CNRS Nantes University UFIP UFIP
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***  GH3  ***

elNémo ID: 200515150729131985

Job options:

ID        	=	 200515150729131985
JOBID     	=	 GH3
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER GH3

HEADER    HYDROLASE                               24-NOV-11   3UT0              
TITLE     CRYSTAL STRUCTURE OF EXO-1,3/1,4-BETA-GLUCANASE (EXOP) FROM           
TITLE    2 PSEUDOALTEROMONAS SP. BB1                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EXO-1,3/1,4-BETA-GLUCANASE;                                
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 28-840;                                       
COMPND   5 EC: 3.2.1.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOALTEROMONAS SP.;                          
SOURCE   3 ORGANISM_TAXID: 368972;                                              
SOURCE   4 STRAIN: BB1;                                                         
SOURCE   5 GENE: EXOP;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYSS;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21(D)                                  
KEYWDS    (ALPHA/BETA)8 BARREL, (ALPHA/BETA)6 SHEET, BETA-SANDWICH, HYDROLASE   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.NAKATANI,S.M.CUTFIELD,J.F.CUTFIELD                                  
REVDAT   1   21-DEC-11 3UT0    0                                                
SPRSDE     21-DEC-11 3UT0      3F93                                             
JRNL        AUTH   Y.NAKATANI,S.M.CUTFIELD,N.P.COWIESON,J.F.CUTFIELD            
JRNL        TITL   STRUCTURE AND ACTIVITY OF EXO-1,3/1,4-BETA-GLUCANASE FROM    
JRNL        TITL 2 MARINE BACTERIUM PSEUDOALTEROMONAS SP. BB1 SHOWING A NOVEL   
JRNL        TITL 3 C-TERMINAL DOMAIN                                            
JRNL        REF    FEBS J.                                    2011              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   22129429                                                     
JRNL        DOI    10.1111/J.1742-4658.2011.08439.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.2_869)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.33                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 143281                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7201                            
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 38.3332 -  4.9520    0.99    13992   702  0.1876 0.2079        
REMARK   3     2  4.9520 -  3.9318    0.99    13822   762  0.1662 0.1993        
REMARK   3     3  3.9318 -  3.4352    0.98    13575   744  0.2186 0.2569        
REMARK   3     4  3.4352 -  3.1212    0.99    13774   689  0.2531 0.3164        
REMARK   3     5  3.1212 -  2.8976    0.98    13675   728  0.2596 0.3240        
REMARK   3     6  2.8976 -  2.7268    0.98    13571   760  0.2563 0.3345        
REMARK   3     7  2.7268 -  2.5903    0.97    13490   709  0.2625 0.3443        
REMARK   3     8  2.5903 -  2.4776    0.97    13565   687  0.2594 0.3316        
REMARK   3     9  2.4776 -  2.3822    0.96    13347   700  0.2854 0.3571        
REMARK   3    10  2.3822 -  2.3000    0.96    13269   720  0.3093 0.3759        
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              : 0.33                                          
REMARK   3   B_SOL              : 34.52                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.760            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.970           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 41.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.83620                                              
REMARK   3    B22 (A**2) : -9.36150                                             
REMARK   3    B33 (A**2) : 24.18570                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.79840                                              
REMARK   3    B23 (A**2) : -0.00000                                             
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      :  0.007          25468                                  
REMARK   3   ANGLE     :  1.037          34563                                  
REMARK   3   CHIRALITY :  0.071           3795                                  
REMARK   3   PLANARITY :  0.005           4460                                  
REMARK   3   DIHEDRAL  : 12.671           9146                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and ((resseq 5:626))                         
REMARK   3    ORIGIN FOR THE GROUP (A): 100.4332  -8.1372  30.9391              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3299 T22:  -0.0773                                     
REMARK   3      T33:  -0.2305 T12:  -0.0293                                     
REMARK   3      T13:   0.1453 T23:   0.0602                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7339 L22:   0.7193                                     
REMARK   3      L33:   0.5246 L12:  -0.1571                                     
REMARK   3      L13:  -0.0705 L23:  -0.0803                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2690 S12:  -0.1622 S13:  -0.6000                       
REMARK   3      S21:   0.4302 S22:   0.1387 S23:   0.6371                       
REMARK   3      S31:   0.0015 S32:  -0.2908 S33:   0.1665                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and ((resseq 632:816))                       
REMARK   3    ORIGIN FOR THE GROUP (A): 110.1041  25.0519  11.0915              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2022 T22:   0.0291                                     
REMARK   3      T33:  -0.0537 T12:   0.0311                                     
REMARK   3      T13:   0.0566 T23:   0.1295                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5344 L22:   0.3273                                     
REMARK   3      L33:   0.4630 L12:   0.1925                                     
REMARK   3      L13:   0.1202 L23:   0.0059                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0108 S12:   0.1220 S13:   0.1474                       
REMARK   3      S21:  -0.1607 S22:   0.0367 S23:   0.0712                       
REMARK   3      S31:  -0.1275 S32:  -0.0330 S33:   0.0408                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'B' and ((resseq 5:626))                         
REMARK   3    ORIGIN FOR THE GROUP (A):  68.4127 -14.8646  -0.4648              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -1.6564 T22:  -1.4263                                     
REMARK   3      T33:  -1.0023 T12:   0.6385                                     
REMARK   3      T13:   0.1364 T23:  -0.6034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1739 L22:   0.1555                                     
REMARK   3      L33:   0.1264 L12:  -0.0007                                     
REMARK   3      L13:   0.1436 L23:   0.0040                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1496 S12:   1.0964 S13:  -0.3372                       
REMARK   3      S21:  -0.6232 S22:   0.2056 S23:  -0.5850                       
REMARK   3      S31:  -0.0407 S32:   0.9479 S33:   0.2722                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'B' and ((resseq 634:814))                       
REMARK   3    ORIGIN FOR THE GROUP (A):  67.1265  19.2739  19.2041              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2980 T22:   0.2044                                     
REMARK   3      T33:   0.1454 T12:  -0.0927                                     
REMARK   3      T13:  -0.0336 T23:  -0.0375                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2801 L22:   0.8365                                     
REMARK   3      L33:   0.5215 L12:  -0.3433                                     
REMARK   3      L13:   0.1390 L23:  -0.2895                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0029 S12:  -0.1322 S13:   0.1469                       
REMARK   3      S21:   0.5175 S22:  -0.0308 S23:  -0.3032                       
REMARK   3      S31:  -0.2496 S32:   0.0720 S33:   0.0094                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'C' and ((resseq 5:626))                         
REMARK   3    ORIGIN FOR THE GROUP (A):  93.2094 -62.6583   3.3778              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.6259 T22:  -1.2579                                     
REMARK   3      T33:   0.2059 T12:   0.0061                                     
REMARK   3      T13:  -0.0313 T23:  -0.3809                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2257 L22:   0.4155                                     
REMARK   3      L33:   0.0550 L12:   0.1069                                     
REMARK   3      L13:   0.0245 L23:   0.1509                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1999 S12:  -0.2245 S13:   0.2359                       
REMARK   3      S21:   0.1771 S22:  -0.1289 S23:   0.6206                       
REMARK   3      S31:  -0.2188 S32:  -0.6282 S33:  -0.3755                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'C' and ((resseq 634:814))                       
REMARK   3    ORIGIN FOR THE GROUP (A): 117.4196 -93.5686   6.0647              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2547 T22:   0.0962                                     
REMARK   3      T33:   0.1343 T12:   0.0357                                     
REMARK   3      T13:   0.0266 T23:   0.0529                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4432 L22:   1.0339                                     
REMARK   3      L33:   0.3612 L12:   0.0937                                     
REMARK   3      L13:   0.1006 L23:   0.1820                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0720 S12:  -0.1175 S13:  -0.0731                       
REMARK   3      S21:   0.3833 S22:  -0.0340 S23:  -0.2988                       
REMARK   3      S31:   0.2154 S32:   0.0931 S33:   0.0413                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'D' and ((resseq 5:626))                         
REMARK   3    ORIGIN FOR THE GROUP (A): 106.8005 -56.1273  45.2101              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.5945 T22:  -2.4832                                     
REMARK   3      T33:  -0.8414 T12:  -1.0986                                     
REMARK   3      T13:   0.1297 T23:   0.0991                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1391 L22:   0.6105                                     
REMARK   3      L33:   0.1377 L12:   0.0702                                     
REMARK   3      L13:   0.1539 L23:   0.2459                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0212 S12:   0.6943 S13:   0.1307                       
REMARK   3      S21:  -0.9845 S22:   0.4351 S23:  -0.3086                       
REMARK   3      S31:  -0.2467 S32:   1.1388 S33:   0.2604                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'D' and ((resseq 634:815))                       
REMARK   3    ORIGIN FOR THE GROUP (A):  90.5300 -91.9484  41.0230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5202 T22:   0.0627                                     
REMARK   3      T33:   0.1090 T12:  -0.0929                                     
REMARK   3      T13:  -0.1210 T23:  -0.0517                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1050 L22:   0.8141                                     
REMARK   3      L33:   0.2336 L12:  -0.0819                                     
REMARK   3      L13:  -0.0012 L23:  -0.0648                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0254 S12:   0.1614 S13:  -0.0339                       
REMARK   3      S21:  -0.6174 S22:   0.0404 S23:   0.2591                       
REMARK   3      S31:  -0.0266 S32:  -0.0525 S33:  -0.0218                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain 'A' and (resseq 5:63 or resseq 80:    
REMARK   3                          626 or resseq 634:769 )                     
REMARK   3     SELECTION          : chain 'B' and (resseq 5:63 or resseq 80:    
REMARK   3                          626 or resseq 634:769 )                     
REMARK   3     ATOM PAIRS NUMBER  : 5773                                        
REMARK   3     RMSD               : 0.052                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: chain 'A' and (resseq 5:63 or resseq 80:    
REMARK   3                          626 or resseq 634:769 )                     
REMARK   3     SELECTION          : chain 'C' and (resseq 5:63 or resseq 80:    
REMARK   3                          626 or resseq 634:769 )                     
REMARK   3     ATOM PAIRS NUMBER  : 5773                                        
REMARK   3     RMSD               : 0.057                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: chain 'A' and (resseq 5:63 or resseq 80:    
REMARK   3                          626 or resseq 634:769 )                     
REMARK   3     SELECTION          : chain 'D' and (resseq 5:63 or resseq 80:    
REMARK   3                          626 or resseq 634:769 )                     
REMARK   3     ATOM PAIRS NUMBER  : 5773                                        
REMARK   3     RMSD               : 0.056                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3UT0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB069171.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-DEC-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 113                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.954                              
REMARK 200  MONOCHROMATOR                  : MIRROR                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 143421                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : 0.09000                            
REMARK 200   FOR THE DATA SET  : 8.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.40500                            
REMARK 200   FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3USZ, 3F95                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES-NAOH, PH7.5, 2% PEG 400,      
REMARK 280  2.0M AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE   
REMARK 280  291K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000      128.91050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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     MET A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     LYS A   627                                                      
REMARK 465     LYS A   628                                                      
REMARK 465     THR A   629                                                      
REMARK 465     VAL A   630                                                      
REMARK 465     ASN A   631                                                      
REMARK 465     ASP A   772                                                      
REMARK 465     GLN A   773                                                      
REMARK 465     ALA A   774                                                      
REMARK 465     HIS A   817                                                      
REMARK 465     HIS A   818                                                      
REMARK 465     HIS A   819                                                      
REMARK 465     HIS A   820                                                      
REMARK 465     HIS A   821                                                      
REMARK 465     MET B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     LYS B   627                                                      
REMARK 465     LYS B   628                                                      
REMARK 465     THR B   629                                                      
REMARK 465     VAL B   630                                                      
REMARK 465     ASN B   631                                                      
REMARK 465     SER B   632                                                      
REMARK 465     ASP B   633                                                      
REMARK 465     ASP B   770                                                      
REMARK 465     SER B   771                                                      
REMARK 465     ASP B   772                                                      
REMARK 465     GLN B   773                                                      
REMARK 465     ALA B   774                                                      
REMARK 465     GLU B   815                                                      
REMARK 465     HIS B   816                                                      
REMARK 465     HIS B   817                                                      
REMARK 465     HIS B   818                                                      
REMARK 465     HIS B   819                                                      
REMARK 465     HIS B   820                                                      
REMARK 465     HIS B   821                                                      
REMARK 465     MET C     0                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     HIS C     3                                                      
REMARK 465     GLU C     4                                                      
REMARK 465     LYS C   627                                                      
REMARK 465     LYS C   628                                                      
REMARK 465     THR C   629                                                      
REMARK 465     VAL C   630                                                      
REMARK 465     ASN C   631                                                      
REMARK 465     SER C   632                                                      
REMARK 465     ASP C   633                                                      
REMARK 465     ASP C   770                                                      
REMARK 465     SER C   771                                                      
REMARK 465     ASP C   772                                                      
REMARK 465     GLN C   773                                                      
REMARK 465     ALA C   774                                                      
REMARK 465     GLU C   815                                                      
REMARK 465     HIS C   816                                                      
REMARK 465     HIS C   817                                                      
REMARK 465     HIS C   818                                                      
REMARK 465     HIS C   819                                                      
REMARK 465     HIS C   820                                                      
REMARK 465     HIS C   821                                                      
REMARK 465     MET D     0                                                      
REMARK 465     ALA D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     HIS D     3                                                      
REMARK 465     GLU D     4                                                      
REMARK 465     LYS D   627                                                      
REMARK 465     LYS D   628                                                      
REMARK 465     THR D   629                                                      
REMARK 465     VAL D   630                                                      
REMARK 465     ASN D   631                                                      
REMARK 465     SER D   632                                                      
REMARK 465     ASP D   633                                                      
REMARK 465     ASP D   770                                                      
REMARK 465     SER D   771                                                      
REMARK 465     ASP D   772                                                      
REMARK 465     GLN D   773                                                      
REMARK 465     ALA D   774                                                      
REMARK 465     HIS D   816                                                      
REMARK 465     HIS D   817                                                      
REMARK 465     HIS D   818                                                      
REMARK 465     HIS D   819                                                      
REMARK 465     HIS D   820                                                      
REMARK 465     HIS D   821                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NZ   LYS A   367     OE1  GLN C   375              2.10            
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    LEU A  97      -55.32     78.53                                   
REMARK 500    HIS A 112       66.26   -152.53                                   
REMARK 500    ALA A 159      148.53   -179.18                                   
REMARK 500    ARG A 224       16.70     57.72                                   
REMARK 500    TRP A 294      104.67    -55.90                                   
REMARK 500    CYS A 308       73.24   -156.39                                   
REMARK 500    VAL A 434      -47.95     69.55                                   
REMARK 500    GLU A 493     -144.41     55.96                                   
REMARK 500    TRP A 550     -135.37     60.27                                   
REMARK 500    ASN A 595       -2.03     78.16                                   
REMARK 500    ARG A 640      -36.17     65.27                                   
REMARK 500    ASP A 652     -168.33   -106.84                                   
REMARK 500    ALA A 665      171.30    179.77                                   
REMARK 500    LYS A 670       14.83     54.34                                   
REMARK 500    GLN A 671      -38.05   -136.03                                   
REMARK 500    MET A 735       78.56     56.86                                   
REMARK 500    SER A 737       40.92   -148.08                                   
REMARK 500    GLU A 738      -43.79     68.59                                   
REMARK 500    ASN A 788      102.28   -166.70                                   
REMARK 500    LEU B  97      -56.36     76.48                                   
REMARK 500    ALA B 110       67.83   -117.20                                   
REMARK 500    HIS B 112       65.83   -151.92                                   
REMARK 500    ALA B 159      149.84   -174.25                                   
REMARK 500    ARG B 224       19.54     58.91                                   
REMARK 500    THR B 277      -63.69   -108.11                                   
REMARK 500    TRP B 294      103.36    -59.01                                   
REMARK 500    CYS B 308       71.82   -158.18                                   
REMARK 500    VAL B 434      -49.15     69.47                                   
REMARK 500    ASN B 448       -2.48     72.44                                   
REMARK 500    GLU B 493     -144.37     54.25                                   
REMARK 500    TRP B 550     -132.92     56.64                                   
REMARK 500    ASN B 595       -2.44     74.73                                   
REMARK 500    ARG B 640      -37.26     65.94                                   
REMARK 500    ASP B 652     -168.64   -104.30                                   
REMARK 500    LYS B 670       14.47     55.98                                   
REMARK 500    GLN B 671      -39.15   -135.17                                   
REMARK 500    MET B 735       77.88     56.25                                   
REMARK 500    SER B 737       42.33   -148.69                                   
REMARK 500    GLU B 738      -44.01     67.51                                   
REMARK 500    THR B 779      -62.12    -99.95                                   
REMARK 500    ASN B 788      101.60   -161.07                                   
REMARK 500    LYS B 813       68.63   -110.35                                   
REMARK 500    ASN C  67        2.52     95.96                                   
REMARK 500    ALA C  76      138.64   -170.77                                   
REMARK 500    LEU C  97      -55.45     76.19                                   
REMARK 500    ALA C 110       68.19   -116.09                                   
REMARK 500    HIS C 112       66.70   -150.51                                   
REMARK 500    ARG C 224       17.59     59.03                                   
REMARK 500    THR C 277      -64.34   -106.78                                   
REMARK 500    TRP C 294      100.89    -56.30                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      91 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    MET A  93        -10.56                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 901  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C 593   OD1                                                    
REMARK 620 2 GLU C 179   OE1  92.4                                              
REMARK 620 3 LEU C 592   O    82.3  92.5                                        
REMARK 620 4 HOH C 831   O    92.1 174.5  84.9                                  
REMARK 620 5 HOH C 832   O   177.4  86.9 100.3  88.7                            
REMARK 620 6 HOH C 829   O    87.2 105.0 159.9  78.4  90.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 901  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 593   OD1                                                    
REMARK 620 2 LEU A 592   O    83.3                                              
REMARK 620 3 GLU A 179   OE1  91.5  93.2                                        
REMARK 620 4 HOH A 837   O   177.1  99.3  87.0                                  
REMARK 620 5 HOH A 830   O    87.9 159.9 105.1  90.1                            
REMARK 620 6 HOH A 836   O    93.1  84.0 174.3  88.5  78.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 901  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU D 592   O                                                      
REMARK 620 2 GLU D 179   OE1  93.4                                              
REMARK 620 3 ASN D 593   OD1  83.2  91.0                                        
REMARK 620 4 HOH D 827   O   159.9 104.6  87.6                                  
REMARK 620 5 HOH D 830   O    99.1  87.8 177.4  90.5                            
REMARK 620 6 HOH D 829   O    84.0 175.0  93.0  78.7  88.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 901  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU B 592   O                                                      
REMARK 620 2 GLU B 179   OE1  93.2                                              
REMARK 620 3 ASN B 593   OD1  83.0  91.5                                        
REMARK 620 4 HOH B 835   O    99.3  88.0 177.6                                  
REMARK 620 5 HOH B 831   O   160.0 104.5  87.4  90.6                            
REMARK 620 6 HOH B 834   O    84.1 174.8  92.6  88.2  78.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 902  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA C  92   O                                                      
REMARK 620 2 ASP C  98   OD2 154.6                                              
REMARK 620 3 ILE C 100   O   102.8  97.9                                        
REMARK 620 4 ASP C  98   OD1 149.1  48.9  81.0                                  
REMARK 620 5 ASP C  94   O    88.4 107.1  87.7  60.9                            
REMARK 620 6 HOH C 830   O    89.1  81.3 147.0  73.7  61.7                      
REMARK 620 7 HOH C 833   O    73.8  89.8  95.6 136.9 162.2 117.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 902  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A  92   O                                                      
REMARK 620 2 ASP A  98   OD2 154.7                                              
REMARK 620 3 ILE A 100   O   103.3  97.3                                        
REMARK 620 4 ASP A  98   OD1 149.5  48.5  80.3                                  
REMARK 620 5 ASP A  94   O    89.7 105.8  87.4  60.0                            
REMARK 620 6 HOH A 838   O    73.3  90.7  94.8 137.0 163.0                      
REMARK 620 7 HOH A 833   O    89.1  80.7 148.0  74.7  63.0 117.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 902  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE B 100   O                                                      
REMARK 620 2 ASP B  98   OD2  98.0                                              
REMARK 620 3 ALA B  92   O   102.8 154.5                                        
REMARK 620 4 ASP B  98   OD1  79.6  49.6 149.2                                  
REMARK 620 5 ASP B  94   O    88.3 108.1  87.3  62.0                            
REMARK 620 6 HOH B 832   O   147.7  81.2  88.9  75.4  61.8                      
REMARK 620 7 HOH B 837   O    94.9  90.0  73.7 137.0 161.0 117.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 902  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE D 100   O                                                      
REMARK 620 2 ASP D  98   OD2  97.5                                              
REMARK 620 3 ALA D  92   O   102.9 155.1                                        
REMARK 620 4 ASP D  98   OD1  79.3  49.9 148.4                                  
REMARK 620 5 ASP D  94   O    86.7 108.9  86.6  61.9                            
REMARK 620 6 HOH D 831   O    94.7  90.2  74.1 137.5 160.5                      
REMARK 620 7 HOH D 828   O   148.1  80.6  89.2  75.4  64.4 117.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 822                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 823                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 824                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 825                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 826                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 827                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 828                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 829                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 822                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 823                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 824                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 825                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 826                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 827                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 828                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 822                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 823                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 824                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 825                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 826                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 828                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 822                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 823                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 824                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 826                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3F95   RELATED DB: PDB                                   
REMARK 900 C-TERMINAL DOMAIN OF EXOP                                            
REMARK 900 RELATED ID: 3RRX   RELATED DB: PDB                                   
REMARK 900 Q683A-EXOP MUTANT                                                    
REMARK 900 RELATED ID: 3USZ   RELATED DB: PDB                                   
REMARK 900 TRANCATED EXOP                                                       
DBREF  3UT0 A    1   813  UNP    Q0QJA3   Q0QJA3_9GAMM    28    840             
DBREF  3UT0 B    1   813  UNP    Q0QJA3   Q0QJA3_9GAMM    28    840             
DBREF  3UT0 C    1   813  UNP    Q0QJA3   Q0QJA3_9GAMM    28    840             
DBREF  3UT0 D    1   813  UNP    Q0QJA3   Q0QJA3_9GAMM    28    840             
SEQADV 3UT0 MET A    0  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 LEU A  814  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 GLU A  815  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS A  816  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS A  817  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS A  818  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS A  819  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS A  820  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS A  821  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 MET B    0  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 LEU B  814  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 GLU B  815  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS B  816  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS B  817  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS B  818  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS B  819  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS B  820  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS B  821  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 MET C    0  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 LEU C  814  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 GLU C  815  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS C  816  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS C  817  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS C  818  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS C  819  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS C  820  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS C  821  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 MET D    0  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 LEU D  814  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 GLU D  815  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS D  816  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS D  817  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS D  818  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS D  819  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS D  820  UNP  Q0QJA3              EXPRESSION TAG                 
SEQADV 3UT0 HIS D  821  UNP  Q0QJA3              EXPRESSION TAG                 
SEQRES   1 A  822  MET ALA GLU HIS GLU GLN VAL ASN TRP PRO TYR VAL ASN          
SEQRES   2 A  822  THR LYS LEU LYS ARG ASP PRO ALA VAL GLU ALA GLN ILE          
SEQRES   3 A  822  GLU LYS LEU LEU ALA LYS MET THR ILE GLU GLN LYS VAL          
SEQRES   4 A  822  ALA GLN MET ILE GLN PRO GLU ILE GLY TYR LEU THR VAL          
SEQRES   5 A  822  GLU GLN MET ARG LYS TYR GLY PHE GLY SER TYR LEU ASN          
SEQRES   6 A  822  GLY GLY ASN THR ALA PRO TYR GLY ASN LYS ARG ALA ASP          
SEQRES   7 A  822  GLN ALA THR TRP LEU LYS TYR ALA ASP GLU MET TYR LEU          
SEQRES   8 A  822  ALA ALA MET ASP SER THR LEU ASP GLY ILE ALA ILE PRO          
SEQRES   9 A  822  THR VAL TRP GLY THR ASP ALA MET HIS GLY HIS SER ASN          
SEQRES  10 A  822  VAL TYR GLY ALA THR LEU PHE PRO HIS ASN ILE GLY LEU          
SEQRES  11 A  822  GLY ALA ALA ARG ASP THR ASP LEU ILE LYS ARG ILE GLY          
SEQRES  12 A  822  GLN ALA THR ALA LYS GLU VAL ALA ALA THR GLY ILE GLU          
SEQRES  13 A  822  TRP SER PHE ALA PRO THR VAL ALA VAL VAL ARG ASP ASP          
SEQRES  14 A  822  ARG TRP GLY ARG THR TYR GLU SER TYR SER GLU ASP PRO          
SEQRES  15 A  822  ASP LEU VAL LYS ARG TYR ALA GLY GLU MET VAL THR GLY          
SEQRES  16 A  822  ILE GLN GLY ASP VAL GLY ALA ASP PHE LEU LYS GLY SER          
SEQRES  17 A  822  ASN ARG ILE ALA THR ALA LYS HIS PHE VAL GLY ASP GLY          
SEQRES  18 A  822  GLY THR GLU ARG GLY VAL ASP ARG GLY ASN THR LEU ILE          
SEQRES  19 A  822  ASP GLU LYS GLY LEU ARG ASP ILE HIS SER ALA GLY TYR          
SEQRES  20 A  822  PHE SER ALA ILE ASN GLN GLY VAL GLN SER VAL MET ALA          
SEQRES  21 A  822  SER PHE ASN SER TRP ASN GLY LYS ARG VAL HIS GLY ASP          
SEQRES  22 A  822  LYS HIS LEU LEU THR ASP VAL LEU LYS ASN GLN LEU GLY          
SEQRES  23 A  822  PHE ASP GLY PHE VAL VAL SER ASP TRP ASN ALA HIS LYS          
SEQRES  24 A  822  PHE VAL GLU GLY CYS ASP LEU GLU GLN CYS ALA GLN ALA          
SEQRES  25 A  822  ILE ASN ALA GLY VAL ASP VAL ILE MET VAL PRO GLU HIS          
SEQRES  26 A  822  PHE GLU ALA PHE TYR HIS ASN THR VAL LYS GLN VAL LYS          
SEQRES  27 A  822  ALA GLY VAL ILE ALA GLU SER ARG ILE ASN ASP ALA VAL          
SEQRES  28 A  822  ARG ARG PHE LEU ARG ALA LYS ILE ARG TRP GLY VAL PHE          
SEQRES  29 A  822  THR LYS SER LYS PRO SER ALA ARG PRO GLU SER GLN HIS          
SEQRES  30 A  822  PRO GLN TRP LEU GLY ALA ALA GLU HIS ARG THR LEU ALA          
SEQRES  31 A  822  ARG GLU ALA VAL ARG LYS SER LEU VAL LEU LEU LYS ASN          
SEQRES  32 A  822  ASN GLU SER ILE LEU PRO ILE LYS ALA SER SER ARG ILE          
SEQRES  33 A  822  LEU VAL ALA GLY LYS GLY ALA ASN ALA ILE ASN MET GLN          
SEQRES  34 A  822  ALA GLY GLY TRP SER VAL SER TRP GLN GLY THR ASP ASN          
SEQRES  35 A  822  THR ASN SER ASP PHE PRO ASN ALA THR SER ILE PHE SER          
SEQRES  36 A  822  GLY LEU GLN SER GLN VAL THR LYS ALA GLY GLY LYS ILE          
SEQRES  37 A  822  THR LEU SER GLU SER GLY GLU TYR THR SER LYS PRO ASP          
SEQRES  38 A  822  VAL ALA ILE VAL VAL ILE GLY GLU GLU PRO TYR ALA GLU          
SEQRES  39 A  822  TRP PHE GLY ASP ILE GLU LEU LEU GLU PHE GLN HIS GLU          
SEQRES  40 A  822  THR LYS HIS ALA LEU ALA LEU LEU LYS GLN LEU LYS ALA          
SEQRES  41 A  822  ASP ASN ILE PRO VAL VAL THR VAL PHE LEU SER GLY ARG          
SEQRES  42 A  822  PRO LEU TRP VAL ASN LYS GLU LEU ASN ALA SER ASP ALA          
SEQRES  43 A  822  PHE VAL ALA ALA TRP LEU PRO GLY SER GLU GLY GLU GLY          
SEQRES  44 A  822  VAL ALA ASP VAL LEU LEU THR ASN LYS GLN GLY LYS THR          
SEQRES  45 A  822  GLN PHE ASP PHE THR GLY LYS LEU SER PHE SER TRP PRO          
SEQRES  46 A  822  LYS TYR ASP ASP GLN PHE THR LEU ASN LEU ASN ASP ALA          
SEQRES  47 A  822  ASP TYR ASP PRO LEU PHE ALA TYR GLY TYR GLY LEU THR          
SEQRES  48 A  822  TYR GLN ASP ASN ILE ASN VAL PRO VAL LEU SER GLU LYS          
SEQRES  49 A  822  THR SER PRO LYS LYS THR VAL ASN SER ASP SER HIS PRO          
SEQRES  50 A  822  LEU PHE VAL ARG SER LEU ALA LYS ASN MET THR TRP GLN          
SEQRES  51 A  822  LEU ALA ASP THR SER THR GLN LYS VAL LEU ALA SER GLY          
SEQRES  52 A  822  ALA SER ALA THR SER GLY ASP LYS GLN SER LEU LEU MET          
SEQRES  53 A  822  GLN SER VAL ASN LEU SER TYR GLN GLU ASP GLY ARG GLY          
SEQRES  54 A  822  PHE ASN TRP ARG ALA GLN ALA ALA LEU SER LEU SER TYR          
SEQRES  55 A  822  LEU GLU PRO THR PRO LEU ASP SER LYS PHE SER THR GLY          
SEQRES  56 A  822  TYR LEU GLU LEU LYS MET ARG ILE ASP LYS ALA PRO GLU          
SEQRES  57 A  822  GLN GLY ALA ASN LEU GLN VAL MET CYS SER GLU SER ASN          
SEQRES  58 A  822  CYS LEU ARG ASP ILE ASP PHE SER SER PHE SER GLN LEU          
SEQRES  59 A  822  MET ALA ASP LYS SER TRP HIS THR LEU ALA ILE PRO LEU          
SEQRES  60 A  822  HIS CYS ASP ASP SER ASP GLN ALA GLU GLN PRO ILE THR          
SEQRES  61 A  822  ASP ALA LEU ARG ILE THR SER GLN ASN LEU SER LEU ALA          
SEQRES  62 A  822  ILE ALA ASP VAL ALA LEU THR ILE LYS PRO SER ASP ASP          
SEQRES  63 A  822  SER ILE SER LEU THR CYS ALA LYS LEU GLU HIS HIS HIS          
SEQRES  64 A  822  HIS HIS HIS                                                  
SEQRES   1 B  822  MET ALA GLU HIS GLU GLN VAL ASN TRP PRO TYR VAL ASN          
SEQRES   2 B  822  THR LYS LEU LYS ARG ASP PRO ALA VAL GLU ALA GLN ILE          
SEQRES   3 B  822  GLU LYS LEU LEU ALA LYS MET THR ILE GLU GLN LYS VAL          
SEQRES   4 B  822  ALA GLN MET ILE GLN PRO GLU ILE GLY TYR LEU THR VAL          
SEQRES   5 B  822  GLU GLN MET ARG LYS TYR GLY PHE GLY SER TYR LEU ASN          
SEQRES   6 B  822  GLY GLY ASN THR ALA PRO TYR GLY ASN LYS ARG ALA ASP          
SEQRES   7 B  822  GLN ALA THR TRP LEU LYS TYR ALA ASP GLU MET TYR LEU          
SEQRES   8 B  822  ALA ALA MET ASP SER THR LEU ASP GLY ILE ALA ILE PRO          
SEQRES   9 B  822  THR VAL TRP GLY THR ASP ALA MET HIS GLY HIS SER ASN          
SEQRES  10 B  822  VAL TYR GLY ALA THR LEU PHE PRO HIS ASN ILE GLY LEU          
SEQRES  11 B  822  GLY ALA ALA ARG ASP THR ASP LEU ILE LYS ARG ILE GLY          
SEQRES  12 B  822  GLN ALA THR ALA LYS GLU VAL ALA ALA THR GLY ILE GLU          
SEQRES  13 B  822  TRP SER PHE ALA PRO THR VAL ALA VAL VAL ARG ASP ASP          
SEQRES  14 B  822  ARG TRP GLY ARG THR TYR GLU SER TYR SER GLU ASP PRO          
SEQRES  15 B  822  ASP LEU VAL LYS ARG TYR ALA GLY GLU MET VAL THR GLY          
SEQRES  16 B  822  ILE GLN GLY ASP VAL GLY ALA ASP PHE LEU LYS GLY SER          
SEQRES  17 B  822  ASN ARG ILE ALA THR ALA LYS HIS PHE VAL GLY ASP GLY          
SEQRES  18 B  822  GLY THR GLU ARG GLY VAL ASP ARG GLY ASN THR LEU ILE          
SEQRES  19 B  822  ASP GLU LYS GLY LEU ARG ASP ILE HIS SER ALA GLY TYR          
SEQRES  20 B  822  PHE SER ALA ILE ASN GLN GLY VAL GLN SER VAL MET ALA          
SEQRES  21 B  822  SER PHE ASN SER TRP ASN GLY LYS ARG VAL HIS GLY ASP          
SEQRES  22 B  822  LYS HIS LEU LEU THR ASP VAL LEU LYS ASN GLN LEU GLY          
SEQRES  23 B  822  PHE ASP GLY PHE VAL VAL SER ASP TRP ASN ALA HIS LYS          
SEQRES  24 B  822  PHE VAL GLU GLY CYS ASP LEU GLU GLN CYS ALA GLN ALA          
SEQRES  25 B  822  ILE ASN ALA GLY VAL ASP VAL ILE MET VAL PRO GLU HIS          
SEQRES  26 B  822  PHE GLU ALA PHE TYR HIS ASN THR VAL LYS GLN VAL LYS          
SEQRES  27 B  822  ALA GLY VAL ILE ALA GLU SER ARG ILE ASN ASP ALA VAL          
SEQRES  28 B  822  ARG ARG PHE LEU ARG ALA LYS ILE ARG TRP GLY VAL PHE          
SEQRES  29 B  822  THR LYS SER LYS PRO SER ALA ARG PRO GLU SER GLN HIS          
SEQRES  30 B  822  PRO GLN TRP LEU GLY ALA ALA GLU HIS ARG THR LEU ALA          
SEQRES  31 B  822  ARG GLU ALA VAL ARG LYS SER LEU VAL LEU LEU LYS ASN          
SEQRES  32 B  822  ASN GLU SER ILE LEU PRO ILE LYS ALA SER SER ARG ILE          
SEQRES  33 B  822  LEU VAL ALA GLY LYS GLY ALA ASN ALA ILE ASN MET GLN          
SEQRES  34 B  822  ALA GLY GLY TRP SER VAL SER TRP GLN GLY THR ASP ASN          
SEQRES  35 B  822  THR ASN SER ASP PHE PRO ASN ALA THR SER ILE PHE SER          
SEQRES  36 B  822  GLY LEU GLN SER GLN VAL THR LYS ALA GLY GLY LYS ILE          
SEQRES  37 B  822  THR LEU SER GLU SER GLY GLU TYR THR SER LYS PRO ASP          
SEQRES  38 B  822  VAL ALA ILE VAL VAL ILE GLY GLU GLU PRO TYR ALA GLU          
SEQRES  39 B  822  TRP PHE GLY ASP ILE GLU LEU LEU GLU PHE GLN HIS GLU          
SEQRES  40 B  822  THR LYS HIS ALA LEU ALA LEU LEU LYS GLN LEU LYS ALA          
SEQRES  41 B  822  ASP ASN ILE PRO VAL VAL THR VAL PHE LEU SER GLY ARG          
SEQRES  42 B  822  PRO LEU TRP VAL ASN LYS GLU LEU ASN ALA SER ASP ALA          
SEQRES  43 B  822  PHE VAL ALA ALA TRP LEU PRO GLY SER GLU GLY GLU GLY          
SEQRES  44 B  822  VAL ALA ASP VAL LEU LEU THR ASN LYS GLN GLY LYS THR          
SEQRES  45 B  822  GLN PHE ASP PHE THR GLY LYS LEU SER PHE SER TRP PRO          
SEQRES  46 B  822  LYS TYR ASP ASP GLN PHE THR LEU ASN LEU ASN ASP ALA          
SEQRES  47 B  822  ASP TYR ASP PRO LEU PHE ALA TYR GLY TYR GLY LEU THR          
SEQRES  48 B  822  TYR GLN ASP ASN ILE ASN VAL PRO VAL LEU SER GLU LYS          
SEQRES  49 B  822  THR SER PRO LYS LYS THR VAL ASN SER ASP SER HIS PRO          
SEQRES  50 B  822  LEU PHE VAL ARG SER LEU ALA LYS ASN MET THR TRP GLN          
SEQRES  51 B  822  LEU ALA ASP THR SER THR GLN LYS VAL LEU ALA SER GLY          
SEQRES  52 B  822  ALA SER ALA THR SER GLY ASP LYS GLN SER LEU LEU MET          
SEQRES  53 B  822  GLN SER VAL ASN LEU SER TYR GLN GLU ASP GLY ARG GLY          
SEQRES  54 B  822  PHE ASN TRP ARG ALA GLN ALA ALA LEU SER LEU SER TYR          
SEQRES  55 B  822  LEU GLU PRO THR PRO LEU ASP SER LYS PHE SER THR GLY          
SEQRES  56 B  822  TYR LEU GLU LEU LYS MET ARG ILE ASP LYS ALA PRO GLU          
SEQRES  57 B  822  GLN GLY ALA ASN LEU GLN VAL MET CYS SER GLU SER ASN          
SEQRES  58 B  822  CYS LEU ARG ASP ILE ASP PHE SER SER PHE SER GLN LEU          
SEQRES  59 B  822  MET ALA ASP LYS SER TRP HIS THR LEU ALA ILE PRO LEU          
SEQRES  60 B  822  HIS CYS ASP ASP SER ASP GLN ALA GLU GLN PRO ILE THR          
SEQRES  61 B  822  ASP ALA LEU ARG ILE THR SER GLN ASN LEU SER LEU ALA          
SEQRES  62 B  822  ILE ALA ASP VAL ALA LEU THR ILE LYS PRO SER ASP ASP          
SEQRES  63 B  822  SER ILE SER LEU THR CYS ALA LYS LEU GLU HIS HIS HIS          
SEQRES  64 B  822  HIS HIS HIS                                                  
SEQRES   1 C  822  MET ALA GLU HIS GLU GLN VAL ASN TRP PRO TYR VAL ASN          
SEQRES   2 C  822  THR LYS LEU LYS ARG ASP PRO ALA VAL GLU ALA GLN ILE          
SEQRES   3 C  822  GLU LYS LEU LEU ALA LYS MET THR ILE GLU GLN LYS VAL          
SEQRES   4 C  822  ALA GLN MET ILE GLN PRO GLU ILE GLY TYR LEU THR VAL          
SEQRES   5 C  822  GLU GLN MET ARG LYS TYR GLY PHE GLY SER TYR LEU ASN          
SEQRES   6 C  822  GLY GLY ASN THR ALA PRO TYR GLY ASN LYS ARG ALA ASP          
SEQRES   7 C  822  GLN ALA THR TRP LEU LYS TYR ALA ASP GLU MET TYR LEU          
SEQRES   8 C  822  ALA ALA MET ASP SER THR LEU ASP GLY ILE ALA ILE PRO          
SEQRES   9 C  822  THR VAL TRP GLY THR ASP ALA MET HIS GLY HIS SER ASN          
SEQRES  10 C  822  VAL TYR GLY ALA THR LEU PHE PRO HIS ASN ILE GLY LEU          
SEQRES  11 C  822  GLY ALA ALA ARG ASP THR ASP LEU ILE LYS ARG ILE GLY          
SEQRES  12 C  822  GLN ALA THR ALA LYS GLU VAL ALA ALA THR GLY ILE GLU          
SEQRES  13 C  822  TRP SER PHE ALA PRO THR VAL ALA VAL VAL ARG ASP ASP          
SEQRES  14 C  822  ARG TRP GLY ARG THR TYR GLU SER TYR SER GLU ASP PRO          
SEQRES  15 C  822  ASP LEU VAL LYS ARG TYR ALA GLY GLU MET VAL THR GLY          
SEQRES  16 C  822  ILE GLN GLY ASP VAL GLY ALA ASP PHE LEU LYS GLY SER          
SEQRES  17 C  822  ASN ARG ILE ALA THR ALA LYS HIS PHE VAL GLY ASP GLY          
SEQRES  18 C  822  GLY THR GLU ARG GLY VAL ASP ARG GLY ASN THR LEU ILE          
SEQRES  19 C  822  ASP GLU LYS GLY LEU ARG ASP ILE HIS SER ALA GLY TYR          
SEQRES  20 C  822  PHE SER ALA ILE ASN GLN GLY VAL GLN SER VAL MET ALA          
SEQRES  21 C  822  SER PHE ASN SER TRP ASN GLY LYS ARG VAL HIS GLY ASP          
SEQRES  22 C  822  LYS HIS LEU LEU THR ASP VAL LEU LYS ASN GLN LEU GLY          
SEQRES  23 C  822  PHE ASP GLY PHE VAL VAL SER ASP TRP ASN ALA HIS LYS          
SEQRES  24 C  822  PHE VAL GLU GLY CYS ASP LEU GLU GLN CYS ALA GLN ALA          
SEQRES  25 C  822  ILE ASN ALA GLY VAL ASP VAL ILE MET VAL PRO GLU HIS          
SEQRES  26 C  822  PHE GLU ALA PHE TYR HIS ASN THR VAL LYS GLN VAL LYS          
SEQRES  27 C  822  ALA GLY VAL ILE ALA GLU SER ARG ILE ASN ASP ALA VAL          
SEQRES  28 C  822  ARG ARG PHE LEU ARG ALA LYS ILE ARG TRP GLY VAL PHE          
SEQRES  29 C  822  THR LYS SER LYS PRO SER ALA ARG PRO GLU SER GLN HIS          
SEQRES  30 C  822  PRO GLN TRP LEU GLY ALA ALA GLU HIS ARG THR LEU ALA          
SEQRES  31 C  822  ARG GLU ALA VAL ARG LYS SER LEU VAL LEU LEU LYS ASN          
SEQRES  32 C  822  ASN GLU SER ILE LEU PRO ILE LYS ALA SER SER ARG ILE          
SEQRES  33 C  822  LEU VAL ALA GLY LYS GLY ALA ASN ALA ILE ASN MET GLN          
SEQRES  34 C  822  ALA GLY GLY TRP SER VAL SER TRP GLN GLY THR ASP ASN          
SEQRES  35 C  822  THR ASN SER ASP PHE PRO ASN ALA THR SER ILE PHE SER          
SEQRES  36 C  822  GLY LEU GLN SER GLN VAL THR LYS ALA GLY GLY LYS ILE          
SEQRES  37 C  822  THR LEU SER GLU SER GLY GLU TYR THR SER LYS PRO ASP          
SEQRES  38 C  822  VAL ALA ILE VAL VAL ILE GLY GLU GLU PRO TYR ALA GLU          
SEQRES  39 C  822  TRP PHE GLY ASP ILE GLU LEU LEU GLU PHE GLN HIS GLU          
SEQRES  40 C  822  THR LYS HIS ALA LEU ALA LEU LEU LYS GLN LEU LYS ALA          
SEQRES  41 C  822  ASP ASN ILE PRO VAL VAL THR VAL PHE LEU SER GLY ARG          
SEQRES  42 C  822  PRO LEU TRP VAL ASN LYS GLU LEU ASN ALA SER ASP ALA          
SEQRES  43 C  822  PHE VAL ALA ALA TRP LEU PRO GLY SER GLU GLY GLU GLY          
SEQRES  44 C  822  VAL ALA ASP VAL LEU LEU THR ASN LYS GLN GLY LYS THR          
SEQRES  45 C  822  GLN PHE ASP PHE THR GLY LYS LEU SER PHE SER TRP PRO          
SEQRES  46 C  822  LYS TYR ASP ASP GLN PHE THR LEU ASN LEU ASN ASP ALA          
SEQRES  47 C  822  ASP TYR ASP PRO LEU PHE ALA TYR GLY TYR GLY LEU THR          
SEQRES  48 C  822  TYR GLN ASP ASN ILE ASN VAL PRO VAL LEU SER GLU LYS          
SEQRES  49 C  822  THR SER PRO LYS LYS THR VAL ASN SER ASP SER HIS PRO          
SEQRES  50 C  822  LEU PHE VAL ARG SER LEU ALA LYS ASN MET THR TRP GLN          
SEQRES  51 C  822  LEU ALA ASP THR SER THR GLN LYS VAL LEU ALA SER GLY          
SEQRES  52 C  822  ALA SER ALA THR SER GLY ASP LYS GLN SER LEU LEU MET          
SEQRES  53 C  822  GLN SER VAL ASN LEU SER TYR GLN GLU ASP GLY ARG GLY          
SEQRES  54 C  822  PHE ASN TRP ARG ALA GLN ALA ALA LEU SER LEU SER TYR          
SEQRES  55 C  822  LEU GLU PRO THR PRO LEU ASP SER LYS PHE SER THR GLY          
SEQRES  56 C  822  TYR LEU GLU LEU LYS MET ARG ILE ASP LYS ALA PRO GLU          
SEQRES  57 C  822  GLN GLY ALA ASN LEU GLN VAL MET CYS SER GLU SER ASN          
SEQRES  58 C  822  CYS LEU ARG ASP ILE ASP PHE SER SER PHE SER GLN LEU          
SEQRES  59 C  822  MET ALA ASP LYS SER TRP HIS THR LEU ALA ILE PRO LEU          
SEQRES  60 C  822  HIS CYS ASP ASP SER ASP GLN ALA GLU GLN PRO ILE THR          
SEQRES  61 C  822  ASP ALA LEU ARG ILE THR SER GLN ASN LEU SER LEU ALA          
SEQRES  62 C  822  ILE ALA ASP VAL ALA LEU THR ILE LYS PRO SER ASP ASP          
SEQRES  63 C  822  SER ILE SER LEU THR CYS ALA LYS LEU GLU HIS HIS HIS          
SEQRES  64 C  822  HIS HIS HIS                                                  
SEQRES   1 D  822  MET ALA GLU HIS GLU GLN VAL ASN TRP PRO TYR VAL ASN          
SEQRES   2 D  822  THR LYS LEU LYS ARG ASP PRO ALA VAL GLU ALA GLN ILE          
SEQRES   3 D  822  GLU LYS LEU LEU ALA LYS MET THR ILE GLU GLN LYS VAL          
SEQRES   4 D  822  ALA GLN MET ILE GLN PRO GLU ILE GLY TYR LEU THR VAL          
SEQRES   5 D  822  GLU GLN MET ARG LYS TYR GLY PHE GLY SER TYR LEU ASN          
SEQRES   6 D  822  GLY GLY ASN THR ALA PRO TYR GLY ASN LYS ARG ALA ASP          
SEQRES   7 D  822  GLN ALA THR TRP LEU LYS TYR ALA ASP GLU MET TYR LEU          
SEQRES   8 D  822  ALA ALA MET ASP SER THR LEU ASP GLY ILE ALA ILE PRO          
SEQRES   9 D  822  THR VAL TRP GLY THR ASP ALA MET HIS GLY HIS SER ASN          
SEQRES  10 D  822  VAL TYR GLY ALA THR LEU PHE PRO HIS ASN ILE GLY LEU          
SEQRES  11 D  822  GLY ALA ALA ARG ASP THR ASP LEU ILE LYS ARG ILE GLY          
SEQRES  12 D  822  GLN ALA THR ALA LYS GLU VAL ALA ALA THR GLY ILE GLU          
SEQRES  13 D  822  TRP SER PHE ALA PRO THR VAL ALA VAL VAL ARG ASP ASP          
SEQRES  14 D  822  ARG TRP GLY ARG THR TYR GLU SER TYR SER GLU ASP PRO          
SEQRES  15 D  822  ASP LEU VAL LYS ARG TYR ALA GLY GLU MET VAL THR GLY          
SEQRES  16 D  822  ILE GLN GLY ASP VAL GLY ALA ASP PHE LEU LYS GLY SER          
SEQRES  17 D  822  ASN ARG ILE ALA THR ALA LYS HIS PHE VAL GLY ASP GLY          
SEQRES  18 D  822  GLY THR GLU ARG GLY VAL ASP ARG GLY ASN THR LEU ILE          
SEQRES  19 D  822  ASP GLU LYS GLY LEU ARG ASP ILE HIS SER ALA GLY TYR          
SEQRES  20 D  822  PHE SER ALA ILE ASN GLN GLY VAL GLN SER VAL MET ALA          
SEQRES  21 D  822  SER PHE ASN SER TRP ASN GLY LYS ARG VAL HIS GLY ASP          
SEQRES  22 D  822  LYS HIS LEU LEU THR ASP VAL LEU LYS ASN GLN LEU GLY          
SEQRES  23 D  822  PHE ASP GLY PHE VAL VAL SER ASP TRP ASN ALA HIS LYS          
SEQRES  24 D  822  PHE VAL GLU GLY CYS ASP LEU GLU GLN CYS ALA GLN ALA          
SEQRES  25 D  822  ILE ASN ALA GLY VAL ASP VAL ILE MET VAL PRO GLU HIS          
SEQRES  26 D  822  PHE GLU ALA PHE TYR HIS ASN THR VAL LYS GLN VAL LYS          
SEQRES  27 D  822  ALA GLY VAL ILE ALA GLU SER ARG ILE ASN ASP ALA VAL          
SEQRES  28 D  822  ARG ARG PHE LEU ARG ALA LYS ILE ARG TRP GLY VAL PHE          
SEQRES  29 D  822  THR LYS SER LYS PRO SER ALA ARG PRO GLU SER GLN HIS          
SEQRES  30 D  822  PRO GLN TRP LEU GLY ALA ALA GLU HIS ARG THR LEU ALA          
SEQRES  31 D  822  ARG GLU ALA VAL ARG LYS SER LEU VAL LEU LEU LYS ASN          
SEQRES  32 D  822  ASN GLU SER ILE LEU PRO ILE LYS ALA SER SER ARG ILE          
SEQRES  33 D  822  LEU VAL ALA GLY LYS GLY ALA ASN ALA ILE ASN MET GLN          
SEQRES  34 D  822  ALA GLY GLY TRP SER VAL SER TRP GLN GLY THR ASP ASN          
SEQRES  35 D  822  THR ASN SER ASP PHE PRO ASN ALA THR SER ILE PHE SER          
SEQRES  36 D  822  GLY LEU GLN SER GLN VAL THR LYS ALA GLY GLY LYS ILE          
SEQRES  37 D  822  THR LEU SER GLU SER GLY GLU TYR THR SER LYS PRO ASP          
SEQRES  38 D  822  VAL ALA ILE VAL VAL ILE GLY GLU GLU PRO TYR ALA GLU          
SEQRES  39 D  822  TRP PHE GLY ASP ILE GLU LEU LEU GLU PHE GLN HIS GLU          
SEQRES  40 D  822  THR LYS HIS ALA LEU ALA LEU LEU LYS GLN LEU LYS ALA          
SEQRES  41 D  822  ASP ASN ILE PRO VAL VAL THR VAL PHE LEU SER GLY ARG          
SEQRES  42 D  822  PRO LEU TRP VAL ASN LYS GLU LEU ASN ALA SER ASP ALA          
SEQRES  43 D  822  PHE VAL ALA ALA TRP LEU PRO GLY SER GLU GLY GLU GLY          
SEQRES  44 D  822  VAL ALA ASP VAL LEU LEU THR ASN LYS GLN GLY LYS THR          
SEQRES  45 D  822  GLN PHE ASP PHE THR GLY LYS LEU SER PHE SER TRP PRO          
SEQRES  46 D  822  LYS TYR ASP ASP GLN PHE THR LEU ASN LEU ASN ASP ALA          
SEQRES  47 D  822  ASP TYR ASP PRO LEU PHE ALA TYR GLY TYR GLY LEU THR          
SEQRES  48 D  822  TYR GLN ASP ASN ILE ASN VAL PRO VAL LEU SER GLU LYS          
SEQRES  49 D  822  THR SER PRO LYS LYS THR VAL ASN SER ASP SER HIS PRO          
SEQRES  50 D  822  LEU PHE VAL ARG SER LEU ALA LYS ASN MET THR TRP GLN          
SEQRES  51 D  822  LEU ALA ASP THR SER THR GLN LYS VAL LEU ALA SER GLY          
SEQRES  52 D  822  ALA SER ALA THR SER GLY ASP LYS GLN SER LEU LEU MET          
SEQRES  53 D  822  GLN SER VAL ASN LEU SER TYR GLN GLU ASP GLY ARG GLY          
SEQRES  54 D  822  PHE ASN TRP ARG ALA GLN ALA ALA LEU SER LEU SER TYR          
SEQRES  55 D  822  LEU GLU PRO THR PRO LEU ASP SER LYS PHE SER THR GLY          
SEQRES  56 D  822  TYR LEU GLU LEU LYS MET ARG ILE ASP LYS ALA PRO GLU          
SEQRES  57 D  822  GLN GLY ALA ASN LEU GLN VAL MET CYS SER GLU SER ASN          
SEQRES  58 D  822  CYS LEU ARG ASP ILE ASP PHE SER SER PHE SER GLN LEU          
SEQRES  59 D  822  MET ALA ASP LYS SER TRP HIS THR LEU ALA ILE PRO LEU          
SEQRES  60 D  822  HIS CYS ASP ASP SER ASP GLN ALA GLU GLN PRO ILE THR          
SEQRES  61 D  822  ASP ALA LEU ARG ILE THR SER GLN ASN LEU SER LEU ALA          
SEQRES  62 D  822  ILE ALA ASP VAL ALA LEU THR ILE LYS PRO SER ASP ASP          
SEQRES  63 D  822  SER ILE SER LEU THR CYS ALA LYS LEU GLU HIS HIS HIS          
SEQRES  64 D  822  HIS HIS HIS                                                  
HET     CA  A 901       1                                                       
HET     NA  A 902       1                                                       
HET    SO4  A 822       5                                                       
HET    SO4  A 823       5                                                       
HET    SO4  A 824       5                                                       
HET    SO4  A 825       5                                                       
HET    SO4  A 826       5                                                       
HET    EDO  A 827       4                                                       
HET    EDO  A 828       4                                                       
HET    EDO  A 829       4                                                       
HET     CA  B 901       1                                                       
HET     NA  B 902       1                                                       
HET    SO4  B 822       5                                                       
HET    SO4  B 823       5                                                       
HET    SO4  B 824       5                                                       
HET    SO4  B 825       5                                                       
HET    SO4  B 826       5                                                       
HET    EDO  B 827       4                                                       
HET    EDO  B 828       4                                                       
HET     CA  C 901       1                                                       
HET     NA  C 902       1                                                       
HET    SO4  C 822       5                                                       
HET    SO4  C 823       5                                                       
HET    SO4  C 824       5                                                       
HET    SO4  C 825       5                                                       
HET    SO4  C 826       5                                                       
HET    EDO  C 827       4                                                       
HET    EDO  C 828       4                                                       
HET     CA  D 901       1                                                       
HET     NA  D 902       1                                                       
HET    SO4  D 822       5                                                       
HET    SO4  D 823       5                                                       
HET    SO4  D 824       5                                                       
HET    EDO  D 825       4                                                       
HET    EDO  D 826       4                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      NA SODIUM ION                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5   CA    4(CA 2+)                                                     
FORMUL   6   NA    4(NA 1+)                                                     
FORMUL   7  SO4    18(O4 S 2-)                                                  
FORMUL  12  EDO    9(C2 H6 O2)                                                  
FORMUL  40  HOH   *828(H2 O)                                                    
HELIX    1   1 ASP A   18  MET A   32  1                                  15    
HELIX    2   2 THR A   33  MET A   41  1                                   9    
HELIX    3   3 THR A   50  GLY A   58  1                                   9    
HELIX    4   4 ALA A   69  ASN A   73  5                                   5    
HELIX    5   5 ASP A   77  ASP A   94  1                                  18    
HELIX    6   6 HIS A  125  ARG A  133  1                                   9    
HELIX    7   7 ASP A  134  ALA A  151  1                                  18    
HELIX    8   8 ARG A  172  SER A  176  5                                   5    
HELIX    9   9 ASP A  180  GLY A  197  1                                  18    
HELIX   10  10 GLY A  218  VAL A  226  5                                   9    
HELIX   11  11 ASP A  234  SER A  243  1                                  10    
HELIX   12  12 SER A  243  GLN A  252  1                                  10    
HELIX   13  13 ASP A  272  THR A  277  1                                   6    
HELIX   14  14 ASN A  295  VAL A  300  5                                   6    
HELIX   15  15 CYS A  308  GLY A  315  1                                   8    
HELIX   16  16 HIS A  324  ALA A  338  1                                  15    
HELIX   17  17 ALA A  342  GLY A  361  1                                  20    
HELIX   18  18 LYS A  367  GLN A  375  5                                   9    
HELIX   19  19 HIS A  376  LEU A  380  5                                   5    
HELIX   20  20 ALA A  382  LEU A  397  1                                  16    
HELIX   21  21 GLU A  404  ILE A  406  5                                   3    
HELIX   22  22 ALA A  424  GLY A  430  1                                   7    
HELIX   23  23 THR A  442  PHE A  446  5                                   5    
HELIX   24  24 SER A  451  ALA A  463  1                                  13    
HELIX   25  25 ALA A  492  ASP A  497  5                                   6    
HELIX   26  26 LYS A  508  ASP A  520  1                                  13    
HELIX   27  27 VAL A  536  ALA A  542  1                                   7    
HELIX   28  28 GLY A  556  LEU A  564  1                                   9    
HELIX   29  29 ASP A  708  SER A  712  5                                   5    
HELIX   30  30 SER A  748  MET A  754  5                                   7    
HELIX   31  31 ASP B   18  MET B   32  1                                  15    
HELIX   32  32 THR B   33  MET B   41  1                                   9    
HELIX   33  33 THR B   50  GLY B   58  1                                   9    
HELIX   34  34 ALA B   69  ASN B   73  5                                   5    
HELIX   35  35 ASP B   77  ASP B   94  1                                  18    
HELIX   36  36 HIS B  125  ARG B  133  1                                   9    
HELIX   37  37 ASP B  134  ALA B  151  1                                  18    
HELIX   38  38 ARG B  172  SER B  176  5                                   5    
HELIX   39  39 ASP B  180  GLY B  197  1                                  18    
HELIX   40  40 GLY B  218  VAL B  226  5                                   9    
HELIX   41  41 ASP B  234  SER B  243  1                                  10    
HELIX   42  42 SER B  243  GLN B  252  1                                  10    
HELIX   43  43 ASP B  272  THR B  277  1                                   6    
HELIX   44  44 ASN B  295  VAL B  300  5                                   6    
HELIX   45  45 CYS B  308  GLY B  315  1                                   8    
HELIX   46  46 HIS B  324  ALA B  338  1                                  15    
HELIX   47  47 ALA B  342  GLY B  361  1                                  20    
HELIX   48  48 LYS B  367  GLN B  375  5                                   9    
HELIX   49  49 HIS B  376  LEU B  380  5                                   5    
HELIX   50  50 ALA B  382  LEU B  397  1                                  16    
HELIX   51  51 GLU B  404  ILE B  406  5                                   3    
HELIX   52  52 ALA B  424  GLY B  430  1                                   7    
HELIX   53  53 THR B  442  PHE B  446  5                                   5    
HELIX   54  54 SER B  451  ALA B  463  1                                  13    
HELIX   55  55 ALA B  492  ASP B  497  5                                   6    
HELIX   56  56 LYS B  508  ASP B  520  1                                  13    
HELIX   57  57 VAL B  536  ALA B  542  1                                   7    
HELIX   58  58 GLY B  556  LEU B  564  1                                   9    
HELIX   59  59 ASP B  708  SER B  712  5                                   5    
HELIX   60  60 SER B  748  MET B  754  5                                   7    
HELIX   61  61 ASP C   18  MET C   32  1                                  15    
HELIX   62  62 THR C   33  MET C   41  1                                   9    
HELIX   63  63 THR C   50  GLY C   58  1                                   9    
HELIX   64  64 ALA C   69  ASN C   73  5                                   5    
HELIX   65  65 ASP C   77  ASP C   94  1                                  18    
HELIX   66  66 HIS C  125  ARG C  133  1                                   9    
HELIX   67  67 ASP C  134  ALA C  151  1                                  18    
HELIX   68  68 ARG C  172  SER C  176  5                                   5    
HELIX   69  69 ASP C  180  GLY C  197  1                                  18    
HELIX   70  70 GLY C  218  VAL C  226  5                                   9    
HELIX   71  71 ASP C  234  SER C  243  1                                  10    
HELIX   72  72 SER C  243  GLN C  252  1                                  10    
HELIX   73  73 ASP C  272  THR C  277  1                                   6    
HELIX   74  74 ASN C  295  VAL C  300  5                                   6    
HELIX   75  75 CYS C  308  GLY C  315  1                                   8    
HELIX   76  76 HIS C  324  ALA C  338  1                                  15    
HELIX   77  77 ALA C  342  GLY C  361  1                                  20    
HELIX   78  78 LYS C  367  GLN C  375  5                                   9    
HELIX   79  79 HIS C  376  LEU C  380  5                                   5    
HELIX   80  80 ALA C  382  LEU C  397  1                                  16    
HELIX   81  81 GLU C  404  ILE C  406  5                                   3    
HELIX   82  82 ALA C  424  GLY C  430  1                                   7    
HELIX   83  83 THR C  442  PHE C  446  5                                   5    
HELIX   84  84 SER C  451  ALA C  463  1                                  13    
HELIX   85  85 ALA C  492  ASP C  497  5                                   6    
HELIX   86  86 LYS C  508  ASP C  520  1                                  13    
HELIX   87  87 VAL C  536  ALA C  542  1                                   7    
HELIX   88  88 GLY C  556  LEU C  564  1                                   9    
HELIX   89  89 ASP C  708  SER C  712  5                                   5    
HELIX   90  90 SER C  748  MET C  754  5                                   7    
HELIX   91  91 ASP D   18  MET D   32  1                                  15    
HELIX   92  92 THR D   33  MET D   41  1                                   9    
HELIX   93  93 THR D   50  GLY D   58  1                                   9    
HELIX   94  94 ALA D   69  ASN D   73  5                                   5    
HELIX   95  95 ASP D   77  ASP D   94  1                                  18    
HELIX   96  96 HIS D  125  ARG D  133  1                                   9    
HELIX   97  97 ASP D  134  ALA D  151  1                                  18    
HELIX   98  98 ARG D  172  SER D  176  5                                   5    
HELIX   99  99 ASP D  180  GLY D  197  1                                  18    
HELIX  100 100 GLY D  218  VAL D  226  5                                   9    
HELIX  101 101 ASP D  234  SER D  243  1                                  10    
HELIX  102 102 SER D  243  GLN D  252  1                                  10    
HELIX  103 103 ASP D  272  THR D  277  1                                   6    
HELIX  104 104 ASN D  295  VAL D  300  5                                   6    
HELIX  105 105 CYS D  308  GLY D  315  1                                   8    
HELIX  106 106 HIS D  324  ALA D  338  1                                  15    
HELIX  107 107 ALA D  342  GLY D  361  1                                  20    
HELIX  108 108 LYS D  367  GLN D  375  5                                   9    
HELIX  109 109 HIS D  376  LEU D  380  5                                   5    
HELIX  110 110 ALA D  382  LEU D  397  1                                  16    
HELIX  111 111 GLU D  404  ILE D  406  5                                   3    
HELIX  112 112 ALA D  424  GLY D  430  1                                   7    
HELIX  113 113 THR D  442  PHE D  446  5                                   5    
HELIX  114 114 SER D  451  ALA D  463  1                                  13    
HELIX  115 115 ALA D  492  ASP D  497  5                                   6    
HELIX  116 116 LYS D  508  ASP D  520  1                                  13    
HELIX  117 117 VAL D  536  ALA D  542  1                                   7    
HELIX  118 118 GLY D  556  LEU D  564  1                                   9    
HELIX  119 119 ASP D  708  SER D  712  5                                   5    
HELIX  120 120 SER D  748  MET D  754  5                                   7    
SHEET    1   A 2 ILE A  42  GLN A  43  0                                        
SHEET    2   A 2 ILE A 319  MET A 320  1  O  ILE A 319   N  GLN A  43           
SHEET    1   B 6 SER A  61  ASN A  64  0                                        
SHEET    2   B 6 VAL A 105  ASP A 109  1  O  GLY A 107   N  ASN A  64           
SHEET    3   B 6 TRP A 156  THR A 161  1  O  PHE A 158   N  THR A 108           
SHEET    4   B 6 ILE A 210  PHE A 216  1  O  ILE A 210   N  SER A 157           
SHEET    5   B 6 SER A 256  ALA A 259  1  O  MET A 258   N  PHE A 216           
SHEET    6   B 6 PHE A 289  VAL A 291  1  O  VAL A 291   N  VAL A 257           
SHEET    1   C 3 ASN A 230  THR A 231  0                                        
SHEET    2   C 3 SER A 263  TRP A 264  1  O  SER A 263   N  THR A 231           
SHEET    3   C 3 LYS A 267  ARG A 268 -1  O  LYS A 267   N  TRP A 264           
SHEET    1   D 6 VAL A 398  ASN A 402  0                                        
SHEET    2   D 6 ALA A 545  TRP A 550 -1  O  ALA A 548   N  VAL A 398           
SHEET    3   D 6 VAL A 524  LEU A 529  1  N  PHE A 528   O  VAL A 547           
SHEET    4   D 6 VAL A 481  GLY A 487  1  N  ILE A 486   O  LEU A 529           
SHEET    5   D 6 ARG A 414  ALA A 418  1  N  ALA A 418   O  VAL A 485           
SHEET    6   D 6 LYS A 466  LEU A 469  1  O  LYS A 466   N  ILE A 415           
SHEET    1   E 5 HIS A 635  PHE A 638  0                                        
SHEET    2   E 5 LEU A 789  THR A 799 -1  O  LEU A 798   N  HIS A 635           
SHEET    3   E 5 GLY A 686  TRP A 691 -1  N  ARG A 687   O  ILE A 793           
SHEET    4   E 5 LEU A 673  VAL A 678 -1  N  GLN A 676   O  GLY A 688           
SHEET    5   E 5 ALA A 665  THR A 666 -1  N  ALA A 665   O  MET A 675           
SHEET    1   F 5 HIS A 635  PHE A 638  0                                        
SHEET    2   F 5 LEU A 789  THR A 799 -1  O  LEU A 798   N  HIS A 635           
SHEET    3   F 5 TYR A 715  LYS A 724 -1  N  LYS A 719   O  ALA A 794           
SHEET    4   F 5 TRP A 759  PRO A 765 -1  O  LEU A 762   N  LEU A 718           
SHEET    5   F 5 ILE A 807  SER A 808  1  O  ILE A 807   N  ALA A 763           
SHEET    1   G 6 VAL A 658  ALA A 660  0                                        
SHEET    2   G 6 MET A 646  ASP A 652 -1  N  TRP A 648   O  ALA A 660           
SHEET    3   G 6 ALA A 695  THR A 705 -1  O  SER A 700   N  THR A 647           
SHEET    4   G 6 ILE A 778  SER A 786 -1  O  ILE A 784   N  LEU A 697           
SHEET    5   G 6 ALA A 730  CYS A 736 -1  N  GLN A 733   O  ARG A 783           
SHEET    6   G 6 CYS A 741  ASP A 746 -1  O  ILE A 745   N  LEU A 732           
SHEET    1   H 2 ILE B  42  GLN B  43  0                                        
SHEET    2   H 2 ILE B 319  MET B 320  1  O  ILE B 319   N  GLN B  43           
SHEET    1   I 6 TYR B  62  ASN B  64  0                                        
SHEET    2   I 6 TRP B 106  ASP B 109  1  O  GLY B 107   N  ASN B  64           
SHEET    3   I 6 TRP B 156  THR B 161  1  O  PHE B 158   N  THR B 108           
SHEET    4   I 6 ILE B 210  PHE B 216  1  O  ILE B 210   N  SER B 157           
SHEET    5   I 6 SER B 256  ALA B 259  1  O  MET B 258   N  PHE B 216           
SHEET    6   I 6 PHE B 289  VAL B 291  1  O  PHE B 289   N  VAL B 257           
SHEET    1   J 3 ASN B 230  THR B 231  0                                        
SHEET    2   J 3 SER B 263  TRP B 264  1  O  SER B 263   N  THR B 231           
SHEET    3   J 3 LYS B 267  ARG B 268 -1  O  LYS B 267   N  TRP B 264           
SHEET    1   K 6 VAL B 398  ASN B 402  0                                        
SHEET    2   K 6 ALA B 545  TRP B 550 -1  O  ALA B 548   N  VAL B 398           
SHEET    3   K 6 VAL B 524  LEU B 529  1  N  PHE B 528   O  VAL B 547           
SHEET    4   K 6 VAL B 481  GLY B 487  1  N  ILE B 486   O  LEU B 529           
SHEET    5   K 6 ARG B 414  ALA B 418  1  N  ALA B 418   O  VAL B 485           
SHEET    6   K 6 LYS B 466  LEU B 469  1  O  LYS B 466   N  ILE B 415           
SHEET    1   L 5 HIS B 635  PHE B 638  0                                        
SHEET    2   L 5 LEU B 789  THR B 799 -1  O  VAL B 796   N  LEU B 637           
SHEET    3   L 5 GLY B 686  TRP B 691 -1  N  PHE B 689   O  LEU B 791           
SHEET    4   L 5 LEU B 673  VAL B 678 -1  N  GLN B 676   O  GLY B 688           
SHEET    5   L 5 ALA B 665  THR B 666 -1  N  ALA B 665   O  MET B 675           
SHEET    1   M 5 HIS B 635  PHE B 638  0                                        
SHEET    2   M 5 LEU B 789  THR B 799 -1  O  VAL B 796   N  LEU B 637           
SHEET    3   M 5 TYR B 715  LYS B 724 -1  N  GLU B 717   O  ALA B 797           
SHEET    4   M 5 TRP B 759  PRO B 765 -1  O  LEU B 762   N  LEU B 718           
SHEET    5   M 5 ILE B 807  SER B 808  1  O  ILE B 807   N  ALA B 763           
SHEET    1   N 6 VAL B 658  ALA B 660  0                                        
SHEET    2   N 6 MET B 646  ASP B 652 -1  N  TRP B 648   O  ALA B 660           
SHEET    3   N 6 ALA B 695  THR B 705 -1  O  SER B 700   N  THR B 647           
SHEET    4   N 6 ILE B 778  SER B 786 -1  O  THR B 779   N  TYR B 701           
SHEET    5   N 6 ASN B 731  CYS B 736 -1  N  GLN B 733   O  ARG B 783           
SHEET    6   N 6 CYS B 741  ASP B 746 -1  O  ILE B 745   N  LEU B 732           
SHEET    1   O 2 ILE C  42  GLN C  43  0                                        
SHEET    2   O 2 ILE C 319  MET C 320  1  O  ILE C 319   N  GLN C  43           
SHEET    1   P 6 TYR C  62  ASN C  64  0                                        
SHEET    2   P 6 TRP C 106  ASP C 109  1  O  GLY C 107   N  TYR C  62           
SHEET    3   P 6 TRP C 156  THR C 161  1  O  PHE C 158   N  THR C 108           
SHEET    4   P 6 ILE C 210  PHE C 216  1  O  ILE C 210   N  SER C 157           
SHEET    5   P 6 SER C 256  ALA C 259  1  O  MET C 258   N  PHE C 216           
SHEET    6   P 6 PHE C 289  VAL C 291  1  O  PHE C 289   N  VAL C 257           
SHEET    1   Q 3 ASN C 230  THR C 231  0                                        
SHEET    2   Q 3 SER C 263  TRP C 264  1  O  SER C 263   N  THR C 231           
SHEET    3   Q 3 LYS C 267  ARG C 268 -1  O  LYS C 267   N  TRP C 264           
SHEET    1   R 6 VAL C 398  ASN C 402  0                                        
SHEET    2   R 6 ALA C 545  TRP C 550 -1  O  ALA C 548   N  VAL C 398           
SHEET    3   R 6 VAL C 524  LEU C 529  1  N  PHE C 528   O  VAL C 547           
SHEET    4   R 6 VAL C 481  GLY C 487  1  N  ILE C 486   O  LEU C 529           
SHEET    5   R 6 ARG C 414  ALA C 418  1  N  ALA C 418   O  VAL C 485           
SHEET    6   R 6 LYS C 466  LEU C 469  1  O  LYS C 466   N  ILE C 415           
SHEET    1   S 5 HIS C 635  PHE C 638  0                                        
SHEET    2   S 5 LEU C 789  THR C 799 -1  O  VAL C 796   N  PHE C 638           
SHEET    3   S 5 GLY C 686  TRP C 691 -1  N  PHE C 689   O  LEU C 791           
SHEET    4   S 5 LEU C 673  VAL C 678 -1  N  GLN C 676   O  GLY C 688           
SHEET    5   S 5 ALA C 665  THR C 666 -1  N  ALA C 665   O  MET C 675           
SHEET    1   T 5 HIS C 635  PHE C 638  0                                        
SHEET    2   T 5 LEU C 789  THR C 799 -1  O  VAL C 796   N  PHE C 638           
SHEET    3   T 5 TYR C 715  LYS C 724 -1  N  LYS C 719   O  ALA C 794           
SHEET    4   T 5 TRP C 759  PRO C 765 -1  O  LEU C 762   N  LEU C 718           
SHEET    5   T 5 ILE C 807  SER C 808  1  O  ILE C 807   N  ALA C 763           
SHEET    1   U 6 VAL C 658  ALA C 660  0                                        
SHEET    2   U 6 MET C 646  ALA C 651 -1  N  TRP C 648   O  ALA C 660           
SHEET    3   U 6 ALA C 695  PRO C 706 -1  O  SER C 700   N  THR C 647           
SHEET    4   U 6 PRO C 777  SER C 786 -1  O  ILE C 778   N  THR C 705           
SHEET    5   U 6 ALA C 730  CYS C 736 -1  N  GLN C 733   O  ARG C 783           
SHEET    6   U 6 CYS C 741  ASP C 746 -1  O  ILE C 745   N  LEU C 732           
SHEET    1   V 2 ILE D  42  GLN D  43  0                                        
SHEET    2   V 2 ILE D 319  MET D 320  1  O  ILE D 319   N  GLN D  43           
SHEET    1   W 6 SER D  61  ASN D  64  0                                        
SHEET    2   W 6 VAL D 105  ASP D 109  1  O  GLY D 107   N  ASN D  64           
SHEET    3   W 6 TRP D 156  THR D 161  1  O  PHE D 158   N  THR D 108           
SHEET    4   W 6 ILE D 210  PHE D 216  1  O  ILE D 210   N  SER D 157           
SHEET    5   W 6 SER D 256  ALA D 259  1  O  MET D 258   N  PHE D 216           
SHEET    6   W 6 PHE D 289  VAL D 291  1  O  PHE D 289   N  VAL D 257           
SHEET    1   X 3 ASN D 230  THR D 231  0                                        
SHEET    2   X 3 SER D 263  TRP D 264  1  O  SER D 263   N  THR D 231           
SHEET    3   X 3 LYS D 267  ARG D 268 -1  O  LYS D 267   N  TRP D 264           
SHEET    1   Y 6 VAL D 398  ASN D 402  0                                        
SHEET    2   Y 6 ALA D 545  TRP D 550 -1  O  ALA D 548   N  VAL D 398           
SHEET    3   Y 6 VAL D 524  LEU D 529  1  N  PHE D 528   O  VAL D 547           
SHEET    4   Y 6 VAL D 481  GLY D 487  1  N  ILE D 486   O  LEU D 529           
SHEET    5   Y 6 ARG D 414  ALA D 418  1  N  ALA D 418   O  VAL D 485           
SHEET    6   Y 6 LYS D 466  LEU D 469  1  O  LYS D 466   N  ILE D 415           
SHEET    1   Z 5 HIS D 635  PHE D 638  0                                        
SHEET    2   Z 5 LEU D 789  THR D 799 -1  O  LEU D 798   N  HIS D 635           
SHEET    3   Z 5 GLY D 686  TRP D 691 -1  N  ARG D 687   O  ILE D 793           
SHEET    4   Z 5 LEU D 673  VAL D 678 -1  N  GLN D 676   O  GLY D 688           
SHEET    5   Z 5 ALA D 665  THR D 666 -1  N  ALA D 665   O  MET D 675           
SHEET    1  AA 5 HIS D 635  PHE D 638  0                                        
SHEET    2  AA 5 LEU D 789  THR D 799 -1  O  LEU D 798   N  HIS D 635           
SHEET    3  AA 5 TYR D 715  LYS D 724 -1  N  LYS D 719   O  ALA D 794           
SHEET    4  AA 5 TRP D 759  PRO D 765 -1  O  LEU D 762   N  LEU D 718           
SHEET    5  AA 5 ILE D 807  SER D 808  1  O  ILE D 807   N  ALA D 763           
SHEET    1  AB 6 VAL D 658  ALA D 660  0                                        
SHEET    2  AB 6 MET D 646  ALA D 651 -1  N  TRP D 648   O  ALA D 660           
SHEET    3  AB 6 ALA D 695  THR D 705 -1  O  SER D 700   N  THR D 647           
SHEET    4  AB 6 ILE D 778  SER D 786 -1  O  ILE D 784   N  LEU D 697           
SHEET    5  AB 6 ALA D 730  CYS D 736 -1  N  CYS D 736   O  ASP D 780           
SHEET    6  AB 6 CYS D 741  ASP D 746 -1  O  ILE D 745   N  LEU D 732           
SSBOND   1 CYS A  303    CYS A  308                          1555   1555  2.05  
SSBOND   2 CYS A  736    CYS A  741                          1555   1555  2.03  
SSBOND   3 CYS A  768    CYS A  811                          1555   1555  2.04  
SSBOND   4 CYS B  303    CYS B  308                          1555   1555  2.05  
SSBOND   5 CYS B  736    CYS B  741                          1555   1555  2.02  
SSBOND   6 CYS B  768    CYS B  811                          1555   1555  2.02  
SSBOND   7 CYS C  303    CYS C  308                          1555   1555  2.04  
SSBOND   8 CYS C  736    CYS C  741                          1555   1555  2.02  
SSBOND   9 CYS C  768    CYS C  811                          1555   1555  2.04  
SSBOND  10 CYS D  303    CYS D  308                          1555   1555  2.04  
SSBOND  11 CYS D  736    CYS D  741                          1555   1555  2.03  
SSBOND  12 CYS D  768    CYS D  811                          1555   1555  2.03  
LINK         OD1 ASN C 593                CA    CA C 901     1555   1555  2.23  
LINK         OD1 ASN A 593                CA    CA A 901     1555   1555  2.29  
LINK         O   LEU D 592                CA    CA D 901     1555   1555  2.30  
LINK         O   LEU A 592                CA    CA A 901     1555   1555  2.32  
LINK         O   LEU B 592                CA    CA B 901     1555   1555  2.33  
LINK         OE1 GLU A 179                CA    CA A 901     1555   1555  2.34  
LINK         OE1 GLU B 179                CA    CA B 901     1555   1555  2.34  
LINK         OE1 GLU C 179                CA    CA C 901     1555   1555  2.35  
LINK         OD1 ASN B 593                CA    CA B 901     1555   1555  2.38  
LINK         O   LEU C 592                CA    CA C 901     1555   1555  2.39  
LINK         OE1 GLU D 179                CA    CA D 901     1555   1555  2.40  
LINK         OD1 ASN D 593                CA    CA D 901     1555   1555  2.41  
LINK         O   ALA C  92                NA    NA C 902     1555   1555  2.49  
LINK         O   ALA A  92                NA    NA A 902     1555   1555  2.49  
LINK         O   ILE B 100                NA    NA B 902     1555   1555  2.49  
LINK         O   ILE D 100                NA    NA D 902     1555   1555  2.50  
LINK         OD2 ASP B  98                NA    NA B 902     1555   1555  2.50  
LINK         O   ALA B  92                NA    NA B 902     1555   1555  2.50  
LINK         OD2 ASP C  98                NA    NA C 902     1555   1555  2.50  
LINK         OD2 ASP A  98                NA    NA A 902     1555   1555  2.50  
LINK         O   ILE A 100                NA    NA A 902     1555   1555  2.50  
LINK         OD2 ASP D  98                NA    NA D 902     1555   1555  2.50  
LINK         O   ALA D  92                NA    NA D 902     1555   1555  2.50  
LINK         O   ILE C 100                NA    NA C 902     1555   1555  2.50  
LINK         OD1 ASP B  98                NA    NA B 902     1555   1555  2.69  
LINK         OD1 ASP D  98                NA    NA D 902     1555   1555  2.70  
LINK         OD1 ASP C  98                NA    NA C 902     1555   1555  2.74  
LINK         OD1 ASP A  98                NA    NA A 902     1555   1555  2.75  
LINK         O   ASP A  94                NA    NA A 902     1555   1555  3.17  
LINK         O   ASP D  94                NA    NA D 902     1555   1555  3.18  
LINK         O   ASP C  94                NA    NA C 902     1555   1555  3.18  
LINK         O   ASP B  94                NA    NA B 902     1555   1555  3.19  
LINK        CA    CA D 901                 O   HOH D 827     1555   1555  2.33  
LINK        CA    CA C 901                 O   HOH C 831     1555   1555  2.36  
LINK        CA    CA D 901                 O   HOH D 830     1555   1555  2.36  
LINK        CA    CA C 901                 O   HOH C 832     1555   1555  2.37  
LINK        CA    CA B 901                 O   HOH B 835     1555   1555  2.37  
LINK        CA    CA A 901                 O   HOH A 837     1555   1555  2.38  
LINK        CA    CA B 901                 O   HOH B 831     1555   1555  2.39  
LINK        CA    CA A 901                 O   HOH A 830     1555   1555  2.39  
LINK        CA    CA C 901                 O   HOH C 829     1555   1555  2.40  
LINK        CA    CA B 901                 O   HOH B 834     1555   1555  2.42  
LINK        CA    CA D 901                 O   HOH D 829     1555   1555  2.48  
LINK        NA    NA C 902                 O   HOH C 830     1555   1555  2.49  
LINK        CA    CA A 901                 O   HOH A 836     1555   1555  2.49  
LINK        NA    NA D 902                 O   HOH D 831     1555   1555  2.50  
LINK        NA    NA B 902                 O   HOH B 832     1555   1555  2.50  
LINK        NA    NA D 902                 O   HOH D 828     1555   1555  2.50  
LINK        NA    NA C 902                 O   HOH C 833     1555   1555  2.50  
LINK        NA    NA B 902                 O   HOH B 837     1555   1555  2.50  
LINK        NA    NA A 902                 O   HOH A 838     1555   1555  2.50  
LINK        NA    NA A 902                 O   HOH A 833     1555   1555  2.50  
CISPEP   1 ALA A  159    PRO A  160          0         4.70                     
CISPEP   2 LYS A  214    HIS A  215          0       -12.72                     
CISPEP   3 PHE A  216    VAL A  217          0         6.23                     
CISPEP   4 LEU A  407    PRO A  408          0         0.74                     
CISPEP   5 ALA B  159    PRO B  160          0         5.17                     
CISPEP   6 LYS B  214    HIS B  215          0       -15.23                     
CISPEP   7 PHE B  216    VAL B  217          0         4.01                     
CISPEP   8 LEU B  407    PRO B  408          0         0.76                     
CISPEP   9 ALA C  159    PRO C  160          0         6.54                     
CISPEP  10 LYS C  214    HIS C  215          0       -15.67                     
CISPEP  11 PHE C  216    VAL C  217          0         6.16                     
CISPEP  12 LEU C  407    PRO C  408          0         1.31                     
CISPEP  13 ALA D  159    PRO D  160          0         2.99                     
CISPEP  14 LYS D  214    HIS D  215          0       -14.43                     
CISPEP  15 PHE D  216    VAL D  217          0         5.62                     
CISPEP  16 LEU D  407    PRO D  408          0         0.73                     
SITE     1 AC1  6 GLU A 179  LEU A 592  ASN A 593  HOH A 830                    
SITE     2 AC1  6 HOH A 836  HOH A 837                                          
SITE     1 AC2  6 ALA A  92  ASP A  94  ASP A  98  ILE A 100                    
SITE     2 AC2  6 HOH A 833  HOH A 838                                          
SITE     1 AC3  3 THR A  13  LYS A  14  ASN A 251                               
SITE     1 AC4  6 ARG A  17  ARG A 351  HOH A 914  ARG B  17                    
SITE     2 AC4  6 ARG B 351  HOH B 978                                          
SITE     1 AC5  3 LYS A 508  LEU A 511  LYS A 538                               
SITE     1 AC6  3 ARG A 133  ARG A 186  TYR A 605                               
SITE     1 AC7  4 TYR A 715  SER A 808  THR A 810  HOH A1008                    
SITE     1 AC8  2 TRP A 294  TRP A 436                                          
SITE     1 AC9  2 LYS A 236  ARG A 239                                          
SITE     1 BC1  1 ARG A 394                                                     
SITE     1 BC2  6 GLU B 179  LEU B 592  ASN B 593  HOH B 831                    
SITE     2 BC2  6 HOH B 834  HOH B 835                                          
SITE     1 BC3  6 ALA B  92  ASP B  94  ASP B  98  ILE B 100                    
SITE     2 BC3  6 HOH B 832  HOH B 837                                          
SITE     1 BC4  3 LYS B 236  ARG B 239  HOH B 841                               
SITE     1 BC5  3 THR B  13  LYS B  14  ASN B 251                               
SITE     1 BC6  3 ARG B 169  ARG B 224  HOH B 981                               
SITE     1 BC7  3 ARG B 133  ARG B 186  TYR B 605                               
SITE     1 BC8  3 TYR B 715  SER B 808  THR B 810                               
SITE     1 BC9  1 TRP B 436                                                     
SITE     1 CC1  3 ARG B 394  HOH B1015  HOH B1064                               
SITE     1 CC2  6 GLU C 179  LEU C 592  ASN C 593  HOH C 829                    
SITE     2 CC2  6 HOH C 831  HOH C 832                                          
SITE     1 CC3  6 ALA C  92  ASP C  94  ASP C  98  ILE C 100                    
SITE     2 CC3  6 HOH C 830  HOH C 833                                          
SITE     1 CC4  5 THR C  13  LYS C  14  ASN C 251  HOH C 835                    
SITE     2 CC4  5 ASN D 614                                                     
SITE     1 CC5  5 ARG C  17  ARG C 351  ARG D  17  ARG D 351                    
SITE     2 CC5  5 HOH D 892                                                     
SITE     1 CC6  4 ARG C 133  ARG C 186  TYR C 605  HOH C 969                    
SITE     1 CC7  5 GLU C 391  ARG C 394  LYS C 395  HOH C 984                    
SITE     2 CC7  5 HOH C 985                                                     
SITE     1 CC8  1 LYS C 538                                                     
SITE     1 CC9  2 ASN C   7  ARG C 239                                          
SITE     1 DC1  6 GLU D 179  LEU D 592  ASN D 593  HOH D 827                    
SITE     2 DC1  6 HOH D 829  HOH D 830                                          
SITE     1 DC2  6 ALA D  92  ASP D  94  ASP D  98  ILE D 100                    
SITE     2 DC2  6 HOH D 828  HOH D 831                                          
SITE     1 DC3  3 THR D  13  LYS D  14  ASN D 251                               
SITE     1 DC4  4 ARG D 133  ARG D 186  TYR D 605  HOH D 861                    
SITE     1 DC5  4 GLU D 391  ARG D 394  LYS D 395  PHE D 573                    
SITE     1 DC6  3 LYS D 236  ARG D 239  HOH D 836                               
CRYST1   84.908  257.821   85.605  90.00 115.47  90.00 P 1 21 1      8          
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      0.011777  0.000000  0.005610        0.00000                         
SCALE2      0.000000  0.003879  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012939        0.00000                         
ATOM      1  N   GLN A   5     131.506   4.023  27.784  1.00 48.08           N  
ANISOU    1  N   GLN A   5     6090   6090   6090      0      0      0       N  
ATOM      2  CA  GLN A   5     131.090   2.678  27.391  1.00 61.20           C  
ANISOU    2  CA  GLN A   5     7751   7751   7751      0      0      0       C  
ATOM      3  C   GLN A   5     130.565   1.886  28.585  1.00 60.21           C  
ANISOU    3  C   GLN A   5     7625   7625   7625      0      0      0       C  
ATOM      4  O   GLN A   5     131.322   1.264  29.323  1.00 68.76           O  
ANISOU    4  O   GLN A   5     8708   8708   8708      0      0      0       O  
ATOM      5  CB  GLN A   5     132.240   1.932  26.714  0.50 66.27           C  
ANISOU    5  CB  GLN A   5     8393   8393   8393      0      0      0       C  
ATOM      6  CG  GLN A   5     132.518   2.406  25.298  0.50 69.23           C  
ANISOU    6  CG  GLN A   5     8769   8769   8769      0      0      0       C  
ATOM      7  CD  GLN A   5     133.796   1.829  24.728  0.50 70.94           C  
ANISOU    7  CD  GLN A   5     8984   8984   8984      0      0      0       C  
ATOM      8  OE1 GLN A   5     134.757   1.580  25.457  0.50 67.06           O  
ANISOU    8  OE1 GLN A   5     8493   8493   8493      0      0      0       O  
ATOM      9  NE2 GLN A   5     133.813   1.608  23.418  0.50 64.98           N  
ANISOU    9  NE2 GLN A   5     8230   8230   8230      0      0      0       N  
ATOM     10  N   VAL A   6     129.256   1.958  28.769  1.00 33.91           N  
ANISOU   10  N   VAL A   6     4294   4294   4294      0      0      0       N  
ATOM     11  CA  VAL A   6     128.506   1.214  29.777  1.00 23.95           C  
ANISOU   11  CA  VAL A   6     3033   3033   3033      0      0      0       C  
ATOM     12  C   VAL A   6     128.687  -0.296  29.732  1.00 32.16           C  
ANISOU   12  C   VAL A   6     4074   4074   4074      0      0      0       C  
ATOM     13  O   VAL A   6     128.554  -0.901  28.663  1.00 34.12           O  
ANISOU   13  O   VAL A   6     4321   4321   4321      0      0      0       O  
ATOM     14  CB  VAL A   6     127.019   1.531  29.695  1.00 27.81           C  
ANISOU   14  CB  VAL A   6     3523   3523   3523      0      0      0       C  
ATOM     15  CG1 VAL A   6     126.265   0.699  30.704  1.00 26.48           C  
ANISOU   15  CG1 VAL A   6     3354   3354   3354      0      0      0       C  
ATOM     16  CG2 VAL A   6     126.797   3.005  29.959  1.00 32.26           C  
ANISOU   16  CG2 VAL A   6     4086   4086   4086      0      0      0       C  
ATOM     17  N   ASN A   7     129.069  -0.905  30.854  1.00 28.14           N  
ANISOU   17  N   ASN A   7     3564   3564   3564      0      0      0       N  
ATOM     18  CA  ASN A   7     129.238  -2.337  30.794  1.00 36.67           C  
ANISOU   18  CA  ASN A   7     4644   4644   4644      0      0      0       C  
ATOM     19  C   ASN A   7     127.963  -3.034  31.299  1.00 33.15           C  
ANISOU   19  C   ASN A   7     4199   4199   4199      0      0      0       C  
ATOM     20  O   ASN A   7     127.603  -2.934  32.480  1.00 33.80           O  
ANISOU   20  O   ASN A   7     4281   4281   4281      0      0      0       O  
ATOM     21  CB  ASN A   7     130.499  -2.749  31.590  1.00 55.64           C  
ANISOU   21  CB  ASN A   7     7047   7047   7047      0      0      0       C  
ATOM     22  CG  ASN A   7     130.572  -4.230  31.902  1.00 59.49           C  
ANISOU   22  CG  ASN A   7     7534   7534   7534      0      0      0       C  
ATOM     23  OD1 ASN A   7     130.131  -5.063  31.121  1.00 69.52           O  
ANISOU   23  OD1 ASN A   7     8805   8805   8805      0      0      0       O  
ATOM     24  ND2 ASN A   7     131.165  -4.565  33.045  1.00 53.09           N  
ANISOU   24  ND2 ASN A   7     6724   6724   6724      0      0      0       N  
ATOM     25  N   TRP A   8     127.377  -3.872  30.429  1.00 22.28           N  
ANISOU   25  N   TRP A   8     2821   2821   2821      0      0      0       N  
ATOM     26  CA  TRP A   8     126.189  -4.633  30.813  1.00 31.22           C  
ANISOU   26  CA  TRP A   8     3953   3953   3953      0      0      0       C  
ATOM     27  C   TRP A   8     126.681  -6.029  31.160  1.00 31.39           C  
ANISOU   27  C   TRP A   8     3976   3976   3976      0      0      0       C  
ATOM     28  O   TRP A   8     127.471  -6.587  30.403  1.00 22.10           O  
ANISOU   28  O   TRP A   8     2799   2799   2799      0      0      0       O  
ATOM     29  CB  TRP A   8     125.200  -4.704  29.642  1.00 22.68           C  
ANISOU   29  CB  TRP A   8     2873   2873   2873      0      0      0       C  
ATOM     30  CG  TRP A   8     124.596  -3.404  29.187  1.00 27.07           C  
ANISOU   30  CG  TRP A   8     3429   3429   3429      0      0      0       C  
ATOM     31  CD1 TRP A   8     125.254  -2.364  28.594  1.00 21.57           C  
ANISOU   31  CD1 TRP A   8     2732   2732   2732      0      0      0       C  
ATOM     32  CD2 TRP A   8     123.225  -2.991  29.307  1.00 28.38           C  
ANISOU   32  CD2 TRP A   8     3594   3594   3594      0      0      0       C  
ATOM     33  NE1 TRP A   8     124.380  -1.347  28.308  1.00 12.39           N  
ANISOU   33  NE1 TRP A   8     1570   1570   1570      0      0      0       N  
ATOM     34  CE2 TRP A   8     123.128  -1.699  28.743  1.00 28.82           C  
ANISOU   34  CE2 TRP A   8     3650   3650   3650      0      0      0       C  
ATOM     35  CE3 TRP A   8     122.070  -3.591  29.818  1.00 25.95           C  
ANISOU   35  CE3 TRP A   8     3287   3287   3287      0      0      0       C  
ATOM     36  CZ2 TRP A   8     121.923  -0.993  28.688  1.00 17.78           C  
ANISOU   36  CZ2 TRP A   8     2252   2252   2252      0      0      0       C  
ATOM     37  CZ3 TRP A   8     120.870  -2.883  29.761  1.00 34.75           C  
ANISOU   37  CZ3 TRP A   8     4402   4402   4402      0      0      0       C  
ATOM     38  CH2 TRP A   8     120.812  -1.602  29.206  1.00 27.22           C  
ANISOU   38  CH2 TRP A   8     3447   3447   3447      0      0      0       C  
ATOM     39  N   PRO A   9     126.095  -6.659  32.187  1.00 22.26           N  
ANISOU   39  N   PRO A   9     2819   2819   2819      0      0      0       N  
ATOM     40  CA  PRO A   9     126.609  -7.971  32.582  1.00 28.01           C  
ANISOU   40  CA  PRO A   9     3548   3548   3548      0      0      0       C  
ATOM     41  C   PRO A   9     126.166  -9.079  31.636  1.00 40.04           C  
ANISOU   41  C   PRO A   9     5071   5071   5071      0      0      0       C  
ATOM     42  O   PRO A   9     125.012  -9.094  31.198  1.00 30.12           O  
ANISOU   42  O   PRO A   9     3815   3815   3815      0      0      0       O  
ATOM     43  CB  PRO A   9     125.965  -8.170  33.958  1.00 32.62           C  
ANISOU   43  CB  PRO A   9     4131   4131   4131      0      0      0       C  
ATOM     44  CG  PRO A   9     124.643  -7.435  33.837  1.00 25.65           C  
ANISOU   44  CG  PRO A   9     3249   3249   3249      0      0      0       C  
ATOM     45  CD  PRO A   9     124.963  -6.216  33.015  1.00 31.01           C  
ANISOU   45  CD  PRO A   9     3928   3928   3928      0      0      0       C  
ATOM     46  N   TYR A  10     127.026 -10.066  31.416  1.00 27.82           N  
ANISOU   46  N   TYR A  10     3523   3523   3523      0      0      0       N  
ATOM     47  CA  TYR A  10     126.603 -11.246  30.661  1.00 24.12           C  
ANISOU   47  CA  TYR A  10     3055   3055   3055      0      0      0       C  
ATOM     48  C   TYR A  10     125.769 -12.121  31.582  1.00 31.06           C  
ANISOU   48  C   TYR A  10     3934   3934   3934      0      0      0       C  
ATOM     49  O   TYR A  10     126.245 -12.556  32.633  1.00 29.06           O  
ANISOU   49  O   TYR A  10     3680   3680   3680      0      0      0       O  
ATOM     50  CB  TYR A  10     127.834 -11.992  30.116  1.00 26.38           C  
ANISOU   50  CB  TYR A  10     3341   3341   3341      0      0      0       C  
ATOM     51  CG  TYR A  10     127.533 -13.213  29.273  1.00 46.58           C  
ANISOU   51  CG  TYR A  10     5899   5899   5899      0      0      0       C  
ATOM     52  CD1 TYR A  10     127.382 -13.098  27.897  1.00 31.70           C  
ANISOU   52  CD1 TYR A  10     4015   4015   4015      0      0      0       C  
ATOM     53  CD2 TYR A  10     127.524 -14.494  29.824  1.00 25.96           C  
ANISOU   53  CD2 TYR A  10     3288   3288   3288      0      0      0       C  
ATOM     54  CE1 TYR A  10     127.147 -14.204  27.106  1.00 40.83           C  
ANISOU   54  CE1 TYR A  10     5171   5171   5171      0      0      0       C  
ATOM     55  CE2 TYR A  10     127.292 -15.612  29.036  1.00 39.52           C  
ANISOU   55  CE2 TYR A  10     5005   5005   5005      0      0      0       C  
ATOM     56  CZ  TYR A  10     127.108 -15.462  27.681  1.00 48.56           C  
ANISOU   56  CZ  TYR A  10     6150   6150   6150      0      0      0       C  
ATOM     57  OH  TYR A  10     126.872 -16.558  26.895  1.00 40.53           O  
ANISOU   57  OH  TYR A  10     5133   5133   5133      0      0      0       O  
ATOM     58  N   VAL A  11     124.534 -12.399  31.180  1.00 16.87           N  
ANISOU   58  N   VAL A  11     2137   2137   2137      0      0      0       N  
ATOM     59  CA  VAL A  11     123.616 -13.094  32.064  1.00 26.83           C  
ANISOU   59  CA  VAL A  11     3398   3398   3398      0      0      0       C  
ATOM     60  C   VAL A  11     123.114 -14.363  31.427  1.00 39.22           C  
ANISOU   60  C   VAL A  11     4967   4967   4967      0      0      0       C  
ATOM     61  O   VAL A  11     122.318 -15.068  32.034  1.00 44.24           O  
ANISOU   61  O   VAL A  11     5603   5603   5603      0      0      0       O  
ATOM     62  CB  VAL A  11     122.411 -12.253  32.521  1.00 35.11           C  
ANISOU   62  CB  VAL A  11     4447   4447   4447      0      0      0       C  
ATOM     63  CG1 VAL A  11     122.868 -10.983  33.229  1.00 34.53           C  
ANISOU   63  CG1 VAL A  11     4374   4374   4374      0      0      0       C  
ATOM     64  CG2 VAL A  11     121.607 -11.862  31.315  1.00 36.36           C  
ANISOU   64  CG2 VAL A  11     4605   4605   4605      0      0      0       C  
ATOM     65  N   ASN A  12     123.603 -14.696  30.233  1.00 25.29           N  
ANISOU   65  N   ASN A  12     3203   3203   3203      0      0      0       N  
ATOM     66  CA  ASN A  12     123.125 -15.933  29.674  1.00 38.92           C  
ANISOU   66  CA  ASN A  12     4930   4930   4930      0      0      0       C  
ATOM     67  C   ASN A  12     123.975 -17.141  30.086  1.00 33.54           C  
ANISOU   67  C   ASN A  12     4248   4248   4248      0      0      0       C  
ATOM     68  O   ASN A  12     124.639 -17.750  29.257  1.00 22.33           O  
ANISOU   68  O   ASN A  12     2828   2828   2828      0      0      0       O  
ATOM     69  CB  ASN A  12     123.073 -15.829  28.141  1.00 29.78           C  
ANISOU   69  CB  ASN A  12     3772   3772   3772      0      0      0       C  
ATOM     70  CG  ASN A  12     122.429 -17.063  27.490  1.00 41.69           C  
ANISOU   70  CG  ASN A  12     5281   5281   5281      0      0      0       C  
ATOM     71  OD1 ASN A  12     121.424 -17.561  28.003  1.00 26.05           O  
ANISOU   71  OD1 ASN A  12     3300   3300   3300      0      0      0       O  
ATOM     72  ND2 ASN A  12     123.023 -17.585  26.409  1.00 14.36           N  
ANISOU   72  ND2 ASN A  12     1819   1819   1819      0      0      0       N  
ATOM     73  N   THR A  13     124.059 -17.357  31.391  1.00 35.81           N  
ANISOU   73  N   THR A  13     4536   4536   4536      0      0      0       N  
ATOM     74  CA  THR A  13     124.959 -18.325  32.000  1.00 37.26           C  
ANISOU   74  CA  THR A  13     4719   4719   4719      0      0      0       C  
ATOM     75  C   THR A  13     124.359 -19.728  32.305  1.00 44.01           C  
ANISOU   75  C   THR A  13     5574   5574   5574      0      0      0       C  
ATOM     76  O   THR A  13     125.131 -20.619  32.653  1.00 40.39           O  
ANISOU   76  O   THR A  13     5115   5115   5115      0      0      0       O  
ATOM     77  CB  THR A  13     125.628 -17.742  33.267  1.00 27.53           C  
ANISOU   77  CB  THR A  13     3487   3487   3487      0      0      0       C  
ATOM     78  OG1 THR A  13     124.635 -17.666  34.300  1.00 32.96           O  
ANISOU   78  OG1 THR A  13     4174   4174   4174      0      0      0       O  
ATOM     79  CG2 THR A  13     126.001 -16.306  33.038  1.00 37.63           C  
ANISOU   79  CG2 THR A  13     4766   4766   4766      0      0      0       C  
ATOM     80  N   LYS A  14     123.037 -19.946  32.161  1.00 37.23           N  
ANISOU   80  N   LYS A  14     4715   4715   4715      0      0      0       N  
ATOM     81  CA  LYS A  14     122.450 -21.247  32.553  1.00 32.80           C  
ANISOU   81  CA  LYS A  14     4155   4155   4155      0      0      0       C  
ATOM     82  C   LYS A  14     122.123 -22.068  31.328  1.00 43.60           C  
ANISOU   82  C   LYS A  14     5522   5522   5522      0      0      0       C  
ATOM     83  O   LYS A  14     122.552 -23.213  31.210  1.00 40.96           O  
ANISOU   83  O   LYS A  14     5188   5188   5188      0      0      0       O  
ATOM     84  CB  LYS A  14     121.163 -21.136  33.395  1.00 36.43           C  
ANISOU   84  CB  LYS A  14     4614   4614   4614      0      0      0       C  
ATOM     85  CG  LYS A  14     121.262 -20.552  34.774  1.00 60.48           C  
ANISOU   85  CG  LYS A  14     7659   7659   7659      0      0      0       C  
ATOM     86  CD  LYS A  14     119.875 -20.319  35.380  1.00 41.45           C  
ANISOU   86  CD  LYS A  14     5249   5249   5249      0      0      0       C  
ATOM     87  CE  LYS A  14     119.887 -20.554  36.890  1.00 44.55           C  
ANISOU   87  CE  LYS A  14     5642   5642   5642      0      0      0       C  
ATOM     88  NZ  LYS A  14     120.077 -21.947  37.347  1.00 74.78           N  
ANISOU   88  NZ  LYS A  14     9470   9470   9470      0      0      0       N  
ATOM     89  N   LEU A  15     121.384 -21.468  30.401  1.00 33.50           N  
ANISOU   89  N   LEU A  15     4243   4243   4243      0      0      0       N  
ATOM     90  CA  LEU A  15     120.919 -22.201  29.241  1.00 37.15           C  
ANISOU   90  CA  LEU A  15     4706   4706   4706      0      0      0       C  
ATOM     91  C   LEU A  15     122.091 -22.490  28.312  1.00 42.18           C  
ANISOU   91  C   LEU A  15     5343   5343   5343      0      0      0       C  
ATOM     92  O   LEU A  15     122.841 -21.574  27.976  1.00 37.74           O  
ANISOU   92  O   LEU A  15     4779   4779   4779      0      0      0       O  
ATOM     93  CB  LEU A  15     119.836 -21.424  28.490  1.00 24.37           C  
ANISOU   93  CB  LEU A  15     3086   3086   3086      0      0      0       C  
ATOM     94  CG  LEU A  15     119.278 -22.200  27.294  1.00 30.61           C  
ANISOU   94  CG  LEU A  15     3876   3876   3876      0      0      0       C  
ATOM     95  CD1 LEU A  15     118.541 -23.457  27.761  1.00 32.07           C  
ANISOU   95  CD1 LEU A  15     4061   4061   4061      0      0      0       C  
ATOM     96  CD2 LEU A  15     118.394 -21.328  26.431  1.00 36.50           C  
ANISOU   96  CD2 LEU A  15     4623   4623   4623      0      0      0       C  
ATOM     97  N   LYS A  16     122.304 -23.758  27.983  1.00 38.19           N  
ANISOU   97  N   LYS A  16     4837   4837   4837      0      0      0       N  
ATOM     98  CA  LYS A  16     123.291 -24.175  26.992  1.00 41.23           C  
ANISOU   98  CA  LYS A  16     5222   5222   5222      0      0      0       C  
ATOM     99  C   LYS A  16     122.606 -24.641  25.730  1.00 41.05           C  
ANISOU   99  C   LYS A  16     5200   5200   5200      0      0      0       C  
ATOM    100  O   LYS A  16     121.510 -25.211  25.798  1.00 37.38           O  
ANISOU  100  O   LYS A  16     4734   4734   4734      0      0      0       O  
ATOM    101  CB  LYS A  16     124.143 -25.315  27.527  1.00 38.24           C  
ANISOU  101  CB  LYS A  16     4844   4844   4844      0      0      0       C  
ATOM    102  CG  LYS A  16     124.592 -25.112  28.955  1.00 41.05           C  
ANISOU  102  CG  LYS A  16     5199   5199   5199      0      0      0       C  
ATOM    103  CD  LYS A  16     125.452 -23.867  29.093  1.00 34.36           C  
ANISOU  103  CD  LYS A  16     4352   4352   4352      0      0      0       C  
ATOM    104  CE  LYS A  16     125.964 -23.755  30.519  1.00 51.53           C  
ANISOU  104  CE  LYS A  16     6526   6526   6526      0      0      0       C  
ATOM    105  NZ  LYS A  16     127.200 -22.938  30.601  1.00 75.91           N  
ANISOU  105  NZ  LYS A  16     9614   9614   9614      0      0      0       N  
ATOM    106  N   ARG A  17     123.219 -24.390  24.577  1.00 32.36           N  
ANISOU  106  N   ARG A  17     4099   4099   4099      0      0      0       N  
ATOM    107  CA  ARG A  17     122.616 -24.875  23.351  1.00 33.86           C  
ANISOU  107  CA  ARG A  17     4278   4271   4314     21    -33    -35       C  
ATOM    108  C   ARG A  17     122.568 -26.405  23.365  1.00 40.97           C  
ANISOU  108  C   ARG A  17     5151   5151   5263     47   -104    -79       C  
ATOM    109  O   ARG A  17     123.395 -27.073  23.978  1.00 35.11           O  
ANISOU  109  O   ARG A  17     4426   4374   4538     59   -113    -95       O  
ATOM    110  CB  ARG A  17     123.385 -24.405  22.128  1.00 25.86           C  
ANISOU  110  CB  ARG A  17     3254   3268   3305     26    -46    -45       C  
ATOM    111  CG  ARG A  17     123.212 -22.947  21.856  1.00 33.53           C  
ANISOU  111  CG  ARG A  17     4245   4246   4247      1     -2     -2       C  
ATOM    112  CD  ARG A  17     123.938 -22.554  20.607  1.00 25.86           C  
ANISOU  112  CD  ARG A  17     3264   3275   3285     12    -17    -21       C  
ATOM    113  NE  ARG A  17     123.795 -21.131  20.362  1.00 26.47           N  
ANISOU  113  NE  ARG A  17     3353   3353   3353      0      0      0       N  
ATOM    114  CZ  ARG A  17     124.393 -20.499  19.360  1.00 41.50           C  
ANISOU  114  CZ  ARG A  17     5256   5256   5256      0      0      0       C  
ATOM    115  NH1 ARG A  17     125.159 -21.195  18.516  1.00 28.23           N  
ANISOU  115  NH1 ARG A  17     3562   3577   3588     21    -21    -39       N  
ATOM    116  NH2 ARG A  17     124.211 -19.186  19.186  1.00 29.85           N  
ANISOU  116  NH2 ARG A  17     3780   3780   3780      0      0      0       N  
ATOM    117  N   ASP A  18     121.604 -26.949  22.641  1.00 36.28           N  
ANISOU  117  N   ASP A  18     4563   4512   4711     67   -128   -116       N  
ATOM    118  CA  ASP A  18     121.454 -28.382  22.487  1.00 23.95           C  
ANISOU  118  CA  ASP A  18     2954   2936   3212     84   -221   -146       C  
ATOM    119  C   ASP A  18     122.051 -28.770  21.145  1.00 28.53           C  
ANISOU  119  C   ASP A  18     3553   3453   3833    117   -236   -206       C  
ATOM    120  O   ASP A  18     121.586 -28.310  20.099  1.00 16.43           O  
ANISOU  120  O   ASP A  18     1969   1981   2291    112   -259   -202       O  
ATOM    121  CB  ASP A  18     119.976 -28.769  22.570  1.00 39.47           C  
ANISOU  121  CB  ASP A  18     4906   4878   5211     82   -245   -148       C  
ATOM    122  CG  ASP A  18     119.731 -30.278  22.382  1.00 41.76           C  
ANISOU  122  CG  ASP A  18     5165   5110   5591     99   -336   -180       C  
ATOM    123  OD1 ASP A  18     120.427 -30.946  21.583  1.00 37.03           O  
ANISOU  123  OD1 ASP A  18     4547   4490   5031    119   -384   -216       O  
ATOM    124  OD2 ASP A  18     118.862 -30.798  23.121  1.00 42.43           O  
ANISOU  124  OD2 ASP A  18     5300   5095   5725     97   -327   -179       O  
ATOM    125  N   PRO A  19     123.136 -29.559  21.176  1.00 20.49           N  
ANISOU  125  N   PRO A  19     2485   2467   2832    122   -305   -210       N  
ATOM    126  CA  PRO A  19     123.859 -29.893  19.947  1.00 21.91           C  
ANISOU  126  CA  PRO A  19     2645   2641   3039    147   -343   -253       C  
ATOM    127  C   PRO A  19     122.962 -30.501  18.863  1.00 35.70           C  
ANISOU  127  C   PRO A  19     4360   4361   4842    165   -395   -293       C  
ATOM    128  O   PRO A  19     123.151 -30.191  17.682  1.00 37.94           O  
ANISOU  128  O   PRO A  19     4697   4582   5136    194   -354   -349       O  
ATOM    129  CB  PRO A  19     124.884 -30.936  20.429  1.00 29.58           C  
ANISOU  129  CB  PRO A  19     3610   3487   4141    218   -486   -367       C  
ATOM    130  CG  PRO A  19     125.092 -30.603  21.874  1.00 31.23           C  
ANISOU  130  CG  PRO A  19     3901   3740   4226    150   -316   -246       C  
ATOM    131  CD  PRO A  19     123.734 -30.170  22.370  1.00 25.99           C  
ANISOU  131  CD  PRO A  19     3192   3147   3534    118   -320   -197       C  
ATOM    132  N   ALA A  20     122.008 -31.345  19.244  1.00 24.49           N  
ANISOU  132  N   ALA A  20     2997   2817   3490    179   -393   -324       N  
ATOM    133  CA  ALA A  20     121.073 -31.932  18.276  1.00 40.81           C  
ANISOU  133  CA  ALA A  20     4959   4939   5607    179   -491   -333       C  
ATOM    134  C   ALA A  20     120.176 -30.868  17.621  1.00 23.08           C  
ANISOU  134  C   ALA A  20     2794   2638   3339    188   -396   -358       C  
ATOM    135  O   ALA A  20     119.979 -30.828  16.395  1.00 25.44           O  
ANISOU  135  O   ALA A  20     3076   2933   3657    206   -413   -397       O  
ATOM    136  CB  ALA A  20     120.220 -33.020  18.957  1.00 16.73           C  
ANISOU  136  CB  ALA A  20     1882   1676   2799    238   -680   -447       C  
ATOM    137  N   VAL A  21     119.707 -29.941  18.445  1.00 45.70           N  
ANISOU  137  N   VAL A  21     5676   5543   6145    161   -339   -307       N  
ATOM    138  CA  VAL A  21     118.861 -28.866  17.953  1.00 26.72           C  
ANISOU  138  CA  VAL A  21     3213   3244   3693    138   -333   -269       C  
ATOM    139  C   VAL A  21     119.669 -28.044  16.971  1.00 23.47           C  
ANISOU  139  C   VAL A  21     2863   2805   3248    156   -271   -302       C  
ATOM    140  O   VAL A  21     119.187 -27.745  15.872  1.00 33.83           O  
ANISOU  140  O   VAL A  21     4163   4122   4570    166   -277   -328       O  
ATOM    141  CB  VAL A  21     118.337 -27.973  19.100  1.00 29.94           C  
ANISOU  141  CB  VAL A  21     3702   3623   4049    119   -238   -234       C  
ATOM    142  CG1 VAL A  21     117.710 -26.688  18.553  1.00 29.63           C  
ANISOU  142  CG1 VAL A  21     3670   3628   3961    106   -191   -213       C  
ATOM    143  CG2 VAL A  21     117.327 -28.729  19.937  1.00 27.83           C  
ANISOU  143  CG2 VAL A  21     3377   3376   3820    104   -298   -208       C  
ATOM    144  N   GLU A  22     120.907 -27.721  17.327  1.00 29.97           N  
ANISOU  144  N   GLU A  22     3648   3708   4030    138   -281   -260       N  
ATOM    145  CA  GLU A  22     121.735 -26.912  16.439  1.00 29.44           C  
ANISOU  145  CA  GLU A  22     3632   3618   3937    152   -227   -286       C  
ATOM    146  C   GLU A  22     122.043 -27.629  15.128  1.00 33.22           C  
ANISOU  146  C   GLU A  22     4013   4071   4538    234   -389   -439       C  
ATOM    147  O   GLU A  22     122.054 -27.012  14.057  1.00 29.15           O  
ANISOU  147  O   GLU A  22     3507   3637   3934    177   -311   -336       O  
ATOM    148  CB  GLU A  22     123.037 -26.511  17.136  1.00 17.34           C  
ANISOU  148  CB  GLU A  22     2062   2109   2418    174   -279   -318       C  
ATOM    149  CG  GLU A  22     122.826 -25.710  18.411  1.00 34.73           C  
ANISOU  149  CG  GLU A  22     4299   4337   4560    131   -206   -238       C  
ATOM    150  CD  GLU A  22     122.083 -24.403  18.131  1.00 49.50           C  
ANISOU  150  CD  GLU A  22     6195   6257   6357     75   -122   -139       C  
ATOM    151  OE1 GLU A  22     122.472 -23.710  17.167  1.00 35.10           O  
ANISOU  151  OE1 GLU A  22     4390   4420   4525     83   -100   -156       O  
ATOM    152  OE2 GLU A  22     121.140 -24.043  18.874  1.00 30.69           O  
ANISOU  152  OE2 GLU A  22     3823   3861   3978     77   -114   -145       O  
ATOM    153  N   ALA A  23     122.236 -28.942  15.210  1.00 38.75           N  
ANISOU  153  N   ALA A  23     4708   4798   5215    191   -380   -358       N  
ATOM    154  CA  ALA A  23     122.465 -29.743  14.022  1.00 26.97           C  
ANISOU  154  CA  ALA A  23     3183   3288   3777    223   -443   -417       C  
ATOM    155  C   ALA A  23     121.262 -29.654  13.081  1.00 18.87           C  
ANISOU  155  C   ALA A  23     2219   2166   2784    251   -403   -483       C  
ATOM    156  O   ALA A  23     121.428 -29.483  11.862  1.00 26.66           O  
ANISOU  156  O   ALA A  23     3079   3158   3894    338   -580   -652       O  
ATOM    157  CB  ALA A  23     122.758 -31.192  14.398  1.00 32.72           C  
ANISOU  157  CB  ALA A  23     3894   3970   4570    239   -512   -444       C  
ATOM    158  N   GLN A  24     120.054 -29.780  13.641  1.00 20.65           N  
ANISOU  158  N   GLN A  24     2446   2372   3029    238   -404   -465       N  
ATOM    159  CA  GLN A  24     118.856 -29.700  12.802  1.00 26.15           C  
ANISOU  159  CA  GLN A  24     3034   3153   3747    225   -474   -451       C  
ATOM    160  C   GLN A  24     118.751 -28.318  12.181  1.00 35.64           C  
ANISOU  160  C   GLN A  24     4227   4313   5003    293   -510   -591       C  
ATOM    161  O   GLN A  24     118.448 -28.187  10.990  1.00 44.78           O  
ANISOU  161  O   GLN A  24     5476   5476   6063    252   -381   -512       O  
ATOM    162  CB  GLN A  24     117.547 -29.977  13.559  1.00 29.53           C  
ANISOU  162  CB  GLN A  24     3434   3432   4353    288   -590   -588       C  
ATOM    163  CG  GLN A  24     117.403 -31.291  14.255  0.70 39.83           C  
ANISOU  163  CG  GLN A  24     4722   4658   5755    293   -666   -598       C  
ATOM    164  CD  GLN A  24     116.099 -31.350  15.034  0.70 41.48           C  
ANISOU  164  CD  GLN A  24     4928   4836   5997    267   -663   -558       C  
ATOM    165  OE1 GLN A  24     116.080 -31.592  16.241  0.70 24.71           O  
ANISOU  165  OE1 GLN A  24     2844   2853   3692    179   -529   -373       O  
ATOM    166  NE2 GLN A  24     114.984 -31.239  14.303  0.70 20.90           N  
ANISOU  166  NE2 GLN A  24     2323   2373   3245    201   -551   -430       N  
ATOM    167  N   ILE A  25     119.012 -27.283  12.988  1.00 29.79           N  
ANISOU  167  N   ILE A  25     3618   3619   4080    205   -306   -411       N  
ATOM    168  CA  ILE A  25     118.970 -25.920  12.455  1.00 25.84           C  
ANISOU  168  CA  ILE A  25     3127   3166   3524    190   -260   -385       C  
ATOM    169  C   ILE A  25     119.878 -25.766  11.277  1.00 19.28           C  
ANISOU  169  C   ILE A  25     2219   2412   2695    192   -317   -385       C  
ATOM    170  O   ILE A  25     119.441 -25.357  10.209  1.00 20.18           O  
ANISOU  170  O   ILE A  25     2387   2471   2809    220   -277   -444       O  
ATOM    171  CB  ILE A  25     119.398 -24.866  13.508  1.00 28.17           C  
ANISOU  171  CB  ILE A  25     3401   3545   3757    142   -234   -286       C  
ATOM    172  CG1 ILE A  25     118.451 -24.824  14.703  1.00 23.14           C  
ANISOU  172  CG1 ILE A  25     2782   2900   3109    122   -209   -249       C  
ATOM    173  CG2 ILE A  25     119.494 -23.483  12.880  1.00 21.10           C  
ANISOU  173  CG2 ILE A  25     2521   2676   2821    128   -195   -260       C  
ATOM    174  CD1 ILE A  25     119.007 -24.028  15.871  1.00 31.93           C  
ANISOU  174  CD1 ILE A  25     3966   3997   4169    101   -132   -206       C  
ATOM    175  N   GLU A  26     121.113 -26.215  11.436  1.00 29.28           N  
ANISOU  175  N   GLU A  26     3552   3610   3963    219   -284   -429       N  
ATOM    176  CA  GLU A  26     122.068 -26.040  10.372  1.00 22.23           C  
ANISOU  176  CA  GLU A  26     2580   2798   3068    218   -345   -422       C  
ATOM    177  C   GLU A  26     121.727 -26.820   9.107  1.00 32.69           C  
ANISOU  177  C   GLU A  26     3835   4049   4536    344   -491   -667       C  
ATOM    178  O   GLU A  26     121.827 -26.288   7.993  1.00 37.39           O  
ANISOU  178  O   GLU A  26     4416   4671   5118    358   -491   -696       O  
ATOM    179  CB  GLU A  26     123.479 -26.361  10.831  1.00 25.75           C  
ANISOU  179  CB  GLU A  26     3102   3176   3506    242   -298   -456       C  
ATOM    180  CG  GLU A  26     124.073 -25.424  11.866  0.70 19.26           C  
ANISOU  180  CG  GLU A  26     2247   2438   2633    190   -289   -356       C  
ATOM    181  CD  GLU A  26     123.883 -23.973  11.482  0.70 24.45           C  
ANISOU  181  CD  GLU A  26     2899   3095   3294    231   -290   -438       C  
ATOM    182  OE1 GLU A  26     124.255 -23.582  10.366  0.70 22.99           O  
ANISOU  182  OE1 GLU A  26     2723   2948   3065    182   -251   -344       O  
ATOM    183  OE2 GLU A  26     123.547 -23.176  12.377  0.70 33.57           O  
ANISOU  183  OE2 GLU A  26     4104   4277   4374    140   -196   -267       O  
ATOM    184  N   LYS A  27     121.230 -28.047   9.289  1.00 44.34           N  
ANISOU  184  N   LYS A  27     5288   5469   6089    365   -557   -712       N  
ATOM    185  CA  LYS A  27     120.832 -28.882   8.151  1.00 33.54           C  
ANISOU  185  CA  LYS A  27     3877   4066   4801    409   -637   -802       C  
ATOM    186  C   LYS A  27     119.687 -28.217   7.400  1.00 37.19           C  
ANISOU  186  C   LYS A  27     4469   4534   5128    325   -442   -649       C  
ATOM    187  O   LYS A  27     119.664 -28.219   6.168  1.00 30.74           O  
ANISOU  187  O   LYS A  27     3482   3738   4458    438   -654   -873       O  
ATOM    188  CB  LYS A  27     120.442 -30.294   8.612  1.00 37.10           C  
ANISOU  188  CB  LYS A  27     4306   4441   5349    425   -715   -837       C  
ATOM    189  CG  LYS A  27     120.111 -31.228   7.461  0.70 18.09           C  
ANISOU  189  CG  LYS A  27     2017   1990   2865    377   -577   -745       C  
ATOM    190  CD  LYS A  27     119.747 -32.627   7.951  0.70 49.06           C  
ANISOU  190  CD  LYS A  27     5928   5839   6876    387   -640   -768       C  
ATOM    191  CE  LYS A  27     119.429 -33.566   6.785  0.70 53.65           C  
ANISOU  191  CE  LYS A  27     6280   6348   7756    530   -990  -1056       C  
ATOM    192  NZ  LYS A  27     119.089 -34.950   7.234  0.70 67.42           N  
ANISOU  192  NZ  LYS A  27     7997   7995   9623    539  -1082  -1079       N  
ATOM    193  N   LEU A  28     118.745 -27.642   8.142  1.00 37.30           N  
ANISOU  193  N   LEU A  28     4497   4558   5120    297   -407   -602       N  
ATOM    194  CA  LEU A  28     117.640 -26.918   7.529  1.00 32.67           C  
ANISOU  194  CA  LEU A  28     3808   4081   4526    268   -455   -554       C  
ATOM    195  C   LEU A  28     118.150 -25.694   6.763  1.00 41.99           C  
ANISOU  195  C   LEU A  28     5000   5303   5651    264   -417   -540       C  
ATOM    196  O   LEU A  28     117.843 -25.539   5.583  1.00 34.65           O  
ANISOU  196  O   LEU A  28     4007   4324   4834    385   -528   -790       O  
ATOM    197  CB  LEU A  28     116.629 -26.495   8.589  1.00 29.49           C  
ANISOU  197  CB  LEU A  28     3517   3586   4102    262   -360   -551       C  
ATOM    198  CG  LEU A  28     115.599 -27.523   9.032  1.00 37.35           C  
ANISOU  198  CG  LEU A  28     4365   4529   5299    335   -561   -714       C  
ATOM    199  CD1 LEU A  28     114.728 -26.950  10.138  1.00 40.48           C  
ANISOU  199  CD1 LEU A  28     4824   5023   5533    216   -413   -470       C  
ATOM    200  CD2 LEU A  28     114.738 -27.913   7.837  1.00 36.81           C  
ANISOU  200  CD2 LEU A  28     4402   4430   5153    294   -444   -634       C  
ATOM    201  N   LEU A  29     118.966 -24.859   7.414  1.00 30.00           N  
ANISOU  201  N   LEU A  29     3481   3760   4159    327   -440   -665       N  
ATOM    202  CA  LEU A  29     119.492 -23.643   6.762  1.00 29.17           C  
ANISOU  202  CA  LEU A  29     3422   3732   3928    232   -331   -469       C  
ATOM    203  C   LEU A  29     120.268 -23.858   5.508  1.00 28.15           C  
