU A 409    17011  12370  12720   2636   2871   1720       C  
ATOM   2898  CD1 LEU A 409     158.182  73.458  13.179  1.00121.68           C  
ANISOU 2898  CD1 LEU A 409    18285  13712  14237   2364   3110   1751       C  
ATOM   2899  CD2 LEU A 409     157.183  71.486  12.004  1.00106.86           C  
ANISOU 2899  CD2 LEU A 409    16401  11990  12210   2748   2823   1643       C  
ATOM   2900  N   VAL A 410     155.746  75.981  13.808  1.00115.46           N  
ANISOU 2900  N   VAL A 410    18106  12595  13170   2551   2977   1903       N  
ATOM   2901  CA  VAL A 410     156.370  77.227  14.248  1.00121.11           C  
ANISOU 2901  CA  VAL A 410    18981  13127  13910   2332   3199   1967       C  
ATOM   2902  C   VAL A 410     155.384  78.075  15.046  1.00119.31           C  
ANISOU 2902  C   VAL A 410    18906  12788  13639   2402   3085   1996       C  
ATOM   2903  O   VAL A 410     155.791  78.830  15.936  1.00131.31           O  
ANISOU 2903  O   VAL A 410    20441  14192  15258   2177   3174   2002       O  
ATOM   2904  CB  VAL A 410     156.951  78.011  13.057  1.00127.19           C  
ANISOU 2904  CB  VAL A 410    20100  13744  14483   2328   3506   2063       C  
ATOM   2905  CG1 VAL A 410     157.987  77.171  12.321  1.00133.59           C  
ANISOU 2905  CG1 VAL A 410    20730  14691  15337   2255   3635   2027       C  
ATOM   2906  CG2 VAL A 410     155.848  78.471  12.115  1.00123.05           C  
ANISOU 2906  CG2 VAL A 410    19960  13128  13664   2673   3466   2141       C  
ATOM   2907  N   VAL A 411     154.086  77.969  14.752  1.00101.75           N  
ANISOU 2907  N   VAL A 411    16790  10614  11255   2715   2889   2003       N  
ATOM   2908  CA  VAL A 411     153.087  78.666  15.555  1.00 93.82           C  
ANISOU 2908  CA  VAL A 411    15885   9557  10207   2824   2760   2018       C  
ATOM   2909  C   VAL A 411     153.023  78.069  16.955  1.00 99.97           C  
ANISOU 2909  C   VAL A 411    16285  10463  11235   2653   2571   1926       C  
ATOM   2910  O   VAL A 411     152.906  78.794  17.952  1.00 93.57           O  
ANISOU 2910  O   VAL A 411    15510   9557  10485   2555   2572   1930       O  
ATOM   2911  CB  VAL A 411     151.716  78.627  14.853  1.00 89.35           C  
ANISOU 2911  CB  VAL A 411    15473   9085   9392   3218   2588   2037       C  
ATOM   2912  CG1 VAL A 411     150.601  78.975  15.827  1.00 87.23           C  
ANISOU 2912  CG1 VAL A 411    15160   8872   9113   3347   2392   2016       C  
ATOM   2913  CG2 VAL A 411     151.702  79.587  13.681  1.00 95.09           C  
ANISOU 2913  CG2 VAL A 411    16666   9628   9837   3411   2791   2154       C  
ATOM   2914  N   MET A 412     153.117  76.742  17.054  1.00106.03           N  
ANISOU 2914  N   MET A 412    16715  11433  12138   2617   2413   1842       N  
ATOM   2915  CA  MET A 412     153.085  76.089  18.357  1.00109.16           C  
ANISOU 2915  CA  MET A 412    16772  11947  12758   2462   2237   1762       C  
ATOM   2916  C   MET A 412     154.303  76.443  19.200  1.00119.96           C  
ANISOU 2916  C   MET A 412    18021  13237  14319   2144   2385   1755       C  
ATOM   2917  O   MET A 412     154.194  76.544  20.427  1.00117.31           O  
ANISOU 2917  O   MET A 412    17536  12920  14116   2019   2287   1719       O  
ATOM   2918  CB  MET A 412     152.985  74.576  18.180  1.00104.50           C  
ANISOU 2918  CB  MET A 412    15912  11550  12243   2496   2062   1681       C  
ATOM   2919  CG  MET A 412     151.638  74.111  17.664  1.00 96.90           C  
ANISOU 2919  CG  MET A 412    14987  10719  11112   2750   1858   1654       C  
ATOM   2920  SD  MET A 412     151.500  72.320  17.606  1.00 86.97           S  
ANISOU 2920  SD  MET A 412    13452   9649   9944   2727   1655   1543       S  
ATOM   2921  CE  MET A 412     149.739  72.154  17.358  1.00 93.91           C  
ANISOU 2921  CE  MET A 412    14359  10704  10619   2952   1411   1502       C  
ATOM   2922  N   VAL A 413     155.463  76.635  18.569  1.00123.37           N  
ANISOU 2922  N   VAL A 413    18507  13608  14761   2003   2619   1781       N  
ATOM   2923  CA  VAL A 413     156.652  77.026  19.320  1.00116.32           C  
ANISOU 2923  CA  VAL A 413    17481  12684  14031   1678   2767   1762       C  
ATOM   2924  C   VAL A 413     156.483  78.430  19.890  1.00110.40           C  
ANISOU 2924  C   VAL A 413    16994  11727  13226   1567   2872   1805       C  
ATOM   2925  O   VAL A 413     156.866  78.700  21.035  1.00100.54           O  
ANISOU 2925  O   VAL A 413    15602  10478  12120   1339   2855   1760       O  
ATOM   2926  CB  VAL A 413     157.907  76.913  18.435  1.00104.40           C  
ANISOU 2926  CB  VAL A 413    15951  11197  12520   1551   3008   1775       C  
ATOM   2927  CG1 VAL A 413     159.095  77.589  19.098  1.00111.47           C  
ANISOU 2927  CG1 VAL A 413    16752  12066  13533   1191   3197   1758       C  
ATOM   2928  CG2 VAL A 413     158.227  75.456  18.161  1.00 95.70           C  
ANISOU 2928  CG2 VAL A 413    14549  10305  11509   1638   2895   1713       C  
ATOM   2929  N   LEU A 414     155.899  79.342  19.108  1.00101.60           N  
ANISOU 2929  N   LEU A 414    16292  10426  11888   1741   2981   1889       N  
ATOM   2930  CA  LEU A 414     155.649  80.688  19.614  1.00107.73           C  
ANISOU 2930  CA  LEU A 414    17388  10965  12579   1680   3083   1932       C  
ATOM   2931  C   LEU A 414     154.627  80.680  20.744  1.00113.90           C  
ANISOU 2931  C   LEU A 414    18075  11796  13407   1792   2843   1890       C  
ATOM   2932  O   LEU A 414     154.629  81.584  21.587  1.00113.70           O  
ANISOU 2932  O   LEU A 414    18192  11617  13392   1663   2896   1887       O  
ATOM   2933  CB  LEU A 414     155.182  81.605  18.482  1.00108.16           C  
ANISOU 2933  CB  LEU A 414    17940  10803  12352   1906   3243   2041       C  
ATOM   2934  CG  LEU A 414     156.135  81.799  17.300  1.00106.84           C  
ANISOU 2934  CG  LEU A 414    17950  10551  12094   1799   3520   2100       C  
ATOM   2935  CD1 LEU A 414     155.599  82.863  16.355  1.00103.90           C  
ANISOU 2935  CD1 LEU A 414    18137   9920  11420   2027   3679   2221       C  
ATOM   2936  CD2 LEU A 414     157.538  82.150  17.775  1.00102.97           C  
ANISOU 2936  CD2 LEU A 414    17351  10017  11758   1342   3741   2064       C  
ATOM   2937  N   LEU A 415     153.747  79.675  20.781  1.00111.52           N  
ANISOU 2937  N   LEU A 415    17544  11707  13122   2014   2589   1853       N  
ATOM   2938  CA  LEU A 415     152.797  79.539  21.878  1.00104.01           C  
ANISOU 2938  CA  LEU A 415    16449  10850  12222   2097   2363   1806       C  
ATOM   2939  C   LEU A 415     153.445  79.044  23.166  1.00100.35           C  
ANISOU 2939  C   LEU A 415    15639  10482  12006   1808   2286   1727       C  
ATOM   2940  O   LEU A 415     152.809  79.108  24.224  1.00 83.74           O  
ANISOU 2940  O   LEU A 415    13445   8425   9948   1821   2138   1691       O  
ATOM   2941  CB  LEU A 415     151.661  78.590  21.487  1.00102.21           C  
ANISOU 2941  CB  LEU A 415    16076  10839  11920   2381   2126   1783       C  
ATOM   2942  CG  LEU A 415     150.671  79.080  20.427  1.00 99.16           C  
ANISOU 2942  CG  LEU A 415    15993  10427  11255   2735   2125   1847       C  
ATOM   2943  CD1 LEU A 415     149.531  78.087  20.245  1.00 94.03           C  
ANISOU 2943  CD1 LEU A 415    15128  10051  10549   2954   1863   1792       C  
ATOM   2944  CD2 LEU A 415     150.133  80.450  20.794  1.00 86.23           C  
ANISOU 2944  CD2 LEU A 415    14692   8602   9472   2865   2200   1903       C  
ATOM   2945  N   ILE A 416     154.681  78.544  23.103  1.00108.17           N  
ANISOU 2945  N   ILE A 416    16428  11527  13143   1568   2379   1698       N  
ATOM   2946  CA  ILE A 416     155.384  78.131  24.313  1.00105.65           C  
ANISOU 2946  CA  ILE A 416    15788  11316  13039   1310   2311   1626       C  
ATOM   2947  C   ILE A 416     156.090  79.308  24.971  1.00111.13           C  
ANISOU 2947  C   ILE A 416    16618  11849  13758   1032   2482   1620       C  
ATOM   2948  O   ILE A 416     156.457  79.229  26.150  1.00103.27           O  
ANISOU 2948  O   ILE A 416    15408  10926  12904    834   2408   1557       O  
ATOM   2949  CB  ILE A 416     156.383  77.009  23.981  1.00 98.09           C  
ANISOU 2949  CB  ILE A 416    14529  10530  12210   1217   2319   1591       C  
ATOM   2950  CG1 ILE A 416     155.683  75.899  23.199  1.00109.80           C  
ANISOU 2950  CG1 ILE A 416    15954  12126  13637   1481   2174   1592       C  
ATOM   2951  CG2 ILE A 416     156.997  76.416  25.240  1.00 96.38           C  
ANISOU 2951  CG2 ILE A 416    13960  10464  12195   1021   2205   1519       C  
ATOM   2952  CD1 ILE A 416     156.599  74.753  22.827  1.00109.02           C  
ANISOU 2952  CD1 ILE A 416    15607  12174  13643   1442   2181   1556       C  
ATOM   2953  N   ILE A 417     156.272  80.405  24.232  1.00112.36           N  
ANISOU 2953  N   ILE A 417    17149  11781  13763   1007   2713   1681       N  
ATOM   2954  CA  ILE A 417     156.990  81.561  24.776  1.00107.40           C  
ANISOU 2954  CA  ILE A 417    16700  10969  13140    697   2904   1667       C  
ATOM   2955  C   ILE A 417     156.370  82.090  26.063  1.00104.59           C  
ANISOU 2955  C   ILE A 417    16392  10546  12804    675   2783   1626       C  
ATOM   2956  O   ILE A 417     157.121  82.387  27.004  1.00109.27           O  
ANISOU 2956  O   ILE A 417    16863  11145  13508    358   2819   1557       O  
ATOM   2957  CB  ILE A 417     157.141  82.640  23.696  1.00108.64           C  
ANISOU 2957  CB  ILE A 417    17329  10855  13095    702   3178   1753       C  
ATOM   2958  CG1 ILE A 417     158.019  82.129  22.553  1.00 99.49           C  
ANISOU 2958  CG1 ILE A 417    16076   9788  11936    640   3330   1778       C  
ATOM   2959  CG2 ILE A 417     157.702  83.925  24.286  1.00108.29           C  
ANISOU 2959  CG2 ILE A 417    17556  10569  13022    378   3377   1735       C  
ATOM   2960  CD1 ILE A 417     158.201  83.136  21.441  1.00101.37           C  
ANISOU 2960  CD1 ILE A 417    16789   9763  11963    635   3615   1872       C  
ATOM   2961  N   PRO A 418     155.047  82.246  26.188  1.00102.27           N  
ANISOU 2961  N   PRO A 418    16257  10208  12395    993   2643   1656       N  
ATOM   2962  CA  PRO A 418     154.499  82.803  27.439  1.00103.25           C  
ANISOU 2962  CA  PRO A 418    16434  10270  12527    974   2550   1612       C  
ATOM   2963  C   PRO A 418     154.820  81.992  28.687  1.00 95.14           C  
ANISOU 2963  C   PRO A 418    14971   9468  11709    789   2369   1521       C  
ATOM   2964  O   PRO A 418     154.638  82.505  29.797  1.00 83.81           O  
ANISOU 2964  O   PRO A 418    13570   7980  10293    694   2323   1473       O  
ATOM   2965  CB  PRO A 418     152.990  82.834  27.173  1.00 94.75           C  
ANISOU 2965  CB  PRO A 418    15511   9205  11286   1404   2411   1660       C  
ATOM   2966  CG  PRO A 418     152.885  82.959  25.704  1.00 92.02           C  
ANISOU 2966  CG  PRO A 418    15407   8779  10779   1602   2531   1745       C  
ATOM   2967  CD  PRO A 418     154.000  82.127  25.156  1.00 99.52           C  
ANISOU 2967  CD  PRO A 418    16095   9851  11867   1386   2593   1730       C  
ATOM   2968  N   LEU A 419     155.285  80.749  28.547  1.00107.73           N  
ANISOU 2968  N   LEU A 419    16185  11302  13445    753   2266   1498       N  
ATOM   2969  CA  LEU A 419     155.616  79.941  29.715  1.00 98.53           C  
ANISOU 2969  CA  LEU A 419    14632  10344  12460    605   2095   1423       C  
ATOM   2970  C   LEU A 419     156.799  80.506  30.495  1.00101.88           C  
ANISOU 2970  C   LEU A 419    14986  10746  12977    228   2205   1357       C  
ATOM   2971  O   LEU A 419     156.984  80.146  31.663  1.00 92.45           O  
ANISOU 2971  O   LEU A 419    13542   9689  11895    106   2066   1293       O  
ATOM   2972  CB  LEU A 419     155.899  78.502  29.279  1.00 89.55           C  
ANISOU 2972  CB  LEU A 419    13165   9433  11425    679   1984   1420       C  
ATOM   2973  CG  LEU A 419     156.079  77.434  30.360  1.00 97.29           C  
ANISOU 2973  CG  LEU A 419    13770  10630  12564    614   1782   1363       C  
ATOM   2974  CD1 LEU A 419     154.903  77.437  31.326  1.00107.96           C  
ANISOU 2974  CD1 LEU A 419    15131  11998  13890    730   1602   1350       C  
ATOM   2975  CD2 LEU A 419     156.253  76.063  29.725  1.00 81.71           C  
ANISOU 2975  CD2 LEU A 419    11579   8819  10650    738   1697   1371       C  
ATOM   2976  N   GLY A 420     157.596  81.386  29.883  1.00110.06           N  
ANISOU 2976  N   GLY A 420    16239  11623  13954     28   2451   1369       N  
ATOM   2977  CA  GLY A 420     158.714  81.994  30.584  1.00105.88           C  
ANISOU 2977  CA  GLY A 420    15648  11088  13492   -374   2567   1291       C  
ATOM   2978  C   GLY A 420     158.306  82.896  31.729  1.00109.39           C  
ANISOU 2978  C   GLY A 420    16281  11383  13898   -479   2535   1240       C  
ATOM   2979  O   GLY A 420     159.131  83.183  32.604  1.00112.69           O  
ANISOU 2979  O   GLY A 420    16564  11863  14391   -810   2555   1150       O  
ATOM   2980  N   GLN A 421     157.055  83.351  31.742  1.00111.12           N  
ANISOU 2980  N   GLN A 421    16805  11429  13988   -194   2485   1288       N  
ATOM   2981  CA  GLN A 421     156.515  84.169  32.827  1.00119.36           C  
ANISOU 2981  CA  GLN A 421    18048  12329  14973   -223   2445   1241       C  
ATOM   2982  C   GLN A 421     155.812  83.327  33.884  1.00111.14           C  
ANISOU 2982  C   GLN A 421    16698  11510  14018    -73   2174   1206       C  
ATOM   2983  O   GLN A 421     154.734  83.691  34.363  1.00106.33           O  
ANISOU 2983  O   GLN A 421    16262  10824  13315    143   2094   1213       O  
ATOM   2984  CB  GLN A 421     155.568  85.217  32.250  1.00116.44           C  
ANISOU 2984  CB  GLN A 421    18207  11648  14386     31   2563   1313       C  
ATOM   2985  CG  GLN A 421     156.154  86.006  31.088  1.00120.42           C  
ANISOU 2985  CG  GLN A 421    19074  11907  14775    -76   2841   1372       C  
ATOM   2986  CD  GLN A 421     157.349  86.848  31.492  1.00124.46           C  
ANISOU 2986  CD  GLN A 421    19704  12274  15310   -565   3042   1295       C  
ATOM   2987  OE1 GLN A 421     157.439  87.317  32.627  1.00119.60           O  
ANISOU 2987  OE1 GLN A 421    19114  11612  14716   -758   3004   1206       O  
ATOM   2988  NE2 GLN A 421     158.276  87.044  30.561  1.00132.97           N  
ANISOU 2988  NE2 GLN A 421    20854  13296  16372   -786   3261   1321       N  
ATOM   2989  N   LEU A 422     156.401  82.195  34.264  1.00107.45           N  
ANISOU 2989  N   LEU A 422    15785  11324  13717   -172   2036   1169       N  
ATOM   2990  CA  LEU A 422     155.764  81.277  35.198  1.00 99.51           C  
ANISOU 2990  CA  LEU A 422    14497  10525  12785    -37   1788   1149       C  
ATOM   2991  C   LEU A 422     156.012  81.725  36.633  1.00101.58           C  
ANISOU 2991  C   LEU A 422    14714  10801  13080   -256   1731   1059       C  
ATOM   2992  O   LEU A 422     157.162  81.906  37.047  1.00 98.42           O  
ANISOU 2992  O   LEU A 422    14184  10457  12753   -577   1788    989       O  
ATOM   2993  CB  LEU A 422     156.290  79.856  34.988  1.00 96.21           C  
ANISOU 2993  CB  LEU A 422    13677  10371  12508    -23   1671   1156       C  
ATOM   2994  CG  LEU A 422     155.713  78.756  35.884  1.00 94.75           C  
ANISOU 2994  CG  LEU A 422    13214  10390  12395     99   1426   1145       C  
ATOM   2995  CD1 LEU A 422     154.250  78.495  35.550  1.00 97.61           C  
ANISOU 2995  CD1 LEU A 422    13691  10735  12663    416   1332   1200       C  
ATOM   2996  CD2 LEU A 422     156.532  77.475  35.774  1.00 80.10           C  
ANISOU 2996  CD2 LEU A 422    11008   8755  10671     64   1344   1141       C  
ATOM   2997  N   SER A 423     154.929  81.904  37.389  1.00101.94           N  
ANISOU 2997  N   SER A 423    14854  10820  13058    -81   1618   1054       N  
ATOM   2998  CA  SER A 423     154.995  82.232  38.805  1.00 99.60           C  
ANISOU 2998  CA  SER A 423    14516  10551  12775   -242   1540    969       C  
ATOM   2999  C   SER A 423     154.181  81.215  39.592  1.00100.88           C  
ANISOU 2999  C   SER A 423    14416  10932  12980    -58   1309    978       C  
ATOM   3000  O   SER A 423     153.190  80.672  39.096  1.00 90.96           O  
ANISOU 3000  O   SER A 423    13144   9730  11684    224   1237   1044       O  
ATOM   3001  CB  SER A 423     154.478  83.649  39.079  1.00 95.64           C  
ANISOU 3001  CB  SER A 423    14459   9764  12115   -227   1663    943       C  
ATOM   3002  OG  SER A 423     153.149  83.804  38.613  1.00 95.29           O  
ANISOU 3002  OG  SER A 423    14621   9644  11941    154   1646   1015       O  
ATOM   3003  N   LEU A 424     154.607  80.960  40.829  1.00109.78           N  
ANISOU 3003  N   LEU A 424    15340  12196  14176   -236   1197    909       N  
ATOM   3004  CA  LEU A 424     154.020  79.917  41.658  1.00 97.47           C  
ANISOU 3004  CA  LEU A 424    13523  10851  12662   -116    989    919       C  
ATOM   3005  C   LEU A 424     153.700  80.461  43.043  1.00 98.64           C  
ANISOU 3005  C   LEU A 424    13735  10993  12752   -188    927    848       C  
ATOM   3006  O   LEU A 424     154.509  81.174  43.642  1.00107.98           O  
ANISOU 3006  O   LEU A 424    14975  12117  13934   -446    983    765       O  
ATOM   3007  CB  LEU A 424     154.967  78.720  41.763  1.00 96.68           C  
ANISOU 3007  CB  LEU A 424    13059  10973  12703   -223    887    920       C  
ATOM   3008  CG  LEU A 424     155.414  78.177  40.404  1.00 98.56           C  
ANISOU 3008  CG  LEU A 424    13234  11220  12994   -161    961    977       C  
ATOM   3009  CD1 LEU A 424     156.813  77.609  40.483  1.00 95.43           C  
ANISOU 3009  CD1 LEU A 424    12556  10991  12712   -350    950    943       C  
ATOM   3010  CD2 LEU A 424     154.436  77.134  39.891  1.00104.45           C  
ANISOU 3010  CD2 LEU A 424    13914  12038  13734    110    855   1052       C  
ATOM   3011  N   GLY A 425     152.517  80.118  43.549  1.00102.18           N  
ANISOU 3011  N   GLY A 425    14167  11517  13142     26    815    874       N  
ATOM   3012  CA  GLY A 425     152.073  80.616  44.837  1.00 99.04           C  
ANISOU 3012  CA  GLY A 425    13842  11121  12667      1    762    812       C  
ATOM   3013  C   GLY A 425     151.321  79.599  45.671  1.00 84.39           C  
ANISOU 3013  C   GLY A 425    11757   9487  10821    114    585    836       C  
ATOM   3014  O   GLY A 425     151.555  78.393  45.553  1.00 89.24           O  
ANISOU 3014  O   GLY A 425    12110  10264  11532    111    480    881       O  
ATOM   3015  N   GLY A 426     150.408  80.076  46.520  1.00 87.18           N  
ANISOU 3015  N   GLY A 426    12225   9841  11059    217    560    806       N  
ATOM   3016  CA  GLY A 426     149.666  79.209  47.411  1.00 89.41           C  
ANISOU 3016  CA  GLY A 426    12311  10333  11327    295    413    823       C  
ATOM   3017  C   GLY A 426     148.199  79.588  47.468  1.00 79.83           C  
ANISOU 3017  C   GLY A 426    11219   9145   9966    558    430    836       C  
ATOM   3018  O   GLY A 426     147.754  80.537  46.820  1.00 56.74           O  
ANISOU 3018  O   GLY A 426     8546   6069   6943    717    547    835       O  
ATOM   3019  N   ILE A 427     147.456  78.824  48.271  1.00 84.54           N  
ANISOU 3019  N   ILE A 427    11638   9949  10536    609    315    850       N  
ATOM   3020  CA  ILE A 427     146.015  79.011  48.369  1.00 84.78           C  
ANISOU 3020  CA  ILE A 427    11704  10087  10422    856    319    859       C  
ATOM   3021  C   ILE A 427     145.709  80.302  49.115  1.00 86.29           C  
ANISOU 3021  C   ILE A 427    12149  10164  10472    929    398    786       C  
ATOM   3022  O   ILE A 427     146.368  80.646  50.106  1.00 81.96           O  
ANISOU 3022  O   ILE A 427    11653   9555   9932    747    388    723       O  
ATOM   3023  CB  ILE A 427     145.355  77.806  49.061  1.00 79.09           C  
ANISOU 3023  CB  ILE A 427    10719   9628   9704    841    191    891       C  
ATOM   3024  CG1 ILE A 427     145.872  76.492  48.473  1.00 80.72           C  
ANISOU 3024  CG1 ILE A 427    10724   9897  10051    729    112    954       C  
ATOM   3025  CG2 ILE A 427     143.841  77.877  48.929  1.00 75.86           C  
ANISOU 3025  CG2 ILE A 427    10283   9392   9148   1086    199    900       C  
ATOM   3026  CD1 ILE A 427     146.899  75.795  49.341  1.00 83.80           C  
ANISOU 3026  CD1 ILE A 427    10991  10308  10542    508     23    953       C  
ATOM   3027  N   SER A 428     144.704  81.026  48.634  1.00 91.67           N  
ANISOU 3027  N   SER A 428    13000  10822  11008   1213    477    790       N  
ATOM   3028  CA  SER A 428     144.207  82.220  49.296  1.00 83.51           C  
ANISOU 3028  CA  SER A 428    12235   9687   9807   1359    558    724       C  
ATOM   3029  C   SER A 428     142.754  82.408  48.886  1.00 79.22           C  
ANISOU 3029  C   SER A 428    11698   9304   9099   1734    579    750       C  
ATOM   3030  O   SER A 428     142.210  81.639  48.089  1.00 71.35           O  
ANISOU 3030  O   SER A 428    10495   8491   8123   1836    527    810       O  
ATOM   3031  CB  SER A 428     145.051  83.448  48.945  1.00 91.04           C  
ANISOU 3031  CB  SER A 428    13563  10289  10742   1286    698    681       C  
ATOM   3032  OG  SER A 428     144.844  83.839  47.598  1.00 83.33           O  
ANISOU 3032  OG  SER A 428    12753   9185   9725   1478    791    736       O  
ATOM   3033  N   GLU A 429     142.123  83.448  49.433  1.00 84.60           N  
ANISOU 3033  N   GLU A 429    12619   9927   9599   1948    655    696       N  
ATOM   3034  CA  GLU A 429     140.739  83.734  49.077  1.00 81.03           C  
ANISOU 3034  CA  GLU A 429    12170   9657   8961   2350    679    712       C  
ATOM   3035  C   GLU A 429     140.590  84.161  47.624  1.00 77.18           C  
ANISOU 3035  C   GLU A 429    11853   9049   8424   2580    750    766       C  
ATOM   3036  O   GLU A 429     139.457  84.269  47.142  1.00 72.91           O  
ANISOU 3036  O   GLU A 429    11265   8709   7729   2932    749    787       O  
ATOM   3037  CB  GLU A 429     140.161  84.813  50.001  1.00 86.17           C  
ANISOU 3037  CB  GLU A 429    13075  10254   9412   2564    756    638       C  
ATOM   3038  CG  GLU A 429     140.821  86.180  49.885  1.00 87.01           C  
ANISOU 3038  CG  GLU A 429    13684   9929   9447   2586    901    593       C  
ATOM   3039  CD  GLU A 429     142.157  86.257  50.604  1.00 84.15           C  
ANISOU 3039  CD  GLU A 429    13407   9344   9223   2154    899    534       C  
ATOM   3040  OE1 GLU A 429     142.817  87.314  50.521  1.00 81.77           O  
ANISOU 3040  OE1 GLU A 429    13509   8684   8876   2082   1020    486       O  
ATOM   3041  OE2 GLU A 429     142.547  85.261  51.250  1.00 79.46           O  
ANISOU 3041  OE2 GLU A 429    12484   8939   8769   1883    778    534       O  
ATOM   3042  N   LYS A 430     141.699  84.397  46.919  1.00 81.83           N  
ANISOU 3042  N   LYS A 430    12624   9341   9125   2394    812    789       N  
ATOM   3043  CA  LYS A 430     141.651  84.763  45.509  1.00 96.21           C  
ANISOU 3043  CA  LYS A 430    14626  11032  10899   2588    887    850       C  
ATOM   3044  C   LYS A 430     141.320  83.585  44.603  1.00 83.10           C  
ANISOU 3044  C   LYS A 430    12619   9636   9319   2606    782    914       C  
ATOM   3045  O   LYS A 430     140.966  83.802  43.438  1.00 72.96           O  
ANISOU 3045  O   LYS A 430    11435   8334   7950   2842    820    964       O  
ATOM   3046  CB  LYS A 430     142.985  85.375  45.077  1.00103.36           C  
ANISOU 3046  CB  LYS A 430    15834  11546  11894   2341   1004    849       C  
ATOM   3047  CG  LYS A 430     143.439  86.552  45.928  1.00104.51           C  
ANISOU 3047  CG  LYS A 430    16358  11391  11959   2251   1117    770       C  
ATOM   3048  CD  LYS A 430     144.727  87.155  45.393  1.00112.00           C  
ANISOU 3048  CD  LYS A 430    17596  11976  12982   1972   1248    764       C  
ATOM   3049  CE  LYS A 430     145.311  88.167  46.367  1.00128.48           C  
ANISOU 3049  CE  LYS A 430    20015  13789  15013   1772   1341    662       C  
ATOM   3050  NZ  LYS A 430     145.808  87.519  47.618  1.00143.95           N  
ANISOU 3050  NZ  LYS A 430    21667  15927  17100   1457   1215    590       N  
ATOM   3051  N   TYR A 431     141.421  82.350  45.105  1.00 78.92           N  
ANISOU 3051  N   TYR A 431    11714   9340   8933   2367    653    913       N  
ATOM   3052  CA  TYR A 431     141.046  81.183  44.316  1.00 65.09           C  
ANISOU 3052  CA  TYR A 431     9656   7834   7243   2364    554    961       C  
ATOM   3053  C   TYR A 431     139.560  81.149  43.989  1.00 72.77           C  
ANISOU 3053  C   TYR A 431    10500   9120   8027   2706    514    962       C  
ATOM   3054  O   TYR A 431     139.144  80.323  43.171  1.00 73.40           O  
ANISOU 3054  O   TYR A 431    10365   9404   8119   2733    441    990       O  
ATOM   3055  CB  TYR A 431     141.436  79.891  45.042  1.00 64.78           C  
ANISOU 3055  CB  TYR A 431     9297   7948   7370   2042    435    958       C  
ATOM   3056  CG  TYR A 431     142.881  79.484  44.860  1.00 67.53           C  
ANISOU 3056  CG  TYR A 431     9653   8089   7916   1736    438    976       C  
ATOM   3057  CD1 TYR A 431     143.848  80.416  44.511  1.00 76.81           C  
ANISOU 3057  CD1 TYR A 431    11109   8955   9120   1678    554    969       C  
ATOM   3058  CD2 TYR A 431     143.275  78.163  45.020  1.00 63.96           C  
ANISOU 3058  CD2 TYR A 431     8934   7759   7609   1511    331    999       C  
ATOM   3059  CE1 TYR A 431     145.168  80.047  44.339  1.00 79.44           C  
ANISOU 3059  CE1 TYR A 431    11407   9154   9623   1400    560    976       C  
ATOM   3060  CE2 TYR A 431     144.594  77.784  44.849  1.00 70.69           C  
ANISOU 3060  CE2 TYR A 431     9775   8458   8626   1277    332   1013       C  
ATOM   3061  CZ  TYR A 431     145.536  78.731  44.506  1.00 66.02           C  
ANISOU 3061  CZ  TYR A 431     9414   7607   8062   1222    445    998       C  
ATOM   3062  OH  TYR A 431     146.851  78.364  44.331  1.00 62.56           O  
ANISOU 3062  OH  TYR A 431     8924   7069   7777    989    450   1003       O  
ATOM   3063  N   LEU A 432     138.762  82.005  44.609  1.00 71.63           N  
ANISOU 3063  N   LEU A 432    10474   9041   7702   2966    559    923       N  
ATOM   3064  CA  LEU A 432     137.347  82.186  44.341  1.00 78.45           C  
ANISOU 3064  CA  LEU A 432    11230  10226   8351   3347    537    913       C  
ATOM   3065  C   LEU A 432     137.132  83.405  43.457  1.00 87.85           C  
ANISOU 3065  C   LEU A 432    12791  11226   9362   3737    645    937       C  
ATOM   3066  O   LEU A 432     138.001  84.278  43.366  1.00 77.20           O  
ANISOU 3066  O   LEU A 432    11830   9468   8035   3697    760    948       O  
ATOM   3067  CB  LEU A 432     136.579  82.353  45.657  1.00 84.68           C  
ANISOU 3067  CB  LEU A 432    11909  11235   9030   3423    527    854       C  
ATOM   3068  CG  LEU A 432     136.609  81.149  46.598  1.00 85.96           C  
ANISOU 3068  CG  LEU A 432    11719  11618   9323   3074    427    837       C  
ATOM   3069  CD1 LEU A 432     136.014  81.513  47.947  1.00 81.41           C  
ANISOU 3069  CD1 LEU A 432    11113  11190   8627   3145    448    779       C  
ATOM   3070  CD2 LEU A 432     135.866  79.977  45.979  1.00 91.94           C  
ANISOU 3070  CD2 LEU A 432    12100  12747  10086   3032    322    855       C  
ATOM   3071  N   PRO A 433     135.993  83.495  42.772  1.00100.20           N  
ANISOU 3071  N   PRO A 433    14256  13081  10733   4115    613    946       N  
ATOM   3072  CA  PRO A 433     135.735  84.671  41.951  1.00100.49           C  
ANISOU 3072  CA  PRO A 433    14675  12939  10565   4541    714    978       C  
ATOM   3073  C   PRO A 433     135.620  85.910  42.814  1.00102.29           C  
ANISOU 3073  C   PRO A 433    15265  12956  10647   4758    831    941       C  
ATOM   3074  O   PRO A 433     135.238  85.834  43.998  1.00 89.21           O  
ANISOU 3074  O   PRO A 433    13459  11465   8971   4714    808    880       O  
ATOM   3075  CB  PRO A 433     134.404  84.336  41.262  1.00102.10           C  
ANISOU 3075  CB  PRO A 433    14592  13621  10580   4899    619    977       C  
ATOM   3076  CG  PRO A 433     133.767  83.318  42.139  1.00107.52           C  
ANISOU 3076  CG  PRO A 433    14795  14738  11319   4701    505    919       C  
ATOM   3077  CD  PRO A 433     134.906  82.507  42.667  1.00106.90           C  
ANISOU 3077  CD  PRO A 433    14643  14446  11527   4162    483    924       C  
ATOM   3078  N   PRO A 434     135.941  87.085  42.263  1.00107.04           N  
ANISOU 3078  N   PRO A 434    16375  13171  11123   4993    968    975       N  
ATOM   3079  CA  PRO A 434     135.931  88.308  43.081  1.00 98.32           C  
ANISOU 3079  CA  PRO A 434    15694  11791   9872   5174   1096    933       C  
ATOM   3080  C   PRO A 434     134.561  88.691  43.610  1.00 94.07           C  
ANISOU 3080  C   PRO A 434    15067  11599   9077   5651   1076    889       C  
ATOM   3081  O   PRO A 434     134.486  89.515  44.531  1.00 96.11           O  
ANISOU 3081  O   PRO A 434    15600  11692   9226   5766   1164    835       O  
ATOM   3082  CB  PRO A 434     136.475  89.377  42.123  1.00105.43           C  
ANISOU 3082  CB  PRO A 434    17169  12219  10670   5342   1249    994       C  
ATOM   3083  CG  PRO A 434     136.219  88.829  40.756  1.00104.38           C  
ANISOU 3083  CG  PRO A 434    16865  12270  10524   5477   1183   1071       C  
ATOM   3084  CD  PRO A 434     136.381  87.346  40.882  1.00106.09           C  
ANISOU 3084  CD  PRO A 434    16505  12819  10984   5079   1025   1054       C  
ATOM   3085  N   ASP A 435     133.479  88.136  43.069  1.00 96.25           N  
ANISOU 3085  N   ASP A 435    14965  12366   9240   5930    967    901       N  
ATOM   3086  CA  ASP A 435     132.139  88.425  43.562  1.00101.95           C  
ANISOU 3086  CA  ASP A 435    15524  13503   9708   6385    943    852       C  
ATOM   3087  C   ASP A 435     131.652  87.392  44.570  1.00 94.66           C  
ANISOU 3087  C   ASP A 435    14048  13036   8882   6122    834    786       C  
ATOM   3088  O   ASP A 435     130.461  87.374  44.900  1.00 83.06           O  
ANISOU 3088  O   ASP A 435    12307  12034   7217   6444    796    741       O  
ATOM   3089  CB  ASP A 435     131.152  88.535  42.394  1.00100.49           C  
ANISOU 3089  CB  ASP A 435    15241  13648   9292   6844    891    887       C  
ATOM   3090  CG  ASP A 435     131.059  87.258  41.582  1.00106.07           C  
ANISOU 3090  CG  ASP A 435    15475  14689  10139   6638    744    912       C  
ATOM   3091  OD1 ASP A 435     132.037  86.482  41.572  1.00 97.70           O  
ANISOU 3091  OD1 ASP A 435    14325  13437   9360   6111    715    929       O  
ATOM   3092  OD2 ASP A 435     130.005  87.035  40.948  1.00102.40           O  
ANISOU 3092  OD2 ASP A 435    14725  14694   9488   6867    655    890       O  
ATOM   3093  N   ASN A 436     132.544  86.537  45.068  1.00 92.03           N  
ANISOU 3093  N   ASN A 436    13550  12588   8829   5553    789    781       N  
ATOM   3094  CA  ASN A 436     132.179  85.548  46.073  1.00100.30           C  
ANISOU 3094  CA  ASN A 436    14136  14006   9965   5270    700    731       C  
ATOM   3095  C   ASN A 436     132.058  86.216  47.438  1.00102.05           C  
ANISOU 3095  C   ASN A 436    14518  14158  10097   5335    779    665       C  
ATOM   3096  O   ASN A 436     132.964  86.938  47.869  1.00 97.22           O  
ANISOU 3096  O   ASN A 436    14320  13078   9539   5217    871    655       O  
ATOM   3097  CB  ASN A 436     133.214  84.425  46.116  1.00102.33           C  
ANISOU 3097  CB  ASN A 436    14214  14134  10531   4684    628    757       C  
ATOM   3098  CG  ASN A 436     132.835  83.318  47.076  1.00109.23           C  
ANISOU 3098  CG  ASN A 436    14643  15373  11485   4385    538    721       C  
ATOM   3099  OD1 ASN A 436     133.254  83.314  48.233  1.00112.13           O  
ANISOU 3099  OD1 ASN A 436    15054  15629  11923   4162    560    690       O  
ATOM   3100  ND2 ASN A 436     132.034  82.370  46.601  1.00122.22           N  
ANISOU 3100  ND2 ASN A 436    15873  17458  13107   4366    440    721       N  
ATOM   3101  N   ALA A 437     130.936  85.966  48.119  1.00104.64           N  
ANISOU 3101  N   ALA A 437    14511  14969  10277   5506    747    612       N  
ATOM   3102  CA  ALA A 437     130.659  86.655  49.377  1.00 95.75           C  
ANISOU 3102  CA  ALA A 437    13536  13828   9018   5647    829    544       C  
ATOM   3103  C   ALA A 437     131.681  86.299  50.450  1.00 88.28           C  
ANISOU 3103  C   ALA A 437    12645  12613   8284   5136    829    523       C  
ATOM   3104  O   ALA A 437     132.106  87.165  51.222  1.00 99.02           O  
ANISOU 3104  O   ALA A 437    14377  13653   9592   5167    921    477       O  
ATOM   3105  CB  ALA A 437     129.244  86.326  49.853  1.00 96.77           C  
ANISOU 3105  CB  ALA A 437    13225  14593   8950   5901    796    493       C  
ATOM   3106  N   VAL A 438     132.084  85.029  50.516  1.00 85.74           N  
ANISOU 3106  N   VAL A 438    11974  12417   8186   4672    724    552       N  
ATOM   3107  CA  VAL A 438     133.055  84.612  51.523  1.00 92.12           C  
ANISOU 3107  CA  VAL A 438    12810  13011   9182   4210    706    538       C  
ATOM   3108  C   VAL A 438     134.403  85.275  51.271  1.00 91.03           C  
ANISOU 3108  C   VAL A 438    13113  12302   9171   4045    762    550       C  
ATOM   3109  O   VAL A 438     135.093  85.690  52.210  1.00 84.82           O  
ANISOU 3109  O   VAL A 438    12550  11259   8418   3863    802    502       O  
ATOM   3110  CB  VAL A 438     133.172  83.077  51.546  1.00 86.73           C  
ANISOU 3110  CB  VAL A 438    11688  12576   8689   3793    584    577       C  
ATOM   3111  CG1 VAL A 438     134.179  82.637  52.594  1.00 73.33           C  
ANISOU 3111  CG1 VAL A 438    10026  10673   7161   3361    557    571       C  
ATOM   3112  CG2 VAL A 438     131.813  82.449  51.810  1.00 84.90           C  
ANISOU 3112  CG2 VAL A 438    11027  12920   8313   3910    547    554       C  
ATOM   3113  N   ARG A 439     134.798  85.388  50.002  1.00 92.39           N  
ANISOU 3113  N   ARG A 439    13413  12285   9405   4092    768    607       N  
ATOM   3114  CA  ARG A 439     136.040  86.082  49.676  1.00 97.14           C  
ANISOU 3114  CA  ARG A 439    14439  12364  10106   3935    844    617       C  
ATOM   3115  C   ARG A 439     135.959  87.560  50.042  1.00 97.31           C  
ANISOU 3115  C   ARG A 439    14964  12085   9925   4231    985    562       C  
ATOM   3116  O   ARG A 439     136.909  88.122  50.598  1.00 97.79           O  
ANISOU 3116  O   ARG A 439    15340  11773  10042   3996   1049    517       O  
ATOM   3117  CB  ARG A 439     136.360  85.916  48.192  1.00 97.06           C  
ANISOU 3117  CB  ARG A 439    14465  12245  10170   3961    838    693       C  
ATOM   3118  CG  ARG A 439     137.456  86.842  47.701  1.00102.40           C  
ANISOU 3118  CG  ARG A 439    15624  12396  10886   3881    955    705       C  
ATOM   3119  CD  ARG A 439     137.655  86.716  46.207  1.00101.28           C  
ANISOU 3119  CD  ARG A 439    15527  12174  10781   3955    963    786       C  
ATOM   3120  NE  ARG A 439     138.711  87.600  45.727  1.00109.73           N  
ANISOU 3120  NE  ARG A 439    17065  12746  11880   3847   1095    800       N  
ATOM   3121  CZ  ARG A 439     139.218  87.554  44.501  1.00116.57           C  
ANISOU 3121  CZ  ARG A 439    18033  13453  12806   3814   1130    869       C  
ATOM   3122  NH1 ARG A 439     140.177  88.397  44.148  1.00117.50           N  
ANISOU 3122  NH1 ARG A 439    18588  13122  12936   3683   1271    876       N  
ATOM   3123  NH2 ARG A 439     138.770  86.659  43.630  1.00118.81           N  
ANISOU 3123  NH2 ARG A 439    17989  14028  13127   3891   1031    925       N  
ATOM   3124  N   GLN A 440     134.828  88.204  49.741  1.00 86.08           N  
ANISOU 3124  N   GLN A 440    13629  10826   8249   4753   1036    558       N  
ATOM   3125  CA  GLN A 440     134.671  89.619  50.058  1.00 89.49           C  
ANISOU 3125  CA  GLN A 440    14586  10959   8457   5095   1180    508       C  
ATOM   3126  C   GLN A 440     134.637  89.869  51.562  1.00101.40           C  
ANISOU 3126  C   GLN A 440    16143  12473   9910   5002   1205    412       C  
ATOM   3127  O   GLN A 440     135.139  90.899  52.025  1.00102.33           O  
ANISOU 3127  O   GLN A 440    16752  12182   9947   5010   1318    353       O  
ATOM   3128  CB  GLN A 440     133.405  90.164  49.401  1.00 90.89           C  
ANISOU 3128  CB  GLN A 440    14808  11371   8356   5730   1215    531       C  
ATOM   3129  CG  GLN A 440     133.477  90.240  47.884  1.00 85.37           C  
ANISOU 3129  CG  GLN A 440    14213  10574   7649   5898   1218    621       C  
ATOM   3130  CD  GLN A 440     132.250  90.889  47.280  1.00102.06           C  
ANISOU 3130  CD  GLN A 440    16412  12914   9450   6576   1251    639       C  
ATOM   3131  OE1 GLN A 440     131.208  91.008  47.929  1.00107.70           O  
ANISOU 3131  OE1 GLN A 440    16948  13997   9976   6906   1242    586       O  
ATOM   3132  NE2 GLN A 440     132.367  91.318  46.032  1.00105.84           N  
ANISOU 3132  NE2 GLN A 440    17164  13192   9858   6804   1291    716       N  
ATOM   3133  N   SER A 441     134.062  88.948  52.336  1.00105.88           N  
ANISOU 3133  N   SER A 441    16232  13489  10509   4897   1108    392       N  
ATOM   3134  CA  SER A 441     134.058  89.106  53.786  1.00 92.24           C  
ANISOU 3134  CA  SER A 441    14535  11785   8728   4787   1128    305       C  
ATOM   3135  C   SER A 441     135.470  89.066  54.354  1.00 85.00           C  
ANISOU 3135  C   SER A 441    13800  10487   8010   4269   1117    273       C  
ATOM   3136  O   SER A 441     135.760  89.748  55.343  1.00 73.46           O  
ANISOU 3136  O   SER A 441    12628   8820   6464   4220   1180    184       O  
ATOM   3137  CB  SER A 441     133.194  88.023  54.430  1.00 91.07           C  
ANISOU 3137  CB  SER A 441    13823  12201   8578   4734   1033    304       C  
ATOM   3138  OG  SER A 441     131.854  88.082  53.966  1.00 92.83           O  
ANISOU 3138  OG  SER A 441    13836  12839   8596   5204   1043    314       O  
ATOM   3139  N   GLN A 442     136.358  88.278  53.745  1.00 85.57           N  
ANISOU 3139  N   GLN A 442    13700  10482   8331   3888   1037    336       N  
ATOM   3140  CA  GLN A 442     137.748  88.255  54.185  1.00 82.58           C  
ANISOU 3140  CA  GLN A 442    13466   9777   8132   3414   1023    303       C  
ATOM   3141  C   GLN A 442     138.469  89.533  53.783  1.00 89.75           C  
ANISOU 3141  C   GLN A 442    14948  10172   8982   3438   1159    265       C  
ATOM   3142  O   GLN A 442     139.214  90.111  54.583  1.00 91.72           O  
ANISOU 3142  O   GLN A 442    15476  10148   9224   3207   1203    176       O  
ATOM   3143  CB  GLN A 442     138.463  87.033  53.608  1.00 74.58           C  
ANISOU 3143  CB  GLN A 442    12097   8854   7384   3047    905    381       C  
ATOM   3144  CG  GLN A 442     139.929  86.926  54.003  1.00 79.66           C  
ANISOU 3144  CG  GLN A 442    12826   9228   8212   2573    877    349       C  
ATOM   3145  CD  GLN A 442     140.115  86.686  55.486  1.00 88.20           C  
ANISOU 3145  CD  GLN A 442    13813  10414   9284   2362    818    277       C  
ATOM   3146  OE1 GLN A 442     139.341  85.962  56.111  1.00 73.21           O  
ANISOU 3146  OE1 GLN A 442    11607   8866   7345   2422    750    292       O  
ATOM   3147  NE2 GLN A 442     141.144  87.297  56.061  1.00105.43           N  
ANISOU 3147  NE2 GLN A 442    16266  12303  11491   2098    848    194       N  
ATOM   3148  N   GLU A 443     138.263  89.985  52.543  1.00 98.77           N  
ANISOU 3148  N   GLU A 443    16285  11175  10067   3701   1230    328       N  
ATOM   3149  CA  GLU A 443     138.887  91.223  52.089  1.00 96.43           C  
ANISOU 3149  CA  GLU A 443    16583  10367   9690   3733   1383    303       C  
ATOM   3150  C   GLU A 443     138.382  92.425  52.873  1.00 95.91           C  
ANISOU 3150  C   GLU A 443    16972  10111   9358   4036   1505    209       C  
ATOM   3151  O   GLU A 443     139.138  93.376  53.106  1.00 94.17           O  
ANISOU 3151  O   GLU A 443    17250   9441   9090   3875   1620    138       O  
ATOM   3152  CB  GLU A 443     138.631  91.415  50.595  1.00 96.94           C  
ANISOU 3152  CB  GLU A 443    16765  10355   9714   4010   1435    404       C  
ATOM   3153  CG  GLU A 443     139.219  90.317  49.728  1.00 98.86           C  
ANISOU 3153  CG  GLU A 443    16630  10726  10206   3712   1334    489       C  
ATOM   3154  CD  GLU A 443     138.848  90.468  48.269  1.00 88.19           C  
ANISOU 3154  CD  GLU A 443    15374   9347   8788   4021   1376    587       C  
ATOM   3155  OE1 GLU A 443     137.792  91.073  47.985  1.00 80.58           O  
ANISOU 3155  OE1 GLU A 443    14574   8460   7583   4535   1425    602       O  
ATOM   3156  OE2 GLU A 443     139.616  89.989  47.407  1.00 82.89           O  
ANISOU 3156  OE2 GLU A 443    14616   8589   8290   3767   1359    647       O  
ATOM   3157  N   GLN A 444     137.111  92.408  53.279  1.00104.08           N  
ANISOU 3157  N   GLN A 444    17851  11487  10207   4467   1488    199       N  
ATOM   3158  CA  GLN A 444     136.588  93.480  54.119  1.00 99.41           C  
ANISOU 3158  CA  GLN A 444    17667  10753   9352   4783   1601    102       C  
ATOM   3159  C   GLN A 444     137.271  93.488  55.480  1.00106.32           C  
ANISOU 3159  C   GLN A 444    18585  11528  10283   4379   1581    -12       C  
ATOM   3160  O   GLN A 444     137.544  94.555  56.042  1.00107.38           O  
ANISOU 3160  O   GLN A 444    19241  11292  10266   4403   1698   -113       O  
ATOM   3161  CB  GLN A 444     135.074  93.330  54.274  1.00111.37           C  
ANISOU 3161  CB  GLN A 444    18910  12744  10660   5324   1579    115       C  
ATOM   3162  CG  GLN A 444     134.420  94.393  55.141  1.00134.32           C  
ANISOU 3162  CG  GLN A 444    22208  15558  13270   5724   1699     16       C  
ATOM   3163  CD  GLN A 444     132.945  94.125  55.374  1.00144.10           C  
ANISOU 3163  CD  GLN A 444    23081  17359  14314   6226   1670     21       C  
ATOM   3164  OE1 GLN A 444     132.427  93.076  54.992  1.00139.44           O  
ANISOU 3164  OE1 GLN A 444    21914  17245  13822   6206   1552     89       O  
ATOM   3165  NE2 GLN A 444     132.262  95.074  56.005  1.00149.51           N  
ANISOU 3165  NE2 GLN A 444    24101  17999  14708   6673   1784    -60       N  
ATOM   3166  N   PHE A 445     137.558  92.303  56.024  1.00109.66           N  
ANISOU 3166  N   PHE A 445    18487  12270  10909   4008   1432     -1       N  
ATOM   3167  CA  PHE A 445     138.262  92.220  57.299  1.00 96.30           C  
ANISOU 3167  CA  PHE A 445    16804  10516   9271   3616   1391   -102       C  
ATOM   3168  C   PHE A 445     139.671  92.792  57.191  1.00 94.48           C  
ANISOU 3168  C   PHE A 445    16947   9808   9145   3191   1440   -160       C  
ATOM   3169  O   PHE A 445     140.129  93.508  58.089  1.00105.06           O  
ANISOU 3169  O   PHE A 445    18625  10901  10392   3031   1494   -285       O  
ATOM   3170  CB  PHE A 445     138.306  90.766  57.773  1.00 89.69           C  
ANISOU 3170  CB  PHE A 445    15346  10109   8623   3326   1220    -55       C  
ATOM   3171  CG  PHE A 445     139.225  90.532  58.937  1.00 87.17           C  
ANISOU 3171  CG  PHE A 445    14999   9733   8389   2879   1151   -138       C  
ATOM   3172  CD1 PHE A 445     138.788  90.741  60.234  1.00 83.96           C  
ANISOU 3172  CD1 PHE A 445    14633   9448   7820   2948   1157   -229       C  
ATOM   3173  CD2 PHE A 445     140.526  90.095  58.735  1.00 80.72           C  
ANISOU 3173  CD2 PHE A 445    14102   8768   7800   2406   1077   -129       C  
ATOM   3174  CE1 PHE A 445     139.633  90.526  61.307  1.00 88.30           C  
ANISOU 3174  CE1 PHE A 445    15160   9963   8429   2549   1082   -308       C  
ATOM   3175  CE2 PHE A 445     141.374  89.883  59.804  1.00 76.27           C  
ANISOU 3175  CE2 PHE A 445    13493   8190   7294   2019    999   -210       C  
ATOM   3176  CZ  PHE A 445     140.928  90.095  61.090  1.00 73.59           C  
ANISOU 3176  CZ  PHE A 445    13208   7965   6788   2089    996   -299       C  
ATOM   3177  N   ASP A 446     140.371  92.491  56.096  1.00 92.61           N  
ANISOU 3177  N   ASP A 446    16649   9448   9090   2990   1428    -79       N  
ATOM   3178  CA  ASP A 446     141.764  92.889  55.948  1.00 95.22           C  
ANISOU 3178  CA  ASP A 446    17241   9398   9541   2529   1471   -131       C  
ATOM   3179  C   ASP A 446     141.942  94.385  55.718  1.00104.20           C  
ANISOU 3179  C   ASP A 446    19090  10020  10483   2640   1667   -203       C  
ATOM   3180  O   ASP A 446     143.075  94.870  55.797  1.00108.28           O  
ANISOU 3180  O   ASP A 446    19879  10206  11057   2220   1724   -281       O  
ATOM   3181  CB  ASP A 446     142.408  92.107  54.802  1.00102.72           C  
ANISOU 3181  CB  ASP A 446    17906  10396  10728   2312   1415    -19       C  
ATOM   3182  CG  ASP A 446     142.412  90.610  55.050  1.00104.02           C  
ANISOU 3182  CG  ASP A 446    17428  11006  11090   2140   1226     44       C  
ATOM   3183  OD1 ASP A 446     142.493  90.204  56.228  1.00102.72           O  
ANISOU 3183  OD1 ASP A 446    17072  11021  10935   1972   1134    -18       O  
ATOM   3184  OD2 ASP A 446     142.333  89.841  54.068  1.00103.66           O  
ANISOU 3184  OD2 ASP A 446    17096  11115  11175   2176   1174    155       O  
ATOM   3185  N   LYS A 447     140.869  95.123  55.435  1.00101.29           N  
ANISOU 3185  N   LYS A 447    19034   9577   9873   3189   1777   -183       N  
ATOM   3186  CA  LYS A 447     140.963  96.573  55.317  1.00112.34           C  
ANISOU 3186  CA  LYS A 447    21180  10455  11049   3337   1975   -253       C  
ATOM   3187  C   LYS A 447     140.411  97.307  56.531  1.00114.01           C  
ANISOU 3187  C   LYS A 447    21703  10599  11018   3550   2032   -385       C  
ATOM   3188  O   LYS A 447     140.876  98.411  56.835  1.00110.74           O  
ANISOU 3188  O   LYS A 447    21904   9715  10458   3445   2173   -496       O  
ATOM   3189  CB  LYS A 447     140.239  97.064  54.056  1.00119.87           C  
ANISOU 3189  CB  LYS A 447    22399  11287  11860   3850   2084   -138       C  
ATOM   3190  CG  LYS A 447     138.725  97.121  54.171  1.00127.44           C  
ANISOU 3190  CG  LYS A 447    23265  12560  12595   4522   2076   -104       C  
ATOM   3191  CD  LYS A 447     138.114  97.916  53.028  1.00134.25           C  
ANISOU 3191  CD  LYS A 447    24555  13206  13250   5057   2209    -16       C  
ATOM   3192  CE  LYS A 447     136.624  98.131  53.241  1.00139.36           C  
ANISOU 3192  CE  LYS A 447    25127  14189  13634   5735   2202      4       C  
ATOM   3193  NZ  LYS A 447     135.883  96.844  53.338  1.00140.75           N  
ANISOU 3193  NZ  LYS A 447    24531  15021  13925   5830   2029     48       N  
ATOM   3194  N   LEU A 448     139.438  96.723  57.234  1.00106.90           N  
ANISOU 3194  N   LEU A 448    20406  10152  10058   3831   1934   -382       N  
ATOM   3195  CA  LEU A 448     138.934  97.334  58.458  1.00 97.72           C  
ANISOU 3195  CA  LEU A 448    19493   8969   8667   4019   1984   -512       C  
ATOM   3196  C   LEU A 448     139.870  97.098  59.633  1.00 96.35           C  
ANISOU 3196  C   LEU A 448    19236   8775   8597   3461   1904   -638       C  
ATOM   3197  O   LEU A 448     139.982  97.957  60.515  1.00 92.39           O  
ANISOU 3197  O   LEU A 448    19178   8013   7911   3439   1987   -784       O  
ATOM   3198  CB  LEU A 448     137.545  96.790  58.795  1.00 98.99           C  
ANISOU 3198  CB  LEU A 448    19238   9661   8713   4510   1923   -465       C  
ATOM   3199  CG  LEU A 448     136.413  97.033  57.798  1.00 98.89           C  
ANISOU 3199  CG  LEU A 448    19254   9780   8539   5149   1986   -361       C  
ATOM   3200  CD1 LEU A 448     135.098  96.513  58.358  1.00 96.94           C  
ANISOU 3200  CD1 LEU A 448    18562  10108   8164   5561   1927   -352       C  
ATOM   3201  CD2 LEU A 448     136.306  98.505  57.460  1.00110.30           C  
ANISOU 3201  CD2 LEU A 448    21493  10699   9717   5512   2186   -405       C  
ATOM   3202  N   PHE A 449     140.545  95.952  59.664  1.00102.40           N  
ANISOU 3202  N   PHE A 449    19456   9813   9639   3025   1740   -590       N  
ATOM   3203  CA  PHE A 449     141.424  95.572  60.768  1.00103.32           C  
ANISOU 3203  CA  PHE A 449    19409   9992   9854   2519   1632   -695       C  
ATOM   3204  C   PHE A 449     142.773  95.128  60.216  1.00106.71           C  
ANISOU 3204  C   PHE A 449    19679  10318  10548   1973   1565   -671       C  
ATOM   3205  O   PHE A 449     143.125  93.944  60.279  1.00 80.49           O  
ANISOU 3205  O   PHE A 449    15808   7336   7440   1733   1403   -604       O  
ATOM   3206  CB  PHE A 449     140.786  94.466  61.609  1.00 85.28           C  
ANISOU 3206  CB  PHE A 449    16554   8243   7607   2586   1482   -659       C  
ATOM   3207  CG  PHE A 449     139.355  94.738  61.980  1.00 92.50           C  
ANISOU 3207  CG  PHE A 449    17504   9364   8277   3153   1548   -658       C  
ATOM   3208  CD1 PHE A 449     139.047  95.571  63.043  1.00 98.36           C  
ANISOU 3208  CD1 PHE A 449    18620   9980   8772   3299   1630   -800       C  
ATOM   3209  CD2 PHE A 449     138.319  94.156  61.269  1.00 92.03           C  
ANISOU 3209  CD2 PHE A 449    17095   9649   8223   3539   1529   -526       C  
ATOM   3210  CE1 PHE A 449     137.732  95.823  63.387  1.00 94.95           C  
ANISOU 3210  CE1 PHE A 449    18203   9770   8103   3846   1700   -803       C  
ATOM   3211  CE2 PHE A 449     137.001  94.404  61.609  1.00 90.21           C  
ANISOU 3211  CE2 PHE A 449    16854   9667   7756   4063   1591   -534       C  
ATOM   3212  CZ  PHE A 449     136.708  95.238  62.669  1.00 94.81           C  
ANISOU 3212  CZ  PHE A 449    17800  10129   8093   4230   1681   -669       C  
ATOM   3213  N   PRO A 450     143.557  96.055  59.666  1.00112.68           N  
ANISOU 3213  N   PRO A 450    20920  10611  11283   1768   1696   -727       N  
ATOM   3214  CA  PRO A 450     144.875  95.677  59.144  1.00104.31           C  
ANISOU 3214  CA  PRO A 450    19694   9480  10460   1237   1647   -716       C  
ATOM   3215  C   PRO A 450     145.835  95.357  60.279  1.00102.69           C  
ANISOU 3215  C   PRO A 450    19296   9391  10329    733   1520   -846       C  
ATOM   3216  O   PRO A 450     145.820  96.001  61.330  1.00 99.91           O  
ANISOU 3216  O   PRO A 450    19238   8921   9803    678   1546   -996       O  
ATOM   3217  CB  PRO A 450     145.325  96.920  58.364  1.00107.09           C  
ANISOU 3217  CB  PRO A 450    20696   9284  10708   1174   1856   -758       C  
ATOM   3218  CG  PRO A 450     144.097  97.782  58.235  1.00103.96           C  
ANISOU 3218  CG  PRO A 450    20757   8704  10040   1780   2000   -741       C  
ATOM   3219  CD  PRO A 450     143.276  97.482  59.442  1.00104.40           C  
ANISOU 3219  CD  PRO A 450    20605   9080   9984   2016   1907   -796       C  
ATOM   3220  N   GLY A 451     146.675  94.349  60.056  1.00 93.00           N  
ANISOU 3220  N   GLY A 451    17577   8408   9349    384   1379   -791       N  
ATOM   3221  CA  GLY A 451     147.652  93.908  61.027  1.00 85.70           C  
ANISOU 3221  CA  GLY A 451    16398   7657   8508    -75   1234   -896       C  
ATOM   3222  C   GLY A 451     147.366  92.548  61.625  1.00 84.72           C  
ANISOU 3222  C   GLY A 451    15674   8021   8494    -20   1031   -812       C  
ATOM   3223  O   GLY A 451     148.304  91.874  62.073  1.00 84.01           O  
ANISOU 3223  O   GLY A 451    15255   8130   8533   -386    885   -842       O  
ATOM   3224  N   PHE A 452     146.102  92.122  61.643  1.00 95.71           N  
ANISOU 3224  N   PHE A 452    16919   9622   9824    425   1021   -710       N  
ATOM   3225  CA  PHE A 452     145.762  90.825  62.219  1.00 97.86           C  
ANISOU 3225  CA  PHE A 452    16662  10339  10182    463    848   -626       C  
ATOM   3226  C   PHE A 452     146.109  89.677  61.276  1.00 96.97           C  
ANISOU 3226  C   PHE A 452    16106  10422  10317    378    755   -474       C  
ATOM   3227  O   PHE A 452     146.523  88.605  61.729  1.00 96.36           O  
ANISOU 3227  O   PHE A 452    15626  10628  10360    193    596   -433       O  
ATOM   3228  CB  PHE A 452     144.277  90.786  62.584  1.00 94.65           C  
ANISOU 3228  CB  PHE A 452    16244  10111   9607    933    886   -582       C  
ATOM   3229  CG  PHE A 452     143.890  91.768  63.652  1.00 95.13           C  
ANISOU 3229  CG  PHE A 452    16698  10034   9412   1048    965   -731       C  
ATOM   3230  CD1 PHE A 452     143.938  91.413  64.990  1.00 93.17           C  
ANISOU 3230  CD1 PHE A 452    16310  10000   9090    921    862   -802       C  
ATOM   3231  CD2 PHE A 452     143.481  93.048  63.320  1.00106.28           C  
ANISOU 3231  CD2 PHE A 452    18649  11092  10640   1299   1146   -798       C  
ATOM   3232  CE1 PHE A 452     143.584  92.315  65.976  1.00 91.43           C  
ANISOU 3232  CE1 PHE A 452    16463   9653   8621   1032    937   -947       C  
ATOM   3233  CE2 PHE A 452     143.124  93.955  64.303  1.00104.36           C  
ANISOU 3233  CE2 PHE A 452    18802  10703  10148   1423   1226   -942       C  
ATOM   3234  CZ  PHE A 452     143.177  93.587  65.632  1.00 94.90           C  
ANISOU 3234  CZ  PHE A 452    17443   9732   8883   1283   1121  -1021       C  
ATOM   3235  N   ARG A 453     145.939  89.879  59.971  1.00 99.51           N  
ANISOU 3235  N   ARG A 453    16520  10592  10700    528    853   -389       N  
ATOM   3236  CA  ARG A 453     146.268  88.858  58.983  1.00 95.42           C  
ANISOU 3236  CA  ARG A 453    15626  10228  10402    459    781   -254       C  
ATOM   3237  C   ARG A 453     147.753  88.945  58.653  1.00 91.50           C  
ANISOU 3237  C   ARG A 453    15130   9586  10050     23    769   -304       C  
ATOM   3238  O   ARG A 453     148.226  89.981  58.174  1.00 85.19           O  
ANISOU 3238  O   ARG A 453    14713   8450   9204    -90    910   -373       O  
ATOM   3239  CB  ARG A 453     145.419  89.044  57.726  1.00 94.15           C  
ANISOU 3239  CB  ARG A 453    15561   9991  10221    821    887   -147       C  
ATOM   3240  CG  ARG A 453     145.392  87.852  56.770  1.00 82.30           C  
ANISOU 3240  CG  ARG A 453    13645   8714   8911    843    803      0       C  
ATOM   3241  CD  ARG A 453     145.018  88.315  55.366  1.00102.21           C  
ANISOU 3241  CD  ARG A 453    16363  11055  11417   1087    927     74       C  
ATOM   3242  NE  ARG A 453     144.404  87.273  54.543  1.00103.19           N  
ANISOU 3242  NE  ARG A 453    16128  11442  11636   1270    856    207       N  
ATOM   3243  CZ  ARG A 453     145.079  86.423  53.776  1.00112.69           C  
ANISOU 3243  CZ  ARG A 453    17070  12710  13035   1083    793    282       C  
ATOM   3244  NH1 ARG A 453     144.431  85.517  53.056  1.00114.97           N  
ANISOU 3244  NH1 ARG A 453    17075  13226  13384   1257    735    388       N  
ATOM   3245  NH2 ARG A 453     146.403  86.471  53.733  1.00120.31           N  
ANISOU 3245  NH2 ARG A 453    18053  13532  14126    718    791    241       N  
ATOM   3246  N   THR A 454     148.489  87.865  58.916  1.00 94.33           N  
ANISOU 3246  N   THR A 454    15069  10202  10570   -220    610   -271       N  
ATOM   3247  CA  THR A 454     149.924  87.829  58.673  1.00 94.48           C  
ANISOU 3247  CA  THR A 454    15003  10174  10723   -626    582   -323       C  
ATOM   3248  C   THR A 454     150.327  86.457  58.155  1.00 80.55           C  
ANISOU 3248  C   THR A 454    12763   8679   9162   -669    452   -197       C  
ATOM   3249  O   THR A 454     149.741  85.437  58.528  1.00 73.89           O  
ANISOU 3249  O   THR A 454    11634   8097   8344   -508    335   -109       O  
ATOM   3250  CB  THR A 454     150.735  88.149  59.940  1.00105.14           C  
ANISOU 3250  CB  THR A 454    16387  11561  12000   -953    503   -483       C  
ATOM   3251  OG1 THR A 454     150.256  87.356  61.034  1.00105.66           O  
ANISOU 3251  OG1 THR A 454    16206  11920  12020   -846    352   -461       O  
ATOM   3252  CG2 THR A 454     150.630  89.625  60.297  1.00104.83           C  
ANISOU 3252  CG2 THR A 454    16883  11181  11767  -1002    654   -635       C  
ATOM   3253  N   GLU A 455     151.340  86.447  57.285  1.00 90.62           N  
ANISOU 3253  N   GLU A 455    13977   9881  10572   -893    488   -191       N  
ATOM   3254  CA  GLU A 455     151.985  85.228  56.798  1.00 94.47           C  
ANISOU 3254  CA  GLU A 455    14043  10603  11248   -974    374    -96       C  
ATOM   3255  C   GLU A 455     153.465  85.332  57.145  1.00 93.34           C  
ANISOU 3255  C   GLU A 455    13780  10523  11163  -1381    322   -207       C  
ATOM   3256  O   GLU A 455     154.286  85.727  56.303  1.00 89.91           O  
ANISOU 3256  O   GLU A 455    13394   9969  10801  -1581    420   -233       O  
ATOM   3257  CB  GLU A 455     151.786  85.034  55.296  1.00 99.02           C  
ANISOU 3257  CB  GLU A 455    14615  11084  11925   -824    470     21       C  
ATOM   3258  CG  GLU A 455     150.345  84.816  54.870  1.00108.76           C  
ANISOU 3258  CG  GLU A 455    15898  12324  13101   -424    500    129       C  
ATOM   3259  CD  GLU A 455     150.217  84.559  53.381  1.00118.32           C  
ANISOU 3259  CD  GLU A 455    17084  13470  14404   -288    574    238       C  
ATOM   3260  OE1 GLU A 455     151.251  84.297  52.730  1.00117.56           O  
ANISOU 3260  OE1 GLU A 455    16864  13365  14439   -495    583    249       O  
ATOM   3261  OE2 GLU A 455     149.083  84.621  52.862  1.00119.67           O  
ANISOU 3261  OE2 GLU A 455    17346  13619  14503     33    623    308       O  
ATOM   3262  N   PRO A 456     153.843  84.993  58.374  1.00 93.15           N  
ANISOU 3262  N   PRO A 456    13588  10709  11095  -1514    170   -278       N  
ATOM   3263  CA  PRO A 456     155.230  85.171  58.806  1.00 96.87           C  
ANISOU 3263  CA  PRO A 456    13932  11287  11588  -1900    108   -407       C  
ATOM   3264  C   PRO A 456     156.114  83.970  58.512  1.00 90.63           C  
ANISOU 3264  C   PRO A 456    12687  10794  10955  -1961    -28   -333       C  
ATOM   3265  O   PRO A 456     155.672  82.820  58.465  1.00 70.75           O  
ANISOU 3265  O   PRO A 456     9934   8446   8503  -1723   -131   -196       O  
ATOM   3266  CB  PRO A 456     155.097  85.380  60.324  1.00 97.97           C  
ANISOU 3266  CB  PRO A 456    14127  11527  11571  -1961     -2   -518       C  
ATOM   3267  CG  PRO A 456     153.632  85.099  60.669  1.00 93.26           C  
ANISOU 3267  CG  PRO A 456    13627  10916  10892  -1583     -3   -420       C  
ATOM   3268  CD  PRO A 456     152.998  84.487  59.465  1.00 85.47           C  
ANISOU 3268  CD  PRO A 456    12548   9900  10026  -1320     55   -251       C  
ATOM   3269  N   LEU A 457     157.394  84.270  58.307  1.00 95.39           N  
ANISOU 3269  N   LEU A 457    13179  11459  11606  -2294    -16   -434       N  
ATOM   3270  CA  LEU A 457     158.439  83.258  58.285  1.00 96.00           C  
ANISOU 3270  CA  LEU A 457    12812  11871  11792  -2381   -162   -408       C  
ATOM   3271  C   LEU A 457     158.932  83.040  59.709  1.00 88.48           C  
ANISOU 3271  C   LEU A 457    11692  11188  10738  -2509   -353   -509       C  
ATOM   3272  O   LEU A 457     159.262  84.001  60.412  1.00 80.68           O  
ANISOU 3272  O   LEU A 457    10878  10147   9629  -2774   -336   -679       O  
ATOM   3273  CB  LEU A 457     159.594  83.682  57.378  1.00 90.99           C  
ANISOU 3273  CB  LEU A 457    12098  11232  11242  -2677    -53   -474       C  
ATOM   3274  CG  LEU A 457     159.291  83.776  55.882  1.00 95.14           C  
ANISOU 3274  CG  LEU A 457    12748  11531  11870  -2557    129   -364       C  
ATOM   3275  CD1 LEU A 457     160.495  84.305  55.118  1.00107.64           C  
ANISOU 3275  CD1 LEU A 457    14271  13118  13508  -2904    254   -450       C  
ATOM   3276  CD2 LEU A 457     158.869  82.424  55.340  1.00 78.87           C  
ANISOU 3276  CD2 LEU A 457    10432   9610   9926  -2216     41   -182       C  
ATOM   3277  N   THR A 458     158.974  81.780  60.132  1.00 84.87           N  
ANISOU 3277  N   THR A 458    10925  11008  10315  -2318   -534   -406       N  
ATOM   3278  CA  THR A 458     159.297  81.429  61.507  1.00 77.16           C  
ANISOU 3278  CA  THR A 458     9800  10295   9222  -2361   -731   -469       C  
ATOM   3279  C   THR A 458     160.738  80.954  61.618  1.00 81.15           C  
ANISOU 3279  C   THR A 458     9919  11150   9766  -2541   -867   -530       C  
ATOM   3280  O   THR A 458     161.246  80.262  60.732  1.00 73.55           O  
ANISOU 3280  O   THR A 458     8717  10292   8938  -2466   -863   -442       O  
ATOM   3281  CB  THR A 458     158.357  80.340  62.023  1.00 75.59           C  
ANISOU 3281  CB  THR A 458     9550  10172   8997  -2020   -841   -310       C  
ATOM   3282  OG1 THR A 458     158.512  79.160  61.226  1.00 69.61           O  
ANISOU 3282  OG1 THR A 458     8549   9518   8381  -1829   -881   -153       O  
ATOM   3283  CG2 THR A 458     156.912  80.807  61.950  1.00 80.84           C  
ANISOU 3283  CG2 THR A 458    10549  10557   9609  -1838   -710   -261       C  
ATOM   3284  N   LEU A 459     161.390  81.330  62.715  1.00 99.70           N  
ANISOU 3284  N   LEU A 459    12201  13699  11981  -2764   -989   -688       N  
ATOM   3285  CA  LEU A 459     162.744  80.886  63.043  1.00103.58           C  
ANISOU 3285  CA  LEU A 459    12292  14600  12464  -2917  -1152   -765       C  
ATOM   3286  C   LEU A 459     162.638  79.973  64.264  1.00100.05           C  
ANISOU 3286  C   LEU A 459    11699  14417  11899  -2705  -1385   -711       C  
ATOM   3287  O   LEU A 459     162.724  80.425  65.407  1.00 98.44           O  
ANISOU 3287  O   LEU A 459    11564  14311  11528  -2843  -1484   -840       O  
ATOM   3288  CB  LEU A 459     163.667  82.075  63.301  1.00101.41           C  
ANISOU 3288  CB  LEU A 459    12038  14385  12109  -3384  -1112  -1009       C  
ATOM   3289  CG  LEU A 459     163.960  82.961  62.088  1.00 97.69           C  
ANISOU 3289  CG  LEU A 459    11706  13674  11739  -3640   -874  -1066       C  
ATOM   3290  CD1 LEU A 459     164.806  84.169  62.477  1.00 96.68           C  
ANISOU 3290  CD1 LEU A 459    11651  13581  11501  -4150   -827  -1320       C  
ATOM   3291  CD2 LEU A 459     164.645  82.150  61.001  1.00 97.41           C  
ANISOU 3291  CD2 LEU A 459    11321  13823  11869  -3548   -859   -960       C  
ATOM   3292  N   VAL A 460     162.447  78.679  64.010  1.00 99.56           N  
ANISOU 3292  N   VAL A 460    11464  14454  11909  -2369  -1467   -519       N  
ATOM   3293  CA  VAL A 460     162.236  77.692  65.069  1.00 92.48           C  
ANISOU 3293  CA  VAL A 460    10483  13756  10897  -2124  -1666   -428       C  
ATOM   3294  C   VAL A 460     163.605  77.285  65.609  1.00 90.83           C  
ANISOU 3294  C   VAL A 460     9899  13994  10616  -2194  -1869   -510       C  
ATOM   3295  O   VAL A 460     164.329  76.512  64.980  1.00 80.01           O  
ANISOU 3295  O   VAL A 460     8245  12816   9338  -2071  -1916   -440       O  
ATOM   3296  CB  VAL A 460     161.443  76.482  64.572  1.00 86.32           C  
ANISOU 3296  CB  VAL A 460     9725  12866  10206  -1756  -1655   -192       C  
ATOM   3297  CG1 VAL A 460     161.343  75.427  65.662  1.00 78.30           C  
ANISOU 3297  CG1 VAL A 460     8642  12054   9056  -1524  -1852    -93       C  
ATOM   3298  CG2 VAL A 460     160.059  76.911  64.113  1.00 88.45           C  
ANISOU 3298  CG2 VAL A 460    10330  12758  10520  -1687  -1470   -127       C  
ATOM   3299  N   MET A 461     163.956  77.797  66.786  1.00 90.64           N  
ANISOU 3299  N   MET A 461     9871  14157  10413  -2373  -1996   -665       N  
ATOM   3300  CA  MET A 461     165.226  77.487  67.426  1.00102.09           C  
ANISOU 3300  CA  MET A 461    10954  16080  11754  -2442  -2211   -765       C  
ATOM   3301  C   MET A 461     165.042  76.302  68.367  1.00101.00           C  
ANISOU 3301  C   MET A 461    10755  16135  11487  -2085  -2418   -621       C  
ATOM   3302  O   MET A 461     164.093  76.273  69.157  1.00 95.12           O  
ANISOU 3302  O   MET A 461    10281  15228  10631  -1983  -2431   -568       O  
ATOM   3303  CB  MET A 461     165.745  78.706  68.189  1.00103.40           C  
ANISOU 3303  CB  MET A 461    11154  16360  11775  -2858  -2242  -1029       C  
ATOM   3304  CG  MET A 461     165.692  79.994  67.378  1.00101.82           C  
ANISOU 3304  CG  MET A 461    11158  15858  11669  -3224  -2004  -1165       C  
ATOM   3305  SD  MET A 461     165.274  81.458  68.343  1.00 86.58           S  
ANISOU 3305  SD  MET A 461     9626  13717   9553  -3580  -1949  -1394       S  
ATOM   3306  CE  MET A 461     166.798  81.716  69.239  1.00106.84           C  
ANISOU 3306  CE  MET A 461    11812  16835  11946  -3933  -2174  -1646       C  
ATOM   3307  N   LYS A 462     165.939  75.322  68.270  1.00103.65           N  
ANISOU 3307  N   LYS A 462    10749  16812  11820  -1883  -2570   -553       N  
ATOM   3308  CA  LYS A 462     165.865  74.126  69.100  1.00108.36           C  
ANISOU 3308  CA  LYS A 462    11307  17586  12279  -1516  -2765   -402       C  
ATOM   3309  C   LYS A 462     167.261  73.721  69.545  1.00111.96           C  
ANISOU 3309  C   LYS A 462    11347  18579  12615  -1466  -2994   -483       C  
ATOM   3310  O   LYS A 462     168.161  73.566  68.714  1.00102.86           O  
ANISOU 3310  O   LYS A 462     9886  17629  11569  -1477  -2982   -512       O  
ATOM   3311  CB  LYS A 462     165.199  72.965  68.351  1.00110.78           C  
ANISOU 3311  CB  LYS A 462    11720  17659  12712  -1152  -2692   -147       C  
ATOM   3312  CG  LYS A 462     165.228  71.650  69.115  1.00113.68           C  
ANISOU 3312  CG  LYS A 462    12073  18191  12930   -767  -2880     22       C  
ATOM   3313  CD  LYS A 462     164.392  70.579  68.433  1.00113.76           C  
ANISOU 3313  CD  LYS A 462    12277  17898  13049   -466  -2781    262       C  
ATOM   3314  CE  LYS A 462     164.358  69.303  69.261  1.00129.01           C  
ANISOU 3314  CE  LYS A 462    14274  19938  14805   -105  -2950    434       C  
ATOM   3315  NZ  LYS A 462     163.465  68.273  68.664  1.00135.13           N  
ANISOU 3315  NZ  LYS A 462    15291  20388  15667    137  -2842    658       N  
ATOM   3316  N   ARG A 463     167.430  73.539  70.851  1.00129.79           N  
ANISOU 3316  N   ARG A 463    13591  21087  14637  -1394  -3202   -518       N  
ATOM   3317  CA  ARG A 463     168.688  73.089  71.429  1.00132.44           C  
ANISOU 3317  CA  ARG A 463    13536  21975  14811  -1288  -3453   -587       C  
ATOM   3318  C   ARG A 463     168.665  71.579  71.619  1.00138.41           C  
ANISOU 3318  C   ARG A 463    14281  22813  15495   -762  -3585   -344       C  
ATOM   3319  O   ARG A 463     167.673  71.017  72.092  1.00130.22           O  
ANISOU 3319  O   ARG A 463    13580  21502  14395   -547  -3572   -173       O  
ATOM   3320  CB  ARG A 463     168.951  73.772  72.772  1.00131.46           C  
ANISOU 3320  CB  ARG A 463    13404  22107  14438  -1506  -3621   -777       C  
ATOM   3321  CG  ARG A 463     169.149  75.269  72.682  1.00133.95           C  
ANISOU 3321  CG  ARG A 463    13732  22379  14783  -2049  -3512  -1047       C  
ATOM   3322  CD  ARG A 463     169.483  75.866  74.039  1.00137.07           C  
ANISOU 3322  CD  ARG A 463    14112  23058  14909  -2257  -3699  -1247       C  
ATOM   3323  NE  ARG A 463     170.606  75.184  74.673  1.00137.29           N  
ANISOU 3323  NE  ARG A 463    13730  23686  14749  -2071  -3986  -1280       N  
ATOM   3324  CZ  ARG A 463     171.173  75.576  75.808  1.00143.21           C  
ANISOU 3324  CZ  ARG A 463    14352  24819  15241  -2229  -4198  -1469       C  
ATOM   3325  NH1 ARG A 463     170.726  76.655  76.438  1.00143.64           N  
ANISOU 3325  NH1 ARG A 463    14680  24694  15202  -2593  -4146  -1647       N  
ATOM   3326  NH2 ARG A 463     172.191  74.892  76.312  1.00146.37           N  
ANISOU 3326  NH2 ARG A 463    14357  25790  15464  -2007  -4465  -1484       N  
ATOM   3327  N   GLU A 464     169.766  70.927  71.248  1.00150.31           N  
ANISOU 3327  N   GLU A 464    15413  24702  16998   -555  -3703   -331       N  
ATOM   3328  CA  GLU A 464     169.895  69.492  71.461  1.00157.12           C  
ANISOU 3328  CA  GLU A 464    16274  25667  17759    -28  -3842   -111       C  
ATOM   3329  C   GLU A 464     170.325  69.149  72.882  1.00150.49           C  
ANISOU 3329  C   GLU A 464    15369  25205  16605    155  -4119   -129       C  
ATOM   3330  O   GLU A 464     170.245  67.980  73.273  1.00153.21           O  
ANISOU 3330  O   GLU A 464    15829  25567  16818    604  -4233     72       O  
ATOM   3331  CB  GLU A 464     170.882  68.901  70.451  1.00167.04           C  
ANISOU 3331  CB  GLU A 464    17171  27173  19122    177  -3848    -83       C  
ATOM   3332  CG  GLU A 464     170.713  67.408  70.207  1.00173.58           C  
ANISOU 3332  CG  GLU A 464    18137  27885  19930    725  -3883    182       C  
ATOM   3333  CD  GLU A 464     171.521  66.917  69.023  1.00176.82           C  
ANISOU 3333  CD  GLU A 464    18254  28449  20482    910  -3830    208       C  
ATOM   3334  OE1 GLU A 464     170.931  66.296  68.113  1.00173.00           O  
ANISOU 3334  OE1 GLU A 464    17994  27581  20158   1082  -3670    374       O  
ATOM   3335  OE2 GLU A 464     172.745  67.161  68.998  1.00180.42           O  
ANISOU 3335  OE2 GLU A 464    18245  29428  20879    874  -3946     53       O  
ATOM   3336  N   ASP A 465     170.769  70.138  73.663  1.00139.40           N  
ANISOU 3336  N   ASP A 465    13812  24090  15065   -183  -4226   -365       N  
ATOM   3337  CA  ASP A 465     171.049  69.909  75.074  1.00131.69           C  
ANISOU 3337  CA  ASP A 465    12818  23446  13770    -37  -4485   -392       C  
ATOM   3338  C   ASP A 465     169.789  69.618  75.874  1.00129.62           C  
ANISOU 3338  C   ASP A 465    13056  22791  13402     84  -4449   -232       C  
ATOM   3339  O   ASP A 465     169.879  69.041  76.963  1.00129.92           O  
ANISOU 3339  O   ASP A 465    13162  23030  13171    348  -4649   -162       O  
ATOM   3340  CB  ASP A 465     171.744  71.127  75.690  1.00131.34           C  
ANISOU 3340  CB  ASP A 465    12523  23774  13606   -489  -4591   -707       C  
ATOM   3341  CG  ASP A 465     173.009  71.517  74.957  1.00136.25           C  
ANISOU 3341  CG  ASP A 465    12685  24726  14357   -680  -4565   -882       C  
ATOM   3342  OD1 ASP A 465     173.368  70.831  73.978  1.00134.72           O  
ANISOU 3342  OD1 ASP A 465    12324  24546  14316   -436  -4498   -763       O  
ATOM   3343  OD2 ASP A 465     173.645  72.513  75.363  1.00137.59           O  
ANISOU 3343  OD2 ASP A 465    12694  25106  14479  -1080  -4585  -1137       O  
ATOM   3344  N   GLY A 466     168.621  70.008  75.364  1.00124.81           N  
ANISOU 3344  N   GLY A 466    12791  21650  12981    -96  -4196   -176       N  
ATOM   3345  CA  GLY A 466     167.413  70.039  76.157  1.00118.96           C  
ANISOU 3345  CA  GLY A 466    12483  20582  12136    -94  -4137    -87       C  
ATOM   3346  C   GLY A 466     167.342  71.182  77.141  1.00114.86           C  
ANISOU 3346  C   GLY A 466    12021  20166  11454   -440  -4191   -311       C  
ATOM   3347  O   GLY A 466     166.281  71.392  77.744  1.00101.67           O  
ANISOU 3347  O   GLY A 466    10712  18210   9709   -483  -4107   -265       O  
ATOM   3348  N   GLU A 467     168.427  71.934  77.317  1.00125.15           N  
ANISOU 3348  N   GLU A 467    12982  21876  12693   -701  -4321   -561       N  
ATOM   3349  CA  GLU A 467     168.463  73.039  78.255  1.00130.70           C  
ANISOU 3349  CA  GLU A 467    13741  22696  13224  -1057  -4383   -802       C  
ATOM   3350  C   GLU A 467     167.690  74.232  77.699  1.00129.87           C  
ANISOU 3350  C   GLU A 467    13885  22156  13305  -1461  -4116   -922       C  
ATOM   3351  O   GLU A 467     167.483  74.340  76.488  1.00107.57           O  
ANISOU 3351  O   GLU A 467    11058  19065  10746  -1525  -3915   -873       O  
ATOM   3352  CB  GLU A 467     169.911  73.431  78.543  1.00133.49           C  
ANISOU 3352  CB  GLU A 467    13629  23645  13447  -1237  -4605  -1042       C  
ATOM   3353  CG  GLU A 467     170.776  72.299  79.088  1.00136.78           C  
ANISOU 3353  CG  GLU A 467    13770  24538  13661   -799  -4880   -937       C  
ATOM   3354  CD  GLU A 467     170.383  71.877  80.491  1.00137.98           C  
ANISOU 3354  CD  GLU A 467    14193  24705  13529   -562  -5026   -852       C  
ATOM   3355  OE1 GLU A 467     169.779  72.697  81.215  1.00137.41           O  
ANISOU 3355  OE1 GLU A 467    14353  24539  13318   -839  -5018   -982       O  
ATOM   3356  OE2 GLU A 467     170.677  70.723  80.869  1.00139.09           O  
ANISOU 3356  OE2 GLU A 467    14339  24934  13575    -96  -5137   -656       O  
ATOM   3357  N   PRO A 468     167.239  75.136  78.570  1.00142.70           N  
ANISOU 3357  N   PRO A 468    15749  23694  14776  -1714  -4107  -1079       N  
ATOM   3358  CA  PRO A 468     166.494  76.309  78.097  1.00143.34           C  
ANISOU 3358  CA  PRO A 468    16109  23352  15001  -2061  -3853  -1197       C  
ATOM   3359  C   PRO A 468     167.319  77.173  77.155  1.00133.02           C  
ANISOU 3359  C   PRO A 468    14569  22108  13865  -2443  -3766  -1397       C  
ATOM   3360  O   PRO A 468     168.547  77.242  77.249  1.00135.89           O  
ANISOU 3360  O   PRO A 468    14546  22927  14158  -2584  -3934  -1549       O  
ATOM   3361  CB  PRO A 468     166.165  77.064  79.390  1.00145.47           C  
ANISOU 3361  CB  PRO A 468    16623  23643  15007  -2239  -3921  -1363       C  
ATOM   3362  CG  PRO A 468     166.177  76.020  80.445  1.00147.29           C  
ANISOU 3362  CG  PRO A 468    16837  24130  14995  -1873  -4141  -1215       C  
ATOM   3363  CD  PRO A 468     167.249  75.052  80.041  1.00149.61           C  
ANISOU 3363  CD  PRO A 468    16714  24809  15323  -1637  -4315  -1125       C  
ATOM   3364  N   ILE A 469     166.623  77.838  76.238  1.00120.96           N  
ANISOU 3364  N   ILE A 469    13279  20132  12550  -2611  -3496  -1396       N  
ATOM   3365  CA  ILE A 469     167.252  78.823  75.365  1.00116.54           C  
ANISOU 3365  CA  ILE A 469    12603  19542  12136  -3023  -3366  -1590       C  
ATOM   3366  C   ILE A 469     167.314  80.149  76.112  1.00108.69           C  
ANISOU 3366  C   ILE A 469    11808  18514  10974  -3457  -3357  -1874       C  
ATOM   3367  O   ILE A 469     166.287  80.670  76.559  1.00101.62           O  
ANISOU 3367  O   ILE A 469    11333  17267  10011  -3466  -3245  -1880       O  
ATOM   3368  CB  ILE A 469     166.487  78.971  74.041  1.00115.30           C  
ANISOU 3368  CB  ILE A 469    12647  18908  12255  -2994  -3081  -1461       C  
ATOM   3369  CG1 ILE A 469     166.469  77.648  73.273  1.00111.09           C  
ANISOU 3369  CG1 ILE A 469    11923  18407  11878  -2587  -3092  -1198       C  
ATOM   3370  CG2 ILE A 469     167.105  80.071  73.189  1.00109.58           C  
ANISOU 3370  CG2 ILE A 469    11864  18117  11653  -3442  -2927  -1663       C  
ATOM   3371  CD1 ILE A 469     165.866  77.753  71.887  1.00103.11           C  
ANISOU 3371  CD1 ILE A 469    11052  16990  11134  -2569  -2832  -1085       C  
ATOM   3372  N   THR A 470     168.519  80.693  76.255  1.00106.04           N  
ANISOU 3372  N   THR A 470    11175  18559  10559  -3820  -3470  -2118       N  
ATOM   3373  CA  THR A 470     168.686  81.944  76.976  1.00108.80           C  
ANISOU 3373  CA  THR A 470    11713  18896  10729  -4276  -3472  -2413       C  
ATOM   3374  C   THR A 470     168.062  83.099  76.198  1.00119.97           C  
ANISOU 3374  C   THR A 470    13531  19762  12289  -4580  -3161  -2494       C  
ATOM   3375  O   THR A 470     167.859  83.030  74.982  1.00103.83           O  
ANISOU 3375  O   THR A 470    11498  17462  10489  -4531  -2965  -2371       O  
ATOM   3376  CB  THR A 470     170.167  82.230  77.229  1.00115.71           C  
ANISOU 3376  CB  THR A 470    12137  20340  11486  -4634  -3663  -2666       C  
ATOM   3377  OG1 THR A 470     170.778  82.703  76.023  1.00118.21           O  
ANISOU 3377  OG1 THR A 470    12282  20623  12011  -4949  -3494  -2746       O  
ATOM   3378  CG2 THR A 470     170.881  80.967  77.683  1.00118.73           C  
ANISOU 3378  CG2 THR A 470    12059  21288  11765  -4255  -3955  -2549       C  
ATOM   3379  N   ASP A 471     167.751  84.176  76.925  1.00133.02           N  
ANISOU 3379  N   ASP A 471    15546  21226  13770  -4877  -3115  -2704       N  
ATOM   3380  CA  ASP A 471     167.254  85.383  76.273  1.00137.55           C  
ANISOU 3380  CA  ASP A 471    16544  21283  14435  -5182  -2826  -2810       C  
ATOM   3381  C   ASP A 471     168.294  85.974  75.330  1.00139.40           C  
ANISOU 3381  C   ASP A 471    16564  21608  14795  -5630  -2731  -2968       C  
ATOM   3382  O   ASP A 471     167.937  86.614  74.334  1.00134.36           O  
ANISOU 3382  O   ASP A 471    16191  20540  14318  -5767  -2465  -2953       O  
ATOM   3383  CB  ASP A 471     166.838  86.418  77.320  1.00137.69           C  
ANISOU 3383  CB  ASP A 471    16997  21112  14206  -5418  -2813  -3030       C  
ATOM   3384  CG  ASP A 471     165.499  86.100  77.957  1.00135.39           C  
ANISOU 3384  CG  ASP A 471    17056  20554  13832  -4993  -2782  -2861       C  
ATOM   3385  OD1 ASP A 471     164.856  85.114  77.538  1.00131.74           O  
ANISOU 3385  OD1 ASP A 471    16517  20026  13514  -4551  -2755  -2576       O  
ATOM   3386  OD2 ASP A 471     165.089  86.840  78.877  1.00132.81           O  
ANISOU 3386  OD2 ASP A 471    17086  20089  13288  -5114  -2776  -3021       O  
ATOM   3387  N   ALA A 472     169.580  85.769  75.624  1.00144.93           N  
ANISOU 3387  N   ALA A 472    16780  22878  15409  -5858  -2942  -3119       N  
ATOM   3388  CA  ALA A 472     170.630  86.267  74.742  1.00146.57           C  
ANISOU 3388  CA  ALA A 472    16722  23242  15725  -6303  -2852  -3272       C  
ATOM   3389  C   ALA A 472     170.682  85.474  73.443  1.00149.72           C  
ANISOU 3389  C   ALA A 472    16871  23615  16402  -6023  -2743  -3029       C  
ATOM   3390  O   ALA A 472     170.918  86.044  72.371  1.00156.96           O  
ANISOU 3390  O   ALA A 472    17837  24326  17476  -6302  -2519  -3069       O  
ATOM   3391  CB  ALA A 472     171.981  86.221  75.454  1.00144.62           C  
ANISOU 3391  CB  ALA A 472    16011  23601  15336  -6502  -3071  -3453       C  
ATOM   3392  N   GLN A 473     170.472  84.156  73.517  1.00140.81           N  
ANISOU 3392  N   GLN A 473    15499  22681  15321  -5476  -2893  -2778       N  
ATOM   3393  CA  GLN A 473     170.413  83.347  72.303  1.00134.72           C  
ANISOU 3393  CA  GLN A 473    14544  21841  14802  -5171  -2787  -2539       C  
ATOM   3394  C   GLN A 473     169.278  83.793  71.393  1.00123.80           C  
ANISOU 3394  C   GLN A 473    13640  19798  13600  -5105  -2483  -2407       C  
ATOM   3395  O   GLN A 473     169.393  83.699  70.166  1.00114.45           O  
ANISOU 3395  O   GLN A 473    12381  18482  12624  -5099  -2315  -2313       O  
ATOM   3396  CB  GLN A 473     170.252  81.868  72.658  1.00135.08           C  
ANISOU 3396  CB  GLN A 473    14352  22139  14835  -4586  -2993  -2293       C  
ATOM   3397  CG  GLN A 473     171.491  81.209  73.244  1.00133.42           C  
ANISOU 3397  CG  GLN A 473    13587  22629  14479  -4538  -3288  -2370       C  
ATOM   3398  CD  GLN A 473     171.207  79.805  73.744  1.00124.88           C  
ANISOU 3398  CD  GLN A 473    12394  21717  13337  -3937  -3485  -2121       C  
ATOM   3399  OE1 GLN A 473     170.128  79.531  74.262  1.00119.25           O  
ANISOU 3399  OE1 GLN A 473    12045  20689  12576  -3671  -3473  -1976       O  
ATOM   3400  NE2 GLN A 473     172.170  78.907  73.580  1.00122.23           N  
ANISOU 3400  NE2 GLN A 473    11570  21879  12993  -3716  -3656  -2069       N  
ATOM   3401  N   ILE A 474     168.179  84.276  71.973  1.00123.23           N  
ANISOU 3401  N   ILE A 474    14056  19328  13438  -5037  -2412  -2399       N  
ATOM   3402  CA  ILE A 474     167.067  84.772  71.168  1.00116.82           C  
ANISOU 3402  CA  ILE A 474    13704  17916  12765  -4954  -2132  -2289       C  
ATOM   3403  C   ILE A 474     167.423  86.115  70.545  1.00118.46           C  
ANISOU 3403  C   ILE A 474    14148  17864  12999  -5467  -1910  -2495       C  
ATOM   3404  O   ILE A 474     167.206  86.342  69.349  1.00110.48           O  
ANISOU 3404  O   ILE A 474    13259  16549  12168  -5477  -1687  -2407       O  
ATOM   3405  CB  ILE A 474     165.789  84.864  72.020  1.00111.66           C  
ANISOU 3405  CB  ILE A 474    13474  16966  11984  -4696  -2124  -2224       C  
ATOM   3406  CG1 ILE A 474     165.500  83.520  72.691  1.00113.16           C  
ANISOU 3406  CG1 ILE A 474    13445  17426  12125  -4233  -2338  -2024       C  
ATOM   3407  CG2 ILE A 474     164.609  85.297  71.164  1.00103.17           C  
ANISOU 3407  CG2 ILE A 474    12831  15327  11042  -4547  -1848  -2098       C  
ATOM   3408  CD1 ILE A 474     164.369  83.571  73.694  1.00112.15           C  
ANISOU 3408  CD1 ILE A 474    13675  17103  11833  -4017  -2352  -1981       C  
ATOM   3409  N   ALA A 475     167.981  87.026  71.347  1.00130.27           N  
ANISOU 3409  N   ALA A 475    15730  19467  14298  -5913  -1965  -2774       N  
ATOM   3410  CA  ALA A 475     168.363  88.338  70.838  1.00129.50           C  
ANISOU 3410  CA  ALA A 475    15902  19107  14194  -6454  -1749  -2989       C  
ATOM   3411  C   ALA A 475     169.541  88.267  69.876  1.00132.38           C  
ANISOU 3411  C   ALA A 475    15846  19758  14694  -6755  -1703  -3039       C  
ATOM   3412  O   ALA A 475     169.759  89.213  69.111  1.00129.55           O  
ANISOU 3412  O   ALA A 475    15723  19114  14385  -7148  -1465  -3146       O  
ATOM   3413  CB  ALA A 475     168.694  89.277  71.998  1.00123.81           C  
ANISOU 3413  CB  ALA A 475    15381  18452  13210  -6880  -1833  -3291       C  
ATOM   3414  N   ASP A 476     170.307  87.174  69.900  1.00135.51           N  
ANISOU 3414  N   ASP A 476    15642  20710  15136  -6569  -1914  -2964       N  
ATOM   3415  CA  ASP A 476     171.392  86.998  68.940  1.00138.55           C  
ANISOU 3415  CA  ASP A 476    15587  21404  15653  -6786  -1865  -2991       C  
ATOM   3416  C   ASP A 476     170.862  86.505  67.599  1.00123.95           C  
ANISOU 3416  C   ASP A 476    13795  19248  14054  -6454  -1669  -2727       C  
ATOM   3417  O   ASP A 476     171.227  87.037  66.544  1.00115.38           O  
ANISOU 3417  O   ASP A 476    12744  18013  13083  -6740  -1447  -2762       O  
ATOM   3418  CB  ASP A 476     172.435  86.028  69.496  1.00143.78           C  
ANISOU 3418  CB  ASP A 476    15582  22806  16241  -6675  -2171  -3019       C  
ATOM   3419  CG  ASP A 476     173.468  85.628  68.461  1.00142.64           C  
ANISOU 3419  CG  ASP A 476    14934  23021  16242  -6766  -2126  -3003       C  
ATOM   3420  OD1 ASP A 476     174.309  86.477  68.097  1.00142.99           O  
ANISOU 3420  OD1 ASP A 476    14951  23080  16298  -7174  -1958  -3151       O  
ATOM   3421  OD2 ASP A 476     173.437  84.464  68.009  1.00137.47           O  
ANISOU 3421  OD2 ASP A 476    13994  22526  15711  -6278  -2197  -2773       O  
ATOM   3422  N   MET A 477     170.004  85.483  67.622  1.00120.59           N  
ANISOU 3422  N   MET A 477    13386  18728  13704  -5866  -1744  -2466       N  
ATOM   3423  CA  MET A 477     169.350  85.040  66.396  1.00117.18           C  
ANISOU 3423  CA  MET A 477    13066  17967  13491  -5544  -1560  -2223       C  
ATOM   3424  C   MET A 477     168.471  86.139  65.814  1.00128.49           C  
ANISOU 3424  C   MET A 477    15094  18766  14961  -5692  -1271  -2232       C  
ATOM   3425  O   MET A 477     168.344  86.251  64.589  1.00137.13           O  
ANISOU 3425  O   MET A 477    16277  19611  16214  -5677  -1061  -2132       O  
ATOM   3426  CB  MET A 477     168.525  83.780  66.668  1.00106.30           C  
ANISOU 3426  CB  MET A 477    11640  16595  12152  -4931  -1700  -1964       C  
ATOM   3427  CG  MET A 477     167.788  83.213  65.460  1.00 97.31           C  
ANISOU 3427  CG  MET A 477    10606  15143  11226  -4577  -1537  -1713       C  
ATOM   3428  SD  MET A 477     168.735  81.994  64.524  1.00 91.16           S  
ANISOU 3428  SD  MET A 477     9261  14768  10606  -4362  -1603  -1579       S  
ATOM   3429  CE  MET A 477     169.693  83.049  63.441  1.00 99.28           C  
ANISOU 3429  CE  MET A 477    10221  15785  11715  -4902  -1370  -1754       C  
ATOM   3430  N   ARG A 478     167.867  86.963  66.674  1.00122.88           N  
ANISOU 3430  N   ARG A 478    14810  17792  14088  -5816  -1255  -2353       N  
ATOM   3431  CA  ARG A 478     167.038  88.062  66.192  1.00124.42           C  
ANISOU 3431  CA  ARG A 478    15608  17382  14282  -5926   -983  -2372       C  
ATOM   3432  C   ARG A 478     167.877  89.150  65.536  1.00124.39           C  
ANISOU 3432  C   ARG A 478    15715  17271  14278  -6503   -784  -2566       C  
ATOM   3433  O   ARG A 478     167.428  89.779  64.571  1.00117.93           O  
ANISOU 3433  O   ARG A 478    15275  15996  13536  -6540   -522  -2509       O  
ATOM   3434  CB  ARG A 478     166.217  88.641  67.346  1.00133.08           C  
ANISOU 3434  CB  ARG A 478    17131  18253  15182  -5887  -1022  -2463       C  
ATOM   3435  CG  ARG A 478     165.248  89.738  66.938  1.00140.58           C  
ANISOU 3435  CG  ARG A 478    18739  18574  16103  -5905   -751  -2472       C  
ATOM   3436  CD  ARG A 478     164.461  90.253  68.132  1.00146.76           C  
ANISOU 3436  CD  ARG A 478    19915  19173  16673  -5829   -797  -2566       C  
ATOM   3437  NE  ARG A 478     163.691  89.196  68.782  1.00153.05           N  
ANISOU 3437  NE  ARG A 478    20548  20142  17462  -5324   -973  -2387       N  
ATOM   3438  CZ  ARG A 478     162.869  89.393  69.807  1.00165.55           C  
ANISOU 3438  CZ  ARG A 478    22414  21615  18873  -5150  -1022  -2417       C  
ATOM   3439  NH1 ARG A 478     162.705  90.612  70.304  1.00169.38           N  
ANISOU 3439  NH1 ARG A 478    23372  21807  19178  -5415   -915  -2624       N  
ATOM   3440  NH2 ARG A 478     162.208  88.372  70.337  1.00170.80           N  
ANISOU 3440  NH2 ARG A 478    22909  22453  19534  -4717  -1167  -2242       N  
ATOM   3441  N   ALA A 479     169.090  89.386  66.041  1.00133.11           N  
ANISOU 3441  N   ALA A 479    16497  18798  15282  -6961   -901  -2795       N  
ATOM   3442  CA  ALA A 479     169.954  90.401  65.448  1.00131.37           C  
ANISOU 3442  CA  ALA A 479    16355  18513  15047  -7573   -706  -2994       C  
ATOM   3443  C   ALA A 479     170.405  90.006  64.048  1.00134.81           C  
ANISOU 3443  C   ALA A 479    16527  19006  15690  -7548   -557  -2856       C  
ATOM   3444  O   ALA A 479     170.603  90.877  63.194  1.00135.72           O  
ANISOU 3444  O   ALA A 479    16919  18813  15834  -7905   -291  -2917       O  
ATOM   3445  CB  ALA A 479     171.165  90.652  66.344  1.00130.56           C  
ANISOU 3445  CB  ALA A 479    15895  18934  14779  -8075   -888  -3280       C  
ATOM   3446  N   LYS A 480     170.574  88.707  63.796  1.00136.18           N  
ANISOU 3446  N   LYS A 480    16196  19555  15993  -7129   -715  -2671       N  
ATOM   3447  CA  LYS A 480     170.958  88.257  62.463  1.00134.25           C  
ANISOU 3447  CA  LYS A 480    15704  19367  15939  -7052   -577  -2532       C  
ATOM   3448  C   LYS A 480     169.795  88.345  61.485  1.00123.85           C  
ANISOU 3448  C   LYS A 480    14849  17460  14748  -6717   -354  -2312       C  
ATOM   3449  O   LYS A 480     170.010  88.546  60.284  1.00124.40           O  
ANISOU 3449  O   LYS A 480    14957  17378  14933  -6818   -137  -2252       O  
ATOM   3450  CB  LYS A 480     171.491  86.827  62.528  1.00129.20           C  
ANISOU 3450  CB  LYS A 480    14419  19295  15377  -6678   -818  -2409       C  
ATOM   3451  CG  LYS A 480     172.729  86.681  63.396  1.00128.24           C  
ANISOU 3451  CG  LYS A 480    13773  19833  15121  -6970  -1048  -2622       C  
ATOM   3452  CD  LYS A 480     173.254  85.258  63.386  1.00126.34           C  
ANISOU 3452  CD  LYS A 480    12927  20133  14943  -6539  -1272  -2484       C  
ATOM   3453  CE  LYS A 480     174.598  85.170  64.089  1.00136.07           C  
ANISOU 3453  CE  LYS A 480    13590  22076  16033  -6837  -1484  -2706       C  
ATOM   3454  NZ  LYS A 480     174.508  85.600  65.510  1.00152.00           N  
ANISOU 3454  NZ  LYS A 480    15753  24160  17840  -6963  -1664  -2864       N  
ATOM   3455  N   ALA A 481     168.563  88.203  61.978  1.00112.87           N  
ANISOU 3455  N   ALA A 481    13801  15760  13326  -6317   -402  -2193       N  
ATOM   3456  CA  ALA A 481     167.395  88.311  61.115  1.00102.58           C  
ANISOU 3456  CA  ALA A 481    12925  13935  12117  -5982   -207  -1996       C  
ATOM   3457  C   ALA A 481     167.130  89.745  60.676  1.00110.17           C  
ANISOU 3457  C   ALA A 481    14483  14371  13005  -6320     76  -2102       C  
ATOM   3458  O   ALA A 481     166.446  89.956  59.668  1.00107.32           O  
ANISOU 3458  O   ALA A 481    14440  13612  12725  -6125    280  -1956       O  
ATOM   3459  CB  ALA A 481     166.169  87.739  61.827  1.00 98.02           C  
ANISOU 3459  CB  ALA A 481    12499  13237  11507  -5475   -341  -1853       C  
ATOM   3460  N   LEU A 482     167.654  90.732  61.405  1.00117.57           N  
ANISOU 3460  N   LEU A 482    15602  15292  13776  -6817     94  -2356       N  
ATOM   3461  CA  LEU A 482     167.517  92.130  61.019  1.00125.56           C  
ANISOU 3461  CA  LEU A 482    17223  15790  14694  -7187    373  -2475       C  
ATOM   3462  C   LEU A 482     168.519  92.551  59.954  1.00136.15           C  
ANISOU 3462  C   LEU A 482    18470  17160  16103  -7641    579  -2537       C  
ATOM   3463  O   LEU A 482     168.340  93.612  59.345  1.00131.81           O  
ANISOU 3463  O   LEU A 482    18461  16124  15499  -7887    854  -2578       O  
ATOM   3464  CB  LEU A 482     167.657  93.030  62.249  1.00121.57           C  
ANISOU 3464  CB  LEU A 482    17000  15226  13965  -7561    318  -2735       C  
ATOM   3465  CG  LEU A 482     166.525  92.920  63.272  1.00111.65           C  
ANISOU 3465  CG  LEU A 482    16006  13813  12601  -7147    187  -2691       C  
ATOM   3466  CD1 LEU A 482     166.806  93.791  64.480  1.00116.15           C  
ANISOU 3466  CD1 LEU A 482    16826  14368  12939  -7555    127  -2970       C  
ATOM   3467  CD2 LEU A 482     165.192  93.294  62.638  1.00112.56           C  
ANISOU 3467  CD2 LEU A 482    16687  13346  12737  -6737    392  -2516       C  
ATOM   3468  N   THR A 483     169.562  91.755  59.715  1.00141.18           N  
ANISOU 3468  N   THR A 483    18450  18352  16840  -7746    463  -2542       N  
ATOM   3469  CA  THR A 483     170.466  91.992  58.596  1.00136.81           C  
ANISOU 3469  CA  THR A 483    17742  17874  16367  -8108    666  -2567       C  
ATOM   3470  C   THR A 483     169.850  91.610  57.258  1.00130.68           C  
ANISOU 3470  C   THR A 483    17093  16808  15753  -7705    838  -2305       C  
ATOM   3471  O   THR A 483     170.482  91.829  56.218  1.00134.82           O  
ANISOU 3471  O   THR A 483    17554  17332  16341  -7963   1040  -2299       O  
ATOM   3472  CB  THR A 483     171.772  91.221  58.801  1.00124.69           C  
ANISOU 3472  CB  THR A 483    15426  17080  14872  -8300    476  -2660       C  
ATOM   3473  OG1 THR A 483     171.492  89.818  58.898  1.00111.70           O  
ANISOU 3473  OG1 THR A 483    13343  15753  13344  -7694    243  -2460       O  
ATOM   3474  CG2 THR A 483     172.470  91.682  60.069  1.00122.96           C  
ANISOU 3474  CG2 THR A 483    15083  17167  14470  -8620    315  -2898       C  
ATOM   3475  N   VAL A 484     168.646  91.046  57.262  1.00123.44           N  
ANISOU 3475  N   VAL A 484    16342  15667  14892  -7099    766  -2097       N  
ATOM   3476  CA  VAL A 484     167.936  90.651  56.052  1.00123.82           C  
ANISOU 3476  CA  VAL A 484    16523  15446  15076  -6680    905  -1852       C  
ATOM   3477  C   VAL A 484     166.796  91.639  55.853  1.00127.30           C  
ANISOU 3477  C   VAL A 484    17712  15232  15424  -6562   1103  -1810       C  
ATOM   3478  O   VAL A 484     165.859  91.691  56.660  1.00116.94           O  
ANISOU 3478  O   VAL A 484    16644  13756  14031  -6280   1001  -1793       O  
ATOM   3479  CB  VAL A 484     167.415  89.211  56.143  1.00119.49           C  
ANISOU 3479  CB  VAL A 484    15585  15164  14653  -6079    676  -1649       C  
ATOM   3480  CG1 VAL A 484     166.747  88.806  54.840  1.00114.18           C  
ANISOU 3480  CG1 VAL A 484    15031  14240  14111  -5693    819  -1417       C  
ATOM   3481  CG2 VAL A 484     168.546  88.256  56.495  1.00121.34           C  
ANISOU 3481  CG2 VAL A 484    15115  16047  14942  -6154    462  -1702       C  
ATOM   3482  N   SER A 485     166.871  92.422  54.781  1.00132.10           N  
ANISOU 3482  N   SER A 485    18692  15475  16026  -6759   1392  -1789       N  
ATOM   3483  CA  SER A 485     165.839  93.404  54.488  1.00126.99           C  
ANISOU 3483  CA  SER A 485    18786  14195  15269  -6623   1598  -1742       C  
ATOM   3484  C   SER A 485     164.576  92.707  53.983  1.00117.16           C  
ANISOU 3484  C   SER A 485    17605  12800  14109  -5931   1557  -1488       C  
ATOM   3485  O   SER A 485     164.534  91.490  53.788  1.00106.47           O  
ANISOU 3485  O   SER A 485    15758  11793  12903  -5603   1390  -1351       O  
ATOM   3486  CB  SER A 485     166.350  94.420  53.468  1.00124.64           C  
ANISOU 3486  CB  SER A 485    18879  13555  14922  -7042   1925  -1786       C  
ATOM   3487  OG  SER A 485     166.716  93.786  52.254  1.00126.86           O  
ANISOU 3487  OG  SER A 485    18853  13991  15356  -6941   2005  -1635       O  
ATOM   3488  N   GLY A 486     163.526  93.496  53.778  1.00116.88           N  
ANISOU 3488  N   GLY A 486    18199  12247  13962  -5703   1710  -1432       N  
ATOM   3489  CA  GLY A 486     162.307  92.966  53.202  1.00119.31           C  
ANISOU 3489  CA  GLY A 486    18596  12410  14326  -5079   1697  -1206       C  
ATOM   3490  C   GLY A 486     161.344  92.336  54.178  1.00120.04           C  
ANISOU 3490  C   GLY A 486    18566  12640  14404  -4648   1469  -1157       C  
ATOM   3491  O   GLY A 486     160.453  91.592  53.757  1.00114.16           O  
ANISOU 3491  O   GLY A 486    17717  11924  13734  -4154   1407   -972       O  
ATOM   3492  N   PHE A 487     161.490  92.606  55.471  1.00131.19           N  
ANISOU 3492  N   PHE A 487    19990  14148  15709  -4835   1345  -1322       N  
ATOM   3493  CA  PHE A 487     160.593  92.073  56.483  1.00121.46           C  
ANISOU 3493  CA  PHE A 487    18669  13043  14437  -4459   1145  -1286       C  
ATOM   3494  C   PHE A 487     159.727  93.187  57.056  1.00115.57           C  
ANISOU 3494  C   PHE A 487    18553  11876  13483  -4375   1253  -1368       C  
ATOM   3495  O   PHE A 487     160.166  94.334  57.191  1.00 92.09           O  
ANISOU 3495  O   PHE A 487    16002   8613  10375  -4761   1409  -1533       O  
ATOM   3496  CB  PHE A 487     161.368  91.371  57.602  1.00109.19           C  
ANISOU 3496  CB  PHE A 487    16607  11974  12905  -4660    890  -1396       C  
ATOM   3497  CG  PHE A 487     161.876  90.011  57.219  1.00 96.30           C  
ANISOU 3497  CG  PHE A 487    14344  10785  11461  -4532    732  -1272       C  
ATOM   3498  CD1 PHE A 487     161.017  88.924  57.178  1.00 88.81           C  
ANISOU 3498  CD1 PHE A 487    13182   9966  10597  -4031    600  -1083       C  
ATOM   3499  CD2 PHE A 487     163.206  89.821  56.887  1.00103.48           C  
ANISOU 3499  CD2 PHE A 487    14885  11984  12450  -4911    725  -1350       C  
ATOM   3500  CE1 PHE A 487     161.478  87.668  56.818  1.00 89.49           C  
ANISOU 3500  CE1 PHE A 487    12743  10418  10839  -3902    464   -971       C  
ATOM   3501  CE2 PHE A 487     163.673  88.570  56.528  1.00100.10           C  
ANISOU 3501  CE2 PHE A 487    13901  11955  12178  -4749    585  -1236       C  
ATOM   3502  CZ  PHE A 487     162.808  87.493  56.493  1.00 95.49           C  
ANISOU 3502  CZ  PHE A 487    13156  11451  11673  -4239    456  -1046       C  
ATOM   3503  N   THR A 488     158.488  92.830  57.386  1.00111.76           N  
ANISOU 3503  N   THR A 488    18134  11365  12965  -3867   1177  -1255       N  
ATOM   3504  CA  THR A 488     157.493  93.810  57.793  1.00108.23           C  
ANISOU 3504  CA  THR A 488    18278  10526  12316  -3660   1291  -1300       C  
ATOM   3505  C   THR A 488     157.900  94.490  59.095  1.00115.55           C  
ANISOU 3505  C   THR A 488    19392  11432  13078  -4002   1241  -1532       C  
ATOM   3506  O   THR A 488     158.524  93.887  59.972  1.00114.70           O  
ANISOU 3506  O   THR A 488    18863  11713  13006  -4203   1037  -1616       O  
ATOM   3507  CB  THR A 488     156.128  93.141  57.962  1.00103.32           C  
ANISOU 3507  CB  THR A 488    17569   9995  11693  -3058   1195  -1140       C  
ATOM   3508  OG1 THR A 488     155.927  92.191  56.908  1.00114.33           O  
ANISOU 3508  OG1 THR A 488    18624  11550  13267  -2802   1170   -941       O  
ATOM   3509  CG2 THR A 488     155.018  94.178  57.908  1.00 95.63           C  
ANISOU 3509  CG2 THR A 488    17224   8589  10523  -2743   1369  -1139       C  
ATOM   3510  N   ASP A 489     157.545  95.768  59.207  1.00118.20           N  
ANISOU 3510  N   ASP A 489    20392  11302  13217  -4055   1432  -1637       N  
ATOM   3511  CA  ASP A 489     157.826  96.558  60.406  1.00116.02           C  
ANISOU 3511  CA  ASP A 489    20406  10927  12748  -4368   1414  -1872       C  
ATOM   3512  C   ASP A 489     156.711  97.578  60.581  1.00125.40           C  
ANISOU 3512  C   ASP A 489    22296  11635  13714  -4041   1581  -1890       C  
ATOM   3513  O   ASP A 489     156.879  98.770  60.295  1.00131.78           O  
ANISOU 3513  O   ASP A 489    23719  11976  14375  -4261   1804  -1995       O  
ATOM   3514  CB  ASP A 489     159.190  97.243  60.309  1.00113.64           C  
ANISOU 3514  CB  ASP A 489    20197  10556  12425  -5066   1507  -2068       C  
ATOM   3515  CG  ASP A 489     159.595  97.931  61.598  1.00118.21           C  
ANISOU 3515  CG  ASP A 489    20994  11109  12811  -5447   1452  -2331       C  
ATOM   3516  OD1 ASP A 489     158.885  97.775  62.614  1.00116.26           O  
ANISOU 3516  OD1 ASP A 489    20772  10943  12460  -5163   1321  -2356       O  
ATOM   3517  OD2 ASP A 489     160.629  98.630  61.595  1.00121.80           O  
ANISOU 3517  OD2 ASP A 489    21598  11474  13208  -6049   1543  -2521       O  
ATOM   3518  N   PRO A 490     155.540  97.140  61.056  1.00127.01           N  
ANISOU 3518  N   PRO A 490    22442  11942  13874  -3501   1487  -1790       N  
ATOM   3519  CA  PRO A 490     154.414  98.077  61.199  1.00122.54           C  
ANISOU 3519  CA  PRO A 490    22516  10960  13084  -3115   1646  -1799       C  
ATOM   3520  C   PRO A 490     154.587  99.075  62.331  1.00121.23           C  
ANISOU 3520  C   PRO A 490    22821  10562  12679  -3375   1685  -2044       C  
ATOM   3521  O   PRO A 490     153.943 100.131  62.301  1.00116.71           O  
ANISOU 3521  O   PRO A 490    22921   9528  11895  -3175   1876  -2090       O  
ATOM   3522  CB  PRO A 490     153.218  97.150  61.450  1.00118.41           C  
ANISOU 3522  CB  PRO A 490    21655  10737  12597  -2516   1507  -1631       C  
ATOM   3523  CG  PRO A 490     153.818  95.941  62.084  1.00112.55           C  
ANISOU 3523  CG  PRO A 490    20218  10528  12017  -2707   1248  -1626       C  
ATOM   3524  CD  PRO A 490     155.175  95.768  61.453  1.00117.86           C  
ANISOU 3524  CD  PRO A 490    20642  11284  12854  -3212   1245  -1659       C  
ATOM   3525  N   ASP A 491     155.429  98.781  63.323  1.00129.85           N  
ANISOU 3525  N   ASP A 491    23599  11957  13779  -3796   1509  -2205       N  
ATOM   3526  CA  ASP A 491     155.627  99.696  64.440  1.00137.94           C  
ANISOU 3526  CA  ASP A 491    25057  12787  14566  -4073   1530  -2456       C  
ATOM   3527  C   ASP A 491     156.667 100.770  64.152  1.00138.05           C  
ANISOU 3527  C   ASP A 491    25511  12444  14499  -4698   1705  -2649       C  
ATOM   3528  O   ASP A 491     156.737 101.754  64.896  1.00142.46           O  
ANISOU 3528  O   ASP A 491    26601  12702  14824  -4922   1784  -2864       O  
ATOM   3529  CB  ASP A 491     156.047  98.923  65.694  1.00144.41           C  
ANISOU 3529  CB  ASP A 491    25359  14110  15398  -4243   1253  -2553       C  
ATOM   3530  CG  ASP A 491     154.987  97.947  66.163  1.00142.84           C  
ANISOU 3530  CG  ASP A 491    24806  14233  15233  -3671   1098  -2387       C  
ATOM   3531  OD1 ASP A 491     153.786  98.235  65.981  1.00142.79           O  
ANISOU 3531  OD1 ASP A 491    25122  14002  15131  -3159   1215  -2288       O  
ATOM   3532  OD2 ASP A 491     155.358  96.891  66.719  1.00140.61           O  
ANISOU 3532  OD2 ASP A 491    23928  14437  15060  -3731    863  -2356       O  
ATOM   3533  N   ASN A 492     157.468 100.603  63.096  1.00140.78           N  
ANISOU 3533  N   ASN A 492    25657  12814  15017  -4995   1775  -2584       N  
ATOM   3534  CA  ASN A 492     158.605 101.475  62.797  1.00138.68           C  
ANISOU 3534  CA  ASN A 492    25693  12302  14698  -5679   1932  -2768       C  
ATOM   3535  C   ASN A 492     159.619 101.448  63.944  1.00133.38           C  
ANISOU 3535  C   ASN A 492    24736  11970  13973  -6240   1752  -3016       C  
ATOM   3536  O   ASN A 492     159.939 102.466  64.559  1.00126.94           O  
ANISOU 3536  O   ASN A 492    24248  11013  12972  -6485   1829  -3151       O  
ATOM   3537  CB  ASN A 492     158.147 102.907  62.489  1.00132.87           C  
ANISOU 3537  CB  ASN A 492    25724  11015  13744  -5536   2212  -2744       C  
ATOM   3538  CG  ASN A 492     157.200 102.976  61.304  1.00137.29           C  
ANISOU 3538  CG  ASN A 492    26571  11261  14330  -4988   2384  -2508       C  
ATOM   3539  OD1 ASN A 492     156.059 103.421  61.430  1.00136.49           O  
ANISOU 3539  OD1 ASN A 492    26904  10884  14070  -4455   2463  -2440       O  
ATOM   3540  ND2 ASN A 492     157.672 102.534  60.143  1.00136.70           N  
ANISOU 3540  ND2 ASN A 492    26231  11262  14446  -5095   2440  -2377       N  
ATOM   3541  N   ASP A 493     160.118 100.241  64.223  1.00141.76           N  
ANISOU 3541  N   ASP A 493    25010  13637  15216  -6283   1492  -2972       N  
ATOM   3542  CA  ASP A 493     161.085  99.990  65.285  1.00137.82           C  
ANISOU 3542  CA  ASP A 493    24118  13568  14678  -6752   1274  -3186       C  
ATOM   3543  C   ASP A 493     161.682  98.599  65.103  1.00142.18           C  
ANISOU 3543  C   ASP A 493    23790  14759  15475  -6715   1039  -3056       C  
ATOM   3544  O   ASP A 493     160.949  97.602  65.128  1.00128.97           O  
ANISOU 3544  O   ASP A 493    21775  13316  13914  -6174    901  -2848       O  
ATOM   3545  CB  ASP A 493     160.423 100.116  66.660  1.00130.48           C  
ANISOU 3545  CB  ASP A 493    23367  12659  13548  -6537   1141  -3295       C  
ATOM   3546  CG  ASP A 493     161.432 100.193  67.798  1.00136.20           C  
ANISOU 3546  CG  ASP A 493    23871  13720  14159  -7088    954  -3568       C  
ATOM   3547  OD1 ASP A 493     162.574  99.715  67.636  1.00136.52           O  
ANISOU 3547  OD1 ASP A 493    23373  14175  14322  -7505    838  -3623       O  
ATOM   3548  OD2 ASP A 493     161.074 100.733  68.867  1.00133.25           O  
ANISOU 3548  OD2 ASP A 493    23835  13230  13564  -7067    921  -3719       O  
ATOM   3549  N   PRO A 494     163.000  98.486  64.915  1.00155.06           N  
ANISOU 3549  N   PRO A 494    25041  16693  17180  -7275    993  -3176       N  
ATOM   3550  CA  PRO A 494     163.602  97.151  64.767  1.00155.44           C  
ANISOU 3550  CA  PRO A 494    24259  17360  17440  -7203    766  -3057       C  
ATOM   3551  C   PRO A 494     163.589  96.330  66.046  1.00147.67           C  
ANISOU 3551  C   PRO A 494    22843  16855  16409  -7044    451  -3095       C  
ATOM   3552  O   PRO A 494     163.780  95.110  65.976  1.00135.77           O  
ANISOU 3552  O   PRO A 494    20718  15806  15063  -6806    258  -2945       O  
ATOM   3553  CB  PRO A 494     165.036  97.459  64.316  1.00159.61           C  
ANISOU 3553  CB  PRO A 494    24566  18072  18007  -7885    826  -3220       C  
ATOM   3554  CG  PRO A 494     165.302  98.834  64.831  1.00163.73           C  
ANISOU 3554  CG  PRO A 494    25621  18283  18306  -8261    976  -3426       C  
ATOM   3555  CD  PRO A 494     163.991  99.564  64.755  1.00162.01           C  
ANISOU 3555  CD  PRO A 494    26169  17423  17964  -7886   1162  -3362       C  
ATOM   3556  N   GLU A 495     163.374  96.955  67.207  1.00151.43           N  
ANISOU 3556  N   GLU A 495    23649  17229  16658  -7160    399  -3288       N  
ATOM   3557  CA  GLU A 495     163.319  96.199  68.455  1.00147.22           C  
ANISOU 3557  CA  GLU A 495    22746  17137  16054  -6992    106  -3318       C  
ATOM   3558  C   GLU A 495     162.055  95.354  68.548  1.00139.98           C  
ANISOU 3558  C   GLU A 495    21758  16225  15203  -6279     39  -3059       C  
ATOM   3559  O   GLU A 495     162.054  94.316  69.219  1.00136.02           O  
ANISOU 3559  O   GLU A 495    20788  16164  14729  -6056   -206  -2983       O  
ATOM   3560  CB  GLU A 495     163.401  97.149  69.650  1.00142.63           C  
ANISOU 3560  CB  GLU A 495    22579  16421  15191  -7312     83  -3603       C  
ATOM   3561  CG  GLU A 495     164.740  97.845  69.812  1.00137.61           C  
ANISOU 3561  CG  GLU A 495    21914  15908  14464  -8078     87  -3897       C  
ATOM   3562  CD  GLU A 495     164.743  98.827  70.967  1.00149.50           C  
ANISOU 3562  CD  GLU A 495    23811  17275  15718  -8241     93  -4095       C  
ATOM   3563  OE1 GLU A 495     163.668  99.383  71.278  1.00150.49           O  
ANISOU 3563  OE1 GLU A 495    24533  16946  15699  -7959    207  -4097       O  
ATOM   3564  OE2 GLU A 495     165.818  99.038  71.567  1.00155.60           O  
ANISOU 3564  OE2 GLU A 495    24285  18405  16429  -8627    -15  -4247       O  
ATOM   3565  N   LYS A 496     160.979  95.778  67.890  1.00135.04           N  
ANISOU 3565  N   LYS A 496    21593  15130  14587  -5919    254  -2923       N  
ATOM   3566  CA  LYS A 496     159.705  95.076  67.928  1.00118.01           C  
ANISOU 3566  CA  LYS A 496    19396  12970  12474  -5268    218  -2692       C  
ATOM   3567  C   LYS A 496     159.567  94.034  66.825  1.00107.45           C  
ANISOU 3567  C   LYS A 496    17637  11796  11395  -4966    208  -2426       C  
ATOM   3568  O   LYS A 496     158.495  93.437  66.686  1.00 94.43           O  
ANISOU 3568  O   LYS A 496    15948  10137   9796  -4450    199  -2227       O  
ATOM   3569  CB  LYS A 496     158.552  96.077  67.832  1.00107.85           C  
ANISOU 3569  CB  LYS A 496    18810  11134  11033  -4990    446  -2692       C  
ATOM   3570  CG  LYS A 496     158.651  97.236  68.805  1.00121.42           C  
ANISOU 3570  CG  LYS A 496    21058  12598  12480  -5284    500  -2964       C  
ATOM   3571  CD  LYS A 496     158.618  96.757  70.244  1.00130.43           C  
ANISOU 3571  CD  LYS A 496    21963  14106  13490  -5244    258  -3055       C  
ATOM   3572  CE  LYS A 496     158.597  97.934  71.203  1.00138.56           C  
ANISOU 3572  CE  LYS A 496    23570  14849  14227  -5493    323  -3327       C  
ATOM   3573  NZ  LYS A 496     157.453  98.842  70.919  1.00142.30           N  
ANISOU 3573  NZ  LYS A 496    24732  14766  14569  -5138    575  -3296       N  
ATOM   3574  N   MET A 497     160.614  93.807  66.039  1.00116.60           N  
ANISOU 3574  N   MET A 497    18482  13113  12707  -5283    215  -2426       N  
ATOM   3575  CA  MET A 497     160.557  92.844  64.951  1.00116.14           C  
ANISOU 3575  CA  MET A 497    18045  13197  12885  -5019    213  -2189       C  
ATOM   3576  C   MET A 497     161.027  91.474  65.424  1.00119.60           C  
ANISOU 3576  C   MET A 497    17817  14200  13425  -4916    -63  -2109       C  
ATOM   3577  O   MET A 497     161.794  91.353  66.384  1.00118.72           O  
ANISOU 3577  O   MET A 497    17470  14415  13223  -5183   -244  -2263       O  
ATOM   3578  CB  MET A 497     161.407  93.313  63.767  1.00113.72           C  
ANISOU 3578  CB  MET A 497    17772  12754  12684  -5379    392  -2217       C  
ATOM   3579  CG  MET A 497     160.920  94.606  63.131  1.00110.21           C  
ANISOU 3579  CG  MET A 497    18025  11709  12141  -5437    688  -2257       C  
ATOM   3580  SD  MET A 497     161.977  95.170  61.785  1.00100.55           S  
ANISOU 3580  SD  MET A 497    16863  10325  11016  -5913    914  -2292       S  
ATOM   3581  CE  MET A 497     161.890  93.764  60.681  1.00104.58           C  
ANISOU 3581  CE  MET A 497    16795  11139  11801  -5515    843  -2006       C  
ATOM   3582  N   TRP A 498     160.552  90.437  64.729  1.00126.86           N  
ANISOU 3582  N   TRP A 498    18455  15228  14518  -4516    -95  -1868       N  
ATOM   3583  CA  TRP A 498     160.859  89.045  65.061  1.00122.38           C  
ANISOU 3583  CA  TRP A 498    17316  15136  14048  -4335   -336  -1752       C  
ATOM   3584  C   TRP A 498     160.464  88.724  66.502  1.00117.40           C  
ANISOU 3584  C   TRP A 498    16653  14699  13257  -4197   -527  -1794       C  
ATOM   3585  O   TRP A 498     161.269  88.248  67.305  1.00110.04           O  
ANISOU 3585  O   TRP A 498    15381  14157  12273  -4352   -736  -1876       O  
ATOM   3586  CB  TRP A 498     162.334  88.729  64.801  1.00119.57           C  
ANISOU 3586  CB  TRP A 498    16514  15139  13778  -4700   -426  -1835       C  
ATOM   3587  CG  TRP A 498     162.689  88.826  63.354  1.00117.02           C  
ANISOU 3587  CG  TRP A 498    16161  14679  13623  -4782   -246  -1758       C  
ATOM   3588  CD1 TRP A 498     163.268  89.886  62.720  1.00115.78           C  
ANISOU 3588  CD1 TRP A 498    16249  14289  13451  -5194    -44  -1891       C  
ATOM   3589  CD2 TRP A 498     162.467  87.829  62.350  1.00114.06           C  
ANISOU 3589  CD2 TRP A 498    15522  14375  13440  -4451   -238  -1531       C  
ATOM   3590  NE1 TRP A 498     163.428  89.608  61.384  1.00119.67           N  
ANISOU 3590  NE1 TRP A 498    16635  14718  14115  -5127     89  -1753       N  
ATOM   3591  CE2 TRP A 498     162.942  88.352  61.131  1.00111.62           C  
ANISOU 3591  CE2 TRP A 498    15301  13884  13225  -4668    -32  -1536       C  
ATOM   3592  CE3 TRP A 498     161.915  86.545  62.363  1.00106.12           C  