ANISOU  203  C   LEU A  29     3230   3583   3884    355   -438   -707       C  
ATOM    204  O   LEU A  29     120.195 -23.039   4.596  1.00 36.36           O  
ANISOU  204  O   LEU A  29     4295   4672   4848    286   -340   -517       O  
ATOM    205  CB  LEU A  29     120.409 -22.813   7.664  1.00 38.05           C  
ANISOU  205  CB  LEU A  29     4647   4813   4999    222   -233   -445       C  
ATOM    206  CG  LEU A  29     119.818 -21.772   8.592  1.00 64.10           C  
ANISOU  206  CG  LEU A  29     7912   8167   8276    183   -215   -338       C  
ATOM    207  CD1 LEU A  29     120.949 -21.133   9.370  1.00 62.88           C  
ANISOU  207  CD1 LEU A  29     7787   8016   8087    159   -180   -290       C  
ATOM    208  CD2 LEU A  29     119.170 -20.737   7.660  1.00 43.60           C  
ANISOU  208  CD2 LEU A  29     5314   5587   5665    180   -202   -337       C  
ATOM    209  N   ALA A  30     121.126 -24.866   5.508  1.00 33.75           N  
ANISOU  209  N   ALA A  30     3962   4311   4550    280   -404   -551       N  
ATOM    210  CA  ALA A  30     121.998 -25.104   4.370  1.00 35.41           C  
ANISOU  210  CA  ALA A  30     4107   4492   4856    421   -525   -817       C  
ATOM    211  C   ALA A  30     121.230 -25.256   3.065  1.00 37.51           C  
ANISOU  211  C   ALA A  30     4337   4759   5157    456   -570   -891       C  
ATOM    212  O   ALA A  30     121.752 -24.995   1.987  1.00 49.89           O  
ANISOU  212  O   ALA A  30     6039   6297   6618    385   -408   -746       O  
ATOM    213  CB  ALA A  30     122.866 -26.319   4.622  1.00 37.65           C  
ANISOU  213  CB  ALA A  30     4518   4701   5086    358   -406   -687       C  
ATOM    214  N   LYS A  31     119.999 -25.716   3.170  1.00 30.53           N  
ANISOU  214  N   LYS A  31     3486   3899   4216    337   -495   -668       N  
ATOM    215  CA  LYS A  31     119.162 -25.996   2.011  1.00 47.51           C  
ANISOU  215  CA  LYS A  31     5551   5986   6513    496   -646   -988       C  
ATOM    216  C   LYS A  31     118.058 -24.974   1.738  1.00 49.54           C  
ANISOU  216  C   LYS A  31     5978   6221   6623    381   -424   -768       C  
ATOM    217  O   LYS A  31     117.443 -24.985   0.673  1.00 58.77           O  
ANISOU  217  O   LYS A  31     7128   7391   7812    404   -448   -817       O  
ATOM    218  CB  LYS A  31     118.581 -27.404   2.132  1.00 47.15           C  
ANISOU  218  CB  LYS A  31     5654   5836   6423    419   -511   -840       C  
ATOM    219  CG  LYS A  31     117.435 -27.516   3.124  1.00 68.68           C  
ANISOU  219  CG  LYS A  31     8265   8658   9173    362   -586   -739       C  
ATOM    220  CD  LYS A  31     116.909 -28.956   3.216  1.00 89.16           C  
ANISOU  220  CD  LYS A  31    10964  11064  11849    417   -566   -855       C  
ATOM    221  CE  LYS A  31     115.605 -29.025   4.008  1.00 83.08           C  
ANISOU  221  CE  LYS A  31    10196  10266  11104    395   -562   -827       C  
ATOM    222  NZ  LYS A  31     115.109 -30.423   4.180  1.00 73.34           N  
ANISOU  222  NZ  LYS A  31     8792   9109   9966    377   -720   -794       N  
ATOM    223  N   MET A  32     117.851 -24.044   2.663  1.00 36.32           N  
ANISOU  223  N   MET A  32     4181   4616   5003    427   -533   -870       N  
ATOM    224  CA  MET A  32     116.766 -23.084   2.495  1.00 34.43           C  
ANISOU  224  CA  MET A  32     4103   4354   4625    298   -364   -680       C  
ATOM    225  C   MET A  32     117.057 -21.975   1.494  1.00 34.80           C  
ANISOU  225  C   MET A  32     4036   4506   4680    327   -377   -607       C  
ATOM    226  O   MET A  32     118.205 -21.576   1.297  1.00 36.70           O  
ANISOU  226  O   MET A  32     4248   4757   4941    407   -455   -821       O  
ATOM    227  CB  MET A  32     116.392 -22.454   3.845  1.00 38.88           C  
ANISOU  227  CB  MET A  32     4592   4986   5196    284   -345   -539       C  
ATOM    228  CG  MET A  32     115.709 -23.408   4.785  1.00 19.74           C  
ANISOU  228  CG  MET A  32     2260   2455   2784    281   -317   -596       C  
ATOM    229  SD  MET A  32     115.536 -22.840   6.476  1.00 31.90           S  
ANISOU  229  SD  MET A  32     3757   4070   4293    217   -317   -466       S  
ATOM    230  CE  MET A  32     114.222 -21.638   6.302  1.00 36.59           C  
ANISOU  230  CE  MET A  32     4439   4623   4839    199   -248   -484       C  
ATOM    231  N   THR A  33     116.010 -21.535   0.800  1.00 23.65           N  
ANISOU  231  N   THR A  33     2611   3104   3271    333   -381   -624       N  
ATOM    232  CA  THR A  33     116.135 -20.384  -0.073  1.00 29.49           C  
ANISOU  232  CA  THR A  33     3354   3874   3976    332   -361   -617       C  
ATOM    233  C   THR A  33     115.997 -19.120   0.776  1.00 41.08           C  
ANISOU  233  C   THR A  33     4864   5348   5396    289   -302   -542       C  
ATOM    234  O   THR A  33     115.561 -19.167   1.930  1.00 37.81           O  
ANISOU  234  O   THR A  33     4437   4924   5006    330   -350   -693       O  
ATOM    235  CB  THR A  33     115.037 -20.371  -1.150  1.00 31.68           C  
ANISOU  235  CB  THR A  33     3600   4160   4275    357   -389   -665       C  
ATOM    236  OG1 THR A  33     113.748 -20.389  -0.519  1.00 43.82           O  
ANISOU  236  OG1 THR A  33     5099   5678   5873    427   -476   -898       O  
ATOM    237  CG2 THR A  33     115.147 -21.607  -2.032  1.00 39.90           C  
ANISOU  237  CG2 THR A  33     4599   5192   5371    402   -453   -743       C  
ATOM    238  N   ILE A  34     116.388 -17.992   0.200  1.00 36.94           N  
ANISOU  238  N   ILE A  34     4312   4866   4859    352   -350   -721       N  
ATOM    239  CA  ILE A  34     116.181 -16.690   0.810  1.00 28.93           C  
ANISOU  239  CA  ILE A  34     3455   3792   3744    224   -213   -510       C  
ATOM    240  C   ILE A  34     114.678 -16.533   1.152  1.00 37.78           C  
ANISOU  240  C   ILE A  34     4577   4906   4870    214   -207   -499       C  
ATOM    241  O   ILE A  34     114.317 -16.129   2.257  1.00 41.18           O  
ANISOU  241  O   ILE A  34     5030   5328   5289    186   -178   -442       O  
ATOM    242  CB  ILE A  34     116.664 -15.596  -0.118  1.00 31.44           C  
ANISOU  242  CB  ILE A  34     3689   4172   4086    246   -223   -454       C  
ATOM    243  CG1 ILE A  34     118.197 -15.706  -0.220  1.00 20.00           C  
ANISOU  243  CG1 ILE A  34     2325   2689   2584    229   -207   -505       C  
ATOM    244  CG2 ILE A  34     116.172 -14.236   0.367  1.00 41.96           C  
ANISOU  244  CG2 ILE A  34     5022   5535   5385    264   -230   -545       C  
ATOM    245  CD1 ILE A  34     118.826 -14.804  -1.260  1.00 37.57           C  
ANISOU  245  CD1 ILE A  34     4546   4937   4792    237   -205   -513       C  
ATOM    246  N   GLU A  35     113.817 -16.963   0.233  1.00 34.13           N  
ANISOU  246  N   GLU A  35     4000   4492   4477    262   -258   -504       N  
ATOM    247  CA  GLU A  35     112.374 -16.843   0.379  1.00 28.02           C  
ANISOU  247  CA  GLU A  35     3315   3667   3664    236   -235   -562       C  
ATOM    248  C   GLU A  35     111.873 -17.598   1.608  1.00 33.61           C  
ANISOU  248  C   GLU A  35     4030   4347   4391    223   -232   -543       C  
ATOM    249  O   GLU A  35     111.062 -17.088   2.378  1.00 42.09           O  
ANISOU  249  O   GLU A  35     5119   5419   5454    200   -207   -499       O  
ATOM    250  CB  GLU A  35     111.680 -17.378  -0.878  1.00 31.48           C  
ANISOU  250  CB  GLU A  35     3616   4161   4183    296   -302   -578       C  
ATOM    251  CG  GLU A  35     111.669 -16.394  -2.042  1.00 25.43           C  
ANISOU  251  CG  GLU A  35     2950   3373   3340    282   -275   -656       C  
ATOM    252  CD  GLU A  35     112.924 -16.468  -2.874  1.00 36.40           C  
ANISOU  252  CD  GLU A  35     4331   4777   4722    301   -289   -683       C  
ATOM    253  OE1 GLU A  35     113.885 -17.159  -2.457  1.00 40.41           O  
ANISOU  253  OE1 GLU A  35     4842   5272   5240    302   -295   -683       O  
ATOM    254  OE2 GLU A  35     112.957 -15.810  -3.935  1.00 48.64           O  
ANISOU  254  OE2 GLU A  35     5755   6406   6319    343   -320   -633       O  
ATOM    255  N   GLN A  36     112.368 -18.811   1.796  1.00 18.71           N  
ANISOU  255  N   GLN A  36     2038   2492   2580    260   -283   -518       N  
ATOM    256  CA  GLN A  36     111.986 -19.617   2.941  1.00 33.10           C  
ANISOU  256  CA  GLN A  36     3829   4280   4467    311   -356   -697       C  
ATOM    257  C   GLN A  36     112.470 -19.040   4.277  1.00 18.79           C  
ANISOU  257  C   GLN A  36     2068   2469   2604    264   -295   -596       C  
ATOM    258  O   GLN A  36     111.770 -19.102   5.299  1.00 29.10           O  
ANISOU  258  O   GLN A  36     3423   3763   3872    192   -219   -403       O  
ATOM    259  CB  GLN A  36     112.478 -21.066   2.741  1.00 33.46           C  
ANISOU  259  CB  GLN A  36     3883   4311   4520    279   -336   -558       C  
ATOM    260  CG  GLN A  36     111.706 -21.788   1.661  1.00 27.46           C  
ANISOU  260  CG  GLN A  36     3195   3466   3771    289   -358   -703       C  
ATOM    261  CD  GLN A  36     112.471 -22.960   1.035  1.00 45.29           C  
ANISOU  261  CD  GLN A  36     5257   5745   6208    439   -558   -950       C  
ATOM    262  OE1 GLN A  36     113.645 -23.183   1.321  1.00 37.93           O  
ANISOU  262  OE1 GLN A  36     4337   4816   5258    437   -553   -933       O  
ATOM    263  NE2 GLN A  36     111.795 -23.710   0.177  1.00 26.16           N  
ANISOU  263  NE2 GLN A  36     2788   3292   3859    479   -628  -1039       N  
ATOM    264  N   LYS A  37     113.671 -18.471   4.259  1.00 25.53           N  
ANISOU  264  N   LYS A  37     2972   3335   3392    202   -216   -406       N  
ATOM    265  CA  LYS A  37     114.253 -17.872   5.460  1.00 26.68           C  
ANISOU  265  CA  LYS A  37     3221   3441   3473    153   -160   -377       C  
ATOM    266  C   LYS A  37     113.442 -16.664   5.902  1.00 11.43           C  
ANISOU  266  C   LYS A  37     1256   1543   1543    139   -139   -289       C  
ATOM    267  O   LYS A  37     113.002 -16.533   7.077  1.00 42.18           O  
ANISOU  267  O   LYS A  37     5223   5401   5402    106   -106   -273       O  
ATOM    268  CB  LYS A  37     115.711 -17.483   5.199  1.00 28.87           C  
ANISOU  268  CB  LYS A  37     3445   3761   3765    166   -167   -328       C  
ATOM    269  CG  LYS A  37     116.649 -18.648   4.924  1.00 23.86           C  
ANISOU  269  CG  LYS A  37     2786   3124   3156    192   -201   -371       C  
ATOM    270  CD  LYS A  37     118.040 -18.157   4.534  1.00 25.83           C  
ANISOU  270  CD  LYS A  37     3042   3385   3389    192   -193   -363       C  
ATOM    271  CE  LYS A  37     118.930 -19.312   4.117  1.00 32.13           C  
ANISOU  271  CE  LYS A  37     3888   4141   4177    204   -212   -460       C  
ATOM    272  NZ  LYS A  37     120.331 -18.847   3.831  1.00 21.87           N  
ANISOU  272  NZ  LYS A  37     2519   2893   2897    222   -223   -404       N  
ATOM    273  N   VAL A  38     113.153 -15.832   4.908  1.00 28.33           N  
ANISOU  273  N   VAL A  38     3389   3699   3677    145   -140   -300       N  
ATOM    274  CA  VAL A  38     112.377 -14.626   5.152  1.00 38.31           C  
ANISOU  274  CA  VAL A  38     4677   4961   4919    122   -113   -259       C  
ATOM    275  C   VAL A  38     111.009 -15.032   5.643  1.00 41.45           C  
ANISOU  275  C   VAL A  38     5119   5328   5301    110   -105   -292       C  
ATOM    276  O   VAL A  38     110.456 -14.427   6.563  1.00 29.67           O  
ANISOU  276  O   VAL A  38     3608   3847   3817     96    -89   -217       O  
ATOM    277  CB  VAL A  38     112.315 -13.699   3.919  1.00 37.31           C  
ANISOU  277  CB  VAL A  38     4514   4877   4784    165   -146   -377       C  
ATOM    278  CG1 VAL A  38     111.322 -12.574   4.135  1.00 26.46           C  
ANISOU  278  CG1 VAL A  38     3184   3474   3395    113    -96   -241       C  
ATOM    279  CG2 VAL A  38     113.702 -13.169   3.579  1.00 28.69           C  
ANISOU  279  CG2 VAL A  38     3455   3765   3682    130   -111   -262       C  
ATOM    280  N   ALA A  39     110.505 -16.113   5.054  1.00 20.68           N  
ANISOU  280  N   ALA A  39     2375   2736   2746    186   -188   -444       N  
ATOM    281  CA  ALA A  39     109.200 -16.621   5.436  1.00 25.23           C  
ANISOU  281  CA  ALA A  39     3030   3256   3299    138   -146   -374       C  
ATOM    282  C   ALA A  39     109.181 -16.964   6.907  1.00 27.65           C  
ANISOU  282  C   ALA A  39     3302   3578   3627    129   -140   -296       C  
ATOM    283  O   ALA A  39     108.185 -16.720   7.598  1.00 29.51           O  
ANISOU  283  O   ALA A  39     3550   3806   3856    114   -125   -273       O  
ATOM    284  CB  ALA A  39     108.821 -17.821   4.606  1.00 34.59           C  
ANISOU  284  CB  ALA A  39     4072   4468   4602    233   -262   -566       C  
ATOM    285  N   GLN A  40     110.286 -17.532   7.389  1.00 19.12           N  
ANISOU  285  N   GLN A  40     2228   2491   2546    128   -141   -288       N  
ATOM    286  CA  GLN A  40     110.394 -17.841   8.808  1.00 11.66           C  
ANISOU  286  CA  GLN A  40     1355   1505   1571     99   -111   -274       C  
ATOM    287  C   GLN A  40     110.309 -16.535   9.619  1.00 31.72           C  
ANISOU  287  C   GLN A  40     3929   4053   4072     68    -72   -196       C  
ATOM    288  O   GLN A  40     109.887 -16.550  10.785  1.00 28.71           O  
ANISOU  288  O   GLN A  40     3525   3680   3703     72    -76   -194       O  
ATOM    289  CB  GLN A  40     111.678 -18.582   9.135  1.00 29.02           C  
ANISOU  289  CB  GLN A  40     3488   3722   3818    141   -162   -345       C  
ATOM    290  CG  GLN A  40     111.635 -20.025   8.691  1.00 33.60           C  
ANISOU  290  CG  GLN A  40     4048   4292   4428    144   -178   -314       C  
ATOM    291  CD  GLN A  40     110.453 -20.756   9.264  1.00 32.65           C  
ANISOU  291  CD  GLN A  40     3914   4150   4342    146   -195   -327       C  
ATOM    292  OE1 GLN A  40     110.308 -20.908  10.475  1.00 28.47           O  
ANISOU  292  OE1 GLN A  40     3407   3610   3801    128   -177   -292       O  
ATOM    293  NE2 GLN A  40     109.585 -21.217   8.378  1.00 24.25           N  
ANISOU  293  NE2 GLN A  40     2813   3075   3326    169   -234   -380       N  
ATOM    294  N   MET A  41     110.716 -15.409   9.018  1.00 13.84           N  
ANISOU  294  N   MET A  41     1642   1811   1804     68    -66   -160       N  
ATOM    295  CA  MET A  41     110.784 -14.173   9.820  1.00 26.37           C  
ANISOU  295  CA  MET A  41     3290   3375   3355     36    -33   -105       C  
ATOM    296  C   MET A  41     109.511 -13.314   9.862  1.00 32.71           C  
ANISOU  296  C   MET A  41     4087   4182   4162     31    -27    -79       C  
ATOM    297  O   MET A  41     109.436 -12.379  10.660  1.00 32.30           O  
ANISOU  297  O   MET A  41     4075   4105   4093     10     -8    -31       O  
ATOM    298  CB  MET A  41     111.923 -13.289   9.292  1.00 19.74           C  
ANISOU  298  CB  MET A  41     2443   2542   2517     35    -30    -82       C  
ATOM    299  CG  MET A  41     113.285 -13.958   9.292  1.00 16.48           C  
ANISOU  299  CG  MET A  41     2040   2125   2098     38    -33   -103       C  
ATOM    300  SD  MET A  41     114.514 -12.933   8.482  1.00 28.22           S  
ANISOU  300  SD  MET A  41     3529   3615   3578     37    -30    -96       S  
ATOM    301  CE  MET A  41     114.496 -11.492   9.572  1.00 11.95           C  
ANISOU  301  CE  MET A  41     1501   1525   1515      8     -6    -18       C  
ATOM    302  N   ILE A  42     108.498 -13.672   9.078  1.00 29.69           N  
ANISOU  302  N   ILE A  42     3661   3825   3795     60    -55   -169       N  
ATOM    303  CA  ILE A  42     107.288 -12.849   8.931  1.00 23.74           C  
ANISOU  303  CA  ILE A  42     2924   3062   3035     44    -39   -115       C  
ATOM    304  C   ILE A  42     106.103 -13.389   9.736  1.00 40.97           C  
ANISOU  304  C   ILE A  42     5126   5228   5210     37    -35   -126       C  
ATOM    305  O   ILE A  42     105.832 -14.584   9.690  1.00 34.31           O  
ANISOU  305  O   ILE A  42     4234   4399   4403     56    -57   -155       O  
ATOM    306  CB  ILE A  42     106.856 -12.772   7.455  1.00 30.36           C  
ANISOU  306  CB  ILE A  42     3756   3911   3869     60    -54   -185       C  
ATOM    307  CG1 ILE A  42     108.029 -12.319   6.595  1.00 35.29           C  
ANISOU  307  CG1 ILE A  42     4345   4557   4506     72    -62   -174       C  
ATOM    308  CG2 ILE A  42     105.644 -11.850   7.276  1.00 16.11           C  
ANISOU  308  CG2 ILE A  42     1954   2110   2058     56    -48   -176       C  
ATOM    309  CD1 ILE A  42     108.627 -11.002   7.021  1.00 34.19           C  
ANISOU  309  CD1 ILE A  42     4266   4393   4333     45    -36   -131       C  
ATOM    310  N   GLN A  43     105.400 -12.526  10.472  1.00 27.40           N  
ANISOU  310  N   GLN A  43     3417   3506   3488     24    -21    -72       N  
ATOM    311  CA  GLN A  43     104.274 -12.975  11.290  1.00 20.43           C  
ANISOU  311  CA  GLN A  43     2535   2618   2608     22    -20    -70       C  
ATOM    312  C   GLN A  43     102.945 -12.263  11.000  1.00 26.76           C  
ANISOU  312  C   GLN A  43     3346   3418   3402     20    -18    -83       C  
ATOM    313  O   GLN A  43     102.727 -11.142  11.462  1.00 29.57           O  
ANISOU  313  O   GLN A  43     3726   3762   3748      9     -7    -37       O  
ATOM    314  CB  GLN A  43     104.609 -12.774  12.761  1.00 20.46           C  
ANISOU  314  CB  GLN A  43     2584   2596   2593      3     -3    -13       C  
ATOM    315  CG  GLN A  43     103.528 -13.256  13.705  1.00 22.99           C  
ANISOU  315  CG  GLN A  43     2906   2915   2914      2     -2    -10       C  
ATOM    316  CD  GLN A  43     103.824 -12.895  15.146  1.00 39.67           C  
ANISOU  316  CD  GLN A  43     5024   5024   5024      0      0      0       C  
ATOM    317  OE1 GLN A  43     103.373 -11.858  15.641  1.00 32.20           O  
ANISOU  317  OE1 GLN A  43     4078   4078   4078      0      0      0       O  
ATOM    318  NE2 GLN A  43     104.604 -13.729  15.817  1.00 33.43           N  
ANISOU  318  NE2 GLN A  43     4234   4234   4234      0      0      0       N  
ATOM    319  N   PRO A  44     102.040 -12.921  10.263  1.00 39.68           N  
ANISOU  319  N   PRO A  44     4953   5066   5060     36    -35   -144       N  
ATOM    320  CA  PRO A  44     100.677 -12.417  10.044  1.00 15.82           C  
ANISOU  320  CA  PRO A  44     1923   2048   2040     38    -37   -158       C  
ATOM    321  C   PRO A  44      99.821 -12.612  11.283  1.00 27.52           C  
ANISOU  321  C   PRO A  44     3395   3529   3533     31    -31   -120       C  
ATOM    322  O   PRO A  44     100.217 -13.305  12.203  1.00 17.55           O  
ANISOU  322  O   PRO A  44     2144   2255   2269     26    -28   -105       O  
ATOM    323  CB  PRO A  44     100.136 -13.326   8.936  1.00 31.22           C  
ANISOU  323  CB  PRO A  44     3832   3999   4029     61    -64   -241       C  
ATOM    324  CG  PRO A  44     101.317 -14.084   8.401  1.00 42.47           C  
ANISOU  324  CG  PRO A  44     5202   5447   5488     79    -86   -244       C  
ATOM    325  CD  PRO A  44     102.279 -14.183   9.543  1.00 31.82           C  
ANISOU  325  CD  PRO A  44     3925   4069   4098     57    -61   -212       C  
ATOM    326  N   GLU A  45      98.673 -11.946  11.323  1.00 28.40           N  
ANISOU  326  N   GLU A  45     3507   3642   3640     28    -27   -118       N  
ATOM    327  CA  GLU A  45      97.693 -12.060  12.418  1.00 35.52           C  
ANISOU  327  CA  GLU A  45     4421   4533   4543     20    -21   -102       C  
ATOM    328  C   GLU A  45      96.407 -12.636  11.845  1.00 18.35           C  
ANISOU  328  C   GLU A  45     2228   2339   2404     30    -36   -178       C  
ATOM    329  O   GLU A  45      96.090 -12.417  10.682  1.00 14.32           O  
ANISOU  329  O   GLU A  45     1637   1859   1944     56    -65   -274       O  
ATOM    330  CB  GLU A  45      97.446 -10.700  13.061  1.00 33.02           C  
ANISOU  330  CB  GLU A  45     4146   4206   4196      8     -7    -47       C  
ATOM    331  CG  GLU A  45      96.769 -10.741  14.419  1.00 34.66           C  
ANISOU  331  CG  GLU A  45     4375   4398   4395      2     -2    -18       C  
ATOM    332  CD  GLU A  45      95.259 -10.776  14.289  1.00 35.98           C  
ANISOU  332  CD  GLU A  45     4516   4575   4578      6     -6    -52       C  
ATOM    333  OE1 GLU A  45      94.751 -10.276  13.267  1.00 37.11           O  
ANISOU  333  OE1 GLU A  45     4653   4726   4722     10     -9    -86       O  
ATOM    334  OE2 GLU A  45      94.578 -11.276  15.209  1.00 35.43           O  
ANISOU  334  OE2 GLU A  45     4444   4497   4520      5     -6    -54       O  
ATOM    335  N   ILE A  46      95.689 -13.405  12.655  1.00  9.91           N  
ANISOU  335  N   ILE A  46     1148   1240   1376     30    -42   -190       N  
ATOM    336  CA  ILE A  46      94.559 -14.201  12.153  1.00 45.83           C  
ANISOU  336  CA  ILE A  46     5605   5775   6033     44    -76   -229       C  
ATOM    337  C   ILE A  46      93.406 -13.394  11.570  1.00 52.85           C  
ANISOU  337  C   ILE A  46     6533   6631   6918     42    -69   -269       C  
ATOM    338  O   ILE A  46      92.621 -13.918  10.781  1.00 52.92           O  
ANISOU  338  O   ILE A  46     6438   6645   7023     58   -106   -294       O  
ATOM    339  CB  ILE A  46      94.008 -15.179  13.205  1.00 41.66           C  
ANISOU  339  CB  ILE A  46     5052   5188   5589     39    -90   -218       C  
ATOM    340  CG1 ILE A  46      93.417 -14.396  14.384  1.00 28.53           C  
ANISOU  340  CG1 ILE A  46     3469   3486   3887     22    -57   -182       C  
ATOM    341  CG2 ILE A  46      95.095 -16.132  13.688  1.00 37.03           C  
ANISOU  341  CG2 ILE A  46     4522   4548   4999     38    -90   -231       C  
ATOM    342  CD1 ILE A  46      92.763 -15.270  15.420  1.00 38.22           C  
ANISOU  342  CD1 ILE A  46     4666   4633   5226     17    -70   -139       C  
ATOM    343  N   GLY A  47      93.306 -12.117  11.929  1.00 39.80           N  
ANISOU  343  N   GLY A  47     4914   5023   5186     31    -44   -223       N  
ATOM    344  CA  GLY A  47      92.277 -11.283  11.342  1.00 26.91           C  
ANISOU  344  CA  GLY A  47     3273   3401   3551     32    -43   -241       C  
ATOM    345  C   GLY A  47      92.495 -11.010   9.872  1.00 26.40           C  
ANISOU  345  C   GLY A  47     3142   3393   3494     49    -60   -258       C  
ATOM    346  O   GLY A  47      91.591 -10.532   9.198  1.00 34.66           O  
ANISOU  346  O   GLY A  47     4221   4418   4532     51    -61   -313       O  
ATOM    347  N   TYR A  48      93.698 -11.292   9.379  1.00 26.76           N  
ANISOU  347  N   TYR A  48     3238   3424   3504     51    -59   -283       N  
ATOM    348  CA  TYR A  48      94.052 -10.952   8.003  1.00 25.54           C  
ANISOU  348  CA  TYR A  48     3069   3295   3338     65    -69   -316       C  
ATOM    349  C   TYR A  48      94.609 -12.125   7.202  1.00 34.39           C  
ANISOU  349  C   TYR A  48     4099   4434   4534     92   -106   -342       C  
ATOM    350  O   TYR A  48      94.712 -12.053   5.973  1.00 49.65           O  
ANISOU  350  O   TYR A  48     5964   6389   6512    139   -156   -524       O  
ATOM    351  CB  TYR A  48      95.081  -9.822   8.017  1.00 40.90           C  
ANISOU  351  CB  TYR A  48     5046   5268   5226     54    -50   -255       C  
ATOM    352  CG  TYR A  48      94.621  -8.611   8.777  1.00 34.53           C  
ANISOU  352  CG  TYR A  48     4233   4478   4408     43    -35   -180       C  
ATOM    353  CD1 TYR A  48      93.818  -7.645   8.178  1.00 38.95           C  
ANISOU  353  CD1 TYR A  48     4819   5044   4934     42    -33   -207       C  
ATOM    354  CD2 TYR A  48      94.925  -8.475  10.121  1.00 28.18           C  
ANISOU  354  CD2 TYR A  48     3468   3649   3589     27    -21   -127       C  
ATOM    355  CE1 TYR A  48      93.379  -6.546   8.892  1.00 18.84           C  
ANISOU  355  CE1 TYR A  48     2294   2495   2369     31    -21   -159       C  
ATOM    356  CE2 TYR A  48      94.483  -7.390  10.851  1.00 37.74           C  
ANISOU  356  CE2 TYR A  48     4709   4847   4783     17    -12    -86       C  
ATOM    357  CZ  TYR A  48      93.710  -6.424  10.231  1.00 28.90           C  
ANISOU  357  CZ  TYR A  48     3598   3741   3643     19    -12   -106       C  
ATOM    358  OH  TYR A  48      93.282  -5.338  10.956  1.00 48.54           O  
ANISOU  358  OH  TYR A  48     6088   6219   6135     13     -7    -64       O  
ATOM    359  N   LEU A  49      94.939 -13.212   7.897  1.00 42.98           N  
ANISOU  359  N   LEU A  49     5245   5449   5634     83   -106   -378       N  
ATOM    360  CA  LEU A  49      95.612 -14.338   7.263  1.00 43.89           C  
ANISOU  360  CA  LEU A  49     5337   5542   5797    102   -137   -427       C  
ATOM    361  C   LEU A  49      94.598 -15.381   6.821  1.00 45.34           C  
ANISOU  361  C   LEU A  49     5477   5661   6088    119   -180   -495       C  
ATOM    362  O   LEU A  49      93.668 -15.707   7.553  1.00 40.06           O  
ANISOU  362  O   LEU A  49     4706   5013   5502    120   -203   -442       O  
ATOM    363  CB  LEU A  49      96.600 -14.971   8.251  1.00 31.89           C  
ANISOU  363  CB  LEU A  49     3835   4012   4271     92   -128   -389       C  
ATOM    364  CG  LEU A  49      97.312 -16.257   7.807  1.00 41.02           C  
ANISOU  364  CG  LEU A  49     4890   5191   5506    121   -178   -396       C  
ATOM    365  CD1 LEU A  49      98.324 -15.955   6.713  1.00 29.97           C  
ANISOU  365  CD1 LEU A  49     3569   3773   4047    123   -166   -454       C  
ATOM    366  CD2 LEU A  49      97.957 -16.990   9.002  1.00 28.25           C  
ANISOU  366  CD2 LEU A  49     3290   3552   3893    109   -171   -364       C  
ATOM    367  N   THR A  50      94.832 -15.965   5.653  1.00 25.03           N  
ANISOU  367  N   THR A  50     2777   3150   3584    156   -237   -506       N  
ATOM    368  CA  THR A  50      94.041 -17.099   5.227  1.00 35.24           C  
ANISOU  368  CA  THR A  50     4010   4382   4996    175   -295   -561       C  
ATOM    369  C   THR A  50      94.910 -18.354   5.281  1.00 42.94           C  
ANISOU  369  C   THR A  50     4968   5327   6022    187   -331   -576       C  
ATOM    370  O   THR A  50      96.142 -18.284   5.241  1.00 40.57           O  
ANISOU  370  O   THR A  50     4811   4973   5633    173   -287   -621       O  
ATOM    371  CB  THR A  50      93.480 -16.929   3.793  1.00 34.91           C  
ANISOU  371  CB  THR A  50     3930   4352   4981    202   -328   -623       C  
ATOM    372  OG1 THR A  50      94.559 -16.889   2.855  1.00 35.50           O  
ANISOU  372  OG1 THR A  50     4007   4469   5012    222   -334   -646       O  
ATOM    373  CG2 THR A  50      92.678 -15.645   3.677  1.00 39.19           C  
ANISOU  373  CG2 THR A  50     4611   4843   5435    175   -269   -671       C  
ATOM    374  N   VAL A  51      94.258 -19.506   5.364  1.00 48.23           N  
ANISOU  374  N   VAL A  51     5591   5926   6809    178   -392   -604       N  
ATOM    375  CA  VAL A  51      94.946 -20.795   5.298  1.00 31.94           C  
ANISOU  375  CA  VAL A  51     3427   3672   5035    260   -541   -853       C  
ATOM    376  C   VAL A  51      95.710 -20.898   3.985  1.00 36.18           C  
ANISOU  376  C   VAL A  51     4027   4397   5324    219   -466   -681       C  
ATOM    377  O   VAL A  51      96.848 -21.349   3.963  1.00 30.87           O  
ANISOU  377  O   VAL A  51     3507   3607   4615    247   -413   -744       O  
ATOM    378  CB  VAL A  51      93.960 -21.945   5.420  1.00 33.08           C  
ANISOU  378  CB  VAL A  51     3743   3727   5098    210   -449   -697       C  
ATOM    379  CG1 VAL A  51      94.690 -23.294   5.340  1.00 39.76           C  
ANISOU  379  CG1 VAL A  51     4571   4521   6016    225   -500   -720       C  
ATOM    380  CG2 VAL A  51      93.188 -21.832   6.723  1.00 41.63           C  
ANISOU  380  CG2 VAL A  51     4673   4922   6224    163   -479   -573       C  
ATOM    381  N   GLU A  52      95.111 -20.395   2.913  1.00 44.30           N  
ANISOU  381  N   GLU A  52     5184   5312   6335    257   -419   -789       N  
ATOM    382  CA  GLU A  52      95.735 -20.442   1.603  1.00 37.91           C  
ANISOU  382  CA  GLU A  52     4132   4541   5732    361   -618  -1059       C  
ATOM    383  C   GLU A  52      97.060 -19.704   1.576  1.00 50.02           C  
ANISOU  383  C   GLU A  52     5937   6153   6916    260   -408   -818       C  
ATOM    384  O   GLU A  52      98.030 -20.180   0.967  1.00 52.28           O  
ANISOU  384  O   GLU A  52     6219   6447   7199    279   -428   -847       O  
ATOM    385  CB  GLU A  52      94.792 -19.836   0.552  1.00 43.72           C  
ANISOU  385  CB  GLU A  52     4922   5422   6266    281   -521   -820       C  
ATOM    386  CG  GLU A  52      95.260 -19.898  -0.886  0.50 51.90           C  
ANISOU  386  CG  GLU A  52     5931   6487   7304    344   -540   -874       C  
ATOM    387  CD  GLU A  52      94.202 -19.409  -1.860  0.50 62.15           C  
ANISOU  387  CD  GLU A  52     7115   7684   8817    454   -700  -1265       C  
ATOM    388  OE1 GLU A  52      93.268 -18.711  -1.416  0.50 56.81           O  
ANISOU  388  OE1 GLU A  52     6532   7120   7933    343   -532   -896       O  
ATOM    389  OE2 GLU A  52      94.319 -19.686  -3.071  0.50 70.39           O  
ANISOU  389  OE2 GLU A  52     8406   8707   9633    366   -553  -1089       O  
ATOM    390  N   GLN A  53      97.123 -18.583   2.299  1.00 36.00           N  
ANISOU  390  N   GLN A  53     4060   4527   5091    254   -381   -677       N  
ATOM    391  CA  GLN A  53      98.343 -17.786   2.359  1.00 31.00           C  
ANISOU  391  CA  GLN A  53     3412   3897   4471    303   -419   -872       C  
ATOM    392  C   GLN A  53      99.442 -18.479   3.162  1.00 35.62           C  
ANISOU  392  C   GLN A  53     4019   4463   5054    292   -413   -834       C  
ATOM    393  O   GLN A  53     100.618 -18.452   2.786  1.00 25.24           O  
ANISOU  393  O   GLN A  53     2886   3144   3560    221   -299   -669       O  
ATOM    394  CB  GLN A  53      98.044 -16.399   2.961  1.00 38.59           C  
ANISOU  394  CB  GLN A  53     4585   4870   5208    195   -253   -633       C  
ATOM    395  CG  GLN A  53      97.371 -15.426   2.015  1.00 28.48           C  
ANISOU  395  CG  GLN A  53     3187   3693   3943    221   -273   -592       C  
ATOM    396  CD  GLN A  53      96.866 -14.193   2.727  1.00 40.79           C  
ANISOU  396  CD  GLN A  53     4884   5213   5401    176   -206   -588       C  
ATOM    397  OE1 GLN A  53      96.288 -14.286   3.813  1.00 34.06           O  
ANISOU  397  OE1 GLN A  53     4041   4339   4560    158   -192   -556       O  
ATOM    398  NE2 GLN A  53      97.009 -13.044   2.088  1.00 50.51           N  
ANISOU  398  NE2 GLN A  53     6124   6490   6577    175   -189   -572       N  
ATOM    399  N   MET A  54      99.024 -19.179   4.211  1.00 23.56           N  
ANISOU  399  N   MET A  54     2663   2857   3430    202   -309   -654       N  
ATOM    400  CA  MET A  54      99.928 -19.949   5.042  1.00 28.11           C  
ANISOU  400  CA  MET A  54     3135   3502   4046    213   -339   -568       C  
ATOM    401  C   MET A  54     100.509 -21.094   4.236  1.00 40.99           C  
ANISOU  401  C   MET A  54     4851   5007   5718    244   -353   -686       C  
ATOM    402  O   MET A  54     101.683 -21.414   4.376  1.00 44.59           O  
ANISOU  402  O   MET A  54     5141   5489   6314    308   -493   -845       O  
ATOM    403  CB  MET A  54      99.239 -20.477   6.304  1.00 28.99           C  
ANISOU  403  CB  MET A  54     3358   3474   4183    194   -303   -593       C  
ATOM    404  CG  MET A  54     100.159 -21.340   7.161  1.00 36.48           C  
ANISOU  404  CG  MET A  54     4315   4401   5145    189   -309   -569       C  
ATOM    405  SD  MET A  54     101.613 -20.549   7.884  1.00 27.05           S  
ANISOU  405  SD  MET A  54     3074   3354   3850    168   -282   -457       S  
ATOM    406  CE  MET A  54     100.877 -19.506   9.149  1.00 26.72           C  
ANISOU  406  CE  MET A  54     3158   3264   3731    123   -206   -431       C  
ATOM    407  N   ARG A  55      99.679 -21.700   3.393  1.00 37.15           N  
ANISOU  407  N   ARG A  55     4126   4480   5508    336   -566   -939       N  
ATOM    408  CA  ARG A  55     100.112 -22.777   2.516  1.00 41.55           C  
ANISOU  408  CA  ARG A  55     4638   4995   6152    377   -647  -1022       C  
ATOM    409  C   ARG A  55     101.112 -22.248   1.493  1.00 41.69           C  
ANISOU  409  C   ARG A  55     4739   5197   5904    294   -521   -769       C  
ATOM    410  O   ARG A  55     102.170 -22.850   1.276  1.00 34.52           O  
ANISOU  410  O   ARG A  55     3828   4289   4999    307   -542   -783       O  
ATOM    411  CB  ARG A  55      98.910 -23.399   1.794  1.00 36.64           C  
ANISOU  411  CB  ARG A  55     3955   4301   5667    404   -726  -1100       C  
ATOM    412  CG  ARG A  55      99.267 -24.620   0.943  1.00 51.28           C  
ANISOU  412  CG  ARG A  55     5842   6272   7369    329   -672   -871       C  
ATOM    413  CD  ARG A  55      98.030 -25.294   0.349  1.00 62.08           C  
ANISOU  413  CD  ARG A  55     7347   7397   8844    377   -651  -1007       C  
ATOM    414  NE  ARG A  55      96.922 -25.336   1.307  1.00 85.94           N  
ANISOU  414  NE  ARG A  55    10167  10555  11933    319   -733   -883       N  
ATOM    415  CZ  ARG A  55      96.761 -26.270   2.245  1.00 80.24           C  
ANISOU  415  CZ  ARG A  55     9429   9768  11292    304   -759   -854       C  
ATOM    416  NH1 ARG A  55      97.636 -27.258   2.356  1.00 77.12           N  
ANISOU  416  NH1 ARG A  55     9024   9349  10929    313   -796   -863       N  
ATOM    417  NH2 ARG A  55      95.720 -26.223   3.071  1.00 41.46           N  
ANISOU  417  NH2 ARG A  55     4710   4611   6431    304   -671   -886       N  
ATOM    418  N   LYS A  56     100.812 -21.088   0.921  1.00 20.65           N  
ANISOU  418  N   LYS A  56     2082   2574   3191    318   -473   -756       N  
ATOM    419  CA  LYS A  56     101.679 -20.518  -0.099  1.00 30.83           C  
ANISOU  419  CA  LYS A  56     3524   3807   4381    307   -427   -856       C  
ATOM    420  C   LYS A  56     103.034 -20.099   0.437  1.00 31.82           C  
ANISOU  420  C   LYS A  56     3543   4063   4483    316   -422   -718       C  
ATOM    421  O   LYS A  56     104.036 -20.290  -0.235  1.00 35.92           O  
ANISOU  421  O   LYS A  56     4197   4506   4947    307   -400   -820       O  
ATOM    422  CB  LYS A  56     101.017 -19.308  -0.754  1.00 47.31           C  
ANISOU  422  CB  LYS A  56     5468   6039   6470    334   -440   -770       C  
ATOM    423  CG  LYS A  56     101.850 -18.683  -1.858  1.00 35.94           C  
ANISOU  423  CG  LYS A  56     4176   4553   4928    322   -400   -870       C  
ATOM    424  CD  LYS A  56     101.127 -17.544  -2.556  1.00 54.08           C  
ANISOU  424  CD  LYS A  56     6261   6961   7327    442   -523  -1081       C  
ATOM    425  CE  LYS A  56     102.029 -16.911  -3.609  1.00 51.28           C  
ANISOU  425  CE  LYS A  56     5908   6665   6912    463   -518  -1093       C  
ATOM    426  NZ  LYS A  56     101.393 -15.751  -4.272  1.00 49.74           N  
ANISOU  426  NZ  LYS A  56     5923   6429   6548    341   -364   -879       N  
ATOM    427  N   TYR A  57     103.068 -19.519   1.635  1.00 35.07           N  
ANISOU  427  N   TYR A  57     4121   4398   4807    256   -339   -721       N  
ATOM    428  CA  TYR A  57     104.298 -18.907   2.126  1.00 36.00           C  
ANISOU  428  CA  TYR A  57     4268   4551   4858    237   -299   -660       C  
ATOM    429  C   TYR A  57     104.968 -19.670   3.278  1.00 25.26           C  
ANISOU  429  C   TYR A  57     2814   3238   3548    245   -321   -566       C  
ATOM    430  O   TYR A  57     106.193 -19.664   3.399  1.00 28.15           O  
ANISOU  430  O   TYR A  57     3196   3614   3885    242   -309   -547       O  
ATOM    431  CB  TYR A  57     104.038 -17.464   2.570  1.00 21.42           C  
ANISOU  431  CB  TYR A  57     2350   2803   2985    228   -270   -533       C  
ATOM    432  CG  TYR A  57     103.630 -16.541   1.437  1.00 36.57           C  
ANISOU  432  CG  TYR A  57     4210   4750   4933    299   -337   -759       C  
ATOM    433  CD1 TYR A  57     104.536 -16.136   0.472  1.00 49.29           C  
ANISOU  433  CD1 TYR A  57     5865   6389   6475    253   -273   -564       C  
ATOM    434  CD2 TYR A  57     102.338 -16.031   1.367  1.00 37.70           C  
ANISOU  434  CD2 TYR A  57     4498   4840   4987    216   -243   -616       C  
ATOM    435  CE1 TYR A  57     104.150 -15.286  -0.562  1.00 43.43           C  
ANISOU  435  CE1 TYR A  57     5217   5619   5665    243   -252   -644       C  
ATOM    436  CE2 TYR A  57     101.952 -15.174   0.343  1.00 25.34           C  
ANISOU  436  CE2 TYR A  57     2769   3372   3489    308   -332   -789       C  
ATOM    437  CZ  TYR A  57     102.861 -14.810  -0.616  1.00 35.83           C  
ANISOU  437  CZ  TYR A  57     4143   4717   4756    262   -271   -586       C  
ATOM    438  OH  TYR A  57     102.482 -13.963  -1.638  1.00 36.34           O  
ANISOU  438  OH  TYR A  57     4195   4810   4802    275   -273   -604       O  
ATOM    439  N   GLY A  58     104.184 -20.359   4.097  1.00 34.15           N  
ANISOU  439  N   GLY A  58     3931   4327   4717    238   -334   -566       N  
ATOM    440  CA  GLY A  58     104.767 -21.100   5.201  1.00 48.66           C  
ANISOU  440  CA  GLY A  58     5783   6140   6564    227   -333   -540       C  
ATOM    441  C   GLY A  58     105.382 -20.211   6.268  1.00 41.63           C  
ANISOU  441  C   GLY A  58     4947   5275   5596    193   -271   -465       C  
ATOM    442  O   GLY A  58     106.510 -20.441   6.698  1.00 40.57           O  
ANISOU  442  O   GLY A  58     4792   5106   5517    235   -327   -612       O  
ATOM    443  N   PHE A  59     104.678 -19.147   6.625  1.00 32.50           N  
ANISOU  443  N   PHE A  59     3897   4080   4370    157   -213   -473       N  
ATOM    444  CA  PHE A  59     105.168 -18.212   7.625  1.00 36.75           C  
ANISOU  444  CA  PHE A  59     4373   4673   4917    174   -223   -487       C  
ATOM    445  C   PHE A  59     105.614 -18.951   8.879  1.00 26.46           C  
ANISOU  445  C   PHE A  59     3118   3367   3568    128   -173   -328       C  
ATOM    446  O   PHE A  59     104.948 -19.880   9.309  1.00 38.22           O  
ANISOU  446  O   PHE A  59     4585   4827   5109    135   -199   -350       O  
ATOM    447  CB  PHE A  59     104.089 -17.185   7.957  1.00 18.35           C  
ANISOU  447  CB  PHE A  59     2156   2331   2487    111   -137   -356       C  
ATOM    448  CG  PHE A  59     103.678 -16.375   6.760  1.00 31.14           C  
ANISOU  448  CG  PHE A  59     3765   3971   4096    120   -141   -380       C  
ATOM    449  CD1 PHE A  59     104.563 -15.502   6.148  1.00 26.73           C  
ANISOU  449  CD1 PHE A  59     3157   3472   3527    128   -139   -326       C  
ATOM    450  CD2 PHE A  59     102.395 -16.487   6.248  1.00 40.19           C  
ANISOU  450  CD2 PHE A  59     4889   5106   5274    132   -160   -424       C  
ATOM    451  CE1 PHE A  59     104.186 -14.783   5.025  1.00 33.44           C  
ANISOU  451  CE1 PHE A  59     4056   4307   4342    128   -134   -386       C  
ATOM    452  CE2 PHE A  59     102.008 -15.754   5.155  1.00 25.66           C  
ANISOU  452  CE2 PHE A  59     2963   3332   3454    154   -179   -407       C  
ATOM    453  CZ  PHE A  59     102.898 -14.907   4.538  1.00 23.69           C  
ANISOU  453  CZ  PHE A  59     2800   3068   3132    140   -151   -430       C  
ATOM    454  N   GLY A  60     106.680 -18.469   9.506  1.00 23.92           N  
ANISOU  454  N   GLY A  60     2833   3057   3198    110   -141   -279       N  
ATOM    455  CA  GLY A  60     107.266 -19.098  10.678  1.00 18.12           C  
ANISOU  455  CA  GLY A  60     2116   2310   2459     99   -133   -253       C  
ATOM    456  C   GLY A  60     106.373 -19.076  11.907  1.00 22.45           C  
ANISOU  456  C   GLY A  60     2684   2848   3000     82   -115   -220       C  
ATOM    457  O   GLY A  60     106.561 -19.865  12.844  1.00 28.51           O  
ANISOU  457  O   GLY A  60     3453   3599   3780     79   -120   -213       O  
ATOM    458  N   SER A  61     105.450 -18.121  11.949  1.00 26.27           N  
ANISOU  458  N   SER A  61     3183   3340   3460     70    -94   -198       N  
ATOM    459  CA  SER A  61     104.523 -18.025  13.063  1.00 15.14           C  
ANISOU  459  CA  SER A  61     1823   1899   2030     51    -72   -186       C  
ATOM    460  C   SER A  61     103.322 -17.176  12.644  1.00 32.68           C  
ANISOU  460  C   SER A  61     4010   4149   4256     53    -72   -170       C  
ATOM    461  O   SER A  61     103.328 -16.526  11.597  1.00 22.95           O  
ANISOU  461  O   SER A  61     2752   2923   3044     73    -93   -251       O  
ATOM    462  CB  SER A  61     105.197 -17.383  14.283  1.00 22.68           C  
ANISOU  462  CB  SER A  61     2788   2877   2953     39    -52   -136       C  
ATOM    463  OG  SER A  61     105.564 -16.027  14.027  1.00 28.03           O  
ANISOU  463  OG  SER A  61     3508   3563   3579     18    -20    -58       O  
ATOM    464  N   TYR A  62     102.275 -17.204  13.454  1.00 29.02           N  
ANISOU  464  N   TYR A  62     3551   3675   3799     46    -67   -159       N  
ATOM    465  CA  TYR A  62     101.142 -16.320  13.230  1.00 27.70           C  
ANISOU  465  CA  TYR A  62     3418   3493   3613     38    -54   -169       C  
ATOM    466  C   TYR A  62     100.534 -15.932  14.565  1.00 36.84           C  
ANISOU  466  C   TYR A  62     4601   4653   4744     23    -34   -119       C  
ATOM    467  O   TYR A  62     100.746 -16.618  15.565  1.00 22.49           O  
ANISOU  467  O   TYR A  62     2768   2841   2937     22    -36    -97       O  
ATOM    468  CB  TYR A  62     100.118 -16.951  12.269  1.00 23.57           C  
ANISOU  468  CB  TYR A  62     2854   2941   3161     56    -87   -242       C  
ATOM    469  CG  TYR A  62      99.451 -18.202  12.787  1.00 31.20           C  
ANISOU  469  CG  TYR A  62     3707   3846   4301     85   -160   -337       C  
ATOM    470  CD1 TYR A  62     100.110 -19.435  12.782  1.00 29.16           C  
ANISOU  470  CD1 TYR A  62     3514   3555   4012     73   -148   -297       C  
ATOM    471  CD2 TYR A  62      98.146 -18.159  13.284  1.00 38.22           C  
ANISOU  471  CD2 TYR A  62     4669   4706   5148     57   -121   -265       C  
ATOM    472  CE1 TYR A  62      99.481 -20.577  13.258  1.00 27.75           C  
ANISOU  472  CE1 TYR A  62     3305   3303   3938     83   -183   -308       C  
ATOM    473  CE2 TYR A  62      97.514 -19.301  13.755  1.00 27.43           C  
ANISOU  473  CE2 TYR A  62     3200   3325   3897     58   -172   -250       C  
ATOM    474  CZ  TYR A  62      98.188 -20.505  13.748  1.00 27.44           C  
ANISOU  474  CZ  TYR A  62     3132   3194   4100     91   -260   -363       C  
ATOM    475  OH  TYR A  62      97.555 -21.636  14.214  1.00 48.94           O  
ANISOU  475  OH  TYR A  62     5846   5949   6800     65   -256   -257       O  
ATOM    476  N   LEU A  63      99.816 -14.816  14.581  1.00 28.30           N  
ANISOU  476  N   LEU A  63     3519   3593   3640     17    -23    -83       N  
ATOM    477  CA  LEU A  63      99.394 -14.218  15.832  1.00 23.40           C  
ANISOU  477  CA  LEU A  63     2938   2968   2984      5     -7    -32       C  
ATOM    478  C   LEU A  63      97.885 -14.269  16.088  1.00 35.35           C  
ANISOU  478  C   LEU A  63     4441   4468   4520      8    -11    -60       C  
ATOM    479  O   LEU A  63      97.061 -13.914  15.231  1.00 23.43           O  
ANISOU  479  O   LEU A  63     2898   2968   3038     13    -19    -84       O  
ATOM    480  CB  LEU A  63      99.863 -12.768  15.861  1.00 19.33           C  
ANISOU  480  CB  LEU A  63     2449   2449   2449      0      0      0       C  
ATOM    481  CG  LEU A  63      99.539 -11.900  17.078  1.00 32.44           C  
ANISOU  481  CG  LEU A  63     4109   4109   4109      0      0      0       C  
ATOM    482  CD1 LEU A  63     100.233 -12.439  18.315  1.00 31.81           C  
ANISOU  482  CD1 LEU A  63     4028   4028   4028      0      0      0       C  
ATOM    483  CD2 LEU A  63      99.991 -10.470  16.809  1.00 24.25           C  
ANISOU  483  CD2 LEU A  63     3071   3071   3071      0      0      0       C  
ATOM    484  N   ASN A  64      97.533 -14.696  17.291  1.00 22.79           N  
ANISOU  484  N   ASN A  64     2855   2869   2935      5    -10    -48       N  
ATOM    485  CA  ASN A  64      96.197 -14.482  17.815  1.00 33.10           C  
ANISOU  485  CA  ASN A  64     4136   4166   4274      5    -13    -48       C  
ATOM    486  C   ASN A  64      96.053 -13.099  18.412  1.00 38.86           C  
ANISOU  486  C   ASN A  64     4921   4921   4921      0      0      0       C  
ATOM    487  O   ASN A  64      96.336 -12.902  19.594  1.00 27.73           O  
ANISOU  487  O   ASN A  64     3512   3512   3512      0      0      0       O  
ATOM    488  CB  ASN A  64      95.918 -15.492  18.910  1.00 29.83           C  
ANISOU  488  CB  ASN A  64     3708   3692   3932      4    -22    -44       C  
ATOM    489  CG  ASN A  64      94.565 -15.292  19.540  1.00 42.90           C  
ANISOU  489  CG  ASN A  64     5335   5302   5665      0    -25     -4       C  
ATOM    490  OD1 ASN A  64      93.575 -15.050  18.854  1.00 43.14           O  
ANISOU  490  OD1 ASN A  64     5300   5336   5753      0    -33     -3       O  
ATOM    491  ND2 ASN A  64      94.516 -15.384  20.862  1.00 32.26           N  
ANISOU  491  ND2 ASN A  64     3929   3935   4395     -3    -27     58       N  
ATOM    492  N   GLY A  65      95.636 -12.146  17.582  1.00 45.17           N  
ANISOU  492  N   GLY A  65     5721   5721   5721      0      0      0       N  
ATOM    493  CA  GLY A  65      95.662 -10.748  17.966  1.00 30.01           C  
ANISOU  493  CA  GLY A  65     3800   3800   3800      0      0      0       C  
ATOM    494  C   GLY A  65      94.662 -10.348  19.032  1.00 35.89           C  
ANISOU  494  C   GLY A  65     4545   4545   4545      0      0      0       C  
ATOM    495  O   GLY A  65      94.875  -9.383  19.765  1.00 43.50           O  
ANISOU  495  O   GLY A  65     5510   5510   5510      0      0      0       O  
ATOM    496  N   GLY A  66      93.563 -11.085  19.134  1.00 41.89           N  
ANISOU  496  N   GLY A  66     5305   5305   5305      0      0      0       N  
ATOM    497  CA  GLY A  66      92.630 -10.838  20.212  1.00 58.10           C  
ANISOU  497  CA  GLY A  66     7323   7331   7421      2      5     46       C  
ATOM    498  C   GLY A  66      91.392 -10.091  19.765  1.00 42.29           C  
ANISOU  498  C   GLY A  66     5273   5334   5461      6     13     85       C  
ATOM    499  O   GLY A  66      90.422 -10.009  20.502  1.00 63.90           O  
ANISOU  499  O   GLY A  66     7980   8043   8255     14     26    176       O  
ATOM    500  N   ASN A  67      91.416  -9.528  18.566  0.50 23.55           N  
ANISOU  500  N   ASN A  67     2949   2957   3044      3      6     45       N  
ATOM    501  CA  ASN A  67      90.270  -8.745  18.134  0.50 17.57           C  
ANISOU  501  CA  ASN A  67     2161   2200   2316      8     13     97       C  
ATOM    502  C   ASN A  67      89.133  -9.638  17.686  0.50 52.01           C  
ANISOU  502  C   ASN A  67     6399   6474   6887      9     24    181       C  
ATOM    503  O   ASN A  67      87.963  -9.271  17.769  0.50 65.62           O  
ANISOU  503  O   ASN A  67     8049   8206   8676     17     42    269       O  
ATOM    504  CB  ASN A  67      90.655  -7.765  17.027  0.50 12.91           C  
ANISOU  504  CB  ASN A  67     1621   1654   1630      2      1     22       C  
ATOM    505  CG  ASN A  67      89.536  -6.802  16.691  0.50 52.89           C  
ANISOU  505  CG  ASN A  67     6638   6763   6693     13      9     88       C  
ATOM    506  OD1 ASN A  67      88.698  -6.495  17.536  0.50 59.69           O  
ANISOU  506  OD1 ASN A  67     7462   7612   7605     26     24    168       O  
ATOM    507  ND2 ASN A  67      89.508  -6.326  15.448  0.50 60.84           N  
ANISOU  507  ND2 ASN A  67     7660   7801   7655      7      0      3       N  
ATOM    508  N   THR A  68      89.491 -10.829  17.237  1.00 56.65           N  
ANISOU  508  N   THR A  68     6967   6994   7563      1      6    115       N  
ATOM    509  CA  THR A  68      88.508 -11.822  16.841  1.00 79.53           C  
ANISOU  509  CA  THR A  68     9749   9822  10646     -4    -12    146       C  
ATOM    510  C   THR A  68      89.023 -13.201  17.249  1.00 75.87           C  
ANISOU  510  C   THR A  68     9282   9290  10253     -4    -35    139       C  
ATOM    511  O   THR A  68      90.233 -13.455  17.238  1.00 55.68           O  
ANISOU  511  O   THR A  68     6814   6787   7555     -1    -36     53       O  
ATOM    512  CB  THR A  68      88.231 -11.809  15.315  1.00 83.48           C  
ANISOU  512  CB  THR A  68    10213  10343  11162     -5    -37     33       C  
ATOM    513  OG1 THR A  68      89.465 -11.932  14.600  1.00 61.77           O  
ANISOU  513  OG1 THR A  68     7564   7577   8329      7    -48   -113       O  
ATOM    514  CG2 THR A  68      87.534 -10.516  14.892  1.00 74.64           C  
ANISOU  514  CG2 THR A  68     9072   9333   9954     -2    -17     47       C  
ATOM    515  N   ALA A  69      88.096 -14.097  17.572  1.00 76.64           N  
ANISOU  515  N   ALA A  69     9276   9307  10536     -9    -52    231       N  
ATOM    516  CA  ALA A  69      88.402 -15.504  17.783  1.00 62.11           C  
ANISOU  516  CA  ALA A  69     7410   7415   8772    -12    -86    220       C  
ATOM    517  C   ALA A  69      88.525 -16.186  16.428  1.00 55.38           C  
ANISOU  517  C   ALA A  69     6535   6508   8000     -8   -137    108       C  
ATOM    518  O   ALA A  69      88.180 -15.581  15.404  1.00 43.26           O  
ANISOU  518  O   ALA A  69     4987   4968   6483     -4   -146     45       O  
ATOM    519  CB  ALA A  69      87.300 -16.162  18.623  1.00 76.55           C  
ANISOU  519  CB  ALA A  69     9130   9181  10774    -17    -90    364       C  
ATOM    520  N   PRO A  70      89.075 -17.416  16.400  1.00 31.03           N  
ANISOU  520  N   PRO A  70     3450   3394   4946     -4   -172     73       N  
ATOM    521  CA  PRO A  70      89.181 -18.102  15.109  1.00 37.14           C  
ANISOU  521  CA  PRO A  70     4203   4127   5782      9   -223    -30       C  
ATOM    522  C   PRO A  70      87.822 -18.257  14.406  1.00 54.54           C  
ANISOU  522  C   PRO A  70     6285   6225   8213      4   -275    -13       C  
ATOM    523  O   PRO A  70      86.819 -18.512  15.092  1.00 46.31           O  
ANISOU  523  O   PRO A  70     5150   5112   7332    -14   -283    115       O  
ATOM    524  CB  PRO A  70      89.769 -19.469  15.474  1.00 43.12           C  
ANISOU  524  CB  PRO A  70     4958   4852   6575     13   -254    -24       C  
ATOM    525  CG  PRO A  70      89.710 -19.547  16.983  1.00 39.95           C  
ANISOU  525  CG  PRO A  70     4552   4458   6169     -3   -225     91       C  
ATOM    526  CD  PRO A  70      89.734 -18.166  17.481  1.00 22.12           C  
ANISOU  526  CD  PRO A  70     2350   2281   3772     -6   -165    117       C  
ATOM    527  N   TYR A  71      87.810 -18.141  13.075  1.00 61.64           N  
ANISOU  527  N   TYR A  71     7183   7125   9114     22   -305   -131       N  
ATOM    528  CA  TYR A  71      86.607 -18.280  12.228  1.00 77.36           C  
ANISOU  528  CA  TYR A  71     9060   9040  11292     20   -362   -142       C  
ATOM    529  C   TYR A  71      85.648 -17.082  12.357  1.00 99.02           C  
ANISOU  529  C   TYR A  71    11760  11903  13962     -5   -312    -68       C  
ATOM    530  O   TYR A  71      84.550 -17.096  11.797  1.00100.95           O  
ANISOU  530  O   TYR A  71    11900  12162  14296    -17   -341    -49       O  
ATOM    531  CB  TYR A  71      85.869 -19.591  12.524  1.00 60.68           C  
ANISOU  531  CB  TYR A  71     6837   6818   9401      5   -426    -64       C  
ATOM    532  CG  TYR A  71      86.727 -20.808  12.254  1.00 57.55           C  
ANISOU  532  CG  TYR A  71     6471   6374   9022     27   -475   -134       C  
ATOM    533  CD1 TYR A  71      87.047 -21.699  13.274  1.00 58.16           C  
ANISOU  533  CD1 TYR A  71     6546   6429   9125     14   -477    -53       C  
ATOM    534  CD2 TYR A  71      87.285 -21.024  10.997  1.00 63.92           C  
ANISOU  534  CD2 TYR A  71     7314   7211   9763     59   -506   -274       C  
ATOM    535  CE1 TYR A  71      87.862 -22.801  13.038  1.00 69.95           C  
ANISOU  535  CE1 TYR A  71     8064   7912  10600     31   -514   -109       C  
ATOM    536  CE2 TYR A  71      88.100 -22.123  10.750  1.00 50.19           C  
ANISOU  536  CE2 TYR A  71     5602   5467   8000     77   -537   -318       C  
ATOM    537  CZ  TYR A  71      88.387 -23.005  11.777  1.00 65.54           C  
ANISOU  537  CZ  TYR A  71     7539   7376   9988     62   -543   -237       C  
ATOM    538  OH  TYR A  71      89.192 -24.098  11.546  1.00 59.57           O  
ANISOU  538  OH  TYR A  71     6805   6611   9219     80   -575   -277       O  
ATOM    539  N   GLY A  72      86.053 -16.067  13.120  1.00 93.60           N  
ANISOU  539  N   GLY A  72    11147  11298  13117    -10   -241    -23       N  
ATOM    540  CA  GLY A  72      85.272 -14.847  13.271  1.00 85.18           C  
ANISOU  540  CA  GLY A  72    10053  10344  11966    -21   -192     42       C  
ATOM    541  C   GLY A  72      84.368 -14.799  14.490  1.00 94.95           C  
ANISOU  541  C   GLY A  72    11223  11576  13278    -36   -155    209       C  
ATOM    542  O   GLY A  72      83.787 -13.762  14.809  1.00101.47           O  
ANISOU  542  O   GLY A  72    12037  12482  14035    -35   -105    275       O  
ATOM    543  N   ASN A  73      84.247 -15.929  15.171  0.50 77.85           N  
ANISOU  543  N   ASN A  73     9014   9307  11259    -44   -180    280       N  
ATOM    544  CA  ASN A  73      83.516 -16.009  16.426  0.50 67.60           C  
ANISOU  544  CA  ASN A  73     7660   7987  10038    -49   -141    444       C  
ATOM    545  C   ASN A  73      83.987 -15.020  17.481  0.50 79.14           C  
ANISOU  545  C   ASN A  73     9213   9511  11346    -32    -71    508       C  
ATOM    546  O   ASN A  73      85.107 -14.517  17.425  0.50 79.62           O  
ANISOU  546  O   ASN A  73     9388   9613  11249    -24    -61    428       O  
ATOM    547  CB  ASN A  73      83.656 -17.413  16.999  0.50 51.47           C  
ANISOU  547  CB  ASN A  73     5582   5826   8150    -53   -183    495       C  
ATOM    548  CG  ASN A  73      83.107 -18.467  16.077  0.50 67.50           C  
ANISOU  548  CG  ASN A  73     7515   7778  10355    -67   -262    447       C  
ATOM    549  OD1 ASN A  73      81.915 -18.765  16.104  0.50 82.68           O  
ANISOU  549  OD1 ASN A  73     9316   9677  12420    -82   -274    527       O  
ATOM    550  ND2 ASN A  73      83.971 -19.035  15.246  0.50 64.78           N  
ANISOU  550  ND2 ASN A  73     7220   7388  10004    -56   -319    316       N  
ATOM    551  N   LYS A  74      83.097 -14.693  18.407  0.50 70.19           N  
ANISOU  551  N   LYS A  74     8026   8385  10259    -22    -24    651       N  
ATOM    552  CA  LYS A  74      83.479 -13.925  19.576  0.50 54.47           C  
ANISOU  552  CA  LYS A  74     6113   6432   8153      6     33    730       C  
ATOM    553  C   LYS A  74      83.851 -14.981  20.600  0.50 46.93           C  
ANISOU  553  C   LYS A  74     5153   5428   7249     10     22    775       C  
ATOM    554  O   LYS A  74      84.756 -14.802  21.407  0.50 60.23           O  
ANISOU  554  O   LYS A  74     6929   7183   8774     20     39    731       O  
ATOM    555  CB  LYS A  74      82.333 -13.068  20.104  0.50 60.32           C  
ANISOU  555  CB  LYS A  74     6798   7212   8911     30     92    851       C  
ATOM    556  CG  LYS A  74      81.809 -11.995  19.181  0.50 68.95           C  
ANISOU  556  CG  LYS A  74     7880   8384   9934     28    106    802       C  
ATOM    557  CD  LYS A  74      80.473 -11.494  19.709  0.50 64.10           C  
ANISOU  557  CD  LYS A  74     7178   7780   9397     52    161    939       C  
ATOM    558  CE  LYS A  74      80.583 -11.174  21.200  0.50 49.54           C  
ANISOU  558  CE  LYS A  74     5375   5924   7522    100    214   1061       C  
ATOM    559  NZ  LYS A  74      79.303 -10.714  21.796  0.50 53.94           N  
ANISOU  559  NZ  LYS A  74     5847   6485   8162    135    276   1197       N  
ATOM    560  N   ARG A  75      83.136 -16.099  20.537  0.50 18.82           N  
ANISOU  560  N   ARG A  75     1483   1770   3898     -3    -11    840       N  
ATOM    561  CA  ARG A  75      83.375 -17.219  21.424  0.50 43.74           C  
ANISOU  561  CA  ARG A  75     4616   4899   7105     -6    -27    872       C  
ATOM    562  C   ARG A  75      83.487 -18.506  20.622  0.50 45.41           C  
ANISOU  562  C   ARG A  75     4777   5006   7470    -30   -106    820       C  
ATOM    563  O   ARG A  75      82.766 -18.712  19.648  0.50 57.38           O  
ANISOU  563  O   ARG A  75     6216   6454   9133    -44   -146    812       O  
ATOM    564  CB  ARG A  75      82.195 -17.343  22.397  0.50 48.57           C  
ANISOU  564  CB  ARG A  75     5122   5491   7842     10     16   1033       C  
ATOM    565  CG  ARG A  75      81.733 -16.019  23.007  0.50 40.18           C  
ANISOU  565  CG  ARG A  75     4081   4512   6673     43     93   1094       C  
ATOM    566  CD  ARG A  75      80.410 -16.150  23.754  0.50 52.89           C  
ANISOU  566  CD  ARG A  75     5568   6088   8440     65    139   1257       C  
ATOM    567  NE  ARG A  75      79.706 -14.868  23.826  0.50 44.85           N  
ANISOU  567  NE  ARG A  75     4547   5124   7369     97    203   1312       N  
ATOM    568  CZ  ARG A  75      79.034 -14.431  24.891  0.50 50.63           C  
ANISOU  568  CZ  ARG A  75     5241   5885   8110    138    273   1417       C  
ATOM    569  NH1 ARG A  75      78.920 -15.197  25.968  0.50 33.81           N  
ANISOU  569  NH1 ARG A  75     3061   3734   6051    150    291   1487       N  
ATOM    570  NH2 ARG A  75      78.431 -13.245  24.864  0.50 45.38           N  
ANISOU  570  NH2 ARG A  75     4580   5267   7395    171    328   1457       N  
ATOM    571  N   ALA A  76      84.393 -19.375  21.051  0.50 44.53           N  
ANISOU  571  N   ALA A  76     4708   4895   7314    -33   -132    773       N  
ATOM    572  CA  ALA A  76      84.634 -20.633  20.364  0.50 31.94           C  
ANISOU  572  CA  ALA A  76     3078   3210   5845    -47   -211    713       C  
ATOM    573  C   ALA A  76      85.036 -21.701  21.364  0.50 31.35           C  
ANISOU  573  C   ALA A  76     2993   3125   5793    -48   -223    756       C  
ATOM    574  O   ALA A  76      85.803 -21.431  22.291  0.50 43.23           O  
ANISOU  574  O   ALA A  76     4576   4712   7138    -37   -182    752       O  
ATOM    575  CB  ALA A  76      85.690 -20.474  19.286  0.50 33.30           C  
ANISOU  575  CB  ALA A  76     3347   3405   5900    -45   -240    549       C  
ATOM    576  N   ASP A  77      84.511 -22.906  21.161  0.50 22.45           N  
ANISOU  576  N   ASP A  77     1767   1892   4872    -61   -286    795       N  
ATOM    577  CA  ASP A  77      84.879 -24.087  21.929  1.00 42.72           C  
ANISOU  577  CA  ASP A  77     4311   4430   7491    -64   -314    831       C  
ATOM    578  C   ASP A  77      86.373 -24.314  21.762  1.00 55.12           C  
ANISOU  578  C   ASP A  77     6002   6053   8889    -58   -328    704       C  
ATOM    579  O   ASP A  77      86.964 -23.823  20.800  1.00 39.28           O  
ANISOU  579  O   ASP A  77     4071   4075   6781    -52   -333    586       O  
ATOM    580  CB  ASP A  77      84.107 -25.305  21.402  1.00 37.36           C  
ANISOU  580  CB  ASP A  77     3508   3618   7068    -80   -395    867       C  
ATOM    581  CG  ASP A  77      84.178 -26.494  22.342  0.50 66.19           C  
ANISOU  581  CG  ASP A  77     7106   7231  10814    -85   -419    945       C  
ATOM    582  OD1 ASP A  77      83.325 -26.564  23.253  0.50 88.21           O  
ANISOU  582  OD1 ASP A  77     9807  10007  13703    -87   -385   1085       O  
ATOM    583  OD2 ASP A  77      85.054 -27.369  22.171  0.50 49.94           O  
ANISOU  583  OD2 ASP A  77     5085   5153   8737    -86   -470    873       O  
ATOM    584  N   GLN A  78      86.993 -25.027  22.700  1.00 62.99           N  
ANISOU  584  N   GLN A  78     7014   7066   9852    -56   -328    731       N  
ATOM    585  CA  GLN A  78      88.412 -25.375  22.569  1.00 64.25           C  
ANISOU  585  CA  GLN A  78     7277   7268   9866    -48   -342    622       C  
ATOM    586  C   GLN A  78      88.662 -26.156  21.277  1.00 60.67           C  
ANISOU  586  C   GLN A  78     6814   6742   9494    -48   -415    527       C  
ATOM    587  O   GLN A  78      89.699 -25.987  20.635  1.00 71.80           O  
ANISOU  587  O   GLN A  78     8319   8199  10764    -34   -412    411       O  
ATOM    588  CB  GLN A  78      88.919 -26.186  23.764  1.00 60.07           C  
ANISOU  588  CB  GLN A  78     6744   6750   9329    -48   -343    678       C  
ATOM    589  CG  GLN A  78      89.165 -25.365  25.018  1.00 63.46           C  
ANISOU  589  CG  GLN A  78     7221   7278   9612    -37   -271    724       C  
ATOM    590  CD  GLN A  78      87.908 -25.160  25.845  1.00 74.91           C  
ANISOU  590  CD  GLN A  78     8568   8711  11183    -36   -239    865       C  
ATOM    591  OE1 GLN A  78      86.819 -24.940  25.305  1.00 66.21           O  
ANISOU  591  OE1 GLN A  78     7391   7558  10209    -42   -242    914       O  
ATOM    592  NE2 GLN A  78      88.051 -25.244  27.165  1.00 70.33           N  
ANISOU  592  NE2 GLN A  78     7979   8175  10570    -25   -206    936       N  
ATOM    593  N   ALA A  79      87.715 -27.025  20.929  1.00 36.63           N  
ANISOU  593  N   ALA A  79     3653   3585   6679    -59   -479    578       N  
ATOM    594  CA  ALA A  79      87.784 -27.879  19.736  1.00 61.98           C  
ANISOU  594  CA  ALA A  79     6836   6712  10002    -55   -561    491       C  
ATOM    595  C   ALA A  79      87.885 -27.046  18.462  1.00 40.26           C  
ANISOU  595  C   ALA A  79     4135   3986   7177    -41   -558    375       C  
ATOM    596  O   ALA A  79      88.492 -27.443  17.469  1.00 59.70           O  
ANISOU  596  O   ALA A  79     6632   6436   9616    -24   -599    262       O  
ATOM    597  CB  ALA A  79      86.566 -28.809  19.670  1.00 67.28           C  
ANISOU  597  CB  ALA A  79     7361   7255  10949    -71   -630    579       C  
ATOM    598  N   THR A  80      87.268 -25.882  18.510  1.00 58.93           N  
ANISOU  598  N   THR A  80     6498   6389   9505    -47   -506    409       N  
ATOM    599  CA  THR A  80      87.229 -24.963  17.387  1.00 67.08           C  
ANISOU  599  CA  THR A  80     7567   7447  10474    -36   -498    312       C  
ATOM    600  C   THR A  80      88.614 -24.315  17.231  1.00 55.78           C  
ANISOU  600  C   THR A  80     6278   6132   8783    -18   -446    208       C  
ATOM    601  O   THR A  80      89.166 -24.207  16.122  1.00 33.22           O  
ANISOU  601  O   THR A  80     3469   3296   5856      2   -460     89       O  
ATOM    602  CB  THR A  80      86.112 -23.921  17.545  1.00 58.15           C  
ANISOU  602  CB  THR A  80     6384   6318   9392    -49   -458    395       C  
ATOM    603  OG1 THR A  80      84.849 -24.584  17.637  1.00 63.93           O  
ANISOU  603  OG1 THR A  80     6977   6940  10372    -65   -504    498       O  
ATOM    604  CG2 THR A  80      86.109 -22.941  16.402  1.00 49.91           C  
ANISOU  604  CG2 THR A  80     5379   5303   8281    -38   -451    293       C  
ATOM    605  N   TRP A  81      89.170 -23.904  18.365  1.00 42.58           N  
ANISOU  605  N   TRP A  81     4669   4540   6970    -21   -384    258       N  
ATOM    606  CA  TRP A  81      90.543 -23.411  18.447  1.00 53.48           C  
ANISOU  606  CA  TRP A  81     6179   6029   8114     -7   -335    180       C  
ATOM    607  C   TRP A  81      91.518 -24.438  17.880  1.00 55.37           C  
ANISOU  607  C   TRP A  81     6450   6257   8333     10   -372    102       C  
ATOM    608  O   TRP A  81      92.380 -24.115  17.059  1.00 45.90           O  
ANISOU  608  O   TRP A  81     5328   5118   6995     29   -350      8       O  
ATOM    609  CB  TRP A  81      90.908 -23.099  19.898  1.00 47.09           C  
ANISOU  609  CB  TRP A  81     5410   5285   7198    -13   -282    252       C  
ATOM    610  CG  TRP A  81      90.292 -21.836  20.386  1.00 57.98           C  
ANISOU  610  CG  TRP A  81     6795   6713   8522    -18   -229    306       C  
ATOM    611  CD1 TRP A  81      89.059 -21.693  20.957  1.00 63.83           C  
ANISOU  611  CD1 TRP A  81     7444   7415   9393    -28   -222    422       C  
ATOM    612  CD2 TRP A  81      90.883 -20.534  20.375  1.00 63.42           C  
ANISOU  612  CD2 TRP A  81     7583   7502   9010    -11   -174    253       C  
ATOM    613  NE1 TRP A  81      88.834 -20.378  21.280  1.00 67.17           N  
ANISOU  613  NE1 TRP A  81     7906   7910   9707    -23   -165    443       N  
ATOM    614  CE2 TRP A  81      89.941 -19.644  20.938  1.00 66.19           C  
ANISOU  614  CE2 TRP A  81     7899   7867   9382    -15   -141    336       C  
ATOM    615  CE3 TRP A  81      92.114 -20.030  19.939  1.00 52.70           C  
ANISOU  615  CE3 TRP A  81     6222   6327   7474    -18   -161    139       C  
ATOM    616  CZ2 TRP A  81      90.192 -18.278  21.076  1.00 57.56           C  
ANISOU  616  CZ2 TRP A  81     6883   6862   8126     -9    -94    310       C  
ATOM    617  CZ3 TRP A  81      92.363 -18.673  20.070  1.00 53.06           C  
ANISOU  617  CZ3 TRP A  81     6283   6288   7591    -18   -144    168       C  
ATOM    618  CH2 TRP A  81      91.405 -17.811  20.638  1.00 53.20           C  
ANISOU  618  CH2 TRP A  81     6344   6465   7403    -16    -85    186       C  
ATOM    619  N   LEU A  82      91.354 -25.688  18.298  1.00 48.56           N  
ANISOU  619  N   LEU A  82     5521   5316   7613      4   -425    151       N  
ATOM    620  CA  LEU A  82      92.266 -26.741  17.886  1.00 38.48           C  
ANISOU  620  CA  LEU A  82     4268   4023   6328     21   -462     92       C  
ATOM    621  C   LEU A  82      92.101 -27.059  16.416  1.00 36.76           C  
ANISOU  621  C   LEU A  82     4025   3759   6184     39   -515      2       C  
ATOM    622  O   LEU A  82      93.066 -27.380  15.753  1.00 39.70           O  
ANISOU  622  O   LEU A  82     4453   4164   6465     63   -513    -74       O  
ATOM    623  CB  LEU A  82      92.084 -27.999  18.734  1.00 39.17           C  
ANISOU  623  CB  LEU A  82     4287   4036   6560      8   -512    172       C  
ATOM    624  CG  LEU A  82      92.495 -27.858  20.192  1.00 48.82           C  
ANISOU  624  CG  LEU A  82     5542   5316   7692     -2   -463    247       C  
ATOM    625  CD1 LEU A  82      92.151 -29.109  20.989  1.00 39.94           C  
ANISOU  625  CD1 LEU A  82     4332   4112   6733    -15   -517    337       C  
ATOM    626  CD2 LEU A  82      93.971 -27.586  20.232  1.00 27.31           C  
ANISOU  626  CD2 LEU A  82     2928   2666   4781    -36   -418    169       C  
ATOM    627  N   LYS A  83      90.887 -26.927  15.895  1.00 41.71           N  
ANISOU  627  N   LYS A  83     4566   4311   6970     31   -556     13       N  
ATOM    628  CA  LYS A  83      90.668 -27.114  14.465  1.00 48.36           C  
ANISOU  628  CA  LYS A  83     5383   5114   7878     52   -608    -83       C  
ATOM    629  C   LYS A  83      91.385 -26.049  13.667  1.00 52.05           C  
ANISOU  629  C   LYS A  83     5948   5692   8136     73   -546   -173       C  
ATOM    630  O   LYS A  83      92.020 -26.341  12.651  1.00 34.67           O  
ANISOU  630  O   LYS A  83     3780   3513   5881    101   -558   -258       O  
ATOM    631  CB  LYS A  83      89.187 -27.092  14.101  1.00 49.59           C  
ANISOU  631  CB  LYS A  83     5422   5169   8250     37   -664    -51       C  
ATOM    632  CG  LYS A  83      88.963 -27.242  12.596  1.00 57.63           C  
ANISOU  632  CG  LYS A  83     6414   6149   9331     63   -723   -165       C  
ATOM    633  CD  LYS A  83      87.514 -27.519  12.247  1.00 86.03           C  
ANISOU  633  CD  LYS A  83     9881   9624  13183     49   -799   -132       C  
ATOM    634  CE  LYS A  83      87.069 -26.567  11.123  1.00 89.89           C  
ANISOU  634  CE  LYS A  83    10369  10134  13650     64   -798   -220       C  
ATOM    635  NZ  LYS A  83      85.644 -26.749  10.757  1.00 95.51           N  
ANISOU  635  NZ  LYS A  83    10950  10726  14614     50   -871   -188       N  
ATOM    636  N   TYR A  84      91.275 -24.803  14.130  1.00 48.29           N  
ANISOU  636  N   TYR A  84     5516   5288   7543     60   -476   -144       N  
ATOM    637  CA  TYR A  84      91.962 -23.713  13.449  1.00 48.00           C  
ANISOU  637  CA  TYR A  84     5574   5364   7299     76   -410   -213       C  
ATOM    638  C   TYR A  84      93.470 -23.933  13.464  1.00 39.44           C  
ANISOU  638  C   TYR A  84     4329   4247   6408     77   -531   -318       C  
ATOM    639  O   TYR A  84      94.137 -23.844  12.413  1.00 32.38           O  
ANISOU  639  O   TYR A  84     3680   3487   5136     84   -395   -331       O  
ATOM    640  CB  TYR A  84      91.623 -22.369  14.118  1.00 52.76           C  
ANISOU  640  CB  TYR A  84     6207   6026   7812     57   -348   -168       C  
ATOM    641  CG  TYR A  84      92.105 -21.179  13.326  1.00 51.96           C  
ANISOU  641  CG  TYR A  84     6189   6027   7527     49   -294   -234       C  
ATOM    642  CD1 TYR A  84      91.290 -20.576  12.374  1.00 54.88           C  
ANISOU  642  CD1 TYR A  84     6519   6386   7949     74   -309   -276       C  
ATOM    643  CD2 TYR A  84      93.367 -20.634  13.550  1.00 48.17           C  
ANISOU  643  CD2 TYR A  84     5648   5751   6901     49   -280   -231       C  
ATOM    644  CE1 TYR A  84      91.730 -19.484  11.644  1.00 58.69           C  
ANISOU  644  CE1 TYR A  84     6880   6900   8518     86   -361   -406       C  
ATOM    645  CE2 TYR A  84      93.812 -19.537  12.828  1.00 38.16           C  
ANISOU  645  CE2 TYR A  84     4431   4555   5513     58   -243   -271       C  
ATOM    646  CZ  TYR A  84      92.990 -18.970  11.878  1.00 40.55           C  
ANISOU  646  CZ  TYR A  84     4657   4709   6040     88   -310   -414       C  
ATOM    647  OH  TYR A  84      93.424 -17.894  11.154  1.00 47.14           O  
ANISOU  647  OH  TYR A  84     5594   5766   6550     72   -217   -332       O  
ATOM    648  N   ALA A  85      93.983 -24.313  14.632  1.00 25.78           N  
ANISOU  648  N   ALA A  85     2692   2769   4334     43   -413   -182       N  
ATOM    649  CA  ALA A  85      95.413 -24.563  14.784  1.00 36.24           C  
ANISOU  649  CA  ALA A  85     4060   4133   5577     52   -405   -206       C  
ATOM    650  C   ALA A  85      95.844 -25.694  13.857  1.00 42.43           C  
ANISOU  650  C   ALA A  85     4954   4724   6445     76   -431   -284       C  
ATOM    651  O   ALA A  85      96.888 -25.596  13.214  1.00 33.21           O  
ANISOU  651  O   ALA A  85     3667   3754   5195     87   -466   -310       O  
ATOM    652  CB  ALA A  85      95.771 -24.867  16.236  1.00 17.17           C  
ANISOU  652  CB  ALA A  85     1789   1575   3158     37   -355   -152       C  
ATOM    653  N   ASP A  86      95.026 -26.751  13.775  1.00 42.03           N  
ANISOU  653  N   ASP A  86     4680   4751   6539     66   -537   -246       N  
ATOM    654  CA  ASP A  86      95.310 -27.881  12.885  1.00 44.15           C  
ANISOU  654  CA  ASP A  86     4904   4975   6894     84   -610   -299       C  
ATOM    655  C   ASP A  86      95.370 -27.406  11.442  1.00 47.17           C  
ANISOU  655  C   ASP A  86     5295   5388   7239    110   -616   -379       C  
ATOM    656  O   ASP A  86      96.271 -27.782  10.703  1.00 36.63           O  
ANISOU  656  O   ASP A  86     3967   4071   5881    132   -640   -433       O  
ATOM    657  CB  ASP A  86      94.261 -28.996  13.001  1.00 52.25           C  
ANISOU  657  CB  ASP A  86     6052   5691   8110     81   -622   -289       C  
ATOM    658  CG  ASP A  86      94.485 -29.919  14.190  1.00 54.85           C  
ANISOU  658  CG  ASP A  86     6364   5976   8501     60   -641   -216       C  
ATOM    659  OD1 ASP A  86      95.483 -29.760  14.923  1.00 50.88           O  
ANISOU  659  OD1 ASP A  86     5897   5529   7904     56   -608   -199       O  
ATOM    660  OD2 ASP A  86      93.681 -30.864  14.346  1.00 61.51           O  
ANISOU  660  OD2 ASP A  86     7107   6729   9534    107   -714   -162       O  
ATOM    661  N   GLU A  87      94.418 -26.574  11.043  1.00 32.43           N  
ANISOU  661  N   GLU A  87     3606   3340   5376    118   -542   -418       N  
ATOM    662  CA  GLU A  87      94.359 -26.104   9.664  1.00 41.96           C  
ANISOU  662  CA  GLU A  87     4544   4476   6923    180   -750   -622       C  
ATOM    663  C   GLU A  87      95.652 -25.360   9.297  1.00 48.34           C  
ANISOU  663  C   GLU A  87     5670   5493   7204    159   -502   -532       C  
ATOM    664  O   GLU A  87      96.285 -25.639   8.272  1.00 40.94           O  
ANISOU  664  O   GLU A  87     4730   4571   6256    185   -526   -596       O  
ATOM    665  CB  GLU A  87      93.156 -25.187   9.462  1.00 41.45           C  
ANISOU  665  CB  GLU A  87     4563   4703   6486    124   -579   -447       C  
ATOM    666  CG  GLU A  87      91.821 -25.873   9.299  1.00 66.82           C  
ANISOU  666  CG  GLU A  87     7845   7610   9934    167   -608   -478       C  
ATOM    667  CD  GLU A  87      90.815 -24.981   8.602  1.00 87.82           C  
ANISOU  667  CD  GLU A  87    10464  10263  12642    168   -620   -519       C  
ATOM    668  OE1 GLU A  87      90.677 -25.069   7.363  1.00 97.46           O  
ANISOU  668  OE1 GLU A  87    11664  11478  13888    196   -658   -603       O  
ATOM    669  OE2 GLU A  87      90.158 -24.179   9.309  1.00 82.60           O  
ANISOU  669  OE2 GLU A  87     9788   9603  11994    140   -592   -465       O  
ATOM    670  N   MET A  88      96.050 -24.420  10.152  1.00 33.67           N  
ANISOU  670  N   MET A  88     3853   3707   5231    141   -437   -484       N  
ATOM    671  CA  MET A  88      97.289 -23.680   9.904  1.00 34.73           C  
ANISOU  671  CA  MET A  88     3897   4071   5227    136   -435   -457       C  
ATOM    672  C   MET A  88      98.520 -24.582   9.928  1.00 33.48           C  
ANISOU  672  C   MET A  88     3740   3909   5073    147   -461   -470       C  
ATOM    673  O   MET A  88      99.416 -24.461   9.081  1.00 28.27           O  
ANISOU  673  O   MET A  88     3091   3287   4363    164   -462   -507       O  
ATOM    674  CB  MET A  88      97.444 -22.531  10.920  1.00 33.58           C  
ANISOU  674  CB  MET A  88     3814   3978   4969    114   -358   -401       C  
ATOM    675  CG  MET A  88      96.418 -21.457  10.645  1.00 27.55           C  
ANISOU  675  CG  MET A  88     3167   3124   4175    118   -296   -435       C  
ATOM    676  SD  MET A  88      96.651 -20.751   9.002  1.00 34.63           S  
ANISOU  676  SD  MET A  88     3955   4182   5023    130   -331   -458       S  
ATOM    677  CE  MET A  88      95.308 -19.571   8.951  1.00 27.62           C  
ANISOU  677  CE  MET A  88     3181   3207   4108    130   -267   -487       C  
ATOM    678  N   TYR A  89      98.551 -25.504  10.885  1.00 36.86           N  
ANISOU  678  N   TYR A  89     4085   4080   5842    185   -604   -595       N  
ATOM    679  CA  TYR A  89      99.661 -26.455  11.012  1.00 38.99           C  
ANISOU  679  CA  TYR A  89     4559   4399   5854    157   -467   -486       C  
ATOM    680  C   TYR A  89      99.839 -27.270   9.738  1.00 26.07           C  
ANISOU  680  C   TYR A  89     2738   2883   4285    172   -584   -513       C  
ATOM    681  O   TYR A  89     100.961 -27.478   9.278  1.00 37.61           O  
ANISOU  681  O   TYR A  89     4366   4213   5710    205   -531   -590       O  
ATOM    682  CB  TYR A  89      99.442 -27.373  12.217  1.00 33.48           C  
ANISOU  682  CB  TYR A  89     3698   3791   5232    126   -543   -396       C  
ATOM    683  CG  TYR A  89     100.433 -28.526  12.317  1.00 46.00           C  
ANISOU  683  CG  TYR A  89     5425   5186   6866    147   -535   -444       C  
ATOM    684  CD1 TYR A  89     101.582 -28.397  13.095  1.00 47.48           C  
ANISOU  684  CD1 TYR A  89     5504   5576   6961    128   -552   -382       C  
ATOM    685  CD2 TYR A  89     100.203 -29.751  11.689  1.00 57.42           C  
ANISOU  685  CD2 TYR A  89     6582   6446   8788    203   -837   -602       C  
ATOM    686  CE1 TYR A  89     102.483 -29.426  13.219  1.00 60.82           C  
ANISOU  686  CE1 TYR A  89     7182   7242   8687    136   -595   -391       C  
ATOM    687  CE2 TYR A  89     101.109 -30.806  11.812  1.00 30.31           C  
ANISOU  687  CE2 TYR A  89     3212   3273   5033    156   -718   -451       C  
ATOM    688  CZ  TYR A  89     102.247 -30.632  12.578  1.00 58.87           C  
ANISOU  688  CZ  TYR A  89     7044   6750   8575    164   -616   -465       C  
ATOM    689  OH  TYR A  89     103.166 -31.657  12.712  1.00 56.80           O  
ANISOU  689  OH  TYR A  89     6777   6456   8350    172   -657   -475       O  
ATOM    690  N   LEU A  90      98.739 -27.767   9.196  1.00 38.27           N  
ANISOU  690  N   LEU A  90     4152   4113   6278    242   -792   -731       N  
ATOM    691  CA  LEU A  90      98.806 -28.589   7.994  1.00 50.68           C  
ANISOU  691  CA  LEU A  90     5940   5722   7595    224   -640   -657       C  
ATOM    692  C   LEU A  90      99.178 -27.740   6.790  1.00 35.97           C  
ANISOU  692  C   LEU A  90     3911   4115   5640    228   -686   -654       C  
ATOM    693  O   LEU A  90      99.958 -28.170   5.939  1.00 26.17           O  
ANISOU  693  O   LEU A  90     2660   2884   4399    253   -719   -702       O  
ATOM    694  CB  LEU A  90      97.496 -29.344   7.743  1.00 38.79           C  
ANISOU  694  CB  LEU A  90     4180   4326   6231    205   -776   -611       C  
ATOM    695  CG  LEU A  90      97.080 -30.386   8.779  1.00 52.34           C  
ANISOU  695  CG  LEU A  90     6074   5739   8074    201   -741   -608       C  
ATOM    696  CD1 LEU A  90      95.651 -30.890   8.529  1.00 57.29           C  
ANISOU  696  CD1 LEU A  90     6417   6518   8834    178   -872   -552       C  
ATOM    697  CD2 LEU A  90      98.057 -31.551   8.820  1.00 37.59           C  
ANISOU  697  CD2 LEU A  90     3977   4071   6234    195   -868   -573       C  
ATOM    698  N   ALA A  91      98.685 -26.503   6.747  1.00 36.48           N  
ANISOU  698  N   ALA A  91     4004   4226   5630    218   -629   -639       N  
ATOM    699  CA  ALA A  91      99.069 -25.601   5.661  1.00 33.18           C  
ANISOU  699  CA  ALA A  91     3532   3671   5406    321   -743   -921       C  
ATOM    700  C   ALA A  91     100.591 -25.348   5.681  1.00 32.48           C  
ANISOU  700  C   ALA A  91     3711   3694   4936    261   -504   -727       C  
ATOM    701  O   ALA A  91     101.230 -25.285   4.626  1.00 34.50           O  
ANISOU  701  O   ALA A  91     3740   3956   5414    357   -716   -965       O  
ATOM    702  CB  ALA A  91      98.299 -24.292   5.775  1.00 36.18           C  
ANISOU  702  CB  ALA A  91     4013   4293   5441    220   -545   -650       C  
ATOM    703  N   ALA A  92     101.165 -25.172   6.870  1.00 42.70           N  
ANISOU  703  N   ALA A  92     4893   5148   6183    216   -524   -609       N  
ATOM    704  CA  ALA A  92     102.620 -24.988   7.016  1.00 51.45           C  
ANISOU  704  CA  ALA A  92     6170   6174   7206    236   -436   -647       C  
ATOM    705  C   ALA A  92     103.410 -26.266   6.710  1.00 47.12           C  
ANISOU  705  C   ALA A  92     5602   5577   6723    259   -492   -687       C  
ATOM    706  O   ALA A  92     104.476 -26.253   6.102  1.00 34.44           O  
ANISOU  706  O   ALA A  92     3863   4140   5083    252   -556   -650       O  
ATOM    707  CB  ALA A  92     102.964 -24.485   8.414  1.00 28.31           C  
ANISOU  707  CB  ALA A  92     3274   3276   4208    205   -384   -572       C  
ATOM    708  N   MET A  93     102.826 -27.407   7.011  1.00 40.25           N  
ANISOU  708  N   MET A  93     4551   4777   5966    239   -614   -641       N  
ATOM    709  CA  MET A  93     103.568 -28.623   6.755  1.00 38.37           C  
ANISOU  709  CA  MET A  93     4450   4337   5793    281   -603   -734       C  
ATOM    710  C   MET A  93     103.499 -29.020   5.322  1.00 27.21           C  
ANISOU  710  C   MET A  93     3008   2902   4427    317   -652   -812       C  
ATOM    711  O   MET A  93     104.434 -29.646   4.841  1.00 50.72           O  
ANISOU  711  O   MET A  93     5729   5826   7717    423   -945  -1059       O  
ATOM    712  CB  MET A  93     103.048 -29.778   7.626  1.00 29.06           C  
ANISOU  712  CB  MET A  93     3249   3066   4727    269   -651   -711       C  
ATOM    713  CG  MET A  93     103.390 -29.837   9.080  1.00 29.91           C  
ANISOU  713  CG  MET A  93     3379   3178   4809    240   -623   -641       C  
ATOM    714  SD  MET A  93     105.164 -29.962   9.224  1.00 49.48           S  
ANISOU  714  SD  MET A  93     5727   5869   7202    228   -674   -588       S  
ATOM    715  CE  MET A  93     105.330 -31.718   8.907  1.00 56.02           C  
ANISOU  715  CE  MET A  93     6498   6619   8168    247   -779   -628       C  
ATOM    716  N   ASP A  94     102.642 -28.346   4.574  1.00 28.63           N  
ANISOU  716  N   ASP A  94     3179   3100   4600    323   -645   -837       N  
ATOM    717  CA  ASP A  94     102.548 -28.598   3.155  1.00 45.00           C  
ANISOU  717  CA  ASP A  94     5038   5350   6709    329   -776   -838       C  
ATOM    718  C   ASP A  94     103.647 -27.957   2.357  1.00 46.67           C  
ANISOU  718  C   ASP A  94     5455   5452   6825    376   -659   -934       C  
ATOM    719  O   ASP A  94     103.677 -26.748   2.188  1.00 60.84           O  
ANISOU  719  O   ASP A  94     7270   7318   8528    366   -604   -910       O  
ATOM    720  CB  ASP A  94     101.197 -28.033   2.673  1.00 48.04           C  
ANISOU  720  CB  ASP A  94     5322   5500   7432    448   -955  -1163       C  
ATOM    721  CG  ASP A  94     100.917 -28.305   1.207  1.00 50.98           C  
ANISOU  721  CG  ASP A  94     5938   5898   7534    397   -738  -1014       C  
ATOM    722  OD1 ASP A  94     101.808 -28.824   0.522  1.00 44.11           O  
ANISOU  722  OD1 ASP A  94     4766   4996   6997    531  -1067  -1323       O  
ATOM    723  OD2 ASP A  94      99.809 -27.968   0.730  1.00 54.53           O  
ANISOU  723  OD2 ASP A  94     6161   6540   8019    368   -845   -950       O  
ATOM    724  N   SER A  95     104.520 -28.805   1.810  1.00 42.58           N  
ANISOU  724  N   SER A  95     4925   4914   6339    403   -702   -978       N  
ATOM    725  CA  SER A  95     105.665 -28.314   1.059  1.00 37.52           C  
ANISOU  725  CA  SER A  95     4297   4338   5620    420   -680   -995       C  
ATOM    726  C   SER A  95     105.315 -28.018  -0.404  1.00 38.27           C  
ANISOU  726  C   SER A  95     4182   4633   5725    415   -804   -973       C  
ATOM    727  O   SER A  95     106.180 -27.636  -1.188  1.00 41.56           O  
ANISOU  727  O   SER A  95     4606   5094   6089    431   -795   -992       O  
ATOM    728  CB  SER A  95     106.856 -29.280   1.161  1.00 32.24           C  
ANISOU  728  CB  SER A  95     3627   3646   4976    434   -711  -1010       C  
ATOM    729  OG  SER A  95     106.555 -30.544   0.587  1.00 75.55           O  
ANISOU  729  OG  SER A  95     8876   9256  10573    425   -899   -986       O  
ATOM    730  N   THR A  96     104.068 -28.267  -0.790  1.00 29.66           N  
ANISOU  730  N   THR A  96     2972   3306   4990    577  -1031  -1372       N  
ATOM    731  CA  THR A  96     103.585 -27.862  -2.099  1.00 45.74           C  
ANISOU  731  CA  THR A  96     4981   5373   7025    613  -1056  -1447       C  
ATOM    732  C   THR A  96     103.626 -26.329  -2.034  1.00 78.48           C  
ANISOU  732  C   THR A  96     9257   9784  10776    429   -782  -1015       C  
ATOM    733  O   THR A  96     103.462 -25.771  -0.941  1.00100.55           O  
ANISOU  733  O   THR A  96    12088  12585  13531    395   -726   -951       O  
ATOM    734  CB  THR A  96     102.167 -28.374  -2.405  1.00 48.57           C  
ANISOU  734  CB  THR A  96     5379   5873   7201    459   -921  -1100       C  
ATOM    735  OG1 THR A  96     102.114 -29.799  -2.269  1.00 58.47           O  
ANISOU  735  OG1 THR A  96     6828   6825   8564    513   -877  -1231       O  
ATOM    736  CG2 THR A  96     101.706 -27.942  -3.789  1.00 47.83           C  
ANISOU  736  CG2 THR A  96     5485   5594   7092    533   -824  -1265       C  
ATOM    737  N   LEU A  97     103.887 -25.652  -3.148  1.00 78.93           N  
ANISOU  737  N   LEU A  97     9313   9892  10786    449   -777  -1044       N  
ATOM    738  CA  LEU A  97     103.870 -24.177  -3.203  1.00 70.84           C  
ANISOU  738  CA  LEU A  97     8324   8927   9664    430   -707  -1001       C  
ATOM    739  C   LEU A  97     105.112 -23.507  -2.635  1.00 57.88           C  
ANISOU  739  C   LEU A  97     6892   7182   7919    445   -549  -1026       C  
ATOM    740  O   LEU A  97     105.761 -22.734  -3.347  1.00 60.72           O  
ANISOU  740  O   LEU A  97     7101   7731   8239    415   -625   -939       O  
ATOM    741  CB  LEU A  97     102.604 -23.586  -2.555  1.00 59.11           C  
ANISOU  741  CB  LEU A  97     6848   7432   8179    405   -675   -968       C  
ATOM    742  CG  LEU A  97     101.253 -24.139  -3.011  1.00 58.77           C  
ANISOU  742  CG  LEU A  97     6758   7346   8226    422   -732  -1021       C  
ATOM    743  CD1 LEU A  97     100.135 -23.295  -2.434  1.00 58.84           C  
ANISOU  743  CD1 LEU A  97     6695   7224   8437    540   -837  -1341       C  
ATOM    744  CD2 LEU A  97     101.179 -24.195  -4.523  1.00 40.93           C  
ANISOU  744  CD2 LEU A  97     4659   4931   5963    504   -669  -1194       C  
ATOM    745  N   ASP A  98     105.467 -23.807  -1.380  1.00 49.00           N  
ANISOU  745  N   ASP A  98     5557   6079   6983    522   -751  -1215       N  
ATOM    746  CA  ASP A  98     106.602 -23.101  -0.780  1.00 53.44           C  
ANISOU  746  CA  ASP A  98     6237   6773   7293    360   -562   -830       C  
ATOM    747  C   ASP A  98     107.881 -23.930  -0.695  1.00 57.11           C  
ANISOU  747  C   ASP A  98     6634   7144   7923    506   -706  -1147       C  
ATOM    748  O   ASP A  98     108.966 -23.387  -0.492  1.00 46.71           O  
ANISOU  748  O   ASP A  98     5349   5870   6529    489   -658  -1096       O  
ATOM    749  CB  ASP A  98     106.245 -22.527   0.608  1.00 54.69           C  
ANISOU  749  CB  ASP A  98     6436   6929   7415    320   -504   -757       C  
ATOM    750  CG  ASP A  98     106.161 -23.592   1.700  1.00 56.94           C  
ANISOU  750  CG  ASP A  98     6851   7046   7738    340   -448   -815       C  
ATOM    751  OD1 ASP A  98     105.761 -24.741   1.447  1.00 43.03           O  
ANISOU  751  OD1 ASP A  98     4849   5243   6258    453   -712  -1085       O  
ATOM    752  OD2 ASP A  98     106.518 -23.266   2.844  1.00 51.91           O  
ANISOU  752  OD2 ASP A  98     6059   6449   7215    387   -576   -936       O  
ATOM    753  N   GLY A  99     107.767 -25.242  -0.840  1.00 43.57           N  
ANISOU  753  N   GLY A  99     4951   5467   6136    393   -650   -890       N  
ATOM    754  CA  GLY A  99     108.951 -26.045  -1.052  1.00 27.86           C  
ANISOU  754  CA  GLY A  99     2952   3469   4162    412   -683   -915       C  
ATOM    755  C   GLY A  99     109.611 -26.552   0.205  1.00 40.02           C  
ANISOU  755  C   GLY A  99     4516   4987   5702    391   -668   -871       C  
ATOM    756  O   GLY A  99     110.744 -26.998   0.141  1.00 41.08           O  
ANISOU  756  O   GLY A  99     4807   4977   5823    438   -586   -960       O  
ATOM    757  N   ILE A 100     108.967 -26.401   1.355  1.00 30.92           N  
ANISOU  757  N   ILE A 100     3318   3695   4733    494   -773  -1122       N  
ATOM    758  CA  ILE A 100     109.587 -26.883   2.573  1.00 19.96           C  
ANISOU  758  CA  ILE A 100     1956   2282   3345    469   -758  -1067       C  
ATOM    759  C   ILE A 100     108.549 -27.244   3.634  1.00 34.66           C  
ANISOU  759  C   ILE A 100     4024   4089   5057    354   -544   -824       C  
ATOM    760  O   ILE A 100     107.384 -26.848   3.549  1.00 33.01           O  
ANISOU  760  O   ILE A 100     3598   3872   5071    434   -754  -1029       O  
ATOM    761  CB  ILE A 100     110.568 -25.818   3.126  1.00 46.65           C  
ANISOU  761  CB  ILE A 100     5390   5736   6599    436   -668   -983       C  
ATOM    762  CG1 ILE A 100     111.588 -26.436   4.087  1.00 42.45           C  
ANISOU  762  CG1 ILE A 100     5058   5170   5902    340   -473   -758       C  
ATOM    763  CG2 ILE A 100     109.826 -24.606   3.730  1.00 26.01           C  
ANISOU  763  CG2 ILE A 100     2983   3139   3761    315   -417   -725       C  
ATOM    764  CD1 ILE A 100     112.737 -25.498   4.430  1.00 46.51           C  
ANISOU  764  CD1 ILE A 100     5600   5741   6332    320   -419   -704       C  
ATOM    765  N   ALA A 101     108.945 -28.050   4.613  1.00 44.82           N  
ANISOU  765  N   ALA A 101     5169   5481   6378    316   -637   -734       N  
ATOM    766  CA  ALA A 101     107.997 -28.418   5.653  1.00 35.32           C  
ANISOU  766  CA  ALA A 101     4112   4090   5219    323   -564   -769       C  
ATOM    767  C   ALA A 101     108.533 -28.018   7.013  1.00 33.18           C  
ANISOU  767  C   ALA A 101     3738   3982   4886    267   -582   -638       C  
ATOM    768  O   ALA A 101     108.901 -28.854   7.830  1.00 35.56           O  
ANISOU  768  O   ALA A 101     4176   4113   5224    286   -535   -680       O  
ATOM    769  CB  ALA A 101     107.666 -29.925   5.594  1.00 47.34           C  
ANISOU  769  CB  ALA A 101     5602   5519   6865    340   -644   -811       C  
ATOM    770  N   ILE A 102     108.450 -26.731   7.299  1.00 47.74           N  
ANISOU  770  N   ILE A 102     5621   5875   6644    246   -511   -594       N  
ATOM    771  CA  ILE A 102     108.848 -26.230   8.598  1.00 28.91           C  
ANISOU  771  CA  ILE A 102     3389   3403   4194    238   -399   -578       C  
ATOM    772  C   ILE A 102     107.560 -25.870   9.257  1.00 36.90           C  
ANISOU  772  C   ILE A 102     4402   4404   5212    217   -382   -548       C  
ATOM    773  O   ILE A 102     106.787 -25.091   8.697  1.00 28.43           O  
ANISOU  773  O   ILE A 102     3328   3354   4121    216   -366   -554       O  
ATOM    774  CB  ILE A 102     109.776 -25.002   8.530  1.00 42.91           C  
ANISOU  774  CB  ILE A 102     5189   5249   5865    224   -340   -539       C  
ATOM    775  CG1 ILE A 102     111.096 -25.354   7.850  1.00 30.92           C  
ANISOU  775  CG1 ILE A 102     3569   3830   4349    224   -412   -521       C  
ATOM    776  CG2 ILE A 102     110.049 -24.470   9.942  1.00 26.37           C  
ANISOU  776  CG2 ILE A 102     3127   3181   3712    192   -290   -465       C  
ATOM    777  CD1 ILE A 102     112.028 -24.176   7.712  1.00 32.96           C  
ANISOU  777  CD1 ILE A 102     3948   4057   4520    231   -308   -529       C  
ATOM    778  N   PRO A 103     107.272 -26.515  10.392  1.00 34.07           N  
ANISOU  778  N   PRO A 103     3938   4114   4895    187   -443   -476       N  
ATOM    779  CA  PRO A 103     106.045 -26.283  11.152  1.00 46.94           C  
ANISOU  779  CA  PRO A 103     5675   5618   6541    183   -381   -486       C  
ATOM    780  C   PRO A 103     105.981 -24.811  11.618  1.00 36.26           C  
ANISOU  780  C   PRO A 103     4266   4428   5081    147   -348   -398       C  
ATOM    781  O   PRO A 103     107.016 -24.258  11.974  1.00 27.60           O  
ANISOU  781  O   PRO A 103     3208   3370   3909    137   -305   -367       O  
ATOM    782  CB  PRO A 103     106.203 -27.199  12.370  1.00 29.50           C  
ANISOU  782  CB  PRO A 103     3466   3364   4379    171   -401   -455       C  
ATOM    783  CG  PRO A 103     107.209 -28.222  11.971  1.00 31.93           C  
ANISOU  783  CG  PRO A 103     3645   3763   4725    176   -499   -450       C  
ATOM    784  CD  PRO A 103     108.154 -27.477  11.072  1.00 34.05           C  
ANISOU  784  CD  PRO A 103     3934   4085   4917    188   -469   -469       C  
ATOM    785  N   THR A 104     104.820 -24.176  11.527  1.00 28.86           N  
ANISOU  785  N   THR A 104     3286   3389   4292    190   -409   -534       N  
ATOM    786  CA  THR A 104     104.608 -22.832  12.056  1.00 28.18           C  
ANISOU  786  CA  THR A 104     3287   3452   3967    118   -264   -343       C  
ATOM    787  C   THR A 104     104.220 -22.945  13.534  1.00 38.44           C  
ANISOU  787  C   THR A 104     4676   4670   5260    107   -217   -325       C  
ATOM    788  O   THR A 104     104.031 -24.045  14.049  1.00 38.58           O  
ANISOU  788  O   THR A 104     4595   4707   5357    101   -285   -303       O  
ATOM    789  CB  THR A 104     103.504 -22.103  11.272  1.00 35.45           C  
ANISOU  789  CB  THR A 104     4274   4311   4885    131   -230   -393       C  
ATOM    790  OG1 THR A 104     103.455 -20.727  11.673  1.00 32.26           O  
ANISOU  790  OG1 THR A 104     3904   3966   4389    109   -174   -339       O  
ATOM    791  CG2 THR A 104     102.153 -22.761  11.515  1.00 25.39           C  
ANISOU  791  CG2 THR A 104     2971   2970   3705    132   -265   -409       C  
ATOM    792  N   VAL A 105     104.125 -21.815  14.221  1.00 29.41           N  
ANISOU  792  N   VAL A 105     3509   3631   4036     79   -186   -249       N  
ATOM    793  CA  VAL A 105     103.607 -21.788  15.589  1.00 29.64           C  
ANISOU  793  CA  VAL A 105     3556   3651   4056     63   -166   -209       C  
ATOM    794  C   VAL A 105     102.655 -20.615  15.770  1.00 27.19           C  
ANISOU  794  C   VAL A 105     3270   3363   3698     51   -129   -183       C  
ATOM    795  O   VAL A 105     102.653 -19.672  15.007  1.00 18.21           O  
ANISOU  795  O   VAL A 105     2147   2253   2517     55   -107   -181       O  
ATOM    796  CB  VAL A 105     104.713 -21.664  16.652  1.00 40.47           C  
ANISOU  796  CB  VAL A 105     4970   5047   5360     51   -131   -167       C  
ATOM    797  CG1 VAL A 105     105.497 -22.944  16.758  1.00 29.95           C  
ANISOU  797  CG1 VAL A 105     3611   3685   4084     62   -172   -189       C  
ATOM    798  CG2 VAL A 105     105.603 -20.437  16.403  1.00 28.40           C  
ANISOU  798  CG2 VAL A 105     3516   3539   3736     44    -74   -145       C  
ATOM    799  N   TRP A 106     101.740 -20.773  16.705  1.00 41.99           N  
ANISOU  799  N   TRP A 106     5139   5214   5601     43   -130   -164       N  
ATOM    800  CA  TRP A 106     100.768 -19.748  16.978  1.00 27.81           C  
ANISOU  800  CA  TRP A 106     3364   3433   3768     33   -101   -141       C  
ATOM    801  C   TRP A 106     101.248 -19.002  18.214  1.00 34.44           C  
ANISOU  801  C   TRP A 106     4264   4310   4511     19    -57    -88       C  
ATOM    802  O   TRP A 106     101.619 -19.620  19.210  1.00 24.09           O  
ANISOU  802  O   TRP A 106     2978   2967   3206     18    -53    -82       O  
ATOM    803  CB  TRP A 106      99.435 -20.437  17.259  1.00 28.20           C  
ANISOU  803  CB  TRP A 106     3361   3424   3931     33   -138   -145       C  
ATOM    804  CG  TRP A 106      98.234 -19.577  17.050  1.00 45.27           C  
ANISOU  804  CG  TRP A 106     5521   5586   6093     29   -125   -140       C  
ATOM    805  CD1 TRP A 106      98.218 -18.246  16.784  1.00 53.65           C  
ANISOU  805  CD1 TRP A 106     6670   6660   7053     28    -77   -144       C  
ATOM    806  CD2 TRP A 106      96.865 -19.995  17.093  1.00 56.36           C  
ANISOU  806  CD2 TRP A 106     6830   6824   7762     35   -194   -177       C  
ATOM    807  NE1 TRP A 106      96.925 -17.805  16.647  1.00 57.75           N  
ANISOU  807  NE1 TRP A 106     7130   7198   7615     23    -89   -132       N  
ATOM    808  CE2 TRP A 106      96.073 -18.858  16.839  1.00 53.33           C  
ANISOU  808  CE2 TRP A 106     6564   6507   7191     25   -117   -138       C  
ATOM    809  CE3 TRP A 106      96.231 -21.223  17.320  1.00 37.77           C  
ANISOU  809  CE3 TRP A 106     4529   4416   5408     25   -189   -120       C  
ATOM    810  CZ2 TRP A 106      94.680 -18.909  16.797  1.00 38.24           C  
ANISOU  810  CZ2 TRP A 106     4542   4607   5381     18   -147   -106       C  
ATOM    811  CZ3 TRP A 106      94.843 -21.267  17.285  1.00 40.88           C  
ANISOU  811  CZ3 TRP A 106     4881   4747   5903     17   -206    -87       C  
ATOM    812  CH2 TRP A 106      94.086 -20.118  17.024  1.00 38.10           C  
ANISOU  812  CH2 TRP A 106     4452   4518   5507     14   -193    -78       C  
ATOM    813  N   GLY A 107     101.188 -17.676  18.183  1.00 23.69           N  
ANISOU  813  N   GLY A 107     2949   2983   3071     11    -24    -53       N  
ATOM    814  CA  GLY A 107     101.578 -16.931  19.364  1.00 24.77           C  
ANISOU  814  CA  GLY A 107     3137   3137   3137      0      0      0       C  
ATOM    815  C   GLY A 107     100.425 -16.075  19.834  1.00 23.02           C  
ANISOU  815  C   GLY A 107     2916   2916   2916      0      0      0       C  
ATOM    816  O   GLY A 107      99.541 -15.720  19.055  1.00 25.39           O  
ANISOU  816  O   GLY A 107     3215   3215   3215      0      0      0       O  
ATOM    817  N   THR A 108     100.459 -15.710  21.110  1.00 23.91           N  
ANISOU  817  N   THR A 108     3028   3028   3028      0      0      0       N  
ATOM    818  CA  THR A 108      99.375 -14.948  21.692  1.00 26.47           C  
ANISOU  818  CA  THR A 108     3352   3352   3352      0      0      0       C  
ATOM    819  C   THR A 108      99.903 -14.138  22.857  1.00 26.16           C  
ANISOU  819  C   THR A 108     3314   3314   3314      0      0      0       C  
ATOM    820  O   THR A 108     100.880 -14.529  23.506  1.00 31.62           O  
ANISOU  820  O   THR A 108     4005   4005   4005      0      0      0       O  
ATOM    821  CB  THR A 108      98.239 -15.880  22.162  1.00 38.22           C  
ANISOU  821  CB  THR A 108     4840   4840   4840      0      0      0       C  
ATOM    822  OG1 THR A 108      97.040 -15.123  22.388  1.00 33.75           O  
ANISOU  822  OG1 THR A 108     4259   4263   4300      0     -2      5       O  
ATOM    823  CG2 THR A 108      98.639 -16.643  23.436  1.00 23.07           C  
ANISOU  823  CG2 THR A 108     2909   2906   2950     -1     -4      6       C  
ATOM    824  N   ASP A 109      99.276 -12.998  23.103  1.00 27.89           N  
ANISOU  824  N   ASP A 109     3532   3532   3532      0      0      0       N  
ATOM    825  CA  ASP A 109      99.628 -12.189  24.253  1.00 33.52           C  
ANISOU  825  CA  ASP A 109     4245   4245   4245      0      0      0       C  
ATOM    826  C   ASP A 109      98.948 -12.798  25.481  1.00 34.00           C  
ANISOU  826  C   ASP A 109     4306   4306   4306      0      0      0       C  
ATOM    827  O   ASP A 109      97.758 -13.119  25.446  1.00 56.78           O  
ANISOU  827  O   ASP A 109     7191   7191   7191      0      0      0       O  
ATOM    828  CB  ASP A 109      99.158 -10.753  23.982  1.00 46.51           C  
ANISOU  828  CB  ASP A 109     5890   5890   5890      0      0      0       C  
ATOM    829  CG  ASP A 109      99.866  -9.711  24.833  1.00 50.69           C  
ANISOU  829  CG  ASP A 109     6420   6420   6420      0      0      0       C  
ATOM    830  OD1 ASP A 109     100.848 -10.035  25.520  1.00 44.06           O  
ANISOU  830  OD1 ASP A 109     5580   5580   5580      0      0      0       O  
ATOM    831  OD2 ASP A 109      99.485  -8.525  24.744  1.00 68.60           O  
ANISOU  831  OD2 ASP A 109     8688   8688   8688      0      0      0       O  
ATOM    832  N   ALA A 110      99.677 -12.873  26.592  1.00 21.07           N  
ANISOU  832  N   ALA A 110     2669   2669   2669      0      0      0       N  
ATOM    833  CA  ALA A 110      99.127 -13.421  27.819  1.00 23.61           C  
ANISOU  833  CA  ALA A 110     2990   2990   2990      0      0      0       C  
ATOM    834  C   ALA A 110      99.322 -12.437  28.952  1.00 41.64           C  
ANISOU  834  C   ALA A 110     5274   5274   5274      0      0      0       C  
ATOM    835  O   ALA A 110     100.099 -12.664  29.876  1.00 53.04           O  
ANISOU  835  O   ALA A 110     6718   6718   6718      0      0      0       O  
ATOM    836  CB  ALA A 110      99.787 -14.766  28.153  1.00 41.14           C  
ANISOU  836  CB  ALA A 110     5210   5210   5210      0      0      0       C  
ATOM    837  N   MET A 111      98.539 -11.367  28.890  1.00 40.55           N  
ANISOU  837  N   MET A 111     5136   5136   5136      0      0      0       N  
ATOM    838  CA  MET A 111      98.706 -10.204  29.749  1.00 41.21           C  
ANISOU  838  CA  MET A 111     5219   5219   5219      0      0      0       C  
ATOM    839  C   MET A 111      98.472 -10.556  31.226  1.00 55.94           C  
ANISOU  839  C   MET A 111     7075   7095   7087      4      4     20       C  
ATOM    840  O   MET A 111      99.264 -10.200  32.097  1.00 58.42           O  
ANISOU  840  O   MET A 111     7399   7399   7399      0      0      0       O  
ATOM    841  CB  MET A 111      97.782  -9.068  29.284  1.00 34.51           C  
ANISOU  841  CB  MET A 111     4371   4371   4371      0      0      0       C  
ATOM    842  CG  MET A 111      98.120  -7.648  29.759  1.00 55.39           C  
ANISOU  842  CG  MET A 111     7016   7016   7016      0      0      0       C  
ATOM    843  SD  MET A 111      99.712  -7.009  29.185  1.00 53.35           S  
ANISOU  843  SD  MET A 111     6756   6756   6756      0      0      0       S  
ATOM    844  CE  MET A 111      99.395  -6.859  27.433  1.00 31.67           C  
ANISOU  844  CE  MET A 111     4011   4011   4011      0      0      0       C  
ATOM    845  N   HIS A 112      97.396 -11.293  31.492  1.00 43.53           N  
ANISOU  845  N   HIS A 112     5455   5546   5540     25     24    113       N  
ATOM    846  CA  HIS A 112      97.087 -11.750  32.849  1.00 42.32           C  
ANISOU  846  CA  HIS A 112     5260   5402   5418     47     48    197       C  
ATOM    847  C   HIS A 112      96.285 -13.043  32.819  1.00 46.35           C  
ANISOU  847  C   HIS A 112     5646   5929   6038     75     88    352       C  
ATOM    848  O   HIS A 112      95.113 -13.094  33.229  1.00 40.15           O  
ANISOU  848  O   HIS A 112     4824   5143   5288     86    106    343       O  
ATOM    849  CB  HIS A 112      96.379 -10.658  33.677  1.00 38.16           C  
ANISOU  849  CB  HIS A 112     4713   4881   4903     76     79    249       C  
ATOM    850  CG  HIS A 112      95.149 -10.076  33.044  1.00 38.81           C  
ANISOU  850  CG  HIS A 112     4778   4960   5010     91    100    291       C  
ATOM    851  ND1 HIS A 112      94.080  -9.618  33.787  1.00 40.96           N  
ANISOU  851  ND1 HIS A 112     4952   5261   5348    142    161    342       N  
ATOM    852  CD2 HIS A 112      94.825  -9.854  31.748  1.00 38.58           C  
ANISOU  852  CD2 HIS A 112     4718   4951   4990     83     90    235       C  
ATOM    853  CE1 HIS A 112      93.151  -9.144  32.977  1.00 25.04           C  
ANISOU  853  CE1 HIS A 112     2924   3243   3349    149    172    361       C  
ATOM    854  NE2 HIS A 112      93.578  -9.278  31.735  1.00 27.45           N  
ANISOU  854  NE2 HIS A 112     3267   3545   3619    112    127    297       N  
ATOM    855  N   GLY A 113      96.948 -14.089  32.339  1.00 43.67           N  
ANISOU  855  N   GLY A 113     5393   5553   5646     36     43    252       N  
ATOM    856  CA  GLY A 113      96.293 -15.317  31.933  1.00 42.48           C  
ANISOU  856  CA  GLY A 113     5199   5374   5567     33     44    319       C  
ATOM    857  C   GLY A 113      96.171 -15.310  30.423  1.00 41.60           C  
ANISOU  857  C   GLY A 113     5062   5283   5461     23     32    249       C  
ATOM    858  O   GLY A 113      96.712 -14.436  29.755  1.00 27.46           O  
ANISOU  858  O   GLY A 113     3372   3477   3584     15     20    185       O  
ATOM    859  N   HIS A 114      95.450 -16.279  29.881  1.00 43.29           N  
ANISOU  859  N   HIS A 114     5281   5424   5743     17     26    328       N  
ATOM    860  CA  HIS A 114      95.220 -16.357  28.445  1.00 24.73           C  
ANISOU  860  CA  HIS A 114     2942   3052   3401      8     14    294       C  
ATOM    861  C   HIS A 114      94.085 -15.388  28.133  1.00 45.71           C  
ANISOU  861  C   HIS A 114     5523   5757   6087     20     34    296       C  
ATOM    862  O   HIS A 114      93.015 -15.790  27.670  1.00 23.11           O  
ANISOU  862  O   HIS A 114     2599   2864   3316     20     37    350       O  
ATOM    863  CB  HIS A 114      94.816 -17.775  28.079  1.00 34.38           C  
ANISOU  863  CB  HIS A 114     4114   4213   4737     -2     -3    346       C  
ATOM    864  CG  HIS A 114      94.925 -18.075  26.617  1.00 39.39           C  
ANISOU  864  CG  HIS A 114     4764   4819   5383     -9    -22    292       C  
ATOM    865  ND1 HIS A 114      95.397 -17.161  25.701  1.00 22.76           N  
ANISOU  865  ND1 HIS A 114     2716   2751   3181     -7    -17    210       N  
ATOM    866  CD2 HIS A 114      94.624 -19.192  25.910  1.00 39.68           C  
ANISOU  866  CD2 HIS A 114     4682   4861   5535    -19    -53    282       C  
ATOM    867  CE1 HIS A 114      95.383 -17.698  24.494  1.00 34.24           C  
ANISOU  867  CE1 HIS A 114     4165   4168   4676    -10    -33    180       C  
ATOM    868  NE2 HIS A 114      94.917 -18.930  24.592  1.00 38.69           N  
ANISOU  868  NE2 HIS A 114     4599   4729   5372    -18    -61    213       N  
ATOM    869  N   SER A 115      94.343 -14.098  28.312  1.00 40.18           N  
ANISOU  869  N   SER A 115     4875   5088   5305     27     41    253       N  
ATOM    870  CA  SER A 115      93.294 -13.093  28.539  1.00 42.34           C  
ANISOU  870  CA  SER A 115     5118   5371   5597     45     66    296       C  
ATOM    871  C   SER A 115      92.548 -12.625  27.279  1.00 28.24           C  
ANISOU  871  C   SER A 115     3335   3577   3819     42     64    289       C  
ATOM    872  O   SER A 115      91.621 -11.840  27.367  1.00 42.77           O  
ANISOU  872  O   SER A 115     5211   5380   5660     54     79    361       O  
ATOM    873  CB  SER A 115      93.839 -11.901  29.334  1.00 42.79           C  
ANISOU  873  CB  SER A 115     5265   5424   5568     50     64    285       C  
ATOM    874  OG  SER A 115      95.096 -11.462  28.837  1.00 48.07           O  
ANISOU  874  OG  SER A 115     5996   6108   6160     30     35    172       O  
ATOM    875  N   ASN A 116      92.991 -13.061  26.109  1.00 49.18           N  
ANISOU  875  N   ASN A 116     6022   6213   6450     25     40    237       N  
ATOM    876  CA  ASN A 116      92.263 -12.809  24.865  1.00 46.31           C  
ANISOU  876  CA  ASN A 116     5702   5798   6095     20     35    257       C  
ATOM    877  C   ASN A 116      91.047 -13.730  24.710  1.00 48.00           C  
ANISOU  877  C   ASN A 116     5775   6006   6459     23     44    317       C  
ATOM    878  O   ASN A 116      90.160 -13.481  23.895  1.00 32.59           O  
ANISOU  878  O   ASN A 116     3874   3975   4535     21     42    365       O  
ATOM    879  CB  ASN A 116      93.175 -13.044  23.665  1.00 38.12           C  
ANISOU  879  CB  ASN A 116     4715   4765   5005      8     15    166       C  
ATOM    880  CG  ASN A 116      94.235 -11.987  23.535  0.70 38.72           C  
ANISOU  880  CG  ASN A 116     4848   4900   4965      5      8     64       C  
ATOM    881  OD1 ASN A 116      94.137 -10.920  24.139  0.70 56.04           O  
ANISOU  881  OD1 ASN A 116     7050   7106   7136      7      9     59       O  
ATOM    882  ND2 ASN A 116      95.309 -12.311  22.821  0.70 38.43           N  
ANISOU  882  ND2 ASN A 116     4868   4868   4868      0      0      0       N  
ATOM    883  N   VAL A 117      90.979 -14.769  25.534  1.00 56.37           N  
ANISOU  883  N   VAL A 117     6862   6978   7577     20     41    402       N  
ATOM    884  CA  VAL A 117      90.042 -15.872  25.298  1.00 34.64           C  
ANISOU  884  CA  VAL A 117     3938   4238   4985     16     34    432       C  
ATOM    885  C   VAL A 117      88.837 -15.896  26.227  1.00 38.75           C  
ANISOU  885  C   VAL A 117     4489   4658   5577     56     48    581       C  
ATOM    886  O   VAL A 117      88.983 -15.826  27.445  1.00 44.00           O  
ANISOU  886  O   VAL A 117     5153   5342   6221     43     82    623       O  
ATOM    887  CB  VAL A 117      90.761 -17.233  25.352  1.00 46.45           C  
ANISOU  887  CB  VAL A 117     5420   5702   6527      1      2    418       C  
ATOM    888  CG1 VAL A 117      89.741 -18.389  25.286  1.00 36.14           C  
ANISOU  888  CG1 VAL A 117     4126   4225   5379     19    -26    538       C  
ATOM    889  CG2 VAL A 117      91.771 -17.350  24.219  1.00 39.81           C  
ANISOU  889  CG2 VAL A 117     4739   4775   5612     -8    -22    351       C  
ATOM    890  N   TYR A 118      87.651 -15.972  25.634  1.00 51.74           N  
ANISOU  890  N   TYR A 118     6041   6251   7366     54     57    665       N  
ATOM    891  CA  TYR A 118      86.413 -16.081  26.391  1.00 50.83           C  
ANISOU  891  CA  TYR A 118     5816   6106   7390     74     93    806       C  
ATOM    892  C   TYR A 118      86.493 -17.262  27.349  1.00 48.96           C  
ANISOU  892  C   TYR A 118     5523   5837   7243     76     86    870       C  
ATOM    893  O   TYR A 118      86.852 -18.371  26.932  1.00 45.71           O  
ANISOU  893  O   TYR A 118     5094   5375   6899     52     41    850       O  
ATOM    894  CB  TYR A 118      85.250 -16.291  25.401  1.00 55.39           C  
ANISOU  894  CB  TYR A 118     6295   6614   8137     62     88    877       C  
ATOM    895  CG  TYR A 118      83.857 -16.522  25.958  1.00 60.56           C  
ANISOU  895  CG  TYR A 118     6819   7222   8969     79    125   1034       C  
ATOM    896  CD1 TYR A 118      83.121 -15.489  26.505  1.00 57.80           C  
ANISOU  896  CD1 TYR A 118     6452   6913   8597    115    187   1102       C  
ATOM    897  CD2 TYR A 118      83.283 -17.794  25.938  1.00 63.79           C  
ANISOU  897  CD2 TYR A 118     7119   7543   9577     63     97   1113       C  
ATOM    898  CE1 TYR A 118      81.846 -15.703  27.006  1.00 59.20           C  
ANISOU  898  CE1 TYR A 118     6506   7047   8940    135    230   1252       C  
ATOM    899  CE2 TYR A 118      82.006 -18.019  26.445  1.00 60.72           C  
ANISOU  899  CE2 TYR A 118     6604   7108   9360     78    133   1263       C  
ATOM    900  CZ  TYR A 118      81.297 -16.966  26.979  1.00 66.83           C  
ANISOU  900  CZ  TYR A 118     7363   7928  10103    116    205   1333       C  
ATOM    901  OH  TYR A 118      80.031 -17.172  27.482  1.00 57.20           O  
ANISOU  901  OH  TYR A 118     6015   6663   9054    136    250   1487       O  
ATOM    902  N   GLY A 119      86.213 -17.023  28.630  1.00 42.49           N  
ANISOU  902  N   GLY A 119     4673   5046   6426    107    129    943       N  
ATOM    903  CA  GLY A 119      86.213 -18.104  29.602  1.00 38.31           C  
ANISOU  903  CA  GLY A 119     4076   4488   5993    111    130   1021       C  
ATOM    904  C   GLY A 119      87.511 -18.378  30.325  1.00 51.00           C  
ANISOU  904  C   GLY A 119     5759   6140   7480    110    110    945       C  
ATOM    905  O   GLY A 119      87.528 -19.141  31.294  1.00 40.22           O  
ANISOU  905  O   GLY A 119     4334   4762   6185    119    118   1017       O  
ATOM    906  N   ALA A 120      88.586 -17.725  29.886  1.00 41.39           N  
ANISOU  906  N   ALA A 120     4667   4974   6087    101     87    805       N  
ATOM    907  CA  ALA A 120      89.910 -17.931  30.490  1.00 46.74           C  
ANISOU  907  CA  ALA A 120     5432   5678   6649     50     92    741       C  
ATOM    908  C   ALA A 120      89.945 -17.343  31.884  1.00 42.36           C  
ANISOU  908  C   ALA A 120     4877   5165   6055     78    133    780       C  
ATOM    909  O   ALA A 120      89.225 -16.399  32.178  1.00 36.14           O  
ANISOU  909  O   ALA A 120     4045   4407   5280    156    147    804       O  
ATOM    910  CB  ALA A 120      91.000 -17.323  29.636  1.00 32.78           C  
ANISOU  910  CB  ALA A 120     3742   3950   4763     37     69    622       C  
ATOM    911  N   THR A 121      90.735 -17.948  32.762  1.00 28.32           N  
ANISOU  911  N   THR A 121     2949   3509   4301     82    139    718       N  
ATOM    912  CA  THR A 121      90.995 -17.356  34.064  1.00 24.58           C  
ANISOU  912  CA  THR A 121     2485   3071   3781    112    178    734       C  
ATOM    913  C   THR A 121      91.723 -16.018  33.877  1.00 45.69           C  
ANISOU  913  C   THR A 121     5251   5780   6329    118    178    647       C  
ATOM    914  O   THR A 121      92.681 -15.915  33.106  1.00 31.76           O  
ANISOU  914  O   THR A 121     3668   3945   4456     84    126    613       O  
ATOM    915  CB  THR A 121      91.881 -18.270  34.920  1.00 26.02           C  
ANISOU  915  CB  THR A 121     2660   3260   3965    102    162    742       C  
ATOM    916  OG1 THR A 121      91.287 -19.572  35.033  1.00 50.35           O  
ANISOU  916  OG1 THR A 121     5750   6208   7171    147    112    898       O  
ATOM    917  CG2 THR A 121      92.125 -17.667  36.287  1.00 24.80           C  
ANISOU  917  CG2 THR A 121     2598   3061   3762    187    161    821       C  
ATOM    918  N   LEU A 122      91.230 -14.981  34.546  1.00 33.49           N  
ANISOU  918  N   LEU A 122     3626   4197   4901    192    279    916       N  
ATOM    919  CA  LEU A 122      91.900 -13.691  34.519  1.00 39.32           C  
ANISOU  919  CA  LEU A 122     4521   5016   5403    160    220    594       C  
ATOM    920  C   LEU A 122      92.569 -13.432  35.857  1.00 38.25           C  
ANISOU  920  C   LEU A 122     4338   4867   5328    227    301    812       C  
ATOM    921  O   LEU A 122      91.896 -13.217  36.865  1.00 32.50           O  
ANISOU  921  O   LEU A 122     3704   4104   4540    261    247    709       O  
ATOM    922  CB  LEU A 122      90.931 -12.558  34.153  1.00 25.95           C  
ANISOU  922  CB  LEU A 122     2940   3244   3673    168    230    671       C  
ATOM    923  CG  LEU A 122      90.232 -12.789  32.815  1.00 35.38           C  
ANISOU  923  CG  LEU A 122     4002   4499   4943    162    231    613       C  
ATOM    924  CD1 LEU A 122      89.151 -11.729  32.542  1.00 42.52           C  
ANISOU  924  CD1 LEU A 122     5015   5319   5822    173    245    708       C  
ATOM    925  CD2 LEU A 122      91.229 -12.880  31.705  1.00 22.80           C  
ANISOU  925  CD2 LEU A 122     2477   2907   3278    123    175    518       C  
ATOM    926  N   PHE A 123      93.893 -13.448  35.866  1.00 21.72           N  
ANISOU  926  N   PHE A 123     2313   2797   3143    196    250    706       N  
ATOM    927  CA  PHE A 123      94.620 -13.159  37.084  1.00 26.31           C  
ANISOU  927  CA  PHE A 123     2965   3411   3619    175    214    507       C  
ATOM    928  C   PHE A 123      94.645 -11.655  37.309  1.00 35.86           C  
ANISOU  928  C   PHE A 123     4305   4573   4749    180    213    524       C  
ATOM    929  O   PHE A 123      94.366 -10.895  36.384  1.00 32.65           O  
ANISOU  929  O   PHE A 123     3918   4167   4323    171    201    487       O  
ATOM    930  CB  PHE A 123      96.027 -13.750  37.011  1.00 43.53           C  
ANISOU  930  CB  PHE A 123     5272   5551   5716    126    150    483       C  
ATOM    931  CG  PHE A 123      96.033 -15.248  36.875  1.00 36.50           C  
ANISOU  931  CG  PHE A 123     4257   4701   4909    118    147    478       C  
ATOM    932  CD1 PHE A 123      95.948 -16.051  38.002  1.00 36.72           C  
ANISOU  932  CD1 PHE A 123     4168   4717   5066    168    211    751       C  
ATOM    933  CD2 PHE A 123      96.068 -15.850  35.629  1.00 35.72           C  
ANISOU  933  CD2 PHE A 123     4170   4586   4816     87    112    450       C  
ATOM    934  CE1 PHE A 123      95.914 -17.429  37.888  1.00 32.57           C  
ANISOU  934  CE1 PHE A 123     3656   4194   4524    113    149    593       C  
ATOM    935  CE2 PHE A 123      96.034 -17.230  35.514  1.00 29.87           C  
ANISOU  935  CE2 PHE A 123     3478   3766   4105     64     88    538       C  
ATOM    936  CZ  PHE A 123      95.951 -18.009  36.643  1.00 24.07           C  
ANISOU  936  CZ  PHE A 123     2698   3025   3422     74    102    616       C  
ATOM    937  N   PRO A 124      94.938 -11.216  38.540  1.00 29.89           N  
ANISOU  937  N   PRO A 124     3556   3818   3983    210    244    542       N  
ATOM    938  CA  PRO A 124      95.135  -9.778  38.748  1.00 34.26           C  
ANISOU  938  CA  PRO A 124     4066   4419   4533    245    278    450       C  
ATOM    939  C   PRO A 124      96.216  -9.256  37.801  1.00 53.88           C  
ANISOU  939  C   PRO A 124     6677   6869   6925    178    191    389       C  
ATOM    940  O   PRO A 124      97.201  -9.974  37.554  1.00 38.43           O  
ANISOU  940  O   PRO A 124     4732   4922   4946    143    148    334       O  
ATOM    941  CB  PRO A 124      95.622  -9.708  40.190  1.00 37.70           C  
ANISOU  941  CB  PRO A 124     4538   4814   4972    309    291    522       C  
ATOM    942  CG  PRO A 124      95.023 -10.934  40.855  1.00 34.66           C  
ANISOU  942  CG  PRO A 124     4070   4437   4662    348    355    656       C  
ATOM    943  CD  PRO A 124      95.052 -11.989  39.793  1.00 25.10           C  
ANISOU  943  CD  PRO A 124     2857   3227   3451    289    272    604       C  
ATOM    944  N   HIS A 125      96.059  -8.026  37.307  1.00 31.57           N  
ANISOU  944  N   HIS A 125     3816   4071   4108    194    205    318       N  
ATOM    945  CA  HIS A 125      97.102  -7.398  36.511  1.00 23.91           C  
ANISOU  945  CA  HIS A 125     2887   3102   3095    182    179    315       C  
ATOM    946  C   HIS A 125      98.353  -7.222  37.341  1.00 28.16           C  
ANISOU  946  C   HIS A 125     3496   3618   3586    114    125    210       C  
ATOM    947  O   HIS A 125      98.289  -7.226  38.566  1.00 29.22           O  
ANISOU  947  O   HIS A 125     3593   3749   3760    181    155    236       O  
ATOM    948  CB  HIS A 125      96.630  -6.053  35.934  1.00 27.42           C  
ANISOU  948  CB  HIS A 125     3358   3533   3526    150    148    217       C  
ATOM    949  CG  HIS A 125      95.905  -6.177  34.634  1.00 28.96           C  
ANISOU  949  CG  HIS A 125     3546   3733   3725    136    133    214       C  
ATOM    950  ND1 HIS A 125      96.500  -6.691  33.501  1.00 27.75           N  
ANISOU  950  ND1 HIS A 125     3448   3561   3533     80     74    168       N  
ATOM    951  CD2 HIS A 125      94.629  -5.884  34.292  1.00 12.71           C  
ANISOU  951  CD2 HIS A 125     1507   1653   1670    152    157    300       C  
ATOM    952  CE1 HIS A 125      95.624  -6.695  32.513  1.00 19.87           C  
ANISOU  952  CE1 HIS A 125     2442   2566   2543     82     77    184       C  
ATOM    953  NE2 HIS A 125      94.481  -6.208  32.965  1.00 22.36           N  
ANISOU  953  NE2 HIS A 125     2686   2902   2906    135    135    237       N  
ATOM    954  N   ASN A 126      99.471  -6.999  36.659  1.00 21.69           N  
ANISOU  954  N   ASN A 126     2688   2791   2763     82     62    112       N  
ATOM    955  CA  ASN A 126     100.780  -7.026  37.315  1.00 40.79           C  
ANISOU  955  CA  ASN A 126     5139   5199   5161     48     44     80       C  
ATOM    956  C   ASN A 126     100.954  -6.134  38.538  1.00 47.91           C  
ANISOU  956  C   ASN A 126     6029   6097   6077     92     71    101       C  
ATOM    957  O   ASN A 126     101.683  -6.515  39.455  1.00 42.48           O  
ANISOU  957  O   ASN A 126     5358   5411   5373     81     81    112       O  
ATOM    958  CB  ASN A 126     101.885  -6.732  36.297  1.00 27.64           C  
ANISOU  958  CB  ASN A 126     3501   3501   3501      0      0      0       C  
ATOM    959  CG  ASN A 126     102.236  -7.963  35.476  1.00 32.33           C  
ANISOU  959  CG  ASN A 126     4095   4095   4095      0      0      0       C  
ATOM    960  OD1 ASN A 126     101.548  -8.983  35.564  1.00 30.21           O  