ANISOU 3592  CE3 TRP A 498    14239  13557  12525  -4008   -378  -1327       C  
ATOM   3593  CZ2 TRP A 498     162.887  87.633  59.941  1.00105.02           C  
ANISOU 3593  CZ2 TRP A 498    14270  13064  12568  -4439     29  -1350       C  
ATOM   3594  CZ3 TRP A 498     161.858  85.835  61.179  1.00102.57           C  
ANISOU 3594  CZ3 TRP A 498    13609  13108  12254  -3797   -318  -1150       C  
ATOM   3595  CH2 TRP A 498     162.341  86.381  59.985  1.00106.23           C  
ANISOU 3595  CH2 TRP A 498    14152  13403  12806  -4003   -121  -1164       C  
ATOM   3596  N   LYS A 499     159.203  88.998  66.824  1.00114.41           N  
ANISOU 3596  N   LYS A 499    16629  14059  12782  -3886   -450  -1738       N  
ATOM   3597  CA  LYS A 499     158.665  88.657  68.129  1.00105.99           C  
ANISOU 3597  CA  LYS A 499    15557  13156  11559  -3705   -602  -1751       C  
ATOM   3598  C   LYS A 499     158.560  87.144  68.286  1.00110.84           C  
ANISOU 3598  C   LYS A 499    15708  14135  12273  -3407   -791  -1553       C  
ATOM   3599  O   LYS A 499     158.564  86.386  67.312  1.00107.64           O  
ANISOU 3599  O   LYS A 499    15066  13776  12056  -3246   -772  -1381       O  
ATOM   3600  CB  LYS A 499     157.282  89.279  68.325  1.00 95.48           C  
ANISOU 3600  CB  LYS A 499    14695  11479  10105  -3407   -450  -1724       C  
ATOM   3601  CG  LYS A 499     157.213  90.774  68.108  1.00 92.36           C  
ANISOU 3601  CG  LYS A 499    14850  10649   9593  -3616   -237  -1895       C  
ATOM   3602  CD  LYS A 499     155.779  91.262  68.246  1.00 94.00           C  
ANISOU 3602  CD  LYS A 499    15482  10556   9676  -3222    -93  -1842       C  
ATOM   3603  CE  LYS A 499     155.697  92.774  68.150  1.00106.13           C  
ANISOU 3603  CE  LYS A 499    17634  11633  11056  -3395    118  -2019       C  
ATOM   3604  NZ  LYS A 499     156.509  93.426  69.213  1.00115.01           N  
ANISOU 3604  NZ  LYS A 499    18900  12795  12003  -3824     41  -2279       N  
ATOM   3605  N   GLU A 500     158.458  86.709  69.536  1.00113.00           N  
ANISOU 3605  N   GLU A 500    15885  14650  12399  -3333   -968  -1579       N  
ATOM   3606  CA  GLU A 500     158.198  85.307  69.816  1.00 98.90           C  
ANISOU 3606  CA  GLU A 500    13759  13156  10665  -3024  -1129  -1383       C  
ATOM   3607  C   GLU A 500     156.755  84.965  69.462  1.00 81.77           C  
ANISOU 3607  C   GLU A 500    11748  10790   8533  -2622  -1009  -1193       C  
ATOM   3608  O   GLU A 500     155.849  85.794  69.579  1.00 78.12           O  
ANISOU 3608  O   GLU A 500    11660  10054   7969  -2531   -860  -1240       O  
ATOM   3609  CB  GLU A 500     158.478  85.000  71.289  1.00102.65           C  
ANISOU 3609  CB  GLU A 500    14132  13930  10940  -3061  -1341  -1465       C  
ATOM   3610  CG  GLU A 500     158.369  83.531  71.665  1.00 99.04           C  
ANISOU 3610  CG  GLU A 500    13345  13779  10506  -2773  -1518  -1268       C  
ATOM   3611  CD  GLU A 500     158.827  83.260  73.084  1.00 94.24           C  
ANISOU 3611  CD  GLU A 500    12633  13489   9686  -2829  -1739  -1356       C  
ATOM   3612  OE1 GLU A 500     158.734  82.095  73.526  1.00 81.71           O  
ANISOU 3612  OE1 GLU A 500    10834  12137   8076  -2590  -1884  -1198       O  
ATOM   3613  OE2 GLU A 500     159.282  84.210  73.756  1.00 89.32           O  
ANISOU 3613  OE2 GLU A 500    12161  12873   8904  -3116  -1764  -1584       O  
ATOM   3614  N   ARG A 501     156.549  83.735  69.004  1.00 85.31           N  
ANISOU 3614  N   ARG A 501    11908  11388   9119  -2380  -1072   -984       N  
ATOM   3615  CA  ARG A 501     155.202  83.279  68.698  1.00 87.99           C  
ANISOU 3615  CA  ARG A 501    12339  11606   9488  -2027   -977   -808       C  
ATOM   3616  C   ARG A 501     154.395  83.137  69.987  1.00 84.78           C  
ANISOU 3616  C   ARG A 501    12047  11289   8878  -1875  -1034   -807       C  
ATOM   3617  O   ARG A 501     154.926  82.684  71.005  1.00 74.10           O  
ANISOU 3617  O   ARG A 501    10550  10190   7416  -1945  -1210   -841       O  
ATOM   3618  CB  ARG A 501     155.246  81.945  67.954  1.00 82.91           C  
ANISOU 3618  CB  ARG A 501    11373  11106   9024  -1848  -1038   -600       C  
ATOM   3619  CG  ARG A 501     153.957  81.142  67.988  1.00 81.30           C  
ANISOU 3619  CG  ARG A 501    11178  10901   8812  -1523  -1007   -418       C  
ATOM   3620  CD  ARG A 501     154.138  79.788  67.323  1.00 85.61           C  
ANISOU 3620  CD  ARG A 501    11429  11581   9516  -1392  -1081   -232       C  
ATOM   3621  NE  ARG A 501     152.916  78.990  67.362  1.00 99.22           N  
ANISOU 3621  NE  ARG A 501    13165  13312  11223  -1134  -1047    -68       N  
ATOM   3622  CZ  ARG A 501     152.771  77.817  66.754  1.00107.19           C  
ANISOU 3622  CZ  ARG A 501    13994  14382  12351   -999  -1078    101       C  
ATOM   3623  NH1 ARG A 501     153.774  77.301  66.056  1.00114.73           N  
ANISOU 3623  NH1 ARG A 501    14747  15395  13451  -1056  -1144    134       N  
ATOM   3624  NH2 ARG A 501     151.623  77.159  66.843  1.00114.61           N  
ANISOU 3624  NH2 ARG A 501    14961  15333  13255   -814  -1035    229       N  
ATOM   3625  N   PRO A 502     153.123  83.534  69.981  1.00 93.98           N  
ANISOU 3625  N   PRO A 502    13405  13701   8602    168   -835  -1251       N  
ATOM   3626  CA  PRO A 502     152.302  83.381  71.188  1.00 99.92           C  
ANISOU 3626  CA  PRO A 502    14227  14562   9175    220   -720  -1396       C  
ATOM   3627  C   PRO A 502     152.179  81.919  71.589  1.00103.90           C  
ANISOU 3627  C   PRO A 502    14547  15321   9611    287   -670  -1193       C  
ATOM   3628  O   PRO A 502     152.116  81.024  70.743  1.00 97.00           O  
ANISOU 3628  O   PRO A 502    13488  14452   8916    426   -655   -995       O  
ATOM   3629  CB  PRO A 502     150.948  83.969  70.775  1.00 90.11           C  
ANISOU 3629  CB  PRO A 502    13086  13056   8094    462   -579  -1631       C  
ATOM   3630  CG  PRO A 502     151.260  84.880  69.634  1.00 88.66           C  
ANISOU 3630  CG  PRO A 502    13048  12562   8079    473   -687  -1646       C  
ATOM   3631  CD  PRO A 502     152.403  84.237  68.907  1.00 81.98           C  
ANISOU 3631  CD  PRO A 502    12024  11830   7294    332   -790  -1353       C  
ATOM   3632  N   ALA A 503     152.149  81.684  72.897  1.00115.98           N  
ANISOU 3632  N   ALA A 503    16178  17038  10852    172   -648  -1244       N  
ATOM   3633  CA  ALA A 503     152.056  80.340  73.452  1.00108.26           C  
ANISOU 3633  CA  ALA A 503    15150  16263   9722    192   -614  -1054       C  
ATOM   3634  C   ALA A 503     150.599  80.055  73.796  1.00 94.17           C  
ANISOU 3634  C   ALA A 503    13416  14453   7912    278   -324  -1220       C  
ATOM   3635  O   ALA A 503     150.052  80.633  74.741  1.00 96.09           O  
ANISOU 3635  O   ALA A 503    13823  14721   7965    181   -198  -1474       O  
ATOM   3636  CB  ALA A 503     152.950  80.192  74.681  1.00113.24           C  
ANISOU 3636  CB  ALA A 503    15915  17110  10003     -6   -789  -1001       C  
ATOM   3637  N   ASN A 504     149.971  79.178  73.020  1.00102.91           N  
ANISOU 3637  N   ASN A 504    14363  15527   9210    440   -204  -1108       N  
ATOM   3638  CA  ASN A 504     148.642  78.705  73.364  1.00 96.21           C  
ANISOU 3638  CA  ASN A 504    13514  14719   8322    473     89  -1270       C  
ATOM   3639  C   ASN A 504     148.722  77.769  74.565  1.00107.47           C  
ANISOU 3639  C   ASN A 504    15133  16333   9368    276    153  -1160       C  
ATOM   3640  O   ASN A 504     149.791  77.270  74.931  1.00 93.47           O  
ANISOU 3640  O   ASN A 504    13460  14640   7412    198    -74   -903       O  
ATOM   3641  CB  ASN A 504     147.996  77.994  72.173  1.00 94.66           C  
ANISOU 3641  CB  ASN A 504    13096  14447   8426    671    187  -1184       C  
ATOM   3642  CG  ASN A 504     147.668  78.944  71.034  1.00101.80           C  
ANISOU 3642  CG  ASN A 504    13879  15137   9666    880    139  -1337       C  
ATOM   3643  OD1 ASN A 504     148.550  79.352  70.276  1.00 87.12           O  
ANISOU 3643  OD1 ASN A 504    12011  13156   7936    910    -69  -1191       O  
ATOM   3644  ND2 ASN A 504     146.392  79.296  70.904  1.00100.53           N  
ANISOU 3644  ND2 ASN A 504    13635  14929   9631   1022    325  -1652       N  
ATOM   3645  N   ASP A 505     147.571  77.533  75.184  1.00139.97           N  
ANISOU 3645  N   ASP A 505    19312  20521  13350    191    460  -1380       N  
ATOM   3646  CA  ASP A 505     147.517  76.730  76.398  1.00157.12           C  
ANISOU 3646  CA  ASP A 505    21762  22838  15098    -54    566  -1312       C  
ATOM   3647  C   ASP A 505     147.490  75.232  76.121  1.00145.32           C  
ANISOU 3647  C   ASP A 505    20311  21355  13548    -60    599  -1008       C  
ATOM   3648  O   ASP A 505     147.305  74.450  77.059  1.00150.11           O  
ANISOU 3648  O   ASP A 505    21218  22038  13780   -277    716   -943       O  
ATOM   3649  CB  ASP A 505     146.301  77.133  77.237  1.00170.22           C  
ANISOU 3649  CB  ASP A 505    23493  24588  16596   -209    927  -1720       C  
ATOM   3650  CG  ASP A 505     146.682  77.558  78.642  1.00174.72           C  
ANISOU 3650  CG  ASP A 505    24393  25255  16737   -462    904  -1811       C  
ATOM   3651  OD1 ASP A 505     147.332  76.759  79.347  1.00176.47           O  
ANISOU 3651  OD1 ASP A 505    24906  25537  16607   -629    779  -1541       O  
ATOM   3652  OD2 ASP A 505     146.344  78.694  79.035  1.00176.28           O  
ANISOU 3652  OD2 ASP A 505    24585  25454  16941   -478    988  -2158       O  
ATOM   3653  N   SER A 506     147.676  74.813  74.870  1.00131.61           N  
ANISOU 3653  N   SER A 506    18334  19523  12148    155    502   -821       N  
ATOM   3654  CA  SER A 506     147.708  73.400  74.516  1.00128.36           C  
ANISOU 3654  CA  SER A 506    17974  19089  11706    173    513   -530       C  
ATOM   3655  C   SER A 506     149.097  72.932  74.103  1.00121.76           C  
ANISOU 3655  C   SER A 506    17135  18215  10912    315    133   -173       C  
ATOM   3656  O   SER A 506     149.242  71.809  73.606  1.00127.62           O  
ANISOU 3656  O   SER A 506    17891  18904  11693    399     93     75       O  
ATOM   3657  CB  SER A 506     146.703  73.108  73.399  1.00130.16           C  
ANISOU 3657  CB  SER A 506    17921  19258  12277    303    736   -627       C  
ATOM   3658  OG  SER A 506     147.022  73.828  72.221  1.00122.39           O  
ANISOU 3658  OG  SER A 506    16649  18169  11685    547    570   -633       O  
ATOM   3659  N   GLY A 507     150.120  73.754  74.300  1.00110.98           N  
ANISOU 3659  N   GLY A 507    15742  16889   9537    336   -142   -170       N  
ATOM   3660  CA  GLY A 507     151.475  73.416  73.910  1.00100.88           C  
ANISOU 3660  CA  GLY A 507    14379  15631   8320    466   -501     88       C  
ATOM   3661  C   GLY A 507     152.370  73.239  75.120  1.00111.59           C  
ANISOU 3661  C   GLY A 507    16007  17107   9286    366   -765    183       C  
ATOM   3662  O   GLY A 507     152.174  73.879  76.156  1.00108.45           O  
ANISOU 3662  O   GLY A 507    15814  16772   8621    179   -713     10       O  
ATOM   3663  N   SER A 508     153.362  72.370  74.979  1.00118.12           N  
ANISOU 3663  N   SER A 508    16837  17966  10079    512  -1070    442       N  
ATOM   3664  CA  SER A 508     154.313  72.101  76.053  1.00125.24           C  
ANISOU 3664  CA  SER A 508    17985  18983  10617    487  -1408    543       C  
ATOM   3665  C   SER A 508     155.419  73.137  75.953  1.00123.38           C  
ANISOU 3665  C   SER A 508    17476  18896  10506    488  -1675    422       C  
ATOM   3666  O   SER A 508     156.299  73.033  75.097  1.00124.90           O  
ANISOU 3666  O   SER A 508    17346  19146  10965    651  -1877    491       O  
ATOM   3667  CB  SER A 508     154.873  70.688  75.943  1.00126.21           C  
ANISOU 3667  CB  SER A 508    18238  19064  10653    695  -1654    840       C  
ATOM   3668  OG  SER A 508     155.606  70.512  74.739  1.00104.37           O  
ANISOU 3668  OG  SER A 508    15063  16318   8276    933  -1811    917       O  
ATOM   3669  N   LYS A 509     155.392  74.128  76.846  1.00123.16           N  
ANISOU 3669  N   LYS A 509    17584  18943  10270    278  -1663    219       N  
ATOM   3670  CA  LYS A 509     156.351  75.232  76.817  1.00139.57           C  
ANISOU 3670  CA  LYS A 509    19442  21154  12436    203  -1870     60       C  
ATOM   3671  C   LYS A 509     157.732  74.703  77.190  1.00131.90           C  
ANISOU 3671  C   LYS A 509    18413  20381  11324    312  -2333    185       C  
ATOM   3672  O   LYS A 509     158.233  74.892  78.302  1.00134.51           O  
ANISOU 3672  O   LYS A 509    18950  20845  11314    210  -2565    135       O  
ATOM   3673  CB  LYS A 509     155.920  76.356  77.755  1.00156.24           C  
ANISOU 3673  CB  LYS A 509    21764  23276  14324    -50  -1736   -195       C  
ATOM   3674  CG  LYS A 509     154.644  77.075  77.345  1.00157.56           C  
ANISOU 3674  CG  LYS A 509    21921  23270  14676   -110  -1327   -399       C  
ATOM   3675  CD  LYS A 509     153.411  76.398  77.915  1.00152.94           C  
ANISOU 3675  CD  LYS A 509    21607  22621  13883   -156  -1027   -401       C  
ATOM   3676  CE  LYS A 509     152.156  77.185  77.593  1.00145.88           C  
ANISOU 3676  CE  LYS A 509    20646  21606  13174   -188   -651   -683       C  
ATOM   3677  NZ  LYS A 509     150.950  76.562  78.199  1.00143.52           N  
ANISOU 3677  NZ  LYS A 509    20562  21304  12665   -288   -320   -756       N  
ATOM   3678  N   ASP A 510     158.358  74.018  76.235  1.00118.66           N  
ANISOU 3678  N   ASP A 510    16440  18732   9914    541  -2485    326       N  
ATOM   3679  CA  ASP A 510     159.718  73.534  76.423  1.00117.72           C  
ANISOU 3679  CA  ASP A 510    16161  18831   9737    704  -2944    386       C  
ATOM   3680  C   ASP A 510     160.692  74.668  76.128  1.00116.56           C  
ANISOU 3680  C   ASP A 510    15632  18894   9761    554  -3072    150       C  
ATOM   3681  O   ASP A 510     160.795  75.113  74.977  1.00107.64           O  
ANISOU 3681  O   ASP A 510    14172  17737   8989    522  -2912     78       O  
ATOM   3682  CB  ASP A 510     159.999  72.328  75.521  1.00106.79           C  
ANISOU 3682  CB  ASP A 510    14600  17403   8574   1019  -3043    590       C  
ATOM   3683  CG  ASP A 510     161.320  71.645  75.845  1.00107.10           C  
ANISOU 3683  CG  ASP A 510    14514  17660   8519   1269  -3558    637       C  
ATOM   3684  OD1 ASP A 510     161.973  72.030  76.840  1.00107.61           O  
ANISOU 3684  OD1 ASP A 510    14661  17913   8314   1197  -3857    531       O  
ATOM   3685  OD2 ASP A 510     161.705  70.716  75.103  1.00 96.54           O  
ANISOU 3685  OD2 ASP A 510    12991  16311   7380   1556  -3680    760       O  
ATOM   3686  N   PRO A 511     161.422  75.165  77.132  1.00110.00           N  
ANISOU 3686  N   PRO A 511    14861  18271   8663    427  -3352     15       N  
ATOM   3687  CA  PRO A 511     162.384  76.248  76.876  1.00118.20           C  
ANISOU 3687  CA  PRO A 511    15539  19528   9844    225  -3461   -240       C  
ATOM   3688  C   PRO A 511     163.559  75.824  76.012  1.00125.52           C  
ANISOU 3688  C   PRO A 511    15957  20685  11049    391  -3702   -268       C  
ATOM   3689  O   PRO A 511     164.359  76.684  75.620  1.00122.46           O  
ANISOU 3689  O   PRO A 511    15229  20490  10812    177  -3735   -500       O  
ATOM   3690  CB  PRO A 511     162.840  76.651  78.283  1.00120.41           C  
ANISOU 3690  CB  PRO A 511    16043  19988   9718     78  -3739   -359       C  
ATOM   3691  CG  PRO A 511     162.653  75.421  79.098  1.00124.99           C  
ANISOU 3691  CG  PRO A 511    16981  20527   9981    327  -3960   -126       C  
ATOM   3692  CD  PRO A 511     161.428  74.743  78.543  1.00113.87           C  
ANISOU 3692  CD  PRO A 511    15776  18806   8682    436  -3589     82       C  
ATOM   3693  N   SER A 512     163.689  74.530  75.707  1.00128.20           N  
ANISOU 3693  N   SER A 512    16246  21012  11452    746  -3859    -64       N  
ATOM   3694  CA  SER A 512     164.681  74.081  74.740  1.00125.36           C  
ANISOU 3694  CA  SER A 512    15374  20852  11404    931  -4025   -115       C  
ATOM   3695  C   SER A 512     164.343  74.537  73.329  1.00116.40           C  
ANISOU 3695  C   SER A 512    13993  19581  10652    797  -3631   -153       C  
ATOM   3696  O   SER A 512     165.235  74.591  72.475  1.00107.66           O  
ANISOU 3696  O   SER A 512    12424  18678   9806    792  -3686   -293       O  
ATOM   3697  CB  SER A 512     164.796  72.556  74.773  1.00131.50           C  
ANISOU 3697  CB  SER A 512    16235  21588  12140   1377  -4283    117       C  
ATOM   3698  OG  SER A 512     164.703  72.067  76.099  1.00145.01           O  
ANISOU 3698  OG  SER A 512    18399  23275  13425   1489  -4572    232       O  
ATOM   3699  N   VAL A 513     163.079  74.862  73.069  1.00110.89           N  
ANISOU 3699  N   VAL A 513    13596  18556   9981    686  -3244    -56       N  
ATOM   3700  CA  VAL A 513     162.617  75.293  71.756  1.00101.04           C  
ANISOU 3700  CA  VAL A 513    12209  17125   9058    585  -2894    -72       C  
ATOM   3701  C   VAL A 513     161.956  76.655  71.907  1.00106.47           C  
ANISOU 3701  C   VAL A 513    13120  17643   9692    260  -2637   -221       C  
ATOM   3702  O   VAL A 513     161.003  76.809  72.682  1.00113.24           O  
ANISOU 3702  O   VAL A 513    14344  18338  10346    237  -2521   -185       O  
ATOM   3703  CB  VAL A 513     161.645  74.281  71.129  1.00 97.44           C  
ANISOU 3703  CB  VAL A 513    11887  16409   8726    838  -2698    175       C  
ATOM   3704  CG1 VAL A 513     161.148  74.791  69.783  1.00 86.29           C  
ANISOU 3704  CG1 VAL A 513    10359  14802   7624    736  -2369    146       C  
ATOM   3705  CG2 VAL A 513     162.315  72.925  70.980  1.00 96.98           C  
ANISOU 3705  CG2 VAL A 513    11660  16478   8711   1180  -2967    316       C  
ATOM   3706  N   ARG A 514     162.462  77.640  71.169  1.00106.41           N  
ANISOU 3706  N   ARG A 514    12913  17664   9852      1  -2542   -408       N  
ATOM   3707  CA  ARG A 514     161.899  78.981  71.133  1.00100.15           C  
ANISOU 3707  CA  ARG A 514    12364  16656   9034   -289  -2315   -559       C  
ATOM   3708  C   ARG A 514     161.857  79.441  69.685  1.00 95.91           C  
ANISOU 3708  C   ARG A 514    11718  15943   8780   -400  -2092   -591       C  
ATOM   3709  O   ARG A 514     162.823  79.252  68.943  1.00 96.49           O  
ANISOU 3709  O   ARG A 514    11450  16204   9008   -465  -2153   -641       O  
ATOM   3710  CB  ARG A 514     162.722  79.957  71.983  1.00103.55           C  
ANISOU 3710  CB  ARG A 514    12796  17292   9257   -603  -2478   -800       C  
ATOM   3711  CG  ARG A 514     162.786  79.587  73.452  1.00104.94           C  
ANISOU 3711  CG  ARG A 514    13130  17634   9107   -520  -2721   -781       C  
ATOM   3712  CD  ARG A 514     161.630  80.190  74.231  1.00116.51           C  
ANISOU 3712  CD  ARG A 514    15049  18851  10370   -596  -2531   -807       C  
ATOM   3713  NE  ARG A 514     161.916  81.565  74.630  1.00132.77           N  
ANISOU 3713  NE  ARG A 514    17230  20906  12310   -949  -2509  -1066       N  
ATOM   3714  CZ  ARG A 514     161.111  82.312  75.379  1.00140.13           C  
ANISOU 3714  CZ  ARG A 514    18532  21657  13052  -1061  -2370  -1172       C  
ATOM   3715  NH1 ARG A 514     159.957  81.821  75.812  1.00141.46           N  
ANISOU 3715  NH1 ARG A 514    18950  21667  13131   -867  -2219  -1063       N  
ATOM   3716  NH2 ARG A 514     161.458  83.553  75.692  1.00144.05           N  
ANISOU 3716  NH2 ARG A 514    19151  22139  13445  -1385  -2366  -1414       N  
ATOM   3717  N   VAL A 515     160.738  80.031  69.276  1.00 89.15           N  
ANISOU 3717  N   VAL A 515    11158  14731   7983   -413  -1842   -580       N  
ATOM   3718  CA  VAL A 515     160.537  80.412  67.884  1.00 94.13           C  
ANISOU 3718  CA  VAL A 515    11786  15130   8850   -477  -1649   -578       C  
ATOM   3719  C   VAL A 515     160.209  81.899  67.808  1.00104.93           C  
ANISOU 3719  C   VAL A 515    13487  16227  10154   -749  -1527   -763       C  
ATOM   3720  O   VAL A 515     159.493  82.439  68.660  1.00 75.24           O  
ANISOU 3720  O   VAL A 515    10011  12338   6240   -738  -1501   -841       O  
ATOM   3721  CB  VAL A 515     159.440  79.555  67.210  1.00 99.28           C  
ANISOU 3721  CB  VAL A 515    12483  15568   9670   -152  -1500   -374       C  
ATOM   3722  CG1 VAL A 515     159.642  78.083  67.535  1.00 89.94           C  
ANISOU 3722  CG1 VAL A 515    11088  14602   8483    122  -1631   -189       C  
ATOM   3723  CG2 VAL A 515     158.056  79.989  67.629  1.00 99.86           C  
ANISOU 3723  CG2 VAL A 515    12896  15369   9678    -53  -1355   -405       C  
ATOM   3724  N   ILE A 516     160.769  82.563  66.798  1.00109.73           N  
ANISOU 3724  N   ILE A 516    14088  16743  10862  -1010  -1450   -849       N  
ATOM   3725  CA  ILE A 516     160.497  83.964  66.507  1.00106.05           C  
ANISOU 3725  CA  ILE A 516    14019  15942  10334  -1275  -1340  -1006       C  
ATOM   3726  C   ILE A 516     160.117  84.070  65.038  1.00 96.45           C  
ANISOU 3726  C   ILE A 516    12930  14413   9302  -1250  -1189   -925       C  
ATOM   3727  O   ILE A 516     160.621  83.323  64.193  1.00 99.58           O  
ANISOU 3727  O   ILE A 516    13037  14951   9847  -1230  -1161   -825       O  
ATOM   3728  CB  ILE A 516     161.699  84.881  66.838  1.00106.20           C  
ANISOU 3728  CB  ILE A 516    14022  16135  10196  -1751  -1404  -1233       C  
ATOM   3729  CG1 ILE A 516     162.953  84.429  66.085  1.00107.47           C  
ANISOU 3729  CG1 ILE A 516    13758  16612  10465  -1959  -1418  -1264       C  
ATOM   3730  CG2 ILE A 516     161.954  84.914  68.342  1.00 92.68           C  
ANISOU 3730  CG2 ILE A 516    12261  14685   8267  -1771  -1575  -1330       C  
ATOM   3731  CD1 ILE A 516     164.176  85.279  66.369  1.00109.10           C  
ANISOU 3731  CD1 ILE A 516    13878  17050  10525  -2473  -1461  -1535       C  
ATOM   3732  N   GLN A 517     159.214  85.000  64.734  1.00 95.38           N  
ANISOU 3732  N   GLN A 517    13249  13843   9147  -1229  -1108   -981       N  
ATOM   3733  CA  GLN A 517     158.601  85.061  63.415  1.00 98.41           C  
ANISOU 3733  CA  GLN A 517    13830  13879   9683  -1113  -1008   -888       C  
ATOM   3734  C   GLN A 517     158.418  86.507  62.976  1.00 94.06           C  
ANISOU 3734  C   GLN A 517    13834  12882   9022  -1348   -976  -1033       C  
ATOM   3735  O   GLN A 517     158.310  87.416  63.803  1.00 86.73           O  
ANISOU 3735  O   GLN A 517    13180  11844   7931  -1461  -1019  -1199       O  
ATOM   3736  CB  GLN A 517     157.249  84.333  63.411  1.00 92.34           C  
ANISOU 3736  CB  GLN A 517    13043  12994   9049   -628   -986   -766       C  
ATOM   3737  CG  GLN A 517     156.306  84.793  64.510  1.00 84.68           C  
ANISOU 3737  CG  GLN A 517    12276  11925   7974   -453  -1007   -896       C  
ATOM   3738  CD  GLN A 517     155.076  83.917  64.633  1.00 89.02           C  
ANISOU 3738  CD  GLN A 517    12703  12477   8645    -34   -954   -816       C  
ATOM   3739  OE1 GLN A 517     155.123  82.717  64.358  1.00 88.69           O  
ANISOU 3739  OE1 GLN A 517    12351  12633   8713    108   -931   -637       O  
ATOM   3740  NE2 GLN A 517     153.964  84.514  65.047  1.00 92.44           N  
ANISOU 3740  NE2 GLN A 517    13375  12692   9055    158   -928   -979       N  
ATOM   3741  N   ASN A 518     158.382  86.705  61.658  1.00 95.84           N  
ANISOU 3741  N   ASN A 518    14271  12826   9318  -1421   -907   -968       N  
ATOM   3742  CA  ASN A 518     158.161  88.018  61.068  1.00 94.75           C  
ANISOU 3742  CA  ASN A 518    14763  12182   9054  -1618   -899  -1072       C  
ATOM   3743  C   ASN A 518     157.768  87.834  59.609  1.00 98.32           C  
ANISOU 3743  C   ASN A 518    15410  12332   9614  -1514   -854   -933       C  
ATOM   3744  O   ASN A 518     158.313  86.968  58.920  1.00 93.43           O  
ANISOU 3744  O   ASN A 518    14445  11951   9104  -1583   -773   -810       O  
ATOM   3745  CB  ASN A 518     159.409  88.904  61.180  1.00 91.79           C  
ANISOU 3745  CB  ASN A 518    14543  11861   8471  -2233   -851  -1233       C  
ATOM   3746  CG  ASN A 518     159.078  90.387  61.198  1.00 84.40           C  
ANISOU 3746  CG  ASN A 518    14334  10400   7333  -2412   -884  -1386       C  
ATOM   3747  OD1 ASN A 518     159.295  91.071  62.199  1.00 85.43           O  
ANISOU 3747  OD1 ASN A 518    14588  10563   7308  -2583   -926  -1556       O  
ATOM   3748  ND2 ASN A 518     158.553  90.891  60.087  1.00 98.35           N  
ANISOU 3748  ND2 ASN A 518    16626  11659   9086  -2365   -883  -1330       N  
ATOM   3749  N   GLY A 519     156.822  88.654  59.146  1.00107.55           N  
ANISOU 3749  N   GLY A 519    17147  12971  10745  -1328   -928   -969       N  
ATOM   3750  CA  GLY A 519     156.332  88.567  57.788  1.00101.14           C  
ANISOU 3750  CA  GLY A 519    16604  11820  10003  -1189   -936   -846       C  
ATOM   3751  C   GLY A 519     157.180  89.352  56.801  1.00100.21           C  
ANISOU 3751  C   GLY A 519    16962  11423   9692  -1718   -859   -857       C  
ATOM   3752  O   GLY A 519     158.125  90.053  57.157  1.00 85.59           O  
ANISOU 3752  O   GLY A 519    15250   9620   7650  -2219   -789   -985       O  
ATOM   3753  N   LEU A 520     156.812  89.228  55.530  1.00110.92           N  
ANISOU 3753  N   LEU A 520    18589  12478  11078  -1629   -865   -732       N  
ATOM   3754  CA  LEU A 520     157.538  89.844  54.429  1.00108.45           C  
ANISOU 3754  CA  LEU A 520    18772  11876  10559  -2141   -765   -718       C  
ATOM   3755  C   LEU A 520     156.799  91.071  53.912  1.00104.65           C  
ANISOU 3755  C   LEU A 520    19214  10667   9882  -2063   -937   -757       C  
ATOM   3756  O   LEU A 520     155.571  91.163  53.998  1.00 93.76           O  
ANISOU 3756  O   LEU A 520    18001   9017   8606  -1487  -1149   -759       O  
ATOM   3757  CB  LEU A 520     157.733  88.850  53.281  1.00103.69           C  
ANISOU 3757  CB  LEU A 520    17902  11419  10077  -2145   -650   -550       C  
ATOM   3758  CG  LEU A 520     158.664  87.663  53.521  1.00100.75           C  
ANISOU 3758  CG  LEU A 520    16699  11713   9868  -2283   -476   -523       C  
ATOM   3759  CD1 LEU A 520     158.464  86.612  52.442  1.00 84.78           C  
ANISOU 3759  CD1 LEU A 520    14442   9761   8008  -2094   -411   -352       C  
ATOM   3760  CD2 LEU A 520     160.111  88.125  53.559  1.00101.10           C  
ANISOU 3760  CD2 LEU A 520    16700  11982   9731  -2989   -287   -679       C  
ATOM   3761  N   GLU A 521     157.566  92.017  53.361  1.00120.52           N  
ANISOU 3761  N   GLU A 521    21838  12359  11595  -2656   -848   -811       N  
ATOM   3762  CA  GLU A 521     156.957  93.173  52.712  1.00119.83           C  
ANISOU 3762  CA  GLU A 521    22752  11508  11271  -2618  -1028   -824       C  
ATOM   3763  C   GLU A 521     156.388  92.809  51.347  1.00119.35           C  
ANISOU 3763  C   GLU A 521    22981  11137  11229  -2389  -1109   -646       C  
ATOM   3764  O   GLU A 521     155.409  93.419  50.901  1.00108.17           O  
ANISOU 3764  O   GLU A 521    22222   9139   9740  -2001  -1381   -635       O  
ATOM   3765  CB  GLU A 521     157.977  94.304  52.576  1.00116.68           C  
ANISOU 3765  CB  GLU A 521    22996  10837  10500  -3392   -888   -938       C  
ATOM   3766  CG  GLU A 521     158.688  94.664  53.871  1.00113.68           C  
ANISOU 3766  CG  GLU A 521    22315  10802  10075  -3711   -793  -1132       C  
ATOM   3767  CD  GLU A 521     159.502  95.939  53.755  1.00129.41           C  
ANISOU 3767  CD  GLU A 521    25071  12423  11674  -4451   -686  -1276       C  
ATOM   3768  OE1 GLU A 521     159.101  96.834  52.981  1.00136.83           O  
ANISOU 3768  OE1 GLU A 521    26984  12646  12360  -4508   -802  -1240       O  
ATOM   3769  OE2 GLU A 521     160.544  96.047  54.437  1.00130.84           O  
ANISOU 3769  OE2 GLU A 521    24907  13022  11786  -4983   -497  -1434       O  
ATOM   3770  N   ASN A 522     156.984  91.826  50.674  1.00129.30           N  
ANISOU 3770  N   ASN A 522    23767  12777  12585  -2603   -897   -525       N  
ATOM   3771  CA  ASN A 522     156.493  91.330  49.395  1.00123.08           C  
ANISOU 3771  CA  ASN A 522    23165  11771  11827  -2400   -950   -355       C  
ATOM   3772  C   ASN A 522     156.580  89.812  49.392  1.00112.61           C  
ANISOU 3772  C   ASN A 522    20888  11072  10828  -2181   -813   -255       C  
ATOM   3773  O   ASN A 522     157.631  89.249  49.714  1.00110.82           O  
ANISOU 3773  O   ASN A 522    20073  11373  10660  -2554   -564   -292       O  
ATOM   3774  CB  ASN A 522     157.296  91.909  48.223  1.00134.38           C  
ANISOU 3774  CB  ASN A 522    25292  12859  12907  -3078   -786   -317       C  
ATOM   3775  CG  ASN A 522     156.950  93.358  47.938  1.00153.36           C  
ANISOU 3775  CG  ASN A 522    28845  14473  14953  -3192   -990   -362       C  
ATOM   3776  OD1 ASN A 522     155.790  93.760  48.028  1.00157.77           O  
ANISOU 3776  OD1 ASN A 522    29787  14605  15552  -2578  -1339   -360       O  
ATOM   3777  ND2 ASN A 522     157.958  94.150  47.590  1.00159.68           N  
ANISOU 3777  ND2 ASN A 522    30211  15070  15390  -3984   -776   -428       N  
ATOM   3778  N   ARG A 523     155.473  89.154  49.032  1.00112.78           N  
ANISOU 3778  N   ARG A 523    20765  11029  11058  -1567   -992   -149       N  
ATOM   3779  CA  ARG A 523     155.470  87.696  48.956  1.00105.53           C  
ANISOU 3779  CA  ARG A 523    19031  10634  10431  -1347   -872    -44       C  
ATOM   3780  C   ARG A 523     156.438  87.184  47.899  1.00100.87           C  
ANISOU 3780  C   ARG A 523    18365  10196   9765  -1823   -616     41       C  
ATOM   3781  O   ARG A 523     156.942  86.060  48.013  1.00 87.49           O  
ANISOU 3781  O   ARG A 523    15945   9028   8271  -1835   -442     77       O  
ATOM   3782  CB  ARG A 523     154.058  87.185  48.665  1.00112.39           C  
ANISOU 3782  CB  ARG A 523    19843  11359  11503   -656  -1106     25       C  
ATOM   3783  CG  ARG A 523     153.317  86.662  49.885  1.00124.85           C  
ANISOU 3783  CG  ARG A 523    20834  13265  13339   -167  -1184    -51       C  
ATOM   3784  CD  ARG A 523     154.104  85.556  50.572  1.00136.63           C  
ANISOU 3784  CD  ARG A 523    21520  15399  14994   -314   -951     -9       C  
ATOM   3785  NE  ARG A 523     154.470  84.482  49.651  1.00147.82           N  
ANISOU 3785  NE  ARG A 523    22624  17029  16511   -391   -804    140       N  
ATOM   3786  CZ  ARG A 523     153.757  83.375  49.468  1.00155.44           C  
ANISOU 3786  CZ  ARG A 523    23184  18173  17702     11   -824    230       C  
ATOM   3787  NH1 ARG A 523     152.632  83.187  50.144  1.00155.57           N  
ANISOU 3787  NH1 ARG A 523    23034  18209  17866    492   -969    174       N  
ATOM   3788  NH2 ARG A 523     154.171  82.453  48.608  1.00154.07           N  
ANISOU 3788  NH2 ARG A 523    22771  18168  17598    -91   -681    353       N  
ATOM   3789  N   ASN A 524     156.713  87.986  46.867  1.00112.72           N  
ANISOU 3789  N   ASN A 524    20635  11231  10962  -2221   -590     60       N  
ATOM   3790  CA  ASN A 524     157.625  87.561  45.812  1.00108.48           C  
ANISOU 3790  CA  ASN A 524    20073  10827  10319  -2727   -312    106       C  
ATOM   3791  C   ASN A 524     159.058  87.418  46.306  1.00115.96           C  
ANISOU 3791  C   ASN A 524    20512  12298  11248  -3319      8    -45       C  
ATOM   3792  O   ASN A 524     159.869  86.771  45.634  1.00116.05           O  
ANISOU 3792  O   ASN A 524    20207  12616  11273  -3662    271    -58       O  
ATOM   3793  CB  ASN A 524     157.570  88.545  44.646  1.00113.35           C  
ANISOU 3793  CB  ASN A 524    21737  10781  10551  -3068   -354    150       C  
ATOM   3794  CG  ASN A 524     156.163  88.743  44.121  1.00116.44           C  
ANISOU 3794  CG  ASN A 524    22659  10638  10946  -2446   -732    269       C  
ATOM   3795  OD1 ASN A 524     155.260  87.961  44.424  1.00100.68           O  
ANISOU 3795  OD1 ASN A 524    20157   8835   9263  -1807   -900    316       O  
ATOM   3796  ND2 ASN A 524     155.968  89.789  43.326  1.00130.83           N  
ANISOU 3796  ND2 ASN A 524    25522  11784  12403  -2638   -878    299       N  
ATOM   3797  N   ASP A 525     159.388  88.002  47.456  1.00116.02           N  
ANISOU 3797  N   ASP A 525    20419  12433  11230  -3437    -16   -187       N  
ATOM   3798  CA  ASP A 525     160.704  87.847  48.059  1.00104.52           C  
ANISOU 3798  CA  ASP A 525    18401  11529   9783  -3935    233   -367       C  
ATOM   3799  C   ASP A 525     160.825  86.580  48.895  1.00 92.19           C  
ANISOU 3799  C   ASP A 525    15838  10614   8577  -3538    225   -360       C  
ATOM   3800  O   ASP A 525     161.852  86.396  49.556  1.00 90.35           O  
ANISOU 3800  O   ASP A 525    15074  10873   8382  -3835    357   -525       O  
ATOM   3801  CB  ASP A 525     161.034  89.066  48.928  1.00106.10           C  
ANISOU 3801  CB  ASP A 525    18975  11570   9768  -4270    196   -535       C  
ATOM   3802  CG  ASP A 525     161.171  90.341  48.120  1.00116.52           C  
ANISOU 3802  CG  ASP A 525    21330  12263  10680  -4802    247   -568       C  
ATOM   3803  OD1 ASP A 525     161.597  90.261  46.948  1.00117.63           O  
ANISOU 3803  OD1 ASP A 525    21740  12294  10661  -5204    445   -538       O  
ATOM   3804  OD2 ASP A 525     160.856  91.423  48.658  1.00115.13           O  
ANISOU 3804  OD2 ASP A 525    21738  11684  10322  -4829     92   -630       O  
ATOM   3805  N   ALA A 526     159.811  85.711  48.880  1.00 93.28           N  
ANISOU 3805  N   ALA A 526    15733  10754   8957  -2888     65   -189       N  
ATOM   3806  CA  ALA A 526     159.824  84.527  49.735  1.00 98.74           C  
ANISOU 3806  CA  ALA A 526    15591  11981   9944  -2498     35   -164       C  
ATOM   3807  C   ALA A 526     161.035  83.649  49.443  1.00102.61           C  
ANISOU 3807  C   ALA A 526    15459  12999  10528  -2790    265   -240       C  
ATOM   3808  O   ALA A 526     161.856  83.388  50.328  1.00 82.60           O  
ANISOU 3808  O   ALA A 526    12392  10931   8060  -2899    295   -377       O  
ATOM   3809  CB  ALA A 526     158.525  83.737  49.561  1.00 92.34           C  
ANISOU 3809  CB  ALA A 526    14699  11044   9340  -1841   -129     20       C  
ATOM   3810  N   ALA A 527     161.170  83.197  48.193  1.00118.59           N  
ANISOU 3810  N   ALA A 527    17547  14961  12552  -2910    415   -178       N  
ATOM   3811  CA  ALA A 527     162.282  82.322  47.836  1.00112.92           C  
ANISOU 3811  CA  ALA A 527    16217  14746  11941  -3147    640   -287       C  
ATOM   3812  C   ALA A 527     163.626  82.978  48.127  1.00112.88           C  
ANISOU 3812  C   ALA A 527    16074  15033  11781  -3797    825   -569       C  
ATOM   3813  O   ALA A 527     164.574  82.307  48.550  1.00108.09           O  
ANISOU 3813  O   ALA A 527    14756  14993  11321  -3860    903   -735       O  
ATOM   3814  CB  ALA A 527     162.184  81.927  46.363  1.00110.33           C  
ANISOU 3814  CB  ALA A 527    16104  14235  11580  -3249    798   -202       C  
ATOM   3815  N   LYS A 528     163.725  84.293  47.917  1.00120.37           N  
ANISOU 3815  N   LYS A 528    17709  15601  12427  -4282    882   -647       N  
ATOM   3816  CA  LYS A 528     164.981  84.991  48.177  1.00127.94           C  
ANISOU 3816  CA  LYS A 528    18577  16824  13209  -4976   1082   -944       C  
ATOM   3817  C   LYS A 528     165.238  85.129  49.673  1.00127.56           C  
ANISOU 3817  C   LYS A 528    18122  17102  13242  -4844    913  -1060       C  
ATOM   3818  O   LYS A 528     166.331  84.813  50.156  1.00122.76           O  
ANISOU 3818  O   LYS A 528    16868  17066  12710  -5080   1003  -1302       O  
ATOM   3819  CB  LYS A 528     164.968  86.366  47.509  1.00125.93           C  
ANISOU 3819  CB  LYS A 528    19280  16003  12566  -5563   1194   -980       C  
ATOM   3820  CG  LYS A 528     166.218  87.194  47.779  1.00131.33           C  
ANISOU 3820  CG  LYS A 528    19952  16923  13026  -6364   1427  -1309       C  
ATOM   3821  CD  LYS A 528     166.063  88.626  47.286  1.00139.05           C  
ANISOU 3821  CD  LYS A 528    22010  17240  13582  -6908   1492  -1314       C  
ATOM   3822  CE  LYS A 528     167.304  89.455  47.598  1.00140.38           C  
ANISOU 3822  CE  LYS A 528    22171  17654  13512  -7764   1748  -1665       C  
ATOM   3823  NZ  LYS A 528     167.132  90.895  47.255  1.00135.90           N  
ANISOU 3823  NZ  LYS A 528    22739  16393  12503  -8297   1789  -1665       N  
ATOM   3824  N   LYS A 529     164.241  85.604  50.426  1.00126.24           N  
ANISOU 3824  N   LYS A 529    18318  16590  13056  -4459    657   -917       N  
ATOM   3825  CA  LYS A 529     164.471  85.895  51.838  1.00120.95           C  
ANISOU 3825  CA  LYS A 529    17385  16172  12401  -4406    511  -1038       C  
ATOM   3826  C   LYS A 529     164.526  84.624  52.676  1.00115.89           C  
ANISOU 3826  C   LYS A 529    15926  16056  12052  -3886    370   -996       C  
ATOM   3827  O   LYS A 529     165.171  84.611  53.731  1.00115.36           O  
ANISOU 3827  O   LYS A 529    15442  16389  12000  -3949    292  -1158       O  
ATOM   3828  CB  LYS A 529     163.392  86.842  52.365  1.00110.11           C  
ANISOU 3828  CB  LYS A 529    16680  14257  10898  -4177    305   -936       C  
ATOM   3829  CG  LYS A 529     163.391  88.199  51.683  1.00121.00           C  
ANISOU 3829  CG  LYS A 529    18959  15069  11947  -4688    393   -992       C  
ATOM   3830  CD  LYS A 529     164.758  88.862  51.764  1.00126.54           C  
ANISOU 3830  CD  LYS A 529    19618  16023  12437  -5496    624  -1282       C  
ATOM   3831  CE  LYS A 529     164.819  90.119  50.912  1.00134.55           C  
ANISOU 3831  CE  LYS A 529    21603  16441  13079  -6085    759  -1325       C  
ATOM   3832  NZ  LYS A 529     166.128  90.815  51.057  1.00140.93           N  
ANISOU 3832  NZ  LYS A 529    22388  17502  13659  -6939   1011  -1641       N  
ATOM   3833  N   ILE A 530     163.856  83.556  52.238  1.00114.47           N  
ANISOU 3833  N   ILE A 530    15550  15864  12080  -3380    320   -784       N  
ATOM   3834  CA  ILE A 530     163.944  82.283  52.951  1.00102.57           C  
ANISOU 3834  CA  ILE A 530    13341  14812  10818  -2912    195   -734       C  
ATOM   3835  C   ILE A 530     165.374  81.761  52.926  1.00 92.44           C  
ANISOU 3835  C   ILE A 530    11403  14114   9607  -3199    308   -975       C  
ATOM   3836  O   ILE A 530     165.894  81.278  53.939  1.00 77.18           O  
ANISOU 3836  O   ILE A 530     8952  12612   7761  -3032    158  -1072       O  
ATOM   3837  CB  ILE A 530     162.952  81.268  52.353  1.00 97.78           C  
ANISOU 3837  CB  ILE A 530    12718  14039  10397  -2383    154   -475       C  
ATOM   3838  CG1 ILE A 530     161.528  81.577  52.818  1.00108.99           C  
ANISOU 3838  CG1 ILE A 530    14556  15051  11806  -1969    -25   -299       C  
ATOM   3839  CG2 ILE A 530     163.342  79.851  52.724  1.00 74.81           C  
ANISOU 3839  CG2 ILE A 530     9110  11600   7714  -2030     94   -450       C  
ATOM   3840  CD1 ILE A 530     160.457  80.971  51.938  1.00103.11           C  
ANISOU 3840  CD1 ILE A 530    13982  14018  11177  -1593    -35    -89       C  
ATOM   3841  N   ASP A 531     166.040  81.867  51.774  1.00106.25           N  
ANISOU 3841  N   ASP A 531    13171  15894  11305  -3640    567  -1103       N  
ATOM   3842  CA  ASP A 531     167.429  81.434  51.682  1.00109.35           C  
ANISOU 3842  CA  ASP A 531    12901  16875  11771  -3945    702  -1407       C  
ATOM   3843  C   ASP A 531     168.347  82.310  52.526  1.00108.47           C  
ANISOU 3843  C   ASP A 531    12657  17046  11511  -4414    694  -1711       C  
ATOM   3844  O   ASP A 531     169.355  81.822  53.050  1.00 96.76           O  
ANISOU 3844  O   ASP A 531    10478  16147  10140  -4437    643  -1965       O  
ATOM   3845  CB  ASP A 531     167.882  81.434  50.221  1.00114.72           C  
ANISOU 3845  CB  ASP A 531    13682  17509  12399  -4377   1030  -1507       C  
ATOM   3846  CG  ASP A 531     167.030  80.529  49.344  1.00108.27           C  
ANISOU 3846  CG  ASP A 531    12973  16442  11724  -3932   1037  -1228       C  
ATOM   3847  OD1 ASP A 531     166.427  79.574  49.878  1.00 95.96           O  
ANISOU 3847  OD1 ASP A 531    11143  14945  10373  -3293    816  -1032       O  
ATOM   3848  OD2 ASP A 531     166.965  80.772  48.120  1.00109.17           O  
ANISOU 3848  OD2 ASP A 531    13472  16288  11719  -4249   1266  -1208       O  
ATOM   3849  N   GLU A 532     168.017  83.597  52.674  1.00120.48           N  
ANISOU 3849  N   GLU A 532    14841  18158  12779  -4773    723  -1708       N  
ATOM   3850  CA  GLU A 532     168.833  84.476  53.507  1.00121.54           C  
ANISOU 3850  CA  GLU A 532    14901  18528  12751  -5244    716  -1998       C  
ATOM   3851  C   GLU A 532     168.683  84.147  54.987  1.00124.07           C  
ANISOU 3851  C   GLU A 532    14874  19101  13166  -4784    388  -1966       C  
ATOM   3852  O   GLU A 532     169.637  84.313  55.756  1.00125.81           O  
ANISOU 3852  O   GLU A 532    14661  19782  13357  -5026    327  -2251       O  
ATOM   3853  CB  GLU A 532     168.470  85.940  53.255  1.00112.06           C  
ANISOU 3853  CB  GLU A 532    14592  16753  11232  -5736    826  -1991       C  
ATOM   3854  CG  GLU A 532     168.638  86.391  51.814  1.00107.44           C  
ANISOU 3854  CG  GLU A 532    14495  15857  10470  -6270   1145  -2021       C  
ATOM   3855  CD  GLU A 532     168.464  87.889  51.649  1.00110.88           C  
ANISOU 3855  CD  GLU A 532    15850  15735  10543  -6823   1235  -2056       C  
ATOM   3856  OE1 GLU A 532     168.968  88.647  52.504  1.00110.21           O  
ANISOU 3856  OE1 GLU A 532    15778  15778  10321  -7169   1208  -2268       O  
ATOM   3857  OE2 GLU A 532     167.819  88.307  50.665  1.00113.58           O  
ANISOU 3857  OE2 GLU A 532    16938  15493  10723  -6904   1315  -1875       O  
ATOM   3858  N   LEU A 533     167.500  83.689  55.405  1.00121.97           N  
ANISOU 3858  N   LEU A 533    14796  18551  12996  -4146    179  -1645       N  
ATOM   3859  CA  LEU A 533     167.302  83.278  56.791  1.00114.80           C  
ANISOU 3859  CA  LEU A 533    13602  17868  12150  -3711   -113  -1597       C  
ATOM   3860  C   LEU A 533     167.980  81.944  57.084  1.00107.22           C  
ANISOU 3860  C   LEU A 533    11860  17471  11407  -3366   -245  -1654       C  
ATOM   3861  O   LEU A 533     168.551  81.762  58.166  1.00 95.35           O  
ANISOU 3861  O   LEU A 533     9972  16359   9899  -3280   -458  -1794       O  
ATOM   3862  CB  LEU A 533     165.809  83.191  57.107  1.00105.11           C  
ANISOU 3862  CB  LEU A 533    12819  16177  10941  -3188   -250  -1275       C  
ATOM   3863  CG  LEU A 533     164.989  84.477  56.993  1.00101.09           C  
ANISOU 3863  CG  LEU A 533    13092  15084  10233  -3371   -206  -1225       C  
ATOM   3864  CD1 LEU A 533     163.528  84.202  57.312  1.00 96.36           C  
ANISOU 3864  CD1 LEU A 533    12771  14136   9707  -2783   -349   -966       C  
ATOM   3865  CD2 LEU A 533     165.551  85.557  57.908  1.00105.31           C  
ANISOU 3865  CD2 LEU A 533    13766  15691  10556  -3785   -248  -1457       C  
ATOM   3866  N   ARG A 534     167.930  81.000  56.140  1.00114.48           N  
ANISOU 3866  N   ARG A 534    12566  18423  12507  -3148   -147  -1555       N  
ATOM   3867  CA  ARG A 534     168.599  79.720  56.340  1.00110.55           C  
ANISOU 3867  CA  ARG A 534    11364  18423  12218  -2793   -284  -1627       C  
ATOM   3868  C   ARG A 534     170.115  79.860  56.326  1.00108.84           C  
ANISOU 3868  C   ARG A 534    10566  18778  12011  -3217   -226  -2059       C  
ATOM   3869  O   ARG A 534     170.811  79.010  56.892  1.00 98.36           O  
ANISOU 3869  O   ARG A 534     8626  17929  10820  -2916   -445  -2199       O  
ATOM   3870  CB  ARG A 534     168.165  78.713  55.270  1.00 99.22           C  
ANISOU 3870  CB  ARG A 534     9878  16854  10966  -2480   -171  -1436       C  
ATOM   3871  CG  ARG A 534     166.664  78.461  55.191  1.00 93.89           C  
ANISOU 3871  CG  ARG A 534     9699  15667  10307  -2056   -220  -1048       C  
ATOM   3872  CD  ARG A 534     166.363  77.192  54.401  1.00108.40           C  
ANISOU 3872  CD  ARG A 534    11344  17495  12349  -1663   -180   -883       C  
ATOM   3873  NE  ARG A 534     165.026  77.190  53.806  1.00127.64           N  
ANISOU 3873  NE  ARG A 534    14294  19418  14786  -1464   -113   -590       N  
ATOM   3874  CZ  ARG A 534     163.937  76.712  54.401  1.00134.45           C  
ANISOU 3874  CZ  ARG A 534    15321  20080  15683  -1005   -269   -345       C  
ATOM   3875  NH1 ARG A 534     164.013  76.198  55.619  1.00138.91           N  
ANISOU 3875  NH1 ARG A 534    15651  20873  16256   -712   -493   -323       N  
ATOM   3876  NH2 ARG A 534     162.767  76.750  53.778  1.00135.21           N  
ANISOU 3876  NH2 ARG A 534    15828  19754  15791   -853   -203   -140       N  
ATOM   3877  N   ALA A 535     170.639  80.902  55.682  1.00119.46           N  
ANISOU 3877  N   ALA A 535    12101  20084  13205  -3911     57  -2293       N  
ATOM   3878  CA  ALA A 535     172.078  81.116  55.621  1.00131.11           C  
ANISOU 3878  CA  ALA A 535    13006  22131  14677  -4406    164  -2764       C  
ATOM   3879  C   ALA A 535     172.640  81.727  56.896  1.00140.26           C  
ANISOU 3879  C   ALA A 535    13989  23591  15714  -4579    -52  -2991       C  
ATOM   3880  O   ALA A 535     173.864  81.747  57.067  1.00145.74           O  
ANISOU 3880  O   ALA A 535    14072  24865  16438  -4884    -49  -3418       O  
ATOM   3881  CB  ALA A 535     172.426  82.011  54.430  1.00128.49           C  
ANISOU 3881  CB  ALA A 535    13003  21632  14185  -5171    592  -2944       C  
ATOM   3882  N   LEU A 536     171.784  82.224  57.784  1.00136.13           N  
ANISOU 3882  N   LEU A 536    13960  22710  15054  -4398   -236  -2749       N  
ATOM   3883  CA  LEU A 536     172.256  82.803  59.032  1.00122.82           C  
ANISOU 3883  CA  LEU A 536    12154  21282  13229  -4551   -452  -2949       C  
ATOM   3884  C   LEU A 536     172.833  81.717  59.929  1.00123.26           C  
ANISOU 3884  C   LEU A 536    11503  21887  13442  -4035   -822  -3044       C  
ATOM   3885  O   LEU A 536     172.274  80.624  60.050  1.00114.83           O  
ANISOU 3885  O   LEU A 536    10356  20751  12525  -3384  -1007  -2766       O  
ATOM   3886  CB  LEU A 536     171.114  83.526  59.745  1.00116.07           C  
ANISOU 3886  CB  LEU A 536    12018  19890  12194  -4430   -550  -2665       C  
ATOM   3887  CG  LEU A 536     170.445  84.670  58.978  1.00115.58           C  
ANISOU 3887  CG  LEU A 536    12753  19210  11951  -4854   -267  -2562       C  
ATOM   3888  CD1 LEU A 536     169.257  85.219  59.755  1.00113.00           C  
ANISOU 3888  CD1 LEU A 536    13047  18392  11496  -4584   -414  -2306       C  
ATOM   3889  CD2 LEU A 536     171.443  85.779  58.666  1.00122.79           C  
ANISOU 3889  CD2 LEU A 536    13730  20255  12669  -5703    -27  -2941       C  
ATOM   3890  N   GLN A 537     173.961  82.021  60.556  1.00137.30           N  
ANISOU 3890  N   GLN A 537    12794  24202  15171  -4333   -945  -3450       N  
ATOM   3891  CA  GLN A 537     174.596  81.075  61.462  1.00146.55           C  
ANISOU 3891  CA  GLN A 537    13316  25906  16461  -3843  -1360  -3583       C  
ATOM   3892  C   GLN A 537     173.897  81.094  62.816  1.00148.95           C  
ANISOU 3892  C   GLN A 537    13962  26019  16614  -3460  -1705  -3324       C  
ATOM   3893  O   GLN A 537     173.982  82.094  63.539  1.00144.19           O  
ANISOU 3893  O   GLN A 537    13594  25395  15795  -3831  -1737  -3445       O  
ATOM   3894  CB  GLN A 537     176.080  81.402  61.613  1.00154.29           C  
ANISOU 3894  CB  GLN A 537    13603  27574  17448  -4302  -1386  -4166       C  
ATOM   3895  CG  GLN A 537     176.960  80.710  60.598  1.00163.07           C  
ANISOU 3895  CG  GLN A 537    14169  28985  18806  -4257  -1180  -4407       C  
ATOM   3896  CD  GLN A 537     177.983  81.639  59.983  1.00174.44           C  
ANISOU 3896  CD  GLN A 537    15519  30587  20172  -4995   -766  -4817       C  
ATOM   3897  OE1 GLN A 537     178.127  82.788  60.400  1.00173.12           O  
ANISOU 3897  OE1 GLN A 537    15638  30363  19778  -5545   -669  -4948       O  
ATOM   3898  NE2 GLN A 537     178.696  81.147  58.977  1.00183.85           N  
ANISOU 3898  NE2 GLN A 537    16359  31965  21531  -5013   -504  -5027       N  
ATOM   3899  N   PRO A 538     173.204  80.019  63.191  1.00152.18           N  
ANISOU 3899  N   PRO A 538    14434  26281  17107  -2758  -1949  -2981       N  
ATOM   3900  CA  PRO A 538     172.432  80.013  64.444  1.00153.32           C  
ANISOU 3900  CA  PRO A 538    14974  26205  17074  -2428  -2225  -2720       C  
ATOM   3901  C   PRO A 538     173.362  79.972  65.642  1.00153.67           C  
ANISOU 3901  C   PRO A 538    14613  26762  17014  -2381  -2625  -2996       C  
ATOM   3902  O   PRO A 538     174.547  79.637  65.492  1.00158.89           O  
ANISOU 3902  O   PRO A 538    14601  27973  17798  -2424  -2754  -3360       O  
ATOM   3903  CB  PRO A 538     171.601  78.725  64.336  1.00153.41           C  
ANISOU 3903  CB  PRO A 538    15092  25983  17215  -1748  -2336  -2332       C  
ATOM   3904  CG  PRO A 538     172.447  77.822  63.477  1.00155.58           C  
ANISOU 3904  CG  PRO A 538    14756  26613  17742  -1590  -2335  -2511       C  
ATOM   3905  CD  PRO A 538     173.140  78.724  62.488  1.00154.70           C  
ANISOU 3905  CD  PRO A 538    14467  26642  17670  -2261  -1972  -2843       C  
ATOM   3906  N   PRO A 539     172.880  80.338  66.834  1.00148.81           N  
ANISOU 3906  N   PRO A 539    14372  26004  16165  -2307  -2829  -2871       N  
ATOM   3907  CA  PRO A 539     173.716  80.237  68.039  1.00150.51           C  
ANISOU 3907  CA  PRO A 539    14249  26691  16248  -2216  -3262  -3109       C  
ATOM   3908  C   PRO A 539     174.336  78.854  68.204  1.00154.53           C  
ANISOU 3908  C   PRO A 539    14240  27557  16916  -1610  -3641  -3135       C  
ATOM   3909  O   PRO A 539     173.729  77.836  67.863  1.00140.42           O  
ANISOU 3909  O   PRO A 539    12556  25558  15241  -1120  -3672  -2831       O  
ATOM   3910  CB  PRO A 539     172.730  80.540  69.170  1.00145.04           C  
ANISOU 3910  CB  PRO A 539    14184  25637  15287  -2080  -3383  -2828       C  
ATOM   3911  CG  PRO A 539     171.777  81.540  68.538  1.00137.60           C  
ANISOU 3911  CG  PRO A 539    13821  24153  14308  -2456  -2934  -2681       C  
ATOM   3912  CD  PRO A 539     171.633  81.084  67.091  1.00139.32           C  
ANISOU 3912  CD  PRO A 539    13917  24227  14790  -2410  -2642  -2587       C  
ATOM   3913  N   HIS A 540     175.547  78.844  68.774  1.00171.51           N  
ANISOU 3913  N   HIS A 540    16016  30018  19132  -1593  -3837  -3424       N  
ATOM   3914  CA  HIS A 540     176.423  77.684  68.969  1.00185.18           C  
ANISOU 3914  CA  HIS A 540    17355  31929  21077  -1038  -4127  -3483       C  
ATOM   3915  C   HIS A 540     175.748  76.325  69.103  1.00179.37           C  
ANISOU 3915  C   HIS A 540    16850  30912  20390   -336  -4352  -3086       C  
ATOM   3916  O   HIS A 540     176.165  75.363  68.451  1.00179.98           O  
ANISOU 3916  O   HIS A 540    16643  31017  20724     14  -4355  -3099       O  
ATOM   3917  CB  HIS A 540     177.321  77.880  70.203  1.00202.79           C  
ANISOU 3917  CB  HIS A 540    19449  34402  23201   -998  -4486  -3693       C  
ATOM   3918  CG  HIS A 540     176.608  78.353  71.436  1.00218.03           C  
ANISOU 3918  CG  HIS A 540    21904  36145  24791  -1032  -4697  -3495       C  
ATOM   3919  ND1 HIS A 540     175.344  78.901  71.418  1.00215.79           N  
ANISOU 3919  ND1 HIS A 540    22146  35554  24289  -1242  -4505  -3246       N  
ATOM   3920  CD2 HIS A 540     177.006  78.379  72.731  1.00225.65           C  
ANISOU 3920  CD2 HIS A 540    22960  37196  25583   -898  -5079  -3533       C  
ATOM   3921  CE1 HIS A 540     174.993  79.242  72.645  1.00217.98           C  
ANISOU 3921  CE1 HIS A 540    22816  35736  24273  -1238  -4730  -3149       C  
ATOM   3922  NE2 HIS A 540     175.983  78.933  73.461  1.00221.83           N  
ANISOU 3922  NE2 HIS A 540    23057  36451  24776  -1040  -5084  -3310       N  
ATOM   3923  N   GLY A 541     174.744  76.217  69.964  1.00174.20           N  
ANISOU 3923  N   GLY A 541    16738  29974  19478   -141  -4524  -2749       N  
ATOM   3924  CA  GLY A 541     174.155  74.926  70.256  1.00171.34           C  
ANISOU 3924  CA  GLY A 541    16671  29315  19114    482  -4741  -2375       C  
ATOM   3925  C   GLY A 541     172.825  74.673  69.578  1.00159.19           C  
ANISOU 3925  C   GLY A 541    15491  27445  17549    559  -4484  -2033       C  
ATOM   3926  O   GLY A 541     172.479  73.523  69.295  1.00159.05           O  
ANISOU 3926  O   GLY A 541    15589  27198  17646   1016  -4530  -1781       O  
ATOM   3927  N   ILE A 542     172.080  75.726  69.297  1.00147.65           N  
ANISOU 3927  N   ILE A 542    14239  25921  15940    107  -4203  -2024       N  
ATOM   3928  CA  ILE A 542     170.710  75.596  68.815  1.00141.22           C  
ANISOU 3928  CA  ILE A 542    13962  24549  15145    168  -3858  -1635       C  
ATOM   3929  C   ILE A 542     170.706  75.456  67.299  1.00133.46           C  
ANISOU 3929  C   ILE A 542    12760  23484  14465     77  -3503  -1652       C  
ATOM   3930  O   ILE A 542     171.584  75.978  66.603  1.00128.84           O  
ANISOU 3930  O   ILE A 542    11746  23188  14019   -273  -3369  -1978       O  
ATOM   3931  CB  ILE A 542     169.869  76.802  69.280  1.00144.91           C  
ANISOU 3931  CB  ILE A 542    14953  24704  15403   -232  -3621  -1565       C  
ATOM   3932  CG1 ILE A 542     169.593  77.760  68.123  1.00146.90           C  
ANISOU 3932  CG1 ILE A 542    15275  24740  15800   -687  -3157  -1634       C  
ATOM   3933  CG2 ILE A 542     170.595  77.550  70.393  1.00139.83           C  
ANISOU 3933  CG2 ILE A 542    14227  24377  14525   -480  -3885  -1832       C  
ATOM   3934  CD1 ILE A 542     169.130  79.115  68.580  1.00147.42           C  
ANISOU 3934  CD1 ILE A 542    15760  24588  15667  -1123  -2989  -1694       C  
ATOM   3935  N   GLU A 543     169.715  74.735  66.777  1.00136.52           N  
ANISOU 3935  N   GLU A 543    13450  23485  14938    363  -3339  -1314       N  
ATOM   3936  CA  GLU A 543     169.506  74.600  65.341  1.00135.66           C  
ANISOU 3936  CA  GLU A 543    13244  23219  15080    282  -2986  -1277       C  
ATOM   3937  C   GLU A 543     168.183  75.253  64.971  1.00120.78           C  
ANISOU 3937  C   GLU A 543    11921  20823  13148     82  -2628  -1034       C  
ATOM   3938  O   GLU A 543     167.184  75.093  65.679  1.00108.40           O  
ANISOU 3938  O   GLU A 543    10789  18973  11427    267  -2665   -784       O  
ATOM   3939  CB  GLU A 543     169.513  73.131  64.901  1.00139.21           C  
ANISOU 3939  CB  GLU A 543    13528  23665  15701    813  -3111  -1123       C  
ATOM   3940  CG  GLU A 543     168.586  72.223  65.693  1.00145.90           C  
ANISOU 3940  CG  GLU A 543    14824  24218  16394   1256  -3294   -761       C  
ATOM   3941  CD  GLU A 543     168.587  70.797  65.180  1.00145.73           C  
ANISOU 3941  CD  GLU A 543    14699  24142  16530   1744  -3394   -612       C  
ATOM   3942  OE1 GLU A 543     168.919  70.588  63.993  1.00144.03           O  
ANISOU 3942  OE1 GLU A 543    14166  23989  16569   1714  -3197   -715       O  
ATOM   3943  OE2 GLU A 543     168.259  69.885  65.968  1.00146.88           O  
ANISOU 3943  OE2 GLU A 543    15121  24164  16523   2141  -3665   -396       O  
ATOM   3944  N   VAL A 544     168.183  75.994  63.866  1.00125.09           N  
ANISOU 3944  N   VAL A 544    12465  21255  13809   -301  -2289  -1133       N  
ATOM   3945  CA  VAL A 544     167.052  76.826  63.471  1.00126.42           C  
ANISOU 3945  CA  VAL A 544    13158  20953  13925   -519  -1989   -975       C  
ATOM   3946  C   VAL A 544     166.353  76.188  62.276  1.00112.33           C  
ANISOU 3946  C   VAL A 544    11466  18884  12329   -335  -1765   -766       C  
ATOM   3947  O   VAL A 544     167.008  75.741  61.326  1.00100.85           O  
ANISOU 3947  O   VAL A 544     9667  17597  11053   -354  -1682   -866       O  
ATOM   3948  CB  VAL A 544     167.496  78.266  63.155  1.00134.78           C  
ANISOU 3948  CB  VAL A 544    14293  22011  14907  -1118  -1797  -1230       C  
ATOM   3949  CG1 VAL A 544     168.613  78.279  62.116  1.00143.61           C  
ANISOU 3949  CG1 VAL A 544    14962  23426  16176  -1410  -1660  -1495       C  
ATOM   3950  CG2 VAL A 544     166.313  79.108  62.694  1.00126.98           C  
ANISOU 3950  CG2 VAL A 544    13892  20490  13864  -1273  -1537  -1073       C  
ATOM   3951  N   PHE A 545     165.025  76.133  62.336  1.00107.81           N  
ANISOU 3951  N   PHE A 545    11337  17906  11718   -160  -1667   -505       N  
ATOM   3952  CA  PHE A 545     164.191  75.682  61.231  1.00103.50           C  
ANISOU 3952  CA  PHE A 545    10945  17051  11328    -17  -1452   -313       C  
ATOM   3953  C   PHE A 545     163.374  76.860  60.719  1.00105.48           C  
ANISOU 3953  C   PHE A 545    11630  16917  11530   -297  -1224   -305       C  
ATOM   3954  O   PHE A 545     162.714  77.548  61.505  1.00100.98           O  
ANISOU 3954  O   PHE A 545    11383  16175  10810   -333  -1250   -293       O  
ATOM   3955  CB  PHE A 545     163.256  74.547  61.659  1.00 98.46           C  
ANISOU 3955  CB  PHE A 545    10449  16267  10695    440  -1535    -43       C  
ATOM   3956  CG  PHE A 545     163.961  73.377  62.281  1.00104.92           C  
ANISOU 3956  CG  PHE A 545    10973  17381  11511    764  -1812    -21       C  
ATOM   3957  CD1 PHE A 545     164.487  72.368  61.491  1.00 99.37           C  
ANISOU 3957  CD1 PHE A 545     9958  16802  10998    977  -1830    -11       C  
ATOM   3958  CD2 PHE A 545     164.086  73.279  63.656  1.00114.48           C  
ANISOU 3958  CD2 PHE A 545    12257  18725  12514    875  -2071    -18       C  
ATOM   3959  CE1 PHE A 545     165.132  71.289  62.062  1.00106.27           C  
ANISOU 3959  CE1 PHE A 545    10602  17912  11866   1332  -2128     -3       C  
ATOM   3960  CE2 PHE A 545     164.730  72.202  64.233  1.00123.09           C  
ANISOU 3960  CE2 PHE A 545    13147  20047  13574   1210  -2378      9       C  
ATOM   3961  CZ  PHE A 545     165.254  71.206  63.434  1.00119.27           C  
ANISOU 3961  CZ  PHE A 545    12357  19667  13291   1458  -2420     14       C  
ATOM   3962  N   VAL A 546     163.418  77.090  59.410  1.00 99.05           N  
ANISOU 3962  N   VAL A 546    10851  15956  10828   -479  -1013   -325       N  
ATOM   3963  CA  VAL A 546     162.705  78.195  58.781  1.00 82.00           C  
ANISOU 3963  CA  VAL A 546     9156  13390   8610   -722   -834   -320       C  
ATOM   3964  C   VAL A 546     161.376  77.675  58.254  1.00 75.10           C  
ANISOU 3964  C   VAL A 546     8528  12174   7833   -384   -764    -86       C  
ATOM   3965  O   VAL A 546     161.344  76.848  57.334  1.00 67.86           O  
ANISOU 3965  O   VAL A 546     7468  11250   7066   -244   -684     12       O  
ATOM   3966  CB  VAL A 546     163.532  78.835  57.656  1.00 89.74           C  
ANISOU 3966  CB  VAL A 546    10120  14380   9597  -1176   -649   -488       C  
ATOM   3967  CG1 VAL A 546     162.732  79.938  56.978  1.00 87.23           C  
ANISOU 3967  CG1 VAL A 546    10393  13567   9184  -1383   -508   -452       C  
ATOM   3968  CG2 VAL A 546     164.842  79.380  58.208  1.00 93.42           C  
ANISOU 3968  CG2 VAL A 546    10303  15228   9964  -1559   -701   -772       C  
ATOM   3969  N   GLY A 547     160.281  78.163  58.831  1.00 83.85           N  
ANISOU 3969  N   GLY A 547     9986  13017   8858   -258   -790    -30       N  
ATOM   3970  CA  GLY A 547     158.956  77.724  58.442  1.00 80.66           C  
ANISOU 3970  CA  GLY A 547     9776  12330   8544     58   -734    135       C  
ATOM   3971  C   GLY A 547     158.012  78.857  58.097  1.00 77.93           C  
ANISOU 3971  C   GLY A 547     9891  11574   8143      0   -680     88       C  
ATOM   3972  O   GLY A 547     158.448  79.959  57.752  1.00 72.86           O  
ANISOU 3972  O   GLY A 547     9490  10789   7406   -325   -649    -36       O  
ATOM   3973  N   GLY A 548     156.714  78.599  58.196  1.00 82.68           N  
ANISOU 3973  N   GLY A 548    10634  11984   8798    313   -677    162       N  
ATOM   3974  CA  GLY A 548     155.705  79.534  57.752  1.00 72.28           C  
ANISOU 3974  CA  GLY A 548     9721  10274   7469    368   -666    100       C  
ATOM   3975  C   GLY A 548     155.164  79.170  56.379  1.00 77.03           C  
ANISOU 3975  C   GLY A 548    10405  10655   8207    498   -609    202       C  
ATOM   3976  O   GLY A 548     155.799  78.467  55.589  1.00 63.08           O  
ANISOU 3976  O   GLY A 548     8442   9005   6521    426   -543    298       O  
ATOM   3977  N   THR A 549     153.959  79.661  56.094  1.00 80.45           N  
ANISOU 3977  N   THR A 549    11128  10772   8666    711   -648    156       N  
ATOM   3978  CA  THR A 549     153.319  79.325  54.825  1.00 87.49           C  
ANISOU 3978  CA  THR A 549    12117  11448   9677    873   -634    239       C  
ATOM   3979  C   THR A 549     154.118  79.761  53.601  1.00 81.95           C  
ANISOU 3979  C   THR A 549    11639  10575   8921    576   -596    278       C  
ATOM   3980  O   THR A 549     154.108  79.016  52.605  1.00 85.94           O  
ANISOU 3980  O   THR A 549    12051  11078   9525    625   -535    393       O  
ATOM   3981  CB  THR A 549     151.892  79.889  54.788  1.00 87.52           C  
ANISOU 3981  CB  THR A 549    12384  11157   9714   1180   -732    125       C  
ATOM   3982  OG1 THR A 549     151.898  81.277  55.138  1.00101.56           O  
ANISOU 3982  OG1 THR A 549    14554  12687  11348   1074   -828    -34       O  
ATOM   3983  CG2 THR A 549     151.021  79.136  55.766  1.00 89.78           C  
ANISOU 3983  CG2 THR A 549    12372  11663  10076   1451   -698     84       C  
ATOM   3984  N   PRO A 550     154.819  80.903  53.583  1.00 88.97           N  
ANISOU 3984  N   PRO A 550    12842  11319   9642    234   -607    180       N  
ATOM   3985  CA  PRO A 550     155.724  81.151  52.450  1.00 88.28           C  
ANISOU 3985  CA  PRO A 550    12924  11140   9477   -138   -509    208       C  
ATOM   3986  C   PRO A 550     156.834  80.122  52.347  1.00 80.98           C  
ANISOU 3986  C   PRO A 550    11490  10644   8635   -303   -371    257       C  
ATOM   3987  O   PRO A 550     157.262  79.795  51.234  1.00 77.72           O  
ANISOU 3987  O   PRO A 550    11079  10211   8242   -461   -259    307       O  
ATOM   3988  CB  PRO A 550     156.272  82.556  52.737  1.00 90.62           C  
ANISOU 3988  CB  PRO A 550    13637  11242   9551   -514   -530     62       C  
ATOM   3989  CG  PRO A 550     155.242  83.190  53.596  1.00 82.18           C  
ANISOU 3989  CG  PRO A 550    12789   9972   8463   -215   -688    -24       C  
ATOM   3990  CD  PRO A 550     154.737  82.083  54.464  1.00 87.16           C  
ANISOU 3990  CD  PRO A 550    12903  10948   9265    143   -692     24       C  
ATOM   3991  N   ALA A 551     157.307  79.587  53.475  1.00 87.80           N  
ANISOU 3991  N   ALA A 551    11929  11891   9539   -252   -389    230       N  
ATOM   3992  CA  ALA A 551     158.332  78.551  53.428  1.00 94.86           C  
ANISOU 3992  CA  ALA A 551    12322  13193  10527   -319   -313    252       C  
ATOM   3993  C   ALA A 551     157.747  77.206  53.019  1.00 99.28           C  
ANISOU 3993  C   ALA A 551    12643  13812  11269     50   -297    415       C  
ATOM   3994  O   ALA A 551     158.396  76.436  52.302  1.00 90.93           O  
ANISOU 3994  O   ALA A 551    11331  12918  10299      0   -203    446       O  
ATOM   3995  CB  ALA A 551     159.034  78.443  54.781  1.00 84.78           C  
ANISOU 3995  CB  ALA A 551    10724  12281   9207   -353   -397    163       C  
ATOM   3996  N   LEU A 552     156.526  76.905  53.470  1.00104.69           N  
ANISOU 3996  N   LEU A 552    13399  14372  12005    404   -371    493       N  
ATOM   3997  CA  LEU A 552     155.855  75.685  53.036  1.00 89.63           C  
ANISOU 3997  CA  LEU A 552    11324  12480  10250    713   -339    635       C  
ATOM   3998  C   LEU A 552     155.614  75.699  51.532  1.00 88.46           C  
ANISOU 3998  C   LEU A 552    11372  12087  10150    668   -265    685       C  
ATOM   3999  O   LEU A 552     155.789  74.678  50.857  1.00 90.82           O  
ANISOU 3999  O   LEU A 552    11464  12483  10560    746   -187    775       O  
ATOM   4000  CB  LEU A 552     154.531  75.520  53.783  1.00 86.83           C  
ANISOU 4000  CB  LEU A 552    11034  12039   9917   1024   -402    651       C  
ATOM   4001  CG  LEU A 552     154.581  75.403  55.305  1.00 75.01           C  
ANISOU 4001  CG  LEU A 552     9399  10762   8341   1082   -461    613       C  
ATOM   4002  CD1 LEU A 552     153.183  75.542  55.883  1.00 66.12           C  
ANISOU 4002  CD1 LEU A 552     8405   9507   7212   1310   -476    559       C  
ATOM   4003  CD2 LEU A 552     155.196  74.081  55.715  1.00 68.95           C  
ANISOU 4003  CD2 LEU A 552     8290  10293   7615   1175   -459    724       C  
ATOM   4004  N   GLU A 553     155.219  76.853  50.990  1.00 84.35           N  
ANISOU 4004  N   GLU A 553    11294  11226   9528    547   -303    625       N  
ATOM   4005  CA  GLU A 553     154.951  76.946  49.559  1.00 82.67           C  
ANISOU 4005  CA  GLU A 553    11359  10739   9313    499   -266    677       C  
ATOM   4006  C   GLU A 553     156.234  76.833  48.744  1.00 83.19           C  
ANISOU 4006  C   GLU A 553    11348  10929   9332    121   -104    663       C  
ATOM   4007  O   GLU A 553     156.272  76.113  47.740  1.00 76.47           O  
ANISOU 4007  O   GLU A 553    10432  10073   8550    139    -12    737       O  
ATOM   4008  CB  GLU A 553     154.222  78.253  49.249  1.00 70.24           C  
ANISOU 4008  CB  GLU A 553    10352   8731   7607    492   -396    610       C  
ATOM   4009  CG  GLU A 553     152.824  78.327  49.847  1.00 79.34           C  
ANISOU 4009  CG  GLU A 553    11548   9762   8835    910   -551    569       C  
ATOM   4010  CD  GLU A 553     152.194  79.695  49.697  1.00 85.71           C  
ANISOU 4010  CD  GLU A 553    12905  10149   9513    950   -723    456       C  
ATOM   4011  OE1 GLU A 553     152.787  80.547  49.004  1.00 82.65           O  
ANISOU 4011  OE1 GLU A 553    12948   9504   8952    640   -724    450       O  
ATOM   4012  OE2 GLU A 553     151.108  79.918  50.272  1.00 83.69           O  
ANISOU 4012  OE2 GLU A 553    12668   9814   9316   1286   -854    354       O  
ATOM   4013  N   GLN A 554     157.298  77.522  49.163  1.00 89.96           N  
ANISOU 4013  N   GLN A 554    12188  11923  10070   -243    -52    539       N  
ATOM   4014  CA  GLN A 554     158.538  77.504  48.395  1.00 94.48           C  
ANISOU 4014  CA  GLN A 554    12660  12651  10588   -660    134    458       C  
ATOM   4015  C   GLN A 554     159.270  76.173  48.491  1.00 85.92           C  
ANISOU 4015  C   GLN A 554    10961  12003   9680   -547    216    458       C  
ATOM   4016  O   GLN A 554     160.126  75.891  47.647  1.00 82.39           O  
ANISOU 4016  O   GLN A 554    10368  11696   9238   -804    389    382       O  
ATOM   4017  CB  GLN A 554     159.465  78.636  48.846  1.00 96.22           C  
ANISOU 4017  CB  GLN A 554    13011  12924  10625  -1119    176    279       C  
ATOM   4018  CG  GLN A 554     158.906  80.035  48.623  1.00 98.41           C  
ANISOU 4018  CG  GLN A 554    13990  12715  10687  -1290    103    261       C  
ATOM   4019  CD  GLN A 554     158.491  80.289  47.187  1.00100.49           C  
ANISOU 4019  CD  GLN A 554    14762  12574  10847  -1390    151    341       C  
ATOM   4020  OE1 GLN A 554     157.490  80.959  46.930  1.00103.35           O  
ANISOU 4020  OE1 GLN A 554    15659  12489  11121  -1213    -12    402       O  
ATOM   4021  NE2 GLN A 554     159.263  79.764  46.242  1.00102.74           N  
ANISOU 4021  NE2 GLN A 554    14891  13014  11130  -1665    362    322       N  
ATOM   4022  N   ASP A 555     158.962  75.352  49.496  1.00 89.94           N  
ANISOU 4022  N   ASP A 555    11136  12719  10318   -174     97    525       N  
ATOM   4023  CA  ASP A 555     159.577  74.031  49.577  1.00 95.65           C  
ANISOU 4023  CA  ASP A 555    11353  13791  11199      2    127    539       C  
ATOM   4024  C   ASP A 555     158.840  73.004  48.727  1.00 87.29           C  
ANISOU 4024  C   ASP A 555    10300  12599  10269    280    175    694       C  
ATOM   4025  O   ASP A 555     159.468  72.083  48.194  1.00 77.03           O  
ANISOU 4025  O   ASP A 555     8701  11493   9075    311    268    678       O  
ATOM   4026  CB  ASP A 555     159.644  73.567  51.033  1.00 95.33           C  
ANISOU 4026  CB  ASP A 555    11031  14000  11191    256    -37    551       C  
ATOM   4027  CG  ASP A 555     160.710  74.299  51.828  1.00 90.34           C  
ANISOU 4027  CG  ASP A 555    10243  13625  10456    -25    -84    361       C  
ATOM   4028  OD1 ASP A 555     161.646  74.843  51.203  1.00 84.22           O  
ANISOU 4028  OD1 ASP A 555     9422  12947   9632   -416     46    193       O  
ATOM   4029  OD2 ASP A 555     160.616  74.329  53.074  1.00 79.00           O  
ANISOU 4029  OD2 ASP A 555     8738  12304   8975    116   -240    363       O  
ATOM   4030  N   SER A 556     157.519  73.143  48.589  1.00 88.33           N  
ANISOU 4030  N   SER A 556    10748  12416  10396    487    108    815       N  
ATOM   4031  CA  SER A 556     156.782  72.287  47.666  1.00 82.53           C  
ANISOU 4031  CA  SER A 556    10056  11538   9765    695    156    937       C  
ATOM   4032  C   SER A 556     157.101  72.645  46.220  1.00 85.37           C  
ANISOU 4032  C   SER A 556    10650  11728  10060    416    290    907       C  
ATOM   4033  O   SER A 556     157.195  71.760  45.361  1.00 80.57           O  
ANISOU 4033  O   SER A 556     9922  11153   9537    469    395    953       O  
ATOM   4034  CB  SER A 556     155.281  72.400  47.932  1.00 77.38           C  
ANISOU 4034  CB  SER A 556     9635  10641   9126    977     38   1015       C  
ATOM   4035  OG  SER A 556     154.546  71.538  47.084  1.00 82.06           O  
ANISOU 4035  OG  SER A 556    10237  11124   9818   1168     75   1111       O  
ATOM   4036  N   ILE A 557     157.265  73.940  45.936  1.00 86.13           N  
ANISOU 4036  N   ILE A 557    11127  11618   9981    100    294    829       N  
ATOM   4037  CA  ILE A 557     157.714  74.375  44.616  1.00 75.04           C  
ANISOU 4037  CA  ILE A 557    10018  10046   8448   -259    442    788       C  
ATOM   4038  C   ILE A 557     159.049  73.728  44.274  1.00 80.04           C  
ANISOU 4038  C   ILE A 557    10231  11045   9137   -498    655    668       C  
ATOM   4039  O   ILE A 557     159.223  73.138  43.202  1.00 76.61           O  
ANISOU 4039  O   ILE A 557     9778  10604   8728   -563    803    677       O  
ATOM   4040  CB  ILE A 557     157.814  75.909  44.567  1.00 79.37           C  
ANISOU 4040  CB  ILE A 557    11085  10315   8758   -606    409    709       C  
ATOM   4041  CG1 ILE A 557     156.428  76.550  44.660  1.00 87.83           C  
ANISOU 4041  CG1 ILE A 557    12616  10977   9781   -318    177    795       C  
ATOM   4042  CG2 ILE A 557     158.551  76.350  43.314  1.00 75.11           C  
ANISOU 4042  CG2 ILE A 557    10851   9654   8034  -1095    612    639       C  
ATOM   4043  CD1 ILE A 557     156.464  78.027  44.983  1.00 96.96           C  
ANISOU 4043  CD1 ILE A 557    14261  11859  10721   -556     87    710       C  
ATOM   4044  N   HIS A 558     160.010  73.823  45.195  1.00102.13           N  
ANISOU 4044  N   HIS A 558    12664  14185  11956   -617    665    527       N  
ATOM   4045  CA  HIS A 558     161.352  73.314  44.936  1.00107.16           C  
ANISOU 4045  CA  HIS A 558    12844  15218  12654   -839    845    339       C  
ATOM   4046  C   HIS A 558     161.354  71.797  44.786  1.00102.96           C  
ANISOU 4046  C   HIS A 558    11895  14884  12343   -452    849    400       C  
ATOM   4047  O   HIS A 558     162.108  71.251  43.972  1.00 90.09           O  
ANISOU 4047  O   HIS A 558    10028  13435  10767   -588   1036    275       O  
ATOM   4048  CB  HIS A 558     162.290  73.749  46.061  1.00104.18           C  
ANISOU 4048  CB  HIS A 558    12147  15179  12259   -992    791    154       C  
ATOM   4049  CG  HIS A 558     163.712  73.327  45.864  1.00112.09           C  
ANISOU 4049  CG  HIS A 558    12619  16639  13332  -1218    951   -113       C  
ATOM   4050  ND1 HIS A 558     164.237  72.190  46.439  1.00114.40           N  
ANISOU 4050  ND1 HIS A 558    12330  17310  13826   -862    852   -173       N  
ATOM   4051  CD2 HIS A 558     164.721  73.893  45.161  1.00120.75           C  
ANISOU 4051  CD2 HIS A 558    13676  17887  14318  -1765   1200   -367       C  
ATOM   4052  CE1 HIS A 558     165.508  72.072  46.097  1.00118.02           C  
ANISOU 4052  CE1 HIS A 558    12362  18156  14324  -1134   1013   -475       C  
ATOM   4053  NE2 HIS A 558     165.826  73.093  45.322  1.00123.38           N  
ANISOU 4053  NE2 HIS A 558    13337  18725  14815  -1713   1251   -608       N  
ATOM   4054  N   SER A 559     160.516  71.100  45.557  1.00102.09           N  
ANISOU 4054  N   SER A 559    11712  14733  12346     12    661    573       N  
ATOM   4055  CA  SER A 559     160.487  69.642  45.483  1.00107.05           C  
ANISOU 4055  CA  SER A 559    12017  15500  13155    377    651    643       C  
ATOM   4056  C   SER A 559     159.916  69.158  44.157  1.00109.59           C  
ANISOU 4056  C   SER A 559    12547  15589  13501    396    783    735       C  
ATOM   4057  O   SER A 559     160.314  68.097  43.663  1.00104.51           O  
ANISOU 4057  O   SER A 559    11638  15088  12982    526    873    705       O  
ATOM   4058  CB  SER A 559     159.679  69.067  46.646  1.00 96.02           C  
ANISOU 4058  CB  SER A 559    10584  14080  11820    794    442    805       C  
ATOM   4059  OG  SER A 559     158.309  69.413  46.535  1.00 89.10           O  
ANISOU 4059  OG  SER A 559    10099  12861  10893    892    390    959       O  
ATOM   4060  N   LEU A 560     158.989  69.916  43.568  1.00111.04           N  
ANISOU 4060  N   LEU A 560    13216  15411  13564    288    775    832       N  
ATOM   4061  CA  LEU A 560     158.419  69.517  42.287  1.00101.79           C  
ANISOU 4061  CA  LEU A 560    12279  14010  12388    297    869    914       C  
ATOM   4062  C   LEU A 560     159.431  69.684  41.160  1.00 95.57           C  
ANISOU 4062  C   LEU A 560    11497  13300  11517   -110   1116    758       C  
ATOM   4063  O   LEU A 560     159.683  68.746  40.395  1.00 98.85           O  
ANISOU 4063  O   LEU A 560    11739  13799  12020    -57   1254    734       O  
ATOM   4064  CB  LEU A 560     157.155  70.325  41.999  1.00 84.78           C  
ANISOU 4064  CB  LEU A 560    10647  11449  10115    332    736   1032       C  
ATOM   4065  CG  LEU A 560     156.485  69.991  40.667  1.00 96.30           C  
ANISOU 4065  CG  LEU A 560    12393  12652  11544    351    782   1113       C  
ATOM   4066  CD1 LEU A 560     155.009  69.729  40.875  1.00104.33           C  
ANISOU 4066  CD1 LEU A 560    13544  13468  12630    728    587   1241       C  
ATOM   4067  CD2 LEU A 560     156.696  71.105  39.654  1.00 98.25           C  
ANISOU 4067  CD2 LEU A 560    13148  12634  11549    -53    848   1065       C  
ATOM   4068  N   PHE A 561     160.027  70.872  41.048  1.00 85.39           N  
ANISOU 4068  N   PHE A 561    10420  11982  10043   -548   1196    630       N  
ATOM   4069  CA  PHE A 561     160.952  71.158  39.959  1.00 87.78           C  
ANISOU 4069  CA  PHE A 561    10796  12343  10213  -1033   1473    456       C  
ATOM   4070  C   PHE A 561     162.300  70.471  40.124  1.00 88.10           C  
ANISOU 4070  C   PHE A 561    10195  12883  10396  -1117   1647    205       C  
ATOM   4071  O   PHE A 561     163.123  70.536  39.204  1.00 78.76           O  
ANISOU 4071  O   PHE A 561     8970  11823   9131  -1516   1922      8       O  
ATOM   4072  CB  PHE A 561     161.141  72.669  39.829  1.00 82.50           C  
ANISOU 4072  CB  PHE A 561    10620  11459   9266  -1520   1511    389       C  
ATOM   4073  CG  PHE A 561     159.925  73.382  39.318  1.00 94.39           C  
ANISOU 4073  CG  PHE A 561    12834  12433  10598  -1469   1349    587       C  
ATOM   4074  CD1 PHE A 561     158.933  73.795  40.188  1.00 98.63           C  
ANISOU 4074  CD1 PHE A 561    13539  12769  11166  -1130   1063    721       C  
ATOM   4075  CD2 PHE A 561     159.766  73.626  37.964  1.00106.63           C  
ANISOU 4075  CD2 PHE A 561    14881  13687  11944  -1742   1470    617       C  
ATOM   4076  CE1 PHE A 561     157.807  74.442  39.721  1.00102.08           C  
ANISOU 4076  CE1 PHE A 561    14584  12737  11463  -1022    877    857       C  
ATOM   4077  CE2 PHE A 561     158.642  74.276  37.490  1.00108.94           C  
ANISOU 4077  CE2 PHE A 561    15840  13482  12072  -1639   1260    784       C  
ATOM   4078  CZ  PHE A 561     157.661  74.685  38.371  1.00105.46           C  
ANISOU 4078  CZ  PHE A 561    15516  12861  11693  -1257    951    892       C  
ATOM   4079  N   ASP A 562     162.548  69.822  41.263  1.00 87.99           N  
ANISOU 4079  N   ASP A 562     9694  13160  10578   -752   1487    187       N  
ATOM   4080  CA  ASP A 562     163.760  69.025  41.409  1.00104.00           C  
ANISOU 4080  CA  ASP A 562    11088  15656  12770   -709   1584    -64       C  
ATOM   4081  C   ASP A 562     163.590  67.642  40.794  1.00103.01           C  
ANISOU 4081  C   ASP A 562    10771  15550  12818   -360   1631    -12       C  
ATOM   4082  O   ASP A 562     164.498  67.140  40.123  1.00 96.53           O  
ANISOU 4082  O   ASP A 562     9621  14989  12065   -484   1840   -252       O  
ATOM   4083  CB  ASP A 562     164.142  68.909  42.885  1.00104.31           C  
ANISOU 4083  CB  ASP A 562    10739  15977  12916   -444   1347   -111       C  
ATOM   4084  CG  ASP A 562     165.234  67.884  43.125  1.00112.73           C  
ANISOU 4084  CG  ASP A 562    11148  17499  14183   -222   1343   -349       C  
ATOM   4085  OD1 ASP A 562     166.378  68.118  42.682  1.00117.69           O  
ANISOU 4085  OD1 ASP A 562    11451  18455  14809   -571   1548   -685       O  
ATOM   4086  OD2 ASP A 562     164.947  66.844  43.757  1.00110.79           O  
ANISOU 4086  OD2 ASP A 562    10724  17282  14089    300   1131   -220       O  
ATOM   4087  N   LYS A 563     162.435  67.016  41.011  1.00108.36           N  
ANISOU 4087  N   LYS A 563    11646  15962  13562     58   1453    270       N  
ATOM   4088  CA  LYS A 563     162.132  65.711  40.444  1.00118.08           C  
ANISOU 4088  CA  LYS A 563    12780  17151  14936    379   1488    345       C  
ATOM   4089  C   LYS A 563     161.275  65.797  39.189  1.00116.53           C  
ANISOU 4089  C   LYS A 563    13048  16599  14631    237   1611    479       C  
ATOM   4090  O   LYS A 563     160.888  64.758  38.646  1.00116.17           O  
ANISOU 4090  O   LYS A 563    12984  16473  14681    475   1644    555       O  
ATOM   4091  CB  LYS A 563     161.445  64.832  41.493  1.00116.96           C  
ANISOU 4091  CB  LYS A 563    12554  16964  14922    902   1231    545       C  
ATOM   4092  CG  LYS A 563     162.395  64.339  42.571  1.00129.59           C  
ANISOU 4092  CG  LYS A 563    13677  18920  16642   1140   1087    405       C  
ATOM   4093  CD  LYS A 563     161.664  63.616  43.685  1.00138.82           C  
ANISOU 4093  CD  LYS A 563    14894  19991  17862   1586    831    626       C  
ATOM   4094  CE  LYS A 563     162.649  62.931  44.618  1.00143.89           C  
ANISOU 4094  CE  LYS A 563    15111  20952  18607   1883    652    491       C  
ATOM   4095  NZ  LYS A 563     163.732  63.860  45.049  1.00145.00           N  
ANISOU 4095  NZ  LYS A 563    14957  21423  18712   1621    638    235       N  
ATOM   4096  N   LEU A 564     160.969  67.007  38.720  1.00109.84           N  
ANISOU 4096  N   LEU A 564    12648  15518  13568   -138   1658    506       N  
ATOM   4097  CA  LEU A 564     160.264  67.150  37.450  1.00 98.23           C  
ANISOU 4097  CA  LEU A 564    11655  13710  11957   -294   1749    608       C  
ATOM   4098  C   LEU A 564     161.046  66.593  36.264  1.00 98.24           C  
ANISOU 4098  C   LEU A 564    11534  13845  11949   -527   2048    430       C  
ATOM   4099  O   LEU A 564     160.427  65.924  35.418  1.00 93.34           O  
ANISOU 4099  O   LEU A 564    11091  13037  11335   -403   2082    533       O  
ATOM   4100  CB  LEU A 564     159.902  68.624  37.220  1.00 95.45           C  
ANISOU 4100  CB  LEU A 564    11866  13059  11343   -647   1707    653       C  
ATOM   4101  CG  LEU A 564     159.007  68.940  36.020  1.00 86.76           C  
ANISOU 4101  CG  LEU A 564    11372  11539  10054   -756   1697    786       C  
ATOM   4102  CD1 LEU A 564     157.692  68.191  36.130  1.00 82.14           C  
ANISOU 4102  CD1 LEU A 564    10829  10775   9607   -264   1477    992       C  
ATOM   4103  CD2 LEU A 564     158.760  70.436  35.912  1.00 88.81           C  
ANISOU 4103  CD2 LEU A 564    12224  11482  10038  -1073   1612    814       C  
ATOM   4104  N   PRO A 565     162.360  66.819  36.123  1.00 99.38           N  
ANISOU 4104  N   PRO A 565    11371  14317  12071   -876   2280    138       N  
ATOM   4105  CA  PRO A 565     163.072  66.187  34.997  1.00 96.81           C  
ANISOU 4105  CA  PRO A 565    10883  14149  11752  -1074   2589    -72       C  
ATOM   4106  C   PRO A 565     163.071  64.669  35.062  1.00 94.28           C  
ANISOU 4106  C   PRO A 565    10146  13976  11700   -574   2551    -75       C  
ATOM   4107  O   PRO A 565     162.832  64.009  34.042  1.00 94.89           O  
ANISOU 4107  O   PRO A 565    10350  13935  11769   -564   2694    -63       O  
ATOM   4108  CB  PRO A 565     164.488  66.775  35.106  1.00 98.58           C  
ANISOU 4108  CB  PRO A 565    10759  14770  11929  -1525   2823   -438       C  
ATOM   4109  CG  PRO A 565     164.610  67.229  36.514  1.00 99.95           C  
ANISOU 4109  CG  PRO A 565    10710  15085  12181  -1360   2576   -417       C  
ATOM   4110  CD  PRO A 565     163.249  67.723  36.875  1.00103.54           C  
ANISOU 4110  CD  PRO A 565    11706  15092  12543  -1166   2302    -53       C  
ATOM   4111  N   LEU A 566     163.334  64.090  36.237  1.00101.53           N  
ANISOU 4111  N   LEU A 566    10616  15125  12835   -159   2351    -90       N  
ATOM   4112  CA  LEU A 566     163.283  62.637  36.365  1.00 95.92           C  
ANISOU 4112  CA  LEU A 566     9607  14488  12353    345   2276    -68       C  
ATOM   4113  C   LEU A 566     161.880  62.112  36.092  1.00 83.37           C  
ANISOU 4113  C   LEU A 566     8431  12497  10750    602   2151    259       C  
ATOM   4114  O   LEU A 566     161.714  61.032  35.514  1.00 85.77           O  
ANISOU 4114  O   LEU A 566     8695  12745  11149    815   2217    270       O  
ATOM   4115  CB  LEU A 566     163.755  62.212  37.755  1.00 98.83           C  
ANISOU 4115  CB  LEU A 566     9535  15116  12898    740   2029   -113       C  
ATOM   4116  CG  LEU A 566     163.628  60.717  38.053  1.00102.04           C  
ANISOU 4116  CG  LEU A 566     9741  15524  13507   1301   1889    -51       C  
ATOM   4117  CD1 LEU A 566     164.454  59.901  37.068  1.00105.39           C  
ANISOU 4117  CD1 LEU A 566     9870  16134  14039   1311   2124   -333       C  
ATOM   4118  CD2 LEU A 566     164.032  60.413  39.485  1.00111.56           C  
ANISOU 4118  CD2 LEU A 566    10632  16931  14826   1678   1596    -63       C  
ATOM   4119  N   MET A 567     160.856  62.865  36.502  1.00 85.12           N  
ANISOU 4119  N   MET A 567     9036  12449  10857    585   1972    498       N  
ATOM   4120  CA  MET A 567     159.485  62.496  36.167  1.00 92.19           C  
ANISOU 4120  CA  MET A 567    10304  12996  11729    775   1863    753       C  
ATOM   4121  C   MET A 567     159.275  62.494  34.659  1.00 89.38           C  
ANISOU 4121  C   MET A 567    10263  12454  11242    513   2059    732       C  
ATOM   4122  O   MET A 567     158.738  61.533  34.097  1.00 81.63           O  
ANISOU 4122  O   MET A 567     9342  11351  10323    704   2081    806       O  
ATOM   4123  CB  MET A 567     158.502  63.456  36.837  1.00 95.10           C  
ANISOU 4123  CB  MET A 567    10988  13150  11996    782   1642    936       C  
ATOM   4124  CG  MET A 567     157.076  63.317  36.330  1.00 72.26           C  
ANISOU 4124  CG  MET A 567     8481   9921   9055    906   1536   1131       C  
ATOM   4125  SD  MET A 567     156.243  64.897  36.116  1.00 57.34           S  
ANISOU 4125  SD  MET A 567     7125   7724   6939    678   1389   1211       S  
ATOM   4126  CE  MET A 567     154.626  64.338  35.600  1.00 63.36           C  
ANISOU 4126  CE  MET A 567     8152   8199   7721    949   1235   1372       C  
ATOM   4127  N   ALA A 568     159.698  63.567  33.987  1.00 92.30           N  
ANISOU 4127  N   ALA A 568    10880  12786  11403     47   2207    629       N  
ATOM   4128  CA  ALA A 568     159.517  63.656  32.542  1.00 89.42           C  
ANISOU 4128  CA  ALA A 568    10901  12221  10855   -250   2388    613       C  
ATOM   4129  C   ALA A 568     160.298  62.574  31.808  1.00 91.29           C  
ANISOU 4129  C   ALA A 568    10822  12668  11195   -252   2655    415       C  
ATOM   4130  O   ALA A 568     159.843  62.079  30.771  1.00 74.43           O  
ANISOU 4130  O   ALA A 568     8936  10351   8992   -281   2744    459       O  
ATOM   4131  CB  ALA A 568     159.929  65.042  32.045  1.00 74.67           C  
ANISOU 4131  CB  ALA A 568     9413  10259   8698   -797   2507    529       C  
ATOM   4132  N   LEU A 569     161.470  62.194  32.324  1.00 96.53           N  
ANISOU 4132  N   LEU A 569    10933  13719  12023   -204   2769    171       N  
ATOM   4133  CA  LEU A 569     162.239  61.121  31.702  1.00 92.72           C  
ANISOU 4133  CA  LEU A 569    10098  13459  11673   -133   3001    -64       C  
ATOM   4134  C   LEU A 569     161.481  59.800  31.762  1.00 90.26           C  
ANISOU 4134  C   LEU A 569     9764  12996  11535    369   2859    106       C  
ATOM   4135  O   LEU A 569     161.324  59.113  30.747  1.00 90.27           O  
ANISOU 4135  O   LEU A 569     9887  12896  11517    350   3018     72       O  
ATOM   4136  CB  LEU A 569     163.604  60.990  32.378  1.00 89.56           C  
ANISOU 4136  CB  LEU A 569     9063  13526  11441    -97   3079   -389       C  
ATOM   4137  CG  LEU A 569     164.449  59.791  31.941  1.00 92.50           C  
ANISOU 4137  CG  LEU A 569     8972  14168  12008    106   3260   -681       C  
ATOM   4138  CD1 LEU A 569     164.799  59.885  30.464  1.00 93.49           C  
ANISOU 4138  CD1 LEU A 569     9265  14293  11963   -360   3650   -886       C  
ATOM   4139  CD2 LEU A 569     165.708  59.674  32.787  1.00 98.14           C  
ANISOU 4139  CD2 LEU A 569     9020  15354  12913    247   3235  -1011       C  
ATOM   4140  N   ILE A 570     161.003  59.430  32.952  1.00 97.05           N  
ANISOU 4140  N   ILE A 570    10501  13830  12544    791   2573    283       N  
ATOM   4141  CA  ILE A 570     160.215  58.208  33.093  1.00 89.45           C  
ANISOU 4141  CA  ILE A 570     9584  12692  11710   1218   2443    455       C  
ATOM   4142  C   ILE A 570     158.923  58.317  32.295  1.00 86.46           C  
ANISOU 4142  C   ILE A 570     9709  11955  11188   1114   2418    671       C  
ATOM   4143  O   ILE A 570     158.480  57.350  31.664  1.00 84.91           O  
ANISOU 4143  O   ILE A 570     9610  11622  11030   1251   2471    709       O  
ATOM   4144  CB  ILE A 570     159.940  57.922  34.582  1.00 80.12           C  
ANISOU 4144  CB  ILE A 570     8247  11540  10655   1608   2156    601       C  
ATOM   4145  CG1 ILE A 570     161.254  57.705  35.336  1.00 86.35           C  
ANISOU 4145  CG1 ILE A 570     8531  12691  11588   1769   2132    366       C  
ATOM   4146  CG2 ILE A 570     159.025  56.717  34.740  1.00 69.53           C  
ANISOU 4146  CG2 ILE A 570     7045   9976   9397   1971   2042    791       C  
ATOM   4147  CD1 ILE A 570     161.070  57.460  36.818  1.00 90.52           C  
ANISOU 4147  CD1 ILE A 570     8955  13244  12196   2132   1834    506       C  
ATOM   4148  N   LEU A 571     158.308  59.502  32.299  1.00 92.24           N  
ANISOU 4148  N   LEU A 571    10773  12527  11747    881   2318    793       N  
ATOM   4149  CA  LEU A 571     157.043  59.697  31.599  1.00 91.61           C  
ANISOU 4149  CA  LEU A 571    11160  12119  11531    828   2225    973       C  
ATOM   4150  C   LEU A 571     157.184  59.448  30.101  1.00 96.13           C  
ANISOU 4150  C   LEU A 571    11959  12596  11970    574   2450    881       C  
ATOM   4151  O   LEU A 571     156.297  58.855  29.476  1.00 84.75           O  
ANISOU 4151  O   LEU A 571    10743  10952  10508    673   2405    982       O  
ATOM   4152  CB  LEU A 571     156.528  61.113  31.861  1.00 88.51           C  
ANISOU 4152  CB  LEU A 571    11085  11576  10968    645   2057   1070       C  
ATOM   4153  CG  LEU A 571     155.434  61.664  30.950  1.00 87.52           C  
ANISOU 4153  CG  LEU A 571    11493  11117  10645    523   1943   1189       C  
ATOM   4154  CD1 LEU A 571     154.184  60.836  31.089  1.00 87.12           C  
ANISOU 4154  CD1 LEU A 571    11460  10935  10706    864   1768   1325       C  
ATOM   4155  CD2 LEU A 571     155.151  63.120  31.275  1.00 88.83           C  
ANISOU 4155  CD2 LEU A 571    11970  11138  10643    365   1769   1242       C  
ATOM   4156  N   ILE A 572     158.295  59.885  29.509  1.00103.67           N  
ANISOU 4156  N   ILE A 572    12858  13711  12822    215   2707    668       N  
ATOM   4157  CA  ILE A 572     158.441  59.803  28.060  1.00 87.55           C  
ANISOU 4157  CA  ILE A 572    11101  11569  10594   -107   2945    571       C  
ATOM   4158  C   ILE A 572     158.827  58.396  27.622  1.00 92.63           C  
ANISOU 4158  C   ILE A 572    11454  12336  11406     90   3129    433       C  
ATOM   4159  O   ILE A 572     158.276  57.868  26.650  1.00101.13           O  
ANISOU 4159  O   ILE A 572    12804  13223  12399     60   3187    475       O  
ATOM   4160  CB  ILE A 572     159.455  60.854  27.572  1.00 92.65           C  
ANISOU 4160  CB  ILE A 572    11847  12334  11023   -645   3192    370       C  
ATOM   4161  CG1 ILE A 572     158.889  62.263  27.759  1.00 95.51           C  
ANISOU 4161  CG1 ILE A 572    12687  12449  11153   -863   2993    535       C  
ATOM   4162  CG2 ILE A 572     159.818  60.619  26.115  1.00 94.62           C  
ANISOU 4162  CG2 ILE A 572    12330  12543  11078  -1007   3509    213       C  
ATOM   4163  CD1 ILE A 572     159.840  63.363  27.342  1.00 88.72           C  
ANISOU 4163  CD1 ILE A 572    12015  11660  10036  -1446   3235    353       C  
ATOM   4164  N   VAL A 573     159.767  57.758  28.325  1.00 87.09           N  
ANISOU 4164  N   VAL A 573    10213  11940  10938    317   3198    256       N  
ATOM   4165  CA  VAL A 573     160.257  56.462  27.862  1.00 82.10           C  
ANISOU 4165  CA  VAL A 573     9319  11417  10460    516   3375     78       C  
ATOM   4166  C   VAL A 573     159.215  55.368  28.072  1.00 81.15           C  
ANISOU 4166  C   VAL A 573     9313  11060  10459    932   3182    296       C  
ATOM   4167  O   VAL A 573     159.168  54.397  27.309  1.00 82.75           O  
ANISOU 4167  O   VAL A 573     9556  11192  10693   1009   3318    225       O  
ATOM   4168  CB  VAL A 573     161.594  56.106  28.542  1.00 76.15           C  
ANISOU 4168  CB  VAL A 573     7953  11059   9922    687   3460   -215       C  
ATOM   4169  CG1 VAL A 573     162.588  57.248  28.395  1.00 74.58           C  
ANISOU 4169  CG1 VAL A 573     7619  11125   9595    215   3664   -459       C  
ATOM   4170  CG2 VAL A 573     161.388  55.750  30.006  1.00 98.99           C  
ANISOU 4170  CG2 VAL A 573    10616  13982  13014   1161   3136    -62       C  
ATOM   4171  N   THR A 574     158.362  55.496  29.091  1.00 79.41           N  
ANISOU 4171  N   THR A 574     9161  10719  10294   1171   2887    543       N  
ATOM   4172  CA  THR A 574     157.362  54.461  29.324  1.00 88.14           C  
ANISOU 4172  CA  THR A 574    10384  11615  11490   1499   2738    724       C  
ATOM   4173  C   THR A 574     156.198  54.578  28.347  1.00 89.00           C  
ANISOU 4173  C   THR A 574    10939  11446  11429   1321   2717    858       C  
ATOM   4174  O   THR A 574     155.705  53.562  27.846  1.00 82.49           O  
ANISOU 4174  O   THR A 574    10222  10484  10638   1441   2755    880       O  
ATOM   4175  CB  THR A 574     156.857  54.513  30.770  1.00 76.87           C  
ANISOU 4175  CB  THR A 574     8868  10179  10161   1777   2466    905       C  
ATOM   4176  OG1 THR A 574     156.316  55.810  31.052  1.00 69.55           O  
ANISOU 4176  OG1 THR A 574     8123   9201   9104   1578   2329   1020       O  
ATOM   4177  CG2 THR A 574     157.992  54.213  31.738  1.00 74.55           C  
ANISOU 4177  CG2 THR A 574     8152  10144  10030   2015   2441    772       C  
ATOM   4178  N   THR A 575     155.745  55.802  28.062  1.00 92.23           N  
ANISOU 4178  N   THR A 575    11636  11759  11648   1048   2633    936       N  
ATOM   4179  CA  THR A 575     154.679  55.974  27.081  1.00 83.33           C  
ANISOU 4179  CA  THR A 575    10946  10373  10343    904   2563   1036       C  
ATOM   4180  C   THR A 575     155.151  55.618  25.678  1.00 83.58           C  
ANISOU 4180  C   THR A 575    11142  10373  10241    651   2828    888       C  
ATOM   4181  O   THR A 575     154.359  55.130  24.863  1.00 72.44           O  
ANISOU 4181  O   THR A 575    10001   8775   8749    640   2802    938       O  
ATOM   4182  CB  THR A 575     154.151  57.410  27.110  1.00 72.44           C  
ANISOU 4182  CB  THR A 575     9878   8869   8775    715   2370   1136       C  
ATOM   4183  OG1 THR A 575     155.249  58.329  27.049  1.00 63.79           O  
ANISOU 4183  OG1 THR A 575     8761   7905   7572    416   2522   1016       O  
ATOM   4184  CG2 THR A 575     153.345  57.663  28.380  1.00 63.24           C  
ANISOU 4184  CG2 THR A 575     8604   7693   7732    987   2090   1279       C  
ATOM   4185  N   THR A 576     156.434  55.842  25.383  1.00 90.10           N  
ANISOU 4185  N   THR A 576    11795  11402  11038    428   3095    677       N  
ATOM   4186  CA  THR A 576     156.952  55.557  24.049  1.00 89.51           C  
ANISOU 4186  CA  THR A 576    11872  11326  10814    136   3395    496       C  
ATOM   4187  C   THR A 576     157.034  54.056  23.789  1.00 91.38           C  
ANISOU 4187  C   THR A 576    11910  11582  11227    403   3519    402       C  
ATOM   4188  O   THR A 576     156.646  53.588  22.712  1.00 89.23           O  
ANISOU 4188  O   THR A 576    11920  11155  10829    283   3620    383       O  
ATOM   4189  CB  THR A 576     158.323  56.212  23.868  1.00 81.31           C  
ANISOU 4189  CB  THR A 576    10650  10546   9700   -210   3682    240       C  
ATOM   4190  OG1 THR A 576     158.188  57.636  23.945  1.00 77.41           O  
ANISOU 4190  OG1 THR A 576    10471   9962   8980   -525   3582    334       O  
ATOM   4191  CG2 THR A 576     158.923  55.843  22.524  1.00 85.56           C  
ANISOU 4191  CG2 THR A 576    11304  11121  10083   -532   4045      5       C  
ATOM   4192  N   VAL A 577     157.528  53.283  24.760  1.00 91.29           N  
ANISOU 4192  N   VAL A 577    11458  11736  11490    774   3494    343       N  
ATOM   4193  CA  VAL A 577     157.657  51.845  24.544  1.00 84.48           C  
ANISOU 4193  CA  VAL A 577    10458  10852  10787   1055   3595    246       C  
ATOM   4194  C   VAL A 577     156.287  51.181  24.466  1.00 80.05           C  
ANISOU 4194  C   VAL A 577    10203   9997  10214   1213   3409    475       C  
ATOM   4195  O   VAL A 577     156.117  50.180  23.760  1.00 83.35           O  
ANISOU 4195  O   VAL A 577    10728  10301  10641   1269   3526    411       O  
ATOM   4196  CB  VAL A 577     158.533  51.201  25.637  1.00 80.59           C  
ANISOU 4196  CB  VAL A 577     9480  10572  10566   1450   3559    126       C  
ATOM   4197  CG1 VAL A 577     159.949  51.753  25.582  1.00 72.81           C  
ANISOU 4197  CG1 VAL A 577     8122   9935   9608   1279   3772   -185       C  
ATOM   4198  CG2 VAL A 577     157.928  51.419  27.010  1.00 98.30           C  
ANISOU 4198  CG2 VAL A 577    11684  12766  12900   1705   3238    373       C  
ATOM   4199  N   LEU A 578     155.290  51.720  25.173  1.00 80.25           N  
ANISOU 4199  N   LEU A 578    10361   9912  10218   1272   3130    712       N  
ATOM   4200  CA  LEU A 578     153.952  51.141  25.118  1.00 92.56           C  
ANISOU 4200  CA  LEU A 578    12162  11242  11765   1381   2965    880       C  
ATOM   4201  C   LEU A 578     153.320  51.312  23.742  1.00 98.08           C  
ANISOU 4201  C   LEU A 578    13250  11775  12243   1099   3007    873       C  
ATOM   4202  O   LEU A 578     152.566  50.440  23.295  1.00 91.59           O  
ANISOU 4202  O   LEU A 578    12583  10800  11417   1157   2993    899       O  
ATOM   4203  CB  LEU A 578     153.063  51.764  26.196  1.00 82.07           C  
ANISOU 4203  CB  LEU A 578    10835   9882  10464   1489   2677   1075       C  
ATOM   4204  CG  LEU A 578     153.389  51.416  27.650  1.00 75.60           C  
ANISOU 4204  CG  LEU A 578     9715   9173   9837   1791   2587   1125       C  
ATOM   4205  CD1 LEU A 578     152.570  52.272  28.600  1.00 80.76           C  
ANISOU 4205  CD1 LEU A 578    10389   9822  10475   1816   2341   1281       C  
ATOM   4206  CD2 LEU A 578     153.142  49.944  27.914  1.00 72.68           C  
ANISOU 4206  CD2 LEU A 578     9336   8692   9586   2044   2614   1143       C  
ATOM   4207  N   MET A 579     153.609  52.422  23.058  1.00 99.52           N  
ANISOU 4207  N   MET A 579    13630  11968  12214    777   3052    834       N  
ATOM   4208  CA  MET A 579     153.110  52.606  21.700  1.00105.77           C  
ANISOU 4208  CA  MET A 579    14853  12585  12748    499   3080    822       C  
ATOM   4209  C   MET A 579     153.877  51.762  20.691  1.00105.69           C  
ANISOU 4209  C   MET A 579    14847  12609  12700    368   3419    617       C  
ATOM   4210  O   MET A 579     153.326  51.403  19.645  1.00105.63           O  
ANISOU 4210  O   MET A 579    15163  12440  12531    232   3444    606       O  
ATOM   4211  CB  MET A 579     153.168  54.082  21.306  1.00 91.34           C  
ANISOU 4211  CB  MET A 579    13341  10706  10659    182   3002    859       C  
ATOM   4212  CG  MET A 579     152.018  54.909  21.851  1.00 70.39           C  
ANISOU 4212  CG  MET A 579    10859   7918   7967    296   2612   1049       C  
ATOM   4213  SD  MET A 579     151.945  56.537  21.093  1.00 52.70           S  
ANISOU 4213  SD  MET A 579     9178   5496   5348    -66   2478   1094       S  
ATOM   4214  CE  MET A 579     153.556  57.165  21.543  1.00 51.42           C  
ANISOU 4214  CE  MET A 579     8774   5567   5196   -307   2786    963       C  
ATOM   4215  N   PHE A 580     155.141  51.440  20.979  1.00 94.56           N  
ANISOU 4215  N   PHE A 580    13071  11422  11436    418   3671    425       N  
ATOM   4216  CA  PHE A 580     155.875  50.496  20.145  1.00 87.56           C  
ANISOU 4216  CA  PHE A 580    12111  10592  10567    374   3995    183       C  
ATOM   4217  C   PHE A 580     155.254  49.104  20.184  1.00 96.81           C  
ANISOU 4217  C   PHE A 580    13284  11611  11888    685   3945    222       C  
ATOM   4218  O   PHE A 580     155.434  48.327  19.239  1.00110.03           O  
ANISOU 4218  O   PHE A 580    15069  13228  13509    613   4160     67       O  
ATOM   4219  CB  PHE A 580     157.340  50.443  20.586  1.00 81.64           C  
ANISOU 4219  CB  PHE A 580    10885  10152   9984    434   4229    -76       C  
ATOM   4220  CG  PHE A 580     158.081  49.225  20.108  1.00 90.24           C  
ANISOU 4220  CG  PHE A 580    11760  11323  11206    584   4501   -351       C  
ATOM   4221  CD1 PHE A 580     158.549  49.144  18.807  1.00 97.03           C  
ANISOU 4221  CD1 PHE A 580    12767  12214  11886    238   4748   -577       C  
ATOM   4222  CD2 PHE A 580     158.315  48.161  20.965  1.00 97.34           C  
ANISOU 4222  CD2 PHE A 580    12336  12252  12398   1068   4403   -385       C  
ATOM   4223  CE1 PHE A 580     159.232  48.025  18.368  1.00104.14           C  
ANISOU 4223  CE1 PHE A 580    13449  13200  12920    388   4876   -841       C  
ATOM   4224  CE2 PHE A 580     158.998  47.040  20.533  1.00 98.63           C  
ANISOU 4224  CE2 PHE A 580    12327  12470  12678   1224   4497   -642       C  
ATOM   4225  CZ  PHE A 580     159.456  46.973  19.233  1.00105.18           C  
ANISOU 4225  CZ  PHE A 580    13258  13356  13348    896   4750   -878       C  
ATOM   4226  N   LEU A 581     154.527  48.776  21.252  1.00 92.75           N  
ANISOU 4226  N   LEU A 581    12678  11024  11539    995   3684    414       N  
ATOM   4227  CA  LEU A 581     153.822  47.504  21.354  1.00 92.79           C  
ANISOU 4227  CA  LEU A 581    12755  10851  11649   1232   3629    469       C  
ATOM   4228  C   LEU A 581     152.409  47.587  20.788  1.00 98.10           C  
ANISOU 4228  C   LEU A 581    13796  11321  12156   1075   3455    615       C  
ATOM   4229  O   LEU A 581     151.955  46.652  20.119  1.00 87.78           O  
ANISOU 4229  O   LEU A 581    12672   9865  10814   1061   3525    571       O  
ATOM   4230  CB  LEU A 581     153.767  47.047  22.815  1.00 94.84           C  
ANISOU 4230  CB  LEU A 581    12770  11129  12136   1603   3461    581       C  
ATOM   4231  CG  LEU A 581     155.063  47.048  23.629  1.00 84.20           C  
ANISOU 4231  CG  LEU A 581    11027   9997  10967   1832   3524    456       C  
ATOM   4232  CD1 LEU A 581     154.746  46.944  25.108  1.00 78.37           C  
ANISOU 4232  CD1 LEU A 581    10162   9249  10368   2125   3278    635       C  
ATOM   4233  CD2 LEU A 581     155.985  45.918  23.204  1.00 78.27           C  
ANISOU 4233  CD2 LEU A 581    10145   9262  10330   2023   3746    209       C  
ATOM   4234  N   ALA A 582     151.702  48.690  21.054  1.00 99.51           N  
ANISOU 4234  N   ALA A 582    14078  11495  12235    972   3211    765       N  
ATOM   4235  CA  ALA A 582     150.386  48.890  20.454  1.00106.64           C  
ANISOU 4235  CA  ALA A 582    15299  12241  12977    844   3004    854       C  
ATOM   4236  C   ALA A 582     150.490  48.969  18.936  1.00102.65           C  
ANISOU 4236  C   ALA A 582    15139  11646  12218    545   3136    749       C  
ATOM   4237  O   ALA A 582     149.721  48.326  18.212  1.00 87.18           O  
ANISOU 4237  O   ALA A 582    13399   9552  10175    490   3102    729       O  
ATOM   4238  CB  ALA A 582     149.737  50.153  21.019  1.00101.46           C  
ANISOU 4238  CB  ALA A 582    14677  11606  12268    835   2702    991       C  
ATOM   4239  N   PHE A 583     151.433  49.764  18.440  1.00102.85           N  
ANISOU 4239  N   PHE A 583    13925  12275  12878    -62    -83   -187       N  
ATOM   4240  CA  PHE A 583     151.798  49.763  17.035  1.00 97.51           C  
ANISOU 4240  CA  PHE A 583    13242  11691  12117    -68    -75   -267       C  
ATOM   4241  C   PHE A 583     152.898  48.725  16.846  1.00 98.53           C  
ANISOU 4241  C   PHE A 583    13497  11786  12154    216     80   -252       C  
ATOM   4242  O   PHE A 583     153.152  47.892  17.719  1.00111.71           O  
ANISOU 4242  O   PHE A 583    15321  13305  13820    412    186   -196       O  
ATOM   4243  CB  PHE A 583     152.233  51.158  16.589  1.00 90.27           C  
ANISOU 4243  CB  PHE A 583    12096  11041  11160   -141   -209   -206       C  
ATOM   4244  CG  PHE A 583     151.340  52.263  17.082  1.00 80.51           C  
ANISOU 4244  CG  PHE A 583    10769   9830   9992   -317   -354   -178       C  
ATOM   4245  CD1 PHE A 583     149.959  52.116  17.102  1.00 95.42           C  
ANISOU 4245  CD1 PHE A 583    12719  11600  11936   -458   -398   -279       C  
ATOM   4246  CD2 PHE A 583     151.888  53.453  17.526  1.00 76.08           C  
ANISOU 4246  CD2 PHE A 583    10061   9428   9419   -345   -435    -70       C  
ATOM   4247  CE1 PHE A 583     149.150  53.137  17.559  1.00 90.48           C  
ANISOU 4247  CE1 PHE A 583    12002  11028  11347   -556   -530   -258       C  
ATOM   4248  CE2 PHE A 583     151.086  54.475  17.980  1.00 76.00           C  
ANISOU 4248  CE2 PHE A 583    10020   9408   9450   -466   -555    -46       C  
ATOM   4249  CZ  PHE A 583     149.718  54.317  17.999  1.00 88.71           C  
ANISOU 4249  CZ  PHE A 583    11684  10911  11109   -539   -607   -132       C  
ATOM   4250  N   GLY A 584     153.563  48.751  15.707  1.00 91.44           N  
ANISOU 4250  N   GLY A 584    12556  11031  11156    276    104   -298       N  
ATOM   4251  CA  GLY A 584     154.611  47.782  15.490  1.00 91.92           C  
ANISOU 4251  CA  GLY A 584    12724  11095  11107    593    254   -296       C  
ATOM   4252  C   GLY A 584     155.886  48.484  15.092  1.00 99.22           C  
ANISOU 4252  C   GLY A 584    13362  12410  11928    710    225   -236       C  
ATOM   4253  O   GLY A 584     156.864  47.848  14.699  1.00 93.45           O  
ANISOU 4253  O   GLY A 584    12641  11794  11072    989    337   -250       O  
ATOM   4254  N   SER A 585     155.871  49.803  15.201  1.00100.91           N  
ANISOU 4254  N   SER A 585    13334  12831  12177    490     92   -180       N  
ATOM   4255  CA  SER A 585     156.937  50.649  14.702  1.00 99.04           C  
ANISOU 4255  CA  SER A 585    12838  12957  11837    464     84   -150       C  
ATOM   4256  C   SER A 585     157.716  51.267  15.846  1.00 91.73           C  
ANISOU 4256  C   SER A 585    11652  12292  10907    505     34    -56       C  
ATOM   4257  O   SER A 585     157.254  51.327  16.991  1.00 82.75           O  
ANISOU 4257  O   SER A 585    10537  11042   9863    505    -32      0       O  
ATOM   4258  CB  SER A 585     156.380  51.763  13.817  1.00 93.30           C  
ANISOU 4258  CB  SER A 585    12097  12248  11105    149      1   -167       C  
ATOM   4259  OG  SER A 585     157.422  52.650  13.465  1.00 92.29           O  
ANISOU 4259  OG  SER A 585    11755  12442  10870     64     26   -129       O  
ATOM   4260  N   VAL A 586     158.905  51.755  15.496  1.00 96.92           N  
ANISOU 4260  N   VAL A 586    12049  13335  11440    510     74    -60       N  
ATOM   4261  CA  VAL A 586     159.745  52.481  16.432  1.00 89.12           C  
ANISOU 4261  CA  VAL A 586    10758  12689  10413    473     29    -17       C  
ATOM   4262  C   VAL A 586     159.727  53.994  16.186  1.00 97.96           C  
ANISOU 4262  C   VAL A 586    11772  13913  11533     50    -23     -9       C  
ATOM   4263  O   VAL A 586     159.816  54.763  17.152  1.00 91.07           O  
ANISOU 4263  O   VAL A 586    10774  13137  10693    -96    -98     21       O  
ATOM   4264  CB  VAL A 586     161.200  51.935  16.428  1.00 90.00           C  
ANISOU 4264  CB  VAL A 586    10598  13249  10349    781    124    -54       C  
ATOM   4265  CG1 VAL A 586     162.223  53.065  16.524  1.00 90.63           C  
ANISOU 4265  CG1 VAL A 586    10290  13818  10326    531    120    -88       C  
ATOM   4266  CG2 VAL A 586     161.400  50.961  17.554  1.00 88.16           C  
ANISOU 4266  CG2 VAL A 586    10390  13012  10094   1200    116    -10       C  
ATOM   4267  N   VAL A 587     159.548  54.447  14.941  1.00104.28           N  
ANISOU 4267  N   VAL A 587    12676  14658  12286   -145     23    -34       N  
ATOM   4268  CA  VAL A 587     159.563  55.880  14.653  1.00102.33           C  
ANISOU 4268  CA  VAL A 587    12422  14458  12002   -525     11    -10       C  
ATOM   4269  C   VAL A 587     158.207  56.515  14.944  1.00 86.94           C  
ANISOU 4269  C   VAL A 587    10724  12138  10172   -668   -116     43       C  
ATOM   4270  O   VAL A 587     158.141  57.702  15.272  1.00 88.59           O  
ANISOU 4270  O   VAL A 587    10958  12331  10373   -923   -150     80       O  
ATOM   4271  CB  VAL A 587     160.001  56.119  13.193  1.00 92.47           C  
ANISOU 4271  CB  VAL A 587    11211  13317  10605   -643    133    -42       C  
ATOM   4272  CG1 VAL A 587     158.963  55.608  12.251  1.00 92.98           C  
ANISOU 4272  CG1 VAL A 587    11565  13068  10693   -548    105    -53       C  
ATOM   4273  CG2 VAL A 587     160.294  57.619  12.899  1.00 92.74           C  
ANISOU 4273  CG2 VAL A 587    11269  13422  10547  -1052    183    -10       C  
ATOM   4274  N   LEU A 588     157.114  55.757  14.804  1.00 77.59           N  
ANISOU 4274  N   LEU A 588     9732  10669   9080   -516   -175     31       N  
ATOM   4275  CA  LEU A 588     155.791  56.275  15.146  1.00 78.74           C  
ANISOU 4275  CA  LEU A 588    10054  10540   9324   -609   -301     58       C  
ATOM   4276  C   LEU A 588     155.666  56.673  16.616  1.00 80.77           C  
ANISOU 4276  C   LEU A 588    10231  10782   9678   -638   -377    105       C  
ATOM   4277  O   LEU A 588     155.098  57.746  16.887  1.00 64.91           O  
ANISOU 4277  O   LEU A 588     8313   8666   7683   -801   -452    141       O  
ATOM   4278  CB  LEU A 588     154.723  55.241  14.759  1.00 70.68           C  
ANISOU 4278  CB  LEU A 588     9190   9300   8366   -472   -328     -9       C  
ATOM   4279  CG  LEU A 588     154.281  55.201  13.293  1.00 84.15           C  
ANISOU 4279  CG  LEU A 588    11039  10961   9971   -503   -319    -71       C  
ATOM   4280  CD1 LEU A 588     153.358  54.015  13.032  1.00 79.14           C  
ANISOU 4280  CD1 LEU A 588    10522  10157   9390   -405   -325   -186       C  
ATOM   4281  CD2 LEU A 588     153.606  56.504  12.886  1.00 78.25           C  
ANISOU 4281  CD2 LEU A 588    10409  10163   9160   -654   -413    -24       C  
ATOM   4282  N   PRO A 589     156.148  55.894  17.594  1.00 84.76           N  
ANISOU 4282  N   PRO A 589    10599  11381  10226   -460   -360    108       N  
ATOM   4283  CA  PRO A 589     156.114  56.390  18.979  1.00 90.47           C  
ANISOU 4283  CA  PRO A 589    11238  12131  11006   -500   -434    150       C  
ATOM   4284  C   PRO A 589     156.965  57.628  19.200  1.00 91.62           C  
ANISOU 4284  C   PRO A 589    11239  12505  11066   -743   -431    151       C  
ATOM   4285  O   PRO A 589     156.587  58.492  20.002  1.00 83.30           O  
ANISOU 4285  O   PRO A 589    10226  11375  10050   -887   -504    172       O  
ATOM   4286  CB  PRO A 589     156.632  55.195  19.792  1.00 90.21           C  
ANISOU 4286  CB  PRO A 589    11107  12194  10975   -202   -396    157       C  
ATOM   4287  CG  PRO A 589     156.348  54.012  18.949  1.00 86.14           C  