ANISOU  960  OD1 ASN A 126     3826   3826   3826      0      0      0       O  
ATOM    961  ND2 ASN A 126     103.306  -7.883  34.698  1.00 29.48           N  
ANISOU  961  ND2 ASN A 126     3734   3734   3734      0      0      0       N  
ATOM    962  N   ILE A 127     100.370  -4.938  38.549  1.00 22.27           N  
ANISOU  962  N   ILE A 127     2787   2840   2833    118     96    120       N  
ATOM    963  CA  ILE A 127     100.571  -4.042  39.680  1.00 28.61           C  
ANISOU  963  CA  ILE A 127     3611   3621   3639    155    136    141       C  
ATOM    964  C   ILE A 127     100.154  -4.703  41.006  1.00 34.66           C  
ANISOU  964  C   ILE A 127     4389   4393   4386    179    215    218       C  
ATOM    965  O   ILE A 127     100.876  -4.625  42.015  1.00 27.89           O  
ANISOU  965  O   ILE A 127     3538   3500   3559    226    213    196       O  
ATOM    966  CB  ILE A 127      99.875  -2.657  39.452  1.00 30.32           C  
ANISOU  966  CB  ILE A 127     3841   3821   3858    179    165    156       C  
ATOM    967  CG1 ILE A 127     100.103  -1.743  40.651  1.00 32.67           C  
ANISOU  967  CG1 ILE A 127     4186   4107   4120    182    235    189       C  
ATOM    968  CG2 ILE A 127      98.384  -2.793  39.153  1.00 21.55           C  
ANISOU  968  CG2 ILE A 127     2713   2721   2754    266    282    286       C  
ATOM    969  CD1 ILE A 127      99.828  -0.272  40.341  1.00 33.58           C  
ANISOU  969  CD1 ILE A 127     4313   4178   4267    224    230    171       C  
ATOM    970  N   GLY A 128      99.000  -5.367  40.999  1.00 25.43           N  
ANISOU  970  N   GLY A 128     3169   3227   3266    300    317    349       N  
ATOM    971  CA  GLY A 128      98.568  -6.090  42.178  1.00 42.61           C  
ANISOU  971  CA  GLY A 128     5334   5384   5472    328    325    373       C  
ATOM    972  C   GLY A 128      99.440  -7.287  42.521  1.00 40.39           C  
ANISOU  972  C   GLY A 128     5035   5125   5184    306    297    363       C  
ATOM    973  O   GLY A 128      99.763  -7.511  43.699  1.00 36.97           O  
ANISOU  973  O   GLY A 128     4607   4688   4754    364    379    430       O  
ATOM    974  N   LEU A 129      99.905  -7.999  41.497  1.00 23.05           N  
ANISOU  974  N   LEU A 129     2821   2957   2980    225    196    264       N  
ATOM    975  CA  LEU A 129     100.818  -9.104  41.728  1.00 24.46           C  
ANISOU  975  CA  LEU A 129     2990   3153   3149    197    164    246       C  
ATOM    976  C   LEU A 129     102.102  -8.611  42.390  1.00 40.34           C  
ANISOU  976  C   LEU A 129     5046   5145   5137    183    145    212       C  
ATOM    977  O   LEU A 129     102.668  -9.267  43.258  1.00 36.22           O  
ANISOU  977  O   LEU A 129     4511   4638   4611    211    181    256       O  
ATOM    978  CB  LEU A 129     101.125  -9.839  40.419  1.00 18.35           C  
ANISOU  978  CB  LEU A 129     2248   2385   2338    119    106    218       C  
ATOM    979  CG  LEU A 129      99.896 -10.468  39.762  1.00 32.19           C  
ANISOU  979  CG  LEU A 129     3927   4164   4138    142    134    244       C  
ATOM    980  CD1 LEU A 129     100.300 -11.279  38.550  1.00 20.29           C  
ANISOU  980  CD1 LEU A 129     2438   2656   2617     93     84    195       C  
ATOM    981  CD2 LEU A 129      99.096 -11.306  40.761  1.00 37.32           C  
ANISOU  981  CD2 LEU A 129     4518   4828   4835    188    190    338       C  
ATOM    982  N   GLY A 130     102.544  -7.432  41.990  1.00 31.27           N  
ANISOU  982  N   GLY A 130     3923   3993   3965    187    175    211       N  
ATOM    983  CA  GLY A 130     103.693  -6.796  42.595  1.00 22.32           C  
ANISOU  983  CA  GLY A 130     2832   2836   2810    118    130    132       C  
ATOM    984  C   GLY A 130     103.412  -6.504  44.048  1.00 42.67           C  
ANISOU  984  C   GLY A 130     5438   5372   5402    238    245    216       C  
ATOM    985  O   GLY A 130     104.253  -6.742  44.918  1.00 38.91           O  
ANISOU  985  O   GLY A 130     4993   4891   4901    233    274    215       O  
ATOM    986  N   ALA A 131     102.215  -5.982  44.315  1.00 32.31           N  
ANISOU  986  N   ALA A 131     4134   4042   4099    306    331    287       N  
ATOM    987  CA  ALA A 131     101.838  -5.756  45.699  1.00 26.34           C  
ANISOU  987  CA  ALA A 131     3421   3280   3308    341    455    351       C  
ATOM    988  C   ALA A 131     101.886  -7.037  46.539  1.00 36.96           C  
ANISOU  988  C   ALA A 131     4741   4677   4627    318    490    398       C  
ATOM    989  O   ALA A 131     102.218  -6.984  47.723  1.00 37.66           O  
ANISOU  989  O   ALA A 131     4877   4774   4658    297    553    415       O  
ATOM    990  CB  ALA A 131     100.453  -5.107  45.779  1.00 25.50           C  
ANISOU  990  CB  ALA A 131     3315   3155   3221    405    539    422       C  
ATOM    991  N   ALA A 132     101.624  -8.181  45.909  1.00 28.06           N  
ANISOU  991  N   ALA A 132     3542   3581   3538    318    445    422       N  
ATOM    992  CA  ALA A 132     101.593  -9.464  46.621  1.00 39.50           C  
ANISOU  992  CA  ALA A 132     4959   5074   4976    296    476    481       C  
ATOM    993  C   ALA A 132     102.943  -9.923  47.177  1.00 41.99           C  
ANISOU  993  C   ALA A 132     5308   5407   5238    231    441    430       C  
ATOM    994  O   ALA A 132     102.980 -10.663  48.154  1.00 46.73           O  
ANISOU  994  O   ALA A 132     5915   6036   5805    206    492    486       O  
ATOM    995  CB  ALA A 132     101.014 -10.546  45.722  1.00 33.78           C  
ANISOU  995  CB  ALA A 132     4146   4372   4317    313    428    523       C  
ATOM    996  N   ARG A 133     104.039  -9.468  46.576  1.00 37.79           N  
ANISOU  996  N   ARG A 133     4799   4856   4703    200    355    332       N  
ATOM    997  CA  ARG A 133     105.389  -9.902  46.960  1.00 37.70           C  
ANISOU  997  CA  ARG A 133     4812   4857   4654    135    311    280       C  
ATOM    998  C   ARG A 133     105.539 -11.413  47.156  1.00 41.64           C  
ANISOU  998  C   ARG A 133     5271   5399   5152    109    298    319       C  
ATOM    999  O   ARG A 133     105.976 -11.865  48.211  1.00 40.25           O  
ANISOU  999  O   ARG A 133     5131   5241   4922     70    337    349       O  
ATOM   1000  CB  ARG A 133     105.839  -9.200  48.240  1.00 29.87           C  
ANISOU 1000  CB  ARG A 133     3897   3858   3593    114    378    287       C  
ATOM   1001  CG  ARG A 133     105.837  -7.688  48.190  1.00 36.51           C  
ANISOU 1001  CG  ARG A 133     4786   4650   4437    139    394    252       C  
ATOM   1002  CD  ARG A 133     106.859  -7.165  47.199  1.00 32.01           C  
ANISOU 1002  CD  ARG A 133     4210   4042   3912    111    295    163       C  
ATOM   1003  NE  ARG A 133     107.301  -5.831  47.596  1.00 47.49           N  
ANISOU 1003  NE  ARG A 133     6234   5951   5859    111    318    137       N  
ATOM   1004  CZ  ARG A 133     106.568  -4.727  47.481  1.00 35.85           C  
ANISOU 1004  CZ  ARG A 133     4790   4436   4395    153    360    149       C  
ATOM   1005  NH1 ARG A 133     105.363  -4.771  46.916  1.00 42.15           N  
ANISOU 1005  NH1 ARG A 133     5554   5238   5221    202    380    187       N  
ATOM   1006  NH2 ARG A 133     107.053  -3.572  47.906  1.00 37.14           N  
ANISOU 1006  NH2 ARG A 133     5018   4551   4543    147    382    128       N  
ATOM   1007  N   ASP A 134     105.230 -12.190  46.128  1.00 31.23           N  
ANISOU 1007  N   ASP A 134     3878   4096   3890    129    234    322       N  
ATOM   1008  CA  ASP A 134     105.193 -13.635  46.281  1.00 41.47           C  
ANISOU 1008  CA  ASP A 134     5123   5431   5201    115    223    380       C  
ATOM   1009  C   ASP A 134     105.722 -14.316  45.014  1.00 28.20           C  
ANISOU 1009  C   ASP A 134     3378   3772   3566    113     99    325       C  
ATOM   1010  O   ASP A 134     104.964 -14.606  44.092  1.00 33.49           O  
ANISOU 1010  O   ASP A 134     4046   4419   4262    108     71    301       O  
ATOM   1011  CB  ASP A 134     103.756 -14.085  46.585  1.00 54.74           C  
ANISOU 1011  CB  ASP A 134     6756   7122   6919    155    301    501       C  
ATOM   1012  CG  ASP A 134     103.674 -15.511  47.089  1.00 50.49           C  
ANISOU 1012  CG  ASP A 134     6172   6612   6401    130    313    588       C  
ATOM   1013  OD1 ASP A 134     104.474 -16.356  46.632  1.00 39.66           O  
ANISOU 1013  OD1 ASP A 134     4768   5260   5040    102    228    556       O  
ATOM   1014  OD2 ASP A 134     102.794 -15.779  47.944  1.00 34.22           O  
ANISOU 1014  OD2 ASP A 134     4102   4551   4350    137    406    696       O  
ATOM   1015  N   THR A 135     107.017 -14.624  44.995  1.00 25.09           N  
ANISOU 1015  N   THR A 135     3001   3382   3153     60     37    249       N  
ATOM   1016  CA  THR A 135     107.614 -15.157  43.773  1.00 30.01           C  
ANISOU 1016  CA  THR A 135     3715   3924   3764     -1     -1    132       C  
ATOM   1017  C   THR A 135     107.078 -16.514  43.351  1.00 35.43           C  
ANISOU 1017  C   THR A 135     4378   4625   4459     -5     -3    179       C  
ATOM   1018  O   THR A 135     106.836 -16.745  42.157  1.00 36.19           O  
ANISOU 1018  O   THR A 135     4467   4704   4581    -13     -8    136       O  
ATOM   1019  CB  THR A 135     109.161 -15.259  43.904  1.00 44.21           C  
ANISOU 1019  CB  THR A 135     5548   5692   5558    -26    -12     73       C  
ATOM   1020  OG1 THR A 135     109.491 -15.936  45.128  1.00 48.17           O  
ANISOU 1020  OG1 THR A 135     6019   6242   6042    -40    -19    120       O  
ATOM   1021  CG2 THR A 135     109.793 -13.880  43.949  1.00 24.98           C  
ANISOU 1021  CG2 THR A 135     3132   3216   3144    -23     -7     27       C  
ATOM   1022  N   ASP A 136     106.774 -17.359  44.334  1.00 42.04           N  
ANISOU 1022  N   ASP A 136     5127   5514   5332     16    -12    255       N  
ATOM   1023  CA  ASP A 136     106.252 -18.689  44.048  1.00 45.84           C  
ANISOU 1023  CA  ASP A 136     5614   5983   5818     -4     -3    334       C  
ATOM   1024  C   ASP A 136     104.864 -18.534  43.412  1.00 22.09           C  
ANISOU 1024  C   ASP A 136     2585   2962   2845     22     19    380       C  
ATOM   1025  O   ASP A 136     104.519 -19.249  42.470  1.00 25.62           O  
ANISOU 1025  O   ASP A 136     3029   3391   3315      6      6    387       O  
ATOM   1026  CB  ASP A 136     106.164 -19.534  45.320  1.00 47.00           C  
ANISOU 1026  CB  ASP A 136     5604   6226   6029     11     -2    502       C  
ATOM   1027  CG  ASP A 136     105.429 -20.841  45.093  1.00 64.20           C  
ANISOU 1027  CG  ASP A 136     7722   8391   8279      7    -12    593       C  
ATOM   1028  OD1 ASP A 136     105.880 -21.615  44.217  1.00 56.82           O  
ANISOU 1028  OD1 ASP A 136     6853   7407   7330    -20    -60    479       O  
ATOM   1029  OD2 ASP A 136     104.358 -21.051  45.704  1.00 61.25           O  
ANISOU 1029  OD2 ASP A 136     7244   8042   7988     47     43    771       O  
ATOM   1030  N   LEU A 137     104.086 -17.574  43.911  1.00 34.72           N  
ANISOU 1030  N   LEU A 137     4097   4604   4491     87     52    440       N  
ATOM   1031  CA  LEU A 137     102.769 -17.287  43.344  1.00 40.55           C  
ANISOU 1031  CA  LEU A 137     4819   5321   5268    118     79    476       C  
ATOM   1032  C   LEU A 137     102.936 -16.931  41.874  1.00 38.94           C  
ANISOU 1032  C   LEU A 137     4736   5063   4998     57     52    364       C  
ATOM   1033  O   LEU A 137     102.179 -17.402  41.023  1.00 37.06           O  
ANISOU 1033  O   LEU A 137     4418   4841   4823     57     55    357       O  
ATOM   1034  CB  LEU A 137     102.092 -16.129  44.084  1.00 40.97           C  
ANISOU 1034  CB  LEU A 137     4841   5387   5338    187    166    568       C  
ATOM   1035  CG  LEU A 137     100.726 -15.688  43.533  1.00 39.84           C  
ANISOU 1035  CG  LEU A 137     4686   5216   5236    217    200    602       C  
ATOM   1036  CD1 LEU A 137      99.669 -16.712  43.792  1.00 44.06           C  
ANISOU 1036  CD1 LEU A 137     5124   5751   5866    242    245    754       C  
ATOM   1037  CD2 LEU A 137     100.305 -14.365  44.132  1.00 30.80           C  
ANISOU 1037  CD2 LEU A 137     3552   4062   4087    285    284    645       C  
ATOM   1038  N   ILE A 138     103.908 -16.079  41.574  1.00 35.40           N  
ANISOU 1038  N   ILE A 138     4294   4625   4532     43     35    241       N  
ATOM   1039  CA  ILE A 138     104.150 -15.687  40.190  1.00 40.48           C  
ANISOU 1039  CA  ILE A 138     5027   5222   5132     18     14    176       C  
ATOM   1040  C   ILE A 138     104.456 -16.909  39.328  1.00 33.53           C  
ANISOU 1040  C   ILE A 138     4126   4340   4273      0      0    149       C  
ATOM   1041  O   ILE A 138     103.894 -17.075  38.240  1.00 34.03           O  
ANISOU 1041  O   ILE A 138     4197   4391   4343     -2     -1    142       O  
ATOM   1042  CB  ILE A 138     105.308 -14.676  40.071  1.00 45.11           C  
ANISOU 1042  CB  ILE A 138     5651   5778   5712      5      3     73       C  
ATOM   1043  CG1 ILE A 138     105.002 -13.401  40.862  1.00 30.32           C  
ANISOU 1043  CG1 ILE A 138     3784   3911   3826     20     13     97       C  
ATOM   1044  CG2 ILE A 138     105.589 -14.359  38.608  1.00 36.48           C  
ANISOU 1044  CG2 ILE A 138     4617   4625   4620      0      0      4       C  
ATOM   1045  CD1 ILE A 138     103.704 -12.744  40.471  1.00 40.56           C  
ANISOU 1045  CD1 ILE A 138     5067   5215   5131     42     31    135       C  
ATOM   1046  N   LYS A 139     105.325 -17.784  39.834  1.00 35.94           N  
ANISOU 1046  N   LYS A 139     4457   4641   4559    -12     -9    167       N  
ATOM   1047  CA  LYS A 139     105.697 -18.990  39.072  1.00 30.98           C  
ANISOU 1047  CA  LYS A 139     3833   3998   3939    -24    -20    164       C  
ATOM   1048  C   LYS A 139     104.472 -19.871  38.798  1.00 19.85           C  
ANISOU 1048  C   LYS A 139     2372   2590   2580    -26    -25    260       C  
ATOM   1049  O   LYS A 139     104.289 -20.381  37.685  1.00 19.10           O  
ANISOU 1049  O   LYS A 139     2283   2472   2501    -31    -33    249       O  
ATOM   1050  CB  LYS A 139     106.800 -19.784  39.779  1.00 29.89           C  
ANISOU 1050  CB  LYS A 139     3696   3866   3795    -37    -30    167       C  
ATOM   1051  CG  LYS A 139     107.400 -20.872  38.897  1.00 34.01           C  
ANISOU 1051  CG  LYS A 139     4206   4377   4339    -49    -43    138       C  
ATOM   1052  CD  LYS A 139     108.540 -21.597  39.588  1.00 36.97           C  
ANISOU 1052  CD  LYS A 139     4608   4744   4693    -58    -49    157       C  
ATOM   1053  CE  LYS A 139     109.247 -22.545  38.629  1.00 38.74           C  
ANISOU 1053  CE  LYS A 139     4849   4945   4926    -58    -54    137       C  
ATOM   1054  NZ  LYS A 139     110.587 -22.985  39.136  1.00 38.65           N  
ANISOU 1054  NZ  LYS A 139     4830   4939   4915    -68    -61    108       N  
ATOM   1055  N   ARG A 140     103.634 -20.034  39.813  1.00 19.98           N  
ANISOU 1055  N   ARG A 140     2332   2621   2639    -14    -15    358       N  
ATOM   1056  CA  ARG A 140     102.424 -20.832  39.658  1.00 41.19           C  
ANISOU 1056  CA  ARG A 140     4959   5284   5405    -10    -11    459       C  
ATOM   1057  C   ARG A 140     101.444 -20.203  38.676  1.00 32.69           C  
ANISOU 1057  C   ARG A 140     3811   4236   4373      2      2    412       C  
ATOM   1058  O   ARG A 140     100.800 -20.916  37.897  1.00 35.82           O  
ANISOU 1058  O   ARG A 140     4258   4554   4797     -6     -8    486       O  
ATOM   1059  CB  ARG A 140     101.751 -21.084  41.012  1.00 36.92           C  
ANISOU 1059  CB  ARG A 140     4261   4808   4958     13     15    521       C  
ATOM   1060  CG  ARG A 140     102.540 -22.010  41.935  1.00 41.62           C  
ANISOU 1060  CG  ARG A 140     4832   5418   5565     -4     -5    553       C  
ATOM   1061  CD  ARG A 140     101.792 -22.277  43.232  1.00 33.62           C  
ANISOU 1061  CD  ARG A 140     3727   4411   4637     55     11    764       C  
ATOM   1062  NE  ARG A 140     101.977 -21.182  44.187  1.00 43.12           N  
ANISOU 1062  NE  ARG A 140     4918   5660   5805     88     68    802       N  
ATOM   1063  CZ  ARG A 140     101.004 -20.586  44.875  1.00 48.20           C  
ANISOU 1063  CZ  ARG A 140     5492   6316   6506    148    156    934       C  
ATOM   1064  NH1 ARG A 140      99.742 -20.959  44.718  1.00 36.46           N  
ANISOU 1064  NH1 ARG A 140     3934   4797   5122    172    192   1040       N  
ATOM   1065  NH2 ARG A 140     101.294 -19.603  45.722  1.00 36.84           N  
ANISOU 1065  NH2 ARG A 140     4107   4898   4994    161    227    917       N  
ATOM   1066  N   ILE A 141     101.358 -18.875  38.675  1.00 49.43           N  
ANISOU 1066  N   ILE A 141     6038   6329   6413     17     19    398       N  
ATOM   1067  CA  ILE A 141     100.504 -18.191  37.712  1.00 27.32           C  
ANISOU 1067  CA  ILE A 141     3246   3516   3616     25     28    383       C  
ATOM   1068  C   ILE A 141     101.039 -18.474  36.312  1.00 11.19           C  
ANISOU 1068  C   ILE A 141     1246   1458   1548      4      4    305       C  
ATOM   1069  O   ILE A 141     100.277 -18.692  35.383  1.00 30.52           O  
ANISOU 1069  O   ILE A 141     3625   3918   4052      3      3    297       O  
ATOM   1070  CB  ILE A 141     100.392 -16.698  38.008  1.00 30.89           C  
ANISOU 1070  CB  ILE A 141     3724   3984   4027     43     46    345       C  
ATOM   1071  CG1 ILE A 141      99.593 -16.517  39.287  1.00 26.98           C  
ANISOU 1071  CG1 ILE A 141     3108   3535   3606     86     94    404       C  
ATOM   1072  CG2 ILE A 141      99.700 -15.974  36.843  1.00 31.76           C  
ANISOU 1072  CG2 ILE A 141     3852   4083   4132     43     47    315       C  
ATOM   1073  CD1 ILE A 141      99.456 -15.069  39.717  1.00 36.50           C  
ANISOU 1073  CD1 ILE A 141     4301   4757   4809    143    150    522       C  
ATOM   1074  N   GLY A 142     102.359 -18.467  36.169  1.00 24.21           N  
ANISOU 1074  N   GLY A 142     2945   3112   3143     -7     -8    219       N  
ATOM   1075  CA  GLY A 142     102.971 -18.855  34.906  1.00 25.35           C  
ANISOU 1075  CA  GLY A 142     3102   3252   3279    -15    -17    139       C  
ATOM   1076  C   GLY A 142     102.613 -20.270  34.450  1.00 30.28           C  
ANISOU 1076  C   GLY A 142     3712   3839   3956    -25    -32    220       C  
ATOM   1077  O   GLY A 142     102.284 -20.482  33.284  1.00 27.64           O  
ANISOU 1077  O   GLY A 142     3382   3484   3638    -25    -37    208       O  
ATOM   1078  N   GLN A 143     102.654 -21.235  35.363  1.00 24.96           N  
ANISOU 1078  N   GLN A 143     2945   3191   3350    -37    -50    269       N  
ATOM   1079  CA  GLN A 143     102.322 -22.628  35.026  1.00 28.34           C  
ANISOU 1079  CA  GLN A 143     3378   3539   3850    -48    -73    362       C  
ATOM   1080  C   GLN A 143     100.845 -22.778  34.615  1.00 34.20           C  
ANISOU 1080  C   GLN A 143     4068   4244   4682    -45    -73    432       C  
ATOM   1081  O   GLN A 143     100.513 -23.399  33.587  1.00 28.38           O  
ANISOU 1081  O   GLN A 143     3178   3462   4143    -70   -127    543       O  
ATOM   1082  CB  GLN A 143     102.690 -23.529  36.211  1.00 32.22           C  
ANISOU 1082  CB  GLN A 143     3757   4081   4402    -65    -97    390       C  
ATOM   1083  CG  GLN A 143     104.185 -23.524  36.466  1.00 34.96           C  
ANISOU 1083  CG  GLN A 143     4130   4421   4733    -89   -126    445       C  
ATOM   1084  CD  GLN A 143     104.564 -24.161  37.771  1.00 44.68           C  
ANISOU 1084  CD  GLN A 143     5432   5641   5902    -78   -106    416       C  
ATOM   1085  OE1 GLN A 143     103.745 -24.232  38.684  1.00 47.23           O  
ANISOU 1085  OE1 GLN A 143     5703   5970   6271    -73    -99    499       O  
ATOM   1086  NE2 GLN A 143     105.805 -24.621  37.881  1.00 44.23           N  
ANISOU 1086  NE2 GLN A 143     5405   5587   5814    -89   -120    378       N  
ATOM   1087  N   ALA A 144      99.980 -22.081  35.346  1.00 29.51           N  
ANISOU 1087  N   ALA A 144     3360   3730   4121    -32    -50    440       N  
ATOM   1088  CA  ALA A 144      98.561 -22.119  35.060  1.00 24.12           C  
ANISOU 1088  CA  ALA A 144     2714   2952   3498    -22    -35    551       C  
ATOM   1089  C   ALA A 144      98.327 -21.494  33.694  1.00 37.46           C  
ANISOU 1089  C   ALA A 144     4347   4702   5183    -23    -39    445       C  
ATOM   1090  O   ALA A 144      97.552 -22.021  32.883  1.00 31.30           O  
ANISOU 1090  O   ALA A 144     3627   3804   4462    -27    -49    515       O  
ATOM   1091  CB  ALA A 144      97.772 -21.389  36.137  1.00 30.49           C  
ANISOU 1091  CB  ALA A 144     3491   3783   4311      3      5    613       C  
ATOM   1092  N   THR A 145      99.009 -20.376  33.437  1.00 33.13           N  
ANISOU 1092  N   THR A 145     3884   4184   4522    -16    -26    361       N  
ATOM   1093  CA  THR A 145      98.894 -19.665  32.164  1.00 26.27           C  
ANISOU 1093  CA  THR A 145     3065   3309   3607    -15    -23    298       C  
ATOM   1094  C   THR A 145      99.315 -20.567  31.021  1.00 17.88           C  
ANISOU 1094  C   THR A 145     2012   2214   2567    -26    -49    270       C  
ATOM   1095  O   THR A 145      98.683 -20.584  29.965  1.00 20.10           O  
ANISOU 1095  O   THR A 145     2282   2470   2884    -27    -55    267       O  
ATOM   1096  CB  THR A 145      99.723 -18.356  32.155  1.00 30.35           C  
ANISOU 1096  CB  THR A 145     3711   3828   3992     -7    -10    225       C  
ATOM   1097  OG1 THR A 145      99.229 -17.453  33.151  1.00 29.26           O  
ANISOU 1097  OG1 THR A 145     3559   3710   3848      5      7    255       O  
ATOM   1098  CG2 THR A 145      99.613 -17.663  30.807  1.00 27.13           C  
ANISOU 1098  CG2 THR A 145     3342   3421   3544     -5     -8    158       C  
ATOM   1099  N   ALA A 146     100.423 -21.272  31.215  1.00 30.75           N  
ANISOU 1099  N   ALA A 146     3665   3843   4178    -34    -63    247       N  
ATOM   1100  CA  ALA A 146     100.896 -22.213  30.207  1.00 31.18           C  
ANISOU 1100  CA  ALA A 146     3720   3863   4266    -40    -89    226       C  
ATOM   1101  C   ALA A 146      99.838 -23.259  29.874  1.00 37.25           C  
ANISOU 1101  C   ALA A 146     4351   4488   5312    -63   -156    399       C  
ATOM   1102  O   ALA A 146      99.571 -23.531  28.707  1.00 21.47           O  
ANISOU 1102  O   ALA A 146     2345   2443   3371    -62   -179    368       O  
ATOM   1103  CB  ALA A 146     102.172 -22.878  30.649  1.00 35.69           C  
ANISOU 1103  CB  ALA A 146     4364   4396   4802    -41    -91    227       C  
ATOM   1104  N   LYS A 147      99.197 -23.810  30.906  1.00 41.42           N  
ANISOU 1104  N   LYS A 147     4948   5015   5775    -53   -122    410       N  
ATOM   1105  CA  LYS A 147      98.148 -24.791  30.639  1.00 28.67           C  
ANISOU 1105  CA  LYS A 147     3150   3422   4321    -67   -166    439       C  
ATOM   1106  C   LYS A 147      96.956 -24.181  29.905  1.00 34.60           C  
ANISOU 1106  C   LYS A 147     3804   4023   5319    -75   -188    611       C  
ATOM   1107  O   LYS A 147      96.464 -24.776  28.936  1.00 30.95           O  
ANISOU 1107  O   LYS A 147     3510   3530   4721    -60   -168    485       O  
ATOM   1108  CB  LYS A 147      97.678 -25.465  31.930  1.00 43.25           C  
ANISOU 1108  CB  LYS A 147     4835   5126   6472    -92   -211    728       C  
ATOM   1109  CG  LYS A 147      98.698 -26.468  32.504  1.00 42.48           C  
ANISOU 1109  CG  LYS A 147     4952   5045   6142    -81   -186    590       C  
ATOM   1110  CD  LYS A 147      98.206 -27.060  33.811  1.00 53.12           C  
ANISOU 1110  CD  LYS A 147     6087   6509   7587    -93   -201    636       C  
ATOM   1111  CE  LYS A 147      99.103 -28.168  34.297  1.00 60.44           C  
ANISOU 1111  CE  LYS A 147     7159   7289   8517   -102   -223    710       C  
ATOM   1112  NZ  LYS A 147      98.489 -28.838  35.471  1.00 67.44           N  
ANISOU 1112  NZ  LYS A 147     7976   8157   9490   -106   -222    822       N  
ATOM   1113  N   GLU A 148      96.495 -23.002  30.323  1.00 30.98           N  
ANISOU 1113  N   GLU A 148     3554   3648   4569    -42    -97    497       N  
ATOM   1114  CA  GLU A 148      95.314 -22.420  29.668  1.00 31.65           C  
ANISOU 1114  CA  GLU A 148     3619   3715   4692    -36    -83    514       C  
ATOM   1115  C   GLU A 148      95.622 -22.060  28.225  1.00 30.64           C  
ANISOU 1115  C   GLU A 148     3535   3583   4523    -36    -94    425       C  
ATOM   1116  O   GLU A 148      94.779 -22.241  27.348  1.00 43.80           O  
ANISOU 1116  O   GLU A 148     5173   5201   6268    -38   -108    433       O  
ATOM   1117  CB  GLU A 148      94.772 -21.202  30.433  1.00 28.14           C  
ANISOU 1117  CB  GLU A 148     3180   3323   4189    -19    -39    542       C  
ATOM   1118  CG  GLU A 148      94.453 -21.437  31.908  1.00 33.55           C  
ANISOU 1118  CG  GLU A 148     3692   4119   4938    -10    -20    577       C  
ATOM   1119  CD  GLU A 148      93.152 -20.775  32.351  1.00 39.20           C  
ANISOU 1119  CD  GLU A 148     4355   4842   5699     12     23    646       C  
ATOM   1120  OE1 GLU A 148      92.504 -20.097  31.533  1.00 47.18           O  
ANISOU 1120  OE1 GLU A 148     5514   5738   6674     16     30    687       O  
ATOM   1121  OE2 GLU A 148      92.777 -20.911  33.533  1.00 39.19           O  
ANISOU 1121  OE2 GLU A 148     4455   4736   5701     27     48    782       O  
ATOM   1122  N   VAL A 149      96.838 -21.591  27.969  1.00 35.06           N  
ANISOU 1122  N   VAL A 149     4162   4195   4965    -33    -87    340       N  
ATOM   1123  CA  VAL A 149      97.253 -21.299  26.599  1.00 29.72           C  
ANISOU 1123  CA  VAL A 149     3451   3589   4251    -32    -99    235       C  
ATOM   1124  C   VAL A 149      97.335 -22.579  25.773  1.00 37.66           C  
ANISOU 1124  C   VAL A 149     4413   4536   5359    -34   -147    227       C  
ATOM   1125  O   VAL A 149      96.839 -22.638  24.647  1.00 30.97           O  
ANISOU 1125  O   VAL A 149     3550   3659   4559    -32   -163    201       O  
ATOM   1126  CB  VAL A 149      98.603 -20.538  26.562  1.00 29.00           C  
ANISOU 1126  CB  VAL A 149     3459   3552   4010    -23    -73    160       C  
ATOM   1127  CG1 VAL A 149      99.184 -20.478  25.144  1.00 19.97           C  
ANISOU 1127  CG1 VAL A 149     2398   2367   2825    -16    -67    103       C  
ATOM   1128  CG2 VAL A 149      98.442 -19.137  27.124  1.00 29.93           C  
ANISOU 1128  CG2 VAL A 149     3623   3717   4034    -16    -40    147       C  
ATOM   1129  N   ALA A 150      97.934 -23.617  26.350  1.00 26.05           N  
ANISOU 1129  N   ALA A 150     2919   3048   3930    -41   -175    247       N  
ATOM   1130  CA  ALA A 150      98.066 -24.897  25.642  1.00 39.44           C  
ANISOU 1130  CA  ALA A 150     4508   4523   5954    -62   -287    323       C  
ATOM   1131  C   ALA A 150      96.701 -25.475  25.289  1.00 36.94           C  
ANISOU 1131  C   ALA A 150     4092   4115   5829    -71   -328    387       C  
ATOM   1132  O   ALA A 150      96.515 -26.039  24.209  1.00 37.28           O  
ANISOU 1132  O   ALA A 150     4316   4172   5678    -53   -277    272       O  
ATOM   1133  CB  ALA A 150      98.860 -25.890  26.483  1.00 23.64           C  
ANISOU 1133  CB  ALA A 150     2554   2675   3755    -54   -257    262       C  
ATOM   1134  N   ALA A 151      95.718 -25.206  26.141  1.00 25.44           N  
ANISOU 1134  N   ALA A 151     2582   2662   4420    -78   -301    491       N  
ATOM   1135  CA  ALA A 151      94.383 -25.739  25.934  1.00 18.88           C  
ANISOU 1135  CA  ALA A 151     1648   1746   3778    -86   -331    570       C  
ATOM   1136  C   ALA A 151      93.710 -25.165  24.693  1.00 42.53           C  
ANISOU 1136  C   ALA A 151     4745   4950   6463    -57   -265    376       C  
ATOM   1137  O   ALA A 151      92.701 -25.692  24.237  1.00 49.09           O  
ANISOU 1137  O   ALA A 151     5399   5469   7785    -83   -368    553       O  
ATOM   1138  CB  ALA A 151      93.520 -25.485  27.162  1.00 39.27           C  
ANISOU 1138  CB  ALA A 151     4441   4420   6060    -65   -210    560       C  
ATOM   1139  N   THR A 152      94.269 -24.098  24.136  1.00 37.76           N  
ANISOU 1139  N   THR A 152     4224   4393   5731    -46   -233    307       N  
ATOM   1140  CA  THR A 152      93.698 -23.534  22.927  1.00 19.70           C  
ANISOU 1140  CA  THR A 152     2076   1962   3446    -43   -212    287       C  
ATOM   1141  C   THR A 152      94.575 -23.819  21.719  1.00 33.11           C  
ANISOU 1141  C   THR A 152     3679   3784   5117    -30   -260    170       C  
ATOM   1142  O   THR A 152      94.329 -23.319  20.625  1.00 24.31           O  
ANISOU 1142  O   THR A 152     2702   2545   3991    -23   -237    129       O  
ATOM   1143  CB  THR A 152      93.467 -22.004  23.051  1.00 28.68           C  
ANISOU 1143  CB  THR A 152     3064   3109   4723    -45   -218    352       C  
ATOM   1144  OG1 THR A 152      94.682 -21.355  23.435  1.00 25.58           O  
ANISOU 1144  OG1 THR A 152     2832   2957   3931    -28   -144    215       O  
ATOM   1145  CG2 THR A 152      92.414 -21.713  24.113  1.00 32.23           C  
ANISOU 1145  CG2 THR A 152     3535   3744   4965    -40   -147    353       C  
ATOM   1146  N   GLY A 153      95.585 -24.655  21.914  1.00 35.48           N  
ANISOU 1146  N   GLY A 153     4112   3950   5418    -32   -261    166       N  
ATOM   1147  CA  GLY A 153      96.443 -25.071  20.819  1.00 36.64           C  
ANISOU 1147  CA  GLY A 153     4277   4092   5554    -17   -287     79       C  
ATOM   1148  C   GLY A 153      97.542 -24.078  20.477  1.00 36.86           C  
ANISOU 1148  C   GLY A 153     4270   4317   5416     -3   -265     14       C  
ATOM   1149  O   GLY A 153      98.092 -24.106  19.365  1.00 35.75           O  
ANISOU 1149  O   GLY A 153     4145   4186   5253     12   -276    -50       O  
ATOM   1150  N   ILE A 154      97.878 -23.209  21.427  1.00 29.84           N  
ANISOU 1150  N   ILE A 154     3435   3482   4421     -8   -213     38       N  
ATOM   1151  CA  ILE A 154      98.862 -22.170  21.162  1.00 18.95           C  
ANISOU 1151  CA  ILE A 154     2203   2103   2893      2   -151     -7       C  
ATOM   1152  C   ILE A 154     100.192 -22.500  21.865  1.00 29.99           C  
ANISOU 1152  C   ILE A 154     3572   3598   4226      2   -154     -8       C  
ATOM   1153  O   ILE A 154     100.222 -22.782  23.065  1.00 24.99           O  
ANISOU 1153  O   ILE A 154     2991   2900   3605     -8   -141     38       O  
ATOM   1154  CB  ILE A 154      98.305 -20.790  21.588  1.00 37.61           C  
ANISOU 1154  CB  ILE A 154     4598   4523   5171     -2   -107     12       C  
ATOM   1155  CG1 ILE A 154      97.151 -20.411  20.666  1.00 33.02           C  
ANISOU 1155  CG1 ILE A 154     3931   3973   4640      0   -125      2       C  
ATOM   1156  CG2 ILE A 154      99.393 -19.718  21.582  1.00 26.75           C  
ANISOU 1156  CG2 ILE A 154     3255   3277   3632      3    -69    -16       C  
ATOM   1157  CD1 ILE A 154      96.303 -19.250  21.142  1.00 40.59           C  
ANISOU 1157  CD1 ILE A 154     4965   4898   5558     -5    -85     37       C  
ATOM   1158  N   GLU A 155     101.304 -22.350  21.145  1.00 20.04           N  
ANISOU 1158  N   GLU A 155     2397   2319   2898     13   -128    -53       N  
ATOM   1159  CA  GLU A 155     102.609 -22.814  21.625  1.00 33.33           C  
ANISOU 1159  CA  GLU A 155     4054   4071   4540     13   -136    -49       C  
ATOM   1160  C   GLU A 155     103.423 -21.723  22.282  1.00 35.79           C  
ANISOU 1160  C   GLU A 155     4425   4408   4765     12    -92    -47       C  
ATOM   1161  O   GLU A 155     104.373 -21.997  23.033  1.00 36.12           O  
ANISOU 1161  O   GLU A 155     4500   4507   4717      7    -62    -25       O  
ATOM   1162  CB  GLU A 155     103.434 -23.364  20.461  1.00 29.88           C  
ANISOU 1162  CB  GLU A 155     3652   3575   4127     28   -147    -98       C  
ATOM   1163  CG  GLU A 155     102.815 -24.544  19.747  1.00 21.16           C  
ANISOU 1163  CG  GLU A 155     2497   2381   3162     36   -212   -122       C  
ATOM   1164  CD  GLU A 155     102.031 -24.089  18.523  1.00 51.10           C  
ANISOU 1164  CD  GLU A 155     6204   6241   6970     41   -238   -145       C  
ATOM   1165  OE1 GLU A 155     101.752 -22.863  18.443  1.00 39.53           O  
ANISOU 1165  OE1 GLU A 155     4778   4822   5421     37   -188   -138       O  
ATOM   1166  OE2 GLU A 155     101.693 -24.935  17.656  1.00 36.50           O  
ANISOU 1166  OE2 GLU A 155     4304   4345   5221     52   -294   -177       O  
ATOM   1167  N   TRP A 156     103.032 -20.477  22.022  1.00 32.97           N  
ANISOU 1167  N   TRP A 156     4133   4116   4276      7    -34    -29       N  
ATOM   1168  CA  TRP A 156     103.910 -19.367  22.296  1.00 19.30           C  
ANISOU 1168  CA  TRP A 156     2444   2444   2444      0      0      0       C  
ATOM   1169  C   TRP A 156     103.103 -18.242  22.970  1.00 29.18           C  
ANISOU 1169  C   TRP A 156     3695   3695   3695      0      0      0       C  
ATOM   1170  O   TRP A 156     102.164 -17.675  22.408  1.00 14.10           O  
ANISOU 1170  O   TRP A 156     1786   1786   1786      0      0      0       O  
ATOM   1171  CB  TRP A 156     104.562 -18.939  20.967  1.00 32.30           C  
ANISOU 1171  CB  TRP A 156     4091   4091   4091      0      0      0       C  
ATOM   1172  CG  TRP A 156     105.423 -17.727  20.975  1.00 33.72           C  
ANISOU 1172  CG  TRP A 156     4271   4271   4271      0      0      0       C  
ATOM   1173  CD1 TRP A 156     105.982 -17.120  22.057  1.00 29.46           C  
ANISOU 1173  CD1 TRP A 156     3732   3732   3732      0      0      0       C  
ATOM   1174  CD2 TRP A 156     105.820 -16.966  19.836  1.00 20.67           C  
ANISOU 1174  CD2 TRP A 156     2618   2618   2618      0      0      0       C  
ATOM   1175  NE1 TRP A 156     106.719 -16.039  21.662  1.00 25.84           N  
ANISOU 1175  NE1 TRP A 156     3272   3272   3272      0      0      0       N  
ATOM   1176  CE2 TRP A 156     106.617 -15.904  20.303  1.00 25.51           C  
ANISOU 1176  CE2 TRP A 156     3231   3231   3231      0      0      0       C  
ATOM   1177  CE3 TRP A 156     105.570 -17.071  18.462  1.00 17.21           C  
ANISOU 1177  CE3 TRP A 156     2179   2179   2179      0      0      0       C  
ATOM   1178  CZ2 TRP A 156     107.167 -14.949  19.449  1.00 17.59           C  
ANISOU 1178  CZ2 TRP A 156     2228   2228   2228      0      0      0       C  
ATOM   1179  CZ3 TRP A 156     106.131 -16.126  17.610  1.00 24.24           C  
ANISOU 1179  CZ3 TRP A 156     3070   3070   3070      0      0      0       C  
ATOM   1180  CH2 TRP A 156     106.918 -15.081  18.109  1.00 22.23           C  
ANISOU 1180  CH2 TRP A 156     2815   2815   2815      0      0      0       C  
ATOM   1181  N   SER A 157     103.527 -17.868  24.167  1.00 27.73           N  
ANISOU 1181  N   SER A 157     3512   3512   3512      0      0      0       N  
ATOM   1182  CA  SER A 157     102.806 -16.845  24.893  1.00 39.52           C  
ANISOU 1182  CA  SER A 157     5005   5005   5005      0      0      0       C  
ATOM   1183  C   SER A 157     103.756 -15.716  25.288  1.00 37.91           C  
ANISOU 1183  C   SER A 157     4802   4802   4802      0      0      0       C  
ATOM   1184  O   SER A 157     104.918 -15.962  25.661  1.00 22.06           O  
ANISOU 1184  O   SER A 157     2795   2795   2795      0      0      0       O  
ATOM   1185  CB  SER A 157     102.141 -17.428  26.146  1.00 27.43           C  
ANISOU 1185  CB  SER A 157     3474   3474   3474      0      0      0       C  
ATOM   1186  OG  SER A 157     103.091 -18.099  26.966  1.00 34.45           O  
ANISOU 1186  OG  SER A 157     4364   4364   4364      0      0      0       O  
ATOM   1187  N   PHE A 158     103.244 -14.484  25.203  1.00 31.32           N  
ANISOU 1187  N   PHE A 158     3966   3966   3966      0      0      0       N  
ATOM   1188  CA  PHE A 158     104.014 -13.288  25.540  1.00 16.72           C  
ANISOU 1188  CA  PHE A 158     2118   2118   2118      0      0      0       C  
ATOM   1189  C   PHE A 158     103.793 -12.951  27.007  1.00 24.63           C  
ANISOU 1189  C   PHE A 158     3119   3119   3119      0      0      0       C  
ATOM   1190  O   PHE A 158     102.738 -12.449  27.382  1.00 32.91           O  
ANISOU 1190  O   PHE A 158     4168   4168   4168      0      0      0       O  
ATOM   1191  CB  PHE A 158     103.628 -12.090  24.660  1.00 14.71           C  
ANISOU 1191  CB  PHE A 158     1863   1863   1863      0      0      0       C  
ATOM   1192  CG  PHE A 158     103.527 -12.402  23.196  1.00 21.62           C  
ANISOU 1192  CG  PHE A 158     2738   2738   2738      0      0      0       C  
ATOM   1193  CD1 PHE A 158     102.673 -11.675  22.385  1.00 17.69           C  
ANISOU 1193  CD1 PHE A 158     2241   2241   2241      0      0      0       C  
ATOM   1194  CD2 PHE A 158     104.350 -13.347  22.608  1.00 23.16           C  
ANISOU 1194  CD2 PHE A 158     2933   2933   2933      0      0      0       C  
ATOM   1195  CE1 PHE A 158     102.582 -11.940  21.024  1.00 22.91           C  
ANISOU 1195  CE1 PHE A 158     2901   2901   2901      0      0      0       C  
ATOM   1196  CE2 PHE A 158     104.270 -13.613  21.252  1.00 29.64           C  
ANISOU 1196  CE2 PHE A 158     3754   3754   3754      0      0      0       C  
ATOM   1197  CZ  PHE A 158     103.385 -12.910  20.456  1.00 23.59           C  
ANISOU 1197  CZ  PHE A 158     2988   2988   2988      0      0      0       C  
ATOM   1198  N   ALA A 159     104.814 -13.213  27.815  1.00 20.05           N  
ANISOU 1198  N   ALA A 159     2539   2539   2539      0      0      0       N  
ATOM   1199  CA  ALA A 159     104.818 -12.893  29.231  1.00 24.10           C  
ANISOU 1199  CA  ALA A 159     3053   3053   3053      0      0      0       C  
ATOM   1200  C   ALA A 159     106.176 -13.354  29.707  1.00 20.85           C  
ANISOU 1200  C   ALA A 159     2641   2641   2641      0      0      0       C  
ATOM   1201  O   ALA A 159     106.730 -14.275  29.136  1.00 20.49           O  
ANISOU 1201  O   ALA A 159     2595   2595   2595      0      0      0       O  
ATOM   1202  CB  ALA A 159     103.725 -13.633  29.953  1.00 17.56           C  
ANISOU 1202  CB  ALA A 159     2224   2224   2224      0      0      0       C  
ATOM   1203  N   PRO A 160     106.750 -12.681  30.714  1.00 17.63           N  
ANISOU 1203  N   PRO A 160     2233   2233   2233      0      0      0       N  
ATOM   1204  CA  PRO A 160     106.215 -11.580  31.521  1.00 18.88           C  
ANISOU 1204  CA  PRO A 160     2391   2391   2391      0      0      0       C  
ATOM   1205  C   PRO A 160     106.359 -10.203  30.872  1.00 35.92           C  
ANISOU 1205  C   PRO A 160     4550   4550   4550      0      0      0       C  
ATOM   1206  O   PRO A 160     107.075 -10.050  29.883  1.00 17.17           O  
ANISOU 1206  O   PRO A 160     2174   2174   2174      0      0      0       O  
ATOM   1207  CB  PRO A 160     107.101 -11.612  32.757  1.00 22.29           C  
ANISOU 1207  CB  PRO A 160     2823   2823   2823      0      0      0       C  
ATOM   1208  CG  PRO A 160     108.423 -12.027  32.207  1.00 20.75           C  
ANISOU 1208  CG  PRO A 160     2629   2629   2629      0      0      0       C  
ATOM   1209  CD  PRO A 160     108.103 -13.066  31.157  1.00 24.21           C  
ANISOU 1209  CD  PRO A 160     3066   3066   3066      0      0      0       C  
ATOM   1210  N   THR A 161     105.691  -9.211  31.447  1.00 31.32           N  
ANISOU 1210  N   THR A 161     3966   3966   3966      0      0      0       N  
ATOM   1211  CA  THR A 161     105.942  -7.826  31.092  1.00 30.37           C  
ANISOU 1211  CA  THR A 161     3847   3847   3847      0      0      0       C  
ATOM   1212  C   THR A 161     106.809  -7.237  32.179  1.00 33.19           C  
ANISOU 1212  C   THR A 161     4204   4204   4204      0      0      0       C  
ATOM   1213  O   THR A 161     106.378  -7.127  33.326  1.00 21.44           O  
ANISOU 1213  O   THR A 161     2715   2715   2715      0      0      0       O  
ATOM   1214  CB  THR A 161     104.654  -7.002  31.045  1.00 29.07           C  
ANISOU 1214  CB  THR A 161     3681   3681   3681      0      0      0       C  
ATOM   1215  OG1 THR A 161     103.818  -7.485  29.989  1.00 25.88           O  
ANISOU 1215  OG1 THR A 161     3277   3277   3277      0      0      0       O  
ATOM   1216  CG2 THR A 161     104.984  -5.502  30.807  1.00 21.28           C  
ANISOU 1216  CG2 THR A 161     2695   2695   2695      0      0      0       C  
ATOM   1217  N   VAL A 162     107.981  -6.748  31.805  1.00 26.02           N  
ANISOU 1217  N   VAL A 162     3296   3296   3296      0      0      0       N  
ATOM   1218  CA  VAL A 162     108.979  -6.352  32.799  1.00 12.71           C  
ANISOU 1218  CA  VAL A 162     1609   1609   1609      0      0      0       C  
ATOM   1219  C   VAL A 162     109.299  -4.849  32.827  1.00 37.29           C  
ANISOU 1219  C   VAL A 162     4723   4723   4723      0      0      0       C  
ATOM   1220  O   VAL A 162     110.374  -4.430  33.258  1.00 42.12           O  
ANISOU 1220  O   VAL A 162     5335   5335   5335      0      0      0       O  
ATOM   1221  CB  VAL A 162     110.252  -7.200  32.641  1.00 27.15           C  
ANISOU 1221  CB  VAL A 162     3439   3439   3439      0      0      0       C  
ATOM   1222  CG1 VAL A 162     109.943  -8.686  32.813  1.00 26.24           C  
ANISOU 1222  CG1 VAL A 162     3323   3323   3323      0      0      0       C  
ATOM   1223  CG2 VAL A 162     110.915  -6.898  31.328  1.00 17.06           C  
ANISOU 1223  CG2 VAL A 162     2161   2161   2161      0      0      0       C  
ATOM   1224  N   ALA A 163     108.359  -4.046  32.346  1.00 16.84           N  
ANISOU 1224  N   ALA A 163     2132   2132   2132      0      0      0       N  
ATOM   1225  CA  ALA A 163     108.491  -2.596  32.415  1.00 33.57           C  
ANISOU 1225  CA  ALA A 163     4251   4251   4251      0      0      0       C  
ATOM   1226  C   ALA A 163     108.626  -2.160  33.866  1.00 33.30           C  
ANISOU 1226  C   ALA A 163     4217   4217   4217      0      0      0       C  
ATOM   1227  O   ALA A 163     107.997  -2.714  34.768  1.00 21.59           O  
ANISOU 1227  O   ALA A 163     2735   2735   2735      0      0      0       O  
ATOM   1228  CB  ALA A 163     107.294  -1.909  31.761  1.00 18.82           C  
ANISOU 1228  CB  ALA A 163     2383   2383   2383      0      0      0       C  
ATOM   1229  N   VAL A 164     109.409  -1.117  34.072  1.00 21.12           N  
ANISOU 1229  N   VAL A 164     2674   2674   2674      0      0      0       N  
ATOM   1230  CA  VAL A 164     109.568  -0.533  35.386  1.00 20.15           C  
ANISOU 1230  CA  VAL A 164     2551   2551   2551      0      0      0       C  
ATOM   1231  C   VAL A 164     109.036   0.897  35.317  1.00 31.02           C  
ANISOU 1231  C   VAL A 164     3928   3928   3928      0      0      0       C  
ATOM   1232  O   VAL A 164     109.686   1.758  34.733  1.00 24.51           O  
ANISOU 1232  O   VAL A 164     3104   3104   3104      0      0      0       O  
ATOM   1233  CB  VAL A 164     111.042  -0.523  35.782  1.00 26.94           C  
ANISOU 1233  CB  VAL A 164     3412   3412   3412      0      0      0       C  
ATOM   1234  CG1 VAL A 164     111.246   0.061  37.151  1.00  3.89           C  
ANISOU 1234  CG1 VAL A 164      492    492    492      0      0      0       C  
ATOM   1235  CG2 VAL A 164     111.612  -1.934  35.693  1.00 18.03           C  
ANISOU 1235  CG2 VAL A 164     2283   2283   2283      0      0      0       C  
ATOM   1236  N   VAL A 165     107.829   1.136  35.831  1.00 20.94           N  
ANISOU 1236  N   VAL A 165     2652   2652   2652      0      0      0       N  
ATOM   1237  CA  VAL A 165     107.114   2.380  35.518  1.00 36.55           C  
ANISOU 1237  CA  VAL A 165     4630   4630   4630      0      0      0       C  
ATOM   1238  C   VAL A 165     107.412   3.512  36.500  1.00 38.48           C  
ANISOU 1238  C   VAL A 165     4874   4874   4874      0      0      0       C  
ATOM   1239  O   VAL A 165     107.186   3.394  37.701  1.00 39.68           O  
ANISOU 1239  O   VAL A 165     5025   5025   5025      0      0      0       O  
ATOM   1240  CB  VAL A 165     105.593   2.119  35.423  1.00 37.94           C  
ANISOU 1240  CB  VAL A 165     4805   4805   4805      0      0      0       C  
ATOM   1241  CG1 VAL A 165     104.810   3.425  35.272  1.00 25.78           C  
ANISOU 1241  CG1 VAL A 165     3266   3266   3266      0      0      0       C  
ATOM   1242  CG2 VAL A 165     105.303   1.182  34.260  1.00 21.49           C  
ANISOU 1242  CG2 VAL A 165     2722   2722   2722      0      0      0       C  
ATOM   1243  N   ARG A 166     107.842   4.644  35.949  1.00 35.46           N  
ANISOU 1243  N   ARG A 166     4491   4491   4491      0      0      0       N  
ATOM   1244  CA  ARG A 166     108.338   5.756  36.753  1.00 45.58           C  
ANISOU 1244  CA  ARG A 166     5773   5773   5773      0      0      0       C  
ATOM   1245  C   ARG A 166     107.400   6.952  36.783  1.00 31.28           C  
ANISOU 1245  C   ARG A 166     3961   3961   3961      0      0      0       C  
ATOM   1246  O   ARG A 166     107.550   7.846  37.619  1.00 23.06           O  
ANISOU 1246  O   ARG A 166     2933   2912   2915      3     13      1       O  
ATOM   1247  CB  ARG A 166     109.721   6.202  36.234  1.00 31.27           C  
ANISOU 1247  CB  ARG A 166     3961   3961   3961      0      0      0       C  
ATOM   1248  CG  ARG A 166     110.725   5.051  36.053  1.00 24.81           C  
ANISOU 1248  CG  ARG A 166     3142   3142   3142      0      0      0       C  
ATOM   1249  CD  ARG A 166     111.109   4.474  37.396  1.00 25.63           C  
ANISOU 1249  CD  ARG A 166     3246   3246   3246      0      0      0       C  
ATOM   1250  NE  ARG A 166     112.040   5.331  38.108  1.00 29.66           N  
ANISOU 1250  NE  ARG A 166     3757   3757   3757      0      0      0       N  
ATOM   1251  CZ  ARG A 166     112.580   5.026  39.282  1.00 38.96           C  
ANISOU 1251  CZ  ARG A 166     4935   4935   4935      0      0      0       C  
ATOM   1252  NH1 ARG A 166     112.229   3.914  39.910  1.00 33.27           N  
ANISOU 1252  NH1 ARG A 166     4213   4213   4213      0      0      0       N  
ATOM   1253  NH2 ARG A 166     113.434   5.856  39.856  1.00 31.39           N  
ANISOU 1253  NH2 ARG A 166     3975   3975   3975      0      0      0       N  
ATOM   1254  N   ASP A 167     106.403   6.941  35.911  1.00 29.04           N  
ANISOU 1254  N   ASP A 167     3678   3678   3678      0      0      0       N  
ATOM   1255  CA  ASP A 167     105.413   8.017  35.847  1.00 34.39           C  
ANISOU 1255  CA  ASP A 167     4357   4355   4356      1      1      0       C  
ATOM   1256  C   ASP A 167     104.048   7.396  35.609  1.00 29.18           C  
ANISOU 1256  C   ASP A 167     3711   3682   3692     14     19      8       C  
ATOM   1257  O   ASP A 167     103.792   6.835  34.543  1.00 38.15           O  
ANISOU 1257  O   ASP A 167     4832   4832   4832      0      0      0       O  
ATOM   1258  CB  ASP A 167     105.771   9.004  34.730  1.00 34.84           C  
ANISOU 1258  CB  ASP A 167     4412   4412   4412      0      0      0       C  
ATOM   1259  CG  ASP A 167     104.910  10.277  34.759  1.00 44.57           C  
ANISOU 1259  CG  ASP A 167     5665   5628   5641     13     21      7       C  
ATOM   1260  OD1 ASP A 167     103.687  10.188  35.037  1.00 29.76           O  
ANISOU 1260  OD1 ASP A 167     3826   3723   3758     46     65     25       O  
ATOM   1261  OD2 ASP A 167     105.469  11.379  34.544  1.00 45.37           O  
ANISOU 1261  OD2 ASP A 167     5769   5728   5742     12     22      7       O  
ATOM   1262  N   ASP A 168     103.187   7.472  36.622  1.00 26.96           N  
ANISOU 1262  N   ASP A 168     3482   3373   3389     55     93     39       N  
ATOM   1263  CA  ASP A 168     101.926   6.736  36.616  1.00 19.96           C  
ANISOU 1263  CA  ASP A 168     2603   2483   2498     81    122     61       C  
ATOM   1264  C   ASP A 168     100.882   7.262  35.645  1.00 36.09           C  
ANISOU 1264  C   ASP A 168     4642   4531   4540     93    129     73       C  
ATOM   1265  O   ASP A 168      99.830   6.653  35.465  1.00 42.22           O  
ANISOU 1265  O   ASP A 168     5413   5290   5339    133    136     87       O  
ATOM   1266  CB  ASP A 168     101.329   6.695  38.022  1.00 14.33           C  
ANISOU 1266  CB  ASP A 168     1978   1692   1777    182    255    124       C  
ATOM   1267  CG  ASP A 168     102.220   5.983  39.018  1.00 40.54           C  
ANISOU 1267  CG  ASP A 168     5311   5001   5094    169    253    111       C  
ATOM   1268  OD1 ASP A 168     103.130   5.233  38.596  1.00 32.66           O  
ANISOU 1268  OD1 ASP A 168     4230   4076   4102     80    137     58       O  
ATOM   1269  OD2 ASP A 168     102.026   6.205  40.237  1.00 30.93           O  
ANISOU 1269  OD2 ASP A 168     4104   3752   3896    178    248    104       O  
ATOM   1270  N   ARG A 169     101.192   8.360  34.970  1.00 39.43           N  
ANISOU 1270  N   ARG A 169     5060   4957   4964     80    112     61       N  
ATOM   1271  CA  ARG A 169     100.299   8.879  33.948  1.00 33.59           C  
ANISOU 1271  CA  ARG A 169     4333   4204   4227    125    142     87       C  
ATOM   1272  C   ARG A 169     100.211   7.941  32.744  1.00 22.24           C  
ANISOU 1272  C   ARG A 169     2839   2801   2809     56     50     36       C  
ATOM   1273  O   ARG A 169      99.306   8.084  31.921  1.00 32.04           O  
ANISOU 1273  O   ARG A 169     4078   4047   4050     67     55     44       O  
ATOM   1274  CB  ARG A 169     100.718  10.275  33.513  1.00 26.44           C  
ANISOU 1274  CB  ARG A 169     3414   3314   3316     84    111     63       C  
ATOM   1275  CG  ARG A 169     100.402  11.323  34.569  1.00 47.21           C  
ANISOU 1275  CG  ARG A 169     6097   5910   5929    129    189     97       C  
ATOM   1276  CD  ARG A 169     100.906  12.671  34.134  1.00 41.42           C  
ANISOU 1276  CD  ARG A 169     5371   5172   5194    122    186     88       C  
ATOM   1277  NE  ARG A 169     102.343  12.762  34.307  1.00 37.09           N  
ANISOU 1277  NE  ARG A 169     4808   4631   4653     88    147     61       N  
ATOM   1278  CZ  ARG A 169     103.043  13.877  34.156  1.00 45.61           C  
ANISOU 1278  CZ  ARG A 169     5898   5679   5755     94    134     50       C  
ATOM   1279  NH1 ARG A 169     102.423  15.026  33.918  1.00 54.85           N  
ANISOU 1279  NH1 ARG A 169     7097   6823   6919    123    172     66       N  
ATOM   1280  NH2 ARG A 169     104.356  13.861  34.328  1.00 37.70           N  
ANISOU 1280  NH2 ARG A 169     4876   4693   4755     61    102     35       N  
ATOM   1281  N   TRP A 170     101.193   7.049  32.599  1.00 28.40           N  
ANISOU 1281  N   TRP A 170     3598   3597   3597      2      2      1       N  
ATOM   1282  CA  TRP A 170     101.201   6.088  31.489  1.00 28.82           C  
ANISOU 1282  CA  TRP A 170     3651   3651   3651      0      0      0       C  
ATOM   1283  C   TRP A 170      99.995   5.175  31.583  1.00 22.21           C  
ANISOU 1283  C   TRP A 170     2814   2814   2814      0      0      0       C  
ATOM   1284  O   TRP A 170      99.704   4.645  32.641  1.00 29.07           O  
ANISOU 1284  O   TRP A 170     3686   3684   3675     19     18     17       O  
ATOM   1285  CB  TRP A 170     102.461   5.238  31.541  1.00 25.81           C  
ANISOU 1285  CB  TRP A 170     3269   3269   3269      0      0      0       C  
ATOM   1286  CG  TRP A 170     102.746   4.435  30.291  1.00 32.60           C  
ANISOU 1286  CG  TRP A 170     4129   4129   4129      0      0      0       C  
ATOM   1287  CD1 TRP A 170     102.362   4.725  29.017  1.00 32.11           C  
ANISOU 1287  CD1 TRP A 170     4067   4067   4067      0      0      0       C  
ATOM   1288  CD2 TRP A 170     103.507   3.220  30.213  1.00 21.86           C  
ANISOU 1288  CD2 TRP A 170     2769   2769   2769      0      0      0       C  
ATOM   1289  NE1 TRP A 170     102.833   3.765  28.146  1.00 26.94           N  
ANISOU 1289  NE1 TRP A 170     3412   3412   3412      0      0      0       N  
ATOM   1290  CE2 TRP A 170     103.535   2.829  28.859  1.00 21.67           C  
ANISOU 1290  CE2 TRP A 170     2744   2744   2744      0      0      0       C  
ATOM   1291  CE3 TRP A 170     104.155   2.422  31.161  1.00 19.97           C  
ANISOU 1291  CE3 TRP A 170     2530   2530   2530      0      0      0       C  
ATOM   1292  CZ2 TRP A 170     104.183   1.679  28.429  1.00 29.68           C  
ANISOU 1292  CZ2 TRP A 170     3759   3759   3759      0      0      0       C  
ATOM   1293  CZ3 TRP A 170     104.804   1.286  30.729  1.00 21.56           C  
ANISOU 1293  CZ3 TRP A 170     2731   2731   2731      0      0      0       C  
ATOM   1294  CH2 TRP A 170     104.812   0.923  29.374  1.00 30.71           C  
ANISOU 1294  CH2 TRP A 170     3889   3889   3889      0      0      0       C  
ATOM   1295  N   GLY A 171      99.288   5.007  30.471  1.00 32.14           N  
ANISOU 1295  N   GLY A 171     4071   4071   4071      0      0      0       N  
ATOM   1296  CA  GLY A 171      98.149   4.104  30.415  1.00 35.13           C  
ANISOU 1296  CA  GLY A 171     4448   4452   4448      8      5      7       C  
ATOM   1297  C   GLY A 171      98.445   2.618  30.527  1.00 43.04           C  
ANISOU 1297  C   GLY A 171     5451   5451   5451      0      0      0       C  
ATOM   1298  O   GLY A 171      97.535   1.786  30.590  1.00 24.01           O  
ANISOU 1298  O   GLY A 171     3038   3049   3036     13     10     15       O  
ATOM   1299  N   ARG A 172      99.724   2.280  30.572  1.00 27.87           N  
ANISOU 1299  N   ARG A 172     3530   3530   3530      0      0      0       N  
ATOM   1300  CA  ARG A 172     100.128   0.893  30.735  1.00 28.07           C  
ANISOU 1300  CA  ARG A 172     3555   3555   3555      0      0      0       C  
ATOM   1301  C   ARG A 172     100.779   0.591  32.067  1.00 36.82           C  
ANISOU 1301  C   ARG A 172     4663   4663   4663      0      0      0       C  
ATOM   1302  O   ARG A 172     101.385  -0.460  32.233  1.00 29.78           O  
ANISOU 1302  O   ARG A 172     3772   3772   3772      0      0      0       O  
ATOM   1303  CB  ARG A 172     101.043   0.491  29.574  1.00 18.94           C  
ANISOU 1303  CB  ARG A 172     2399   2399   2399      0      0      0       C  
ATOM   1304  CG  ARG A 172     100.475   0.875  28.214  1.00 20.21           C  
ANISOU 1304  CG  ARG A 172     2560   2560   2560      0      0      0       C  
ATOM   1305  CD  ARG A 172     101.223   0.242  27.062  1.00 26.97           C  
ANISOU 1305  CD  ARG A 172     3416   3416   3416      0      0      0       C  
ATOM   1306  NE  ARG A 172     100.990  -1.190  27.005  1.00 28.12           N  
ANISOU 1306  NE  ARG A 172     3561   3561   3561      0      0      0       N  
ATOM   1307  CZ  ARG A 172     101.369  -1.967  26.000  1.00 38.22           C  
ANISOU 1307  CZ  ARG A 172     4841   4841   4841      0      0      0       C  
ATOM   1308  NH1 ARG A 172     101.956  -1.439  24.940  1.00 25.02           N  
ANISOU 1308  NH1 ARG A 172     3169   3169   3169      0      0      0       N  
ATOM   1309  NH2 ARG A 172     101.122  -3.269  26.036  1.00 37.80           N  
ANISOU 1309  NH2 ARG A 172     4788   4788   4788      0      0      0       N  
ATOM   1310  N   THR A 173     100.612   1.502  33.019  1.00 18.50           N  
ANISOU 1310  N   THR A 173     2344   2344   2344      0      0      0       N  
ATOM   1311  CA  THR A 173     101.186   1.339  34.354  1.00 26.44           C  
ANISOU 1311  CA  THR A 173     3348   3348   3348      0      0      0       C  
ATOM   1312  C   THR A 173     100.827   0.009  35.044  1.00 28.33           C  
ANISOU 1312  C   THR A 173     3588   3589   3587      8      6      6       C  
ATOM   1313  O   THR A 173     101.655  -0.575  35.730  1.00 28.51           O  
ANISOU 1313  O   THR A 173     3610   3610   3610      0      0      0       O  
ATOM   1314  CB  THR A 173     100.782   2.523  35.257  1.00 25.03           C  
ANISOU 1314  CB  THR A 173     3179   3163   3167     42     36     30       C  
ATOM   1315  OG1 THR A 173     101.342   3.743  34.744  1.00 47.00           O  
ANISOU 1315  OG1 THR A 173     5959   5949   5951     19     16     13       O  
ATOM   1316  CG2 THR A 173     101.274   2.323  36.681  1.00 22.62           C  
ANISOU 1316  CG2 THR A 173     2893   2853   2850     60     72     52       C  
ATOM   1317  N   TYR A 174      99.586  -0.434  34.903  1.00 24.93           N  
ANISOU 1317  N   TYR A 174     3151   3165   3156     49     37     43       N  
ATOM   1318  CA  TYR A 174      99.140  -1.630  35.591  1.00 27.67           C  
ANISOU 1318  CA  TYR A 174     3497   3521   3493     69     69     83       C  
ATOM   1319  C   TYR A 174      99.790  -2.891  35.049  1.00 37.42           C  
ANISOU 1319  C   TYR A 174     4727   4751   4738     32     22     32       C  
ATOM   1320  O   TYR A 174      99.743  -3.924  35.689  1.00 38.92           O  
ANISOU 1320  O   TYR A 174     4916   4950   4922     42     39     59       O  
ATOM   1321  CB  TYR A 174      97.616  -1.759  35.560  1.00 27.97           C  
ANISOU 1321  CB  TYR A 174     3524   3568   3537    115    124    150       C  
ATOM   1322  CG  TYR A 174      96.989  -1.928  34.191  1.00 26.30           C  
ANISOU 1322  CG  TYR A 174     3287   3361   3345    116     92    125       C  
ATOM   1323  CD1 TYR A 174      96.979  -3.153  33.558  1.00 11.35           C  
ANISOU 1323  CD1 TYR A 174     1383   1486   1442    109     94    148       C  
ATOM   1324  CD2 TYR A 174      96.368  -0.858  33.551  1.00 30.56           C  
ANISOU 1324  CD2 TYR A 174     3844   3905   3863    107    110    146       C  
ATOM   1325  CE1 TYR A 174      96.395  -3.315  32.312  1.00 22.84           C  
ANISOU 1325  CE1 TYR A 174     2843   2934   2903     76     55     98       C  
ATOM   1326  CE2 TYR A 174      95.772  -1.010  32.306  1.00 20.26           C  
ANISOU 1326  CE2 TYR A 174     2516   2604   2577    111     85    125       C  
ATOM   1327  CZ  TYR A 174      95.795  -2.236  31.690  1.00 32.81           C  
ANISOU 1327  CZ  TYR A 174     4119   4198   4149     72     68    115       C  
ATOM   1328  OH  TYR A 174      95.199  -2.378  30.458  1.00 33.01           O  
ANISOU 1328  OH  TYR A 174     4127   4227   4188     74     52     98       O  
ATOM   1329  N   GLU A 175     100.408  -2.802  33.879  1.00 37.37           N  
ANISOU 1329  N   GLU A 175     4733   4733   4733      0      0      0       N  
ATOM   1330  CA  GLU A 175     101.075  -3.956  33.304  1.00 24.76           C  
ANISOU 1330  CA  GLU A 175     3135   3135   3135      0      0      0       C  
ATOM   1331  C   GLU A 175     102.445  -4.185  33.952  1.00 32.33           C  
ANISOU 1331  C   GLU A 175     4095   4095   4095      0      0      0       C  
ATOM   1332  O   GLU A 175     103.153  -5.124  33.601  1.00 33.16           O  
ANISOU 1332  O   GLU A 175     4199   4199   4199      0      0      0       O  
ATOM   1333  CB  GLU A 175     101.234  -3.788  31.786  1.00 20.62           C  
ANISOU 1333  CB  GLU A 175     2612   2612   2612      0      0      0       C  
ATOM   1334  CG  GLU A 175      99.920  -3.611  31.046  1.00 33.70           C  
ANISOU 1334  CG  GLU A 175     4268   4268   4268      0      0      0       C  
ATOM   1335  CD  GLU A 175     100.114  -3.336  29.572  1.00 36.03           C  
ANISOU 1335  CD  GLU A 175     4563   4563   4563      0      0      0       C  
ATOM   1336  OE1 GLU A 175     101.078  -3.868  28.990  1.00 28.17           O  
ANISOU 1336  OE1 GLU A 175     3568   3568   3568      0      0      0       O  
ATOM   1337  OE2 GLU A 175      99.298  -2.600  28.986  1.00 28.42           O  
ANISOU 1337  OE2 GLU A 175     3600   3600   3600      0      0      0       O  
ATOM   1338  N   SER A 176     102.842  -3.285  34.844  1.00 22.35           N  
ANISOU 1338  N   SER A 176     2831   2831   2831      0      0      0       N  
ATOM   1339  CA  SER A 176     104.156  -3.364  35.494  1.00 34.79           C  
ANISOU 1339  CA  SER A 176     4406   4406   4406      0      0      0       C  
ATOM   1340  C   SER A 176     104.030  -3.831  36.952  1.00 29.62           C  
ANISOU 1340  C   SER A 176     3752   3752   3752      0      0      0       C  
ATOM   1341  O   SER A 176     103.090  -3.476  37.649  1.00 29.50           O  
ANISOU 1341  O   SER A 176     3736   3736   3736      0      0      0       O  
ATOM   1342  CB  SER A 176     104.839  -1.977  35.459  1.00 26.18           C  
ANISOU 1342  CB  SER A 176     3315   3315   3315      0      0      0       C  
ATOM   1343  OG  SER A 176     106.044  -1.960  36.210  1.00 19.97           O  
ANISOU 1343  OG  SER A 176     2529   2529   2529      0      0      0       O  
ATOM   1344  N   TYR A 177     104.951  -4.679  37.382  1.00 27.20           N  
ANISOU 1344  N   TYR A 177     3445   3445   3445      0      0      0       N  
ATOM   1345  CA  TYR A 177     104.977  -5.168  38.751  1.00 29.22           C  
ANISOU 1345  CA  TYR A 177     3701   3701   3701      0      0      0       C  
ATOM   1346  C   TYR A 177     105.333  -4.104  39.780  1.00 37.33           C  
ANISOU 1346  C   TYR A 177     4729   4729   4729      0      0      0       C  
ATOM   1347  O   TYR A 177     104.904  -4.196  40.930  1.00 43.72           O  
ANISOU 1347  O   TYR A 177     5551   5527   5536     40     37     28       O  
ATOM   1348  CB  TYR A 177     105.980  -6.301  38.900  1.00 16.38           C  
ANISOU 1348  CB  TYR A 177     2074   2074   2074      0      0      0       C  
ATOM   1349  CG  TYR A 177     105.647  -7.529  38.099  1.00 19.72           C  
ANISOU 1349  CG  TYR A 177     2497   2497   2497      0      0      0       C  
ATOM   1350  CD1 TYR A 177     104.504  -8.268  38.380  1.00 38.69           C  
ANISOU 1350  CD1 TYR A 177     4900   4900   4900      0      0      0       C  
ATOM   1351  CD2 TYR A 177     106.515  -8.020  37.135  1.00 37.43           C  
ANISOU 1351  CD2 TYR A 177     4741   4741   4741      0      0      0       C  
ATOM   1352  CE1 TYR A 177     104.196  -9.419  37.683  1.00 19.78           C  
ANISOU 1352  CE1 TYR A 177     2505   2505   2505      0      0      0       C  
ATOM   1353  CE2 TYR A 177     106.220  -9.186  36.430  1.00 30.30           C  
ANISOU 1353  CE2 TYR A 177     3838   3838   3838      0      0      0       C  
ATOM   1354  CZ  TYR A 177     105.056  -9.877  36.714  1.00 22.45           C  
ANISOU 1354  CZ  TYR A 177     2843   2843   2843      0      0      0       C  
ATOM   1355  OH  TYR A 177     104.737 -11.017  36.031  1.00 32.04           O  
ANISOU 1355  OH  TYR A 177     4058   4058   4058      0      0      0       O  
ATOM   1356  N   SER A 178     106.082  -3.080  39.376  1.00 30.01           N  
ANISOU 1356  N   SER A 178     3801   3801   3801      0      0      0       N  
ATOM   1357  CA  SER A 178     106.673  -2.138  40.331  1.00 31.20           C  
ANISOU 1357  CA  SER A 178     3951   3951   3951      0      0      0       C  
ATOM   1358  C   SER A 178     107.291  -0.912  39.675  1.00 38.79           C  
ANISOU 1358  C   SER A 178     4913   4913   4913      0      0      0       C  
ATOM   1359  O   SER A 178     107.610  -0.940  38.487  1.00 33.68           O  
ANISOU 1359  O   SER A 178     4265   4265   4265      0      0      0       O  
ATOM   1360  CB  SER A 178     107.757  -2.857  41.148  1.00 29.54           C  
ANISOU 1360  CB  SER A 178     3741   3741   3741      0      0      0       C  
ATOM   1361  OG  SER A 178     108.328  -2.005  42.119  1.00 34.79           O  
ANISOU 1361  OG  SER A 178     4420   4396   4404      2     11      1       O  
ATOM   1362  N   GLU A 179     107.367   0.200  40.415  1.00 28.56           N  
ANISOU 1362  N   GLU A 179     3618   3618   3618      0      0      0       N  
ATOM   1363  CA  GLU A 179     108.162   1.337  39.965  1.00 31.58           C  
ANISOU 1363  CA  GLU A 179     3999   3999   3999      0      0      0       C  
ATOM   1364  C   GLU A 179     109.674   1.118  40.152  1.00 41.08           C  
ANISOU 1364  C   GLU A 179     5203   5203   5203      0      0      0       C  
ATOM   1365  O   GLU A 179     110.498   1.840  39.614  1.00 33.60           O  
ANISOU 1365  O   GLU A 179     4256   4256   4256      0      0      0       O  
ATOM   1366  CB  GLU A 179     107.746   2.581  40.766  1.00 18.31           C  
ANISOU 1366  CB  GLU A 179     2360   2292   2304      8     40      4       C  
ATOM   1367  CG  GLU A 179     108.132   2.550  42.245  1.00 34.63           C  
ANISOU 1367  CG  GLU A 179     4493   4301   4364     19     88      9       C  
ATOM   1368  CD  GLU A 179     107.520   3.681  43.059  1.00 42.70           C  
ANISOU 1368  CD  GLU A 179     5592   5261   5371     46    157     24       C  
ATOM   1369  OE1 GLU A 179     106.428   4.152  42.696  1.00 33.96           O  
ANISOU 1369  OE1 GLU A 179     4488   4180   4234     66    197     36       O  
ATOM   1370  OE2 GLU A 179     108.142   4.106  44.055  1.00 38.16           O  
ANISOU 1370  OE2 GLU A 179     5059   4692   4747     40    206     20       O  
ATOM   1371  N   ASP A 180     109.988   0.148  40.996  1.00 32.72           N  
ANISOU 1371  N   ASP A 180     4144   4144   4144      0      0      0       N  
ATOM   1372  CA  ASP A 180     111.321  -0.210  41.479  1.00 34.14           C  
ANISOU 1372  CA  ASP A 180     4324   4324   4324      0      0      0       C  
ATOM   1373  C   ASP A 180     111.860  -1.412  40.664  1.00 42.04           C  
ANISOU 1373  C   ASP A 180     5324   5324   5324      0      0      0       C  
ATOM   1374  O   ASP A 180     111.145  -2.402  40.577  1.00 34.55           O  
ANISOU 1374  O   ASP A 180     4376   4376   4376      0      0      0       O  
ATOM   1375  CB  ASP A 180     111.271  -0.608  42.931  1.00 55.26           C  
ANISOU 1375  CB  ASP A 180     7012   6991   6992     -5     10     -2       C  
ATOM   1376  CG  ASP A 180     112.619  -1.021  43.454  1.00 57.20           C  
ANISOU 1376  CG  ASP A 180     7260   7236   7237     -8     10     -3       C  
ATOM   1377  OD1 ASP A 180     113.638  -0.605  42.879  1.00 50.73           O  
ANISOU 1377  OD1 ASP A 180     6425   6425   6425      0      0      0       O  
ATOM   1378  OD2 ASP A 180     112.668  -1.912  44.312  1.00 71.49           O  
ANISOU 1378  OD2 ASP A 180     9094   9036   9033    -19     26     -8       O  
ATOM   1379  N   PRO A 181     113.023  -1.336  40.003  1.00 25.60           N  
ANISOU 1379  N   PRO A 181     3242   3242   3242      0      0      0       N  
ATOM   1380  CA  PRO A 181     113.512  -2.491  39.229  1.00 23.37           C  
ANISOU 1380  CA  PRO A 181     2960   2960   2960      0      0      0       C  
ATOM   1381  C   PRO A 181     113.737  -3.816  40.007  1.00 33.64           C  
ANISOU 1381  C   PRO A 181     4261   4261   4261      0      0      0       C  
ATOM   1382  O   PRO A 181     113.601  -4.868  39.380  1.00 32.79           O  
ANISOU 1382  O   PRO A 181     4153   4153   4153      0      0      0       O  
ATOM   1383  CB  PRO A 181     114.854  -2.014  38.679  1.00 18.11           C  
ANISOU 1383  CB  PRO A 181     2294   2294   2294      0      0      0       C  
ATOM   1384  CG  PRO A 181     115.259  -0.892  39.554  1.00 24.91           C  
ANISOU 1384  CG  PRO A 181     3154   3154   3154      0      0      0       C  
ATOM   1385  CD  PRO A 181     113.991  -0.232  39.997  1.00 29.13           C  
ANISOU 1385  CD  PRO A 181     3689   3689   3689      0      0      0       C  
ATOM   1386  N   ASP A 182     114.063  -3.776  41.301  1.00 38.89           N  
ANISOU 1386  N   ASP A 182     4926   4926   4926      0      0      0       N  
ATOM   1387  CA  ASP A 182     114.368  -4.998  42.076  1.00 41.68           C  
ANISOU 1387  CA  ASP A 182     5279   5279   5279      0      0      0       C  
ATOM   1388  C   ASP A 182     113.273  -6.063  42.136  1.00 30.99           C  
ANISOU 1388  C   ASP A 182     3925   3925   3925      0      0      0       C  
ATOM   1389  O   ASP A 182     113.536  -7.257  41.928  1.00 34.97           O  
ANISOU 1389  O   ASP A 182     4429   4429   4429      0      0      0       O  
ATOM   1390  CB  ASP A 182     114.685  -4.615  43.525  1.00 36.68           C  
ANISOU 1390  CB  ASP A 182     4646   4646   4646      0      0      0       C  
ATOM   1391  CG  ASP A 182     115.949  -3.795  43.649  1.00 74.80           C  
ANISOU 1391  CG  ASP A 182     9473   9473   9473      0      0      0       C  
ATOM   1392  OD1 ASP A 182     116.722  -3.728  42.664  1.00 74.43           O  
ANISOU 1392  OD1 ASP A 182     9427   9427   9427      0      0      0       O  
ATOM   1393  OD2 ASP A 182     116.142  -3.165  44.719  1.00 80.37           O  
ANISOU 1393  OD2 ASP A 182    10186  10177  10173     -7      4     -2       O  
ATOM   1394  N   LEU A 183     112.040  -5.612  42.302  1.00 39.78           N  
ANISOU 1394  N   LEU A 183     5038   5038   5038      0      0      0       N  
ATOM   1395  CA  LEU A 183     110.910  -6.501  42.374  1.00 34.93           C  
ANISOU 1395  CA  LEU A 183     4424   4424   4424      0      0      0       C  
ATOM   1396  C   LEU A 183     110.741  -7.147  41.004  1.00 42.91           C  
ANISOU 1396  C   LEU A 183     5435   5435   5435      0      0      0       C  
ATOM   1397  O   LEU A 183     110.568  -8.365  40.892  1.00 44.42           O  
ANISOU 1397  O   LEU A 183     5626   5626   5626      0      0      0       O  
ATOM   1398  CB  LEU A 183     109.638  -5.779  42.838  1.00 34.68           C  
ANISOU 1398  CB  LEU A 183     4393   4393   4393      0      0      0       C  
ATOM   1399  CG  LEU A 183     108.372  -6.609  43.001  1.00 44.82           C  
ANISOU 1399  CG  LEU A 183     5676   5676   5676      0      0      0       C  
ATOM   1400  CD1 LEU A 183     108.705  -7.860  43.837  1.00 31.67           C  
ANISOU 1400  CD1 LEU A 183     4020   4006   4008      6     11      4       C  
ATOM   1401  CD2 LEU A 183     107.339  -5.808  43.733  1.00 34.06           C  
ANISOU 1401  CD2 LEU A 183     4377   4268   4297     59     86     37       C  
ATOM   1402  N   VAL A 184     110.841  -6.321  39.963  1.00 29.23           N  
ANISOU 1402  N   VAL A 184     3702   3702   3702      0      0      0       N  
ATOM   1403  CA  VAL A 184     110.717  -6.800  38.590  1.00 28.73           C  
ANISOU 1403  CA  VAL A 184     3638   3638   3638      0      0      0       C  
ATOM   1404  C   VAL A 184     111.788  -7.852  38.284  1.00 32.52           C  
ANISOU 1404  C   VAL A 184     4118   4118   4118      0      0      0       C  
ATOM   1405  O   VAL A 184     111.492  -8.848  37.597  1.00 23.83           O  
ANISOU 1405  O   VAL A 184     3019   3019   3019      0      0      0       O  
ATOM   1406  CB  VAL A 184     110.753  -5.614  37.570  1.00 28.78           C  
ANISOU 1406  CB  VAL A 184     3645   3645   3645      0      0      0       C  
ATOM   1407  CG1 VAL A 184     110.717  -6.089  36.124  1.00 12.63           C  
ANISOU 1407  CG1 VAL A 184     1600   1600   1600      0      0      0       C  
ATOM   1408  CG2 VAL A 184     109.572  -4.683  37.824  1.00 21.09           C  
ANISOU 1408  CG2 VAL A 184     2671   2671   2671      0      0      0       C  
ATOM   1409  N   LYS A 185     113.017  -7.638  38.761  1.00 29.58           N  
ANISOU 1409  N   LYS A 185     3746   3746   3746      0      0      0       N  
ATOM   1410  CA  LYS A 185     114.047  -8.643  38.556  1.00 28.03           C  
ANISOU 1410  CA  LYS A 185     3550   3550   3550      0      0      0       C  
ATOM   1411  C   LYS A 185     113.672  -9.957  39.266  1.00 25.54           C  
ANISOU 1411  C   LYS A 185     3235   3235   3235      0      0      0       C  
ATOM   1412  O   LYS A 185     113.792 -11.017  38.672  1.00 26.82           O  
ANISOU 1412  O   LYS A 185     3396   3396   3396      0      0      0       O  
ATOM   1413  CB  LYS A 185     115.420  -8.172  39.039  1.00 39.40           C  
ANISOU 1413  CB  LYS A 185     4990   4990   4990      0      0      0       C  
ATOM   1414  CG  LYS A 185     116.454  -9.273  38.825  1.00 36.09           C  
ANISOU 1414  CG  LYS A 185     4571   4571   4571      0      0      0       C  
ATOM   1415  CD  LYS A 185     117.925  -8.885  38.794  1.00 35.91           C  
ANISOU 1415  CD  LYS A 185     4548   4548   4548      0      0      0       C  
ATOM   1416  CE  LYS A 185     118.445  -8.393  40.119  1.00 70.42           C  
ANISOU 1416  CE  LYS A 185     8919   8919   8919      0      0      0       C  
ATOM   1417  NZ  LYS A 185     119.812  -7.817  39.986  1.00 87.03           N  
ANISOU 1417  NZ  LYS A 185    11023  11023  11023      0      0      0       N  
ATOM   1418  N   ARG A 186     113.202  -9.877  40.520  1.00 33.55           N  
ANISOU 1418  N   ARG A 186     4249   4249   4249      0      0      0       N  
ATOM   1419  CA  ARG A 186     112.807 -11.101  41.229  1.00 30.87           C  
ANISOU 1419  CA  ARG A 186     3909   3909   3909      0      0      0       C  
ATOM   1420  C   ARG A 186     111.708 -11.851  40.511  1.00 32.26           C  
ANISOU 1420  C   ARG A 186     4086   4086   4086      0      0      0       C  
ATOM   1421  O   ARG A 186     111.727 -13.069  40.449  1.00 49.29           O  
ANISOU 1421  O   ARG A 186     6243   6243   6243      0      0      0       O  
ATOM   1422  CB  ARG A 186     112.263 -10.826  42.624  1.00 31.25           C  
ANISOU 1422  CB  ARG A 186     3958   3958   3958      0      0      0       C  
ATOM   1423  CG  ARG A 186     113.283 -10.797  43.724  1.00 45.76           C  
ANISOU 1423  CG  ARG A 186     5796   5796   5796      0      0      0       C  
ATOM   1424  CD  ARG A 186     112.571 -10.493  45.027  1.00 57.50           C  
ANISOU 1424  CD  ARG A 186     7285   7286   7275    -10      1     -1       C  
ATOM   1425  NE  ARG A 186     112.595  -9.120  45.480  1.00 84.95           N  
ANISOU 1425  NE  ARG A 186    10774  10759  10744    -27      7     -5       N  
ATOM   1426  CZ  ARG A 186     111.646  -8.609  46.257  1.00 84.86           C  
ANISOU 1426  CZ  ARG A 186    10815  10717  10713    -53     31    -19       C  
ATOM   1427  NH1 ARG A 186     110.664  -9.384  46.710  1.00 63.09           N  
ANISOU 1427  NH1 ARG A 186     8075   8007   7891    -37     89     34       N  
ATOM   1428  NH2 ARG A 186     111.713  -7.345  46.639  1.00 83.94           N  
ANISOU 1428  NH2 ARG A 186    10746  10565  10581    -55     62    -22       N  
ATOM   1429  N   TYR A 187     110.777 -11.121  39.917  1.00 30.30           N  
ANISOU 1429  N   TYR A 187     3838   3838   3838      0      0      0       N  
ATOM   1430  CA  TYR A 187     109.589 -11.747  39.352  1.00 37.10           C  
ANISOU 1430  CA  TYR A 187     4699   4699   4699      0      0      0       C  
ATOM   1431  C   TYR A 187     109.830 -12.337  37.974  1.00 42.42           C  
ANISOU 1431  C   TYR A 187     5373   5373   5373      0      0      0       C  
ATOM   1432  O   TYR A 187     109.324 -13.428  37.663  1.00 33.89           O  
ANISOU 1432  O   TYR A 187     4292   4292   4292      0      0      0       O  
ATOM   1433  CB  TYR A 187     108.468 -10.718  39.238  1.00 35.10           C  
ANISOU 1433  CB  TYR A 187     4445   4445   4445      0      0      0       C  
ATOM   1434  CG  TYR A 187     107.611 -10.589  40.457  1.00 30.75           C  
ANISOU 1434  CG  TYR A 187     3894   3894   3894      0      0      0       C  
ATOM   1435  CD1 TYR A 187     108.075 -10.994  41.701  1.00 31.24           C  
ANISOU 1435  CD1 TYR A 187     3956   3956   3956      0      0      0       C  
ATOM   1436  CD2 TYR A 187     106.346 -10.050  40.371  1.00 24.82           C  
ANISOU 1436  CD2 TYR A 187     3143   3143   3143      0      0      0       C  
ATOM   1437  CE1 TYR A 187     107.289 -10.873  42.826  1.00 36.58           C  
ANISOU 1437  CE1 TYR A 187     4606   4667   4625     13      7     30       C  
ATOM   1438  CE2 TYR A 187     105.554  -9.920  41.484  1.00 38.23           C  
ANISOU 1438  CE2 TYR A 187     4822   4873   4831     23     16     42       C  
ATOM   1439  CZ  TYR A 187     106.027 -10.335  42.706  1.00 34.67           C  
ANISOU 1439  CZ  TYR A 187     4341   4456   4376     60     40     92       C  
ATOM   1440  OH  TYR A 187     105.229 -10.213  43.809  1.00 37.60           O  
ANISOU 1440  OH  TYR A 187     4699   4831   4758    137    102    170       O  
ATOM   1441  N   ALA A 188     110.604 -11.628  37.151  1.00 29.68           N  
ANISOU 1441  N   ALA A 188     3759   3759   3759      0      0      0       N  
ATOM   1442  CA  ALA A 188     110.641 -11.936  35.724  1.00 32.81           C  
ANISOU 1442  CA  ALA A 188     4155   4155   4155      0      0      0       C  
ATOM   1443  C   ALA A 188     111.045 -13.392  35.452  1.00 28.37           C  
ANISOU 1443  C   ALA A 188     3593   3593   3593      0      0      0       C  
ATOM   1444  O   ALA A 188     110.405 -14.079  34.645  1.00 26.98           O  
ANISOU 1444  O   ALA A 188     3417   3417   3417      0      0      0       O  
ATOM   1445  CB  ALA A 188     111.576 -10.969  34.994  1.00 18.75           C  
ANISOU 1445  CB  ALA A 188     2375   2375   2375      0      0      0       C  
ATOM   1446  N   GLY A 189     112.098 -13.849  36.134  1.00 30.65           N  
ANISOU 1446  N   GLY A 189     3882   3882   3882      0      0      0       N  
ATOM   1447  CA  GLY A 189     112.594 -15.203  35.960  1.00 34.99           C  
ANISOU 1447  CA  GLY A 189     4432   4432   4432      0      0      0       C  
ATOM   1448  C   GLY A 189     111.615 -16.254  36.451  1.00 19.10           C  
ANISOU 1448  C   GLY A 189     2419   2419   2419      0      0      0       C  
ATOM   1449  O   GLY A 189     111.549 -17.346  35.899  1.00 31.96           O  
ANISOU 1449  O   GLY A 189     4048   4048   4048      0      0      0       O  
ATOM   1450  N   GLU A 190     110.854 -15.912  37.485  1.00 29.98           N  
ANISOU 1450  N   GLU A 190     3797   3797   3797      0      0      0       N  
ATOM   1451  CA  GLU A 190     109.842 -16.811  38.012  1.00 29.40           C  
ANISOU 1451  CA  GLU A 190     3724   3724   3724      0      0      0       C  
ATOM   1452  C   GLU A 190     108.749 -17.009  36.980  1.00 32.25           C  
ANISOU 1452  C   GLU A 190     4085   4085   4085      0      0      0       C  
ATOM   1453  O   GLU A 190     108.314 -18.136  36.748  1.00 25.16           O  
ANISOU 1453  O   GLU A 190     3187   3187   3187      0      0      0       O  
ATOM   1454  CB  GLU A 190     109.237 -16.299  39.318  1.00 21.25           C  
ANISOU 1454  CB  GLU A 190     2691   2691   2691      0      0      0       C  
ATOM   1455  CG  GLU A 190     110.205 -16.075  40.458  1.00 35.63           C  
ANISOU 1455  CG  GLU A 190     4513   4513   4513      0      0      0       C  
ATOM   1456  CD  GLU A 190     110.778 -17.362  41.028  1.00 40.67           C  
ANISOU 1456  CD  GLU A 190     5151   5151   5151      0      0      0       C  
ATOM   1457  OE1 GLU A 190     110.295 -18.452  40.674  1.00 43.83           O  
ANISOU 1457  OE1 GLU A 190     5539   5572   5543    -14     -7     19       O  
ATOM   1458  OE2 GLU A 190     111.692 -17.271  41.874  1.00 68.84           O  
ANISOU 1458  OE2 GLU A 190     8718   8718   8718      0      0      0       O  
ATOM   1459  N   MET A 191     108.320 -15.917  36.350  1.00 24.76           N  
ANISOU 1459  N   MET A 191     3136   3136   3136      0      0      0       N  
ATOM   1460  CA  MET A 191     107.283 -16.036  35.328  1.00 19.21           C  
ANISOU 1460  CA  MET A 191     2432   2432   2432      0      0      0       C  
ATOM   1461  C   MET A 191     107.808 -16.842  34.131  1.00 18.75           C  
ANISOU 1461  C   MET A 191     2375   2375   2375      0      0      0       C  
ATOM   1462  O   MET A 191     107.088 -17.665  33.546  1.00 28.27           O  
ANISOU 1462  O   MET A 191     3581   3581   3581      0      0      0       O  
ATOM   1463  CB  MET A 191     106.798 -14.658  34.873  1.00 30.75           C  
ANISOU 1463  CB  MET A 191     3895   3895   3895      0      0      0       C  
ATOM   1464  CG  MET A 191     105.575 -14.684  33.954  1.00 33.11           C  
ANISOU 1464  CG  MET A 191     4193   4193   4193      0      0      0       C  
ATOM   1465  SD  MET A 191     104.172 -15.465  34.784  1.00 33.63           S  
ANISOU 1465  SD  MET A 191     4260   4260   4260      0      0      0       S  
ATOM   1466  CE  MET A 191     102.919 -15.447  33.502  1.00 36.69           C  
ANISOU 1466  CE  MET A 191     4646   4646   4646      0      0      0       C  
ATOM   1467  N   VAL A 192     109.060 -16.569  33.749  1.00 24.12           N  
ANISOU 1467  N   VAL A 192     3055   3055   3055      0      0      0       N  
ATOM   1468  CA  VAL A 192     109.672 -17.283  32.632  1.00 16.50           C  
ANISOU 1468  CA  VAL A 192     2090   2090   2090      0      0      0       C  
ATOM   1469  C   VAL A 192     109.763 -18.795  32.893  1.00 33.80           C  
ANISOU 1469  C   VAL A 192     4281   4281   4281      0      0      0       C  
ATOM   1470  O   VAL A 192     109.435 -19.586  32.015  1.00 23.29           O  
ANISOU 1470  O   VAL A 192     2949   2949   2949      0      0      0       O  
ATOM   1471  CB  VAL A 192     111.052 -16.725  32.269  1.00 29.49           C  
ANISOU 1471  CB  VAL A 192     3735   3735   3735      0      0      0       C  
ATOM   1472  CG1 VAL A 192     111.771 -17.658  31.286  1.00 21.69           C  
ANISOU 1472  CG1 VAL A 192     2747   2747   2747      0      0      0       C  
ATOM   1473  CG2 VAL A 192     110.916 -15.315  31.662  1.00 16.58           C  
ANISOU 1473  CG2 VAL A 192     2100   2100   2100      0      0      0       C  
ATOM   1474  N   THR A 193     110.269 -19.192  34.060  1.00 22.99           N  
ANISOU 1474  N   THR A 193     2912   2912   2912      0      0      0       N  
ATOM   1475  CA  THR A 193     110.370 -20.613  34.351  1.00 44.53           C  
ANISOU 1475  CA  THR A 193     5640   5640   5640      0      0      0       C  
ATOM   1476  C   THR A 193     108.999 -21.230  34.548  1.00 40.53           C  
ANISOU 1476  C   THR A 193     5133   5133   5133      0      0      0       C  
ATOM   1477  O   THR A 193     108.771 -22.370  34.176  1.00 30.42           O  
ANISOU 1477  O   THR A 193     3848   3853   3859     -6     -8     15       O  
ATOM   1478  CB  THR A 193     111.263 -20.915  35.578  1.00 29.19           C  
ANISOU 1478  CB  THR A 193     3697   3697   3697      0      0      0       C  
ATOM   1479  OG1 THR A 193     110.735 -20.258  36.740  1.00 36.08           O  
ANISOU 1479  OG1 THR A 193     4569   4569   4569      0      0      0       O  
ATOM   1480  CG2 THR A 193     112.704 -20.460  35.330  1.00 19.86           C  
ANISOU 1480  CG2 THR A 193     2515   2515   2515      0      0      0       C  
ATOM   1481  N   GLY A 194     108.055 -20.433  35.035  1.00 36.64           N  
ANISOU 1481  N   GLY A 194     4641   4641   4641      0      0      0       N  
ATOM   1482  CA  GLY A 194     106.693 -20.902  35.172  1.00 37.68           C  
ANISOU 1482  CA  GLY A 194     4744   4783   4789    -18    -19     58       C  
ATOM   1483  C   GLY A 194     106.086 -21.278  33.838  1.00 44.43           C  
ANISOU 1483  C   GLY A 194     5584   5635   5662    -20    -25     59       C  
ATOM   1484  O   GLY A 194     105.391 -22.288  33.740  1.00 41.74           O  
ANISOU 1484  O   GLY A 194     5184   5286   5390    -39    -58    133       O  
ATOM   1485  N   ILE A 195     106.326 -20.463  32.816  1.00 32.63           N  
ANISOU 1485  N   ILE A 195     4132   4132   4132      0      0      0       N  
ATOM   1486  CA  ILE A 195     105.801 -20.739  31.477  1.00 29.60           C  
ANISOU 1486  CA  ILE A 195     3749   3749   3749      0      0      0       C  
ATOM   1487  C   ILE A 195     106.575 -21.797  30.697  1.00 29.03           C  
ANISOU 1487  C   ILE A 195     3676   3676   3677      0     -1      1       C  
ATOM   1488  O   ILE A 195     105.982 -22.679  30.079  1.00 27.96           O  
ANISOU 1488  O   ILE A 195     3506   3502   3614    -16    -37     52       O  
ATOM   1489  CB  ILE A 195     105.725 -19.451  30.652  1.00 27.98           C  
ANISOU 1489  CB  ILE A 195     3544   3544   3544      0      0      0       C  
ATOM   1490  CG1 ILE A 195     104.633 -18.566  31.240  1.00 27.83           C  
ANISOU 1490  CG1 ILE A 195     3524   3524   3524      0      0      0       C  
ATOM   1491  CG2 ILE A 195     105.356 -19.749  29.216  1.00 22.64           C  
ANISOU 1491  CG2 ILE A 195     2867   2867   2867      0      0      0       C  
ATOM   1492  CD1 ILE A 195     104.557 -17.206  30.604  1.00 47.97           C  
ANISOU 1492  CD1 ILE A 195     6075   6075   6075      0      0      0       C  
ATOM   1493  N   GLN A 196     107.897 -21.652  30.682  1.00 38.15           N  
ANISOU 1493  N   GLN A 196     4832   4832   4832      0      0      0       N  
ATOM   1494  CA  GLN A 196     108.763 -22.477  29.855  1.00 34.63           C  
ANISOU 1494  CA  GLN A 196     4386   4386   4386      0      0      0       C  
ATOM   1495  C   GLN A 196     109.288 -23.706  30.577  1.00 31.69           C  
ANISOU 1495  C   GLN A 196     4007   4008   4027     -3    -10      8       C  
ATOM   1496  O   GLN A 196     109.800 -24.608  29.934  1.00 21.80           O  
ANISOU 1496  O   GLN A 196     2735   2732   2815     -9    -43     22       O  
ATOM   1497  CB  GLN A 196     109.975 -21.672  29.364  1.00 30.32           C  
ANISOU 1497  CB  GLN A 196     3840   3840   3840      0      0      0       C  
ATOM   1498  CG  GLN A 196     109.624 -20.467  28.483  1.00 30.44           C  
ANISOU 1498  CG  GLN A 196     3855   3855   3855      0      0      0       C  
ATOM   1499  CD  GLN A 196     110.831 -19.882  27.759  1.00 30.48           C  
ANISOU 1499  CD  GLN A 196     3861   3861   3861      0      0      0       C  
ATOM   1500  OE1 GLN A 196     110.685 -19.321  26.673  1.00 39.60           O  
ANISOU 1500  OE1 GLN A 196     5015   5015   5015      0      0      0       O  
ATOM   1501  NE2 GLN A 196     112.016 -19.972  28.367  1.00 22.28           N  
ANISOU 1501  NE2 GLN A 196     2822   2822   2822      0      0      0       N  
ATOM   1502  N   GLY A 197     109.183 -23.727  31.902  1.00 28.67           N  
ANISOU 1502  N   GLY A 197     3615   3622   3659    -10    -24     23       N  
ATOM   1503  CA  GLY A 197     109.863 -24.743  32.692  1.00 31.34           C  
ANISOU 1503  CA  GLY A 197     3925   3927   4055    -37    -77     79       C  
ATOM   1504  C   GLY A 197     111.255 -24.257  33.049  1.00 32.97           C  
ANISOU 1504  C   GLY A 197     4172   4170   4184     -5     -9     10       C  
ATOM   1505  O   GLY A 197     111.802 -23.371  32.397  1.00 30.67           O  
ANISOU 1505  O   GLY A 197     3884   3884   3884      0      0      0       O  
ATOM   1506  N   ASP A 198     111.853 -24.852  34.064  1.00 26.41           N  
ANISOU 1506  N   ASP A 198     3334   3327   3373    -22    -33     37       N  
ATOM   1507  CA  ASP A 198     113.224 -24.511  34.421  1.00 38.71           C  
ANISOU 1507  CA  ASP A 198     4903   4903   4903      0      0      0       C  
ATOM   1508  C   ASP A 198     114.198 -24.964  33.352  1.00 24.96           C  
ANISOU 1508  C   ASP A 198     3162   3162   3162      0      0      0       C  
ATOM   1509  O   ASP A 198     113.890 -25.846  32.555  1.00 26.38           O  
ANISOU 1509  O   ASP A 198     3337   3318   3368    -11    -30     19       O  
ATOM   1510  CB  ASP A 198     113.616 -25.123  35.765  1.00 39.55           C  
ANISOU 1510  CB  ASP A 198     4998   4998   5033    -33    -47     48       C  
ATOM   1511  CG  ASP A 198     113.091 -24.337  36.941  1.00 57.79           C  
ANISOU 1511  CG  ASP A 198     7307   7320   7332    -31    -30     38       C  
ATOM   1512  OD1 ASP A 198     113.608 -23.220  37.170  1.00 69.99           O  
ANISOU 1512  OD1 ASP A 198     8865   8865   8865      0      0      0       O  
ATOM   1513  OD2 ASP A 198     112.178 -24.816  37.636  1.00 45.36           O  
ANISOU 1513  OD2 ASP A 198     5715   5742   5779    -67    -68    107       O  
ATOM   1514  N   VAL A 199     115.324 -24.273  33.259  1.00 38.71           N  
ANISOU 1514  N   VAL A 199     4903   4903   4903      0      0      0       N  
ATOM   1515  CA  VAL A 199     116.446 -24.780  32.492  1.00 15.86           C  
ANISOU 1515  CA  VAL A 199     2009   2009   2009      0      0      0       C  
ATOM   1516  C   VAL A 199     116.761 -26.162  33.035  1.00 26.14           C  
ANISOU 1516  C   VAL A 199     3311   3309   3313     -1     -3      1       C  
ATOM   1517  O   VAL A 199     116.917 -26.327  34.240  1.00 34.72           O  
ANISOU 1517  O   VAL A 199     4397   4382   4412    -11    -28     14       O  
ATOM   1518  CB  VAL A 199     117.674 -23.880  32.610  1.00 34.87           C  
ANISOU 1518  CB  VAL A 199     4416   4416   4416      0      0      0       C  
ATOM   1519  CG1 VAL A 199     118.885 -24.541  31.951  1.00 24.98           C  
ANISOU 1519  CG1 VAL A 199     3163   3163   3163      0      0      0       C  
ATOM   1520  CG2 VAL A 199     117.385 -22.503  31.980  1.00 30.24           C  
ANISOU 1520  CG2 VAL A 199     3830   3830   3830      0      0      0       C  
ATOM   1521  N   GLY A 200     116.912 -27.133  32.137  1.00 33.75           N  
ANISOU 1521  N   GLY A 200     4267   4239   4317    -10    -63     15       N  
ATOM   1522  CA  GLY A 200     117.141 -28.518  32.509  1.00 34.15           C  
ANISOU 1522  CA  GLY A 200     4323   4210   4443    -28   -140     43       C  
ATOM   1523  C   GLY A 200     116.323 -29.514  31.717  1.00 48.77           C  
ANISOU 1523  C   GLY A 200     6157   5995   6378    -34   -210     57       C  
ATOM   1524  O   GLY A 200     115.977 -29.228  30.564  1.00 30.16           O  
ANISOU 1524  O   GLY A 200     3765   3683   4012    -18   -217     31       O  
ATOM   1525  N   ALA A 201     116.056 -30.686  32.297  1.00 48.39           N  
ANISOU 1525  N   ALA A 201     6049   5943   6394    -51   -310     87       N  
ATOM   1526  CA  ALA A 201     115.434 -31.781  31.559  1.00 43.84           C  
ANISOU 1526  CA  ALA A 201     5430   5308   5919    -54   -388     97       C  
ATOM   1527  C   ALA A 201     114.048 -31.474  31.028  1.00 42.37           C  
ANISOU 1527  C   ALA A 201     5220   5118   5762    -54   -383    104       C  
ATOM   1528  O   ALA A 201     113.669 -31.977  29.972  1.00 40.39           O  
ANISOU 1528  O   ALA A 201     4941   4829   5575    -44   -421     87       O  
ATOM   1529  CB  ALA A 201     115.404 -33.057  32.425  1.00 40.33           C  
ANISOU 1529  CB  ALA A 201     5024   4724   5575    -87   -429    159       C  
ATOM   1530  N   ASP A 202     113.296 -30.648  31.748  1.00 35.67           N  
ANISOU 1530  N   ASP A 202     4374   4194   4985    -87   -421    171       N  
ATOM   1531  CA  ASP A 202     111.931 -30.343  31.332  1.00 53.02           C  
ANISOU 1531  CA  ASP A 202     6551   6496   7098    -65   -335    138       C  
ATOM   1532  C   ASP A 202     111.789 -29.012  30.591  1.00 47.62           C  
ANISOU 1532  C   ASP A 202     5952   5803   6337    -49   -236    103       C  
ATOM   1533  O   ASP A 202     110.676 -28.566  30.324  1.00 43.04           O  
ANISOU 1533  O   ASP A 202     5314   5281   5760    -45   -248    101       O  
ATOM   1534  CB  ASP A 202     110.965 -30.421  32.518  1.00 60.29           C  
ANISOU 1534  CB  ASP A 202     7439   7420   8050    -91   -349    200       C  
ATOM   1535  CG  ASP A 202     110.662 -31.854  32.924  1.00 82.05           C  
ANISOU 1535  CG  ASP A 202    10131  10119  10925   -113   -432    257       C  
ATOM   1536  OD1 ASP A 202     110.409 -32.680  32.023  1.00 59.73           O  
ANISOU 1536  OD1 ASP A 202     7243   7068   8386   -147   -602    342       O  
ATOM   1537  OD2 ASP A 202     110.686 -32.160  34.138  1.00101.72           O  
ANISOU 1537  OD2 ASP A 202    12695  12520  13436   -148   -404    337       O  
ATOM   1538  N   PHE A 203     112.920 -28.392  30.259  1.00 54.44           N  
ANISOU 1538  N   PHE A 203     6811   6759   7113    -28   -205     55       N  
ATOM   1539  CA  PHE A 203     112.935 -27.126  29.518  1.00 36.75           C  
ANISOU 1539  CA  PHE A 203     4604   4568   4792    -12   -129     24       C  
ATOM   1540  C   PHE A 203     112.128 -27.218  28.221  1.00 24.34           C  
ANISOU 1540  C   PHE A 203     3038   2940   3270     -7   -140     14       C  
ATOM   1541  O   PHE A 203     112.457 -27.985  27.327  1.00 33.54           O  
ANISOU 1541  O   PHE A 203     4154   4103   4487      1   -201     -3       O  
ATOM   1542  CB  PHE A 203     114.375 -26.675  29.251  1.00 29.10           C  
ANISOU 1542  CB  PHE A 203     3672   3618   3765     -3    -72      5       C  
ATOM   1543  CG  PHE A 203     114.486 -25.304  28.644  1.00 42.33           C  
ANISOU 1543  CG  PHE A 203     5362   5362   5362      0      0      0       C  
ATOM   1544  CD1 PHE A 203     114.944 -25.148  27.343  1.00 20.42           C  
ANISOU 1544  CD1 PHE A 203     2586   2586   2586      0      0      0       C  
ATOM   1545  CD2 PHE A 203     114.182 -24.173  29.380  1.00 32.85           C  
ANISOU 1545  CD2 PHE A 203     4160   4160   4160      0      0      0       C  
ATOM   1546  CE1 PHE A 203     115.060 -23.885  26.770  1.00 36.89           C  
ANISOU 1546  CE1 PHE A 203     4672   4672   4672      0      0      0       C  
ATOM   1547  CE2 PHE A 203     114.307 -22.915  28.819  1.00 40.44           C  
ANISOU 1547  CE2 PHE A 203     5121   5121   5121      0      0      0       C  
ATOM   1548  CZ  PHE A 203     114.753 -22.768  27.514  1.00 23.07           C  
ANISOU 1548  CZ  PHE A 203     2921   2921   2921      0      0      0       C  
ATOM   1549  N   LEU A 204     111.071 -26.419  28.137  1.00 35.07           N  
ANISOU 1549  N   LEU A 204     4376   4350   4598     -7   -124     16       N  
ATOM   1550  CA  LEU A 204     110.200 -26.342  26.961  1.00 43.32           C  
ANISOU 1550  CA  LEU A 204     5402   5376   5680     -2   -141      4       C  
ATOM   1551  C   LEU A 204     109.438 -27.645  26.647  1.00 38.55           C  
ANISOU 1551  C   LEU A 204     4737   4700   5210     -7   -228     16       C  
ATOM   1552  O   LEU A 204     108.943 -27.807  25.538  1.00 52.24           O  
ANISOU 1552  O   LEU A 204     6448   6410   6993      2   -253     -5       O  
ATOM   1553  CB  LEU A 204     110.985 -25.885  25.718  1.00 23.59           C  
ANISOU 1553  CB  LEU A 204     2922   2902   3141     10   -114    -22       C  
ATOM   1554  CG  LEU A 204     111.625 -24.497  25.749  1.00 38.90           C  
ANISOU 1554  CG  LEU A 204     4910   4906   4964      4    -29    -10       C  
ATOM   1555  CD1 LEU A 204     112.432 -24.227  24.474  1.00 31.14           C  
ANISOU 1555  CD1 LEU A 204     3929   3928   3975      6    -24    -14       C  
ATOM   1556  CD2 LEU A 204     110.585 -23.398  25.984  1.00 29.63           C  
ANISOU 1556  CD2 LEU A 204     3753   3753   3753      0      0      0       C  
ATOM   1557  N   LYS A 205     109.303 -28.539  27.627  1.00 27.29           N  
ANISOU 1557  N   LYS A 205     3337   3174   3857    -24   -252     60       N  
ATOM   1558  CA  LYS A 205     108.634 -29.838  27.414  1.00 41.72           C  
ANISOU 1558  CA  LYS A 205     5042   4998   5813    -31   -358     79       C  
ATOM   1559  C   LYS A 205     107.172 -29.822  27.813  1.00 43.96           C  
ANISOU 1559  C   LYS A 205     5367   5166   6171    -50   -338    139       C  
ATOM   1560  O   LYS A 205     106.748 -29.035  28.658  1.00 32.96           O  
ANISOU 1560  O   LYS A 205     3903   3905   4713    -55   -326    155       O  
ATOM   1561  CB  LYS A 205     109.329 -30.960  28.211  1.00 32.26           C  
ANISOU 1561  CB  LYS A 205     3909   3671   4678    -47   -375    117       C  
ATOM   1562  CG  LYS A 205     110.796 -31.217  27.883  1.00 53.20           C  
ANISOU 1562  CG  LYS A 205     6587   6334   7292    -32   -378     73       C  
ATOM   1563  CD  LYS A 205     110.952 -31.728  26.450  1.00 57.15           C  
ANISOU 1563  CD  LYS A 205     7075   6792   7848     -9   -414     21       C  
ATOM   1564  CE  LYS A 205     112.406 -32.035  26.124  1.00 67.38           C  
ANISOU 1564  CE  LYS A 205     8306   8197   9098      7   -459    -15       C  
ATOM   1565  NZ  LYS A 205     112.592 -32.429  24.700  1.00 68.41           N  
ANISOU 1565  NZ  LYS A 205     8416   8304   9273     30   -494    -65       N  
ATOM   1566  N   GLY A 206     106.403 -30.703  27.183  1.00 47.05           N  
ANISOU 1566  N   GLY A 206     5572   5406   6898    -66   -536    186       N  
ATOM   1567  CA  GLY A 206     105.031 -30.953  27.584  1.00 32.80           C  
ANISOU 1567  CA  GLY A 206     3746   3757   4961    -65   -450    196       C  
ATOM   1568  C   GLY A 206     104.115 -29.758  27.429  1.00 44.32           C  
ANISOU 1568  C   GLY A 206     5220   5249   6370    -61   -395    196       C  
ATOM   1569  O   GLY A 206     103.983 -29.231  26.330  1.00 34.30           O  
ANISOU 1569  O   GLY A 206     3971   3986   5076    -45   -379    146       O  
ATOM   1570  N   SER A 207     103.450 -29.364  28.515  1.00 24.67           N  
ANISOU 1570  N   SER A 207     2715   2783   3875    -75   -370    255       N  
ATOM   1571  CA  SER A 207     102.536 -28.223  28.476  1.00 42.04           C  
ANISOU 1571  CA  SER A 207     4927   5015   6033    -70   -321    261       C  
ATOM   1572  C   SER A 207     103.219 -26.846  28.536  1.00 46.68           C  
ANISOU 1572  C   SER A 207     5602   5673   6463    -57   -253    210       C  
ATOM   1573  O   SER A 207     102.551 -25.825  28.399  1.00 39.53           O  
ANISOU 1573  O   SER A 207     4714   4794   5513    -51   -215    204       O  
ATOM   1574  CB  SER A 207     101.481 -28.323  29.578  1.00 28.65           C  
ANISOU 1574  CB  SER A 207     3285   3201   4399    -92   -289    379       C  
ATOM   1575  OG  SER A 207     102.069 -28.172  30.852  1.00 39.48           O  
ANISOU 1575  OG  SER A 207     4558   4729   5712    -91   -299    375       O  
ATOM   1576  N   ASN A 208     104.531 -26.824  28.770  1.00 37.28           N  
ANISOU 1576  N   ASN A 208     4428   4398   5339    -71   -297    240       N  
ATOM   1577  CA  ASN A 208     105.304 -25.583  28.781  1.00 32.39           C  
ANISOU 1577  CA  ASN A 208     3922   3953   4431    -38   -173    125       C  
ATOM   1578  C   ASN A 208     105.255 -24.861  27.432  1.00 38.56           C  
ANISOU 1578  C   ASN A 208     4776   4705   5170    -25   -132     82       C  
ATOM   1579  O   ASN A 208     105.269 -25.494  26.371  1.00 22.77           O  
ANISOU 1579  O   ASN A 208     2710   2714   3230    -18   -179     57       O  
ATOM   1580  CB  ASN A 208     106.764 -25.856  29.167  1.00 41.27           C  
ANISOU 1580  CB  ASN A 208     5082   5097   5503    -35   -164    103       C  
ATOM   1581  CG  ASN A 208     106.906 -26.444  30.566  1.00 41.06           C  
ANISOU 1581  CG  ASN A 208     5010   4991   5600    -71   -233    206       C  
ATOM   1582  OD1 ASN A 208     106.001 -26.345  31.400  1.00 34.05           O  
ANISOU 1582  OD1 ASN A 208     4081   4104   4753    -87   -240    273       O  
ATOM   1583  ND2 ASN A 208     108.036 -27.088  30.817  1.00 23.47           N  
ANISOU 1583  ND2 ASN A 208     2860   2781   3277    -59   -185    156       N  
ATOM   1584  N   ARG A 209     105.220 -23.528  27.469  1.00 24.49           N  
ANISOU 1584  N   ARG A 209     3008   3019   3278    -15    -87     50       N  
ATOM   1585  CA  ARG A 209     105.155 -22.774  26.224  1.00 28.73           C  
ANISOU 1585  CA  ARG A 209     3591   3558   3766     -6    -54     20       C  
ATOM   1586  C   ARG A 209     106.466 -22.057  25.964  1.00 30.81           C  
ANISOU 1586  C   ARG A 209     3899   3897   3911      0     -4      0       C  
ATOM   1587  O   ARG A 209     107.311 -21.946  26.847  1.00 25.57           O  
ANISOU 1587  O   ARG A 209     3238   3238   3238      0      0      0       O  
ATOM   1588  CB  ARG A 209     104.039 -21.721  26.279  1.00 27.86           C  
ANISOU 1588  CB  ARG A 209     3490   3469   3626     -5    -36     22       C  
ATOM   1589  CG  ARG A 209     102.656 -22.231  26.784  1.00 21.59           C  
ANISOU 1589  CG  ARG A 209     2613   2642   2950    -16    -81     70       C  
ATOM   1590  CD  ARG A 209     101.987 -23.166  25.783  1.00 33.98           C  
ANISOU 1590  CD  ARG A 209     4092   4073   4745    -25   -159    110       C  
ATOM   1591  NE  ARG A 209     102.470 -24.543  25.924  1.00 30.61           N  
ANISOU 1591  NE  ARG A 209     3617   3581   4431    -33   -220    131       N  
ATOM   1592  CZ  ARG A 209     102.230 -25.528  25.056  1.00 47.91           C  
ANISOU 1592  CZ  ARG A 209     5752   5690   6761    -32   -286    121       C  
ATOM   1593  NH1 ARG A 209     102.701 -26.759  25.290  1.00 24.84           N  
ANISOU 1593  NH1 ARG A 209     2831   2856   3751    -29   -279    103       N  
ATOM   1594  NH2 ARG A 209     101.508 -25.296  23.960  1.00 31.67           N  
ANISOU 1594  NH2 ARG A 209     3716   3743   4575    -16   -236     64       N  
ATOM   1595  N   ILE A 210     106.643 -21.613  24.726  1.00 31.44           N  
ANISOU 1595  N   ILE A 210     3982   3982   3982      0      0      0       N  
ATOM   1596  CA  ILE A 210     107.688 -20.654  24.399  1.00 30.94           C  
ANISOU 1596  CA  ILE A 210     3919   3919   3919      0      0      0       C  
ATOM   1597  C   ILE A 210     107.237 -19.327  25.017  1.00 40.80           C  
ANISOU 1597  C   ILE A 210     5167   5167   5167      0      0      0       C  
ATOM   1598  O   ILE A 210     106.059 -18.954  24.892  1.00 27.15           O  
ANISOU 1598  O   ILE A 210     3439   3439   3439      0      0      0       O  
ATOM   1599  CB  ILE A 210     107.843 -20.506  22.882  1.00 27.33           C  
ANISOU 1599  CB  ILE A 210     3462   3462   3462      0      0      0       C  
ATOM   1600  CG1 ILE A 210     108.308 -21.829  22.274  1.00 26.27           C  
ANISOU 1600  CG1 ILE A 210     3318   3321   3345      3    -10    -10       C  
ATOM   1601  CG2 ILE A 210     108.791 -19.388  22.550  1.00 17.33           C  
ANISOU 1601  CG2 ILE A 210     2195   2195   2195      0      0      0       C  
ATOM   1602  CD1 ILE A 210     108.152 -21.900  20.774  1.00 21.59           C  
ANISOU 1602  CD1 ILE A 210     2706   2701   2797     15    -34    -46       C  
ATOM   1603  N   ALA A 211     108.146 -18.627  25.697  1.00 21.54           N  
ANISOU 1603  N   ALA A 211     2728   2728   2728      0      0      0       N  
ATOM   1604  CA  ALA A 211     107.786 -17.347  26.300  1.00 25.81           C  
ANISOU 1604  CA  ALA A 211     3268   3268   3268      0      0      0       C  
ATOM   1605  C   ALA A 211     108.455 -16.154  25.637  1.00 23.75           C  
ANISOU 1605  C   ALA A 211     3008   3008   3008      0      0      0       C  
ATOM   1606  O   ALA A 211     109.565 -16.256  25.123  1.00 27.43           O  
ANISOU 1606  O   ALA A 211     3473   3473   3473      0      0      0       O  
ATOM   1607  CB  ALA A 211     108.097 -17.347  27.789  1.00 30.01           C  
ANISOU 1607  CB  ALA A 211     3801   3801   3801      0      0      0       C  
ATOM   1608  N   THR A 212     107.760 -15.017  25.657  1.00 47.91           N  
ANISOU 1608  N   THR A 212     6068   6068   6068      0      0      0       N  
ATOM   1609  CA  THR A 212     108.359 -13.753  25.217  1.00 31.55           C  
ANISOU 1609  CA  THR A 212     3995   3995   3995      0      0      0       C  
ATOM   1610  C   THR A 212     108.321 -12.747  26.364  1.00 19.96           C  
ANISOU 1610  C   THR A 212     2528   2528   2528      0      0      0       C  
ATOM   1611  O   THR A 212     107.257 -12.420  26.881  1.00 31.21           O  
ANISOU 1611  O   THR A 212     3952   3952   3952      0      0      0       O  
ATOM   1612  CB  THR A 212     107.597 -13.120  24.036  1.00 30.80           C  
ANISOU 1612  CB  THR A 212     3901   3901   3901      0      0      0       C  
ATOM   1613  OG1 THR A 212     107.762 -13.915  22.859  1.00 21.42           O  
ANISOU 1613  OG1 THR A 212     2713   2713   2713      0      0      0       O  
ATOM   1614  CG2 THR A 212     108.149 -11.741  23.744  1.00 23.58           C  
ANISOU 1614  CG2 THR A 212     2987   2987   2987      0      0      0       C  
ATOM   1615  N   ALA A 213     109.485 -12.230  26.730  1.00 14.88           N  
ANISOU 1615  N   ALA A 213     1885   1885   1885      0      0      0       N  
ATOM   1616  CA  ALA A 213     109.549 -11.172  27.726  1.00 39.29           C  
ANISOU 1616  CA  ALA A 213     4976   4976   4976      0      0      0       C  
ATOM   1617  C   ALA A 213     109.468  -9.785  27.048  1.00 27.20           C  
ANISOU 1617  C   ALA A 213     3445   3445   3445      0      0      0       C  
ATOM   1618  O   ALA A 213     110.226  -9.494  26.118  1.00 14.25           O  
ANISOU 1618  O   ALA A 213     1804   1804   1804      0      0      0       O  
ATOM   1619  CB  ALA A 213     110.823 -11.309  28.559  1.00 15.83           C  
ANISOU 1619  CB  ALA A 213     2004   2004   2004      0      0      0       C  
ATOM   1620  N   LYS A 214     108.519  -8.967  27.502  1.00 15.66           N  
ANISOU 1620  N   LYS A 214     1983   1983   1983      0      0      0       N  
ATOM   1621  CA  LYS A 214     108.238  -7.636  26.919  1.00 28.74           C  
ANISOU 1621  CA  LYS A 214     3640   3640   3640      0      0      0       C  
ATOM   1622  C   LYS A 214     108.480  -6.545  27.971  1.00 22.40           C  
ANISOU 1622  C   LYS A 214     2837   2837   2837      0      0      0       C  
ATOM   1623  O   LYS A 214     108.314  -6.801  29.174  1.00 17.07           O  
ANISOU 1623  O   LYS A 214     2161   2161   2161      0      0      0       O  
ATOM   1624  CB  LYS A 214     106.756  -7.536  26.543  1.00 23.76           C  
ANISOU 1624  CB  LYS A 214     3009   3009   3009      0      0      0       C  
ATOM   1625  CG  LYS A 214     106.185  -8.715  25.763  1.00 37.31           C  
ANISOU 1625  CG  LYS A 214     4725   4725   4725      0      0      0       C  
ATOM   1626  CD  LYS A 214     104.662  -8.554  25.664  1.00 27.23           C  
ANISOU 1626  CD  LYS A 214     3448   3448   3448      0      0      0       C  
ATOM   1627  CE  LYS A 214     104.017  -8.867  27.026  1.00 30.86           C  
ANISOU 1627  CE  LYS A 214     3908   3908   3908      0      0      0       C  
ATOM   1628  NZ  LYS A 214     102.563  -8.624  27.048  1.00 52.31           N  
ANISOU 1628  NZ  LYS A 214     6625   6625   6625      0      0      0       N  
ATOM   1629  N   HIS A 215     108.878  -5.338  27.558  1.00 31.38           N  
ANISOU 1629  N   HIS A 215     3974   3974   3974      0      0      0       N  
ATOM   1630  CA  HIS A 215     109.363  -4.998  26.221  1.00 33.99           C  
ANISOU 1630  CA  HIS A 215     4305   4305   4305      0      0      0       C  
ATOM   1631  C   HIS A 215     110.752  -4.414  26.425  1.00 21.80           C  
ANISOU 1631  C   HIS A 215     2761   2761   2761      0      0      0       C  
ATOM   1632  O   HIS A 215     111.009  -3.779  27.443  1.00 30.16           O  
ANISOU 1632  O   HIS A 215     3820   3820   3820      0      0      0       O  
ATOM   1633  CB  HIS A 215     108.505  -3.896  25.571  1.00 25.00           C  
ANISOU 1633  CB  HIS A 215     3166   3166   3166      0      0      0       C  
ATOM   1634  CG  HIS A 215     107.079  -4.279  25.328  1.00 24.96           C  
ANISOU 1634  CG  HIS A 215     3161   3161   3161      0      0      0       C  
ATOM   1635  ND1 HIS A 215     106.108  -4.185  26.305  1.00 22.15           N  
ANISOU 1635  ND1 HIS A 215     2805   2805   2805      0      0      0       N  
ATOM   1636  CD2 HIS A 215     106.453  -4.740  24.219  1.00 28.84           C  
ANISOU 1636  CD2 HIS A 215     3653   3653   3653      0      0      0       C  
ATOM   1637  CE1 HIS A 215     104.948  -4.577  25.808  1.00 19.79           C  
ANISOU 1637  CE1 HIS A 215     2506   2506   2506      0      0      0       C  
ATOM   1638  NE2 HIS A 215     105.130  -4.923  24.546  1.00 28.94           N  
ANISOU 1638  NE2 HIS A 215     3666   3666   3666      0      0      0       N  
ATOM   1639  N   PHE A 216     111.660  -4.698  25.502  1.00 30.03           N  
ANISOU 1639  N   PHE A 216     3804   3804   3804      0      0      0       N  
ATOM   1640  CA  PHE A 216     113.024  -4.188  25.561  1.00 31.00           C  
ANISOU 1640  CA  PHE A 216     3927   3927   3927      0      0      0       C  
ATOM   1641  C   PHE A 216     113.119  -2.925  24.676  1.00 23.36           C  
ANISOU 1641  C   PHE A 216     2959   2959   2959      0      0      0       C  
ATOM   1642  O   PHE A 216     112.983  -3.033  23.460  1.00 16.27           O  
ANISOU 1642  O   PHE A 216     2061   2061   2061      0      0      0       O  
ATOM   1643  CB  PHE A 216     113.989  -5.253  25.046  1.00 22.75           C  
ANISOU 1643  CB  PHE A 216     2882   2882   2882      0      0      0       C  
ATOM   1644  CG  PHE A 216     115.421  -4.978  25.390  1.00 27.90           C  
ANISOU 1644  CG  PHE A 216     3533   3533   3533      0      0      0       C  
ATOM   1645  CD1 PHE A 216     115.952  -5.397  26.589  1.00 30.04           C  
ANISOU 1645  CD1 PHE A 216     3804   3804   3804      0      0      0       C  
ATOM   1646  CD2 PHE A 216     116.221  -4.261  24.536  1.00 25.12           C  
ANISOU 1646  CD2 PHE A 216     3182   3182   3182      0      0      0       C  
ATOM   1647  CE1 PHE A 216     117.261  -5.134  26.913  1.00 30.43           C  
ANISOU 1647  CE1 PHE A 216     3854   3854   3854      0      0      0       C  
ATOM   1648  CE2 PHE A 216     117.532  -3.988  24.865  1.00 17.77           C  
ANISOU 1648  CE2 PHE A 216     2251   2251   2251      0      0      0       C  
ATOM   1649  CZ  PHE A 216     118.052  -4.422  26.052  1.00 24.06           C  
ANISOU 1649  CZ  PHE A 216     3047   3047   3047      0      0      0       C  
ATOM   1650  N   VAL A 217     113.293  -1.732  25.252  1.00 17.83           N  
ANISOU 1650  N   VAL A 217     2258   2258   2258      0      0      0       N  
ATOM   1651  CA  VAL A 217     113.533  -1.519  26.670  1.00 10.62           C  
ANISOU 1651  CA  VAL A 217     1345   1345   1345      0      0      0       C  
ATOM   1652  C   VAL A 217     113.196  -0.042  27.013  1.00 34.88           C  
ANISOU 1652  C   VAL A 217     4418   4418   4418      0      0      0       C  
ATOM   1653  O   VAL A 217     113.256   0.841  26.158  1.00 20.07           O  
ANISOU 1653  O   VAL A 217     2541   2541   2541      0      0      0       O  
ATOM   1654  CB  VAL A 217     115.042  -1.764  27.007  1.00 22.62           C  
ANISOU 1654  CB  VAL A 217     2865   2865   2865      0      0      0       C  
ATOM   1655  CG1 VAL A 217     115.959  -0.830  26.190  1.00 14.06           C  
ANISOU 1655  CG1 VAL A 217     1781   1781   1781      0      0      0       C  
ATOM   1656  CG2 VAL A 217     115.333  -1.611  28.481  1.00 18.68           C  
ANISOU 1656  CG2 VAL A 217     2366   2366   2366      0      0      0       C  
ATOM   1657  N   GLY A 218     112.837   0.210  28.268  1.00 35.00           N  
ANISOU 1657  N   GLY A 218     4432   4432   4432      0      0      0       N  
ATOM   1658  CA  GLY A 218     112.623   1.555  28.758  1.00 28.09           C  
ANISOU 1658  CA  GLY A 218     3558   3558   3558      0      0      0       C  
ATOM   1659  C   GLY A 218     111.234   2.153  28.578  1.00 32.41           C  
ANISOU 1659  C   GLY A 218     4105   4105   4105      0      0      0       C  
ATOM   1660  O   GLY A 218     111.067   3.345  28.803  1.00 32.25           O  
ANISOU 1660  O   GLY A 218     4085   4085   4085      0      0      0       O  
ATOM   1661  N   ASP A 219     110.242   1.354  28.191  1.00 31.33           N  
ANISOU 1661  N   ASP A 219     3969   3969   3969      0      0      0       N  
ATOM   1662  CA  ASP A 219     108.894   1.889  27.920  1.00 22.11           C  
ANISOU 1662  CA  ASP A 219     2801   2801   2801      0      0      0       C  
ATOM   1663  C   ASP A 219     108.158   2.458  29.134  1.00 22.08           C  
ANISOU 1663  C   ASP A 219     2797   2797   2797      0      0      0       C  
ATOM   1664  O   ASP A 219     107.171   3.158  28.981  1.00 29.59           O  
ANISOU 1664  O   ASP A 219     3748   3748   3748      0      0      0       O  
ATOM   1665  CB  ASP A 219     108.026   0.865  27.196  1.00 27.95           C  
ANISOU 1665  CB  ASP A 219     3540   3540   3540      0      0      0       C  
ATOM   1666  CG  ASP A 219     107.966  -0.456  27.926  1.00 44.16           C  
ANISOU 1666  CG  ASP A 219     5593   5593   5593      0      0      0       C  
ATOM   1667  OD1 ASP A 219     108.803  -0.657  28.830  1.00 19.17           O  
ANISOU 1667  OD1 ASP A 219     2428   2428   2428      0      0      0       O  
ATOM   1668  OD2 ASP A 219     107.094  -1.282  27.591  1.00 22.67           O  
ANISOU 1668  OD2 ASP A 219     2871   2871   2871      0      0      0       O  
ATOM   1669  N   GLY A 220     108.598   2.102  30.335  1.00 31.32           N  
ANISOU 1669  N   GLY A 220     3966   3966   3966      0      0      0       N  
ATOM   1670  CA  GLY A 220     108.040   2.669  31.550  1.00 20.91           C  
ANISOU 1670  CA  GLY A 220     2648   2648   2648      0      0      0       C  
ATOM   1671  C   GLY A 220     108.741   3.950  32.011  1.00 22.30           C  
ANISOU 1671  C   GLY A 220     2824   2824   2824      0      0      0       C  
ATOM   1672  O   GLY A 220     108.514   4.435  33.123  1.00 21.50           O  
ANISOU 1672  O   GLY A 220     2723   2723   2723      0      0      0       O  
ATOM   1673  N   GLY A 221     109.609   4.487  31.158  1.00 33.60           N  
ANISOU 1673  N   GLY A 221     4256   4256   4256      0      0      0       N  
ATOM   1674  CA  GLY A 221     110.348   5.689  31.492  1.00 30.66           C  
ANISOU 1674  CA  GLY A 221     3883   3883   3883      0      0      0       C  
ATOM   1675  C   GLY A 221     110.189   6.860  30.531  1.00 42.95           C  
ANISOU 1675  C   GLY A 221     5440   5440   5440      0      0      0       C  
ATOM   1676  O   GLY A 221     111.082   7.703  30.443  1.00 18.23           O  
ANISOU 1676  O   GLY A 221     2309   2309   2309      0      0      0       O  
ATOM   1677  N   THR A 222     109.106   6.876  29.758  1.00 30.34           N  
ANISOU 1677  N   THR A 222     3843   3843   3843      0      0      0       N  
ATOM   1678  CA  THR A 222     108.914   7.927  28.773  1.00 15.83           C  
ANISOU 1678  CA  THR A 222     2005   2005   2005      0      0      0       C  
ATOM   1679  C   THR A 222     108.600   9.235  29.491  1.00 39.09           C  
ANISOU 1679  C   THR A 222     4951   4951   4951      0      0      0       C  
ATOM   1680  O   THR A 222     108.049   9.247  30.596  1.00 27.25           O  
ANISOU 1680  O   THR A 222     3451   3451   3451      0      0      0       O  
ATOM   1681  CB  THR A 222     107.814   7.627  27.759  1.00 23.24           C  
ANISOU 1681  CB  THR A 222     2944   2944   2944      0      0      0       C  
ATOM   1682  OG1 THR A 222     106.543   7.554  28.427  1.00 18.28           O  
ANISOU 1682  OG1 THR A 222     2316   2316   2316      0      0      0       O  
ATOM   1683  CG2 THR A 222     108.118   6.344  27.004  1.00 16.82           C  
ANISOU 1683  CG2 THR A 222     2130   2130   2130      0      0      0       C  
ATOM   1684  N   GLU A 223     108.950  10.338  28.840  1.00 27.18           N  
ANISOU 1684  N   GLU A 223     3443   3443   3443      0      0      0       N  
ATOM   1685  CA  GLU A 223     108.782  11.659  29.428  1.00 33.48           C  
ANISOU 1685  CA  GLU A 223     4240   4240   4240      0      0      0       C  
ATOM   1686  C   GLU A 223     107.276  11.920  29.637  1.00 27.32           C  
ANISOU 1686  C   GLU A 223     3460   3460   3460      0      0      0       C  
ATOM   1687  O   GLU A 223     106.465  11.694  28.729  1.00 28.40           O  
ANISOU 1687  O   GLU A 223     3596   3596   3596      0      0      0       O  
ATOM   1688  CB  GLU A 223     109.422  12.715  28.510  1.00 22.91           C  
ANISOU 1688  CB  GLU A 223     2902   2902   2902      0      0      0       C  
ATOM   1689  CG  GLU A 223     109.764  14.036  29.096  1.00 66.96           C  
ANISOU 1689  CG  GLU A 223     8480   8480   8480      0      0      0       C  
ATOM   1690  CD  GLU A 223     110.865  13.868  30.130  1.00 82.23           C  
ANISOU 1690  CD  GLU A 223    10414  10414  10414      0      0      0       C  
ATOM   1691  OE1 GLU A 223     111.587  12.843  30.051  1.00 52.44           O  
ANISOU 1691  OE1 GLU A 223     6642   6642   6642      0      0      0       O  
ATOM   1692  OE2 GLU A 223     111.052  14.761  30.982  1.00 92.81           O  
ANISOU 1692  OE2 GLU A 223    11755  11755  11755      0      0      0       O  
ATOM   1693  N   ARG A 224     106.922  12.330  30.855  1.00 26.58           N  
ANISOU 1693  N   ARG A 224     3367   3367   3367      0      0      0       N  
ATOM   1694  CA  ARG A 224     105.533  12.563  31.310  1.00 31.08           C  
ANISOU 1694  CA  ARG A 224     3936   3936   3936      0      0      0       C  
ATOM   1695  C   ARG A 224     104.629  11.316  31.177  1.00 20.61           C  
ANISOU 1695  C   ARG A 224     2610   2610   2610      0      0      0       C  
ATOM   1696  O   ARG A 224     103.396  11.433  31.161  1.00 28.62           O  
ANISOU 1696  O   ARG A 224     3625   3625   3625      0      0      0       O  
ATOM   1697  CB  ARG A 224     104.839  13.768  30.648  1.00 28.53           C  
ANISOU 1697  CB  ARG A 224     3614   3614   3614      0      0      0       C  
ATOM   1698  CG  ARG A 224     105.459  15.136  30.948  1.00 54.05           C  
ANISOU 1698  CG  ARG A 224     6845   6845   6845      0      0      0       C  
ATOM   1699  CD  ARG A 224     104.666  16.232  30.244  1.00 37.06           C  
ANISOU 1699  CD  ARG A 224     4707   4685   4691     10     13      5       C  
ATOM   1700  NE  ARG A 224     104.822  16.230  28.810  0.50 36.66           N  
ANISOU 1700  NE  ARG A 224     4643   4643   4643      0      0      0       N  
ATOM   1701  CZ  ARG A 224     103.827  15.874  28.001  0.50 36.81           C  
ANISOU 1701  CZ  ARG A 224     4662   4662   4662      0      0      0       C  
ATOM   1702  NH1 ARG A 224     102.652  15.517  28.513  0.50 29.13           N  
ANISOU 1702  NH1 ARG A 224     3690   3689   3689      1      1      1       N  
ATOM   1703  NH2 ARG A 224     103.991  15.870  26.688  0.50 25.14           N  
ANISOU 1703  NH2 ARG A 224     3184   3184   3184      0      0      0       N  
ATOM   1704  N   GLY A 225     105.233  10.143  31.018  1.00 36.73           N  
ANISOU 1704  N   GLY A 225     4652   4652   4652      0      0      0       N  
ATOM   1705  CA  GLY A 225     104.472   8.910  30.902  1.00 22.08           C  
ANISOU 1705  CA  GLY A 225     2797   2797   2797      0      0      0       C  
ATOM   1706  C   GLY A 225     103.653   8.778  29.632  1.00 31.03           C  
ANISOU 1706  C   GLY A 225     3930   3930   3930      0      0      0       C  
ATOM   1707  O   GLY A 225     102.617   8.117  29.609  1.00 37.44           O  
ANISOU 1707  O   GLY A 225     4741   4741   4741      0      0      0       O  
ATOM   1708  N   VAL A 226     104.058   9.503  28.597  1.00 32.24           N  
ANISOU 1708  N   VAL A 226     4083   4083   4083      0      0      0       N  
ATOM   1709  CA  VAL A 226     103.361   9.430  27.328  1.00 16.51           C  
ANISOU 1709  CA  VAL A 226     2091   2091   2091      0      0      0       C  
ATOM   1710  C   VAL A 226     103.613   8.054  26.704  1.00 29.46           C  
ANISOU 1710  C   VAL A 226     3731   3731   3731      0      0      0       C  
ATOM   1711  O   VAL A 226     104.755   7.603  26.591  1.00 30.31           O  
ANISOU 1711  O   VAL A 226     3839   3839   3839      0      0      0       O  
ATOM   1712  CB  VAL A 226     103.827  10.541  26.376  1.00 20.84           C  
ANISOU 1712  CB  VAL A 226     2640   2640   2640      0      0      0       C  
ATOM   1713  CG1 VAL A 226     103.238  10.355  24.987  1.00 12.28           C  
ANISOU 1713  CG1 VAL A 226     1555   1555   1555      0      0      0       C  
ATOM   1714  CG2 VAL A 226     103.465  11.923  26.959  1.00 20.94           C  
ANISOU 1714  CG2 VAL A 226     2652   2652   2652      0      0      0       C  
ATOM   1715  N   ASP A 227     102.542   7.383  26.315  1.00 34.85           N  
ANISOU 1715  N   ASP A 227     4413   4413   4413      0      0      0       N  
ATOM   1716  CA  ASP A 227     102.645   6.051  25.730  1.00 22.13           C  
ANISOU 1716  CA  ASP A 227     2802   2802   2802      0      0      0       C  
ATOM   1717  C   ASP A 227     103.374   6.098  24.378  1.00 18.94           C  
ANISOU 1717  C   ASP A 227     2399   2399   2399      0      0      0       C  
ATOM   1718  O   ASP A 227     103.061   6.946  23.534  1.00 33.27           O  
ANISOU 1718  O   ASP A 227     4214   4214   4214      0      0      0       O  
ATOM   1719  CB  ASP A 227     101.256   5.446  25.575  1.00 21.37           C  
ANISOU 1719  CB  ASP A 227     2707   2707   2707      0      0      0       C  
ATOM   1720  CG  ASP A 227     101.303   3.996  25.122  1.00 34.80           C  
ANISOU 1720  CG  ASP A 227     4408   4408   4408      0      0      0       C  
ATOM   1721  OD1 ASP A 227     102.100   3.242  25.733  1.00 30.66           O  
ANISOU 1721  OD1 ASP A 227     3883   3883   3883      0      0      0       O  
ATOM   1722  OD2 ASP A 227     100.513   3.613  24.241  1.00 18.80           O  
ANISOU 1722  OD2 ASP A 227     2381   2381   2381      0      0      0       O  
ATOM   1723  N   ARG A 228     104.391   5.249  24.207  1.00 35.83           N  
ANISOU 1723  N   ARG A 228     4538   4538   4538      0      0      0       N  
ATOM   1724  CA  ARG A 228     105.202   5.213  22.982  1.00 19.38           C  
ANISOU 1724  CA  ARG A 228     2454   2454   2454      0      0      0       C  
ATOM   1725  C   ARG A 228     106.015   6.486  22.853  1.00 28.33           C  
ANISOU 1725  C   ARG A 228     3588   3588   3588      0      0      0       C  
ATOM   1726  O   ARG A 228     106.425   6.879  21.764  1.00 28.22           O  
ANISOU 1726  O   ARG A 228     3574   3574   3574      0      0      0       O  
ATOM   1727  CB  ARG A 228     104.326   5.029  21.736  1.00 25.56           C  
ANISOU 1727  CB  ARG A 228     3238   3238   3238      0      0      0       C  
ATOM   1728  CG  ARG A 228     103.389   3.827  21.809  1.00 30.79           C  
ANISOU 1728  CG  ARG A 228     3900   3900   3900      0      0      0       C  
ATOM   1729  CD  ARG A 228     102.820   3.513  20.447  1.00 27.15           C  
ANISOU 1729  CD  ARG A 228     3438   3438   3438      0      0      0       C  
ATOM   1730  NE  ARG A 228     101.862   2.424  20.519  1.00 39.39           N  
ANISOU 1730  NE  ARG A 228     4989   4989   4989      0      0      0       N  
ATOM   1731  CZ  ARG A 228     101.321   1.844  19.454  1.00 48.32           C  
ANISOU 1731  CZ  ARG A 228     6120   6120   6120      0      0      0       C  
ATOM   1732  NH1 ARG A 228     101.593   2.317  18.245  1.00 40.22           N  
ANISOU 1732  NH1 ARG A 228     5094   5094   5094      0      0      0       N  
ATOM   1733  NH2 ARG A 228     100.453   0.845  19.598  1.00 21.10           N  
ANISOU 1733  NH2 ARG A 228     2673   2673   2673      0      0      0       N  
ATOM   1734  N   GLY A 229     106.254   7.125  23.986  1.00 24.25           N  
ANISOU 1734  N   GLY A 229     3071   3071   3071      0      0      0       N  
ATOM   1735  CA  GLY A 229     106.940   8.400  24.035  1.00 21.36           C  
ANISOU 1735  CA  GLY A 229     2705   2705   2705      0      0      0       C  
ATOM   1736  C   GLY A 229     108.448   8.215  24.021  1.00 34.62           C  
ANISOU 1736  C   GLY A 229     4384   4384   4384      0      0      0       C  
ATOM   1737  O   GLY A 229     108.973   7.273  23.424  1.00 18.58           O  
ANISOU 1737  O   GLY A 229     2354   2354   2354      0      0      0       O  
ATOM   1738  N   ASN A 230     109.135   9.216  24.545  1.00 21.01           N  
ANISOU 1738  N   ASN A 230     2661   2661   2661      0      0      0       N  
ATOM   1739  CA  ASN A 230     110.581   9.333  24.497  1.00 20.48           C  
ANISOU 1739  CA  ASN A 230     2593   2593   2593      0      0      0       C  
ATOM   1740  C   ASN A 230     111.207   9.106  25.860  1.00 21.89           C  
ANISOU 1740  C   ASN A 230     2772   2772   2772      0      0      0       C  
ATOM   1741  O   ASN A 230     110.786   9.717  26.838  1.00 28.03           O  
ANISOU 1741  O   ASN A 230     3550   3550   3550      0      0      0       O  
ATOM   1742  CB  ASN A 230     110.987  10.703  23.977  1.00 32.72           C  
ANISOU 1742  CB  ASN A 230     4144   4144   4144      0      0      0       C  
ATOM   1743  CG  ASN A 230     112.449  10.770  23.597  1.00 40.90           C  
ANISOU 1743  CG  ASN A 230     5181   5181   5181      0      0      0       C  
ATOM   1744  OD1 ASN A 230     113.083   9.749  23.331  1.00 42.29           O  
ANISOU 1744  OD1 ASN A 230     5356   5356   5356      0      0      0       O  
ATOM   1745  ND2 ASN A 230     113.017  11.970  23.652  1.00 39.38           N  
ANISOU 1745  ND2 ASN A 230     4987   4987   4987      0      0      0       N  
ATOM   1746  N   THR A 231     112.095   8.140  25.967  1.00 18.06           N  
ANISOU 1746  N   THR A 231     2287   2287   2287      0      0      0       N  
ATOM   1747  CA  THR A 231     112.738   7.866  27.242  1.00 28.79           C  
ANISOU 1747  CA  THR A 231     3647   3647   3647      0      0      0       C  
ATOM   1748  C   THR A 231     114.064   8.589  27.347  1.00 17.24           C  
ANISOU 1748  C   THR A 231     2184   2184   2184      0      0      0       C  
ATOM   1749  O   THR A 231     115.027   8.201  26.695  1.00 21.56           O  
ANISOU 1749  O   THR A 231     2730   2730   2730      0      0      0       O  
ATOM   1750  CB  THR A 231     112.946   6.359  27.428  1.00 20.94           C  
ANISOU 1750  CB  THR A 231     2652   2652   2652      0      0      0       C  
ATOM   1751  OG1 THR A 231     111.669   5.735  27.417  1.00 22.86           O  
ANISOU 1751  OG1 THR A 231     2895   2895   2895      0      0      0       O  
ATOM   1752  CG2 THR A 231     113.675   6.075  28.721  1.00 10.59           C  
ANISOU 1752  CG2 THR A 231     1341   1341   1341      0      0      0       C  
ATOM   1753  N   LEU A 232     114.135   9.581  28.226  1.00 39.02           N  
ANISOU 1753  N   LEU A 232     4942   4942   4942      0      0      0       N  
ATOM   1754  CA  LEU A 232     115.317  10.430  28.296  1.00 30.54           C  
ANISOU 1754  CA  LEU A 232     3868   3868   3868      0      0      0       C  
ATOM   1755  C   LEU A 232     116.156  10.059  29.494  1.00 16.58           C  
ANISOU 1755  C   LEU A 232     2100   2100   2100      0      0      0       C  
ATOM   1756  O   LEU A 232     115.842  10.409  30.624  1.00 35.60           O  
ANISOU 1756  O   LEU A 232     4508   4508   4508      0      0      0       O  
ATOM   1757  CB  LEU A 232     114.893  11.889  28.440  1.00 23.32           C  
ANISOU 1757  CB  LEU A 232     2954   2954   2954      0      0      0       C  
ATOM   1758  CG  LEU A 232     115.037  12.721  27.174  1.00 40.91           C  
ANISOU 1758  CG  LEU A 232     5181   5181   5181      0      0      0       C  
ATOM   1759  CD1 LEU A 232     114.470  14.126  27.378  1.00 59.27           C  
ANISOU 1759  CD1 LEU A 232     7506   7506   7506      0      0      0       C  
ATOM   1760  CD2 LEU A 232     116.489  12.776  26.771  1.00 30.19           C  
ANISOU 1760  CD2 LEU A 232     3823   3823   3823      0      0      0       C  
ATOM   1761  N   ILE A 233     117.191   9.272  29.241  1.00 36.08           N  
ANISOU 1761  N   ILE A 233     4570   4570   4570      0      0      0       N  
ATOM   1762  CA  ILE A 233     118.025   8.755  30.318  1.00 22.31           C  
ANISOU 1762  CA  ILE A 233     2825   2825   2825      0      0      0       C  
ATOM   1763  C   ILE A 233     119.358   8.248  29.754  1.00 24.09           C  
ANISOU 1763  C   ILE A 233     3051   3051   3051      0      0      0       C  
ATOM   1764  O   ILE A 233     119.430   7.879  28.588  1.00 23.13           O  
ANISOU 1764  O   ILE A 233     2929   2929   2929      0      0      0       O  
ATOM   1765  CB  ILE A 233     117.297   7.600  31.060  1.00 26.40           C  
ANISOU 1765  CB  ILE A 233     3343   3343   3343      0      0      0       C  
ATOM   1766  CG1 ILE A 233     117.885   7.385  32.455  1.00 27.49           C  
ANISOU 1766  CG1 ILE A 233     3482   3482   3482      0      0      0       C  
ATOM   1767  CG2 ILE A 233     117.249   6.313  30.204  1.00 19.68           C  
ANISOU 1767  CG2 ILE A 233     2493   2493   2493      0      0      0       C  
ATOM   1768  CD1 ILE A 233     117.062   6.421  33.290  1.00 29.64           C  
ANISOU 1768  CD1 ILE A 233     3754   3754   3754      0      0      0       C  
ATOM   1769  N   ASP A 234     120.433   8.305  30.534  1.00 20.38           N  
ANISOU 1769  N   ASP A 234     2581   2581   2581      0      0      0       N  
ATOM   1770  CA  ASP A 234     121.705   7.771  30.032  1.00 27.06           C  
ANISOU 1770  CA  ASP A 234     3427   3427   3427      0      0      0       C  
ATOM   1771  C   ASP A 234     121.662   6.237  30.025  1.00 32.20           C  
ANISOU 1771  C   ASP A 234     4078   4078   4078      0      0      0       C  
ATOM   1772  O   ASP A 234     120.762   5.631  30.600  1.00 20.78           O  
ANISOU 1772  O   ASP A 234     2632   2632   2632      0      0      0       O  
ATOM   1773  CB  ASP A 234     122.939   8.263  30.794  1.00 27.21           C  
ANISOU 1773  CB  ASP A 234     3447   3447   3447      0      0      0       C  
ATOM   1774  CG  ASP A 234     122.918   7.897  32.258  1.00 34.85           C  
ANISOU 1774  CG  ASP A 234     4414   4414   4414      0      0      0       C  
ATOM   1775  OD1 ASP A 234     123.752   8.437  32.995  1.00 55.15           O  
ANISOU 1775  OD1 ASP A 234     6985   6985   6985      0      0      0       O  
ATOM   1776  OD2 ASP A 234     121.952   7.254  32.719  1.00 47.24           O  
ANISOU 1776  OD2 ASP A 234     5983   5983   5983      0      0      0       O  
ATOM   1777  N   GLU A 235     122.652   5.621  29.391  1.00 18.87           N  
ANISOU 1777  N   GLU A 235     2389   2389   2389      0      0      0       N  
ATOM   1778  CA  GLU A 235     122.661   4.177  29.211  1.00 36.15           C  
ANISOU 1778  CA  GLU A 235     4579   4579   4579      0      0      0       C  
ATOM   1779  C   GLU A 235     122.769   3.428  30.532  1.00 43.93           C  
ANISOU 1779  C   GLU A 235     5564   5564   5564      0      0      0       C  
ATOM   1780  O   GLU A 235     122.113   2.399  30.702  1.00 32.07           O  
ANISOU 1780  O   GLU A 235     4061   4061   4061      0      0      0       O  
ATOM   1781  CB  GLU A 235     123.795   3.771  28.250  1.00 22.63           C  
ANISOU 1781  CB  GLU A 235     2866   2866   2866      0      0      0       C  
ATOM   1782  CG  GLU A 235     123.747   2.318  27.780  1.00 35.94           C  
ANISOU 1782  CG  GLU A 235     4552   4552   4552      0      0      0       C  
ATOM   1783  CD  GLU A 235     124.777   1.991  26.706  1.00 33.65           C  
ANISOU 1783  CD  GLU A 235     4262   4262   4262      0      0      0       C  
ATOM   1784  OE1 GLU A 235     125.450   2.927  26.222  1.00 39.79           O  
ANISOU 1784  OE1 GLU A 235     5039   5039   5039      0      0      0       O  
ATOM   1785  OE2 GLU A 235     124.949   0.798  26.383  1.00 27.38           O  
ANISOU 1785  OE2 GLU A 235     3467   3467   3467      0      0      0       O  
ATOM   1786  N   LYS A 236     123.499   3.988  31.495  1.00 26.10           N  
ANISOU 1786  N   LYS A 236     3306   3306   3306      0      0      0       N  
ATOM   1787  CA  LYS A 236     123.603   3.357  32.807  1.00 32.18           C  
ANISOU 1787  CA  LYS A 236     4076   4076   4076      0      0      0       C  
ATOM   1788  C   LYS A 236     122.256   3.336  33.506  1.00 33.41           C  
ANISOU 1788  C   LYS A 236     4231   4231   4231      0      0      0       C  
ATOM   1789  O   LYS A 236     121.939   2.381  34.206  1.00 35.03           O  
ANISOU 1789  O   LYS A 236     4437   4437   4437      0      0      0       O  
ATOM   1790  CB  LYS A 236     124.637   4.041  33.720  1.00 28.60           C  
ANISOU 1790  CB  LYS A 236     3622   3622   3622      0      0      0       C  
ATOM   1791  CG  LYS A 236     126.062   3.856  33.313  1.00 57.46           C  
ANISOU 1791  CG  LYS A 236     7278   7278   7278      0      0      0       C  
ATOM   1792  CD  LYS A 236     127.017   4.442  34.347  1.00 84.99           C  
ANISOU 1792  CD  LYS A 236    10764  10764  10764      0      0      0       C  
ATOM   1793  CE  LYS A 236     128.466   4.191  33.949  1.00 95.40           C  
ANISOU 1793  CE  LYS A 236    12083  12083  12083      0      0      0       C  
ATOM   1794  NZ  LYS A 236     129.431   4.801  34.901  1.00100.00           N  
ANISOU 1794  NZ  LYS A 236    12665  12665  12665      0      0      0       N  
ATOM   1795  N   GLY A 237     121.451   4.369  33.292  1.00 26.58           N  
ANISOU 1795  N   GLY A 237     3367   3367   3367      0      0      0       N  
ATOM   1796  CA  GLY A 237     120.134   4.448  33.911  1.00 20.96           C  
ANISOU 1796  CA  GLY A 237     2655   2655   2655      0      0      0       C  
ATOM   1797  C   GLY A 237     119.187   3.469  33.240  1.00 27.87           C  
ANISOU 1797  C   GLY A 237     3530   3530   3530      0      0      0       C  
ATOM   1798  O   GLY A 237     118.319   2.886  33.874  1.00 26.68           O  
ANISOU 1798  O   GLY A 237     3379   3379   3379      0      0      0       O  
ATOM   1799  N   LEU A 238     119.318   3.345  31.929  1.00 17.08           N  
ANISOU 1799  N   LEU A 238     2163   2163   2163      0      0      0       N  
ATOM   1800  CA  LEU A 238     118.544   2.375  31.178  1.00 32.85           C  
ANISOU 1800  CA  LEU A 238     4160   4160   4160      0      0      0       C  
ATOM   1801  C   LEU A 238     118.816   0.962  31.714  1.00 27.11           C  
ANISOU 1801  C   LEU A 238     3434   3434   3434      0      0      0       C  
ATOM   1802  O   LEU A 238     117.887   0.194  31.999  1.00 28.65           O  
ANISOU 1802  O   LEU A 238     3628   3628   3628      0      0      0       O  
ATOM   1803  CB  LEU A 238     118.881   2.480  29.694  1.00 13.66           C  
ANISOU 1803  CB  LEU A 238     1730   1730   1730      0      0      0       C  
ATOM   1804  CG  LEU A 238     117.910   1.858  28.706  1.00 26.40           C  
ANISOU 1804  CG  LEU A 238     3343   3343   3343      0      0      0       C  
ATOM   1805  CD1 LEU A 238     116.599   2.610  28.762  1.00 18.81           C  
ANISOU 1805  CD1 LEU A 238     2382   2382   2382      0      0      0       C  
ATOM   1806  CD2 LEU A 238     118.526   1.934  27.329  1.00 17.66           C  
ANISOU 1806  CD2 LEU A 238     2236   2236   2236      0      0      0       C  
ATOM   1807  N   ARG A 239     120.095   0.708  31.973  1.00 24.34           N  
ANISOU 1807  N   ARG A 239     3082   3082   3082      0      0      0       N  
ATOM   1808  CA  ARG A 239     120.572  -0.552  32.521  1.00 28.85           C  
ANISOU 1808  CA  ARG A 239     3654   3654   3654      0      0      0       C  
ATOM   1809  C   ARG A 239     120.048  -0.794  33.944  1.00 27.77           C  
ANISOU 1809  C   ARG A 239     3517   3517   3517      0      0      0       C  
ATOM   1810  O   ARG A 239     119.451  -1.834  34.223  1.00 28.26           O  
ANISOU 1810  O   ARG A 239     3579   3579   3579      0      0      0       O  
ATOM   1811  CB  ARG A 239     122.105  -0.568  32.532  1.00 24.37           C  
ANISOU 1811  CB  ARG A 239     3086   3086   3086      0      0      0       C  
ATOM   1812  CG  ARG A 239     122.672  -1.877  33.027  1.00 21.27           C  
ANISOU 1812  CG  ARG A 239     2694   2694   2694      0      0      0       C  
ATOM   1813  CD  ARG A 239     124.151  -1.830  33.364  1.00 24.60           C  
ANISOU 1813  CD  ARG A 239     3116   3116   3116      0      0      0       C  
ATOM   1814  NE  ARG A 239     124.388  -0.952  34.499  1.00 33.58           N  
ANISOU 1814  NE  ARG A 239     4253   4253   4253      0      0      0       N  
ATOM   1815  CZ  ARG A 239     125.572  -0.477  34.846  1.00 40.63           C  
ANISOU 1815  CZ  ARG A 239     5146   5146   5146      0      0      0       C  
ATOM   1816  NH1 ARG A 239     126.660  -0.848  34.187  1.00 37.12           N  
ANISOU 1816  NH1 ARG A 239     4701   4701   4701      0      0      0       N  
ATOM   1817  NH2 ARG A 239     125.666   0.318  35.900  1.00 41.93           N  
ANISOU 1817  NH2 ARG A 239     5311   5311   5311      0      0      0       N  
ATOM   1818  N   ASP A 240     120.277   0.177  34.831  1.00 28.33           N  
ANISOU 1818  N   ASP A 240     3588   3588   3588      0      0      0       N  
ATOM   1819  CA  ASP A 240     120.068   0.014  36.264  1.00 19.96           C  
ANISOU 1819  CA  ASP A 240     2528   2528   2528      0      0      0       C  
ATOM   1820  C   ASP A 240     118.607   0.152  36.690  1.00 20.42           C  
ANISOU 1820  C   ASP A 240     2586   2586   2586      0      0      0       C  
ATOM   1821  O   ASP A 240     118.232  -0.289  37.771  1.00 27.50           O  
ANISOU 1821  O   ASP A 240     3482   3482   3482      0      0      0       O  
ATOM   1822  CB  ASP A 240     120.927   1.007  37.048  1.00 32.15           C  
ANISOU 1822  CB  ASP A 240     4072   4072   4072      0      0      0       C  
ATOM   1823  CG  ASP A 240     122.412   0.761  36.874  1.00 27.29           C  
ANISOU 1823  CG  ASP A 240     3457   3457   3457      0      0      0       C  
ATOM   1824  OD1 ASP A 240     122.819  -0.377  36.586  1.00 38.91           O  
ANISOU 1824  OD1 ASP A 240     4928   4928   4928      0      0      0       O  
ATOM   1825  OD2 ASP A 240     123.186   1.717  37.078  1.00 50.97           O  
ANISOU 1825  OD2 ASP A 240     6456   6456   6456      0      0      0       O  
ATOM   1826  N   ILE A 241     117.834   0.909  35.926  1.00 25.83           N  
ANISOU 1826  N   ILE A 241     3271   3271   3271      0      0      0       N  
ATOM   1827  CA  ILE A 241     116.400   1.079  36.181  1.00 26.12           C  
ANISOU 1827  CA  ILE A 241     3309   3309   3309      0      0      0       C  
ATOM   1828  C   ILE A 241     115.472   0.207  35.337  1.00 24.80           C  
ANISOU 1828  C   ILE A 241     3141   3141   3141      0      0      0       C  
ATOM   1829  O   ILE A 241     114.536  -0.384  35.853  1.00 34.75           O  
ANISOU 1829  O   ILE A 241     4402   4402   4402      0      0      0       O  
ATOM   1830  CB  ILE A 241     116.008   2.561  36.036  1.00 28.93           C  
ANISOU 1830  CB  ILE A 241     3664   3664   3664      0      0      0       C  
ATOM   1831  CG1 ILE A 241     116.802   3.369  37.063  1.00 17.46           C  
ANISOU 1831  CG1 ILE A 241     2211   2211   2211      0      0      0       C  
ATOM   1832  CG2 ILE A 241     114.532   2.789  36.319  1.00 25.77           C  
ANISOU 1832  CG2 ILE A 241     3264   3264   3264      0      0      0       C  
ATOM   1833  CD1 ILE A 241     116.472   4.843  37.057  1.00 41.47           C  
ANISOU 1833  CD1 ILE A 241     5253   5253   5253      0      0      0       C  
ATOM   1834  N   HIS A 242     115.654   0.242  34.023  1.00 20.60           N  
ANISOU 1834  N   HIS A 242     2609   2609   2609      0      0      0       N  
ATOM   1835  CA  HIS A 242     114.652  -0.325  33.116  1.00 23.89           C  
ANISOU 1835  CA  HIS A 242     3026   3026   3026      0      0      0       C  
ATOM   1836  C   HIS A 242     114.895  -1.777  32.629  1.00 24.75           C  
ANISOU 1836  C   HIS A 242     3134   3134   3134      0      0      0       C  
ATOM   1837  O   HIS A 242     114.059  -2.351  31.938  1.00 16.28           O  
ANISOU 1837  O   HIS A 242     2062   2062   2062      0      0      0       O  
ATOM   1838  CB  HIS A 242     114.424   0.633  31.947  1.00 18.82           C  
ANISOU 1838  CB  HIS A 242     2384   2384   2384      0      0      0       C  
ATOM   1839  CG  HIS A 242     113.848   1.944  32.378  1.00 24.70           C  
ANISOU 1839  CG  HIS A 242     3128   3128   3128      0      0      0       C  
ATOM   1840  ND1 HIS A 242     112.514   2.116  32.680  1.00 32.36           N  
ANISOU 1840  ND1 HIS A 242     4098   4098   4098      0      0      0       N  
ATOM   1841  CD2 HIS A 242     114.449   3.127  32.646  1.00 20.03           C  
ANISOU 1841  CD2 HIS A 242     2537   2537   2537      0      0      0       C  
ATOM   1842  CE1 HIS A 242     112.310   3.363  33.071  1.00 26.02           C  
ANISOU 1842  CE1 HIS A 242     3295   3295   3295      0      0      0       C  
ATOM   1843  NE2 HIS A 242     113.470   3.997  33.057  1.00 25.24           N  
ANISOU 1843  NE2 HIS A 242     3196   3196   3196      0      0      0       N  
ATOM   1844  N   SER A 243     116.087  -2.299  32.888  1.00 10.61           N  
ANISOU 1844  N   SER A 243     1344   1344   1344      0      0      0       N  
ATOM   1845  CA  SER A 243     116.490  -3.574  32.342  1.00 37.64           C  
ANISOU 1845  CA  SER A 243     4767   4767   4767      0      0      0       C  
ATOM   1846  C   SER A 243     116.528  -4.772  33.279  1.00 21.59           C  
ANISOU 1846  C   SER A 243     2735   2735   2735      0      0      0       C  
ATOM   1847  O   SER A 243     116.837  -5.870  32.848  1.00 37.90           O  
ANISOU 1847  O   SER A 243     4800   4800   4800      0      0      0       O  
ATOM   1848  CB  SER A 243     117.856  -3.380  31.708  1.00 27.40           C  
ANISOU 1848  CB  SER A 243     3471   3471   3471      0      0      0       C  
ATOM   1849  OG  SER A 243     117.765  -2.398  30.702  1.00 28.94           O  
ANISOU 1849  OG  SER A 243     3665   3665   3665      0      0      0       O  
ATOM   1850  N   ALA A 244     116.243  -4.534  34.551  1.00 32.13           N  
ANISOU 1850  N   ALA A 244     4070   4070   4070      0      0      0       N  
ATOM   1851  CA  ALA A 244     116.371  -5.549  35.591  1.00 49.76           C  
ANISOU 1851  CA  ALA A 244     6302   6302   6302      0      0      0       C  
ATOM   1852  C   ALA A 244     115.600  -6.841  35.301  1.00 32.09           C  
ANISOU 1852  C   ALA A 244     4064   4064   4064      0      0      0       C  
ATOM   1853  O   ALA A 244     116.118  -7.931  35.515  1.00 31.48           O  
ANISOU 1853  O   ALA A 244     3987   3987   3987      0      0      0       O  
ATOM   1854  CB  ALA A 244     115.953  -4.973  36.935  1.00 35.85           C  
ANISOU 1854  CB  ALA A 244     4541   4541   4541      0      0      0       C  
ATOM   1855  N   GLY A 245     114.390  -6.716  34.778  1.00 27.99           N  
ANISOU 1855  N   GLY A 245     3545   3545   3545      0      0      0       N  
ATOM   1856  CA  GLY A 245     113.625  -7.884  34.427  1.00 13.44           C  
ANISOU 1856  CA  GLY A 245     1702   1702   1702      0      0      0       C  
ATOM   1857  C   GLY A 245     114.300  -8.724  33.358  1.00 33.83           C  
ANISOU 1857  C   GLY A 245     4285   4285   4285      0      0      0       C  
ATOM   1858  O   GLY A 245     114.192  -9.956  33.356  1.00 28.68           O  
ANISOU 1858  O   GLY A 245     3632   3632   3632      0      0      0       O  
ATOM   1859  N   TYR A 246     115.041  -8.079  32.475  1.00 17.76           N  
ANISOU 1859  N   TYR A 246     2249   2249   2249      0      0      0       N  
ATOM   1860  CA  TYR A 246     115.697  -8.831  31.431  1.00 26.61           C  
ANISOU 1860  CA  TYR A 246     3371   3371   3371      0      0      0       C  
ATOM   1861  C   TYR A 246     116.910  -9.624  31.927  1.00 33.58           C  
ANISOU 1861  C   TYR A 246     4253   4253   4253      0      0      0       C  
ATOM   1862  O   TYR A 246     117.274 -10.619  31.310  1.00 23.41           O  
ANISOU 1862  O   TYR A 246     2965   2965   2965      0      0      0       O  
ATOM   1863  CB  TYR A 246     116.064  -7.934  30.261  1.00 17.78           C  
ANISOU 1863  CB  TYR A 246     2252   2252   2252      0      0      0       C  
ATOM   1864  CG  TYR A 246     114.862  -7.708  29.404  1.00 27.64           C  
ANISOU 1864  CG  TYR A 246     3500   3500   3500      0      0      0       C  
ATOM   1865  CD1 TYR A 246     114.423  -8.705  28.556  1.00 24.82           C  
ANISOU 1865  CD1 TYR A 246     3144   3144   3144      0      0      0       C  
ATOM   1866  CD2 TYR A 246     114.128  -6.521  29.475  1.00 23.82           C  
ANISOU 1866  CD2 TYR A 246     3017   3017   3017      0      0      0       C  
ATOM   1867  CE1 TYR A 246     113.313  -8.546  27.789  1.00 32.55           C  
ANISOU 1867  CE1 TYR A 246     4123   4123   4123      0      0      0       C  
ATOM   1868  CE2 TYR A 246     113.008  -6.343  28.699  1.00 22.61           C  
ANISOU 1868  CE2 TYR A 246     2863   2863   2863      0      0      0       C  
ATOM   1869  CZ  TYR A 246     112.599  -7.361  27.858  1.00 36.52           C  
ANISOU 1869  CZ  TYR A 246     4626   4626   4626      0      0      0       C  
ATOM   1870  OH  TYR A 246     111.477  -7.221  27.076  1.00 25.76           O  
ANISOU 1870  OH  TYR A 246     3262   3262   3262      0      0      0       O  
ATOM   1871  N   PHE A 247     117.554  -9.175  33.001  1.00 21.37           N  
ANISOU 1871  N   PHE A 247     2707   2707   2707      0      0      0       N  
ATOM   1872  CA  PHE A 247     118.686  -9.914  33.536  1.00 30.27           C  
ANISOU 1872  CA  PHE A 247     3833   3833   3833      0      0      0       C  
ATOM   1873  C   PHE A 247     118.240 -11.326  33.953  1.00 21.88           C  
ANISOU 1873  C   PHE A 247     2771   2771   2771      0      0      0       C  
ATOM   1874  O   PHE A 247     118.837 -12.312  33.540  1.00 27.82           O  
ANISOU 1874  O   PHE A 247     3523   3523   3523      0      0      0       O  
ATOM   1875  CB  PHE A 247     119.286  -9.174  34.727  1.00 38.60           C  
ANISOU 1875  CB  PHE A 247     4888   4888   4888      0      0      0       C  
ATOM   1876  CG  PHE A 247     119.837  -7.821  34.386  1.00 34.30           C  
ANISOU 1876  CG  PHE A 247     4345   4345   4345      0      0      0       C  
ATOM   1877  CD1 PHE A 247     120.133  -7.486  33.080  1.00 32.46           C  
ANISOU 1877  CD1 PHE A 247     4111   4111   4111      0      0      0       C  
ATOM   1878  CD2 PHE A 247     119.991  -6.863  35.362  1.00 44.76           C  
ANISOU 1878  CD2 PHE A 247     5669   5669   5669      0      0      0       C  
ATOM   1879  CE1 PHE A 247     120.610  -6.241  32.756  1.00 30.53           C  
ANISOU 1879  CE1 PHE A 247     3867   3867   3867      0      0      0       C  
ATOM   1880  CE2 PHE A 247     120.470  -5.607  35.042  1.00 45.21           C  
ANISOU 1880  CE2 PHE A 247     5727   5727   5727      0      0      0       C  
ATOM   1881  CZ  PHE A 247     120.784  -5.301  33.734  1.00 25.28           C  
ANISOU 1881  CZ  PHE A 247     3202   3202   3202      0      0      0       C  
ATOM   1882  N   SER A 248     117.157 -11.406  34.729  1.00 30.47           N  
ANISOU 1882  N   SER A 248     3860   3860   3860      0      0      0       N  
ATOM   1883  CA  SER A 248     116.664 -12.692  35.221  1.00 35.99           C  
ANISOU 1883  CA  SER A 248     4558   4558   4558      0      0      0       C  
ATOM   1884  C   SER A 248     115.898 -13.447  34.155  1.00 31.26           C  
ANISOU 1884  C   SER A 248     3959   3959   3959      0      0      0       C  
ATOM   1885  O   SER A 248     116.002 -14.654  34.082  1.00 24.63           O  
ANISOU 1885  O   SER A 248     3120   3120   3120      0      0      0       O  
ATOM   1886  CB  SER A 248     115.863 -12.549  36.511  1.00 29.51           C  
ANISOU 1886  CB  SER A 248     3738   3738   3738      0      0      0       C  
ATOM   1887  OG  SER A 248     114.663 -11.845  36.271  1.00 36.47           O  
ANISOU 1887  OG  SER A 248     4619   4619   4619      0      0      0       O  
ATOM   1888  N   ALA A 249     115.196 -12.734  33.274  1.00 22.73           N  
ANISOU 1888  N   ALA A 249     2879   2879   2879      0      0      0       N  
ATOM   1889  CA  ALA A 249     114.449 -13.422  32.225  1.00 27.54           C  
ANISOU 1889  CA  ALA A 249     3488   3488   3488      0      0      0       C  
ATOM   1890  C   ALA A 249     115.409 -14.115  31.256  1.00 35.54           C  
ANISOU 1890  C   ALA A 249     4501   4501   4501      0      0      0       C  
ATOM   1891  O   ALA A 249     115.196 -15.270  30.903  1.00 28.87           O  
ANISOU 1891  O   ALA A 249     3656   3656   3656      0      0      0       O  
ATOM   1892  CB  ALA A 249     113.538 -12.483  31.497  1.00 14.50           C  
ANISOU 1892  CB  ALA A 249     1837   1837   1837      0      0      0       C  
ATOM   1893  N   ILE A 250     116.481 -13.415  30.873  1.00 23.65           N  
ANISOU 1893  N   ILE A 250     2995   2995   2995      0      0      0       N  
ATOM   1894  CA  ILE A 250     117.518 -13.964  29.991  1.00 27.51           C  
ANISOU 1894  CA  ILE A 250     3484   3484   3484      0      0      0       C  
ATOM   1895  C   ILE A 250     118.271 -15.065  30.717  1.00 30.82           C  
ANISOU 1895  C   ILE A 250     3903   3903   3903      0      0      0       C  
ATOM   1896  O   ILE A 250     118.652 -16.064  30.100  1.00 22.44           O  
ANISOU 1896  O   ILE A 250     2843   2843   2843      0      0      0       O  
ATOM   1897  CB  ILE A 250     118.486 -12.907  29.468  1.00 11.89           C  
ANISOU 1897  CB  ILE A 250     1506   1506   1506      0      0      0       C  
ATOM   1898  CG1 ILE A 250     117.761 -11.989  28.482  1.00 33.75           C  
ANISOU 1898  CG1 ILE A 250     4275   4275   4275      0      0      0       C  
ATOM   1899  CG2 ILE A 250     119.633 -13.550  28.707  1.00 12.49           C  
ANISOU 1899  CG2 ILE A 250     1581   1581   1581      0      0      0       C  
ATOM   1900  CD1 ILE A 250     118.511 -10.675  28.222  1.00 21.08           C  
ANISOU 1900  CD1 ILE A 250     2670   2670   2670      0      0      0       C  
ATOM   1901  N   ASN A 251     118.525 -14.854  32.009  1.00 30.54           N  
ANISOU 1901  N   ASN A 251     3868   3868   3868      0      0      0       N  
ATOM   1902  CA  ASN A 251     119.210 -15.870  32.793  1.00 27.63           C  
ANISOU 1902  CA  ASN A 251     3499   3499   3499      0      0      0       C  
ATOM   1903  C   ASN A 251     118.492 -17.205  32.855  1.00 37.81           C  
ANISOU 1903  C   ASN A 251     4788   4788   4788      0      0      0       C  
ATOM   1904  O   ASN A 251     119.110 -18.257  32.722  1.00 33.17           O  
ANISOU 1904  O   ASN A 251     4201   4201   4201      0      0      0       O  
ATOM   1905  CB  ASN A 251     119.451 -15.381  34.221  1.00 32.11           C  
ANISOU 1905  CB  ASN A 251     4067   4067   4067      0      0      0       C  
ATOM   1906  CG  ASN A 251     120.412 -16.244  34.988  1.00 42.76           C  
ANISOU 1906  CG  ASN A 251     5416   5416   5416      0      0      0       C  
ATOM   1907  OD1 ASN A 251     121.423 -16.691  34.473  1.00 37.70           O  
ANISOU 1907  OD1 ASN A 251     4775   4775   4775      0      0      0       O  
ATOM   1908  ND2 ASN A 251     120.021 -16.584  36.213  1.00 36.33           N  
ANISOU 1908  ND2 ASN A 251     4601   4601   4601      0      0      0       N  
ATOM   1909  N   GLN A 252     117.168 -17.132  32.917  1.00 30.77           N  
ANISOU 1909  N   GLN A 252     3898   3898   3898      0      0      0       N  
ATOM   1910  CA  GLN A 252     116.299 -18.295  32.945  1.00 15.90           C  
ANISOU 1910  CA  GLN A 252     2014   2014   2014      0      0      0       C  
ATOM   1911  C   GLN A 252     115.993 -18.846  31.576  1.00 15.20           C  
ANISOU 1911  C   GLN A 252     1925   1925   1925      0      0      0       C  
ATOM   1912  O   GLN A 252     115.139 -19.708  31.430  1.00 49.16           O  
ANISOU 1912  O   GLN A 252     6227   6227   6227      0      0      0       O  
ATOM   1913  CB  GLN A 252     115.010 -17.998  33.711  1.00 17.26           C  
ANISOU 1913  CB  GLN A 252     2185   2185   2185      0      0      0       C  
ATOM   1914  CG  GLN A 252     115.182 -17.680  35.208  1.00 30.10           C  
ANISOU 1914  CG  GLN A 252     3812   3812   3812      0      0      0       C  
ATOM   1915  CD  GLN A 252     115.994 -18.763  35.955  1.00 45.46           C  
ANISOU 1915  CD  GLN A 252     5758   5758   5758      0      0      0       C  
ATOM   1916  OE1 GLN A 252     115.985 -19.927  35.568  1.00 36.48           O  
ANISOU 1916  OE1 GLN A 252     4620   4620   4620      0      0      0       O  
ATOM   1917  NE2 GLN A 252     116.565 -18.401  37.095  1.00 69.49           N  
ANISOU 1917  NE2 GLN A 252     8800   8800   8800      0      0      0       N  
ATOM   1918  N   GLY A 253     116.618 -18.295  30.555  1.00 27.83           N  
ANISOU 1918  N   GLY A 253     3525   3525   3525      0      0      0       N  
ATOM   1919  CA  GLY A 253     116.526 -18.898  29.244  1.00 17.62           C  
ANISOU 1919  CA  GLY A 253     2231   2231   2231      0      0      0       C  
ATOM   1920  C   GLY A 253     115.285 -18.520  28.452  1.00 32.17           C  
ANISOU 1920  C   GLY A 253     4074   4074   4074      0      0      0       C  
ATOM   1921  O   GLY A 253     114.829 -19.327  27.619  1.00 18.11           O  
ANISOU 1921  O   GLY A 253     2293   2293   2293      0      0      0       O  
ATOM   1922  N   VAL A 254     114.729 -17.328  28.707  1.00 22.72           N  
ANISOU 1922  N   VAL A 254     2877   2877   2877      0      0      0       N  
ATOM   1923  CA  VAL A 254     113.564 -16.869  27.953  1.00 20.08           C  
ANISOU 1923  CA  VAL A 254     2543   2543   2543      0      0      0       C  
ATOM   1924  C   VAL A 254     113.898 -16.957  26.468  1.00 14.51           C  
ANISOU 1924  C   VAL A 254     1838   1838   1838      0      0      0       C  
ATOM   1925  O   VAL A 254     115.004 -16.647  26.057  1.00 27.47           O  
ANISOU 1925  O   VAL A 254     3479   3479   3479      0      0      0       O  
ATOM   1926  CB  VAL A 254     113.157 -15.414  28.358  1.00 23.93           C  
ANISOU 1926  CB  VAL A 254     3031   3031   3031      0      0      0       C  
ATOM   1927  CG1 VAL A 254     114.115 -14.383  27.806  1.00 13.58           C  
ANISOU 1927  CG1 VAL A 254     1719   1719   1719      0      0      0       C  
ATOM   1928  CG2 VAL A 254     111.710 -15.118  27.931  1.00 20.11           C  
ANISOU 1928  CG2 VAL A 254     2547   2547   2547      0      0      0       C  
ATOM   1929  N   GLN A 255     112.967 -17.482  25.677  1.00 26.33           N  
ANISOU 1929  N   GLN A 255     3335   3335   3335      0      0      0       N  
ATOM   1930  CA  GLN A 255     113.275 -17.771  24.275  1.00 20.48           C  
ANISOU 1930  CA  GLN A 255     2594   2594   2594      0      0      0       C  
ATOM   1931  C   GLN A 255     113.121 -16.595  23.340  1.00 31.90           C  
ANISOU 1931  C   GLN A 255     4041   4041   4041      0      0      0       C  
ATOM   1932  O   GLN A 255     113.781 -16.514  22.307  1.00 25.52           O  
ANISOU 1932  O   GLN A 255     3232   3232   3232      0      0      0       O  
ATOM   1933  CB  GLN A 255     112.431 -18.946  23.753  1.00 19.54           C  
ANISOU 1933  CB  GLN A 255     2475   2475   2475      0      0      0       C  
ATOM   1934  CG  GLN A 255     112.876 -20.292  24.275  1.00 14.85           C  
ANISOU 1934  CG  GLN A 255     1881   1881   1881      0      0      0       C  
ATOM   1935  CD  GLN A 255     114.292 -20.604  23.838  1.00 25.53           C  
ANISOU 1935  CD  GLN A 255     3234   3234   3234      0      0      0       C  
ATOM   1936  OE1 GLN A 255     114.553 -20.943  22.688  1.00 24.05           O  
ANISOU 1936  OE1 GLN A 255     3047   3047   3047      0      0      0       O  
ATOM   1937  NE2 GLN A 255     115.220 -20.468  24.765  1.00 14.33           N  
ANISOU 1937  NE2 GLN A 255     1815   1815   1815      0      0      0       N  
ATOM   1938  N   SER A 256     112.292 -15.647  23.745  1.00 27.12           N  
ANISOU 1938  N   SER A 256     3434   3434   3434      0      0      0       N  
ATOM   1939  CA  SER A 256     111.982 -14.515  22.908  1.00 34.46           C  
ANISOU 1939  CA  SER A 256     4364   4364   4364      0      0      0       C  
ATOM   1940  C   SER A 256     111.972 -13.219  23.696  1.00 30.18           C  
ANISOU 1940  C   SER A 256     3822   3822   3822      0      0      0       C  
ATOM   1941  O   SER A 256     111.559 -13.188  24.855  1.00 22.62           O  
ANISOU 1941  O   SER A 256     2865   2865   2865      0      0      0       O  
ATOM   1942  CB  SER A 256     110.610 -14.746  22.263  1.00 29.39           C  
ANISOU 1942  CB  SER A 256     3723   3723   3723      0      0      0       C  
ATOM   1943  OG  SER A 256     110.221 -13.681  21.430  1.00 32.64           O  
ANISOU 1943  OG  SER A 256     4134   4134   4134      0      0      0       O  
ATOM   1944  N   VAL A 257     112.406 -12.142  23.044  1.00 26.12           N  
ANISOU 1944  N   VAL A 257     3308   3308   3308      0      0      0       N  
ATOM   1945  CA  VAL A 257     112.321 -10.802  23.617  1.00 21.54           C  
ANISOU 1945  CA  VAL A 257     2728   2728   2728      0      0      0       C  
ATOM   1946  C   VAL A 257     111.576  -9.894  22.638  1.00 25.37           C  
ANISOU 1946  C   VAL A 257     3214   3214   3214      0      0      0       C  
ATOM   1947  O   VAL A 257     111.897  -9.875  21.446  1.00 17.25           O  
ANISOU 1947  O   VAL A 257     2184   2184   2184      0      0      0       O  
ATOM   1948  CB  VAL A 257     113.734 -10.254  23.874  1.00 28.28           C  
ANISOU 1948  CB  VAL A 257     3582   3582   3582      0      0      0       C  
ATOM   1949  CG1 VAL A 257     113.676  -8.778  24.249  1.00 27.60           C  
ANISOU 1949  CG1 VAL A 257     3496   3496   3496      0      0      0       C  
ATOM   1950  CG2 VAL A 257     114.373 -11.022  25.000  1.00 17.46           C  
ANISOU 1950  CG2 VAL A 257     2211   2211   2211      0      0      0       C  
ATOM   1951  N   MET A 258     110.592  -9.138  23.129  1.00 22.23           N  
ANISOU 1951  N   MET A 258     2815   2815   2815      0      0      0       N  
ATOM   1952  CA  MET A 258     109.886  -8.197  22.262  1.00 25.21           C  
ANISOU 1952  CA  MET A 258     3193   3193   3193      0      0      0       C  
ATOM   1953  C   MET A 258     110.458  -6.769  22.386  1.00 25.24           C  
ANISOU 1953  C   MET A 258     3196   3196   3196      0      0      0       C  
ATOM   1954  O   MET A 258     110.604  -6.234  23.483  1.00 22.00           O  
ANISOU 1954  O   MET A 258     2787   2787   2787      0      0      0       O  
ATOM   1955  CB  MET A 258     108.375  -8.223  22.544  1.00 14.08           C  
ANISOU 1955  CB  MET A 258     1783   1783   1783      0      0      0       C  
ATOM   1956  CG  MET A 258     107.574  -7.382  21.565  1.00 13.20           C  
ANISOU 1956  CG  MET A 258     1672   1672   1672      0      0      0       C  
ATOM   1957  SD  MET A 258     105.788  -7.375  21.857  1.00 25.65           S  
ANISOU 1957  SD  MET A 258     3249   3249   3249      0      0      0       S  
ATOM   1958  CE  MET A 258     105.347  -9.058  21.397  1.00 31.54           C  
ANISOU 1958  CE  MET A 258     3994   3994   3994      0      0      0       C  
ATOM   1959  N   ALA A 259     110.765  -6.151  21.258  1.00 22.74           N  
ANISOU 1959  N   ALA A 259     2880   2880   2880      0      0      0       N  
ATOM   1960  CA  ALA A 259     111.268  -4.787  21.264  1.00 29.31           C  
ANISOU 1960  CA  ALA A 259     3712   3712   3712      0      0      0       C  
ATOM   1961  C   ALA A 259     110.175  -3.771  21.628  1.00 25.88           C  
ANISOU 1961  C   ALA A 259     3278   3278   3278      0      0      0       C  
ATOM   1962  O   ALA A 259     108.987  -4.067  21.510  1.00 26.26           O  
ANISOU 1962  O   ALA A 259     3326   3326   3326      0      0      0       O  
ATOM   1963  CB  ALA A 259     111.875  -4.458  19.921  1.00 17.76           C  
ANISOU 1963  CB  ALA A 259     2249   2249   2249      0      0      0       C  
ATOM   1964  N   SER A 260     110.573  -2.586  22.082  1.00 19.49           N  
ANISOU 1964  N   SER A 260     2469   2469   2469      0      0      0       N  
ATOM   1965  CA  SER A 260     109.594  -1.630  22.632  1.00 29.82           C  
ANISOU 1965  CA  SER A 260     3777   3777   3777      0      0      0       C  
ATOM   1966  C   SER A 260     109.231  -0.505  21.655  1.00 27.15           C  
ANISOU 1966  C   SER A 260     3438   3438   3438      0      0      0       C  
ATOM   1967  O   SER A 260     110.039  -0.140  20.788  1.00 20.53           O  
ANISOU 1967  O   SER A 260     2600   2600   2600      0      0      0       O  
ATOM   1968  CB  SER A 260     110.111  -1.009  23.925  1.00 17.55           C  
ANISOU 1968  CB  SER A 260     2223   2223   2223      0      0      0       C  
ATOM   1969  OG  SER A 260     111.326  -0.313  23.721  1.00 30.14           O  
ANISOU 1969  OG  SER A 260     3817   3817   3817      0      0      0       O  
ATOM   1970  N   PHE A 261     108.020   0.029  21.800  1.00 14.59           N  
ANISOU 1970  N   PHE A 261     1847   1847   1847      0      0      0       N  
ATOM   1971  CA  PHE A 261     107.545   1.131  20.960  1.00 27.34           C  
ANISOU 1971  CA  PHE A 261     3463   3463   3463      0      0      0       C  
ATOM   1972  C   PHE A 261     108.223   2.476  21.194  1.00 34.56           C  
ANISOU 1972  C   PHE A 261     4377   4377   4377      0      0      0       C  
ATOM   1973  O   PHE A 261     108.315   3.292  20.286  1.00 21.76           O  
ANISOU 1973  O   PHE A 261     2756   2756   2756      0      0      0       O  
ATOM   1974  CB  PHE A 261     106.050   1.382  21.212  1.00 16.70           C  
ANISOU 1974  CB  PHE A 261     2115   2115   2115      0      0      0       C  
ATOM   1975  CG  PHE A 261     105.120   0.446  20.498  1.00 22.01           C  
ANISOU 1975  CG  PHE A 261     2787   2787   2787      0      0      0       C  
ATOM   1976  CD1 PHE A 261     105.109   0.414  19.125  1.00 16.01           C  
ANISOU 1976  CD1 PHE A 261     2028   2028   2028      0      0      0       C  
ATOM   1977  CD2 PHE A 261     104.210  -0.342  21.183  1.00 23.86           C  
ANISOU 1977  CD2 PHE A 261     3022   3022   3022      0      0      0       C  
ATOM   1978  CE1 PHE A 261     104.240  -0.399  18.439  1.00 26.22           C  
ANISOU 1978  CE1 PHE A 261     3321   3321   3321      0      0      0       C  
ATOM   1979  CE2 PHE A 261     103.331  -1.145  20.491  1.00 15.59           C  
ANISOU 1979  CE2 PHE A 261     1975   1975   1975      0      0      0       C  
ATOM   1980  CZ  PHE A 261     103.356  -1.182  19.120  1.00 23.25           C  
ANISOU 1980  CZ  PHE A 261     2945   2945   2945      0      0      0       C  
ATOM   1981  N   ASN A 262     108.678   2.710  22.409  1.00 23.75           N  
ANISOU 1981  N   ASN A 262     3008   3008   3008      0      0      0       N  
ATOM   1982  CA  ASN A 262     109.224   4.005  22.751  1.00 31.58           C  
ANISOU 1982  CA  ASN A 262     3999   3999   3999      0      0      0       C  
ATOM   1983  C   ASN A 262     110.527   4.297  22.030  1.00 31.13           C  
ANISOU 1983  C   ASN A 262     3943   3943   3943      0      0      0       C  
ATOM   1984  O   ASN A 262     111.175   3.392  21.489  1.00 31.19           O  
ANISOU 1984  O   ASN A 262     3951   3951   3951      0      0      0       O  
ATOM   1985  CB  ASN A 262     109.410   4.098  24.266  1.00 20.06           C  
ANISOU 1985  CB  ASN A 262     2541   2541   2541      0      0      0       C  
ATOM   1986  CG  ASN A 262     110.371   3.036  24.787  1.00 29.27           C  
ANISOU 1986  CG  ASN A 262     3707   3707   3707      0      0      0       C  
ATOM   1987  OD1 ASN A 262     109.997   1.868  24.848  1.00 33.94           O  
ANISOU 1987  OD1 ASN A 262     4298   4298   4298      0      0      0       O  
ATOM   1988  ND2 ASN A 262     111.575   3.420  25.175  1.00  8.51           N  
ANISOU 1988  ND2 ASN A 262     1077   1077   1077      0      0      0       N  
ATOM   1989  N   SER A 263     110.955   5.547  22.113  1.00 31.68           N  
ANISOU 1989  N   SER A 263     4012   4012   4012      0      0      0       N  
ATOM   1990  CA  SER A 263     112.274   5.921  21.641  1.00 28.00           C  
ANISOU 1990  CA  SER A 263     3546   3546   3546      0      0      0       C  
ATOM   1991  C   SER A 263     113.155   6.055  22.857  1.00 11.98           C  
ANISOU 1991  C   SER A 263     1517   1517   1517      0      0      0       C  
ATOM   1992  O   SER A 263     112.673   6.204  23.975  1.00 10.41           O  
ANISOU 1992  O   SER A 263     1319   1319   1319      0      0      0       O  
ATOM   1993  CB  SER A 263     112.228   7.235  20.856  1.00 31.15           C  
ANISOU 1993  CB  SER A 263     3945   3945   3945      0      0      0       C  
ATOM   1994  OG  SER A 263     111.689   8.312  21.612  1.00 27.34           O  
ANISOU 1994  OG  SER A 263     3463   3463   3463      0      0      0       O  
ATOM   1995  N   TRP A 264     114.454   5.963  22.626  1.00 20.55           N  
ANISOU 1995  N   TRP A 264     2602   2602   2602      0      0      0       N  
ATOM   1996  CA  TRP A 264     115.441   6.234  23.655  1.00 27.59           C  
ANISOU 1996  CA  TRP A 264     3495   3495   3495      0      0      0       C  
ATOM   1997  C   TRP A 264     116.285   7.403  23.192  1.00 22.66           C  
ANISOU 1997  C   TRP A 264     2870   2870   2870      0      0      0       C  
ATOM   1998  O   TRP A 264     116.904   7.341  22.134  1.00 24.08           O  
ANISOU 1998  O   TRP A 264     3050   3050   3050      0      0      0       O  
ATOM   1999  CB  TRP A 264     116.326   5.010  23.914  1.00 15.44           C  
ANISOU 1999  CB  TRP A 264     1955   1955   1955      0      0      0       C  
ATOM   2000  CG  TRP A 264     117.440   5.250  24.862  1.00 17.22           C  
ANISOU 2000  CG  TRP A 264     2181   2181   2181      0      0      0       C  
ATOM   2001  CD1 TRP A 264     117.350   5.875  26.071  1.00 22.29           C  
ANISOU 2001  CD1 TRP A 264     2823   2823   2823      0      0      0       C  
ATOM   2002  CD2 TRP A 264     118.812   4.867  24.709  1.00 21.98           C  
ANISOU 2002  CD2 TRP A 264     2783   2783   2783      0      0      0       C  
ATOM   2003  NE1 TRP A 264     118.579   5.909  26.678  1.00 14.93           N  
ANISOU 2003  NE1 TRP A 264     1891   1891   1891      0      0      0       N  
ATOM   2004  CE2 TRP A 264     119.497   5.303  25.861  1.00 19.07           C  
ANISOU 2004  CE2 TRP A 264     2415   2415   2415      0      0      0       C  
ATOM   2005  CE3 TRP A 264     119.530   4.207  23.709  1.00 26.20           C  
ANISOU 2005  CE3 TRP A 264     3319   3319   3319      0      0      0       C  
ATOM   2006  CZ2 TRP A 264     120.866   5.092  26.046  1.00 16.75           C  
ANISOU 2006  CZ2 TRP A 264     2122   2122   2122      0      0      0       C  
ATOM   2007  CZ3 TRP A 264     120.885   4.012  23.891  1.00 17.96           C  
ANISOU 2007  CZ3 TRP A 264     2275   2275   2275      0      0      0       C  
ATOM   2008  CH2 TRP A 264     121.540   4.453  25.051  1.00 25.52           C  
ANISOU 2008  CH2 TRP A 264     3232   3232   3232      0      0      0       C  
ATOM   2009  N   ASN A 265     116.241   8.484  23.965  1.00 25.72           N  
ANISOU 2009  N   ASN A 265     3257   3257   3257      0      0      0       N  
ATOM   2010  CA  ASN A 265     116.931   9.728  23.656  1.00 24.40           C  
ANISOU 2010  CA  ASN A 265     3091   3091   3091      0      0      0       C  
ATOM   2011  C   ASN A 265     116.714  10.113  22.187  1.00 11.23           C  
ANISOU 2011  C   ASN A 265     1422   1422   1422      0      0      0       C  
ATOM   2012  O   ASN A 265     117.652  10.419  21.466  1.00 28.87           O  
ANISOU 2012  O   ASN A 265     3657   3657   3657      0      0      0       O  
ATOM   2013  CB  ASN A 265     118.423   9.611  23.977  1.00 12.39           C  
ANISOU 2013  CB  ASN A 265     1569   1569   1569      0      0      0       C  
ATOM   2014  CG  ASN A 265     118.678   9.383  25.471  1.00 18.74           C  
ANISOU 2014  CG  ASN A 265     2374   2374   2374      0      0      0       C  
ATOM   2015  OD1 ASN A 265     117.884   9.771  26.317  1.00 29.24           O  
ANISOU 2015  OD1 ASN A 265     3703   3703   3703      0      0      0       O  
ATOM   2016  ND2 ASN A 265     119.801   8.757  25.790  1.00 18.35           N  
ANISOU 2016  ND2 ASN A 265     2324   2324   2324      0      0      0       N  
ATOM   2017  N   GLY A 266     115.472  10.020  21.741  1.00 23.40           N  
ANISOU 2017  N   GLY A 266     2964   2964   2964      0      0      0       N  
ATOM   2018  CA  GLY A 266     115.057  10.452  20.418  1.00 22.34           C  
ANISOU 2018  CA  GLY A 266     2829   2829   2829      0      0      0       C  
ATOM   2019  C   GLY A 266     115.075   9.377  19.331  1.00 36.69           C  
ANISOU 2019  C   GLY A 266     4647   4647   4647      0      0      0       C  
ATOM   2020  O   GLY A 266     114.438   9.553  18.287  1.00 32.79           O  
ANISOU 2020  O   GLY A 266     4152   4152   4152      0      0      0       O  
ATOM   2021  N   LYS A 267     115.644   8.204  19.605  1.00 23.37           N  
ANISOU 2021  N   LYS A 267     2960   2960   2960      0      0      0       N  
ATOM   2022  CA  LYS A 267     115.680   7.175  18.560  1.00 32.37           C  
ANISOU 2022  CA  LYS A 267     4100   4100   4100      0      0      0       C  
ATOM   2023  C   LYS A 267     114.865   5.951  18.925  1.00 18.50           C  
ANISOU 2023  C   LYS A 267     2343   2343   2343      0      0      0       C  
ATOM   2024  O   LYS A 267     114.985   5.399  20.014  1.00 20.34           O  
ANISOU 2024  O   LYS A 267     2576   2576   2576      0      0      0       O  
ATOM   2025  CB  LYS A 267     117.128   6.741  18.260  1.00 38.10           C  
ANISOU 2025  CB  LYS A 267     4825   4825   4825      0      0      0       C  
ATOM   2026  CG  LYS A 267     117.176   5.578  17.240  0.70 14.71           C  
ANISOU 2026  CG  LYS A 267     1863   1863   1863      0      0      0       C  
ATOM   2027  CD  LYS A 267     118.476   4.795  17.290  0.70 19.47           C  
ANISOU 2027  CD  LYS A 267     2466   2466   2466      0      0      0       C  
ATOM   2028  CE  LYS A 267     119.352   5.099  16.073  0.70 38.60           C  
ANISOU 2028  CE  LYS A 267     4889   4889   4889      0      0      0       C  
ATOM   2029  NZ  LYS A 267     120.060   6.389  16.137  0.70 52.47           N  
ANISOU 2029  NZ  LYS A 267     6646   6646   6646      0      0      0       N  
ATOM   2030  N   ARG A 268     114.001   5.565  17.994  1.00 22.81           N  
ANISOU 2030  N   ARG A 268     2889   2889   2889      0      0      0       N  
ATOM   2031  CA  ARG A 268     113.158   4.402  18.180  1.00 26.90           C  
ANISOU 2031  CA  ARG A 268     3407   3407   3407      0      0      0       C  
ATOM   2032  C   ARG A 268     113.990   3.134  18.453  1.00 22.48           C  
ANISOU 2032  C   ARG A 268     2847   2847   2847      0      0      0       C  
ATOM   2033  O   ARG A 268     114.929   2.821  17.713  1.00 21.88           O  
ANISOU 2033  O   ARG A 268     2771   2771   2771      0      0      0       O  
ATOM   2034  CB  ARG A 268     112.284   4.165  16.957  1.00 11.81           C  
ANISOU 2034  CB  ARG A 268     1496   1496   1496      0      0      0       C  
ATOM   2035  CG  ARG A 268     111.215   5.220  16.673  1.00 32.08           C  
ANISOU 2035  CG  ARG A 268     4063   4063   4063      0      0      0       C  
ATOM   2036  CD  ARG A 268     110.040   5.077  17.610  1.00 10.32           C  
ANISOU 2036  CD  ARG A 268     1306   1306   1306      0      0      0       C  
ATOM   2037  NE  ARG A 268     109.032   6.099  17.352  1.00 30.11           N  
ANISOU 2037  NE  ARG A 268     3813   3813   3813      0      0      0       N  
ATOM   2038  CZ  ARG A 268     108.094   6.494  18.210  1.00 28.22           C  
ANISOU 2038  CZ  ARG A 268     3575   3575   3575      0      0      0       C  
ATOM   2039  NH1 ARG A 268     108.055   6.012  19.444  1.00 26.67           N  
ANISOU 2039  NH1 ARG A 268     3378   3378   3378      0      0      0       N  
ATOM   2040  NH2 ARG A 268     107.228   7.431  17.852  1.00 32.61           N  
ANISOU 2040  NH2 ARG A 268     4130   4130   4130      0      0      0       N  
ATOM   2041  N   VAL A 269     113.652   2.438  19.536  1.00 24.09           N  
ANISOU 2041  N   VAL A 269     3051   3051   3051      0      0      0       N  
ATOM   2042  CA  VAL A 269     114.347   1.206  19.921  1.00 25.24           C  
ANISOU 2042  CA  VAL A 269     3197   3197   3197      0      0      0       C  
ATOM   2043  C   VAL A 269     114.325   0.158  18.789  1.00 18.72           C  
ANISOU 2043  C   VAL A 269     2371   2371   2371      0      0      0       C  
ATOM   2044  O   VAL A 269     115.297  -0.564  18.591  1.00 20.93           O  
ANISOU 2044  O   VAL A 269     2651   2651   2651      0      0      0       O  
ATOM   2045  CB  VAL A 269     113.771   0.626  21.212  1.00 31.70           C  
ANISOU 2045  CB  VAL A 269     4015   4015   4015      0      0      0       C  
ATOM   2046  CG1 VAL A 269     114.457  -0.691  21.539  1.00 24.16           C  
ANISOU 2046  CG1 VAL A 269     3060   3060   3060      0      0      0       C  
ATOM   2047  CG2 VAL A 269     114.012   1.602  22.340  1.00 29.98           C  
ANISOU 2047  CG2 VAL A 269     3796   3796   3796      0      0      0       C  
ATOM   2048  N   HIS A 270     113.223   0.072  18.052  1.00 19.79           N  
ANISOU 2048  N   HIS A 270     2507   2507   2507      0      0      0       N  
ATOM   2049  CA  HIS A 270     113.103  -0.935  17.004  1.00 10.02           C  
ANISOU 2049  CA  HIS A 270     1270   1270   1270      0      0      0       C  
ATOM   2050  C   HIS A 270     114.121  -0.780  15.890  1.00 21.94           C  
ANISOU 2050  C   HIS A 270     2779   2779   2779      0      0      0       C  
ATOM   2051  O   HIS A 270     114.335  -1.720  15.125  1.00 20.85           O  
ANISOU 2051  O   HIS A 270     2641   2641   2641      0      0      0       O  
ATOM   2052  CB  HIS A 270     111.706  -0.933  16.393  1.00 17.03           C  
ANISOU 2052  CB  HIS A 270     2157   2157   2157      0      0      0       C  
ATOM   2053  CG  HIS A 270     110.729  -1.795  17.120  1.00 22.59           C  
ANISOU 2053  CG  HIS A 270     2861   2861   2861      0      0      0       C  
ATOM   2054  ND1 HIS A 270     110.217  -1.457  18.350  1.00 22.21           N  
ANISOU 2054  ND1 HIS A 270     2814   2814   2814      0      0      0       N  
ATOM   2055  CD2 HIS A 270     110.169  -2.987  16.790  1.00 17.84           C  
ANISOU 2055  CD2 HIS A 270     2260   2260   2260      0      0      0       C  
ATOM   2056  CE1 HIS A 270     109.391  -2.404  18.757  1.00 28.46           C  
ANISOU 2056  CE1 HIS A 270     3604   3604   3604      0      0      0       C  
ATOM   2057  NE2 HIS A 270     109.341  -3.343  17.828  1.00 23.33           N  
ANISOU 2057  NE2 HIS A 270     2954   2954   2954      0      0      0       N  
ATOM   2058  N   GLY A 271     114.740   0.395  15.790  1.00 15.37           N  
ANISOU 2058  N   GLY A 271     1947   1947   1947      0      0      0       N  
ATOM   2059  CA  GLY A 271     115.736   0.635  14.760  1.00 11.91           C  
ANISOU 2059  CA  GLY A 271     1509   1509   1509      0      0      0       C  
ATOM   2060  C   GLY A 271     117.146   0.771  15.319  1.00 19.71           C  
ANISOU 2060  C   GLY A 271     2496   2496   2496      0      0      0       C  
ATOM   2061  O   GLY A 271     118.077   1.137  14.610  1.00 17.30           O  
ANISOU 2061  O   GLY A 271     2191   2191   2191      0      0      0       O  
ATOM   2062  N   ASP A 272     117.304   0.464  16.598  1.00 14.71           N  
ANISOU 2062  N   ASP A 272     1863   1863   1863      0      0      0       N  
ATOM   2063  CA  ASP A 272     118.558   0.732  17.300  1.00 19.80           C  
ANISOU 2063  CA  ASP A 272     2508   2508   2508      0      0      0       C  
ATOM   2064  C   ASP A 272     119.447  -0.505  17.426  1.00 23.55           C  
ANISOU 2064  C   ASP A 272     2983   2983   2983      0      0      0       C  
ATOM   2065  O   ASP A 272     119.231  -1.341  18.302  1.00 24.37           O  
ANISOU 2065  O   ASP A 272     3086   3086   3086      0      0      0       O  
ATOM   2066  CB  ASP A 272     118.278   1.304  18.687  1.00 20.06           C  
ANISOU 2066  CB  ASP A 272     2541   2541   2541      0      0      0       C  
ATOM   2067  CG  ASP A 272     119.500   1.955  19.315  1.00 19.08           C  
ANISOU 2067  CG  ASP A 272     2416   2416   2416      0      0      0       C  
ATOM   2068  OD1 ASP A 272     120.638   1.565  18.999  1.00 30.44           O  
ANISOU 2068  OD1 ASP A 272     3856   3856   3856      0      0      0       O  
ATOM   2069  OD2 ASP A 272     119.308   2.821  20.197  1.00 28.79           O  
ANISOU 2069  OD2 ASP A 272     3646   3646   3646      0      0      0       O  
ATOM   2070  N   LYS A 273     120.447  -0.621  16.557  1.00 17.54           N  
ANISOU 2070  N   LYS A 273     2221   2221   2221      0      0      0       N  
ATOM   2071  CA  LYS A 273     121.324  -1.780  16.594  1.00 21.30           C  
ANISOU 2071  CA  LYS A 273     2697   2697   2697      0      0      0       C  
ATOM   2072  C   LYS A 273     122.123  -1.871  17.882  1.00 30.57           C  
ANISOU 2072  C   LYS A 273     3872   3872   3872      0      0      0       C  
ATOM   2073  O   LYS A 273     122.434  -2.976  18.326  1.00 22.44           O  
ANISOU 2073  O   LYS A 273     2842   2842   2842      0      0      0       O  
ATOM   2074  CB  LYS A 273     122.282  -1.803  15.390  1.00 22.18           C  
ANISOU 2074  CB  LYS A 273     2809   2809   2809      0      0      0       C  
ATOM   2075  CG  LYS A 273     123.136  -3.072  15.293  1.00 21.12           C  
ANISOU 2075  CG  LYS A 273     2675   2675   2675      0      0      0       C  
ATOM   2076  CD  LYS A 273     123.951  -3.129  14.004  1.00 32.56           C  
ANISOU 2076  CD  LYS A 273     4124   4124   4124      0      0      0       C  
ATOM   2077  CE  LYS A 273     124.798  -4.399  13.928  1.00 37.70           C  
ANISOU 2077  CE  LYS A 273     4775   4775   4775      0      0      0       C  
ATOM   2078  NZ  LYS A 273     125.759  -4.380  12.807  1.00 59.78           N  
ANISOU 2078  NZ  LYS A 273     7571   7571   7571      0      0      0       N  
ATOM   2079  N   HIS A 274     122.452  -0.732  18.484  1.00 20.56           N  
ANISOU 2079  N   HIS A 274     2604   2604   2604      0      0      0       N  
ATOM   2080  CA  HIS A 274     123.188  -0.755  19.747  1.00 25.43           C  
ANISOU 2080  CA  HIS A 274     3221   3221   3221      0      0      0       C  
ATOM   2081  C   HIS A 274     122.406  -1.461  20.844  1.00 23.24           C  
ANISOU 2081  C   HIS A 274     2943   2943   2943      0      0      0       C  
ATOM   2082  O   HIS A 274     122.985  -2.198  21.630  1.00 32.17           O  
ANISOU 2082  O   HIS A 274     4074   4074   4074      0      0      0       O  
ATOM   2083  CB  HIS A 274     123.546   0.662  20.216  1.00 30.00           C  
ANISOU 2083  CB  HIS A 274     3800   3800   3800      0      0      0       C  
ATOM   2084  CG  HIS A 274     124.231   0.670  21.545  1.00 24.63           C  
ANISOU 2084  CG  HIS A 274     3120   3120   3120      0      0      0       C  
ATOM   2085  ND1 HIS A 274     125.501   0.161  21.721  1.00 21.67           N  
ANISOU 2085  ND1 HIS A 274     2745   2745   2745      0      0      0       N  
ATOM   2086  CD2 HIS A 274     123.832   1.121  22.757  1.00 22.35           C  
ANISOU 2086  CD2 HIS A 274     2830   2830   2830      0      0      0       C  
ATOM   2087  CE1 HIS A 274     125.850   0.295  22.988  1.00 17.58           C  
ANISOU 2087  CE1 HIS A 274     2227   2227   2227      0      0      0       C  
ATOM   2088  NE2 HIS A 274     124.856   0.874  23.637  1.00 29.29           N  
ANISOU 2088  NE2 HIS A 274     3710   3710   3710      0      0      0       N  
ATOM   2089  N   LEU A 275     121.113  -1.170  20.956  1.00 23.17           N  
ANISOU 2089  N   LEU A 275     2934   2934   2934      0      0      0       N  
ATOM   2090  CA  LEU A 275     120.289  -1.794  21.990  1.00 20.18           C  
ANISOU 2090  CA  LEU A 275     2556   2556   2556      0      0      0       C  
ATOM   2091  C   LEU A 275     119.920  -3.260  21.678  1.00 31.41           C  
ANISOU 2091  C   LEU A 275     3979   3979   3979      0      0      0       C  
ATOM   2092  O   LEU A 275     120.066  -4.137  22.518  1.00 17.03           O  
ANISOU 2092  O   LEU A 275     2157   2157   2157      0      0      0       O  
ATOM   2093  CB  LEU A 275     119.019  -0.989  22.221  1.00  5.73           C  
ANISOU 2093  CB  LEU A 275      726    726    726      0      0      0       C  
ATOM   2094  CG  LEU A 275     119.180   0.335  22.957  1.00 17.93           C  
ANISOU 2094  CG  LEU A 275     2271   2271   2271      0      0      0       C  
ATOM   2095  CD1 LEU A 275     117.826   0.979  23.142  1.00 21.60           C  
ANISOU 2095  CD1 LEU A 275     2736   2736   2736      0      0      0       C  
ATOM   2096  CD2 LEU A 275     119.857   0.121  24.289  1.00 17.39           C  
ANISOU 2096  CD2 LEU A 275     2203   2203   2203      0      0      0       C  
ATOM   2097  N   LEU A 276     119.440  -3.513  20.466  1.00 13.59           N  
ANISOU 2097  N   LEU A 276     1722   1722   1722      0      0      0       N  
ATOM   2098  CA  LEU A 276     118.861  -4.794  20.136  1.00 33.09           C  
ANISOU 2098  CA  LEU A 276     4191   4191   4191      0      0      0       C  
ATOM   2099  C   LEU A 276     119.909  -5.829  19.772  1.00 29.13           C  
ANISOU 2099  C   LEU A 276     3690   3690   3690      0      0      0       C  
ATOM   2100  O   LEU A 276     119.675  -7.007  19.940  1.00 31.01           O  
ANISOU 2100  O   LEU A 276     3927   3927   3927      0      0      0       O  
ATOM   2101  CB  LEU A 276     117.834  -4.666  19.005  1.00 12.61           C  
ANISOU 2101  CB  LEU A 276     1598   1598   1598      0      0      0       C  
ATOM   2102  CG  LEU A 276     116.596  -3.845  19.326  1.00 21.09           C  
ANISOU 2102  CG  LEU A 276     2672   2672   2672      0      0      0       C  
ATOM   2103  CD1 LEU A 276     115.602  -3.913  18.185  1.00 23.61           C  
ANISOU 2103  CD1 LEU A 276     2990   2990   2990      0      0      0       C  
ATOM   2104  CD2 LEU A 276     115.972  -4.337  20.630  1.00 13.08           C  
ANISOU 2104  CD2 LEU A 276     1656   1656   1656      0      0      0       C  
ATOM   2105  N   THR A 277     121.093  -5.382  19.379  1.00 29.82           N  
ANISOU 2105  N   THR A 277     3777   3777   3777      0      0      0       N  
ATOM   2106  CA  THR A 277     122.144  -6.316  19.047  1.00 20.49           C  
ANISOU 2106  CA  THR A 277     2595   2595   2595      0      0      0       C  
ATOM   2107  C   THR A 277     123.301  -6.244  20.022  1.00 28.64           C  
ANISOU 2107  C   THR A 277     3628   3628   3628      0      0      0       C  
ATOM   2108  O   THR A 277     123.579  -7.232  20.715  1.00 30.14           O  
ANISOU 2108  O   THR A 277     3818   3818   3818      0      0      0       O  
ATOM   2109  CB  THR A 277     122.645  -6.132  17.596  1.00 27.50           C  
ANISOU 2109  CB  THR A 277     3483   3483   3483      0      0      0       C  
ATOM   2110  OG1 THR A 277     121.588  -6.416  16.669  1.00 23.25           O  
ANISOU 2110  OG1 THR A 277     2945   2945   2945      0      0      0       O  
ATOM   2111  CG2 THR A 277     123.811  -7.039  17.301  1.00 27.02           C  
ANISOU 2111  CG2 THR A 277     3422   3422   3422      0      0      0       C  
ATOM   2112  N   ASP A 278     123.971  -5.100  20.101  1.00 34.22           N  
ANISOU 2112  N   ASP A 278     4334   4334   4334      0      0      0       N  
ATOM   2113  CA  ASP A 278     125.183  -5.020  20.919  1.00 35.05           C  
ANISOU 2113  CA  ASP A 278     4439   4439   4439      0      0      0       C  
ATOM   2114  C   ASP A 278     124.879  -5.256  22.404  1.00 34.33           C  
ANISOU 2114  C   ASP A 278     4348   4348   4348      0      0      0       C  
ATOM   2115  O   ASP A 278     125.606  -5.987  23.076  1.00 31.00           O  
ANISOU 2115  O   ASP A 278     3926   3926   3926      0      0      0       O  
ATOM   2116  CB  ASP A 278     125.947  -3.714  20.734  1.00 30.36           C  
ANISOU 2116  CB  ASP A 278     3845   3845   3845      0      0      0       C  
ATOM   2117  CG  ASP A 278     127.334  -3.782  21.354  1.00 48.05           C  
ANISOU 2117  CG  ASP A 278     6085   6085   6085      0      0      0       C  
ATOM   2118  OD1 ASP A 278     128.208  -4.475  20.779  1.00 75.22           O  
ANISOU 2118  OD1 ASP A 278     9527   9527   9527      0      0      0       O  
ATOM   2119  OD2 ASP A 278     127.516  -3.286  22.477  1.00 44.74           O  
ANISOU 2119  OD2 ASP A 278     5666   5666   5666      0      0      0       O  
ATOM   2120  N   VAL A 279     123.858  -4.573  22.925  1.00 27.57           N  
ANISOU 2120  N   VAL A 279     3491   3491   3491      0      0      0       N  
ATOM   2121  CA  VAL A 279     123.481  -4.737  24.334  1.00 34.71           C  
ANISOU 2121  CA  VAL A 279     4395   4395   4395      0      0      0       C  
ATOM   2122  C   VAL A 279     122.733  -6.064  24.579  1.00 28.59           C  
ANISOU 2122  C   VAL A 279     3621   3621   3621      0      0      0       C  
ATOM   2123  O   VAL A 279     123.159  -6.869  25.407  1.00 25.85           O  
ANISOU 2123  O   VAL A 279     3273   3273   3273      0      0      0       O  
ATOM   2124  CB  VAL A 279     122.653  -3.556  24.863  1.00 12.54           C  
ANISOU 2124  CB  VAL A 279     1588   1588   1588      0      0      0       C  
ATOM   2125  CG1 VAL A 279     122.126  -3.874  26.244  1.00  9.92           C  
ANISOU 2125  CG1 VAL A 279     1257   1257   1257      0      0      0       C  
ATOM   2126  CG2 VAL A 279     123.518  -2.328  24.934  1.00 25.26           C  
ANISOU 2126  CG2 VAL A 279     3199   3199   3199      0      0      0       C  
ATOM   2127  N   LEU A 280     121.596  -6.257  23.914  1.00 22.04           N  
ANISOU 2127  N   LEU A 280     2792   2792   2792      0      0      0       N  
ATOM   2128  CA  LEU A 280     120.740  -7.393  24.199  1.00 15.84           C  
ANISOU 2128  CA  LEU A 280     2006   2006   2006      0      0      0       C  
ATOM   2129  C   LEU A 280     121.412  -8.710  23.879  1.00 29.10           C  
ANISOU 2129  C   LEU A 280     3686   3686   3686      0      0      0       C  
ATOM   2130  O   LEU A 280     121.460  -9.590  24.724  1.00 17.04           O  
ANISOU 2130  O   LEU A 280     2158   2158   2158      0      0      0       O  
ATOM   2131  CB  LEU A 280     119.419  -7.291  23.434  1.00 27.76           C  
ANISOU 2131  CB  LEU A 280     3516   3516   3516      0      0      0       C  
ATOM   2132  CG  LEU A 280     118.498  -8.499  23.607  1.00 28.46           C  
ANISOU 2132  CG  LEU A 280     3604   3604   3604      0      0      0       C  
ATOM   2133  CD1 LEU A 280     118.131  -8.728  25.074  1.00 16.40           C  
ANISOU 2133  CD1 LEU A 280     2076   2076   2076      0      0      0       C  
ATOM   2134  CD2 LEU A 280     117.228  -8.323  22.802  1.00 31.29           C  
ANISOU 2134  CD2 LEU A 280     3963   3963   3963      0      0      0       C  
ATOM   2135  N   LYS A 281     121.993  -8.805  22.685  1.00 25.46           N  
ANISOU 2135  N   LYS A 281     3224   3224   3224      0      0      0       N  
ATOM   2136  CA  LYS A 281     122.526 -10.068  22.202  1.00 26.62           C  
ANISOU 2136  CA  LYS A 281     3372   3372   3372      0      0      0       C  
ATOM   2137  C   LYS A 281     124.011 -10.267  22.547  1.00 30.16           C  
ANISOU 2137  C   LYS A 281     3820   3820   3820      0      0      0       C  
ATOM   2138  O   LYS A 281     124.396 -11.352  22.943  1.00 36.33           O  
ANISOU 2138  O   LYS A 281     4601   4601   4601      0      0      0       O  
ATOM   2139  CB  LYS A 281     122.274 -10.216  20.697  1.00 24.07           C  
ANISOU 2139  CB  LYS A 281     3049   3049   3049      0      0      0       C  
ATOM   2140  CG  LYS A 281     120.781 -10.362  20.359  1.00 23.71           C  
ANISOU 2140  CG  LYS A 281     3003   3003   3003      0      0      0       C  
ATOM   2141  CD  LYS A 281     120.525 -10.382  18.847  1.00 25.71           C  
ANISOU 2141  CD  LYS A 281     3257   3257   3257      0      0      0       C  
ATOM   2142  CE  LYS A 281     119.048 -10.628  18.536  1.00 26.13           C  
ANISOU 2142  CE  LYS A 281     3309   3309   3309      0      0      0       C  
ATOM   2143  NZ  LYS A 281     118.797 -10.688  17.077  1.00 20.91           N  
ANISOU 2143  NZ  LYS A 281     2649   2649   2649      0      0      0       N  
ATOM   2144  N   ASN A 282     124.845  -9.248  22.368  1.00 29.68           N  
ANISOU 2144  N   ASN A 282     3759   3759   3759      0      0      0       N  
ATOM   2145  CA  ASN A 282     126.274  -9.428  22.564  1.00 26.34           C  
ANISOU 2145  CA  ASN A 282     3336   3336   3336      0      0      0       C  
ATOM   2146  C   ASN A 282     126.723  -9.348  24.031  1.00 28.66           C  
ANISOU 2146  C   ASN A 282     3630   3630   3630      0      0      0       C  
ATOM   2147  O   ASN A 282     127.405 -10.246  24.534  1.00 38.50           O  
ANISOU 2147  O   ASN A 282     4877   4877   4877      0      0      0       O  
ATOM   2148  CB  ASN A 282     127.075  -8.454  21.721  1.00 25.92           C  
ANISOU 2148  CB  ASN A 282     3283   3283   3283      0      0      0       C  
ATOM   2149  CG  ASN A 282     126.998  -8.750  20.249  1.00 45.55           C  
ANISOU 2149  CG  ASN A 282     5769   5769   5769      0      0      0       C  
ATOM   2150  OD1 ASN A 282     126.652  -9.851  19.836  1.00 47.62           O  
ANISOU 2150  OD1 ASN A 282     6031   6031   6031      0      0      0       O  
ATOM   2151  ND2 ASN A 282     127.365  -7.762  19.437  1.00 36.96           N  
ANISOU 2151  ND2 ASN A 282     4681   4681   4681      0      0      0       N  
ATOM   2152  N   GLN A 283     126.235  -8.346  24.755  1.00 11.87           N  
ANISOU 2152  N   GLN A 283     1503   1503   1503      0      0      0       N  
ATOM   2153  CA  GLN A 283     126.699  -8.146  26.126  1.00 22.52           C  
ANISOU 2153  CA  GLN A 283     2852   2852   2852      0      0      0       C  
ATOM   2154  C   GLN A 283     125.875  -8.944  27.108  1.00 17.78           C  
ANISOU 2154  C   GLN A 283     2252   2252   2252      0      0      0       C  
ATOM   2155  O   GLN A 283     126.448  -9.599  27.961  1.00 33.56           O  
ANISOU 2155  O   GLN A 283     4250   4250   4250      0      0      0       O  
ATOM   2156  CB  GLN A 283     126.732  -6.662  26.526  1.00 26.52           C  
ANISOU 2156  CB  GLN A 283     3359   3359   3359      0      0      0       C  
ATOM   2157  CG  GLN A 283     127.685  -5.788  25.735  1.00 22.60           C  
ANISOU 2157  CG  GLN A 283     2862   2862   2862      0      0      0       C  
ATOM   2158  CD  GLN A 283     127.760  -4.352  26.276  1.00 23.99           C  
ANISOU 2158  CD  GLN A 283     3039   3039   3039      0      0      0       C  
ATOM   2159  OE1 GLN A 283     128.140  -4.126  27.425  1.00 26.24           O  
ANISOU 2159  OE1 GLN A 283     3323   3323   3323      0      0      0       O  
ATOM   2160  NE2 GLN A 283     127.440  -3.385  25.429  1.00 21.12           N  
ANISOU 2160  NE2 GLN A 283     2675   2675   2675      0      0      0       N  
ATOM   2161  N   LEU A 284     124.550  -8.834  27.049  1.00 17.25           N  
ANISOU 2161  N   LEU A 284     2184   2184   2184      0      0      0       N  
ATOM   2162  CA  LEU A 284     123.692  -9.605  27.940  1.00 26.08           C  
ANISOU 2162  CA  LEU A 284     3303   3303   3303      0      0      0       C  
ATOM   2163  C   LEU A 284     123.792 -11.083  27.562  1.00 31.26           C  
ANISOU 2163  C   LEU A 284     3960   3960   3960      0      0      0       C  
ATOM   2164  O   LEU A 284     123.669 -11.963  28.412  1.00 26.33           O  
ANISOU 2164  O   LEU A 284     3335   3335   3335      0      0      0       O  
ATOM   2165  CB  LEU A 284     122.241  -9.114  27.867  1.00 12.53           C  
ANISOU 2165  CB  LEU A 284     1587   1587   1587      0      0      0       C  
ATOM   2166  CG  LEU A 284     121.985  -7.713  28.429  1.00 15.65           C  
ANISOU 2166  CG  LEU A 284     1982   1982   1982      0      0      0       C  
ATOM   2167  CD1 LEU A 284     120.541  -7.360  28.341  1.00 21.22           C  
ANISOU 2167  CD1 LEU A 284     2687   2687   2687      0      0      0       C  
ATOM   2168  CD2 LEU A 284     122.437  -7.644  29.871  1.00 12.30           C  
ANISOU 2168  CD2 LEU A 284     1558   1558   1558      0      0      0       C  
ATOM   2169  N   GLY A 285     124.089 -11.331  26.292  1.00 20.47           N  
ANISOU 2169  N   GLY A 285     2592   2592   2592      0      0      0       N  
ATOM   2170  CA  GLY A 285     124.270 -12.678  25.780  1.00 20.40           C  
ANISOU 2170  CA  GLY A 285     2584   2584   2584      0      0      0       C  
ATOM   2171  C   GLY A 285     123.019 -13.446  25.387  1.00 28.13           C  
ANISOU 2171  C   GLY A 285     3563   3563   3563      0      0      0       C  
ATOM   2172  O   GLY A 285     123.081 -14.674  25.233  1.00 27.05           O  
ANISOU 2172  O   GLY A 285     3426   3426   3426      0      0      0       O  
ATOM   2173  N   PHE A 286     121.895 -12.741  25.233  1.00 23.16           N  
ANISOU 2173  N   PHE A 286     2934   2934   2934      0      0      0       N  
ATOM   2174  CA  PHE A 286     120.632 -13.347  24.787  1.00 30.47           C  
ANISOU 2174  CA  PHE A 286     3860   3860   3860      0      0      0       C  
ATOM   2175  C   PHE A 286     120.797 -14.175  23.509  1.00 38.40           C  
ANISOU 2175  C   PHE A 286     4864   4864   4864      0      0      0       C  
ATOM   2176  O   PHE A 286     121.201 -13.659  22.459  1.00 33.69           O  
ANISOU 2176  O   PHE A 286     4267   4267   4267      0      0      0       O  
ATOM   2177  CB  PHE A 286     119.608 -12.253  24.560  1.00 16.18           C  
ANISOU 2177  CB  PHE A 286     2049   2049   2049      0      0      0       C  
ATOM   2178  CG  PHE A 286     118.288 -12.722  24.039  1.00 15.22           C  
ANISOU 2178  CG  PHE A 286     1928   1928   1928      0      0      0       C  
ATOM   2179  CD1 PHE A 286     117.521 -13.632  24.760  1.00 21.02           C  
ANISOU 2179  CD1 PHE A 286     2662   2662   2662      0      0      0       C  
ATOM   2180  CD2 PHE A 286     117.800 -12.244  22.829  1.00 23.72           C  
ANISOU 2180  CD2 PHE A 286     3005   3005   3005      0      0      0       C  
ATOM   2181  CE1 PHE A 286     116.272 -14.049  24.282  1.00 26.90           C  
ANISOU 2181  CE1 PHE A 286     3407   3407   3407      0      0      0       C  
ATOM   2182  CE2 PHE A 286     116.554 -12.659  22.334  1.00 25.88           C  
ANISOU 2182  CE2 PHE A 286     3278   3278   3278      0      0      0       C  
ATOM   2183  CZ  PHE A 286     115.788 -13.553  23.067  1.00 17.08           C  
ANISOU 2183  CZ  PHE A 286     2164   2164   2164      0      0      0       C  
ATOM   2184  N   ASP A 287     120.432 -15.450  23.599  1.00 24.78           N  
ANISOU 2184  N   ASP A 287     3138   3138   3138      0      0      0       N  
ATOM   2185  CA  ASP A 287     120.635 -16.390  22.499  1.00 37.25           C  
ANISOU 2185  CA  ASP A 287     4717   4717   4717      0      0      0       C  
ATOM   2186  C   ASP A 287     119.351 -16.722  21.753  1.00 34.15           C  
ANISOU 2186  C   ASP A 287     4325   4325   4325      0      0      0       C  
ATOM   2187  O   ASP A 287     119.359 -17.495  20.797  1.00 27.55           O  
ANISOU 2187  O   ASP A 287     3490   3490   3490      0      0      0       O  
ATOM   2188  CB  ASP A 287     121.273 -17.681  23.052  1.00 22.53           C  
ANISOU 2188  CB  ASP A 287     2854   2854   2854      0      0      0       C  
ATOM   2189  CG  ASP A 287     122.016 -18.466  21.985  1.00 29.58           C  
ANISOU 2189  CG  ASP A 287     3747   3747   3747      0      0      0       C  
ATOM   2190  OD1 ASP A 287     122.801 -17.851  21.226  1.00 41.26           O  
ANISOU 2190  OD1 ASP A 287     5226   5226   5226      0      0      0       O  
ATOM   2191  OD2 ASP A 287     121.837 -19.700  21.912  1.00 33.12           O  
ANISOU 2191  OD2 ASP A 287     4194   4194   4194      0      0      0       O  
ATOM   2192  N   GLY A 288     118.256 -16.094  22.158  1.00 25.97           N  
ANISOU 2192  N   GLY A 288     3289   3289   3289      0      0      0       N  
ATOM   2193  CA  GLY A 288     116.971 -16.365  21.544  1.00 25.40           C  
ANISOU 2193  CA  GLY A 288     3217   3217   3217      0      0      0       C  
ATOM   2194  C   GLY A 288     116.669 -15.350  20.442  1.00 26.02           C  
ANISOU 2194  C   GLY A 288     3296   3296   3296      0      0      0       C  
ATOM   2195  O   GLY A 288     117.579 -14.739  19.881  1.00 20.19           O  
ANISOU 2195  O   GLY A 288     2557   2557   2557      0      0      0       O  
ATOM   2196  N   PHE A 289     115.392 -15.177  20.123  1.00 20.98           N  
ANISOU 2196  N   PHE A 289     2657   2657   2657      0      0      0       N  
ATOM   2197  CA  PHE A 289     114.986 -14.324  19.015  1.00 24.33           C  
ANISOU 2197  CA  PHE A 289     3081   3081   3081      0      0      0       C  
ATOM   2198  C   PHE A 289     114.195 -13.083  19.447  1.00 17.44           C  
ANISOU 2198  C   PHE A 289     2209   2209   2209      0      0      0       C  
ATOM   2199  O   PHE A 289     113.465 -13.110  20.449  1.00 22.41           O  
ANISOU 2199  O   PHE A 289     2838   2838   2838      0      0      0       O  
ATOM   2200  CB  PHE A 289     114.221 -15.135  17.950  1.00 20.94           C  
ANISOU 2200  CB  PHE A 289     2652   2652   2652      0      0      0       C  
ATOM   2201  CG  PHE A 289     112.837 -15.581  18.371  1.00 22.93           C  
ANISOU 2201  CG  PHE A 289     2904   2904   2904      0      0      0       C  
ATOM   2202  CD1 PHE A 289     111.721 -14.860  18.000  1.00 32.03           C  
ANISOU 2202  CD1 PHE A 289     4057   4057   4057      0      0      0       C  
ATOM   2203  CD2 PHE A 289     112.656 -16.713  19.138  1.00 37.18           C  
ANISOU 2203  CD2 PHE A 289     4709   4709   4709      0      0      0       C  
ATOM   2204  CE1 PHE A 289     110.451 -15.269  18.374  1.00 22.94           C  
ANISOU 2204  CE1 PHE A 289     2906   2906   2906      0      0      0       C  
ATOM   2205  CE2 PHE A 289     111.387 -17.121  19.517  1.00 35.46           C  
ANISOU 2205  CE2 PHE A 289     4491   4491   4491      0      0      0       C  
ATOM   2206  CZ  PHE A 289     110.285 -16.376  19.139  1.00 27.66           C  
ANISOU 2206  CZ  PHE A 289     3504   3504   3504      0      0      0       C  
ATOM   2207  N   VAL A 290     114.407 -11.988  18.724  1.00 14.89           N  
ANISOU 2207  N   VAL A 290     1886   1886   1886      0      0      0       N  
ATOM   2208  CA  VAL A 290     113.664 -10.753  18.965  1.00 22.81           C  
ANISOU 2208  CA  VAL A 290     2889   2889   2889      0      0      0       C  
ATOM   2209  C   VAL A 290     112.438 -10.671  18.061  1.00 17.97           C  
ANISOU 2209  C   VAL A 290     2276   2276   2276      0      0      0       C  
ATOM   2210  O   VAL A 290     112.541 -10.717  16.831  1.00 25.01           O  
ANISOU 2210  O   VAL A 290     3167   3167   3167      0      0      0       O  
ATOM   2211  CB  VAL A 290     114.575  -9.527  18.718  1.00 20.35           C  
ANISOU 2211  CB  VAL A 290     2578   2578   2578      0      0      0       C  
ATOM   2212  CG1 VAL A 290     113.792  -8.211  18.749  1.00 10.52           C  
ANISOU 2212  CG1 VAL A 290     1333   1333   1333      0      0      0       C  
ATOM   2213  CG2 VAL A 290     115.746  -9.532  19.709  1.00 16.64           C  
ANISOU 2213  CG2 VAL A 290     2107   2107   2107      0      0      0       C  
ATOM   2214  N   VAL A 291     111.288 -10.429  18.674  1.00 13.46           N  
ANISOU 2214  N   VAL A 291     1705   1705   1705      0      0      0       N  
ATOM   2215  CA  VAL A 291     110.071 -10.201  17.912  1.00 18.22           C  
ANISOU 2215  CA  VAL A 291     2307   2307   2307      0      0      0       C  
ATOM   2216  C   VAL A 291     109.709  -8.727  18.074  1.00 28.13           C  
ANISOU 2216  C   VAL A 291     3563   3563   3563      0      0      0       C  
ATOM   2217  O   VAL A 291     109.896  -8.148  19.144  1.00 30.92           O  
ANISOU 2217  O   VAL A 291     3917   3917   3917      0      0      0       O  
ATOM   2218  CB  VAL A 291     108.901 -11.123  18.374  1.00 17.32           C  
ANISOU 2218  CB  VAL A 291     2193   2193   2193      0      0      0       C  
ATOM   2219  CG1 VAL A 291     108.564 -10.901  19.824  1.00 14.25           C  
ANISOU 2219  CG1 VAL A 291     1804   1804   1804      0      0      0       C  
ATOM   2220  CG2 VAL A 291     107.669 -10.927  17.530  1.00 19.87           C  
ANISOU 2220  CG2 VAL A 291     2516   2516   2516      0      0      0       C  
ATOM   2221  N   SER A 292     109.218  -8.107  17.009  1.00 21.40           N  
ANISOU 2221  N   SER A 292     2710   2710   2710      0      0      0       N  
ATOM   2222  CA  SER A 292     108.771  -6.713  17.090  1.00 31.05           C  
ANISOU 2222  CA  SER A 292     3933   3933   3933      0      0      0       C  
ATOM   2223  C   SER A 292     107.366  -6.634  17.655  1.00 29.95           C  
ANISOU 2223  C   SER A 292     3793   3793   3793      0      0      0       C  
ATOM   2224  O   SER A 292     106.709  -7.658  17.821  1.00 25.79           O  
ANISOU 2224  O   SER A 292     3266   3266   3266      0      0      0       O  
ATOM   2225  CB  SER A 292     108.826  -6.038  15.724  1.00 17.19           C  
ANISOU 2225  CB  SER A 292     2177   2177   2177      0      0      0       C  
ATOM   2226  OG  SER A 292     107.986  -6.680  14.790  1.00 14.89           O  
ANISOU 2226  OG  SER A 292     1886   1886   1886      0      0      0       O  
ATOM   2227  N   ASP A 293     106.940  -5.436  18.035  1.00 29.53           N  
ANISOU 2227  N   ASP A 293     3740   3740   3740      0      0      0       N  
ATOM   2228  CA  ASP A 293     105.563  -5.219  18.482  1.00 27.04           C  
ANISOU 2228  CA  ASP A 293     3425   3425   3425      0      0      0       C  
ATOM   2229  C   ASP A 293     104.643  -4.853  17.321  1.00 21.15           C  
ANISOU 2229  C   ASP A 293     2679   2679   2679      0      0      0       C  
ATOM   2230  O   ASP A 293     105.093  -4.735  16.177  1.00 16.45           O  
ANISOU 2230  O   ASP A 293     2084   2084   2084      0      0      0       O  
ATOM   2231  CB  ASP A 293     105.525  -4.158  19.576  1.00 23.79           C  
ANISOU 2231  CB  ASP A 293     3013   3013   3013      0      0      0       C  
ATOM   2232  CG  ASP A 293     104.375  -4.366  20.539  1.00 33.93           C  
ANISOU 2232  CG  ASP A 293     4297   4297   4297      0      0      0       C  
ATOM   2233  OD1 ASP A 293     103.361  -4.960  20.119  1.00 28.33           O  
ANISOU 2233  OD1 ASP A 293     3588   3588   3588      0      0      0       O  
ATOM   2234  OD2 ASP A 293     104.504  -3.986  21.722  1.00 24.87           O  
ANISOU 2234  OD2 ASP A 293     3149   3149   3149      0      0      0       O  
ATOM   2235  N   TRP A 294     103.350  -4.732  17.613  1.00 18.02           N  
ANISOU 2235  N   TRP A 294     2283   2283   2283      0      0      0       N  
ATOM   2236  CA  TRP A 294     102.303  -4.626  16.587  1.00 13.84           C  
ANISOU 2236  CA  TRP A 294     1753   1753   1753      0      0      0       C  
ATOM   2237  C   TRP A 294     102.549  -3.455  15.607  1.00 29.94           C  
ANISOU 2237  C   TRP A 294     3792   3792   3792      0      0      0       C  
ATOM   2238  O   TRP A 294     102.308  -2.308  15.947  1.00 25.42           O  
ANISOU 2238  O   TRP A 294     3220   3220   3220      0      0      0       O  
ATOM   2239  CB  TRP A 294     100.944  -4.464  17.274  1.00 25.27           C  
ANISOU 2239  CB  TRP A 294     3201   3201   3201      0      0      0       C  
ATOM   2240  CG  TRP A 294      99.756  -4.490  16.337  1.00 27.06           C  
ANISOU 2240  CG  TRP A 294     3428   3428   3428      0      0      0       C  
ATOM   2241  CD1 TRP A 294      99.342  -3.515  15.474  1.00 25.99           C  
ANISOU 2241  CD1 TRP A 294     3291   3291   3291      0      0      0       C  
ATOM   2242  CD2 TRP A 294      98.793  -5.539  16.240  1.00 25.90           C  
ANISOU 2242  CD2 TRP A 294     3280   3280   3280      0      0      0       C  
ATOM   2243  NE1 TRP A 294      98.209  -3.921  14.809  1.00 30.83           N  
ANISOU 2243  NE1 TRP A 294     3905   3905   3905      0      0      0       N  
ATOM   2244  CE2 TRP A 294      97.844  -5.155  15.275  1.00 37.52           C  
ANISOU 2244  CE2 TRP A 294     4752   4752   4752      0      0      0       C  
ATOM   2245  CE3 TRP A 294      98.645  -6.777  16.874  1.00 28.55           C  
ANISOU 2245  CE3 TRP A 294     3616   3616   3616      0      0      0       C  
ATOM   2246  CZ2 TRP A 294      96.769  -5.961  14.930  1.00 33.45           C  
ANISOU 2246  CZ2 TRP A 294     4237   4237   4237      0      0      0       C  
ATOM   2247  CZ3 TRP A 294      97.578  -7.575  16.527  1.00 38.65           C  
ANISOU 2247  CZ3 TRP A 294     4895   4895   4895      0      0      0       C  
ATOM   2248  CH2 TRP A 294      96.654  -7.166  15.563  1.00 35.01           C  
ANISOU 2248  CH2 TRP A 294     4434   4434   4434      0      0      0       C  
ATOM   2249  N   ASN A 295     102.993  -3.768  14.393  1.00 19.43           N  
ANISOU 2249  N   ASN A 295     2461   2461   2461      0      0      0       N  
ATOM   2250  CA  ASN A 295     103.368  -2.786  13.384  1.00 26.90           C  
ANISOU 2250  CA  ASN A 295     3407   3407   3407      0      0      0       C  
ATOM   2251  C   ASN A 295     104.377  -1.740  13.838  1.00 31.44           C  
ANISOU 2251  C   ASN A 295     3982   3982   3982      0      0      0       C  
ATOM   2252  O   ASN A 295     104.474  -0.684  13.225  1.00 29.65           O  
ANISOU 2252  O   ASN A 295     3755   3755   3755      0      0      0       O  
ATOM   2253  CB  ASN A 295     102.123  -2.064  12.844  1.00 34.13           C  
ANISOU 2253  CB  ASN A 295     4322   4322   4322      0      0      0       C  
ATOM   2254  CG  ASN A 295     101.340  -2.890  11.854  1.00 38.21           C  
ANISOU 2254  CG  ASN A 295     4839   4839   4839      0      0      0       C  
ATOM   2255  OD1 ASN A 295     101.898  -3.705  11.119  1.00 33.57           O  
ANISOU 2255  OD1 ASN A 295     4251   4251   4251      0      0      0       O  
ATOM   2256  ND2 ASN A 295     100.033  -2.690  11.835  1.00 30.19           N  
ANISOU 2256  ND2 ASN A 295     3824   3824   3824      0      0      0       N  
ATOM   2257  N   ALA A 296     105.171  -2.060  14.851  1.00 20.20           N  
ANISOU 2257  N   ALA A 296     2559   2559   2559      0      0      0       N  
ATOM   2258  CA  ALA A 296     106.162  -1.133  15.364  1.00 29.01           C  
ANISOU 2258  CA  ALA A 296     3674   3674   3674      0      0      0       C  
ATOM   2259  C   ALA A 296     107.184  -0.718  14.318  1.00 33.41           C  
ANISOU 2259  C   ALA A 296     4231   4231   4231      0      0      0       C  
ATOM   2260  O   ALA A 296     107.684   0.417  14.338  1.00 23.97           O  
ANISOU 2260  O   ALA A 296     3036   3036   3036      0      0      0       O  
ATOM   2261  CB  ALA A 296     106.869  -1.746  16.555  1.00 15.50           C  
ANISOU 2261  CB  ALA A 296     1963   1963   1963      0      0      0       C  
ATOM   2262  N   HIS A 297     107.392  -1.584  13.337  1.00 17.98           N  
ANISOU 2262  N   HIS A 297     2278   2278   2278      0      0      0       N  
ATOM   2263  CA  HIS A 297     108.413  -1.356  12.325  1.00 20.20           C  
ANISOU 2263  CA  HIS A 297     2558   2558   2558      0      0      0       C  
ATOM   2264  C   HIS A 297     108.079  -0.109  11.506  1.00 26.27           C  
ANISOU 2264  C   HIS A 297     3327   3327   3327      0      0      0       C  
ATOM   2265  O   HIS A 297     108.960   0.519  10.919  1.00 36.67           O  
ANISOU 2265  O   HIS A 297     4645   4645   4645      0      0      0       O  
ATOM   2266  CB  HIS A 297     108.565  -2.565  11.408  1.00 18.40           C  
ANISOU 2266  CB  HIS A 297     2331   2331   2331      0      0      0       C  
ATOM   2267  CG  HIS A 297     107.334  -2.870  10.628  1.00 22.79           C  
ANISOU 2267  CG  HIS A 297     2887   2887   2887      0      0      0       C  
ATOM   2268  ND1 HIS A 297     106.277  -3.580  11.152  1.00 19.50           N  
ANISOU 2268  ND1 HIS A 297     2470   2470   2470      0      0      0       N  
ATOM   2269  CD2 HIS A 297     106.995  -2.571   9.354  1.00 22.08           C  
ANISOU 2269  CD2 HIS A 297     2796   2796   2796      0      0      0       C  
ATOM   2270  CE1 HIS A 297     105.336  -3.697  10.236  1.00 20.27           C  
ANISOU 2270  CE1 HIS A 297     2567   2567   2567      0      0      0       C  
ATOM   2271  NE2 HIS A 297     105.743  -3.083   9.139  1.00 25.26           N  
ANISOU 2271  NE2 HIS A 297     3200   3200   3200      0      0      0       N  
ATOM   2272  N   LYS A 298     106.793   0.216  11.425  1.00 19.23           N  
ANISOU 2272  N   LYS A 298     2435   2435   2435      0      0      0       N  
ATOM   2273  CA  LYS A 298     106.346   1.344  10.602  1.00 32.50           C  
ANISOU 2273  CA  LYS A 298     4116   4116   4116      0      0      0       C  
ATOM   2274  C   LYS A 298     106.854   2.681  11.166  1.00 30.13           C  
ANISOU 2274  C   LYS A 298     3815   3815   3815      0      0      0       C  
ATOM   2275  O   LYS A 298     106.831   3.685  10.471  1.00 29.73           O  
ANISOU 2275  O   LYS A 298     3765   3765   3765      0      0      0       O  
ATOM   2276  CB  LYS A 298     104.828   1.301  10.407  1.00 32.03           C  
ANISOU 2276  CB  LYS A 298     4057   4057   4057      0      0      0       C  
ATOM   2277  CG  LYS A 298     104.016   2.006  11.473  1.00 31.36           C  
ANISOU 2277  CG  LYS A 298     3972   3972   3972      0      0      0       C  
ATOM   2278  CD  LYS A 298     102.555   2.092  11.108  1.00 34.39           C  
ANISOU 2278  CD  LYS A 298     4356   4356   4356      0      0      0       C  
ATOM   2279  CE  LYS A 298     101.788   3.060  11.978  1.00 38.86           C  
ANISOU 2279  CE  LYS A 298     4922   4922   4922      0      0      0       C  
ATOM   2280  NZ  LYS A 298     100.361   3.143  11.565  1.00 29.98           N  
ANISOU 2280  NZ  LYS A 298     3797   3797   3797      0      0      0       N  
ATOM   2281  N   PHE A 299     107.232   2.694  12.448  1.00 23.85           N  
ANISOU 2281  N   PHE A 299     3021   3021   3021      0      0      0       N  
ATOM   2282  CA  PHE A 299     107.702   3.913  13.094  1.00 18.06           C  
ANISOU 2282  CA  PHE A 299     2288   2288   2288      0      0      0       C  
ATOM   2283  C   PHE A 299     109.202   4.149  12.999  1.00 26.03           C  
ANISOU 2283  C   PHE A 299     3297   3297   3297      0      0      0       C  
ATOM   2284  O   PHE A 299     109.701   5.200  13.399  1.00 37.43           O  
ANISOU 2284  O   PHE A 299     4741   4741   4741      0      0      0       O  
ATOM   2285  CB  PHE A 299     107.249   3.971  14.550  1.00 35.21           C  
ANISOU 2285  CB  PHE A 299     4459   4459   4459      0      0      0       C  
ATOM   2286  CG  PHE A 299     105.758   3.942  14.723  1.00 38.97           C  
ANISOU 2286  CG  PHE A 299     4936   4936   4936      0      0      0       C  
ATOM   2287  CD1 PHE A 299     105.027   5.117  14.581  1.00 24.26           C  
ANISOU 2287  CD1 PHE A 299     3073   3073   3073      0      0      0       C  
ATOM   2288  CD2 PHE A 299     105.088   2.790  15.078  1.00 23.33           C  
ANISOU 2288  CD2 PHE A 299     2955   2955   2955      0      0      0       C  
ATOM   2289  CE1 PHE A 299     103.651   5.120  14.744  1.00 26.85           C  
ANISOU 2289  CE1 PHE A 299     3400   3400   3400      0      0      0       C  
ATOM   2290  CE2 PHE A 299     103.706   2.799  15.256  1.00 25.10           C  
ANISOU 2290  CE2 PHE A 299     3178   3178   3178      0      0      0       C  
ATOM   2291  CZ  PHE A 299     102.989   3.958  15.081  1.00 24.88           C  
ANISOU 2291  CZ  PHE A 299     3151   3151   3151      0      0      0       C  
ATOM   2292  N   VAL A 300     109.916   3.169  12.474  1.00 27.21           N  
ANISOU 2292  N   VAL A 300     3446   3446   3446      0      0      0       N  
ATOM   2293  CA  VAL A 300     111.350   3.261  12.326  1.00 33.67           C  
ANISOU 2293  CA  VAL A 300     4264   4264   4264      0      0      0       C  
ATOM   2294  C   VAL A 300     111.743   4.164  11.161  1.00 35.82           C  
ANISOU 2294  C   VAL A 300     4536   4536   4536      0      0      0       C  
ATOM   2295  O   VAL A 300     111.067   4.161  10.133  1.00 36.49           O  
ANISOU 2295  O   VAL A 300     4622   4622   4622      0      0      0       O  
ATOM   2296  CB  VAL A 300     111.930   1.845  12.147  1.00 20.61           C  
ANISOU 2296  CB  VAL A 300     2610   2610   2610      0      0      0       C  
ATOM   2297  CG1 VAL A 300     113.437   1.886  11.961  1.00 20.27           C  
ANISOU 2297  CG1 VAL A 300     2567   2567   2567      0      0      0       C  
ATOM   2298  CG2 VAL A 300     111.603   1.021  13.381  1.00 16.41           C  
ANISOU 2298  CG2 VAL A 300     2078   2078   2078      0      0      0       C  
ATOM   2299  N   GLU A 301     112.819   4.936  11.313  1.00 27.54           N  
ANISOU 2299  N   GLU A 301     3488   3488   3488      0      0      0       N  
ATOM   2300  CA  GLU A 301     113.258   5.875  10.271  1.00 38.96           C  
ANISOU 2300  CA  GLU A 301     4935   4935   4935      0      0      0       C  
ATOM   2301  C   GLU A 301     113.574   5.151   8.968  1.00 40.38           C  
ANISOU 2301  C   GLU A 301     5115   5115   5115      0      0      0       C  
ATOM   2302  O   GLU A 301     114.310   4.166   8.977  1.00 38.45           O  
ANISOU 2302  O   GLU A 301     4870   4870   4870      0      0      0       O  
ATOM   2303  CB  GLU A 301     114.486   6.682  10.701  1.00 37.91           C  
ANISOU 2303  CB  GLU A 301     4801   4801   4801      0      0      0       C  
ATOM   2304  CG  GLU A 301     115.375   6.004  11.699  1.00 64.88           C  
ANISOU 2304  CG  GLU A 301     8217   8217   8217      0      0      0       C  
ATOM   2305  CD  GLU A 301     116.603   6.841  12.008  0.50 78.99           C  
ANISOU 2305  CD  GLU A 301    10004  10004  10004      0      0      0       C  
ATOM   2306  OE1 GLU A 301     116.894   7.779  11.241  0.50 59.58           O  
ANISOU 2306  OE1 GLU A 301     7546   7546   7546      0      0      0       O  
ATOM   2307  OE2 GLU A 301     117.198   6.630  13.088  0.50 95.66           O  
ANISOU 2307  OE2 GLU A 301    12115  12115  12115      0      0      0       O  
ATOM   2308  N   GLY A 302     112.960   5.589   7.870  1.00 27.66           N  
ANISOU 2308  N   GLY A 302     3504   3504   3504      0      0      0       N  
ATOM   2309  CA  GLY A 302     113.235   4.990   6.580  1.00 17.36           C  
ANISOU 2309  CA  GLY A 302     2198   2198   2198      0      0      0       C  
ATOM   2310  C   GLY A 302     112.309   3.828   6.277  1.00 30.07           C  
ANISOU 2310  C   GLY A 302     3809   3809   3809      0      0      0       C  
ATOM   2311  O   GLY A 302     112.419   3.179   5.240  1.00 33.42           O  
ANISOU 2311  O   GLY A 302     4232   4232   4232      0      0      0       O  
ATOM   2312  N   CYS A 303     111.534   3.442   7.274  1.00 15.25           N  
ANISOU 2312  N   CYS A 303     1932   1932   1932      0      0      0       N  
ATOM   2313  CA  CYS A 303     110.588   2.339   7.143  1.00 30.41           C  
ANISOU 2313  CA  CYS A 303     3851   3851   3851      0      0      0       C  
ATOM   2314  C   CYS A 303     109.135   2.773   6.923  1.00 26.05           C  
ANISOU 2314  C   CYS A 303     3299   3299   3299      0      0      0       C  
ATOM   2315  O   CYS A 303     108.786   3.940   7.106  1.00 27.57           O  
ANISOU 2315  O   CYS A 303     3492   3492   3492      0      0      0       O  
ATOM   2316  CB  CYS A 303     110.661   1.464   8.394  1.00 19.48           C  
ANISOU 2316  CB  CYS A 303     2467   2467   2467      0      0      0       C  
ATOM   2317  SG  CYS A 303     112.285   0.736   8.642  1.00 29.98           S  
ANISOU 2317  SG  CYS A 303     3797   3797   3797      0      0      0       S  
ATOM   2318  N   ASP A 304     108.304   1.819   6.526  1.00 26.92           N  
ANISOU 2318  N   ASP A 304     3409   3409   3409      0      0      0       N  
ATOM   2319  CA  ASP A 304     106.847   1.993   6.453  1.00 33.79           C  
ANISOU 2319  CA  ASP A 304     4280   4280   4280      0      0      0       C  
ATOM   2320  C   ASP A 304     106.136   0.658   6.725  1.00 38.81           C  
ANISOU 2320  C   ASP A 304     4916   4916   4916      0      0      0       C  
ATOM   2321  O   ASP A 304     106.775  -0.289   7.168  1.00 27.65           O  
ANISOU 2321  O   ASP A 304     3502   3502   3502      0      0      0       O  
ATOM   2322  CB  ASP A 304     106.441   2.615   5.110  1.00 29.27           C  
ANISOU 2322  CB  ASP A 304     3707   3707   3707      0      0      0       C  
ATOM   2323  CG  ASP A 304     106.879   1.782   3.917  1.00 32.66           C  
ANISOU 2323  CG  ASP A 304     4130   4149   4131      5     -2    -10       C  
ATOM   2324  OD1 ASP A 304     106.665   0.555   3.941  1.00 43.53           O  
ANISOU 2324  OD1 ASP A 304     5493   5541   5506     12     -6    -22       O  
ATOM   2325  OD2 ASP A 304     107.496   2.353   2.989  1.00 42.77           O  
ANISOU 2325  OD2 ASP A 304     5402   5444   5405     11     -5    -23       O  
ATOM   2326  N   LEU A 305     104.812   0.610   6.588  1.00 30.57           N  
ANISOU 2326  N   LEU A 305     3872   3872   3872      0      0      0       N  
ATOM   2327  CA  LEU A 305     104.074  -0.614   6.898  1.00 22.48           C  
ANISOU 2327  CA  LEU A 305     2847   2847   2847      0      0      0       C  
ATOM   2328  C   LEU A 305     104.536  -1.837   6.097  1.00 34.65           C  
ANISOU 2328  C   LEU A 305     4377   4403   4385      5     -3    -12       C  
ATOM   2329  O   LEU A 305     104.469  -2.941   6.593  1.00 19.19           O  
ANISOU 2329  O   LEU A 305     2416   2449   2425      7     -4    -18       O  
ATOM   2330  CB  LEU A 305     102.565  -0.425   6.695  1.00 20.07           C  
ANISOU 2330  CB  LEU A 305     2540   2544   2541      1      0     -2       C  
ATOM   2331  CG  LEU A 305     101.792   0.225   7.841  1.00 30.74           C  
ANISOU 2331  CG  LEU A 305     3894   3894   3894      0      0      0       C  
ATOM   2332  CD1 LEU A 305     100.411   0.692   7.422  1.00 17.75           C  
ANISOU 2332  CD1 LEU A 305     2248   2248   2248      0      0      0       C  
ATOM   2333  CD2 LEU A 305     101.673  -0.803   8.962  1.00 23.85           C  
ANISOU 2333  CD2 LEU A 305     3021   3021   3021      0      0      0       C  
ATOM   2334  N   GLU A 306     105.054  -1.625   4.894  1.00 27.99           N  
ANISOU 2334  N   GLU A 306     3513   3586   3536     17     -9    -36       N  
ATOM   2335  CA  GLU A 306     105.355  -2.724   3.981  1.00 32.46           C  
ANISOU 2335  CA  GLU A 306     4064   4183   4085     31    -17    -80       C  
ATOM   2336  C   GLU A 306     106.839  -3.059   3.799  1.00 28.60           C  
ANISOU 2336  C   GLU A 306     3578   3691   3599     31    -18    -78       C  
ATOM   2337  O   GLU A 306     107.195  -3.893   2.975  1.00 39.62           O  
ANISOU 2337  O   GLU A 306     4953   5113   4987     47    -28   -116       O  
ATOM   2338  CB  GLU A 306     104.718  -2.471   2.604  1.00 24.92           C  
ANISOU 2338  CB  GLU A 306     3085   3268   3116     51    -28   -124       C  
ATOM   2339  CG  GLU A 306     103.232  -2.314   2.584  1.00 33.80           C  
ANISOU 2339  CG  GLU A 306     4200   4406   4235     55    -31   -137       C  
ATOM   2340  CD  GLU A 306     102.695  -2.154   1.170  1.00 44.32           C  
ANISOU 2340  CD  GLU A 306     5507   5781   5553     78    -44   -186       C  
ATOM   2341  OE1 GLU A 306     103.429  -1.656   0.294  1.00 39.54           O  
ANISOU 2341  OE1 GLU A 306     4856   5196   4971     95    -52   -179       O  
ATOM   2342  OE2 GLU A 306     101.537  -2.543   0.928  1.00 44.32           O  
ANISOU 2342  OE2 GLU A 306     5490   5801   5547     89    -51   -216       O  
ATOM   2343  N   GLN A 307     107.691  -2.353   4.510  1.00 25.28           N  
ANISOU 2343  N   GLN A 307     3179   3237   3188     15     -8    -38       N  
ATOM   2344  CA  GLN A 307     109.129  -2.491   4.403  1.00 20.62           C  
ANISOU 2344  CA  GLN A 307     2592   2642   2600     13     -7    -33       C  
ATOM   2345  C   GLN A 307     109.865  -1.959   5.632  1.00 41.82           C  
ANISOU 2345  C   GLN A 307     5297   5297   5297      0      0      0       C  
ATOM   2346  O   GLN A 307     109.579  -0.849   6.070  1.00 40.42           O  
ANISOU 2346  O   GLN A 307     5119   5119   5119      0      0      0       O  
ATOM   2347  CB  GLN A 307     109.588  -1.764   3.148  1.00 34.89           C  
ANISOU 2347  CB  GLN A 307     4375   4473   4408     26    -14    -51       C  
ATOM   2348  CG  GLN A 307     111.060  -1.642   2.943  1.00 60.67           C  
ANISOU 2348  CG  GLN A 307     7655   7732   7667     22    -12    -51       C  
ATOM   2349  CD  GLN A 307     111.603  -0.397   3.656  1.00 50.57           C  
ANISOU 2349  CD  GLN A 307     6396   6418   6401      6     -3    -12       C  
ATOM   2350  OE1 GLN A 307     112.692  -0.404   4.240  1.00 60.46           O  
ANISOU 2350  OE1 GLN A 307     7657   7657   7657      0      0      0       O  
ATOM   2351  NE2 GLN A 307     110.815   0.674   3.629  1.00 51.19           N  
ANISOU 2351  NE2 GLN A 307     6481   6485   6482      1      0     -2       N  
ATOM   2352  N   CYS A 308     110.798  -2.715   6.194  1.00 27.95           N  
ANISOU 2352  N   CYS A 308     3539   3539   3539      0      0      0       N  
ATOM   2353  CA  CYS A 308     111.680  -2.164   7.234  1.00 26.59           C  
ANISOU 2353  CA  CYS A 308     3368   3368   3368      0      0      0       C  
ATOM   2354  C   CYS A 308     113.007  -2.870   7.404  1.00 21.66           C  
ANISOU 2354  C   CYS A 308     2743   2743   2743      0      0      0       C  
ATOM   2355  O   CYS A 308     113.246  -3.504   8.426  1.00 22.81           O  
ANISOU 2355  O   CYS A 308     2888   2888   2888      0      0      0       O  
ATOM   2356  CB  CYS A 308     110.964  -2.051   8.573  1.00 26.65           C  
ANISOU 2356  CB  CYS A 308     3376   3376   3376      0      0      0       C  
ATOM   2357  SG  CYS A 308     111.777  -0.942   9.702  1.00 35.52           S  
ANISOU 2357  SG  CYS A 308     4499   4499   4499      0      0      0       S  
ATOM   2358  N   ALA A 309     113.912  -2.668   6.453  1.00 20.48           N  
ANISOU 2358  N   ALA A 309     2594   2594   2594      0      0      0       N  
ATOM   2359  CA  ALA A 309     115.247  -3.236   6.551  1.00 25.01           C  
ANISOU 2359  CA  ALA A 309     3168   3168   3168      0      0      0       C  
ATOM   2360  C   ALA A 309     115.980  -2.837   7.834  1.00 27.20           C  
ANISOU 2360  C   ALA A 309     3445   3445   3445      0      0      0       C  
ATOM   2361  O   ALA A 309     116.723  -3.643   8.382  1.00 27.41           O  
ANISOU 2361  O   ALA A 309     3472   3472   3472      0      0      0       O  
ATOM   2362  CB  ALA A 309     116.068  -2.822   5.333  1.00 20.35           C  
ANISOU 2362  CB  ALA A 309     2578   2578   2578      0      0      0       C  
ATOM   2363  N   GLN A 310     115.814  -1.597   8.277  1.00 23.94           N  
ANISOU 2363  N   GLN A 310     3032   3032   3032      0      0      0       N  
ATOM   2364  CA  GLN A 310     116.544  -1.089   9.437  1.00 27.50           C  
ANISOU 2364  CA  GLN A 310     3483   3483   3483      0      0      0       C  
ATOM   2365  C   GLN A 310     116.276  -1.862  10.716  1.00 12.09           C  
ANISOU 2365  C   GLN A 310     1531   1531   1531      0      0      0       C  
ATOM   2366  O   GLN A 310     117.178  -2.073  11.521  1.00 24.97           O  
ANISOU 2366  O   GLN A 310     3162   3162   3162      0      0      0       O  
ATOM   2367  CB  GLN A 310     116.279   0.407   9.666  1.00 18.76           C  
ANISOU 2367  CB  GLN A 310     2376   2376   2376      0      0      0       C  
ATOM   2368  CG  GLN A 310     116.957   0.954  10.909  0.50 18.06           C  
ANISOU 2368  CG  GLN A 310     2287   2287   2287      0      0      0       C  
ATOM   2369  CD  GLN A 310     118.476   0.923  10.825  0.50 36.78           C  
ANISOU 2369  CD  GLN A 310     4659   4659   4659      0      0      0       C  
ATOM   2370  OE1 GLN A 310     119.079   1.624  10.014  0.50 62.55           O  
ANISOU 2370  OE1 GLN A 310     7922   7922   7922      0      0      0       O  
ATOM   2371  NE2 GLN A 310     119.099   0.107  11.664  0.50 48.41           N  
ANISOU 2371  NE2 GLN A 310     6131   6131   6131      0      0      0       N  
ATOM   2372  N   ALA A 311     115.021  -2.240  10.924  1.00 24.37           N  
ANISOU 2372  N   ALA A 311     3087   3087   3087      0      0      0       N  
ATOM   2373  CA  ALA A 311     114.661  -2.983  12.127  1.00 24.12           C  
ANISOU 2373  CA  ALA A 311     3054   3054   3054      0      0      0       C  
ATOM   2374  C   ALA A 311     115.334  -4.349  12.116  1.00 34.76           C  
ANISOU 2374  C   ALA A 311     4403   4403   4403      0      0      0       C  
ATOM   2375  O   ALA A 311     115.883  -4.782  13.124  1.00 26.64           O  
ANISOU 2375  O   ALA A 311     3374   3374   3374      0      0      0       O  
ATOM   2376  CB  ALA A 311     113.163  -3.148  12.231  1.00 20.51           C  
ANISOU 2376  CB  ALA A 311     2598   2598   2598      0      0      0       C  
ATOM   2377  N   ILE A 312     115.278  -5.020  10.971  1.00 33.10           N  
ANISOU 2377  N   ILE A 312     4192   4192   4192      0      0      0       N  
ATOM   2378  CA  ILE A 312     115.932  -6.315  10.780  1.00 38.27           C  
ANISOU 2378  CA  ILE A 312     4847   4847   4847      0      0      0       C  
ATOM   2379  C   ILE A 312     117.432  -6.204  11.009  1.00 29.67           C  
ANISOU 2379  C   ILE A 312     3758   3758   3758      0      0      0       C  
ATOM   2380  O   ILE A 312     118.010  -6.985  11.754  1.00 20.50           O  
ANISOU 2380  O   ILE A 312     2596   2596   2596      0      0      0       O  
ATOM   2381  CB  ILE A 312     115.604  -6.900   9.385  1.00 27.07           C  
ANISOU 2381  CB  ILE A 312     3429   3429   3429      0      0      0       C  
ATOM   2382  CG1 ILE A 312     114.122  -7.302   9.346  1.00 15.71           C  
ANISOU 2382  CG1 ILE A 312     1990   1990   1990      0      0      0       C  
ATOM   2383  CG2 ILE A 312     116.476  -8.102   9.066  1.00 22.72           C  
ANISOU 2383  CG2 ILE A 312     2877   2877   2877      0      0      0       C  
ATOM   2384  CD1 ILE A 312     113.626  -7.697   7.995  1.00 30.24           C  
ANISOU 2384  CD1 ILE A 312     3830   3830   3830      0      0      0       C  
ATOM   2385  N   ASN A 313     118.054  -5.217  10.379  1.00 23.17           N  
ANISOU 2385  N   ASN A 313     2935   2935   2935      0      0      0       N  
ATOM   2386  CA  ASN A 313     119.481  -4.998  10.536  1.00 24.03           C  
ANISOU 2386  CA  ASN A 313     3043   3043   3043      0      0      0       C  
ATOM   2387  C   ASN A 313     119.863  -4.648  11.970  1.00 20.51           C  
ANISOU 2387  C   ASN A 313     2597   2597   2597      0      0      0       C  
ATOM   2388  O   ASN A 313     120.990  -4.890  12.393  1.00 28.63           O  
ANISOU 2388  O   ASN A 313     3626   3626   3626      0      0      0       O  
ATOM   2389  CB  ASN A 313     119.966  -3.934   9.559  1.00  9.02           C  
ANISOU 2389  CB  ASN A 313     1142   1142   1142      0      0      0       C  
ATOM   2390  CG  ASN A 313     119.939  -4.423   8.136  1.00 31.42           C  
ANISOU 2390  CG  ASN A 313     3979   3979   3979      0      0      0       C  
ATOM   2391  OD1 ASN A 313     119.990  -5.636   7.882  1.00 33.52           O  
ANISOU 2391  OD1 ASN A 313     4246   4246   4246      0      0      0       O  
ATOM   2392  ND2 ASN A 313     119.845  -3.506   7.196  1.00 18.01           N  
ANISOU 2392  ND2 ASN A 313     2281   2281   2281      0      0      0       N  
ATOM   2393  N   ALA A 314     118.933  -4.029  12.689  1.00 14.99           N  
ANISOU 2393  N   ALA A 314     1899   1899   1899      0      0      0       N  
ATOM   2394  CA  ALA A 314     119.163  -3.647  14.076  1.00 28.82           C  
ANISOU 2394  CA  ALA A 314     3651   3651   3651      0      0      0       C  
ATOM   2395  C   ALA A 314     119.163  -4.825  15.018  1.00 23.22           C  
ANISOU 2395  C   ALA A 314     2940   2940   2940      0      0      0       C  
ATOM   2396  O   ALA A 314     119.696  -4.726  16.121  1.00 26.32           O  
ANISOU 2396  O   ALA A 314     3333   3333   3333      0      0      0       O  
ATOM   2397  CB  ALA A 314     118.110  -2.611  14.520  1.00 27.41           C  
ANISOU 2397  CB  ALA A 314     3472   3472   3472      0      0      0       C  
ATOM   2398  N   GLY A 315     118.557  -5.931  14.594  1.00 17.78           N  
ANISOU 2398  N   GLY A 315     2252   2252   2252      0      0      0       N  
ATOM   2399  CA  GLY A 315     118.516  -7.132  15.413  1.00 31.17           C  
ANISOU 2399  CA  GLY A 315     3947   3947   3947      0      0      0       C  
ATOM   2400  C   GLY A 315     117.146  -7.763  15.630  1.00 43.16           C  
ANISOU 2400  C   GLY A 315     5466   5466   5466      0      0      0       C  
ATOM   2401  O   GLY A 315     117.034  -8.771  16.346  1.00 40.30           O  
ANISOU 2401  O   GLY A 315     5105   5105   5105      0      0      0       O  
ATOM   2402  N   VAL A 316     116.109  -7.207  15.002  1.00 29.87           N  
ANISOU 2402  N   VAL A 316     3783   3783   3783      0      0      0       N  
ATOM   2403  CA  VAL A 316     114.793  -7.840  15.041  1.00 26.65           C  
ANISOU 2403  CA  VAL A 316     3375   3375   3375      0      0      0       C  
ATOM   2404  C   VAL A 316     114.824  -9.100  14.191  1.00 17.83           C  
ANISOU 2404  C   VAL A 316     2258   2258   2258      0      0      0       C  
ATOM   2405  O   VAL A 316     115.359  -9.092  13.077  1.00 27.87           O  
ANISOU 2405  O   VAL A 316     3530   3530   3530      0      0      0       O  
ATOM   2406  CB  VAL A 316     113.674  -6.899  14.550  1.00 25.14           C  
ANISOU 2406  CB  VAL A 316     3184   3184   3184      0      0      0       C  
ATOM   2407  CG1 VAL A 316     112.338  -7.616  14.557  1.00 23.83           C  
ANISOU 2407  CG1 VAL A 316     3018   3018   3018      0      0      0       C  
ATOM   2408  CG2 VAL A 316     113.604  -5.668  15.437  1.00 27.07           C  
ANISOU 2408  CG2 VAL A 316     3428   3428   3428      0      0      0       C  
ATOM   2409  N   ASP A 317     114.305 -10.192  14.748  1.00 22.04           N  
ANISOU 2409  N   ASP A 317     2792   2792   2792      0      0      0       N  
ATOM   2410  CA  ASP A 317     114.324 -11.488  14.074  1.00 21.13           C  
ANISOU 2410  CA  ASP A 317     2677   2677   2677      0      0      0       C  
ATOM   2411  C   ASP A 317     112.981 -11.928  13.497  1.00 34.45           C  
ANISOU 2411  C   ASP A 317     4364   4364   4364      0      0      0       C  
ATOM   2412  O   ASP A 317     112.918 -12.584  12.453  1.00 23.03           O  
ANISOU 2412  O   ASP A 317     2917   2917   2917      0      0      0       O  
ATOM   2413  CB  ASP A 317     114.830 -12.527  15.058  1.00 16.98           C  
ANISOU 2413  CB  ASP A 317     2150   2150   2150      0      0      0       C  
ATOM   2414  CG  ASP A 317     116.195 -12.174  15.591  1.00 26.95           C  
ANISOU 2414  CG  ASP A 317     3413   3413   3413      0      0      0       C  
ATOM   2415  OD1 ASP A 317     117.070 -11.810  14.774  1.00 20.69           O  
ANISOU 2415  OD1 ASP A 317     2621   2621   2621      0      0      0       O  
ATOM   2416  OD2 ASP A 317     116.370 -12.188  16.825  1.00 26.11           O  
ANISOU 2416  OD2 ASP A 317     3306   3306   3306      0      0      0       O  
ATOM   2417  N   VAL A 318     111.905 -11.515  14.162  1.00 19.86           N  
ANISOU 2417  N   VAL A 318     2516   2516   2516      0      0      0       N  
ATOM   2418  CA  VAL A 318     110.566 -11.824  13.701  1.00 25.29           C  
ANISOU 2418  CA  VAL A 318     3203   3203   3203      0      0      0       C  
ATOM   2419  C   VAL A 318     109.720 -10.551  13.688  1.00 26.63           C  
ANISOU 2419  C   VAL A 318     3373   3373   3373      0      0      0       C  
ATOM   2420  O   VAL A 318     109.542  -9.894  14.710  1.00 23.03           O  
ANISOU 2420  O   VAL A 318     2916   2916   2916      0      0      0       O  
ATOM   2421  CB  VAL A 318     109.884 -12.912  14.573  1.00 22.60           C  
ANISOU 2421  CB  VAL A 318     2862   2862   2862      0      0      0       C  
ATOM   2422  CG1 VAL A 318     108.431 -13.094  14.175  1.00 25.44           C  
ANISOU 2422  CG1 VAL A 318     3222   3222   3222      0      0      0       C  
ATOM   2423  CG2 VAL A 318     110.641 -14.242  14.482  1.00 32.36           C  
ANISOU 2423  CG2 VAL A 318     4098   4098   4098      0      0      0       C  
ATOM   2424  N   ILE A 319     109.124 -10.257  12.541  1.00 28.10           N  
ANISOU 2424  N   ILE A 319     3559   3559   3559      0      0      0       N  
ATOM   2425  CA  ILE A 319     108.391  -9.014  12.370  1.00 30.01           C  
ANISOU 2425  CA  ILE A 319     3800   3800   3800      0      0      0       C  
ATOM   2426  C   ILE A 319     106.901  -9.208  12.553  1.00 25.87           C  
ANISOU 2426  C   ILE A 319     3276   3276   3276      0      0      0       C  
ATOM   2427  O   ILE A 319     106.253  -9.862  11.745  1.00 28.54           O  
ANISOU 2427  O   ILE A 319     3615   3615   3615      0      0      0       O  
ATOM   2428  CB  ILE A 319     108.639  -8.404  10.981  1.00 24.64           C  
ANISOU 2428  CB  ILE A 319     3121   3121   3121      0      0      0       C  
ATOM   2429  CG1 ILE A 319     110.118  -8.091  10.774  1.00 15.25           C  
ANISOU 2429  CG1 ILE A 319     1932   1932   1932      0      0      0       C  
ATOM   2430  CG2 ILE A 319     107.791  -7.140  10.803  1.00 20.22           C  
ANISOU 2430  CG2 ILE A 319     2561   2561   2561      0      0      0       C  
ATOM   2431  CD1 ILE A 319     110.585  -6.862  11.545  1.00 38.27           C  
ANISOU 2431  CD1 ILE A 319     4847   4847   4847      0      0      0       C  
ATOM   2432  N   MET A 320     106.341  -8.531  13.544  1.00 19.08           N  
ANISOU 2432  N   MET A 320     2416   2416   2416      0      0      0       N  
ATOM   2433  CA  MET A 320     104.917  -8.607  13.780  1.00 19.10           C  
ANISOU 2433  CA  MET A 320     2419   2419   2419      0      0      0       C  
ATOM   2434  C   MET A 320     104.248  -7.652  12.823  1.00 37.51           C  
ANISOU 2434  C   MET A 320     4751   4751   4751      0      0      0       C  
ATOM   2435  O   MET A 320     104.161  -6.451  13.087  1.00 32.35           O  
ANISOU 2435  O   MET A 320     4097   4097   4097      0      0      0       O  
ATOM   2436  CB  MET A 320     104.592  -8.236  15.225  1.00 22.32           C  
ANISOU 2436  CB  MET A 320     2827   2827   2827      0      0      0       C  
ATOM   2437  CG  MET A 320     103.140  -8.464  15.593  1.00  7.77           C  
ANISOU 2437  CG  MET A 320      984    984    984      0      0      0       C  
ATOM   2438  SD  MET A 320     102.810  -8.065  17.320  1.00 32.79           S  
ANISOU 2438  SD  MET A 320     4153   4153   4153      0      0      0       S  
ATOM   2439  CE  MET A 320     103.728  -9.335  18.200  1.00 28.81           C  
ANISOU 2439  CE  MET A 320     3648   3648   3648      0      0      0       C  
ATOM   2440  N   VAL A 321     103.799  -8.185  11.689  1.00 18.17           N  
ANISOU 2440  N   VAL A 321     2301   2301   2301      0      0      0       N  
ATOM   2441  CA  VAL A 321     103.162  -7.351  10.677  1.00 18.24           C  
ANISOU 2441  CA  VAL A 321     2310   2310   2310      0      0      0       C  
ATOM   2442  C   VAL A 321     101.801  -7.958  10.323  1.00 19.49           C  
ANISOU 2442  C   VAL A 321     2459   2478   2469      3     -2    -12       C  
ATOM   2443  O   VAL A 321     101.615  -8.602   9.295  1.00 31.65           O  
ANISOU 2443  O   VAL A 321     3963   4050   4012     17    -12    -57       O  
ATOM   2444  CB  VAL A 321     104.090  -7.131   9.450  1.00 24.07           C  
ANISOU 2444  CB  VAL A 321     3049   3049   3049      0      0      0       C  
ATOM   2445  CG1 VAL A 321     104.647  -8.453   8.933  1.00 16.75           C  
ANISOU 2445  CG1 VAL A 321     2091   2153   2120     14    -10    -45       C  
ATOM   2446  CG2 VAL A 321     103.378  -6.327   8.357  1.00 18.85           C  
ANISOU 2446  CG2 VAL A 321     2367   2409   2386      8     -5    -24       C  
ATOM   2447  N   PRO A 322     100.811  -7.685  11.173  1.00 31.32           N  
ANISOU 2447  N   PRO A 322     3966   3966   3966      0      0      0       N  
ATOM   2448  CA  PRO A 322      99.545  -8.412  11.170  1.00 27.35           C  
ANISOU 2448  CA  PRO A 322     3451   3480   3463      5     -3    -24       C  
ATOM   2449  C   PRO A 322      98.776  -8.343   9.853  1.00 34.52           C  
ANISOU 2449  C   PRO A 322     4329   4419   4369     17    -12    -77       C  
ATOM   2450  O   PRO A 322      98.225  -9.345   9.421  1.00 34.59           O  
ANISOU 2450  O   PRO A 322     4291   4452   4400     30    -24   -116       O  
ATOM   2451  CB  PRO A 322      98.753  -7.735  12.303  1.00 21.67           C  
ANISOU 2451  CB  PRO A 322     2745   2745   2745      0      0      0       C  
ATOM   2452  CG  PRO A 322      99.463  -6.467  12.591  1.00 32.51           C  
ANISOU 2452  CG  PRO A 322     4117   4117   4117      0      0      0       C  
ATOM   2453  CD  PRO A 322     100.882  -6.689  12.256  1.00 20.92           C  
ANISOU 2453  CD  PRO A 322     2650   2650   2650      0      0      0       C  
ATOM   2454  N   GLU A 323      98.804  -7.202   9.184  1.00 40.47           N  
ANISOU 2454  N   GLU A 323     5084   5177   5117     17    -12    -74       N  
ATOM   2455  CA  GLU A 323      97.959  -6.995   8.017  1.00 33.08           C  
ANISOU 2455  CA  GLU A 323     4122   4271   4176     30    -20   -121       C  
ATOM   2456  C   GLU A 323      98.742  -6.960   6.720  1.00 26.08           C  
ANISOU 2456  C   GLU A 323     3218   3403   3287     42    -29   -153       C  
ATOM   2457  O   GLU A 323      98.276  -7.459   5.702  1.00 48.58           O  
ANISOU 2457  O   GLU A 323     6002   6289   6165     65    -47   -192       O  
ATOM   2458  CB  GLU A 323      97.159  -5.698   8.166  1.00 35.00           C  
ANISOU 2458  CB  GLU A 323     4356   4517   4426     27    -17    -91       C  
ATOM   2459  CG  GLU A 323      96.336  -5.309   6.934  1.00 40.19           C  
ANISOU 2459  CG  GLU A 323     4979   5212   5080     42    -26   -132       C  
ATOM   2460  CD  GLU A 323      95.456  -4.090   7.177  1.00 47.34           C  
ANISOU 2460  CD  GLU A 323     5919   6112   5958     34    -19   -125       C  
ATOM   2461  OE1 GLU A 323      95.641  -3.421   8.218  1.00 35.23           O  
ANISOU 2461  OE1 GLU A 323     4394   4550   4444     24    -12    -73       O  
ATOM   2462  OE2 GLU A 323      94.616  -3.773   6.304  1.00 43.15           O  
ANISOU 2462  OE2 GLU A 323     5366   5612   5415     46    -25   -159       O  
ATOM   2463  N   HIS A 324      99.920  -6.354   6.748  1.00 17.67           N  
ANISOU 2463  N   HIS A 324     2170   2324   2219     35    -23   -121       N  
ATOM   2464  CA  HIS A 324     100.668  -6.096   5.527  1.00 19.47           C  
ANISOU 2464  CA  HIS A 324     2357   2578   2461     50    -33   -134       C  
ATOM   2465  C   HIS A 324     101.789  -7.102   5.275  1.00 23.23           C  
ANISOU 2465  C   HIS A 324     2824   3057   2945     57    -40   -150       C  
ATOM   2466  O   HIS A 324     102.734  -6.843   4.517  1.00 30.88           O  
ANISOU 2466  O   HIS A 324     3769   4066   3898     80    -55   -217       O  
ATOM   2467  CB  HIS A 324     101.221  -4.666   5.574  1.00 39.35           C  
ANISOU 2467  CB  HIS A 324     4921   5072   4958     35    -21   -108       C  
ATOM   2468  CG  HIS A 324     100.158  -3.634   5.762  1.00 36.32           C  
ANISOU 2468  CG  HIS A 324     4524   4691   4585     34    -19    -87       C  
ATOM   2469  ND1 HIS A 324      99.589  -3.388   6.994  1.00 30.95           N  
ANISOU 2469  ND1 HIS A 324     3881   3980   3898     19    -10    -62       N  
ATOM   2470  CD2 HIS A 324      99.547  -2.797   4.890  1.00 29.48           C  
ANISOU 2470  CD2 HIS A 324     3641   3849   3712     44    -24   -105       C  
ATOM   2471  CE1 HIS A 324      98.663  -2.453   6.871  1.00 33.45           C  
ANISOU 2471  CE1 HIS A 324     4196   4304   4211     21    -10    -63       C  
ATOM   2472  NE2 HIS A 324      98.621  -2.075   5.606  1.00 32.61           N  
ANISOU 2472  NE2 HIS A 324     4070   4228   4091     33    -17    -94       N  
ATOM   2473  N   PHE A 325     101.632  -8.287   5.842  1.00 33.33           N  
ANISOU 2473  N   PHE A 325     4128   4322   4214     54    -40   -178       N  
ATOM   2474  CA  PHE A 325     102.674  -9.302   5.821  1.00 33.69           C  