ANISOU 4287  CG  PRO A 589    10748  11519  10461    -23   -314    122       C  
ATOM   4288  CD  PRO A 589     156.570  54.480  17.545  1.00 86.52           C  
ANISOU 4288  CD  PRO A 589    10804  11637  10434   -173   -276     79       C  
ATOM   4289  N   ILE A 590     158.106  57.740  18.514  1.00 93.48           N  
ANISOU 4289  N   ILE A 590    11316  13025  11175   -815   -332    113       N  
ATOM   4290  CA  ILE A 590     158.947  58.925  18.659  1.00 86.36           C  
ANISOU 4290  CA  ILE A 590    10284  12356  10173  -1133   -291     82       C  
ATOM   4291  C   ILE A 590     158.297  60.130  17.994  1.00 82.24           C  
ANISOU 4291  C   ILE A 590    10056  11562   9629  -1419   -282    118       C  
ATOM   4292  O   ILE A 590     158.446  61.265  18.465  1.00 81.46           O  
ANISOU 4292  O   ILE A 590    10011  11450   9491  -1697   -277    112       O  
ATOM   4293  CB  ILE A 590     160.353  58.646  18.094  1.00 84.01           C  
ANISOU 4293  CB  ILE A 590     9699  12495   9726  -1143   -163     11       C  
ATOM   4294  CG1 ILE A 590     161.064  57.599  18.954  1.00 88.90           C  
ANISOU 4294  CG1 ILE A 590    10025  13430  10322   -801   -187    -21       C  
ATOM   4295  CG2 ILE A 590     161.177  59.924  18.018  1.00 71.89           C  
ANISOU 4295  CG2 ILE A 590     8057  11190   8065  -1580    -76    -49       C  
ATOM   4296  CD1 ILE A 590     162.474  57.292  18.506  1.00 96.35           C  
ANISOU 4296  CD1 ILE A 590    10622  14896  11091   -742    -72   -111       C  
ATOM   4297  N   LYS A 591     157.565  59.912  16.901  1.00 88.56           N  
ANISOU 4297  N   LYS A 591    11079  12140  10429  -1339   -277    150       N  
ATOM   4298  CA  LYS A 591     156.786  60.989  16.302  1.00 89.25           C  
ANISOU 4298  CA  LYS A 591    11491  11953  10466  -1501   -292    202       C  
ATOM   4299  C   LYS A 591     155.766  61.529  17.297  1.00 94.36           C  
ANISOU 4299  C   LYS A 591    12279  12362  11211  -1479   -422    236       C  
ATOM   4300  O   LYS A 591     155.751  62.726  17.603  1.00 93.78           O  
ANISOU 4300  O   LYS A 591    12373  12181  11080  -1689   -409    259       O  
ATOM   4301  CB  LYS A 591     156.093  60.491  15.031  1.00 73.35           C  
ANISOU 4301  CB  LYS A 591     9649   9804   8417  -1346   -298    212       C  
ATOM   4302  CG  LYS A 591     155.293  61.557  14.302  1.00 69.16           C  
ANISOU 4302  CG  LYS A 591     9466   9030   7780  -1425   -322    275       C  
ATOM   4303  CD  LYS A 591     154.496  60.960  13.154  1.00 74.84           C  
ANISOU 4303  CD  LYS A 591    10307   9676   8453  -1229   -368    258       C  
ATOM   4304  CE  LYS A 591     153.403  60.036  13.660  1.00 75.46           C  
ANISOU 4304  CE  LYS A 591    10310   9676   8685  -1011   -508    200       C  
ATOM   4305  NZ  LYS A 591     152.371  60.761  14.444  1.00 84.79           N  
ANISOU 4305  NZ  LYS A 591    11604  10693   9919   -982   -633    232       N  
ATOM   4306  N   ALA A 592     154.924  60.642  17.836  1.00 98.60           N  
ANISOU 4306  N   ALA A 592    12768  12813  11883  -1238   -526    228       N  
ATOM   4307  CA  ALA A 592     153.867  61.062  18.752  1.00104.51           C  
ANISOU 4307  CA  ALA A 592    13624  13368  12717  -1192   -641    249       C  
ATOM   4308  C   ALA A 592     154.428  61.779  19.973  1.00 89.17           C  
ANISOU 4308  C   ALA A 592    11604  11498  10778  -1345   -644    247       C  
ATOM   4309  O   ALA A 592     153.827  62.742  20.466  1.00 69.74           O  
ANISOU 4309  O   ALA A 592     9325   8863   8312  -1416   -696    267       O  
ATOM   4310  CB  ALA A 592     153.042  59.852  19.184  1.00 97.47           C  
ANISOU 4310  CB  ALA A 592    12655  12421  11957   -964   -705    223       C  
ATOM   4311  N   ALA A 593     155.575  61.319  20.482  1.00 75.83           N  
ANISOU 4311  N   ALA A 593     9645  10091   9077  -1374   -594    209       N  
ATOM   4312  CA  ALA A 593     156.191  61.978  21.629  1.00 84.41           C  
ANISOU 4312  CA  ALA A 593    10616  11321  10137  -1540   -605    174       C  
ATOM   4313  C   ALA A 593     156.509  63.435  21.320  1.00 84.27           C  
ANISOU 4313  C   ALA A 593    10792  11227  10001  -1895   -532    156       C  
ATOM   4314  O   ALA A 593     156.287  64.318  22.157  1.00 86.21           O  
ANISOU 4314  O   ALA A 593    11157  11360  10237  -2036   -565    139       O  
ATOM   4315  CB  ALA A 593     157.454  61.229  22.051  1.00 84.34           C  
ANISOU 4315  CB  ALA A 593    10245  11721  10081  -1478   -566    117       C  
ATOM   4316  N   LEU A 594     157.027  63.706  20.119  1.00 90.17           N  
ANISOU 4316  N   LEU A 594    11614  12009  10640  -2052   -412    158       N  
ATOM   4317  CA  LEU A 594     157.288  65.085  19.721  1.00 88.23           C  
ANISOU 4317  CA  LEU A 594    11648  11620  10254  -2410   -298    155       C  
ATOM   4318  C   LEU A 594     155.991  65.868  19.569  1.00 81.49           C  
ANISOU 4318  C   LEU A 594    11238  10326   9399  -2317   -360    241       C  
ATOM   4319  O   LEU A 594     155.895  67.017  20.016  1.00 73.75           O  
ANISOU 4319  O   LEU A 594    10528   9147   8348  -2521   -325    236       O  
ATOM   4320  CB  LEU A 594     158.087  65.112  18.419  1.00 79.05           C  
ANISOU 4320  CB  LEU A 594    10488  10591   8958  -2580   -134    151       C  
ATOM   4321  CG  LEU A 594     159.447  64.412  18.438  1.00 77.75           C  
ANISOU 4321  CG  LEU A 594     9864  10927   8751  -2656    -52     49       C  
ATOM   4322  CD1 LEU A 594     160.074  64.426  17.053  1.00 89.39           C  
ANISOU 4322  CD1 LEU A 594    11369  12510  10086  -2794    120     51       C  
ATOM   4323  CD2 LEU A 594     160.374  65.066  19.450  1.00 75.23           C  
ANISOU 4323  CD2 LEU A 594     9335  10883   8367  -2996     -7    -74       C  
ATOM   4324  N   MET A 595     154.980  65.261  18.944  1.00 77.00           N  
ANISOU 4324  N   MET A 595    10750   9621   8884  -1999   -451    304       N  
ATOM   4325  CA  MET A 595     153.689  65.919  18.801  1.00 89.64           C  
ANISOU 4325  CA  MET A 595    12706  10895  10458  -1830   -534    370       C  
ATOM   4326  C   MET A 595     152.966  66.058  20.135  1.00 91.99           C  
ANISOU 4326  C   MET A 595    12978  11110  10864  -1717   -654    350       C  
ATOM   4327  O   MET A 595     152.125  66.952  20.280  1.00 85.65           O  
ANISOU 4327  O   MET A 595    12489  10054  10000  -1636   -695    386       O  
ATOM   4328  CB  MET A 595     152.823  65.149  17.803  1.00 97.09           C  
ANISOU 4328  CB  MET A 595    13659  11820  11413  -1537   -610    398       C  
ATOM   4329  CG  MET A 595     153.605  64.600  16.621  1.00 83.73           C  
ANISOU 4329  CG  MET A 595    11882  10287   9647  -1602   -504    394       C  
ATOM   4330  SD  MET A 595     153.288  65.427  15.060  1.00 70.83           S  
ANISOU 4330  SD  MET A 595    10677   8463   7774  -1589   -434    479       S  
ATOM   4331  CE  MET A 595     151.584  64.962  14.811  1.00 78.47           C  
ANISOU 4331  CE  MET A 595    11688   9351   8775  -1174   -645    473       C  
ATOM   4332  N   SER A 596     153.273  65.198  21.110  1.00 95.74           N  
ANISOU 4332  N   SER A 596    13107  11796  11473  -1676   -704    298       N  
ATOM   4333  CA  SER A 596     152.707  65.352  22.445  1.00 78.41           C  
ANISOU 4333  CA  SER A 596    10887   9547   9360  -1598   -796    278       C  
ATOM   4334  C   SER A 596     153.461  66.393  23.264  1.00 83.28           C  
ANISOU 4334  C   SER A 596    11579  10164   9899  -1892   -738    227       C  
ATOM   4335  O   SER A 596     152.855  67.075  24.098  1.00 71.68           O  
ANISOU 4335  O   SER A 596    10281   8527   8429  -1866   -789    218       O  
ATOM   4336  CB  SER A 596     152.700  64.010  23.178  1.00 70.15           C  
ANISOU 4336  CB  SER A 596     9503   8698   8454  -1419   -856    256       C  
ATOM   4337  OG  SER A 596     151.853  63.078  22.525  1.00 87.38           O  
ANISOU 4337  OG  SER A 596    11661  10835  10706  -1194   -895    274       O  
ATOM   4338  N   ALA A 597     154.772  66.530  23.045  1.00 80.13           N  
ANISOU 4338  N   ALA A 597    11047   9978   9420  -2185   -625    171       N  
ATOM   4339  CA  ALA A 597     155.525  67.586  23.714  1.00 72.91           C  
ANISOU 4339  CA  ALA A 597    10213   9086   8403  -2552   -547     83       C  
ATOM   4340  C   ALA A 597     155.155  68.959  23.166  1.00 89.46           C  
ANISOU 4340  C   ALA A 597    12843  10785  10362  -2731   -447    118       C  
ATOM   4341  O   ALA A 597     155.038  69.927  23.927  1.00 87.59           O  
ANISOU 4341  O   ALA A 597    12852  10363  10065  -2890   -427     69       O  
ATOM   4342  CB  ALA A 597     157.026  67.336  23.571  1.00 67.79           C  
ANISOU 4342  CB  ALA A 597     9226   8850   7681  -2840   -442    -17       C  
ATOM   4343  N   LEU A 598     154.973  69.063  21.846  1.00106.53           N  
ANISOU 4343  N   LEU A 598    15231  12797  12447  -2688   -374    205       N  
ATOM   4344  CA  LEU A 598     154.538  70.325  21.254  1.00104.00           C  
ANISOU 4344  CA  LEU A 598    15495  12060  11959  -2770   -272    272       C  
ATOM   4345  C   LEU A 598     153.155  70.717  21.755  1.00100.74           C  
ANISOU 4345  C   LEU A 598    15356  11351  11568  -2412   -408    328       C  
ATOM   4346  O   LEU A 598     152.918  71.881  22.102  1.00108.46           O  
ANISOU 4346  O   LEU A 598    16776  12009  12425  -2502   -343    327       O  
ATOM   4347  CB  LEU A 598     154.546  70.222  19.728  1.00103.40           C  
ANISOU 4347  CB  LEU A 598    15589  11921  11776  -2713   -187    367       C  
ATOM   4348  CG  LEU A 598     155.709  70.877  18.978  1.00102.89           C  
ANISOU 4348  CG  LEU A 598    15702  11859  11533  -3178     62    346       C  
ATOM   4349  CD1 LEU A 598     157.042  70.280  19.400  1.00104.85           C  
ANISOU 4349  CD1 LEU A 598    15412  12585  11841  -3501    122    203       C  
ATOM   4350  CD2 LEU A 598     155.511  70.746  17.478  1.00105.97           C  
ANISOU 4350  CD2 LEU A 598    16300  12160  11803  -3036    127    462       C  
ATOM   4351  N   THR A 599     152.227  69.758  21.802  1.00 83.30           N  
ANISOU 4351  N   THR A 599    12900   9252   9497  -2011   -579    362       N  
ATOM   4352  CA  THR A 599     150.894  70.050  22.319  1.00 85.12           C  
ANISOU 4352  CA  THR A 599    13299   9298   9742  -1665   -708    389       C  
ATOM   4353  C   THR A 599     150.941  70.429  23.794  1.00 92.36           C  
ANISOU 4353  C   THR A 599    14180  10200  10713  -1761   -736    310       C  
ATOM   4354  O   THR A 599     150.143  71.257  24.248  1.00 87.76           O  
ANISOU 4354  O   THR A 599    13919   9369  10059  -1601   -765    318       O  
ATOM   4355  CB  THR A 599     149.971  68.848  22.111  1.00 78.74           C  
ANISOU 4355  CB  THR A 599    12168   8680   9070  -1308   -860    401       C  
ATOM   4356  OG1 THR A 599     150.135  68.340  20.781  1.00 73.72           O  
ANISOU 4356  OG1 THR A 599    11500   8121   8389  -1273   -831    442       O  
ATOM   4357  CG2 THR A 599     148.518  69.253  22.309  1.00 79.82           C  
ANISOU 4357  CG2 THR A 599    12489   8676   9164   -937   -977    421       C  
ATOM   4358  N   LEU A 600     151.873  69.847  24.552  1.00 98.23           N  
ANISOU 4358  N   LEU A 600    14543  11225  11554  -1988   -729    227       N  
ATOM   4359  CA  LEU A 600     151.982  70.158  25.974  1.00100.23           C  
ANISOU 4359  CA  LEU A 600    14735  11514  11836  -2083   -763    139       C  
ATOM   4360  C   LEU A 600     152.449  71.592  26.188  1.00104.22           C  
ANISOU 4360  C   LEU A 600    15670  11757  12171  -2420   -630     76       C  
ATOM   4361  O   LEU A 600     151.781  72.382  26.865  1.00112.89           O  
ANISOU 4361  O   LEU A 600    17076  12602  13215  -2325   -650     58       O  
ATOM   4362  CB  LEU A 600     152.938  69.173  26.651  1.00 92.87           C  
ANISOU 4362  CB  LEU A 600    13294  10992  10999  -2205   -792     66       C  
ATOM   4363  CG  LEU A 600     153.164  69.353  28.154  1.00 86.08           C  
ANISOU 4363  CG  LEU A 600    12307  10253  10145  -2290   -843    -34       C  
ATOM   4364  CD1 LEU A 600     151.880  69.080  28.925  1.00 82.84           C  
ANISOU 4364  CD1 LEU A 600    11919   9734   9825  -1927   -962     10       C  
ATOM   4365  CD2 LEU A 600     154.292  68.459  28.645  1.00 74.31           C  
ANISOU 4365  CD2 LEU A 600    10337   9216   8682  -2392   -861   -103       C  
ATOM   4366  N   GLY A 601     153.601  71.945  25.613  1.00 99.49           N  
ANISOU 4366  N   GLY A 601    15115  11216  11472  -2834   -473     29       N  
ATOM   4367  CA  GLY A 601     154.145  73.278  25.821  1.00 98.81           C  
ANISOU 4367  CA  GLY A 601    15455  10877  11210  -3256   -305    -60       C  
ATOM   4368  C   GLY A 601     153.245  74.374  25.284  1.00 96.80           C  
ANISOU 4368  C   GLY A 601    15895  10078  10806  -3091   -231     42       C  
ATOM   4369  O   GLY A 601     153.141  75.451  25.876  1.00 89.61           O  
ANISOU 4369  O   GLY A 601    15422   8851   9773  -3238   -149    -21       O  
ATOM   4370  N   SER A 602     152.582  74.115  24.154  1.00 98.63           N  
ANISOU 4370  N   SER A 602    16258  10198  11017  -2756   -259    194       N  
ATOM   4371  CA  SER A 602     151.645  75.090  23.610  1.00 89.94           C  
ANISOU 4371  CA  SER A 602    15810   8626   9738  -2477   -216    307       C  
ATOM   4372  C   SER A 602     150.414  75.240  24.495  1.00 89.90           C  
ANISOU 4372  C   SER A 602    15873   8513   9771  -2032   -377    309       C  
ATOM   4373  O   SER A 602     149.848  76.334  24.583  1.00 74.54           O  
ANISOU 4373  O   SER A 602    14516   6158   7649  -1882   -314    340       O  
ATOM   4374  CB  SER A 602     151.235  74.691  22.192  1.00 84.36           C  
ANISOU 4374  CB  SER A 602    15157   7920   8976  -2192   -235    452       C  
ATOM   4375  OG  SER A 602     152.356  74.684  21.325  1.00 88.82           O  
ANISOU 4375  OG  SER A 602    15731   8548   9467  -2602    -54    456       O  
ATOM   4376  N   THR A 603     149.989  74.161  25.156  1.00 95.82           N  
ANISOU 4376  N   THR A 603    16059   9617  10731  -1809   -565    274       N  
ATOM   4377  CA  THR A 603     148.835  74.241  26.045  1.00 95.47           C  
ANISOU 4377  CA  THR A 603    16020   9531  10723  -1418   -701    260       C  
ATOM   4378  C   THR A 603     149.179  74.958  27.347  1.00 86.94           C  
ANISOU 4378  C   THR A 603    15089   8333   9613  -1657   -650    138       C  
ATOM   4379  O   THR A 603     148.412  75.809  27.810  1.00 89.44           O  
ANISOU 4379  O   THR A 603    15805   8364   9815  -1424   -650    132       O  
ATOM   4380  CB  THR A 603     148.296  72.839  26.336  1.00 92.92           C  
ANISOU 4380  CB  THR A 603    15083   9607  10616  -1169   -876    256       C  
ATOM   4381  OG1 THR A 603     148.011  72.171  25.101  1.00 79.45           O  
ANISOU 4381  OG1 THR A 603    13250   8013   8923   -992   -915    338       O  
ATOM   4382  CG2 THR A 603     147.021  72.921  27.166  1.00 94.03           C  
ANISOU 4382  CG2 THR A 603    15215   9739  10774   -770   -995    236       C  
ATOM   4383  N   MET A 604     150.326  74.632  27.949  1.00 84.87           N  
ANISOU 4383  N   MET A 604    14507   8313   9428  -2096   -610     26       N  
ATOM   4384  CA  MET A 604     150.715  75.284  29.194  1.00 77.91           C  
ANISOU 4384  CA  MET A 604    13730   7375   8497  -2358   -571   -122       C  
ATOM   4385  C   MET A 604     151.140  76.732  28.984  1.00 94.83           C  
ANISOU 4385  C   MET A 604    16549   9068  10414  -2697   -361   -176       C  
ATOM   4386  O   MET A 604     151.067  77.527  29.928  1.00 94.39           O  
ANISOU 4386  O   MET A 604    16781   8814  10270  -2801   -321   -290       O  
ATOM   4387  CB  MET A 604     151.841  74.505  29.876  1.00 82.48           C  
ANISOU 4387  CB  MET A 604    13741   8416   9182  -2701   -603   -242       C  
ATOM   4388  CG  MET A 604     151.408  73.169  30.471  1.00 68.03           C  
ANISOU 4388  CG  MET A 604    11346   6960   7543  -2370   -786   -205       C  
ATOM   4389  SD  MET A 604     152.481  72.634  31.818  1.00 69.77           S  
ANISOU 4389  SD  MET A 604    11074   7639   7795  -2642   -840   -363       S  
ATOM   4390  CE  MET A 604     154.081  72.676  31.015  1.00 85.72           C  
ANISOU 4390  CE  MET A 604    12933   9899   9739  -3158   -705   -447       C  
ATOM   4391  N   GLY A 605     151.588  77.090  27.778  1.00103.33           N  
ANISOU 4391  N   GLY A 605    17921   9962  11379  -2888   -207   -104       N  
ATOM   4392  CA  GLY A 605     151.907  78.482  27.504  1.00 91.85           C  
ANISOU 4392  CA  GLY A 605    17218   8001   9681  -3205     33   -136       C  
ATOM   4393  C   GLY A 605     150.669  79.346  27.366  1.00 87.61           C  
ANISOU 4393  C   GLY A 605    17345   6958   8984  -2699     37    -23       C  
ATOM   4394  O   GLY A 605     150.670  80.516  27.759  1.00 78.78           O  
ANISOU 4394  O   GLY A 605    16869   5389   7677  -2848    195    -89       O  
ATOM   4395  N   ILE A 606     149.597  78.786  26.801  1.00 92.42           N  
ANISOU 4395  N   ILE A 606    17819   7652   9645  -2087   -129    134       N  
ATOM   4396  CA  ILE A 606     148.329  79.503  26.734  1.00 88.90           C  
ANISOU 4396  CA  ILE A 606    17895   6849   9033  -1499   -167    227       C  
ATOM   4397  C   ILE A 606     147.726  79.643  28.127  1.00 95.33           C  
ANISOU 4397  C   ILE A 606    18621   7699   9903  -1305   -272    113       C  
ATOM   4398  O   ILE A 606     147.195  80.701  28.484  1.00 84.10           O  
ANISOU 4398  O   ILE A 606    17814   5855   8284  -1094   -196    101       O  
ATOM   4399  CB  ILE A 606     147.364  78.792  25.768  1.00 93.71           C  
ANISOU 4399  CB  ILE A 606    18273   7663   9669   -922   -335    383       C  
ATOM   4400  CG1 ILE A 606     147.936  78.777  24.348  1.00 97.67           C  
ANISOU 4400  CG1 ILE A 606    18957   8086  10069  -1088   -214    500       C  
ATOM   4401  CG2 ILE A 606     146.003  79.462  25.781  1.00 97.25           C  
ANISOU 4401  CG2 ILE A 606    19151   7872   9929   -246   -407    454       C  
ATOM   4402  CD1 ILE A 606     147.148  77.914  23.384  1.00 89.50           C  
ANISOU 4402  CD1 ILE A 606    17589   7344   9072   -610   -391    614       C  
ATOM   4403  N   LEU A 607     147.807  78.582  28.936  1.00 99.95           N  
ANISOU 4403  N   LEU A 607    18476   8767  10732  -1356   -435     32       N  
ATOM   4404  CA  LEU A 607     147.292  78.645  30.301  1.00 82.07           C  
ANISOU 4404  CA  LEU A 607    16094   6574   8515  -1201   -525    -77       C  
ATOM   4405  C   LEU A 607     148.046  79.679  31.127  1.00 88.99           C  
ANISOU 4405  C   LEU A 607    17401   7153   9260  -1660   -362   -239       C  
ATOM   4406  O   LEU A 607     147.439  80.427  31.903  1.00 90.68           O  
ANISOU 4406  O   LEU A 607    17985   7110   9357  -1447   -348   -302       O  
ATOM   4407  CB  LEU A 607     147.372  77.267  30.957  1.00 68.42           C  
ANISOU 4407  CB  LEU A 607    13548   5402   7046  -1217   -695   -117       C  
ATOM   4408  CG  LEU A 607     146.402  76.220  30.408  1.00 68.96           C  
ANISOU 4408  CG  LEU A 607    13195   5763   7243   -752   -856     -3       C  
ATOM   4409  CD1 LEU A 607     146.722  74.848  30.972  1.00 64.51           C  
ANISOU 4409  CD1 LEU A 607    11924   5672   6915   -872   -963    -37       C  
ATOM   4410  CD2 LEU A 607     144.963  76.607  30.721  1.00 75.46           C  
ANISOU 4410  CD2 LEU A 607    14195   6498   7977   -179   -936     15       C  
ATOM   4411  N   THR A 608     149.372  79.733  30.980  1.00 93.72           N  
ANISOU 4411  N   THR A 608    17942   7808   9859  -2302   -231   -330       N  
ATOM   4412  CA  THR A 608     150.139  80.795  31.622  1.00 98.97           C  
ANISOU 4412  CA  THR A 608    19059   8181  10362  -2827    -44   -516       C  
ATOM   4413  C   THR A 608     149.738  82.160  31.082  1.00 92.75           C  
ANISOU 4413  C   THR A 608    19246   6695   9300  -2730    165   -459       C  
ATOM   4414  O   THR A 608     149.806  83.163  31.800  1.00 95.46           O  
ANISOU 4414  O   THR A 608    20034   6755   9481  -2879    297   -585       O  
ATOM   4415  CB  THR A 608     151.638  80.560  31.419  1.00102.02           C  
ANISOU 4415  CB  THR A 608    19143   8842  10777  -3550     67   -640       C  
ATOM   4416  OG1 THR A 608     151.983  79.240  31.858  1.00103.07           O  
ANISOU 4416  OG1 THR A 608    18406   9620  11135  -3533   -131   -666       O  
ATOM   4417  CG2 THR A 608     152.458  81.574  32.206  1.00 96.39           C  
ANISOU 4417  CG2 THR A 608    18796   7931   9897  -4169    250   -891       C  
ATOM   4418  N   TRP A 609     149.299  82.211  29.826  1.00108.18           N  
ANISOU 4418  N   TRP A 609    21475   8453  11177  -2411    200   -255       N  
ATOM   4419  CA  TRP A 609     148.890  83.458  29.198  1.00117.36           C  
ANISOU 4419  CA  TRP A 609    23428   9124  12039  -2170    397   -153       C  
ATOM   4420  C   TRP A 609     147.520  83.932  29.669  1.00108.83           C  
ANISOU 4420  C   TRP A 609    22684   7821  10844  -1444    297   -102       C  
ATOM   4421  O   TRP A 609     147.207  85.119  29.524  1.00 92.69           O  
ANISOU 4421  O   TRP A 609    21260   5442   8515  -1246    467    -69       O  
ATOM   4422  CB  TRP A 609     148.902  83.282  27.674  1.00109.61           C  
ANISOU 4422  CB  TRP A 609    22558   8102  10986  -2035    449     43       C  
ATOM   4423  CG  TRP A 609     148.602  84.520  26.895  1.00108.60           C  
ANISOU 4423  CG  TRP A 609    23166   7584  10514  -1791    661    144       C  
ATOM   4424  CD1 TRP A 609     149.428  85.587  26.704  1.00124.00           C  
ANISOU 4424  CD1 TRP A 609    25578   9303  12234  -2253    964     73       C  
ATOM   4425  CD2 TRP A 609     147.395  84.813  26.183  1.00109.04           C  
ANISOU 4425  CD2 TRP A 609    23576   7470  10384  -1016    588    318       C  
ATOM   4426  NE1 TRP A 609     148.807  86.533  25.925  1.00129.90           N  
ANISOU 4426  NE1 TRP A 609    27005   9691  12661  -1816   1094    200       N  
ATOM   4427  CE2 TRP A 609     147.557  86.082  25.592  1.00122.43           C  
ANISOU 4427  CE2 TRP A 609    25984   8802  11732  -1038    859    348       C  
ATOM   4428  CE3 TRP A 609     146.189  84.130  25.992  1.00 99.30           C  
ANISOU 4428  CE3 TRP A 609    22104   6403   9222   -297    321    435       C  
ATOM   4429  CZ2 TRP A 609     146.561  86.680  24.823  1.00120.65           C  
ANISOU 4429  CZ2 TRP A 609    26241   8378  11223   -344    862    488       C  
ATOM   4430  CZ3 TRP A 609     145.201  84.726  25.229  1.00105.33           C  
ANISOU 4430  CZ3 TRP A 609    23279   7034   9708    385    316    562       C  
ATOM   4431  CH2 TRP A 609     145.394  85.988  24.653  1.00 99.66           C  
ANISOU 4431  CH2 TRP A 609    23274   5952   8639    368    581    586       C  
ATOM   4432  N   MET A 610     146.706  83.044  30.243  1.00110.14           N  
ANISOU 4432  N   MET A 610    22388   8255  11204  -1029     35   -104       N  
ATOM   4433  CA  MET A 610     145.344  83.387  30.635  1.00118.68           C  
ANISOU 4433  CA  MET A 610    23686   9231  12176   -283    -73    -62       C  
ATOM   4434  C   MET A 610     145.077  83.305  32.132  1.00115.11           C  
ANISOU 4434  C   MET A 610    22962   8958  11815   -262   -163   -235       C  
ATOM   4435  O   MET A 610     144.180  84.001  32.615  1.00101.17           O  
ANISOU 4435  O   MET A 610    21612   6947   9882    223   -161   -252       O  
ATOM   4436  CB  MET A 610     144.332  82.493  29.896  1.00109.80           C  
ANISOU 4436  CB  MET A 610    22073   8510  11137    342   -294     93       C  
ATOM   4437  CG  MET A 610     144.520  81.004  30.083  1.00109.41           C  
ANISOU 4437  CG  MET A 610    21036   9115  11418    176   -484     66       C  
ATOM   4438  SD  MET A 610     143.711  80.073  28.768  1.00 74.41           S  
ANISOU 4438  SD  MET A 610    16195   5043   7036    668   -655    233       S  
ATOM   4439  CE  MET A 610     142.037  80.686  28.910  1.00 76.87           C  
ANISOU 4439  CE  MET A 610    16796   5292   7119   1562   -759    266       C  
ATOM   4440  N   PHE A 611     145.820  82.488  32.880  1.00106.92           N  
ANISOU 4440  N   PHE A 611    21262   8351  11013   -732   -240   -360       N  
ATOM   4441  CA  PHE A 611     145.628  82.408  34.323  1.00 98.13           C  
ANISOU 4441  CA  PHE A 611    19909   7417   9960   -730   -318   -521       C  
ATOM   4442  C   PHE A 611     146.707  83.130  35.119  1.00108.79           C  
ANISOU 4442  C   PHE A 611    21564   8550  11222  -1393   -157   -737       C  
ATOM   4443  O   PHE A 611     146.505  83.386  36.311  1.00125.30           O  
ANISOU 4443  O   PHE A 611    23672  10657  13279  -1368   -184   -887       O  
ATOM   4444  CB  PHE A 611     145.560  80.945  34.776  1.00 80.22           C  
ANISOU 4444  CB  PHE A 611    16689   5814   7977   -697   -531   -515       C  
ATOM   4445  CG  PHE A 611     144.249  80.283  34.471  1.00 86.68           C  
ANISOU 4445  CG  PHE A 611    17181   6888   8866    -32   -693   -385       C  
ATOM   4446  CD1 PHE A 611     143.169  80.441  35.321  1.00 88.61           C  
ANISOU 4446  CD1 PHE A 611    17417   7193   9058    442   -764   -431       C  
ATOM   4447  CD2 PHE A 611     144.093  79.512  33.332  1.00 92.38           C  
ANISOU 4447  CD2 PHE A 611    17591   7821   9687    102   -766   -241       C  
ATOM   4448  CE1 PHE A 611     141.958  79.840  35.044  1.00 92.17           C  
ANISOU 4448  CE1 PHE A 611    17520   7945   9554   1009   -901   -348       C  
ATOM   4449  CE2 PHE A 611     142.883  78.906  33.048  1.00100.55           C  
ANISOU 4449  CE2 PHE A 611    18300   9138  10767    661   -911   -163       C  
ATOM   4450  CZ  PHE A 611     141.814  79.071  33.907  1.00101.38           C  
ANISOU 4450  CZ  PHE A 611    18366   9336  10818   1101   -976   -222       C  
ATOM   4451  N   VAL A 612     147.835  83.461  34.498  1.00104.82           N  
ANISOU 4451  N   VAL A 612    21285   7878  10664  -2002     16   -775       N  
ATOM   4452  CA  VAL A 612     148.887  84.231  35.141  1.00103.21           C  
ANISOU 4452  CA  VAL A 612    21261   7607  10348  -2653    200   -977       C  
ATOM   4453  C   VAL A 612     148.917  85.669  34.637  1.00110.00           C  
ANISOU 4453  C   VAL A 612    22860   8015  10921  -2670    481   -910       C  
ATOM   4454  O   VAL A 612     149.044  86.604  35.430  1.00 97.75           O  
ANISOU 4454  O   VAL A 612    21647   6284   9211  -2827    614  -1039       O  
ATOM   4455  CB  VAL A 612     150.260  83.551  34.949  1.00 97.45           C  
ANISOU 4455  CB  VAL A 612    19974   7303   9751  -3342    210  -1075       C  
ATOM   4456  CG1 VAL A 612     151.359  84.378  35.591  1.00 91.32           C  
ANISOU 4456  CG1 VAL A 612    19257   6598   8841  -3975    406  -1284       C  
ATOM   4457  CG2 VAL A 612     150.239  82.150  35.530  1.00 92.69           C  
ANISOU 4457  CG2 VAL A 612    18512   7308   9398  -3226    -61  -1094       C  
ATOM   4458  N   ASP A 613     148.791  85.867  33.324  1.00106.50           N  
ANISOU 4458  N   ASP A 613    22700   7382  10382  -2502    578   -715       N  
ATOM   4459  CA  ASP A 613     148.771  87.207  32.752  1.00108.98           C  
ANISOU 4459  CA  ASP A 613    23771   7261  10376  -2473    848   -641       C  
ATOM   4460  C   ASP A 613     147.367  87.791  32.640  1.00104.92           C  
ANISOU 4460  C   ASP A 613    23763   6432   9669  -1647    809   -498       C  
ATOM   4461  O   ASP A 613     147.233  88.998  32.411  1.00107.92           O  
ANISOU 4461  O   ASP A 613    24836   6432   9738  -1558   1028   -460       O  
ATOM   4462  CB  ASP A 613     149.447  87.202  31.377  1.00113.52           C  
ANISOU 4462  CB  ASP A 613    24428   7817  10888  -2741    999   -527       C  
ATOM   4463  CG  ASP A 613     150.937  86.919  31.463  1.00112.75           C  
ANISOU 4463  CG  ASP A 613    23912   8035  10892  -3585   1106   -693       C  
ATOM   4464  OD1 ASP A 613     151.540  87.217  32.515  1.00115.96           O  
ANISOU 4464  OD1 ASP A 613    24202   8558  11299  -4018   1159   -905       O  
ATOM   4465  OD2 ASP A 613     151.506  86.400  30.480  1.00118.96           O  
ANISOU 4465  OD2 ASP A 613    24465   8992  11741  -3796   1136   -621       O  
ATOM   4466  N   GLY A 614     146.328  86.975  32.790  1.00120.64           N  
ANISOU 4466  N   GLY A 614    25424   8604  11810  -1036    545   -428       N  
ATOM   4467  CA  GLY A 614     144.976  87.473  32.940  1.00126.29           C  
ANISOU 4467  CA  GLY A 614    26482   9159  12346   -234    480   -344       C  
ATOM   4468  C   GLY A 614     144.123  87.539  31.694  1.00119.66           C  
ANISOU 4468  C   GLY A 614    25852   8269  11346    411    441   -131       C  
ATOM   4469  O   GLY A 614     142.998  88.044  31.770  1.00108.91           O  
ANISOU 4469  O   GLY A 614    24767   6833   9779   1108    396    -74       O  
ATOM   4470  N   HIS A 615     144.605  87.043  30.556  1.00126.91           N  
ANISOU 4470  N   HIS A 615    26619   9272  12330    222    450    -23       N  
ATOM   4471  CA  HIS A 615     143.841  87.135  29.317  1.00116.21           C  
ANISOU 4471  CA  HIS A 615    25464   7899  10793    821    415    164       C  
ATOM   4472  C   HIS A 615     142.671  86.160  29.323  1.00103.35           C  
ANISOU 4472  C   HIS A 615    23314   6639   9313   1504    107    221       C  
ATOM   4473  O   HIS A 615     142.821  84.995  28.948  1.00 92.23           O  
ANISOU 4473  O   HIS A 615    21357   5521   8166   1413    -57    265       O  
ATOM   4474  CB  HIS A 615     144.748  86.886  28.112  1.00113.51           C  
ANISOU 4474  CB  HIS A 615    25109   7549  10469    391    526    249       C  
ATOM   4475  CG  HIS A 615     145.820  87.919  27.949  1.00119.51           C  
ANISOU 4475  CG  HIS A 615    26403   7978  11026   -229    856    190       C  
ATOM   4476  ND1 HIS A 615     147.113  87.725  28.385  1.00120.60           N  
ANISOU 4476  ND1 HIS A 615    26292   8199  11331  -1068    968     47       N  
ATOM   4477  CD2 HIS A 615     145.787  89.164  27.416  1.00119.29           C  
ANISOU 4477  CD2 HIS A 615    27142   7564  10618   -130   1105    236       C  
ATOM   4478  CE1 HIS A 615     147.832  88.800  28.119  1.00118.98           C  
ANISOU 4478  CE1 HIS A 615    26651   7690  10866  -1479   1277      4       C  
ATOM   4479  NE2 HIS A 615     147.051  89.689  27.532  1.00124.79           N  
ANISOU 4479  NE2 HIS A 615    28046   8101  11267   -931   1373    124       N  
ATOM   4480  N   GLY A 616     141.498  86.634  29.738  1.00113.83           N  
ANISOU 4480  N   GLY A 616    24803   7990  10458   2190     34    216       N  
ATOM   4481  CA  GLY A 616     140.321  85.791  29.815  1.00 99.07           C  
ANISOU 4481  CA  GLY A 616    22402   6547   8694   2851   -242    237       C  
ATOM   4482  C   GLY A 616     139.704  85.761  31.199  1.00106.31           C  
ANISOU 4482  C   GLY A 616    23135   7579   9677   3081   -333     99       C  
ATOM   4483  O   GLY A 616     138.848  84.919  31.487  1.00 99.70           O  
ANISOU 4483  O   GLY A 616    21747   7151   8983   3513   -555     76       O  
ATOM   4484  N   SER A 617     140.134  86.684  32.066  1.00114.15           N  
ANISOU 4484  N   SER A 617    24577   8240  10555   2785   -154     -1       N  
ATOM   4485  CA  SER A 617     139.677  86.742  33.451  1.00110.37           C  
ANISOU 4485  CA  SER A 617    23981   7832  10123   2932   -210   -150       C  
ATOM   4486  C   SER A 617     138.363  87.491  33.630  1.00105.98           C  
ANISOU 4486  C   SER A 617    23676   7335   9256   3745   -232   -131       C  
ATOM   4487  O   SER A 617     137.556  87.106  34.483  1.00108.77           O  
ANISOU 4487  O   SER A 617    23660   7986   9682   4127   -372   -223       O  
ATOM   4488  CB  SER A 617     140.749  87.391  34.328  1.00 99.54           C  
ANISOU 4488  CB  SER A 617    22945   6124   8753   2223    -12   -285       C  
ATOM   4489  OG  SER A 617     141.144  88.654  33.821  1.00105.11           O  
ANISOU 4489  OG  SER A 617    24381   6412   9143   2072    242   -223       O  
ATOM   4490  N   GLY A 618     138.121  88.544  32.847  1.00111.09           N  
ANISOU 4490  N   GLY A 618    24938   7734   9537   4030    -88    -25       N  
ATOM   4491  CA  GLY A 618     136.869  89.268  32.972  1.00115.81           C  
ANISOU 4491  CA  GLY A 618    25782   8424   9797   4830   -111    -13       C  
ATOM   4492  C   GLY A 618     135.673  88.497  32.451  1.00126.46           C  
ANISOU 4492  C   GLY A 618    26537  10359  11153   5534   -356     15       C  
ATOM   4493  O   GLY A 618     134.544  88.729  32.889  1.00127.01           O  
ANISOU 4493  O   GLY A 618    26505  10711  11042   6174   -438    -37       O  
ATOM   4494  N   LEU A 619     135.893  87.576  31.513  1.00129.39           N  
ANISOU 4494  N   LEU A 619    26484  10961  11716   5414   -469     84       N  
ATOM   4495  CA  LEU A 619     134.772  86.829  30.952  1.00126.48           C  
ANISOU 4495  CA  LEU A 619    25509  11203  11344   6032   -697     90       C  
ATOM   4496  C   LEU A 619     134.460  85.599  31.795  1.00114.55           C  
ANISOU 4496  C   LEU A 619    23179  10153  10193   5999   -896    -15       C  
ATOM   4497  O   LEU A 619     133.298  85.343  32.135  1.00112.75           O  
ANISOU 4497  O   LEU A 619    22511  10432   9899   6557  -1033   -100       O  
ATOM   4498  CB  LEU A 619     135.079  86.430  29.506  1.00132.20           C  
ANISOU 4498  CB  LEU A 619    26167  11987  12076   5956   -727    211       C  
ATOM   4499  CG  LEU A 619     134.090  85.474  28.831  1.00132.08           C  
ANISOU 4499  CG  LEU A 619    25425  12652  12107   6444   -971    199       C  
ATOM   4500  CD1 LEU A 619     132.703  86.089  28.746  1.00133.79           C  
ANISOU 4500  CD1 LEU A 619    25668  13222  11943   7266  -1022    133       C  
ATOM   4501  CD2 LEU A 619     134.593  85.077  27.451  1.00128.63           C  
ANISOU 4501  CD2 LEU A 619    24970  12206  11699   6259   -983    318       C  
ATOM   4502  N   MET A 620     135.487  84.829  32.140  1.00112.55           N  
ANISOU 4502  N   MET A 620    22707   9756  10300   5341   -901    -25       N  
ATOM   4503  CA  MET A 620     135.308  83.604  32.906  1.00115.33           C  
ANISOU 4503  CA  MET A 620    22326  10504  10989   5267  -1072   -117       C  
ATOM   4504  C   MET A 620     135.186  83.848  34.405  1.00107.39           C  
ANISOU 4504  C   MET A 620    21305   9476  10022   5204  -1019   -277       C  
ATOM   4505  O   MET A 620     135.016  82.887  35.164  1.00 98.08           O  
ANISOU 4505  O   MET A 620    19372   8800   9093   4983  -1107   -373       O  
ATOM   4506  CB  MET A 620     136.463  82.639  32.623  1.00111.63           C  
ANISOU 4506  CB  MET A 620    21425  10129  10862   4438  -1071    -85       C  
ATOM   4507  CG  MET A 620     136.657  82.340  31.139  1.00 95.21           C  
ANISOU 4507  CG  MET A 620    19341   8081   8753   4449  -1114     64       C  
ATOM   4508  SD  MET A 620     135.117  81.915  30.296  1.00 86.77           S  
ANISOU 4508  SD  MET A 620    17817   7632   7517   5302  -1334     87       S  
ATOM   4509  CE  MET A 620     134.628  80.444  31.188  1.00 94.83           C  
ANISOU 4509  CE  MET A 620    17712   9425   8895   5063  -1476    -76       C  
ATOM   4510  N   ASN A 621     135.264  85.104  34.845  1.00117.17           N  
ANISOU 4510  N   ASN A 621    23246  10273  10998   5272   -851   -304       N  
ATOM   4511  CA  ASN A 621     135.104  85.456  36.252  1.00125.80           C  
ANISOU 4511  CA  ASN A 621    24419  11302  12076   5278   -796   -459       C  
ATOM   4512  C   ASN A 621     136.136  84.788  37.155  1.00118.22           C  
ANISOU 4512  C   ASN A 621    23189  10292  11438   4532   -779   -574       C  
ATOM   4513  O   ASN A 621     135.797  83.861  37.900  1.00113.44           O  
ANISOU 4513  O   ASN A 621    21827  10236  11037   4459   -886   -652       O  
ATOM   4514  CB  ASN A 621     133.695  85.102  36.733  1.00120.47           C  
ANISOU 4514  CB  ASN A 621    23219  11215  11339   5975   -936   -541       C  
ATOM   4515  CG  ASN A 621     133.304  85.874  37.972  1.00117.39           C  
ANISOU 4515  CG  ASN A 621    23091  10731  10780   6161   -845   -665       C  
ATOM   4516  OD1 ASN A 621     133.820  86.960  38.218  1.00102.58           O  
ANISOU 4516  OD1 ASN A 621    21910   8346   8721   5955   -677   -649       O  
ATOM   4517  ND2 ASN A 621     132.379  85.325  38.756  1.00132.48           N  
ANISOU 4517  ND2 ASN A 621    24438  13157  12741   6537   -941   -790       N  
ATOM   4518  N   TYR A 622     137.387  85.243  37.107  1.00111.71           N  
ANISOU 4518  N   TYR A 622    22852   8959  10634   3886   -631   -581       N  
ATOM   4519  CA  TYR A 622     138.414  84.788  38.037  1.00116.39           C  
ANISOU 4519  CA  TYR A 622    23133   9632  11459   3120   -605   -705       C  
ATOM   4520  C   TYR A 622     139.514  85.841  38.071  1.00121.51           C  
ANISOU 4520  C   TYR A 622    24592   9613  11964   2594   -390   -769       C  
ATOM   4521  O   TYR A 622     139.531  86.771  37.261  1.00121.65           O  
ANISOU 4521  O   TYR A 622    25123   9349  11751   2683   -253   -633       O  
ATOM   4522  CB  TYR A 622     138.971  83.412  37.643  1.00113.03           C  
ANISOU 4522  CB  TYR A 622    21879   9703  11366   2664   -728   -638       C  
ATOM   4523  CG  TYR A 622     139.765  83.410  36.353  1.00122.19           C  
ANISOU 4523  CG  TYR A 622    23240  10641  12547   2346   -676   -507       C  
ATOM   4524  CD1 TYR A 622     139.135  83.210  35.131  1.00127.80           C  
ANISOU 4524  CD1 TYR A 622    23902  11457  13199   2786   -749   -351       C  
ATOM   4525  CD2 TYR A 622     141.142  83.599  36.356  1.00118.17           C  
ANISOU 4525  CD2 TYR A 622    22939   9865  12096   1601   -551   -557       C  
ATOM   4526  CE1 TYR A 622     139.848  83.207  33.948  1.00114.94           C  
ANISOU 4526  CE1 TYR A 622    22470   9631  11570   2509   -691   -229       C  
ATOM   4527  CE2 TYR A 622     141.865  83.601  35.172  1.00117.00           C  
ANISOU 4527  CE2 TYR A 622    22963   9538  11952   1301   -481   -444       C  
ATOM   4528  CZ  TYR A 622     141.211  83.404  33.971  1.00107.33           C  
ANISOU 4528  CZ  TYR A 622    21727   8383  10672   1764   -548   -270       C  
ATOM   4529  OH  TYR A 622     141.919  83.402  32.791  1.00 91.64           O  
ANISOU 4529  OH  TYR A 622    19924   6223   8671   1477   -470   -154       O  
ATOM   4530  N   THR A 623     140.446  85.683  39.012  1.00118.48           N  
ANISOU 4530  N   THR A 623    24055   9255  11706   1939   -352   -932       N  
ATOM   4531  CA  THR A 623     141.534  86.651  39.103  1.00113.25           C  
ANISOU 4531  CA  THR A 623    23931   8179  10919   1312   -138   -995       C  
ATOM   4532  C   THR A 623     142.860  85.995  38.753  1.00 99.47           C  
ANISOU 4532  C   THR A 623    21886   6528   9379    529   -134  -1036       C  
ATOM   4533  O   THR A 623     143.152  84.901  39.256  1.00 89.36           O  
ANISOU 4533  O   THR A 623    19859   5755   8341    301   -289  -1089       O  
ATOM   4534  CB  THR A 623     141.614  87.265  40.507  1.00 97.10           C  
ANISOU 4534  CB  THR A 623    22062   6056   8776   1165    -68  -1194       C  
ATOM   4535  OG1 THR A 623     142.040  86.275  41.447  1.00105.74           O  
ANISOU 4535  OG1 THR A 623    22604   7494  10077    827   -207  -1386       O  
ATOM   4536  CG2 THR A 623     140.262  87.809  40.925  1.00 99.62           C  
ANISOU 4536  CG2 THR A 623    22598   6355   8898   1968    -85  -1163       C  
ATOM   4537  N   PRO A 624     143.683  86.613  37.902  1.00104.79           N  
ANISOU 4537  N   PRO A 624    22894   6960   9962    107     48   -952       N  
ATOM   4538  CA  PRO A 624     144.995  86.026  37.602  1.00110.50           C  
ANISOU 4538  CA  PRO A 624    23275   7851  10860   -652     66  -1009       C  
ATOM   4539  C   PRO A 624     145.923  86.100  38.805  1.00112.57           C  
ANISOU 4539  C   PRO A 624    23350   8262  11158  -1281    100  -1260       C  
ATOM   4540  O   PRO A 624     145.941  87.089  39.541  1.00109.68           O  
ANISOU 4540  O   PRO A 624    23375   7682  10616  -1356    235  -1365       O  
ATOM   4541  CB  PRO A 624     145.512  86.880  36.439  1.00112.25           C  
ANISOU 4541  CB  PRO A 624    23979   7767  10903   -868    296   -870       C  
ATOM   4542  CG  PRO A 624     144.810  88.181  36.592  1.00104.69           C  
ANISOU 4542  CG  PRO A 624    23718   6423   9635   -460    448   -825       C  
ATOM   4543  CD  PRO A 624     143.446  87.850  37.136  1.00103.96           C  
ANISOU 4543  CD  PRO A 624    23483   6459   9557    325    251   -806       C  
ATOM   4544  N   GLN A 625     146.699  85.041  38.994  1.00117.21           N  
ANISOU 4544  N   GLN A 625    23328   9253  11955  -1720    -30  -1360       N  
ATOM   4545  CA  GLN A 625     147.546  84.889  40.169  1.00112.38           C  
ANISOU 4545  CA  GLN A 625    22388   8940  11371  -2251    -60  -1607       C  
ATOM   4546  C   GLN A 625     148.536  83.757  39.902  1.00111.10           C  
ANISOU 4546  C   GLN A 625    21464   9334  11416  -2685   -171  -1605       C  
ATOM   4547  O   GLN A 625     148.322  82.949  38.993  1.00100.74           O  
ANISOU 4547  O   GLN A 625    19787   8225  10265  -2447   -257  -1391       O  
ATOM   4548  CB  GLN A 625     146.708  84.593  41.424  1.00104.33           C  
ANISOU 4548  CB  GLN A 625    21130   8144  10366  -1822   -213  -1681       C  
ATOM   4549  CG  GLN A 625     145.648  83.520  41.219  1.00 92.74           C  
ANISOU 4549  CG  GLN A 625    19080   7068   9088  -1167   -407  -1457       C  
ATOM   4550  CD  GLN A 625     144.708  83.388  42.400  1.00 97.86           C  
ANISOU 4550  CD  GLN A 625    19568   7902   9714   -716   -502  -1515       C  
ATOM   4551  OE1 GLN A 625     145.127  83.470  43.555  1.00 87.01           O  
ANISOU 4551  OE1 GLN A 625    18104   6669   8288   -982   -515  -1706       O  
ATOM   4552  NE2 GLN A 625     143.426  83.189  42.114  1.00105.59           N  
ANISOU 4552  NE2 GLN A 625    20494   8917  10707    -31   -567  -1362       N  
ATOM   4553  N   PRO A 626     149.631  83.695  40.666  1.00112.31           N  
ANISOU 4553  N   PRO A 626    21342   9783  11549  -3294   -170  -1841       N  
ATOM   4554  CA  PRO A 626     150.547  82.554  40.545  1.00 94.99           C  
ANISOU 4554  CA  PRO A 626    18336   8225   9531  -3593   -296  -1831       C  
ATOM   4555  C   PRO A 626     149.835  81.230  40.783  1.00103.24           C  
ANISOU 4555  C   PRO A 626    18698   9737  10793  -3034   -527  -1641       C  
ATOM   4556  O   PRO A 626     148.864  81.145  41.540  1.00 92.49           O  
ANISOU 4556  O   PRO A 626    17331   8377   9433  -2572   -612  -1613       O  
ATOM   4557  CB  PRO A 626     151.597  82.828  41.625  1.00 96.31           C  
ANISOU 4557  CB  PRO A 626    18354   8664   9574  -4196   -284  -2154       C  
ATOM   4558  CG  PRO A 626     151.602  84.313  41.762  1.00 92.36           C  
ANISOU 4558  CG  PRO A 626    18505   7694   8892  -4335    -31  -2218       C  
ATOM   4559  CD  PRO A 626     150.180  84.753  41.535  1.00 92.02           C  
ANISOU 4559  CD  PRO A 626    19050   7111   8805  -3675    -13  -2051       C  
ATOM   4560  N   LEU A 627     150.336  80.188  40.124  1.00103.17           N  
ANISOU 4560  N   LEU A 627    18126  10119  10953  -3098   -608  -1518       N  
ATOM   4561  CA  LEU A 627     149.698  78.881  40.111  1.00105.28           C  
ANISOU 4561  CA  LEU A 627    17815  10762  11426  -2618   -784  -1321       C  
ATOM   4562  C   LEU A 627     150.222  77.996  41.237  1.00106.12           C  
ANISOU 4562  C   LEU A 627    17316  11428  11575  -2698   -924  -1410       C  
ATOM   4563  O   LEU A 627     151.324  78.189  41.757  1.00109.20           O  
ANISOU 4563  O   LEU A 627    17576  12054  11862  -3168   -914  -1612       O  
ATOM   4564  CB  LEU A 627     149.930  78.190  38.769  1.00111.03           C  
ANISOU 4564  CB  LEU A 627    18311  11580  12294  -2607   -784  -1140       C  
ATOM   4565  CG  LEU A 627     149.728  79.055  37.525  1.00112.91           C  
ANISOU 4565  CG  LEU A 627    19140  11311  12449  -2623   -630  -1057       C  
ATOM   4566  CD1 LEU A 627     150.181  78.308  36.283  1.00106.71           C  
ANISOU 4566  CD1 LEU A 627    18059  10701  11786  -2697   -632   -912       C  
ATOM   4567  CD2 LEU A 627     148.275  79.486  37.400  1.00116.99           C  
ANISOU 4567  CD2 LEU A 627    20053  11476  12921  -2021   -641   -937       C  
ATOM   4568  N   MET A 628     149.411  77.005  41.602  1.00 94.54           N  
ANISOU 4568  N   MET A 628    15484  10197  10241  -2231  -1048  -1262       N  
ATOM   4569  CA  MET A 628     149.828  76.008  42.579  1.00 92.33           C  
ANISOU 4569  CA  MET A 628    14658  10431   9993  -2215  -1173  -1288       C  
ATOM   4570  C   MET A 628     150.832  75.062  41.932  1.00 84.16           C  
ANISOU 4570  C   MET A 628    13160   9763   9055  -2404  -1215  -1226       C  
ATOM   4571  O   MET A 628     150.503  74.360  40.970  1.00 62.06           O  
ANISOU 4571  O   MET A 628    10221   6949   6412  -2201  -1220  -1038       O  
ATOM   4572  CB  MET A 628     148.613  75.247  43.108  1.00100.09           C  
ANISOU 4572  CB  MET A 628    15462  11499  11071  -1687  -1245  -1141       C  
ATOM   4573  CG  MET A 628     148.904  74.357  44.303  1.00 86.36           C  
ANISOU 4573  CG  MET A 628    13298  10206   9308  -1623  -1344  -1161       C  
ATOM   4574  SD  MET A 628     147.496  74.208  45.415  1.00 62.45           S  
ANISOU 4574  SD  MET A 628    10318   7154   6255  -1159  -1357  -1117       S  
ATOM   4575  CE  MET A 628     146.276  73.471  44.335  1.00 70.02           C  
ANISOU 4575  CE  MET A 628    11181   7999   7425   -770  -1331   -882       C  
ATOM   4576  N   ALA A 629     152.061  75.059  42.448  1.00 88.05           N  
ANISOU 4576  N   ALA A 629    13407  10614   9432  -2785  -1244  -1403       N  
ATOM   4577  CA  ALA A 629     153.145  74.288  41.837  1.00 90.79           C  
ANISOU 4577  CA  ALA A 629    13319  11353   9826  -2976  -1272  -1382       C  
ATOM   4578  C   ALA A 629     152.820  72.812  41.641  1.00 90.66           C  
ANISOU 4578  C   ALA A 629    12891  11583   9974  -2548  -1363  -1151       C  
ATOM   4579  O   ALA A 629     153.092  72.290  40.548  1.00 86.86           O  
ANISOU 4579  O   ALA A 629    12272  11128   9602  -2552  -1335  -1038       O  
ATOM   4580  CB  ALA A 629     154.425  74.460  42.666  1.00 99.49           C  
ANISOU 4580  CB  ALA A 629    14143  12923  10735  -3374  -1320  -1639       C  
ATOM   4581  N   PRO A 630     152.258  72.085  42.615  1.00 94.27           N  
ANISOU 4581  N   PRO A 630    13174  12203  10443  -2193  -1449  -1077       N  
ATOM   4582  CA  PRO A 630     151.901  70.682  42.346  1.00 93.99           C  
ANISOU 4582  CA  PRO A 630    12839  12317  10555  -1825  -1490   -855       C  
ATOM   4583  C   PRO A 630     150.878  70.518  41.237  1.00 78.99           C  
ANISOU 4583  C   PRO A 630    11114  10062   8839  -1626  -1427   -686       C  
ATOM   4584  O   PRO A 630     150.745  69.414  40.697  1.00 76.40           O  
ANISOU 4584  O   PRO A 630    10563   9828   8636  -1430  -1433   -532       O  
ATOM   4585  CB  PRO A 630     151.355  70.188  43.694  1.00 92.78           C  
ANISOU 4585  CB  PRO A 630    12601  12312  10340  -1532  -1548   -826       C  
ATOM   4586  CG  PRO A 630     150.998  71.419  44.444  1.00 86.22           C  
ANISOU 4586  CG  PRO A 630    12096  11282   9380  -1659  -1532   -995       C  
ATOM   4587  CD  PRO A 630     151.998  72.441  44.022  1.00 88.36           C  
ANISOU 4587  CD  PRO A 630    12495  11527   9549  -2133  -1498  -1195       C  
ATOM   4588  N   MET A 631     150.160  71.581  40.867  1.00 87.62           N  
ANISOU 4588  N   MET A 631    12611  10757   9925  -1653  -1365   -719       N  
ATOM   4589  CA  MET A 631     149.158  71.479  39.816  1.00 86.16           C  
ANISOU 4589  CA  MET A 631    12573  10295   9870  -1424  -1325   -576       C  
ATOM   4590  C   MET A 631     149.768  71.462  38.420  1.00 88.01           C  
ANISOU 4590  C   MET A 631    12815  10468  10158  -1609  -1280   -530       C  
ATOM   4591  O   MET A 631     149.121  70.975  37.486  1.00 68.37           O  
ANISOU 4591  O   MET A 631    10308   7883   7786  -1405  -1272   -398       O  
ATOM   4592  CB  MET A 631     148.158  72.632  39.926  1.00 92.20           C  
ANISOU 4592  CB  MET A 631    13785  10684  10562  -1296  -1281   -622       C  
ATOM   4593  CG  MET A 631     146.806  72.345  39.304  1.00 86.79           C  
ANISOU 4593  CG  MET A 631    13142   9858   9975   -908  -1280   -491       C  
ATOM   4594  SD  MET A 631     145.838  71.188  40.283  1.00 62.58           S  
ANISOU 4594  SD  MET A 631     9729   7058   6992   -578  -1322   -422       S  
ATOM   4595  CE  MET A 631     144.365  71.070  39.277  1.00 73.92           C  
ANISOU 4595  CE  MET A 631    11208   8371   8509   -230  -1309   -332       C  
ATOM   4596  N   ILE A 632     150.986  71.984  38.250  1.00 95.62           N  
ANISOU 4596  N   ILE A 632    13793  11513  11025  -2011  -1241   -651       N  
ATOM   4597  CA  ILE A 632     151.613  71.906  36.934  1.00 97.29           C  
ANISOU 4597  CA  ILE A 632    13985  11706  11275  -2200  -1178   -607       C  
ATOM   4598  C   ILE A 632     152.162  70.506  36.689  1.00 98.98           C  
ANISOU 4598  C   ILE A 632    13715  12304  11588  -2094  -1234   -519       C  
ATOM   4599  O   ILE A 632     152.280  70.078  35.536  1.00102.85           O  
ANISOU 4599  O   ILE A 632    14149  12772  12157  -2078  -1198   -426       O  
ATOM   4600  CB  ILE A 632     152.704  72.983  36.764  1.00 97.07           C  
ANISOU 4600  CB  ILE A 632    14156  11635  11093  -2717  -1077   -783       C  
ATOM   4601  CG1 ILE A 632     154.006  72.579  37.461  1.00107.84           C  
ANISOU 4601  CG1 ILE A 632    15081  13519  12374  -2990  -1125   -933       C  
ATOM   4602  CG2 ILE A 632     152.210  74.338  37.266  1.00 88.53           C  
ANISOU 4602  CG2 ILE A 632    13605  10152   9879  -2817  -1009   -893       C  
ATOM   4603  CD1 ILE A 632     155.098  72.124  36.503  1.00108.32           C  
ANISOU 4603  CD1 ILE A 632    14851  13863  12442  -3221  -1078   -937       C  
ATOM   4604  N   GLY A 633     152.502  69.771  37.749  1.00 96.89           N  
ANISOU 4604  N   GLY A 633    13130  12385  11298  -1990  -1315   -543       N  
ATOM   4605  CA  GLY A 633     152.873  68.378  37.571  1.00 87.47           C  
ANISOU 4605  CA  GLY A 633    11561  11494  10179  -1788  -1354   -435       C  
ATOM   4606  C   GLY A 633     151.691  67.527  37.149  1.00 80.94           C  
ANISOU 4606  C   GLY A 633    10767  10472   9513  -1437  -1348   -259       C  
ATOM   4607  O   GLY A 633     151.810  66.676  36.262  1.00 60.72           O  
ANISOU 4607  O   GLY A 633     8073   7954   7044  -1347  -1326   -163       O  
ATOM   4608  N   LEU A 634     150.532  67.754  37.770  1.00 83.48           N  
ANISOU 4608  N   LEU A 634    11260  10600   9858  -1254  -1357   -236       N  
ATOM   4609  CA  LEU A 634     149.327  67.020  37.401  1.00 73.65           C  
ANISOU 4609  CA  LEU A 634    10022   9215   8746   -974  -1339   -111       C  
ATOM   4610  C   LEU A 634     148.911  67.319  35.966  1.00 80.28           C  
ANISOU 4610  C   LEU A 634    11011   9834   9657   -990  -1305    -72       C  
ATOM   4611  O   LEU A 634     148.550  66.406  35.215  1.00 69.38           O  
ANISOU 4611  O   LEU A 634     9515   8465   8382   -865  -1289     14       O  
ATOM   4612  CB  LEU A 634     148.195  67.365  38.368  1.00 69.27           C  
ANISOU 4612  CB  LEU A 634     9597   8552   8168   -802  -1344   -129       C  
ATOM   4613  CG  LEU A 634     146.789  66.927  37.956  1.00 73.63           C  
ANISOU 4613  CG  LEU A 634    10168   8981   8826   -566  -1314    -56       C  
ATOM   4614  CD1 LEU A 634     146.666  65.413  37.988  1.00 70.73           C  
ANISOU 4614  CD1 LEU A 634     9566   8758   8553   -454  -1277     43       C  
ATOM   4615  CD2 LEU A 634     145.742  67.581  38.842  1.00 71.59           C  
ANISOU 4615  CD2 LEU A 634    10053   8642   8507   -416  -1313   -110       C  
ATOM   4616  N   ILE A 635     148.956  68.595  35.566  1.00 92.43           N  
ANISOU 4616  N   ILE A 635    12845  11159  11116  -1142  -1284   -138       N  
ATOM   4617  CA  ILE A 635     148.511  68.970  34.226  1.00 79.95           C  
ANISOU 4617  CA  ILE A 635    11465   9357   9557  -1107  -1252    -87       C  
ATOM   4618  C   ILE A 635     149.462  68.422  33.166  1.00 72.73           C  
ANISOU 4618  C   ILE A 635    10398   8557   8679  -1268  -1220    -49       C  
ATOM   4619  O   ILE A 635     149.049  68.156  32.032  1.00 65.15           O  
ANISOU 4619  O   ILE A 635     9475   7511   7768  -1170  -1207     20       O  
ATOM   4620  CB  ILE A 635     148.356  70.501  34.122  1.00 71.29           C  
ANISOU 4620  CB  ILE A 635    10814   7950   8323  -1201  -1210   -152       C  
ATOM   4621  CG1 ILE A 635     147.475  70.880  32.933  1.00 77.29           C  
ANISOU 4621  CG1 ILE A 635    11826   8473   9068   -996  -1197    -77       C  
ATOM   4622  CG2 ILE A 635     149.702  71.184  33.991  1.00 73.11           C  
ANISOU 4622  CG2 ILE A 635    11150   8176   8451  -1620  -1140   -241       C  
ATOM   4623  CD1 ILE A 635     146.000  70.773  33.212  1.00 84.02           C  
ANISOU 4623  CD1 ILE A 635    12679   9306   9940   -605  -1254    -55       C  
ATOM   4624  N   ILE A 636     150.739  68.236  33.511  1.00 86.05           N  
ANISOU 4624  N   ILE A 636    11891  10483  10323  -1499  -1209   -108       N  
ATOM   4625  CA  ILE A 636     151.677  67.603  32.589  1.00 70.95           C  
ANISOU 4625  CA  ILE A 636     9776   8749   8433  -1611  -1173    -81       C  
ATOM   4626  C   ILE A 636     151.310  66.139  32.385  1.00 77.37           C  
ANISOU 4626  C   ILE A 636    10345   9683   9370  -1335  -1199     21       C  
ATOM   4627  O   ILE A 636     151.365  65.619  31.264  1.00 79.64           O  
ANISOU 4627  O   ILE A 636    10593   9957   9710  -1301  -1166     75       O  
ATOM   4628  CB  ILE A 636     153.118  67.763  33.109  1.00 70.93           C  
ANISOU 4628  CB  ILE A 636     9567   9063   8321  -1898  -1162   -198       C  
ATOM   4629  CG1 ILE A 636     153.615  69.193  32.887  1.00 70.84           C  
ANISOU 4629  CG1 ILE A 636     9840   8896   8179  -2290  -1079   -317       C  
ATOM   4630  CG2 ILE A 636     154.051  66.760  32.449  1.00 75.19           C  
ANISOU 4630  CG2 ILE A 636     9783   9905   8880  -1888  -1143   -168       C  
ATOM   4631  CD1 ILE A 636     154.946  69.489  33.548  1.00 82.90           C  
ANISOU 4631  CD1 ILE A 636    11146  10783   9571  -2638  -1067   -491       C  
ATOM   4632  N   ALA A 637     150.909  65.460  33.461  1.00 87.26           N  
ANISOU 4632  N   ALA A 637    11471  11030  10654  -1144  -1239     43       N  
ATOM   4633  CA  ALA A 637     150.585  64.040  33.378  1.00 80.82           C  
ANISOU 4633  CA  ALA A 637    10491  10283   9932   -915  -1226    133       C  
ATOM   4634  C   ALA A 637     149.310  63.804  32.577  1.00 70.09           C  
ANISOU 4634  C   ALA A 637     9246   8710   8675   -792  -1208    178       C  
ATOM   4635  O   ALA A 637     149.262  62.919  31.715  1.00 62.25           O  