ANISOU 2474  CA  PHE A 325     4168   4365   4267     60    -47   -193       C  
ATOM   2475  C   PHE A 325     103.138  -9.743   4.448  1.00 30.71           C  
ANISOU 2475  C   PHE A 325     3764   4010   3897     83    -67   -252       C  
ATOM   2476  O   PHE A 325     104.320 -10.028   4.258  1.00 36.54           O  
ANISOU 2476  O   PHE A 325     4503   4746   4635     86    -69   -253       O  
ATOM   2477  CB  PHE A 325     102.216 -10.518   6.625  1.00 24.44           C  
ANISOU 2477  CB  PHE A 325     2958   3198   3132     66    -55   -186       C  
ATOM   2478  CG  PHE A 325     100.866 -11.030   6.216  1.00 35.48           C  
ANISOU 2478  CG  PHE A 325     4364   4588   4526     74    -66   -257       C  
ATOM   2479  CD1 PHE A 325      99.716 -10.523   6.808  1.00 34.76           C  
ANISOU 2479  CD1 PHE A 325     4243   4512   4454     70    -61   -215       C  
ATOM   2480  CD2 PHE A 325     100.736 -11.979   5.211  1.00 39.90           C  
ANISOU 2480  CD2 PHE A 325     4835   5178   5145    109   -103   -301       C  
ATOM   2481  CE1 PHE A 325      98.467 -10.988   6.432  1.00 33.29           C  
ANISOU 2481  CE1 PHE A 325     4071   4311   4268     77    -71   -289       C  
ATOM   2482  CE2 PHE A 325      99.484 -12.439   4.823  1.00 26.97           C  
ANISOU 2482  CE2 PHE A 325     3163   3541   3541    124   -124   -351       C  
ATOM   2483  CZ  PHE A 325      98.356 -11.947   5.434  1.00 37.10           C  
ANISOU 2483  CZ  PHE A 325     4458   4821   4817    111   -110   -331       C  
ATOM   2484  N   GLU A 326     102.218  -9.801   3.494  1.00 26.19           N  
ANISOU 2484  N   GLU A 326     3114   3475   3362    111    -91   -277       N  
ATOM   2485  CA  GLU A 326     102.564 -10.303   2.177  1.00 35.31           C  
ANISOU 2485  CA  GLU A 326     4198   4691   4527    176   -148   -460       C  
ATOM   2486  C   GLU A 326     103.509  -9.371   1.411  1.00 28.45           C  
ANISOU 2486  C   GLU A 326     3430   3774   3607    131   -104   -357       C  
ATOM   2487  O   GLU A 326     104.605  -9.792   0.951  1.00 28.00           O  
ANISOU 2487  O   GLU A 326     3303   3743   3592    154   -123   -339       O  
ATOM   2488  CB  GLU A 326     101.289 -10.600   1.390  1.00 27.73           C  
ANISOU 2488  CB  GLU A 326     3233   3709   3595    164   -142   -393       C  
ATOM   2489  CG  GLU A 326     101.501 -11.386   0.118  1.00 49.93           C  
ANISOU 2489  CG  GLU A 326     5999   6536   6435    201   -180   -463       C  
ATOM   2490  CD  GLU A 326     100.216 -12.048  -0.388  1.00 57.29           C  
ANISOU 2490  CD  GLU A 326     6890   7468   7407    225   -212   -526       C  
ATOM   2491  OE1 GLU A 326      99.136 -11.840   0.217  1.00 45.63           O  
ANISOU 2491  OE1 GLU A 326     5513   5939   5884    194   -184   -567       O  
ATOM   2492  OE2 GLU A 326     100.284 -12.776  -1.402  1.00 47.31           O  
ANISOU 2492  OE2 GLU A 326     5696   6158   6122    236   -230   -652       O  
ATOM   2493  N   ALA A 327     103.134  -8.092   1.353  1.00 35.42           N  
ANISOU 2493  N   ALA A 327     4268   4683   4508    131    -98   -294       N  
ATOM   2494  CA  ALA A 327     103.997  -7.084   0.742  1.00 36.13           C  
ANISOU 2494  CA  ALA A 327     4421   4762   4546    119    -84   -307       C  
ATOM   2495  C   ALA A 327     105.322  -6.960   1.489  1.00 28.04           C  
ANISOU 2495  C   ALA A 327     3419   3713   3521    100    -70   -259       C  
ATOM   2496  O   ALA A 327     106.376  -6.821   0.866  1.00 35.37           O  
ANISOU 2496  O   ALA A 327     4344   4648   4446    107    -74   -268       O  
ATOM   2497  CB  ALA A 327     103.292  -5.745   0.686  1.00 33.29           C  
ANISOU 2497  CB  ALA A 327     4020   4421   4209    120    -80   -255       C  
ATOM   2498  N   PHE A 328     105.267  -7.056   2.816  1.00 25.40           N  
ANISOU 2498  N   PHE A 328     3070   3364   3219     86    -60   -193       N  
ATOM   2499  CA  PHE A 328     106.475  -6.976   3.636  1.00 37.95           C  
ANISOU 2499  CA  PHE A 328     4689   4925   4806     68    -46   -153       C  
ATOM   2500  C   PHE A 328     107.426  -8.114   3.300  1.00 31.98           C  
ANISOU 2500  C   PHE A 328     3949   4169   4033     75    -54   -200       C  
ATOM   2501  O   PHE A 328     108.646  -7.929   3.226  1.00 35.46           O  
ANISOU 2501  O   PHE A 328     4397   4605   4473     72    -51   -187       O  
ATOM   2502  CB  PHE A 328     106.133  -6.984   5.134  1.00 23.13           C  
ANISOU 2502  CB  PHE A 328     2845   3015   2928     45    -31   -108       C  
ATOM   2503  CG  PHE A 328     107.287  -6.596   6.014  1.00 32.78           C  
ANISOU 2503  CG  PHE A 328     4101   4204   4148     27    -17    -63       C  
ATOM   2504  CD1 PHE A 328     107.393  -5.311   6.524  1.00 25.93           C  
ANISOU 2504  CD1 PHE A 328     3269   3307   3278     10     -6    -28       C  
ATOM   2505  CD2 PHE A 328     108.243  -7.539   6.376  1.00 17.94           C  
ANISOU 2505  CD2 PHE A 328     2235   2319   2263     24    -17    -70       C  
ATOM   2506  CE1 PHE A 328     108.466  -4.953   7.334  1.00 32.56           C  
ANISOU 2506  CE1 PHE A 328     4124   4124   4124      0      0      0       C  
ATOM   2507  CE2 PHE A 328     109.309  -7.197   7.190  1.00 41.68           C  
ANISOU 2507  CE2 PHE A 328     5259   5301   5278     11     -7    -26       C  
ATOM   2508  CZ  PHE A 328     109.424  -5.906   7.673  1.00 30.45           C  
ANISOU 2508  CZ  PHE A 328     3856   3856   3856      0      0      0       C  
ATOM   2509  N   TYR A 329     106.851  -9.291   3.114  1.00 25.15           N  
ANISOU 2509  N   TYR A 329     3064   3313   3178     91    -70   -246       N  
ATOM   2510  CA  TYR A 329     107.595 -10.477   2.731  1.00 31.00           C  
ANISOU 2510  CA  TYR A 329     3738   4078   3961    119    -95   -262       C  
ATOM   2511  C   TYR A 329     108.345 -10.239   1.423  1.00 33.88           C  
ANISOU 2511  C   TYR A 329     4137   4445   4291    128   -102   -326       C  
ATOM   2512  O   TYR A 329     109.583 -10.360   1.367  1.00 36.74           O  
ANISOU 2512  O   TYR A 329     4448   4825   4686    140   -111   -289       O  
ATOM   2513  CB  TYR A 329     106.646 -11.667   2.613  1.00 26.25           C  
ANISOU 2513  CB  TYR A 329     3106   3482   3385    139   -119   -310       C  
ATOM   2514  CG  TYR A 329     107.226 -12.928   2.003  1.00 35.72           C  
ANISOU 2514  CG  TYR A 329     4340   4658   4575    153   -138   -404       C  
ATOM   2515  CD1 TYR A 329     107.975 -13.822   2.754  1.00 32.58           C  
ANISOU 2515  CD1 TYR A 329     3882   4274   4224    163   -152   -358       C  
ATOM   2516  CD2 TYR A 329     107.027 -13.209   0.661  1.00 40.85           C  
ANISOU 2516  CD2 TYR A 329     4846   5391   5285    250   -228   -587       C  
ATOM   2517  CE1 TYR A 329     108.497 -14.965   2.184  1.00 53.98           C  
ANISOU 2517  CE1 TYR A 329     6525   7007   6977    239   -233   -565       C  
ATOM   2518  CE2 TYR A 329     107.543 -14.341   0.083  1.00 37.81           C  
ANISOU 2518  CE2 TYR A 329     4467   4974   4926    229   -218   -481       C  
ATOM   2519  CZ  TYR A 329     108.275 -15.221   0.845  1.00 51.04           C  
ANISOU 2519  CZ  TYR A 329     6149   6629   6613    224   -221   -473       C  
ATOM   2520  OH  TYR A 329     108.781 -16.351   0.251  1.00 43.59           O  
ANISOU 2520  OH  TYR A 329     5174   5683   5705    255   -261   -528       O  
ATOM   2521  N   HIS A 330     107.609  -9.848   0.381  1.00 31.56           N  
ANISOU 2521  N   HIS A 330     3764   4195   4034    158   -124   -329       N  
ATOM   2522  CA  HIS A 330     108.270  -9.636  -0.916  1.00 36.40           C  
ANISOU 2522  CA  HIS A 330     4422   4808   4601    167   -129   -402       C  
ATOM   2523  C   HIS A 330     109.321  -8.511  -0.901  1.00 29.76           C  
ANISOU 2523  C   HIS A 330     3538   3985   3785    165   -121   -322       C  
ATOM   2524  O   HIS A 330     110.410  -8.652  -1.486  1.00 47.46           O  
ANISOU 2524  O   HIS A 330     5770   6236   6026    177   -130   -337       O  
ATOM   2525  CB  HIS A 330     107.225  -9.402  -2.000  1.00 38.19           C  
ANISOU 2525  CB  HIS A 330     4627   5058   4825    189   -147   -451       C  
ATOM   2526  CG  HIS A 330     106.395 -10.615  -2.270  1.00 48.66           C  
ANISOU 2526  CG  HIS A 330     5841   6416   6230    232   -190   -465       C  
ATOM   2527  ND1 HIS A 330     106.915 -11.750  -2.851  1.00 37.34           N  
ANISOU 2527  ND1 HIS A 330     4379   4988   4823    261   -222   -517       N  
ATOM   2528  CD2 HIS A 330     105.086 -10.873  -2.041  1.00 44.43           C  
ANISOU 2528  CD2 HIS A 330     5253   5931   5698    292   -244   -659       C  
ATOM   2529  CE1 HIS A 330     105.965 -12.664  -2.949  1.00 49.98           C  
ANISOU 2529  CE1 HIS A 330     5952   6583   6456    279   -249   -563       C  
ATOM   2530  NE2 HIS A 330     104.844 -12.154  -2.471  1.00 40.88           N  
ANISOU 2530  NE2 HIS A 330     4910   5384   5239    241   -213   -600       N  
ATOM   2531  N   ASN A 331     109.024  -7.420  -0.209  1.00 15.43           N  
ANISOU 2531  N   ASN A 331     1808   2135   1921    126    -89   -299       N  
ATOM   2532  CA  ASN A 331     110.011  -6.353  -0.080  1.00 33.92           C  
ANISOU 2532  CA  ASN A 331     4121   4478   4288    121    -81   -233       C  
ATOM   2533  C   ASN A 331     111.264  -6.819   0.654  1.00 12.54           C  
ANISOU 2533  C   ASN A 331     1472   1738   1554     99    -67   -232       C  
ATOM   2534  O   ASN A 331     112.366  -6.511   0.228  1.00 30.33           O  
ANISOU 2534  O   ASN A 331     3684   4007   3834    111    -74   -210       O  
ATOM   2535  CB  ASN A 331     109.406  -5.113   0.599  1.00 21.93           C  
ANISOU 2535  CB  ASN A 331     2633   2937   2764     96    -61   -187       C  
ATOM   2536  CG  ASN A 331     108.484  -4.340  -0.318  1.00 33.04           C  
ANISOU 2536  CG  ASN A 331     4065   4356   4133    100    -62   -228       C  
ATOM   2537  OD1 ASN A 331     108.652  -4.356  -1.537  1.00 34.65           O  
ANISOU 2537  OD1 ASN A 331     4248   4589   4328    122    -77   -272       O  
ATOM   2538  ND2 ASN A 331     107.488  -3.689   0.255  1.00 28.46           N  
ANISOU 2538  ND2 ASN A 331     3458   3773   3582     95    -58   -183       N  
ATOM   2539  N   THR A 332     111.097  -7.590   1.726  1.00 23.80           N  
ANISOU 2539  N   THR A 332     2870   3158   3015     97    -67   -194       N  
ATOM   2540  CA  THR A 332     112.254  -8.046   2.489  1.00 17.57           C  
ANISOU 2540  CA  THR A 332     2131   2340   2204     79    -55   -190       C  
ATOM   2541  C   THR A 332     113.090  -8.969   1.615  1.00 30.14           C  
ANISOU 2541  C   THR A 332     3658   3966   3826    112    -81   -219       C  
ATOM   2542  O   THR A 332     114.319  -8.906   1.628  1.00 46.50           O  
ANISOU 2542  O   THR A 332     5738   6035   5897    109    -79   -211       O  
ATOM   2543  CB  THR A 332     111.863  -8.757   3.808  1.00 30.92           C  
ANISOU 2543  CB  THR A 332     3792   4047   3911     89    -64   -203       C  
ATOM   2544  OG1 THR A 332     111.099  -7.880   4.635  1.00 23.08           O  
ANISOU 2544  OG1 THR A 332     2842   3003   2923     49    -34   -106       O  
ATOM   2545  CG2 THR A 332     113.119  -9.192   4.569  1.00 25.84           C  
ANISOU 2545  CG2 THR A 332     3203   3353   3261     56    -40   -140       C  
ATOM   2546  N   VAL A 333     112.424  -9.799   0.818  1.00 26.49           N  
ANISOU 2546  N   VAL A 333     3162   3528   3375    139   -105   -272       N  
ATOM   2547  CA  VAL A 333     113.157 -10.679  -0.086  1.00 28.08           C  
ANISOU 2547  CA  VAL A 333     3303   3794   3572    211   -165   -445       C  
ATOM   2548  C   VAL A 333     113.985  -9.885  -1.082  1.00 29.11           C  
ANISOU 2548  C   VAL A 333     3518   3875   3667    163   -124   -367       C  
ATOM   2549  O   VAL A 333     115.182 -10.152  -1.251  1.00 32.75           O  
ANISOU 2549  O   VAL A 333     3978   4338   4128    169   -128   -375       O  
ATOM   2550  CB  VAL A 333     112.198 -11.619  -0.843  1.00 43.02           C  
ANISOU 2550  CB  VAL A 333     5257   5632   5455    184   -150   -427       C  
ATOM   2551  CG1 VAL A 333     112.921 -12.345  -1.989  1.00 27.76           C  
ANISOU 2551  CG1 VAL A 333     3181   3798   3570    296   -246   -612       C  
ATOM   2552  CG2 VAL A 333     111.584 -12.612   0.134  1.00 27.67           C  
ANISOU 2552  CG2 VAL A 333     3315   3668   3529    179   -152   -426       C  
ATOM   2553  N   LYS A 334     113.382  -8.852  -1.667  1.00 23.78           N  
ANISOU 2553  N   LYS A 334     2842   3211   2980    163   -119   -363       N  
ATOM   2554  CA  LYS A 334     114.122  -8.023  -2.619  1.00 28.68           C  
ANISOU 2554  CA  LYS A 334     3394   3869   3635    187   -132   -335       C  
ATOM   2555  C   LYS A 334     115.271  -7.296  -1.930  1.00 37.98           C  
ANISOU 2555  C   LYS A 334     4660   5007   4765    147   -101   -316       C  
ATOM   2556  O   LYS A 334     116.325  -7.091  -2.521  1.00 41.37           O  
ANISOU 2556  O   LYS A 334     5025   5463   5231    169   -115   -296       O  
ATOM   2557  CB  LYS A 334     113.218  -6.988  -3.299  1.00 36.40           C  
ANISOU 2557  CB  LYS A 334     4433   4842   4556    174   -120   -373       C  
ATOM   2558  CG  LYS A 334     112.186  -7.546  -4.248  1.00 75.90           C  
ANISOU 2558  CG  LYS A 334     9410   9870   9559    204   -144   -435       C  
ATOM   2559  CD  LYS A 334     111.597  -6.430  -5.113  1.00 88.58           C  
ANISOU 2559  CD  LYS A 334    11011  11497  11150    211   -144   -441       C  
ATOM   2560  CE  LYS A 334     110.640  -6.993  -6.158  1.00 92.89           C  
ANISOU 2560  CE  LYS A 334    11439  12098  11759    267   -186   -460       C  
ATOM   2561  NZ  LYS A 334     109.492  -7.711  -5.538  1.00 86.71           N  
ANISOU 2561  NZ  LYS A 334    10743  11276  10927    242   -174   -518       N  
ATOM   2562  N   GLN A 335     115.073  -6.940  -0.662  1.00 36.35           N  
ANISOU 2562  N   GLN A 335     4430   4784   4596    129    -88   -236       N  
ATOM   2563  CA  GLN A 335     116.106  -6.232   0.081  1.00 43.24           C  
ANISOU 2563  CA  GLN A 335     5372   5620   5439     96    -63   -211       C  
ATOM   2564  C   GLN A 335     117.296  -7.123   0.414  1.00 35.12           C  
ANISOU 2564  C   GLN A 335     4342   4589   4414     99    -67   -217       C  
ATOM   2565  O   GLN A 335     118.432  -6.680   0.348  1.00 29.88           O  
ANISOU 2565  O   GLN A 335     3647   3931   3775    103    -68   -186       O  
ATOM   2566  CB  GLN A 335     115.520  -5.641   1.365  1.00 32.27           C  
ANISOU 2566  CB  GLN A 335     3965   4236   4059     94    -60   -193       C  
ATOM   2567  CG  GLN A 335     114.705  -4.372   1.142  1.00 34.31           C  
ANISOU 2567  CG  GLN A 335     4234   4487   4314     84    -52   -172       C  
ATOM   2568  CD  GLN A 335     114.092  -3.833   2.425  1.00 37.89           C  
ANISOU 2568  CD  GLN A 335     4750   4870   4775     39    -23    -88       C  
ATOM   2569  OE1 GLN A 335     113.553  -4.585   3.230  1.00 28.76           O  
ANISOU 2569  OE1 GLN A 335     3600   3705   3623     34    -21    -80       O  
ATOM   2570  NE2 GLN A 335     114.061  -2.515   2.556  1.00 36.29           N  
ANISOU 2570  NE2 GLN A 335     4563   4650   4577     27    -15    -61       N  
ATOM   2571  N   VAL A 336     117.030  -8.383   0.756  1.00 24.60           N  
ANISOU 2571  N   VAL A 336     2960   3271   3117    117    -82   -216       N  
ATOM   2572  CA  VAL A 336     118.107  -9.330   0.993  1.00 31.93           C  
ANISOU 2572  CA  VAL A 336     3925   4185   4020    114    -82   -253       C  
ATOM   2573  C   VAL A 336     118.873  -9.570  -0.290  1.00 37.83           C  
ANISOU 2573  C   VAL A 336     4598   4975   4800    153   -112   -275       C  
ATOM   2574  O   VAL A 336     120.107  -9.556  -0.297  1.00 36.11           O  
ANISOU 2574  O   VAL A 336     4358   4802   4559    191   -139   -374       O  
ATOM   2575  CB  VAL A 336     117.587 -10.677   1.531  1.00 22.55           C  
ANISOU 2575  CB  VAL A 336     2662   3047   2859    165   -125   -339       C  
ATOM   2576  CG1 VAL A 336     118.763 -11.643   1.698  1.00 23.27           C  
ANISOU 2576  CG1 VAL A 336     2766   3103   2972    143   -111   -264       C  
ATOM   2577  CG2 VAL A 336     116.908 -10.473   2.878  1.00 32.64           C  
ANISOU 2577  CG2 VAL A 336     3994   4261   4148    103    -78   -198       C  
ATOM   2578  N   LYS A 337     118.148  -9.771  -1.388  1.00 32.68           N  
ANISOU 2578  N   LYS A 337     3916   4348   4151    180   -133   -320       N  
ATOM   2579  CA  LYS A 337     118.838  -9.960  -2.664  1.00 46.22           C  
ANISOU 2579  CA  LYS A 337     5601   6092   5869    211   -156   -367       C  
ATOM   2580  C   LYS A 337     119.637  -8.752  -3.154  1.00 44.01           C  
ANISOU 2580  C   LYS A 337     5300   5877   5545    254   -181   -479       C  
ATOM   2581  O   LYS A 337     120.674  -8.911  -3.789  1.00 42.76           O  
ANISOU 2581  O   LYS A 337     5229   5651   5366    202   -144   -413       O  
ATOM   2582  CB  LYS A 337     117.831 -10.413  -3.731  1.00 43.59           C  
ANISOU 2582  CB  LYS A 337     5234   5784   5544    243   -184   -422       C  
ATOM   2583  CG  LYS A 337     117.256 -11.813  -3.459  1.00 42.62           C  
ANISOU 2583  CG  LYS A 337     5057   5717   5421    324   -257   -628       C  
ATOM   2584  CD  LYS A 337     116.247 -12.241  -4.517  1.00 48.73           C  
ANISOU 2584  CD  LYS A 337     5792   6516   6209    367   -296   -708       C  
ATOM   2585  CE  LYS A 337     115.815 -13.677  -4.325  1.00 38.10           C  
ANISOU 2585  CE  LYS A 337     4422   5155   4901    392   -332   -765       C  
ATOM   2586  NZ  LYS A 337     114.593 -14.003  -5.106  1.00 57.50           N  
ANISOU 2586  NZ  LYS A 337     7003   7522   7321    312   -269   -673       N  
ATOM   2587  N   ALA A 338     119.147  -7.556  -2.866  1.00 40.30           N  
ANISOU 2587  N   ALA A 338     4943   5315   5052    165   -114   -343       N  
ATOM   2588  CA  ALA A 338     119.851  -6.318  -3.194  1.00 40.02           C  
ANISOU 2588  CA  ALA A 338     4833   5355   5018    213   -141   -395       C  
ATOM   2589  C   ALA A 338     121.037  -6.016  -2.267  1.00 35.30           C  
ANISOU 2589  C   ALA A 338     4288   4672   4453    146    -95   -248       C  
ATOM   2590  O   ALA A 338     121.837  -5.127  -2.552  1.00 31.37           O  
ANISOU 2590  O   ALA A 338     3796   4172   3950    141    -89   -236       O  
ATOM   2591  CB  ALA A 338     118.882  -5.145  -3.191  1.00 25.65           C  
ANISOU 2591  CB  ALA A 338     3106   3454   3185    143    -91   -291       C  
ATOM   2592  N   GLY A 339     121.175  -6.770  -1.181  1.00 40.04           N  
ANISOU 2592  N   GLY A 339     4948   5239   5025    122    -81   -256       N  
ATOM   2593  CA  GLY A 339     122.266  -6.517  -0.264  1.00 22.81           C  
ANISOU 2593  CA  GLY A 339     2783   3035   2848    103    -68   -217       C  
ATOM   2594  C   GLY A 339     121.967  -5.469   0.804  1.00 41.78           C  
ANISOU 2594  C   GLY A 339     5212   5404   5257     73    -47   -157       C  
ATOM   2595  O   GLY A 339     122.868  -5.124   1.578  1.00 29.71           O  
ANISOU 2595  O   GLY A 339     3676   3861   3751     63    -40   -113       O  
ATOM   2596  N   VAL A 340     120.728  -4.964   0.905  1.00 31.16           N  
ANISOU 2596  N   VAL A 340     3835   4090   3917     91    -57   -178       N  
ATOM   2597  CA  VAL A 340     120.561  -3.925   1.909  1.00 24.61           C  
ANISOU 2597  CA  VAL A 340     3044   3213   3095     56    -34   -112       C  
ATOM   2598  C   VAL A 340     120.200  -4.586   3.220  1.00 17.85           C  
ANISOU 2598  C   VAL A 340     2216   2313   2254     31    -19    -57       C  
ATOM   2599  O   VAL A 340     120.252  -3.969   4.276  1.00 38.97           O  
ANISOU 2599  O   VAL A 340     4919   4958   4931     12     -7    -26       O  
ATOM   2600  CB  VAL A 340     119.521  -2.835   1.547  1.00 38.40           C  
ANISOU 2600  CB  VAL A 340     4804   4935   4851     41    -24    -74       C  
ATOM   2601  CG1 VAL A 340     119.770  -2.350   0.132  1.00 44.10           C  
ANISOU 2601  CG1 VAL A 340     5523   5682   5550     55    -32   -115       C  
ATOM   2602  CG2 VAL A 340     118.172  -3.445   1.497  1.00 34.98           C  
ANISOU 2602  CG2 VAL A 340     4361   4513   4418     48    -29    -88       C  
ATOM   2603  N   ILE A 341     119.902  -5.876   3.159  1.00 26.93           N  
ANISOU 2603  N   ILE A 341     3339   3499   3394     55    -35   -113       N  
ATOM   2604  CA  ILE A 341     119.906  -6.722   4.337  1.00 24.50           C  
ANISOU 2604  CA  ILE A 341     3067   3153   3090     31    -20    -72       C  
ATOM   2605  C   ILE A 341     120.853  -7.886   4.035  1.00 30.21           C  
ANISOU 2605  C   ILE A 341     3745   3920   3813     64    -43   -133       C  
ATOM   2606  O   ILE A 341     120.617  -8.615   3.072  1.00 41.03           O  
ANISOU 2606  O   ILE A 341     5080   5326   5183     95    -66   -194       O  
ATOM   2607  CB  ILE A 341     118.528  -7.297   4.650  1.00 27.76           C  
ANISOU 2607  CB  ILE A 341     3477   3566   3503     32    -21    -75       C  
ATOM   2608  CG1 ILE A 341     117.513  -6.191   4.876  1.00 22.14           C  
ANISOU 2608  CG1 ILE A 341     2780   2839   2795     20    -13    -47       C  
ATOM   2609  CG2 ILE A 341     118.619  -8.290   5.819  1.00 17.20           C  
ANISOU 2609  CG2 ILE A 341     2138   2220   2178     27    -19    -54       C  
ATOM   2610  CD1 ILE A 341     116.128  -6.710   5.076  1.00 28.74           C  
ANISOU 2610  CD1 ILE A 341     3601   3680   3637     24    -16    -49       C  
ATOM   2611  N   ALA A 342     121.925  -8.054   4.793  1.00 31.42           N  
ANISOU 2611  N   ALA A 342     3922   4041   3978     42    -28    -78       N  
ATOM   2612  CA  ALA A 342     122.891  -9.108   4.477  1.00 40.58           C  
ANISOU 2612  CA  ALA A 342     5049   5241   5130     75    -52   -152       C  
ATOM   2613  C   ALA A 342     122.265 -10.489   4.751  1.00 22.89           C  
ANISOU 2613  C   ALA A 342     2805   2989   2905     72    -53   -133       C  
ATOM   2614  O   ALA A 342     121.499 -10.617   5.711  1.00 28.76           O  
ANISOU 2614  O   ALA A 342     3566   3714   3647     56    -42   -107       O  
ATOM   2615  CB  ALA A 342     124.181  -8.919   5.271  1.00 30.46           C  
ANISOU 2615  CB  ALA A 342     3794   3921   3856     46    -32    -86       C  
ATOM   2616  N   GLU A 343     122.578 -11.524   3.955  1.00 46.05           N  
ANISOU 2616  N   GLU A 343     5741   5935   5822     92    -70   -203       N  
ATOM   2617  CA  GLU A 343     122.018 -12.854   4.267  1.00 24.45           C  
ANISOU 2617  CA  GLU A 343     2956   3214   3120    114    -91   -208       C  
ATOM   2618  C   GLU A 343     122.431 -13.390   5.605  1.00 26.64           C  
ANISOU 2618  C   GLU A 343     3253   3473   3397     98    -79   -180       C  
ATOM   2619  O   GLU A 343     121.659 -14.116   6.212  1.00 23.04           O  
ANISOU 2619  O   GLU A 343     2798   3011   2946     97    -81   -180       O  
ATOM   2620  CB  GLU A 343     122.351 -13.970   3.254  1.00 33.14           C  
ANISOU 2620  CB  GLU A 343     4068   4318   4204    138   -115   -302       C  
ATOM   2621  CG  GLU A 343     121.555 -14.073   1.996  1.00 57.88           C  
ANISOU 2621  CG  GLU A 343     7098   7527   7369    221   -185   -437       C  
ATOM   2622  CD  GLU A 343     121.925 -15.327   1.197  1.00 53.91           C  
ANISOU 2622  CD  GLU A 343     6653   6976   6856    198   -172   -425       C  
ATOM   2623  OE1 GLU A 343     122.569 -15.222   0.141  1.00 62.99           O  
ANISOU 2623  OE1 GLU A 343     7712   8174   8048    237   -204   -415       O  
ATOM   2624  OE2 GLU A 343     121.548 -16.445   1.651  1.00 37.95           O  
ANISOU 2624  OE2 GLU A 343     4552   4974   4894    225   -204   -401       O  
ATOM   2625  N   SER A 344     123.618 -13.033   6.075  1.00 28.11           N  
ANISOU 2625  N   SER A 344     3453   3650   3577     86    -68   -157       N  
ATOM   2626  CA  SER A 344     124.064 -13.486   7.382  1.00 19.42           C  
ANISOU 2626  CA  SER A 344     2396   2524   2459     65    -52   -144       C  
ATOM   2627  C   SER A 344     123.109 -13.045   8.469  1.00 25.74           C  
ANISOU 2627  C   SER A 344     3202   3309   3269     45    -36    -85       C  
ATOM   2628  O   SER A 344     122.903 -13.767   9.442  1.00 30.44           O  
ANISOU 2628  O   SER A 344     3819   3891   3856     36    -29    -81       O  
ATOM   2629  CB  SER A 344     125.464 -12.972   7.682  1.00 21.95           C  
ANISOU 2629  CB  SER A 344     2725   2839   2777     57    -44   -125       C  
ATOM   2630  OG  SER A 344     125.446 -11.566   7.818  1.00 45.45           O  
ANISOU 2630  OG  SER A 344     5718   5800   5750     37    -28    -83       O  
ATOM   2631  N   ARG A 345     122.477 -11.893   8.268  1.00 30.48           N  
ANISOU 2631  N   ARG A 345     3828   3895   3856     30    -23    -69       N  
ATOM   2632  CA  ARG A 345     121.534 -11.351   9.241  1.00 16.06           C  
ANISOU 2632  CA  ARG A 345     2019   2047   2035     10     -8    -20       C  
ATOM   2633  C   ARG A 345     120.230 -12.180   9.255  1.00 20.65           C  
ANISOU 2633  C   ARG A 345     2590   2639   2619     19    -14    -37       C  
ATOM   2634  O   ARG A 345     119.712 -12.527  10.334  1.00 22.96           O  
ANISOU 2634  O   ARG A 345     2901   2915   2907      6     -5    -15       O  
ATOM   2635  CB  ARG A 345     121.250  -9.863   8.962  1.00 24.15           C  
ANISOU 2635  CB  ARG A 345     3059   3059   3059      0      0      0       C  
ATOM   2636  CG  ARG A 345     120.181  -9.230   9.858  1.00 23.45           C  
ANISOU 2636  CG  ARG A 345     2970   2970   2970      0      0      0       C  
ATOM   2637  CD  ARG A 345     120.669  -8.879  11.247  1.00 14.06           C  
ANISOU 2637  CD  ARG A 345     1781   1781   1781      0      0      0       C  
ATOM   2638  NE  ARG A 345     120.614 -10.010  12.157  1.00 13.95           N  
ANISOU 2638  NE  ARG A 345     1766   1766   1766      0      0      0       N  
ATOM   2639  CZ  ARG A 345     119.522 -10.387  12.812  1.00 29.17           C  
ANISOU 2639  CZ  ARG A 345     3695   3695   3695      0      0      0       C  
ATOM   2640  NH1 ARG A 345     118.372  -9.742  12.622  1.00 21.05           N  
ANISOU 2640  NH1 ARG A 345     2666   2666   2666      0      0      0       N  
ATOM   2641  NH2 ARG A 345     119.565 -11.440  13.626  1.00 18.16           N  
ANISOU 2641  NH2 ARG A 345     2300   2300   2300      0      0      0       N  
ATOM   2642  N   ILE A 346     119.672 -12.479   8.085  1.00  7.97           N  
ANISOU 2642  N   ILE A 346      970   1051   1009     37    -29    -87       N  
ATOM   2643  CA  ILE A 346     118.494 -13.322   8.056  1.00 27.92           C  
ANISOU 2643  CA  ILE A 346     3485   3584   3539     47    -38   -112       C  
ATOM   2644  C   ILE A 346     118.832 -14.739   8.535  1.00 26.80           C  
ANISOU 2644  C   ILE A 346     3311   3454   3418     63    -54   -124       C  
ATOM   2645  O   ILE A 346     118.017 -15.366   9.186  1.00 37.49           O  
ANISOU 2645  O   ILE A 346     4667   4803   4776     61    -54   -122       O  
ATOM   2646  CB  ILE A 346     117.746 -13.332   6.706  1.00 32.22           C  
ANISOU 2646  CB  ILE A 346     3968   4176   4100     92    -76   -201       C  
ATOM   2647  CG1 ILE A 346     118.525 -14.086   5.645  1.00 33.49           C  
ANISOU 2647  CG1 ILE A 346     4145   4326   4255     95    -81   -222       C  
ATOM   2648  CG2 ILE A 346     117.339 -11.904   6.278  1.00 26.25           C  
ANISOU 2648  CG2 ILE A 346     3227   3415   3332     77    -60   -169       C  
ATOM   2649  CD1 ILE A 346     117.765 -14.198   4.359  1.00 56.77           C  
ANISOU 2649  CD1 ILE A 346     7003   7334   7232    161   -139   -341       C  
ATOM   2650  N   ASN A 347     120.041 -15.220   8.230  1.00 19.66           N  
ANISOU 2650  N   ASN A 347     2420   2546   2504     70    -61   -162       N  
ATOM   2651  CA  ASN A 347     120.506 -16.520   8.708  1.00 31.03           C  
ANISOU 2651  CA  ASN A 347     3820   3998   3971     89    -82   -168       C  
ATOM   2652  C   ASN A 347     120.484 -16.562  10.212  1.00 33.05           C  
ANISOU 2652  C   ASN A 347     4106   4236   4216     64    -59   -122       C  
ATOM   2653  O   ASN A 347     120.010 -17.536  10.800  1.00 26.69           O  
ANISOU 2653  O   ASN A 347     3285   3433   3422     86    -84   -182       O  
ATOM   2654  CB  ASN A 347     121.928 -16.852   8.212  1.00 23.02           C  
ANISOU 2654  CB  ASN A 347     2777   3006   2965    131   -122   -267       C  
ATOM   2655  CG  ASN A 347     121.970 -17.281   6.751  1.00 31.49           C  
ANISOU 2655  CG  ASN A 347     3874   4063   4028    128   -120   -283       C  
ATOM   2656  OD1 ASN A 347     120.948 -17.621   6.155  1.00 30.23           O  
ANISOU 2656  OD1 ASN A 347     3702   3906   3880    142   -136   -317       O  
ATOM   2657  ND2 ASN A 347     123.169 -17.291   6.175  1.00 20.44           N  
ANISOU 2657  ND2 ASN A 347     2416   2695   2655    153   -142   -273       N  
ATOM   2658  N   ASP A 348     120.996 -15.497  10.828  1.00 24.98           N  
ANISOU 2658  N   ASP A 348     3108   3204   3177     48    -42   -102       N  
ATOM   2659  CA  ASP A 348     121.069 -15.412  12.284  1.00 21.67           C  
ANISOU 2659  CA  ASP A 348     2730   2756   2747     13    -12    -31       C  
ATOM   2660  C   ASP A 348     119.670 -15.365  12.892  1.00 17.49           C  
ANISOU 2660  C   ASP A 348     2211   2218   2215      3     -3     -8       C  
ATOM   2661  O   ASP A 348     119.392 -15.995  13.916  1.00 28.67           O  
ANISOU 2661  O   ASP A 348     3631   3631   3631      0      0      0       O  
ATOM   2662  CB  ASP A 348     121.849 -14.170  12.731  1.00 23.85           C  
ANISOU 2662  CB  ASP A 348     3020   3020   3020      0      0      0       C  
ATOM   2663  CG  ASP A 348     122.112 -14.141  14.221  1.00 26.63           C  
ANISOU 2663  CG  ASP A 348     3373   3373   3373      0      0      0       C  
ATOM   2664  OD1 ASP A 348     122.649 -15.118  14.772  1.00 34.09           O  
ANISOU 2664  OD1 ASP A 348     4318   4318   4318      0      0      0       O  
ATOM   2665  OD2 ASP A 348     121.627 -13.186  14.868  1.00 38.27           O  
ANISOU 2665  OD2 ASP A 348     4847   4847   4847      0      0      0       O  
ATOM   2666  N   ALA A 349     118.786 -14.622  12.238  1.00 30.24           N  
ANISOU 2666  N   ALA A 349     3826   3834   3832      3     -3     -7       N  
ATOM   2667  CA  ALA A 349     117.390 -14.505  12.674  1.00 24.66           C  
ANISOU 2667  CA  ALA A 349     3123   3123   3123      0      0      0       C  
ATOM   2668  C   ALA A 349     116.730 -15.887  12.644  1.00 24.36           C  
ANISOU 2668  C   ALA A 349     3066   3098   3093     14    -13    -29       C  
ATOM   2669  O   ALA A 349     116.070 -16.319  13.616  1.00 22.57           O  
ANISOU 2669  O   ALA A 349     2850   2864   2863      6     -5    -13       O  
ATOM   2670  CB  ALA A 349     116.632 -13.532  11.790  1.00 25.85           C  
ANISOU 2670  CB  ALA A 349     3274   3274   3274      0      0      0       C  
ATOM   2671  N   VAL A 350     116.934 -16.596  11.534  1.00 36.38           N  
ANISOU 2671  N   VAL A 350     4566   4632   4624     37    -35    -93       N  
ATOM   2672  CA  VAL A 350     116.332 -17.908  11.376  1.00 20.03           C  
ANISOU 2672  CA  VAL A 350     2452   2576   2585     63    -65   -131       C  
ATOM   2673  C   VAL A 350     116.894 -18.899  12.375  1.00 20.38           C  
ANISOU 2673  C   VAL A 350     2522   2600   2623     58    -63   -143       C  
ATOM   2674  O   VAL A 350     116.135 -19.619  13.003  1.00 27.46           O  
ANISOU 2674  O   VAL A 350     3416   3487   3529     59    -68   -149       O  
ATOM   2675  CB  VAL A 350     116.437 -18.431   9.918  1.00 31.36           C  
ANISOU 2675  CB  VAL A 350     3830   4026   4057    120   -127   -268       C  
ATOM   2676  CG1 VAL A 350     115.976 -19.871   9.822  1.00 32.13           C  
ANISOU 2676  CG1 VAL A 350     3912   4114   4182    122   -140   -246       C  
ATOM   2677  CG2 VAL A 350     115.687 -17.539   8.954  1.00 30.53           C  
ANISOU 2677  CG2 VAL A 350     3719   3935   3946    122   -125   -276       C  
ATOM   2678  N   ARG A 351     118.201 -18.868  12.586  1.00 24.78           N  
ANISOU 2678  N   ARG A 351     3053   3170   3190     75    -79   -163       N  
ATOM   2679  CA  ARG A 351     118.824 -19.680  13.613  1.00 25.58           C  
ANISOU 2679  CA  ARG A 351     3169   3264   3286     58    -64   -112       C  
ATOM   2680  C   ARG A 351     118.177 -19.445  14.965  1.00 34.76           C  
ANISOU 2680  C   ARG A 351     4374   4410   4424     29    -33    -71       C  
ATOM   2681  O   ARG A 351     117.802 -20.393  15.646  1.00 28.52           O  
ANISOU 2681  O   ARG A 351     3579   3615   3643     35    -41    -83       O  
ATOM   2682  CB  ARG A 351     120.311 -19.355  13.715  1.00 29.94           C  
ANISOU 2682  CB  ARG A 351     3749   3807   3821     48    -51   -109       C  
ATOM   2683  CG  ARG A 351     121.116 -20.101  12.680  1.00 31.53           C  
ANISOU 2683  CG  ARG A 351     3889   4027   4064    104   -114   -212       C  
ATOM   2684  CD  ARG A 351     122.590 -20.057  12.964  1.00 36.09           C  
ANISOU 2684  CD  ARG A 351     4474   4607   4633    101   -108   -200       C  
ATOM   2685  NE  ARG A 351     123.344 -20.630  11.861  1.00 28.39           N  
ANISOU 2685  NE  ARG A 351     3514   3618   3654    103   -111   -221       N  
ATOM   2686  CZ  ARG A 351     123.921 -19.962  10.873  1.00 36.18           C  
ANISOU 2686  CZ  ARG A 351     4457   4637   4653    118   -123   -208       C  
ATOM   2687  NH1 ARG A 351     123.875 -18.640  10.819  1.00 40.15           N  
ANISOU 2687  NH1 ARG A 351     5012   5126   5119     87    -85   -188       N  
ATOM   2688  NH2 ARG A 351     124.569 -20.634   9.930  1.00 38.95           N  
ANISOU 2688  NH2 ARG A 351     4827   4970   5003    137   -145   -290       N  
ATOM   2689  N   ARG A 352     118.062 -18.179  15.361  1.00 33.01           N  
ANISOU 2689  N   ARG A 352     4175   4183   4184      6     -6    -14       N  
ATOM   2690  CA  ARG A 352     117.533 -17.851  16.688  1.00 32.60           C  
ANISOU 2690  CA  ARG A 352     4128   4128   4128      0      0      0       C  
ATOM   2691  C   ARG A 352     116.072 -18.277  16.870  1.00 20.66           C  
ANISOU 2691  C   ARG A 352     2616   2616   2616      0      0      0       C  
ATOM   2692  O   ARG A 352     115.674 -18.729  17.942  1.00 22.33           O  
ANISOU 2692  O   ARG A 352     2829   2829   2829      0      0      0       O  
ATOM   2693  CB  ARG A 352     117.669 -16.337  16.947  1.00 38.27           C  
ANISOU 2693  CB  ARG A 352     4846   4846   4846      0      0      0       C  
ATOM   2694  CG  ARG A 352     119.121 -15.877  17.112  1.00 25.85           C  
ANISOU 2694  CG  ARG A 352     3274   3274   3274      0      0      0       C  
ATOM   2695  CD  ARG A 352     119.279 -14.374  17.124  1.00 26.76           C  
ANISOU 2695  CD  ARG A 352     3389   3389   3389      0      0      0       C  
ATOM   2696  NE  ARG A 352     120.657 -13.995  17.427  1.00 28.17           N  
ANISOU 2696  NE  ARG A 352     3568   3568   3568      0      0      0       N  
ATOM   2697  CZ  ARG A 352     121.132 -13.851  18.655  1.00 26.20           C  
ANISOU 2697  CZ  ARG A 352     3318   3318   3318      0      0      0       C  
ATOM   2698  NH1 ARG A 352     120.326 -14.012  19.702  1.00 25.79           N  
ANISOU 2698  NH1 ARG A 352     3266   3266   3266      0      0      0       N  
ATOM   2699  NH2 ARG A 352     122.398 -13.522  18.831  1.00 10.72           N  
ANISOU 2699  NH2 ARG A 352     1358   1358   1358      0      0      0       N  
ATOM   2700  N   PHE A 353     115.264 -18.099  15.835  1.00 16.15           N  
ANISOU 2700  N   PHE A 353     2045   2045   2045      0      0      0       N  
ATOM   2701  CA  PHE A 353     113.843 -18.459  15.934  1.00 20.86           C  
ANISOU 2701  CA  PHE A 353     2636   2643   2647      5     -5    -14       C  
ATOM   2702  C   PHE A 353     113.647 -20.009  15.873  1.00 32.41           C  
ANISOU 2702  C   PHE A 353     4059   4111   4144     30    -38    -67       C  
ATOM   2703  O   PHE A 353     112.895 -20.601  16.675  1.00 31.09           O  
ANISOU 2703  O   PHE A 353     3905   3930   3979     27    -37    -75       O  
ATOM   2704  CB  PHE A 353     113.059 -17.753  14.821  1.00  9.44           C  
ANISOU 2704  CB  PHE A 353     1181   1200   1205     11    -12    -31       C  
ATOM   2705  CG  PHE A 353     111.587 -18.019  14.860  1.00 21.67           C  
ANISOU 2705  CG  PHE A 353     2723   2750   2762     16    -18    -48       C  
ATOM   2706  CD1 PHE A 353     110.875 -17.847  16.036  1.00 13.29           C  
ANISOU 2706  CD1 PHE A 353     1681   1684   1685      2     -2     -5       C  
ATOM   2707  CD2 PHE A 353     110.901 -18.375  13.704  1.00 23.74           C  
ANISOU 2707  CD2 PHE A 353     2932   3022   3068     49    -58   -133       C  
ATOM   2708  CE1 PHE A 353     109.517 -18.090  16.067  1.00 26.46           C  
ANISOU 2708  CE1 PHE A 353     3340   3353   3363      7     -9    -24       C  
ATOM   2709  CE2 PHE A 353     109.539 -18.614  13.730  1.00 24.09           C  
ANISOU 2709  CE2 PHE A 353     2992   3051   3109     41    -51   -127       C  
ATOM   2710  CZ  PHE A 353     108.853 -18.470  14.915  1.00 15.78           C  
ANISOU 2710  CZ  PHE A 353     1943   2007   2046     29    -37    -77       C  
ATOM   2711  N   LEU A 354     114.326 -20.654  14.929  1.00 30.58           N  
ANISOU 2711  N   LEU A 354     3788   3873   3957     67    -87   -158       N  
ATOM   2712  CA  LEU A 354     114.273 -22.104  14.816  1.00 42.39           C  
ANISOU 2712  CA  LEU A 354     5245   5344   5516     99   -143   -231       C  
ATOM   2713  C   LEU A 354     114.832 -22.741  16.074  1.00 34.26           C  
ANISOU 2713  C   LEU A 354     4269   4301   4448     72    -97   -164       C  
ATOM   2714  O   LEU A 354     114.399 -23.799  16.442  1.00 30.85           O  
ANISOU 2714  O   LEU A 354     3824   3840   4057     84   -127   -192       O  
ATOM   2715  CB  LEU A 354     115.043 -22.624  13.598  1.00 21.81           C  
ANISOU 2715  CB  LEU A 354     2661   2722   2906    107   -135   -241       C  
ATOM   2716  CG  LEU A 354     114.395 -22.410  12.230  1.00 24.19           C  
ANISOU 2716  CG  LEU A 354     2898   3061   3231    114   -181   -261       C  
ATOM   2717  CD1 LEU A 354     115.238 -23.030  11.120  1.00 21.81           C  
ANISOU 2717  CD1 LEU A 354     2567   2758   2961    141   -224   -313       C  
ATOM   2718  CD2 LEU A 354     112.969 -22.923  12.194  1.00 28.38           C  
ANISOU 2718  CD2 LEU A 354     3384   3537   3862    166   -249   -390       C  
ATOM   2719  N   ARG A 355     115.831 -22.138  16.704  1.00 23.75           N  
ANISOU 2719  N   ARG A 355     2941   3005   3080     48    -77   -108       N  
ATOM   2720  CA  ARG A 355     116.346 -22.666  17.965  1.00 31.34           C  
ANISOU 2720  CA  ARG A 355     3929   3946   4031     44    -59    -97       C  
ATOM   2721  C   ARG A 355     115.206 -22.858  18.974  1.00 26.22           C  
ANISOU 2721  C   ARG A 355     3275   3310   3379     32    -58    -71       C  
ATOM   2722  O   ARG A 355     115.149 -23.868  19.695  1.00 20.68           O  
ANISOU 2722  O   ARG A 355     2579   2576   2703     43    -71    -95       O  
ATOM   2723  CB  ARG A 355     117.437 -21.735  18.505  1.00 27.80           C  
ANISOU 2723  CB  ARG A 355     3504   3516   3544     20    -23    -42       C  
ATOM   2724  CG  ARG A 355     118.096 -22.119  19.822  1.00 30.12           C  
ANISOU 2724  CG  ARG A 355     3808   3812   3825      8    -10    -17       C  
ATOM   2725  CD  ARG A 355     119.281 -21.196  20.044  1.00 25.65           C  
ANISOU 2725  CD  ARG A 355     3249   3249   3249      0      0      0       C  
ATOM   2726  NE  ARG A 355     120.278 -21.380  18.993  1.00 14.91           N  
ANISOU 2726  NE  ARG A 355     1881   1890   1895      6     -9    -13       N  
ATOM   2727  CZ  ARG A 355     120.906 -20.407  18.343  1.00 21.68           C  
ANISOU 2727  CZ  ARG A 355     2746   2746   2746      0      0      0       C  
ATOM   2728  NH1 ARG A 355     120.572 -19.133  18.555  1.00 19.39           N  
ANISOU 2728  NH1 ARG A 355     2455   2455   2455      0      0      0       N  
ATOM   2729  NH2 ARG A 355     121.791 -20.715  17.394  1.00 24.12           N  
ANISOU 2729  NH2 ARG A 355     3040   3057   3068     19    -22    -42       N  
ATOM   2730  N   ALA A 356     114.289 -21.893  18.994  1.00 33.72           N  
ANISOU 2730  N   ALA A 356     4244   4266   4301     17    -30    -41       N  
ATOM   2731  CA  ALA A 356     113.138 -21.942  19.880  1.00 30.99           C  
ANISOU 2731  CA  ALA A 356     3912   3916   3946     11    -16    -27       C  
ATOM   2732  C   ALA A 356     112.119 -22.965  19.418  1.00 25.09           C  
ANISOU 2732  C   ALA A 356     3136   3137   3261     34    -60    -85       C  
ATOM   2733  O   ALA A 356     111.686 -23.778  20.229  1.00 23.50           O  
ANISOU 2733  O   ALA A 356     2907   2933   3089     35    -88    -86       O  
ATOM   2734  CB  ALA A 356     112.496 -20.584  20.010  1.00 22.94           C  
ANISOU 2734  CB  ALA A 356     2905   2905   2905      0      0      0       C  
ATOM   2735  N   LYS A 357     111.701 -22.900  18.148  1.00 27.51           N  
ANISOU 2735  N   LYS A 357     3424   3431   3596     49    -81   -122       N  
ATOM   2736  CA  LYS A 357     110.642 -23.812  17.681  1.00 34.98           C  
ANISOU 2736  CA  LYS A 357     4341   4332   4617     68   -128   -173       C  
ATOM   2737  C   LYS A 357     111.095 -25.276  17.740  1.00 43.64           C  
ANISOU 2737  C   LYS A 357     5369   5424   5788     79   -204   -193       C  
ATOM   2738  O   LYS A 357     110.350 -26.133  18.203  1.00 30.69           O  
ANISOU 2738  O   LYS A 357     3704   3744   4213     81   -244   -200       O  
ATOM   2739  CB  LYS A 357     110.193 -23.483  16.255  1.00 26.07           C  
ANISOU 2739  CB  LYS A 357     3156   3240   3510     74   -161   -192       C  
ATOM   2740  CG  LYS A 357     109.480 -22.174  16.121  1.00 29.03           C  
ANISOU 2740  CG  LYS A 357     3589   3611   3831     65   -104   -176       C  
ATOM   2741  CD  LYS A 357     108.618 -22.131  14.860  1.00 23.21           C  
ANISOU 2741  CD  LYS A 357     2827   2858   3132     81   -129   -223       C  
ATOM   2742  CE  LYS A 357     109.473 -22.171  13.612  1.00 26.69           C  
ANISOU 2742  CE  LYS A 357     3255   3304   3581     99   -145   -260       C  
ATOM   2743  NZ  LYS A 357     108.633 -22.008  12.394  1.00 36.77           N  
ANISOU 2743  NZ  LYS A 357     4510   4573   4888    115   -166   -304       N  
ATOM   2744  N   ILE A 358     112.329 -25.539  17.316  1.00 44.31           N  
ANISOU 2744  N   ILE A 358     5452   5514   5869     88   -215   -208       N  
ATOM   2745  CA  ILE A 358     112.881 -26.885  17.276  1.00 35.37           C  
ANISOU 2745  CA  ILE A 358     4291   4343   4805    105   -277   -241       C  
ATOM   2746  C   ILE A 358     113.109 -27.408  18.679  1.00 36.71           C  
ANISOU 2746  C   ILE A 358     4457   4412   5080    127   -342   -288       C  
ATOM   2747  O   ILE A 358     112.712 -28.524  18.980  1.00 31.84           O  
ANISOU 2747  O   ILE A 358     3828   3833   4439     98   -335   -222       O  
ATOM   2748  CB  ILE A 358     114.173 -26.950  16.466  1.00 30.84           C  
ANISOU 2748  CB  ILE A 358     3774   3719   4224    130   -255   -289       C  
ATOM   2749  CG1 ILE A 358     113.905 -26.559  15.019  1.00 27.04           C  
ANISOU 2749  CG1 ILE A 358     3192   3234   3848    183   -365   -409       C  
ATOM   2750  CG2 ILE A 358     114.773 -28.344  16.550  1.00 39.13           C  
ANISOU 2750  CG2 ILE A 358     4738   4790   5338    136   -352   -295       C  
ATOM   2751  CD1 ILE A 358     115.149 -26.638  14.146  1.00 21.71           C  
ANISOU 2751  CD1 ILE A 358     2599   2581   3069    164   -274   -356       C  
ATOM   2752  N   ARG A 359     113.689 -26.597  19.563  1.00 24.49           N  
ANISOU 2752  N   ARG A 359     3009   2941   3353     83   -193   -185       N  
ATOM   2753  CA  ARG A 359     113.874 -27.098  20.921  1.00 21.81           C  
ANISOU 2753  CA  ARG A 359     2678   2591   3016     72   -195   -158       C  
ATOM   2754  C   ARG A 359     112.539 -27.313  21.627  1.00 37.58           C  
ANISOU 2754  C   ARG A 359     4624   4613   5042     57   -228   -129       C  
ATOM   2755  O   ARG A 359     112.411 -28.217  22.448  1.00 32.87           O  
ANISOU 2755  O   ARG A 359     4011   3980   4496     53   -268   -119       O  
ATOM   2756  CB  ARG A 359     114.811 -26.209  21.745  1.00 28.90           C  
ANISOU 2756  CB  ARG A 359     3576   3581   3823     50   -149   -106       C  
ATOM   2757  CG  ARG A 359     115.279 -26.875  23.035  1.00 25.74           C  
ANISOU 2757  CG  ARG A 359     3176   3119   3483     61   -196   -125       C  
ATOM   2758  CD  ARG A 359     116.460 -26.171  23.645  1.00 23.95           C  
ANISOU 2758  CD  ARG A 359     2986   2979   3135     32   -102    -64       C  
ATOM   2759  NE  ARG A 359     117.012 -26.931  24.759  1.00 32.49           N  
ANISOU 2759  NE  ARG A 359     4087   4022   4234     35   -109    -65       N  
ATOM   2760  CZ  ARG A 359     118.171 -26.674  25.350  1.00 35.73           C  
ANISOU 2760  CZ  ARG A 359     4495   4477   4605     25    -89    -45       C  
ATOM   2761  NH1 ARG A 359     118.944 -25.684  24.924  1.00 38.17           N  
ANISOU 2761  NH1 ARG A 359     4818   4814   4869     15    -42    -27       N  
ATOM   2762  NH2 ARG A 359     118.571 -27.431  26.358  1.00 23.70           N  
ANISOU 2762  NH2 ARG A 359     2986   2914   3105     28   -104    -49       N  
ATOM   2763  N   TRP A 360     111.539 -26.492  21.318  1.00 42.04           N  
ANISOU 2763  N   TRP A 360     5236   5149   5588     56   -180   -134       N  
ATOM   2764  CA  TRP A 360     110.218 -26.729  21.895  1.00 32.61           C  
ANISOU 2764  CA  TRP A 360     3983   3973   4434     44   -217   -109       C  
ATOM   2765  C   TRP A 360     109.621 -28.043  21.393  1.00 38.20           C  
ANISOU 2765  C   TRP A 360     4698   4539   5277     57   -276   -143       C  
ATOM   2766  O   TRP A 360     108.862 -28.697  22.106  1.00 20.57           O  
ANISOU 2766  O   TRP A 360     2373   2338   3105     41   -339   -106       O  
ATOM   2767  CB  TRP A 360     109.264 -25.580  21.595  1.00 26.13           C  
ANISOU 2767  CB  TRP A 360     3218   3139   3570     42   -157   -109       C  
ATOM   2768  CG  TRP A 360     107.870 -25.808  22.143  1.00 26.10           C  
ANISOU 2768  CG  TRP A 360     3198   3097   3624     33   -178    -92       C  
ATOM   2769  CD1 TRP A 360     107.405 -25.455  23.386  1.00 20.44           C  
ANISOU 2769  CD1 TRP A 360     2492   2398   2877     19   -155    -53       C  
ATOM   2770  CD2 TRP A 360     106.754 -26.383  21.448  1.00 16.16           C  
ANISOU 2770  CD2 TRP A 360     1901   1771   2467     38   -227   -109       C  
ATOM   2771  NE1 TRP A 360     106.084 -25.805  23.512  1.00 29.56           N  
ANISOU 2771  NE1 TRP A 360     3616   3499   4116     12   -187    -35       N  
ATOM   2772  CE2 TRP A 360     105.661 -26.373  22.336  1.00 31.09           C  
ANISOU 2772  CE2 TRP A 360     3780   3639   4395     22   -230    -67       C  
ATOM   2773  CE3 TRP A 360     106.583 -26.931  20.173  1.00 35.04           C  
ANISOU 2773  CE3 TRP A 360     4266   4118   4931     54   -270   -154       C  
ATOM   2774  CZ2 TRP A 360     104.418 -26.888  21.988  1.00 20.52           C  
ANISOU 2774  CZ2 TRP A 360     2322   2316   3158     17   -298    -54       C  
ATOM   2775  CZ3 TRP A 360     105.336 -27.425  19.826  1.00 24.51           C  
ANISOU 2775  CZ3 TRP A 360     2776   2660   3876     67   -427   -195       C  
ATOM   2776  CH2 TRP A 360     104.278 -27.402  20.728  1.00 25.83           C  
ANISOU 2776  CH2 TRP A 360     2961   2957   3899     32   -342    -97       C  
ATOM   2777  N   GLY A 361     109.887 -28.374  20.136  1.00 31.23           N  
ANISOU 2777  N   GLY A 361     3706   3591   4569     96   -418   -238       N  
ATOM   2778  CA  GLY A 361     109.526 -29.677  19.628  1.00 41.16           C  
ANISOU 2778  CA  GLY A 361     4932   4908   5801     81   -421   -199       C  
ATOM   2779  C   GLY A 361     108.560 -29.669  18.463  1.00 51.05           C  
ANISOU 2779  C   GLY A 361     6150   6139   7109     92   -448   -233       C  
ATOM   2780  O   GLY A 361     107.781 -30.605  18.327  1.00 51.81           O  
ANISOU 2780  O   GLY A 361     6308   6048   7328    100   -466   -258       O  
ATOM   2781  N   VAL A 362     108.617 -28.657  17.607  1.00 42.04           N  
ANISOU 2781  N   VAL A 362     5030   5044   5900    100   -404   -254       N  
ATOM   2782  CA  VAL A 362     107.662 -28.557  16.503  1.00 33.99           C  
ANISOU 2782  CA  VAL A 362     4076   3903   4935    120   -387   -313       C  
ATOM   2783  C   VAL A 362     107.772 -29.723  15.527  1.00 38.41           C  
ANISOU 2783  C   VAL A 362     4488   4518   5586    132   -507   -337       C  
ATOM   2784  O   VAL A 362     106.802 -30.055  14.854  1.00 35.32           O  
ANISOU 2784  O   VAL A 362     4010   3885   5523    189   -682   -492       O  
ATOM   2785  CB  VAL A 362     107.754 -27.232  15.743  1.00 40.22           C  
ANISOU 2785  CB  VAL A 362     4799   4859   5625    113   -369   -297       C  
ATOM   2786  CG1 VAL A 362     107.395 -26.047  16.666  1.00 30.68           C  
ANISOU 2786  CG1 VAL A 362     3607   3585   4466    124   -367   -337       C  
ATOM   2787  CG2 VAL A 362     109.134 -27.083  15.109  1.00 24.79           C  
ANISOU 2787  CG2 VAL A 362     2830   2820   3771    172   -444   -432       C  
ATOM   2788  N   PHE A 363     108.961 -30.307  15.432  1.00 23.40           N  
ANISOU 2788  N   PHE A 363     2590   2616   3683    143   -530   -354       N  
ATOM   2789  CA  PHE A 363     109.194 -31.464  14.557  1.00 37.77           C  
ANISOU 2789  CA  PHE A 363     4367   4390   5596    166   -609   -402       C  
ATOM   2790  C   PHE A 363     108.807 -32.798  15.191  1.00 35.11           C  
ANISOU 2790  C   PHE A 363     3944   3732   5666    216   -847   -528       C  
ATOM   2791  O   PHE A 363     108.404 -33.716  14.489  1.00 46.87           O  
ANISOU 2791  O   PHE A 363     5428   5414   6964    172   -752   -421       O  
ATOM   2792  CB  PHE A 363     110.664 -31.501  14.113  1.00 33.10           C  
ANISOU 2792  CB  PHE A 363     3920   3690   4967    199   -546   -467       C  
ATOM   2793  CG  PHE A 363     111.004 -30.501  13.040  1.00 50.13           C  
ANISOU 2793  CG  PHE A 363     6086   5912   7049    213   -507   -495       C  
ATOM   2794  CD1 PHE A 363     110.530 -30.654  11.750  1.00 35.49           C  
ANISOU 2794  CD1 PHE A 363     4078   4175   5232    216   -603   -505       C  
ATOM   2795  CD2 PHE A 363     111.654 -29.313  13.368  1.00 46.96           C  
ANISOU 2795  CD2 PHE A 363     5613   5702   6529    182   -487   -420       C  
ATOM   2796  CE1 PHE A 363     110.821 -29.709  10.770  1.00 31.44           C  
ANISOU 2796  CE1 PHE A 363     3701   3584   4660    246   -506   -572       C  
ATOM   2797  CE2 PHE A 363     111.919 -28.351  12.400  1.00 30.00           C  
ANISOU 2797  CE2 PHE A 363     3574   3498   4327    206   -403   -474       C  
ATOM   2798  CZ  PHE A 363     111.505 -28.554  11.101  1.00 34.43           C  
ANISOU 2798  CZ  PHE A 363     3964   4014   5104    287   -608   -663       C  
ATOM   2799  N   THR A 364     108.848 -32.874  16.518  1.00 21.72           N  
ANISOU 2799  N   THR A 364     2266   2031   3954    185   -825   -453       N  
ATOM   2800  CA  THR A 364     108.611 -34.130  17.217  1.00 39.99           C  
ANISOU 2800  CA  THR A 364     4584   4524   6085    124   -730   -306       C  
ATOM   2801  C   THR A 364     107.176 -34.313  17.698  1.00 52.31           C  
ANISOU 2801  C   THR A 364     6107   6042   7727    104   -748   -265       C  
ATOM   2802  O   THR A 364     106.716 -35.437  17.845  1.00 57.08           O  
ANISOU 2802  O   THR A 364     6658   6578   8451     97   -818   -251       O  
ATOM   2803  CB  THR A 364     109.565 -34.301  18.412  1.00 46.06           C  
ANISOU 2803  CB  THR A 364     5344   5037   7120    151   -889   -365       C  
ATOM   2804  OG1 THR A 364     109.363 -33.245  19.363  1.00 26.24           O  
ANISOU 2804  OG1 THR A 364     3049   2694   4227    100   -582   -242       O  
ATOM   2805  CG2 THR A 364     111.008 -34.336  17.930  1.00 46.78           C  
ANISOU 2805  CG2 THR A 364     5643   5265   6866    144   -646   -333       C  
ATOM   2806  N   LYS A 365     106.466 -33.216  17.945  1.00 38.87           N  
ANISOU 2806  N   LYS A 365     4579   4205   5983    101   -626   -264       N  
ATOM   2807  CA  LYS A 365     105.062 -33.318  18.351  1.00 42.83           C  
ANISOU 2807  CA  LYS A 365     4889   4839   6545     73   -699   -200       C  
ATOM   2808  C   LYS A 365     104.124 -33.505  17.160  1.00 37.30           C  
ANISOU 2808  C   LYS A 365     4143   4103   5928     86   -739   -240       C  
ATOM   2809  O   LYS A 365     104.498 -33.314  16.003  1.00 27.21           O  
ANISOU 2809  O   LYS A 365     2872   2844   4624    111   -743   -302       O  
ATOM   2810  CB  LYS A 365     104.629 -32.079  19.150  1.00 34.36           C  
ANISOU 2810  CB  LYS A 365     3858   3818   5379     56   -618   -158       C  
ATOM   2811  CG  LYS A 365     105.364 -31.905  20.465  1.00 44.46           C  
ANISOU 2811  CG  LYS A 365     5176   5129   6587     40   -581   -113       C  
ATOM   2812  CD  LYS A 365     104.659 -30.922  21.391  1.00 49.76           C  
ANISOU 2812  CD  LYS A 365     5870   5835   7200     22   -520    -63       C  
ATOM   2813  CE  LYS A 365     105.443 -30.748  22.683  1.00 43.47           C  
ANISOU 2813  CE  LYS A 365     5114   5074   6331      9   -486    -25       C  
ATOM   2814  NZ  LYS A 365     104.637 -30.093  23.761  1.00 51.64           N  
ANISOU 2814  NZ  LYS A 365     6153   6129   7339    -11   -445     33       N  
ATOM   2815  N   SER A 366     102.921 -33.974  17.457  1.00 32.17           N  
ANISOU 2815  N   SER A 366     3438   3397   5387     70   -773   -201       N  
ATOM   2816  CA  SER A 366     101.912 -34.149  16.432  1.00 45.91           C  
ANISOU 2816  CA  SER A 366     5051   4737   7656    109  -1015   -318       C  
ATOM   2817  C   SER A 366     101.226 -32.825  16.133  1.00 51.11           C  
ANISOU 2817  C   SER A 366     5816   5803   7799     80   -748   -238       C  
ATOM   2818  O   SER A 366     101.595 -31.775  16.669  1.00 34.61           O  
ANISOU 2818  O   SER A 366     3956   3590   5604     80   -616   -240       O  
ATOM   2819  CB  SER A 366     100.869 -35.167  16.895  1.00 49.41           C  
ANISOU 2819  CB  SER A 366     5716   5219   7838     66   -800   -198       C  
ATOM   2820  OG  SER A 366     100.209 -34.730  18.078  1.00 52.09           O  
ANISOU 2820  OG  SER A 366     5836   5810   8147     33   -832   -101       O  
ATOM   2821  N   LYS A 367     100.204 -32.880  15.291  1.00 48.57           N  
ANISOU 2821  N   LYS A 367     5451   5447   7556     86   -778   -261       N  
ATOM   2822  CA  LYS A 367      99.407 -31.701  15.020  1.00 28.72           C  
ANISOU 2822  CA  LYS A 367     2956   2968   4989     84   -725   -262       C  
ATOM   2823  C   LYS A 367      98.753 -31.235  16.332  1.00 46.20           C  
ANISOU 2823  C   LYS A 367     5175   5187   7192     55   -680   -179       C  
ATOM   2824  O   LYS A 367      98.530 -32.044  17.242  1.00 35.51           O  
ANISOU 2824  O   LYS A 367     3783   3789   5919     36   -710   -120       O  
ATOM   2825  CB  LYS A 367      98.363 -32.020  13.944  1.00 41.81           C  
ANISOU 2825  CB  LYS A 367     4556   4576   6754     95   -777   -298       C  
ATOM   2826  CG  LYS A 367      97.282 -33.026  14.366  1.00 63.51           C  
ANISOU 2826  CG  LYS A 367     7225   7239   9666     77   -838   -247       C  
ATOM   2827  CD  LYS A 367      96.353 -33.310  13.205  1.00 63.30           C  
ANISOU 2827  CD  LYS A 367     7145   7166   9742     91   -891   -292       C  
ATOM   2828  CE  LYS A 367      95.290 -34.332  13.562  1.00 41.10           C  
ANISOU 2828  CE  LYS A 367     4474   4005   7137    160   -881   -236       C  
ATOM   2829  NZ  LYS A 367      94.464 -34.683  12.379  1.00 49.09           N  
ANISOU 2829  NZ  LYS A 367     5413   4933   8307    176   -963   -300       N  
ATOM   2830  N   PRO A 368      98.440 -29.929  16.428  1.00 37.56           N  
ANISOU 2830  N   PRO A 368     4125   4147   6001     51   -610   -172       N  
ATOM   2831  CA  PRO A 368      97.959 -29.326  17.676  1.00 45.77           C  
ANISOU 2831  CA  PRO A 368     5179   5205   7007     27   -560    -97       C  
ATOM   2832  C   PRO A 368      96.884 -30.141  18.391  1.00 32.25           C  
ANISOU 2832  C   PRO A 368     3575   3229   5450      7   -550    -25       C  
ATOM   2833  O   PRO A 368      97.014 -30.366  19.593  1.00 23.52           O  
ANISOU 2833  O   PRO A 368     2282   2323   4330    -11   -587     41       O  
ATOM   2834  CB  PRO A 368      97.416 -27.970  17.210  1.00 51.43           C  
ANISOU 2834  CB  PRO A 368     6085   5802   7654     34   -461   -126       C  
ATOM   2835  CG  PRO A 368      98.328 -27.599  16.075  1.00 32.42           C  
ANISOU 2835  CG  PRO A 368     3492   3348   5477     76   -618   -266       C  
ATOM   2836  CD  PRO A 368      98.616 -28.919  15.367  1.00 40.17           C  
ANISOU 2836  CD  PRO A 368     4495   4530   6238     70   -574   -233       C  
ATOM   2837  N   SER A 369      95.819 -30.507  17.688  1.00 26.19           N  
ANISOU 2837  N   SER A 369     2562   2604   4784      8   -642    -28       N  
ATOM   2838  CA  SER A 369      94.685 -31.179  18.326  1.00 51.39           C  
ANISOU 2838  CA  SER A 369     5674   5734   8116    -13   -673     52       C  
ATOM   2839  C   SER A 369      95.020 -32.557  18.927  1.00 35.44           C  
ANISOU 2839  C   SER A 369     3605   3664   6194    -23   -732     89       C  
ATOM   2840  O   SER A 369      94.322 -33.037  19.812  1.00 28.69           O  
ANISOU 2840  O   SER A 369     2889   2532   5479     26   -707    209       O  
ATOM   2841  CB  SER A 369      93.530 -31.328  17.336  1.00 49.29           C  
ANISOU 2841  CB  SER A 369     5527   5170   8029     51   -684     51       C  
ATOM   2842  OG  SER A 369      93.895 -32.222  16.309  1.00 38.76           O  
ANISOU 2842  OG  SER A 369     4181   3788   6759     76   -746    -24       O  
ATOM   2843  N   ALA A 370      96.097 -33.171  18.446  1.00 37.44           N  
ANISOU 2843  N   ALA A 370     3880   3915   6430     -8   -769     29       N  
ATOM   2844  CA  ALA A 370      96.483 -34.521  18.860  1.00 45.61           C  
ANISOU 2844  CA  ALA A 370     5114   4635   7580    -16   -763     58       C  
ATOM   2845  C   ALA A 370      97.539 -34.506  19.955  1.00 49.47           C  
ANISOU 2845  C   ALA A 370     5406   5429   7961    -24   -802     84       C  
ATOM   2846  O   ALA A 370      97.884 -35.553  20.478  1.00 44.15           O  
ANISOU 2846  O   ALA A 370     4699   4719   7357    -33   -848    114       O  
ATOM   2847  CB  ALA A 370      96.951 -35.337  17.672  1.00 23.09           C  
ANISOU 2847  CB  ALA A 370     2002   2009   4762      8   -902    -28       C  
ATOM   2848  N   ARG A 371      98.063 -33.328  20.295  1.00 52.83           N  
ANISOU 2848  N   ARG A 371     6119   5703   8253    -24   -665     82       N  
ATOM   2849  CA  ARG A 371      99.102 -33.248  21.316  1.00 39.85           C  
ANISOU 2849  CA  ARG A 371     4310   4329   6501    -29   -696     99       C  
ATOM   2850  C   ARG A 371      98.564 -33.552  22.710  1.00 26.00           C  
ANISOU 2850  C   ARG A 371     2515   2564   4798    -55   -690    199       C  
ATOM   2851  O   ARG A 371      97.395 -33.307  22.995  1.00 29.34           O  
ANISOU 2851  O   ARG A 371     2895   2975   5279    -67   -675    253       O  
ATOM   2852  CB  ARG A 371      99.761 -31.864  21.307  1.00 58.19           C  
ANISOU 2852  CB  ARG A 371     6897   6544   8667    -20   -564     70       C  
ATOM   2853  CG  ARG A 371     100.435 -31.509  19.991  1.00 57.80           C  
ANISOU 2853  CG  ARG A 371     6712   6709   8540      8   -613    -26       C  
ATOM   2854  CD  ARG A 371     100.944 -30.072  19.957  1.00 50.40           C  
ANISOU 2854  CD  ARG A 371     6000   5695   7456     17   -487    -56       C  
ATOM   2855  NE  ARG A 371     101.480 -29.727  18.638  1.00 29.32           N  
ANISOU 2855  NE  ARG A 371     3350   3055   4736     44   -483   -140       N  
ATOM   2856  CZ  ARG A 371     101.639 -28.490  18.178  1.00 39.74           C  
ANISOU 2856  CZ  ARG A 371     4705   4453   5940     53   -427   -171       C  
ATOM   2857  NH1 ARG A 371     101.372 -27.436  18.949  1.00 29.73           N  
ANISOU 2857  NH1 ARG A 371     3352   3366   4578     36   -403   -121       N  
ATOM   2858  NH2 ARG A 371     102.122 -28.296  16.961  1.00 30.65           N  
ANISOU 2858  NH2 ARG A 371     3562   3325   4757     77   -430   -238       N  
ATOM   2859  N   PRO A 372      99.417 -34.139  23.574  1.00 34.45           N  
ANISOU 2859  N   PRO A 372     3594   3640   5856    -64   -703    226       N  
ATOM   2860  CA  PRO A 372      98.992 -34.469  24.946  1.00 42.64           C  
ANISOU 2860  CA  PRO A 372     4804   4446   6951    -96   -637    352       C  
ATOM   2861  C   PRO A 372      98.456 -33.274  25.726  1.00 45.55           C  
ANISOU 2861  C   PRO A 372     4981   5101   7225    -95   -620    368       C  
ATOM   2862  O   PRO A 372      97.443 -33.397  26.418  1.00 46.75           O  
ANISOU 2862  O   PRO A 372     4953   4886   7923   -148   -765    611       O  
ATOM   2863  CB  PRO A 372     100.293 -34.942  25.612  1.00 28.30           C  
ANISOU 2863  CB  PRO A 372     2707   2515   5531   -125   -885    436       C  
ATOM   2864  CG  PRO A 372     101.196 -35.322  24.488  1.00 42.35           C  
ANISOU 2864  CG  PRO A 372     4523   4272   7295    -96   -932    316       C  
ATOM   2865  CD  PRO A 372     100.826 -34.493  23.313  1.00 34.46           C  
ANISOU 2865  CD  PRO A 372     3642   3653   5797    -51   -721    169       C  
ATOM   2866  N   GLU A 373      99.082 -32.115  25.556  1.00 43.67           N  
ANISOU 2866  N   GLU A 373     4827   4928   6838    -82   -562    316       N  
ATOM   2867  CA  GLU A 373      98.702 -30.913  26.304  1.00 49.83           C  
ANISOU 2867  CA  GLU A 373     5638   5768   7527    -85   -490    350       C  
ATOM   2868  C   GLU A 373      97.428 -30.291  25.744  1.00 37.92           C  
ANISOU 2868  C   GLU A 373     4279   4070   6060    -89   -429    392       C  
ATOM   2869  O   GLU A 373      96.864 -29.365  26.333  1.00 42.31           O  
ANISOU 2869  O   GLU A 373     4839   4674   6563    -91   -379    433       O  
ATOM   2870  CB  GLU A 373      99.837 -29.891  26.311  1.00 43.60           C  
ANISOU 2870  CB  GLU A 373     5096   4896   6574    -80   -398    317       C  
ATOM   2871  CG  GLU A 373     100.128 -29.353  24.929  1.00 48.33           C  
ANISOU 2871  CG  GLU A 373     5592   5656   7115    -54   -428    205       C  
ATOM   2872  CD  GLU A 373     101.341 -30.006  24.303  1.00 46.46           C  
ANISOU 2872  CD  GLU A 373     5515   5263   6875    -45   -423    159       C  
ATOM   2873  OE1 GLU A 373     101.551 -31.232  24.500  1.00 57.55           O  
ANISOU 2873  OE1 GLU A 373     6738   6764   8364    -48   -522    165       O  
ATOM   2874  OE2 GLU A 373     102.058 -29.314  23.559  1.00 35.88           O  
ANISOU 2874  OE2 GLU A 373     4097   4107   5428    -24   -430     81       O  
ATOM   2875  N   SER A 374      96.932 -30.875  24.655  1.00 41.07           N  
ANISOU 2875  N   SER A 374     4647   4395   6561    -84   -474    360       N  
ATOM   2876  CA  SER A 374      95.690 -30.441  24.031  1.00 40.45           C  
ANISOU 2876  CA  SER A 374     4345   4490   6533    -75   -512    337       C  
ATOM   2877  C   SER A 374      94.498 -31.298  24.457  1.00 59.19           C  
ANISOU 2877  C   SER A 374     6614   6804   9070    -90   -547    423       C  
ATOM   2878  O   SER A 374      93.383 -31.070  23.988  1.00 49.23           O  
ANISOU 2878  O   SER A 374     5485   5299   7918    -29   -531    500       O  
ATOM   2879  CB  SER A 374      95.801 -30.506  22.512  1.00 42.55           C  
ANISOU 2879  CB  SER A 374     4624   4731   6813    -59   -545    249       C  
ATOM   2880  OG  SER A 374      96.878 -29.736  22.041  1.00 30.65           O  
ANISOU 2880  OG  SER A 374     3203   3279   5162    -43   -511    174       O  
ATOM   2881  N   GLN A 375      94.717 -32.269  25.349  1.00 44.69           N  
ANISOU 2881  N   GLN A 375     4936   4749   7296    -27   -548    535       N  
ATOM   2882  CA  GLN A 375      93.640 -33.191  25.699  1.00 52.68           C  
ANISOU 2882  CA  GLN A 375     5816   5661   8540    -45   -607    642       C  
ATOM   2883  C   GLN A 375      92.920 -32.800  26.979  1.00 58.05           C  
ANISOU 2883  C   GLN A 375     6439   6369   9248    -57   -566    762       C  
ATOM   2884  O   GLN A 375      92.188 -33.612  27.547  1.00 59.22           O  
ANISOU 2884  O   GLN A 375     6475   6450   9578    -71   -603    870       O  
ATOM   2885  CB  GLN A 375      94.158 -34.626  25.838  1.00 44.19           C  
ANISOU 2885  CB  GLN A 375     4704   4522   7564    -47   -678    654       C  
ATOM   2886  CG  GLN A 375      95.011 -35.081  24.669  1.00 50.39           C  
ANISOU 2886  CG  GLN A 375     5546   5287   8311    -27   -714    537       C  
ATOM   2887  CD  GLN A 375      94.246 -34.950  23.356  1.00 49.23           C  
ANISOU 2887  CD  GLN A 375     5365   5078   8261    -23   -747    486       C  
ATOM   2888  OE1 GLN A 375      93.062 -35.287  23.270  1.00 52.68           O  
ANISOU 2888  OE1 GLN A 375     5696   5429   8890    -39   -790    551       O  
ATOM   2889  NE2 GLN A 375      94.952 -34.550  22.305  1.00 47.46           N  
ANISOU 2889  NE2 GLN A 375     5223   4893   7917      0   -730    371       N  
ATOM   2890  N   HIS A 376      93.170 -31.585  27.463  1.00 23.89           N  
ANISOU 2890  N   HIS A 376     2185   2145   4747    -48   -490    746       N  
ATOM   2891  CA  HIS A 376      92.604 -31.155  28.733  1.00 30.74           C  
ANISOU 2891  CA  HIS A 376     3005   3053   5624    -51   -445    853       C  
ATOM   2892  C   HIS A 376      91.903 -29.807  28.573  1.00 58.18           C  
ANISOU 2892  C   HIS A 376     6498   6574   9035    -44   -384    853       C  
ATOM   2893  O   HIS A 376      92.420 -28.773  28.999  1.00 55.22           O  
ANISOU 2893  O   HIS A 376     6207   6295   8480    -31   -327    811       O  
ATOM   2894  CB  HIS A 376      93.683 -31.041  29.806  1.00 47.81           C  
ANISOU 2894  CB  HIS A 376     5231   5299   7635    -43   -415    841       C  
ATOM   2895  CG  HIS A 376      94.485 -32.289  29.987  1.00 69.07           C  
ANISOU 2895  CG  HIS A 376     7916   7957  10372    -48   -471    837       C  
ATOM   2896  ND1 HIS A 376      95.360 -32.752  29.029  1.00 64.58           N  
ANISOU 2896  ND1 HIS A 376     7215   7544   9779   -131   -520    671       N  
ATOM   2897  CD2 HIS A 376      94.517 -33.190  30.998  1.00 63.60           C  
ANISOU 2897  CD2 HIS A 376     7147   7241   9775    -58   -500    928       C  
ATOM   2898  CE1 HIS A 376      95.908 -33.876  29.448  1.00 72.94           C  
ANISOU 2898  CE1 HIS A 376     8242   8572  10897   -142   -569    693       C  
ATOM   2899  NE2 HIS A 376      95.418 -34.162  30.642  1.00 71.26           N  
ANISOU 2899  NE2 HIS A 376     8147   8179  10751    -59   -554    876       N  
ATOM   2900  N   PRO A 377      90.705 -29.820  27.965  1.00 49.53           N  
ANISOU 2900  N   PRO A 377     5317   5407   8096    -53   -400    901       N  
ATOM   2901  CA  PRO A 377      89.978 -28.585  27.676  1.00 50.95           C  
ANISOU 2901  CA  PRO A 377     5507   5620   8232    -47   -348    903       C  
ATOM   2902  C   PRO A 377      89.614 -27.878  28.970  1.00 66.41           C  
ANISOU 2902  C   PRO A 377     7444   7646  10143    -34   -281    993       C  
ATOM   2903  O   PRO A 377      89.405 -26.663  28.976  1.00 63.49           O  
ANISOU 2903  O   PRO A 377     7120   7339   9666    -22   -227    974       O  
ATOM   2904  CB  PRO A 377      88.725 -29.081  26.957  1.00 54.44           C  
ANISOU 2904  CB  PRO A 377     5832   5953   8900    -61   -391    963       C  
ATOM   2905  CG  PRO A 377      88.536 -30.479  27.460  1.00 57.33           C  
ANISOU 2905  CG  PRO A 377     6099   6239   9444    -73   -446   1046       C  
ATOM   2906  CD  PRO A 377      89.925 -31.017  27.607  1.00 50.87           C  
ANISOU 2906  CD  PRO A 377     5368   5455   8506    -69   -470    966       C  
ATOM   2907  N   GLN A 378      89.542 -28.638  30.058  1.00 68.60           N  
ANISOU 2907  N   GLN A 378     7649   7911  10506    -35   -286   1091       N  
ATOM   2908  CA  GLN A 378      89.136 -28.102  31.359  1.00 64.78           C  
ANISOU 2908  CA  GLN A 378     7122   7483  10009    -18   -222   1191       C  
ATOM   2909  C   GLN A 378      90.199 -27.179  31.943  1.00 44.59           C  
ANISOU 2909  C   GLN A 378     4683   5038   7223      0   -180   1108       C  
ATOM   2910  O   GLN A 378      89.934 -26.434  32.883  1.00 46.99           O  
ANISOU 2910  O   GLN A 378     4971   5399   7484     22   -120   1163       O  
ATOM   2911  CB  GLN A 378      88.807 -29.234  32.338  1.00 60.10           C  
ANISOU 2911  CB  GLN A 378     6407   6841   9585    -24   -239   1323       C  
ATOM   2912  CG  GLN A 378      90.014 -29.988  32.889  0.70 37.26           C  
ANISOU 2912  CG  GLN A 378     3555   3973   6630    -31   -274   1288       C  
ATOM   2913  CD  GLN A 378      90.518 -31.009  31.910  0.70 41.09           C  
ANISOU 2913  CD  GLN A 378     4061   4385   7165    -51   -356   1214       C  
ATOM   2914  OE1 GLN A 378      89.939 -31.189  30.839  0.70 39.43           O  
ANISOU 2914  OE1 GLN A 378     3828   4104   7049    -60   -390   1192       O  
ATOM   2915  NE2 GLN A 378      91.563 -31.732  32.291  0.70 48.48           N  
ANISOU 2915  NE2 GLN A 378     5031   5334   8056    -56   -390   1184       N  
ATOM   2916  N   TRP A 379      91.396 -27.217  31.363  1.00 42.29           N  
ANISOU 2916  N   TRP A 379     4505   4774   6790     -5   -208    977       N  
ATOM   2917  CA  TRP A 379      92.480 -26.343  31.794  1.00 39.50           C  
ANISOU 2917  CA  TRP A 379     4268   4519   6221      9   -175    884       C  
ATOM   2918  C   TRP A 379      92.046 -24.881  31.607  1.00 47.89           C  
ANISOU 2918  C   TRP A 379     5376   5634   7186     25   -122    854       C  
ATOM   2919  O   TRP A 379      92.362 -24.014  32.423  1.00 35.93           O  
ANISOU 2919  O   TRP A 379     3902   4192   5560     43    -83    839       O  
ATOM   2920  CB  TRP A 379      93.760 -26.625  31.004  1.00 41.24           C  
ANISOU 2920  CB  TRP A 379     4420   4874   6377    -78   -195    711       C  
ATOM   2921  CG  TRP A 379      94.563 -27.810  31.484  1.00 60.32           C  
ANISOU 2921  CG  TRP A 379     7011   7099   8808    -86   -218    792       C  
ATOM   2922  CD1 TRP A 379      94.333 -28.576  32.595  1.00 58.10           C  
ANISOU 2922  CD1 TRP A 379     6464   6981   8628    -99   -241    809       C  
ATOM   2923  CD2 TRP A 379      95.721 -28.367  30.848  1.00 52.75           C  
ANISOU 2923  CD2 TRP A 379     5909   6293   7842   -103   -284    652       C  
ATOM   2924  NE1 TRP A 379      95.278 -29.577  32.685  1.00 48.64           N  
ANISOU 2924  NE1 TRP A 379     5272   5762   7448   -115   -291    794       N  
ATOM   2925  CE2 TRP A 379      96.144 -29.463  31.628  1.00 48.54           C  
ANISOU 2925  CE2 TRP A 379     5333   5741   7368   -117   -317    697       C  
ATOM   2926  CE3 TRP A 379      96.440 -28.045  29.695  1.00 40.28           C  
ANISOU 2926  CE3 TRP A 379     4571   4557   6177    -91   -272    608       C  
ATOM   2927  CZ2 TRP A 379      97.261 -30.234  31.294  1.00 41.54           C  
ANISOU 2927  CZ2 TRP A 379     4478   4833   6472   -127   -365    648       C  
ATOM   2928  CZ3 TRP A 379      97.541 -28.810  29.363  1.00 51.64           C  
ANISOU 2928  CZ3 TRP A 379     6033   5977   7612   -105   -308    555       C  
ATOM   2929  CH2 TRP A 379      97.942 -29.897  30.161  1.00 48.36           C  
ANISOU 2929  CH2 TRP A 379     5587   5531   7257   -119   -341    606       C  
ATOM   2930  N   LEU A 380      91.276 -24.630  30.554  1.00 38.53           N  
ANISOU 2930  N   LEU A 380     4174   4406   6062     18   -127    850       N  
ATOM   2931  CA  LEU A 380      90.774 -23.292  30.265  1.00 32.38           C  
ANISOU 2931  CA  LEU A 380     3428   3667   5208     30    -83    828       C  
ATOM   2932  C   LEU A 380      89.688 -22.926  31.253  1.00 45.53           C  
ANISOU 2932  C   LEU A 380     4997   5336   6965     51    -35    959       C  
ATOM   2933  O   LEU A 380      88.586 -23.479  31.214  1.00 41.89           O  
ANISOU 2933  O   LEU A 380     4422   4808   6687     47    -35   1071       O  
ATOM   2934  CB  LEU A 380      90.235 -23.196  28.840  1.00 30.26           C  
ANISOU 2934  CB  LEU A 380     3153   3347   4997     15   -103    796       C  
ATOM   2935  CG  LEU A 380      89.807 -21.782  28.427  1.00 52.35           C  
ANISOU 2935  CG  LEU A 380     5992   6189   7708     25    -63    766       C  
ATOM   2936  CD1 LEU A 380      91.014 -20.886  28.303  1.00 35.99           C  
ANISOU 2936  CD1 LEU A 380     3907   4311   5457    -15    -35    597       C  
ATOM   2937  CD2 LEU A 380      89.014 -21.786  27.130  1.00 51.97           C  
ANISOU 2937  CD2 LEU A 380     5900   6078   7768     10    -83    767       C  
ATOM   2938  N   GLY A 381      90.030 -22.052  32.188  1.00 44.27           N  
ANISOU 2938  N   GLY A 381     4879   5252   6691     75      8    948       N  
ATOM   2939  CA  GLY A 381      89.100 -21.641  33.219  1.00 57.56           C  
ANISOU 2939  CA  GLY A 381     6474   6945   8452    105     68   1072       C  
ATOM   2940  C   GLY A 381      88.970 -22.667  34.342  1.00 56.85           C  
ANISOU 2940  C   GLY A 381     6280   6832   8488    110     77   1193       C  
ATOM   2941  O   GLY A 381      87.939 -22.695  35.039  1.00 44.83           O  
ANISOU 2941  O   GLY A 381     4648   5289   7096    133    130   1334       O  
ATOM   2942  N   ALA A 382      89.995 -23.514  34.498  1.00 35.68           N  
ANISOU 2942  N   ALA A 382     3630   4152   5774     90     29   1145       N  
ATOM   2943  CA  ALA A 382      90.020 -24.562  35.516  1.00 35.02           C  
ANISOU 2943  CA  ALA A 382     3452   4048   5806     88     27   1255       C  
ATOM   2944  C   ALA A 382      89.706 -24.016  36.906  1.00 53.97           C  
ANISOU 2944  C   ALA A 382     5792   6494   8220    126    106   1359       C  
ATOM   2945  O   ALA A 382      90.132 -22.908  37.259  1.00 50.75           O  
ANISOU 2945  O   ALA A 382     5456   6152   7673    149    143   1298       O  
ATOM   2946  CB  ALA A 382      91.373 -25.240  35.527  1.00 33.10           C  
ANISOU 2946  CB  ALA A 382     3278   3820   5476     66    -29   1164       C  
ATOM   2947  N   ALA A 383      88.946 -24.789  37.680  1.00 45.41           N  
ANISOU 2947  N   ALA A 383     4572   5368   7312    134    136   1521       N  
ATOM   2948  CA  ALA A 383      88.634 -24.442  39.062  1.00 55.53           C  
ANISOU 2948  CA  ALA A 383     5782   6685   8630    176    225   1646       C  
ATOM   2949  C   ALA A 383      89.911 -24.213  39.866  1.00 51.92           C  
ANISOU 2949  C   ALA A 383     5392   6300   8037    181    228   1587       C  
ATOM   2950  O   ALA A 383      90.001 -23.259  40.647  1.00 41.97           O  
ANISOU 2950  O   ALA A 383     4150   5093   6704    223    300   1601       O  
ATOM   2951  CB  ALA A 383      87.776 -25.524  39.701  1.00 56.25           C  
ANISOU 2951  CB  ALA A 383     5718   6714   8940    178    249   1830       C  
ATOM   2952  N   GLU A 384      90.913 -25.057  39.617  1.00 45.16           N  
ANISOU 2952  N   GLU A 384     4575   5438   7144    140    148   1514       N  
ATOM   2953  CA  GLU A 384      92.187 -24.957  40.317  1.00 65.92           C  
ANISOU 2953  CA  GLU A 384     7263   8129   9654    137    140   1456       C  
ATOM   2954  C   GLU A 384      92.895 -23.632  40.025  1.00 58.08           C  
ANISOU 2954  C   GLU A 384     6404   7200   8465    150    146   1303       C  
ATOM   2955  O   GLU A 384      93.455 -22.987  40.926  1.00 55.57           O  
ANISOU 2955  O   GLU A 384     6106   6937   8071    173    188   1302       O  
ATOM   2956  CB  GLU A 384      93.109 -26.102  39.874  1.00 56.56           C  
ANISOU 2956  CB  GLU A 384     6108   6918   8462     90     47   1390       C  
ATOM   2957  CG  GLU A 384      94.393 -26.205  40.687  1.00 88.27           C  
ANISOU 2957  CG  GLU A 384    10164  10992  12385     81     36   1355       C  
ATOM   2958  CD  GLU A 384      95.229 -27.415  40.313  0.70101.32           C  
ANISOU 2958  CD  GLU A 384    11836  12612  14048     39    -50   1307       C  
ATOM   2959  OE1 GLU A 384      96.025 -27.888  41.156  0.70 91.82           O  
ANISOU 2959  OE1 GLU A 384    10614  11435  12839     26    -61   1340       O  
ATOM   2960  OE2 GLU A 384      95.109 -27.872  39.152  0.70106.68           O  
ANISOU 2960  OE2 GLU A 384    12552  13238  14742     24   -103   1237       O  
ATOM   2961  N   HIS A 385      92.766 -23.178  38.782  1.00 42.30           N  
ANISOU 2961  N   HIS A 385     4485   5186   6400    138    111   1189       N  
ATOM   2962  CA  HIS A 385      93.381 -21.928  38.372  1.00 44.19           C  
ANISOU 2962  CA  HIS A 385     4849   5475   6467    144    110   1044       C  
ATOM   2963  C   HIS A 385      92.652 -20.744  38.944  1.00 47.48           C  
ANISOU 2963  C   HIS A 385     5241   5916   6883    189    188   1100       C  
ATOM   2964  O   HIS A 385      93.272 -19.748  39.281  1.00 41.31           O  
ANISOU 2964  O   HIS A 385     4529   5180   5988    204    204   1026       O  
ATOM   2965  CB  HIS A 385      93.456 -21.822  36.840  1.00 40.00           C  
ANISOU 2965  CB  HIS A 385     4408   4919   5870    120     57    919       C  
ATOM   2966  CG  HIS A 385      94.269 -22.897  36.187  1.00 37.15           C  
ANISOU 2966  CG  HIS A 385     4146   4491   5479     19     32    879       C  
ATOM   2967  ND1 HIS A 385      94.267 -23.106  34.824  1.00 25.39           N  
ANISOU 2967  ND1 HIS A 385     2512   3091   4044     -2     -3    756       N  
ATOM   2968  CD2 HIS A 385      95.156 -23.783  36.701  1.00 35.37           C  
ANISOU 2968  CD2 HIS A 385     3749   4390   5299      3      4    808       C  
ATOM   2969  CE1 HIS A 385      95.085 -24.102  34.533  1.00 40.53           C  
ANISOU 2969  CE1 HIS A 385     4598   4859   5942    -25    -47    798       C  
ATOM   2970  NE2 HIS A 385      95.638 -24.531  35.654  1.00 34.94           N  
ANISOU 2970  NE2 HIS A 385     3715   4298   5264    -27    -49    764       N  
ATOM   2971  N   ARG A 386      91.344 -20.883  39.117  1.00 48.39           N  
ANISOU 2971  N   ARG A 386     5254   5995   7139    214    242   1239       N  
ATOM   2972  CA  ARG A 386      90.559 -19.819  39.718  1.00 48.22           C  
ANISOU 2972  CA  ARG A 386     5203   5988   7129    267    332   1311       C  
ATOM   2973  C   ARG A 386      90.849 -19.733  41.205  1.00 52.01           C  
ANISOU 2973  C   ARG A 386     5638   6501   7623    310    408   1406       C  
ATOM   2974  O   ARG A 386      90.800 -18.657  41.794  1.00 43.53           O  
ANISOU 2974  O   ARG A 386     4591   5455   6494    359    477   1411       O  
ATOM   2975  CB  ARG A 386      89.066 -19.998  39.441  1.00 42.51           C  
ANISOU 2975  CB  ARG A 386     4384   5213   6556    284    374   1435       C  
ATOM   2976  CG  ARG A 386      88.736 -20.003  37.964  1.00 45.96           C  
ANISOU 2976  CG  ARG A 386     4863   5616   6984    247    310   1352       C  
ATOM   2977  CD  ARG A 386      87.255 -19.902  37.711  1.00 54.56           C  
ANISOU 2977  CD  ARG A 386     5861   6658   8210    267    359   1468       C  
ATOM   2978  NE  ARG A 386      86.980 -19.874  36.278  1.00 65.45           N  
ANISOU 2978  NE  ARG A 386     7281   8006   9583    232    300   1392       N  
ATOM   2979  CZ  ARG A 386      86.958 -18.760  35.551  1.00 69.03           C  
ANISOU 2979  CZ  ARG A 386     7817   8485   9929    235    298   1301       C  
ATOM   2980  NH1 ARG A 386      87.211 -17.587  36.123  1.00 62.56           N  
ANISOU 2980  NH1 ARG A 386     7050   7717   9001    270    343   1267       N  
ATOM   2981  NH2 ARG A 386      86.715 -18.820  34.247  1.00 62.71           N  
ANISOU 2981  NH2 ARG A 386     7041   7652   9133    202    251   1245       N  
ATOM   2982  N   THR A 387      91.143 -20.873  41.814  1.00 45.94           N  
ANISOU 2982  N   THR A 387     4799   5723   6933    296    398   1487       N  
ATOM   2983  CA  THR A 387      91.573 -20.898  43.201  1.00 53.71           C  
ANISOU 2983  CA  THR A 387     5744   6742   7923    334    467   1579       C  
ATOM   2984  C   THR A 387      92.910 -20.184  43.388  1.00 37.72           C  
ANISOU 2984  C   THR A 387     3828   4772   5731    329    440   1443       C  
ATOM   2985  O   THR A 387      93.086 -19.360  44.303  1.00 42.15           O  
ANISOU 2985  O   THR A 387     4412   5365   6237    373    521   1463       O  
ATOM   2986  CB  THR A 387      91.683 -22.363  43.718  1.00 64.46           C  
ANISOU 2986  CB  THR A 387     7006   8081   9406    308    446   1693       C  
ATOM   2987  OG1 THR A 387      90.394 -22.986  43.685  1.00 47.99           O  
ANISOU 2987  OG1 THR A 387     4804   5935   7495    318    480   1836       O  
ATOM   2988  CG2 THR A 387      92.257 -22.405  45.134  1.00 44.98           C  
ANISOU 2988  CG2 THR A 387     4560   5659   6870    289    523   1722       C  
ATOM   2989  N   LEU A 388      93.817 -20.438  42.448  1.00 32.62           N  
ANISOU 2989  N   LEU A 388     3268   4132   4996    267    332   1288       N  
ATOM   2990  CA  LEU A 388      95.099 -19.742  42.423  1.00 41.07           C  
ANISOU 2990  CA  LEU A 388     4448   5245   5912    252    294   1140       C  
ATOM   2991  C   LEU A 388      94.901 -18.234  42.257  1.00 45.05           C  
ANISOU 2991  C   LEU A 388     5019   5761   6335    286    331   1072       C  
ATOM   2992  O   LEU A 388      95.463 -17.422  43.005  1.00 42.92           O  
ANISOU 2992  O   LEU A 388     4783   5520   6003    317    371   1056       O  
ATOM   2993  CB  LEU A 388      95.968 -20.279  41.288  1.00 41.34           C  
ANISOU 2993  CB  LEU A 388     4567   5269   5869    188    184    984       C  
ATOM   2994  CG  LEU A 388      97.283 -19.556  40.993  1.00 38.59           C  
ANISOU 2994  CG  LEU A 388     4343   4953   5366    166    136    807       C  
ATOM   2995  CD1 LEU A 388      98.197 -19.652  42.209  1.00 32.86           C  
ANISOU 2995  CD1 LEU A 388     3596   4266   4622    172    157    848       C  
ATOM   2996  CD2 LEU A 388      97.970 -20.107  39.775  1.00 22.25           C  
ANISOU 2996  CD2 LEU A 388     2220   2882   3351     93    122    878       C  
ATOM   2997  N   ALA A 389      94.029 -17.874  41.325  1.00 30.60           N  
ANISOU 2997  N   ALA A 389     3202   3903   4522    283    321   1048       N  
ATOM   2998  CA  ALA A 389      93.768 -16.472  41.040  1.00 40.82           C  
ANISOU 2998  CA  ALA A 389     4558   5202   5749    307    345    985       C  
ATOM   2999  C   ALA A 389      93.153 -15.775  42.228  1.00 41.71           C  
ANISOU 2999  C   ALA A 389     4622   5319   5908    384    465   1110       C  
ATOM   3000  O   ALA A 389      93.480 -14.633  42.519  1.00 42.42           O  
ANISOU 3000  O   ALA A 389     4772   5419   5924    412    493   1058       O  
ATOM   3001  CB  ALA A 389      92.870 -16.331  39.818  1.00 19.29           C  
ANISOU 3001  CB  ALA A 389     1841   2446   3044    289    317    957       C  
ATOM   3002  N   ARG A 390      92.251 -16.468  42.906  1.00 33.00           N  
ANISOU 3002  N   ARG A 390     3410   4197   4932    422    541   1279       N  
ATOM   3003  CA  ARG A 390      91.623 -15.941  44.107  1.00 47.32           C  
ANISOU 3003  CA  ARG A 390     5188   6009   6780    490    675   1397       C  
ATOM   3004  C   ARG A 390      92.657 -15.674  45.205  1.00 47.44           C  
ANISOU 3004  C   ARG A 390     5281   6064   6681    464    712   1339       C  
ATOM   3005  O   ARG A 390      92.615 -14.634  45.890  1.00 51.78           O  
ANISOU 3005  O   ARG A 390     5897   6619   7157    484    790   1315       O  
ATOM   3006  CB  ARG A 390      90.539 -16.907  44.579  1.00 50.95           C  
ANISOU 3006  CB  ARG A 390     5544   6447   7368    481    739   1545       C  
ATOM   3007  CG  ARG A 390      89.695 -16.387  45.732  1.00 57.97           C  
ANISOU 3007  CG  ARG A 390     6433   7338   8254    500    885   1626       C  
ATOM   3008  CD  ARG A 390      88.525 -17.309  45.960  1.00 61.09           C  
ANISOU 3008  CD  ARG A 390     6714   7703   8794    492    938   1773       C  
ATOM   3009  NE  ARG A 390      87.857 -17.068  47.231  1.00 67.61           N  
ANISOU 3009  NE  ARG A 390     7538   8535   9613    501   1080   1863       N  
ATOM   3010  CZ  ARG A 390      86.765 -17.714  47.619  1.00 65.19           C  
ANISOU 3010  CZ  ARG A 390     7139   8204   9427    497   1151   2000       C  
ATOM   3011  NH1 ARG A 390      86.238 -18.646  46.836  1.00 61.96           N  
ANISOU 3011  NH1 ARG A 390     6628   7755   9158    480   1087   2059       N  
ATOM   3012  NH2 ARG A 390      86.216 -17.455  48.797  1.00 51.48           N  
ANISOU 3012  NH2 ARG A 390     5413   6476   7671    507   1284   2079       N  
ATOM   3013  N   GLU A 391      93.607 -16.597  45.336  1.00 32.54           N  
ANISOU 3013  N   GLU A 391     3389   4196   4778    418    651   1315       N  
ATOM   3014  CA  GLU A 391      94.721 -16.401  46.264  1.00 38.63           C  
ANISOU 3014  CA  GLU A 391     4241   5001   5437    384    669   1252       C  
ATOM   3015  C   GLU A 391      95.494 -15.132  45.891  1.00 50.54           C  
ANISOU 3015  C   GLU A 391     5845   6515   6843    400    632   1117       C  
ATOM   3016  O   GLU A 391      95.824 -14.295  46.750  1.00 36.14           O  
ANISOU 3016  O   GLU A 391     4100   4698   4935    398    696   1082       O  
ATOM   3017  CB  GLU A 391      95.670 -17.598  46.226  1.00 36.40           C  
ANISOU 3017  CB  GLU A 391     3935   4736   5161    333    589   1240       C  
ATOM   3018  CG  GLU A 391      96.933 -17.436  47.067  1.00 48.46           C  
ANISOU 3018  CG  GLU A 391     5550   6293   6569    291    592   1168       C  
ATOM   3019  CD  GLU A 391      97.975 -18.522  46.781  1.00 59.21           C  
ANISOU 3019  CD  GLU A 391     6891   7672   7934    245    492   1138       C  
ATOM   3020  OE1 GLU A 391      97.637 -19.547  46.145  1.00 54.61           O  
ANISOU 3020  OE1 GLU A 391     6221   7075   7455    242    433   1196       O  
ATOM   3021  OE2 GLU A 391      99.145 -18.353  47.186  1.00 46.63           O  
ANISOU 3021  OE2 GLU A 391     5370   6101   6246    210    470   1059       O  
ATOM   3022  N   ALA A 392      95.750 -14.982  44.597  1.00 37.02           N  
ANISOU 3022  N   ALA A 392     4128   4794   5142    415    528   1047       N  
ATOM   3023  CA  ALA A 392      96.475 -13.827  44.094  1.00 36.71           C  
ANISOU 3023  CA  ALA A 392     4178   4754   5017    417    479    916       C  
ATOM   3024  C   ALA A 392      95.728 -12.525  44.381  1.00 42.63           C  
ANISOU 3024  C   ALA A 392     4963   5479   5757    467    564    933       C  
ATOM   3025  O   ALA A 392      96.335 -11.517  44.754  1.00 33.02           O  
ANISOU 3025  O   ALA A 392     3826   4256   4464    464    579    858       O  
ATOM   3026  CB  ALA A 392      96.746 -13.977  42.614  1.00 30.31           C  
ANISOU 3026  CB  ALA A 392     3418   3937   4160    332    352    768       C  
ATOM   3027  N   VAL A 393      94.409 -12.564  44.220  1.00 35.64           N  
ANISOU 3027  N   VAL A 393     4019   4572   4949    503    618   1030       N  
ATOM   3028  CA  VAL A 393      93.574 -11.425  44.541  1.00 33.94           C  
ANISOU 3028  CA  VAL A 393     3832   4334   4727    546    708   1057       C  
ATOM   3029  C   VAL A 393      93.756 -11.050  46.000  1.00 40.88           C  
ANISOU 3029  C   VAL A 393     4764   5224   5543    537    813   1073       C  
ATOM   3030  O   VAL A 393      94.015  -9.888  46.312  1.00 53.02           O  
ANISOU 3030  O   VAL A 393     6381   6748   7017    552    844   1017       O  
ATOM   3031  CB  VAL A 393      92.094 -11.699  44.252  1.00 35.24           C  
ANISOU 3031  CB  VAL A 393     3915   4478   4997    580    758   1175       C  
ATOM   3032  CG1 VAL A 393      91.244 -10.559  44.787  1.00 35.59           C  
ANISOU 3032  CG1 VAL A 393     3988   4502   5030    625    867   1212       C  
ATOM   3033  CG2 VAL A 393      91.874 -11.864  42.751  1.00 24.71           C  
ANISOU 3033  CG2 VAL A 393     2581   3141   3668    526    647   1100       C  
ATOM   3034  N   ARG A 394      93.618 -12.035  46.888  1.00 49.42           N  
ANISOU 3034  N   ARG A 394     5807   6325   6644    511    868   1153       N  
ATOM   3035  CA  ARG A 394      93.745 -11.773  48.321  1.00 44.51           C  
ANISOU 3035  CA  ARG A 394     5243   5714   5955    499    972   1182       C  
ATOM   3036  C   ARG A 394      95.087 -11.141  48.663  1.00 31.87           C  
ANISOU 3036  C   ARG A 394     3745   4122   4243    469    935   1066       C  
ATOM   3037  O   ARG A 394      95.165 -10.199  49.445  1.00 48.12           O  
ANISOU 3037  O   ARG A 394     5879   6171   6235    480   1004   1050       O  
ATOM   3038  CB  ARG A 394      93.602 -13.059  49.134  1.00 44.88           C  
ANISOU 3038  CB  ARG A 394     5238   5781   6032    461   1015   1282       C  
ATOM   3039  CG  ARG A 394      92.230 -13.691  49.091  1.00 48.10           C  
ANISOU 3039  CG  ARG A 394     5543   6174   6558    483   1073   1416       C  
ATOM   3040  CD  ARG A 394      92.109 -14.744  50.164  1.00 54.81           C  
ANISOU 3040  CD  ARG A 394     6362   7038   7425    444   1138   1521       C  
ATOM   3041  NE  ARG A 394      92.992 -15.883  49.928  1.00 54.13           N  
ANISOU 3041  NE  ARG A 394     6251   6966   7350    390   1046   1501       N  
ATOM   3042  CZ  ARG A 394      92.608 -17.009  49.346  1.00 48.70           C  
ANISOU 3042  CZ  ARG A 394     5461   6265   6778    375    995   1567       C  
ATOM   3043  NH1 ARG A 394      91.367 -17.119  48.906  1.00 42.79           N  
ANISOU 3043  NH1 ARG A 394     4627   5488   6144    407   1024   1651       N  
ATOM   3044  NH2 ARG A 394      93.472 -18.003  49.176  1.00 54.92           N  
ANISOU 3044  NH2 ARG A 394     6232   7063   7572    327    911   1547       N  
ATOM   3045  N   LYS A 395      96.144 -11.653  48.042  1.00 39.19           N  
ANISOU 3045  N   LYS A 395     4672   5063   5156    431    824    987       N  
ATOM   3046  CA  LYS A 395      97.492 -11.206  48.367  1.00 35.41           C  
ANISOU 3046  CA  LYS A 395     4279   4591   4583    392    783    882       C  
ATOM   3047  C   LYS A 395      97.818  -9.868  47.717  1.00 46.13           C  
ANISOU 3047  C   LYS A 395     5693   5917   5916    415    741    785       C  
ATOM   3048  O   LYS A 395      98.758  -9.203  48.147  1.00 44.42           O  
ANISOU 3048  O   LYS A 395     5554   5694   5630    390    731    712       O  
ATOM   3049  CB  LYS A 395      98.525 -12.272  47.975  1.00 41.96           C  
ANISOU 3049  CB  LYS A 395     5085   5446   5412    341    683    838       C  
ATOM   3050  CG  LYS A 395      98.441 -13.549  48.804  1.00 46.24           C  
ANISOU 3050  CG  LYS A 395     5591   6013   5967    305    723    932       C  
ATOM   3051  CD  LYS A 395      99.487 -14.558  48.386  1.00 44.40           C  
ANISOU 3051  CD  LYS A 395     5336   5800   5733    258    621    887       C  
ATOM   3052  CE  LYS A 395      99.534 -15.737  49.346  1.00 47.48           C  
ANISOU 3052  CE  LYS A 395     5707   6208   6126    215    663    981       C  
ATOM   3053  NZ  LYS A 395     100.519 -16.783  48.886  1.00 29.83           N  
ANISOU 3053  NZ  LYS A 395     3445   3989   3901    171    560    945       N  
ATOM   3054  N   SER A 396      97.065  -9.484  46.682  1.00 35.09           N  
ANISOU 3054  N   SER A 396     4257   4498   4577    459    714    790       N  
ATOM   3055  CA  SER A 396      97.338  -8.230  45.962  1.00 42.23           C  
ANISOU 3055  CA  SER A 396     5212   5367   5466    477    668    707       C  
ATOM   3056  C   SER A 396      96.766  -7.013  46.668  1.00 53.22           C  
ANISOU 3056  C   SER A 396     6661   6729   6833    514    768    731       C  
ATOM   3057  O   SER A 396      97.238  -5.908  46.453  1.00 44.62           O  
ANISOU 3057  O   SER A 396     5632   5606   5714    516    744    663       O  
ATOM   3058  CB  SER A 396      96.765  -8.267  44.539  1.00 27.36           C  
ANISOU 3058  CB  SER A 396     3277   3472   3648    506    595    708       C  
ATOM   3059  OG  SER A 396      95.359  -8.161  44.552  1.00 28.40           O  
ANISOU 3059  OG  SER A 396     3366   3592   3835    555    672    806       O  
ATOM   3060  N   LEU A 397      95.746  -7.202  47.498  1.00 50.79           N  
ANISOU 3060  N   LEU A 397     6330   6427   6540    541    881    834       N  
ATOM   3061  CA  LEU A 397      95.057  -6.053  48.070  1.00 47.85           C  
ANISOU 3061  CA  LEU A 397     6006   6025   6150    585    979    865       C  
ATOM   3062  C   LEU A 397      95.957  -5.320  49.042  1.00 43.19           C  
ANISOU 3062  C   LEU A 397     5513   5426   5472    561   1010    811       C  
ATOM   3063  O   LEU A 397      96.726  -5.929  49.774  1.00 43.58           O  
ANISOU 3063  O   LEU A 397     5584   5504   5471    516   1008    800       O  
ATOM   3064  CB  LEU A 397      93.765  -6.470  48.785  1.00 53.89           C  
ANISOU 3064  CB  LEU A 397     6721   6801   6954    619   1099    994       C  
ATOM   3065  CG  LEU A 397      92.797  -7.414  48.066  1.00 50.92           C  
ANISOU 3065  CG  LEU A 397     6235   6435   6677    635   1085   1075       C  
ATOM   3066  CD1 LEU A 397      91.580  -7.670  48.941  1.00 39.01           C  
ANISOU 3066  CD1 LEU A 397     4684   4929   5207    663   1217   1205       C  
ATOM   3067  CD2 LEU A 397      92.368  -6.799  46.733  1.00 38.32           C  
ANISOU 3067  CD2 LEU A 397     4619   4810   5130    669   1021   1047       C  
ATOM   3068  N   VAL A 398      95.927  -3.995  48.965  1.00 50.79           N  
ANISOU 3068  N   VAL A 398     6536   6345   6415    589   1028    774       N  
ATOM   3069  CA  VAL A 398      96.676  -3.171  49.899  1.00 42.96           C  
ANISOU 3069  CA  VAL A 398     5641   5337   5347    571   1064    731       C  
ATOM   3070  C   VAL A 398      95.719  -2.295  50.704  1.00 53.88           C  
ANISOU 3070  C   VAL A 398     7064   6696   6712    624   1193    796       C  
ATOM   3071  O   VAL A 398      95.012  -1.445  50.158  1.00 49.47           O  
ANISOU 3071  O   VAL A 398     6505   6100   6191    670   1211    807       O  
ATOM   3072  CB  VAL A 398      97.731  -2.323  49.196  1.00 46.44           C  
ANISOU 3072  CB  VAL A 398     6128   5739   5777    546    968    624       C  
ATOM   3073  CG1 VAL A 398      98.451  -1.456  50.194  1.00 32.76           C  
ANISOU 3073  CG1 VAL A 398     4492   3984   3972    528   1010    590       C  
ATOM   3074  CG2 VAL A 398      98.715  -3.227  48.481  1.00 44.24           C  
ANISOU 3074  CG2 VAL A 398     5810   5486   5512    493    848    562       C  
ATOM   3075  N   LEU A 399      95.762  -2.464  52.021  1.00 52.15           N  
ANISOU 3075  N   LEU A 399     6886   6497   6430    614   1282    838       N  
ATOM   3076  CA  LEU A 399      94.926  -1.692  52.924  1.00 53.54           C  
ANISOU 3076  CA  LEU A 399     7108   6656   6580    660   1412    901       C  
ATOM   3077  C   LEU A 399      95.579  -0.349  53.208  1.00 47.27           C  
ANISOU 3077  C   LEU A 399     6415   5815   5728    661   1416    831       C  
ATOM   3078  O   LEU A 399      96.578  -0.274  53.917  1.00 48.59           O  
ANISOU 3078  O   LEU A 399     6647   5990   5824    619   1405    787       O  
ATOM   3079  CB  LEU A 399      94.707  -2.480  54.221  1.00 63.09           C  
ANISOU 3079  CB  LEU A 399     8322   7908   7740    646   1506    981       C  
ATOM   3080  CG  LEU A 399      93.822  -1.882  55.313  1.00 64.44           C  
ANISOU 3080  CG  LEU A 399     8537   8071   7875    691   1653   1060       C  
ATOM   3081  CD1 LEU A 399      92.400  -1.706  54.805  1.00 50.43           C  
ANISOU 3081  CD1 LEU A 399     6696   6279   6188    755   1713   1137       C  
ATOM   3082  CD2 LEU A 399      93.839  -2.725  56.575  1.00 64.28           C  
ANISOU 3082  CD2 LEU A 399     8529   8098   7796    664   1729   1132       C  
ATOM   3083  N   LEU A 400      94.990   0.712  52.664  1.00 47.46           N  
ANISOU 3083  N   LEU A 400     6453   5791   5788    708   1434    828       N  
ATOM   3084  CA  LEU A 400      95.548   2.040  52.826  1.00 32.29           C  
ANISOU 3084  CA  LEU A 400     4624   3817   3826    709   1436    768       C  
ATOM   3085  C   LEU A 400      95.066   2.716  54.083  1.00 47.39           C  
ANISOU 3085  C   LEU A 400     6610   5718   5678    742   1571    817       C  
ATOM   3086  O   LEU A 400      95.841   3.394  54.759  1.00 52.61           O  
ANISOU 3086  O   LEU A 400     7359   6359   6271    719   1583    772       O  
ATOM   3087  CB  LEU A 400      95.209   2.922  51.620  1.00 40.03           C  
ANISOU 3087  CB  LEU A 400     5593   4748   4871    741   1388    742       C  
ATOM   3088  CG  LEU A 400      95.718   2.529  50.241  1.00 50.43           C  
ANISOU 3088  CG  LEU A 400     6852   6066   6244    711   1250    684       C  
ATOM   3089  CD1 LEU A 400      95.278   3.562  49.221  1.00 51.85           C  
ANISOU 3089  CD1 LEU A 400     7034   6194   6472    747   1224    674       C  
ATOM   3090  CD2 LEU A 400      97.240   2.464  50.292  1.00 44.45           C  
ANISOU 3090  CD2 LEU A 400     6134   5307   5447    643   1161    595       C  
ATOM   3091  N   LYS A 401      93.817   2.465  54.458  1.00 60.40           N  
ANISOU 3091  N   LYS A 401     8219   7381   7347    791   1675    914       N  
ATOM   3092  CA  LYS A 401      93.255   3.168  55.610  1.00 56.16           C  
ANISOU 3092  CA  LYS A 401     7751   6831   6755    829   1812    966       C  
ATOM   3093  C   LYS A 401      92.269   2.244  56.301  1.00 55.74           C  
ANISOU 3093  C   LYS A 401     7643   6825   6711    851   1911   1077       C  
ATOM   3094  O   LYS A 401      91.481   1.559  55.657  1.00 42.25           O  
ANISOU 3094  O   LYS A 401     5838   5132   5083    869   1902   1131       O  
ATOM   3095  CB  LYS A 401      92.562   4.456  55.165  1.00 64.99           C  
ANISOU 3095  CB  LYS A 401     8898   7888   7907    887   1853    970       C  
ATOM   3096  CG  LYS A 401      91.853   5.206  56.289  1.00 68.72           C  
ANISOU 3096  CG  LYS A 401     9438   8344   8330    934   2002   1030       C  
ATOM   3097  CD  LYS A 401      91.283   6.519  55.786  1.00 46.22           C  
ANISOU 3097  CD  LYS A 401     6621   5429   5514    987   2034   1027       C  
ATOM   3098  CE  LYS A 401      90.573   7.274  56.896  1.00 53.68           C  
ANISOU 3098  CE  LYS A 401     7634   6355   6408   1036   2186   1085       C  
ATOM   3099  NZ  LYS A 401      90.045   8.578  56.400  1.00 64.93           N  
ANISOU 3099  NZ  LYS A 401     9094   7713   7864   1088   2217   1083       N  
ATOM   3100  N   ASN A 402      92.330   2.202  57.624  1.00 55.54           N  
ANISOU 3100  N   ASN A 402     7678   6822   6604    844   2005   1114       N  
ATOM   3101  CA  ASN A 402      91.392   1.383  58.375  1.00 67.00           C  
ANISOU 3101  CA  ASN A 402     9082   8314   8060    863   2110   1228       C  
ATOM   3102  C   ASN A 402      91.089   1.992  59.749  1.00 72.47           C  
ANISOU 3102  C   ASN A 402     9864   9007   8666    888   2249   1275       C  
ATOM   3103  O   ASN A 402      91.512   1.467  60.780  1.00 75.37           O  
ANISOU 3103  O   ASN A 402    10269   9414   8953    853   2285   1299       O  
ATOM   3104  CB  ASN A 402      91.963  -0.022  58.559  1.00 54.26           C  
ANISOU 3104  CB  ASN A 402     7422   6759   6435    802   2056   1241       C  
ATOM   3105  CG  ASN A 402      90.945  -0.994  59.100  1.00 46.02           C  
ANISOU 3105  CG  ASN A 402     6308   5753   5423    816   2149   1367       C  
ATOM   3106  OD1 ASN A 402      89.742  -0.775  58.981  1.00 50.63           O  
ANISOU 3106  OD1 ASN A 402     6847   6321   6070    872   2230   1443       O  
ATOM   3107  ND2 ASN A 402      91.421  -2.042  59.759  1.00 44.49           N  
ANISOU 3107  ND2 ASN A 402     6109   5607   5186    765   2145   1397       N  
ATOM   3108  N   ASN A 403      90.421   3.138  59.756  1.00 60.71           N  
ANISOU 3108  N   ASN A 403     8413   7470   7185    946   2323   1286       N  
ATOM   3109  CA  ASN A 403      90.187   3.877  60.988  1.00 71.57           C  
ANISOU 3109  CA  ASN A 403     9884   8837   8474    973   2451   1318       C  
ATOM   3110  C   ASN A 403      89.269   3.153  61.973  1.00 66.69           C  
ANISOU 3110  C   ASN A 403     9235   8262   7841    993   2580   1441       C  
ATOM   3111  O   ASN A 403      88.231   2.595  61.594  1.00 51.33           O  
ANISOU 3111  O   ASN A 403     7192   6327   5984   1024   2617   1524       O  
ATOM   3112  CB  ASN A 403      89.660   5.273  60.666  1.00 76.92           C  
ANISOU 3112  CB  ASN A 403    10606   9448   9173   1032   2497   1302       C  
ATOM   3113  CG  ASN A 403      90.771   6.223  60.278  1.00 64.96           C  
ANISOU 3113  CG  ASN A 403     9171   7887   7625   1004   2407   1186       C  
ATOM   3114  OD1 ASN A 403      91.858   5.790  59.898  1.00 55.99           O  
ANISOU 3114  OD1 ASN A 403     8030   6764   6478    944   2288   1113       O  
ATOM   3115  ND2 ASN A 403      90.501   7.519  60.349  1.00 64.44           N  
ANISOU 3115  ND2 ASN A 403     9176   7763   7547   1046   2463   1172       N  
ATOM   3116  N   GLU A 404      89.661   3.202  63.244  1.00 67.14           N  
ANISOU 3116  N   GLU A 404     9379   8346   7787    975   2651   1454       N  
ATOM   3117  CA  GLU A 404      88.952   2.534  64.340  1.00 75.63           C  
ANISOU 3117  CA  GLU A 404    10444   9466   8827    985   2777   1570       C  
ATOM   3118  C   GLU A 404      88.764   1.049  64.061  1.00 73.03           C  
ANISOU 3118  C   GLU A 404    10004   9184   8561    950   2737   1632       C  
ATOM   3119  O   GLU A 404      87.852   0.423  64.590  1.00 61.68           O  
ANISOU 3119  O   GLU A 404     8516   7773   7146    969   2837   1747       O  
ATOM   3120  CB  GLU A 404      87.589   3.197  64.617  1.00 69.90           C  
ANISOU 3120  CB  GLU A 404     9712   8714   8135   1064   2920   1654       C  
ATOM   3121  CG  GLU A 404      87.642   4.692  64.920  1.00 71.67           C  
ANISOU 3121  CG  GLU A 404    10045   8885   8301   1104   2975   1604       C  
ATOM   3122  CD  GLU A 404      88.594   5.016  66.064  0.70 73.06           C  
ANISOU 3122  CD  GLU A 404    10347   9080   8335   1068   2998   1562       C  
ATOM   3123  OE1 GLU A 404      88.695   4.202  67.010  0.70 65.18           O  
ANISOU 3123  OE1 GLU A 404     9358   8138   7269   1040   3045   1620       O  
ATOM   3124  OE2 GLU A 404      89.225   6.093  66.032  0.70 69.78           O  
ANISOU 3124  OE2 GLU A 404    10021   8621   7872   1068   2970   1476       O  
ATOM   3125  N   SER A 405      89.648   0.499  63.235  1.00 71.53           N  
ANISOU 3125  N   SER A 405     9777   9002   8399    899   2593   1558       N  
ATOM   3126  CA  SER A 405      89.659  -0.923  62.894  1.00 71.83           C  
ANISOU 3126  CA  SER A 405     9717   9082   8495    857   2536   1603       C  
ATOM   3127  C   SER A 405      88.294  -1.439  62.464  1.00 56.49           C  
ANISOU 3127  C   SER A 405     7659   7137   6670    899   2595   1709       C  
ATOM   3128  O   SER A 405      87.869  -2.503  62.895  1.00 58.29           O  
ANISOU 3128  O   SER A 405     7827   7400   6920    880   2640   1806       O  
ATOM   3129  CB  SER A 405      90.188  -1.750  64.071  1.00 71.62           C  
ANISOU 3129  CB  SER A 405     9732   9109   8373    805   2570   1648       C  
ATOM   3130  OG  SER A 405      91.513  -1.351  64.418  1.00 82.39           O  
ANISOU 3130  OG  SER A 405    11195  10478   9632    761   2503   1550       O  
ATOM   3131  N   ILE A 406      87.630  -0.705  61.579  1.00 66.43           N  
ANISOU 3131  N   ILE A 406     8881   8351   8007    952   2590   1695       N  
ATOM   3132  CA  ILE A 406      86.317  -1.114  61.086  1.00 60.69           C  
ANISOU 3132  CA  ILE A 406     8040   7619   7401    993   2641   1795       C  
ATOM   3133  C   ILE A 406      86.377  -2.404  60.281  1.00 53.80           C  
ANISOU 3133  C   ILE A 406     7054   6770   6616    952   2544   1813       C  
ATOM   3134  O   ILE A 406      85.462  -3.217  60.347  1.00 60.09           O  
ANISOU 3134  O   ILE A 406     7757   7582   7491    960   2600   1924       O  
ATOM   3135  CB  ILE A 406      85.643   0.005  60.267  1.00 56.18           C  
ANISOU 3135  CB  ILE A 406     7460   6994   6890   1058   2648   1773       C  
ATOM   3136  CG1 ILE A 406      84.313  -0.492  59.715  1.00 55.78           C  
ANISOU 3136  CG1 ILE A 406     7283   6942   6968   1096   2691   1879       C  
ATOM   3137  CG2 ILE A 406      86.527   0.426  59.109  1.00 66.22           C  
ANISOU 3137  CG2 ILE A 406     8746   8239   8175   1037   2498   1647       C  
ATOM   3138  CD1 ILE A 406      83.556   0.542  58.940  1.00 76.67           C  
ANISOU 3138  CD1 ILE A 406     9915   9540   9676   1160   2705   1874       C  
ATOM   3139  N   LEU A 407      87.481  -2.619  59.567  1.00 67.59           N  
ANISOU 3139  N   LEU A 407     8810   8521   8351    904   2402   1708       N  
ATOM   3140  CA  LEU A 407      87.706  -3.904  58.912  1.00 61.55           C  
ANISOU 3140  CA  LEU A 407     7951   7782   7654    858   2308   1719       C  
ATOM   3141  C   LEU A 407      88.490  -4.802  59.863  1.00 59.68           C  
ANISOU 3141  C   LEU A 407     7748   7588   7337    795   2309   1736       C  
ATOM   3142  O   LEU A 407      89.355  -4.333  60.609  1.00 62.68           O  
ANISOU 3142  O   LEU A 407     8235   7976   7603    773   2314   1680       O  
ATOM   3143  CB  LEU A 407      88.498  -3.704  57.616  1.00 53.40           C  
ANISOU 3143  CB  LEU A 407     6909   6731   6649    839   2154   1599       C  
ATOM   3144  CG  LEU A 407      87.731  -3.038  56.469  1.00 48.69           C  
ANISOU 3144  CG  LEU A 407     6262   6095   6143    893   2130   1590       C  
ATOM   3145  CD1 LEU A 407      88.652  -2.781  55.297  1.00 54.34           C  
ANISOU 3145  CD1 LEU A 407     6987   6794   6864    870   1980   1468       C  
ATOM   3146  CD2 LEU A 407      86.566  -3.890  56.029  1.00 45.73           C  
ANISOU 3146  CD2 LEU A 407     5759   5728   5887    911   2158   1700       C  
ATOM   3147  N   PRO A 408      88.198  -6.110  59.834  1.00 54.13           N  
ANISOU 3147  N   PRO A 408     6956   6912   6698    762   2302   1818       N  
ATOM   3148  CA  PRO A 408      87.210  -6.766  58.968  1.00 59.73           C  
ANISOU 3148  CA  PRO A 408     7534   7612   7550    781   2291   1889       C  
ATOM   3149  C   PRO A 408      85.761  -6.623  59.446  1.00 60.87           C  
ANISOU 3149  C   PRO A 408     7629   7746   7754    835   2435   2019       C  
ATOM   3150  O   PRO A 408      85.508  -6.409  60.630  1.00 46.13           O  
ANISOU 3150  O   PRO A 408     5818   5891   5819    846   2553   2080       O  
ATOM   3151  CB  PRO A 408      87.624  -8.239  59.046  1.00 45.37           C  
ANISOU 3151  CB  PRO A 408     5658   5825   5757    715   2238   1931       C  
ATOM   3152  CG  PRO A 408      88.218  -8.384  60.400  1.00 47.09           C  
ANISOU 3152  CG  PRO A 408     5967   6071   5852    681   2300   1953       C  
ATOM   3153  CD  PRO A 408      88.921  -7.079  60.679  1.00 47.96           C  
ANISOU 3153  CD  PRO A 408     6202   6171   5850    698   2297   1845       C  
ATOM   3154  N   ILE A 409      84.829  -6.703  58.497  1.00 51.55           N  
ANISOU 3154  N   ILE A 409     6344   6542   6698    868   2421   2059       N  
ATOM   3155  CA  ILE A 409      83.410  -6.538  58.768  1.00 62.02           C  
ANISOU 3155  CA  ILE A 409     7610   7855   8101    921   2548   2181       C  
ATOM   3156  C   ILE A 409      82.795  -7.893  59.113  1.00 82.64           C  
ANISOU 3156  C   ILE A 409    10118  10485  10797    890   2591   2313       C  
ATOM   3157  O   ILE A 409      83.069  -8.898  58.450  1.00 83.05           O  
ANISOU 3157  O   ILE A 409    10094  10543  10918    845   2493   2312       O  
ATOM   3158  CB  ILE A 409      82.673  -5.983  57.528  1.00 60.60           C  
ANISOU 3158  CB  ILE A 409     7363   7639   8022    970   2508   2167       C  
ATOM   3159  CG1 ILE A 409      83.101  -4.543  57.247  1.00 50.25           C  
ANISOU 3159  CG1 ILE A 409     6154   6302   6637   1008   2485   2056       C  
ATOM   3160  CG2 ILE A 409      81.165  -6.049  57.716  1.00 63.77           C  
ANISOU 3160  CG2 ILE A 409     7677   8029   8525   1016   2628   2306       C  
ATOM   3161  CD1 ILE A 409      82.863  -4.108  55.823  1.00 51.20           C  
ANISOU 3161  CD1 ILE A 409     6227   6392   6835   1034   2392   2006       C  
ATOM   3162  N   LYS A 410      82.002  -7.921  60.185  1.00 68.13           N  
ANISOU 3162  N   LYS A 410     8281   8654   8953    911   2738   2428       N  
ATOM   3163  CA  LYS A 410      81.236  -9.107  60.563  1.00 63.47           C  
ANISOU 3163  CA  LYS A 410     7586   8072   8455    887   2799   2572       C  
ATOM   3164  C   LYS A 410      80.377  -9.593  59.399  1.00 56.04           C  
ANISOU 3164  C   LYS A 410     6502   7108   7684    897   2748   2620       C  
ATOM   3165  O   LYS A 410      79.540  -8.848  58.878  1.00 64.90           O  
ANISOU 3165  O   LYS A 410     7591   8204   8865    954   2780   2631       O  
ATOM   3166  CB  LYS A 410      80.337  -8.789  61.763  1.00 71.17           C  
ANISOU 3166  CB  LYS A 410     8583   9052   9406    925   2977   2687       C  
ATOM   3167  CG  LYS A 410      81.076  -8.577  63.080  1.00 82.57           C  
ANISOU 3167  CG  LYS A 410    10158  10525  10689    905   3042   2673       C  
ATOM   3168  CD  LYS A 410      81.697  -9.862  63.611  1.00 91.83           C  
ANISOU 3168  CD  LYS A 410    11324  11728  11841    830   3011   2718       C  
ATOM   3169  CE  LYS A 410      82.367  -9.618  64.957  1.00 93.45           C  
ANISOU 3169  CE  LYS A 410    11663  11964  11881    812   3081   2714       C  
ATOM   3170  NZ  LYS A 410      81.375  -9.321  66.022  1.00107.24           N  
ANISOU 3170  NZ  LYS A 410    13422  13714  13609    854   3257   2833       N  
ATOM   3171  N   ALA A 411      80.567 -10.851  59.013  1.00 50.79           N  
ANISOU 3171  N   ALA A 411     5753   6447   7098    841   2671   2653       N  
ATOM   3172  CA  ALA A 411      79.845 -11.415  57.875  1.00 63.07           C  
ANISOU 3172  CA  ALA A 411     7172   7978   8816    842   2608   2695       C  
ATOM   3173  C   ALA A 411      78.336 -11.514  58.117  1.00 76.58           C  
ANISOU 3173  C   ALA A 411     8782   9669  10645    877   2731   2844       C  
ATOM   3174  O   ALA A 411      77.552 -11.609  57.167  1.00 73.70           O  
ANISOU 3174  O   ALA A 411     8315   9278  10410    895   2696   2876       O  
ATOM   3175  CB  ALA A 411      80.417 -12.778  57.510  1.00 55.34           C  
ANISOU 3175  CB  ALA A 411     6130   7004   7894    771   2503   2702       C  
ATOM   3176  N   SER A 412      77.942 -11.527  59.390  1.00 69.83           N  
ANISOU 3176  N   SER A 412     7958   8828   9748    885   2873   2937       N  
ATOM   3177  CA  SER A 412      76.533 -11.622  59.764  1.00 63.98           C  
ANISOU 3177  CA  SER A 412     7126   8070   9112    918   3005   3085       C  
ATOM   3178  C   SER A 412      75.830 -10.264  59.836  1.00 68.05           C  
ANISOU 3178  C   SER A 412     7683   8574   9599    998   3097   3078       C  
ATOM   3179  O   SER A 412      74.658 -10.197  60.213  1.00 80.81           O  
ANISOU 3179  O   SER A 412     9234  10178  11290   1032   3219   3198       O  
ATOM   3180  CB  SER A 412      76.394 -12.336  61.111  1.00 61.69           C  
ANISOU 3180  CB  SER A 412     6846   7799   8793    888   3121   3202       C  
ATOM   3181  OG  SER A 412      77.130 -11.671  62.126  1.00 58.55           O  
ANISOU 3181  OG  SER A 412     6597   7430   8219    896   3178   3147       O  
ATOM   3182  N   SER A 413      76.521  -9.195  59.441  1.00 64.35           N  
ANISOU 3182  N   SER A 413     7316   8105   9031   1026   3038   2942       N  
ATOM   3183  CA  SER A 413      75.946  -7.847  59.510  1.00 66.52           C  
ANISOU 3183  CA  SER A 413     7641   8362   9271   1101   3120   2928       C  
ATOM   3184  C   SER A 413      74.939  -7.577  58.401  1.00 66.20           C  
ANISOU 3184  C   SER A 413     7496   8289   9367   1140   3098   2960       C  
ATOM   3185  O   SER A 413      74.727  -8.401  57.516  1.00 61.19           O  
ANISOU 3185  O   SER A 413     6754   7646   8851   1108   3009   2984       O  
ATOM   3186  CB  SER A 413      77.053  -6.786  59.404  1.00 63.37           C  
ANISOU 3186  CB  SER A 413     7384   7964   8728   1114   3056   2771       C  
ATOM   3187  OG  SER A 413      78.057  -6.968  60.389  1.00 68.25           O  
ANISOU 3187  OG  SER A 413     8107   8612   9214   1075   3067   2731       O  
ATOM   3188  N   ARG A 414      74.307  -6.409  58.470  1.00 69.89           N  
ANISOU 3188  N   ARG A 414     7999   8738   9816   1209   3180   2965       N  
ATOM   3189  CA  ARG A 414      73.518  -5.908  57.355  1.00 69.96           C  
ANISOU 3189  CA  ARG A 414     7937   8717   9926   1250   3146   2971       C  
ATOM   3190  C   ARG A 414      74.427  -4.944  56.612  1.00 66.91           C  
ANISOU 3190  C   ARG A 414     7651   8320   9452   1263   3036   2816       C  
ATOM   3191  O   ARG A 414      74.822  -3.908  57.142  1.00 71.98           O  
ANISOU 3191  O   ARG A 414     8413   8958   9979   1297   3084   2754       O  
ATOM   3192  CB  ARG A 414      72.233  -5.220  57.829  1.00 71.06           C  
ANISOU 3192  CB  ARG A 414     8050   8841  10111   1317   3303   3078       C  
ATOM   3193  CG  ARG A 414      71.380  -4.666  56.695  1.00 75.05           C  
ANISOU 3193  CG  ARG A 414     8483   9315  10719   1359   3272   3092       C  
ATOM   3194  CD  ARG A 414      70.130  -3.941  57.180  1.00 85.94           C  
ANISOU 3194  CD  ARG A 414     9837  10677  12137   1428   3430   3196       C  
ATOM   3195  NE  ARG A 414      69.368  -4.708  58.164  1.00 88.00           N  
ANISOU 3195  NE  ARG A 414    10026  10952  12457   1420   3561   3339       N  
ATOM   3196  CZ  ARG A 414      68.361  -5.518  57.846  1.00 96.97           C  
ANISOU 3196  CZ  ARG A 414    11013  12080  13752   1405   3582   3461       C  
ATOM   3197  NH1 ARG A 414      68.019  -5.675  56.571  1.00 88.13           N  
ANISOU 3197  NH1 ARG A 414     9803  10940  12741   1395   3476   3453       N  
ATOM   3198  NH2 ARG A 414      67.710  -6.183  58.795  1.00 99.28           N  
ANISOU 3198  NH2 ARG A 414    11246  12382  14093   1395   3706   3591       N  
ATOM   3199  N   ILE A 415      74.746  -5.297  55.374  1.00 81.48           N  
ANISOU 3199  N   ILE A 415     9447  10158  11354   1235   2890   2758       N  
ATOM   3200  CA  ILE A 415      75.743  -4.575  54.602  1.00 77.02           C  
ANISOU 3200  CA  ILE A 415     8969   9585  10709   1234   2769   2609       C  
ATOM   3201  C   ILE A 415      75.113  -4.001  53.350  1.00 71.43           C  
ANISOU 3201  C   ILE A 415     8213   8849  10079   1269   2714   2602       C  
ATOM   3202  O   ILE A 415      74.354  -4.689  52.660  1.00 61.19           O  
ANISOU 3202  O   ILE A 415     6794   7544   8909   1257   2685   2677       O  
ATOM   3203  CB  ILE A 415      76.918  -5.509  54.217  1.00 68.02           C  
ANISOU 3203  CB  ILE A 415     7834   8467   9544   1163   2629   2528       C  
ATOM   3204  CG1 ILE A 415      77.587  -6.064  55.476  1.00 70.48           C  
ANISOU 3204  CG1 ILE A 415     8201   8809   9770   1125   2682   2537       C  
ATOM   3205  CG2 ILE A 415      77.911  -4.780  53.330  1.00 70.08           C  
ANISOU 3205  CG2 ILE A 415     8176   8718   9733   1161   2501   2379       C  
ATOM   3206  CD1 ILE A 415      78.611  -7.134  55.217  1.00 60.20           C  
ANISOU 3206  CD1 ILE A 415     6887   7529   8457   1053   2562   2483       C  
ATOM   3207  N   LEU A 416      75.466  -2.758  53.033  1.00 61.92           N  
ANISOU 3207  N   LEU A 416     7104   7624   8798   1307   2693   2512       N  
ATOM   3208  CA  LEU A 416      75.101  -2.183  51.749  1.00 46.64           C  
ANISOU 3208  CA  LEU A 416     5140   5663   6916   1331   2617   2487       C  
ATOM   3209  C   LEU A 416      76.299  -2.146  50.835  1.00 68.46           C  
ANISOU 3209  C   LEU A 416     7958   8430   9625   1293   2455   2350       C  
ATOM   3210  O   LEU A 416      77.353  -1.685  51.217  1.00 67.17           O  
ANISOU 3210  O   LEU A 416     7903   8269   9349   1283   2429   2250       O  
ATOM   3211  CB  LEU A 416      74.612  -0.749  51.943  1.00 50.79           C  
ANISOU 3211  CB  LEU A 416     5734   6160   7403   1402   2706   2488       C  
ATOM   3212  CG  LEU A 416      74.374   0.037  50.652  1.00 57.64           C  
ANISOU 3212  CG  LEU A 416     6598   7001   8301   1428   2627   2450       C  
ATOM   3213  CD1 LEU A 416      73.187  -0.512  49.882  1.00 72.26           C  
ANISOU 3213  CD1 LEU A 416     8312   8850  10295   1431   2625   2557       C  
ATOM   3214  CD2 LEU A 416      74.182   1.527  50.950  1.00 58.05           C  
ANISOU 3214  CD2 LEU A 416     6746   7022   8290   1493   2707   2429       C  
ATOM   3215  N   VAL A 417      76.137  -2.641  49.616  1.00 69.73           N  
ANISOU 3215  N   VAL A 417     8042   8587   9865   1270   2346   2348       N  
ATOM   3216  CA  VAL A 417      77.201  -2.537  48.630  1.00 64.07           C  
ANISOU 3216  CA  VAL A 417     7375   7871   9099   1238   2192   2221       C  
ATOM   3217  C   VAL A 417      76.799  -1.563  47.532  1.00 65.84           C  
ANISOU 3217  C   VAL A 417     7610   8068   9340   1273   2149   2199       C  
ATOM   3218  O   VAL A 417      75.778  -1.747  46.865  1.00 62.55           O  
ANISOU 3218  O   VAL A 417     7101   7642   9023   1285   2153   2281       O  
ATOM   3219  CB  VAL A 417      77.524  -3.902  47.987  1.00 71.11           C  
ANISOU 3219  CB  VAL A 417     8185   8780  10052   1175   2081   2220       C  
ATOM   3220  CG1 VAL A 417      78.699  -3.778  47.033  1.00 71.52           C  
ANISOU 3220  CG1 VAL A 417     8298   8835  10041   1143   1929   2086       C  
ATOM   3221  CG2 VAL A 417      77.799  -4.946  49.055  1.00 51.81           C  
ANISOU 3221  CG2 VAL A 417     5718   6362   7606   1138   2130   2262       C  
ATOM   3222  N   ALA A 418      77.635  -0.549  47.319  1.00 49.95           N  
ANISOU 3222  N   ALA A 418     5708   6042   7230   1284   2102   2090       N  
ATOM   3223  CA  ALA A 418      77.302   0.525  46.393  1.00 51.98           C  
ANISOU 3223  CA  ALA A 418     5990   6270   7488   1320   2072   2070       C  
ATOM   3224  C   ALA A 418      78.505   0.766  45.500  1.00 53.99           C  
ANISOU 3224  C   ALA A 418     6313   6523   7676   1284   1925   1940       C  
ATOM   3225  O   ALA A 418      79.528   0.109  45.641  1.00 61.30           O  
ANISOU 3225  O   ALA A 418     7262   7470   8560   1236   1854   1869       O  
ATOM   3226  CB  ALA A 418      76.939   1.806  47.147  1.00 46.63           C  
ANISOU 3226  CB  ALA A 418     5387   5565   6765   1383   2193   2086       C  
ATOM   3227  N   GLY A 419      78.358   1.697  44.569  1.00 48.66           N  
ANISOU 3227  N   GLY A 419     5667   5826   6995   1307   1880   1913       N  
ATOM   3228  CA  GLY A 419      79.412   2.065  43.648  1.00 35.22           C  
ANISOU 3228  CA  GLY A 419     4030   4120   5233   1276   1746   1797       C  
ATOM   3229  C   GLY A 419      79.253   1.399  42.290  1.00 51.30           C  
ANISOU 3229  C   GLY A 419     6001   6196   7296   1200   1618   1766       C  
ATOM   3230  O   GLY A 419      78.747   0.281  42.170  1.00 52.73           O  
ANISOU 3230  O   GLY A 419     6089   6388   7560   1189   1617   1842       O  
ATOM   3231  N   LYS A 420      79.703   2.111  41.262  1.00 52.32           N  
ANISOU 3231  N   LYS A 420     6180   6346   7352   1141   1510   1649       N  
ATOM   3232  CA  LYS A 420      79.607   1.672  39.874  1.00 52.13           C  
ANISOU 3232  CA  LYS A 420     6116   6361   7329   1062   1387   1598       C  
ATOM   3233  C   LYS A 420      80.353   0.359  39.619  1.00 60.34           C  
ANISOU 3233  C   LYS A 420     7130   7429   8367    992   1291   1546       C  
ATOM   3234  O   LYS A 420      80.016  -0.386  38.695  1.00 54.16           O  
ANISOU 3234  O   LYS A 420     6290   6667   7620    942   1223   1549       O  
ATOM   3235  CB  LYS A 420      80.164   2.781  38.975  1.00 51.71           C  
ANISOU 3235  CB  LYS A 420     6139   6323   7184   1017   1296   1475       C  
ATOM   3236  CG  LYS A 420      79.803   2.693  37.508  0.70 47.53           C  
ANISOU 3236  CG  LYS A 420     5578   5827   6654    957   1201   1440       C  
ATOM   3237  CD  LYS A 420      80.545   3.770  36.733  0.70 34.98           C  
ANISOU 3237  CD  LYS A 420     4068   4253   4969    911   1111   1314       C  
ATOM   3238  CE  LYS A 420      80.225   3.735  35.247  0.70 40.53           C  
ANISOU 3238  CE  LYS A 420     4748   4988   5662    856   1022   1278       C  
ATOM   3239  NZ  LYS A 420      80.420   2.390  34.645  0.70 45.07           N  
ANISOU 3239  NZ  LYS A 420     5281   5587   6256    795    946   1257       N  
ATOM   3240  N   GLY A 421      81.387   0.101  40.423  1.00 52.83           N  
ANISOU 3240  N   GLY A 421     6226   6476   7372    989   1286   1496       N  
ATOM   3241  CA  GLY A 421      82.196  -1.097  40.276  1.00 40.45           C  
ANISOU 3241  CA  GLY A 421     4641   4934   5795    926   1199   1444       C  
ATOM   3242  C   GLY A 421      81.755  -2.299  41.092  1.00 55.04           C  
ANISOU 3242  C   GLY A 421     6406   6771   7737    961   1273   1565       C  
ATOM   3243  O   GLY A 421      82.401  -3.342  41.078  1.00 49.78           O  
ANISOU 3243  O   GLY A 421     5721   6123   7072    915   1212   1535       O  
ATOM   3244  N   ALA A 422      80.673  -2.135  41.838  1.00 57.33           N  
ANISOU 3244  N   ALA A 422     6644   7028   8108   1045   1411   1708       N  
ATOM   3245  CA  ALA A 422      80.218  -3.155  42.770  1.00 53.08           C  
ANISOU 3245  CA  ALA A 422     6026   6479   7662   1081   1500   1833       C  
ATOM   3246  C   ALA A 422      79.932  -4.479  42.075  1.00 60.06           C  
ANISOU 3246  C   ALA A 422     6814   7375   8632   1029   1429   1873       C  
ATOM   3247  O   ALA A 422      80.304  -5.545  42.566  1.00 60.28           O  
ANISOU 3247  O   ALA A 422     6805   7415   8684   1001   1422   1888       O  
ATOM   3248  CB  ALA A 422      79.003  -2.679  43.546  1.00 78.92           C  
ANISOU 3248  CB  ALA A 422     9264   9739  10983   1134   1648   1943       C  
ATOM   3249  N   ASN A 423      79.299  -4.402  40.909  1.00 58.97           N  
ANISOU 3249  N   ASN A 423     6643   7242   8519    989   1370   1863       N  
ATOM   3250  CA  ASN A 423      78.880  -5.607  40.211  1.00 43.93           C  
ANISOU 3250  CA  ASN A 423     4648   5339   6705    935   1311   1905       C  
ATOM   3251  C   ASN A 423      79.281  -5.533  38.741  1.00 49.91           C  
ANISOU 3251  C   ASN A 423     5447   6121   7394    850   1172   1776       C  
ATOM   3252  O   ASN A 423      78.596  -6.050  37.859  1.00 53.08           O  
ANISOU 3252  O   ASN A 423     5785   6515   7867    816   1137   1813       O  
ATOM   3253  CB  ASN A 423      77.358  -5.773  40.330  1.00 44.58           C  
ANISOU 3253  CB  ASN A 423     4618   5388   6934    985   1411   2075       C  
ATOM   3254  CG  ASN A 423      76.871  -7.120  39.846  1.00 60.70           C  
ANISOU 3254  CG  ASN A 423     6551   7414   9099    937   1368   2146       C  
ATOM   3255  OD1 ASN A 423      77.481  -8.159  40.126  1.00 57.15           O  
ANISOU 3255  OD1 ASN A 423     6079   6966   8667    904   1328   2137       O  
ATOM   3256  ND2 ASN A 423      75.796  -7.106  39.061  1.00 57.27           N  
ANISOU 3256  ND2 ASN A 423     6047   6961   8753    929   1371   2214       N  
ATOM   3257  N   ALA A 424      80.418  -4.897  38.480  1.00 44.99           N  
ANISOU 3257  N   ALA A 424     4932   5525   6637    816   1096   1626       N  
ATOM   3258  CA  ALA A 424      80.868  -4.672  37.109  1.00 46.97           C  
ANISOU 3258  CA  ALA A 424     5235   5801   6810    742    973   1498       C  
ATOM   3259  C   ALA A 424      82.217  -5.371  36.934  1.00 49.49           C  
ANISOU 3259  C   ALA A 424     5607   6143   7054    675    868   1375       C  
ATOM   3260  O   ALA A 424      83.262  -4.821  37.273  1.00 54.22           O  
ANISOU 3260  O   ALA A 424     6286   6756   7557    667    838   1277       O  
ATOM   3261  CB  ALA A 424      80.977  -3.209  36.804  1.00 31.43           C  
ANISOU 3261  CB  ALA A 424     3344   3842   4756    756    970   1430       C  
ATOM   3262  N   ILE A 425      82.188  -6.591  36.413  1.00 57.00           N  
ANISOU 3262  N   ILE A 425     6510   7092   8057    627    815   1386       N  
ATOM   3263  CA  ILE A 425      83.407  -7.385  36.266  1.00 64.83           C  
ANISOU 3263  CA  ILE A 425     7544   8101   8988    568    723   1281       C  
ATOM   3264  C   ILE A 425      84.387  -6.686  35.316  1.00 53.47           C  
ANISOU 3264  C   ILE A 425     6211   6689   7415    512    620   1114       C  
ATOM   3265  O   ILE A 425      85.608  -6.791  35.469  1.00 40.23           O  
ANISOU 3265  O   ILE A 425     4599   5030   5658    478    559   1008       O  
ATOM   3266  CB  ILE A 425      83.114  -8.827  35.838  1.00 55.53           C  
ANISOU 3266  CB  ILE A 425     6292   6904   7901    529    690   1331       C  
ATOM   3267  CG1 ILE A 425      82.245  -9.520  36.883  1.00 64.06           C  
ANISOU 3267  CG1 ILE A 425     7261   7954   9124    582    790   1501       C  
ATOM   3268  CG2 ILE A 425      84.418  -9.598  35.586  1.00 42.88           C  
ANISOU 3268  CG2 ILE A 425     4748   5320   6226    468    594   1214       C  
ATOM   3269  CD1 ILE A 425      81.693 -10.849  36.430  1.00 60.43           C  
ANISOU 3269  CD1 ILE A 425     6708   7460   8791    546    764   1576       C  
ATOM   3270  N   ASN A 426      83.852  -5.934  34.363  1.00 33.17           N  
ANISOU 3270  N   ASN A 426     3655   4120   4827    504    604   1095       N  
ATOM   3271  CA  ASN A 426      84.703  -5.246  33.398  1.00 37.65           C  
ANISOU 3271  CA  ASN A 426     4316   4712   5279    451    511    947       C  
ATOM   3272  C   ASN A 426      85.634  -4.233  34.053  1.00 35.32           C  
ANISOU 3272  C   ASN A 426     4093   4427   4901    459    502    868       C  
ATOM   3273  O   ASN A 426      86.754  -4.029  33.594  1.00 48.64           O  
ANISOU 3273  O   ASN A 426     5851   6129   6502    404    413    737       O  
ATOM   3274  CB  ASN A 426      83.887  -4.638  32.248  1.00 37.80           C  
ANISOU 3274  CB  ASN A 426     4327   4732   5303    445    504    958       C  
ATOM   3275  CG  ASN A 426      83.216  -3.322  32.631  1.00 54.90           C  
ANISOU 3275  CG  ASN A 426     6491   6894   7473    503    575   1010       C  
ATOM   3276  OD1 ASN A 426      82.671  -3.179  33.732  1.00 54.10           O  
ANISOU 3276  OD1 ASN A 426     6349   6775   7431    567    670   1111       O  
ATOM   3277  ND2 ASN A 426      83.236  -2.362  31.713  1.00 38.74           N  
ANISOU 3277  ND2 ASN A 426     4490   4863   5367    484    535    947       N  
ATOM   3278  N   MET A 427      85.162  -3.598  35.121  1.00 30.77           N  
ANISOU 3278  N   MET A 427     3496   3836   4360    529    599    952       N  
ATOM   3279  CA  MET A 427      85.975  -2.647  35.879  1.00 50.15           C  
ANISOU 3279  CA  MET A 427     6013   6289   6755    545    609    897       C  
ATOM   3280  C   MET A 427      87.029  -3.343  36.734  1.00 45.00           C  
ANISOU 3280  C   MET A 427     5375   5639   6082    534    594    864       C  
ATOM   3281  O   MET A 427      88.144  -2.852  36.880  1.00 38.03           O  
ANISOU 3281  O   MET A 427     4555   4762   5132    504    543    766       O  
ATOM   3282  CB  MET A 427      85.081  -1.776  36.762  1.00 38.36           C  
ANISOU 3282  CB  MET A 427     4499   4769   5306    632    734   1006       C  
ATOM   3283  CG  MET A 427      84.370  -0.693  35.973  1.00 42.48           C  
ANISOU 3283  CG  MET A 427     5031   5290   5819    641    738   1008       C  
ATOM   3284  SD  MET A 427      83.380   0.427  36.975  1.00 53.87           S  
ANISOU 3284  SD  MET A 427     6465   6698   7306    745    888   1126       S  
ATOM   3285  CE  MET A 427      84.628   1.325  37.881  1.00 26.28           C  
ANISOU 3285  CE  MET A 427     3061   3187   3735    752    890   1044       C  
ATOM   3286  N   GLN A 428      86.670  -4.482  37.315  1.00 49.70           N  
ANISOU 3286  N   GLN A 428     5907   6230   6748    557    642    954       N  
ATOM   3287  CA  GLN A 428      87.622  -5.247  38.128  1.00 48.76           C  
ANISOU 3287  CA  GLN A 428     5794   6117   6616    548    634    936       C  
ATOM   3288  C   GLN A 428      88.687  -5.961  37.288  1.00 45.91           C  
ANISOU 3288  C   GLN A 428     5470   5778   6194    463    506    810       C  
ATOM   3289  O   GLN A 428      89.767  -6.282  37.792  1.00 31.87           O  
ANISOU 3289  O   GLN A 428     3722   4009   4379    443    475    755       O  
ATOM   3290  CB  GLN A 428      86.898  -6.232  39.057  1.00 36.93           C  
ANISOU 3290  CB  GLN A 428     4208   4605   5219    602    730   1084       C  
ATOM   3291  CG  GLN A 428      86.534  -7.562  38.432  1.00 45.72           C  
ANISOU 3291  CG  GLN A 428     5256   5720   6396    562    687   1118       C  
ATOM   3292  CD  GLN A 428      85.531  -8.357  39.254  1.00 47.68           C  
ANISOU 3292  CD  GLN A 428     5397   5945   6772    617    790   1288       C  
ATOM   3293  OE1 GLN A 428      84.579  -7.815  39.813  1.00 46.01           O  
ANISOU 3293  OE1 GLN A 428     5150   5714   6620    684    895   1395       O  
ATOM   3294  NE2 GLN A 428      85.790  -9.649  39.387  1.00 48.77           N  
ANISOU 3294  NE2 GLN A 428     5488   6084   6960    589    762   1317       N  
ATOM   3295  N   ALA A 429      88.367  -6.229  36.022  1.00 36.62           N  
ANISOU 3295  N   ALA A 429     4295   4606   5013    417    441    770       N  
ATOM   3296  CA  ALA A 429      89.296  -6.915  35.120  1.00 34.93           C  
ANISOU 3296  CA  ALA A 429     4041   4477   4751    318    396    613       C  
ATOM   3297  C   ALA A 429      90.251  -5.973  34.401  1.00 41.92           C  
ANISOU 3297  C   ALA A 429     4998   5372   5559    286    342    518       C  
ATOM   3298  O   ALA A 429      91.417  -6.318  34.154  1.00 26.25           O  
ANISOU 3298  O   ALA A 429     3137   3344   3495    225    262    502       O  
ATOM   3299  CB  ALA A 429      88.534  -7.751  34.112  1.00 34.69           C  
ANISOU 3299  CB  ALA A 429     4087   4364   4729    271    349    717       C  
ATOM   3300  N   GLY A 430      89.749  -4.787  34.064  1.00 38.40           N  
ANISOU 3300  N   GLY A 430     4536   4904   5149    380    450    719       N  
ATOM   3301  CA  GLY A 430      90.513  -3.777  33.350  1.00 24.58           C  
ANISOU 3301  CA  GLY A 430     2944   3125   3271    276    271    489       C  
ATOM   3302  C   GLY A 430      90.753  -4.150  31.892  1.00 52.35           C  
ANISOU 3302  C   GLY A 430     6474   6666   6752    208    230    437       C  
ATOM   3303  O   GLY A 430      90.145  -5.106  31.379  1.00 42.20           O  
ANISOU 3303  O   GLY A 430     5159   5375   5499    202    230    471       O  
ATOM   3304  N   GLY A 431      91.674  -3.430  31.240  1.00 43.00           N  
ANISOU 3304  N   GLY A 431     5325   5494   5518    176    182    349       N  
ATOM   3305  CA  GLY A 431      91.968  -3.616  29.822  1.00 32.61           C  
ANISOU 3305  CA  GLY A 431     3976   4211   4202    148    146    254       C  
ATOM   3306  C   GLY A 431      92.625  -4.971  29.567  1.00 33.40           C  
ANISOU 3306  C   GLY A 431     4088   4307   4296    115    113    222       C  
ATOM   3307  O   GLY A 431      93.047  -5.645  30.505  1.00 34.88           O  
ANISOU 3307  O   GLY A 431     4250   4501   4502    150    151    322       O  
ATOM   3308  N   TRP A 432      92.746  -5.346  28.297  1.00 29.15           N  
ANISOU 3308  N   TRP A 432     3605   3749   3723     78     73    199       N  
ATOM   3309  CA  TRP A 432      93.317  -6.630  27.897  1.00 37.69           C  
ANISOU 3309  CA  TRP A 432     4696   4821   4801     55     52    163       C  
ATOM   3310  C   TRP A 432      92.557  -7.784  28.562  1.00 39.99           C  
ANISOU 3310  C   TRP A 432     4943   5108   5145     77     83    255       C  
ATOM   3311  O   TRP A 432      93.160  -8.700  29.121  1.00 40.36           O  
ANISOU 3311  O   TRP A 432     4948   5172   5216     77     84    227       O  
ATOM   3312  CB  TRP A 432      94.800  -6.744  28.263  1.00 22.16           C  
ANISOU 3312  CB  TRP A 432     2753   2847   2820     31     26     74       C  
ATOM   3313  CG  TRP A 432      95.682  -5.670  27.709  1.00 43.07           C  
ANISOU 3313  CG  TRP A 432     5454   5457   5455      1      1      3       C  
ATOM   3314  CD1 TRP A 432      96.234  -4.626  28.392  1.00 27.37           C  
ANISOU 3314  CD1 TRP A 432     3466   3466   3466      0      0      0       C  
ATOM   3315  CD2 TRP A 432      96.133  -5.542  26.350  1.00 42.94           C  
ANISOU 3315  CD2 TRP A 432     5439   5439   5439      0      0      0       C  
ATOM   3316  NE1 TRP A 432      97.004  -3.864  27.545  1.00 34.93           N  
ANISOU 3316  NE1 TRP A 432     4423   4423   4423      0      0      0       N  
ATOM   3317  CE2 TRP A 432      96.952  -4.398  26.286  1.00 34.30           C  
ANISOU 3317  CE2 TRP A 432     4345   4345   4345      0      0      0       C  
ATOM   3318  CE3 TRP A 432      95.919  -6.281  25.185  1.00 58.29           C  
ANISOU 3318  CE3 TRP A 432     7382   7382   7382      0      0      0       C  
ATOM   3319  CZ2 TRP A 432      97.559  -3.974  25.103  1.00 36.70           C  
ANISOU 3319  CZ2 TRP A 432     4649   4649   4649      0      0      0       C  
ATOM   3320  CZ3 TRP A 432      96.520  -5.862  24.013  1.00 54.03           C  
ANISOU 3320  CZ3 TRP A 432     6843   6843   6843      0      0      0       C  
ATOM   3321  CH2 TRP A 432      97.330  -4.716  23.981  1.00 50.78           C  
ANISOU 3321  CH2 TRP A 432     6432   6432   6432      0      0      0       C  
ATOM   3322  N   SER A 433      91.234  -7.714  28.518  1.00 43.01           N  
ANISOU 3322  N   SER A 433     5227   5513   5601    111    128    309       N  
ATOM   3323  CA  SER A 433      90.379  -8.709  29.144  1.00 35.72           C  
ANISOU 3323  CA  SER A 433     4232   4579   4760    131    165    398       C  
ATOM   3324  C   SER A 433      89.241  -9.055  28.195  1.00 43.50           C  
ANISOU 3324  C   SER A 433     5125   5526   5877    164    217    610       C  
ATOM   3325  O   SER A 433      88.231  -8.350  28.154  1.00 51.73           O  
ANISOU 3325  O   SER A 433     6182   6594   6879    155    206    494       O  
ATOM   3326  CB  SER A 433      89.822  -8.205  30.466  1.00 24.48           C  
ANISOU 3326  CB  SER A 433     2771   3160   3371    174    218    464       C  
ATOM   3327  OG  SER A 433      90.876  -7.929  31.371  1.00 47.07           O  
ANISOU 3327  OG  SER A 433     5750   5981   6155    160    192    468       O  
ATOM   3328  N   VAL A 434      89.432 -10.109  27.408  1.00 31.12           N  
ANISOU 3328  N   VAL A 434     3686   3906   4233     95    134    471       N  
ATOM   3329  CA  VAL A 434      88.516 -10.507  26.331  1.00 53.28           C  
ANISOU 3329  CA  VAL A 434     6462   6679   7101     87    131    504       C  
ATOM   3330  C   VAL A 434      88.524  -9.539  25.164  1.00 45.67           C  
ANISOU 3330  C   VAL A 434     5456   5794   6103     87    126    407       C  
ATOM   3331  O   VAL A 434      88.636  -9.939  24.007  1.00 51.04           O  
ANISOU 3331  O   VAL A 434     6155   6457   6782     66    101    372       O  
ATOM   3332  CB  VAL A 434      87.061 -10.728  26.852  1.00 58.84           C  
ANISOU 3332  CB  VAL A 434     6912   7368   8076    150    233    778       C  
ATOM   3333  CG1 VAL A 434      86.140 -11.117  25.705  1.00 71.36           C  
ANISOU 3333  CG1 VAL A 434     8609   8894   9610    125    159    674       C  
ATOM   3334  CG2 VAL A 434      87.038 -11.798  27.925  1.00 59.59           C  
ANISOU 3334  CG2 VAL A 434     7136   7418   8089    148    166    677       C  
ATOM   3335  N   SER A 435      88.419  -8.259  25.484  1.00 50.01           N  
ANISOU 3335  N   SER A 435     6100   6321   6578     97    130    441       N  
ATOM   3336  CA  SER A 435      88.585  -7.184  24.517  1.00 55.62           C  
ANISOU 3336  CA  SER A 435     6784   7100   7249     98    122    347       C  
ATOM   3337  C   SER A 435      89.746  -6.274  24.894  1.00 38.53           C  
ANISOU 3337  C   SER A 435     4734   4926   4981     83     91    298       C  
ATOM   3338  O   SER A 435      90.345  -6.426  25.955  1.00 41.64           O  
ANISOU 3338  O   SER A 435     5082   5346   5391     94    102    267       O  
ATOM   3339  CB  SER A 435      87.298  -6.378  24.374  1.00 63.62           C  
ANISOU 3339  CB  SER A 435     7828   8072   8271    115    143    454       C  
ATOM   3340  OG  SER A 435      87.132  -5.496  25.470  1.00 57.79           O  
ANISOU 3340  OG  SER A 435     7003   7396   7559    158    190    442       O  
ATOM   3341  N   TRP A 436      90.095  -5.365  23.994  1.00 41.38           N  
ANISOU 3341  N   TRP A 436     5128   5303   5292     69     67    233       N  
ATOM   3342  CA  TRP A 436      91.272  -4.518  24.167  1.00 44.11           C  
ANISOU 3342  CA  TRP A 436     5514   5651   5595     51     42    148       C  
ATOM   3343  C   TRP A 436      91.083  -3.501  25.287  1.00 45.63           C  
ANISOU 3343  C   TRP A 436     5662   5866   5811     82     70    170       C  
ATOM   3344  O   TRP A 436      91.767  -3.579  26.307  1.00 30.99           O  
ANISOU 3344  O   TRP A 436     3816   4005   3953     82     70    161       O  
ATOM   3345  CB  TRP A 436      91.574  -3.807  22.851  1.00 47.74           C  
ANISOU 3345  CB  TRP A 436     6003   6103   6035     30     20     83       C  
ATOM   3346  CG  TRP A 436      92.810  -2.981  22.858  1.00 52.83           C  
ANISOU 3346  CG  TRP A 436     6679   6707   6687      7      3     13       C  
ATOM   3347  CD1 TRP A 436      94.008  -3.304  23.421  1.00 55.68           C  
ANISOU 3347  CD1 TRP A 436     7052   7052   7052      0      0      0       C  
ATOM   3348  CD2 TRP A 436      92.995  -1.704  22.227  1.00 42.53           C  
ANISOU 3348  CD2 TRP A 436     5386   5386   5386      0      0      0       C  
ATOM   3349  NE1 TRP A 436      94.923  -2.298  23.201  1.00 47.12           N  
ANISOU 3349  NE1 TRP A 436     5967   5967   5967      0      0      0       N  
ATOM   3350  CE2 TRP A 436      94.323  -1.309  22.465  1.00 39.79           C  
ANISOU 3350  CE2 TRP A 436     5039   5039   5039      0      0      0       C  
ATOM   3351  CE3 TRP A 436      92.165  -0.855  21.485  1.00 41.29           C  
ANISOU 3351  CE3 TRP A 436     5212   5256   5221     12      4     18       C  
ATOM   3352  CZ2 TRP A 436      94.835  -0.104  21.995  1.00 38.82           C  
ANISOU 3352  CZ2 TRP A 436     4916   4916   4916      0      0      0       C  
ATOM   3353  CZ3 TRP A 436      92.684   0.341  21.012  1.00 31.74           C  
ANISOU 3353  CZ3 TRP A 436     4019   4022   4019      1      0      1       C  
ATOM   3354  CH2 TRP A 436      94.000   0.702  21.269  1.00 35.71           C  
ANISOU 3354  CH2 TRP A 436     4523   4523   4523      0      0      0       C  
ATOM   3355  N   GLN A 437      90.121  -2.592  25.129  1.00 39.42           N  
ANISOU 3355  N   GLN A 437     4848   5094   5037    110     97    217       N  
ATOM   3356  CA  GLN A 437      89.896  -1.552  26.136  1.00 41.95           C  
ANISOU 3356  CA  GLN A 437     5137   5438   5365    180    163    347       C  
ATOM   3357  C   GLN A 437      89.097  -2.042  27.334  1.00 38.00           C  
ANISOU 3357  C   GLN A 437     4667   4885   4886    171    172    375       C  
ATOM   3358  O   GLN A 437      89.314  -1.578  28.454  1.00 38.61           O  
ANISOU 3358  O   GLN A 437     4685   4988   4999    211    214    351       O  
ATOM   3359  CB  GLN A 437      89.189  -0.337  25.509  1.00 42.23           C  
ANISOU 3359  CB  GLN A 437     5165   5488   5394    204    180    373       C  
ATOM   3360  CG  GLN A 437      90.058   0.468  24.538  1.00 44.85           C  
ANISOU 3360  CG  GLN A 437     5561   5789   5692    131     88    195       C  
ATOM   3361  CD  GLN A 437      91.333   0.995  25.187  1.00 45.51           C  
ANISOU 3361  CD  GLN A 437     5701   5851   5738     91     74    157       C  
ATOM   3362  OE1 GLN A 437      91.292   1.552  26.280  1.00 37.14           O  
ANISOU 3362  OE1 GLN A 437     4597   4819   4694    166    128    240       O  
ATOM   3363  NE2 GLN A 437      92.467   0.802  24.530  1.00 27.90           N  
ANISOU 3363  NE2 GLN A 437     3485   3595   3521     54     29     71       N  
ATOM   3364  N   GLY A 438      88.194  -2.990  27.108  1.00 38.93           N  
ANISOU 3364  N   GLY A 438     4678   5031   5083    195    208    392       N  
ATOM   3365  CA  GLY A 438      87.341  -3.494  28.176  1.00 45.83           C  
ANISOU 3365  CA  GLY A 438     5583   5843   5986    214    244    533       C  
ATOM   3366  C   GLY A 438      86.068  -2.699  28.356  1.00 42.35           C  
ANISOU 3366  C   GLY A 438     5013   5454   5626    279    325    554       C  
ATOM   3367  O   GLY A 438      85.185  -3.082  29.120  1.00 45.46           O  
ANISOU 3367  O   GLY A 438     5351   5835   6086    312    380    634       O  
ATOM   3368  N   THR A 439      86.016  -1.549  27.694  1.00 38.13           N  
ANISOU 3368  N   THR A 439     4468   4926   5094    352    395    728       N  
ATOM   3369  CA  THR A 439      84.893  -0.620  27.799  1.00 45.91           C  
ANISOU 3369  CA  THR A 439     5568   5854   6023    300    340    661       C  
ATOM   3370  C   THR A 439      83.573  -1.290  27.439  1.00 43.31           C  
ANISOU 3370  C   THR A 439     5012   5562   5882    424    504    926       C  
ATOM   3371  O   THR A 439      82.544  -1.020  28.056  1.00 37.72           O  
ANISOU 3371  O   THR A 439     4405   4779   5148    407    423    847       O  
ATOM   3372  CB  THR A 439      85.072   0.588  26.845  1.00 53.24           C  
ANISOU 3372  CB  THR A 439     6523   6807   6900    293    316    611       C  
ATOM   3373  OG1 THR A 439      86.358   1.177  27.086  1.00 45.25           O  
ANISOU 3373  OG1 THR A 439     5467   5849   5876    299    307    470       O  
ATOM   3374  CG2 THR A 439      84.040   1.654  27.146  1.00 75.27           C  
ANISOU 3374  CG2 THR A 439     9299   9587   9712    341    373    685       C  
ATOM   3375  N   ASP A 440      83.596  -2.148  26.427  1.00 52.23           N  
ANISOU 3375  N   ASP A 440     6183   6713   6951    300    360    653       N  
ATOM   3376  CA  ASP A 440      82.355  -2.709  25.916  1.00 55.16           C  
ANISOU 3376  CA  ASP A 440     6574   6993   7392    328    356    836       C  
ATOM   3377  C   ASP A 440      81.992  -4.048  26.576  1.00 57.46           C  
ANISOU 3377  C   ASP A 440     6792   7250   7790    336    390    923       C  
ATOM   3378  O   ASP A 440      80.996  -4.666  26.228  1.00 58.70           O  
ANISOU 3378  O   ASP A 440     6859   7383   8063    344    427   1033       O  
ATOM   3379  CB  ASP A 440      82.415  -2.864  24.396  1.00 54.75           C  
ANISOU 3379  CB  ASP A 440     6531   6956   7315    288    313    794       C  
ATOM   3380  CG  ASP A 440      82.573  -1.539  23.688  0.70 80.32           C  
ANISOU 3380  CG  ASP A 440     9823  10228  10468    285    288    730       C  
ATOM   3381  OD1 ASP A 440      81.999  -0.538  24.170  0.70 70.11           O  
ANISOU 3381  OD1 ASP A 440     8518   8937   9182    329    330    779       O  
ATOM   3382  OD2 ASP A 440      83.250  -1.496  22.639  0.70 94.54           O  
ANISOU 3382  OD2 ASP A 440    11675  12047  12200    243    231    635       O  
ATOM   3383  N   ASN A 441      82.823  -4.511  27.505  1.00 54.21           N  
ANISOU 3383  N   ASN A 441     6413   6834   7351    329    374    878       N  
ATOM   3384  CA  ASN A 441      82.535  -5.740  28.252  1.00 55.29           C  
ANISOU 3384  CA  ASN A 441     6479   6939   7589    339    406    962       C  
ATOM   3385  C   ASN A 441      81.391  -5.590  29.236  1.00 50.93           C  
ANISOU 3385  C   ASN A 441     5840   6365   7146    403    502   1110       C  
ATOM   3386  O   ASN A 441      81.264  -4.572  29.902  1.00 49.26           O  
ANISOU 3386  O   ASN A 441     5650   6165   6902    447    545   1122       O  
ATOM   3387  CB  ASN A 441      83.766  -6.204  29.025  1.00 48.29           C  
ANISOU 3387  CB  ASN A 441     5650   6058   6638    320    366    877       C  
ATOM   3388  CG  ASN A 441      84.860  -6.716  28.117  1.00 45.88           C  
ANISOU 3388  CG  ASN A 441     5417   5763   6252    258    281    748       C  
ATOM   3389  OD1 ASN A 441      84.587  -7.276  27.054  1.00 52.60           O  
ANISOU 3389  OD1 ASN A 441     6246   6602   7139    232    265    757       O  
ATOM   3390  ND2 ASN A 441      86.107  -6.592  28.565  1.00 48.30           N  
ANISOU 3390  ND2 ASN A 441     5795   6092   6465    207    273    674       N  
ATOM   3391  N   THR A 442      80.576  -6.633  29.332  1.00 53.83           N  
ANISOU 3391  N   THR A 442     6106   6694   7651    408    536   1226       N  
ATOM   3392  CA  THR A 442      79.558  -6.760  30.375  1.00 51.69           C  
ANISOU 3392  CA  THR A 442     5742   6395   7501    465    630   1375       C  
ATOM   3393  C   THR A 442      79.828  -8.052  31.135  1.00 57.73           C  
ANISOU 3393  C   THR A 442     6461   7134   8339    456    630   1414       C  
ATOM   3394  O   THR A 442      80.709  -8.824  30.762  1.00 61.85           O  
ANISOU 3394  O   THR A 442     7021   7657   8822    405    557   1329       O  
ATOM   3395  CB  THR A 442      78.136  -6.782  29.806  1.00 51.03           C  
ANISOU 3395  CB  THR A 442     5554   6282   7551    482    678   1505       C  
ATOM   3396  OG1 THR A 442      77.991  -7.898  28.928  1.00 46.54           O  
ANISOU 3396  OG1 THR A 442     4931   5678   7072    428    628   1519       O  
ATOM   3397  CG2 THR A 442      77.857  -5.506  29.023  1.00 50.82           C  
ANISOU 3397  CG2 THR A 442     5571   6287   7453    493    680   1473       C  
ATOM   3398  N   ASN A 443      79.118  -8.257  32.233  1.00 63.19           N  
ANISOU 3398  N   ASN A 443     7073   7802   9132    508    716   1542       N  
ATOM   3399  CA  ASN A 443      79.321  -9.439  33.062  1.00 51.77           C  
ANISOU 3399  CA  ASN A 443     5574   6333   7764    506    725   1595       C  
ATOM   3400  C   ASN A 443      79.208 -10.756  32.293  1.00 56.15           C  
ANISOU 3400  C   ASN A 443     6068   6847   8419    448    664   1611       C  
ATOM   3401  O   ASN A 443      79.840 -11.751  32.649  1.00 49.91           O  
ANISOU 3401  O   ASN A 443     5273   6045   7644    423    629   1594       O  
ATOM   3402  CB  ASN A 443      78.426  -9.440  34.294  1.00 44.79           C  
ANISOU 3402  CB  ASN A 443     4601   5426   6991    576    840   1750       C  
ATOM   3403  CG  ASN A 443      78.850  -8.437  35.344  1.00 54.51           C  
ANISOU 3403  CG  ASN A 443     5897   6686   8128    634    902   1727       C  
ATOM   3404  OD1 ASN A 443      79.809  -7.694  35.167  1.00 48.41           O  
ANISOU 3404  OD1 ASN A 443     5232   5949   7211    619    852   1594       O  
ATOM   3405  ND2 ASN A 443      78.133  -8.425  36.463  1.00 56.96           N  
ANISOU 3405  ND2 ASN A 443     6138   6976   8529    702   1014   1863       N  
ATOM   3406  N   SER A 444      78.393 -10.767  31.242  1.00 51.75           N  
ANISOU 3406  N   SER A 444     5461   6261   7939    427    651   1650       N  
ATOM   3407  CA  SER A 444      78.214 -11.994  30.467  1.00 58.52           C  
ANISOU 3407  CA  SER A 444     6253   7065   8918    373    594   1671       C  
ATOM   3408  C   SER A 444      79.425 -12.381  29.612  1.00 56.34           C  
ANISOU 3408  C   SER A 444     6071   6802   8535    314    496   1518       C  
ATOM   3409  O   SER A 444      79.492 -13.491  29.082  1.00 52.76           O  
ANISOU 3409  O   SER A 444     5575   6297   8176    270    444   1520       O  
ATOM   3410  CB  SER A 444      76.976 -11.864  29.578  1.00 59.35           C  
ANISOU 3410  CB  SER A 444     6268   7128   9153    369    610   1762       C  
ATOM   3411  OG  SER A 444      77.110 -10.815  28.638  1.00 73.43           O  
ANISOU 3411  OG  SER A 444     8125   8952  10825    363    591   1681       O  
ATOM   3412  N   ASP A 445      80.366 -11.459  29.448  1.00 45.37           N  
ANISOU 3412  N   ASP A 445     4806   5473   6960    313    472   1388       N  
ATOM   3413  CA  ASP A 445      81.623 -11.746  28.745  1.00 46.26           C  
ANISOU 3413  CA  ASP A 445     5017   5604   6956    263    389   1239       C  
ATOM   3414  C   ASP A 445      82.621 -12.471  29.645  1.00 49.73           C  
ANISOU 3414  C   ASP A 445     5490   6053   7352    257    368   1195       C  
ATOM   3415  O   ASP A 445      83.694 -12.864  29.207  1.00 48.75           O  
ANISOU 3415  O   ASP A 445     5442   5940   7142    220    305   1082       O  
ATOM   3416  CB  ASP A 445      82.234 -10.452  28.213  1.00 45.07           C  
ANISOU 3416  CB  ASP A 445     4978   5511   6634    262    369   1121       C  
ATOM   3417  CG  ASP A 445      81.381  -9.813  27.131  1.00 59.39           C  
ANISOU 3417  CG  ASP A 445     6762   7320   8483    261    380   1153       C  
ATOM   3418  OD1 ASP A 445      80.801 -10.563  26.314  1.00 76.34           O  
ANISOU 3418  OD1 ASP A 445     8833   9416  10757    234    365   1206       O  
ATOM   3419  OD2 ASP A 445      81.255  -8.568  27.135  1.00 49.23           O  
ANISOU 3419  OD2 ASP A 445     5518   6074   7113    288    403   1133       O  
ATOM   3420  N   PHE A 446      82.240 -12.683  30.896  1.00 26.34           N  
ANISOU 3420  N   PHE A 446     2467   3085   4458    297    425   1294       N  
ATOM   3421  CA  PHE A 446      83.130 -13.299  31.856  1.00 29.57           C  
ANISOU 3421  CA  PHE A 446     2897   3506   4831    297    414   1269       C  
ATOM   3422  C   PHE A 446      82.445 -14.470  32.549  1.00 46.92           C  
ANISOU 3422  C   PHE A 446     4970   5652   7205    307    447   1411       C  
ATOM   3423  O   PHE A 446      82.169 -14.407  33.743  1.00 39.30           O  
ANISOU 3423  O   PHE A 446     3957   4694   6281    353    515   1500       O  
ATOM   3424  CB  PHE A 446      83.591 -12.299  32.932  1.00 40.99           C  
ANISOU 3424  CB  PHE A 446     4399   5002   6174    342    458   1243       C  
ATOM   3425  CG  PHE A 446      84.160 -11.021  32.408  1.00 48.96           C  
ANISOU 3425  CG  PHE A 446     5517   6053   7031    336    429   1118       C  
ATOM   3426  CD1 PHE A 446      85.489 -10.949  32.043  1.00 43.90           C  
ANISOU 3426  CD1 PHE A 446     4982   5442   6256    296    354    967       C  
ATOM   3427  CD2 PHE A 446      83.377  -9.883  32.297  1.00 69.12           C  
ANISOU 3427  CD2 PHE A 446     8064   8614   9583    372    478   1156       C  
ATOM   3428  CE1 PHE A 446      86.033  -9.769  31.581  1.00 50.77           C  
ANISOU 3428  CE1 PHE A 446     5944   6344   7001    286    322    856       C  
ATOM   3429  CE2 PHE A 446      83.918  -8.693  31.829  1.00 66.93           C  
ANISOU 3429  CE2 PHE A 446     7883   8372   9177    364    445   1044       C  
ATOM   3430  CZ  PHE A 446      85.244  -8.639  31.466  1.00 51.40           C  
ANISOU 3430  CZ  PHE A 446     6014   6430   7085    319    365    895       C  
ATOM   3431  N   PRO A 447      82.187 -15.555  31.803  1.00 35.46           N  
ANISOU 3431  N   PRO A 447     3461   4143   5868    265    399   1435       N  
ATOM   3432  CA  PRO A 447      81.609 -16.753  32.412  1.00 35.03           C  
ANISOU 3432  CA  PRO A 447     3284   4031   5993    266    415   1565       C  
ATOM   3433  C   PRO A 447      82.535 -17.291  33.504  1.00 34.29           C  
ANISOU 3433  C   PRO A 447     3212   3965   5852    274    413   1551       C  
ATOM   3434  O   PRO A 447      83.760 -17.271  33.347  1.00 42.70           O  
ANISOU 3434  O   PRO A 447     4381   5067   6775    251    360   1420       O  
ATOM   3435  CB  PRO A 447      81.534 -17.743  31.243  1.00 43.30           C  
ANISOU 3435  CB  PRO A 447     4301   5012   7140    210    337   1542       C  
ATOM   3436  CG  PRO A 447      82.538 -17.264  30.262  1.00 47.59           C  
ANISOU 3436  CG  PRO A 447     4973   5592   7516    181    279   1377       C  
ATOM   3437  CD  PRO A 447      82.523 -15.773  30.385  1.00 42.45           C  
ANISOU 3437  CD  PRO A 447     4393   5009   6728    214    325   1339       C  
ATOM   3438  N   ASN A 448      81.947 -17.696  34.622  1.00 40.40           N  
ANISOU 3438  N   ASN A 448     3885   4721   6744    309    479   1691       N  
ATOM   3439  CA  ASN A 448      82.685 -18.322  35.730  1.00 62.34           C  
ANISOU 3439  CA  ASN A 448     6656   7518   9512    318    487   1711       C  
ATOM   3440  C   ASN A 448      83.528 -17.350  36.560  1.00 63.27           C  
ANISOU 3440  C   ASN A 448     6865   7709   9466    355    525   1644       C  
ATOM   3441  O   ASN A 448      84.150 -17.733  37.552  1.00 46.72           O  
ANISOU 3441  O   ASN A 448     4761   5634   7357    369    543   1665       O  
ATOM   3442  CB  ASN A 448      83.535 -19.501  35.224  1.00 67.93           C  
ANISOU 3442  CB  ASN A 448     7385   8201  10225    261    391   1639       C  
ATOM   3443  CG  ASN A 448      82.698 -20.653  34.696  1.00 80.95           C  
ANISOU 3443  CG  ASN A 448     8920   9760  12077    230    357   1731       C  
ATOM   3444  OD1 ASN A 448      81.569 -20.890  35.140  1.00 77.91           O  
ANISOU 3444  OD1 ASN A 448     8413   9332  11856    253    413   1881       O  
ATOM   3445  ND2 ASN A 448      83.219 -21.320  33.669  1.00 85.01           N  
ANISOU 3445  ND2 ASN A 448     9474  10240  12586    179    267   1638       N  
ATOM   3446  N   ALA A 449      83.462 -16.074  36.200  1.00 48.67           N  
ANISOU 3446  N   ALA A 449     5089   5894   7510    374    543   1577       N  
ATOM   3447  CA  ALA A 449      84.068 -15.024  37.006  1.00 51.82           C  
ANISOU 3447  CA  ALA A 449     5561   6347   7781    416    587   1528       C  
ATOM   3448  C   ALA A 449      83.114 -14.685  38.131  1.00 57.18           C  
ANISOU 3448  C   ALA A 449     6155   7015   8555    488    710   1684       C  
ATOM   3449  O   ALA A 449      81.955 -15.101  38.115  1.00 55.01           O  
ANISOU 3449  O   ALA A 449     5775   6696   8431    503    755   1816       O  
ATOM   3450  CB  ALA A 449      84.369 -13.800  36.169  1.00 45.91           C  
ANISOU 3450  CB  ALA A 449     4919   5629   6894    406    553   1399       C  
ATOM   3451  N   THR A 450      83.592 -13.940  39.116  1.00 40.04           N  
ANISOU 3451  N   THR A 450     4030   4879   6306    537    769   1674       N  
ATOM   3452  CA  THR A 450      82.735 -13.585  40.229  1.00 52.53           C  
ANISOU 3452  CA  THR A 450     5543   6447   7970    617    901   1823       C  
ATOM   3453  C   THR A 450      82.896 -12.094  40.478  1.00 51.11           C  
ANISOU 3453  C   THR A 450     5452   6293   7675    664    949   1763       C  
ATOM   3454  O   THR A 450      84.018 -11.642  40.737  1.00 62.26           O  
ANISOU 3454  O   THR A 450     6956   7737   8963    657    918   1654       O  
ATOM   3455  CB  THR A 450      83.150 -14.354  41.500  1.00 50.45           C  
ANISOU 3455  CB  THR A 450     5231   6187   7752    645    954   1908       C  
ATOM   3456  OG1 THR A 450      83.123 -15.765  41.263  1.00 56.80           O  
ANISOU 3456  OG1 THR A 450     5955   6963   8662    595    897   1955       O  
ATOM   3457  CG2 THR A 450      82.291 -13.972  42.692  1.00 49.06           C  
ANISOU 3457  CG2 THR A 450     5011   6012   7618    695   1103   2022       C  
ATOM   3458  N   SER A 451      81.804 -11.327  40.428  1.00 42.23           N  
ANISOU 3458  N   SER A 451     4300   5150   6597    711   1024   1837       N  
ATOM   3459  CA  SER A 451      81.900  -9.896  40.724  1.00 37.35           C  
ANISOU 3459  CA  SER A 451     3763   4546   5882    760   1076   1791       C  
ATOM   3460  C   SER A 451      82.191  -9.722  42.208  1.00 41.46           C  
ANISOU 3460  C   SER A 451     4291   5067   6395    830   1184   1854       C  
ATOM   3461  O   SER A 451      81.964 -10.644  42.988  1.00 52.10           O  
ANISOU 3461  O   SER A 451     5573   6420   7803    811   1234   1929       O  
ATOM   3462  CB  SER A 451      80.619  -9.161  40.334  1.00 44.18           C  
ANISOU 3462  CB  SER A 451     4592   5389   6805    796   1136   1865       C  
ATOM   3463  OG  SER A 451      79.605  -9.337  41.310  1.00 42.78           O  
ANISOU 3463  OG  SER A 451     4324   5181   6751    869   1269   2037       O  
ATOM   3464  N   ILE A 452      82.618  -8.532  42.618  1.00 50.90           N  
ANISOU 3464  N   ILE A 452     5581   6274   7486    864   1221   1787       N  
ATOM   3465  CA  ILE A 452      82.931  -8.313  44.024  1.00 45.30           C  
ANISOU 3465  CA  ILE A 452     4911   5584   6717    876   1319   1790       C  
ATOM   3466  C   ILE A 452      81.682  -8.410  44.901  1.00 49.78           C  
ANISOU 3466  C   ILE A 452     5409   6143   7362    904   1458   1925       C  
ATOM   3467  O   ILE A 452      81.688  -9.061  45.972  1.00 37.96           O  
ANISOU 3467  O   ILE A 452     3888   4662   5874    888   1529   1980       O  
ATOM   3468  CB  ILE A 452      83.664  -6.979  44.233  1.00 43.25           C  
ANISOU 3468  CB  ILE A 452     4771   5326   6336    902   1324   1688       C  
ATOM   3469  CG1 ILE A 452      85.044  -7.004  43.570  1.00 45.28           C  
ANISOU 3469  CG1 ILE A 452     5095   5595   6516    866   1192   1556       C  
ATOM   3470  CG2 ILE A 452      83.783  -6.656  45.704  1.00 49.76           C  
ANISOU 3470  CG2 ILE A 452     5641   6162   7104    917   1441   1705       C  
ATOM   3471  CD1 ILE A 452      85.626  -5.629  43.276  1.00 46.06           C  
ANISOU 3471  CD1 ILE A 452     5298   5684   6518    877   1162   1449       C  
ATOM   3472  N   PHE A 453      80.598  -7.810  44.420  1.00 51.04           N  
ANISOU 3472  N   PHE A 453     5534   6278   7579    941   1497   1984       N  
ATOM   3473  CA  PHE A 453      79.321  -7.920  45.107  1.00 57.48           C  
ANISOU 3473  CA  PHE A 453     6273   7085   8483    968   1626   2118       C  
ATOM   3474  C   PHE A 453      78.887  -9.364  45.272  1.00 57.20           C  
ANISOU 3474  C   PHE A 453     6124   7047   8563    926   1628   2214       C  
ATOM   3475  O   PHE A 453      78.482  -9.758  46.347  1.00 54.85           O  
ANISOU 3475  O   PHE A 453     5790   6757   8295    927   1731   2298       O  
ATOM   3476  CB  PHE A 453      78.210  -7.146  44.391  1.00 55.12           C  
ANISOU 3476  CB  PHE A 453     5942   6759   8240   1008   1653   2169       C  
ATOM   3477  CG  PHE A 453      76.838  -7.467  44.917  1.00 66.29           C  
ANISOU 3477  CG  PHE A 453     7255   8162   9771   1027   1770   2317       C  
ATOM   3478  CD1 PHE A 453      76.428  -7.009  46.159  1.00 67.47           C  
ANISOU 3478  CD1 PHE A 453     7422   8317   9895   1066   1913   2373       C  
ATOM   3479  CD2 PHE A 453      75.977  -8.274  44.186  1.00 60.78           C  
ANISOU 3479  CD2 PHE A 453     6442   7444   9210   1000   1738   2400       C  
ATOM   3480  CE1 PHE A 453      75.180  -7.333  46.651  1.00 59.65           C  
ANISOU 3480  CE1 PHE A 453     6336   7316   9014   1081   2023   2512       C  
ATOM   3481  CE2 PHE A 453      74.727  -8.599  44.671  1.00 58.72           C  
ANISOU 3481  CE2 PHE A 453     6078   7168   9063   1012   1845   2537       C  
ATOM   3482  CZ  PHE A 453      74.327  -8.126  45.905  1.00 67.01           C  
ANISOU 3482  CZ  PHE A 453     7146   8228  10087   1054   1988   2595       C  
ATOM   3483  N   SER A 454      79.001 -10.154  44.211  1.00 38.65           N  
ANISOU 3483  N   SER A 454     3723   4684   6279    885   1512   2202       N  
ATOM   3484  CA  SER A 454      78.548 -11.538  44.246  1.00 43.75           C  
ANISOU 3484  CA  SER A 454     4255   5315   7054    841   1502   2295       C  
ATOM   3485  C   SER A 454      79.295 -12.370  45.301  1.00 51.89           C  
ANISOU 3485  C   SER A 454     5291   6370   8053    809   1524   2298       C  
ATOM   3486  O   SER A 454      78.698 -13.191  45.997  1.00 58.04           O  
ANISOU 3486  O   SER A 454     5988   7143   8923    791   1592   2408       O  
ATOM   3487  CB  SER A 454      78.685 -12.168  42.853  1.00 46.88           C  
ANISOU 3487  CB  SER A 454     4615   5685   7511    802   1363   2262       C  
ATOM   3488  OG  SER A 454      78.415 -13.555  42.872  1.00 58.34           O  
ANISOU 3488  OG  SER A 454     5965   7115   9088    754   1339   2339       O  
ATOM   3489  N   GLY A 455      80.600 -12.153  45.409  1.00 55.24           N  
ANISOU 3489  N   GLY A 455     5814   6823   8353    798   1465   2179       N  
ATOM   3490  CA  GLY A 455      81.418 -12.801  46.417  1.00 39.71           C  
ANISOU 3490  CA  GLY A 455     3870   4883   6333    765   1484   2170       C  
ATOM   3491  C   GLY A 455      80.992 -12.411  47.820  1.00 54.06           C  
ANISOU 3491  C   GLY A 455     5709   6716   8115    789   1637   2239       C  
ATOM   3492  O   GLY A 455      80.800 -13.275  48.712  1.00 66.64           O  
ANISOU 3492  O   GLY A 455     7254   8315   9750    761   1700   2327       O  
ATOM   3493  N   LEU A 456      80.804 -11.098  48.010  1.00 53.46           N  
ANISOU 3493  N   LEU A 456     5707   6642   7965    842   1699   2205       N  
ATOM   3494  CA  LEU A 456      80.350 -10.622  49.313  1.00 60.64           C  
ANISOU 3494  CA  LEU A 456     6646   7559   8834    871   1849   2269       C  
ATOM   3495  C   LEU A 456      78.988 -11.209  49.662  1.00 66.22           C  
ANISOU 3495  C   LEU A 456     7236   8249   9676    877   1946   2427       C  
ATOM   3496  O   LEU A 456      78.768 -11.612  50.799  1.00 59.47           O  
ANISOU 3496  O   LEU A 456     6370   7405   8820    868   2048   2507       O  
ATOM   3497  CB  LEU A 456      80.254  -9.098  49.348  1.00 42.05           C  
ANISOU 3497  CB  LEU A 456     4383   5199   6397    930   1897   2214       C  
ATOM   3498  CG  LEU A 456      81.539  -8.285  49.263  1.00 58.71           C  
ANISOU 3498  CG  LEU A 456     6620   7320   8367    928   1831   2065       C  
ATOM   3499  CD1 LEU A 456      81.244  -6.817  48.928  1.00 56.58           C  
ANISOU 3499  CD1 LEU A 456     6414   7027   8055    986   1856   2023       C  
ATOM   3500  CD2 LEU A 456      82.280  -8.424  50.577  1.00 51.91           C  
ANISOU 3500  CD2 LEU A 456     5831   6485   7408    906   1892   2051       C  
ATOM   3501  N   GLN A 457      78.078 -11.230  48.698  1.00 46.24           N  
ANISOU 3501  N   GLN A 457     4622   5689   7258    891   1917   2474       N  
ATOM   3502  CA  GLN A 457      76.719 -11.691  48.916  1.00 49.67           C  
ANISOU 3502  CA  GLN A 457     4938   6101   7832    897   2005   2622       C  
ATOM   3503  C   GLN A 457      76.757 -13.170  49.296  1.00 63.34           C  
ANISOU 3503  C   GLN A 457     6585   7829   9651    837   1993   2699       C  
ATOM   3504  O   GLN A 457      76.009 -13.615  50.164  1.00 46.21           O  
ANISOU 3504  O   GLN A 457     4354   5656   7548    834   2103   2820       O  
ATOM   3505  CB  GLN A 457      75.865 -11.470  47.668  1.00 67.52           C  
ANISOU 3505  CB  GLN A 457     7131   8330  10196    912   1953   2644       C  
ATOM   3506  CG  GLN A 457      74.509 -12.137  47.712  1.00 79.13           C  
ANISOU 3506  CG  GLN A 457     8463   9771  11834    904   2018   2796       C  
ATOM   3507  CD  GLN A 457      73.743 -11.967  46.416  1.00 68.32           C  
ANISOU 3507  CD  GLN A 457     7029   8369  10561    908   1954   2810       C  
ATOM   3508  OE1 GLN A 457      74.204 -12.382  45.355  1.00 68.04           O  
ANISOU 3508  OE1 GLN A 457     6988   8320  10545    873   1821   2748       O  
ATOM   3509  NE2 GLN A 457      72.589 -11.321  46.489  1.00 65.93           N  
ANISOU 3509  NE2 GLN A 457     6683   8053  10313    951   2049   2892       N  
ATOM   3510  N   SER A 458      77.602 -13.929  48.598  1.00 67.69           N  
ANISOU 3510  N   SER A 458     7130   8379  10209    790   1859   2632       N  
ATOM   3511  CA  SER A 458      77.765 -15.351  48.870  1.00 56.84           C  
ANISOU 3511  CA  SER A 458     5682   6997   8918    729   1830   2694       C  
ATOM   3512  C   SER A 458      78.199 -15.606  50.309  1.00 66.24           C  
ANISOU 3512  C   SER A 458     6919   8218  10031    714   1925   2727       C  
ATOM   3513  O   SER A 458      77.585 -16.413  51.030  1.00 65.26           O  
ANISOU 3513  O   SER A 458     6718   8083   9995    689   2001   2852       O  
ATOM   3514  CB  SER A 458      78.779 -15.952  47.903  1.00 46.44           C  
ANISOU 3514  CB  SER A 458     4376   5676   7592    688   1668   2595       C  
ATOM   3515  OG  SER A 458      78.967 -17.334  48.162  1.00 70.11           O  
ANISOU 3515  OG  SER A 458     7303   8660  10674    630   1636   2655       O  
ATOM   3516  N   GLN A 459      79.172 -14.829  50.780  1.00 67.81           N  
ANISOU 3516  N   GLN A 459     7247   8453  10065    729   1932   2624       N  
ATOM   3517  CA  GLN A 459      79.680 -15.087  52.127  1.00 69.04           C  
ANISOU 3517  CA  GLN A 459     7460   8637  10134    707   2013   2649       C  
ATOM   3518  C   GLN A 459      78.739 -14.555  53.196  1.00 69.81           C  
ANISOU 3518  C   GLN A 459     7563   8738  10225    746   2181   2750       C  
ATOM   3519  O   GLN A 459      78.633 -15.142  54.274  1.00 69.51           O  
ANISOU 3519  O   GLN A 459     7518   8710  10184    722   2268   2838       O  
ATOM   3520  CB  GLN A 459      81.101 -14.547  52.307  1.00 49.86           C  
ANISOU 3520  CB  GLN A 459     5167   6243   7536    700   1957   2506       C  
ATOM   3521  CG  GLN A 459      82.101 -15.250  51.403  1.00 61.51           C  
ANISOU 3521  CG  GLN A 459     6635   7719   9016    654   1800   2418       C  
ATOM   3522  CD  GLN A 459      83.536 -14.937  51.764  1.00 63.34           C  
ANISOU 3522  CD  GLN A 459     6989   7986   9090    634   1754   2295       C  
ATOM   3523  OE1 GLN A 459      83.825 -14.447  52.857  1.00 61.09           O  
ANISOU 3523  OE1 GLN A 459     6790   7723   8698    640   1841   2292       O  
ATOM   3524  NE2 GLN A 459      84.453 -15.327  50.895  1.00 60.05           N  
ANISOU 3524  NE2 GLN A 459     6579   7573   8664    605   1616   2201       N  
ATOM   3525  N   VAL A 460      78.091 -13.434  52.921  1.00 72.72           N  
ANISOU 3525  N   VAL A 460     7949   9097  10585    807   2228   2739       N  
ATOM   3526  CA  VAL A 460      77.147 -12.855  53.866  1.00 75.94           C  
ANISOU 3526  CA  VAL A 460     8360   9504  10989    852   2390   2833       C  
ATOM   3527  C   VAL A 460      75.944 -13.797  54.006  1.00 73.50           C  
ANISOU 3527  C   VAL A 460     7908   9170  10848    835   2453   2995       C  
ATOM   3528  O   VAL A 460      75.441 -14.005  55.112  1.00 81.21           O  
ANISOU 3528  O   VAL A 460     8874  10154  11829    837   2582   3100       O  
ATOM   3529  CB  VAL A 460      76.704 -11.457  53.429  1.00 75.17           C  
ANISOU 3529  CB  VAL A 460     8307   9396  10857    921   2417   2786       C  
ATOM   3530  CG1 VAL A 460      75.501 -11.009  54.218  1.00 72.33           C  
ANISOU 3530  CG1 VAL A 460     7918   9028  10534    968   2580   2906       C  
ATOM   3531  CG2 VAL A 460      77.847 -10.475  53.629  1.00 89.02           C  
ANISOU 3531  CG2 VAL A 460    10213  11171  12441    937   2387   2645       C  
ATOM   3532  N   THR A 461      75.500 -14.378  52.890  1.00 72.67           N  
ANISOU 3532  N   THR A 461     7695   9034  10882    816   2361   3016       N  
ATOM   3533  CA  THR A 461      74.386 -15.331  52.909  1.00 74.37           C  
ANISOU 3533  CA  THR A 461     7765   9218  11275    792   2404   3165       C  
ATOM   3534  C   THR A 461      74.730 -16.576  53.701  1.00 70.80           C  
ANISOU 3534  C   THR A 461     7282   8769  10851    730   2418   3234       C  
ATOM   3535  O   THR A 461      73.933 -17.047  54.519  1.00 56.38           O  
ANISOU 3535  O   THR A 461     5392   6933   9098    722   2532   3369       O  
ATOM   3536  CB  THR A 461      73.962 -15.734  51.477  1.00 76.03           C  
ANISOU 3536  CB  THR A 461     7875   9389  11625    775   2283   3160       C  
ATOM   3537  OG1 THR A 461      73.326 -14.623  50.831  1.00 66.31           O  
ANISOU 3537  OG1 THR A 461     6653   8148  10392    833   2298   3136       O  
ATOM   3538  CG2 THR A 461      72.980 -16.886  51.520  1.00 73.09           C  
ANISOU 3538  CG2 THR A 461     7352   8976  11442    735   2310   3307       C  
ATOM   3539  N   LYS A 462      75.925 -17.105  53.461  1.00 60.95           N  
ANISOU 3539  N   LYS A 462     6081   7533   9543    686   2304   3144       N  
ATOM   3540  CA  LYS A 462      76.373 -18.253  54.233  1.00 54.42           C  
ANISOU 3540  CA  LYS A 462     5239   6710   8728    625   2312   3203       C  
ATOM   3541  C   LYS A 462      76.436 -17.941  55.733  1.00 61.51           C  
ANISOU 3541  C   LYS A 462     6218   7640   9511    636   2459   3254       C  
ATOM   3542  O   LYS A 462      76.234 -18.828  56.561  1.00 60.29           O  
ANISOU 3542  O   LYS A 462     6025   7481   9401    596   2522   3365       O  
ATOM   3543  CB  LYS A 462      77.738 -18.750  53.736  1.00 85.02           C  
ANISOU 3543  CB  LYS A 462     9166  10598  12541    580   2166   3087       C  
ATOM   3544  CG  LYS A 462      77.691 -19.497  52.408  1.00 91.56           C  
ANISOU 3544  CG  LYS A 462     9898  11386  13506    551   2022   3067       C  
ATOM   3545  CD  LYS A 462      79.085 -19.924  51.961  1.00 93.46           C  
ANISOU 3545  CD  LYS A 462    10197  11642  13672    512   1884   2949       C  
ATOM   3546  CE  LYS A 462      79.032 -20.751  50.679  1.00 92.70           C  
ANISOU 3546  CE  LYS A 462    10006  11500  13714    481   1743   2937       C  
ATOM   3547  NZ  LYS A 462      78.234 -20.104  49.604  1.00 99.19           N  
ANISOU 3547  NZ  LYS A 462    10788  12297  14604    522   1713   2920       N  
ATOM   3548  N   ALA A 463      76.719 -16.686  56.081  1.00 75.79           N  
ANISOU 3548  N   ALA A 463     8144   9479  11172    688   2511   3176       N  
ATOM   3549  CA  ALA A 463      76.837 -16.305  57.489  1.00 78.25           C  
ANISOU 3549  CA  ALA A 463     8549   9822  11362    700   2645   3213       C  
ATOM   3550  C   ALA A 463      75.537 -15.800  58.122  1.00 77.96           C  
ANISOU 3550  C   ALA A 463     8475   9776  11370    751   2807   3331       C  
ATOM   3551  O   ALA A 463      75.531 -15.421  59.295  1.00 75.93           O  
ANISOU 3551  O   ALA A 463     8295   9542  11011    768   2928   3368       O  
ATOM   3552  CB  ALA A 463      77.930 -15.264  57.650  1.00 68.77           C  
ANISOU 3552  CB  ALA A 463     7503   8654   9973    723   2617   3065       C  
ATOM   3553  N   GLY A 464      74.458 -15.733  57.347  1.00 70.68           N  
ANISOU 3553  N   GLY A 464     7441   8822  10593    777   2808   3386       N  
ATOM   3554  CA  GLY A 464      73.190 -15.267  57.891  1.00 67.46           C  
ANISOU 3554  CA  GLY A 464     6988   8404  10239    825   2960   3502       C  
ATOM   3555  C   GLY A 464      73.019 -13.764  58.050  1.00 80.38           C  
ANISOU 3555  C   GLY A 464     8719  10054  11767    902   3031   3443       C  
ATOM   3556  O   GLY A 464      72.114 -13.304  58.748  1.00 86.71           O  
ANISOU 3556  O   GLY A 464     9511  10856  12581    945   3176   3534       O  
ATOM   3557  N   GLY A 465      73.874 -12.998  57.387  1.00 65.17           N  
ANISOU 3557  N   GLY A 465     6881   8136   9743    919   2931   3292       N  
ATOM   3558  CA  GLY A 465      73.789 -11.546  57.359  1.00 67.74           C  
ANISOU 3558  CA  GLY A 465     7297   8466   9976    988   2975   3222       C  
ATOM   3559  C   GLY A 465      72.813 -11.034  56.323  1.00 72.58           C  
ANISOU 3559  C   GLY A 465     7829   9048  10702   1031   2958   3241       C  
ATOM   3560  O   GLY A 465      72.070 -11.815  55.726  1.00 78.44           O  
ANISOU 3560  O   GLY A 465     8438   9766  11600   1008   2929   3324       O  
ATOM   3561  N   LYS A 466      72.836  -9.728  56.076  1.00 72.11           N  
ANISOU 3561  N   LYS A 466     7849   8985  10564   1091   2970   3164       N  
ATOM   3562  CA  LYS A 466      71.945  -9.153  55.084  1.00 69.69           C  
ANISOU 3562  CA  LYS A 466     7478   8651  10352   1132   2953   3180       C  
ATOM   3563  C   LYS A 466      72.748  -8.284  54.135  1.00 70.07           C  
ANISOU 3563  C   LYS A 466     7612   8696  10318   1149   2833   3029       C  
ATOM   3564  O   LYS A 466      73.616  -7.527  54.571  1.00 66.14           O  
ANISOU 3564  O   LYS A 466     7244   8212   9676   1165   2835   2931       O  
ATOM   3565  CB  LYS A 466      70.882  -8.270  55.745  1.00 70.99           C  
ANISOU 3565  CB  LYS A 466     7646   8808  10521   1201   3116   3265       C  
ATOM   3566  CG  LYS A 466      69.857  -8.872  56.668  0.50 77.66           C  
ANISOU 3566  CG  LYS A 466     8403   9652  11451   1200   3260   3427       C  
ATOM   3567  CD  LYS A 466      68.989  -9.896  55.998  0.50 85.95           C  
ANISOU 3567  CD  LYS A 466     9288  10679  12691   1164   3226   3531       C  
ATOM   3568  CE  LYS A 466      68.056 -10.502  57.020  0.50 92.97           C  
ANISOU 3568  CE  LYS A 466    10098  11568  13660   1160   3375   3693       C  
ATOM   3569  NZ  LYS A 466      67.194  -9.432  57.613  0.50101.79           N  
ANISOU 3569  NZ  LYS A 466    11243  12684  14750   1236   3529   3748       N  
ATOM   3570  N   ILE A 467      72.463  -8.391  52.838  1.00 62.51           N  
ANISOU 3570  N   ILE A 467     6582   7716   9451   1143   2727   3012       N  
ATOM   3571  CA  ILE A 467      73.224  -7.615  51.866  1.00 79.95           C  
ANISOU 3571  CA  ILE A 467     8870   9922  11586   1154   2608   2873       C  
ATOM   3572  C   ILE A 467      72.299  -7.050  50.782  1.00 76.90           C  
ANISOU 3572  C   ILE A 467     8424   9508  11288   1189   2585   2899       C  
ATOM   3573  O   ILE A 467      71.335  -7.710  50.374  1.00 69.47           O  
ANISOU 3573  O   ILE A 467     7356   8550  10489   1174   2592   3001       O  
ATOM   3574  CB  ILE A 467      74.387  -8.442  51.256  1.00 80.93           C  
ANISOU 3574  CB  ILE A 467     9006  10057  11688   1090   2453   2779       C  
ATOM   3575  CG1 ILE A 467      75.441  -7.531  50.636  1.00 71.54           C  
ANISOU 3575  CG1 ILE A 467     7933   8872  10378   1102   2354   2623       C  
ATOM   3576  CG2 ILE A 467      73.880  -9.496  50.282  1.00 65.24           C  
ANISOU 3576  CG2 ILE A 467     6886   8051   9852   1048   2367   2835       C  
ATOM   3577  CD1 ILE A 467      76.732  -8.248  50.331  1.00 54.94           C  
ANISOU 3577  CD1 ILE A 467     5864   6787   8224   1044   2224   2525       C  
ATOM   3578  N   THR A 468      72.619  -5.851  50.298  1.00 63.88           N  
ANISOU 3578  N   THR A 468     6866   7851   9555   1229   2554   2806       N  
ATOM   3579  CA  THR A 468      71.818  -5.174  49.278  1.00 73.28           C  
ANISOU 3579  CA  THR A 468     8018   9017  10808   1264   2533   2824       C  
ATOM   3580  C   THR A 468      72.749  -4.548  48.245  1.00 75.75           C  
ANISOU 3580  C   THR A 468     8416   9327  11039   1259   2396   2684       C  
ATOM   3581  O   THR A 468      73.760  -3.944  48.614  1.00 75.10           O  
ANISOU 3581  O   THR A 468     8452   9253  10829   1267   2379   2581       O  
ATOM   3582  CB  THR A 468      70.945  -4.080  49.916  1.00 71.64           C  
ANISOU 3582  CB  THR A 468     7835   8798  10586   1336   2681   2886       C  
ATOM   3583  OG1 THR A 468      69.946  -4.700  50.731  1.00 84.63           O  
ANISOU 3583  OG1 THR A 468     9385  10445  12325   1339   2806   3028       O  
ATOM   3584  CG2 THR A 468      70.248  -3.239  48.860  1.00 73.27           C  
ANISOU 3584  CG2 THR A 468     8021   8982  10837   1373   2655   2892       C  
ATOM   3585  N   LEU A 469      72.406  -4.659  46.965  1.00 69.99           N  
ANISOU 3585  N   LEU A 469     7628   8583  10381   1244   2301   2683       N  
ATOM   3586  CA  LEU A 469      73.174  -3.990  45.920  1.00 69.28           C  
ANISOU 3586  CA  LEU A 469     7618   8490  10217   1241   2178   2562       C  
ATOM   3587  C   LEU A 469      72.457  -2.743  45.409  1.00 75.77           C  
ANISOU 3587  C   LEU A 469     8460   9291  11036   1297   2215   2577       C  
ATOM   3588  O   LEU A 469      71.316  -2.811  44.955  1.00 80.13           O  
ANISOU 3588  O   LEU A 469     8920   9832  11695   1307   2247   2673       O  
ATOM   3589  CB  LEU A 469      73.417  -4.937  44.746  1.00 55.23           C  
ANISOU 3589  CB  LEU A 469     5777   6709   8498   1180   2035   2537       C  
ATOM   3590  CG  LEU A 469      74.034  -4.266  43.519  1.00 59.32           C  
ANISOU 3590  CG  LEU A 469     6365   7222   8950   1175   1911   2429       C  
ATOM   3591  CD1 LEU A 469      75.465  -3.817  43.805  1.00 53.02           C  
ANISOU 3591  CD1 LEU A 469     5695   6438   8011   1172   1859   2294       C  
ATOM   3592  CD2 LEU A 469      73.974  -5.173  42.306  1.00 59.69           C  
ANISOU 3592  CD2 LEU A 469     6342   7263   9074   1117   1789   2429       C  
ATOM   3593  N   SER A 470      73.142  -1.607  45.467  1.00 83.16           N  
ANISOU 3593  N   SER A 470     9518  10223  11856   1329   2207   2483       N  
ATOM   3594  CA  SER A 470      72.631  -0.373  44.878  1.00 82.05           C  
ANISOU 3594  CA  SER A 470     9411  10062  11704   1379   2224   2484       C  
ATOM   3595  C   SER A 470      73.790   0.544  44.516  1.00 67.50           C  
ANISOU 3595  C   SER A 470     7698   8213   9738   1382   2142   2347       C  
ATOM   3596  O   SER A 470      74.381   1.168  45.392  1.00 57.33           O  
ANISOU 3596  O   SER A 470     6503   6917   8361   1405   2195   2296       O  
ATOM   3597  CB  SER A 470      71.669   0.336  45.836  1.00 79.61           C  
ANISOU 3597  CB  SER A 470     9097   9739  11412   1444   2391   2576       C  
ATOM   3598  OG  SER A 470      71.359   1.641  45.387  1.00 60.50           O  
ANISOU 3598  OG  SER A 470     6730   7296   8960   1495   2410   2562       O  
ATOM   3599  N   GLU A 471      74.121   0.597  43.226  1.00 61.19           N  
ANISOU 3599  N   GLU A 471     6904   7414   8933   1353   2014   2289       N  
ATOM   3600  CA  GLU A 471      75.245   1.393  42.736  1.00 67.47           C  
ANISOU 3600  CA  GLU A 471     7813   8202   9621   1347   1922   2161       C  
ATOM   3601  C   GLU A 471      75.180   2.829  43.232  1.00 70.98           C  
ANISOU 3601  C   GLU A 471     8347   8619  10003   1409   2006   2146       C  
ATOM   3602  O   GLU A 471      76.204   3.450  43.521  1.00 54.87           O  
ANISOU 3602  O   GLU A 471     6411   6567   7868   1408   1979   2048       O  
ATOM   3603  CB  GLU A 471      75.336   1.362  41.207  1.00 69.93           C  
ANISOU 3603  CB  GLU A 471     8110   8530   9929   1293   1785   2105       C  
ATOM   3604  CG  GLU A 471      75.656  -0.010  40.622  1.00 67.40           C  
ANISOU 3604  CG  GLU A 471     7728   8238   9644   1214   1680   2082       C  
ATOM   3605  CD  GLU A 471      75.715   0.006  39.104  0.70 70.86           C  
ANISOU 3605  CD  GLU A 471     8165   8710  10051   1132   1548   1996       C  
ATOM   3606  OE1 GLU A 471      75.656  -1.082  38.491  0.70 65.52           O  
ANISOU 3606  OE1 GLU A 471     7424   8045   9425   1074   1478   2002       O  
ATOM   3607  OE2 GLU A 471      75.876   1.105  38.526  0.70 62.69           O  
ANISOU 3607  OE2 GLU A 471     7197   7685   8937   1125   1514   1920       O  
ATOM   3608  N   SER A 472      73.963   3.351  43.301  1.00 72.45           N  
ANISOU 3608  N   SER A 472     8488   8792  10248   1459   2106   2247       N  
ATOM   3609  CA  SER A 472      73.726   4.732  43.677  1.00 53.06           C  
ANISOU 3609  CA  SER A 472     6109   6305   7748   1523   2192   2249       C  
ATOM   3610  C   SER A 472      73.575   4.962  45.184  1.00 65.28           C  
ANISOU 3610  C   SER A 472     7692   7842   9270   1562   2337   2283       C  
ATOM   3611  O   SER A 472      73.363   6.093  45.621  1.00 78.54           O  
ANISOU 3611  O   SER A 472     9439   9492  10912   1616   2421   2288       O  
ATOM   3612  CB  SER A 472      72.505   5.263  42.929  1.00 70.87           C  
ANISOU 3612  CB  SER A 472     8303   8551  10072   1560   2226   2338       C  
ATOM   3613  OG  SER A 472      71.340   4.560  43.334  1.00 82.62           O  
ANISOU 3613  OG  SER A 472     9677  10050  11665   1570   2318   2464       O  
ATOM   3614  N   GLY A 473      73.740   3.908  45.979  1.00 64.24           N  
ANISOU 3614  N   GLY A 473     7522   7735   9153   1532   2364   2303       N  
ATOM   3615  CA  GLY A 473      73.701   4.039  47.429  1.00 61.29           C  
ANISOU 3615  CA  GLY A 473     7189   7357   8740   1559   2497   2331       C  
ATOM   3616  C   GLY A 473      72.320   4.120  48.059  1.00 73.35           C  
ANISOU 3616  C   GLY A 473     8647   8881  10343   1611   2651   2469       C  
ATOM   3617  O   GLY A 473      72.185   4.532  49.212  1.00 61.60           O  
ANISOU 3617  O   GLY A 473     7209   7383   8813   1646   2775   2494       O  
ATOM   3618  N   GLU A 474      71.302   3.673  47.327  1.00 80.11           N  
ANISOU 3618  N   GLU A 474     9385   9743  11309   1610   2644   2559       N  
ATOM   3619  CA  GLU A 474      69.928   3.631  47.827  1.00 71.23           C  
ANISOU 3619  CA  GLU A 474     8175   8616  10275   1653   2783   2699       C  
ATOM   3620  C   GLU A 474      69.791   2.490  48.836  1.00 74.12           C  
ANISOU 3620  C   GLU A 474     8480   9006  10677   1626   2851   2763       C  
ATOM   3621  O   GLU A 474      70.403   1.440  48.658  1.00 77.38           O  
ANISOU 3621  O   GLU A 474     8861   9440  11098   1564   2761   2730       O  
ATOM   3622  CB  GLU A 474      68.947   3.399  46.668  1.00 63.33           C  
ANISOU 3622  CB  GLU A 474     7058   7616   9388   1648   2740   2774       C  
ATOM   3623  CG  GLU A 474      68.854   4.478  45.604  0.70 60.77           C  
ANISOU 3623  CG  GLU A 474     6775   7272   9043   1674   2684   2738       C  
ATOM   3624  CD  GLU A 474      68.234   5.753  46.085  0.70 85.97           C  
ANISOU 3624  CD  GLU A 474    10016  10435  12212   1752   2810   2779       C  
ATOM   3625  OE1 GLU A 474      67.260   5.676  46.859  0.70 98.95           O  
ANISOU 3625  OE1 GLU A 474    11602  12079  13915   1789   2947   2887       O  
ATOM   3626  OE2 GLU A 474      68.689   6.834  45.654  0.70 88.82           O  
ANISOU 3626  OE2 GLU A 474    10471  10774  12501   1777   2773   2708       O  
ATOM   3627  N   TYR A 475      69.020   2.684  49.905  1.00 84.51           N  
ANISOU 3627  N   TYR A 475     9783  10318  12009   1670   3010   2855       N  
ATOM   3628  CA  TYR A 475      68.772   1.566  50.817  1.00 88.43           C  
ANISOU 3628  CA  TYR A 475    10210  10838  12549   1642   3080   2933       C  
ATOM   3629  C   TYR A 475      67.388   1.615  51.465  1.00 86.63           C  
ANISOU 3629  C   TYR A 475     9901  10606  12409   1688   3242   3082       C  
ATOM   3630  O   TYR A 475      66.787   2.681  51.584  1.00 79.30           O  
ANISOU 3630  O   TYR A 475     9006   9656  11470   1753   3330   3111       O  
ATOM   3631  CB  TYR A 475      69.862   1.509  51.897  1.00 88.78           C  
ANISOU 3631  CB  TYR A 475    10365  10896  12471   1625   3101   2858       C  
ATOM   3632  CG  TYR A 475      70.005   2.747  52.767  1.00 83.42           C  
ANISOU 3632  CG  TYR A 475     9811  10196  11687   1683   3208   2828       C  
ATOM   3633  CD1 TYR A 475      69.254   2.898  53.924  1.00 76.13           C  
ANISOU 3633  CD1 TYR A 475     8884   9274  10767   1724   3377   2924       C  
ATOM   3634  CD2 TYR A 475      70.869   3.774  52.412  1.00 86.46           C  
ANISOU 3634  CD2 TYR A 475    10316  10559  11975   1695   3141   2707       C  
ATOM   3635  CE1 TYR A 475      69.383   4.020  54.723  1.00 83.96           C  
ANISOU 3635  CE1 TYR A 475     9994  10245  11661   1776   3477   2897       C  
ATOM   3636  CE2 TYR A 475      71.000   4.910  53.196  1.00 83.77           C  
ANISOU 3636  CE2 TYR A 475    10092  10193  11545   1744   3237   2680       C  
ATOM   3637  CZ  TYR A 475      70.256   5.028  54.352  1.00 89.46           C  
ANISOU 3637  CZ  TYR A 475    10811  10915  12265   1785   3405   2774       C  
ATOM   3638  OH  TYR A 475      70.390   6.151  55.134  1.00 88.78           O  
ANISOU 3638  OH  TYR A 475    10843  10801  12087   1833   3502   2747       O  
ATOM   3639  N   THR A 476      66.930   0.469  51.962  1.00 88.41           N  
ANISOU 3639  N   THR A 476    10026  10850  12714   1656   3288   3175       N  
ATOM   3640  CA  THR A 476      65.656   0.399  52.668  1.00 82.58           C  
ANISOU 3640  CA  THR A 476     9205  10109  12062   1693   3448   3321       C  
ATOM   3641  C   THR A 476      65.851   0.321  54.163  1.00 89.62           C  
ANISOU 3641  C   THR A 476    10157  11015  12878   1706   3577   3347       C  
ATOM   3642  O   THR A 476      65.345   1.156  54.909  1.00 86.74           O  
ANISOU 3642  O   THR A 476     9840  10640  12478   1767   3715   3390       O  
ATOM   3643  CB  THR A 476      64.849  -0.844  52.226  1.00 84.75           C  
ANISOU 3643  CB  THR A 476     9311  10391  12497   1646   3425   3430       C  
ATOM   3644  OG1 THR A 476      64.506  -0.736  50.839  1.00 85.49           O  
ANISOU 3644  OG1 THR A 476     9344  10473  12667   1636   3317   3420       O  
ATOM   3645  CG2 THR A 476      63.572  -0.958  53.024  1.00 99.72           C  
ANISOU 3645  CG2 THR A 476    11119  12286  14484   1681   3593   3584       C  
ATOM   3646  N   SER A 477      66.633  -0.661  54.588  1.00 88.41           N  
ANISOU 3646  N   SER A 477    10011  10886  12694   1646   3531   3319       N  
ATOM   3647  CA  SER A 477      67.015  -0.799  55.982  1.00 90.70           C  
ANISOU 3647  CA  SER A 477    10374  11195  12894   1645   3636   3329       C  
ATOM   3648  C   SER A 477      68.401  -0.200  56.131  1.00 86.84           C  
ANISOU 3648  C   SER A 477    10042  10709  12246   1636   3564   3176       C  
ATOM   3649  O   SER A 477      69.323  -0.599  55.411  1.00 92.93           O  
ANISOU 3649  O   SER A 477    10827  11486  12996   1586   3414   3080       O  
ATOM   3650  CB  SER A 477      67.022  -2.269  56.405  1.00 93.56           C  
ANISOU 3650  CB  SER A 477    10648  11582  13319   1580   3634   3400       C  
ATOM   3651  OG  SER A 477      65.808  -2.913  56.050  1.00 90.24           O  
ANISOU 3651  OG  SER A 477    10069  11154  13063   1576   3670   3533       O  
ATOM   3652  N   LYS A 478      68.546   0.780  57.023  1.00 64.77           N  
ANISOU 3652  N   LYS A 478     7362   7904   9342   1684   3668   3153       N  
ATOM   3653  CA  LYS A 478      69.839   1.431  57.200  1.00 66.93           C  
ANISOU 3653  CA  LYS A 478     7787   8174   9469   1675   3605   3009       C  
ATOM   3654  C   LYS A 478      70.858   0.355  57.587  1.00 76.54           C  
ANISOU 3654  C   LYS A 478     9019   9427  10637   1600   3534   2965       C  
ATOM   3655  O   LYS A 478      70.686  -0.334  58.592  1.00 75.80           O  
ANISOU 3655  O   LYS A 478     8907   9357  10535   1582   3624   3041       O  
ATOM   3656  CB  LYS A 478      69.758   2.536  58.257  1.00 71.46           C  
ANISOU 3656  CB  LYS A 478     8478   8733   9941   1733   3744   3007       C  
ATOM   3657  CG  LYS A 478      70.957   3.464  58.329  1.00 66.91           C  
ANISOU 3657  CG  LYS A 478     8058   8140   9226   1732   3684   2862       C  
ATOM   3658  CD  LYS A 478      70.689   4.601  59.299  1.00 72.36           C  
ANISOU 3658  CD  LYS A 478     8853   8807   9833   1795   3830   2874       C  
ATOM   3659  CE  LYS A 478      71.382   5.881  58.877  1.00 78.02           C  
ANISOU 3659  CE  LYS A 478     9691   9483  10471   1818   3771   2753       C  
ATOM   3660  NZ  LYS A 478      71.151   6.982  59.856  1.00 88.31           N  
ANISOU 3660  NZ  LYS A 478    11102  10759  11692   1876   3914   2764       N  
ATOM   3661  N   PRO A 479      71.963   0.271  56.833  1.00 64.41           N  
ANISOU 3661  N   PRO A 479     7525   7891   9057   1557   3376   2840       N  
ATOM   3662  CA  PRO A 479      72.951  -0.793  57.010  1.00 59.40           C  
ANISOU 3662  CA  PRO A 479     6894   7289   8386   1483   3290   2794       C  
ATOM   3663  C   PRO A 479      73.917  -0.515  58.150  1.00 64.48           C  
ANISOU 3663  C   PRO A 479     7673   7948   8880   1469   3331   2731       C  
ATOM   3664  O   PRO A 479      74.054   0.642  58.559  1.00 59.25           O  
ANISOU 3664  O   PRO A 479     7117   7264   8131   1513   3389   2686       O  
ATOM   3665  CB  PRO A 479      73.696  -0.780  55.679  1.00 62.00           C  
ANISOU 3665  CB  PRO A 479     7223   7609   8726   1453   3112   2683       C  
ATOM   3666  CG  PRO A 479      73.640   0.642  55.246  1.00 56.96           C  
ANISOU 3666  CG  PRO A 479     6661   6934   8047   1509   3114   2623       C  
ATOM   3667  CD  PRO A 479      72.320   1.179  55.727  1.00 63.81           C  
ANISOU 3667  CD  PRO A 479     7492   7786   8966   1575   3270   2741       C  
ATOM   3668  N   ASP A 480      74.583  -1.559  58.647  1.00 52.57           N  
ANISOU 3668  N   ASP A 480     6160   6473   7340   1407   3300   2729       N  
ATOM   3669  CA  ASP A 480      75.641  -1.377  59.632  1.00 72.33           C  
ANISOU 3669  CA  ASP A 480     8792   8994   9695   1382   3316   2659       C  
ATOM   3670  C   ASP A 480      76.879  -0.767  58.997  1.00 75.45           C  
ANISOU 3670  C   ASP A 480     9281   9376  10009   1362   3179   2500       C  
ATOM   3671  O   ASP A 480      77.641  -0.054  59.658  1.00 77.79           O  
ANISOU 3671  O   ASP A 480     9705   9670  10182   1363   3198   2426       O  
ATOM   3672  CB  ASP A 480      76.012  -2.726  60.252  1.00 71.21           C  
ANISOU 3672  CB  ASP A 480     8615   8893   9549   1316   3311   2707       C  
ATOM   3673  CG  ASP A 480      74.846  -3.379  60.958  1.00 78.22           C  
ANISOU 3673  CG  ASP A 480     9412   9793  10516   1329   3449   2869       C  
ATOM   3674  OD1 ASP A 480      74.045  -2.658  61.586  1.00 85.18           O  
ANISOU 3674  OD1 ASP A 480    10316  10662  11385   1387   3588   2933       O  
ATOM   3675  OD2 ASP A 480      74.737  -4.621  60.901  1.00 89.57           O  
ANISOU 3675  OD2 ASP A 480    10755  11249  12028   1279   3420   2936       O  
ATOM   3676  N   VAL A 481      77.087  -1.055  57.715  1.00 74.72           N  
ANISOU 3676  N   VAL A 481     9126   9276   9988   1341   3041   2450       N  
ATOM   3677  CA  VAL A 481      78.259  -0.538  57.023  1.00 68.34           C  
ANISOU 3677  CA  VAL A 481     8398   8456   9114   1318   2906   2303       C  
ATOM   3678  C   VAL A 481      77.997  -0.599  55.513  1.00 66.55           C  
ANISOU 3678  C   VAL A 481     8088   8212   8987   1321   2789   2281       C  
ATOM   3679  O   VAL A 481      77.289  -1.490  55.006  1.00 60.68           O  
ANISOU 3679  O   VAL A 481     7222   7478   8356   1310   2773   2361       O  
ATOM   3680  CB  VAL A 481      79.532  -1.343  57.387  1.00 55.98           C  
ANISOU 3680  CB  VAL A 481     6874   6925   7472   1245   2825   2234       C  
ATOM   3681  CG1 VAL A 481      79.395  -2.805  56.972  1.00 49.22           C  
ANISOU 3681  CG1 VAL A 481     5897   6096   6708   1196   2765   2291       C  
ATOM   3682  CG2 VAL A 481      80.766  -0.733  56.750  1.00 60.79           C  
ANISOU 3682  CG2 VAL A 481     7569   7519   8010   1223   2695   2083       C  
ATOM   3683  N   ALA A 482      78.596   0.336  54.788  1.00 62.52           N  
ANISOU 3683  N   ALA A 482     7647   7674   8434   1332   2706   2173       N  
ATOM   3684  CA  ALA A 482      78.517   0.331  53.341  1.00 58.59           C  
ANISOU 3684  CA  ALA A 482     7090   7162   8010   1329   2584   2139       C  
ATOM   3685  C   ALA A 482      79.895   0.088  52.733  1.00 59.98           C  
ANISOU 3685  C   ALA A 482     7311   7347   8131   1272   2430   2009       C  
ATOM   3686  O   ALA A 482      80.852   0.813  53.020  1.00 75.07           O  
ANISOU 3686  O   ALA A 482     9334   9247   9944   1264   2405   1912       O  
ATOM   3687  CB  ALA A 482      77.944   1.651  52.845  1.00 46.40           C  
ANISOU 3687  CB  ALA A 482     5579   5575   6475   1392   2614   2134       C  
ATOM   3688  N   ILE A 483      79.974  -0.925  51.872  1.00 63.59           N  
ANISOU 3688  N   ILE A 483     7680   7824   8659   1233   2327   2011       N  
ATOM   3689  CA  ILE A 483      81.150  -1.186  51.066  1.00 56.93           C  
ANISOU 3689  CA  ILE A 483     6862   6988   7782   1183   2173   1896       C  
ATOM   3690  C   ILE A 483      80.929  -0.591  49.679  1.00 62.01           C  
ANISOU 3690  C   ILE A 483     7488   7605   8470   1204   2084   1860       C  
ATOM   3691  O   ILE A 483      80.041  -1.023  48.934  1.00 58.43           O  
ANISOU 3691  O   ILE A 483     6936   7151   8115   1213   2070   1931       O  
ATOM   3692  CB  ILE A 483      81.395  -2.697  50.931  1.00 54.57           C  
ANISOU 3692  CB  ILE A 483     6480   6725   7532   1126   2110   1921       C  
ATOM   3693  CG1 ILE A 483      81.623  -3.327  52.307  1.00 47.40           C  
ANISOU 3693  CG1 ILE A 483     5589   5844   6575   1101   2197   1965       C  
ATOM   3694  CG2 ILE A 483      82.546  -2.982  49.977  1.00 51.89           C  
ANISOU 3694  CG2 ILE A 483     6159   6392   7165   1079   1949   1805       C  
ATOM   3695  CD1 ILE A 483      81.725  -4.842  52.271  1.00 47.57           C  
ANISOU 3695  CD1 ILE A 483     5522   5896   6656   1046   2153   2011       C  
ATOM   3696  N   VAL A 484      81.757   0.391  49.332  1.00 53.54           N  
ANISOU 3696  N   VAL A 484     6511   6508   7324   1206   2023   1753       N  
ATOM   3697  CA  VAL A 484      81.579   1.139  48.096  1.00 46.29           C  
ANISOU 3697  CA  VAL A 484     5593   5562   6432   1227   1950   1720       C  
ATOM   3698  C   VAL A 484      82.703   0.829  47.132  1.00 59.64           C  
ANISOU 3698  C   VAL A 484     7301   7262   8098   1174   1790   1612       C  
ATOM   3699  O   VAL A 484      83.869   1.102  47.419  1.00 52.31           O  
ANISOU 3699  O   VAL A 484     6455   6331   7089   1145   1745   1515       O  
ATOM   3700  CB  VAL A 484      81.517   2.646  48.354  1.00 65.90           C  
ANISOU 3700  CB  VAL A 484     8171   8003   8863   1275   2011   1694       C  
ATOM   3701  CG1 VAL A 484      81.224   3.374  47.051  1.00 65.35           C  
ANISOU 3701  CG1 VAL A 484     8095   7907   8828   1296   1940   1677       C  
ATOM   3702  CG2 VAL A 484      80.434   2.954  49.356  1.00 65.17           C  
ANISOU 3702  CG2 VAL A 484     8069   7903   8790   1328   2175   1799       C  
ATOM   3703  N   VAL A 485      82.351   0.229  46.004  1.00 56.80           N  
ANISOU 3703  N   VAL A 485     6862   6913   7808   1160   1707   1632       N  
ATOM   3704  CA  VAL A 485      83.334  -0.197  45.040  1.00 53.11           C  
ANISOU 3704  CA  VAL A 485     6401   6457   7322   1110   1558   1540       C  
ATOM   3705  C   VAL A 485      83.360   0.776  43.880  1.00 51.56           C  
ANISOU 3705  C   VAL A 485     6239   6241   7111   1113   1482   1486       C  
ATOM   3706  O   VAL A 485      82.394   0.858  43.121  1.00 39.89           O  
ANISOU 3706  O   VAL A 485     4705   4772   5680   1110   1475   1529       O  
ATOM   3707  CB  VAL A 485      83.044  -1.614  44.505  1.00 47.42           C  
ANISOU 3707  CB  VAL A 485     5575   5765   6677   1075   1501   1588       C  
ATOM   3708  CG1 VAL A 485      84.209  -2.131  43.685  1.00 46.10           C  
ANISOU 3708  CG1 VAL A 485     5427   5615   6475   1018   1353   1485       C  
ATOM   3709  CG2 VAL A 485      82.727  -2.555  45.648  1.00 51.63           C  
ANISOU 3709  CG2 VAL A 485     6058   6321   7238   1066   1592   1665       C  
ATOM   3710  N   ILE A 486      84.464   1.513  43.761  1.00 54.77           N  
ANISOU 3710  N   ILE A 486     6736   6645   7428   1072   1412   1361       N  
ATOM   3711  CA  ILE A 486      84.598   2.594  42.787  1.00 42.28           C  
ANISOU 3711  CA  ILE A 486     5197   5070   5797   1028   1332   1271       C  
ATOM   3712  C   ILE A 486      85.968   2.506  42.146  1.00 49.77           C  
ANISOU 3712  C   ILE A 486     6187   6050   6675    932   1182   1124       C  
ATOM   3713  O   ILE A 486      86.848   1.785  42.626  1.00 43.55           O  
ANISOU 3713  O   ILE A 486     5409   5268   5868    911   1157   1092       O  
ATOM   3714  CB  ILE A 486      84.482   3.962  43.473  1.00 50.05           C  
ANISOU 3714  CB  ILE A 486     6260   6004   6754   1091   1429   1285       C  
ATOM   3715  CG1 ILE A 486      85.527   4.091  44.580  1.00 43.11           C  
ANISOU 3715  CG1 ILE A 486     5462   5091   5826   1108   1469   1249       C  
ATOM   3716  CG2 ILE A 486      83.124   4.134  44.095  1.00 48.34           C  
ANISOU 3716  CG2 ILE A 486     6008   5754   6607   1189   1583   1430       C  
ATOM   3717  CD1 ILE A 486      85.656   5.490  45.118  1.00 43.57           C  
ANISOU 3717  CD1 ILE A 486     5616   5096   5844   1149   1540   1234       C  
ATOM   3718  N   GLY A 487      86.154   3.223  41.043  1.00 39.35           N  
ANISOU 3718  N   GLY A 487     4887   4748   5318    875   1084   1039       N  
ATOM   3719  CA  GLY A 487      87.452   3.226  40.416  1.00 42.48           C  
ANISOU 3719  CA  GLY A 487     5319   5170   5653    784    946    904       C  
ATOM   3720  C   GLY A 487      87.488   3.703  38.984  1.00 47.32           C  
ANISOU 3720  C   GLY A 487     5928   5812   6238    716    831    826       C  
ATOM   3721  O   GLY A 487      86.504   4.200  38.444  1.00 47.38           O  
ANISOU 3721  O   GLY A 487     5914   5819   6268    740    859    871       O  
ATOM   3722  N   GLU A 488      88.645   3.510  38.362  1.00 43.35           N  
ANISOU 3722  N   GLU A 488     5446   5335   5691    630    704    711       N  
ATOM   3723  CA  GLU A 488      88.821   3.850  36.970  1.00 43.05           C  
ANISOU 3723  CA  GLU A 488     5407   5324   5624    558    591    629       C  
ATOM   3724  C   GLU A 488      88.016   2.892  36.109  1.00 38.60           C  
ANISOU 3724  C   GLU A 488     4790   4788   5087    543    564    658       C  
ATOM   3725  O   GLU A 488      87.785   1.746  36.488  1.00 29.31           O  
ANISOU 3725  O   GLU A 488     3576   3617   3944    557    591    706       O  
ATOM   3726  CB  GLU A 488      90.289   3.709  36.561  1.00 34.49           C  
ANISOU 3726  CB  GLU A 488     4313   4283   4507    492    502    486       C  
ATOM   3727  CG  GLU A 488      91.270   4.600  37.306  1.00 55.40           C  
ANISOU 3727  CG  GLU A 488     7036   6899   7113    581    691    615       C  
ATOM   3728  CD  GLU A 488      92.661   4.556  36.702  1.00 52.84           C  
ANISOU 3728  CD  GLU A 488     6727   6598   6750    497    577    507       C  
ATOM   3729  OE1 GLU A 488      93.331   3.510  36.822  1.00 45.90           O  
ANISOU 3729  OE1 GLU A 488     5841   5774   5824    318    420    378       O  
ATOM   3730  OE2 GLU A 488      93.094   5.581  36.131  1.00 55.09           O  
ANISOU 3730  OE2 GLU A 488     7036   6884   7013    472    543    462       O  
ATOM   3731  N   GLU A 489      87.600   3.374  34.946  1.00 38.36           N  
ANISOU 3731  N   GLU A 489     4694   4809   5070    628    738    808       N  
ATOM   3732  CA  GLU A 489      87.031   2.541  33.898  1.00 42.12           C  
ANISOU 3732  CA  GLU A 489     5114   5318   5571    597    696    824       C  
ATOM   3733  C   GLU A 489      88.170   1.771  33.243  1.00 39.53           C  
ANISOU 3733  C   GLU A 489     4876   5025   5120    351    467    577       C  
ATOM   3734  O   GLU A 489      89.337   2.131  33.392  1.00 33.94           O  
ANISOU 3734  O   GLU A 489     4141   4311   4444    481    534    637       O  
ATOM   3735  CB  GLU A 489      86.332   3.420  32.854  1.00 35.77           C  
ANISOU 3735  CB  GLU A 489     4385   4538   4666    412    556    669       C  
ATOM   3736  CG  GLU A 489      85.193   4.184  33.499  1.00 40.84           C  
ANISOU 3736  CG  GLU A 489     5013   5095   5411    573    583    754       C  
ATOM   3737  CD  GLU A 489      84.042   3.258  33.899  1.00 55.94           C  
ANISOU 3737  CD  GLU A 489     6855   7001   7397    627    672    879       C  
ATOM   3738  OE1 GLU A 489      83.938   2.131  33.353  1.00 59.78           O  
ANISOU 3738  OE1 GLU A 489     7306   7505   7901    591    629    878       O  
ATOM   3739  OE2 GLU A 489      83.302   3.620  34.841  1.00 56.86           O  
ANISOU 3739  OE2 GLU A 489     6952   7090   7560    705    788    981       O  
ATOM   3740  N   PRO A 490      87.845   0.668  32.561  1.00 31.69           N  
ANISOU 3740  N   PRO A 490     3763   4047   4231    484    549    733       N  
ATOM   3741  CA  PRO A 490      88.936  -0.096  31.954  1.00 39.80           C  
ANISOU 3741  CA  PRO A 490     4895   5050   5177    328    313    507       C  
ATOM   3742  C   PRO A 490      89.579   0.626  30.768  1.00 41.41           C  
ANISOU 3742  C   PRO A 490     5122   5304   5309    245    298    428       C  
ATOM   3743  O   PRO A 490      88.890   1.356  30.050  1.00 39.68           O  
ANISOU 3743  O   PRO A 490     4898   5091   5089    256    308    446       O  
ATOM   3744  CB  PRO A 490      88.241  -1.378  31.467  1.00 32.32           C  
ANISOU 3744  CB  PRO A 490     3839   4175   4267    292    376    501       C  
ATOM   3745  CG  PRO A 490      86.790  -1.025  31.383  1.00 32.06           C  
ANISOU 3745  CG  PRO A 490     3760   4140   4281    331    438    582       C  
ATOM   3746  CD  PRO A 490      86.549  -0.018  32.448  1.00 37.98           C  
ANISOU 3746  CD  PRO A 490     4608   4786   5035    412    420    672       C  
ATOM   3747  N   TYR A 491      90.883   0.431  30.581  1.00 38.39           N  
ANISOU 3747  N   TYR A 491     4709   4942   4935    298    295    433       N  
ATOM   3748  CA  TYR A 491      91.599   1.036  29.466  1.00 31.30           C  
ANISOU 3748  CA  TYR A 491     3843   4054   3994    241    221    338       C  
ATOM   3749  C   TYR A 491      92.843   0.216  29.124  1.00 38.17           C  
ANISOU 3749  C   TYR A 491     4775   4901   4827    118    114    190       C  
ATOM   3750  O   TYR A 491      93.351  -0.532  29.963  1.00 30.22           O  
ANISOU 3750  O   TYR A 491     3769   3889   3825    115    115    189       O  
ATOM   3751  CB  TYR A 491      92.016   2.470  29.806  1.00 30.95           C  
ANISOU 3751  CB  TYR A 491     3833   3977   3949    213    169    236       C  
ATOM   3752  CG  TYR A 491      92.784   2.586  31.110  1.00 41.20           C  
ANISOU 3752  CG  TYR A 491     5148   5258   5249    222    183    233       C  
ATOM   3753  CD1 TYR A 491      94.142   2.295  31.161  1.00 20.47           C  
ANISOU 3753  CD1 TYR A 491     2542   2629   2605    169    133    171       C  
ATOM   3754  CD2 TYR A 491      92.150   2.962  32.289  1.00 31.18           C  
ANISOU 3754  CD2 TYR A 491     3877   3968   4003    284    250    294       C  
ATOM   3755  CE1 TYR A 491      94.852   2.389  32.337  1.00 26.94           C  
ANISOU 3755  CE1 TYR A 491     3395   3445   3398    149    158    186       C  
ATOM   3756  CE2 TYR A 491      92.851   3.060  33.477  1.00 30.36           C  
ANISOU 3756  CE2 TYR A 491     3821   3862   3850    244    291    317       C  
ATOM   3757  CZ  TYR A 491      94.203   2.769  33.496  1.00 32.70           C  
ANISOU 3757  CZ  TYR A 491     4110   4156   4157    289    289    313       C  
ATOM   3758  OH  TYR A 491      94.915   2.857  34.674  1.00 33.19           O  
ANISOU 3758  OH  TYR A 491     4198   4194   4217    301    312    310       O  
ATOM   3759  N   ALA A 492      93.398   0.462  27.942  1.00 37.41           N  
ANISOU 3759  N   ALA A 492     4696   4799   4721     79     67    124       N  
ATOM   3760  CA  ALA A 492      94.653  -0.158  27.516  1.00 42.27           C  
ANISOU 3760  CA  ALA A 492     5335   5385   5341     30     22     46       C  
ATOM   3761  C   ALA A 492      95.459   0.831  26.672  1.00 34.24           C  
ANISOU 3761  C   ALA A 492     4336   4336   4336      0      0      0       C  
ATOM   3762  O   ALA A 492      94.893   1.599  25.895  1.00 38.02           O  
ANISOU 3762  O   ALA A 492     4812   4821   4813      5      3      6       O  
ATOM   3763  CB  ALA A 492      94.378  -1.409  26.714  1.00 19.44           C  
ANISOU 3763  CB  ALA A 492     2437   2495   2453     27     17     43       C  
ATOM   3764  N   GLU A 493      96.778   0.794  26.828  1.00 27.28           N  
ANISOU 3764  N   GLU A 493     3455   3455   3455      0      0      0       N  
ATOM   3765  CA  GLU A 493      97.698   1.612  26.036  1.00 29.96           C  
ANISOU 3765  CA  GLU A 493     3794   3794   3794      0      0      0       C  
ATOM   3766  C   GLU A 493      97.362   3.116  26.144  1.00 33.35           C  
ANISOU 3766  C   GLU A 493     4223   4223   4223      0      0      0       C  
ATOM   3767  O   GLU A 493      96.966   3.602  27.210  1.00 26.10           O  
ANISOU 3767  O   GLU A 493     3306   3306   3306      0      0      0       O  
ATOM   3768  CB  GLU A 493      97.756   1.136  24.575  1.00 27.48           C  
ANISOU 3768  CB  GLU A 493     3481   3481   3481      0      0      0       C  
ATOM   3769  CG  GLU A 493      98.097  -0.353  24.445  1.00 23.12           C  
ANISOU 3769  CG  GLU A 493     2928   2928   2928      0      0      0       C  
ATOM   3770  CD  GLU A 493      98.292  -0.794  23.015  1.00 36.02           C  
ANISOU 3770  CD  GLU A 493     4562   4562   4562      0      0      0       C  
ATOM   3771  OE1 GLU A 493      97.554  -1.704  22.572  1.00 46.40           O  
ANISOU 3771  OE1 GLU A 493     5877   5877   5877      0      0      0       O  
ATOM   3772  OE2 GLU A 493      99.248  -0.311  22.372  1.00 49.51           O  
ANISOU 3772  OE2 GLU A 493     6271   6271   6271      0      0      0       O  
ATOM   3773  N   TRP A 494      97.544   3.857  25.059  1.00 18.93           N  
ANISOU 3773  N   TRP A 494     2398   2398   2398      0      0      0       N  
ATOM   3774  CA  TRP A 494      97.470   5.314  25.161  1.00 39.63           C  
ANISOU 3774  CA  TRP A 494     5020   5020   5020      0      0      0       C  
ATOM   3775  C   TRP A 494      96.098   5.830  25.597  1.00 40.32           C  
ANISOU 3775  C   TRP A 494     5106   5106   5106      0      0      0       C  
ATOM   3776  O   TRP A 494      96.012   6.929  26.123  1.00 41.47           O  
ANISOU 3776  O   TRP A 494     5247   5263   5247     17      8     13       O  
ATOM   3777  CB  TRP A 494      97.925   5.982  23.872  1.00 33.20           C  
ANISOU 3777  CB  TRP A 494     4205   4205   4205      0      0      0       C  
ATOM   3778  CG  TRP A 494      97.010   5.758  22.726  1.00 42.36           C  
ANISOU 3778  CG  TRP A 494     5366   5366   5366      0      0      0       C  
ATOM   3779  CD1 TRP A 494      95.961   6.532  22.348  1.00 25.13           C  
ANISOU 3779  CD1 TRP A 494     3183   3183   3183      0      0      0       C  
ATOM   3780  CD2 TRP A 494      97.058   4.663  21.807  1.00 31.49           C  
ANISOU 3780  CD2 TRP A 494     3989   3989   3989      0      0      0       C  
ATOM   3781  NE1 TRP A 494      95.355   5.995  21.235  1.00 38.82           N  
ANISOU 3781  NE1 TRP A 494     4917   4917   4917      0      0      0       N  
ATOM   3782  CE2 TRP A 494      96.006   4.844  20.886  1.00 22.46           C  
ANISOU 3782  CE2 TRP A 494     2844   2844   2844      0      0      0       C  
ATOM   3783  CE3 TRP A 494      97.897   3.556  21.664  1.00 28.86           C  
ANISOU 3783  CE3 TRP A 494     3656   3656   3656      0      0      0       C  
ATOM   3784  CZ2 TRP A 494      95.761   3.953  19.843  1.00 28.25           C  
ANISOU 3784  CZ2 TRP A 494     3578   3578   3578      0      0      0       C  
ATOM   3785  CZ3 TRP A 494      97.655   2.670  20.626  1.00 32.64           C  
ANISOU 3785  CZ3 TRP A 494     4134   4134   4134      0      0      0       C  
ATOM   3786  CH2 TRP A 494      96.595   2.875  19.727  1.00 39.00           C  
ANISOU 3786  CH2 TRP A 494     4939   4939   4939      0      0      0       C  
ATOM   3787  N   PHE A 495      95.044   5.025  25.429  1.00 33.44           N  
ANISOU 3787  N   PHE A 495     4229   4249   4226     15      8     16       N  
ATOM   3788  CA  PHE A 495      93.706   5.407  25.895  1.00 31.17           C  
ANISOU 3788  CA  PHE A 495     3911   4016   3915    101     63    104       C  
ATOM   3789  C   PHE A 495      93.716   5.720  27.380  1.00 33.86           C  
ANISOU 3789  C   PHE A 495     4268   4344   4254    106     86    123       C  
ATOM   3790  O   PHE A 495      92.853   6.437  27.880  1.00 37.60           O  
ANISOU 3790  O   PHE A 495     4718   4814   4753    181    127    166       O  
ATOM   3791  CB  PHE A 495      92.687   4.307  25.646  1.00 26.68           C  
ANISOU 3791  CB  PHE A 495     3327   3448   3363    102     60    105       C  
ATOM   3792  CG  PHE A 495      92.171   4.263  24.241  1.00 31.24           C  
ANISOU 3792  CG  PHE A 495     3919   4034   3918     79     53    103       C  
ATOM   3793  CD1 PHE A 495      90.811   4.331  23.993  1.00 50.27           C  
ANISOU 3793  CD1 PHE A 495     6283   6471   6348    135     79    152       C  
ATOM   3794  CD2 PHE A 495      93.033   4.083  23.174  1.00 35.80           C  
ANISOU 3794  CD2 PHE A 495     4504   4591   4508     46     22     51       C  
ATOM   3795  CE1 PHE A 495      90.317   4.277  22.703  1.00 57.20           C  
ANISOU 3795  CE1 PHE A 495     7155   7360   7218    126     69    145       C  
ATOM   3796  CE2 PHE A 495      92.548   4.016  21.881  1.00 35.56           C  
ANISOU 3796  CE2 PHE A 495     4484   4550   4478     30     14     36       C  
ATOM   3797  CZ  PHE A 495      91.185   4.112  21.644  1.00 45.24           C  
ANISOU 3797  CZ  PHE A 495     5662   5848   5678     92     45    110       C  
ATOM   3798  N   GLY A 496      94.668   5.143  28.096  1.00 38.20           N  
ANISOU 3798  N   GLY A 496     4824   4881   4810     83     67     94       N  
ATOM   3799  CA  GLY A 496      94.743   5.343  29.527  1.00 28.99           C  
ANISOU 3799  CA  GLY A 496     3663   3711   3642    116    106    130       C  
ATOM   3800  C   GLY A 496      95.741   6.409  29.935  1.00 31.75           C  
ANISOU 3800  C   GLY A 496     4013   4040   4011    122     88     99       C  
ATOM   3801  O   GLY A 496      95.897   6.667  31.128  1.00 36.13           O  
ANISOU 3801  O   GLY A 496     4589   4589   4551    187    166    166       O  
ATOM   3802  N   ASP A 497      96.398   7.050  28.968  1.00 26.11           N  
ANISOU 3802  N   ASP A 497     3304   3334   3284     94     70     81       N  
ATOM   3803  CA  ASP A 497      97.317   8.131  29.314  1.00 32.33           C  
ANISOU 3803  CA  ASP A 497     4102   4108   4073     58     50     52       C  
ATOM   3804  C   ASP A 497      96.492   9.273  29.909  1.00 42.23           C  
ANISOU 3804  C   ASP A 497     5365   5348   5334    136    105     98       C  
ATOM   3805  O   ASP A 497      95.426   9.636  29.410  1.00 31.79           O  
ANISOU 3805  O   ASP A 497     4052   4040   3988    207    178    173       O  
ATOM   3806  CB  ASP A 497      98.050   8.675  28.081  1.00 32.08           C  
ANISOU 3806  CB  ASP A 497     4063   4066   4061     11      7      8       C  
ATOM   3807  CG  ASP A 497      99.179   7.776  27.621  1.00 46.25           C  
ANISOU 3807  CG  ASP A 497     5858   5858   5858      0      0      0       C  
ATOM   3808  OD1 ASP A 497      99.340   6.676  28.193  1.00 33.60           O  
ANISOU 3808  OD1 ASP A 497     4256   4256   4256      0      0      0       O  
ATOM   3809  OD2 ASP A 497      99.973   8.230  26.764  1.00 36.44           O  
ANISOU 3809  OD2 ASP A 497     4615   4615   4615      0      0      0       O  
ATOM   3810  N   ILE A 498      96.980   9.817  31.011  1.00 28.98           N  
ANISOU 3810  N   ILE A 498     3716   3665   3630    135    144    119       N  
ATOM   3811  CA  ILE A 498      96.310  10.931  31.642  1.00 33.78           C  
ANISOU 3811  CA  ILE A 498     4354   4253   4228    187    215    165       C  
ATOM   3812  C   ILE A 498      97.308  12.054  31.883  1.00 40.25           C  
ANISOU 3812  C   ILE A 498     5191   5058   5044    176    212    147       C  
ATOM   3813  O   ILE A 498      98.520  11.848  31.788  1.00 36.41           O  
ANISOU 3813  O   ILE A 498     4689   4579   4566    133    159    106       O  
ATOM   3814  CB  ILE A 498      95.678  10.523  32.981  1.00 38.56           C  
ANISOU 3814  CB  ILE A 498     4981   4839   4833    231    285    211       C  
ATOM   3815  CG1 ILE A 498      96.726   9.830  33.853  1.00 42.30           C  
ANISOU 3815  CG1 ILE A 498     5458   5305   5307    208    265    185       C  
ATOM   3816  CG2 ILE A 498      94.486   9.595  32.757  1.00 32.18           C  
ANISOU 3816  CG2 ILE A 498     4137   4010   4079    298    279    226       C  
ATOM   3817  CD1 ILE A 498      96.215   9.434  35.206  1.00 39.28           C  
ANISOU 3817  CD1 ILE A 498     5093   4856   4976    294    307    208       C  
ATOM   3818  N   GLU A 499      96.793  13.245  32.154  1.00 37.67           N  
ANISOU 3818  N   GLU A 499     4895   4711   4707    215    270    178       N  
ATOM   3819  CA  GLU A 499      97.629  14.396  32.462  1.00 42.81           C  
ANISOU 3819  CA  GLU A 499     5566   5301   5397    245    257    153       C  
ATOM   3820  C   GLU A 499      97.440  14.819  33.917  1.00 33.17           C  
ANISOU 3820  C   GLU A 499     4399   4028   4177    290    330    181       C  
ATOM   3821  O   GLU A 499      98.339  15.416  34.506  1.00 39.04           O  
ANISOU 3821  O   GLU A 499     5171   4748   4915    278    337    167       O  
ATOM   3822  CB  GLU A 499      97.328  15.542  31.501  1.00 41.90           C  
ANISOU 3822  CB  GLU A 499     5451   5189   5279    253    259    158       C  
ATOM   3823  CG  GLU A 499      97.653  15.133  30.060  1.00 41.11           C  
ANISOU 3823  CG  GLU A 499     5304   5136   5179    202    187    125       C  
ATOM   3824  CD  GLU A 499      97.311  16.200  29.043  0.50 62.99           C  
ANISOU 3824  CD  GLU A 499     8074   7912   7946    212    190    131       C  
ATOM   3825  OE1 GLU A 499      96.708  17.223  29.433  0.50 74.73           O  
ANISOU 3825  OE1 GLU A 499     9594   9368   9430    263    248    163       O  
ATOM   3826  OE2 GLU A 499      97.642  16.016  27.852  0.50 66.10           O  
ANISOU 3826  OE2 GLU A 499     8462   8339   8313    205    188    140       O  
ATOM   3827  N   LEU A 500      96.289  14.481  34.502  1.00 31.08           N  
ANISOU 3827  N   LEU A 500     4150   3805   3855    293    422    241       N  
ATOM   3828  CA  LEU A 500      95.988  14.879  35.876  1.00 42.84           C  
ANISOU 3828  CA  LEU A 500     5690   5178   5410    390    465    251       C  
ATOM   3829  C   LEU A 500      95.889  13.637  36.766  1.00 47.59           C  
ANISOU 3829  C   LEU A 500     6287   5775   6018    398    476    260       C  
ATOM   3830  O   LEU A 500      95.354  12.613  36.355  1.00 43.48           O  
ANISOU 3830  O   LEU A 500     5726   5287   5506    397    455    268       O  
ATOM   3831  CB  LEU A 500      94.652  15.639  35.923  1.00 39.93           C  
ANISOU 3831  CB  LEU A 500     5340   4782   5050    454    536    300       C  
ATOM   3832  CG  LEU A 500      94.503  16.857  35.015  1.00 45.15           C  
ANISOU 3832  CG  LEU A 500     6092   5417   5646    553    729    409       C  
ATOM   3833  CD1 LEU A 500      93.143  17.494  35.206  1.00 34.39           C  
ANISOU 3833  CD1 LEU A 500     4659   4053   4354    527    612    354       C  
ATOM   3834  CD2 LEU A 500      95.611  17.859  35.330  1.00 23.77           C  
ANISOU 3834  CD2 LEU A 500     3335   2798   2899    371    581    297       C  
ATOM   3835  N   LEU A 501      96.431  13.729  37.979  1.00 33.94           N  
ANISOU 3835  N   LEU A 501     4604   4008   4285    404    510    258       N  
ATOM   3836  CA  LEU A 501      96.421  12.596  38.905  1.00 42.61           C  
ANISOU 3836  CA  LEU A 501     5795   5065   5331    500    716    364       C  
ATOM   3837  C   LEU A 501      95.162  12.467  39.750  1.00 52.10           C  
ANISOU 3837  C   LEU A 501     6925   6265   6603    485    609    322       C  
ATOM   3838  O   LEU A 501      94.902  11.418  40.331  1.00 47.82           O  
ANISOU 3838  O   LEU A 501     6390   5715   6063    494    627    368       O  
ATOM   3839  CB  LEU A 501      97.639  12.647  39.829  1.00 33.86           C  
ANISOU 3839  CB  LEU A 501     4634   3966   4267    386    521    238       C  
ATOM   3840  CG  LEU A 501      98.992  12.289  39.236  1.00 38.24           C  
ANISOU 3840  CG  LEU A 501     5154   4561   4814    316    436    189       C  
ATOM   3841  CD1 LEU A 501     100.048  12.260  40.313  1.00 34.36           C  
ANISOU 3841  CD1 LEU A 501     4801   4000   4253    361    607    233       C  
ATOM   3842  CD2 LEU A 501      98.894  10.938  38.563  1.00 25.82           C  
ANISOU 3842  CD2 LEU A 501     3518   3104   3188    250    415    195       C  
ATOM   3843  N   GLU A 502      94.384  13.534  39.833  1.00 46.42           N  
ANISOU 3843  N   GLU A 502     6252   5503   5881    517    664    382       N  
ATOM   3844  CA  GLU A 502      93.172  13.488  40.641  1.00 51.41           C  
ANISOU 3844  CA  GLU A 502     6921   6093   6520    613    803    467       C  
ATOM   3845  C   GLU A 502      92.106  12.592  40.042  1.00 39.88           C  
ANISOU 3845  C   GLU A 502     5398   4671   5084    634    798    507       C  
ATOM   3846  O   GLU A 502      91.788  12.695  38.858  1.00 34.16           O  
ANISOU 3846  O   GLU A 502     4625   3988   4368    600    721    488       O  
ATOM   3847  CB  GLU A 502      92.616  14.894  40.923  1.00 30.17           C  
ANISOU 3847  CB  GLU A 502     4289   3350   3823    667    896    506       C  
ATOM   3848  CG  GLU A 502      91.294  14.883  41.662  1.00 52.73           C  
ANISOU 3848  CG  GLU A 502     7175   6166   6694    769   1043    601       C  
ATOM   3849  CD  GLU A 502      90.892  16.241  42.190  1.00 58.53           C  
ANISOU 3849  CD  GLU A 502     7984   6837   7419    826   1150    638       C  
ATOM   3850  OE1 GLU A 502      91.424  17.260  41.696  1.00 44.57           O  
ANISOU 3850  OE1 GLU A 502     6232   5066   5637    785   1099    593       O  
ATOM   3851  OE2 GLU A 502      89.993  16.279  43.060  1.00 31.44           O  
ANISOU 3851  OE2 GLU A 502     4592   3359   3996    914   1288    717       O  
ATOM   3852  N   PHE A 503      91.602  11.681  40.865  1.00 42.70           N  
ANISOU 3852  N   PHE A 503     5756   5014   5452    689    879    565       N  
ATOM   3853  CA  PHE A 503      90.559  10.748  40.462  1.00 50.68           C  
ANISOU 3853  CA  PHE A 503     6705   6057   6492    716    890    617       C  
ATOM   3854  C   PHE A 503      89.312  11.543  40.073  1.00 48.91           C  
ANISOU 3854  C   PHE A 503     6474   5822   6287    770    953    680       C  
ATOM   3855  O   PHE A 503      88.863  12.398  40.842  1.00 42.15           O  
ANISOU 3855  O   PHE A 503     5671   4912   5431    838   1068    733       O  
ATOM   3856  CB  PHE A 503      90.264   9.775  41.613  1.00 49.17           C  
ANISOU 3856  CB  PHE A 503     6520   5845   6316    777    990    683       C  
ATOM   3857  CG  PHE A 503      89.156   8.795  41.329  1.00 48.15           C  
ANISOU 3857  CG  PHE A 503     6322   5745   6228    810   1016    754       C  
ATOM   3858  CD1 PHE A 503      89.279   7.863  40.310  1.00 31.03           C  
ANISOU 3858  CD1 PHE A 503     4089   3636   4067    744    901    712       C  
ATOM   3859  CD2 PHE A 503      87.991   8.803  42.088  1.00 55.59           C  
ANISOU 3859  CD2 PHE A 503     7263   6654   7204    907   1161    866       C  
ATOM   3860  CE1 PHE A 503      88.264   6.962  40.053  1.00 44.01           C  
ANISOU 3860  CE1 PHE A 503     5669   5302   5750    772    927    780       C  
ATOM   3861  CE2 PHE A 503      86.969   7.906  41.831  1.00 51.76           C  
ANISOU 3861  CE2 PHE A 503     6703   6196   6768    935   1187    941       C  
ATOM   3862  CZ  PHE A 503      87.108   6.982  40.812  1.00 51.36           C  
ANISOU 3862  CZ  PHE A 503     6589   6203   6724    866   1069    898       C  
ATOM   3863  N   GLN A 504      88.732  11.221  38.917  1.00 35.91           N  
ANISOU 3863  N   GLN A 504     4766   4223   4656    743    886    678       N  
ATOM   3864  CA  GLN A 504      87.499  11.859  38.435  1.00 49.70           C  
ANISOU 3864  CA  GLN A 504     6496   5965   6422    792    940    741       C  
ATOM   3865  C   GLN A 504      87.491  13.387  38.545  1.00 53.55           C  
ANISOU 3865  C   GLN A 504     7040   6413   6895    817    985    742       C  
ATOM   3866  O   GLN A 504      86.504  13.963  38.998  1.00 63.05           O  
ANISOU 3866  O   GLN A 504     8260   7580   8117    897   1102    823       O  
ATOM   3867  CB  GLN A 504      86.300  11.312  39.217  1.00 43.15           C  
ANISOU 3867  CB  GLN A 504     5646   5115   5636    882   1073    856       C  
ATOM   3868  CG  GLN A 504      86.007   9.850  38.967  1.00 39.18           C  
ANISOU 3868  CG  GLN A 504     5073   4652   5160    865   1040    878       C  
ATOM   3869  CD  GLN A 504      84.823   9.368  39.748  1.00 55.27           C  
ANISOU 3869  CD  GLN A 504     7080   6669   7252    955   1175   1003       C  
ATOM   3870  OE1 GLN A 504      84.391  10.019  40.704  1.00 55.70           O  
ANISOU 3870  OE1 GLN A 504     7174   6672   7317   1032   1302   1069       O  
ATOM   3871  NE2 GLN A 504      84.314   8.195  39.387  1.00 45.29           N  
ANISOU 3871  NE2 GLN A 504     5743   5439   6025    945   1155   1041       N  
ATOM   3872  N   HIS A 505      88.590  14.035  38.158  1.00 50.52           N  
ANISOU 3872  N   HIS A 505     6680   6033   6481    751    897    657       N  
ATOM   3873  CA  HIS A 505      88.719  15.482  38.320  1.00 55.61           C  
ANISOU 3873  CA  HIS A 505     7381   6637   7111    770    938    654       C  
ATOM   3874  C   HIS A 505      87.591  16.274  37.660  1.00 45.86           C  
ANISOU 3874  C   HIS A 505     6134   5402   5890    813    978    706       C  
ATOM   3875  O   HIS A 505      87.266  17.381  38.070  1.00 57.47           O  
ANISOU 3875  O   HIS A 505     7653   6826   7356    863   1062    741       O  
ATOM   3876  CB  HIS A 505      90.062  15.991  37.804  1.00 60.18           C  
ANISOU 3876  CB  HIS A 505     7969   7232   7665    684    824    560       C  
ATOM   3877  CG  HIS A 505      90.261  15.766  36.335  0.70 79.24           C  
ANISOU 3877  CG  HIS A 505    10298   9724  10087    648    735    478       C  
ATOM   3878  ND1 HIS A 505      89.634  16.546  35.384  0.70 90.03           N  
ANISOU 3878  ND1 HIS A 505    11664  11204  11340    558    805    539       N  
ATOM   3879  CD2 HIS A 505      90.979  14.846  35.650  0.70 88.50           C  
ANISOU 3879  CD2 HIS A 505    11433  10944  11250    588    652    435       C  
ATOM   3880  CE1 HIS A 505      89.975  16.129  34.178  0.70 93.84           C  
ANISOU 3880  CE1 HIS A 505    12107  11725  11822    518    721    503       C  
ATOM   3881  NE2 HIS A 505      90.790  15.097  34.311  0.70 90.23           N  
ANISOU 3881  NE2 HIS A 505    11635  11283  11367    478    663    462       N  
ATOM   3882  N   GLU A 506      87.013  15.685  36.621  1.00 56.48           N  
ANISOU 3882  N   GLU A 506     7413   6798   7248    791    917    710       N  
ATOM   3883  CA  GLU A 506      85.993  16.341  35.821  1.00 55.68           C  
ANISOU 3883  CA  GLU A 506     7292   6706   7158    822    938    754       C  
ATOM   3884  C   GLU A 506      84.616  16.243  36.493  1.00 73.87           C  
ANISOU 3884  C   GLU A 506     9589   8982   9498    921   1080    870       C  
ATOM   3885  O   GLU A 506      83.769  17.103  36.282  1.00 68.07           O  
ANISOU 3885  O   GLU A 506     8858   8230   8774    972   1143    925       O  
ATOM   3886  CB  GLU A 506      85.970  15.757  34.399  1.00 67.28           C  
ANISOU 3886  CB  GLU A 506     8702   8238   8623    755    817    710       C  
ATOM   3887  CG  GLU A 506      85.002  16.394  33.409  0.70 82.75           C  
ANISOU 3887  CG  GLU A 506    10638  10214  10589    777    824    747       C  
ATOM   3888  CD  GLU A 506      85.428  17.801  33.014  0.70 93.52           C  
ANISOU 3888  CD  GLU A 506    12024  11690  11821    673    922    722       C  
ATOM   3889  OE1 GLU A 506      86.638  18.108  33.130  0.70102.06           O  
ANISOU 3889  OE1 GLU A 506    13134  12762  12881    640    880    660       O  
ATOM   3890  OE2 GLU A 506      84.571  18.587  32.553  0.70 84.50           O  
ANISOU 3890  OE2 GLU A 506    10877  10548  10681    706    963    765       O  
ATOM   3891  N   THR A 507      84.373  15.184  37.270  1.00 62.83           N  
ANISOU 3891  N   THR A 507     8171   7578   8122    950   1132    914       N  
ATOM   3892  CA  THR A 507      83.021  14.962  37.796  1.00 56.85           C  
ANISOU 3892  CA  THR A 507     7388   6801   7411   1041   1262   1033       C  
ATOM   3893  C   THR A 507      82.917  14.774  39.317  1.00 60.54           C  
ANISOU 3893  C   THR A 507     7895   7214   7895   1112   1394   1095       C  
ATOM   3894  O   THR A 507      81.912  15.181  39.909  1.00 56.70           O  
ANISOU 3894  O   THR A 507     7414   6688   7439   1199   1527   1192       O  
ATOM   3895  CB  THR A 507      82.347  13.731  37.143  1.00 57.18           C  
ANISOU 3895  CB  THR A 507     7344   6894   7489   1026   1224   1068       C  
ATOM   3896  OG1 THR A 507      83.016  12.522  37.526  1.00 58.07           O  
ANISOU 3896  OG1 THR A 507     7442   7023   7601    989   1181   1035       O  
ATOM   3897  CG2 THR A 507      82.291  13.876  35.626  1.00 51.76           C  
ANISOU 3897  CG2 THR A 507     6623   6257   6786    965   1111   1019       C  
ATOM   3898  N   LYS A 508      83.948  14.194  39.946  1.00 55.30           N  
ANISOU 3898  N   LYS A 508     7259   6544   7209   1078   1362   1041       N  
ATOM   3899  CA  LYS A 508      83.920  13.866  41.389  1.00 49.35           C  
ANISOU 3899  CA  LYS A 508     6545   5741   6465   1143   1485   1097       C  
ATOM   3900  C   LYS A 508      82.647  13.122  41.835  1.00 53.03           C  
ANISOU 3900  C   LYS A 508     6953   6204   6992   1221   1597   1220       C  
ATOM   3901  O   LYS A 508      82.099  13.384  42.903  1.00 60.70           O  
ANISOU 3901  O   LYS A 508     7960   7122   7983   1307   1743   1303       O  
ATOM   3902  CB  LYS A 508      84.081  15.140  42.233  1.00 45.54           C  
ANISOU 3902  CB  LYS A 508     6158   5187   5956   1191   1584   1104       C  
ATOM   3903  CG  LYS A 508      85.311  15.971  41.895  1.00 52.68           C  
ANISOU 3903  CG  LYS A 508     7117   6088   6811   1118   1489    996       C  
ATOM   3904  CD  LYS A 508      86.608  15.153  41.926  1.00 63.35           C  
ANISOU 3904  CD  LYS A 508     8467   7467   8137   1039   1382    909       C  
ATOM   3905  CE  LYS A 508      86.886  14.544  43.295  1.00 62.07           C  
ANISOU 3905  CE  LYS A 508     8350   7263   7970   1081   1475    939       C  
ATOM   3906  NZ  LYS A 508      88.241  13.944  43.367  1.00 55.99           N  
ANISOU 3906  NZ  LYS A 508     7589   6513   7171   1005   1375    852       N  
ATOM   3907  N   HIS A 509      82.202  12.179  41.010  1.00 52.56           N  
ANISOU 3907  N   HIS A 509     6805   6199   6965   1190   1530   1235       N  
ATOM   3908  CA  HIS A 509      80.975  11.421  41.247  1.00 45.11           C  
ANISOU 3908  CA  HIS A 509     5789   5261   6092   1252   1621   1356       C  
ATOM   3909  C   HIS A 509      81.040  10.480  42.445  1.00 51.93           C  
ANISOU 3909  C   HIS A 509     6648   6102   6982   1295   1705   1413       C  
ATOM   3910  O   HIS A 509      80.157  10.470  43.339  1.00 65.71           O  
ANISOU 3910  O   HIS A 509     8384   7809   8775   1386   1853   1529       O  
ATOM   3911  CB  HIS A 509      80.648  10.629  39.972  1.00 50.84           C  
ANISOU 3911  CB  HIS A 509     6427   6050   6839   1191   1511   1343       C  
ATOM   3912  CG  HIS A 509      79.354   9.887  40.010  0.70 37.18           C  
ANISOU 3912  CG  HIS A 509     4609   4328   5191   1243   1589   1469       C  
ATOM   3913  ND1 HIS A 509      79.286   8.535  40.271  0.70 37.68           N  
ANISOU 3913  ND1 HIS A 509     4611   4410   5297   1234   1586   1507       N  
ATOM   3914  CD2 HIS A 509      78.086  10.290  39.775  0.70 50.19           C  
ANISOU 3914  CD2 HIS A 509     6212   5967   6890   1300   1668   1570       C  
ATOM   3915  CE1 HIS A 509      78.027   8.144  40.225  0.70 50.49           C  
ANISOU 3915  CE1 HIS A 509     6152   6032   7000   1282   1662   1630       C  
ATOM   3916  NE2 HIS A 509      77.278   9.189  39.925  0.70 54.87           N  
ANISOU 3916  NE2 HIS A 509     6715   6572   7562   1323   1713   1670       N  
ATOM   3917  N   ALA A 510      82.153   9.768  42.525  1.00 51.33           N  
ANISOU 3917  N   ALA A 510     6584   6046   6871   1233   1618   1332       N  
ATOM   3918  CA  ALA A 510      82.342   8.829  43.606  1.00 58.99           C  
ANISOU 3918  CA  ALA A 510     7552   7001   7861   1267   1687   1378       C  
ATOM   3919  C   ALA A 510      82.415   9.559  44.936  1.00 47.70           C  
ANISOU 3919  C   ALA A 510     6212   5500   6413   1346   1829   1416       C  
ATOM   3920  O   ALA A 510      81.837   9.118  45.931  1.00 46.40           O  
ANISOU 3920  O   ALA A 510     6035   5309   6284   1419   1957   1515       O  
ATOM   3921  CB  ALA A 510      83.599   7.971  43.372  1.00 53.97           C  
ANISOU 3921  CB  ALA A 510     6917   6403   7188   1181   1559   1276       C  
ATOM   3922  N   LEU A 511      83.113  10.690  44.937  1.00 44.06           N  
ANISOU 3922  N   LEU A 511     5839   5010   5892   1325   1805   1338       N  
ATOM   3923  CA  LEU A 511      83.221  11.498  46.140  1.00 50.58           C  
ANISOU 3923  CA  LEU A 511     6766   5762   6692   1394   1937   1365       C  
ATOM   3924  C   LEU A 511      81.857  11.893  46.672  1.00 60.20           C  
ANISOU 3924  C   LEU A 511     7972   6943   7958   1496   2096   1492       C  
ATOM   3925  O   LEU A 511      81.613  11.835  47.875  1.00 65.72           O  
ANISOU 3925  O   LEU A 511     8696   7641   8632   1516   2210   1524       O  
ATOM   3926  CB  LEU A 511      84.086  12.733  45.894  1.00 51.81           C  
ANISOU 3926  CB  LEU A 511     7007   5892   6785   1347   1879   1265       C  
ATOM   3927  CG  LEU A 511      84.238  13.625  47.120  1.00 50.36           C  
ANISOU 3927  CG  LEU A 511     6940   5624   6569   1412   2014   1286       C  
ATOM   3928  CD1 LEU A 511      84.920  12.836  48.226  1.00 36.38           C  
ANISOU 3928  CD1 LEU A 511     5198   3863   4759   1391   2043   1264       C  
ATOM   3929  CD2 LEU A 511      85.031  14.885  46.784  1.00 59.58           C  
ANISOU 3929  CD2 LEU A 511     8184   6770   7686   1361   1954   1194       C  
ATOM   3930  N   ALA A 512      80.978  12.316  45.770  1.00 68.86           N  
ANISOU 3930  N   ALA A 512     9014   8059   9089   1502   2080   1527       N  
ATOM   3931  CA  ALA A 512      79.614  12.661  46.150  1.00 62.30           C  
ANISOU 3931  CA  ALA A 512     8159   7197   8316   1600   2227   1657       C  
ATOM   3932  C   ALA A 512      78.904  11.487  46.803  1.00 62.08           C  
ANISOU 3932  C   ALA A 512     8045   7211   8331   1611   2297   1738       C  
ATOM   3933  O   ALA A 512      78.230  11.646  47.835  1.00 60.81           O  
ANISOU 3933  O   ALA A 512     7892   7042   8170   1654   2436   1804       O  
ATOM   3934  CB  ALA A 512      78.824  13.143  44.938  1.00 47.15           C  
ANISOU 3934  CB  ALA A 512     6178   5312   6424   1583   2174   1670       C  
ATOM   3935  N   LEU A 513      79.103  10.294  46.241  1.00 49.00           N  
ANISOU 3935  N   LEU A 513     6309   5603   6707   1563   2201   1729       N  
ATOM   3936  CA  LEU A 513      78.457   9.129  46.840  1.00 51.91           C  
ANISOU 3936  CA  LEU A 513     6589   6014   7120   1560   2262   1806       C  
ATOM   3937  C   LEU A 513      78.999   8.858  48.252  1.00 63.23           C  
ANISOU 3937  C   LEU A 513     8078   7455   8493   1546   2336   1783       C  
ATOM   3938  O   LEU A 513      78.227   8.653  49.215  1.00 69.28           O  
ANISOU 3938  O   LEU A 513     8820   8229   9274   1579   2465   1867       O  
ATOM   3939  CB  LEU A 513      78.654   7.899  45.952  1.00 43.37           C  
ANISOU 3939  CB  LEU A 513     5418   4979   6083   1506   2139   1796       C  
ATOM   3940  CG  LEU A 513      78.259   6.557  46.572  1.00 46.82           C  
ANISOU 3940  CG  LEU A 513     5768   5459   6564   1487   2181   1860       C  
ATOM   3941  CD1 LEU A 513      76.797   6.591  46.976  1.00 55.43           C  
ANISOU 3941  CD1 LEU A 513     6788   6548   7725   1543   2316   1993       C  
ATOM   3942  CD2 LEU A 513      78.512   5.411  45.600  1.00 52.17           C  
ANISOU 3942  CD2 LEU A 513     6364   6173   7284   1432   2052   1843       C  
ATOM   3943  N   LEU A 514      80.321   8.907  48.385  1.00 52.99           N  
ANISOU 3943  N   LEU A 514     6857   6152   7124   1497   2257   1674       N  
ATOM   3944  CA  LEU A 514      80.952   8.660  49.674  1.00 50.50           C  
ANISOU 3944  CA  LEU A 514     6602   5846   6739   1475   2314   1645       C  
ATOM   3945  C   LEU A 514      80.503   9.661  50.722  1.00 60.48           C  
ANISOU 3945  C   LEU A 514     7943   7073   7963   1528   2461   1681       C  
ATOM   3946  O   LEU A 514      80.184   9.273  51.841  1.00 52.25           O  
ANISOU 3946  O   LEU A 514     6901   6051   6901   1538   2568   1732       O  
ATOM   3947  CB  LEU A 514      82.474   8.691  49.551  1.00 53.88           C  
ANISOU 3947  CB  LEU A 514     7102   6269   7099   1411   2199   1519       C  
ATOM   3948  CG  LEU A 514      83.158   7.663  48.652  1.00 53.59           C  
ANISOU 3948  CG  LEU A 514     7006   6272   7085   1351   2051   1466       C  
ATOM   3949  CD1 LEU A 514      84.644   7.961  48.578  1.00 42.03           C  
ANISOU 3949  CD1 LEU A 514     5625   4792   5552   1296   1953   1344       C  
ATOM   3950  CD2 LEU A 514      82.902   6.254  49.140  1.00 46.92           C  
ANISOU 3950  CD2 LEU A 514     6079   5481   6265   1328   2072   1519       C  
ATOM   3951  N   LYS A 515      80.491  10.948  50.363  1.00 79.29           N  
ANISOU 3951  N   LYS A 515    10394   9402  10332   1561   2469   1657       N  
ATOM   3952  CA  LYS A 515      80.092  11.989  51.310  1.00 74.36           C  
ANISOU 3952  CA  LYS A 515     9851   8735   9668   1613   2608   1687       C  
ATOM   3953  C   LYS A 515      78.626  11.856  51.686  1.00 61.81           C  
ANISOU 3953  C   LYS A 515     8191   7157   8136   1677   2742   1815       C  
ATOM   3954  O   LYS A 515      78.274  12.090  52.829  1.00 46.72           O  
ANISOU 3954  O   LYS A 515     6322   5240   6190   1707   2874   1857       O  
ATOM   3955  CB  LYS A 515      80.354  13.378  50.726  1.00 70.77           C  
ANISOU 3955  CB  LYS A 515     9477   8217   9197   1634   2582   1639       C  
ATOM   3956  CG  LYS A 515      81.822  13.764  50.674  1.00 66.34           C  
ANISOU 3956  CG  LYS A 515     9008   7631   8567   1575   2485   1517       C  
ATOM   3957  CD  LYS A 515      81.996  15.169  50.128  1.00 60.09           C  
ANISOU 3957  CD  LYS A 515     8292   6772   7766   1597   2472   1484       C  
ATOM   3958  CE  LYS A 515      83.387  15.703  50.400  1.00 57.29           C  
ANISOU 3958  CE  LYS A 515     8044   6384   7340   1542   2414   1375       C  
ATOM   3959  NZ  LYS A 515      83.555  17.080  49.875  1.00 57.31           N  
ANISOU 3959  NZ  LYS A 515     8120   6317   7339   1561   2405   1349       N  
ATOM   3960  N   GLN A 516      77.790  11.423  50.748  1.00 61.61           N  
ANISOU 3960  N   GLN A 516     8057   7151   8201   1693   2709   1880       N  
ATOM   3961  CA  GLN A 516      76.366  11.232  51.032  1.00 64.62           C  
ANISOU 3961  CA  GLN A 516     8357   7545   8652   1749   2832   2010       C  
ATOM   3962  C   GLN A 516      76.191  10.179  52.115  1.00 70.36           C  
ANISOU 3962  C   GLN A 516     9044   8316   9374   1732   2908   2060       C  
ATOM   3963  O   GLN A 516      75.469  10.371  53.127  1.00 75.27           O  
ANISOU 3963  O   GLN A 516     9675   8935   9990   1776   3057   2137       O  
ATOM   3964  CB  GLN A 516      75.622  10.816  49.772  1.00 71.95           C  
ANISOU 3964  CB  GLN A 516     9169   8491   9677   1753   2763   2064       C  
ATOM   3965  CG  GLN A 516      74.139  10.630  49.992  1.00 74.11           C  
ANISOU 3965  CG  GLN A 516     9350   8776  10033   1807   2885   2202       C  
ATOM   3966  CD  GLN A 516      73.419  10.282  48.709  1.00 89.41           C  
ANISOU 3966  CD  GLN A 516    11177  10730  12065   1807   2813   2255       C  
ATOM   3967  OE1 GLN A 516      73.185   9.111  48.411  1.00 83.37           O  
ANISOU 3967  OE1 GLN A 516    10310  10006  11359   1770   2768   2292       O  
ATOM   3968  NE2 GLN A 516      73.051  11.304  47.941  1.00104.24           N  
ANISOU 3968  NE2 GLN A 516    13076  12575  13956   1845   2804   2262       N  
ATOM   3969  N   LEU A 517      76.919   9.082  51.932  1.00 61.68           N  
ANISOU 3969  N   LEU A 517     7907   7258   8271   1667   2806   2015       N  
ATOM   3970  CA  LEU A 517      76.862   7.993  52.900  1.00 57.94           C  
ANISOU 3970  CA  LEU A 517     7394   6828   7791   1642   2865   2061       C  
ATOM   3971  C   LEU A 517      77.439   8.435  54.245  1.00 59.36           C  
ANISOU 3971  C   LEU A 517     7690   7000   7866   1642   2953   2027       C  
ATOM   3972  O   LEU A 517      76.896   8.090  55.293  1.00 65.99           O  
ANISOU 3972  O   LEU A 517     8518   7860   8697   1660   3076   2104       O  
ATOM   3973  CB  LEU A 517      77.605   6.765  52.375  1.00 64.14           C  
ANISOU 3973  CB  LEU A 517     8122   7656   8592   1570   2730   2015       C  
ATOM   3974  CG  LEU A 517      76.930   6.068  51.193  1.00 68.86           C  
ANISOU 3974  CG  LEU A 517     8592   8271   9298   1564   2657   2067       C  
ATOM   3975  CD1 LEU A 517      77.926   5.199  50.440  1.00 56.65           C  
ANISOU 3975  CD1 LEU A 517     7023   6752   7748   1494   2497   1984       C  
ATOM   3976  CD2 LEU A 517      75.742   5.234  51.658  1.00 66.46           C  
ANISOU 3976  CD2 LEU A 517     8178   7995   9078   1582   2760   2202       C  
ATOM   3977  N   LYS A 518      78.541   9.177  54.225  1.00 71.78           N  
ANISOU 3977  N   LYS A 518     9373   8542   9357   1619   2890   1915       N  
ATOM   3978  CA  LYS A 518      79.142   9.667  55.464  1.00 77.50           C  
ANISOU 3978  CA  LYS A 518    10215   9254   9976   1615   2966   1877       C  
ATOM   3979  C   LYS A 518      78.182  10.602  56.224  1.00 74.69           C  
ANISOU 3979  C   LYS A 518     9902   8866   9609   1688   3132   1952       C  
ATOM   3980  O   LYS A 518      78.124  10.592  57.454  1.00 69.33           O  
ANISOU 3980  O   LYS A 518     9275   8199   8868   1697   3245   1981       O  
ATOM   3981  CB  LYS A 518      80.477  10.362  55.162  1.00 68.81           C  
ANISOU 3981  CB  LYS A 518     9218   8121   8805   1574   2860   1745       C  
ATOM   3982  CG  LYS A 518      81.112  11.014  56.361  1.00 63.65           C  
ANISOU 3982  CG  LYS A 518     8693   7448   8043   1568   2933   1702       C  
ATOM   3983  CD  LYS A 518      82.501  11.511  56.036  1.00 54.27           C  
ANISOU 3983  CD  LYS A 518     7592   6232   6797   1515   2816   1575       C  
ATOM   3984  CE  LYS A 518      83.055  12.341  57.181  1.00 56.37           C  
ANISOU 3984  CE  LYS A 518     7991   6469   6958   1513   2894   1536       C  
ATOM   3985  NZ  LYS A 518      84.519  12.584  57.056  1.00 67.92           N  
ANISOU 3985  NZ  LYS A 518     9530   7916   8360   1446   2781   1417       N  
ATOM   3986  N   ALA A 519      77.481  11.447  55.472  1.00 70.71           N  
ANISOU 3986  N   ALA A 519     9384   8322   9162   1741   3145   1979       N  
ATOM   3987  CA  ALA A 519      76.461  12.363  55.994  1.00 77.50           C  
ANISOU 3987  CA  ALA A 519    10271   9146  10027   1817   3297   2057       C  
ATOM   3988  C   ALA A 519      75.284  11.642  56.643  1.00 76.36           C  
ANISOU 3988  C   ALA A 519    10037   9040   9936   1851   3425   2187       C  