ANISOU 4635  O   ALA A 637     8182   7720   7749   -732  -1172    220       O  
ATOM   4636  CB  ALA A 637     150.450  63.457  34.784  1.00 72.40           C  
ANISOU 4636  CB  ALA A 637     9331   9339   8839   -760  -1244    153       C  
ATOM   4637  N   VAL A 638     148.264  64.584  32.852  1.00 79.75           N  
ANISOU 4637  N   VAL A 638    10634   9777   9891   -739  -1233    150       N  
ATOM   4638  CA  VAL A 638     146.974  64.357  32.205  1.00 83.75           C  
ANISOU 4638  CA  VAL A 638    11182  10178  10460   -593  -1232    162       C  
ATOM   4639  C   VAL A 638     147.059  64.662  30.714  1.00 83.13           C  
ANISOU 4639  C   VAL A 638    11200  10015  10370   -635  -1234    170       C  
ATOM   4640  O   VAL A 638     146.605  63.873  29.879  1.00 81.58           O  
ANISOU 4640  O   VAL A 638    10920   9841  10234   -567  -1222    182       O  
ATOM   4641  CB  VAL A 638     145.877  65.193  32.888  1.00 87.52           C  
ANISOU 4641  CB  VAL A 638    11790  10570  10893   -473  -1264    118       C  
ATOM   4642  CG1 VAL A 638     144.536  64.955  32.212  1.00 86.86           C  
ANISOU 4642  CG1 VAL A 638    11679  10480  10844   -306  -1274    100       C  
ATOM   4643  CG2 VAL A 638     145.802  64.857  34.367  1.00 89.13           C  
ANISOU 4643  CG2 VAL A 638    11904  10868  11091   -435  -1249    112       C  
ATOM   4644  N   ILE A 639     147.639  65.811  30.360  1.00 91.02           N  
ANISOU 4644  N   ILE A 639    12403  10909  11274   -767  -1234    156       N  
ATOM   4645  CA  ILE A 639     147.706  66.211  28.956  1.00 83.89           C  
ANISOU 4645  CA  ILE A 639    11653   9899  10321   -798  -1218    179       C  
ATOM   4646  C   ILE A 639     148.527  65.212  28.151  1.00 80.92           C  
ANISOU 4646  C   ILE A 639    11085   9661  10000   -883  -1177    206       C  
ATOM   4647  O   ILE A 639     148.146  64.828  27.039  1.00 67.86           O  
ANISOU 4647  O   ILE A 639     9436   7989   8358   -807  -1177    225       O  
ATOM   4648  CB  ILE A 639     148.270  67.639  28.834  1.00 87.40           C  
ANISOU 4648  CB  ILE A 639    12419  10163  10629   -973  -1180    162       C  
ATOM   4649  CG1 ILE A 639     147.287  68.653  29.421  1.00 85.22           C  
ANISOU 4649  CG1 ILE A 639    12413   9695  10272   -809  -1212    137       C  
ATOM   4650  CG2 ILE A 639     148.579  67.978  27.382  1.00 86.42           C  
ANISOU 4650  CG2 ILE A 639    12473   9934  10429  -1043  -1129    204       C  
ATOM   4651  CD1 ILE A 639     147.773  70.080  29.338  1.00 88.40           C  
ANISOU 4651  CD1 ILE A 639    13233   9838  10517   -984  -1143    115       C  
ATOM   4652  N   TRP A 640     149.658  64.767  28.703  1.00 87.80           N  
ANISOU 4652  N   TRP A 640    11777  10700  10882  -1012  -1146    198       N  
ATOM   4653  CA  TRP A 640     150.515  63.832  27.980  1.00 79.26           C  
ANISOU 4653  CA  TRP A 640    10516   9772   9826  -1045  -1100    218       C  
ATOM   4654  C   TRP A 640     149.798  62.513  27.723  1.00 72.47           C  
ANISOU 4654  C   TRP A 640     9546   8920   9069   -850  -1096    245       C  
ATOM   4655  O   TRP A 640     149.730  62.042  26.581  1.00 82.29           O  
ANISOU 4655  O   TRP A 640    10792  10147  10327   -827  -1070    251       O  
ATOM   4656  CB  TRP A 640     151.809  63.596  28.758  1.00 74.86           C  
ANISOU 4656  CB  TRP A 640     9754   9463   9225  -1148  -1082    189       C  
ATOM   4657  CG  TRP A 640     152.809  62.790  27.995  1.00 85.87           C  
ANISOU 4657  CG  TRP A 640    10966  11053  10606  -1155  -1027    198       C  
ATOM   4658  CD1 TRP A 640     152.907  61.431  27.954  1.00 87.78           C  
ANISOU 4658  CD1 TRP A 640    11062  11390  10902   -946  -1006    237       C  
ATOM   4659  CD2 TRP A 640     153.852  63.294  27.153  1.00 99.40           C  
ANISOU 4659  CD2 TRP A 640    12651  12886  12230  -1377   -964    159       C  
ATOM   4660  NE1 TRP A 640     153.950  61.056  27.144  1.00 95.38           N  
ANISOU 4660  NE1 TRP A 640    11891  12539  11811   -980   -948    224       N  
ATOM   4661  CE2 TRP A 640     154.546  62.182  26.639  1.00104.66           C  
ANISOU 4661  CE2 TRP A 640    13108  13758  12901  -1256   -921    174       C  
ATOM   4662  CE3 TRP A 640     154.267  64.577  26.786  1.00 99.06           C  
ANISOU 4662  CE3 TRP A 640    12770  12781  12086  -1677   -915    111       C  
ATOM   4663  CZ2 TRP A 640     155.632  62.314  25.776  1.00105.49           C  
ANISOU 4663  CZ2 TRP A 640    13102  14063  12917  -1416   -843    134       C  
ATOM   4664  CZ3 TRP A 640     155.344  64.706  25.930  1.00103.05           C  
ANISOU 4664  CZ3 TRP A 640    13189  13462  12506  -1886   -820     74       C  
ATOM   4665  CH2 TRP A 640     156.014  63.582  25.435  1.00106.66           C  
ANISOU 4665  CH2 TRP A 640    13377  14177  12973  -1750   -790     82       C  
ATOM   4666  N   GLY A 641     149.255  61.900  28.777  1.00 68.93           N  
ANISOU 4666  N   GLY A 641     9025   8489   8678   -732  -1105    251       N  
ATOM   4667  CA  GLY A 641     148.554  60.639  28.605  1.00 82.21           C  
ANISOU 4667  CA  GLY A 641    10648  10144  10443   -611  -1062    260       C  
ATOM   4668  C   GLY A 641     147.310  60.764  27.750  1.00 84.94           C  
ANISOU 4668  C   GLY A 641    11060  10400  10814   -581  -1087    213       C  
ATOM   4669  O   GLY A 641     146.902  59.801  27.093  1.00 87.71           O  
ANISOU 4669  O   GLY A 641    11370  10744  11210   -558  -1044    185       O  
ATOM   4670  N   LEU A 642     146.699  61.948  27.733  1.00 77.64           N  
ANISOU 4670  N   LEU A 642    10248   9417   9834   -565  -1156    192       N  
ATOM   4671  CA  LEU A 642     145.511  62.168  26.919  1.00 86.71           C  
ANISOU 4671  CA  LEU A 642    11436  10550  10959   -471  -1204    139       C  
ATOM   4672  C   LEU A 642     145.867  62.323  25.446  1.00 94.43           C  
ANISOU 4672  C   LEU A 642    12493  11510  11875   -493  -1213    147       C  
ATOM   4673  O   LEU A 642     145.211  61.737  24.576  1.00 75.81           O  
ANISOU 4673  O   LEU A 642    10075   9210   9518   -443  -1226     91       O  
ATOM   4674  CB  LEU A 642     144.762  63.400  27.416  1.00 94.98           C  
ANISOU 4674  CB  LEU A 642    12614  11546  11928   -363  -1272    123       C  
ATOM   4675  CG  LEU A 642     143.279  63.438  27.079  1.00104.71           C  
ANISOU 4675  CG  LEU A 642    13792  12869  13126   -188  -1330     43       C  
ATOM   4676  CD1 LEU A 642     142.600  62.217  27.679  1.00 99.31           C  
ANISOU 4676  CD1 LEU A 642    12874  12314  12546   -228  -1273    -23       C  
ATOM   4677  CD2 LEU A 642     142.666  64.729  27.594  1.00111.06           C  
ANISOU 4677  CD2 LEU A 642    14761  13618  13821    -15  -1390     37       C  
ATOM   4678  N   SER A 643     146.901  63.114  25.148  1.00 97.72           N  
ANISOU 4678  N   SER A 643    13046  11863  12220   -594  -1196    201       N  
ATOM   4679  CA  SER A 643     147.320  63.284  23.761  1.00 85.17           C  
ANISOU 4679  CA  SER A 643    11556  10254  10551   -632  -1177    220       C  
ATOM   4680  C   SER A 643     147.882  61.992  23.188  1.00 81.29           C  
ANISOU 4680  C   SER A 643    10894   9864  10126   -675  -1117    205       C  
ATOM   4681  O   SER A 643     147.696  61.710  21.998  1.00 77.84           O  
ANISOU 4681  O   SER A 643    10486   9446   9645   -644  -1117    184       O  
ATOM   4682  CB  SER A 643     148.350  64.409  23.657  1.00 73.85           C  
ANISOU 4682  CB  SER A 643    10317   8728   9013   -797  -1129    268       C  
ATOM   4683  OG  SER A 643     149.510  64.113  24.413  1.00 88.41           O  
ANISOU 4683  OG  SER A 643    12007  10680  10903   -963  -1073    266       O  
ATOM   4684  N   THR A 644     148.558  61.192  24.015  1.00 89.66           N  
ANISOU 4684  N   THR A 644    11803  10994  11268   -713  -1064    215       N  
ATOM   4685  CA  THR A 644     149.074  59.911  23.546  1.00 84.05           C  
ANISOU 4685  CA  THR A 644    10983  10351  10602   -694   -992    204       C  
ATOM   4686  C   THR A 644     147.942  58.935  23.254  1.00 70.69           C  
ANISOU 4686  C   THR A 644     9267   8620   8970   -624   -986    134       C  
ATOM   4687  O   THR A 644     148.000  58.183  22.274  1.00 65.30           O  
ANISOU 4687  O   THR A 644     8584   7945   8280   -622   -944     90       O  
ATOM   4688  CB  THR A 644     150.035  59.324  24.579  1.00 76.82           C  
ANISOU 4688  CB  THR A 644     9946   9527   9715   -676   -940    240       C  
ATOM   4689  OG1 THR A 644     151.042  60.292  24.897  1.00 73.84           O  
ANISOU 4689  OG1 THR A 644     9545   9248   9262   -793   -950    261       O  
ATOM   4690  CG2 THR A 644     150.699  58.079  24.032  1.00 79.19           C  
ANISOU 4690  CG2 THR A 644    10184   9883  10021   -598   -852    237       C  
ATOM   4691  N   ASP A 645     146.903  58.935  24.092  1.00 79.42           N  
ANISOU 4691  N   ASP A 645    10350   9703  10125   -593  -1016    101       N  
ATOM   4692  CA  ASP A 645     145.764  58.055  23.856  1.00 78.08           C  
ANISOU 4692  CA  ASP A 645    10131   9539   9998   -596   -992     -2       C  
ATOM   4693  C   ASP A 645     145.097  58.356  22.521  1.00 68.53           C  
ANISOU 4693  C   ASP A 645     8931   8399   8709   -580  -1065    -86       C  
ATOM   4694  O   ASP A 645     144.715  57.435  21.788  1.00 61.99           O  
ANISOU 4694  O   ASP A 645     8067   7601   7885   -630  -1025   -189       O  
ATOM   4695  CB  ASP A 645     144.758  58.183  24.999  1.00 62.29           C  
ANISOU 4695  CB  ASP A 645     8076   7556   8037   -584  -1004    -32       C  
ATOM   4696  CG  ASP A 645     145.030  57.205  26.120  1.00 61.03           C  
ANISOU 4696  CG  ASP A 645     7917   7325   7947   -609   -884      9       C  
ATOM   4697  OD1 ASP A 645     146.218  57.000  26.456  1.00 53.83           O  
ANISOU 4697  OD1 ASP A 645     7042   6380   7030   -567   -846    104       O  
ATOM   4698  OD2 ASP A 645     144.055  56.649  26.671  1.00 53.85           O  
ANISOU 4698  OD2 ASP A 645     6971   6416   7074   -663   -821    -59       O  
ATOM   4699  N   TYR A 646     144.956  59.639  22.181  1.00 84.61           N  
ANISOU 4699  N   TYR A 646    11048  10454  10647   -501  -1166    -50       N  
ATOM   4700  CA  TYR A 646     144.326  60.002  20.918  1.00 89.01           C  
ANISOU 4700  CA  TYR A 646    11642  11096  11080   -420  -1247   -113       C  
ATOM   4701  C   TYR A 646     145.227  59.723  19.724  1.00 80.95           C  
ANISOU 4701  C   TYR A 646    10698  10055  10005   -467  -1203    -88       C  
ATOM   4702  O   TYR A 646     144.725  59.567  18.605  1.00 56.37           O  
ANISOU 4702  O   TYR A 646     7586   7036   6796   -419  -1250   -168       O  
ATOM   4703  CB  TYR A 646     143.900  61.470  20.949  1.00 78.56           C  
ANISOU 4703  CB  TYR A 646    10462   9756   9630   -262  -1349    -61       C  
ATOM   4704  CG  TYR A 646     142.569  61.665  21.633  1.00 77.95           C  
ANISOU 4704  CG  TYR A 646    10269   9803   9545   -136  -1422   -148       C  
ATOM   4705  CD1 TYR A 646     142.467  61.643  23.018  1.00 81.21           C  
ANISOU 4705  CD1 TYR A 646    10619  10176  10060   -175  -1384   -133       C  
ATOM   4706  CD2 TYR A 646     141.408  61.845  20.894  1.00 80.82           C  
ANISOU 4706  CD2 TYR A 646    10558  10373   9776     38  -1528   -259       C  
ATOM   4707  CE1 TYR A 646     141.248  61.807  23.647  1.00 83.28           C  
ANISOU 4707  CE1 TYR A 646    10753  10585  10304    -63  -1432   -222       C  
ATOM   4708  CE2 TYR A 646     140.185  62.011  21.512  1.00 83.30           C  
ANISOU 4708  CE2 TYR A 646    10709  10877  10063    165  -1590   -363       C  
ATOM   4709  CZ  TYR A 646     140.109  61.991  22.888  1.00 85.08           C  
ANISOU 4709  CZ  TYR A 646    10879  11044  10403    105  -1533   -343       C  
ATOM   4710  OH  TYR A 646     138.891  62.156  23.506  1.00 79.66           O  
ANISOU 4710  OH  TYR A 646    10012  10576   9677    230  -1577   -454       O  
ATOM   4711  N   GLU A 647     146.541  59.649  19.936  1.00 81.88           N  
ANISOU 4711  N   GLU A 647    10853  10097  10161   -553  -1116      5       N  
ATOM   4712  CA  GLU A 647     147.424  59.169  18.881  1.00 79.43           C  
ANISOU 4712  CA  GLU A 647    10569   9805   9805   -597  -1047     10       C  
ATOM   4713  C   GLU A 647     147.275  57.665  18.692  1.00 83.87           C  
ANISOU 4713  C   GLU A 647    11042  10382  10444   -617   -975    -89       C  
ATOM   4714  O   GLU A 647     147.331  57.166  17.562  1.00 79.16           O  
ANISOU 4714  O   GLU A 647    10472   9821   9784   -619   -952   -155       O  
ATOM   4715  CB  GLU A 647     148.872  59.524  19.208  1.00 79.06           C  
ANISOU 4715  CB  GLU A 647    10535   9750   9755   -681   -968    111       C  
ATOM   4716  CG  GLU A 647     149.819  59.330  18.044  1.00 97.12           C  
ANISOU 4716  CG  GLU A 647    12850  12096  11953   -723   -891    121       C  
ATOM   4717  CD  GLU A 647     150.077  60.618  17.291  1.00 98.12           C  
ANISOU 4717  CD  GLU A 647    13161  12193  11926   -785   -895    185       C  
ATOM   4718  OE1 GLU A 647     150.661  60.559  16.188  1.00 99.03           O  
ANISOU 4718  OE1 GLU A 647    13329  12360  11938   -821   -829    191       O  
ATOM   4719  OE2 GLU A 647     149.696  61.690  17.805  1.00 94.50           O  
ANISOU 4719  OE2 GLU A 647    12832  11641  11434   -794   -947    231       O  
ATOM   4720  N   VAL A 648     147.084  56.930  19.790  1.00 88.65           N  
ANISOU 4720  N   VAL A 648    11581  10934  11166   -634   -922   -103       N  
ATOM   4721  CA  VAL A 648     146.905  55.484  19.703  1.00 80.05           C  
ANISOU 4721  CA  VAL A 648    10494   9786  10134   -669   -814   -195       C  
ATOM   4722  C   VAL A 648     145.607  55.148  18.980  1.00 77.80           C  
ANISOU 4722  C   VAL A 648    10177   9567   9816   -741   -856   -368       C  
ATOM   4723  O   VAL A 648     145.555  54.209  18.178  1.00 63.77           O  
ANISOU 4723  O   VAL A 648     8443   7770   8015   -801   -786   -481       O  
ATOM   4724  CB  VAL A 648     146.957  54.853  21.108  1.00 74.80           C  
ANISOU 4724  CB  VAL A 648     9830   9023   9568   -663   -728   -149       C  
ATOM   4725  CG1 VAL A 648     146.529  53.395  21.057  1.00 74.01           C  
ANISOU 4725  CG1 VAL A 648     9819   8796   9507   -729   -588   -254       C  
ATOM   4726  CG2 VAL A 648     148.358  54.966  21.684  1.00 62.19           C  
ANISOU 4726  CG2 VAL A 648     8230   7435   7964   -564   -690    -12       C  
ATOM   4727  N   PHE A 649     144.543  55.912  19.242  1.00 80.78           N  
ANISOU 4727  N   PHE A 649    10469  10056  10169   -729   -970   -411       N  
ATOM   4728  CA  PHE A 649     143.274  55.672  18.561  1.00 88.98           C  
ANISOU 4728  CA  PHE A 649    11404  11263  11139   -782  -1032   -605       C  
ATOM   4729  C   PHE A 649     143.414  55.854  17.055  1.00 95.74           C  
ANISOU 4729  C   PHE A 649    12304  12221  11852   -726  -1100   -656       C  
ATOM   4730  O   PHE A 649     142.783  55.135  16.272  1.00 91.47           O  
ANISOU 4730  O   PHE A 649    11705  11795  11253   -817  -1098   -845       O  
ATOM   4731  CB  PHE A 649     142.200  56.613  19.103  1.00 88.52           C  
ANISOU 4731  CB  PHE A 649    11223  11368  11041   -695  -1157   -631       C  
ATOM   4732  CG  PHE A 649     141.989  56.511  20.585  1.00 98.92           C  
ANISOU 4732  CG  PHE A 649    12497  12611  12478   -744  -1091   -587       C  
ATOM   4733  CD1 PHE A 649     142.149  55.304  21.244  1.00113.46           C  
ANISOU 4733  CD1 PHE A 649    14369  14310  14432   -909   -922   -612       C  
ATOM   4734  CD2 PHE A 649     141.627  57.627  21.319  1.00 98.65           C  
ANISOU 4734  CD2 PHE A 649    12434  12630  12419   -606  -1184   -516       C  
ATOM   4735  CE1 PHE A 649     141.952  55.213  22.609  1.00113.49           C  
ANISOU 4735  CE1 PHE A 649    14358  14246  14516   -940   -852   -559       C  
ATOM   4736  CE2 PHE A 649     141.430  57.542  22.683  1.00102.16           C  
ANISOU 4736  CE2 PHE A 649    12841  13021  12955   -645  -1121   -481       C  
ATOM   4737  CZ  PHE A 649     141.593  56.333  23.328  1.00106.94           C  
ANISOU 4737  CZ  PHE A 649    13460  13506  13667   -815   -957   -498       C  
ATOM   4738  N   LEU A 650     144.242  56.811  16.636  1.00 98.51           N  
ANISOU 4738  N   LEU A 650    12769  12534  12126   -602  -1146   -501       N  
ATOM   4739  CA  LEU A 650     144.387  57.139  15.223  1.00 83.96           C  
ANISOU 4739  CA  LEU A 650    11007  10782  10113   -527  -1203   -519       C  
ATOM   4740  C   LEU A 650     145.279  56.134  14.503  1.00 77.41           C  
ANISOU 4740  C   LEU A 650    10236   9881   9294   -611  -1078   -552       C  
ATOM   4741  O   LEU A 650     144.853  55.476  13.549  1.00 80.41           O  
ANISOU 4741  O   LEU A 650    10602  10358   9592   -650  -1085   -712       O  
ATOM   4742  CB  LEU A 650     144.954  58.554  15.087  1.00 79.15           C  
ANISOU 4742  CB  LEU A 650    10557  10117   9398   -402  -1254   -336       C  
ATOM   4743  CG  LEU A 650     145.135  59.125  13.685  1.00 83.43           C  
ANISOU 4743  CG  LEU A 650    11253  10722   9725   -300  -1297   -308       C  
ATOM   4744  CD1 LEU A 650     143.795  59.234  12.976  1.00 70.44           C  
ANISOU 4744  CD1 LEU A 650     9540   9308   7914   -146  -1451   -453       C  
ATOM   4745  CD2 LEU A 650     145.820  60.478  13.775  1.00 80.89           C  
ANISOU 4745  CD2 LEU A 650    11159  10262   9315   -248  -1281   -113       C  
ATOM   4746  N   VAL A 651     146.527  56.004  14.960  1.00 69.26           N  
ANISOU 4746  N   VAL A 651     9262   8712   8343   -627   -965   -418       N  
ATOM   4747  CA  VAL A 651     147.511  55.181  14.270  1.00 73.27           C  
ANISOU 4747  CA  VAL A 651     9830   9180   8831   -639   -842   -430       C  
ATOM   4748  C   VAL A 651     147.194  53.690  14.363  1.00 89.06           C  
ANISOU 4748  C   VAL A 651    11841  11091  10907   -712   -736   -582       C  
ATOM   4749  O   VAL A 651     147.652  52.912  13.516  1.00 87.19           O  
ANISOU 4749  O   VAL A 651    11686  10831  10614   -708   -648   -655       O  
ATOM   4750  CB  VAL A 651     148.907  55.516  14.829  1.00 67.07           C  
ANISOU 4750  CB  VAL A 651     9046   8353   8084   -611   -759   -263       C  
ATOM   4751  CG1 VAL A 651     149.993  54.721  14.130  1.00 70.14           C  
ANISOU 4751  CG1 VAL A 651     9465   8759   8427   -572   -629   -276       C  
ATOM   4752  CG2 VAL A 651     149.175  57.009  14.686  1.00 60.58           C  
ANISOU 4752  CG2 VAL A 651     8273   7578   7168   -614   -828   -140       C  
ATOM   4753  N   SER A 652     146.402  53.266  15.354  1.00 97.43           N  
ANISOU 4753  N   SER A 652    12856  12085  12077   -792   -721   -638       N  
ATOM   4754  CA  SER A 652     146.039  51.853  15.452  1.00 91.08           C  
ANISOU 4754  CA  SER A 652    12135  11146  11325   -912   -582   -790       C  
ATOM   4755  C   SER A 652     145.306  51.370  14.207  1.00 82.13           C  
ANISOU 4755  C   SER A 652    11008  10116  10080  -1029   -604  -1019       C  
ATOM   4756  O   SER A 652     145.403  50.191  13.850  1.00 87.39           O  
ANISOU 4756  O   SER A 652    11822  10642  10742  -1120   -459  -1150       O  
ATOM   4757  CB  SER A 652     145.181  51.602  16.692  1.00 87.05           C  
ANISOU 4757  CB  SER A 652    11581  10571  10924  -1026   -548   -820       C  
ATOM   4758  OG  SER A 652     145.940  51.756  17.879  1.00 74.18           O  
ANISOU 4758  OG  SER A 652     9983   8822   9380   -913   -498   -628       O  
ATOM   4759  N   ARG A 653     144.567  52.256  13.540  1.00 81.27           N  
ANISOU 4759  N   ARG A 653    10766  10255   9859  -1009   -780  -1079       N  
ATOM   4760  CA  ARG A 653     143.949  51.918  12.264  1.00 87.86           C  
ANISOU 4760  CA  ARG A 653    11579  11264  10541  -1081   -834  -1300       C  
ATOM   4761  C   ARG A 653     144.887  52.142  11.088  1.00 80.54           C  
ANISOU 4761  C   ARG A 653    10764  10355   9480   -944   -838  -1232       C  
ATOM   4762  O   ARG A 653     144.757  51.461  10.064  1.00 68.77           O  
ANISOU 4762  O   ARG A 653     9330   8919   7879  -1010   -810  -1412       O  
ATOM   4763  CB  ARG A 653     142.669  52.731  12.060  1.00 85.67           C  
ANISOU 4763  CB  ARG A 653    11092  11306  10151  -1059  -1034  -1409       C  
ATOM   4764  CG  ARG A 653     141.585  52.437  13.078  1.00 70.11           C  
ANISOU 4764  CG  ARG A 653     8959   9401   8278  -1228  -1022  -1536       C  
ATOM   4765  CD  ARG A 653     141.287  50.953  13.136  1.00 79.97           C  
ANISOU 4765  CD  ARG A 653    10274  10521   9588  -1539   -834  -1761       C  
ATOM   4766  NE  ARG A 653     139.862  50.674  12.993  1.00 93.40           N  
ANISOU 4766  NE  ARG A 653    11741  12535  11211  -1767   -888  -2066       N  
ATOM   4767  CZ  ARG A 653     139.299  50.207  11.884  1.00105.21           C  
ANISOU 4767  CZ  ARG A 653    13163  14264  12548  -1910   -930  -2346       C  
ATOM   4768  NH1 ARG A 653     140.042  49.959  10.815  1.00117.70           N  
ANISOU 4768  NH1 ARG A 653    14920  15761  14037  -1831   -920  -2342       N  
ATOM   4769  NH2 ARG A 653     137.994  49.982  11.846  1.00108.99           N  
ANISOU 4769  NH2 ARG A 653    13369  15098  12943  -2142   -980  -2648       N  
ATOM   4770  N   MET A 654     145.826  53.082  11.212  1.00 78.90           N  
ANISOU 4770  N   MET A 654    10596  10116   9267   -784   -857   -993       N  
ATOM   4771  CA  MET A 654     146.842  53.251  10.179  1.00 81.89           C  
ANISOU 4771  CA  MET A 654    11083  10511   9521   -689   -813   -920       C  
ATOM   4772  C   MET A 654     147.742  52.024  10.096  1.00 86.94           C  
ANISOU 4772  C   MET A 654    11827  10991  10216   -706   -622   -961       C  
ATOM   4773  O   MET A 654     148.029  51.524   9.002  1.00 77.73           O  
ANISOU 4773  O   MET A 654    10749   9860   8926   -690   -570  -1063       O  
ATOM   4774  CB  MET A 654     147.667  54.510  10.452  1.00 82.79           C  
ANISOU 4774  CB  MET A 654    11217  10623   9616   -589   -835   -676       C  
ATOM   4775  CG  MET A 654     146.875  55.801  10.365  1.00 63.31           C  
ANISOU 4775  CG  MET A 654     8749   8266   7040   -512  -1003   -617       C  
ATOM   4776  SD  MET A 654     147.900  57.257  10.603  1.00 51.72           S  
ANISOU 4776  SD  MET A 654     7406   6723   5523   -465   -975   -353       S  
ATOM   4777  CE  MET A 654     146.691  58.539  10.314  1.00 78.98           C  
ANISOU 4777  CE  MET A 654    10955  10262   8794   -302  -1164   -326       C  
ATOM   4778  N   VAL A 655     148.192  51.519  11.247  1.00 88.04           N  
ANISOU 4778  N   VAL A 655    11980  10956  10517   -699   -514   -884       N  
ATOM   4779  CA  VAL A 655     149.028  50.322  11.244  1.00 77.31           C  
ANISOU 4779  CA  VAL A 655    10762   9431   9181   -636   -326   -913       C  
ATOM   4780  C   VAL A 655     148.212  49.103  10.832  1.00 75.39           C  
ANISOU 4780  C   VAL A 655    10663   9061   8921   -782   -245  -1161       C  
ATOM   4781  O   VAL A 655     148.709  48.220  10.125  1.00 66.49           O  
ANISOU 4781  O   VAL A 655     9705   7840   7719   -735   -116  -1256       O  
ATOM   4782  CB  VAL A 655     149.707  50.123  12.614  1.00 86.73           C  
ANISOU 4782  CB  VAL A 655    11952  10494  10507   -535   -240   -755       C  
ATOM   4783  CG1 VAL A 655     150.578  51.318  12.954  1.00 80.49           C  
ANISOU 4783  CG1 VAL A 655    11007   9865   9711   -446   -309   -555       C  
ATOM   4784  CG2 VAL A 655     148.680  49.882  13.710  1.00103.49           C  
ANISOU 4784  CG2 VAL A 655    14075  12490  12755   -664   -252   -793       C  
ATOM   4785  N   GLU A 656     146.942  49.043  11.246  1.00 84.75           N  
ANISOU 4785  N   GLU A 656    11785  10259  10158   -980   -307  -1291       N  
ATOM   4786  CA  GLU A 656     146.105  47.903  10.884  1.00 84.61           C  
ANISOU 4786  CA  GLU A 656    11893  10143  10112  -1208   -212  -1567       C  
ATOM   4787  C   GLU A 656     145.868  47.854   9.381  1.00 88.25           C  
ANISOU 4787  C   GLU A 656    12350  10792  10388  -1251   -280  -1759       C  
ATOM   4788  O   GLU A 656     145.876  46.775   8.777  1.00 92.11           O  
ANISOU 4788  O   GLU A 656    13039  11144  10814  -1356   -142  -1956       O  
ATOM   4789  CB  GLU A 656     144.776  47.964  11.634  1.00 71.56           C  
ANISOU 4789  CB  GLU A 656    10101   8557   8531  -1446   -265  -1687       C  
ATOM   4790  CG  GLU A 656     143.864  46.794  11.339  1.00 82.89           C  
ANISOU 4790  CG  GLU A 656    11650   9913   9930  -1773   -139  -2007       C  
ATOM   4791  CD  GLU A 656     142.516  46.923  12.008  1.00 87.58           C  
ANISOU 4791  CD  GLU A 656    12037  10669  10569  -2041   -189  -2155       C  
ATOM   4792  OE1 GLU A 656     142.380  47.753  12.931  1.00 79.22           O  
ANISOU 4792  OE1 GLU A 656    10811   9689   9600  -1936   -282  -1976       O  
ATOM   4793  OE2 GLU A 656     141.585  46.192  11.606  1.00 89.69           O  
ANISOU 4793  OE2 GLU A 656    12300  11010  10769  -2372   -127  -2471       O  
ATOM   4794  N   ALA A 657     145.649  49.015   8.760  1.00 94.24           N  
ANISOU 4794  N   ALA A 657    12923  11848  11035  -1159   -483  -1705       N  
ATOM   4795  CA  ALA A 657     145.539  49.062   7.306  1.00 95.05           C  
ANISOU 4795  CA  ALA A 657    13038  12153  10925  -1141   -556  -1851       C  
ATOM   4796  C   ALA A 657     146.882  48.776   6.646  1.00 83.45           C  
ANISOU 4796  C   ALA A 657    11747  10570   9392   -970   -425  -1751       C  
ATOM   4797  O   ALA A 657     146.942  48.106   5.608  1.00 63.82           O  
ANISOU 4797  O   ALA A 657     9382   8100   6765  -1002   -368  -1934       O  
ATOM   4798  CB  ALA A 657     144.998  50.422   6.866  1.00 93.21           C  
ANISOU 4798  CB  ALA A 657    12620  12241  10552  -1022   -793  -1781       C  
ATOM   4799  N   ARG A 658     147.970  49.271   7.239  1.00 82.69           N  
ANISOU 4799  N   ARG A 658    11646  10391   9381   -794   -371  -1484       N  
ATOM   4800  CA  ARG A 658     149.298  49.019   6.687  1.00 82.84           C  
ANISOU 4800  CA  ARG A 658    11774  10372   9331   -622   -236  -1397       C  
ATOM   4801  C   ARG A 658     149.647  47.537   6.738  1.00 85.64           C  
ANISOU 4801  C   ARG A 658    12351  10473   9716   -608    -28  -1533       C  
ATOM   4802  O   ARG A 658     150.243  47.000   5.797  1.00 83.65           O  
ANISOU 4802  O   ARG A 658    12232  10220   9330   -514     73  -1615       O  
ATOM   4803  CB  ARG A 658     150.339  49.845   7.442  1.00 88.39           C  
ANISOU 4803  CB  ARG A 658    12371  11101  10111   -481   -220  -1119       C  
ATOM   4804  CG  ARG A 658     151.773  49.543   7.057  1.00 96.71           C  
ANISOU 4804  CG  ARG A 658    13466  12182  11095   -302    -63  -1041       C  
ATOM   4805  CD  ARG A 658     152.005  49.784   5.579  1.00107.82           C  
ANISOU 4805  CD  ARG A 658    14920  13760  12286   -281    -63  -1103       C  
ATOM   4806  NE  ARG A 658     153.422  49.736   5.235  1.00115.21           N  
ANISOU 4806  NE  ARG A 658    15833  14801  13140   -121     87  -1011       N  
ATOM   4807  CZ  ARG A 658     153.897  49.908   4.006  1.00108.26           C  
ANISOU 4807  CZ  ARG A 658    14992  14081  12060    -81    137  -1040       C  
ATOM   4808  NH1 ARG A 658     153.066  50.132   2.997  1.00103.72           N  
ANISOU 4808  NH1 ARG A 658    14506  13568  11337   -165     35  -1151       N  
ATOM   4809  NH2 ARG A 658     155.204  49.853   3.786  1.00107.18           N  
ANISOU 4809  NH2 ARG A 658    14791  14085  11848     56    290   -966       N  
ATOM   4810  N   GLU A 659     149.277  46.855   7.826  1.00 97.66           N  
ANISOU 4810  N   GLU A 659    13958  11759  11391   -686     54  -1556       N  
ATOM   4811  CA  GLU A 659     149.559  45.429   7.951  1.00106.13           C  
ANISOU 4811  CA  GLU A 659    15337  12515  12472   -657    280  -1672       C  
ATOM   4812  C   GLU A 659     148.832  44.588   6.910  1.00106.83           C  
ANISOU 4812  C   GLU A 659    15610  12546  12436   -868    333  -1990       C  
ATOM   4813  O   GLU A 659     149.165  43.408   6.751  1.00101.79           O  
ANISOU 4813  O   GLU A 659    15297  11622  11756   -829    543  -2108       O  
ATOM   4814  CB  GLU A 659     149.192  44.933   9.351  1.00111.54           C  
ANISOU 4814  CB  GLU A 659    16123  12937  13319   -725    370  -1622       C  
ATOM   4815  CG  GLU A 659     150.060  45.480  10.476  1.00117.09           C  
ANISOU 4815  CG  GLU A 659    16704  13660  14123   -481    357  -1332       C  
ATOM   4816  CD  GLU A 659     151.536  45.192  10.284  1.00116.86           C  
ANISOU 4816  CD  GLU A 659    16742  13646  14015   -124    472  -1208       C  
ATOM   4817  OE1 GLU A 659     152.360  46.064  10.635  1.00110.20           O  
ANISOU 4817  OE1 GLU A 659    15657  13030  13184     37    394  -1011       O  
ATOM   4818  OE2 GLU A 659     151.873  44.097   9.785  1.00115.64           O  
ANISOU 4818  OE2 GLU A 659    16878  13292  13769    -10    648  -1324       O  
ATOM   4819  N   ARG A 660     147.853  45.154   6.207  1.00102.84           N  
ANISOU 4819  N   ARG A 660    14920  12309  11844  -1072    151  -2144       N  
ATOM   4820  CA  ARG A 660     147.163  44.458   5.131  1.00103.05           C  
ANISOU 4820  CA  ARG A 660    15064  12376  11715  -1286    169  -2477       C  
ATOM   4821  C   ARG A 660     147.870  44.605   3.788  1.00 99.08           C  
ANISOU 4821  C   ARG A 660    14600  12036  11009  -1104    153  -2498       C  
ATOM   4822  O   ARG A 660     147.312  44.206   2.761  1.00 82.99           O  
ANISOU 4822  O   ARG A 660    12622  10108   8801  -1259    127  -2775       O  
ATOM   4823  CB  ARG A 660     145.720  44.958   5.018  1.00 97.32           C  
ANISOU 4823  CB  ARG A 660    14078  11947  10951  -1566    -33  -2664       C  
ATOM   4824  CG  ARG A 660     144.922  44.844   6.306  1.00100.05           C  
ANISOU 4824  CG  ARG A 660    14350  12186  11477  -1778    -11  -2670       C  
ATOM   4825  CD  ARG A 660     143.471  45.244   6.094  1.00111.84           C  
ANISOU 4825  CD  ARG A 660    15548  14052  12894  -2044   -201  -2909       C  
ATOM   4826  NE  ARG A 660     142.812  44.393   5.107  1.00127.91           N  
ANISOU 4826  NE  ARG A 660    17661  16181  14760  -2332   -161  -3304       N  
ATOM   4827  CZ  ARG A 660     141.533  44.499   4.761  1.00138.22           C  
ANISOU 4827  CZ  ARG A 660    18699  17872  15947  -2603   -307  -3605       C  
ATOM   4828  NH1 ARG A 660     140.766  45.424   5.324  1.00135.29           N  
ANISOU 4828  NH1 ARG A 660    17977  17820  15609  -2578   -500  -3539       N  
ATOM   4829  NH2 ARG A 660     141.019  43.680   3.853  1.00133.10           N  
ANISOU 4829  NH2 ARG A 660    18125  17320  15126  -2892   -260  -3990       N  
ATOM   4830  N   GLY A 661     149.076  45.168   3.773  1.00105.21           N  
ANISOU 4830  N   GLY A 661    15332  12862  11782   -801    174  -2230       N  
ATOM   4831  CA  GLY A 661     149.842  45.319   2.553  1.00115.19           C  
ANISOU 4831  CA  GLY A 661    16633  14287  12846   -629    195  -2230       C  
ATOM   4832  C   GLY A 661     149.662  46.631   1.825  1.00113.43           C  
ANISOU 4832  C   GLY A 661    16193  14424  12482   -600    -10  -2132       C  
ATOM   4833  O   GLY A 661     150.186  46.780   0.715  1.00125.86           O  
ANISOU 4833  O   GLY A 661    17816  16150  13857   -488     10  -2147       O  
ATOM   4834  N   MET A 662     148.951  47.588   2.411  1.00115.67           N  
ANISOU 4834  N   MET A 662    16275  14833  12841   -674   -191  -2027       N  
ATOM   4835  CA  MET A 662     148.663  48.846   1.744  1.00104.24           C  
ANISOU 4835  CA  MET A 662    14697  13684  11227   -612   -380  -1931       C  
ATOM   4836  C   MET A 662     149.855  49.796   1.834  1.00 99.97           C  
ANISOU 4836  C   MET A 662    14129  13175  10681   -437   -327  -1620       C  
ATOM   4837  O   MET A 662     150.758  49.630   2.659  1.00 77.45           O  
ANISOU 4837  O   MET A 662    11261  10178   7988   -375   -195  -1474       O  
ATOM   4838  CB  MET A 662     147.417  49.491   2.351  1.00 90.60           C  
ANISOU 4838  CB  MET A 662    12790  12076   9556   -716   -582  -1951       C  
ATOM   4839  CG  MET A 662     146.177  48.618   2.235  1.00 86.28           C  
ANISOU 4839  CG  MET A 662    12209  11587   8988   -951   -631  -2296       C  
ATOM   4840  SD  MET A 662     144.881  49.080   3.390  1.00 68.26           S  
ANISOU 4840  SD  MET A 662     9680   9406   6850  -1091   -788  -2323       S  
ATOM   4841  CE  MET A 662     144.791  50.825   3.054  1.00 68.12           C  
ANISOU 4841  CE  MET A 662     9543   9670   6668   -813  -1016  -2072       C  
ATOM   4842  N   SER A 663     149.850  50.800   0.960  1.00113.00           N  
ANISOU 4842  N   SER A 663    15782  15036  12117   -363   -423  -1530       N  
ATOM   4843  CA  SER A 663     150.924  51.779   0.941  1.00114.78           C  
ANISOU 4843  CA  SER A 663    16011  15301  12300   -273   -348  -1259       C  
ATOM   4844  C   SER A 663     150.819  52.709   2.149  1.00113.91           C  
ANISOU 4844  C   SER A 663    15796  15120  12365   -307   -418  -1056       C  
ATOM   4845  O   SER A 663     149.829  52.712   2.887  1.00113.02           O  
ANISOU 4845  O   SER A 663    15604  14961  12375   -363   -548  -1113       O  
ATOM   4846  CB  SER A 663     150.892  52.586  -0.357  1.00101.91           C  
ANISOU 4846  CB  SER A 663    14494  13868  10357   -197   -401  -1214       C  
ATOM   4847  OG  SER A 663     149.714  53.367  -0.442  1.00 98.05           O  
ANISOU 4847  OG  SER A 663    14003  13487   9766   -168   -621  -1216       O  
ATOM   4848  N   THR A 664     151.869  53.508   2.348  1.00103.00           N  
ANISOU 4848  N   THR A 664    14408  13748  10978   -295   -317   -836       N  
ATOM   4849  CA  THR A 664     151.890  54.434   3.476  1.00 84.18           C  
ANISOU 4849  CA  THR A 664    11953  11291   8741   -349   -364   -655       C  
ATOM   4850  C   THR A 664     150.796  55.485   3.338  1.00 79.07           C  
ANISOU 4850  C   THR A 664    11388  10672   7982   -320   -553   -604       C  
ATOM   4851  O   THR A 664     150.032  55.727   4.278  1.00 80.24           O  
ANISOU 4851  O   THR A 664    11460  10756   8272   -333   -671   -597       O  
ATOM   4852  CB  THR A 664     153.264  55.095   3.592  1.00 72.08           C  
ANISOU 4852  CB  THR A 664    10400   9806   7183   -399   -200   -472       C  
ATOM   4853  OG1 THR A 664     154.262  54.090   3.818  1.00 69.09           O  
ANISOU 4853  OG1 THR A 664     9898   9460   6892   -356    -41   -529       O  
ATOM   4854  CG2 THR A 664     153.281  56.084   4.746  1.00 65.91           C  
ANISOU 4854  CG2 THR A 664     9569   8944   6532   -489   -245   -312       C  
ATOM   4855  N   ALA A 665     150.698  56.112   2.163  1.00 92.04           N  
ANISOU 4855  N   ALA A 665    13202  12423   9345   -245   -578   -567       N  
ATOM   4856  CA  ALA A 665     149.659  57.114   1.945  1.00 86.17           C  
ANISOU 4856  CA  ALA A 665    12578  11725   8437   -127   -760   -512       C  
ATOM   4857  C   ALA A 665     148.265  56.508   2.032  1.00 83.59           C  
ANISOU 4857  C   ALA A 665    12109  11518   8134    -67   -961   -737       C  
ATOM   4858  O   ALA A 665     147.316  57.191   2.434  1.00 79.13           O  
ANISOU 4858  O   ALA A 665    11527  10999   7540     35  -1126   -712       O  
ATOM   4859  CB  ALA A 665     149.861  57.796   0.591  1.00 75.60           C  
ANISOU 4859  CB  ALA A 665    11496  10481   6747    -17   -732   -428       C  
ATOM   4860  N   GLU A 666     148.117  55.234   1.664  1.00 96.67           N  
ANISOU 4860  N   GLU A 666    13666  13239   9825   -137   -937   -974       N  
ATOM   4861  CA  GLU A 666     146.823  54.575   1.808  1.00105.49           C  
ANISOU 4861  CA  GLU A 666    14623  14487  10972   -174  -1093  -1230       C  
ATOM   4862  C   GLU A 666     146.535  54.237   3.265  1.00104.89           C  
ANISOU 4862  C   GLU A 666    14388  14259  11207   -303  -1081  -1240       C  
ATOM   4863  O   GLU A 666     145.415  54.443   3.746  1.00 98.08           O  
ANISOU 4863  O   GLU A 666    13388  13513  10367   -300  -1234  -1327       O  
ATOM   4864  CB  GLU A 666     146.771  53.316   0.943  1.00105.96           C  
ANISOU 4864  CB  GLU A 666    14684  14625  10952   -262  -1039  -1503       C  
ATOM   4865  CG  GLU A 666     146.454  53.580  -0.517  1.00105.24           C  
ANISOU 4865  CG  GLU A 666    14690  14797  10500   -124  -1139  -1591       C  
ATOM   4866  CD  GLU A 666     145.125  54.286  -0.702  1.00105.32           C  
ANISOU 4866  CD  GLU A 666    14602  15097  10316     21  -1399  -1662       C  
ATOM   4867  OE1 GLU A 666     145.114  55.534  -0.761  1.00102.45           O  
ANISOU 4867  OE1 GLU A 666    14359  14757   9810    236  -1474  -1426       O  
ATOM   4868  OE2 GLU A 666     144.089  53.591  -0.778  1.00104.33           O  
ANISOU 4868  OE2 GLU A 666    14289  15188  10165    -79  -1518  -1965       O  
ATOM   4869  N   ALA A 667     147.535  53.715   3.981  1.00100.51           N  
ANISOU 4869  N   ALA A 667    13841  13477  10869   -395   -900  -1156       N  
ATOM   4870  CA  ALA A 667     147.348  53.399   5.393  1.00 80.39           C  
ANISOU 4870  CA  ALA A 667    11179  10772   8592   -493   -874  -1140       C  
ATOM   4871  C   ALA A 667     147.012  54.649   6.195  1.00 81.03           C  
ANISOU 4871  C   ALA A 667    11215  10858   8715   -426   -987   -958       C  
ATOM   4872  O   ALA A 667     146.139  54.617   7.071  1.00 72.14           O  
ANISOU 4872  O   ALA A 667     9963   9737   7709   -472  -1068  -1017       O  
ATOM   4873  CB  ALA A 667     148.600  52.722   5.948  1.00 70.42           C  
ANISOU 4873  CB  ALA A 667     9955   9309   7493   -518   -668  -1055       C  
ATOM   4874  N   ILE A 668     147.696  55.760   5.906  1.00 85.34           N  
ANISOU 4874  N   ILE A 668    11887  11392   9147   -334   -972   -743       N  
ATOM   4875  CA  ILE A 668     147.370  57.033   6.546  1.00 72.02           C  
ANISOU 4875  CA  ILE A 668    10240   9670   7453   -258  -1066   -576       C  
ATOM   4876  C   ILE A 668     145.914  57.395   6.286  1.00 72.02           C  
ANISOU 4876  C   ILE A 668    10193   9861   7310   -116  -1276   -689       C  
ATOM   4877  O   ILE A 668     145.105  57.496   7.214  1.00 71.64           O  
ANISOU 4877  O   ILE A 668    10007   9834   7379   -112  -1365   -731       O  
ATOM   4878  CB  ILE A 668     148.315  58.144   6.055  1.00 66.25           C  
ANISOU 4878  CB  ILE A 668     9732   8875   6566   -223   -980   -356       C  
ATOM   4879  CG1 ILE A 668     149.755  57.863   6.487  1.00 77.50           C  
ANISOU 4879  CG1 ILE A 668    11116  10199   8131   -377   -779   -266       C  
ATOM   4880  CG2 ILE A 668     147.860  59.496   6.585  1.00 59.57           C  
ANISOU 4880  CG2 ILE A 668     9022   7950   5663   -127  -1069   -202       C  
ATOM   4881  CD1 ILE A 668     150.782  58.727   5.779  1.00 70.44           C  
ANISOU 4881  CD1 ILE A 668    10413   9298   7055   -425   -644   -108       C  
ATOM   4882  N   ARG A 669     145.558  57.564   5.009  1.00 84.93           N  
ANISOU 4882  N   ARG A 669    11921  11682   8665     22  -1357   -754       N  
ATOM   4883  CA  ARG A 669     144.207  57.982   4.641  1.00 93.65           C  
ANISOU 4883  CA  ARG A 669    12961  13057   9564    226  -1577   -867       C  
ATOM   4884  C   ARG A 669     143.147  57.074   5.256  1.00102.89           C  
ANISOU 4884  C   ARG A 669    13816  14396  10881     98  -1661  -1133       C  
ATOM   4885  O   ARG A 669     142.208  57.549   5.903  1.00 87.66           O  
ANISOU 4885  O   ARG A 669    11752  12596   8957    201  -1792  -1160       O  
ATOM   4886  CB  ARG A 669     144.067  58.007   3.116  1.00 80.79           C  
ANISOU 4886  CB  ARG A 669    11451  11647   7599    380  -1643   -940       C  
ATOM   4887  CG  ARG A 669     142.705  58.481   2.635  1.00 93.25           C  
ANISOU 4887  CG  ARG A 669    12947  13586   8898    660  -1892  -1063       C  
ATOM   4888  CD  ARG A 669     142.574  58.393   1.123  1.00109.89           C  
ANISOU 4888  CD  ARG A 669    15158  15948  10649    818  -1966  -1158       C  
ATOM   4889  NE  ARG A 669     142.531  57.009   0.657  1.00123.22           N  
ANISOU 4889  NE  ARG A 669    16655  17770  12395    567  -1929  -1456       N  
ATOM   4890  CZ  ARG A 669     141.429  56.265   0.633  1.00128.22           C  
ANISOU 4890  CZ  ARG A 669    16981  18732  13004    478  -2066  -1787       C  
ATOM   4891  NH1 ARG A 669     140.276  56.770   1.052  1.00135.84           N  
ANISOU 4891  NH1 ARG A 669    17738  19986  13887    648  -2263  -1864       N  
ATOM   4892  NH2 ARG A 669     141.480  55.015   0.193  1.00120.86           N  
ANISOU 4892  NH2 ARG A 669    15953  17853  12114    209  -1993  -2060       N  
ATOM   4893  N   ILE A 670     143.285  55.759   5.063  1.00117.16           N  
ANISOU 4893  N   ILE A 670    15526  16197  12793   -136  -1565  -1339       N  
ATOM   4894  CA  ILE A 670     142.312  54.817   5.611  1.00110.71           C  
ANISOU 4894  CA  ILE A 670    14457  15506  12102   -338  -1593  -1612       C  
ATOM   4895  C   ILE A 670     142.292  54.895   7.132  1.00 99.03           C  
ANISOU 4895  C   ILE A 670    12899  13829  10899   -431  -1531  -1506       C  
ATOM   4896  O   ILE A 670     141.235  54.772   7.764  1.00 82.43           O  
ANISOU 4896  O   ILE A 670    10580  11895   8845   -499  -1608  -1656       O  
ATOM   4897  CB  ILE A 670     142.615  53.390   5.113  1.00 98.48           C  
ANISOU 4897  CB  ILE A 670    12934  13885  10600   -588  -1449  -1834       C  
ATOM   4898  CG1 ILE A 670     142.379  53.297   3.604  1.00 91.91           C  
ANISOU 4898  CG1 ILE A 670    12136  13327   9459   -504  -1544  -1999       C  
ATOM   4899  CG2 ILE A 670     141.771  52.360   5.854  1.00 83.78           C  
ANISOU 4899  CG2 ILE A 670    10893  12042   8899   -882  -1401  -2095       C  
ATOM   4900  CD1 ILE A 670     140.940  53.508   3.198  1.00102.20           C  
ANISOU 4900  CD1 ILE A 670    13194  15097  10540   -443  -1775  -2247       C  
ATOM   4901  N   GLY A 671     143.455  55.115   7.742  1.00 99.13           N  
ANISOU 4901  N   GLY A 671    13065  13525  11075   -436  -1391  -1262       N  
ATOM   4902  CA  GLY A 671     143.535  55.291   9.178  1.00 96.83           C  
ANISOU 4902  CA  GLY A 671    12720  13058  11014   -492  -1341  -1143       C  
ATOM   4903  C   GLY A 671     142.692  56.448   9.673  1.00 94.51           C  
ANISOU 4903  C   GLY A 671    12354  12902  10655   -315  -1503  -1073       C  
ATOM   4904  O   GLY A 671     141.757  56.247  10.452  1.00 74.35           O  
ANISOU 4904  O   GLY A 671     9607  10458   8185   -378  -1550  -1194       O  
ATOM   4905  N   THR A 672     142.998  57.664   9.213  1.00107.37           N  
ANISOU 4905  N   THR A 672    14163  14521  12112    -89  -1570   -885       N  
ATOM   4906  CA  THR A 672     142.289  58.864   9.644  1.00107.69           C  
ANISOU 4906  CA  THR A 672    14226  14637  12055    144  -1707   -793       C  
ATOM   4907  C   THR A 672     140.953  59.070   8.927  1.00 89.14           C  
ANISOU 4907  C   THR A 672    11735  12684   9449    367  -1911   -974       C  
ATOM   4908  O   THR A 672     140.423  60.187   8.948  1.00 84.87           O  
ANISOU 4908  O   THR A 672    11287  12231   8730    676  -2037   -880       O  
ATOM   4909  CB  THR A 672     143.175  60.100   9.458  1.00100.14           C  
ANISOU 4909  CB  THR A 672    13601  13456  10991    283  -1662   -518       C  
ATOM   4910  OG1 THR A 672     142.374  61.286   9.540  1.00101.78           O  
ANISOU 4910  OG1 THR A 672    13922  13739  11012    588  -1802   -446       O  
ATOM   4911  CG2 THR A 672     143.861  60.060   8.123  1.00 89.36           C  
ANISOU 4911  CG2 THR A 672    12422  12093   9438    302  -1609   -480       C  
ATOM   4912  N   ALA A 673     140.403  58.037   8.300  1.00 96.52           N  
ANISOU 4912  N   ALA A 673    12461  13876  10336    233  -1945  -1244       N  
ATOM   4913  CA  ALA A 673     139.060  58.093   7.734  1.00 96.83           C  
ANISOU 4913  CA  ALA A 673    12263  14395  10132    401  -2148  -1480       C  
ATOM   4914  C   ALA A 673     138.108  57.105   8.383  1.00104.35           C  
ANISOU 4914  C   ALA A 673    12844  15579  11226    123  -2144  -1780       C  
ATOM   4915  O   ALA A 673     136.931  57.421   8.570  1.00 83.13           O  
ANISOU 4915  O   ALA A 673     9888  13288   8409    265  -2299  -1935       O  
ATOM   4916  CB  ALA A 673     139.101  57.840   6.220  1.00 73.37           C  
ANISOU 4916  CB  ALA A 673     9356  11634   6889    479  -2215  -1593       C  
ATOM   4917  N   THR A 674     138.590  55.910   8.731  1.00122.81           N  
ANISOU 4917  N   THR A 674    15174  17685  13803   -265  -1953  -1870       N  
ATOM   4918  CA  THR A 674     137.786  54.954   9.479  1.00119.05           C  
ANISOU 4918  CA  THR A 674    14430  17329  13476   -593  -1884  -2127       C  
ATOM   4919  C   THR A 674     137.658  55.325  10.950  1.00116.73           C  
ANISOU 4919  C   THR A 674    14083  16880  13387   -600  -1830  -1987       C  
ATOM   4920  O   THR A 674     136.891  54.677  11.670  1.00120.93           O  
ANISOU 4920  O   THR A 674    14391  17535  14021   -855  -1766  -2183       O  
ATOM   4921  CB  THR A 674     138.385  53.551   9.352  1.00111.33           C  
ANISOU 4921  CB  THR A 674    13569  16077  12652   -973  -1667  -2248       C  
ATOM   4922  OG1 THR A 674     139.736  53.559   9.831  1.00106.45           O  
ANISOU 4922  OG1 THR A 674    13240  14981  12226   -948  -1507  -1955       O  
ATOM   4923  CG2 THR A 674     138.372  53.094   7.900  1.00113.98           C  
ANISOU 4923  CG2 THR A 674    13933  16607  12768   -998  -1718  -2445       C  
ATOM   4924  N   THR A 675     138.386  56.345  11.409  1.00112.92           N  
ANISOU 4924  N   THR A 675    13814  16138  12952   -354  -1838  -1669       N  
ATOM   4925  CA  THR A 675     138.317  56.787  12.792  1.00105.58           C  
ANISOU 4925  CA  THR A 675    12860  15063  12194   -336  -1797  -1534       C  
ATOM   4926  C   THR A 675     138.216  58.300  12.936  1.00102.65           C  
ANISOU 4926  C   THR A 675    12599  14719  11685     58  -1938  -1333       C  
ATOM   4927  O   THR A 675     138.154  58.791  14.068  1.00 91.17           O  
ANISOU 4927  O   THR A 675    11147  13146  10346    104  -1914  -1222       O  
ATOM   4928  CB  THR A 675     139.541  56.290  13.580  1.00 98.67           C  
ANISOU 4928  CB  THR A 675    12188  13725  11577   -529  -1590  -1350       C  
ATOM   4929  OG1 THR A 675     139.282  56.392  14.986  1.00106.97           O  
ANISOU 4929  OG1 THR A 675    13163  14690  12791   -585  -1536  -1295       O  
ATOM   4930  CG2 THR A 675     140.767  57.125  13.242  1.00 81.99           C  
ANISOU 4930  CG2 THR A 675    10360  11361   9431   -350  -1582  -1075       C  
ATOM   4931  N   GLY A 676     138.194  59.049  11.829  1.00127.01           N  
ANISOU 4931  N   GLY A 676    15818  17935  14506    354  -2072  -1282       N  
ATOM   4932  CA  GLY A 676     138.125  60.499  11.923  1.00131.43           C  
ANISOU 4932  CA  GLY A 676    16588  18450  14901    747  -2175  -1077       C  
ATOM   4933  C   GLY A 676     136.860  60.999  12.590  1.00132.10           C  
ANISOU 4933  C   GLY A 676    16435  18855  14901    979  -2307  -1184       C  
ATOM   4934  O   GLY A 676     136.852  62.082  13.181  1.00132.33           O  
ANISOU 4934  O   GLY A 676    16651  18740  14886   1244  -2335  -1008       O  
ATOM   4935  N   ARG A 677     135.775  60.227  12.505  1.00118.30           N  
ANISOU 4935  N   ARG A 677    14274  17562  13114    870  -2376  -1491       N  
ATOM   4936  CA  ARG A 677     134.540  60.587  13.191  1.00101.63           C  
ANISOU 4936  CA  ARG A 677    11854  15837  10923   1057  -2484  -1633       C  
ATOM   4937  C   ARG A 677     134.543  60.126  14.644  1.00108.43           C  
ANISOU 4937  C   ARG A 677    12592  16521  12087    748  -2325  -1637       C  
ATOM   4938  O   ARG A 677     133.981  60.810  15.507  1.00104.22           O  
ANISOU 4938  O   ARG A 677    11982  16080  11535    959  -2366  -1605       O  
ATOM   4939  CB  ARG A 677     133.341  59.992  12.451  1.00104.63           C  
ANISOU 4939  CB  ARG A 677    11793  16870  11092   1046  -2623  -1998       C  
ATOM   4940  CG  ARG A 677     131.983  60.392  13.005  1.00114.26           C  
ANISOU 4940  CG  ARG A 677    12618  18632  12164   1285  -2753  -2187       C  
ATOM   4941  CD  ARG A 677     130.872  59.617  12.309  1.00133.57           C  
ANISOU 4941  CD  ARG A 677    14555  21777  14419   1147  -2864  -2605       C  
ATOM   4942  NE  ARG A 677     129.547  59.949  12.825  1.00145.02           N  
ANISOU 4942  NE  ARG A 677    15546  23847  15706   1362  -2983  -2826       N  
ATOM   4943  CZ  ARG A 677     128.675  60.735  12.201  1.00157.94           C  
ANISOU 4943  CZ  ARG A 677    17069  25903  17039   1885  -3118  -2856       C  
ATOM   4944  NH1 ARG A 677     128.983  61.272  11.028  1.00163.99           N  
ANISOU 4944  NH1 ARG A 677    18115  26629  17567   2257  -3236  -2726       N  
ATOM   4945  NH2 ARG A 677     127.492  60.980  12.746  1.00161.14           N  
ANISOU 4945  NH2 ARG A 677    17107  26738  17381   2039  -3092  -3007       N  
ATOM   4946  N   LEU A 678     135.165  58.980  14.932  1.00109.35           N  
ANISOU 4946  N   LEU A 678    12715  16376  12457    284  -2137  -1672       N  
ATOM   4947  CA  LEU A 678     135.239  58.497  16.307  1.00104.50           C  
ANISOU 4947  CA  LEU A 678    12042  15560  12104      8  -1970  -1650       C  
ATOM   4948  C   LEU A 678     136.104  59.413  17.162  1.00 86.85           C  
ANISOU 4948  C   LEU A 678    10114  12909   9975    176  -1929  -1337       C  
ATOM   4949  O   LEU A 678     135.679  59.868  18.230  1.00 84.41           O  
ANISOU 4949  O   LEU A 678     9734  12623   9714    261  -1923  -1305       O  
ATOM   4950  CB  LEU A 678     135.786  57.070  16.338  1.00114.16           C  
ANISOU 4950  CB  LEU A 678    13296  16552  13527   -459  -1768  -1733       C  
ATOM   4951  CG  LEU A 678     135.019  56.003  15.558  1.00132.41           C  
ANISOU 4951  CG  LEU A 678    15354  19202  15754   -743  -1755  -2077       C  
ATOM   4952  CD1 LEU A 678     135.701  54.652  15.704  1.00141.93           C  
ANISOU 4952  CD1 LEU A 678    16724  20044  17158  -1170  -1514  -2112       C  
ATOM   4953  CD2 LEU A 678     133.575  55.937  16.023  1.00134.52           C  
ANISOU 4953  CD2 LEU A 678    15197  19977  15937   -817  -1801  -2351       C  
ATOM   4954  N   ILE A 679     137.328  59.689  16.706  1.00 83.27           N  
ANISOU 4954  N   ILE A 679     9994  12097   9548    203  -1890  -1123       N  
ATOM   4955  CA  ILE A 679     138.228  60.568  17.445  1.00 83.87           C  
ANISOU 4955  CA  ILE A 679    10358  11804   9705    301  -1842   -857       C  
ATOM   4956  C   ILE A 679     137.625  61.958  17.593  1.00 77.57           C  
ANISOU 4956  C   ILE A 679     9660  11099   8715    703  -1979   -785       C  
ATOM   4957  O   ILE A 679     137.841  62.635  18.606  1.00 67.28           O  
ANISOU 4957  O   ILE A 679     8489   9595   7479    767  -1943   -657       O  
ATOM   4958  CB  ILE A 679     139.600  60.609  16.746  1.00 79.21           C  
ANISOU 4958  CB  ILE A 679    10060  10907   9131    229  -1771   -687       C  
ATOM   4959  CG1 ILE A 679     140.168  59.195  16.636  1.00 72.51           C  
ANISOU 4959  CG1 ILE A 679     9129   9971   8450   -102  -1630   -766       C  
ATOM   4960  CG2 ILE A 679     140.565  61.518  17.492  1.00 79.08           C  
ANISOU 4960  CG2 ILE A 679    10313  10555   9178    261  -1709   -453       C  
ATOM   4961  CD1 ILE A 679     141.574  59.155  16.109  1.00 76.75           C  
ANISOU 4961  CD1 ILE A 679     9898  10249   9014   -170  -1539   -610       C  
ATOM   4962  N   THR A 680     136.853  62.403  16.598  1.00 85.00           N  
ANISOU 4962  N   THR A 680    10558  12350   9388   1008  -2136   -872       N  
ATOM   4963  CA  THR A 680     136.157  63.681  16.711  1.00 93.95           C  
ANISOU 4963  CA  THR A 680    11806  13598  10293   1475  -2267   -816       C  
ATOM   4964  C   THR A 680     135.081  63.627  17.789  1.00105.24           C  
ANISOU 4964  C   THR A 680    12906  15316  11765   1532  -2294   -966       C  
ATOM   4965  O   THR A 680     134.960  64.552  18.603  1.00113.90           O  
ANISOU 4965  O   THR A 680    14162  16282  12832   1765  -2299   -857       O  
ATOM   4966  CB  THR A 680     135.544  64.066  15.362  1.00 83.16           C  
ANISOU 4966  CB  THR A 680    10453  12557   8588   1842  -2439   -885       C  
ATOM   4967  OG1 THR A 680     136.576  64.164  14.373  1.00 79.06           O  
ANISOU 4967  OG1 THR A 680    10273  11753   8014   1785  -2391   -731       O  
ATOM   4968  CG2 THR A 680     134.814  65.396  15.463  1.00 67.29           C  
ANISOU 4968  CG2 THR A 680     8614  10655   6297   2412  -2571   -814       C  
ATOM   4969  N   GLY A 681     134.293  62.552  17.811  1.00102.26           N  
ANISOU 4969  N   GLY A 681    12082  15329  11444   1297  -2292  -1229       N  
ATOM   4970  CA  GLY A 681     133.271  62.364  18.820  1.00106.54           C  
ANISOU 4970  CA  GLY A 681    12267  16186  12026   1270  -2280  -1398       C  
ATOM   4971  C   GLY A 681     133.823  62.040  20.194  1.00101.10           C  
ANISOU 4971  C   GLY A 681    11648  15141  11623    966  -2096  -1292       C  
ATOM   4972  O   GLY A 681     133.280  62.497  21.203  1.00 83.18           O  
ANISOU 4972  O   GLY A 681     9292  12958   9356   1098  -2088  -1300       O  
ATOM   4973  N   ALA A 682     134.905  61.256  20.246  1.00 96.31           N  
ANISOU 4973  N   ALA A 682    11203  14157  11233    596  -1949  -1195       N  
ATOM   4974  CA  ALA A 682     135.533  60.942  21.524  1.00 88.64           C  
ANISOU 4974  CA  ALA A 682    10327  12856  10498    355  -1785  -1076       C  
ATOM   4975  C   ALA A 682     136.122  62.175  22.197  1.00 92.60           C  
ANISOU 4975  C   ALA A 682    11139  13058  10987    599  -1808   -849       C  
ATOM   4976  O   ALA A 682     136.318  62.171  23.418  1.00 69.95           O  
ANISOU 4976  O   ALA A 682     8293  10036   8249    500  -1715   -786       O  
ATOM   4977  CB  ALA A 682     136.622  59.886  21.328  1.00 77.93           C  
ANISOU 4977  CB  ALA A 682     9099  11189   9323      1  -1640  -1014       C  
ATOM   4978  N   ALA A 683     136.413  63.225  21.430  1.00 99.02           N  
ANISOU 4978  N   ALA A 683    12225  13774  11626    900  -1916   -731       N  
ATOM   4979  CA  ALA A 683     136.968  64.451  21.984  1.00 96.83           C  
ANISOU 4979  CA  ALA A 683    12307  13177  11307   1093  -1915   -538       C  
ATOM   4980  C   ALA A 683     135.888  65.397  22.491  1.00 99.03           C  
ANISOU 4980  C   ALA A 683    12560  13652  11413   1490  -2009   -588       C  
ATOM   4981  O   ALA A 683     136.090  66.070  23.506  1.00 95.66           O  
ANISOU 4981  O   ALA A 683    12313  13012  11021   1551  -1963   -499       O  
ATOM   4982  CB  ALA A 683     137.831  65.156  20.935  1.00101.66           C  
ANISOU 4982  CB  ALA A 683    13303  13532  11791   1195  -1939   -381       C  