ATOM   3989  O   ALA A 519      74.608  12.207  57.501  1.00 76.88           O  
ANISOU 3989  O   ALA A 519    10141   9089   9980   1904   3574   2249       O  
ATOM   3990  CB  ALA A 519      75.965  13.287  54.899  1.00 60.76           C  
ANISOU 3990  CB  ALA A 519     8139   6981   7966   1860   3267   2064       C  
ATOM   3991  N   ASP A 520      75.038  10.396  56.239  1.00 68.93           N  
ANISOU 3991  N   ASP A 520     8977   8149   9066   1818   3370   2230       N  
ATOM   3992  CA  ASP A 520      73.940   9.644  56.856  1.00 56.46           C  
ANISOU 3992  CA  ASP A 520     7305   6604   7545   1842   3490   2359       C  
ATOM   3993  C   ASP A 520      74.439   8.884  58.083  1.00 63.76           C  
ANISOU 3993  C   ASP A 520     8263   7569   8396   1803   3541   2361       C  
ATOM   3994  O   ASP A 520      73.707   8.085  58.668  1.00 60.27           O  
ANISOU 3994  O   ASP A 520     7745   7162   7994   1809   3630   2464       O  
ATOM   3995  CB  ASP A 520      73.362   8.625  55.874  0.50 59.47           C  
ANISOU 3995  CB  ASP A 520     7535   7016   8045   1823   3414   2418       C  
ATOM   3996  CG  ASP A 520      72.149   9.144  55.145  0.50 70.07           C  
ANISOU 3996  CG  ASP A 520     8805   8335   9485   1883   3457   2501       C  
ATOM   3997  OD1 ASP A 520      71.414   8.324  54.560  0.50 61.86           O  
ANISOU 3997  OD1 ASP A 520     7634   7320   8549   1875   3434   2579       O  
ATOM   3998  OD2 ASP A 520      71.944  10.375  55.136  0.50 74.49           O  
ANISOU 3998  OD2 ASP A 520     9437   8849  10017   1935   3509   2490       O  
ATOM   3999  N   ASN A 521      75.693   9.142  58.451  1.00 68.13           N  
ANISOU 3999  N   ASN A 521     8928   8117   8842   1762   3483   2251       N  
ATOM   4000  CA  ASN A 521      76.365   8.531  59.600  1.00 72.23           C  
ANISOU 4000  CA  ASN A 521     9499   8673   9270   1718   3516   2236       C  
ATOM   4001  C   ASN A 521      76.514   7.013  59.410  1.00 84.26           C  
ANISOU 4001  C   ASN A 521    10919  10254  10843   1660   3445   2264       C  
ATOM   4002  O   ASN A 521      76.520   6.242  60.374  1.00 69.59           O  
ANISOU 4002  O   ASN A 521     9054   8436   8950   1636   3511   2314       O  
ATOM   4003  CB  ASN A 521      75.617   8.846  60.903  0.50 54.98           C  
ANISOU 4003  CB  ASN A 521     7356   6492   7044   1767   3703   2324       C  
ATOM   4004  CG  ASN A 521      76.452   8.561  62.137  0.50 70.85           C  
ANISOU 4004  CG  ASN A 521     9459   8533   8930   1725   3740   2291       C  
ATOM   4005  OD1 ASN A 521      76.032   7.824  63.031  0.50 86.25           O  
ANISOU 4005  OD1 ASN A 521    11378  10524  10869   1722   3835   2376       O  
ATOM   4006  ND2 ASN A 521      77.651   9.129  62.181  0.50 64.85           N  
ANISOU 4006  ND2 ASN A 521     8811   7752   8077   1691   3661   2170       N  
ATOM   4007  N   ILE A 522      76.687   6.601  58.153  1.00 95.24           N  
ANISOU 4007  N   ILE A 522    12234  11646  12308   1633   3307   2230       N  
ATOM   4008  CA  ILE A 522      76.962   5.203  57.810  1.00 88.43           C  
ANISOU 4008  CA  ILE A 522    11277  10830  11492   1573   3217   2240       C  
ATOM   4009  C   ILE A 522      78.463   5.007  57.603  1.00 76.73           C  
ANISOU 4009  C   ILE A 522     9863   9358   9934   1506   3080   2110       C  
ATOM   4010  O   ILE A 522      79.084   5.723  56.811  1.00 71.30           O  
ANISOU 4010  O   ILE A 522     9224   8637   9230   1502   2982   2014       O  
ATOM   4011  CB  ILE A 522      76.246   4.788  56.506  1.00 81.72           C  
ANISOU 4011  CB  ILE A 522    10298   9978  10772   1580   3144   2282       C  
ATOM   4012  CG1 ILE A 522      74.728   4.896  56.643  1.00 79.13           C  
ANISOU 4012  CG1 ILE A 522     9887   9643  10535   1642   3274   2419       C  
ATOM   4013  CG2 ILE A 522      76.646   3.375  56.105  1.00 72.58           C  
ANISOU 4013  CG2 ILE A 522     9055   8864   9660   1513   3041   2281       C  
ATOM   4014  CD1 ILE A 522      74.009   4.856  55.313  1.00 81.06           C  
ANISOU 4014  CD1 ILE A 522    10028   9875  10897   1658   3206   2453       C  
ATOM   4015  N   PRO A 523      79.053   4.038  58.319  1.00 59.57           N  
ANISOU 4015  N   PRO A 523     7693   7229   7714   1452   3073   2110       N  
ATOM   4016  CA  PRO A 523      80.481   3.719  58.174  1.00 67.06           C  
ANISOU 4016  CA  PRO A 523     8696   8192   8593   1384   2944   1994       C  
ATOM   4017  C   PRO A 523      80.818   3.264  56.759  1.00 74.85           C  
ANISOU 4017  C   PRO A 523     9609   9178   9653   1354   2786   1940       C  
ATOM   4018  O   PRO A 523      80.054   2.483  56.181  1.00 59.37           O  
ANISOU 4018  O   PRO A 523     7530   7234   7794   1356   2773   2014       O  
ATOM   4019  CB  PRO A 523      80.670   2.547  59.143  1.00 64.18           C  
ANISOU 4019  CB  PRO A 523     8311   7881   8196   1340   2985   2047       C  
ATOM   4020  CG  PRO A 523      79.529   2.630  60.098  1.00 63.83           C  
ANISOU 4020  CG  PRO A 523     8250   7841   8162   1389   3158   2171       C  
ATOM   4021  CD  PRO A 523      78.385   3.190  59.318  1.00 61.08           C  
ANISOU 4021  CD  PRO A 523     7834   7458   7917   1452   3191   2226       C  
ATOM   4022  N   VAL A 524      81.916   3.780  56.196  1.00 73.53           N  
ANISOU 4022  N   VAL A 524     9511   8991   9437   1325   2670   1817       N  
ATOM   4023  CA  VAL A 524      82.215   3.542  54.784  1.00 66.20           C  
ANISOU 4023  CA  VAL A 524     8524   8056   8571   1303   2523   1762       C  
ATOM   4024  C   VAL A 524      83.550   2.828  54.563  1.00 60.25           C  
ANISOU 4024  C   VAL A 524     7788   7331   7775   1229   2393   1667       C  
ATOM   4025  O   VAL A 524      84.611   3.306  54.969  1.00 60.74           O  
ANISOU 4025  O   VAL A 524     7948   7382   7746   1201   2363   1579       O  
ATOM   4026  CB  VAL A 524      82.251   4.877  54.008  1.00 60.47           C  
ANISOU 4026  CB  VAL A 524     7853   7276   7845   1339   2488   1703       C  
ATOM   4027  CG1 VAL A 524      82.930   4.698  52.658  1.00 51.83           C  
ANISOU 4027  CG1 VAL A 524     6731   6179   6783   1302   2323   1621       C  
ATOM   4028  CG2 VAL A 524      80.844   5.432  53.843  1.00 61.69           C  
ANISOU 4028  CG2 VAL A 524     7963   7407   8071   1411   2588   1802       C  
ATOM   4029  N   VAL A 525      83.476   1.679  53.900  1.00 58.41           N  
ANISOU 4029  N   VAL A 525     7454   7130   7611   1197   2317   1689       N  
ATOM   4030  CA  VAL A 525      84.647   0.940  53.444  1.00 45.46           C  
ANISOU 4030  CA  VAL A 525     5811   5514   5949   1131   2182   1603       C  
ATOM   4031  C   VAL A 525      84.726   1.003  51.925  1.00 53.23           C  
ANISOU 4031  C   VAL A 525     6747   6482   6996   1127   2054   1554       C  
ATOM   4032  O   VAL A 525      83.820   0.534  51.237  1.00 46.80           O  
ANISOU 4032  O   VAL A 525     5834   5673   6273   1146   2048   1623       O  
ATOM   4033  CB  VAL A 525      84.584  -0.533  53.864  1.00 58.83           C  
ANISOU 4033  CB  VAL A 525     7429   7257   7669   1090   2188   1667       C  
ATOM   4034  CG1 VAL A 525      85.684  -1.337  53.170  1.00 42.30           C  
ANISOU 4034  CG1 VAL A 525     5317   5186   5570   1026   2040   1583       C  
ATOM   4035  CG2 VAL A 525      84.702  -0.651  55.381  1.00 55.41           C  
ANISOU 4035  CG2 VAL A 525     7054   6844   7154   1081   2302   1708       C  
ATOM   4036  N   THR A 526      85.780   1.625  51.411  1.00 56.18           N  
ANISOU 4036  N   THR A 526     7192   6835   7320   1104   1955   1440       N  
ATOM   4037  CA  THR A 526      85.946   1.835  49.979  1.00 46.70           C  
ANISOU 4037  CA  THR A 526     5963   5617   6165   1100   1834   1387       C  
ATOM   4038  C   THR A 526      86.861   0.806  49.326  1.00 53.10           C  
ANISOU 4038  C   THR A 526     6736   6460   6981   1038   1700   1324       C  
ATOM   4039  O   THR A 526      87.993   0.619  49.747  1.00 41.87           O  
ANISOU 4039  O   THR A 526     5367   5050   5493    991   1657   1251       O  
ATOM   4040  CB  THR A 526      86.478   3.253  49.682  1.00 49.72           C  
ANISOU 4040  CB  THR A 526     6442   5949   6500   1114   1807   1306       C  
ATOM   4041  OG1 THR A 526      85.490   4.224  50.050  1.00 52.71           O  
ANISOU 4041  OG1 THR A 526     6845   6294   6889   1178   1923   1370       O  
ATOM   4042  CG2 THR A 526      86.785   3.406  48.203  1.00 49.31           C  
ANISOU 4042  CG2 THR A 526     6366   5884   6485   1100   1673   1249       C  
ATOM   4043  N   VAL A 527      86.369   0.161  48.278  1.00 48.62           N  
ANISOU 4043  N   VAL A 527     6077   5904   6490   1037   1634   1355       N  
ATOM   4044  CA  VAL A 527      87.194  -0.727  47.488  1.00 39.67           C  
ANISOU 4044  CA  VAL A 527     4911   4797   5366    983   1502   1293       C  
ATOM   4045  C   VAL A 527      87.499   0.002  46.189  1.00 50.60           C  
ANISOU 4045  C   VAL A 527     6317   6154   6756    985   1396   1223       C  
ATOM   4046  O   VAL A 527      86.605   0.318  45.405  1.00 51.38           O  
ANISOU 4046  O   VAL A 527     6375   6238   6910   1020   1396   1271       O  
ATOM   4047  CB  VAL A 527      86.487  -2.082  47.195  1.00 49.01           C  
ANISOU 4047  CB  VAL A 527     5978   6012   6633    972   1494   1378       C  
ATOM   4048  CG1 VAL A 527      87.336  -2.965  46.299  1.00 37.31           C  
ANISOU 4048  CG1 VAL A 527     4466   4552   5159    920   1354   1312       C  
ATOM   4049  CG2 VAL A 527      86.144  -2.804  48.489  1.00 36.85           C  
ANISOU 4049  CG2 VAL A 527     4413   4498   5092    967   1603   1459       C  
ATOM   4050  N   PHE A 528      88.777   0.310  45.997  1.00 43.05           N  
ANISOU 4050  N   PHE A 528     5426   5190   5740    945   1309   1114       N  
ATOM   4051  CA  PHE A 528      89.186   1.186  44.912  1.00 35.96           C  
ANISOU 4051  CA  PHE A 528     4564   4268   4831    932   1215   1038       C  
ATOM   4052  C   PHE A 528      89.836   0.352  43.813  1.00 37.45           C  
ANISOU 4052  C   PHE A 528     4708   4513   5007    833   1055    949       C  
ATOM   4053  O   PHE A 528      90.860  -0.294  44.037  1.00 34.97           O  
ANISOU 4053  O   PHE A 528     4406   4214   4667    796   1004    897       O  
ATOM   4054  CB  PHE A 528      90.157   2.230  45.446  1.00 43.70           C  
ANISOU 4054  CB  PHE A 528     5650   5208   5747    928   1222    966       C  
ATOM   4055  CG  PHE A 528      90.485   3.303  44.457  1.00 37.85           C  
ANISOU 4055  CG  PHE A 528     4937   4473   4972    864   1123    870       C  
ATOM   4056  CD1 PHE A 528      89.492   4.161  44.013  1.00 48.78           C  
ANISOU 4056  CD1 PHE A 528     6313   5847   6375    893   1158    906       C  
ATOM   4057  CD2 PHE A 528      91.772   3.461  43.966  1.00 43.81           C  
ANISOU 4057  CD2 PHE A 528     5719   5245   5680    777    998    751       C  
ATOM   4058  CE1 PHE A 528      89.777   5.169  43.102  1.00 60.37           C  
ANISOU 4058  CE1 PHE A 528     7803   7322   7813    838   1071    826       C  
ATOM   4059  CE2 PHE A 528      92.062   4.465  43.056  1.00 51.08           C  
ANISOU 4059  CE2 PHE A 528     6656   6174   6579    721    911    675       C  
ATOM   4060  CZ  PHE A 528      91.062   5.319  42.621  1.00 41.50           C  
ANISOU 4060  CZ  PHE A 528     5436   4950   5381    752    948    712       C  
ATOM   4061  N   LEU A 529      89.211   0.339  42.646  1.00 34.99           N  
ANISOU 4061  N   LEU A 529     4350   4231   4715    794    986    935       N  
ATOM   4062  CA  LEU A 529      89.735  -0.349  41.480  1.00 34.38           C  
ANISOU 4062  CA  LEU A 529     4244   4199   4619    700    839    845       C  
ATOM   4063  C   LEU A 529      90.514   0.619  40.596  1.00 47.21           C  
ANISOU 4063  C   LEU A 529     5920   5832   6186    629    729    721       C  
ATOM   4064  O   LEU A 529      89.977   1.629  40.159  1.00 39.82           O  
ANISOU 4064  O   LEU A 529     4998   4884   5247    640    740    723       O  
ATOM   4065  CB  LEU A 529      88.588  -0.952  40.671  1.00 32.51           C  
ANISOU 4065  CB  LEU A 529     3933   3983   4436    697    832    903       C  
ATOM   4066  CG  LEU A 529      87.639  -1.935  41.362  1.00 44.61           C  
ANISOU 4066  CG  LEU A 529     5390   5508   6050    759    934   1043       C  
ATOM   4067  CD1 LEU A 529      86.478  -2.275  40.440  1.00 36.30           C  
ANISOU 4067  CD1 LEU A 529     4270   4468   5055    751    923   1097       C  
ATOM   4068  CD2 LEU A 529      88.361  -3.209  41.788  1.00 27.68           C  
ANISOU 4068  CD2 LEU A 529     3222   3383   3913    736    907   1041       C  
ATOM   4069  N   SER A 530      91.780   0.314  40.320  1.00 43.32           N  
ANISOU 4069  N   SER A 530     5448   5357   5652    556    625    619       N  
ATOM   4070  CA  SER A 530      92.601   1.214  39.509  1.00 33.95           C  
ANISOU 4070  CA  SER A 530     4299   4178   4424    485    521    509       C  
ATOM   4071  C   SER A 530      93.826   0.489  38.978  1.00 44.51           C  
ANISOU 4071  C   SER A 530     5612   5560   5741    407    415    389       C  
ATOM   4072  O   SER A 530      94.247  -0.534  39.531  1.00 29.14           O  
ANISOU 4072  O   SER A 530     3675   3605   3792    398    404    418       O  
ATOM   4073  CB  SER A 530      93.067   2.416  40.323  1.00 35.02           C  
ANISOU 4073  CB  SER A 530     4493   4273   4540    515    577    506       C  
ATOM   4074  OG  SER A 530      94.070   2.007  41.231  1.00 37.93           O  
ANISOU 4074  OG  SER A 530     4889   4630   4892    513    589    489       O  
ATOM   4075  N   GLY A 531      94.412   1.043  37.926  1.00 26.22           N  
ANISOU 4075  N   GLY A 531     3315   3263   3383    423    483    454       N  
ATOM   4076  CA  GLY A 531      95.610   0.488  37.347  1.00 30.67           C  
ANISOU 4076  CA  GLY A 531     3868   3848   3937    288    276    267       C  
ATOM   4077  C   GLY A 531      96.859   1.156  37.867  1.00 20.82           C  
ANISOU 4077  C   GLY A 531     2671   2612   2627    220    281    245       C  
ATOM   4078  O   GLY A 531      97.920   0.976  37.299  1.00 26.04           O  
ANISOU 4078  O   GLY A 531     3315   3263   3315    204    192    169       O  
ATOM   4079  N   ARG A 532      96.710   1.966  38.911  1.00 19.65           N  
ANISOU 4079  N   ARG A 532     2554   2436   2476    258    346    276       N  
ATOM   4080  CA  ARG A 532      97.797   2.822  39.385  1.00 46.26           C  
ANISOU 4080  CA  ARG A 532     5950   5748   5881    289    308    219       C  
ATOM   4081  C   ARG A 532      97.366   3.604  40.612  1.00 43.31           C  
ANISOU 4081  C   ARG A 532     5621   5323   5511    349    391    258       C  
ATOM   4082  O   ARG A 532      96.181   3.773  40.849  1.00 30.47           O  
ANISOU 4082  O   ARG A 532     4009   3672   3897    403    457    334       O  
ATOM   4083  CB  ARG A 532      98.154   3.833  38.293  1.00 39.53           C  
ANISOU 4083  CB  ARG A 532     5094   4909   5017    250    263    183       C  
ATOM   4084  CG  ARG A 532      96.923   4.558  37.767  1.00 34.31           C  
ANISOU 4084  CG  ARG A 532     4430   4243   4365    287    299    218       C  
ATOM   4085  CD  ARG A 532      97.256   5.467  36.613  1.00 38.66           C  
ANISOU 4085  CD  ARG A 532     4983   4845   4863    210    277    201       C  
ATOM   4086  NE  ARG A 532      96.082   5.671  35.776  1.00 31.67           N  
ANISOU 4086  NE  ARG A 532     4082   3970   3981    228    292    229       N  
ATOM   4087  CZ  ARG A 532      96.135   6.039  34.505  1.00 34.26           C  
ANISOU 4087  CZ  ARG A 532     4381   4289   4347    236    222    183       C  
ATOM   4088  NH1 ARG A 532      97.308   6.233  33.919  1.00 28.40           N  
ANISOU 4088  NH1 ARG A 532     3643   3581   3565    150    175    142       N  
ATOM   4089  NH2 ARG A 532      95.020   6.180  33.815  1.00 33.29           N  
ANISOU 4089  NH2 ARG A 532     4259   4202   4188    219    262    230       N  
ATOM   4090  N   PRO A 533      98.321   4.054  41.426  1.00 33.59           N  
ANISOU 4090  N   PRO A 533     4433   4064   4268    338    398    236       N  
ATOM   4091  CA  PRO A 533      97.898   5.008  42.441  1.00 22.89           C  
ANISOU 4091  CA  PRO A 533     3155   2643   2900    405    515    301       C  
ATOM   4092  C   PRO A 533      97.344   6.259  41.755  1.00 35.69           C  
ANISOU 4092  C   PRO A 533     4777   4258   4524    404    507    299       C  
ATOM   4093  O   PRO A 533      97.777   6.581  40.659  1.00 29.15           O  
ANISOU 4093  O   PRO A 533     3906   3538   3631    300    467    261       O  
ATOM   4094  CB  PRO A 533      99.207   5.365  43.146  1.00 31.89           C  
ANISOU 4094  CB  PRO A 533     4342   3757   4018    375    509    261       C  
ATOM   4095  CG  PRO A 533     100.128   4.233  42.852  1.00 33.49           C  
ANISOU 4095  CG  PRO A 533     4496   4004   4226    314    415    215       C  
ATOM   4096  CD  PRO A 533      99.767   3.802  41.474  1.00 36.04           C  
ANISOU 4096  CD  PRO A 533     4745   4438   4510    239    373    204       C  
ATOM   4097  N   LEU A 534      96.367   6.914  42.371  1.00 39.18           N  
ANISOU 4097  N   LEU A 534     5265   4655   4967    485    628    368       N  
ATOM   4098  CA  LEU A 534      95.871   8.197  41.886  1.00 45.53           C  
ANISOU 4098  CA  LEU A 534     6082   5445   5771    493    638    372       C  
ATOM   4099  C   LEU A 534      95.717   9.093  43.104  1.00 33.55           C  
ANISOU 4099  C   LEU A 534     4654   3855   4237    561    771    417       C  
ATOM   4100  O   LEU A 534      95.789   8.618  44.241  1.00 40.72           O  
ANISOU 4100  O   LEU A 534     5611   4727   5134    609    862    453       O  
ATOM   4101  CB  LEU A 534      94.531   8.058  41.154  1.00 35.89           C  
ANISOU 4101  CB  LEU A 534     4817   4247   4574    525    651    418       C  
ATOM   4102  CG  LEU A 534      94.457   7.328  39.814  1.00 35.51           C  
ANISOU 4102  CG  LEU A 534     4695   4261   4537    459    529    375       C  
ATOM   4103  CD1 LEU A 534      93.011   7.163  39.397  1.00 34.93           C  
ANISOU 4103  CD1 LEU A 534     4592   4195   4486    509    578    441       C  
ATOM   4104  CD2 LEU A 534      95.212   8.114  38.751  1.00 24.63           C  
ANISOU 4104  CD2 LEU A 534     3304   2982   3073    350    514    329       C  
ATOM   4105  N   TRP A 535      95.555  10.391  42.879  1.00 37.37           N  
ANISOU 4105  N   TRP A 535     5168   4316   4715    566    786    414       N  
ATOM   4106  CA  TRP A 535      95.364  11.315  43.993  1.00 50.47           C  
ANISOU 4106  CA  TRP A 535     6922   5900   6355    629    917    454       C  
ATOM   4107  C   TRP A 535      93.930  11.265  44.484  1.00 47.30           C  
ANISOU 4107  C   TRP A 535     6535   5467   5968    729   1050    548       C  
ATOM   4108  O   TRP A 535      93.011  11.735  43.804  1.00 46.75           O  
ANISOU 4108  O   TRP A 535     6434   5411   5918    750   1055    577       O  
ATOM   4109  CB  TRP A 535      95.767  12.738  43.604  1.00 40.89           C  
ANISOU 4109  CB  TRP A 535     5736   4671   5131    597    887    418       C  
ATOM   4110  CG  TRP A 535      95.789  13.680  44.756  1.00 40.67           C  
ANISOU 4110  CG  TRP A 535     5816   4562   5075    648   1011    445       C  
ATOM   4111  CD1 TRP A 535      96.744  13.774  45.728  1.00 43.94           C  
ANISOU 4111  CD1 TRP A 535     6304   4933   5458    635   1044    421       C  
ATOM   4112  CD2 TRP A 535      94.834  14.715  45.027  1.00 56.36           C  
ANISOU 4112  CD2 TRP A 535     7855   6498   7060    716   1120    499       C  
ATOM   4113  NE1 TRP A 535      96.420  14.777  46.611  1.00 55.22           N  
ANISOU 4113  NE1 TRP A 535     7835   6285   6863    691   1169    456       N  
ATOM   4114  CE2 TRP A 535      95.256  15.375  46.197  1.00 64.11           C  
ANISOU 4114  CE2 TRP A 535     8948   7405   8008    742   1218    504       C  
ATOM   4115  CE3 TRP A 535      93.656  15.136  44.401  1.00 55.50           C  
ANISOU 4115  CE3 TRP A 535     7713   6399   6974    758   1146    544       C  
ATOM   4116  CZ2 TRP A 535      94.544  16.431  46.749  1.00 60.98           C  
ANISOU 4116  CZ2 TRP A 535     8628   6941   7598    809   1341    551       C  
ATOM   4117  CZ3 TRP A 535      92.951  16.182  44.951  1.00 61.72           C  
ANISOU 4117  CZ3 TRP A 535     8572   7125   7754    827   1268    595       C  
ATOM   4118  CH2 TRP A 535      93.396  16.819  46.114  1.00 69.70           C  
ANISOU 4118  CH2 TRP A 535     9692   8059   8730    852   1365    597       C  
ATOM   4119  N   VAL A 536      93.755  10.693  45.668  1.00 36.80           N  
ANISOU 4119  N   VAL A 536     5253   4098   4632    792   1161    600       N  
ATOM   4120  CA  VAL A 536      92.430  10.454  46.217  1.00 42.40           C  
ANISOU 4120  CA  VAL A 536     5963   4783   5365    891   1295    703       C  
ATOM   4121  C   VAL A 536      92.225  10.949  47.651  1.00 51.95           C  
ANISOU 4121  C   VAL A 536     7279   5907   6550    975   1460    760       C  
ATOM   4122  O   VAL A 536      91.492  10.319  48.413  1.00 62.06           O  
ANISOU 4122  O   VAL A 536     8547   7198   7835   1027   1558    830       O  
ATOM   4123  CB  VAL A 536      92.076   8.958  46.155  1.00 47.08           C  
ANISOU 4123  CB  VAL A 536     6479   5421   5987    903   1284    741       C  
ATOM   4124  CG1 VAL A 536      91.812   8.523  44.720  1.00 44.22           C  
ANISOU 4124  CG1 VAL A 536     6016   5133   5652    842   1153    710       C  
ATOM   4125  CG2 VAL A 536      93.174   8.132  46.788  1.00 30.91           C  
ANISOU 4125  CG2 VAL A 536     4457   3371   3915    874   1260    703       C  
ATOM   4126  N   ASN A 537      92.920  12.015  48.039  1.00 49.14           N  
ANISOU 4126  N   ASN A 537     7013   5502   6156    955   1474    716       N  
ATOM   4127  CA  ASN A 537      92.807  12.554  49.397  1.00 48.56           C  
ANISOU 4127  CA  ASN A 537     7037   5376   6035    999   1612    745       C  
ATOM   4128  C   ASN A 537      91.362  12.838  49.801  1.00 42.67           C  
ANISOU 4128  C   ASN A 537     6283   4626   5302   1080   1742    837       C  
ATOM   4129  O   ASN A 537      90.957  12.561  50.931  1.00 54.58           O  
ANISOU 4129  O   ASN A 537     7810   6155   6772   1101   1845    877       O  
ATOM   4130  CB  ASN A 537      93.664  13.807  49.563  1.00 44.14           C  
ANISOU 4130  CB  ASN A 537     6577   4749   5443    971   1608    691       C  
ATOM   4131  CG  ASN A 537      95.133  13.501  49.562  1.00 55.19           C  
ANISOU 4131  CG  ASN A 537     7994   6156   6819    889   1508    609       C  
ATOM   4132  OD1 ASN A 537      95.544  12.418  49.163  1.00 46.11           O  
ANISOU 4132  OD1 ASN A 537     6776   5058   5686    851   1422    586       O  
ATOM   4133  ND2 ASN A 537      95.943  14.469  49.980  1.00 60.73           N  
ANISOU 4133  ND2 ASN A 537     8786   6806   7484    857   1519    566       N  
ATOM   4134  N   LYS A 538      90.597  13.419  48.880  1.00 48.66           N  
ANISOU 4134  N   LYS A 538     7016   5359   6114   1124   1739    874       N  
ATOM   4135  CA  LYS A 538      89.194  13.728  49.139  1.00 52.31           C  
ANISOU 4135  CA  LYS A 538     7462   5814   6599   1203   1858    966       C  
ATOM   4136  C   LYS A 538      88.379  12.464  49.423  1.00 67.60           C  
ANISOU 4136  C   LYS A 538     9307   7817   8560   1223   1896   1032       C  
ATOM   4137  O   LYS A 538      87.620  12.409  50.395  1.00 67.11           O  
ANISOU 4137  O   LYS A 538     9252   7763   8481   1264   2021   1096       O  
ATOM   4138  CB  LYS A 538      88.576  14.503  47.965  1.00 52.81           C  
ANISOU 4138  CB  LYS A 538     7487   5877   6703   1212   1816    977       C  
ATOM   4139  CG  LYS A 538      89.228  15.852  47.695  1.00 55.28           C  
ANISOU 4139  CG  LYS A 538     7864   6160   6980   1167   1775    908       C  
ATOM   4140  CD  LYS A 538      88.740  16.469  46.392  1.00 48.78           C  
ANISOU 4140  CD  LYS A 538     6972   5381   6180   1137   1694    896       C  
ATOM   4141  CE  LYS A 538      89.460  17.765  46.106  1.00 40.80           C  
ANISOU 4141  CE  LYS A 538     6018   4346   5139   1089   1651    831       C  
ATOM   4142  NZ  LYS A 538      89.094  18.310  44.773  1.00 56.45           N  
ANISOU 4142  NZ  LYS A 538     7932   6376   7140   1056   1562    814       N  
ATOM   4143  N   GLU A 539      88.564  11.443  48.587  1.00 52.07           N  
ANISOU 4143  N   GLU A 539     7256   5896   6632   1190   1790   1018       N  
ATOM   4144  CA  GLU A 539      87.830  10.197  48.733  1.00 44.70           C  
ANISOU 4144  CA  GLU A 539     6229   5024   5731   1202   1814   1082       C  
ATOM   4145  C   GLU A 539      88.298   9.464  49.986  1.00 50.67           C  
ANISOU 4145  C   GLU A 539     7007   5814   6431   1172   1861   1074       C  
ATOM   4146  O   GLU A 539      87.500   8.822  50.681  1.00 41.74           O  
ANISOU 4146  O   GLU A 539     5834   4718   5308   1199   1952   1150       O  
ATOM   4147  CB  GLU A 539      87.993   9.301  47.491  1.00 45.86           C  
ANISOU 4147  CB  GLU A 539     6287   5208   5929   1170   1683   1064       C  
ATOM   4148  CG  GLU A 539      87.317   9.808  46.224  1.00 41.14           C  
ANISOU 4148  CG  GLU A 539     5637   4626   5369   1166   1623   1070       C  
ATOM   4149  CD  GLU A 539      88.122  10.882  45.506  1.00 59.32           C  
ANISOU 4149  CD  GLU A 539     7980   6931   7629   1092   1519    966       C  
ATOM   4150  OE1 GLU A 539      89.285  11.122  45.897  1.00 54.72           O  
ANISOU 4150  OE1 GLU A 539     7462   6327   7003   1051   1485    895       O  
ATOM   4151  OE2 GLU A 539      87.594  11.482  44.543  1.00 58.33           O  
ANISOU 4151  OE2 GLU A 539     7820   6828   7517   1076   1474    961       O  
ATOM   4152  N   LEU A 540      89.602   9.535  50.254  1.00 41.33           N  
ANISOU 4152  N   LEU A 540     5885   4624   5194   1113   1798    987       N  
ATOM   4153  CA  LEU A 540      90.153   8.943  51.472  1.00 54.75           C  
ANISOU 4153  CA  LEU A 540     7618   6356   6829   1080   1840    975       C  
ATOM   4154  C   LEU A 540      89.508   9.563  52.710  1.00 59.76           C  
ANISOU 4154  C   LEU A 540     8316   6973   7416   1126   1995   1032       C  
ATOM   4155  O   LEU A 540      89.156   8.849  53.655  1.00 47.54           O  
ANISOU 4155  O   LEU A 540     6754   5468   5843   1131   2073   1084       O  
ATOM   4156  CB  LEU A 540      91.671   9.134  51.522  1.00 41.08           C  
ANISOU 4156  CB  LEU A 540     5950   4611   5047   1011   1749    873       C  
ATOM   4157  CG  LEU A 540      92.530   8.124  50.759  1.00 47.05           C  
ANISOU 4157  CG  LEU A 540     6646   5405   5825    950   1611    817       C  
ATOM   4158  CD1 LEU A 540      93.924   8.657  50.511  1.00 43.86           C  
ANISOU 4158  CD1 LEU A 540     6302   4969   5393    891   1518    720       C  
ATOM   4159  CD2 LEU A 540      92.597   6.823  51.521  1.00 32.46           C  
ANISOU 4159  CD2 LEU A 540     4759   3623   3952    927   1632    843       C  
ATOM   4160  N   ASN A 541      89.351  10.887  52.707  1.00 51.65           N  
ANISOU 4160  N   ASN A 541     7362   5884   6379   1159   2040   1024       N  
ATOM   4161  CA  ASN A 541      88.735  11.578  53.836  1.00 47.55           C  
ANISOU 4161  CA  ASN A 541     6911   5342   5814   1206   2190   1075       C  
ATOM   4162  C   ASN A 541      87.269  11.185  54.026  1.00 63.94           C  
ANISOU 4162  C   ASN A 541     8915   7443   7936   1271   2296   1187       C  
ATOM   4163  O   ASN A 541      86.768  11.131  55.158  1.00 53.50           O  
ANISOU 4163  O   ASN A 541     7619   6135   6573   1298   2420   1243       O  
ATOM   4164  CB  ASN A 541      88.824  13.094  53.660  1.00 47.88           C  
ANISOU 4164  CB  ASN A 541     7040   5308   5845   1229   2213   1047       C  
ATOM   4165  CG  ASN A 541      90.218  13.638  53.909  1.00 54.95           C  
ANISOU 4165  CG  ASN A 541     8027   6172   6679   1167   2152    952       C  
ATOM   4166  OD1 ASN A 541      91.066  12.963  54.500  1.00 49.64           O  
ANISOU 4166  OD1 ASN A 541     7369   5537   5957   1113   2119    913       O  
ATOM   4167  ND2 ASN A 541      90.453  14.882  53.481  1.00 55.90           N  
ANISOU 4167  ND2 ASN A 541     8211   6224   6805   1173   2141    919       N  
ATOM   4168  N   ALA A 542      86.610  10.829  52.925  1.00 54.66           N  
ANISOU 4168  N   ALA A 542     7644   6278   6845   1292   2245   1222       N  
ATOM   4169  CA  ALA A 542      85.204  10.443  52.969  1.00 44.62           C  
ANISOU 4169  CA  ALA A 542     6293   5029   5633   1350   2336   1333       C  
ATOM   4170  C   ALA A 542      85.024   8.961  53.234  1.00 59.93           C  
ANISOU 4170  C   ALA A 542     8143   7036   7591   1325   2331   1376       C  
ATOM   4171  O   ALA A 542      83.912   8.435  53.155  1.00 71.90           O  
ANISOU 4171  O   ALA A 542     9573   8577   9171   1361   2389   1471       O  
ATOM   4172  CB  ALA A 542      84.498  10.846  51.673  1.00 51.67           C  
ANISOU 4172  CB  ALA A 542     7127   5899   6607   1386   2292   1360       C  
ATOM   4173  N   SER A 543      86.122   8.295  53.571  1.00 46.66           N  
ANISOU 4173  N   SER A 543     6483   5386   5860   1260   2263   1312       N  
ATOM   4174  CA  SER A 543      86.098   6.857  53.784  1.00 58.41           C  
ANISOU 4174  CA  SER A 543     7892   6938   7365   1228   2246   1347       C  
ATOM   4175  C   SER A 543      86.623   6.555  55.183  1.00 65.11           C  
ANISOU 4175  C   SER A 543     8803   7812   8122   1200   2314   1345       C  
ATOM   4176  O   SER A 543      87.586   7.176  55.644  1.00 71.66           O  
ANISOU 4176  O   SER A 543     9731   8620   8875   1172   2298   1270       O  
ATOM   4177  CB  SER A 543      86.971   6.151  52.754  1.00 67.17           C  
ANISOU 4177  CB  SER A 543     8955   8067   8499   1170   2086   1274       C  
ATOM   4178  OG  SER A 543      86.566   6.496  51.440  1.00 60.19           O  
ANISOU 4178  OG  SER A 543     8023   7160   7686   1192   2017   1271       O  
ATOM   4179  N   ASP A 544      85.980   5.608  55.862  1.00 65.02           N  
ANISOU 4179  N   ASP A 544     8735   7848   8122   1206   2392   1433       N  
ATOM   4180  CA  ASP A 544      86.484   5.087  57.128  1.00 45.17           C  
ANISOU 4180  CA  ASP A 544     6268   5371   5523   1171   2445   1441       C  
ATOM   4181  C   ASP A 544      87.594   4.076  56.904  1.00 54.27           C  
ANISOU 4181  C   ASP A 544     7398   6564   6657   1097   2324   1379       C  
ATOM   4182  O   ASP A 544      88.600   4.072  57.615  1.00 60.81           O  
ANISOU 4182  O   ASP A 544     8303   7404   7397   1052   2308   1325       O  
ATOM   4183  CB  ASP A 544      85.339   4.464  57.921  1.00 58.02           C  
ANISOU 4183  CB  ASP A 544     7839   7032   7173   1204   2579   1569       C  
ATOM   4184  CG  ASP A 544      84.265   5.485  58.276  1.00 82.79           C  
ANISOU 4184  CG  ASP A 544    11005  10131  10320   1279   2712   1633       C  
ATOM   4185  OD1 ASP A 544      83.253   5.553  57.538  1.00 83.68           O  
ANISOU 4185  OD1 ASP A 544    11038  10230  10528   1324   2728   1691       O  
ATOM   4186  OD2 ASP A 544      84.440   6.248  59.246  1.00 88.96           O  
ANISOU 4186  OD2 ASP A 544    11889  10896  11017   1294   2798   1623       O  
ATOM   4187  N   ALA A 545      87.418   3.239  55.887  1.00 58.78           N  
ANISOU 4187  N   ALA A 545     7868   7155   7312   1083   2237   1387       N  
ATOM   4188  CA  ALA A 545      88.482   2.356  55.438  1.00 59.93           C  
ANISOU 4188  CA  ALA A 545     7990   7332   7451   1016   2108   1320       C  
ATOM   4189  C   ALA A 545      88.637   2.500  53.931  1.00 55.21           C  
ANISOU 4189  C   ALA A 545     7343   6710   6922   1013   1982   1262       C  
ATOM   4190  O   ALA A 545      87.672   2.804  53.231  1.00 50.43           O  
ANISOU 4190  O   ALA A 545     6686   6084   6389   1061   1999   1309       O  
ATOM   4191  CB  ALA A 545      88.189   0.913  55.813  1.00 51.23           C  
ANISOU 4191  CB  ALA A 545     6807   6286   6374    990   2127   1396       C  
ATOM   4192  N   PHE A 546      89.841   2.246  53.427  1.00 48.61           N  
ANISOU 4192  N   PHE A 546     6524   5881   6065    957   1856   1167       N  
ATOM   4193  CA  PHE A 546      90.117   2.418  52.013  1.00 51.68           C  
ANISOU 4193  CA  PHE A 546     6879   6249   6508    950   1733   1106       C  
ATOM   4194  C   PHE A 546      91.126   1.344  51.613  1.00 50.43           C  
ANISOU 4194  C   PHE A 546     6686   6129   6347    884   1614   1048       C  
ATOM   4195  O   PHE A 546      92.236   1.247  52.196  1.00 47.96           O  
ANISOU 4195  O   PHE A 546     6432   5827   5965    836   1585    988       O  
ATOM   4196  CB  PHE A 546      90.685   3.828  51.752  1.00 53.90           C  
ANISOU 4196  CB  PHE A 546     7251   6472   6756    956   1706   1029       C  
ATOM   4197  CG  PHE A 546      90.771   4.220  50.284  1.00 59.36           C  
ANISOU 4197  CG  PHE A 546     7912   7135   7505    958   1597    983       C  
ATOM   4198  CD1 PHE A 546      89.867   5.130  49.756  1.00 58.82           C  
ANISOU 4198  CD1 PHE A 546     7843   7028   7478   1015   1635   1021       C  
ATOM   4199  CD2 PHE A 546      91.734   3.690  49.442  1.00 55.61           C  
ANISOU 4199  CD2 PHE A 546     7413   6674   7040    905   1460    908       C  
ATOM   4200  CE1 PHE A 546      89.934   5.518  48.433  1.00 37.74           C  
ANISOU 4200  CE1 PHE A 546     5151   4335   4853   1015   1538    986       C  
ATOM   4201  CE2 PHE A 546      91.790   4.070  48.106  1.00 60.37           C  
ANISOU 4201  CE2 PHE A 546     7993   7254   7689    906   1364    872       C  
ATOM   4202  CZ  PHE A 546      90.889   4.982  47.605  1.00 47.33           C  
ANISOU 4202  CZ  PHE A 546     6343   5566   6073    960   1403    912       C  
ATOM   4203  N   VAL A 547      90.724   0.548  50.624  1.00 30.59           N  
ANISOU 4203  N   VAL A 547     4079   3636   3909    884   1549   1071       N  
ATOM   4204  CA  VAL A 547      91.507  -0.558  50.101  1.00 29.13           C  
ANISOU 4204  CA  VAL A 547     3846   3486   3734    829   1438   1027       C  
ATOM   4205  C   VAL A 547      91.860  -0.346  48.642  1.00 45.49           C  
ANISOU 4205  C   VAL A 547     5895   5540   5847    820   1311    960       C  
ATOM   4206  O   VAL A 547      90.976  -0.176  47.811  1.00 47.53           O  
ANISOU 4206  O   VAL A 547     6105   5787   6169    857   1305   1000       O  
ATOM   4207  CB  VAL A 547      90.743  -1.878  50.222  1.00 37.86           C  
ANISOU 4207  CB  VAL A 547     4854   4636   4896    828   1470   1121       C  
ATOM   4208  CG1 VAL A 547      91.540  -3.011  49.604  1.00 43.76           C  
ANISOU 4208  CG1 VAL A 547     5554   5416   5658    773   1353   1076       C  
ATOM   4209  CG2 VAL A 547      90.407  -2.169  51.674  1.00 41.31           C  
ANISOU 4209  CG2 VAL A 547     5311   5094   5291    831   1597   1197       C  
ATOM   4210  N   ALA A 548      93.150  -0.403  48.329  1.00 40.39           N  
ANISOU 4210  N   ALA A 548     5285   4896   5167    768   1208    863       N  
ATOM   4211  CA  ALA A 548      93.607  -0.410  46.943  1.00 35.03           C  
ANISOU 4211  CA  ALA A 548     4579   4208   4523    749   1078    799       C  
ATOM   4212  C   ALA A 548      93.538  -1.842  46.434  1.00 44.65           C  
ANISOU 4212  C   ALA A 548     5710   5473   5783    726   1018    821       C  
ATOM   4213  O   ALA A 548      94.300  -2.699  46.878  1.00 49.74           O  
ANISOU 4213  O   ALA A 548     6350   6150   6400    681    992    797       O  
ATOM   4214  CB  ALA A 548      95.028   0.124  46.842  1.00 39.89           C  
ANISOU 4214  CB  ALA A 548     5262   4801   5091    700    998    692       C  
ATOM   4215  N   ALA A 549      92.597  -2.107  45.532  1.00 46.31           N  
ANISOU 4215  N   ALA A 549     5851   5685   6060    756   1001    873       N  
ATOM   4216  CA  ALA A 549      92.390  -3.455  45.028  1.00 21.50           C  
ANISOU 4216  CA  ALA A 549     2623   2581   2966    738    951    907       C  
ATOM   4217  C   ALA A 549      92.955  -3.697  43.631  1.00 40.68           C  
ANISOU 4217  C   ALA A 549     5038   5039   5382    655    792    802       C  
ATOM   4218  O   ALA A 549      92.937  -4.836  43.128  1.00 32.91           O  
ANISOU 4218  O   ALA A 549     3996   4089   4420    616    732    802       O  
ATOM   4219  CB  ALA A 549      90.911  -3.787  45.055  1.00 32.99           C  
ANISOU 4219  CB  ALA A 549     4005   4039   4492    782   1032   1026       C  
ATOM   4220  N   TRP A 550      93.446  -2.626  43.013  1.00 26.70           N  
ANISOU 4220  N   TRP A 550     3321   3261   3565    609    722    702       N  
ATOM   4221  CA  TRP A 550      94.078  -2.679  41.694  1.00 27.46           C  
ANISOU 4221  CA  TRP A 550     3416   3389   3630    507    568    581       C  
ATOM   4222  C   TRP A 550      93.076  -3.203  40.675  1.00 35.13           C  
ANISOU 4222  C   TRP A 550     4334   4383   4632    489    534    603       C  
ATOM   4223  O   TRP A 550      91.922  -2.780  40.655  1.00 30.96           O  
ANISOU 4223  O   TRP A 550     3784   3841   4139    540    605    679       O  
ATOM   4224  CB  TRP A 550      95.376  -3.491  41.714  1.00 27.81           C  
ANISOU 4224  CB  TRP A 550     3466   3454   3646    448    487    507       C  
ATOM   4225  CG  TRP A 550      96.251  -3.161  42.890  1.00 24.08           C  
ANISOU 4225  CG  TRP A 550     3043   2955   3152    480    544    511       C  
ATOM   4226  CD1 TRP A 550      96.541  -3.978  43.935  1.00 34.71           C  
ANISOU 4226  CD1 TRP A 550     4385   4298   4506    526    614    571       C  
ATOM   4227  CD2 TRP A 550      96.881  -1.905  43.174  1.00 40.24           C  
ANISOU 4227  CD2 TRP A 550     5155   4967   5167    474    550    463       C  
ATOM   4228  NE1 TRP A 550      97.338  -3.327  44.841  1.00 28.40           N  
ANISOU 4228  NE1 TRP A 550     3657   3461   3674    549    663    555       N  
ATOM   4229  CE2 TRP A 550      97.567  -2.053  44.397  1.00 29.96           C  
ANISOU 4229  CE2 TRP A 550     3898   3636   3849    515    623    488       C  
ATOM   4230  CE3 TRP A 550      96.941  -0.672  42.510  1.00 34.70           C  
ANISOU 4230  CE3 TRP A 550     4478   4254   4451    438    501    406       C  
ATOM   4231  CZ2 TRP A 550      98.310  -1.022  44.969  1.00 41.07           C  
ANISOU 4231  CZ2 TRP A 550     5383   4998   5224    514    647    451       C  
ATOM   4232  CZ3 TRP A 550      97.682   0.355  43.079  1.00 35.04           C  
ANISOU 4232  CZ3 TRP A 550     4583   4260   4470    438    523    377       C  
ATOM   4233  CH2 TRP A 550      98.358   0.173  44.296  1.00 30.80           C  
ANISOU 4233  CH2 TRP A 550     4098   3689   3915    473    595    397       C  
ATOM   4234  N   LEU A 551      93.517  -4.117  39.821  1.00 40.43           N  
ANISOU 4234  N   LEU A 551     4989   5082   5290    418    430    535       N  
ATOM   4235  CA  LEU A 551      92.623  -4.723  38.840  1.00 32.24           C  
ANISOU 4235  CA  LEU A 551     3912   4057   4279    400    401    553       C  
ATOM   4236  C   LEU A 551      92.655  -6.250  39.051  1.00 33.45           C  
ANISOU 4236  C   LEU A 551     4020   4226   4466    395    400    595       C  
ATOM   4237  O   LEU A 551      93.366  -6.968  38.344  1.00 33.63           O  
ANISOU 4237  O   LEU A 551     3987   4298   4494    386    447    662       O  
ATOM   4238  CB  LEU A 551      93.061  -4.359  37.417  1.00 27.37           C  
ANISOU 4238  CB  LEU A 551     3342   3452   3604    315    312    474       C  
ATOM   4239  CG  LEU A 551      93.080  -2.854  37.077  1.00 38.27           C  
ANISOU 4239  CG  LEU A 551     4749   4863   4930    272    359    442       C  
ATOM   4240  CD1 LEU A 551      93.806  -2.603  35.771  1.00 29.28           C  
ANISOU 4240  CD1 LEU A 551     3626   3739   3761    222    278    358       C  
ATOM   4241  CD2 LEU A 551      91.690  -2.233  37.036  1.00 33.04           C  
ANISOU 4241  CD2 LEU A 551     4022   4175   4357    391    388    472       C  
ATOM   4242  N   PRO A 552      91.879  -6.742  40.036  1.00 48.54           N  
ANISOU 4242  N   PRO A 552     5869   6128   6444    467    511    734       N  
ATOM   4243  CA  PRO A 552      91.972  -8.108  40.587  1.00 37.15           C  
ANISOU 4243  CA  PRO A 552     4372   4697   5048    474    532    801       C  
ATOM   4244  C   PRO A 552      91.653  -9.265  39.627  1.00 39.01           C  
ANISOU 4244  C   PRO A 552     4568   4941   5315    424    465    795       C  
ATOM   4245  O   PRO A 552      92.033 -10.401  39.909  1.00 42.94           O  
ANISOU 4245  O   PRO A 552     5033   5448   5836    409    450    818       O  
ATOM   4246  CB  PRO A 552      90.967  -8.100  41.751  1.00 39.68           C  
ANISOU 4246  CB  PRO A 552     4632   4997   5449    568    679    965       C  
ATOM   4247  CG  PRO A 552      90.087  -6.924  41.493  1.00 47.12           C  
ANISOU 4247  CG  PRO A 552     5591   5917   6395    603    725    984       C  
ATOM   4248  CD  PRO A 552      90.901  -5.920  40.769  1.00 28.75           C  
ANISOU 4248  CD  PRO A 552     3348   3597   3980    550    634    840       C  
ATOM   4249  N   GLY A 553      90.978  -9.003  38.517  1.00 31.30           N  
ANISOU 4249  N   GLY A 553     3596   3957   4339    400    428    769       N  
ATOM   4250  CA  GLY A 553      90.693 -10.067  37.570  1.00 30.13           C  
ANISOU 4250  CA  GLY A 553     3423   3807   4219    357    373    762       C  
ATOM   4251  C   GLY A 553      89.351 -10.748  37.793  1.00 28.82           C  
ANISOU 4251  C   GLY A 553     3153   3618   4177    396    449    919       C  
ATOM   4252  O   GLY A 553      88.409 -10.131  38.281  1.00 40.70           O  
ANISOU 4252  O   GLY A 553     4618   5110   5736    454    537   1018       O  
ATOM   4253  N   SER A 554      89.264 -12.029  37.447  1.00 43.12           N  
ANISOU 4253  N   SER A 554     4921   5420   6045    366    417    948       N  
ATOM   4254  CA  SER A 554      87.973 -12.725  37.445  1.00 44.98           C  
ANISOU 4254  CA  SER A 554     5050   5623   6419    388    470   1093       C  
ATOM   4255  C   SER A 554      87.445 -13.127  38.831  1.00 43.06           C  
ANISOU 4255  C   SER A 554     4712   5368   6281    448    573   1252       C  
ATOM   4256  O   SER A 554      86.238 -13.255  39.021  1.00 54.10           O  
ANISOU 4256  O   SER A 554     6023   6738   7795    484    644   1384       O  
ATOM   4257  CB  SER A 554      88.022 -13.947  36.532  1.00 29.94           C  
ANISOU 4257  CB  SER A 554     3126   3696   4554    334    399   1074       C  
ATOM   4258  OG  SER A 554      89.085 -14.800  36.905  1.00 47.95           O  
ANISOU 4258  OG  SER A 554     5426   5989   6805    307    356   1030       O  
ATOM   4259  N   GLU A 555      88.333 -13.277  39.806  1.00 40.88           N  
ANISOU 4259  N   GLU A 555     4451   5114   5967    462    589   1245       N  
ATOM   4260  CA  GLU A 555      87.967 -13.879  41.091  1.00 38.74           C  
ANISOU 4260  CA  GLU A 555     4089   4833   5797    515    685   1399       C  
ATOM   4261  C   GLU A 555      87.643 -12.832  42.156  1.00 45.70           C  
ANISOU 4261  C   GLU A 555     4979   5715   6669    598    805   1467       C  
ATOM   4262  O   GLU A 555      88.398 -12.637  43.116  1.00 46.71           O  
ANISOU 4262  O   GLU A 555     5138   5860   6750    630    845   1464       O  
ATOM   4263  CB  GLU A 555      89.052 -14.846  41.577  1.00 42.53           C  
ANISOU 4263  CB  GLU A 555     4568   5333   6260    485    642   1379       C  
ATOM   4264  CG  GLU A 555      89.314 -15.959  40.581  1.00 38.44           C  
ANISOU 4264  CG  GLU A 555     4043   4802   5762    411    535   1324       C  
ATOM   4265  CD  GLU A 555      88.011 -16.494  39.990  1.00 45.98           C  
ANISOU 4265  CD  GLU A 555     4911   5710   6850    407    547   1422       C  
ATOM   4266  OE1 GLU A 555      87.109 -16.896  40.760  1.00 51.55           O  
ANISOU 4266  OE1 GLU A 555     5509   6390   7688    448    630   1584       O  
ATOM   4267  OE2 GLU A 555      87.874 -16.494  38.749  1.00 45.91           O  
ANISOU 4267  OE2 GLU A 555     4940   5685   6818    364    477   1341       O  
ATOM   4268  N   GLY A 556      86.529 -12.131  41.967  1.00 35.21           N  
ANISOU 4268  N   GLY A 556     3629   4364   5385    636    866   1525       N  
ATOM   4269  CA  GLY A 556      86.181 -11.045  42.859  1.00 36.50           C  
ANISOU 4269  CA  GLY A 556     3816   4520   5534    718    982   1579       C  
ATOM   4270  C   GLY A 556      85.923 -11.429  44.295  1.00 50.52           C  
ANISOU 4270  C   GLY A 556     5560   6308   7327    724   1099   1664       C  
ATOM   4271  O   GLY A 556      86.025 -10.589  45.195  1.00 56.91           O  
ANISOU 4271  O   GLY A 556     6433   7129   8063    747   1183   1649       O  
ATOM   4272  N   GLU A 557      85.693 -12.712  44.539  1.00 54.04           N  
ANISOU 4272  N   GLU A 557     5921   6754   7859    690   1099   1744       N  
ATOM   4273  CA  GLU A 557      85.447 -13.151  45.908  1.00 57.50           C  
ANISOU 4273  CA  GLU A 557     6334   7206   8306    680   1209   1827       C  
ATOM   4274  C   GLU A 557      86.680 -13.086  46.791  1.00 46.88           C  
ANISOU 4274  C   GLU A 557     5076   5897   6839    655   1214   1752       C  
ATOM   4275  O   GLU A 557      86.569 -13.004  48.019  1.00 51.24           O  
ANISOU 4275  O   GLU A 557     5652   6463   7354    654   1320   1800       O  
ATOM   4276  CB  GLU A 557      84.805 -14.542  45.948  1.00 61.11           C  
ANISOU 4276  CB  GLU A 557     6673   7646   8902    647   1211   1945       C  
ATOM   4277  CG  GLU A 557      84.367 -14.953  47.338  1.00 77.09           C  
ANISOU 4277  CG  GLU A 557     8667   9679  10943    637   1337   2050       C  
ATOM   4278  CD  GLU A 557      83.437 -16.138  47.343  1.00 71.21           C  
ANISOU 4278  CD  GLU A 557     7793   8904  10358    611   1354   2185       C  
ATOM   4279  OE1 GLU A 557      83.107 -16.640  46.247  1.00 68.14           O  
ANISOU 4279  OE1 GLU A 557     7337   8482  10072    601   1266   2195       O  
ATOM   4280  OE2 GLU A 557      83.015 -16.544  48.445  1.00 71.39           O  
ANISOU 4280  OE2 GLU A 557     7786   8931  10407    599   1458   2284       O  
ATOM   4281  N   GLY A 558      87.832 -12.922  46.152  1.00 43.27           N  
ANISOU 4281  N   GLY A 558     4680   5452   6308    638   1104   1628       N  
ATOM   4282  CA  GLY A 558      89.067 -12.681  46.870  1.00 41.47           C  
ANISOU 4282  CA  GLY A 558     4544   5255   5958    613   1098   1541       C  
ATOM   4283  C   GLY A 558      88.944 -11.447  47.725  1.00 43.54           C  
ANISOU 4283  C   GLY A 558     4889   5516   6138    646   1199   1525       C  
ATOM   4284  O   GLY A 558      89.632 -11.317  48.736  1.00 46.59           O  
ANISOU 4284  O   GLY A 558     5343   5922   6436    625   1242   1499       O  
ATOM   4285  N   VAL A 559      88.093 -10.519  47.304  1.00 38.15           N  
ANISOU 4285  N   VAL A 559     4206   4808   5481    696   1234   1541       N  
ATOM   4286  CA  VAL A 559      87.865  -9.329  48.103  1.00 45.66           C  
ANISOU 4286  CA  VAL A 559     5232   5751   6366    734   1335   1537       C  
ATOM   4287  C   VAL A 559      87.105  -9.630  49.399  1.00 57.72           C  
ANISOU 4287  C   VAL A 559     6736   7286   7910    741   1476   1655       C  
ATOM   4288  O   VAL A 559      87.577  -9.311  50.502  1.00 41.25           O  
ANISOU 4288  O   VAL A 559     4726   5214   5734    732   1542   1642       O  
ATOM   4289  CB  VAL A 559      87.127  -8.243  47.308  1.00 40.01           C  
ANISOU 4289  CB  VAL A 559     4522   5004   5676    787   1339   1530       C  
ATOM   4290  CG1 VAL A 559      86.777  -7.094  48.233  1.00 44.77           C  
ANISOU 4290  CG1 VAL A 559     5195   5594   6222    828   1456   1544       C  
ATOM   4291  CG2 VAL A 559      87.974  -7.760  46.135  1.00 39.94           C  
ANISOU 4291  CG2 VAL A 559     4559   4986   5628    778   1208   1408       C  
ATOM   4292  N   ALA A 560      85.997 -10.365  49.262  1.00 63.23           N  
ANISOU 4292  N   ALA A 560     7325   7974   8725    747   1514   1773       N  
ATOM   4293  CA  ALA A 560      85.216 -10.775  50.426  1.00 69.10           C  
ANISOU 4293  CA  ALA A 560     8033   8722   9499    750   1646   1899       C  
ATOM   4294  C   ALA A 560      86.051 -11.549  51.430  1.00 62.21           C  
ANISOU 4294  C   ALA A 560     7194   7880   8565    697   1660   1903       C  
ATOM   4295  O   ALA A 560      86.060 -11.209  52.623  1.00 65.06           O  
ANISOU 4295  O   ALA A 560     7616   8252   8851    702   1764   1932       O  
ATOM   4296  CB  ALA A 560      84.010 -11.593  49.996  1.00 54.99           C  
ANISOU 4296  CB  ALA A 560     6114   6916   7865    753   1663   2022       C  
ATOM   4297  N   ASP A 561      86.899 -12.428  50.907  1.00 46.27           N  
ANISOU 4297  N   ASP A 561     5154   5872   6554    648   1547   1854       N  
ATOM   4298  CA  ASP A 561      87.757 -13.276  51.718  1.00 48.57           C  
ANISOU 4298  CA  ASP A 561     5472   6190   6793    592   1541   1858       C  
ATOM   4299  C   ASP A 561      88.544 -12.447  52.717  1.00 48.60           C  
ANISOU 4299  C   ASP A 561     5604   6213   6648    589   1592   1794       C  
ATOM   4300  O   ASP A 561      88.790 -12.897  53.834  1.00 51.56           O  
ANISOU 4300  O   ASP A 561     6011   6607   6973    558   1655   1844       O  
ATOM   4301  CB  ASP A 561      88.762 -14.052  50.855  1.00 47.25           C  
ANISOU 4301  CB  ASP A 561     5287   6032   6635    547   1396   1780       C  
ATOM   4302  CG  ASP A 561      88.113 -15.141  50.030  1.00 54.49           C  
ANISOU 4302  CG  ASP A 561     6078   6928   7699    535   1341   1854       C  
ATOM   4303  OD1 ASP A 561      86.985 -15.541  50.375  1.00 48.61           O  
ANISOU 4303  OD1 ASP A 561     5254   6165   7051    544   1423   1981       O  
ATOM   4304  OD2 ASP A 561      88.765 -15.627  49.081  1.00 43.41           O  
ANISOU 4304  OD2 ASP A 561     4655   5524   6316    512   1217   1788       O  
ATOM   4305  N   VAL A 562      88.975 -11.258  52.309  1.00 36.48           N  
ANISOU 4305  N   VAL A 562     4146   4670   5045    619   1560   1685       N  
ATOM   4306  CA  VAL A 562      89.769 -10.436  53.205  1.00 51.32           C  
ANISOU 4306  CA  VAL A 562     6148   6560   6792    613   1598   1619       C  
ATOM   4307  C   VAL A 562      88.903  -9.474  54.021  1.00 56.08           C  
ANISOU 4307  C   VAL A 562     6791   7149   7368    665   1734   1676       C  
ATOM   4308  O   VAL A 562      89.158  -9.246  55.211  1.00 40.38           O  
ANISOU 4308  O   VAL A 562     4877   5173   5291    655   1815   1694       O  
ATOM   4309  CB  VAL A 562      90.858  -9.667  52.447  1.00 45.04           C  
ANISOU 4309  CB  VAL A 562     5422   5758   5933    608   1488   1468       C  
ATOM   4310  CG1 VAL A 562      91.704  -8.861  53.421  1.00 42.01           C  
ANISOU 4310  CG1 VAL A 562     5161   5379   5421    596   1525   1406       C  
ATOM   4311  CG2 VAL A 562      91.758 -10.644  51.747  1.00 29.24           C  
ANISOU 4311  CG2 VAL A 562     3386   3774   3949    557   1362   1415       C  
ATOM   4312  N   LEU A 563      87.909  -8.870  53.367  1.00 60.03           N  
ANISOU 4312  N   LEU A 563     7247   7621   7941    720   1758   1702       N  
ATOM   4313  CA  LEU A 563      87.114  -7.835  54.045  1.00 53.14           C  
ANISOU 4313  CA  LEU A 563     6416   6731   7043    775   1883   1747       C  
ATOM   4314  C   LEU A 563      86.135  -8.376  55.083  1.00 56.32           C  
ANISOU 4314  C   LEU A 563     6775   7143   7480    783   2019   1891       C  
ATOM   4315  O   LEU A 563      85.841  -7.704  56.069  1.00 61.62           O  
ANISOU 4315  O   LEU A 563     7510   7813   8088    810   2133   1924       O  
ATOM   4316  CB  LEU A 563      86.362  -6.963  53.028  1.00 57.48           C  
ANISOU 4316  CB  LEU A 563     6937   7245   7655    832   1868   1733       C  
ATOM   4317  CG  LEU A 563      87.076  -5.714  52.477  1.00 46.17           C  
ANISOU 4317  CG  LEU A 563     5596   5789   6156    849   1804   1605       C  
ATOM   4318  CD1 LEU A 563      88.415  -5.973  51.786  1.00 28.74           C  
ANISOU 4318  CD1 LEU A 563     3418   3593   3910    800   1659   1484       C  
ATOM   4319  CD2 LEU A 563      86.141  -4.914  51.575  1.00 44.80           C  
ANISOU 4319  CD2 LEU A 563     5390   5581   6051    906   1807   1621       C  
ATOM   4320  N   LEU A 564      85.651  -9.593  54.884  1.00 60.76           N  
ANISOU 4320  N   LEU A 564     7230   7714   8143    757   2009   1980       N  
ATOM   4321  CA  LEU A 564      84.661 -10.165  55.793  1.00 55.07           C  
ANISOU 4321  CA  LEU A 564     6454   6997   7473    762   2135   2128       C  
ATOM   4322  C   LEU A 564      85.310 -11.158  56.749  1.00 58.80           C  
ANISOU 4322  C   LEU A 564     6948   7499   7894    700   2149   2166       C  
ATOM   4323  O   LEU A 564      86.314 -11.790  56.422  1.00 58.62           O  
ANISOU 4323  O   LEU A 564     6934   7490   7847    649   2043   2102       O  
ATOM   4324  CB  LEU A 564      83.562 -10.879  55.009  1.00 52.10           C  
ANISOU 4324  CB  LEU A 564     5935   6601   7259    771   2126   2223       C  
ATOM   4325  CG  LEU A 564      82.764 -10.012  54.034  1.00 55.44           C  
ANISOU 4325  CG  LEU A 564     6323   6994   7746    829   2116   2209       C  
ATOM   4326  CD1 LEU A 564      81.641 -10.830  53.415  1.00 44.86           C  
ANISOU 4326  CD1 LEU A 564     4840   5635   6570    830   2115   2320       C  
ATOM   4327  CD2 LEU A 564      82.184  -8.813  54.789  1.00 44.59           C  
ANISOU 4327  CD2 LEU A 564     5017   5611   6315    888   2245   2232       C  
ATOM   4328  N   THR A 565      84.745 -11.271  57.944  1.00 65.88           N  
ANISOU 4328  N   THR A 565     7859   8405   8768    706   2283   2272       N  
ATOM   4329  CA  THR A 565      85.081 -12.364  58.843  1.00 63.77           C  
ANISOU 4329  CA  THR A 565     7591   8161   8478    648   2310   2346       C  
ATOM   4330  C   THR A 565      84.443 -13.631  58.295  1.00 50.74           C  
ANISOU 4330  C   THR A 565     5799   6496   6984    621   2278   2444       C  
ATOM   4331  O   THR A 565      83.679 -13.577  57.332  1.00 57.26           O  
ANISOU 4331  O   THR A 565     6534   7297   7927    651   2250   2459       O  
ATOM   4332  CB  THR A 565      84.518 -12.124  60.267  1.00 52.16           C  
ANISOU 4332  CB  THR A 565     6171   6702   6947    665   2472   2447       C  
ATOM   4333  OG1 THR A 565      83.087 -12.065  60.210  1.00 59.58           O  
ANISOU 4333  OG1 THR A 565     7019   7620   8000    712   2569   2561       O  
ATOM   4334  CG2 THR A 565      85.003 -10.795  60.826  1.00 52.32           C  
ANISOU 4334  CG2 THR A 565     6328   6729   6823    698   2513   2360       C  
ATOM   4335  N   ASN A 566      84.780 -14.778  58.871  1.00 62.18           N  
ANISOU 4335  N   ASN A 566     7231   7957   8439    562   2276   2510       N  
ATOM   4336  CA  ASN A 566      84.004 -15.984  58.605  1.00 78.47           C  
ANISOU 4336  CA  ASN A 566     9158   9998  10659    537   2276   2633       C  
ATOM   4337  C   ASN A 566      82.689 -15.992  59.397  1.00 83.96           C  
ANISOU 4337  C   ASN A 566     9803  10683  11416    566   2432   2784       C  
ATOM   4338  O   ASN A 566      82.344 -14.993  60.044  1.00 70.38           O  
ANISOU 4338  O   ASN A 566     8152   8972   9617    613   2536   2786       O  
ATOM   4339  CB  ASN A 566      84.853 -17.237  58.884  1.00 77.89           C  
ANISOU 4339  CB  ASN A 566     9083   9933  10579    461   2212   2653       C  
ATOM   4340  CG  ASN A 566      85.317 -17.343  60.331  1.00 86.21           C  
ANISOU 4340  CG  ASN A 566    10238  11013  11504    432   2299   2698       C  
ATOM   4341  OD1 ASN A 566      84.705 -16.797  61.251  1.00 93.07           O  
ANISOU 4341  OD1 ASN A 566    11147  11891  12325    464   2431   2764       O  
ATOM   4342  ND2 ASN A 566      86.428 -18.049  60.531  1.00 74.94           N  
ANISOU 4342  ND2 ASN A 566     8857   9599  10016    372   2222   2664       N  
ATOM   4343  N   LYS A 567      81.951 -17.099  59.341  1.00 84.10           N  
ANISOU 4343  N   LYS A 567     9700  10677  11578    538   2448   2910       N  
ATOM   4344  CA  LYS A 567      80.653 -17.180  60.012  1.00 74.62           C  
ANISOU 4344  CA  LYS A 567     8435   9462  10454    563   2593   3061       C  
ATOM   4345  C   LYS A 567      80.762 -16.963  61.512  1.00 77.82           C  
ANISOU 4345  C   LYS A 567     8941   9896  10732    562   2724   3118       C  
ATOM   4346  O   LYS A 567      79.906 -16.315  62.118  1.00 82.40           O  
ANISOU 4346  O   LYS A 567     9531  10478  11301    611   2856   3184       O  
ATOM   4347  CB  LYS A 567      79.975 -18.526  59.770  1.00 77.16           C  
ANISOU 4347  CB  LYS A 567     8612   9750  10955    521   2580   3190       C  
ATOM   4348  CG  LYS A 567      79.696 -18.890  58.329  1.00 85.76           C  
ANISOU 4348  CG  LYS A 567     9586  10805  12192    518   2458   3159       C  
ATOM   4349  CD  LYS A 567      78.800 -20.119  58.312  1.00103.96           C  
ANISOU 4349  CD  LYS A 567    11747  13070  14683    481   2479   3311       C  
ATOM   4350  CE  LYS A 567      79.458 -21.297  59.016  1.00102.56           C  
ANISOU 4350  CE  LYS A 567    11580  12892  14494    409   2465   3367       C  
ATOM   4351  NZ  LYS A 567      78.585 -22.510  58.994  1.00 99.49           N  
ANISOU 4351  NZ  LYS A 567    11048  12455  14297    370   2482   3518       N  
ATOM   4352  N   GLN A 568      81.841 -17.475  62.097  1.00 89.12           N  
ANISOU 4352  N   GLN A 568    10452  11348  12060    508   2687   3091       N  
ATOM   4353  CA  GLN A 568      82.050 -17.374  63.538  1.00 92.94           C  
ANISOU 4353  CA  GLN A 568    11040  11861  12413    498   2800   3148       C  
ATOM   4354  C   GLN A 568      82.488 -15.977  63.975  1.00 86.17           C  
ANISOU 4354  C   GLN A 568    10321  11031  11390    544   2841   3044       C  
ATOM   4355  O   GLN A 568      82.681 -15.723  65.164  1.00 80.07           O  
ANISOU 4355  O   GLN A 568     9647  10284  10493    543   2935   3078       O  
ATOM   4356  CB  GLN A 568      83.072 -18.426  63.996  1.00 94.38           C  
ANISOU 4356  CB  GLN A 568    11263  12055  12543    421   2739   3159       C  
ATOM   4357  CG  GLN A 568      82.575 -19.876  63.894  0.70 97.63           C  
ANISOU 4357  CG  GLN A 568    11549  12434  13113    372   2728   3292       C  
ATOM   4358  CD  GLN A 568      82.489 -20.388  62.462  0.70 96.54           C  
ANISOU 4358  CD  GLN A 568    11289  12261  13129    361   2595   3250       C  
ATOM   4359  OE1 GLN A 568      83.265 -19.989  61.591  0.70 91.19           O  
ANISOU 4359  OE1 GLN A 568    10642  11592  12414    365   2477   3108       O  
ATOM   4360  NE2 GLN A 568      81.528 -21.272  62.214  0.70 89.66           N  
ANISOU 4360  NE2 GLN A 568    10279  11351  12436    346   2615   3375       N  
ATOM   4361  N   GLY A 569      82.695 -15.086  63.011  1.00 83.34           N  
ANISOU 4361  N   GLY A 569     9973  10665  11028    582   2764   2917       N  
ATOM   4362  CA  GLY A 569      83.045 -13.720  63.341  1.00 71.88           C  
ANISOU 4362  CA  GLY A 569     8644   9228   9439    628   2799   2821       C  
ATOM   4363  C   GLY A 569      84.526 -13.513  63.508  1.00 75.27           C  
ANISOU 4363  C   GLY A 569     9194   9682   9722    589   2709   2694       C  
ATOM   4364  O   GLY A 569      84.955 -12.467  63.988  1.00 69.16           O  
ANISOU 4364  O   GLY A 569     8534   8921   8821    615   2740   2620       O  
ATOM   4365  N   LYS A 570      85.309 -14.508  63.113  1.00 82.98           N  
ANISOU 4365  N   LYS A 570    10143  10662  10722    527   2597   2671       N  
ATOM   4366  CA  LYS A 570      86.757 -14.435  63.238  1.00 81.56           C  
ANISOU 4366  CA  LYS A 570    10070  10506  10414    483   2503   2556       C  
ATOM   4367  C   LYS A 570      87.401 -14.048  61.923  1.00 79.58           C  
ANISOU 4367  C   LYS A 570     9806  10243  10186    488   2361   2411       C  
ATOM   4368  O   LYS A 570      86.807 -14.258  60.864  1.00 66.90           O  
ANISOU 4368  O   LYS A 570     8094   8614   8712    507   2313   2415       O  
ATOM   4369  CB  LYS A 570      87.310 -15.780  63.709  0.50 80.33           C  
ANISOU 4369  CB  LYS A 570     9906  10361  10255    409   2471   2624       C  
ATOM   4370  CG  LYS A 570      86.651 -16.301  64.966  0.50 87.17           C  
ANISOU 4370  CG  LYS A 570    10776  11234  11109    399   2608   2782       C  
ATOM   4371  CD  LYS A 570      87.180 -17.671  65.335  0.50 94.36           C  
ANISOU 4371  CD  LYS A 570    11675  12148  12032    324   2567   2854       C  
ATOM   4372  CE  LYS A 570      86.399 -18.254  66.501  0.50 94.60           C  
ANISOU 4372  CE  LYS A 570    11694  12179  12070    315   2706   3026       C  
ATOM   4373  NZ  LYS A 570      86.565 -19.732  66.600  0.50 86.85           N  
ANISOU 4373  NZ  LYS A 570    10654  11179  11165    248   2666   3123       N  
ATOM   4374  N   THR A 571      88.599 -13.469  61.987  1.00 76.60           N  
ANISOU 4374  N   THR A 571     9538   9884   9684    471   2293   2284       N  
ATOM   4375  CA  THR A 571      89.323 -13.109  60.778  1.00 65.22           C  
ANISOU 4375  CA  THR A 571     8093   8433   8256    471   2156   2144       C  
ATOM   4376  C   THR A 571      89.587 -14.381  59.976  1.00 64.85           C  
ANISOU 4376  C   THR A 571     7951   8381   8309    423   2049   2156       C  
ATOM   4377  O   THR A 571      90.086 -15.360  60.529  1.00 53.10           O  
ANISOU 4377  O   THR A 571     6472   6906   6798    366   2037   2206       O  
ATOM   4378  CB  THR A 571      90.659 -12.438  61.127  1.00 55.02           C  
ANISOU 4378  CB  THR A 571     6932   7160   6815    447   2103   2020       C  
ATOM   4379  OG1 THR A 571      90.419 -11.224  61.848  1.00 55.32           O  
ANISOU 4379  OG1 THR A 571     7056   7196   6765    492   2199   2006       O  
ATOM   4380  CG2 THR A 571      91.454 -12.121  59.867  1.00 55.99           C  
ANISOU 4380  CG2 THR A 571     7047   7272   6956    443   1960   1878       C  
ATOM   4381  N   GLN A 572      89.286 -14.366  58.679  1.00 62.95           N  
ANISOU 4381  N   GLN A 572     7624   8118   8174    446   1970   2113       N  
ATOM   4382  CA  GLN A 572      89.607 -15.505  57.815  1.00 56.73           C  
ANISOU 4382  CA  GLN A 572     6750   7324   7480    404   1857   2111       C  
ATOM   4383  C   GLN A 572      90.887 -15.288  57.020  1.00 67.31           C  
ANISOU 4383  C   GLN A 572     8138   8673   8763    381   1719   1958       C  
ATOM   4384  O   GLN A 572      91.710 -16.194  56.896  1.00 65.26           O  
ANISOU 4384  O   GLN A 572     7872   8422   8500    327   1638   1941       O  
ATOM   4385  CB  GLN A 572      88.448 -15.904  56.902  1.00 53.63           C  
ANISOU 4385  CB  GLN A 572     6220   6903   7255    432   1850   2180       C  
ATOM   4386  CG  GLN A 572      87.699 -14.752  56.285  1.00 57.73           C  
ANISOU 4386  CG  GLN A 572     6729   7404   7800    502   1876   2144       C  
ATOM   4387  CD  GLN A 572      86.638 -15.227  55.316  1.00 63.28           C  
ANISOU 4387  CD  GLN A 572     7296   8078   8670    522   1853   2211       C  
ATOM   4388  OE1 GLN A 572      86.553 -16.419  55.012  1.00 50.70           O  
ANISOU 4388  OE1 GLN A 572     5614   6475   7175    482   1804   2271       O  
ATOM   4389  NE2 GLN A 572      85.812 -14.300  54.833  1.00 58.35           N  
ANISOU 4389  NE2 GLN A 572     6654   7436   8081    582   1887   2205       N  
ATOM   4390  N   PHE A 573      91.017 -14.103  56.426  1.00 61.10           N  
ANISOU 4390  N   PHE A 573     7394   7881   7942    424   1691   1852       N  
ATOM   4391  CA  PHE A 573      92.267 -13.716  55.794  1.00 42.38           C  
ANISOU 4391  CA  PHE A 573     5082   5516   5503    405   1573   1704       C  
ATOM   4392  C   PHE A 573      92.635 -12.269  56.154  1.00 54.93           C  
ANISOU 4392  C   PHE A 573     6783   7104   6983    435   1605   1617       C  
ATOM   4393  O   PHE A 573      91.784 -11.374  56.135  1.00 57.17           O  
ANISOU 4393  O   PHE A 573     7068   7369   7285    492   1675   1634       O  
ATOM   4394  CB  PHE A 573      92.139 -13.822  54.282  1.00 39.96           C  
ANISOU 4394  CB  PHE A 573     4695   5193   5295    423   1466   1649       C  
ATOM   4395  CG  PHE A 573      92.005 -15.223  53.791  1.00 41.02           C  
ANISOU 4395  CG  PHE A 573     4725   5326   5536    388   1408   1713       C  
ATOM   4396  CD1 PHE A 573      93.132 -15.965  53.484  1.00 47.53           C  
ANISOU 4396  CD1 PHE A 573     5558   6163   6337    336   1302   1652       C  
ATOM   4397  CD2 PHE A 573      90.757 -15.779  53.550  1.00 46.24           C  
ANISOU 4397  CD2 PHE A 573     5275   5965   6328    408   1450   1829       C  
ATOM   4398  CE1 PHE A 573      93.025 -17.267  53.010  1.00 37.54           C  
ANISOU 4398  CE1 PHE A 573     4196   4890   5177    304   1243   1712       C  
ATOM   4399  CE2 PHE A 573      90.637 -17.078  53.071  1.00 34.77           C  
ANISOU 4399  CE2 PHE A 573     3722   4502   4986    374   1389   1889       C  
ATOM   4400  CZ  PHE A 573      91.776 -17.823  52.797  1.00 41.79           C  
ANISOU 4400  CZ  PHE A 573     4625   5404   5851    323   1284   1830       C  
ATOM   4401  N   ASP A 574      93.907 -12.036  56.471  1.00 49.72           N  
ANISOU 4401  N   ASP A 574     6216   6461   6217    396   1552   1525       N  
ATOM   4402  CA  ASP A 574      94.383 -10.685  56.739  1.00 41.18           C  
ANISOU 4402  CA  ASP A 574     5236   5371   5041    418   1565   1434       C  
ATOM   4403  C   ASP A 574      94.961 -10.105  55.442  1.00 53.07           C  
ANISOU 4403  C   ASP A 574     6736   6856   6571    428   1446   1306       C  
ATOM   4404  O   ASP A 574      95.264 -10.852  54.509  1.00 50.02           O  
ANISOU 4404  O   ASP A 574     6286   6473   6245    406   1349   1278       O  
ATOM   4405  CB  ASP A 574      95.469 -10.729  57.817  1.00 37.25           C  
ANISOU 4405  CB  ASP A 574     4839   4898   4416    367   1570   1410       C  
ATOM   4406  CG  ASP A 574      95.680  -9.384  58.489  1.00 50.24           C  
ANISOU 4406  CG  ASP A 574     6590   6534   5967    393   1626   1361       C  
ATOM   4407  OD1 ASP A 574      95.203  -8.368  57.945  1.00 59.38           O  
ANISOU 4407  OD1 ASP A 574     7747   7660   7156    446   1637   1321       O  
ATOM   4408  OD2 ASP A 574      96.371  -9.331  59.531  1.00 40.75           O  
ANISOU 4408  OD2 ASP A 574     5472   5353   4658    359   1652   1361       O  
ATOM   4409  N   PHE A 575      95.143  -8.786  55.391  1.00 59.98           N  
ANISOU 4409  N   PHE A 575     7681   7708   7400    459   1454   1231       N  
ATOM   4410  CA  PHE A 575      95.873  -8.154  54.293  1.00 40.91           C  
ANISOU 4410  CA  PHE A 575     5279   5270   4993    460   1341   1107       C  
ATOM   4411  C   PHE A 575      97.345  -8.559  54.361  1.00 43.16           C  
ANISOU 4411  C   PHE A 575     5607   5576   5216    394   1249   1025       C  
ATOM   4412  O   PHE A 575      97.910  -8.692  55.449  1.00 43.65           O  
ANISOU 4412  O   PHE A 575     5732   5659   5193    359   1285   1040       O  
ATOM   4413  CB  PHE A 575      95.763  -6.627  54.374  1.00 56.92           C  
ANISOU 4413  CB  PHE A 575     7380   7261   6986    503   1379   1057       C  
ATOM   4414  CG  PHE A 575      94.410  -6.093  53.985  1.00 54.53           C  
ANISOU 4414  CG  PHE A 575     7034   6931   6755    570   1445   1117       C  
ATOM   4415  CD1 PHE A 575      94.139  -5.717  52.680  1.00 50.55           C  
ANISOU 4415  CD1 PHE A 575     6485   6399   6321    599   1374   1074       C  
ATOM   4416  CD2 PHE A 575      93.419  -5.943  54.940  1.00 41.66           C  
ANISOU 4416  CD2 PHE A 575     5410   5303   5116    605   1580   1218       C  
ATOM   4417  CE1 PHE A 575      92.893  -5.225  52.331  1.00 60.52           C  
ANISOU 4417  CE1 PHE A 575     7710   7638   7649    659   1434   1134       C  
ATOM   4418  CE2 PHE A 575      92.170  -5.454  54.599  1.00 46.85           C  
ANISOU 4418  CE2 PHE A 575     6025   5935   5843    667   1644   1277       C  
ATOM   4419  CZ  PHE A 575      91.903  -5.093  53.296  1.00 58.85           C  
ANISOU 4419  CZ  PHE A 575     7500   7428   7435    694   1571   1236       C  
ATOM   4420  N   THR A 576      97.960  -8.755  53.200  1.00 45.71           N  
ANISOU 4420  N   THR A 576     5895   5892   5579    377   1129    943       N  
ATOM   4421  CA  THR A 576      99.381  -9.053  53.123  1.00 45.11           C  
ANISOU 4421  CA  THR A 576     5855   5832   5455    318   1035    857       C  
ATOM   4422  C   THR A 576     100.104  -8.167  52.104  1.00 49.44           C  
ANISOU 4422  C   THR A 576     6422   6348   6014    321    939    736       C  
ATOM   4423  O   THR A 576     101.321  -7.980  52.177  1.00 41.59           O  
ANISOU 4423  O   THR A 576     5476   5354   4973    278    877    658       O  
ATOM   4424  CB  THR A 576      99.623 -10.523  52.770  1.00 47.94           C  
ANISOU 4424  CB  THR A 576     6143   6218   5852    278    975    885       C  
ATOM   4425  OG1 THR A 576      98.861 -10.855  51.603  1.00 40.26           O  
ANISOU 4425  OG1 THR A 576     5080   5236   4981    312    936    900       O  
ATOM   4426  CG2 THR A 576      99.190 -11.434  53.917  1.00 47.67           C  
ANISOU 4426  CG2 THR A 576     6104   6211   5798    257   1062   1004       C  
ATOM   4427  N   GLY A 577      99.343  -7.594  51.177  1.00 47.78           N  
ANISOU 4427  N   GLY A 577     6177   6108   5869    371    929    729       N  
ATOM   4428  CA  GLY A 577      99.946  -6.808  50.119  1.00 43.51           C  
ANISOU 4428  CA  GLY A 577     5649   5533   5348    372    836    628       C  
ATOM   4429  C   GLY A 577     100.607  -5.555  50.626  1.00 38.29           C  
ANISOU 4429  C   GLY A 577     5079   4840   4630    366    851    570       C  
ATOM   4430  O   GLY A 577     100.203  -4.989  51.631  1.00 46.14           O  
ANISOU 4430  O   GLY A 577     6126   5827   5579    387    950    614       O  
ATOM   4431  N   LYS A 578     101.624  -5.113  49.897  1.00 51.62           N  
ANISOU 4431  N   LYS A 578     6784   6503   6326    338    754    476       N  
ATOM   4432  CA  LYS A 578     102.361  -3.904  50.234  1.00 52.39           C  
ANISOU 4432  CA  LYS A 578     6960   6559   6387    327    754    419       C  
ATOM   4433  C   LYS A 578     102.587  -3.147  48.935  1.00 40.25           C  
ANISOU 4433  C   LYS A 578     5411   4974   4910    333    670    354       C  
ATOM   4434  O   LYS A 578     102.804  -3.753  47.884  1.00 48.57           O  
ANISOU 4434  O   LYS A 578     6405   6038   6011    319    581    324       O  
ATOM   4435  CB  LYS A 578     103.725  -4.253  50.854  1.00 50.70           C  
ANISOU 4435  CB  LYS A 578     6780   6363   6119    265    715    375       C  
ATOM   4436  CG  LYS A 578     103.675  -5.151  52.079  1.00 56.03           C  
ANISOU 4436  CG  LYS A 578     7468   7092   6729    246    781    441       C  
ATOM   4437  CD  LYS A 578     103.053  -4.393  53.258  1.00 67.69           C  
ANISOU 4437  CD  LYS A 578     9013   8561   8147    278    901    496       C  
ATOM   4438  CE  LYS A 578     103.054  -5.225  54.531  1.00 62.25           C  
ANISOU 4438  CE  LYS A 578     8344   7924   7384    255    968    567       C  
ATOM   4439  NZ  LYS A 578     102.685  -4.403  55.720  1.00 49.32           N  
ANISOU 4439  NZ  LYS A 578     6786   6278   5676    280   1078    609       N  
ATOM   4440  N   LEU A 579     102.497  -1.823  49.002  1.00 37.44           N  
ANISOU 4440  N   LEU A 579     5112   4566   4549    355    700    340       N  
ATOM   4441  CA  LEU A 579     102.670  -1.002  47.810  1.00 41.30           C  
ANISOU 4441  CA  LEU A 579     5594   5004   5092    358    628    291       C  
ATOM   4442  C   LEU A 579     103.949  -1.291  47.035  1.00 41.40           C  
ANISOU 4442  C   LEU A 579     5584   5012   5134    299    509    216       C  
ATOM   4443  O   LEU A 579     105.044  -1.272  47.590  1.00 36.79           O  
ANISOU 4443  O   LEU A 579     5033   4424   4521    252    493    180       O  
ATOM   4444  CB  LEU A 579     102.623   0.485  48.160  1.00 40.88           C  
ANISOU 4444  CB  LEU A 579     5617   4892   5023    377    679    285       C  
ATOM   4445  CG  LEU A 579     101.259   1.046  48.553  1.00 38.42           C  
ANISOU 4445  CG  LEU A 579     5323   4569   4704    444    787    355       C  
ATOM   4446  CD1 LEU A 579     101.390   2.536  48.826  1.00 37.50           C  
ANISOU 4446  CD1 LEU A 579     5287   4389   4571    455    827    339       C  
ATOM   4447  CD2 LEU A 579     100.258   0.767  47.446  1.00 28.07           C  
ANISOU 4447  CD2 LEU A 579     3942   3265   3457    484    761    386       C  
ATOM   4448  N   SER A 580     103.788  -1.553  45.745  1.00 32.20           N  
ANISOU 4448  N   SER A 580     4353   3862   4022    288    422    195       N  
ATOM   4449  CA  SER A 580     104.913  -1.641  44.824  1.00 41.46           C  
ANISOU 4449  CA  SER A 580     5459   5083   5212    185    277    114       C  
ATOM   4450  C   SER A 580     105.013  -0.351  44.004  1.00 45.08           C  
ANISOU 4450  C   SER A 580     5884   5557   5685    140    211     78       C  
ATOM   4451  O   SER A 580     105.918  -0.183  43.195  1.00 34.23           O  
ANISOU 4451  O   SER A 580     4475   4219   4314     85    148     50       O  
ATOM   4452  CB  SER A 580     104.795  -2.868  43.921  1.00 25.20           C  
ANISOU 4452  CB  SER A 580     3318   3082   3175    152    194     97       C  
ATOM   4453  OG  SER A 580     103.691  -2.734  43.057  1.00 40.73           O  
ANISOU 4453  OG  SER A 580     5251   5071   5154    161    182    107       O  
ATOM   4454  N   PHE A 581     104.066   0.556  44.244  1.00 37.97           N  
ANISOU 4454  N   PHE A 581     5030   4621   4776    191    285    115       N  
ATOM   4455  CA  PHE A 581     104.085   1.905  43.687  1.00 41.11           C  
ANISOU 4455  CA  PHE A 581     5422   5020   5178    169    260     95       C  
ATOM   4456  C   PHE A 581     103.820   2.920  44.790  1.00 45.22           C  
ANISOU 4456  C   PHE A 581     6040   5468   5672    222    370    129       C  
ATOM   4457  O   PHE A 581     102.942   2.716  45.626  1.00 42.61           O  
ANISOU 4457  O   PHE A 581     5774   5091   5324    302    492    188       O  
ATOM   4458  CB  PHE A 581     102.980   2.041  42.641  1.00 32.13           C  
ANISOU 4458  CB  PHE A 581     4247   3952   4010    158    275    119       C  
ATOM   4459  CG  PHE A 581     103.296   1.399  41.323  1.00 36.28           C  
ANISOU 4459  CG  PHE A 581     4749   4476   4560    162    236    110       C  
ATOM   4460  CD1 PHE A 581     103.706   2.178  40.246  1.00 24.37           C  
ANISOU 4460  CD1 PHE A 581     3177   3028   3055     81    137     60       C  
ATOM   4461  CD2 PHE A 581     103.268   0.016  41.176  1.00 27.90           C  
ANISOU 4461  CD2 PHE A 581     3622   3477   3501    107    162     85       C  
ATOM   4462  CE1 PHE A 581     104.010   1.591  39.023  1.00 36.42           C  
ANISOU 4462  CE1 PHE A 581     4651   4578   4607     46     56     27       C  
ATOM   4463  CE2 PHE A 581     103.575  -0.575  39.962  1.00 31.08           C  
ANISOU 4463  CE2 PHE A 581     3981   3911   3919     62     87     51       C  
ATOM   4464  CZ  PHE A 581     103.951   0.212  38.883  1.00 41.08           C  
ANISOU 4464  CZ  PHE A 581     5224   5192   5195     27     37     21       C  
ATOM   4465  N   SER A 582     104.551   4.032  44.777  1.00 44.10           N  
ANISOU 4465  N   SER A 582     5909   5318   5528    185    343    101       N  
ATOM   4466  CA  SER A 582     104.348   5.062  45.795  1.00 40.44           C  
ANISOU 4466  CA  SER A 582     5554   4780   5031    231    457    128       C  
ATOM   4467  C   SER A 582     103.019   5.758  45.571  1.00 29.67           C  
ANISOU 4467  C   SER A 582     4208   3396   3671    288    519    169       C  
ATOM   4468  O   SER A 582     102.623   5.998  44.438  1.00 39.18           O  
ANISOU 4468  O   SER A 582     5338   4646   4902    264    443    156       O  
ATOM   4469  CB  SER A 582     105.484   6.085  45.774  1.00 30.36           C  
ANISOU 4469  CB  SER A 582     4277   3505   3754    175    408     90       C  
ATOM   4470  OG  SER A 582     106.739   5.473  46.007  1.00 36.84           O  
ANISOU 4470  OG  SER A 582     5072   4349   4576    126    354     60       O  
ATOM   4471  N   TRP A 583     102.331   6.079  46.659  1.00 36.53           N  
ANISOU 4471  N   TRP A 583     5177   4193   4510    367    661    222       N  
ATOM   4472  CA  TRP A 583     101.024   6.718  46.569  1.00 34.49           C  
ANISOU 4472  CA  TRP A 583     4934   3911   4257    433    737    273       C  
ATOM   4473  C   TRP A 583     101.177   8.234  46.782  1.00 33.54           C  
ANISOU 4473  C   TRP A 583     4876   3746   4120    430    771    263       C  
ATOM   4474  O   TRP A 583     101.800   8.669  47.749  1.00 31.53           O  
ANISOU 4474  O   TRP A 583     4713   3437   3831    432    831    257       O  
ATOM   4475  CB  TRP A 583     100.049   6.132  47.591  1.00 34.16           C  
ANISOU 4475  CB  TRP A 583     4949   3826   4205    535    883    354       C  
ATOM   4476  CG  TRP A 583      98.629   6.317  47.167  1.00 29.82           C  
ANISOU 4476  CG  TRP A 583     4362   3285   3683    594    930    413       C  
ATOM   4477  CD1 TRP A 583      97.881   7.458  47.247  1.00 35.27           C  
ANISOU 4477  CD1 TRP A 583     5092   3937   4371    637   1000    445       C  
ATOM   4478  CD2 TRP A 583      97.795   5.327  46.565  1.00 34.33           C  
ANISOU 4478  CD2 TRP A 583     4847   3909   4290    613    908    450       C  
ATOM   4479  NE1 TRP A 583      96.626   7.229  46.735  1.00 43.57           N  
ANISOU 4479  NE1 TRP A 583     6084   5014   5456    682   1024    501       N  
ATOM   4480  CE2 TRP A 583      96.549   5.927  46.313  1.00 32.79           C  
ANISOU 4480  CE2 TRP A 583     4640   3704   4114    667    968    506       C  
ATOM   4481  CE3 TRP A 583      97.977   3.980  46.227  1.00 39.79           C  
ANISOU 4481  CE3 TRP A 583     5469   4651   4997    590    847    445       C  
ATOM   4482  CZ2 TRP A 583      95.492   5.231  45.731  1.00 35.11           C  
ANISOU 4482  CZ2 TRP A 583     4855   4039   4445    693    965    556       C  
ATOM   4483  CZ3 TRP A 583      96.929   3.296  45.649  1.00 41.90           C  
ANISOU 4483  CZ3 TRP A 583     5661   4959   5299    615    844    493       C  
ATOM   4484  CH2 TRP A 583      95.701   3.922  45.407  1.00 33.65           C  
ANISOU 4484  CH2 TRP A 583     4606   3904   4276    664    902    548       C  
ATOM   4485  N   PRO A 584     100.650   9.040  45.848  1.00 31.58           N  
ANISOU 4485  N   PRO A 584     4583   3523   3894    420    729    260       N  
ATOM   4486  CA  PRO A 584     100.883  10.489  45.864  1.00 48.18           C  
ANISOU 4486  CA  PRO A 584     6729   5592   5985    409    743    246       C  
ATOM   4487  C   PRO A 584     100.097  11.233  46.951  1.00 54.89           C  
ANISOU 4487  C   PRO A 584     7694   6357   6805    493    902    302       C  
ATOM   4488  O   PRO A 584      98.938  10.910  47.233  1.00 52.74           O  
ANISOU 4488  O   PRO A 584     7434   6067   6539    570    992    364       O  
ATOM   4489  CB  PRO A 584     100.405  10.924  44.476  1.00 41.06           C  
ANISOU 4489  CB  PRO A 584     5740   4745   5116    382    655    234       C  
ATOM   4490  CG  PRO A 584      99.348   9.946  44.137  1.00 40.36           C  
ANISOU 4490  CG  PRO A 584     5607   4684   5045    421    666    271       C  
ATOM   4491  CD  PRO A 584      99.851   8.633  44.683  1.00 36.18           C  
ANISOU 4491  CD  PRO A 584     5072   4164   4510    415    662    266       C  
ATOM   4492  N   LYS A 585     100.736  12.237  47.548  1.00 58.08           N  
ANISOU 4492  N   LYS A 585     8179   6710   7180    478    939    283       N  
ATOM   4493  CA  LYS A 585     100.086  13.068  48.553  1.00 42.95           C  
ANISOU 4493  CA  LYS A 585     6380   4708   5232    551   1089    330       C  
ATOM   4494  C   LYS A 585      99.503  14.316  47.884  1.00 46.83           C  
ANISOU 4494  C   LYS A 585     6859   5196   5738    560   1088    338       C  
ATOM   4495  O   LYS A 585      98.506  14.858  48.345  1.00 38.35           O  
ANISOU 4495  O   LYS A 585     5846   4070   4656    635   1205    392       O  
ATOM   4496  CB  LYS A 585     101.114  13.455  49.618  1.00 39.95           C  
ANISOU 4496  CB  LYS A 585     6108   4268   4804    527   1134    303       C  
ATOM   4497  CG  LYS A 585     100.646  14.459  50.656  1.00 58.45           C  
ANISOU 4497  CG  LYS A 585     8587   6515   7105    589   1283    340       C  
ATOM   4498  CD  LYS A 585     101.809  14.857  51.569  1.00 61.87           C  
ANISOU 4498  CD  LYS A 585     9113   6911   7485    539   1300    300       C  
ATOM   4499  CE  LYS A 585     102.303  13.694  52.403  1.00 71.26           C  
ANISOU 4499  CE  LYS A 585    10285   8165   8625    509   1291    288       C  
ATOM   4500  NZ  LYS A 585     103.340  14.114  53.386  1.00 60.94           N  
ANISOU 4500  NZ  LYS A 585     9058   6845   7250    458   1309    253       N  
ATOM   4501  N   TYR A 586     100.085  14.713  46.754  1.00 42.73           N  
ANISOU 4501  N   TYR A 586     6256   4737   5244    487    958    290       N  
ATOM   4502  CA  TYR A 586      99.645  15.903  46.022  1.00 37.23           C  
ANISOU 4502  CA  TYR A 586     5543   4041   4560    489    946    293       C  
ATOM   4503  C   TYR A 586      99.299  15.514  44.582  1.00 46.82           C  
ANISOU 4503  C   TYR A 586     6634   5339   5815    458    829    280       C  
ATOM   4504  O   TYR A 586      99.799  14.503  44.072  1.00 56.53           O  
ANISOU 4504  O   TYR A 586     7787   6629   7063    411    732    250       O  
ATOM   4505  CB  TYR A 586     100.749  16.969  46.011  1.00 38.61           C  
ANISOU 4505  CB  TYR A 586     5743   4204   4722    431    908    250       C  
ATOM   4506  CG  TYR A 586     101.229  17.347  47.400  1.00 49.73           C  
ANISOU 4506  CG  TYR A 586     7280   5531   6084    447   1013    253       C  
ATOM   4507  CD1 TYR A 586     100.441  18.116  48.251  1.00 52.25           C  
ANISOU 4507  CD1 TYR A 586     7712   5766   6373    517   1157    297       C  
ATOM   4508  CD2 TYR A 586     102.475  16.946  47.853  1.00 40.56           C  
ANISOU 4508  CD2 TYR A 586     6131   4375   4907    390    972    214       C  
ATOM   4509  CE1 TYR A 586     100.883  18.455  49.519  1.00 55.64           C  
ANISOU 4509  CE1 TYR A 586     8271   6117   6754    529   1256    297       C  
ATOM   4510  CE2 TYR A 586     102.919  17.279  49.112  1.00 49.15           C  
ANISOU 4510  CE2 TYR A 586     7344   5385   5945    399   1068    214       C  
ATOM   4511  CZ  TYR A 586     102.123  18.031  49.941  1.00 62.05           C  
ANISOU 4511  CZ  TYR A 586     9098   6934   7545    467   1209    254       C  
ATOM   4512  OH  TYR A 586     102.572  18.361  51.198  1.00 61.02           O  
ANISOU 4512  OH  TYR A 586     9105   6723   7359    474   1307    253       O  
ATOM   4513  N   ASP A 587      98.418  16.282  43.940  1.00 34.53           N  
ANISOU 4513  N   ASP A 587     5065   3784   4272    486    844    304       N  
ATOM   4514  CA  ASP A 587      97.927  15.918  42.611  1.00 37.69           C  
ANISOU 4514  CA  ASP A 587     5364   4254   4703    463    749    297       C  
ATOM   4515  C   ASP A 587      98.956  16.132  41.501  1.00 48.76           C  
ANISOU 4515  C   ASP A 587     6700   5713   6114    383    626    244       C  
ATOM   4516  O   ASP A 587      98.659  15.875  40.331  1.00 48.95           O  
ANISOU 4516  O   ASP A 587     6644   5897   6057    329    636    241       O  
ATOM   4517  CB  ASP A 587      96.597  16.635  42.292  1.00 49.88           C  
ANISOU 4517  CB  ASP A 587     6921   5777   6254    525    817    348       C  
ATOM   4518  CG  ASP A 587      96.725  18.140  42.114  1.00 50.96           C  
ANISOU 4518  CG  ASP A 587     7096   5883   6382    523    836    343       C  
ATOM   4519  OD1 ASP A 587      97.806  18.710  42.356  1.00 49.93           O  
ANISOU 4519  OD1 ASP A 587     6992   5739   6239    479    810    305       O  
ATOM   4520  OD2 ASP A 587      95.703  18.751  41.721  1.00 44.60           O  
ANISOU 4520  OD2 ASP A 587     6294   5067   5584    568    880    381       O  
ATOM   4521  N   ASP A 588     100.131  16.655  41.852  1.00 33.43           N  
ANISOU 4521  N   ASP A 588     4785   3757   4159    346    613    212       N  
ATOM   4522  CA  ASP A 588     101.172  16.896  40.848  1.00 45.09           C  
ANISOU 4522  CA  ASP A 588     6191   5391   5549    267    595    159       C  
ATOM   4523  C   ASP A 588     102.466  16.158  41.147  1.00 32.40           C  
ANISOU 4523  C   ASP A 588     4566   3799   3945    222    540    128       C  
ATOM   4524  O   ASP A 588     103.514  16.479  40.596  1.00 41.17           O  
ANISOU 4524  O   ASP A 588     5652   4928   5061    183    486    103       O  
ATOM   4525  CB  ASP A 588     101.447  18.405  40.666  1.00 46.66           C  
ANISOU 4525  CB  ASP A 588     6425   5568   5735    265    621    156       C  
ATOM   4526  CG  ASP A 588     102.110  19.049  41.893  1.00 46.33           C  
ANISOU 4526  CG  ASP A 588     6456   5480   5667    261    672    149       C  
ATOM   4527  OD1 ASP A 588     102.210  18.407  42.962  1.00 61.93           O  
ANISOU 4527  OD1 ASP A 588     8492   7301   7736    290    637    165       O  
ATOM   4528  OD2 ASP A 588     102.583  20.195  41.769  1.00 60.69           O  
ANISOU 4528  OD2 ASP A 588     8332   7150   7578    272    623    153       O  
ATOM   4529  N   GLN A 589     102.381  15.123  41.969  1.00 49.91           N  
ANISOU 4529  N   GLN A 589     6816   5906   6243    250    502    145       N  
ATOM   4530  CA  GLN A 589     103.541  14.285  42.224  1.00 43.88           C  
ANISOU 4530  CA  GLN A 589     6028   5167   5477    206    455    116       C  
ATOM   4531  C   GLN A 589     103.648  13.214  41.152  1.00 52.63           C  
ANISOU 4531  C   GLN A 589     7053   6344   6600    181    381    103       C  
ATOM   4532  O   GLN A 589     103.424  12.032  41.407  1.00 43.59           O  
ANISOU 4532  O   GLN A 589     5872   5290   5399    170    408     98       O  
ATOM   4533  CB  GLN A 589     103.433  13.658  43.607  1.00 48.04           C  
ANISOU 4533  CB  GLN A 589     6582   5759   5910    209    553    117       C  
ATOM   4534  CG  GLN A 589     103.927  14.564  44.728  1.00 53.37           C  
ANISOU 4534  CG  GLN A 589     7367   6264   6646    231    564    125       C  
ATOM   4535  CD  GLN A 589     103.844  13.893  46.081  1.00 45.29           C  
ANISOU 4535  CD  GLN A 589     6442   5179   5585    268    667    144       C  
ATOM   4536  OE1 GLN A 589     102.861  13.218  46.387  1.00 37.54           O  
ANISOU 4536  OE1 GLN A 589     5485   4179   4598    325    733    180       O  
ATOM   4537  NE2 GLN A 589     104.879  14.059  46.893  1.00 38.81           N  
ANISOU 4537  NE2 GLN A 589     5679   4328   4738    239    685    124       N  
ATOM   4538  N   PHE A 590     104.025  13.642  39.952  1.00 54.04           N  
ANISOU 4538  N   PHE A 590     7167   6634   6731    141    362     79       N  
ATOM   4539  CA  PHE A 590     103.962  12.796  38.764  1.00 38.60           C  
ANISOU 4539  CA  PHE A 590     5152   4671   4844    132    262     75       C  
ATOM   4540  C   PHE A 590     105.077  11.758  38.739  1.00 41.41           C  
ANISOU 4540  C   PHE A 590     5520   5042   5172    114    280     64       C  
ATOM   4541  O   PHE A 590     104.904  10.638  38.233  1.00 22.80           O  
ANISOU 4541  O   PHE A 590     3056   2749   2858     79    164     45       O  
ATOM   4542  CB  PHE A 590     103.990  13.629  37.481  1.00 36.29           C  
ANISOU 4542  CB  PHE A 590     4815   4455   4519    109    252     62       C  
ATOM   4543  CG  PHE A 590     102.816  14.562  37.332  1.00 45.62           C  
ANISOU 4543  CG  PHE A 590     6031   5613   5688    147    310     86       C  
ATOM   4544  CD1 PHE A 590     101.531  14.060  37.213  1.00 46.82           C  
ANISOU 4544  CD1 PHE A 590     6267   5677   5846    243    417    149       C  
ATOM   4545  CD2 PHE A 590     103.002  15.929  37.265  1.00 47.52           C  
ANISOU 4545  CD2 PHE A 590     6318   5770   5968    167    307     97       C  
ATOM   4546  CE1 PHE A 590     100.451  14.904  37.060  1.00 49.88           C  
ANISOU 4546  CE1 PHE A 590     6606   6068   6277    244    356    137       C  
ATOM   4547  CE2 PHE A 590     101.919  16.789  37.110  1.00 44.12           C  
ANISOU 4547  CE2 PHE A 590     5903   5383   5478    191    393    114       C  
ATOM   4548  CZ  PHE A 590     100.643  16.267  37.010  1.00 46.80           C  
ANISOU 4548  CZ  PHE A 590     6241   5723   5818    217    417    152       C  
ATOM   4549  N   THR A 591     106.221  12.109  39.315  1.00 29.68           N  
ANISOU 4549  N   THR A 591     3980   3618   3680     66    224     35       N  
ATOM   4550  CA  THR A 591     107.334  11.174  39.298  1.00 40.90           C  
ANISOU 4550  CA  THR A 591     5355   5069   5117     37    168     19       C  
ATOM   4551  C   THR A 591     107.828  10.902  40.703  1.00 52.20           C  
ANISOU 4551  C   THR A 591     6845   6426   6563     41    192     21       C  
ATOM   4552  O   THR A 591     108.899  11.357  41.104  1.00 65.48           O  
ANISOU 4552  O   THR A 591     8530   8146   8202     21    209     10       O  
ATOM   4553  CB  THR A 591     108.514  11.704  38.434  1.00 45.42           C  
ANISOU 4553  CB  THR A 591     5876   5674   5706     15    114      7       C  
ATOM   4554  OG1 THR A 591     108.833  13.040  38.820  1.00 43.12           O  
ANISOU 4554  OG1 THR A 591     5641   5321   5423     19    143      9       O  
ATOM   4555  CG2 THR A 591     108.153  11.701  36.950  1.00 52.56           C  
ANISOU 4555  CG2 THR A 591     6721   6616   6633     10     60      5       C  
ATOM   4556  N   LEU A 592     106.971  10.239  41.478  1.00 35.62           N  
ANISOU 4556  N   LEU A 592     4783   4295   4457     67    231     35       N  
ATOM   4557  CA  LEU A 592     107.261   9.914  42.866  1.00 30.01           C  
ANISOU 4557  CA  LEU A 592     4118   3601   3683     66    298     34       C  
ATOM   4558  C   LEU A 592     107.751   8.443  42.964  1.00 40.01           C  
ANISOU 4558  C   LEU A 592     5345   4895   4964     50    255     25       C  
ATOM   4559  O   LEU A 592     106.948   7.492  42.867  1.00 31.28           O  
ANISOU 4559  O   LEU A 592     4223   3795   3865     66    255     34       O  
ATOM   4560  CB  LEU A 592     105.953  10.073  43.638  1.00 34.37           C  
ANISOU 4560  CB  LEU A 592     4731   4113   4216    113    379     60       C  
ATOM   4561  CG  LEU A 592     105.885   9.748  45.118  1.00 37.39           C  
ANISOU 4561  CG  LEU A 592     5181   4454   4572    133    443     70       C  
ATOM   4562  CD1 LEU A 592     106.680  10.784  45.881  1.00 39.61           C  
ANISOU 4562  CD1 LEU A 592     5543   4603   4904    131    437     64       C  
ATOM   4563  CD2 LEU A 592     104.435   9.746  45.560  1.00 35.39           C  
ANISOU 4563  CD2 LEU A 592     5010   4061   4375    219    505    116       C  
ATOM   4564  N   ASN A 593     109.052   8.236  43.159  1.00 34.58           N  
ANISOU 4564  N   ASN A 593     4648   4173   4318     23    204     11       N  
ATOM   4565  CA  ASN A 593     109.592   6.864  43.162  1.00 36.26           C  
ANISOU 4565  CA  ASN A 593     4808   4462   4507      7    181      3       C  
ATOM   4566  C   ASN A 593     110.542   6.603  44.327  1.00 42.40           C  
ANISOU 4566  C   ASN A 593     5625   5220   5265     -7    202     -3       C  
ATOM   4567  O   ASN A 593     111.249   7.516  44.737  1.00 47.62           O  
ANISOU 4567  O   ASN A 593     6326   5814   5951    -20    202     -9       O  
ATOM   4568  CB  ASN A 593     110.287   6.579  41.841  1.00 21.92           C  
ANISOU 4568  CB  ASN A 593     2906   2679   2744     -7     94     -3       C  
ATOM   4569  CG  ASN A 593     109.330   6.633  40.667  1.00 42.09           C  
ANISOU 4569  CG  ASN A 593     5418   5277   5298      2     76      1       C  
ATOM   4570  OD1 ASN A 593     108.327   5.924  40.631  1.00 27.41           O  
ANISOU 4570  OD1 ASN A 593     3563   3414   3438     11     84      6       O  
ATOM   4571  ND2 ASN A 593     109.624   7.500  39.707  1.00 27.28           N  
ANISOU 4571  ND2 ASN A 593     3510   3412   3442     -1     43     -1       N  
ATOM   4572  N   LEU A 594     110.570   5.382  44.873  1.00 39.75           N  
ANISOU 4572  N   LEU A 594     5290   4884   4928     -7    201     -3       N  
ATOM   4573  CA  LEU A 594     111.459   5.135  46.018  1.00 31.28           C  
ANISOU 4573  CA  LEU A 594     4270   3740   3876    -24    203    -10       C  
ATOM   4574  C   LEU A 594     112.905   5.430  45.626  1.00 41.11           C  
ANISOU 4574  C   LEU A 594     5470   5024   5127    -53    164    -21       C  
ATOM   4575  O   LEU A 594     113.305   5.262  44.457  1.00 36.12           O  
ANISOU 4575  O   LEU A 594     4752   4479   4491    -46    124    -18       O  
ATOM   4576  CB  LEU A 594     111.370   3.711  46.550  1.00 35.34           C  
ANISOU 4576  CB  LEU A 594     4785   4253   4389    -22    202     -9       C  
ATOM   4577  CG  LEU A 594     112.295   2.605  46.072  1.00 53.67           C  
ANISOU 4577  CG  LEU A 594     7034   6631   6725    -43    147    -17       C  
ATOM   4578  CD1 LEU A 594     112.162   1.399  46.997  1.00 45.38           C  
ANISOU 4578  CD1 LEU A 594     6013   5603   5628    -38    182    -15       C  
ATOM   4579  CD2 LEU A 594     112.121   2.256  44.625  1.00 91.45           C  
ANISOU 4579  CD2 LEU A 594    11726  11504  11516    -31    102    -13       C  
ATOM   4580  N   ASN A 595     113.659   5.903  46.618  1.00 35.89           N  
ANISOU 4580  N   ASN A 595     4859   4378   4399    -65    210    -25       N  
ATOM   4581  CA  ASN A 595     115.057   6.317  46.475  1.00 30.62           C  
ANISOU 4581  CA  ASN A 595     4167   3731   3735    -85    186    -32       C  
ATOM   4582  C   ASN A 595     115.208   7.705  45.834  1.00 45.99           C  
ANISOU 4582  C   ASN A 595     6112   5633   5728    -92    169    -35       C  
ATOM   4583  O   ASN A 595     116.332   8.206  45.699  1.00 44.01           O  
ANISOU 4583  O   ASN A 595     5846   5399   5478   -107    157    -36       O  
ATOM   4584  CB  ASN A 595     115.888   5.290  45.692  1.00 40.33           C  
ANISOU 4584  CB  ASN A 595     5313   4977   5032    -90    117    -29       C  
ATOM   4585  CG  ASN A 595     115.960   3.948  46.383  0.70 46.70           C  
ANISOU 4585  CG  ASN A 595     6128   5815   5801    -86    128    -33       C  
ATOM   4586  OD1 ASN A 595     115.814   3.856  47.601  0.70 41.91           O  
ANISOU 4586  OD1 ASN A 595     5599   5125   5202   -111    156    -35       O  
ATOM   4587  ND2 ASN A 595     116.134   2.889  45.598  0.70 44.06           N  
ANISOU 4587  ND2 ASN A 595     5724   5518   5500    -70     85    -26       N  
ATOM   4588  N   ASP A 596     114.092   8.332  45.456  1.00 27.68           N  
ANISOU 4588  N   ASP A 596     3803   3347   3367    -68    204    -27       N  
ATOM   4589  CA  ASP A 596     114.131   9.713  44.949  1.00 39.55           C  
ANISOU 4589  CA  ASP A 596     5319   4794   4913    -74    193    -30       C  
ATOM   4590  C   ASP A 596     114.722  10.616  46.020  1.00 41.93           C  
ANISOU 4590  C   ASP A 596     5691   5107   5132    -86    259    -34       C  
ATOM   4591  O   ASP A 596     114.547  10.364  47.217  1.00 46.97           O  
ANISOU 4591  O   ASP A 596     6408   5634   5805    -97    276    -38       O  
ATOM   4592  CB  ASP A 596     112.734  10.208  44.561  1.00 27.43           C  
ANISOU 4592  CB  ASP A 596     3802   3239   3380    -49    215    -21       C  
ATOM   4593  CG  ASP A 596     112.337   9.807  43.156  1.00 37.36           C  
ANISOU 4593  CG  ASP A 596     4976   4555   4664    -37    164    -16       C  
ATOM   4594  OD1 ASP A 596     113.145   9.162  42.456  1.00 41.74           O  
ANISOU 4594  OD1 ASP A 596     5457   5165   5236    -41    113    -17       O  
ATOM   4595  OD2 ASP A 596     111.177  10.063  42.770  1.00 31.82           O  
ANISOU 4595  OD2 ASP A 596     4276   3886   3928    -17    194     -7       O  
ATOM   4596  N   ALA A 597     115.448  11.642  45.593  1.00 47.72           N  
ANISOU 4596  N   ALA A 597     6421   5787   5922   -105    229    -41       N  
ATOM   4597  CA  ALA A 597     116.046  12.597  46.522  1.00 62.71           C  
ANISOU 4597  CA  ALA A 597     8386   7711   7729   -117    295    -45       C  
ATOM   4598  C   ALA A 597     114.994  13.279  47.393  1.00 55.98           C  
ANISOU 4598  C   ALA A 597     7637   6712   6919   -113    333    -45       C  
ATOM   4599  O   ALA A 597     115.109  13.302  48.618  1.00 57.16           O  
ANISOU 4599  O   ALA A 597     7852   6912   6955   -112    408    -43       O  
ATOM   4600  CB  ALA A 597     116.856  13.632  45.761  1.00 68.61           C  
ANISOU 4600  CB  ALA A 597     9111   8409   8549   -138    251    -53       C  
ATOM   4601  N   ASP A 598     113.981  13.855  46.754  1.00 52.04           N  
ANISOU 4601  N   ASP A 598     7124   6297   6352    -80    376    -32       N  
ATOM   4602  CA  ASP A 598     112.857  14.409  47.491  1.00 61.18           C  
ANISOU 4602  CA  ASP A 598     8363   7401   7480    -54    447    -23       C  
ATOM   4603  C   ASP A 598     111.687  13.443  47.426  1.00 74.29           C  
ANISOU 4603  C   ASP A 598    10010   9064   9154    -22    452     -9       C  
ATOM   4604  O   ASP A 598     110.942  13.424  46.446  1.00 74.99           O  
ANISOU 4604  O   ASP A 598    10051   9174   9268     -4    431     -2       O  
ATOM   4605  CB  ASP A 598     112.456  15.761  46.899  0.50 54.87           C  
ANISOU 4605  CB  ASP A 598     7593   6484   6773    -48    429    -21       C  
ATOM   4606  CG  ASP A 598     111.316  16.408  47.651  0.50 70.80           C  
ANISOU 4606  CG  ASP A 598     9679   8554   8669    -11    547     -5       C  
ATOM   4607  OD1 ASP A 598     111.213  16.213  48.880  0.50 71.61           O  
ANISOU 4607  OD1 ASP A 598     9925   8461   8824     -7    591      1       O  
ATOM   4608  OD2 ASP A 598     110.518  17.119  47.008  0.50 75.52           O  
ANISOU 4608  OD2 ASP A 598    10272   9146   9274     12    563      5       O  
ATOM   4609  N   TYR A 599     111.503  12.675  48.496  1.00 70.82           N  
ANISOU 4609  N   TYR A 599     9656   8478   8773    -16    462     -5       N  
ATOM   4610  CA  TYR A 599     110.508  11.613  48.511  1.00 51.84           C  
ANISOU 4610  CA  TYR A 599     7258   6070   6368     20    485      8       C  
ATOM   4611  C   TYR A 599     109.478  11.898  49.590  1.00 45.19           C  
ANISOU 4611  C   TYR A 599     6578   5126   5466     73    629     32       C  
ATOM   4612  O   TYR A 599     109.739  11.702  50.777  1.00 44.99           O  
ANISOU 4612  O   TYR A 599     6674   5035   5385     76    711     33       O  
ATOM   4613  CB  TYR A 599     111.181  10.250  48.742  1.00 46.74           C  
ANISOU 4613  CB  TYR A 599     6575   5457   5726     -3    445     -2       C  
ATOM   4614  CG  TYR A 599     110.279   9.035  48.600  1.00 53.26           C  
ANISOU 4614  CG  TYR A 599     7386   6292   6559     30    452     11       C  
ATOM   4615  CD1 TYR A 599     110.127   8.124  49.647  1.00 42.43           C  
ANISOU 4615  CD1 TYR A 599     6114   4867   5140     48    530     19       C  
ATOM   4616  CD2 TYR A 599     109.599   8.782  47.410  1.00 54.87           C  
ANISOU 4616  CD2 TYR A 599     7478   6557   6811     42    383     17       C  
ATOM   4617  CE1 TYR A 599     109.310   7.013  49.515  1.00 34.72           C  
ANISOU 4617  CE1 TYR A 599     5123   3900   4171     85    544     37       C  
ATOM   4618  CE2 TYR A 599     108.784   7.669  47.274  1.00 34.62           C  
ANISOU 4618  CE2 TYR A 599     4900   4001   4251     70    391     29       C  
ATOM   4619  CZ  TYR A 599     108.641   6.792  48.329  1.00 52.47           C  
ANISOU 4619  CZ  TYR A 599     7257   6210   6471     95    474     41       C  
ATOM   4620  OH  TYR A 599     107.824   5.684  48.203  1.00 48.35           O  
ANISOU 4620  OH  TYR A 599     6720   5696   5954    132    490     61       O  
ATOM   4621  N   ASP A 600     108.324  12.406  49.177  1.00 36.62           N  
ANISOU 4621  N   ASP A 600     5496   4028   4391    120    663     55       N  
ATOM   4622  CA  ASP A 600     107.280  12.823  50.118  1.00 49.95           C  
ANISOU 4622  CA  ASP A 600     7325   5623   6032    188    809     89       C  
ATOM   4623  C   ASP A 600     105.917  12.221  49.745  1.00 44.78           C  
ANISOU 4623  C   ASP A 600     6640   4977   5397    255    839    127       C  
ATOM   4624  O   ASP A 600     104.968  12.957  49.476  1.00 40.77           O  
ANISOU 4624  O   ASP A 600     6143   4450   4896    299    883    153       O  
ATOM   4625  CB  ASP A 600     107.208  14.362  50.130  1.00 44.17           C  
ANISOU 4625  CB  ASP A 600     6643   4852   5288    190    847     90       C  
ATOM   4626  CG  ASP A 600     106.289  14.920  51.205  1.00 62.11           C  
ANISOU 4626  CG  ASP A 600     9071   7022   7508    261   1006    127       C  
ATOM   4627  OD1 ASP A 600     106.045  14.246  52.225  1.00 78.58           O  
ANISOU 4627  OD1 ASP A 600    11253   9052   9551    301   1097    147       O  
ATOM   4628  OD2 ASP A 600     105.772  16.039  50.997  1.00 64.88           O  
ANISOU 4628  OD2 ASP A 600     9445   7346   7860    283   1042    140       O  
ATOM   4629  N   PRO A 601     105.805  10.880  49.757  1.00 42.35           N  
ANISOU 4629  N   PRO A 601     6296   4697   5098    265    821    133       N  
ATOM   4630  CA  PRO A 601     104.548  10.238  49.354  1.00 42.43           C  
ANISOU 4630  CA  PRO A 601     6265   4725   5131    326    845    172       C  
ATOM   4631  C   PRO A 601     103.502  10.283  50.463  1.00 46.50           C  
ANISOU 4631  C   PRO A 601     6892   5171   5606    418   1004    230       C  
ATOM   4632  O   PRO A 601     103.877  10.485  51.615  1.00 50.02           O  
ANISOU 4632  O   PRO A 601     7405   5618   5983    405   1063    227       O  
ATOM   4633  CB  PRO A 601     104.973   8.780  49.129  1.00 45.06           C  
ANISOU 4633  CB  PRO A 601     6529   5111   5482    300    776    158       C  
ATOM   4634  CG  PRO A 601     106.048   8.578  50.124  1.00 42.20           C  
ANISOU 4634  CG  PRO A 601     6247   4709   5077    269    801    136       C  
ATOM   4635  CD  PRO A 601     106.810   9.882  50.171  1.00 37.72           C  
ANISOU 4635  CD  PRO A 601     5707   4126   4499    222    783    108       C  
ATOM   4636  N   LEU A 602     102.225  10.094  50.121  1.00 39.86           N  
ANISOU 4636  N   LEU A 602     6014   4344   4788    483   1044    279       N  
ATOM   4637  CA  LEU A 602     101.177   9.885  51.123  1.00 41.23           C  
ANISOU 4637  CA  LEU A 602     6209   4544   4913    540   1162    336       C  
ATOM   4638  C   LEU A 602     101.451   8.545  51.786  1.00 57.38           C  
ANISOU 4638  C   LEU A 602     8220   6661   6922    518   1155    340       C  
ATOM   4639  O   LEU A 602     101.413   8.424  53.010  1.00 44.10           O  
ANISOU 4639  O   LEU A 602     6587   5001   5168    522   1235    362       O  
ATOM   4640  CB  LEU A 602      99.789   9.889  50.487  1.00 45.81           C  
ANISOU 4640  CB  LEU A 602     6740   5125   5539    609   1197    393       C  
ATOM   4641  CG  LEU A 602      98.601   9.679  51.436  1.00 48.54           C  
ANISOU 4641  CG  LEU A 602     7097   5498   5849    672   1325    465       C  
ATOM   4642  CD1 LEU A 602      98.555  10.715  52.541  1.00 47.71           C  
ANISOU 4642  CD1 LEU A 602     7095   5353   5679    688   1431    475       C  
ATOM   4643  CD2 LEU A 602      97.304   9.708  50.651  1.00 35.43           C  
ANISOU 4643  CD2 LEU A 602     5379   3836   4248    736   1348    521       C  
ATOM   4644  N   PHE A 603     101.663   7.525  50.962  1.00 60.62           N  
ANISOU 4644  N   PHE A 603     8545   7108   7378    496   1064    325       N  
ATOM   4645  CA  PHE A 603     101.989   6.196  51.455  1.00 36.65           C  
ANISOU 4645  CA  PHE A 603     5470   4141   4315    470   1047    328       C  
ATOM   4646  C   PHE A 603     103.197   5.710  50.651  1.00 50.91           C  
ANISOU 4646  C   PHE A 603     7234   5952   6159    405    918    265       C  
ATOM   4647  O   PHE A 603     103.147   5.606  49.425  1.00 42.89           O  
ANISOU 4647  O   PHE A 603     6160   4926   5210    402    840    248       O  
ATOM   4648  CB  PHE A 603     100.826   5.238  51.228  1.00 32.47           C  
ANISOU 4648  CB  PHE A 603     4866   3660   3810    515   1075    387       C  
ATOM   4649  CG  PHE A 603      99.538   5.696  51.849  1.00 42.75           C  
ANISOU 4649  CG  PHE A 603     6194   4956   5095    583   1201    459       C  
ATOM   4650  CD1 PHE A 603      99.421   5.809  53.224  1.00 31.95           C  
ANISOU 4650  CD1 PHE A 603     4888   3600   3649    592   1304    491       C  
ATOM   4651  CD2 PHE A 603      98.439   6.000  51.063  1.00 40.29           C  
ANISOU 4651  CD2 PHE A 603     5843   4626   4841    637   1219    498       C  
ATOM   4652  CE1 PHE A 603      98.240   6.228  53.800  1.00 44.03           C  
ANISOU 4652  CE1 PHE A 603     6441   5123   5164    654   1426    561       C  
ATOM   4653  CE2 PHE A 603      97.254   6.412  51.636  1.00 41.39           C  
ANISOU 4653  CE2 PHE A 603     6000   4757   4968    700   1339    569       C  
ATOM   4654  CZ  PHE A 603      97.155   6.532  53.005  1.00 51.73           C  
ANISOU 4654  CZ  PHE A 603     7373   6078   6206    709   1444    600       C  
ATOM   4655  N   ALA A 604     104.252   5.326  51.360  1.00 45.30           N  
ANISOU 4655  N   ALA A 604     6548   5261   5403    354    899    235       N  
ATOM   4656  CA  ALA A 604     105.530   5.014  50.734  1.00 45.77           C  
ANISOU 4656  CA  ALA A 604     6577   5316   5497    289    788    177       C  
ATOM   4657  C   ALA A 604     105.456   3.651  50.078  1.00 47.68           C  
ANISOU 4657  C   ALA A 604     6728   5612   5777    281    722    177       C  
ATOM   4658  O   ALA A 604     104.525   2.880  50.334  1.00 49.74           O  
ANISOU 4658  O   ALA A 604     6957   5920   6023    319    768    224       O  
ATOM   4659  CB  ALA A 604     106.667   5.072  51.743  1.00 36.53           C  
ANISOU 4659  CB  ALA A 604     5464   4149   4267    240    794    151       C  
ATOM   4660  N   TYR A 605     106.359   3.414  49.134  1.00 43.48           N  
ANISOU 4660  N   TYR A 605     6152   5070   5300    233    616    129       N  
ATOM   4661  CA  TYR A 605     106.650   2.071  48.647  1.00 40.53           C  
ANISOU 4661  CA  TYR A 605     5702   4747   4952    210    545    116       C  
ATOM   4662  C   TYR A 605     106.808   1.143  49.864  1.00 40.47           C  
ANISOU 4662  C   TYR A 605     5707   4796   4873    202    593    139       C  
ATOM   4663  O   TYR A 605     107.526   1.476  50.812  1.00 42.44           O  
ANISOU 4663  O   TYR A 605     6018   5039   5070    176    622    130       O  
ATOM   4664  CB  TYR A 605     107.966   2.094  47.862  1.00 28.32           C  
ANISOU 4664  CB  TYR A 605     4074   3240   3445    124    414     59       C  
ATOM   4665  CG  TYR A 605     108.402   0.745  47.328  1.00 34.14           C  
ANISOU 4665  CG  TYR A 605     4724   4038   4210     92    332     42       C  
ATOM   4666  CD1 TYR A 605     108.040   0.360  46.036  1.00 27.62           C  
ANISOU 4666  CD1 TYR A 605     3776   3286   3433     75    235     33       C  
ATOM   4667  CD2 TYR A 605     109.146  -0.152  48.093  1.00 39.79           C  
ANISOU 4667  CD2 TYR A 605     5484   4734   4899     76    353     35       C  
ATOM   4668  CE1 TYR A 605     108.417  -0.862  45.514  1.00 36.62           C  
ANISOU 4668  CE1 TYR A 605     4844   4476   4593     47    168     24       C  
ATOM   4669  CE2 TYR A 605     109.527  -1.394  47.569  1.00 34.50           C  
ANISOU 4669  CE2 TYR A 605     4732   4120   4256     48    280     20       C  
ATOM   4670  CZ  TYR A 605     109.155  -1.735  46.283  1.00 45.12           C  
ANISOU 4670  CZ  TYR A 605     5951   5538   5652     38    186     13       C  
ATOM   4671  OH  TYR A 605     109.525  -2.953  45.759  1.00 36.48           O  
ANISOU 4671  OH  TYR A 605     4785   4494   4580     14    122      6       O  
ATOM   4672  N   GLY A 606     106.169  -0.024  49.820  1.00 42.34           N  
ANISOU 4672  N   GLY A 606     5887   5091   5108    220    599    173       N  
ATOM   4673  CA  GLY A 606     106.234  -0.971  50.925  1.00 52.13           C  
ANISOU 4673  CA  GLY A 606     7135   6392   6281    210    645    208       C  
ATOM   4674  C   GLY A 606     105.187  -0.846  52.020  1.00 52.72           C  
ANISOU 4674  C   GLY A 606     7249   6487   6294    255    767    280       C  
ATOM   4675  O   GLY A 606     105.127  -1.673  52.930  1.00 63.21           O  
ANISOU 4675  O   GLY A 606     8581   7870   7567    246    812    323       O  
ATOM   4676  N   TYR A 607     104.368   0.192  51.940  1.00 41.67           N  
ANISOU 4676  N   TYR A 607     5881   5046   4906    301    824    298       N  
ATOM   4677  CA  TYR A 607     103.301   0.431  52.910  1.00 45.22           C  
ANISOU 4677  CA  TYR A 607     6367   5507   5308    349    948    370       C  
ATOM   4678  C   TYR A 607     102.117  -0.505  52.677  1.00 52.98           C  
ANISOU 4678  C   TYR A 607     7276   6531   6321    385    983    439       C  
ATOM   4679  O   TYR A 607     101.791  -0.849  51.536  1.00 43.00           O  
ANISOU 4679  O   TYR A 607     5943   5266   5128    395    921    429       O  
ATOM   4680  CB  TYR A 607     102.836   1.885  52.804  1.00 44.93           C  
ANISOU 4680  CB  TYR A 607     6385   5406   5281    388    995    366       C  
ATOM   4681  CG  TYR A 607     101.628   2.282  53.628  1.00 48.23           C  
ANISOU 4681  CG  TYR A 607     6837   5825   5665    446   1126    440       C  
ATOM   4682  CD1 TYR A 607     100.330   2.150  53.139  1.00 48.32           C  
ANISOU 4682  CD1 TYR A 607     6795   5838   5726    501   1167    496       C  
ATOM   4683  CD2 TYR A 607     101.796   2.802  54.905  1.00 51.40           C  
ANISOU 4683  CD2 TYR A 607     7323   6223   5982    445   1210    456       C  
ATOM   4684  CE1 TYR A 607      99.235   2.532  53.903  1.00 40.38           C  
ANISOU 4684  CE1 TYR A 607     5817   4830   4695    555   1292    569       C  
ATOM   4685  CE2 TYR A 607     100.716   3.184  55.671  1.00 43.64           C  
ANISOU 4685  CE2 TYR A 607     6374   5241   4967    498   1334    525       C  
ATOM   4686  CZ  TYR A 607      99.435   3.049  55.169  1.00 51.99           C  
ANISOU 4686  CZ  TYR A 607     7374   6297   6081    553   1377    582       C  
ATOM   4687  OH  TYR A 607      98.363   3.442  55.947  1.00 50.94           O  
ANISOU 4687  OH  TYR A 607     7271   6162   5921    607   1506    655       O  
ATOM   4688  N   GLY A 608     101.510  -0.941  53.776  1.00 39.05           N  
ANISOU 4688  N   GLY A 608     5527   4806   4504    401   1082    513       N  
ATOM   4689  CA  GLY A 608     100.270  -1.682  53.727  1.00 43.52           C  
ANISOU 4689  CA  GLY A 608     6029   5402   5103    439   1139    596       C  
ATOM   4690  C   GLY A 608      99.846  -2.052  55.131  1.00 52.27           C  
ANISOU 4690  C   GLY A 608     7171   6549   6141    444   1252    677       C  
ATOM   4691  O   GLY A 608     100.601  -2.673  55.875  1.00 47.15           O  
ANISOU 4691  O   GLY A 608     6546   5938   5431    397   1244    678       O  
ATOM   4692  N   LEU A 609      98.659  -1.616  55.527  1.00 39.75           N  
ANISOU 4692  N   LEU A 609     5591   4951   4561    499   1361    748       N  
ATOM   4693  CA  LEU A 609      98.172  -1.931  56.852  1.00 41.32           C  
ANISOU 4693  CA  LEU A 609     5821   5184   4695    507   1477    834       C  
ATOM   4694  C   LEU A 609      97.749  -3.402  56.947  1.00 56.63           C  
ANISOU 4694  C   LEU A 609     7682   7176   6661    489   1485    912       C  
ATOM   4695  O   LEU A 609      97.430  -4.036  55.945  1.00 42.10           O  
ANISOU 4695  O   LEU A 609     5755   5338   4902    492   1426    915       O  
ATOM   4696  CB  LEU A 609      97.002  -1.018  57.209  1.00 54.10           C  
ANISOU 4696  CB  LEU A 609     7465   6770   6319    574   1595    891       C  
ATOM   4697  CG  LEU A 609      97.296   0.486  57.215  1.00 53.86           C  
ANISOU 4697  CG  LEU A 609     7520   6682   6263    594   1604    829       C  
ATOM   4698  CD1 LEU A 609      96.031   1.259  57.525  1.00 38.03           C  
ANISOU 4698  CD1 LEU A 609     5532   4649   4270    664   1725    895       C  
ATOM   4699  CD2 LEU A 609      98.396   0.822  58.217  1.00 38.20           C  
ANISOU 4699  CD2 LEU A 609     5632   4705   4177    552   1607    787       C  
ATOM   4700  N   THR A 610      97.708  -3.930  58.163  1.00 56.78           N  
ANISOU 4700  N   THR A 610     7732   7234   6610    470   1562    981       N  
ATOM   4701  CA  THR A 610      97.106  -5.233  58.402  1.00 57.78           C  
ANISOU 4701  CA  THR A 610     7788   7401   6765    458   1595   1079       C  
ATOM   4702  C   THR A 610      96.176  -5.109  59.590  1.00 64.30           C  
ANISOU 4702  C   THR A 610     8644   8238   7549    490   1743   1186       C  
ATOM   4703  O   THR A 610      96.104  -4.058  60.229  1.00 64.67           O  
ANISOU 4703  O   THR A 610     8771   8266   7535    518   1811   1175       O  
ATOM   4704  CB  THR A 610      98.163  -6.336  58.730  1.00 56.89           C  
ANISOU 4704  CB  THR A 610     7677   7332   6606    385   1528   1070       C  
ATOM   4705  OG1 THR A 610      98.735  -6.095  60.023  1.00 65.05           O  
ANISOU 4705  OG1 THR A 610     8806   8388   7524    360   1580   1083       O  
ATOM   4706  CG2 THR A 610      99.286  -6.349  57.701  1.00 43.46           C  
ANISOU 4706  CG2 THR A 610     5963   5621   4929    349   1386    955       C  
ATOM   4707  N   TYR A 611      95.434  -6.175  59.863  1.00 61.33           N  
ANISOU 4707  N   TYR A 611     8202   7890   7211    486   1794   1293       N  
ATOM   4708  CA  TYR A 611      94.520  -6.190  60.991  1.00 61.46           C  
ANISOU 4708  CA  TYR A 611     8238   7920   7194    513   1938   1407       C  
ATOM   4709  C   TYR A 611      95.263  -6.131  62.322  1.00 70.13           C  
ANISOU 4709  C   TYR A 611     9439   9048   8158    477   1980   1416       C  
ATOM   4710  O   TYR A 611      94.667  -5.841  63.356  1.00 72.77           O  
ANISOU 4710  O   TYR A 611     9820   9391   8438    502   2101   1491       O  
ATOM   4711  CB  TYR A 611      93.623  -7.416  60.906  1.00 54.10           C  
ANISOU 4711  CB  TYR A 611     7204   7006   6348    510   1973   1524       C  
ATOM   4712  CG  TYR A 611      92.664  -7.349  59.743  1.00 44.69           C  
ANISOU 4712  CG  TYR A 611     5912   5784   5286    557   1957   1536       C  
ATOM   4713  CD1 TYR A 611      92.225  -6.127  59.259  1.00 42.45           C  
ANISOU 4713  CD1 TYR A 611     5645   5461   5022    615   1974   1490       C  
ATOM   4714  CD2 TYR A 611      92.220  -8.498  59.111  1.00 48.00           C  
ANISOU 4714  CD2 TYR A 611     6220   6211   5807    542   1920   1595       C  
ATOM   4715  CE1 TYR A 611      91.349  -6.052  58.196  1.00 45.21           C  
ANISOU 4715  CE1 TYR A 611     5907   5784   5485    657   1957   1506       C  
ATOM   4716  CE2 TYR A 611      91.345  -8.433  58.047  1.00 46.25           C  
ANISOU 4716  CE2 TYR A 611     5907   5964   5703    584   1902   1609       C  
ATOM   4717  CZ  TYR A 611      90.911  -7.208  57.597  1.00 44.28           C  
ANISOU 4717  CZ  TYR A 611     5679   5680   5465    642   1920   1565       C  
ATOM   4718  OH  TYR A 611      90.036  -7.144  56.539  1.00 46.03           O  
ANISOU 4718  OH  TYR A 611     5812   5877   5799    683   1900   1585       O  
ATOM   4719  N   GLN A 612      96.566  -6.394  62.287  1.00 68.79           N  
ANISOU 4719  N   GLN A 612     9306   8896   7934    419   1879   1340       N  
ATOM   4720  CA  GLN A 612      97.415  -6.286  63.472  1.00 54.80           C  
ANISOU 4720  CA  GLN A 612     7635   7154   6031    381   1901   1336       C  
ATOM   4721  C   GLN A 612      97.751  -4.831  63.775  1.00 56.85           C  
ANISOU 4721  C   GLN A 612     7989   7387   6226    410   1924   1261       C  
ATOM   4722  O   GLN A 612      98.235  -4.512  64.863  1.00 51.09           O  
ANISOU 4722  O   GLN A 612     7350   6678   5384    395   1968   1268       O  
ATOM   4723  CB  GLN A 612      98.692  -7.118  63.320  1.00 59.75           C  
ANISOU 4723  CB  GLN A 612     8263   7811   6629    308   1783   1289       C  
ATOM   4724  CG  GLN A 612      98.481  -8.613  63.302  1.00 75.27           C  
ANISOU 4724  CG  GLN A 612    10159   9804   8637    270   1770   1375       C  
ATOM   4725  CD  GLN A 612      97.789  -9.111  64.555  1.00 82.76           C  
ANISOU 4725  CD  GLN A 612    11132  10780   9533    270   1894   1511       C  
ATOM   4726  OE1 GLN A 612      98.085  -8.650  65.658  1.00 87.67           O  
ANISOU 4726  OE1 GLN A 612    11847  11423  10040    265   1954   1526       O  
ATOM   4727  NE2 GLN A 612      96.877 -10.063  64.396  1.00 73.35           N  
ANISOU 4727  NE2 GLN A 612     9855   9588   8426    274   1933   1614       N  
ATOM   4728  N   ASP A 613      97.559  -3.960  62.789  1.00 54.59           N  
ANISOU 4728  N   ASP A 613     7683   7051   6009    449   1887   1189       N  
ATOM   4729  CA  ASP A 613      97.794  -2.536  63.008  1.00 69.86           C  
ANISOU 4729  CA  ASP A 613     9703   8945   7896    478   1912   1124       C  
ATOM   4730  C   ASP A 613      96.585  -1.867  63.675  1.00 67.54           C  
ANISOU 4730  C   ASP A 613     9438   8635   7588    541   2059   1201       C  
ATOM   4731  O   ASP A 613      95.432  -2.241  63.432  1.00 64.16           O  
ANISOU 4731  O   ASP A 613     8939   8206   7233    579   2119   1280       O  
ATOM   4732  CB  ASP A 613      98.118  -1.831  61.681  1.00 72.81           C  
ANISOU 4732  CB  ASP A 613    10050   9265   8349    490   1812   1021       C  
ATOM   4733  CG  ASP A 613      99.400  -2.361  61.023  1.00 74.84           C  
ANISOU 4733  CG  ASP A 613    10284   9533   8617    428   1669    937       C  
ATOM   4734  OD1 ASP A 613     100.412  -2.542  61.737  1.00 54.05           O  
ANISOU 4734  OD1 ASP A 613     7707   6929   5899    381   1643    915       O  
ATOM   4735  OD2 ASP A 613      99.407  -2.585  59.791  1.00 77.88           O  
ANISOU 4735  OD2 ASP A 613    10597   9899   9093    428   1582    895       O  
ATOM   4736  N   ASN A 614      96.862  -0.830  64.458  1.00 59.60           N  
ANISOU 4736  N   ASN A 614     8536   7614   6494    555   2113   1173       N  
ATOM   4737  CA  ASN A 614      95.838   0.044  65.019  1.00 64.10           C  
ANISOU 4737  CA  ASN A 614     9149   8159   7047    618   2247   1225       C  
ATOM   4738  C   ASN A 614      96.186   1.478  64.662  1.00 73.51           C  
ANISOU 4738  C   ASN A 614    10407   9289   8235    642   2225   1133       C  
ATOM   4739  O   ASN A 614      96.510   2.287  65.530  1.00 81.35           O  
ANISOU 4739  O   ASN A 614    11502  10274   9135    645   2280   1116       O  
ATOM   4740  CB  ASN A 614      95.695  -0.135  66.533  0.50 52.43           C  
ANISOU 4740  CB  ASN A 614     7743   6727   5452    614   2361   1305       C  
ATOM   4741  CG  ASN A 614      95.288  -1.537  66.917  0.50 55.24           C  
ANISOU 4741  CG  ASN A 614     8036   7138   5816    590   2391   1410       C  
ATOM   4742  OD1 ASN A 614      94.111  -1.901  66.831  0.50 59.52           O  
ANISOU 4742  OD1 ASN A 614     8511   7678   6426    627   2469   1501       O  
ATOM   4743  ND2 ASN A 614      96.262  -2.344  67.334  0.50 46.89           N  
ANISOU 4743  ND2 ASN A 614     6996   6126   4693    525   2329   1404       N  
ATOM   4744  N   ILE A 615      96.195   1.760  63.366  1.00 73.27           N  
ANISOU 4744  N   ILE A 615    10320   9214   8303    652   2139   1073       N  
ATOM   4745  CA  ILE A 615      96.594   3.064  62.871  1.00 62.90           C  
ANISOU 4745  CA  ILE A 615     9063   7837   7001    666   2102    986       C  