ATOM   4983  N   LEU A 684     134.741  65.463  21.808  1.00 98.13           N  
ANISOU 4983  N   LEU A 684    12216  13976  11093   1782  -2142   -746       N  
ATOM   4984  CA  LEU A 684     133.670  66.351  22.252  1.00 94.87           C  
ANISOU 4984  CA  LEU A 684    11750  13819  10479   2235  -2238   -809       C  
ATOM   4985  C   LEU A 684     133.128  65.937  23.615  1.00103.50           C  
ANISOU 4985  C   LEU A 684    12538  15064  11722   2074  -2152   -918       C  
ATOM   4986  O   LEU A 684     132.824  66.793  24.455  1.00107.51           O  
ANISOU 4986  O   LEU A 684    13172  15517  12159   2344  -2155   -876       O  
ATOM   4987  CB  LEU A 684     132.542  66.379  21.220  1.00 90.87           C  
ANISOU 4987  CB  LEU A 684    10971  13861   9695   2589  -2410   -989       C  
ATOM   4988  CG  LEU A 684     132.707  67.332  20.037  1.00 96.13           C  
ANISOU 4988  CG  LEU A 684    12030  14429  10066   3031  -2532   -859       C  
ATOM   4989  CD1 LEU A 684     131.408  67.425  19.251  1.00 91.46           C  
ANISOU 4989  CD1 LEU A 684    11105  14492   9152   3482  -2728  -1064       C  
ATOM   4990  CD2 LEU A 684     133.151  68.706  20.512  1.00100.98           C  
ANISOU 4990  CD2 LEU A 684    13217  14573  10577   3351  -2497   -631       C  
ATOM   4991  N   ILE A 685     132.997  64.629  23.851  1.00107.19           N  
ANISOU 4991  N   ILE A 685    12644  15702  12380   1636  -2056  -1058       N  
ATOM   4992  CA  ILE A 685     132.471  64.144  25.126  1.00102.55           C  
ANISOU 4992  CA  ILE A 685    11788  15258  11920   1443  -1940  -1159       C  
ATOM   4993  C   ILE A 685     133.366  64.593  26.273  1.00 89.39           C  
ANISOU 4993  C   ILE A 685    10450  13119  10395   1373  -1838   -956       C  
ATOM   4994  O   ILE A 685     132.903  65.191  27.251  1.00 83.57           O  
ANISOU 4994  O   ILE A 685     9710  12433   9611   1562  -1825   -962       O  
ATOM   4995  CB  ILE A 685     132.323  62.613  25.098  1.00100.93           C  
ANISOU 4995  CB  ILE A 685    11259  15210  11882    934  -1811  -1321       C  
ATOM   4996  CG1 ILE A 685     131.362  62.191  23.986  1.00109.80           C  
ANISOU 4996  CG1 ILE A 685    12018  16862  12837    965  -1916  -1575       C  
ATOM   4997  CG2 ILE A 685     131.853  62.097  26.450  1.00 95.11           C  
ANISOU 4997  CG2 ILE A 685    10314  14561  11262    702  -1650  -1397       C  
ATOM   4998  CD1 ILE A 685     131.237  60.695  23.831  1.00116.51           C  
ANISOU 4998  CD1 ILE A 685    12619  17822  13829    422  -1769  -1759       C  
ATOM   4999  N   LEU A 686     134.665  64.310  26.166  1.00 85.64           N  
ANISOU 4999  N   LEU A 686    10246  12219  10076   1109  -1767   -790       N  
ATOM   5000  CA  LEU A 686     135.621  64.745  27.175  1.00 83.41           C  
ANISOU 5000  CA  LEU A 686    10255  11537   9900   1027  -1687   -618       C  
ATOM   5001  C   LEU A 686     135.741  66.263  27.237  1.00 91.89           C  
ANISOU 5001  C   LEU A 686    11694  12415  10805   1392  -1767   -513       C  
ATOM   5002  O   LEU A 686     136.135  66.799  28.277  1.00 96.66           O  
ANISOU 5002  O   LEU A 686    12488  12794  11445   1384  -1713   -437       O  
ATOM   5003  CB  LEU A 686     136.980  64.109  26.888  1.00 80.95           C  
ANISOU 5003  CB  LEU A 686    10099  10910   9748    699  -1608   -493       C  
ATOM   5004  CG  LEU A 686     138.114  64.281  27.891  1.00 95.06           C  
ANISOU 5004  CG  LEU A 686    12102  12365  11650    538  -1522   -346       C  
ATOM   5005  CD1 LEU A 686     137.728  63.717  29.245  1.00106.07           C  
ANISOU 5005  CD1 LEU A 686    13321  13843  13140    422  -1424   -391       C  
ATOM   5006  CD2 LEU A 686     139.335  63.580  27.352  1.00 91.89           C  
ANISOU 5006  CD2 LEU A 686    11775  11778  11360    281  -1464   -260       C  
ATOM   5007  N   ALA A 687     135.401  66.963  26.152  1.00 99.50           N  
ANISOU 5007  N   ALA A 687    12796  13447  11562   1719  -1884   -511       N  
ATOM   5008  CA  ALA A 687     135.416  68.421  26.160  1.00 97.53           C  
ANISOU 5008  CA  ALA A 687    12976  12972  11108   2106  -1935   -411       C  
ATOM   5009  C   ALA A 687     134.188  68.998  26.851  1.00 93.98           C  
ANISOU 5009  C   ALA A 687    12404  12801  10504   2509  -1988   -521       C  
ATOM   5010  O   ALA A 687     134.283  70.046  27.500  1.00 88.73           O  
ANISOU 5010  O   ALA A 687    12090  11880   9743   2731  -1967   -449       O  
ATOM   5011  CB  ALA A 687     135.512  68.953  24.729  1.00 95.88           C  
ANISOU 5011  CB  ALA A 687    13025  12710  10694   2352  -2024   -346       C  
ATOM   5012  N   VAL A 688     133.035  68.338  26.720  1.00 90.77           N  
ANISOU 5012  N   VAL A 688    11502  12933  10055   2597  -2044   -714       N  
ATOM   5013  CA  VAL A 688     131.819  68.821  27.369  1.00 85.99           C  
ANISOU 5013  CA  VAL A 688    10695  12690   9285   2988  -2087   -847       C  
ATOM   5014  C   VAL A 688     131.972  68.780  28.884  1.00 95.34           C  
ANISOU 5014  C   VAL A 688    11874  13728  10622   2796  -1957   -835       C  
ATOM   5015  O   VAL A 688     131.682  69.760  29.582  1.00 91.89           O  
ANISOU 5015  O   VAL A 688    11656  13204  10052   3135  -1960   -815       O  
ATOM   5016  CB  VAL A 688     130.600  68.003  26.904  1.00 82.70           C  
ANISOU 5016  CB  VAL A 688     9669  12958   8794   3022  -2156  -1097       C  
ATOM   5017  CG1 VAL A 688     129.426  68.230  27.838  1.00 88.24           C  
ANISOU 5017  CG1 VAL A 688    10046  14095   9385   3281  -2149  -1264       C  
ATOM   5018  CG2 VAL A 688     130.223  68.382  25.488  1.00 85.82           C  
ANISOU 5018  CG2 VAL A 688    10095  13582   8930   3407  -2327  -1127       C  
ATOM   5019  N   VAL A 689     132.431  67.645  29.417  1.00109.82           N  
ANISOU 5019  N   VAL A 689    13491  15521  12713   2274  -1835   -845       N  
ATOM   5020  CA  VAL A 689     132.601  67.532  30.863  1.00111.91           C  
ANISOU 5020  CA  VAL A 689    13754  15665  13100   2095  -1710   -825       C  
ATOM   5021  C   VAL A 689     133.709  68.457  31.349  1.00102.15           C  
ANISOU 5021  C   VAL A 689    13039  13895  11877   2109  -1689   -645       C  
ATOM   5022  O   VAL A 689     133.654  68.960  32.478  1.00 91.30           O  
ANISOU 5022  O   VAL A 689    11781  12428  10482   2186  -1637   -640       O  
ATOM   5023  CB  VAL A 689     132.863  66.068  31.265  1.00102.26           C  
ANISOU 5023  CB  VAL A 689    12247  14497  12112   1570  -1571   -859       C  
ATOM   5024  CG1 VAL A 689     131.669  65.201  30.902  1.00101.38           C  
ANISOU 5024  CG1 VAL A 689    11631  14924  11966   1494  -1556  -1082       C  
ATOM   5025  CG2 VAL A 689     134.126  65.543  30.602  1.00102.99           C  
ANISOU 5025  CG2 VAL A 689    12537  14244  12353   1262  -1554   -723       C  
ATOM   5026  N   ALA A 690     134.724  68.704  30.517  1.00 96.11           N  
ANISOU 5026  N   ALA A 690    12593  12795  11132   2010  -1718   -514       N  
ATOM   5027  CA  ALA A 690     135.727  69.703  30.864  1.00 85.01           C  
ANISOU 5027  CA  ALA A 690    11688  10916   9694   1998  -1689   -379       C  
ATOM   5028  C   ALA A 690     135.128  71.103  30.849  1.00 87.00           C  
ANISOU 5028  C   ALA A 690    12295  11074   9686   2500  -1744   -382       C  
ATOM   5029  O   ALA A 690     135.440  71.928  31.715  1.00 74.91           O  
ANISOU 5029  O   ALA A 690    11094   9264   8105   2546  -1692   -352       O  
ATOM   5030  CB  ALA A 690     136.917  69.612  29.910  1.00 88.58           C  
ANISOU 5030  CB  ALA A 690    12364  11085  10207   1745  -1682   -259       C  
ATOM   5031  N   GLY A 691     134.254  71.381  29.881  1.00 94.88           N  
ANISOU 5031  N   GLY A 691    13246  12313  10490   2905  -1848   -429       N  
ATOM   5032  CA  GLY A 691     133.580  72.663  29.799  1.00 95.06           C  
ANISOU 5032  CA  GLY A 691    13620  12280  10220   3487  -1903   -429       C  
ATOM   5033  C   GLY A 691     132.617  72.944  30.933  1.00103.47           C  
ANISOU 5033  C   GLY A 691    14515  13593  11206   3774  -1890   -551       C  
ATOM   5034  O   GLY A 691     132.132  74.075  31.043  1.00108.25           O  
ANISOU 5034  O   GLY A 691    15476  14097  11558   4286  -1916   -548       O  
ATOM   5035  N   ALA A 692     132.320  71.947  31.765  1.00 99.64           N  
ANISOU 5035  N   ALA A 692    13528  13420  10909   3476  -1835   -655       N  
ATOM   5036  CA  ALA A 692     131.497  72.163  32.946  1.00107.63           C  
ANISOU 5036  CA  ALA A 692    14374  14664  11859   3683  -1792   -769       C  
ATOM   5037  C   ALA A 692     132.315  72.553  34.167  1.00114.62           C  
ANISOU 5037  C   ALA A 692    15586  15128  12835   3455  -1682   -698       C  
ATOM   5038  O   ALA A 692     131.780  73.198  35.076  1.00122.38           O  
ANISOU 5038  O   ALA A 692    16662  16147  13692   3741  -1650   -763       O  
ATOM   5039  CB  ALA A 692     130.679  70.907  33.259  1.00115.22           C  
ANISOU 5039  CB  ALA A 692    14646  16192  12939   3461  -1755   -931       C  
ATOM   5040  N   PHE A 693     133.593  72.179  34.209  1.00109.29           N  
ANISOU 5040  N   PHE A 693    15070  14100  12356   2965  -1629   -584       N  
ATOM   5041  CA  PHE A 693     134.479  72.562  35.298  1.00104.60           C  
ANISOU 5041  CA  PHE A 693    14774  13147  11823   2726  -1544   -535       C  
ATOM   5042  C   PHE A 693     135.211  73.872  35.037  1.00101.31           C  
ANISOU 5042  C   PHE A 693    15018  12215  11260   2827  -1539   -455       C  
ATOM   5043  O   PHE A 693     135.850  74.398  35.955  1.00 92.06           O  
ANISOU 5043  O   PHE A 693    14137  10756  10084   2665  -1471   -455       O  
ATOM   5044  CB  PHE A 693     135.503  71.453  35.568  1.00106.93           C  
ANISOU 5044  CB  PHE A 693    14863  13393  12371   2163  -1487   -474       C  
ATOM   5045  CG  PHE A 693     134.924  70.234  36.233  1.00103.98           C  
ANISOU 5045  CG  PHE A 693    13981  13400  12128   1999  -1427   -544       C  
ATOM   5046  CD1 PHE A 693     134.202  69.305  35.504  1.00105.58           C  
ANISOU 5046  CD1 PHE A 693    13775  13957  12382   1976  -1442   -607       C  
ATOM   5047  CD2 PHE A 693     135.116  70.010  37.585  1.00 94.55           C  
ANISOU 5047  CD2 PHE A 693    12745  12199  10982   1842  -1340   -554       C  
ATOM   5048  CE1 PHE A 693     133.676  68.180  36.111  1.00 92.41           C  
ANISOU 5048  CE1 PHE A 693    11698  12596  10818   1764  -1344   -680       C  
ATOM   5049  CE2 PHE A 693     134.594  68.887  38.196  1.00 96.71           C  
ANISOU 5049  CE2 PHE A 693    12617  12778  11349   1676  -1249   -602       C  
ATOM   5050  CZ  PHE A 693     133.871  67.973  37.457  1.00 88.83           C  
ANISOU 5050  CZ  PHE A 693    11246  12096  10408   1619  -1238   -666       C  
ATOM   5051  N   VAL A 694     135.141  74.411  33.815  1.00101.93           N  
ANISOU 5051  N   VAL A 694    15365  12167  11199   3069  -1595   -395       N  
ATOM   5052  CA  VAL A 694     135.715  75.726  33.549  1.00107.99           C  
ANISOU 5052  CA  VAL A 694    16843  12407  11782   3186  -1551   -321       C  
ATOM   5053  C   VAL A 694     134.887  76.847  34.150  1.00 99.88           C  
ANISOU 5053  C   VAL A 694    16168  11283  10498   3718  -1536   -384       C  
ATOM   5054  O   VAL A 694     135.331  77.999  34.156  1.00107.84           O  
ANISOU 5054  O   VAL A 694    17849  11791  11334   3804  -1462   -341       O  
ATOM   5055  CB  VAL A 694     135.881  75.989  32.037  1.00113.57           C  
ANISOU 5055  CB  VAL A 694    17800  12976  12374   3317  -1593   -217       C  
ATOM   5056  CG1 VAL A 694     136.680  74.879  31.380  1.00115.67           C  
ANISOU 5056  CG1 VAL A 694    17724  13348  12875   2826  -1603   -164       C  
ATOM   5057  CG2 VAL A 694     134.527  76.161  31.369  1.00108.38           C  
ANISOU 5057  CG2 VAL A 694    17012  12670  11497   3962  -1707   -259       C  
ATOM   5058  N   PHE A 695     133.687  76.543  34.640  1.00 96.41           N  
ANISOU 5058  N   PHE A 695    15310  11311  10011   4074  -1586   -496       N  
ATOM   5059  CA  PHE A 695     132.857  77.504  35.350  1.00101.55           C  
ANISOU 5059  CA  PHE A 695    16220  11945  10420   4606  -1565   -578       C  
ATOM   5060  C   PHE A 695     132.965  77.353  36.860  1.00106.59           C  
ANISOU 5060  C   PHE A 695    16728  12610  11161   4375  -1483   -667       C  
ATOM   5061  O   PHE A 695     132.174  77.957  37.592  1.00110.78           O  
ANISOU 5061  O   PHE A 695    17350  13229  11513   4800  -1460   -762       O  
ATOM   5062  CB  PHE A 695     131.397  77.366  34.914  1.00103.39           C  
ANISOU 5062  CB  PHE A 695    16054  12754  10477   5214  -1671   -670       C  
ATOM   5063  CG  PHE A 695     131.162  77.702  33.470  1.00101.73           C  
ANISOU 5063  CG  PHE A 695    16035  12542  10077   5586  -1768   -594       C  
ATOM   5064  CD1 PHE A 695     130.942  79.012  33.078  1.00107.17           C  
ANISOU 5064  CD1 PHE A 695    17411  12881  10430   6174  -1764   -531       C  
ATOM   5065  CD2 PHE A 695     131.154  76.709  32.507  1.00 96.37           C  
ANISOU 5065  CD2 PHE A 695    14893  12196   9529   5367  -1854   -583       C  
ATOM   5066  CE1 PHE A 695     130.724  79.327  31.750  1.00104.30           C  
ANISOU 5066  CE1 PHE A 695    17261  12515   9851   6559  -1851   -444       C  
ATOM   5067  CE2 PHE A 695     130.935  77.017  31.178  1.00 91.79           C  
ANISOU 5067  CE2 PHE A 695    14489  11641   8747   5725  -1951   -517       C  
ATOM   5068  CZ  PHE A 695     130.720  78.327  30.799  1.00 93.13           C  
ANISOU 5068  CZ  PHE A 695    15338  11477   8569   6333  -1953   -438       C  
ATOM   5069  N   SER A 696     133.922  76.563  37.339  1.00107.27           N  
ANISOU 5069  N   SER A 696    16609  12642  11506   3750  -1439   -639       N  
ATOM   5070  CA  SER A 696     134.076  76.348  38.770  1.00117.21           C  
ANISOU 5070  CA  SER A 696    17740  13952  12844   3529  -1368   -713       C  
ATOM   5071  C   SER A 696     134.573  77.614  39.452  1.00109.39           C  
ANISOU 5071  C   SER A 696    17407  12469  11686   3580  -1295   -743       C  
ATOM   5072  O   SER A 696     135.459  78.307  38.944  1.00102.82           O  
ANISOU 5072  O   SER A 696    17094  11169  10805   3405  -1264   -683       O  
ATOM   5073  CB  SER A 696     135.054  75.205  39.034  1.00116.09           C  
ANISOU 5073  CB  SER A 696    17265  13868  12975   2906  -1347   -660       C  
ATOM   5074  OG  SER A 696     136.375  75.582  38.692  1.00121.92           O  
ANISOU 5074  OG  SER A 696    18388  14181  13755   2542  -1330   -585       O  
ATOM   5075  N   ASP A 697     133.994  77.913  40.617  1.00108.80           N  
ANISOU 5075  N   ASP A 697    17322  12504  11512   3792  -1248   -854       N  
ATOM   5076  CA  ASP A 697     134.482  79.028  41.418  1.00 97.63           C  
ANISOU 5076  CA  ASP A 697    16516  10636   9943   3781  -1167   -917       C  
ATOM   5077  C   ASP A 697     135.931  78.830  41.843  1.00 84.56           C  
ANISOU 5077  C   ASP A 697    14966   8726   8439   3106  -1130   -902       C  
ATOM   5078  O   ASP A 697     136.619  79.813  42.138  1.00 74.59           O  
ANISOU 5078  O   ASP A 697    14283   7007   7049   2960  -1060   -955       O  
ATOM   5079  CB  ASP A 697     133.591  79.220  42.646  1.00 98.32           C  
ANISOU 5079  CB  ASP A 697    16491  10961   9907   4110  -1123  -1049       C  
ATOM   5080  CG  ASP A 697     132.203  79.713  42.287  1.00100.49           C  
ANISOU 5080  CG  ASP A 697    16760  11466   9954   4854  -1149  -1097       C  
ATOM   5081  OD1 ASP A 697     131.943  79.944  41.087  1.00102.18           O  
ANISOU 5081  OD1 ASP A 697    17094  11641  10090   5136  -1212  -1024       O  
ATOM   5082  OD2 ASP A 697     131.371  79.871  43.206  1.00102.99           O  
ANISOU 5082  OD2 ASP A 697    16944  12039  10148   5182  -1108  -1214       O  
ATOM   5083  N   LEU A 698     136.408  77.588  41.872  1.00 83.32           N  
ANISOU 5083  N   LEU A 698    14271   8865   8524   2699  -1168   -847       N  
ATOM   5084  CA  LEU A 698     137.800  77.297  42.189  1.00 89.20           C  
ANISOU 5084  CA  LEU A 698    15031   9467   9392   2109  -1154   -834       C  
ATOM   5085  C   LEU A 698     138.653  77.522  40.945  1.00 78.87           C  
ANISOU 5085  C   LEU A 698    13971   7875   8122   1869  -1160   -746       C  
ATOM   5086  O   LEU A 698     138.393  76.927  39.894  1.00 82.86           O  
ANISOU 5086  O   LEU A 698    14232   8530   8722   1948  -1212   -647       O  
ATOM   5087  CB  LEU A 698     137.935  75.863  42.697  1.00 85.21           C  
ANISOU 5087  CB  LEU A 698    13899   9384   9091   1856  -1180   -795       C  
ATOM   5088  CG  LEU A 698     139.312  75.406  43.178  1.00 74.53           C  
ANISOU 5088  CG  LEU A 698    12467   8011   7839   1333  -1183   -786       C  
ATOM   5089  CD1 LEU A 698     139.801  76.279  44.323  1.00 72.91           C  
ANISOU 5089  CD1 LEU A 698    12605   7621   7475   1214  -1144   -922       C  
ATOM   5090  CD2 LEU A 698     139.258  73.945  43.595  1.00 74.85           C  
ANISOU 5090  CD2 LEU A 698    11948   8447   8044   1210  -1193   -719       C  
ATOM   5091  N   VAL A 699     139.674  78.374  41.066  1.00 90.23           N  
ANISOU 5091  N   VAL A 699    15891   8919   9473   1546  -1096   -799       N  
ATOM   5092  CA  VAL A 699     140.410  78.822  39.887  1.00 91.24           C  
ANISOU 5092  CA  VAL A 699    16366   8721   9580   1335  -1059   -729       C  
ATOM   5093  C   VAL A 699     141.317  77.717  39.356  1.00 81.72           C  
ANISOU 5093  C   VAL A 699    14697   7755   8596    908  -1106   -649       C  
ATOM   5094  O   VAL A 699     141.506  77.585  38.141  1.00 84.28           O  
ANISOU 5094  O   VAL A 699    15053   8011   8959    879  -1111   -546       O  
ATOM   5095  CB  VAL A 699     141.198  80.109  40.202  1.00 87.56           C  
ANISOU 5095  CB  VAL A 699    16588   7753   8928   1063   -936   -841       C  
ATOM   5096  CG1 VAL A 699     142.287  79.847  41.234  1.00 78.94           C  
ANISOU 5096  CG1 VAL A 699    15303   6790   7900    515   -930   -967       C  
ATOM   5097  CG2 VAL A 699     141.791  80.695  38.930  1.00 91.67           C  
ANISOU 5097  CG2 VAL A 699    17561   7890   9379    890   -854   -762       C  
ATOM   5098  N   MET A 700     141.887  76.904  40.244  1.00 82.99           N  
ANISOU 5098  N   MET A 700    14443   8207   8883    611  -1139   -690       N  
ATOM   5099  CA  MET A 700     142.772  75.838  39.796  1.00 83.68           C  
ANISOU 5099  CA  MET A 700    14112   8530   9154    265  -1178   -616       C  
ATOM   5100  C   MET A 700     142.019  74.668  39.180  1.00 76.45           C  
ANISOU 5100  C   MET A 700    12736   7916   8395    498  -1240   -498       C  
ATOM   5101  O   MET A 700     142.654  73.781  38.601  1.00 69.92           O  
ANISOU 5101  O   MET A 700    11617   7240   7709    274  -1263   -425       O  
ATOM   5102  CB  MET A 700     143.644  75.349  40.955  1.00 85.64           C  
ANISOU 5102  CB  MET A 700    14095   9005   9437    -63  -1196   -694       C  
ATOM   5103  CG  MET A 700     144.450  76.454  41.619  1.00 86.21           C  
ANISOU 5103  CG  MET A 700    14571   8843   9341   -367  -1138   -858       C  
ATOM   5104  SD  MET A 700     145.208  77.596  40.444  1.00 74.66           S  
ANISOU 5104  SD  MET A 700    13673   6923   7772   -670  -1029   -883       S  
ATOM   5105  CE  MET A 700     146.405  76.532  39.645  1.00 75.12           C  
ANISOU 5105  CE  MET A 700    13255   7287   8001  -1060  -1065   -805       C  
ATOM   5106  N   MET A 701     140.691  74.638  39.296  1.00 76.66           N  
ANISOU 5106  N   MET A 701    12683   8058   8385    927  -1259   -500       N  
ATOM   5107  CA  MET A 701     139.909  73.699  38.502  1.00 85.48           C  
ANISOU 5107  CA  MET A 701    13421   9445   9614   1119  -1305   -425       C  
ATOM   5108  C   MET A 701     139.639  74.259  37.109  1.00 91.21           C  
ANISOU 5108  C   MET A 701    14405   9992  10259   1319  -1326   -369       C  
ATOM   5109  O   MET A 701     139.601  73.504  36.130  1.00 71.10           O  
ANISOU 5109  O   MET A 701    11607   7594   7814   1288  -1365   -301       O  
ATOM   5110  CB  MET A 701     138.600  73.362  39.217  1.00 83.40           C  
ANISOU 5110  CB  MET A 701    12887   9474   9328   1452  -1307   -480       C  
ATOM   5111  CG  MET A 701     137.651  72.494  38.401  1.00 84.97           C  
ANISOU 5111  CG  MET A 701    12694   9988   9605   1634  -1342   -454       C  
ATOM   5112  SD  MET A 701     138.387  70.926  37.909  1.00 53.76           S  
ANISOU 5112  SD  MET A 701     8333   6203   5891   1229  -1338   -366       S  
ATOM   5113  CE  MET A 701     138.251  70.015  39.440  1.00 79.36           C  
ANISOU 5113  CE  MET A 701    11274   9679   9201   1098  -1262   -392       C  
ATOM   5114  N   LYS A 702     139.450  75.578  37.005  1.00 95.83           N  
ANISOU 5114  N   LYS A 702    15531  10243  10638   1540  -1293   -397       N  
ATOM   5115  CA  LYS A 702     139.415  76.225  35.697  1.00 88.73           C  
ANISOU 5115  CA  LYS A 702    15002   9095   9618   1706  -1291   -322       C  
ATOM   5116  C   LYS A 702     140.710  75.985  34.936  1.00 81.41           C  
ANISOU 5116  C   LYS A 702    14124   8022   8787   1231  -1254   -253       C  
ATOM   5117  O   LYS A 702     140.694  75.740  33.725  1.00 73.52           O  
ANISOU 5117  O   LYS A 702    13101   7039   7795   1284  -1280   -166       O  
ATOM   5118  CB  LYS A 702     139.178  77.726  35.858  1.00 95.14           C  
ANISOU 5118  CB  LYS A 702    16505   9478  10165   1981  -1219   -358       C  
ATOM   5119  CG  LYS A 702     137.778  78.128  36.273  1.00 93.48           C  
ANISOU 5119  CG  LYS A 702    16316   9409   9794   2598  -1257   -415       C  
ATOM   5120  CD  LYS A 702     137.705  79.636  36.437  1.00 89.43           C  
ANISOU 5120  CD  LYS A 702    16588   8390   9000   2862  -1162   -445       C  
ATOM   5121  CE  LYS A 702     136.310  80.160  36.173  1.00103.56           C  
ANISOU 5121  CE  LYS A 702    18507  10285  10555   3631  -1211   -451       C  
ATOM   5122  NZ  LYS A 702     135.289  79.481  37.010  1.00121.89           N  
ANISOU 5122  NZ  LYS A 702    20222  13149  12942   3887  -1283   -550       N  
ATOM   5123  N   TYR A 703     141.844  76.058  35.635  1.00 91.30           N  
ANISOU 5123  N   TYR A 703    15426   9173  10091    770  -1195   -305       N  
ATOM   5124  CA  TYR A 703     143.137  75.819  35.005  1.00 78.67           C  
ANISOU 5124  CA  TYR A 703    13811   7513   8568    299  -1152   -268       C  
ATOM   5125  C   TYR A 703     143.235  74.397  34.465  1.00 87.33           C  
ANISOU 5125  C   TYR A 703    14336   8977   9870    232  -1224   -194       C  
ATOM   5126  O   TYR A 703     143.718  74.180  33.348  1.00 89.34           O  
ANISOU 5126  O   TYR A 703    14594   9199  10152    103  -1210   -121       O  
ATOM   5127  CB  TYR A 703     144.249  76.101  36.016  1.00 74.95           C  
ANISOU 5127  CB  TYR A 703    13397   6992   8090   -153  -1094   -381       C  
ATOM   5128  CG  TYR A 703     145.653  75.808  35.544  1.00 79.69           C  
ANISOU 5128  CG  TYR A 703    13882   7643   8753   -662  -1048   -382       C  
ATOM   5129  CD1 TYR A 703     146.385  76.759  34.845  1.00 87.27           C  
ANISOU 5129  CD1 TYR A 703    15315   8263   9581   -951   -923   -399       C  
ATOM   5130  CD2 TYR A 703     146.259  74.591  35.826  1.00 80.05           C  
ANISOU 5130  CD2 TYR A 703    13366   8084   8966   -846  -1112   -373       C  
ATOM   5131  CE1 TYR A 703     147.675  76.498  34.423  1.00 89.60           C  
ANISOU 5131  CE1 TYR A 703    15458   8669   9918  -1436   -867   -424       C  
ATOM   5132  CE2 TYR A 703     147.547  74.322  35.409  1.00 85.30           C  
ANISOU 5132  CE2 TYR A 703    13888   8859   9665  -1261  -1074   -389       C  
ATOM   5133  CZ  TYR A 703     148.251  75.278  34.709  1.00 89.97           C  
ANISOU 5133  CZ  TYR A 703    14887   9166  10131  -1569   -953   -424       C  
ATOM   5134  OH  TYR A 703     149.534  75.012  34.292  1.00 95.76           O  
ANISOU 5134  OH  TYR A 703    15432  10071  10883  -2001   -901   -461       O  
ATOM   5135  N   LEU A 704     142.768  73.417  35.241  1.00 93.47           N  
ANISOU 5135  N   LEU A 704    14656  10084  10775    316  -1282   -213       N  
ATOM   5136  CA  LEU A 704     142.839  72.023  34.813  1.00 83.40           C  
ANISOU 5136  CA  LEU A 704    12899   9110   9680    243  -1323   -153       C  
ATOM   5137  C   LEU A 704     141.852  71.740  33.686  1.00 81.68           C  
ANISOU 5137  C   LEU A 704    12598   8976   9460    543  -1370   -106       C  
ATOM   5138  O   LEU A 704     142.212  71.136  32.668  1.00 67.29           O  
ANISOU 5138  O   LEU A 704    10645   7212   7710    434  -1379    -48       O  
ATOM   5139  CB  LEU A 704     142.579  71.103  36.008  1.00 83.99           C  
ANISOU 5139  CB  LEU A 704    12600   9457   9855    242  -1335   -183       C  
ATOM   5140  CG  LEU A 704     142.455  69.595  35.781  1.00 76.87           C  
ANISOU 5140  CG  LEU A 704    11259   8831   9119    201  -1343   -130       C  
ATOM   5141  CD1 LEU A 704     143.767  68.998  35.312  1.00 76.39           C  
ANISOU 5141  CD1 LEU A 704    11096   8789   9138    -99  -1330    -77       C  
ATOM   5142  CD2 LEU A 704     141.993  68.916  37.057  1.00 65.73           C  
ANISOU 5142  CD2 LEU A 704     9611   7617   7746    249  -1318   -156       C  
ATOM   5143  N   ALA A 705     140.599  72.172  33.849  1.00 77.99           N  
ANISOU 5143  N   ALA A 705    12187   8558   8889    937  -1404   -147       N  
ATOM   5144  CA  ALA A 705     139.578  71.881  32.847  1.00 78.31           C  
ANISOU 5144  CA  ALA A 705    12077   8784   8895   1248  -1468   -138       C  
ATOM   5145  C   ALA A 705     139.879  72.574  31.522  1.00 83.37           C  
ANISOU 5145  C   ALA A 705    13083   9187   9407   1323  -1475    -64       C  
ATOM   5146  O   ALA A 705     139.613  72.016  30.451  1.00 81.63           O  
ANISOU 5146  O   ALA A 705    12686   9128   9204   1393  -1526    -36       O  
ATOM   5147  CB  ALA A 705     138.202  72.290  33.368  1.00 78.27           C  
ANISOU 5147  CB  ALA A 705    12032   8945   8763   1686  -1504   -221       C  
ATOM   5148  N   PHE A 706     140.426  73.792  31.571  1.00 89.76           N  
ANISOU 5148  N   PHE A 706    14434   9603  10066   1296  -1410    -37       N  
ATOM   5149  CA  PHE A 706     140.833  74.465  30.341  1.00 86.62           C  
ANISOU 5149  CA  PHE A 706    14458   8927   9526   1313  -1374     51       C  
ATOM   5150  C   PHE A 706     142.000  73.744  29.679  1.00 95.22           C  
ANISOU 5150  C   PHE A 706    15375  10043  10762    864  -1336    103       C  
ATOM   5151  O   PHE A 706     142.084  73.691  28.447  1.00 91.06           O  
ANISOU 5151  O   PHE A 706    14935   9488  10175    910  -1341    176       O  
ATOM   5152  CB  PHE A 706     141.205  75.920  30.626  1.00 85.83           C  
ANISOU 5152  CB  PHE A 706    15041   8349   9222   1314  -1265     55       C  
ATOM   5153  CG  PHE A 706     140.131  76.906  30.263  1.00 99.94           C  
ANISOU 5153  CG  PHE A 706    17262   9972  10740   1903  -1285     80       C  
ATOM   5154  CD1 PHE A 706     139.963  77.314  28.948  1.00 93.18           C  
ANISOU 5154  CD1 PHE A 706    16731   8972   9700   2150  -1285    186       C  
ATOM   5155  CD2 PHE A 706     139.301  77.439  31.235  1.00107.71           C  
ANISOU 5155  CD2 PHE A 706    18346  10955  11622   2250  -1300      1       C  
ATOM   5156  CE1 PHE A 706     138.980  78.225  28.609  1.00 89.64           C  
ANISOU 5156  CE1 PHE A 706    16706   8392   8960   2772  -1310    219       C  
ATOM   5157  CE2 PHE A 706     138.317  78.353  30.903  1.00112.78           C  
ANISOU 5157  CE2 PHE A 706    19396  11472  11984   2866  -1320     22       C  
ATOM   5158  CZ  PHE A 706     138.156  78.745  29.587  1.00108.14           C  
ANISOU 5158  CZ  PHE A 706    19137  10749  11202   3146  -1329    135       C  
ATOM   5159  N   GLY A 707     142.914  73.190  30.482  1.00101.35           N  
ANISOU 5159  N   GLY A 707    15906  10900  11702    461  -1298     64       N  
ATOM   5160  CA  GLY A 707     144.029  72.448  29.916  1.00103.49           C  
ANISOU 5160  CA  GLY A 707    15969  11258  12096     85  -1264    101       C  
ATOM   5161  C   GLY A 707     143.581  71.237  29.121  1.00 94.64           C  
ANISOU 5161  C   GLY A 707    14441  10426  11092    199  -1336    132       C  
ATOM   5162  O   GLY A 707     144.135  70.937  28.061  1.00 87.06           O  
ANISOU 5162  O   GLY A 707    13474   9466  10141     70  -1313    185       O  
ATOM   5163  N   LEU A 708     142.574  70.521  29.625  1.00 92.86           N  
ANISOU 5163  N   LEU A 708    13879  10455  10947    412  -1407     83       N  
ATOM   5164  CA  LEU A 708     141.987  69.431  28.854  1.00 79.01           C  
ANISOU 5164  CA  LEU A 708    11777   8967   9275    506  -1462     76       C  
ATOM   5165  C   LEU A 708     141.276  69.962  27.618  1.00 70.11           C  
ANISOU 5165  C   LEU A 708    10839   7822   7978    811  -1521     97       C  
ATOM   5166  O   LEU A 708     141.404  69.392  26.529  1.00 77.23           O  
ANISOU 5166  O   LEU A 708    11634   8817   8894    771  -1540    118       O  
ATOM   5167  CB  LEU A 708     141.014  68.632  29.722  1.00 84.69           C  
ANISOU 5167  CB  LEU A 708    12128   9961  10088    615  -1490     -5       C  
ATOM   5168  CG  LEU A 708     141.559  67.487  30.578  1.00 83.92           C  
ANISOU 5168  CG  LEU A 708    11733   9979  10172    346  -1434     -9       C  
ATOM   5169  CD1 LEU A 708     142.612  67.972  31.559  1.00 96.40           C  
ANISOU 5169  CD1 LEU A 708    13471  11403  11754    150  -1389     17       C  
ATOM   5170  CD2 LEU A 708     140.418  66.802  31.314  1.00 87.74           C  
ANISOU 5170  CD2 LEU A 708    11925  10707  10706    460  -1429    -88       C  
ATOM   5171  N   LEU A 709     140.532  71.059  27.769  1.00 81.82           N  
ANISOU 5171  N   LEU A 709    12626   9190   9272   1153  -1550     90       N  
ATOM   5172  CA  LEU A 709     139.775  71.616  26.652  1.00 88.79           C  
ANISOU 5172  CA  LEU A 709    13711  10086   9937   1546  -1619    116       C  
ATOM   5173  C   LEU A 709     140.697  72.088  25.533  1.00 89.81           C  
ANISOU 5173  C   LEU A 709    14226   9932   9966   1408  -1556    230       C  
ATOM   5174  O   LEU A 709     140.413  71.870  24.350  1.00 84.37           O  
ANISOU 5174  O   LEU A 709    13514   9359   9182   1567  -1611    257       O  
ATOM   5175  CB  LEU A 709     138.901  72.766  27.151  1.00 92.35           C  
ANISOU 5175  CB  LEU A 709    14479  10433  10175   1987  -1644     96       C  
ATOM   5176  CG  LEU A 709     137.647  73.106  26.351  1.00104.46           C  
ANISOU 5176  CG  LEU A 709    16030  12191  11470   2558  -1762     72       C  
ATOM   5177  CD1 LEU A 709     136.729  71.904  26.307  1.00102.19           C  
ANISOU 5177  CD1 LEU A 709    15077  12457  11295   2602  -1863    -65       C  
ATOM   5178  CD2 LEU A 709     136.936  74.300  26.967  1.00111.57           C  
ANISOU 5178  CD2 LEU A 709    17303  12946  12145   3019  -1764     60       C  
ATOM   5179  N   ILE A 710     141.808  72.736  25.889  1.00100.90           N  
ANISOU 5179  N   ILE A 710    15977  10989  11372   1090  -1430    282       N  
ATOM   5180  CA  ILE A 710     142.726  73.259  24.880  1.00 90.01           C  
ANISOU 5180  CA  ILE A 710    14990   9331   9877    900  -1327    382       C  
ATOM   5181  C   ILE A 710     143.462  72.121  24.181  1.00 90.64           C  
ANISOU 5181  C   ILE A 710    14697   9623  10120    591  -1321    390       C  
ATOM   5182  O   ILE A 710     143.521  72.066  22.947  1.00 87.31           O  
ANISOU 5182  O   ILE A 710    14379   9202   9595    659  -1320    452       O  
ATOM   5183  CB  ILE A 710     143.709  74.257  25.519  1.00 91.26           C  
ANISOU 5183  CB  ILE A 710    15593   9100   9982    569  -1171    391       C  
ATOM   5184  CG1 ILE A 710     142.979  75.536  25.932  1.00 91.57           C  
ANISOU 5184  CG1 ILE A 710    16168   8831   9792    928  -1149    398       C  
ATOM   5185  CG2 ILE A 710     144.851  74.572  24.564  1.00 82.86           C  
ANISOU 5185  CG2 ILE A 710    14824   7818   8840    217  -1026    467       C  
ATOM   5186  CD1 ILE A 710     143.875  76.560  26.590  1.00 87.19           C  
ANISOU 5186  CD1 ILE A 710    16103   7862   9162    572   -978    374       C  
ATOM   5187  N   ALA A 711     144.037  71.199  24.959  1.00 95.48           N  
ANISOU 5187  N   ALA A 711    14896  10416  10966    282  -1311    331       N  
ATOM   5188  CA  ALA A 711     144.803  70.103  24.373  1.00 84.57           C  
ANISOU 5188  CA  ALA A 711    13190   9218   9726     22  -1289    336       C  
ATOM   5189  C   ALA A 711     143.925  69.176  23.544  1.00 81.14           C  
ANISOU 5189  C   ALA A 711    12466   9047   9315    256  -1392    309       C  
ATOM   5190  O   ALA A 711     144.386  68.625  22.537  1.00 69.20           O  
ANISOU 5190  O   ALA A 711    10880   7603   7810    152  -1371    332       O  
ATOM   5191  CB  ALA A 711     145.516  69.313  25.471  1.00 75.91           C  
ANISOU 5191  CB  ALA A 711    11746   8265   8831   -260  -1264    283       C  
ATOM   5192  N   LEU A 712     142.667  68.990  23.947  1.00 86.48           N  
ANISOU 5192  N   LEU A 712    12965   9903   9991    550  -1495    238       N  
ATOM   5193  CA  LEU A 712     141.754  68.151  23.178  1.00 82.84           C  
ANISOU 5193  CA  LEU A 712    12208   9742   9526    733  -1591    167       C  
ATOM   5194  C   LEU A 712     141.507  68.739  21.795  1.00 86.79           C  
ANISOU 5194  C   LEU A 712    12978  10206   9792    975  -1636    219       C  
ATOM   5195  O   LEU A 712     141.596  68.036  20.782  1.00 80.80           O  
ANISOU 5195  O   LEU A 712    12074   9593   9031    927  -1657    200       O  
ATOM   5196  CB  LEU A 712     140.440  67.992  23.938  1.00 84.36           C  
ANISOU 5196  CB  LEU A 712    12152  10177   9726    979  -1675     56       C  
ATOM   5197  CG  LEU A 712     139.788  66.615  23.962  1.00100.23           C  
ANISOU 5197  CG  LEU A 712    13676  12532  11875    895  -1704    -76       C  
ATOM   5198  CD1 LEU A 712     140.828  65.536  24.196  1.00 98.78           C  
ANISOU 5198  CD1 LEU A 712    13342  12284  11906    507  -1601    -53       C  
ATOM   5199  CD2 LEU A 712     138.749  66.598  25.061  1.00111.85           C  
ANISOU 5199  CD2 LEU A 712    14936  14195  13367   1033  -1728   -176       C  
ATOM   5200  N   LEU A 713     141.188  70.035  21.737  1.00107.00           N  
ANISOU 5200  N   LEU A 713    15972  12556  12129   1261  -1643    287       N  
ATOM   5201  CA  LEU A 713     140.987  70.702  20.455  1.00114.93           C  
ANISOU 5201  CA  LEU A 713    17329  13480  12860   1541  -1671    368       C  
ATOM   5202  C   LEU A 713     142.262  70.687  19.620  1.00106.28           C  
ANISOU 5202  C   LEU A 713    16450  12171  11762   1205  -1542    470       C  
ATOM   5203  O   LEU A 713     142.212  70.494  18.399  1.00100.27           O  
ANISOU 5203  O   LEU A 713    15731  11500  10868   1308  -1571    499       O  
ATOM   5204  CB  LEU A 713     140.511  72.136  20.690  1.00123.35           C  
ANISOU 5204  CB  LEU A 713    18919  14277  13670   1919  -1665    441       C  
ATOM   5205  CG  LEU A 713     140.514  73.102  19.503  1.00144.34           C  
ANISOU 5205  CG  LEU A 713    22149  16700  15993   2215  -1638    576       C  
ATOM   5206  CD1 LEU A 713     139.549  72.644  18.422  1.00150.21           C  
ANISOU 5206  CD1 LEU A 713    22658  17847  16567   2619  -1809    527       C  
ATOM   5207  CD2 LEU A 713     140.175  74.511  19.967  1.00146.17           C  
ANISOU 5207  CD2 LEU A 713    22982  16571  15986   2552  -1586    652       C  
ATOM   5208  N   LEU A 714     143.414  70.885  20.263  1.00103.12           N  
ANISOU 5208  N   LEU A 714    16162  11531  11487    797  -1398    508       N  
ATOM   5209  CA  LEU A 714     144.682  70.885  19.540  1.00 93.15           C  
ANISOU 5209  CA  LEU A 714    15056  10123  10215    441  -1254    581       C  
ATOM   5210  C   LEU A 714     144.994  69.506  18.968  1.00101.00           C  
ANISOU 5210  C   LEU A 714    15587  11419  11369    283  -1284    524       C  
ATOM   5211  O   LEU A 714     145.462  69.393  17.829  1.00 94.24           O  
ANISOU 5211  O   LEU A 714    14833  10560  10413    222  -1232    574       O  
ATOM   5212  CB  LEU A 714     145.805  71.353  20.466  1.00 93.25           C  
ANISOU 5212  CB  LEU A 714    15198   9917  10317     23  -1105    586       C  
ATOM   5213  CG  LEU A 714     146.654  72.544  20.016  1.00100.57           C  
ANISOU 5213  CG  LEU A 714    16707  10465  11041   -197   -916    678       C  
ATOM   5214  CD1 LEU A 714     145.777  73.725  19.627  1.00100.12           C  
ANISOU 5214  CD1 LEU A 714    17240  10109  10693    218   -921    767       C  
ATOM   5215  CD2 LEU A 714     147.630  72.941  21.113  1.00 89.07           C  
ANISOU 5215  CD2 LEU A 714    15284   8882   9677   -634   -792    619       C  
ATOM   5216  N   ASP A 715     144.739  68.447  19.740  1.00103.31           N  
ANISOU 5216  N   ASP A 715    15411  11951  11891    222  -1350    421       N  
ATOM   5217  CA  ASP A 715     145.038  67.098  19.268  1.00 90.97           C  
ANISOU 5217  CA  ASP A 715    13472  10621  10472     77  -1354    360       C  
ATOM   5218  C   ASP A 715     144.048  66.648  18.202  1.00 81.57           C  
ANISOU 5218  C   ASP A 715    12180   9643   9172    343  -1469    299       C  
ATOM   5219  O   ASP A 715     144.442  66.048  17.196  1.00 73.75           O  
ANISOU 5219  O   ASP A 715    11129   8737   8158    264  -1444    291       O  
ATOM   5220  CB  ASP A 715     145.034  66.115  20.439  1.00 85.63           C  
ANISOU 5220  CB  ASP A 715    12412  10083  10038    -56  -1362    278       C  
ATOM   5221  CG  ASP A 715     146.197  66.327  21.386  1.00 89.80           C  
ANISOU 5221  CG  ASP A 715    12962  10495  10663   -336  -1259    316       C  
ATOM   5222  OD1 ASP A 715     147.312  66.623  20.905  1.00 86.43           O  
ANISOU 5222  OD1 ASP A 715    12667   9988  10185   -551  -1156    368       O  
ATOM   5223  OD2 ASP A 715     145.993  66.200  22.611  1.00 87.17           O  
ANISOU 5223  OD2 ASP A 715    12496  10187  10438   -348  -1278    281       O  
ATOM   5224  N   ALA A 716     142.760  66.928  18.404  1.00 87.96           N  
ANISOU 5224  N   ALA A 716    12946  10583   9892    667  -1597    238       N  
ATOM   5225  CA  ALA A 716     141.716  66.408  17.530  1.00 82.21           C  
ANISOU 5225  CA  ALA A 716    12015  10166   9053    906  -1728    126       C  
ATOM   5226  C   ALA A 716     141.536  67.215  16.251  1.00 83.28           C  
ANISOU 5226  C   ALA A 716    12494  10269   8879   1195  -1776    206       C  
ATOM   5227  O   ALA A 716     140.761  66.796  15.385  1.00 74.52           O  
ANISOU 5227  O   ALA A 716    11216   9460   7637   1398  -1895    105       O  
ATOM   5228  CB  ALA A 716     140.386  66.343  18.286  1.00 77.06           C  
ANISOU 5228  CB  ALA A 716    11106   9766   8407   1137  -1845     -2       C  
ATOM   5229  N   THR A 717     142.217  68.355  16.108  1.00 95.38           N  
ANISOU 5229  N   THR A 717    14521  11450  10268   1208  -1676    375       N  
ATOM   5230  CA  THR A 717     142.117  69.162  14.892  1.00 87.61           C  
ANISOU 5230  CA  THR A 717    13959  10373   8956   1488  -1685    483       C  
ATOM   5231  C   THR A 717     143.493  69.412  14.289  1.00 89.97           C  
ANISOU 5231  C   THR A 717    14574  10384   9229   1155  -1492    616       C  
ATOM   5232  O   THR A 717     143.808  68.841  13.243  1.00 90.24           O  
ANISOU 5232  O   THR A 717    14534  10546   9209   1088  -1480    608       O  
ATOM   5233  CB  THR A 717     141.393  70.482  15.171  1.00 77.29           C  
ANISOU 5233  CB  THR A 717    13074   8892   7399   1918  -1728    566       C  
ATOM   5234  OG1 THR A 717     142.141  71.251  16.123  1.00 68.88           O  
ANISOU 5234  OG1 THR A 717    12326   7426   6419   1680  -1573    656       O  
ATOM   5235  CG2 THR A 717     139.992  70.225  15.710  1.00 80.26           C  
ANISOU 5235  CG2 THR A 717    13080   9644   7772   2278  -1920    412       C  
ATOM   5236  N   ILE A 718     144.324  70.248  14.914  1.00 93.51           N  
ANISOU 5236  N   ILE A 718    15360  10472   9698    920  -1330    719       N  
ATOM   5237  CA  ILE A 718     145.609  70.609  14.322  1.00 96.23           C  
ANISOU 5237  CA  ILE A 718    16013  10575   9976    573  -1121    827       C  
ATOM   5238  C   ILE A 718     146.494  69.377  14.172  1.00 90.76           C  
ANISOU 5238  C   ILE A 718    14864  10106   9515    205  -1071    747       C  
ATOM   5239  O   ILE A 718     147.078  69.133  13.109  1.00 81.02           O  
ANISOU 5239  O   ILE A 718    13690   8911   8185    100   -989    784       O  
ATOM   5240  CB  ILE A 718     146.297  71.697  15.164  1.00 92.13           C  
ANISOU 5240  CB  ILE A 718    15890   9670   9443    321   -950    898       C  
ATOM   5241  CG1 ILE A 718     145.371  72.900  15.335  1.00104.64           C  
ANISOU 5241  CG1 ILE A 718    17986  10994  10780    746   -990    975       C  
ATOM   5242  CG2 ILE A 718     147.591  72.126  14.507  1.00103.20           C  
ANISOU 5242  CG2 ILE A 718    17610  10858  10742    -83   -708    986       C  
ATOM   5243  CD1 ILE A 718     145.066  73.623  14.041  1.00107.88           C  
ANISOU 5243  CD1 ILE A 718    18935  11241  10814   1080   -958   1117       C  
ATOM   5244  N   ILE A 719     146.600  68.579  15.235  1.00 92.88           N  
ANISOU 5244  N   ILE A 719    14698  10523  10070     37  -1111    641       N  
ATOM   5245  CA  ILE A 719     147.473  67.409  15.210  1.00 87.83           C  
ANISOU 5245  CA  ILE A 719    13667  10072   9633   -256  -1052    573       C  
ATOM   5246  C   ILE A 719     146.921  66.351  14.261  1.00 89.89           C  
ANISOU 5246  C   ILE A 719    13679  10591   9884    -91  -1152    491       C  
ATOM   5247  O   ILE A 719     147.580  65.951  13.295  1.00 89.08           O  
ANISOU 5247  O   ILE A 719    13578  10548   9722   -201  -1072    501       O  
ATOM   5248  CB  ILE A 719     147.658  66.846  16.630  1.00 81.64           C  
ANISOU 5248  CB  ILE A 719    12544   9361   9113   -411  -1069    497       C  
ATOM   5249  CG1 ILE A 719     148.302  67.891  17.545  1.00 70.67           C  
ANISOU 5249  CG1 ILE A 719    11390   7748   7714   -619   -967    548       C  
ATOM   5250  CG2 ILE A 719     148.484  65.570  16.600  1.00 73.13           C  
ANISOU 5250  CG2 ILE A 719    11095   8481   8210   -614  -1015    433       C  
ATOM   5251  CD1 ILE A 719     149.657  68.370  17.072  1.00 65.03           C  
ANISOU 5251  CD1 ILE A 719    10860   6939   6909   -971   -774    600       C  
ATOM   5252  N   ARG A 720     145.689  65.901  14.513  1.00 89.36           N  
ANISOU 5252  N   ARG A 720    13396  10700   9856    157  -1318    388       N  
ATOM   5253  CA  ARG A 720     145.159  64.737  13.810  1.00 85.03           C  
ANISOU 5253  CA  ARG A 720    12550  10424   9333    225  -1403    254       C  
ATOM   5254  C   ARG A 720     144.935  65.015  12.326  1.00 89.11           C  
ANISOU 5254  C   ARG A 720    13276  11009   9571    418  -1440    279       C  
ATOM   5255  O   ARG A 720     145.227  64.161  11.481  1.00 78.94           O  
ANISOU 5255  O   ARG A 720    11857   9858   8278    334  -1418    210       O  
ATOM   5256  CB  ARG A 720     143.855  64.284  14.464  1.00 69.87           C  
ANISOU 5256  CB  ARG A 720    10345   8710   7493    391  -1550    111       C  
ATOM   5257  CG  ARG A 720     143.199  63.109  13.763  1.00 81.66           C  
ANISOU 5257  CG  ARG A 720    11541  10495   8991    407  -1627    -71       C  
ATOM   5258  CD  ARG A 720     141.800  62.856  14.288  1.00 89.06           C  
ANISOU 5258  CD  ARG A 720    12208  11689   9942    559  -1763   -232       C  
ATOM   5259  NE  ARG A 720     140.981  64.063  14.266  1.00 83.52           N  
ANISOU 5259  NE  ARG A 720    11681  11037   9017    926  -1885   -181       N  
ATOM   5260  CZ  ARG A 720     139.653  64.063  14.228  1.00 94.67           C  
ANISOU 5260  CZ  ARG A 720    12876  12788  10306   1183  -2040   -333       C  
ATOM   5261  NH1 ARG A 720     138.988  65.208  14.214  1.00109.67           N  
ANISOU 5261  NH1 ARG A 720    14972  14725  11973   1588  -2144   -270       N  
ATOM   5262  NH2 ARG A 720     138.989  62.916  14.191  1.00105.96           N  
ANISOU 5262  NH2 ARG A 720    13903  14532  11823   1037  -2079   -561       N  
ATOM   5263  N   MET A 721     144.412  66.194  11.987  1.00 89.57           N  
ANISOU 5263  N   MET A 721    13693  10969   9372    707  -1493    379       N  
ATOM   5264  CA  MET A 721     143.997  66.445  10.612  1.00 92.48           C  
ANISOU 5264  CA  MET A 721    14261  11448   9429    981  -1560    400       C  
ATOM   5265  C   MET A 721     145.133  66.922   9.717  1.00 90.96           C  
ANISOU 5265  C   MET A 721    14446  11034   9081    823  -1377    556       C  
ATOM   5266  O   MET A 721     145.039  66.771   8.494  1.00 81.22           O  
ANISOU 5266  O   MET A 721    13305   9928   7629    961  -1403    555       O  
ATOM   5267  CB  MET A 721     142.857  67.469  10.577  1.00 82.59           C  
ANISOU 5267  CB  MET A 721    13254  10218   7909   1458  -1704    443       C  
ATOM   5268  CG  MET A 721     141.694  67.138  11.497  1.00 82.69           C  
ANISOU 5268  CG  MET A 721    12888  10490   8042   1626  -1869    283       C  
ATOM   5269  SD  MET A 721     140.222  68.114  11.136  1.00 76.40           S  
ANISOU 5269  SD  MET A 721    12267   9904   6857   2299  -2078    279       S  
ATOM   5270  CE  MET A 721     140.886  69.770  11.245  1.00 86.28           C  
ANISOU 5270  CE  MET A 721    14300  10583   7901   2433  -1915    569       C  
ATOM   5271  N   PHE A 722     146.200  67.485  10.282  1.00 99.25           N  
ANISOU 5271  N   PHE A 722    15700  11790  10219    518  -1187    671       N  
ATOM   5272  CA  PHE A 722     147.237  68.080   9.448  1.00 95.50           C  
ANISOU 5272  CA  PHE A 722    15613  11113   9560    334   -982    812       C  
ATOM   5273  C   PHE A 722     148.626  67.549   9.776  1.00 93.33           C  
ANISOU 5273  C   PHE A 722    15120  10838   9504   -144   -795    788       C  
ATOM   5274  O   PHE A 722     149.330  67.056   8.889  1.00 88.72           O  
ANISOU 5274  O   PHE A 722    14483  10361   8867   -283   -693    782       O  
ATOM   5275  CB  PHE A 722     147.215  69.604   9.587  1.00 94.10           C  
ANISOU 5275  CB  PHE A 722    16042  10559   9153    428   -884    984       C  
ATOM   5276  CG  PHE A 722     145.895  70.227   9.232  1.00106.70           C  
ANISOU 5276  CG  PHE A 722    17905  12163  10473    988  -1060   1026       C  
ATOM   5277  CD1 PHE A 722     145.540  70.422   7.907  1.00110.85           C  
ANISOU 5277  CD1 PHE A 722    18699  12758  10659   1301  -1098   1095       C  
ATOM   5278  CD2 PHE A 722     145.011  70.622  10.222  1.00109.09           C  
ANISOU 5278  CD2 PHE A 722    18183  12440  10829   1236  -1190    992       C  
ATOM   5279  CE1 PHE A 722     144.326  70.997   7.577  1.00107.22           C  
ANISOU 5279  CE1 PHE A 722    18464  12369   9905   1882  -1277   1127       C  
ATOM   5280  CE2 PHE A 722     143.797  71.199   9.898  1.00109.85           C  
ANISOU 5280  CE2 PHE A 722    18491  12605  10641   1808  -1357   1019       C  
ATOM   5281  CZ  PHE A 722     143.453  71.385   8.574  1.00106.44           C  
ANISOU 5281  CZ  PHE A 722    18312  12270   9859   2147  -1409   1085       C  
ATOM   5282  N   LEU A 723     149.032  67.642  11.044  1.00 92.10           N  
ANISOU 5282  N   LEU A 723    14822  10601   9570   -369   -752    765       N  
ATOM   5283  CA  LEU A 723     150.419  67.351  11.389  1.00 93.48           C  
ANISOU 5283  CA  LEU A 723    14819  10810   9889   -795   -571    746       C  
ATOM   5284  C   LEU A 723     150.721  65.858  11.303  1.00101.93           C  
ANISOU 5284  C   LEU A 723    15392  12181  11155   -835   -611    620       C  
ATOM   5285  O   LEU A 723     151.832  65.468  10.925  1.00 96.04           O  
ANISOU 5285  O   LEU A 723    14524  11547  10418  -1067   -461    607       O  
ATOM   5286  CB  LEU A 723     150.735  67.891  12.783  1.00 91.25           C  
ANISOU 5286  CB  LEU A 723    14524  10396   9751   -997   -533    740       C  
ATOM   5287  CG  LEU A 723     152.201  68.235  13.048  1.00 90.52           C  
ANISOU 5287  CG  LEU A 723    14431  10291   9672  -1463   -309    741       C  
ATOM   5288  CD1 LEU A 723     152.706  69.243  12.026  1.00 80.20           C  
ANISOU 5288  CD1 LEU A 723    13622   8772   8077  -1628   -102    853       C  
ATOM   5289  CD2 LEU A 723     152.376  68.772  14.460  1.00 85.14           C  
ANISOU 5289  CD2 LEU A 723    13731   9509   9110  -1639   -304    705       C  
ATOM   5290  N   VAL A 724     149.757  65.009  11.647  1.00106.11           N  
ANISOU 5290  N   VAL A 724    15650  12844  11824   -614   -791    518       N  
ATOM   5291  CA  VAL A 724     149.953  63.561  11.562  1.00104.76           C  
ANISOU 5291  CA  VAL A 724    15097  12891  11817   -640   -807    395       C  
ATOM   5292  C   VAL A 724     150.093  63.138  10.099  1.00 98.62           C  
ANISOU 5292  C   VAL A 724    14379  12223  10869   -580   -771    373       C  
ATOM   5293  O   VAL A 724     151.097  62.497   9.755  1.00 90.83           O  
ANISOU 5293  O   VAL A 724    13255  11338   9918   -732   -643    345       O  
ATOM   5294  CB  VAL A 724     148.822  62.786  12.264  1.00 95.11           C  
ANISOU 5294  CB  VAL A 724    13624  11753  10758   -476   -973    278       C  
ATOM   5295  CG1 VAL A 724     149.006  61.292  12.067  1.00 84.85           C  
ANISOU 5295  CG1 VAL A 724    12040  10608   9591   -513   -953    150       C  
ATOM   5296  CG2 VAL A 724     148.779  63.114  13.745  1.00 90.89           C  
ANISOU 5296  CG2 VAL A 724    13016  11129  10390   -541   -990    298       C  
ATOM   5297  N   PRO A 725     149.150  63.462   9.200  1.00103.87           N  
ANISOU 5297  N   PRO A 725    15238  12905  11325   -337   -881    376       N  
ATOM   5298  CA  PRO A 725     149.306  62.998   7.811  1.00 98.90           C  
ANISOU 5298  CA  PRO A 725    14655  12406  10517   -280   -851    339       C  
ATOM   5299  C   PRO A 725     150.484  63.626   7.089  1.00101.46           C  
ANISOU 5299  C   PRO A 725    15234  12646  10670   -462   -638    468       C  
ATOM   5300  O   PRO A 725     151.057  62.986   6.198  1.00106.57           O  
ANISOU 5300  O   PRO A 725    15816  13428  11250   -514   -550    423       O  
ATOM   5301  CB  PRO A 725     147.975  63.391   7.152  1.00 96.55           C  
ANISOU 5301  CB  PRO A 725    14513  12179   9992     56  -1038    318       C  
ATOM   5302  CG  PRO A 725     147.031  63.620   8.281  1.00 98.31           C  
ANISOU 5302  CG  PRO A 725    14623  12382  10347    174  -1182    283       C  
ATOM   5303  CD  PRO A 725     147.876  64.186   9.369  1.00104.37           C  
ANISOU 5303  CD  PRO A 725    15455  12926  11275    -57  -1049    393       C  
ATOM   5304  N   ALA A 726     150.863  64.857   7.437  1.00105.37           N  
ANISOU 5304  N   ALA A 726    16035  12921  11079   -580   -533    615       N  
ATOM   5305  CA  ALA A 726     151.969  65.511   6.744  1.00106.96           C  
ANISOU 5305  CA  ALA A 726    16507  13039  11093   -820   -292    726       C  
ATOM   5306  C   ALA A 726     153.305  64.883   7.121  1.00106.57           C  
ANISOU 5306  C   ALA A 726    16122  13152  11219  -1153   -125    659       C  
ATOM   5307  O   ALA A 726     154.116  64.555   6.247  1.00102.44           O  
ANISOU 5307  O   ALA A 726    15565  12769  10588  -1268     26    649       O  
ATOM   5308  CB  ALA A 726     151.973  67.009   7.052  1.00103.38           C  
ANISOU 5308  CB  ALA A 726    16530  12267  10484   -898   -197    880       C  
ATOM   5309  N   VAL A 727     153.551  64.710   8.421  1.00101.03           N  
ANISOU 5309  N   VAL A 727    15157  12467  10762  -1279   -152    609       N  
ATOM   5310  CA  VAL A 727     154.834  64.177   8.869  1.00 97.70           C  
ANISOU 5310  CA  VAL A 727    14398  12254  10471  -1542    -10    542       C  
ATOM   5311  C   VAL A 727     154.975  62.713   8.471  1.00 92.35           C  
ANISOU 5311  C   VAL A 727    13385  11816   9888  -1386    -47    426       C  
ATOM   5312  O   VAL A 727     156.060  62.261   8.085  1.00 83.19           O  
ANISOU 5312  O   VAL A 727    12045  10868   8695  -1510    107    385       O  
ATOM   5313  CB  VAL A 727     154.992  64.380  10.387  1.00 93.24           C  
ANISOU 5313  CB  VAL A 727    13656  11665  10107  -1667    -52    516       C  
ATOM   5314  CG1 VAL A 727     156.241  63.677  10.900  1.00 94.52           C  
ANISOU 5314  CG1 VAL A 727    13403  12126  10385  -1844     52    427       C  
ATOM   5315  CG2 VAL A 727     155.049  65.864  10.715  1.00 72.62           C  
ANISOU 5315  CG2 VAL A 727    11422   8798   7372  -1882     37    611       C  
ATOM   5316  N   MET A 728     153.882  61.950   8.545  1.00 94.87           N  
ANISOU 5316  N   MET A 728    13626  12112  10307  -1118   -237    357       N  
ATOM   5317  CA  MET A 728     153.947  60.545   8.161  1.00 91.84           C  
ANISOU 5317  CA  MET A 728    13006  11891   9999   -988   -251    231       C  
ATOM   5318  C   MET A 728     154.173  60.377   6.663  1.00 95.19           C  
ANISOU 5318  C   MET A 728    13564  12404  10200   -946   -168    218       C  
ATOM   5319  O   MET A 728     154.770  59.382   6.236  1.00 93.08           O  
ANISOU 5319  O   MET A 728    13127  12293   9946   -914    -87    127       O  
ATOM   5320  CB  MET A 728     152.676  59.817   8.601  1.00 83.33           C  
ANISOU 5320  CB  MET A 728    11844  10757   9062   -791   -444    135       C  
ATOM   5321  CG  MET A 728     152.561  59.634  10.108  1.00 67.90           C  
ANISOU 5321  CG  MET A 728     9709   8750   7340   -818   -498    128       C  
ATOM   5322  SD  MET A 728     151.073  58.754  10.611  1.00 51.94           S  
ANISOU 5322  SD  MET A 728     7591   6679   5465   -653   -675      1       S  
ATOM   5323  CE  MET A 728     151.383  57.150   9.889  1.00 90.62           C  
ANISOU 5323  CE  MET A 728    12384  11666  10382   -599   -594   -148       C  
ATOM   5324  N   LYS A 729     153.718  61.335   5.853  1.00100.99           N  
ANISOU 5324  N   LYS A 729    14631  13036  10705   -915   -179    310       N  
ATOM   5325  CA  LYS A 729     153.965  61.259   4.417  1.00 90.84           C  
ANISOU 5325  CA  LYS A 729    13506  11840   9169   -874    -89    313       C  
ATOM   5326  C   LYS A 729     155.439  61.480   4.097  1.00 85.10           C  
ANISOU 5326  C   LYS A 729    12747  11230   8357  -1131    174    359       C  
ATOM   5327  O   LYS A 729     155.995  60.813   3.216  1.00 83.87           O  
ANISOU 5327  O   LYS A 729    12513  11250   8102  -1109    279    294       O  
ATOM   5328  CB  LYS A 729     153.094  62.276   3.680  1.00 90.80           C  
ANISOU 5328  CB  LYS A 729    13905  11696   8899   -727   -167    420       C  
ATOM   5329  CG  LYS A 729     153.268  62.259   2.172  1.00111.63           C  
ANISOU 5329  CG  LYS A 729    16753  14427  11235   -653    -84    436       C  
ATOM   5330  CD  LYS A 729     152.979  60.882   1.603  1.00122.80           C  
ANISOU 5330  CD  LYS A 729    17922  16048  12691   -504   -173    241       C  
ATOM   5331  CE  LYS A 729     153.253  60.831   0.109  1.00125.51           C  
ANISOU 5331  CE  LYS A 729    18460  16508  12722   -440    -77    244       C  
ATOM   5332  NZ  LYS A 729     153.119  59.448  -0.427  1.00133.38           N  
ANISOU 5332  NZ  LYS A 729    19233  17690  13757   -338   -129     28       N  
ATOM   5333  N   LEU A 730     156.086  62.414   4.800  1.00 90.80           N  
ANISOU 5333  N   LEU A 730    13517  11881   9100  -1394    294    451       N  
ATOM   5334  CA  LEU A 730     157.518  62.635   4.609  1.00 96.32           C  
ANISOU 5334  CA  LEU A 730    14114  12766   9719  -1701    556    457       C  
ATOM   5335  C   LEU A 730     158.317  61.381   4.932  1.00106.02           C  
ANISOU 5335  C   LEU A 730    14872  14303  11107  -1653    589    316       C  
ATOM   5336  O   LEU A 730     159.256  61.029   4.208  1.00114.21           O  
ANISOU 5336  O   LEU A 730    15785  15586  12022  -1721    769    271       O  
ATOM   5337  CB  LEU A 730     157.996  63.796   5.484  1.00106.14           C  
ANISOU 5337  CB  LEU A 730    15455  13897  10978  -2034    663    531       C  
ATOM   5338  CG  LEU A 730     158.002  65.216   4.919  1.00110.78           C  
ANISOU 5338  CG  LEU A 730    16567  14226  11299  -2251    825    679       C  
ATOM   5339  CD1 LEU A 730     156.634  65.593   4.424  1.00108.34           C  
ANISOU 5339  CD1 LEU A 730    16670  13628  10866  -1911    647    780       C  
ATOM   5340  CD2 LEU A 730     158.468  66.201   5.981  1.00105.34           C  
ANISOU 5340  CD2 LEU A 730    15941  13419  10665  -2610    925    701       C  
ATOM   5341  N   LEU A 731     157.961  60.699   6.021  1.00103.17           N  
ANISOU 5341  N   LEU A 731    14268  13935  10997  -1509    431    250       N  
ATOM   5342  CA  LEU A 731     158.703  59.513   6.432  1.00100.73           C  
ANISOU 5342  CA  LEU A 731    13573  13882  10815  -1399    465    135       C  
ATOM   5343  C   LEU A 731     158.474  58.350   5.476  1.00 89.83           C  
ANISOU 5343  C   LEU A 731    12193  12552   9386  -1139    454     41       C  
ATOM   5344  O   LEU A 731     159.383  57.540   5.260  1.00 75.27           O  
ANISOU 5344  O   LEU A 731    10127  10955   7518  -1057    575    -41       O  
ATOM   5345  CB  LEU A 731     158.307  59.119   7.856  1.00100.46           C  
ANISOU 5345  CB  LEU A 731    13362  13777  11030  -1298    311    110       C  
ATOM   5346  CG  LEU A 731     158.952  59.810   9.064  1.00 92.56           C  
ANISOU 5346  CG  LEU A 731    12192  12869  10107  -1517    341    138       C  
ATOM   5347  CD1 LEU A 731     159.061  61.318   8.898  1.00 93.42           C  
ANISOU 5347  CD1 LEU A 731    12556  12860  10078  -1853    431    229       C  
ATOM   5348  CD2 LEU A 731     158.159  59.478  10.319  1.00 90.88           C  
ANISOU 5348  CD2 LEU A 731    11921  12498  10112  -1369    156    134       C  
ATOM   5349  N   GLY A 732     157.279  58.252   4.897  1.00 91.09           N  
ANISOU 5349  N   GLY A 732    12593  12509   9508   -997    312     32       N  
ATOM   5350  CA  GLY A 732     157.008  57.185   3.947  1.00 90.97           C  
ANISOU 5350  CA  GLY A 732    12605  12536   9423   -795    303    -88       C  
ATOM   5351  C   GLY A 732     156.946  55.833   4.629  1.00101.13           C  
ANISOU 5351  C   GLY A 732    13699  13817  10908   -612    258   -213       C  
ATOM   5352  O   GLY A 732     156.365  55.677   5.709  1.00 98.87           O  
ANISOU 5352  O   GLY A 732    13354  13393  10817   -585    137   -213       O  
ATOM   5353  N   ASP A 733     157.558  54.833   3.991  1.00113.78           N  
ANISOU 5353  N   ASP A 733    15239  15552  12441   -473    376   -320       N  
ATOM   5354  CA  ASP A 733     157.605  53.495   4.566  1.00115.49           C  
ANISOU 5354  CA  ASP A 733    15358  15720  12803   -266    379   -432       C  
ATOM   5355  C   ASP A 733     158.460  53.424   5.823  1.00110.01           C  
ANISOU 5355  C   ASP A 733    14415  15142  12242   -229    427   -375       C  
ATOM   5356  O   ASP A 733     158.401  52.414   6.533  1.00106.55           O  
ANISOU 5356  O   ASP A 733    13944  14612  11927    -33    417   -431       O  
ATOM   5357  CB  ASP A 733     158.118  52.493   3.531  1.00118.33           C  
ANISOU 5357  CB  ASP A 733    15761  16181  13018    -90    515   -560       C  
ATOM   5358  CG  ASP A 733     157.141  52.284   2.392  1.00114.58           C  
ANISOU 5358  CG  ASP A 733    15528  15589  12416    -92    441   -666       C  
ATOM   5359  OD1 ASP A 733     156.236  53.127   2.222  1.00112.07           O  
ANISOU 5359  OD1 ASP A 733    15322  15193  12068   -220    299   -614       O  
ATOM   5360  OD2 ASP A 733     157.271  51.270   1.675  1.00113.48           O  
ANISOU 5360  OD2 ASP A 733    15475  15452  12190     56    522   -814       O  
ATOM   5361  N   ASP A 734     159.250  54.462   6.114  1.00110.74           N  
ANISOU 5361  N   ASP A 734    14351  15436  12289   -419    488   -275       N  
ATOM   5362  CA  ASP A 734     159.981  54.498   7.376  1.00106.20           C  
ANISOU 5362  CA  ASP A 734    13509  15021  11821   -406    500   -242       C  
ATOM   5363  C   ASP A 734     159.034  54.547   8.566  1.00 96.96           C  
ANISOU 5363  C   ASP A 734    12394  13589  10856   -403    329   -200       C  
ATOM   5364  O   ASP A 734     159.399  54.103   9.660  1.00 80.26           O  
ANISOU 5364  O   ASP A 734    10112  11540   8842   -273    314   -197       O  
ATOM   5365  CB  ASP A 734     160.927  55.699   7.409  1.00107.45           C  
ANISOU 5365  CB  ASP A 734    13501  15454  11872   -702    605   -179       C  
ATOM   5366  CG  ASP A 734     162.108  55.537   6.477  1.00113.71           C  
ANISOU 5366  CG  ASP A 734    14133  16611  12461   -703    812   -238       C  
ATOM   5367  OD1 ASP A 734     162.636  54.410   6.377  1.00117.51           O  
ANISOU 5367  OD1 ASP A 734    14473  17258  12916   -392    872   -326       O  
ATOM   5368  OD2 ASP A 734     162.509  56.537   5.844  1.00117.27           O  
ANISOU 5368  OD2 ASP A 734    14625  17175  12759  -1007    931   -196       O  
ATOM   5369  N   CYS A 735     157.818  55.072   8.368  1.00100.46           N  
ANISOU 5369  N   CYS A 735    13065  13769  11337   -515    201   -171       N  
ATOM   5370  CA  CYS A 735     156.843  55.184   9.451  1.00 87.80           C  
ANISOU 5370  CA  CYS A 735    11504  11945   9911   -523     47   -142       C  
ATOM   5371  C   CYS A 735     156.626  53.865  10.176  1.00 88.06           C  
ANISOU 5371  C   CYS A 735    11506  11873  10079   -301     36   -210       C  
ATOM   5372  O   CYS A 735     156.375  53.854  11.385  1.00 70.69           O  
ANISOU 5372  O   CYS A 735     9248   9595   8016   -284    -31   -170       O  
ATOM   5373  CB  CYS A 735     155.503  55.685   8.909  1.00 70.48           C  
ANISOU 5373  CB  CYS A 735     9540   9546   7693   -589    -85   -144       C  
ATOM   5374  SG  CYS A 735     155.403  57.453   8.654  1.00 56.07           S  
ANISOU 5374  SG  CYS A 735     7863   7698   5742   -809   -110    -10       S  
ATOM   5375  N   TRP A 736     156.715  52.748   9.462  1.00 99.94           N  
ANISOU 5375  N   TRP A 736    13093  13350  11529   -129    117   -314       N  
ATOM   5376  CA  TRP A 736     156.380  51.447  10.016  1.00101.46           C  
ANISOU 5376  CA  TRP A 736    13379  13352  11820     66    140   -386       C  
ATOM   5377  C   TRP A 736     157.603  50.629  10.404  1.00 95.71           C  
ANISOU 5377  C   TRP A 736    12541  12777  11046    346    275   -380       C  
ATOM   5378  O   TRP A 736     157.451  49.491  10.857  1.00 92.95           O  
ANISOU 5378  O   TRP A 736    12339  12237  10742    558    330   -424       O  
ATOM   5379  CB  TRP A 736     155.530  50.669   9.009  1.00101.22           C  
ANISOU 5379  CB  TRP A 736    13581  13136  11742     67    149   -536       C  
ATOM   5380  CG  TRP A 736     154.654  51.555   8.173  1.00 96.15           C  
ANISOU 5380  CG  TRP A 736    12997  12503  11033   -135     29   -555       C  
ATOM   5381  CD1 TRP A 736     154.897  51.982   6.899  1.00105.91           C  
ANISOU 5381  CD1 TRP A 736    14276  13880  12087   -173     55   -574       C  
ATOM   5382  CD2 TRP A 736     153.400  52.134   8.557  1.00 95.48           C  
ANISOU 5382  CD2 TRP A 736    12942  12308  11027   -279   -133   -554       C  
ATOM   5383  NE1 TRP A 736     153.868  52.784   6.463  1.00110.64           N  
ANISOU 5383  NE1 TRP A 736    14954  14450  12633   -302    -89   -574       N  
ATOM   5384  CE2 TRP A 736     152.937  52.892   7.462  1.00112.00           C  
ANISOU 5384  CE2 TRP A 736    15103  14488  12964   -357   -211   -569       C  
ATOM   5385  CE3 TRP A 736     152.623  52.080   9.717  1.00 88.83           C  
ANISOU 5385  CE3 TRP A 736    12077  11324  10351   -326   -213   -542       C  
ATOM   5386  CZ2 TRP A 736     151.732  53.592   7.496  1.00118.40           C  
ANISOU 5386  CZ2 TRP A 736    15945  15271  13769   -435   -378   -577       C  
ATOM   5387  CZ3 TRP A 736     151.426  52.775   9.747  1.00 96.25           C  
ANISOU 5387  CZ3 TRP A 736    13023  12245  11301   -442   -369   -562       C  
ATOM   5388  CH2 TRP A 736     150.993  53.520   8.644  1.00108.87           C  
ANISOU 5388  CH2 TRP A 736    14677  13954  12733   -474   -457   -581       C  
ATOM   5389  N   TRP A 737     158.804  51.181  10.254  1.00101.41           N  
ANISOU 5389  N   TRP A 737    13020  13853  11659    357    341   -335       N  
ATOM   5390  CA  TRP A 737     160.016  50.400  10.451  1.00 96.49           C  
ANISOU 5390  CA  TRP A 737    12246  13477  10940    680    467   -355       C  
ATOM   5391  C   TRP A 737     160.248  50.097  11.926  1.00 94.93           C  
ANISOU 5391  C   TRP A 737    11948  13298  10824    870    426   -288       C  
ATOM   5392  O   TRP A 737     159.895  50.878  12.814  1.00 92.64           O  
ANISOU 5392  O   TRP A 737    11571  12988  10640    679    312   -215       O  
ATOM   5393  CB  TRP A 737     161.229  51.133   9.881  1.00100.75           C  
ANISOU 5393  CB  TRP A 737    12489  14473  11317    593    557   -353       C  
ATOM   5394  CG  TRP A 737     162.517  50.411  10.132  1.00103.10           C  
ANISOU 5394  CG  TRP A 737    12549  15137  11487    956    673   -390       C  
ATOM   5395  CD1 TRP A 737     163.002  49.338   9.443  1.00119.98           C  
ANISOU 5395  CD1 TRP A 737    14767  17324  13495   1305    806   -474       C  
ATOM   5396  CD2 TRP A 737     163.481  50.701  11.153  1.00 96.46           C  
ANISOU 5396  CD2 TRP A 737    11344  14700  10607   1044    662   -360       C  
ATOM   5397  NE1 TRP A 737     164.209  48.944   9.968  1.00123.73           N  
ANISOU 5397  NE1 TRP A 737    14946  18221  13844   1649    877   -487       N  
ATOM   5398  CE2 TRP A 737     164.526  49.765  11.018  1.00108.72           C  
ANISOU 5398  CE2 TRP A 737    12745  16572  11991   1490    782   -424       C  
ATOM   5399  CE3 TRP A 737     163.564  51.663  12.164  1.00 92.37           C  
ANISOU 5399  CE3 TRP A 737    10612  14327  10159    801    560   -301       C  
ATOM   5400  CZ2 TRP A 737     165.640  49.761  11.856  1.00102.01           C  
ANISOU 5400  CZ2 TRP A 737    11496  16235  11029   1717    788   -434       C  
ATOM   5401  CZ3 TRP A 737     164.671  51.658  12.996  1.00 95.96           C  
ANISOU 5401  CZ3 TRP A 737    10680  15271  10511    976    570   -323       C  
ATOM   5402  CH2 TRP A 737     165.694  50.714  12.836  1.00 99.89           C  
ANISOU 5402  CH2 TRP A 737    10991  16133  10829   1438    675   -390       C  
ATOM   5403  N   ALA A 738     160.860  48.936  12.177  1.00103.14           N  
ANISOU 5403  N   ALA A 738    13029  14374  11787   1287    526   -314       N  
ATOM   5404  CA  ALA A 738     161.249  48.514  13.512  1.00 98.19           C  
ANISOU 5404  CA  ALA A 738    12326  13813  11170   1575    506   -245       C  
ATOM   5405  C   ALA A 738     162.324  47.453  13.373  1.00 93.08           C  
ANISOU 5405  C   ALA A 738    11653  13378  10335   2091    645   -282       C  
ATOM   5406  O   ALA A 738     162.211  46.595  12.487  1.00 87.91           O  
ANISOU 5406  O   ALA A 738    11270  12517   9616   2254    763   -360       O  
ATOM   5407  CB  ALA A 738     160.056  47.961  14.300  1.00 92.84           C  
ANISOU 5407  CB  ALA A 738    11990  12639  10647   1569    461   -206       C  
ATOM   5408  N   PRO A 739     163.375  47.484  14.194  1.00106.36           N  
ANISOU 5408  N   PRO A 739    13016  15495  11901   2375    634   -245       N  
ATOM   5409  CA  PRO A 739     164.365  46.402  14.160  1.00103.88           C  
ANISOU 5409  CA  PRO A 739    12695  15401  11375   2977    758   -275       C  
ATOM   5410  C   PRO A 739     163.715  45.056  14.441  1.00106.03           C  
ANISOU 5410  C   PRO A 739    13525  15101  11662   3332    845   -245       C  
ATOM   5411  O   PRO A 739     162.710  44.960  15.149  1.00103.19           O  
ANISOU 5411  O   PRO A 739    13444  14304  11460   3174    792   -179       O  
ATOM   5412  CB  PRO A 739     165.355  46.792  15.263  1.00102.80           C  
ANISOU 5412  CB  PRO A 739    12107  15829  11124   3181    678   -236       C  
ATOM   5413  CG  PRO A 739     165.231  48.275  15.358  1.00105.80           C  
ANISOU 5413  CG  PRO A 739    12162  16421  11617   2577    563   -240       C  
ATOM   5414  CD  PRO A 739     163.777  48.571  15.103  1.00106.48           C  
ANISOU 5414  CD  PRO A 739    12634  15887  11937   2162    510   -199       C  
ATOM   5415  N   ARG A 740     164.305  44.003  13.873  1.00121.97           N  
ANISOU 5415  N   ARG A 740    15727  17119  13496   3809   1004   -303       N  
ATOM   5416  CA  ARG A 740     163.663  42.694  13.906  1.00123.19           C  
ANISOU 5416  CA  ARG A 740    16515  16647  13643   4086   1139   -303       C  
ATOM   5417  C   ARG A 740     163.743  42.048  15.284  1.00121.33           C  
ANISOU 5417  C   ARG A 740    16485  16269  13348   4518   1146   -171       C  
ATOM   5418  O   ARG A 740     162.789  41.388  15.712  1.00119.44           O  
ANISOU 5418  O   ARG A 740    16762  15420  13199   4469   1213   -131       O  
ATOM   5419  CB  ARG A 740     164.277  41.780  12.847  1.00131.65           C  
ANISOU 5419  CB  ARG A 740    17780  17726  14514   4482   1324   -413       C  
ATOM   5420  CG  ARG A 740     163.245  40.971  12.080  1.00133.23           C  
ANISOU 5420  CG  ARG A 740    18585  17252  14785   4309   1452   -513       C  
ATOM   5421  CD  ARG A 740     163.802  40.440  10.774  1.00146.36           C  
ANISOU 5421  CD  ARG A 740    20338  19001  16270   4528   1603   -657       C  
ATOM   5422  NE  ARG A 740     162.747  39.916   9.911  1.00166.13           N  
ANISOU 5422  NE  ARG A 740    23331  20938  18852   4210   1691   -795       N  
ATOM   5423  CZ  ARG A 740     162.937  39.511   8.659  1.00184.18           C  
ANISOU 5423  CZ  ARG A 740    25759  23208  21012   4263   1811   -950       C  
ATOM   5424  NH1 ARG A 740     161.919  39.050   7.946  1.00185.05           N  
ANISOU 5424  NH1 ARG A 740    26301  22825  21184   3936   1874  -1099       N  
ATOM   5425  NH2 ARG A 740     164.147  39.570   8.118  1.00190.92           N  
ANISOU 5425  NH2 ARG A 740    26302  24577  21663   4632   1871   -975       N  
ATOM   5426  N   TRP A 741     164.856  42.229  16.001  1.00129.48           N  
ANISOU 5426  N   TRP A 741    17117  17875  14204   4930   1085   -112       N  
ATOM   5427  CA  TRP A 741     164.958  41.654  17.337  1.00136.94           C  
ANISOU 5427  CA  TRP A 741    18254  18724  15050   5386   1077     26       C  
ATOM   5428  C   TRP A 741     164.013  42.318  18.327  1.00131.96           C  
ANISOU 5428  C   TRP A 741    17633  17864  14641   4937    939    120       C  
ATOM   5429  O   TRP A 741     163.850  41.804  19.438  1.00135.58           O  
ANISOU 5429  O   TRP A 741    18356  18116  15041   5240    951    244       O  
ATOM   5430  CB  TRP A 741     166.403  41.732  17.851  1.00157.64           C  
ANISOU 5430  CB  TRP A 741    20376  22126  17392   5958   1019     41       C  
ATOM   5431  CG  TRP A 741     166.816  43.061  18.439  1.00172.59           C  
ANISOU 5431  CG  TRP A 741    21584  24655  19337   5606    810     32       C  
ATOM   5432  CD1 TRP A 741     166.526  43.533  19.691  1.00178.31           C  
ANISOU 5432  CD1 TRP A 741    22213  25412  20127   5495    666    130       C  
ATOM   5433  CD2 TRP A 741     167.624  44.066  17.812  1.00180.53           C  
ANISOU 5433  CD2 TRP A 741    21938  26351  20306   5309    749    -95       C  
ATOM   5434  NE1 TRP A 741     167.085  44.775  19.870  1.00180.83           N  
ANISOU 5434  NE1 TRP A 741    21875  26375  20457   5133    513     58       N  
ATOM   5435  CE2 TRP A 741     167.766  45.124  18.733  1.00182.11           C  
ANISOU 5435  CE2 TRP A 741    21695  26942  20557   4994    571    -80       C  
ATOM   5436  CE3 TRP A 741     168.234  44.177  16.559  1.00187.57           C  
ANISOU 5436  CE3 TRP A 741    22601  27555  21113   5252    847   -228       C  
ATOM   5437  CZ2 TRP A 741     168.492  46.278  18.440  1.00181.02           C  
ANISOU 5437  CZ2 TRP A 741    20923  27466  20389   4592    504   -201       C  
ATOM   5438  CZ3 TRP A 741     168.955  45.324  16.270  1.00186.29           C  
ANISOU 5438  CZ3 TRP A 741    21794  28068  20920   4862    784   -332       C  
ATOM   5439  CH2 TRP A 741     169.077  46.358  17.206  1.00182.01           C  
ANISOU 5439  CH2 TRP A 741    20848  27876  20431   4519    621   -322       C  
ATOM   5440  N   MET A 742     163.396  43.439  17.953  1.00123.73           N  
ANISOU 5440  N   MET A 742    16334  16852  13826   4258    819     68       N  
ATOM   5441  CA  MET A 742     162.426  44.122  18.797  1.00112.91           C  
ANISOU 5441  CA  MET A 742    14976  15260  12666   3822    694    139       C  
ATOM   5442  C   MET A 742     160.984  43.781  18.445  1.00110.51           C  
ANISOU 5442  C   MET A 742    15153  14275  12561   3436    763    110       C  
ATOM   5443  O   MET A 742     160.107  43.898  19.309  1.00 99.49           O  
ANISOU 5443  O   MET A 742    13917  12591  11295   3230    720    179       O  
ATOM   5444  CB  MET A 742     162.626  45.640  18.701  1.00100.46           C  
ANISOU 5444  CB  MET A 742    12839  14145  11186   3341    520    100       C  
ATOM   5445  CG  MET A 742     164.031  46.100  19.063  1.00105.70           C  
ANISOU 5445  CG  MET A 742    12954  15557  11650   3595    453     83       C  
ATOM   5446  SD  MET A 742     164.313  47.849  18.733  1.00 71.88           S  
ANISOU 5446  SD  MET A 742     8106  11751   7454   2944    321      2       S  
ATOM   5447  CE  MET A 742     162.996  48.582  19.691  1.00 69.50           C  
ANISOU 5447  CE  MET A 742     7983  11024   7400   2501    184     90       C  
ATOM   5448  N   LYS A 743     160.721  43.362  17.205  1.00118.39           N  
ANISOU 5448  N   LYS A 743    16362  15053  13568   3326    871    -10       N  
ATOM   5449  CA  LYS A 743     159.368  42.992  16.805  1.00109.71           C  
ANISOU 5449  CA  LYS A 743    15680  13380  12625   2944    937    -85       C  
ATOM   5450  C   LYS A 743     158.984  41.607  17.312  1.00105.63           C  
ANISOU 5450  C   LYS A 743    15782  12313  12039   3229   1139    -57       C  
ATOM   5451  O   LYS A 743     157.808  41.366  17.607  1.00103.53           O  
ANISOU 5451  O   LYS A 743    15828  11602  11908   2890   1185    -81       O  
ATOM   5452  CB  LYS A 743     159.239  43.054  15.281  1.00109.11           C  
ANISOU 5452  CB  LYS A 743    15602  13305  12551   2718    973   -244       C  
ATOM   5453  CG  LYS A 743     158.002  43.786  14.771  1.00106.33           C  
ANISOU 5453  CG  LYS A 743    15213  12799  12387   2112    866   -328       C  
ATOM   5454  CD  LYS A 743     156.728  43.007  15.057  1.00119.22           C  
ANISOU 5454  CD  LYS A 743    17305  13878  14117   1904    958   -391       C  
ATOM   5455  CE  LYS A 743     155.508  43.705  14.479  1.00125.11           C  
ANISOU 5455  CE  LYS A 743    17959  14568  15009   1354    839   -506       C  
ATOM   5456  NZ  LYS A 743     154.250  42.968  14.788  1.00132.00           N  
ANISOU 5456  NZ  LYS A 743    19208  14983  15964   1096    936   -604       N  
ATOM   5457  N   ARG A 744     159.952  40.692  17.423  1.00113.04           N  
ANISOU 5457  N   ARG A 744    16922  13278  12750   3850   1276    -11       N  
ATOM   5458  CA  ARG A 744     159.652  39.361  17.942  1.00110.76           C  
ANISOU 5458  CA  ARG A 744    17317  12413  12356   4167   1502     37       C  
ATOM   5459  C   ARG A 744     159.371  39.388  19.439  1.00106.30           C  
ANISOU 5459  C   ARG A 744    16846  11738  11805   4251   1470    212       C  
ATOM   5460  O   ARG A 744     158.582  38.573  19.931  1.00102.41           O  
ANISOU 5460  O   ARG A 744    16931  10661  11320   4194   1648    242       O  
ATOM   5461  CB  ARG A 744     160.800  38.397  17.640  1.00122.47           C  
ANISOU 5461  CB  ARG A 744    19023  13960  13550   4896   1661     49       C  
ATOM   5462  CG  ARG A 744     160.823  37.861  16.214  1.00130.24           C  
ANISOU 5462  CG  ARG A 744    20229  14772  14485   4858   1801   -136       C  
ATOM   5463  CD  ARG A 744     159.497  37.212  15.833  1.00134.77           C  
ANISOU 5463  CD  ARG A 744    21390  14632  15185   4380   1964   -266       C  
ATOM   5464  NE  ARG A 744     158.977  36.339  16.884  1.00144.17           N  
ANISOU 5464  NE  ARG A 744    23190  15253  16333   4505   2142   -162       N  
ATOM   5465  CZ  ARG A 744     159.251  35.043  16.990  1.00146.44           C  
ANISOU 5465  CZ  ARG A 744    24177  15064  16400   4992   2417   -139       C  
ATOM   5466  NH1 ARG A 744     160.048  34.456  16.108  1.00142.57           N  
ANISOU 5466  NH1 ARG A 744    23838  14617  15714   5430   2532   -224       N  
ATOM   5467  NH2 ARG A 744     158.728  34.333  17.981  1.00152.63           N  
ANISOU 5467  NH2 ARG A 744    25542  15310  17139   5051   2594    -28       N  
ATOM   5468  N   VAL A 745     160.004  40.305  20.175  1.00109.54           N  
ANISOU 5468  N   VAL A 745    16715  12702  12201   4361   1264    315       N  
ATOM   5469  CA  VAL A 745     159.721  40.440  21.603  1.00109.90           C  
ANISOU 5469  CA  VAL A 745    16810  12693  12255   4416   1210    472       C  
ATOM   5470  C   VAL A 745     158.259  40.810  21.820  1.00101.36           C  
ANISOU 5470  C   VAL A 745    15856  11223  11432   3749   1197    436       C  
ATOM   5471  O   VAL A 745     157.583  40.253  22.694  1.00101.15           O  
ANISOU 5471  O   VAL A 745    16254  10774  11406   3737   1318    521       O  
ATOM   5472  CB  VAL A 745     160.666  41.475  22.241  1.00105.35           C  
ANISOU 5472  CB  VAL A 745    15567  12845  11615   4574    973    537       C  
ATOM   5473  CG1 VAL A 745     160.346  41.646  23.717  1.00105.32           C  
ANISOU 5473  CG1 VAL A 745    15611  12798  11606   4621    908    687       C  
ATOM   5474  CG2 VAL A 745     162.113  41.056  22.056  1.00111.36           C  
ANISOU 5474  CG2 VAL A 745    16150  14074  12086   5257    992    547       C  
ATOM   5475  N   GLN A 746     157.810  41.773  21.052  1.00100.76           N  
ANISOU 5475  N   GLN A 746    15423  11306  11555   3203   1059    308       N  
ATOM   5476  CA  GLN A 746     156.447  42.174  21.143  1.00104.76           C  
ANISOU 5476  CA  GLN A 746    16007  11515  12283   2603   1037    243       C  
ATOM   5477  C   GLN A 746     155.643  40.955  20.787  1.00110.49           C  
ANISOU 5477  C   GLN A 746    17366  11608  13008   2470   1293    157       C  
ATOM   5478  O   GLN A 746     154.633  40.670  21.403  1.00110.91           O  
ANISOU 5478  O   GLN A 746    17646  11340  13155   2163   1364    160       O  
ATOM   5479  CB  GLN A 746     156.183  43.276  20.139  1.00102.67           C  
ANISOU 5479  CB  GLN A 746    15312  11532  12168   2153    863    115       C  
ATOM   5480  CG  GLN A 746     154.717  43.517  19.883  1.00116.01           C  
ANISOU 5480  CG  GLN A 746    17057  12975  14047   1585    833     10       C  
ATOM   5481  CD  GLN A 746     154.489  44.211  18.572  1.00124.31           C  
ANISOU 5481  CD  GLN A 746    17868  14196  15169   1254    726   -141       C  
ATOM   5482  OE1 GLN A 746     155.433  44.568  17.889  1.00119.85           O  
ANISOU 5482  OE1 GLN A 746    17176  13849  14512   1420    720   -175       O  
ATOM   5483  NE2 GLN A 746     153.234  44.400  18.211  1.00133.37           N  
ANISOU 5483  NE2 GLN A 746    18951  15270  16455    809    646   -234       N  
ATOM   5484  N   GLU A 747     156.099  40.226  19.784  1.00113.46           N  
ANISOU 5484  N   GLU A 747    18043  11803  13265   2679   1453     63       N  
ATOM   5485  CA  GLU A 747     155.415  39.026  19.356  1.00111.31           C  
ANISOU 5485  CA  GLU A 747    18407  10912  12975   2498   1719    -60       C  
ATOM   5486  C   GLU A 747     155.424  37.982  20.445  1.00109.63           C  
ANISOU 5486  C   GLU A 747    18813  10247  12594   2893   1965     88       C  
ATOM   5487  O   GLU A 747     154.429  37.318  20.687  1.00108.00           O  
ANISOU 5487  O   GLU A 747    19113   9507  12415   2584   2181     33       O  
ATOM   5488  CB  GLU A 747     156.046  38.492  18.083  1.00105.60           C  
ANISOU 5488  CB  GLU A 747    17815  10142  12167   2574   1808   -229       C  
ATOM   5489  CG  GLU A 747     156.048  39.513  16.971  1.00 99.75           C  
ANISOU 5489  CG  GLU A 747    16544   9798  11557   2179   1593   -374       C  
ATOM   5490  CD  GLU A 747     155.992  38.882  15.612  1.00 96.26           C  
ANISOU 5490  CD  GLU A 747    16217   9355  11001   2298   1679   -531       C  
ATOM   5491  OE1 GLU A 747     157.014  38.335  15.179  1.00 97.52           O  
ANISOU 5491  OE1 GLU A 747    16781   9301  10971   2782   1877   -510       O  
ATOM   5492  OE2 GLU A 747     154.928  38.941  14.979  1.00 93.20           O  
ANISOU 5492  OE2 GLU A 747    15538   9182  10692   1940   1553   -675       O  
ATOM   5493  N   LYS A 748     156.548  37.856  21.128  1.00 30.00           N  
ATOM   5494  CA  LYS A 748     156.685  36.839  22.151  1.00 30.00           C  
ATOM   5495  C   LYS A 748     155.710  37.037  23.298  1.00 30.00           C  
ATOM   5496  O   LYS A 748     155.192  36.076  23.838  1.00 30.00           O  
ATOM   5497  CB  LYS A 748     158.125  36.742  22.638  1.00 30.00           C  
ATOM   5498  CG  LYS A 748     159.012  35.989  21.660  1.00 30.00           C  
ATOM   5499  CD  LYS A 748     160.451  35.903  22.131  1.00 30.00           C  
ATOM   5500  CE  LYS A 748     161.334  35.274  21.066  1.00 30.00           C  
ATOM   5501  NZ  LYS A 748     162.782  35.437  21.365  1.00 30.00           N  
ATOM   5502  N   LEU A 749     155.468  38.281  23.675  1.00110.51           N  
ANISOU 5502  N   LEU A 749    18897  10484  12607   3347   1879    540       N  
ATOM   5503  CA  LEU A 749     154.586  38.595  24.786  1.00116.60           C  
ANISOU 5503  CA  LEU A 749    19628  11199  13478   3062   1841    632       C  
ATOM   5504  C   LEU A 749     153.088  38.373  24.552  1.00120.04           C  
ANISOU 5504  C   LEU A 749    20229  11269  14113   2327   1954    461       C  
ATOM   5505  O   LEU A 749     152.318  38.405  25.498  1.00120.61           O  
ANISOU 5505  O   LEU A 749    20303  11261  14262   2049   1963    514       O  
ATOM   5506  CB  LEU A 749     154.847  40.009  25.290  1.00120.21           C  
ANISOU 5506  CB  LEU A 749    19330  12312  14032   3026   1500    687       C  
ATOM   5507  CG  LEU A 749     156.177  40.206  26.009  1.00116.09           C  
ANISOU 5507  CG  LEU A 749    18605  12192  13310   3632   1376    882       C  
ATOM   5508  CD1 LEU A 749     157.305  39.534  25.252  1.00125.27           C  
ANISOU 5508  CD1 LEU A 749    19942  13447  14209   4323   1460    929       C  
ATOM   5509  CD2 LEU A 749     156.471  41.677  26.201  1.00 98.81           C  
ANISOU 5509  CD2 LEU A 749    15657  10642  11243   3436   1055    855       C  
ATOM   5510  N   GLY A 750     152.664  38.191  23.308  1.00121.50           N  
ANISOU 5510  N   GLY A 750    20527  11274  14362   2011   2038    243       N  
ATOM   5511  CA  GLY A 750     151.253  38.163  22.981  1.00114.39           C  
ANISOU 5511  CA  GLY A 750    19699  10138  13626   1303   2122     35       C  
ATOM   5512  C   GLY A 750     150.677  39.507  22.604  1.00106.60           C  
ANISOU 5512  C   GLY A 750    18019   9631  12851    875   1820    -72       C  
ATOM   5513  O   GLY A 750     149.480  39.739  22.800  1.00104.31           O  
ANISOU 5513  O   GLY A 750    17659   9286  12687    358   1832   -188       O  
ATOM   5514  N   LEU A 751     151.499  40.405  22.060  1.00104.42           N  
ANISOU 5514  N   LEU A 751    17241   9836  12597   1083   1562    -42       N  
ATOM   5515  CA  LEU A 751     151.074  41.760  21.726  1.00103.83           C  
ANISOU 5515  CA  LEU A 751    16565  10197  12687    752   1280   -110       C  
ATOM   5516  C   LEU A 751     151.287  42.084  20.250  1.00109.55           C  
ANISOU 5516  C   LEU A 751    17066  11131  13426    658   1175   -267       C  
ATOM   5517  O   LEU A 751     151.344  43.262  19.881  1.00 95.15           O  
ANISOU 5517  O   LEU A 751    14768   9706  11681    544    937   -273       O  
ATOM   5518  CB  LEU A 751     151.810  42.771  22.607  1.00 99.25           C  
ANISOU 5518  CB  LEU A 751    15581  10019  12111   1018   1065     87       C  
ATOM   5519  CG  LEU A 751     151.741  42.501  24.113  1.00 94.57           C  
ANISOU 5519  CG  LEU A 751    15189   9277  11466   1187   1147    262       C  
ATOM   5520  CD1 LEU A 751     152.694  43.410  24.874  1.00 83.16           C  
ANISOU 5520  CD1 LEU A 751    13345   8278   9976   1506    933    426       C  
ATOM   5521  CD2 LEU A 751     150.316  42.663  24.623  1.00 92.50           C  
ANISOU 5521  CD2 LEU A 751    14966   8845  11336    695   1191    187       C  
ATOM   5522  N   GLY A 752     151.400  41.067  19.398  1.00122.36           N  
ANISOU 5522  N   GLY A 752    19062  12473  14956    703   1362   -395       N  
ATOM   5523  CA  GLY A 752     151.652  41.286  17.987  1.00124.22           C  
ANISOU 5523  CA  GLY A 752    19125  12900  15172    648   1283   -544       C  
ATOM   5524  C   GLY A 752     150.430  41.106  17.111  1.00140.16           C  
ANISOU 5524  C   GLY A 752    21210  14793  17250    125   1313   -812       C  
ATOM   5525  O   GLY A 752     150.547  40.738  15.939  1.00139.76           O  
ANISOU 5525  O   GLY A 752    21255  14718  17128     91   1357   -976       O  
ATOM   5526  N   GLU A 753     149.249  41.366  17.667  1.00156.68           N  
ANISOU 5526  N   GLU A 753    23228  16850  19453   -280   1290   -877       N  
ATOM   5527  CA  GLU A 753     147.993  41.269  16.925  1.00162.28           C  
ANISOU 5527  CA  GLU A 753    23909  17548  20201   -799   1295  -1162       C  
ATOM   5528  C   GLU A 753     147.631  42.573  16.230  1.00161.46           C  
ANISOU 5528  C   GLU A 753    23261  17931  20157   -949    991  -1220       C  
ATOM   5529  O   GLU A 753     146.468  42.986  16.235  1.00166.37           O  
ANISOU 5529  O   GLU A 753    23673  18702  20838  -1317    903  -1365       O  
ATOM   5530  CB  GLU A 753     146.878  40.826  17.864  1.00161.81           C  
ANISOU 5530  CB  GLU A 753    24036  17246  20199  -1165   1451  -1229       C  
ATOM   5531  CG  GLU A 753     147.027  39.403  18.369  1.00159.71           C  
ANISOU 5531  CG  GLU A 753    24438  16408  19838  -1110   1810  -1219       C  
ATOM   5532  CD  GLU A 753     146.302  39.178  19.677  1.00156.35           C  
ANISOU 5532  CD  GLU A 753    24178  15772  19455  -1320   1960  -1151       C  
ATOM   5533  OE1 GLU A 753     146.164  40.149  20.450  1.00151.77           O  
ANISOU 5533  OE1 GLU A 753    23204  15494  18968  -1277   1767  -1004       O  
ATOM   5534  OE2 GLU A 753     145.868  38.035  19.933  1.00158.09           O  
ANISOU 5534  OE2 GLU A 753    24953  15512  19603  -1541   2288  -1249       O  
ATOM   5535  N   THR A 754     148.612  43.245  15.624  1.00151.59           N  
ANISOU 5535  N   THR A 754    21785  16946  18866   -655    840  -1111       N  
ATOM   5536  CA  THR A 754     148.351  44.483  14.899  1.00132.35           C  
ANISOU 5536  CA  THR A 754    18924  14917  16446   -761    582  -1143       C  
ATOM   5537  C   THR A 754     147.571  44.256  13.612  1.00132.07           C  
ANISOU 5537  C   THR A 754    18892  14950  16338  -1042    559  -1422       C  
ATOM   5538  O   THR A 754     147.119  45.230  13.001  1.00118.79           O  
ANISOU 5538  O   THR A 754    16899  13597  14640  -1140    348  -1470       O  
ATOM   5539  CB  THR A 754     149.668  45.192  14.580  1.00111.41           C  
ANISOU 5539  CB  THR A 754    16083  12504  13745   -417    479   -961       C  
ATOM   5540  OG1 THR A 754     150.392  44.440  13.599  1.00106.01           O  
ANISOU 5540  OG1 THR A 754    15600  11740  12938   -251    601  -1039       O  
ATOM   5541  CG2 THR A 754     150.519  45.319  15.834  1.00 97.22           C  
ANISOU 5541  CG2 THR A 754    14264  10693  11983   -129    502   -721       C  
ATOM   5542  N   GLU A 755     147.411  42.980  13.242  1.00139.08           N  
ANISOU 5542  N   GLU A 755    20150  15535  17157  -1159    775  -1612       N  
ATOM   5543  CA  GLU A 755     146.697  42.538  12.036  1.00138.79           C  
ANISOU 5543  CA  GLU A 755    20138  15569  17028  -1456    768  -1921       C  
ATOM   5544  C   GLU A 755     145.760  41.334  12.266  1.00132.20           C  
ANISOU 5544  C   GLU A 755    19588  14441  16202  -1867    979  -2164       C  
ATOM   5545  O   GLU A 755     146.094  40.426  13.013  1.00126.85           O  
ANISOU 5545  O   GLU A 755    19358  13319  15519  -1815   1246  -2127       O  
ATOM   5546  CB  GLU A 755     147.726  42.167  10.966  1.00141.49           C  
ANISOU 5546  CB  GLU A 755    20684  15843  17233  -1232    849  -1970       C  
ATOM   5547  CG  GLU A 755     147.156  41.681   9.644  1.00146.24           C  
ANISOU 5547  CG  GLU A 755    21314  16541  17709  -1524    833  -2302       C  
ATOM   5548  CD  GLU A 755     148.148  40.856   8.845  1.00140.21           C  
ANISOU 5548  CD  GLU A 755    20819  15656  16799  -1298    954  -2364       C  
ATOM   5549  OE1 GLU A 755     149.232  40.535   9.370  1.00135.96           O  
ANISOU 5549  OE1 GLU A 755    20432  14973  16255   -896   1059  -2151       O  
ATOM   5550  OE2 GLU A 755     147.839  40.522   7.690  1.00136.07           O  
ANISOU 5550  OE2 GLU A 755    20337  15217  16146  -1507    943  -2640       O  
ATOM   5551  N   LEU A 756     144.622  41.311  11.565  1.00131.85           N  
ANISOU 5551  N   LEU A 756    19294  14660  16145  -2272    870  -2417       N  
ATOM   5552  CA  LEU A 756     143.625  40.220  11.643  1.00125.48           C  
ANISOU 5552  CA  LEU A 756    18707  13651  15318  -2764   1080  -2718       C  
ATOM   5553  C   LEU A 756     143.873  38.960  10.771  1.00134.05           C  
ANISOU 5553  C   LEU A 756    20270  14388  16277  -2857   1317  -2935       C  
ATOM   5554  O   LEU A 756     144.572  39.027   9.760  1.00127.07           O  
ANISOU 5554  O   LEU A 756    19403  13580  15299  -2597   1245  -2926       O  
ATOM   5555  CB  LEU A 756     142.222  40.769  11.365  1.00117.12           C  
ANISOU 5555  CB  LEU A 756    17195  13079  14225  -3146    882  -2989       C  
ATOM   5556  CG  LEU A 756     141.718  41.855  12.318  1.00125.16           C  
ANISOU 5556  CG  LEU A 756    17866  14335  15355  -3237    770  -2897       C  
ATOM   5557  CD1 LEU A 756     140.352  42.362  11.882  1.00126.84           C  
ANISOU 5557  CD1 LEU A 756    17602  15109  15481  -3524    555  -3188       C  
ATOM   5558  CD2 LEU A 756     141.671  41.336  13.747  1.00125.25           C  
ANISOU 5558  CD2 LEU A 756    18208  13935  15445  -3496   1077  -2896       C  
ATOM   5559  N   PRO A 757     143.288  37.811  11.182  1.00152.83           N  
ANISOU 5559  N   PRO A 757    23077  16358  18633  -3240   1627  -3138       N  
ATOM   5560  CA  PRO A 757     143.268  36.437  10.631  1.00151.13           C  
ANISOU 5560  CA  PRO A 757    23373  15773  18277  -3372   1874  -3384       C  
ATOM   5561  C   PRO A 757     142.258  36.179   9.489  1.00146.78           C  
ANISOU 5561  C   PRO A 757    22554  15620  17596  -3678   1716  -3755       C  
ATOM   5562  O   PRO A 757     141.367  37.005   9.290  1.00141.01           O  
ANISOU 5562  O   PRO A 757    21260  15442  16877  -3829   1437  -3841       O  
ATOM   5563  CB  PRO A 757     142.901  35.591  11.848  1.00153.12           C  
ANISOU 5563  CB  PRO A 757    24119  15529  18532  -3818   2244  -3534       C  
ATOM   5564  CG  PRO A 757     142.026  36.487  12.653  1.00157.67           C  
ANISOU 5564  CG  PRO A 757    24247  16434  19225  -4111   2124  -3523       C  
ATOM   5565  CD  PRO A 757     142.524  37.893  12.441  1.00159.09           C  
ANISOU 5565  CD  PRO A 757    23958  16976  19512  -3579   1797  -3151       C  
ATOM   5566  N   ASP A 758     142.393  35.063   8.759  1.00187.40           N  
ANISOU 5566  N   ASP A 758    29538  20103  21564   9103   2781  -4059       N  
ATOM   5567  CA  ASP A 758     141.489  34.759   7.681  1.00180.19           C  
ANISOU 5567  CA  ASP A 758    28631  19423  20412   8932   2931  -4223       C  
ATOM   5568  C   ASP A 758     140.266  34.172   8.334  1.00177.85           C  
ANISOU 5568  C   ASP A 758    28677  18741  20158   8767   2906  -4312       C  
ATOM   5569  O   ASP A 758     140.322  33.156   9.015  1.00173.72           O  
ANISOU 5569  O   ASP A 758    28319  17826  19859   8883   2840  -4451       O  
ATOM   5570  CB  ASP A 758     142.108  33.752   6.718  1.00178.36           C  
ANISOU 5570  CB  ASP A 758    28143  19503  20122   9130   3092  -4574       C  
ATOM   5571  N   GLU A 759     139.152  34.831   8.093  1.00179.72           N  
ANISOU 5571  N   GLU A 759    29018  19092  20177   8495   2960  -4227       N  
ATOM   5572  CA  GLU A 759     137.865  34.428   8.618  1.00185.67           C  
ANISOU 5572  CA  GLU A 759    30083  19530  20932   8310   2951  -4300       C  
ATOM   5573  C   GLU A 759     136.907  34.429   7.447  1.00192.81           C  
ANISOU 5573  C   GLU A 759    30926  20703  21630   8232   3130  -4578       C  
ATOM   5574  O   GLU A 759     137.142  35.073   6.423  1.00195.04           O  
ANISOU 5574  O   GLU A 759    30937  21434  21737   8275   3255  -4656       O  
ATOM   5575  CB  GLU A 759     137.371  35.387   9.700  1.00178.46           C  
ANISOU 5575  CB  GLU A 759    29386  18471  19949   8039   2848  -3940       C  
ATOM   5576  CG  GLU A 759     138.313  35.573  10.875  1.00175.00           C  
ANISOU 5576  CG  GLU A 759    28982  17828  19680   8098   2675  -3629       C  
ATOM   5577  CD  GLU A 759     137.574  35.822  12.174  1.00166.06           C  
ANISOU 5577  CD  GLU A 759    28104  16489  18502   7836   2565  -3296       C  
ATOM   5578  OE1 GLU A 759     136.331  35.814  12.157  1.00162.81           O  
ANISOU 5578  OE1 GLU A 759    27863  16049  17948   7615   2619  -3319       O  
ATOM   5579  OE2 GLU A 759     138.235  36.012  13.215  1.00163.10           O  
ANISOU 5579  OE2 GLU A 759    27760  15977  18234   7852   2425  -3010       O  
ATOM   5580  N   ARG A 760     135.816  33.705   7.581  1.00192.29           N  
ANISOU 5580  N   ARG A 760    31115  20357  21588   8116   3142  -4729       N  
ATOM   5581  CA  ARG A 760     134.878  33.624   6.465  1.00184.47           C  
ANISOU 5581  CA  ARG A 760    30104  19561  20425   8040   3303  -5011       C  
ATOM   5582  C   ARG A 760     133.509  34.099   6.932  1.00165.16           C  
ANISOU 5582  C   ARG A 760    27892  17012  17850   7703   3290  -4870       C  
ATOM   5583  O   ARG A 760     132.834  33.401   7.697  1.00163.51           O  
ANISOU 5583  O   ARG A 760    27924  16403  17798   7581   3185  -4836       O  
ATOM   5584  CB  ARG A 760     134.803  32.199   5.914  1.00186.80           C  
ANISOU 5584  CB  ARG A 760    30337  19696  20943   8108   3293  -5316       C  
ATOM   5585  N   LYS A 761     133.101  35.278   6.469  1.00150.78           N  
ANISOU 5585  N   LYS A 761    25983  15560  15747   7544   3394  -4780       N  
ATOM   5586  CA  LYS A 761     131.777  35.816   6.767  1.00147.83           C  
ANISOU 5586  CA  LYS A 761    25791  15153  15226   7211   3397  -4652       C  
ATOM   5587  C   LYS A 761     131.463  37.019   5.882  1.00145.78           C  
ANISOU 5587  C   LYS A 761    25327  15400  14664   7056   3534  -4622       C  
ATOM   5588  O   LYS A 761     132.240  37.972   5.809  1.00144.96           O  
ANISOU 5588  O   LYS A 761    25054  15592  14431   7120   3560  -4463       O  
ATOM   5589  CB  LYS A 761     131.671  36.210   8.240  1.00154.42           C  
ANISOU 5589  CB  LYS A 761    26882  15676  16115   7092   3249  -4300       C  
TER    5590      LYS A 761                                                      
HETATM 5591  N   L9Q A 801     142.757  76.157  52.888  0.99 99.83           N  
HETATM 5592  P   L9Q A 801     145.648  73.709  53.630  0.99102.58           P  
HETATM 5593  C1  L9Q A 801     145.673  76.281  53.232  0.99107.78           C  
HETATM 5594  C2  L9Q A 801     145.600  77.551  54.045  0.99117.26           C  
HETATM 5595  O2  L9Q A 801     146.898  77.937  54.334  0.99122.60           O  
HETATM 5596  C3  L9Q A 801     144.857  78.621  53.237  0.99110.97           C  
HETATM 5597  O3  L9Q A 801     145.127  79.920  53.725  0.99110.60           O  
HETATM 5598  C4  L9Q A 801     143.958  74.512  51.794  0.99 81.13           C  
HETATM 5599  C5  L9Q A 801     142.600  74.885  52.258  0.99 83.85           C  
HETATM 5600  C11 L9Q A 801     144.016  80.814  53.694  0.99106.53           C  
HETATM 5601  O11 L9Q A 801     143.049  80.535  53.108  0.99 99.21           O  
HETATM 5602  C12 L9Q A 801     144.070  82.154  54.441  0.99104.28           C  
HETATM 5603  C13 L9Q A 801     142.676  82.644  54.790  0.99 98.87           C  
HETATM 5604  C14 L9Q A 801     142.696  83.691  55.910  0.99105.72           C  
HETATM 5605  C15 L9Q A 801     143.900  83.506  56.827  0.99105.94           C  
HETATM 5606  C16 L9Q A 801     144.010  84.559  57.941  0.99104.59           C  
HETATM 5607  C17 L9Q A 801     142.666  85.025  58.560  0.99105.98           C  
HETATM 5608  C18 L9Q A 801     142.814  86.345  59.373  0.99 95.16           C  
HETATM 5609  C19 L9Q A 801     142.173  86.349  60.776  0.99 95.31           C  
HETATM 5610  O1P L9Q A 801     145.398  72.876  54.832  0.99105.39           O  
HETATM 5611  C20 L9Q A 801     143.106  86.914  61.869  0.99 91.59           C  
HETATM 5612  C21 L9Q A 801     142.466  86.954  63.265  0.99 91.75           C  
HETATM 5613  C22 L9Q A 801     143.464  86.763  64.416  0.99 99.85           C  
HETATM 5614  C23 L9Q A 801     143.292  87.729  65.591  0.99 99.53           C  
HETATM 5615  C24 L9Q A 801     142.733  87.110  66.876  0.99103.64           C  
HETATM 5616  C25 L9Q A 801     143.504  87.592  68.114  0.99100.64           C  
HETATM 5617  C26 L9Q A 801     142.533  88.181  69.128  0.99 93.33           C  
HETATM 5618  C27 L9Q A 801     142.820  87.743  70.558  0.99 85.98           C  
HETATM 5619  O2P L9Q A 801     146.845  73.112  53.027  0.99108.66           O  
HETATM 5620  C31 L9Q A 801     147.087  78.233  55.708  0.99124.02           C  
HETATM 5621  O31 L9Q A 801     146.980  77.393  56.504  0.99112.51           O  
HETATM 5622  C32 L9Q A 801     147.433  79.670  56.116  0.99132.75           C  
HETATM 5623  C33 L9Q A 801     147.106  80.059  57.575  0.99129.84           C  
HETATM 5624  C34 L9Q A 801     147.723  81.426  57.941  0.99116.19           C  
HETATM 5625  C35 L9Q A 801     146.735  82.593  58.098  0.99102.89           C  
HETATM 5626  C36 L9Q A 801     146.963  83.148  59.505  0.99102.59           C  
HETATM 5627  C37 L9Q A 801     146.190  84.455  59.776  0.99110.13           C  
HETATM 5628  C38 L9Q A 801     146.365  84.925  61.234  0.99108.10           C  
HETATM 5629  C39 L9Q A 801     147.790  85.324  61.614  0.99104.48           C  
HETATM 5630  O3P L9Q A 801     145.981  75.255  54.106  0.99 99.29           O  
HETATM 5631  C40 L9Q A 801     148.527  84.189  62.336  0.99104.83           C  
HETATM 5632  C41 L9Q A 801     149.339  83.282  61.398  0.99 99.61           C  
HETATM 5633  C42 L9Q A 801     150.280  82.379  62.221  0.99101.74           C  
HETATM 5634  C43 L9Q A 801     150.810  83.079  63.514  0.99105.92           C  
HETATM 5635  C44 L9Q A 801     151.789  82.116  64.249  0.99113.63           C  
HETATM 5636  C45 L9Q A 801     150.949  81.265  65.242  0.99119.48           C  
HETATM 5637  C46 L9Q A 801     150.164  82.128  66.232  0.99126.05           C  
HETATM 5638  C47 L9Q A 801     150.157  81.527  67.624  0.99136.06           C  
HETATM 5639  C48 L9Q A 801     149.019  82.051  68.471  0.99139.76           C  
HETATM 5640  O4P L9Q A 801     144.372  73.541  52.653  0.99 90.47           O  
HETATM 5641  C1B LMT A 802     159.430  81.179  40.444  0.95104.76           C  
HETATM 5642  C2B LMT A 802     159.422  82.707  40.463  0.95104.44           C  
HETATM 5643  C3B LMT A 802     158.939  83.211  41.792  0.95107.42           C  
HETATM 5644  C4B LMT A 802     159.507  82.269  42.830  0.95118.49           C  
HETATM 5645  C5B LMT A 802     158.790  80.944  42.726  0.95 90.36           C  
HETATM 5646  C6B LMT A 802     157.521  81.009  43.537  0.95 89.27           C  
HETATM 5647  O1B LMT A 802     160.672  80.675  40.902  0.95100.97           O  
HETATM 5648  O2B LMT A 802     160.733  83.231  40.274  0.95104.17           O  
HETATM 5649  O3B LMT A 802     157.528  83.049  41.763  0.95 88.98           O  
HETATM 5650  O4' LMT A 802     160.884  82.014  42.548  0.95132.65           O  
HETATM 5651  O5B LMT A 802     158.471  80.672  41.364  0.95 93.62           O  
HETATM 5652  O6B LMT A 802     156.809  82.140  43.065  0.95 73.95           O  
HETATM 5653  C1' LMT A 802     162.309  77.159  39.531  0.95 99.24           C  
HETATM 5654  C2' LMT A 802     161.532  77.971  38.537  0.95 91.75           C  
HETATM 5655  C3' LMT A 802     161.299  79.384  39.002  0.95 97.52           C  
HETATM 5656  C4' LMT A 802     160.797  79.350  40.424  0.95102.19           C  
HETATM 5657  C5' LMT A 802     161.778  78.576  41.269  0.95105.93           C  
HETATM 5658  C6' LMT A 802     161.384  78.701  42.724  0.95106.95           C  
HETATM 5659  O1' LMT A 802     162.246  75.851  39.019  0.95112.39           O  
HETATM 5660  O2' LMT A 802     162.366  78.016  37.396  0.95 87.23           O  
HETATM 5661  O3' LMT A 802     160.315  79.979  38.161  0.95 83.87           O  
HETATM 5662  O5' LMT A 802     161.750  77.230  40.828  0.95 96.74           O  
HETATM 5663  O6' LMT A 802     161.332  80.095  43.012  0.95 98.16           O  
HETATM 5664  C1  LMT A 802     163.460  75.549  38.346  0.95128.32           C  
HETATM 5665  C2  LMT A 802     163.242  74.415  37.354  0.95128.35           C  
HETATM 5666  C3  LMT A 802     162.936  74.947  35.964  0.95118.84           C  
HETATM 5667  C4  LMT A 802     162.246  73.898  35.106  0.95112.57           C  
HETATM 5668  C5  LMT A 802     162.692  72.498  35.487  0.95111.57           C  
HETATM 5669  C6  LMT A 802     162.650  71.554  34.295  0.95115.10           C  
HETATM 5670  C7  LMT A 802     161.289  71.506  33.620  0.95112.20           C  
HETATM 5671  C8  LMT A 802     161.215  70.313  32.678  0.95106.83           C  
HETATM 5672  C9  LMT A 802     159.869  70.268  31.978  0.95101.01           C  
HETATM 5673  C10 LMT A 802     159.563  68.887  31.425  0.95 93.67           C  
HETATM 5674  C11 LMT A 802     158.194  68.907  30.767  0.95 93.25           C  
HETATM 5675  C12 LMT A 802     157.788  67.540  30.276  0.95 95.87           C  
HETATM 5676  O   HOH A 901     135.458  33.114  18.597  1.00 97.22           O  
HETATM 5677  O   HOH A 902     142.231  74.608  56.879  1.00 54.70           O  
HETATM 5678  O   HOH A 903     145.581  48.775  18.911  1.00 50.39           O  
HETATM 5679  O   HOH A 904     141.975  89.440  48.316  1.00 61.36           O  
HETATM 5680  O   HOH A 905     137.489  81.610  40.340  1.00 60.44           O  
HETATM 5681  O   HOH A 906     131.820  76.125  41.284  1.00 64.74           O  
HETATM 5682  O   HOH A 907     129.045  79.630  46.573  1.00 67.31           O  
HETATM 5683  O   HOH A 908     153.154  81.685  57.873  1.00 55.02           O  
HETATM 5684  O   HOH A 909     133.586  65.268  11.700  1.00 78.62           O  
HETATM 5685  O   HOH A 910     129.910  65.463  45.734  1.00 66.50           O  
HETATM 5686  O   HOH A 911     129.317  63.213  47.435  1.00 81.28           O  
CONECT 5591 5599                                                                
CONECT 5592 5610 5619 5630 5640                                                 
CONECT 5593 5594 5630                                                           
CONECT 5594 5593 5595 5596                                                      
CONECT 5595 5594 5620                                                           
CONECT 5596 5594 5597                                                           
CONECT 5597 5596 5600                                                           
CONECT 5598 5599 5640                                                           
CONECT 5599 5591 5598                                                           
CONECT 5600 5597 5601 5602                                                      
CONECT 5601 5600                                                                
CONECT 5602 5600 5603                                                           
CONECT 5603 5602 5604                                                           
CONECT 5604 5603 5605                                                           
CONECT 5605 5604 5606                                                           
CONECT 5606 5605 5607                                                           
CONECT 5607 5606 5608                                                           
CONECT 5608 5607 5609                                                           
CONECT 5609 5608 5611                                                           
CONECT 5610 5592                                                                
CONECT 5611 5609 5612                                                           
CONECT 5612 5611 5613                                                           
CONECT 5613 5612 5614                                                           
CONECT 5614 5613 5615                                                           
CONECT 5615 5614 5616                                                           
CONECT 5616 5615 5617                                                           
CONECT 5617 5616 5618                                                           
CONECT 5618 5617                                                                
CONECT 5619 5592                                                                
CONECT 5620 5595 5621 5622                                                      
CONECT 5621 5620                                                                
CONECT 5622 5620 5623                                                           
CONECT 5623 5622 5624                                                           
CONECT 5624 5623 5625                                                           
CONECT 5625 5624 5626                                                           
CONECT 5626 5625 5627                                                           
CONECT 5627 5626 5628                                                           
CONECT 5628 5627 5629                                                           
CONECT 5629 5628 5631                                                           
CONECT 5630 5592 5593                                                           
CONECT 5631 5629 5632                                                           
CONECT 5632 5631 5633                                                           
CONECT 5633 5632 5634                                                           
CONECT 5634 5633 5635                                                           
CONECT 5635 5634 5636                                                           
CONECT 5636 5635 5637                                                           
CONECT 5637 5636 5638                                                           
CONECT 5638 5637 5639                                                           
CONECT 5639 5638                                                                
CONECT 5640 5592 5598                                                           
CONECT 5641 5642 5647 5651                                                      
CONECT 5642 5641 5643 5648                                                      
CONECT 5643 5642 5644 5649                                                      
CONECT 5644 5643 5645 5650                                                      
CONECT 5645 5644 5646 5651                                                      
CONECT 5646 5645 5652                                                           
CONECT 5647 5641 5656                                                           
CONECT 5648 5642                                                                
CONECT 5649 5643                                                                
CONECT 5650 5644                                                                
CONECT 5651 5641 5645                                                           
CONECT 5652 5646                                                                
CONECT 5653 5654 5659 5662                                                      
CONECT 5654 5653 5655 5660                                                      
CONECT 5655 5654 5656 5661                                                      
CONECT 5656 5647 5655 5657                                                      
CONECT 5657 5656 5658 5662                                                      
CONECT 5658 5657 5663                                                           
CONECT 5659 5653 5664                                                           
CONECT 5660 5654                                                                
CONECT 5661 5655                                                                
CONECT 5662 5653 5657                                                           
CONECT 5663 5658                                                                
CONECT 5664 5659 5665                                                           
CONECT 5665 5664 5666                                                           
CONECT 5666 5665 5667                                                           
CONECT 5667 5666 5668                                                           
CONECT 5668 5667 5669                                                           
CONECT 5669 5668 5670                                                           
CONECT 5670 5669 5671                                                           
CONECT 5671 5670 5672                                                           
CONECT 5672 5671 5673                                                           
CONECT 5673 5672 5674                                                           
CONECT 5674 5673 5675                                                           
CONECT 5675 5674                                                                
MASTER      449    0    2   39   10    0    6    6 5677    1   85   60          
END                                                                             



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