ATOM   4746  C   ILE A 615      95.405   3.830  62.300  1.00 68.67           C  
ANISOU 4746  C   ILE A 615     9768   8516   7807    736   2164   1015       C  
ATOM   4747  O   ILE A 615      94.627   3.291  61.515  1.00 79.86           O  
ANISOU 4747  O   ILE A 615    11089   9936   9316    760   2152   1055       O  
ATOM   4748  CB  ILE A 615      97.653   2.894  61.774  1.00 64.43           C  
ANISOU 4748  CB  ILE A 615     9219   8014   7247    618   1946    890       C  
ATOM   4749  CG1 ILE A 615      98.917   2.256  62.356  1.00 74.37           C  
ANISOU 4749  CG1 ILE A 615    10509   9319   8429    550   1884    857       C  
ATOM   4750  CG2 ILE A 615      97.981   4.232  61.132  1.00 72.92           C  
ANISOU 4750  CG2 ILE A 615    10340   9016   8350    632   1907    811       C  
ATOM   4751  CD1 ILE A 615     100.002   1.976  61.333  1.00 74.33           C  
ANISOU 4751  CD1 ILE A 615    10463   9304   8475    500   1734    769       C  
ATOM   4752  N   ASN A 616      95.282   5.100  62.675  1.00 69.90           N  
ANISOU 4752  N   ASN A 616    10010   8623   7925    769   2229    996       N  
ATOM   4753  CA  ASN A 616      94.277   5.958  62.068  1.00 74.66           C  
ANISOU 4753  CA  ASN A 616    10598   9171   8599    834   2278   1015       C  
ATOM   4754  C   ASN A 616      94.921   6.894  61.070  1.00 67.90           C  
ANISOU 4754  C   ASN A 616     9763   8250   7786    823   2180    920       C  
ATOM   4755  O   ASN A 616      96.052   7.348  61.259  1.00 79.26           O  
ANISOU 4755  O   ASN A 616    11269   9672   9173    778   2124    846       O  
ATOM   4756  CB  ASN A 616      93.546   6.787  63.131  1.00 72.22           C  
ANISOU 4756  CB  ASN A 616    10370   8846   8226    884   2430   1069       C  
ATOM   4757  CG  ASN A 616      92.578   5.965  63.951  1.00 88.86           C  
ANISOU 4757  CG  ASN A 616    12441  11007  10314    911   2545   1183       C  
ATOM   4758  OD1 ASN A 616      91.932   5.057  63.432  1.00 95.87           O  
ANISOU 4758  OD1 ASN A 616    13224  11920  11280    920   2533   1239       O  
ATOM   4759  ND2 ASN A 616      92.440   6.305  65.230  1.00 90.15           N  
ANISOU 4759  ND2 ASN A 616    12691  11186  10377    924   2660   1222       N  
ATOM   4760  N   VAL A 617      94.197   7.176  59.993  1.00 70.27           N  
ANISOU 4760  N   VAL A 617    10002   8513   8184    863   2160    929       N  
ATOM   4761  CA  VAL A 617      94.648   8.167  59.033  1.00 59.92           C  
ANISOU 4761  CA  VAL A 617     8713   7136   6917    859   2081    854       C  
ATOM   4762  C   VAL A 617      93.863   9.440  59.258  1.00 63.86           C  
ANISOU 4762  C   VAL A 617     9274   7577   7412    920   2185    881       C  
ATOM   4763  O   VAL A 617      92.629   9.428  59.227  1.00 62.75           O  
ANISOU 4763  O   VAL A 617     9093   7438   7312    981   2270    958       O  
ATOM   4764  CB  VAL A 617      94.430   7.693  57.588  1.00 57.82           C  
ANISOU 4764  CB  VAL A 617     8343   6867   6758    861   1979    842       C  
ATOM   4765  CG1 VAL A 617      94.860   8.763  56.623  1.00 49.80           C  
ANISOU 4765  CG1 VAL A 617     7355   5784   5784    858   1906    775       C  
ATOM   4766  CG2 VAL A 617      95.183   6.390  57.328  1.00 40.29           C  
ANISOU 4766  CG2 VAL A 617     6060   4704   4545    802   1878    817       C  
ATOM   4767  N   PRO A 618      94.574  10.550  59.470  1.00 56.89           N  
ANISOU 4767  N   PRO A 618     8487   6642   6485    903   2180    821       N  
ATOM   4768  CA  PRO A 618      93.948  11.837  59.781  1.00 65.53           C  
ANISOU 4768  CA  PRO A 618     9656   7677   7564    956   2282    841       C  
ATOM   4769  C   PRO A 618      93.332  12.458  58.533  1.00 71.18           C  
ANISOU 4769  C   PRO A 618    10328   8339   8377    996   2250    844       C  
ATOM   4770  O   PRO A 618      93.522  11.926  57.430  1.00 57.46           O  
ANISOU 4770  O   PRO A 618     8510   6611   6712    976   2140    821       O  
ATOM   4771  CB  PRO A 618      95.124  12.677  60.271  1.00 59.86           C  
ANISOU 4771  CB  PRO A 618     9046   6924   6774    908   2257    766       C  
ATOM   4772  CG  PRO A 618      96.314  12.117  59.569  1.00 56.63           C  
ANISOU 4772  CG  PRO A 618     8598   6529   6391    837   2108    694       C  
ATOM   4773  CD  PRO A 618      96.046  10.631  59.447  1.00 50.63           C  
ANISOU 4773  CD  PRO A 618     7738   5844   5656    830   2077    733       C  
ATOM   4774  N   VAL A 619      92.535  13.510  58.716  1.00 65.24           N  
ANISOU 4774  N   VAL A 619     9626   7537   7627   1054   2351    879       N  
ATOM   4775  CA  VAL A 619      92.055  14.298  57.588  1.00 55.21           C  
ANISOU 4775  CA  VAL A 619     8333   6207   6436   1090   2323    879       C  
ATOM   4776  C   VAL A 619      93.229  14.838  56.777  1.00 53.81           C  
ANISOU 4776  C   VAL A 619     8182   5987   6277   1032   2197    789       C  
ATOM   4777  O   VAL A 619      94.181  15.383  57.336  1.00 66.35           O  
ANISOU 4777  O   VAL A 619     9856   7551   7802    988   2189    735       O  
ATOM   4778  CB  VAL A 619      91.138  15.438  58.058  1.00 56.62           C  
ANISOU 4778  CB  VAL A 619     8578   6335   6601   1158   2459    928       C  
ATOM   4779  CG1 VAL A 619      90.844  16.385  56.901  1.00 56.69           C  
ANISOU 4779  CG1 VAL A 619     8579   6277   6683   1186   2422    920       C  
ATOM   4780  CG2 VAL A 619      89.826  14.872  58.539  1.00 53.18           C  
ANISOU 4780  CG2 VAL A 619     8088   5940   6178   1221   2574   1029       C  
ATOM   4781  N   LEU A 620      93.161  14.679  55.461  1.00 50.35           N  
ANISOU 4781  N   LEU A 620     7668   5540   5922   1030   2099    777       N  
ATOM   4782  CA  LEU A 620      94.276  15.018  54.591  1.00 58.03           C  
ANISOU 4782  CA  LEU A 620     8648   6480   6920    971   1971    699       C  
ATOM   4783  C   LEU A 620      93.914  16.307  53.858  1.00 60.45           C  
ANISOU 4783  C   LEU A 620     8988   6712   7268   1005   1982    702       C  
ATOM   4784  O   LEU A 620      92.730  16.615  53.710  1.00 62.90           O  
ANISOU 4784  O   LEU A 620     9280   7010   7610   1074   2060    768       O  
ATOM   4785  CB  LEU A 620      94.517  13.891  53.588  1.00 46.97           C  
ANISOU 4785  CB  LEU A 620     7140   5127   5579    941   1848    682       C  
ATOM   4786  CG  LEU A 620      94.845  12.523  54.196  1.00 52.65           C  
ANISOU 4786  CG  LEU A 620     7817   5923   6266    908   1831    683       C  
ATOM   4787  CD1 LEU A 620      94.807  11.445  53.127  1.00 37.96           C  
ANISOU 4787  CD1 LEU A 620     5844   4104   4473    893   1726    680       C  
ATOM   4788  CD2 LEU A 620      96.189  12.522  54.920  1.00 46.09           C  
ANISOU 4788  CD2 LEU A 620     7051   5095   5364    839   1796    618       C  
ATOM   4789  N   SER A 621      94.914  17.050  53.393  1.00 49.52           N  
ANISOU 4789  N   SER A 621     7649   5279   5886    955   1908    638       N  
ATOM   4790  CA  SER A 621      94.648  18.247  52.609  1.00 29.21           C  
ANISOU 4790  CA  SER A 621     5106   2637   3356    980   1909    643       C  
ATOM   4791  C   SER A 621      93.896  17.890  51.336  1.00 48.24           C  
ANISOU 4791  C   SER A 621     7418   5063   5848   1015   1853    678       C  
ATOM   4792  O   SER A 621      94.224  16.904  50.678  1.00 61.68           O  
ANISOU 4792  O   SER A 621     9039   6813   7584    983   1752    658       O  
ATOM   4793  CB  SER A 621      95.942  18.969  52.263  1.00 33.95           C  
ANISOU 4793  CB  SER A 621     5759   3189   3950    910   1829    571       C  
ATOM   4794  OG  SER A 621      95.724  19.938  51.253  1.00 64.08           O  
ANISOU 4794  OG  SER A 621     9563   6974   7812    914   1794    571       O  
ATOM   4795  N   GLU A 622      92.871  18.671  51.004  1.00 51.52           N  
ANISOU 4795  N   GLU A 622     7841   5440   6294   1082   1922    733       N  
ATOM   4796  CA  GLU A 622      92.127  18.442  49.771  1.00 49.14           C  
ANISOU 4796  CA  GLU A 622     7425   5195   6052   1089   1850    756       C  
ATOM   4797  C   GLU A 622      92.457  19.524  48.754  1.00 50.86           C  
ANISOU 4797  C   GLU A 622     7615   5436   6275   1027   1755    704       C  
ATOM   4798  O   GLU A 622      91.825  19.634  47.701  1.00 51.85           O  
ANISOU 4798  O   GLU A 622     7654   5612   6435   1023   1697    716       O  
ATOM   4799  CB  GLU A 622      90.618  18.379  50.043  1.00 53.73           C  
ANISOU 4799  CB  GLU A 622     7996   5756   6663   1197   1982    860       C  
ATOM   4800  CG  GLU A 622      90.165  17.229  50.923  1.00 68.19           C  
ANISOU 4800  CG  GLU A 622     9788   7645   8476   1215   2042    900       C  
ATOM   4801  CD  GLU A 622      88.647  17.194  51.117  1.00 70.50           C  
ANISOU 4801  CD  GLU A 622    10039   7950   8799   1299   2157    999       C  
ATOM   4802  OE1 GLU A 622      87.928  17.994  50.469  1.00 59.13           O  
ANISOU 4802  OE1 GLU A 622     8597   6471   7400   1349   2183   1039       O  
ATOM   4803  OE2 GLU A 622      88.176  16.395  51.955  1.00 55.50           O  
ANISOU 4803  OE2 GLU A 622     8111   6097   6880   1315   2227   1042       O  
ATOM   4804  N   LYS A 623      93.441  20.340  49.111  1.00 43.79           N  
ANISOU 4804  N   LYS A 623     6798   4499   5342    980   1746    651       N  
ATOM   4805  CA  LYS A 623      93.941  21.432  48.278  1.00 57.18           C  
ANISOU 4805  CA  LYS A 623     8477   6210   7039    919   1663    601       C  
ATOM   4806  C   LYS A 623      94.639  20.889  47.019  1.00 60.76           C  
ANISOU 4806  C   LYS A 623     8808   6760   7519    828   1481    540       C  
ATOM   4807  O   LYS A 623      95.453  19.968  47.103  1.00 52.55           O  
ANISOU 4807  O   LYS A 623     7739   5753   6475    779   1410    502       O  
ATOM   4808  CB  LYS A 623      94.870  22.318  49.099  1.00 58.82           C  
ANISOU 4808  CB  LYS A 623     8800   6348   7199    892   1707    565       C  
ATOM   4809  CG  LYS A 623      95.266  23.600  48.390  1.00 87.44           C  
ANISOU 4809  CG  LYS A 623    12422   9975  10826    845   1653    530       C  
ATOM   4810  CD  LYS A 623      96.104  24.486  49.305  1.00 86.69           C  
ANISOU 4810  CD  LYS A 623    12451   9804  10684    823   1714    502       C  
ATOM   4811  CE  LYS A 623      96.458  25.795  48.624  1.00 92.73           C  
ANISOU 4811  CE  LYS A 623    13212  10568  11452    783   1671    474       C  
ATOM   4812  NZ  LYS A 623      97.358  26.631  49.467  1.00 99.39           N  
ANISOU 4812  NZ  LYS A 623    14170  11343  12250    751   1722    443       N  
ATOM   4813  N   THR A 624      94.330  21.472  45.862  1.00 62.03           N  
ANISOU 4813  N   THR A 624     8901   6962   7704    808   1410    533       N  
ATOM   4814  CA  THR A 624      94.961  21.080  44.602  1.00 62.81           C  
ANISOU 4814  CA  THR A 624     8889   7149   7827    725   1244    477       C  
ATOM   4815  C   THR A 624      95.914  22.120  44.028  1.00 70.05           C  
ANISOU 4815  C   THR A 624     9802   8075   8738    658   1166    424       C  
ATOM   4816  O   THR A 624      95.877  23.284  44.423  1.00 80.36           O  
ANISOU 4816  O   THR A 624    11185   9321  10026    680   1241    434       O  
ATOM   4817  CB  THR A 624      93.886  20.837  43.527  1.00 66.65           C  
ANISOU 4817  CB  THR A 624     9290   7688   8347    747   1208    508       C  
ATOM   4818  OG1 THR A 624      93.142  22.044  43.308  1.00 79.82           O  
ANISOU 4818  OG1 THR A 624    10990   9322  10017    791   1272    543       O  
ATOM   4819  CG2 THR A 624      92.963  19.690  43.910  1.00 67.52           C  
ANISOU 4819  CG2 THR A 624     9377   7805   8471    806   1266    563       C  
ATOM   4820  N   SER A 625      96.819  21.684  43.152  0.50 72.79           N  
ANISOU 4820  N   SER A 625    10062   8494   9102    577   1023    368       N  
ATOM   4821  CA  SER A 625      97.804  22.591  42.562  0.50 74.71           C  
ANISOU 4821  CA  SER A 625    10287   8755   9346    514    945    323       C  
ATOM   4822  C   SER A 625      97.118  23.420  41.479  0.50 76.50           C  
ANISOU 4822  C   SER A 625    10476   9001   9590    526    922    337       C  
ATOM   4823  O   SER A 625      96.148  22.958  40.877  0.50 77.48           O  
ANISOU 4823  O   SER A 625    10552   9155   9730    554    913    364       O  
ATOM   4824  CB  SER A 625      99.016  21.849  42.003  0.50 54.03           C  
ANISOU 4824  CB  SER A 625     7583   6205   6741    431    807    267       C  
ATOM   4825  OG  SER A 625      98.592  20.865  41.083  0.50 55.56           O  
ANISOU 4825  OG  SER A 625     7873   6385   6851    536   1031    333       O  
ATOM   4826  N   PRO A 626      97.649  24.612  41.176  0.50 72.37           N  
ANISOU 4826  N   PRO A 626     9971   8465   9063    500    908    319       N  
ATOM   4827  CA  PRO A 626      97.007  25.449  40.156  0.50 78.12           C  
ANISOU 4827  CA  PRO A 626    10633   9388   9662    482   1007    303       C  
ATOM   4828  C   PRO A 626      97.170  24.888  38.746  0.50 78.12           C  
ANISOU 4828  C   PRO A 626    10594   9279   9810    496    825    313       C  
ATOM   4829  O   PRO A 626      96.183  24.400  38.193  0.50 65.82           O  
ANISOU 4829  O   PRO A 626     8985   7755   8270    541    828    313       O  
ATOM   4830  CB  PRO A 626      97.758  26.776  40.283  0.50 79.26           C  
ANISOU 4830  CB  PRO A 626    10831   9500   9786    465   1030    286       C  
ATOM   4831  CG  PRO A 626      99.100  26.397  40.811  0.50 75.27           C  
ANISOU 4831  CG  PRO A 626    10335   8993   9272    414    985    247       C  
ATOM   4832  CD  PRO A 626      98.842  25.258  41.753  0.50 70.34           C  
ANISOU 4832  CD  PRO A 626     9763   8176   8786    460    911    287       C  
ATOM   4833  N   SER A 632      93.214  31.089  22.298  0.50 49.86           N  
ANISOU 4833  N   SER A 632     6652   6201   6093    557    411    489       N  
ATOM   4834  CA  SER A 632      92.988  32.373  21.642  0.50 52.84           C  
ANISOU 4834  CA  SER A 632     7052   6545   6480    575    407    520       C  
ATOM   4835  C   SER A 632      93.204  32.269  20.135  0.50 55.94           C  
ANISOU 4835  C   SER A 632     7459   6930   6865    559    370    541       C  
ATOM   4836  O   SER A 632      93.235  31.169  19.581  0.50 56.30           O  
ANISOU 4836  O   SER A 632     7492   7000   6898    537    347    537       O  
ATOM   4837  CB  SER A 632      93.885  33.457  22.242  0.50 38.76           C  
ANISOU 4837  CB  SER A 632     5299   4726   4702    582    440    502       C  
ATOM   4838  OG  SER A 632      95.248  33.070  22.207  0.50 48.80           O  
ANISOU 4838  OG  SER A 632     6587   5993   5962    557    448    468       O  
ATOM   4839  N   ASP A 633      93.360  33.417  19.480  0.50 50.67           N  
ANISOU 4839  N   ASP A 633     6819   6225   6208    569    362    566       N  
ATOM   4840  CA  ASP A 633      93.394  33.470  18.020  0.50 36.27           C  
ANISOU 4840  CA  ASP A 633     5010   4392   4380    557    324    595       C  
ATOM   4841  C   ASP A 633      94.767  33.208  17.398  0.50 48.99           C  
ANISOU 4841  C   ASP A 633     6644   5996   5972    527    324    575       C  
ATOM   4842  O   ASP A 633      95.422  34.115  16.882  0.50 44.89           O  
ANISOU 4842  O   ASP A 633     6154   5445   5456    524    323    587       O  
ATOM   4843  CB  ASP A 633      92.804  34.784  17.504  0.50 25.74           C  
ANISOU 4843  CB  ASP A 633     3692   3018   3069    582    304    638       C  
ATOM   4844  CG  ASP A 633      93.412  36.008  18.166  0.50 66.50           C  
ANISOU 4844  CG  ASP A 633     8880   8140   8249    596    333    630       C  
ATOM   4845  OD1 ASP A 633      93.930  35.892  19.298  0.50 66.34           O  
ANISOU 4845  OD1 ASP A 633     8857   8126   8223    594    373    593       O  
ATOM   4846  OD2 ASP A 633      93.363  37.095  17.549  0.50 80.20           O  
ANISOU 4846  OD2 ASP A 633    10637   9831  10005    608    313    661       O  
ATOM   4847  N   SER A 634      95.186  31.949  17.447  1.00 81.70           N  
ANISOU 4847  N   SER A 634    10773  10168  10100    504    323    547       N  
ATOM   4848  CA  SER A 634      96.375  31.503  16.738  1.00 74.48           C  
ANISOU 4848  CA  SER A 634     9876   9251   9170    477    317    530       C  
ATOM   4849  C   SER A 634      95.968  30.835  15.433  1.00 67.78           C  
ANISOU 4849  C   SER A 634     9026   8418   8310    459    276    556       C  
ATOM   4850  O   SER A 634      94.881  30.268  15.328  1.00 77.89           O  
ANISOU 4850  O   SER A 634    10285   9721   9591    463    256    572       O  
ATOM   4851  CB  SER A 634      97.162  30.517  17.595  1.00 68.67           C  
ANISOU 4851  CB  SER A 634     9129   8532   8432    464    336    482       C  
ATOM   4852  OG  SER A 634      96.416  29.329  17.800  1.00 87.22           O  
ANISOU 4852  OG  SER A 634    11448  10912  10779    457    321    478       O  
ATOM   4853  N   HIS A 635      96.850  30.908  14.443  1.00 52.44           N  
ANISOU 4853  N   HIS A 635     7107   6463   6354    440    264    560       N  
ATOM   4854  CA  HIS A 635      96.614  30.302  13.135  1.00 51.69           C  
ANISOU 4854  CA  HIS A 635     7016   6381   6244    419    227    585       C  
ATOM   4855  C   HIS A 635      97.526  29.078  12.913  1.00 38.90           C  
ANISOU 4855  C   HIS A 635     5395   4778   4609    393    226    552       C  
ATOM   4856  O   HIS A 635      98.715  29.226  12.634  1.00 47.93           O  
ANISOU 4856  O   HIS A 635     6558   5908   5746    381    237    536       O  
ATOM   4857  CB  HIS A 635      96.837  31.344  12.034  1.00 31.25           C  
ANISOU 4857  CB  HIS A 635     4457   3765   3651    416    208    624       C  
ATOM   4858  CG  HIS A 635      96.723  30.801  10.642  1.00 69.32           C  
ANISOU 4858  CG  HIS A 635     9287   8598   8452    392    169    650       C  
ATOM   4859  ND1 HIS A 635      97.819  30.400   9.908  1.00 82.30           N  
ANISOU 4859  ND1 HIS A 635    10948  10245  10078    366    168    639       N  
ATOM   4860  CD2 HIS A 635      95.645  30.605   9.847  1.00 72.52           C  
ANISOU 4860  CD2 HIS A 635     9688   9014   8853    389    131    688       C  
ATOM   4861  CE1 HIS A 635      97.421  29.975   8.722  1.00 67.09           C  
ANISOU 4861  CE1 HIS A 635     9028   8331   8134    347    131    670       C  
ATOM   4862  NE2 HIS A 635      96.107  30.090   8.660  1.00 74.04           N  
ANISOU 4862  NE2 HIS A 635     9896   9216   9022    360    107    700       N  
ATOM   4863  N   PRO A 636      96.957  27.866  13.019  1.00 44.78           N  
ANISOU 4863  N   PRO A 636     6116   5549   5349    383    212    543       N  
ATOM   4864  CA  PRO A 636      97.713  26.608  12.971  1.00 43.31           C  
ANISOU 4864  CA  PRO A 636     5926   5376   5154    360    210    511       C  
ATOM   4865  C   PRO A 636      98.272  26.259  11.589  1.00 37.04           C  
ANISOU 4865  C   PRO A 636     5152   4581   4339    335    187    523       C  
ATOM   4866  O   PRO A 636      97.582  26.417  10.583  1.00 36.05           O  
ANISOU 4866  O   PRO A 636     5033   4461   4202    329    158    561       O  
ATOM   4867  CB  PRO A 636      96.673  25.568  13.386  1.00 28.49           C  
ANISOU 4867  CB  PRO A 636     4020   3526   3279    356    195    510       C  
ATOM   4868  CG  PRO A 636      95.385  26.147  12.936  1.00 48.03           C  
ANISOU 4868  CG  PRO A 636     6490   6004   5754    368    174    553       C  
ATOM   4869  CD  PRO A 636      95.513  27.626  13.181  1.00 49.23           C  
ANISOU 4869  CD  PRO A 636     6657   6131   5918    393    194    566       C  
ATOM   4870  N   LEU A 637      99.515  25.782  11.563  1.00 36.11           N  
ANISOU 4870  N   LEU A 637     5043   4459   4217    323    199    493       N  
ATOM   4871  CA  LEU A 637     100.150  25.289  10.341  1.00 34.18           C  
ANISOU 4871  CA  LEU A 637     4817   4218   3953    299    181    500       C  
ATOM   4872  C   LEU A 637     100.374  23.786  10.454  1.00 40.44           C  
ANISOU 4872  C   LEU A 637     5597   5027   4743    283    174    472       C  
ATOM   4873  O   LEU A 637     100.083  23.028   9.537  1.00 28.69           O  
ANISOU 4873  O   LEU A 637     4111   3553   3237    263    148    487       O  
ATOM   4874  CB  LEU A 637     101.484  25.996  10.099  1.00 37.97           C  
ANISOU 4874  CB  LEU A 637     5320   4676   4429    298    201    490       C  
ATOM   4875  CG  LEU A 637     101.409  27.525   9.948  1.00 39.64           C  
ANISOU 4875  CG  LEU A 637     5549   4868   4644    310    207    519       C  
ATOM   4876  CD1 LEU A 637     102.797  28.116   9.750  1.00 33.35           C  
ANISOU 4876  CD1 LEU A 637     4777   4053   3843    304    226    508       C  
ATOM   4877  CD2 LEU A 637     100.496  27.895   8.788  1.00 24.73           C  
ANISOU 4877  CD2 LEU A 637     3670   2985   2742    303    174    570       C  
ATOM   4878  N   PHE A 638     100.916  23.371  11.592  1.00 47.72           N  
ANISOU 4878  N   PHE A 638     6506   5944   5680    289    195    435       N  
ATOM   4879  CA  PHE A 638     100.970  21.964  11.954  1.00 32.46           C  
ANISOU 4879  CA  PHE A 638     4559   4025   3751    276    186    411       C  
ATOM   4880  C   PHE A 638     100.700  21.789  13.438  1.00 33.35           C  
ANISOU 4880  C   PHE A 638     4649   4139   3883    287    201    390       C  
ATOM   4881  O   PHE A 638     101.623  21.789  14.249  1.00 24.58           O  
ANISOU 4881  O   PHE A 638     3539   3016   2786    292    221    360       O  
ATOM   4882  CB  PHE A 638     102.302  21.318  11.578  1.00 33.06           C  
ANISOU 4882  CB  PHE A 638     4649   4092   3821    263    191    387       C  
ATOM   4883  CG  PHE A 638     102.343  19.827  11.849  1.00 46.38           C  
ANISOU 4883  CG  PHE A 638     6324   5790   5510    248    178    367       C  
ATOM   4884  CD1 PHE A 638     101.729  18.938  10.982  1.00 38.65           C  
ANISOU 4884  CD1 PHE A 638     5344   4827   4514    229    151    384       C  
ATOM   4885  CD2 PHE A 638     102.976  19.318  12.975  1.00 35.59           C  
ANISOU 4885  CD2 PHE A 638     4946   4415   4161    251    192    334       C  
ATOM   4886  CE1 PHE A 638     101.747  17.569  11.227  1.00 45.13           C  
ANISOU 4886  CE1 PHE A 638     6154   5655   5336    213    139    368       C  
ATOM   4887  CE2 PHE A 638     102.997  17.957  13.223  1.00 43.84           C  
ANISOU 4887  CE2 PHE A 638     5981   5468   5208    235    178    321       C  
ATOM   4888  CZ  PHE A 638     102.383  17.078  12.345  1.00 41.85           C  
ANISOU 4888  CZ  PHE A 638     5730   5231   4939    217    153    337       C  
ATOM   4889  N   VAL A 639      99.424  21.674  13.784  1.00 24.74           N  
ANISOU 4889  N   VAL A 639     3539   3064   2796    290    190    407       N  
ATOM   4890  CA  VAL A 639      99.035  21.305  15.133  1.00 35.22           C  
ANISOU 4890  CA  VAL A 639     4841   4399   4139    296    199    391       C  
ATOM   4891  C   VAL A 639      98.315  19.965  15.050  1.00 36.13           C  
ANISOU 4891  C   VAL A 639     4941   4537   4250    273    172    396       C  
ATOM   4892  O   VAL A 639      97.218  19.883  14.502  1.00 45.99           O  
ANISOU 4892  O   VAL A 639     6185   5801   5490    268    151    425       O  
ATOM   4893  CB  VAL A 639      98.108  22.343  15.757  1.00 39.68           C  
ANISOU 4893  CB  VAL A 639     5395   4966   4713    320    212    408       C  
ATOM   4894  CG1 VAL A 639      97.666  21.899  17.148  1.00 30.95           C  
ANISOU 4894  CG1 VAL A 639     4264   3872   3622    324    221    393       C  
ATOM   4895  CG2 VAL A 639      98.802  23.713  15.813  1.00 50.98           C  
ANISOU 4895  CG2 VAL A 639     6847   6374   6149    340    238    405       C  
ATOM   4896  N   ARG A 640      98.952  18.923  15.581  1.00 45.09           N  
ANISOU 4896  N   ARG A 640     6071   5672   5390    258    170    370       N  
ATOM   4897  CA  ARG A 640      98.483  17.534  15.487  1.00 35.68           C  
ANISOU 4897  CA  ARG A 640     4868   4496   4191    231    144    373       C  
ATOM   4898  C   ARG A 640      98.485  16.998  14.047  1.00 33.77           C  
ANISOU 4898  C   ARG A 640     4643   4258   3929    213    120    388       C  
ATOM   4899  O   ARG A 640      98.794  15.837  13.820  1.00 48.30           O  
ANISOU 4899  O   ARG A 640     6485   6102   5764    191    106    379       O  
ATOM   4900  CB  ARG A 640      97.114  17.347  16.154  1.00 32.65           C  
ANISOU 4900  CB  ARG A 640     4460   4133   3811    229    133    391       C  
ATOM   4901  CG  ARG A 640      97.054  17.771  17.607  1.00 38.51           C  
ANISOU 4901  CG  ARG A 640     5184   4876   4571    244    155    378       C  
ATOM   4902  CD  ARG A 640      95.854  17.149  18.312  1.00 56.60           C  
ANISOU 4902  CD  ARG A 640     7450   7191   6863    233    141    392       C  
ATOM   4903  NE  ARG A 640      95.914  15.689  18.249  1.00 85.09           N  
ANISOU 4903  NE  ARG A 640    11057  10808  10464    198    116    387       N  
ATOM   4904  CZ  ARG A 640      94.963  14.871  18.691  1.00 79.98           C  
ANISOU 4904  CZ  ARG A 640    10395  10180   9813    177     97    399       C  
ATOM   4905  NH1 ARG A 640      93.858  15.364  19.234  1.00 79.13           N  
ANISOU 4905  NH1 ARG A 640    10268  10089   9708    191    102    416       N  
ATOM   4906  NH2 ARG A 640      95.117  13.558  18.581  1.00 65.32           N  
ANISOU 4906  NH2 ARG A 640     8543   8326   7949    143     73    394       N  
ATOM   4907  N   SER A 641      98.164  17.845  13.074  1.00 32.97           N  
ANISOU 4907  N   SER A 641     4555   4157   3817    221    116    413       N  
ATOM   4908  CA  SER A 641      98.230  17.458  11.669  1.00 36.10           C  
ANISOU 4908  CA  SER A 641     4969   4557   4191    203     94    429       C  
ATOM   4909  C   SER A 641      98.412  18.676  10.764  1.00 36.12           C  
ANISOU 4909  C   SER A 641     4991   4549   4183    216     99    450       C  
ATOM   4910  O   SER A 641      98.246  19.812  11.194  1.00 41.13           O  
ANISOU 4910  O   SER A 641     5624   5175   4828    238    116    456       O  
ATOM   4911  CB  SER A 641      96.985  16.670  11.255  1.00 44.72           C  
ANISOU 4911  CB  SER A 641     6052   5669   5270    181     60    455       C  
ATOM   4912  OG  SER A 641      95.798  17.392  11.546  1.00 55.00           O  
ANISOU 4912  OG  SER A 641     7342   6978   6575    194     55    479       O  
ATOM   4913  N   LEU A 642      98.764  18.426   9.509  1.00 35.67           N  
ANISOU 4913  N   LEU A 642     4953   4494   4105    201     84    462       N  
ATOM   4914  CA  LEU A 642      98.948  19.487   8.529  1.00 41.12           C  
ANISOU 4914  CA  LEU A 642     5664   5178   4782    206     83    487       C  
ATOM   4915  C   LEU A 642      97.666  20.293   8.310  1.00 53.64           C  
ANISOU 4915  C   LEU A 642     7245   6770   6366    213     66    526       C  
ATOM   4916  O   LEU A 642      96.590  19.728   8.118  1.00 50.04           O  
ANISOU 4916  O   LEU A 642     6780   6331   5903    200     39    545       O  
ATOM   4917  CB  LEU A 642      99.375  18.878   7.200  1.00 25.27           C  
ANISOU 4917  CB  LEU A 642     3673   3178   2748    183     66    497       C  
ATOM   4918  CG  LEU A 642     100.813  18.958   6.686  1.00 36.92           C  
ANISOU 4918  CG  LEU A 642     5170   4642   4215    183     84    479       C  
ATOM   4919  CD1 LEU A 642     101.814  19.532   7.653  1.00 42.78           C  
ANISOU 4919  CD1 LEU A 642     5913   5362   4980    203    118    448       C  
ATOM   4920  CD2 LEU A 642     101.279  17.636   6.117  1.00 33.45           C  
ANISOU 4920  CD2 LEU A 642     4736   4212   3762    164     75    465       C  
ATOM   4921  N   ALA A 643      97.784  21.616   8.333  1.00 38.22           N  
ANISOU 4921  N   ALA A 643     5301   4801   4418    232     80    539       N  
ATOM   4922  CA  ALA A 643      96.648  22.472   8.029  1.00 44.22           C  
ANISOU 4922  CA  ALA A 643     6062   5563   5178    242     61    579       C  
ATOM   4923  C   ALA A 643      96.369  22.443   6.529  1.00 55.80           C  
ANISOU 4923  C   ALA A 643     7547   7037   6617    220     27    617       C  
ATOM   4924  O   ALA A 643      97.215  21.992   5.744  1.00 34.66           O  
ANISOU 4924  O   ALA A 643     4884   4364   3922    201     24    612       O  
ATOM   4925  CB  ALA A 643      96.908  23.914   8.500  1.00 40.75           C  
ANISOU 4925  CB  ALA A 643     5629   5102   4754    269     86    584       C  
ATOM   4926  N   LYS A 644      95.183  22.916   6.147  1.00 62.51           N  
ANISOU 4926  N   LYS A 644     8398   7889   7464    224     -1    657       N  
ATOM   4927  CA  LYS A 644      94.821  23.096   4.748  1.00 64.67           C  
ANISOU 4927  CA  LYS A 644     8693   8168   7712    204    -39    700       C  
ATOM   4928  C   LYS A 644      95.879  23.933   4.035  1.00 70.29           C  
ANISOU 4928  C   LYS A 644     9427   8866   8413    201    -29    711       C  
ATOM   4929  O   LYS A 644      96.350  24.945   4.568  1.00 64.67           O  
ANISOU 4929  O   LYS A 644     8718   8133   7718    222     -3    706       O  
ATOM   4930  CB  LYS A 644      93.472  23.813   4.633  0.50 67.23           C  
ANISOU 4930  CB  LYS A 644     9016   8486   8040    219    -67    739       C  
ATOM   4931  CG  LYS A 644      92.320  23.168   5.385  0.50 65.59           C  
ANISOU 4931  CG  LYS A 644     8785   8291   7843    228    -76    732       C  
ATOM   4932  CD  LYS A 644      91.050  23.992   5.220  0.50 62.62           C  
ANISOU 4932  CD  LYS A 644     8410   7908   7474    251   -102    772       C  
ATOM   4933  CE  LYS A 644      89.859  23.323   5.883  0.50 67.70           C  
ANISOU 4933  CE  LYS A 644     9030   8569   8125    261   -112    768       C  
ATOM   4934  NZ  LYS A 644      88.602  24.090   5.651  0.50 69.29           N  
ANISOU 4934  NZ  LYS A 644     9229   8765   8333    288   -139    809       N  
ATOM   4935  N   ASN A 645      96.245  23.497   2.835  1.00 53.89           N  
ANISOU 4935  N   ASN A 645     7366   6804   6307    172    -48    728       N  
ATOM   4936  CA  ASN A 645      97.196  24.210   1.985  1.00 55.27           C  
ANISOU 4936  CA  ASN A 645     7563   6972   6466    163    -43    746       C  
ATOM   4937  C   ASN A 645      98.648  24.073   2.442  1.00 51.05           C  
ANISOU 4937  C   ASN A 645     7029   6429   5937    168     -1    702       C  
ATOM   4938  O   ASN A 645      99.533  24.721   1.890  1.00 53.96           O  
ANISOU 4938  O   ASN A 645     7416   6790   6294    163      8    712       O  
ATOM   4939  CB  ASN A 645      96.812  25.689   1.811  0.50 47.26           C  
ANISOU 4939  CB  ASN A 645     6562   5934   5459    177    -54    787       C  
ATOM   4940  CG  ASN A 645      96.478  26.043   0.373  0.50 72.42           C  
ANISOU 4940  CG  ASN A 645     9772   9129   8616    151    -96    843       C  
ATOM   4941  OD1 ASN A 645      96.923  25.375  -0.560  0.50 85.39           O  
ANISOU 4941  OD1 ASN A 645    11419  10796  10228    122   -105    850       O  
ATOM   4942  ND2 ASN A 645      95.733  27.123   0.186  0.50 80.02           N  
ANISOU 4942  ND2 ASN A 645    10747  10070   9587    162   -120    885       N  
ATOM   4943  N   MET A 646      98.888  23.211   3.429  1.00 42.96           N  
ANISOU 4943  N   MET A 646     5987   5406   4929    177     20    655       N  
ATOM   4944  CA  MET A 646     100.235  22.972   3.953  1.00 29.57           C  
ANISOU 4944  CA  MET A 646     4295   3700   3242    183     56    611       C  
ATOM   4945  C   MET A 646     100.720  21.550   3.657  1.00 60.01           C  
ANISOU 4945  C   MET A 646     8146   7571   7084    166     54    585       C  
ATOM   4946  O   MET A 646      99.944  20.597   3.663  1.00 33.29           O  
ANISOU 4946  O   MET A 646     4748   4203   3696    156     35    585       O  
ATOM   4947  CB  MET A 646     100.288  23.203   5.472  1.00 29.58           C  
ANISOU 4947  CB  MET A 646     4278   3684   3275    209     84    576       C  
ATOM   4948  CG  MET A 646      99.762  24.551   5.940  1.00 54.26           C  
ANISOU 4948  CG  MET A 646     7405   6793   6417    231     90    597       C  
ATOM   4949  SD  MET A 646     100.786  25.876   5.289  1.00 45.83           S  
ANISOU 4949  SD  MET A 646     6367   5704   5341    229    102    617       S  
ATOM   4950  CE  MET A 646     102.276  25.642   6.237  1.00 42.36           C  
ANISOU 4950  CE  MET A 646     5928   5252   4917    237    143    561       C  
ATOM   4951  N   THR A 647     102.018  21.421   3.421  1.00 51.38           N  
ANISOU 4951  N   THR A 647     7066   6470   5984    163     75    563       N  
ATOM   4952  CA  THR A 647     102.637  20.137   3.149  1.00 49.45           C  
ANISOU 4952  CA  THR A 647     6824   6236   5729    152     77    536       C  
ATOM   4953  C   THR A 647     104.080  20.165   3.637  1.00 50.14           C  
ANISOU 4953  C   THR A 647     6919   6303   5827    161    109    498       C  
ATOM   4954  O   THR A 647     104.674  21.231   3.763  1.00 33.89           O  
ANISOU 4954  O   THR A 647     4872   4230   3775    169    125    501       O  
ATOM   4955  CB  THR A 647     102.651  19.838   1.643  1.00 43.94           C  
ANISOU 4955  CB  THR A 647     6141   5562   4993    128     57    567       C  
ATOM   4956  OG1 THR A 647     103.415  18.654   1.397  1.00 36.13           O  
ANISOU 4956  OG1 THR A 647     5157   4578   3993    121     64    537       O  
ATOM   4957  CG2 THR A 647     103.292  20.984   0.882  1.00 48.24           C  
ANISOU 4957  CG2 THR A 647     6706   6102   5520    124     63    593       C  
ATOM   4958  N   TRP A 648     104.641  18.993   3.915  1.00 26.61           N  
ANISOU 4958  N   TRP A 648     3937   3322   2852    159    115    463       N  
ATOM   4959  CA  TRP A 648     106.076  18.890   4.164  1.00 29.64           C  
ANISOU 4959  CA  TRP A 648     4331   3688   3242    165    140    431       C  
ATOM   4960  C   TRP A 648     106.789  18.768   2.834  1.00 20.24           C  
ANISOU 4960  C   TRP A 648     3162   2508   2018    148    138    445       C  
ATOM   4961  O   TRP A 648     106.206  18.323   1.852  1.00 35.83           O  
ANISOU 4961  O   TRP A 648     5142   4506   3967    133    118    469       O  
ATOM   4962  CB  TRP A 648     106.426  17.673   5.032  1.00 29.41           C  
ANISOU 4962  CB  TRP A 648     4291   3650   3232    170    147    391       C  
ATOM   4963  CG  TRP A 648     105.773  17.669   6.380  1.00 32.59           C  
ANISOU 4963  CG  TRP A 648     4671   4047   3665    183    149    377       C  
ATOM   4964  CD1 TRP A 648     104.697  16.919   6.766  1.00 43.30           C  
ANISOU 4964  CD1 TRP A 648     6009   5416   5027    178    131    380       C  
ATOM   4965  CD2 TRP A 648     106.137  18.459   7.521  1.00 45.62           C  
ANISOU 4965  CD2 TRP A 648     6313   5679   5341    201    170    360       C  
ATOM   4966  NE1 TRP A 648     104.375  17.184   8.071  1.00 31.41           N  
ANISOU 4966  NE1 TRP A 648     4484   3903   3548    192    141    367       N  
ATOM   4967  CE2 TRP A 648     105.239  18.128   8.558  1.00 34.09           C  
ANISOU 4967  CE2 TRP A 648     4830   4224   3899    206    165    354       C  
ATOM   4968  CE3 TRP A 648     107.124  19.421   7.766  1.00 14.95           C  
ANISOU 4968  CE3 TRP A 648     2439   1778   1463    210    193    352       C  
ATOM   4969  CZ2 TRP A 648     105.309  18.713   9.818  1.00 28.79           C  
ANISOU 4969  CZ2 TRP A 648     4145   3541   3252    223    183    338       C  
ATOM   4970  CZ3 TRP A 648     107.194  19.983   9.018  1.00 23.38           C  
ANISOU 4970  CZ3 TRP A 648     3495   2832   2555    226    210    336       C  
ATOM   4971  CH2 TRP A 648     106.296  19.630  10.027  1.00 27.74           C  
ANISOU 4971  CH2 TRP A 648     4025   3390   3125    233    205    328       C  
ATOM   4972  N   GLN A 649     108.043  19.200   2.804  1.00 32.54           N  
ANISOU 4972  N   GLN A 649     4734   4053   3577    150    160    433       N  
ATOM   4973  CA  GLN A 649     108.889  19.066   1.628  1.00 33.07           C  
ANISOU 4973  CA  GLN A 649     4822   4133   3612    133    163    443       C  
ATOM   4974  C   GLN A 649     110.223  18.556   2.098  1.00 30.56           C  
ANISOU 4974  C   GLN A 649     4507   3797   3307    139    185    405       C  
ATOM   4975  O   GLN A 649     110.799  19.085   3.052  1.00 40.00           O  
ANISOU 4975  O   GLN A 649     5698   4972   4529    152    203    387       O  
ATOM   4976  CB  GLN A 649     109.116  20.395   0.900  1.00 24.55           C  
ANISOU 4976  CB  GLN A 649     3756   3058   2513    123    166    479       C  
ATOM   4977  CG  GLN A 649     107.957  20.913   0.086  1.00 48.26           C  
ANISOU 4977  CG  GLN A 649     6759   6082   5494    112    140    527       C  
ATOM   4978  CD  GLN A 649     108.389  21.980  -0.914  1.00 53.34           C  
ANISOU 4978  CD  GLN A 649     7421   6736   6109     96    141    567       C  
ATOM   4979  OE1 GLN A 649     109.586  22.201  -1.137  1.00 46.12           O  
ANISOU 4979  OE1 GLN A 649     6519   5818   5185     89    160    559       O  
ATOM   4980  NE2 GLN A 649     107.414  22.643  -1.525  1.00 43.91           N  
ANISOU 4980  NE2 GLN A 649     6228   5556   4901     87    117    614       N  
ATOM   4981  N   LEU A 650     110.717  17.533   1.418  1.00 27.80           N  
ANISOU 4981  N   LEU A 650     4168   3458   2938    130    184    395       N  
ATOM   4982  CA  LEU A 650     111.989  16.947   1.772  1.00 40.41           C  
ANISOU 4982  CA  LEU A 650     5769   5039   4545    134    203    363       C  
ATOM   4983  C   LEU A 650     112.868  17.000   0.545  1.00 42.82           C  
ANISOU 4983  C   LEU A 650     6094   5363   4814    117    211    377       C  
ATOM   4984  O   LEU A 650     112.579  16.368  -0.468  1.00 57.66           O  
ANISOU 4984  O   LEU A 650     7983   7265   6660    104    199    388       O  
ATOM   4985  CB  LEU A 650     111.796  15.507   2.250  1.00 39.20           C  
ANISOU 4985  CB  LEU A 650     5609   4879   4406    141    195    335       C  
ATOM   4986  CG  LEU A 650     111.193  15.286   3.642  1.00 38.37           C  
ANISOU 4986  CG  LEU A 650     5483   4758   4339    156    192    315       C  
ATOM   4987  CD1 LEU A 650     109.719  15.632   3.697  1.00 30.09           C  
ANISOU 4987  CD1 LEU A 650     4421   3721   3289    155    173    338       C  
ATOM   4988  CD2 LEU A 650     111.412  13.842   4.097  1.00 37.88           C  
ANISOU 4988  CD2 LEU A 650     5418   4686   4289    160    188    287       C  
ATOM   4989  N   ALA A 651     113.945  17.766   0.629  1.00 38.99           N  
ANISOU 4989  N   ALA A 651     5614   4870   4330    115    231    376       N  
ATOM   4990  CA  ALA A 651     114.755  18.023  -0.555  1.00 27.90           C  
ANISOU 4990  CA  ALA A 651     4225   3489   2885     94    240    395       C  
ATOM   4991  C   ALA A 651     116.197  17.645  -0.321  1.00 35.29           C  
ANISOU 4991  C   ALA A 651     5164   4417   3828     95    262    371       C  
ATOM   4992  O   ALA A 651     116.841  18.165   0.582  1.00 49.75           O  
ANISOU 4992  O   ALA A 651     6988   6227   5687    105    276    357       O  
ATOM   4993  CB  ALA A 651     114.648  19.493  -0.969  1.00 31.04           C  
ANISOU 4993  CB  ALA A 651     4629   3896   3269     83    241    433       C  
ATOM   4994  N   ASP A 652     116.712  16.739  -1.141  1.00 53.10           N  
ANISOU 4994  N   ASP A 652     7428   6691   6054     85    265    365       N  
ATOM   4995  CA  ASP A 652     118.111  16.347  -1.036  1.00 50.21           C  
ANISOU 4995  CA  ASP A 652     7064   6324   5690     85    287    345       C  
ATOM   4996  C   ASP A 652     118.911  16.927  -2.184  1.00 52.15           C  
ANISOU 4996  C   ASP A 652     7321   6605   5890     60    301    369       C  
ATOM   4997  O   ASP A 652     118.418  17.774  -2.925  1.00 41.95           O  
ANISOU 4997  O   ASP A 652     6035   5333   4570     44    295    402       O  
ATOM   4998  CB  ASP A 652     118.274  14.824  -0.968  1.00 56.88           C  
ANISOU 4998  CB  ASP A 652     7910   7164   6538     94    284    317       C  
ATOM   4999  CG  ASP A 652     117.450  14.095  -2.014  1.00 65.28           C  
ANISOU 4999  CG  ASP A 652     8986   8254   7565     83    268    327       C  
ATOM   5000  OD1 ASP A 652     117.320  14.603  -3.151  1.00 69.90           O  
ANISOU 5000  OD1 ASP A 652     9580   8873   8107     63    267    355       O  
ATOM   5001  OD2 ASP A 652     116.921  13.005  -1.696  1.00 51.36           O  
ANISOU 5001  OD2 ASP A 652     7221   6477   5815     94    255    309       O  
ATOM   5002  N   THR A 653     120.140  16.446  -2.331  1.00 50.58           N  
ANISOU 5002  N   THR A 653     7122   6415   5681     55    321    353       N  
ATOM   5003  CA  THR A 653     121.088  16.995  -3.291  1.00 55.29           C  
ANISOU 5003  CA  THR A 653     7725   7050   6235     30    340    372       C  
ATOM   5004  C   THR A 653     120.855  16.512  -4.718  1.00 64.65           C  
ANISOU 5004  C   THR A 653     8921   8281   7362     12    337    387       C  
ATOM   5005  O   THR A 653     121.101  17.244  -5.673  1.00 76.71           O  
ANISOU 5005  O   THR A 653    10454   9846   8846    -11    345    416       O  
ATOM   5006  CB  THR A 653     122.525  16.597  -2.923  1.00 61.41           C  
ANISOU 5006  CB  THR A 653     8492   7825   7017     32    364    349       C  
ATOM   5007  OG1 THR A 653     122.603  16.291  -1.527  1.00 74.25           O  
ANISOU 5007  OG1 THR A 653    10106   9406   8698     56    360    323       O  
ATOM   5008  CG2 THR A 653     123.487  17.713  -3.257  1.00 76.22           C  
ANISOU 5008  CG2 THR A 653    10365   9722   8871     10    384    370       C  
ATOM   5009  N   SER A 654     120.375  15.283  -4.858  1.00 59.51           N  
ANISOU 5009  N   SER A 654     8274   7629   6707     21    326    367       N  
ATOM   5010  CA  SER A 654     120.429  14.594  -6.139  1.00 58.42           C  
ANISOU 5010  CA  SER A 654     8148   7538   6513      6    329    370       C  
ATOM   5011  C   SER A 654     119.087  14.374  -6.823  1.00 61.27           C  
ANISOU 5011  C   SER A 654     8517   7913   6849      1    304    388       C  
ATOM   5012  O   SER A 654     119.049  13.922  -7.967  1.00 69.29           O  
ANISOU 5012  O   SER A 654     9543   8973   7812    -13    305    393       O  
ATOM   5013  CB  SER A 654     121.093  13.235  -5.941  1.00 72.56           C  
ANISOU 5013  CB  SER A 654     9938   9324   8308     18    339    332       C  
ATOM   5014  OG  SER A 654     120.259  12.391  -5.167  1.00 71.23           O  
ANISOU 5014  OG  SER A 654     9771   9116   8179     39    319    314       O  
ATOM   5015  N   THR A 655     117.989  14.661  -6.131  1.00 55.59           N  
ANISOU 5015  N   THR A 655     7793   7162   6167     14    281    395       N  
ATOM   5016  CA  THR A 655     116.666  14.341  -6.663  1.00 57.77           C  
ANISOU 5016  CA  THR A 655     8074   7450   6425     11    255    411       C  
ATOM   5017  C   THR A 655     115.651  15.458  -6.480  1.00 60.71           C  
ANISOU 5017  C   THR A 655     8441   7816   6811     10    237    445       C  
ATOM   5018  O   THR A 655     115.881  16.406  -5.732  1.00 57.86           O  
ANISOU 5018  O   THR A 655     8072   7430   6481     16    243    450       O  
ATOM   5019  CB  THR A 655     116.096  13.093  -5.988  1.00 59.22           C  
ANISOU 5019  CB  THR A 655     8256   7605   6638     29    241    380       C  
ATOM   5020  OG1 THR A 655     116.062  13.308  -4.575  1.00 61.60           O  
ANISOU 5020  OG1 THR A 655     8545   7860   7001     50    240    364       O  
ATOM   5021  CG2 THR A 655     116.956  11.876  -6.292  1.00 45.27           C  
ANISOU 5021  CG2 THR A 655     6500   5848   4854     30    255    349       C  
ATOM   5022  N   GLN A 656     114.517  15.325  -7.162  1.00 60.91           N  
ANISOU 5022  N   GLN A 656     8469   7863   6810      4    213    468       N  
ATOM   5023  CA  GLN A 656     113.437  16.296  -7.052  1.00 65.08           C  
ANISOU 5023  CA  GLN A 656     8989   8389   7349      4    193    504       C  
ATOM   5024  C   GLN A 656     112.906  16.327  -5.617  1.00 62.21           C  
ANISOU 5024  C   GLN A 656     8612   7979   7047     26    186    484       C  
ATOM   5025  O   GLN A 656     112.961  15.325  -4.900  1.00 57.58           O  
ANISOU 5025  O   GLN A 656     8021   7369   6488     40    187    447       O  
ATOM   5026  CB  GLN A 656     112.311  15.970  -8.043  1.00 74.39           C  
ANISOU 5026  CB  GLN A 656    10172   9604   8488     -6    168    532       C  
ATOM   5027  CG  GLN A 656     112.772  15.724  -9.486  1.00 96.06           C  
ANISOU 5027  CG  GLN A 656    12931  12401  11165    -25    176    547       C  
ATOM   5028  CD  GLN A 656     113.113  14.260  -9.780  1.00105.36           C  
ANISOU 5028  CD  GLN A 656    14120  13589  12324    -24    182    508       C  
ATOM   5029  OE1 GLN A 656     113.628  13.539  -8.922  1.00 94.94           O  
ANISOU 5029  OE1 GLN A 656    12798  12235  11040    -11    192    467       O  
ATOM   5030  NE2 GLN A 656     112.824  13.822 -11.003  1.00 99.98           N  
ANISOU 5030  NE2 GLN A 656    13451  12955  11584    -36    175    521       N  
ATOM   5031  N   LYS A 657     112.409  17.484  -5.200  1.00 55.43           N  
ANISOU 5031  N   LYS A 657     7745   7108   6208     29    180    509       N  
ATOM   5032  CA  LYS A 657     111.876  17.643  -3.857  1.00 50.47           C  
ANISOU 5032  CA  LYS A 657     7101   6442   5632     50    175    491       C  
ATOM   5033  C   LYS A 657     110.672  16.735  -3.678  1.00 52.25           C  
ANISOU 5033  C   LYS A 657     7317   6669   5866     57    152    485       C  
ATOM   5034  O   LYS A 657     109.910  16.511  -4.617  1.00 54.14           O  
ANISOU 5034  O   LYS A 657     7560   6939   6071     44    133    512       O  
ATOM   5035  CB  LYS A 657     111.499  19.110  -3.594  1.00 52.08           C  
ANISOU 5035  CB  LYS A 657     7301   6638   5849     51    172    522       C  
ATOM   5036  CG  LYS A 657     110.499  19.703  -4.589  1.00 62.70           C  
ANISOU 5036  CG  LYS A 657     8648   8014   7161     36    149    575       C  
ATOM   5037  CD  LYS A 657     110.296  21.192  -4.366  1.00 75.84           C  
ANISOU 5037  CD  LYS A 657    10312   9665   8837     36    147    608       C  
ATOM   5038  CE  LYS A 657     109.444  21.811  -5.477  1.00 91.27           C  
ANISOU 5038  CE  LYS A 657    12270  11653  10757     19    123    668       C  
ATOM   5039  NZ  LYS A 657     109.363  23.302  -5.389  1.00 93.41           N  
ANISOU 5039  NZ  LYS A 657    12544  11911  11036     16    121    707       N  
ATOM   5040  N   VAL A 658     110.511  16.199  -2.474  1.00 41.04           N  
ANISOU 5040  N   VAL A 658     5885   5219   4489     75    154    452       N  
ATOM   5041  CA  VAL A 658     109.386  15.328  -2.187  1.00 45.38           C  
ANISOU 5041  CA  VAL A 658     6424   5771   5048     80    132    446       C  
ATOM   5042  C   VAL A 658     108.351  16.031  -1.320  1.00 47.77           C  
ANISOU 5042  C   VAL A 658     6708   6063   5381     90    121    459       C  
ATOM   5043  O   VAL A 658     108.675  16.544  -0.249  1.00 41.35           O  
ANISOU 5043  O   VAL A 658     5886   5224   4603    105    136    441       O  
ATOM   5044  CB  VAL A 658     109.850  14.041  -1.484  1.00 37.30           C  
ANISOU 5044  CB  VAL A 658     5400   4726   4047     90    139    403       C  
ATOM   5045  CG1 VAL A 658     108.657  13.212  -1.048  1.00 28.33           C  
ANISOU 5045  CG1 VAL A 658     4251   3590   2923     93    117    399       C  
ATOM   5046  CG2 VAL A 658     110.760  13.243  -2.403  1.00 31.68           C  
ANISOU 5046  CG2 VAL A 658     4708   4027   3302     80    148    391       C  
ATOM   5047  N   LEU A 659     107.107  16.048  -1.786  1.00 45.74           N  
ANISOU 5047  N   LEU A 659     6443   5828   5109     82     96    490       N  
ATOM   5048  CA  LEU A 659     106.008  16.608  -1.008  1.00 41.24           C  
ANISOU 5048  CA  LEU A 659     5854   5252   4566     90     83    504       C  
ATOM   5049  C   LEU A 659     105.343  15.504  -0.208  1.00 48.62           C  
ANISOU 5049  C   LEU A 659     6772   6181   5522     96     73    480       C  
ATOM   5050  O   LEU A 659     104.808  14.562  -0.778  1.00 58.65           O  
ANISOU 5050  O   LEU A 659     8043   7470   6772     86     56    485       O  
ATOM   5051  CB  LEU A 659     104.973  17.271  -1.924  1.00 50.74           C  
ANISOU 5051  CB  LEU A 659     7054   6482   5742     77     58    557       C  
ATOM   5052  CG  LEU A 659     105.085  18.774  -2.199  1.00 65.54           C  
ANISOU 5052  CG  LEU A 659     8935   8354   7612     75     60    592       C  
ATOM   5053  CD1 LEU A 659     106.470  19.146  -2.719  1.00 53.03           C  
ANISOU 5053  CD1 LEU A 659     7372   6768   6010     69     84    586       C  
ATOM   5054  CD2 LEU A 659     104.004  19.192  -3.190  1.00 55.44           C  
ANISOU 5054  CD2 LEU A 659     7654   7107   6305     60     30    648       C  
ATOM   5055  N   ALA A 660     105.357  15.631   1.114  1.00 47.18           N  
ANISOU 5055  N   ALA A 660     6575   5974   5379    112     84    456       N  
ATOM   5056  CA  ALA A 660     104.785  14.600   1.975  1.00 36.42           C  
ANISOU 5056  CA  ALA A 660     5194   4606   4036    116     76    434       C  
ATOM   5057  C   ALA A 660     103.725  15.155   2.917  1.00 41.78           C  
ANISOU 5057  C   ALA A 660     5850   5285   4740    123     69    445       C  
ATOM   5058  O   ALA A 660     103.937  16.184   3.559  1.00 53.41           O  
ANISOU 5058  O   ALA A 660     7319   6742   6231    137     84    443       O  
ATOM   5059  CB  ALA A 660     105.872  13.945   2.761  1.00 32.01           C  
ANISOU 5059  CB  ALA A 660     4640   4024   3500    126     97    391       C  
ATOM   5060  N   SER A 661     102.595  14.463   3.018  1.00 33.52           N  
ANISOU 5060  N   SER A 661     4788   4255   3693    114     46    457       N  
ATOM   5061  CA  SER A 661     101.506  14.925   3.872  1.00 38.24           C  
ANISOU 5061  CA  SER A 661     5362   4855   4311    119     37    470       C  
ATOM   5062  C   SER A 661     101.127  13.910   4.947  1.00 46.92           C  
ANISOU 5062  C   SER A 661     6443   5953   5432    118     34    448       C  
ATOM   5063  O   SER A 661     100.179  14.116   5.710  1.00 45.29           O  
ANISOU 5063  O   SER A 661     6216   5752   5241    119     25    458       O  
ATOM   5064  CB  SER A 661     100.283  15.241   3.028  1.00 43.23           C  
ANISOU 5064  CB  SER A 661     5990   5513   4921    105      7    517       C  
ATOM   5065  OG  SER A 661      99.895  14.101   2.289  1.00 68.43           O  
ANISOU 5065  OG  SER A 661     9181   8728   8091     88    -13    526       O  
ATOM   5066  N   GLY A 662     101.873  12.817   5.010  1.00 28.39           N  
ANISOU 5066  N   GLY A 662     4104   3598   3086    115     40    419       N  
ATOM   5067  CA  GLY A 662     101.530  11.740   5.916  1.00 38.57           C  
ANISOU 5067  CA  GLY A 662     5377   4887   4392    110     33    402       C  
ATOM   5068  C   GLY A 662     102.298  11.681   7.221  1.00 47.12           C  
ANISOU 5068  C   GLY A 662     6453   5946   5504    124     55    367       C  
ATOM   5069  O   GLY A 662     102.805  12.693   7.705  1.00 46.52           O  
ANISOU 5069  O   GLY A 662     6377   5856   5442    139     75    359       O  
ATOM   5070  N   ALA A 663     102.383  10.473   7.780  1.00 33.45           N  
ANISOU 5070  N   ALA A 663     4716   4211   3781    116     49    348       N  
ATOM   5071  CA  ALA A 663     103.048  10.238   9.051  1.00 36.66           C  
ANISOU 5071  CA  ALA A 663     5114   4599   4214    124     65    319       C  
ATOM   5072  C   ALA A 663     104.550  10.065   8.880  1.00 29.68           C  
ANISOU 5072  C   ALA A 663     4254   3692   3333    135     84    290       C  
ATOM   5073  O   ALA A 663     105.307  10.188   9.842  1.00 37.26           O  
ANISOU 5073  O   ALA A 663     5209   4636   4314    145    101    268       O  
ATOM   5074  CB  ALA A 663     102.455   9.020   9.754  1.00 43.34           C  
ANISOU 5074  CB  ALA A 663     5946   5454   5069    109     48    317       C  
ATOM   5075  N   SER A 664     104.981   9.779   7.658  1.00 19.69           N  
ANISOU 5075  N   SER A 664     3012   2425   2044    131     82    293       N  
ATOM   5076  CA  SER A 664     106.391   9.509   7.406  1.00 25.79           C  
ANISOU 5076  CA  SER A 664     3807   3176   2816    139     99    268       C  
ATOM   5077  C   SER A 664     106.732   9.607   5.933  1.00 16.80           C  
ANISOU 5077  C   SER A 664     2693   2043   1646    135     98    280       C  
ATOM   5078  O   SER A 664     105.861   9.522   5.081  1.00 29.16           O  
ANISOU 5078  O   SER A 664     4261   3630   3189    123     80    304       O  
ATOM   5079  CB  SER A 664     106.772   8.100   7.907  1.00 49.84           C  
ANISOU 5079  CB  SER A 664     6857   6209   5871    135     93    245       C  
ATOM   5080  OG  SER A 664     106.276   7.096   7.042  1.00 31.98           O  
ANISOU 5080  OG  SER A 664     4609   3955   3587    121     74    253       O  
ATOM   5081  N   ALA A 665     108.022   9.743   5.646  1.00 10.31           N  
ANISOU 5081  N   ALA A 665     1888   1206    823    143    117    264       N  
ATOM   5082  CA  ALA A 665     108.509   9.959   4.287  1.00 23.15           C  
ANISOU 5082  CA  ALA A 665     3538   2840   2417    138    120    276       C  
ATOM   5083  C   ALA A 665     110.012  10.080   4.280  1.00 25.34           C  
ANISOU 5083  C   ALA A 665     3829   3100   2700    148    143    257       C  
ATOM   5084  O   ALA A 665     110.639  10.138   5.321  1.00 23.69           O  
ANISOU 5084  O   ALA A 665     3610   2872   2519    159    156    237       O  
ATOM   5085  CB  ALA A 665     107.913  11.227   3.684  1.00 32.15           C  
ANISOU 5085  CB  ALA A 665     4674   3999   3542    135    117    308       C  
ATOM   5086  N   THR A 666     110.583  10.099   3.088  1.00 26.09           N  
ANISOU 5086  N   THR A 666     3945   3203   2764    141    148    265       N  
ATOM   5087  CA  THR A 666     112.012  10.317   2.926  1.00 22.76           C  
ANISOU 5087  CA  THR A 666     3535   2771   2342    147    171    253       C  
ATOM   5088  C   THR A 666     112.201  11.295   1.785  1.00 34.31           C  
ANISOU 5088  C   THR A 666     5010   4255   3773    136    176    279       C  
ATOM   5089  O   THR A 666     111.262  11.583   1.029  1.00 26.65           O  
ANISOU 5089  O   THR A 666     4041   3307   2778    125    161    304       O  
ATOM   5090  CB  THR A 666     112.751   9.029   2.516  1.00 38.08           C  
ANISOU 5090  CB  THR A 666     5494   4704   4270    146    173    235       C  
ATOM   5091  OG1 THR A 666     112.456   8.744   1.149  1.00 43.43           O  
ANISOU 5091  OG1 THR A 666     6191   5406   4906    131    164    251       O  
ATOM   5092  CG2 THR A 666     112.325   7.847   3.374  1.00 23.85           C  
ANISOU 5092  CG2 THR A 666     3686   2885   2490    150    160    216       C  
ATOM   5093  N   SER A 667     113.420  11.789   1.637  1.00 33.09           N  
ANISOU 5093  N   SER A 667     4862   4096   3615    138    198    275       N  
ATOM   5094  CA  SER A 667     113.742  12.587   0.465  1.00 47.32           C  
ANISOU 5094  CA  SER A 667     6677   5921   5381    124    204    300       C  
ATOM   5095  C   SER A 667     113.825  11.670  -0.749  1.00 56.23           C  
ANISOU 5095  C   SER A 667     7824   7073   6468    110    199    303       C  
ATOM   5096  O   SER A 667     113.624  10.466  -0.630  1.00 51.65           O  
ANISOU 5096  O   SER A 667     7248   6485   5891    114    190    285       O  
ATOM   5097  CB  SER A 667     115.051  13.342   0.669  1.00 46.03           C  
ANISOU 5097  CB  SER A 667     6514   5750   5224    126    229    296       C  
ATOM   5098  OG  SER A 667     116.077  12.457   1.093  1.00 34.62           O  
ANISOU 5098  OG  SER A 667     5070   4289   3793    135    241    269       O  
ATOM   5099  N   GLY A 668     114.110  12.240  -1.912  1.00 57.59           N  
ANISOU 5099  N   GLY A 668     8008   7274   6599     94    204    325       N  
ATOM   5100  CA  GLY A 668     114.134  11.473  -3.140  1.00 40.85           C  
ANISOU 5100  CA  GLY A 668     5906   5184   4433     79    200    330       C  
ATOM   5101  C   GLY A 668     115.111  10.315  -3.123  1.00 58.22           C  
ANISOU 5101  C   GLY A 668     8115   7374   6630     84    213    299       C  
ATOM   5102  O   GLY A 668     114.804   9.223  -3.622  1.00 52.23           O  
ANISOU 5102  O   GLY A 668     7370   6626   5851     81    203    289       O  
ATOM   5103  N   ASP A 669     116.285  10.543  -2.540  1.00 57.96           N  
ANISOU 5103  N   ASP A 669     8077   7325   6619     93    235    285       N  
ATOM   5104  CA  ASP A 669     117.324   9.522  -2.504  1.00 46.17           C  
ANISOU 5104  CA  ASP A 669     6592   5827   5125    100    249    259       C  
ATOM   5105  C   ASP A 669     117.072   8.449  -1.448  1.00 45.10           C  
ANISOU 5105  C   ASP A 669     6452   5654   5028    119    238    235       C  
ATOM   5106  O   ASP A 669     117.928   7.589  -1.213  1.00 55.64           O  
ANISOU 5106  O   ASP A 669     7791   6977   6370    128    248    214       O  
ATOM   5107  CB  ASP A 669     118.708  10.155  -2.294  1.00 58.98           C  
ANISOU 5107  CB  ASP A 669     8208   7450   6753    100    276    257       C  
ATOM   5108  CG  ASP A 669     118.832  10.907  -0.971  1.00 56.06           C  
ANISOU 5108  CG  ASP A 669     7820   7047   6434    115    278    253       C  
ATOM   5109  OD1 ASP A 669     118.103  10.600  -0.003  1.00 49.26           O  
ANISOU 5109  OD1 ASP A 669     6950   6157   5609    129    264    243       O  
ATOM   5110  OD2 ASP A 669     119.679  11.820  -0.905  1.00 61.10           O  
ANISOU 5110  OD2 ASP A 669     8452   7690   7072    110    296    261       O  
ATOM   5111  N   LYS A 670     115.919   8.531  -0.791  1.00 43.44           N  
ANISOU 5111  N   LYS A 670     6232   5428   4844    124    218    238       N  
ATOM   5112  CA  LYS A 670     115.536   7.578   0.247  1.00 40.96           C  
ANISOU 5112  CA  LYS A 670     5913   5085   4566    137    206    218       C  
ATOM   5113  C   LYS A 670     116.574   7.425   1.376  1.00 33.78           C  
ANISOU 5113  C   LYS A 670     4993   4147   3695    155    221    198       C  
ATOM   5114  O   LYS A 670     116.510   6.484   2.158  1.00 40.10           O  
ANISOU 5114  O   LYS A 670     5791   4925   4518    165    214    181       O  
ATOM   5115  CB  LYS A 670     115.223   6.207  -0.379  1.00 40.45           C  
ANISOU 5115  CB  LYS A 670     5868   5025   4477    133    193    208       C  
ATOM   5116  CG  LYS A 670     114.182   6.235  -1.502  1.00 60.32           C  
ANISOU 5116  CG  LYS A 670     8395   7572   6952    114    176    228       C  
ATOM   5117  CD  LYS A 670     112.759   6.449  -0.970  1.00 77.61           C  
ANISOU 5117  CD  LYS A 670    10569   9758   9160    112    153    240       C  
ATOM   5118  CE  LYS A 670     111.695   6.199  -2.042  1.00 85.67           C  
ANISOU 5118  CE  LYS A 670    11600  10809  10140     95    131    258       C  
ATOM   5119  NZ  LYS A 670     111.455   4.743  -2.295  1.00 91.02           N  
ANISOU 5119  NZ  LYS A 670    12297  11481  10805     92    118    241       N  
ATOM   5120  N   GLN A 671     117.529   8.344   1.476  1.00 51.93           N  
ANISOU 5120  N   GLN A 671     7285   6449   5998    156    241    203       N  
ATOM   5121  CA  GLN A 671     118.567   8.218   2.500  1.00 50.90           C  
ANISOU 5121  CA  GLN A 671     7144   6296   5901    171    255    187       C  
ATOM   5122  C   GLN A 671     118.919   9.501   3.267  1.00 52.13           C  
ANISOU 5122  C   GLN A 671     7282   6445   6081    174    266    192       C  
ATOM   5123  O   GLN A 671     119.162   9.449   4.470  1.00 39.52           O  
ANISOU 5123  O   GLN A 671     5669   4826   4519    187    267    178       O  
ATOM   5124  CB  GLN A 671     119.838   7.612   1.894  1.00 53.98           C  
ANISOU 5124  CB  GLN A 671     7545   6695   6269    170    272    180       C  
ATOM   5125  CG  GLN A 671     119.705   6.157   1.481  0.50 51.82           C  
ANISOU 5125  CG  GLN A 671     7289   6419   5980    173    263    168       C  
ATOM   5126  CD  GLN A 671     119.447   5.233   2.659  0.50 55.77           C  
ANISOU 5126  CD  GLN A 671     7785   6887   6519    190    250    151       C  
ATOM   5127  OE1 GLN A 671     119.780   5.551   3.798  0.50 63.47           O  
ANISOU 5127  OE1 GLN A 671     8742   7844   7530    200    253    146       O  
ATOM   5128  NE2 GLN A 671     118.851   4.079   2.386  0.50 47.34           N  
ANISOU 5128  NE2 GLN A 671     6733   5813   5440    189    234    144       N  
ATOM   5129  N   SER A 672     118.938  10.641   2.579  1.00 50.33           N  
ANISOU 5129  N   SER A 672     7055   6236   5831    162    273    211       N  
ATOM   5130  CA  SER A 672     119.449  11.883   3.164  1.00 54.82           C  
ANISOU 5130  CA  SER A 672     7613   6800   6417    163    286    217       C  
ATOM   5131  C   SER A 672     118.578  12.492   4.254  1.00 37.19           C  
ANISOU 5131  C   SER A 672     5364   4550   4216    172    277    214       C  
ATOM   5132  O   SER A 672     119.094  12.933   5.285  1.00 35.60           O  
ANISOU 5132  O   SER A 672     5150   4334   4043    181    285    204       O  
ATOM   5133  CB  SER A 672     119.709  12.928   2.075  1.00 58.11           C  
ANISOU 5133  CB  SER A 672     8038   7243   6798    144    296    241       C  
ATOM   5134  OG  SER A 672     120.798  12.535   1.249  1.00 56.26           O  
ANISOU 5134  OG  SER A 672     7813   7029   6534    133    312    241       O  
ATOM   5135  N   LEU A 673     117.271  12.528   4.031  1.00 40.74           N  
ANISOU 5135  N   LEU A 673     5813   5007   4658    170    260    223       N  
ATOM   5136  CA  LEU A 673     116.370  13.168   4.977  1.00 35.87           C  
ANISOU 5136  CA  LEU A 673     5180   4381   4066    177    253    223       C  
ATOM   5137  C   LEU A 673     115.187  12.261   5.258  1.00 34.34           C  
ANISOU 5137  C   LEU A 673     4981   4189   3879    179    232    218       C  
ATOM   5138  O   LEU A 673     114.390  11.974   4.371  1.00 34.47           O  
ANISOU 5138  O   LEU A 673     5005   4220   3870    169    218    232       O  
ATOM   5139  CB  LEU A 673     115.876  14.505   4.418  1.00 26.99           C  
ANISOU 5139  CB  LEU A 673     4059   3271   2925    169    253    249       C  
ATOM   5140  CG  LEU A 673     114.924  15.306   5.302  1.00 39.04           C  
ANISOU 5140  CG  LEU A 673     5569   4791   4473    177    248    253       C  
ATOM   5141  CD1 LEU A 673     115.511  15.467   6.704  1.00 25.53           C  
ANISOU 5141  CD1 LEU A 673     3844   3060   2797    191    260    230       C  
ATOM   5142  CD2 LEU A 673     114.621  16.678   4.665  1.00 46.36           C  
ANISOU 5142  CD2 LEU A 673     6503   5730   5381    169    251    282       C  
ATOM   5143  N   LEU A 674     115.055  11.831   6.502  1.00 33.59           N  
ANISOU 5143  N   LEU A 674     4869   4078   3814    190    229    199       N  
ATOM   5144  CA  LEU A 674     113.988  10.899   6.844  1.00 31.04           C  
ANISOU 5144  CA  LEU A 674     4539   3757   3496    188    210    194       C  
ATOM   5145  C   LEU A 674     113.006  11.537   7.806  1.00 33.83           C  
ANISOU 5145  C   LEU A 674     4872   4114   3869    191    204    197       C  
ATOM   5146  O   LEU A 674     113.419  12.193   8.758  1.00 34.19           O  
ANISOU 5146  O   LEU A 674     4905   4150   3936    200    216    189       O  
ATOM   5147  CB  LEU A 674     114.579   9.642   7.480  1.00 24.14           C  
ANISOU 5147  CB  LEU A 674     3665   2868   2638    193    209    171       C  
ATOM   5148  CG  LEU A 674     115.763   9.025   6.741  1.00 36.59           C  
ANISOU 5148  CG  LEU A 674     5262   4439   4201    194    219    166       C  
ATOM   5149  CD1 LEU A 674     116.285   7.788   7.478  1.00 36.43           C  
ANISOU 5149  CD1 LEU A 674     5242   4402   4199    202    216    146       C  
ATOM   5150  CD2 LEU A 674     115.353   8.674   5.320  1.00 23.82           C  
ANISOU 5150  CD2 LEU A 674     3666   2838   2548    183    210    180       C  
ATOM   5151  N   MET A 675     111.717  11.328   7.567  1.00 23.92           N  
ANISOU 5151  N   MET A 675     3611   2873   2604    184    186    210       N  
ATOM   5152  CA  MET A 675     110.686  11.876   8.432  1.00 31.61           C  
ANISOU 5152  CA  MET A 675     4564   3854   3593    186    180    217       C  
ATOM   5153  C   MET A 675     109.886  10.745   9.042  1.00 29.82           C  
ANISOU 5153  C   MET A 675     4324   3632   3375    179    163    210       C  
ATOM   5154  O   MET A 675     109.456   9.836   8.340  1.00 33.29           O  
ANISOU 5154  O   MET A 675     4774   4078   3798    168    147    216       O  
ATOM   5155  CB  MET A 675     109.732  12.816   7.666  1.00 21.55           C  
ANISOU 5155  CB  MET A 675     3290   2598   2301    181    173    246       C  
ATOM   5156  CG  MET A 675     108.522  13.265   8.501  1.00 17.49           C  
ANISOU 5156  CG  MET A 675     2752   2093   1800    183    165    256       C  
ATOM   5157  SD  MET A 675     107.357  14.402   7.671  1.00 32.31           S  
ANISOU 5157  SD  MET A 675     4629   3989   3657    179    155    295       S  
ATOM   5158  CE  MET A 675     106.394  13.214   6.733  1.00 51.48           C  
ANISOU 5158  CE  MET A 675     7060   6439   6062    160    126    311       C  
ATOM   5159  N   GLN A 676     109.672  10.824  10.347  1.00 27.28           N  
ANISOU 5159  N   GLN A 676     3982   3308   3077    183    165    201       N  
ATOM   5160  CA  GLN A 676     108.807   9.890  11.032  1.00 26.39           C  
ANISOU 5160  CA  GLN A 676     3854   3203   2971    172    147    200       C  
ATOM   5161  C   GLN A 676     107.821  10.615  11.921  1.00 29.01           C  
ANISOU 5161  C   GLN A 676     4161   3548   3315    173    145    211       C  
ATOM   5162  O   GLN A 676     107.854  11.844  12.006  1.00 38.86           O  
ANISOU 5162  O   GLN A 676     5405   4795   4566    184    159    217       O  
ATOM   5163  CB  GLN A 676     109.634   8.901  11.856  1.00 26.89           C  
ANISOU 5163  CB  GLN A 676     3916   3252   3050    172    149    177       C  
ATOM   5164  CG  GLN A 676     109.867   7.585  11.160  1.00 17.23           C  
ANISOU 5164  CG  GLN A 676     2713   2023   1813    164    137    171       C  
ATOM   5165  CD  GLN A 676     108.591   6.794  10.953  1.00 28.89           C  
ANISOU 5165  CD  GLN A 676     4184   3514   3278    146    113    185       C  
ATOM   5166  OE1 GLN A 676     107.546   7.095  11.543  1.00 22.47           O  
ANISOU 5166  OE1 GLN A 676     3349   2718   2472    139    104    199       O  
ATOM   5167  NE2 GLN A 676     108.666   5.781  10.103  1.00 29.99           N  
ANISOU 5167  NE2 GLN A 676     4345   3648   3400    139    102    183       N  
ATOM   5168  N   SER A 677     106.940   9.867  12.582  1.00 30.08           N  
ANISOU 5168  N   SER A 677     4279   3695   3456    160    129    216       N  
ATOM   5169  CA  SER A 677     106.040  10.475  13.543  1.00 33.89           C  
ANISOU 5169  CA  SER A 677     4737   4191   3951    160    128    226       C  
ATOM   5170  C   SER A 677     106.501  10.187  14.967  1.00 32.60           C  
ANISOU 5170  C   SER A 677     4558   4021   3808    160    133    209       C  
ATOM   5171  O   SER A 677     107.012   9.105  15.252  1.00 32.76           O  
ANISOU 5171  O   SER A 677     4581   4035   3831    151    127    196       O  
ATOM   5172  CB  SER A 677     104.606  10.005  13.320  1.00 26.59           C  
ANISOU 5172  CB  SER A 677     3798   3288   3015    143    104    251       C  
ATOM   5173  OG  SER A 677     104.501   8.609  13.539  1.00 50.11           O  
ANISOU 5173  OG  SER A 677     6776   6271   5994    126     87    246       O  
ATOM   5174  N   VAL A 678     106.333  11.172  15.847  1.00 26.32           N  
ANISOU 5174  N   VAL A 678     3747   3227   3025    170    146    209       N  
ATOM   5175  CA  VAL A 678     106.647  11.026  17.261  1.00 23.60           C  
ANISOU 5175  CA  VAL A 678     3387   2882   2699    168    150    197       C  
ATOM   5176  C   VAL A 678     105.474  11.504  18.115  1.00 29.40           C  
ANISOU 5176  C   VAL A 678     4098   3634   3439    165    146    212       C  
ATOM   5177  O   VAL A 678     104.493  12.032  17.599  1.00 18.16           O  
ANISOU 5177  O   VAL A 678     2671   2223   2007    167    142    231       O  
ATOM   5178  CB  VAL A 678     107.931  11.795  17.670  1.00 28.75           C  
ANISOU 5178  CB  VAL A 678     4048   3515   3363    184    172    178       C  
ATOM   5179  CG1 VAL A 678     109.140  11.244  16.936  1.00 32.27           C  
ANISOU 5179  CG1 VAL A 678     4514   3943   3803    187    176    163       C  
ATOM   5180  CG2 VAL A 678     107.779  13.294  17.410  1.00 24.18           C  
ANISOU 5180  CG2 VAL A 678     3472   2932   2782    202    189    184       C  
ATOM   5181  N   ASN A 679     105.587  11.319  19.424  1.00 19.32           N  
ANISOU 5181  N   ASN A 679     2805   2360   2175    158    146    206       N  
ATOM   5182  CA  ASN A 679     104.484  11.577  20.334  1.00 22.53           C  
ANISOU 5182  CA  ASN A 679     3189   2786   2586    152    141    221       C  
ATOM   5183  C   ASN A 679     104.863  12.611  21.391  1.00 37.61           C  
ANISOU 5183  C   ASN A 679     5093   4689   4509    167    161    211       C  
ATOM   5184  O   ASN A 679     105.592  12.305  22.331  1.00 39.24           O  
ANISOU 5184  O   ASN A 679     5294   4890   4724    160    162    199       O  
ATOM   5185  CB  ASN A 679     104.038  10.285  21.034  1.00 32.67           C  
ANISOU 5185  CB  ASN A 679     4457   4086   3869    122    118    229       C  
ATOM   5186  CG  ASN A 679     103.636   9.197  20.065  1.00 35.30           C  
ANISOU 5186  CG  ASN A 679     4797   4427   4190    106     97    240       C  
ATOM   5187  OD1 ASN A 679     102.937   9.446  19.090  1.00 25.30           O  
ANISOU 5187  OD1 ASN A 679     3535   3166   2912    108     93    254       O  
ATOM   5188  ND2 ASN A 679     104.073   7.978  20.334  1.00 56.52           N  
ANISOU 5188  ND2 ASN A 679     7485   7113   6878     88     84    235       N  
ATOM   5189  N   LEU A 680     104.369  13.837  21.239  1.00 26.48           N  
ANISOU 5189  N   LEU A 680     3684   3278   3099    187    176    218       N  
ATOM   5190  CA  LEU A 680     104.538  14.850  22.276  1.00 28.25           C  
ANISOU 5190  CA  LEU A 680     3903   3496   3335    202    194    212       C  
ATOM   5191  C   LEU A 680     103.527  14.623  23.408  1.00 34.25           C  
ANISOU 5191  C   LEU A 680     4638   4276   4097    189    185    225       C  
ATOM   5192  O   LEU A 680     103.910  14.302  24.532  1.00 38.76           O  
ANISOU 5192  O   LEU A 680     5201   4850   4676    177    183    217       O  
ATOM   5193  CB  LEU A 680     104.392  16.260  21.682  1.00 30.29           C  
ANISOU 5193  CB  LEU A 680     4173   3744   3592    228    214    216       C  
ATOM   5194  CG  LEU A 680     104.594  17.444  22.621  1.00 22.84           C  
ANISOU 5194  CG  LEU A 680     3230   2789   2659    246    236    210       C  
ATOM   5195  CD1 LEU A 680     105.758  17.206  23.573  1.00 42.95           C  
ANISOU 5195  CD1 LEU A 680     5780   5324   5217    238    239    189       C  
ATOM   5196  CD2 LEU A 680     104.876  18.654  21.791  1.00 30.58           C  
ANISOU 5196  CD2 LEU A 680     4231   3753   3636    268    255    211       C  
ATOM   5197  N   SER A 681     102.243  14.796  23.114  1.00 40.31           N  
ANISOU 5197  N   SER A 681     5396   5062   4859    191    180    246       N  
ATOM   5198  CA  SER A 681     101.201  14.542  24.100  1.00 58.29           C  
ANISOU 5198  CA  SER A 681     7651   7362   7136    177    171    260       C  
ATOM   5199  C   SER A 681     100.275  13.438  23.606  1.00 60.14           C  
ANISOU 5199  C   SER A 681     7876   7617   7358    151    144    279       C  
ATOM   5200  O   SER A 681     100.071  12.425  24.276  1.00 46.91           O  
ANISOU 5200  O   SER A 681     6190   5955   5680    121    125    283       O  
ATOM   5201  CB  SER A 681     100.399  15.813  24.379  1.00 65.59           C  
ANISOU 5201  CB  SER A 681     8568   8289   8063    204    190    271       C  
ATOM   5202  OG  SER A 681      99.216  15.501  25.102  1.00 80.96           O  
ANISOU 5202  OG  SER A 681    10493  10261  10006    191    180    288       O  
ATOM   5203  N   TYR A 682      99.719  13.647  22.420  1.00 44.64           N  
ANISOU 5203  N   TYR A 682     5921   5655   5386    159    140    291       N  
ATOM   5204  CA  TYR A 682      98.869  12.654  21.778  1.00 33.09           C  
ANISOU 5204  CA  TYR A 682     4455   4209   3910    133    113    310       C  
ATOM   5205  C   TYR A 682      99.725  11.715  20.928  1.00 43.71           C  
ANISOU 5205  C   TYR A 682     5816   5543   5249    119    100    301       C  
ATOM   5206  O   TYR A 682     100.936  11.878  20.832  1.00 44.74           O  
ANISOU 5206  O   TYR A 682     5959   5653   5386    131    114    279       O  
ATOM   5207  CB  TYR A 682      97.839  13.340  20.878  1.00 27.71           C  
ANISOU 5207  CB  TYR A 682     3775   3535   3220    147    112    331       C  
ATOM   5208  CG  TYR A 682      96.947  14.344  21.590  1.00 57.07           C  
ANISOU 5208  CG  TYR A 682     7477   7264   6943    169    128    342       C  
ATOM   5209  CD1 TYR A 682      95.681  13.985  22.023  1.00 65.13           C  
ANISOU 5209  CD1 TYR A 682     8481   8308   7958    156    115    362       C  
ATOM   5210  CD2 TYR A 682      97.372  15.651  21.818  1.00 59.72           C  
ANISOU 5210  CD2 TYR A 682     7816   7586   7289    203    157    334       C  
ATOM   5211  CE1 TYR A 682      94.869  14.886  22.669  1.00 86.92           C  
ANISOU 5211  CE1 TYR A 682    11223  11081  10723    180    132    373       C  
ATOM   5212  CE2 TYR A 682      96.563  16.557  22.466  1.00 68.42           C  
ANISOU 5212  CE2 TYR A 682     8904   8697   8396    225    173    345       C  
ATOM   5213  CZ  TYR A 682      95.307  16.168  22.888  1.00 91.08           C  
ANISOU 5213  CZ  TYR A 682    11752  11593  11261    215    161    365       C  
ATOM   5214  OH  TYR A 682      94.481  17.061  23.537  1.00 98.95           O  
ANISOU 5214  OH  TYR A 682    12732  12602  12263    240    178    377       O  
ATOM   5215  N   GLN A 683      99.093  10.741  20.290  1.00 39.90           N  
ANISOU 5215  N   GLN A 683     5334   5072   4753     93     74    317       N  
ATOM   5216  CA  GLN A 683      99.811   9.879  19.374  1.00 33.96           C  
ANISOU 5216  CA  GLN A 683     4596   4311   3995     84     64    310       C  
ATOM   5217  C   GLN A 683     100.014  10.577  18.037  1.00 25.33           C  
ANISOU 5217  C   GLN A 683     3523   3207   2894    105     73    311       C  
ATOM   5218  O   GLN A 683      99.065  11.058  17.429  1.00 28.98           O  
ANISOU 5218  O   GLN A 683     3984   3680   3347    107     66    332       O  
ATOM   5219  CB  GLN A 683      99.073   8.545  19.162  1.00 29.78           C  
ANISOU 5219  CB  GLN A 683     4060   3800   3455     49     32    330       C  
ATOM   5220  CG  GLN A 683      98.994   7.663  20.395  1.00 32.76           C  
ANISOU 5220  CG  GLN A 683     4420   4189   3838     22     20    333       C  
ATOM   5221  CD  GLN A 683     100.356   7.381  21.019  1.00 34.07           C  
ANISOU 5221  CD  GLN A 683     4589   4340   4017     31     34    308       C  
ATOM   5222  OE1 GLN A 683     101.196   6.702  20.433  1.00 34.25           O  
ANISOU 5222  OE1 GLN A 683     4625   4349   4039     35     34    296       O  
ATOM   5223  NE2 GLN A 683     100.572   7.896  22.223  1.00 29.14           N  
ANISOU 5223  NE2 GLN A 683     3955   3714   3402     33     45    300       N  
ATOM   5224  N   GLU A 684     101.261  10.597  17.582  1.00 21.94           N  
ANISOU 5224  N   GLU A 684     3112   2757   2467    118     86    289       N  
ATOM   5225  CA  GLU A 684     101.624  11.106  16.262  1.00 29.62           C  
ANISOU 5225  CA  GLU A 684     4106   3719   3427    132     93    290       C  
ATOM   5226  C   GLU A 684     101.334  12.599  16.047  1.00 39.73           C  
ANISOU 5226  C   GLU A 684     5389   4998   4708    155    109    298       C  
ATOM   5227  O   GLU A 684     101.123  13.040  14.917  1.00 28.81           O  
ANISOU 5227  O   GLU A 684     4019   3616   3312    160    106    313       O  
ATOM   5228  CB  GLU A 684     100.993  10.248  15.160  1.00 24.84           C  
ANISOU 5228  CB  GLU A 684     3507   3127   2804    113     68    309       C  
ATOM   5229  CG  GLU A 684     101.313   8.750  15.328  1.00 32.45           C  
ANISOU 5229  CG  GLU A 684     4471   4091   3767     93     53    301       C  
ATOM   5230  CD  GLU A 684     100.789   7.887  14.187  1.00 45.54           C  
ANISOU 5230  CD  GLU A 684     6138   5759   5406     78     32    317       C  
ATOM   5231  OE1 GLU A 684     100.644   8.393  13.054  1.00 48.95           O  
ANISOU 5231  OE1 GLU A 684     6583   6192   5823     85     31    328       O  
ATOM   5232  OE2 GLU A 684     100.523   6.691  14.427  1.00 52.77           O  
ANISOU 5232  OE2 GLU A 684     7046   6683   6321     60     16    322       O  
ATOM   5233  N   ASP A 685     101.355  13.372  17.132  1.00 21.43           N  
ANISOU 5233  N   ASP A 685     3059   2677   2406    170    127    291       N  
ATOM   5234  CA  ASP A 685     101.125  14.808  17.047  1.00 19.74           C  
ANISOU 5234  CA  ASP A 685     2849   2459   2194    195    145    299       C  
ATOM   5235  C   ASP A 685     102.405  15.553  16.645  1.00 41.92           C  
ANISOU 5235  C   ASP A 685     5679   5245   5005    212    167    281       C  
ATOM   5236  O   ASP A 685     102.366  16.744  16.340  1.00 48.48           O  
ANISOU 5236  O   ASP A 685     6518   6068   5834    231    181    289       O  
ATOM   5237  CB  ASP A 685     100.551  15.359  18.360  1.00 34.89           C  
ANISOU 5237  CB  ASP A 685     4746   4384   4126    204    156    300       C  
ATOM   5238  CG  ASP A 685     101.441  15.075  19.561  1.00 35.53           C  
ANISOU 5238  CG  ASP A 685     4821   4455   4222    202    166    275       C  
ATOM   5239  OD1 ASP A 685     102.467  14.366  19.416  1.00 28.15           O  
ANISOU 5239  OD1 ASP A 685     3897   3509   3288    193    163    258       O  
ATOM   5240  OD2 ASP A 685     101.103  15.548  20.662  1.00 41.84           O  
ANISOU 5240  OD2 ASP A 685     5607   5260   5031    210    176    275       O  
ATOM   5241  N   GLY A 686     103.533  14.847  16.631  1.00 29.82           N  
ANISOU 5241  N   GLY A 686     4157   3700   3475    206    168    260       N  
ATOM   5242  CA  GLY A 686     104.794  15.437  16.222  1.00 30.36           C  
ANISOU 5242  CA  GLY A 686     4245   3746   3543    218    186    244       C  
ATOM   5243  C   GLY A 686     105.398  14.755  15.005  1.00 33.29           C  
ANISOU 5243  C   GLY A 686     4637   4113   3901    209    177    242       C  
ATOM   5244  O   GLY A 686     104.959  13.673  14.617  1.00 28.02           O  
ANISOU 5244  O   GLY A 686     3967   3456   3224    193    157    248       O  
ATOM   5245  N   ARG A 687     106.394  15.401  14.393  1.00 21.83           N  
ANISOU 5245  N   ARG A 687     3205   2645   2444    219    192    236       N  
ATOM   5246  CA  ARG A 687     107.195  14.789  13.335  1.00 25.90           C  
ANISOU 5246  CA  ARG A 687     3740   3153   2946    212    188    231       C  
ATOM   5247  C   ARG A 687     108.659  14.849  13.696  1.00 28.71           C  
ANISOU 5247  C   ARG A 687     4106   3489   3313    219    205    208       C  
ATOM   5248  O   ARG A 687     109.164  15.909  14.044  1.00 23.65           O  
ANISOU 5248  O   ARG A 687     3469   2839   2680    230    223    204       O  
ATOM   5249  CB  ARG A 687     106.966  15.458  11.981  1.00 15.26           C  
ANISOU 5249  CB  ARG A 687     2410   1811   1578    212    186    254       C  
ATOM   5250  CG  ARG A 687     105.540  15.322  11.427  1.00 28.69           C  
ANISOU 5250  CG  ARG A 687     4104   3533   3265    203    165    282       C  
ATOM   5251  CD  ARG A 687     105.172  13.859  11.090  1.00 26.33           C  
ANISOU 5251  CD  ARG A 687     3803   3245   2958    185    143    282       C  
ATOM   5252  NE  ARG A 687     103.789  13.732  10.636  1.00 17.72           N  
ANISOU 5252  NE  ARG A 687     2703   2176   1854    173    120    310       N  
ATOM   5253  CZ  ARG A 687     102.748  13.573  11.449  1.00 31.56           C  
ANISOU 5253  CZ  ARG A 687     4433   3943   3617    168    110    319       C  
ATOM   5254  NH1 ARG A 687     102.937  13.520  12.754  1.00 27.00           N  
ANISOU 5254  NH1 ARG A 687     3839   3359   3060    174    121    301       N  
ATOM   5255  NH2 ARG A 687     101.516  13.484  10.965  1.00 18.45           N  
ANISOU 5255  NH2 ARG A 687     2764   2302   1944    156     88    348       N  
ATOM   5256  N   GLY A 688     109.334  13.700  13.639  1.00 15.89           N  
ANISOU 5256  N   GLY A 688     2488   1861   1690    211    199    193       N  
ATOM   5257  CA  GLY A 688     110.777  13.650  13.801  1.00 23.59           C  
ANISOU 5257  CA  GLY A 688     3473   2818   2673    216    213    174       C  
ATOM   5258  C   GLY A 688     111.481  13.633  12.459  1.00 15.45           C  
ANISOU 5258  C   GLY A 688     2465   1781   1623    215    217    179       C  
ATOM   5259  O   GLY A 688     110.927  13.211  11.451  1.00 28.80           O  
ANISOU 5259  O   GLY A 688     4166   3482   3296    208    204    192       O  
ATOM   5260  N   PHE A 689     112.718  14.084  12.438  1.00 17.52           N  
ANISOU 5260  N   PHE A 689     2738   2030   1890    221    233    170       N  
ATOM   5261  CA  PHE A 689     113.436  14.256  11.183  1.00 19.34           C  
ANISOU 5261  CA  PHE A 689     2989   2257   2101    218    239    178       C  
ATOM   5262  C   PHE A 689     114.891  13.899  11.414  1.00 20.68           C  
ANISOU 5262  C   PHE A 689     3164   2412   2279    221    250    162       C  
ATOM   5263  O   PHE A 689     115.448  14.175  12.479  1.00 31.83           O  
ANISOU 5263  O   PHE A 689     4566   3816   3711    226    258    150       O  
ATOM   5264  CB  PHE A 689     113.344  15.717  10.674  1.00 26.55           C  
ANISOU 5264  CB  PHE A 689     3910   3173   3004    220    249    196       C  
ATOM   5265  CG  PHE A 689     111.948  16.147  10.302  1.00 28.27           C  
ANISOU 5265  CG  PHE A 689     4125   3406   3212    219    237    218       C  
ATOM   5266  CD1 PHE A 689     111.429  15.846   9.053  1.00 27.98           C  
ANISOU 5266  CD1 PHE A 689     4100   3383   3150    208    224    237       C  
ATOM   5267  CD2 PHE A 689     111.149  16.823  11.206  1.00 21.32           C  
ANISOU 5267  CD2 PHE A 689     3228   2527   2344    226    239    220       C  
ATOM   5268  CE1 PHE A 689     110.151  16.216   8.716  1.00 22.95           C  
ANISOU 5268  CE1 PHE A 689     3457   2760   2501    205    211    260       C  
ATOM   5269  CE2 PHE A 689     109.862  17.190  10.869  1.00 19.51           C  
ANISOU 5269  CE2 PHE A 689     2994   2313   2106    225    228    242       C  
ATOM   5270  CZ  PHE A 689     109.367  16.880   9.623  1.00 20.11           C  
ANISOU 5270  CZ  PHE A 689     3080   2402   2157    214    213    263       C  
ATOM   5271  N   ASN A 690     115.520  13.323  10.400  1.00 25.50           N  
ANISOU 5271  N   ASN A 690     3791   3022   2873    216    250    165       N  
ATOM   5272  CA  ASN A 690     116.930  12.944  10.483  1.00 28.77           C  
ANISOU 5272  CA  ASN A 690     4212   3426   3294    218    261    154       C  
ATOM   5273  C   ASN A 690     117.657  13.321   9.228  1.00 39.19           C  
ANISOU 5273  C   ASN A 690     5550   4750   4590    212    271    167       C  
ATOM   5274  O   ASN A 690     117.292  12.871   8.126  1.00 28.72           O  
ANISOU 5274  O   ASN A 690     4238   3435   3240    205    264    177       O  
ATOM   5275  CB  ASN A 690     117.097  11.434  10.675  1.00 32.66           C  
ANISOU 5275  CB  ASN A 690     4705   3914   3791    219    252    140       C  
ATOM   5276  CG  ASN A 690     117.076  11.025  12.127  1.00 68.76           C  
ANISOU 5276  CG  ASN A 690     9257   8480   8388    223    247    125       C  
ATOM   5277  OD1 ASN A 690     117.387  11.823  13.006  1.00 96.63           O  
ANISOU 5277  OD1 ASN A 690    12774  12007  11933    226    256    122       O  
ATOM   5278  ND2 ASN A 690     116.719   9.773  12.390  1.00104.11           N  
ANISOU 5278  ND2 ASN A 690    13733  12958  12868    220    234    117       N  
ATOM   5279  N   TRP A 691     118.701  14.124   9.410  1.00 23.82           N  
ANISOU 5279  N   TRP A 691     3604   2799   2648    212    287    168       N  
ATOM   5280  CA  TRP A 691     119.543  14.570   8.320  1.00 29.59           C  
ANISOU 5280  CA  TRP A 691     4350   3537   3355    202    299    182       C  
ATOM   5281  C   TRP A 691     120.770  13.712   8.381  1.00 35.63           C  
ANISOU 5281  C   TRP A 691     5116   4298   4124    203    306    172       C  
ATOM   5282  O   TRP A 691     121.485  13.741   9.380  1.00 32.78           O  
ANISOU 5282  O   TRP A 691     4743   3927   3786    208    312    161       O  
ATOM   5283  CB  TRP A 691     119.964  16.038   8.509  1.00 27.40           C  
ANISOU 5283  CB  TRP A 691     4073   3259   3080    197    313    192       C  
ATOM   5284  CG  TRP A 691     118.927  17.053   8.119  1.00 32.35           C  
ANISOU 5284  CG  TRP A 691     4704   3893   3695    194    309    209       C  
ATOM   5285  CD1 TRP A 691     118.876  17.762   6.954  1.00 34.60           C  
ANISOU 5285  CD1 TRP A 691     5005   4193   3951    180    312    234       C  
ATOM   5286  CD2 TRP A 691     117.815  17.493   8.902  1.00 27.22           C  
ANISOU 5286  CD2 TRP A 691     4044   3239   3060    203    302    207       C  
ATOM   5287  NE1 TRP A 691     117.782  18.597   6.954  1.00 29.01           N  
ANISOU 5287  NE1 TRP A 691     4296   3487   3240    182    305    248       N  
ATOM   5288  CE2 TRP A 691     117.118  18.451   8.141  1.00 31.98           C  
ANISOU 5288  CE2 TRP A 691     4656   3851   3643    197    300    231       C  
ATOM   5289  CE3 TRP A 691     117.329  17.160  10.165  1.00 27.11           C  
ANISOU 5289  CE3 TRP A 691     4012   3216   3072    215    297    190       C  
ATOM   5290  CZ2 TRP A 691     115.974  19.074   8.603  1.00 37.02           C  
ANISOU 5290  CZ2 TRP A 691     5286   4490   4289    204    294    238       C  
ATOM   5291  CZ3 TRP A 691     116.182  17.779  10.613  1.00 31.41           C  
ANISOU 5291  CZ3 TRP A 691     4548   3763   3622    220    292    195       C  
ATOM   5292  CH2 TRP A 691     115.527  18.730   9.842  1.00 26.03           C  
ANISOU 5292  CH2 TRP A 691     3877   3091   2923    217    291    219       C  
ATOM   5293  N   ARG A 692     121.024  12.952   7.321  1.00 37.69           N  
ANISOU 5293  N   ARG A 692     5390   4569   4361    197    306    177       N  
ATOM   5294  CA  ARG A 692     122.219  12.120   7.265  1.00 39.17           C  
ANISOU 5294  CA  ARG A 692     5580   4756   4548    199    314    170       C  
ATOM   5295  C   ARG A 692     123.180  12.714   6.258  1.00 42.26           C  
ANISOU 5295  C   ARG A 692     5980   5166   4910    184    332    185       C  
ATOM   5296  O   ARG A 692     124.395  12.568   6.380  1.00 58.03           O  
ANISOU 5296  O   ARG A 692     7973   7168   6909    183    345    182       O  
ATOM   5297  CB  ARG A 692     121.857  10.688   6.890  1.00 53.44           C  
ANISOU 5297  CB  ARG A 692     7396   6561   6347    205    303    162       C  
ATOM   5298  CG  ARG A 692     120.680  10.156   7.672  0.50 46.86           C  
ANISOU 5298  CG  ARG A 692     6555   5715   5533    213    284    151       C  
ATOM   5299  CD  ARG A 692     120.579   8.659   7.495  0.50 60.67           C  
ANISOU 5299  CD  ARG A 692     8314   7459   7278    218    274    141       C  
ATOM   5300  NE  ARG A 692     119.572   8.079   8.366  0.50 73.64           N  
ANISOU 5300  NE  ARG A 692     9947   9092   8939    221    257    130       N  
ATOM   5301  CZ  ARG A 692     119.627   6.823   8.808  0.50 87.46           C  
ANISOU 5301  CZ  ARG A 692    11700  10832  10699    227    248    118       C  
ATOM   5302  NH1 ARG A 692     120.652   6.024   8.478  0.50 91.47           N  
ANISOU 5302  NH1 ARG A 692    12219  11334  11200    234    255    114       N  
ATOM   5303  NH2 ARG A 692     118.665   6.348   9.593  0.50 80.34           N  
ANISOU 5303  NH2 ARG A 692    10789   9927   9809    225    232    110       N  
ATOM   5304  N   ALA A 693     122.630  13.393   5.261  1.00 42.76           N  
ANISOU 5304  N   ALA A 693     6055   5247   4946    171    332    201       N  
ATOM   5305  CA  ALA A 693     123.439  14.132   4.302  1.00 37.68           C  
ANISOU 5305  CA  ALA A 693     5419   4627   4270    152    348    219       C  
ATOM   5306  C   ALA A 693     122.796  15.490   4.069  1.00 35.53           C  
ANISOU 5306  C   ALA A 693     5151   4360   3990    142    347    237       C  
ATOM   5307  O   ALA A 693     121.723  15.766   4.595  1.00 49.09           O  
ANISOU 5307  O   ALA A 693     6864   6063   5725    152    334    236       O  
ATOM   5308  CB  ALA A 693     123.549  13.370   3.005  1.00 32.45           C  
ANISOU 5308  CB  ALA A 693     4770   3991   3568    142    351    224       C  
ATOM   5309  N   GLN A 694     123.458  16.330   3.285  1.00 39.38           N  
ANISOU 5309  N   GLN A 694     5644   4870   4448    122    362    256       N  
ATOM   5310  CA  GLN A 694     122.946  17.653   2.966  1.00 37.41           C  
ANISOU 5310  CA  GLN A 694     5402   4626   4187    110    361    279       C  
ATOM   5311  C   GLN A 694     121.500  17.599   2.472  1.00 38.73           C  
ANISOU 5311  C   GLN A 694     5576   4796   4344    113    342    290       C  
ATOM   5312  O   GLN A 694     121.205  16.942   1.478  1.00 51.81           O  
ANISOU 5312  O   GLN A 694     7241   6473   5969    105    336    297       O  
ATOM   5313  CB  GLN A 694     123.835  18.302   1.914  1.00 39.81           C  
ANISOU 5313  CB  GLN A 694     5713   4962   4451     84    378    301       C  
ATOM   5314  CG  GLN A 694     123.464  19.732   1.603  1.00 44.46           C  
ANISOU 5314  CG  GLN A 694     6310   5556   5027     69    378    329       C  
ATOM   5315  CD  GLN A 694     123.599  20.621   2.806  1.00 47.90           C  
ANISOU 5315  CD  GLN A 694     6738   5963   5499     78    382    322       C  
ATOM   5316  OE1 GLN A 694     124.601  20.562   3.516  1.00 50.48           O  
ANISOU 5316  OE1 GLN A 694     7055   6281   5843     79    394    307       O  
ATOM   5317  NE2 GLN A 694     122.587  21.447   3.053  1.00 45.25           N  
ANISOU 5317  NE2 GLN A 694     6407   5614   5173     84    372    333       N  
ATOM   5318  N   ALA A 695     120.602  18.276   3.183  1.00 33.25           N  
ANISOU 5318  N   ALA A 695     4877   4085   3673    124    333    292       N  
ATOM   5319  CA  ALA A 695     119.204  18.320   2.781  1.00 33.18           C  
ANISOU 5319  CA  ALA A 695     4872   4082   3654    126    314    305       C  
ATOM   5320  C   ALA A 695     118.439  19.420   3.487  1.00 35.21           C  
ANISOU 5320  C   ALA A 695     5123   4324   3930    134    310    313       C  
ATOM   5321  O   ALA A 695     118.873  19.941   4.510  1.00 34.08           O  
ANISOU 5321  O   ALA A 695     4972   4162   3815    142    320    300       O  
ATOM   5322  CB  ALA A 695     118.528  16.971   3.036  1.00 30.98           C  
ANISOU 5322  CB  ALA A 695     4587   3796   3387    139    299    286       C  
ATOM   5323  N   ALA A 696     117.288  19.766   2.934  1.00 24.76           N  
ANISOU 5323  N   ALA A 696     3803   3011   2592    130    295    336       N  
ATOM   5324  CA  ALA A 696     116.468  20.788   3.522  1.00 32.34           C  
ANISOU 5324  CA  ALA A 696     4760   3961   3568    139    291    347       C  
ATOM   5325  C   ALA A 696     115.064  20.255   3.710  1.00 19.98           C  
ANISOU 5325  C   ALA A 696     3183   2397   2009    149    272    346       C  
ATOM   5326  O   ALA A 696     114.449  19.717   2.789  1.00 23.35           O  
ANISOU 5326  O   ALA A 696     3616   2844   2412    140    256    361       O  
ATOM   5327  CB  ALA A 696     116.453  22.039   2.632  1.00 25.89           C  
ANISOU 5327  CB  ALA A 696     3956   3156   2723    121    293    386       C  
ATOM   5328  N   LEU A 697     114.567  20.425   4.923  1.00 24.31           N  
ANISOU 5328  N   LEU A 697     3718   2930   2590    167    272    329       N  
ATOM   5329  CA  LEU A 697     113.170  20.201   5.246  1.00 31.21           C  
ANISOU 5329  CA  LEU A 697     4579   3807   3472    176    255    333       C  
ATOM   5330  C   LEU A 697     112.414  21.513   5.209  1.00 21.70           C  
ANISOU 5330  C   LEU A 697     3376   2603   2264    178    253    361       C  
ATOM   5331  O   LEU A 697     112.922  22.517   5.689  1.00 37.72           O  
ANISOU 5331  O   LEU A 697     5410   4619   4304    181    268    361       O  
ATOM   5332  CB  LEU A 697     113.050  19.616   6.654  1.00 25.86           C  
ANISOU 5332  CB  LEU A 697     3882   3114   2828    193    259    300       C  
ATOM   5333  CG  LEU A 697     111.627  19.646   7.200  1.00 32.55           C  
ANISOU 5333  CG  LEU A 697     4714   3968   3687    202    245    306       C  
ATOM   5334  CD1 LEU A 697     110.748  18.684   6.419  1.00 27.63           C  
ANISOU 5334  CD1 LEU A 697     4090   3363   3045    193    223    318       C  
ATOM   5335  CD2 LEU A 697     111.626  19.333   8.663  1.00 30.89           C  
ANISOU 5335  CD2 LEU A 697     4485   3744   3507    216    252    277       C  
ATOM   5336  N   SER A 698     111.201  21.518   4.670  1.00 22.24           N  
ANISOU 5336  N   SER A 698     3443   2687   2320    174    233    387       N  
ATOM   5337  CA  SER A 698     110.390  22.718   4.808  1.00 37.19           C  
ANISOU 5337  CA  SER A 698     5336   4577   4216    179    230    413       C  
ATOM   5338  C   SER A 698     108.936  22.398   5.110  1.00 36.00           C  
ANISOU 5338  C   SER A 698     5168   4436   4073    187    211    421       C  
ATOM   5339  O   SER A 698     108.404  21.390   4.646  1.00 36.86           O  
ANISOU 5339  O   SER A 698     5273   4561   4171    180    194    423       O  
ATOM   5340  CB  SER A 698     110.547  23.651   3.585  1.00 26.74           C  
ANISOU 5340  CB  SER A 698     4033   3264   2863    161    225    456       C  
ATOM   5341  OG  SER A 698     110.309  22.980   2.363  1.00 55.27           O  
ANISOU 5341  OG  SER A 698     7653   6902   6445    143    207    476       O  
ATOM   5342  N   LEU A 699     108.320  23.233   5.934  1.00 27.89           N  
ANISOU 5342  N   LEU A 699     4132   3398   3065    202    216    425       N  
ATOM   5343  CA  LEU A 699     106.878  23.235   6.062  1.00 30.78           C  
ANISOU 5343  CA  LEU A 699     4484   3775   3434    208    198    444       C  
ATOM   5344  C   LEU A 699     106.395  24.313   5.092  1.00 37.12           C  
ANISOU 5344  C   LEU A 699     5303   4583   4219    200    184    493       C  
ATOM   5345  O   LEU A 699     106.697  25.491   5.269  1.00 28.28           O  
ANISOU 5345  O   LEU A 699     4194   3447   3105    205    196    505       O  
ATOM   5346  CB  LEU A 699     106.488  23.546   7.502  1.00 29.00           C  
ANISOU 5346  CB  LEU A 699     4242   3538   3239    230    212    424       C  
ATOM   5347  CG  LEU A 699     104.999  23.650   7.817  1.00 34.34           C  
ANISOU 5347  CG  LEU A 699     4901   4224   3922    238    197    443       C  
ATOM   5348  CD1 LEU A 699     104.300  22.439   7.301  1.00 23.21           C  
ANISOU 5348  CD1 LEU A 699     3482   2836   2501    225    172    448       C  
ATOM   5349  CD2 LEU A 699     104.764  23.823   9.317  1.00 27.42           C  
ANISOU 5349  CD2 LEU A 699     4006   3338   3073    258    215    417       C  
ATOM   5350  N   SER A 700     105.690  23.890   4.047  1.00 42.44           N  
ANISOU 5350  N   SER A 700     5979   5278   4870    184    157    523       N  
ATOM   5351  CA  SER A 700     105.415  24.739   2.895  1.00 50.24           C  
ANISOU 5351  CA  SER A 700     6984   6273   5833    169    140    574       C  
ATOM   5352  C   SER A 700     103.939  24.899   2.566  1.00 49.69           C  
ANISOU 5352  C   SER A 700     6905   6215   5759    168    109    612       C  
ATOM   5353  O   SER A 700     103.129  24.013   2.817  1.00 37.25           O  
ANISOU 5353  O   SER A 700     5313   4653   4189    170     96    603       O  
ATOM   5354  CB  SER A 700     106.123  24.176   1.667  1.00 34.89           C  
ANISOU 5354  CB  SER A 700     5054   4348   3855    145    134    583       C  
ATOM   5355  OG  SER A 700     107.494  23.962   1.928  1.00 43.07           O  
ANISOU 5355  OG  SER A 700     6096   5373   4894    146    160    549       O  
ATOM   5356  N   TYR A 701     103.606  26.038   1.974  1.00 45.42           N  
ANISOU 5356  N   TYR A 701     6379   5670   5211    163     95    659       N  
ATOM   5357  CA  TYR A 701     102.279  26.258   1.425  1.00 40.61           C  
ANISOU 5357  CA  TYR A 701     5766   5071   4594    158     60    704       C  
ATOM   5358  C   TYR A 701     102.199  25.540   0.070  1.00 37.22           C  
ANISOU 5358  C   TYR A 701     5343   4673   4127    129     34    731       C  
ATOM   5359  O   TYR A 701     103.160  25.548  -0.698  1.00 37.09           O  
ANISOU 5359  O   TYR A 701     5341   4666   4086    113     42    736       O  
ATOM   5360  CB  TYR A 701     102.005  27.773   1.285  1.00 35.13           C  
ANISOU 5360  CB  TYR A 701     5086   4355   3906    164     51    748       C  
ATOM   5361  CG  TYR A 701     101.969  28.533   2.602  1.00 24.73           C  
ANISOU 5361  CG  TYR A 701     3763   3009   2625    194     76    726       C  
ATOM   5362  CD1 TYR A 701     100.782  28.679   3.307  1.00 25.74           C  
ANISOU 5362  CD1 TYR A 701     3875   3130   2774    215     67    730       C  
ATOM   5363  CD2 TYR A 701     103.120  29.093   3.142  1.00 33.98           C  
ANISOU 5363  CD2 TYR A 701     4944   4161   3806    200    109    701       C  
ATOM   5364  CE1 TYR A 701     100.736  29.359   4.509  1.00 35.42           C  
ANISOU 5364  CE1 TYR A 701     5094   4334   4030    243     92    710       C  
ATOM   5365  CE2 TYR A 701     103.083  29.779   4.353  1.00 33.85           C  
ANISOU 5365  CE2 TYR A 701     4922   4120   3820    226    133    680       C  
ATOM   5366  CZ  TYR A 701     101.885  29.912   5.026  1.00 42.15           C  
ANISOU 5366  CZ  TYR A 701     5957   5168   4891    248    125    685       C  
ATOM   5367  OH  TYR A 701     101.829  30.590   6.222  1.00 41.29           O  
ANISOU 5367  OH  TYR A 701     5841   5037   4808    273    150    666       O  
ATOM   5368  N   LEU A 702     101.067  24.905  -0.217  1.00 45.27           N  
ANISOU 5368  N   LEU A 702     6351   5711   5139    122      4    748       N  
ATOM   5369  CA  LEU A 702     100.861  24.285  -1.524  1.00 51.20           C  
ANISOU 5369  CA  LEU A 702     7105   6496   5851     94    -22    779       C  
ATOM   5370  C   LEU A 702     100.800  25.358  -2.612  1.00 58.59           C  
ANISOU 5370  C   LEU A 702     8059   7437   6764     78    -44    840       C  
ATOM   5371  O   LEU A 702     101.313  25.178  -3.714  1.00 57.10           O  
ANISOU 5371  O   LEU A 702     7879   7276   6540     56    -48    863       O  
ATOM   5372  CB  LEU A 702      99.581  23.442  -1.537  1.00 47.39           C  
ANISOU 5372  CB  LEU A 702     6607   6032   5368     89    -53    787       C  
ATOM   5373  CG  LEU A 702      99.681  21.952  -1.169  1.00 61.73           C  
ANISOU 5373  CG  LEU A 702     8407   7862   7184     87    -43    743       C  
ATOM   5374  CD1 LEU A 702     100.837  21.291  -1.910  1.00 52.68           C  
ANISOU 5374  CD1 LEU A 702     7271   6733   6011     76    -26    727       C  
ATOM   5375  CD2 LEU A 702      99.814  21.754   0.323  1.00 59.04           C  
ANISOU 5375  CD2 LEU A 702     8053   7497   6882    112    -17    694       C  
ATOM   5376  N   GLU A 703     100.172  26.481  -2.288  1.00 57.68           N  
ANISOU 5376  N   GLU A 703     7950   7296   6670     89    -58    869       N  
ATOM   5377  CA  GLU A 703     100.156  27.647  -3.169  1.00 60.10           C  
ANISOU 5377  CA  GLU A 703     8276   7598   6962     75    -79    930       C  
ATOM   5378  C   GLU A 703     100.694  28.868  -2.416  1.00 57.47           C  
ANISOU 5378  C   GLU A 703     7954   7225   6658     95    -56    924       C  
ATOM   5379  O   GLU A 703     100.115  29.277  -1.400  1.00 59.32           O  
ANISOU 5379  O   GLU A 703     8181   7431   6926    123    -51    910       O  
ATOM   5380  CB  GLU A 703      98.735  27.917  -3.669  0.50 54.48           C  
ANISOU 5380  CB  GLU A 703     7564   6887   6250     70   -127    974       C  
ATOM   5381  CG  GLU A 703      98.124  26.759  -4.434  0.50 61.70           C  
ANISOU 5381  CG  GLU A 703     8464   7840   7141     52   -149    972       C  
ATOM   5382  CD  GLU A 703      96.696  27.026  -4.855  0.50 70.72           C  
ANISOU 5382  CD  GLU A 703     9611   8974   8284     47   -199   1006       C  
ATOM   5383  OE1 GLU A 703      96.021  27.843  -4.193  0.50 69.96           O  
ANISOU 5383  OE1 GLU A 703     9528   8839   8216     70   -212   1016       O  
ATOM   5384  OE2 GLU A 703      96.253  26.422  -5.854  0.50 68.65           O  
ANISOU 5384  OE2 GLU A 703     9342   8747   7996     24   -224   1023       O  
ATOM   5385  N   PRO A 704     101.806  29.446  -2.908  1.00 54.15           N  
ANISOU 5385  N   PRO A 704     7548   6803   6222     82    -39    937       N  
ATOM   5386  CA  PRO A 704     102.456  30.637  -2.340  1.00 64.42           C  
ANISOU 5386  CA  PRO A 704     8863   8069   7546     95    -17    937       C  
ATOM   5387  C   PRO A 704     101.450  31.679  -1.875  1.00 56.86           C  
ANISOU 5387  C   PRO A 704     7909   7076   6618    114    -39    968       C  
ATOM   5388  O   PRO A 704     100.582  32.087  -2.641  1.00 57.45           O  
ANISOU 5388  O   PRO A 704     7992   7152   6685    103    -82   1024       O  
ATOM   5389  CB  PRO A 704     103.279  31.171  -3.509  1.00 60.67           C  
ANISOU 5389  CB  PRO A 704     8404   7608   7038     65    -22    982       C  
ATOM   5390  CG  PRO A 704     103.642  29.954  -4.265  1.00 63.78           C  
ANISOU 5390  CG  PRO A 704     8791   8048   7396     47    -18    968       C  
ATOM   5391  CD  PRO A 704     102.475  29.003  -4.142  1.00 60.82           C  
ANISOU 5391  CD  PRO A 704     8398   7686   7023     53    -41    958       C  
ATOM   5392  N   THR A 705     101.560  32.073  -0.614  1.00 54.15           N  
ANISOU 5392  N   THR A 705     7561   6704   6311    144    -10    930       N  
ATOM   5393  CA  THR A 705     100.563  32.920   0.014  1.00 76.01           C  
ANISOU 5393  CA  THR A 705    10328   9439   9111    171    -25    949       C  
ATOM   5394  C   THR A 705     101.236  34.091   0.700  1.00 77.43           C  
ANISOU 5394  C   THR A 705    10520   9582   9316    186      2    945       C  
ATOM   5395  O   THR A 705     102.142  33.894   1.509  1.00 77.20           O  
ANISOU 5395  O   THR A 705    10487   9552   9295    194     43    894       O  
ATOM   5396  CB  THR A 705      99.778  32.134   1.084  1.00 76.15           C  
ANISOU 5396  CB  THR A 705    10320   9463   9150    198    -13    904       C  
ATOM   5397  OG1 THR A 705      99.665  30.764   0.681  1.00 57.19           O  
ANISOU 5397  OG1 THR A 705     7906   7100   6726    182    -20    884       O  
ATOM   5398  CG2 THR A 705      98.389  32.733   1.275  1.00 89.65           C  
ANISOU 5398  CG2 THR A 705    12028  11154  10882    220    -44    938       C  
ATOM   5399  N   PRO A 706     100.800  35.316   0.380  1.00 69.61           N  
ANISOU 5399  N   PRO A 706     9549   8561   8340    188    -25    999       N  
ATOM   5400  CA  PRO A 706     101.325  36.497   1.063  1.00 63.73           C  
ANISOU 5400  CA  PRO A 706     8817   7776   7623    203     -3   1000       C  
ATOM   5401  C   PRO A 706     101.054  36.370   2.548  1.00 61.87           C  
ANISOU 5401  C   PRO A 706     8562   7528   7417    240     30    945       C  
ATOM   5402  O   PRO A 706     100.032  35.790   2.917  1.00 62.08           O  
ANISOU 5402  O   PRO A 706     8569   7567   7453    259     21    933       O  
ATOM   5403  CB  PRO A 706     100.496  37.635   0.468  1.00 56.95           C  
ANISOU 5403  CB  PRO A 706     7977   6883   6779    205    -50   1071       C  
ATOM   5404  CG  PRO A 706     100.048  37.117  -0.864  1.00 59.27           C  
ANISOU 5404  CG  PRO A 706     8275   7206   7039    175    -94   1115       C  
ATOM   5405  CD  PRO A 706      99.804  35.663  -0.648  1.00 68.49           C  
ANISOU 5405  CD  PRO A 706     9418   8416   8190    177    -81   1066       C  
ATOM   5406  N   LEU A 707     101.952  36.874   3.385  1.00 58.83           N  
ANISOU 5406  N   LEU A 707     8183   7124   7047    248     69    914       N  
ATOM   5407  CA  LEU A 707     101.757  36.791   4.829  1.00 59.48           C  
ANISOU 5407  CA  LEU A 707     8247   7197   7155    281    103    864       C  
ATOM   5408  C   LEU A 707     100.540  37.609   5.240  1.00 61.81           C  
ANISOU 5408  C   LEU A 707     8540   7462   7482    311     84    893       C  
ATOM   5409  O   LEU A 707     100.394  38.760   4.825  1.00 44.95           O  
ANISOU 5409  O   LEU A 707     6427   5291   5363    311     61    942       O  
ATOM   5410  CB  LEU A 707     102.991  37.299   5.573  1.00 72.09           C  
ANISOU 5410  CB  LEU A 707     9856   8777   8759    280    144    831       C  
ATOM   5411  CG  LEU A 707     102.901  37.274   7.099  1.00 75.47           C  
ANISOU 5411  CG  LEU A 707    10267   9197   9210    309    181    780       C  
ATOM   5412  CD1 LEU A 707     102.705  35.840   7.583  1.00 56.67           C  
ANISOU 5412  CD1 LEU A 707     7858   6855   6820    315    194    731       C  
ATOM   5413  CD2 LEU A 707     104.134  37.924   7.742  1.00 58.43           C  
ANISOU 5413  CD2 LEU A 707     8126   7017   7058    305    216    755       C  
ATOM   5414  N   ASP A 708      99.667  37.005   6.044  1.00 66.70           N  
ANISOU 5414  N   ASP A 708     9132   8096   8114    336     92    865       N  
ATOM   5415  CA  ASP A 708      98.478  37.690   6.549  1.00 68.66           C  
ANISOU 5415  CA  ASP A 708     9375   8319   8395    370     78    887       C  
ATOM   5416  C   ASP A 708      98.897  38.845   7.446  1.00 66.07           C  
ANISOU 5416  C   ASP A 708     9059   7950   8096    389    105    879       C  
ATOM   5417  O   ASP A 708      99.691  38.665   8.371  1.00 45.52           O  
ANISOU 5417  O   ASP A 708     6451   5352   5491    390    149    830       O  
ATOM   5418  CB  ASP A 708      97.576  36.712   7.310  1.00 77.44           C  
ANISOU 5418  CB  ASP A 708    10452   9461   9510    390     88    854       C  
ATOM   5419  CG  ASP A 708      96.251  37.334   7.730  1.00 95.86           C  
ANISOU 5419  CG  ASP A 708    12774  11772  11875    426     69    880       C  
ATOM   5420  OD1 ASP A 708      95.820  38.326   7.105  1.00102.57           O  
ANISOU 5420  OD1 ASP A 708    13644  12586  12743    433     33    931       O  
ATOM   5421  OD2 ASP A 708      95.636  36.824   8.691  1.00100.98           O  
ANISOU 5421  OD2 ASP A 708    13395  12438  12534    448     89    849       O  
ATOM   5422  N   SER A 709      98.367  40.032   7.161  1.00 73.80           N  
ANISOU 5422  N   SER A 709    10056   8883   9103    402     76    928       N  
ATOM   5423  CA  SER A 709      98.747  41.241   7.888  1.00 63.54           C  
ANISOU 5423  CA  SER A 709     8773   7535   7835    418     95    928       C  
ATOM   5424  C   SER A 709      98.437  41.116   9.372  1.00 47.59           C  
ANISOU 5424  C   SER A 709     6731   5518   5834    449    135    879       C  
ATOM   5425  O   SER A 709      99.067  41.778  10.190  1.00 35.33           O  
ANISOU 5425  O   SER A 709     5190   3939   4296    455    167    858       O  
ATOM   5426  CB  SER A 709      98.072  42.485   7.293  1.00 66.76           C  
ANISOU 5426  CB  SER A 709     9201   7887   8277    431     47    992       C  
ATOM   5427  OG  SER A 709      96.668  42.447   7.476  1.00 66.65           O  
ANISOU 5427  OG  SER A 709     9169   7868   8288    466     22   1007       O  
ATOM   5428  N   LYS A 710      97.487  40.244   9.711  1.00 43.77           N  
ANISOU 5428  N   LYS A 710     6217   5068   5348    466    134    864       N  
ATOM   5429  CA  LYS A 710      97.175  39.943  11.106  1.00 62.30           C  
ANISOU 5429  CA  LYS A 710     8539   7427   7705    491    173    818       C  
ATOM   5430  C   LYS A 710      98.418  39.511  11.882  1.00 60.03           C  
ANISOU 5430  C   LYS A 710     8252   7158   7397    474    222    763       C  
ATOM   5431  O   LYS A 710      98.524  39.746  13.086  1.00 61.11           O  
ANISOU 5431  O   LYS A 710     8384   7287   7547    491    258    730       O  
ATOM   5432  CB  LYS A 710      96.111  38.849  11.193  1.00 58.90           C  
ANISOU 5432  CB  LYS A 710     8074   7038   7266    502    163    810       C  
ATOM   5433  CG  LYS A 710      95.719  38.472  12.613  1.00 58.25           C  
ANISOU 5433  CG  LYS A 710     7964   6974   7193    525    201    768       C  
ATOM   5434  CD  LYS A 710      94.728  37.313  12.628  1.00 65.40           C  
ANISOU 5434  CD  LYS A 710     8837   7924   8089    529    189    763       C  
ATOM   5435  CE  LYS A 710      94.210  37.059  14.035  1.00 81.93           C  
ANISOU 5435  CE  LYS A 710    10902  10033  10193    553    223    731       C  
ATOM   5436  NZ  LYS A 710      93.496  35.764  14.156  1.00 85.94           N  
ANISOU 5436  NZ  LYS A 710    11377  10589  10685    549    217    719       N  
ATOM   5437  N   PHE A 711      99.359  38.889  11.179  1.00 40.19           N  
ANISOU 5437  N   PHE A 711     5748   4667   4854    442    222    753       N  
ATOM   5438  CA  PHE A 711     100.575  38.385  11.801  1.00 49.65           C  
ANISOU 5438  CA  PHE A 711     6947   5883   6035    426    261    701       C  
ATOM   5439  C   PHE A 711     101.821  39.084  11.291  1.00 61.92           C  
ANISOU 5439  C   PHE A 711     8532   7413   7581    402    265    711       C  
ATOM   5440  O   PHE A 711     102.902  38.508  11.334  1.00 57.56           O  
ANISOU 5440  O   PHE A 711     7981   6879   7009    382    284    677       O  
ATOM   5441  CB  PHE A 711     100.716  36.884  11.550  1.00 46.91           C  
ANISOU 5441  CB  PHE A 711     6578   5585   5662    410    260    672       C  
ATOM   5442  CG  PHE A 711      99.581  36.081  12.088  1.00 39.18           C  
ANISOU 5442  CG  PHE A 711     5567   4632   4688    429    258    661       C  
ATOM   5443  CD1 PHE A 711      99.439  35.892  13.456  1.00 42.22           C  
ANISOU 5443  CD1 PHE A 711     5934   5025   5083    447    292    623       C  
ATOM   5444  CD2 PHE A 711      98.645  35.521  11.233  1.00 47.79           C  
ANISOU 5444  CD2 PHE A 711     6646   5742   5772    426    221    690       C  
ATOM   5445  CE1 PHE A 711      98.381  35.161  13.963  1.00 46.49           C  
ANISOU 5445  CE1 PHE A 711     6444   5592   5628    462    289    615       C  
ATOM   5446  CE2 PHE A 711      97.586  34.789  11.734  1.00 43.48           C  
ANISOU 5446  CE2 PHE A 711     6069   5221   5230    441    218    682       C  
ATOM   5447  CZ  PHE A 711      97.454  34.610  13.101  1.00 52.15           C  
ANISOU 5447  CZ  PHE A 711     7148   6326   6339    459    252    645       C  
ATOM   5448  N   SER A 712     101.675  40.317  10.814  1.00 55.43           N  
ANISOU 5448  N   SER A 712     7734   6548   6779    404    244    758       N  
ATOM   5449  CA  SER A 712     102.804  41.036  10.242  1.00 57.77           C  
ANISOU 5449  CA  SER A 712     8062   6820   7069    378    243    775       C  
ATOM   5450  C   SER A 712     103.821  41.401  11.317  1.00 52.30           C  
ANISOU 5450  C   SER A 712     7378   6114   6380    376    286    733       C  
ATOM   5451  O   SER A 712     105.028  41.393  11.068  1.00 59.92           O  
ANISOU 5451  O   SER A 712     8357   7082   7328    350    298    721       O  
ATOM   5452  CB  SER A 712     102.338  42.290   9.486  1.00 72.99           C  
ANISOU 5452  CB  SER A 712    10012   8699   9021    380    204    841       C  
ATOM   5453  OG  SER A 712     101.703  43.216  10.350  1.00 69.26           O  
ANISOU 5453  OG  SER A 712     9543   8184   8588    412    209    846       O  
ATOM   5454  N   THR A 713     103.332  41.722  12.510  1.00 49.46           N  
ANISOU 5454  N   THR A 713     7009   5740   6042    403    309    711       N  
ATOM   5455  CA  THR A 713     104.214  41.985  13.636  1.00 56.46           C  
ANISOU 5455  CA  THR A 713     7904   6618   6931    401    350    667       C  
ATOM   5456  C   THR A 713     104.047  40.859  14.628  1.00 42.85           C  
ANISOU 5456  C   THR A 713     6150   4935   5195    413    378    614       C  
ATOM   5457  O   THR A 713     104.115  41.063  15.840  1.00 34.72           O  
ANISOU 5457  O   THR A 713     5117   3899   4174    425    410    582       O  
ATOM   5458  CB  THR A 713     103.869  43.302  14.344  1.00 65.36           C  
ANISOU 5458  CB  THR A 713     9048   7692   8094    421    357    682       C  
ATOM   5459  OG1 THR A 713     102.617  43.158  15.026  1.00 53.38           O  
ANISOU 5459  OG1 THR A 713     7508   6178   6595    455    359    678       O  
ATOM   5460  CG2 THR A 713     103.787  44.447  13.338  1.00 49.34           C  
ANISOU 5460  CG2 THR A 713     7046   5613   6086    414    320    743       C  
ATOM   5461  N   GLY A 714     103.827  39.661  14.098  1.00 42.08           N  
ANISOU 5461  N   GLY A 714     6031   4879   5078    407    365    606       N  
ATOM   5462  CA  GLY A 714     103.596  38.483  14.919  1.00 42.38           C  
ANISOU 5462  CA  GLY A 714     6039   4956   5108    415    383    561       C  
ATOM   5463  C   GLY A 714     104.747  37.498  15.029  1.00 38.50           C  
ANISOU 5463  C   GLY A 714     5542   4489   4597    395    397    517       C  
ATOM   5464  O   GLY A 714     105.919  37.854  14.917  1.00 34.20           O  
ANISOU 5464  O   GLY A 714     5017   3930   4046    377    407    508       O  
ATOM   5465  N   TYR A 715     104.400  36.240  15.267  1.00 36.24           N  
ANISOU 5465  N   TYR A 715     5227   4237   4304    399    395    491       N  
ATOM   5466  CA  TYR A 715     105.392  35.230  15.568  1.00 33.12           C  
ANISOU 5466  CA  TYR A 715     4824   3860   3900    385    405    448       C  
ATOM   5467  C   TYR A 715     105.086  33.906  14.877  1.00 40.45           C  
ANISOU 5467  C   TYR A 715     5732   4820   4818    377    381    446       C  
ATOM   5468  O   TYR A 715     103.931  33.501  14.751  1.00 37.45           O  
ANISOU 5468  O   TYR A 715     5333   4456   4440    387    366    461       O  
ATOM   5469  CB  TYR A 715     105.453  34.997  17.079  1.00 37.09           C  
ANISOU 5469  CB  TYR A 715     5313   4367   4413    397    434    406       C  
ATOM   5470  CG  TYR A 715     105.908  36.185  17.883  1.00 41.68           C  
ANISOU 5470  CG  TYR A 715     5915   4918   5002    401    461    400       C  
ATOM   5471  CD1 TYR A 715     107.207  36.264  18.358  1.00 32.40           C  
ANISOU 5471  CD1 TYR A 715     4754   3732   3825    387    479    370       C  
ATOM   5472  CD2 TYR A 715     105.032  37.222  18.188  1.00 43.32           C  
ANISOU 5472  CD2 TYR A 715     6131   5106   5223    420    468    426       C  
ATOM   5473  CE1 TYR A 715     107.628  37.351  19.097  1.00 53.40           C  
ANISOU 5473  CE1 TYR A 715     7435   6364   6491    387    503    364       C  
ATOM   5474  CE2 TYR A 715     105.444  38.312  18.922  1.00 47.62           C  
ANISOU 5474  CE2 TYR A 715     6698   5620   5776    421    492    422       C  
ATOM   5475  CZ  TYR A 715     106.751  38.372  19.379  1.00 59.38           C  
ANISOU 5475  CZ  TYR A 715     8201   7101   7259    404    511    390       C  
ATOM   5476  OH  TYR A 715     107.182  39.458  20.115  1.00 57.80           O  
ANISOU 5476  OH  TYR A 715     8025   6871   7067    402    535    385       O  
ATOM   5477  N   LEU A 716     106.131  33.228  14.426  1.00 45.23           N  
ANISOU 5477  N   LEU A 716     6341   5432   5412    357    378    427       N  
ATOM   5478  CA  LEU A 716     106.007  31.813  14.116  1.00 35.82           C  
ANISOU 5478  CA  LEU A 716     5128   4267   4214    350    361    413       C  
ATOM   5479  C   LEU A 716     106.400  31.070  15.379  1.00 31.30           C  
ANISOU 5479  C   LEU A 716     4538   3700   3653    355    378    366       C  
ATOM   5480  O   LEU A 716     107.486  31.264  15.912  1.00 38.25           O  
ANISOU 5480  O   LEU A 716     5429   4567   4539    350    395    342       O  
ATOM   5481  CB  LEU A 716     106.911  31.388  12.966  1.00 39.13           C  
ANISOU 5481  CB  LEU A 716     5561   4691   4617    327    347    418       C  
ATOM   5482  CG  LEU A 716     106.856  29.864  12.761  1.00 44.44           C  
ANISOU 5482  CG  LEU A 716     6213   5387   5285    319    332    399       C  
ATOM   5483  CD1 LEU A 716     105.754  29.473  11.805  1.00 34.34           C  
ANISOU 5483  CD1 LEU A 716     4927   4126   3995    316    304    432       C  
ATOM   5484  CD2 LEU A 716     108.189  29.307  12.294  1.00 51.87           C  
ANISOU 5484  CD2 LEU A 716     7164   6328   6218    301    333    381       C  
ATOM   5485  N   GLU A 717     105.501  30.238  15.873  1.00 27.23           N  
ANISOU 5485  N   GLU A 717     3997   3204   3145    364    371    358       N  
ATOM   5486  CA  GLU A 717     105.754  29.525  17.108  1.00 35.10           C  
ANISOU 5486  CA  GLU A 717     4976   4205   4154    368    383    321       C  
ATOM   5487  C   GLU A 717     105.758  28.013  16.837  1.00 39.96           C  
ANISOU 5487  C   GLU A 717     5573   4842   4769    356    361    309       C  
ATOM   5488  O   GLU A 717     104.940  27.515  16.058  1.00 25.97           O  
ANISOU 5488  O   GLU A 717     3792   3087   2988    352    340    330       O  
ATOM   5489  CB  GLU A 717     104.692  29.897  18.137  1.00 39.02           C  
ANISOU 5489  CB  GLU A 717     5458   4706   4662    388    395    323       C  
ATOM   5490  CG  GLU A 717     105.013  29.489  19.551  1.00 54.92           C  
ANISOU 5490  CG  GLU A 717     7459   6718   6690    392    410    288       C  
ATOM   5491  CD  GLU A 717     103.933  29.900  20.517  1.00 63.49           C  
ANISOU 5491  CD  GLU A 717     8531   7808   7784    411    423    293       C  
ATOM   5492  OE1 GLU A 717     103.233  29.006  21.033  1.00 73.25           O  
ANISOU 5492  OE1 GLU A 717     9741   9064   9027    413    413    289       O  
ATOM   5493  OE2 GLU A 717     103.782  31.114  20.754  1.00 55.95           O  
ANISOU 5493  OE2 GLU A 717     7592   6836   6830    424    444    304       O  
ATOM   5494  N   LEU A 718     106.688  27.285  17.450  1.00 30.00           N  
ANISOU 5494  N   LEU A 718     4307   3577   3515    347    364    277       N  
ATOM   5495  CA  LEU A 718     106.724  25.824  17.280  1.00 29.86           C  
ANISOU 5495  CA  LEU A 718     4272   3575   3497    335    344    266       C  
ATOM   5496  C   LEU A 718     107.363  25.185  18.495  1.00 33.42           C  
ANISOU 5496  C   LEU A 718     4712   4021   3964    332    349    234       C  
ATOM   5497  O   LEU A 718     108.033  25.856  19.271  1.00 24.59           O  
ANISOU 5497  O   LEU A 718     3603   2887   2854    336    367    220       O  
ATOM   5498  CB  LEU A 718     107.486  25.398  16.025  1.00 14.63           C  
ANISOU 5498  CB  LEU A 718     2358   1646   1554    319    332    271       C  
ATOM   5499  CG  LEU A 718     108.996  25.650  16.051  1.00 38.06           C  
ANISOU 5499  CG  LEU A 718     5343   4595   4523    311    344    253       C  
ATOM   5500  CD1 LEU A 718     109.741  24.698  15.133  1.00 42.47           C  
ANISOU 5500  CD1 LEU A 718     5906   5158   5072    295    330    249       C  
ATOM   5501  CD2 LEU A 718     109.339  27.085  15.665  1.00 35.36           C  
ANISOU 5501  CD2 LEU A 718     5025   4237   4174    313    359    269       C  
ATOM   5502  N   LYS A 719     107.125  23.897  18.679  1.00 27.76           N  
ANISOU 5502  N   LYS A 719     3976   3320   3251    323    331    226       N  
ATOM   5503  CA  LYS A 719     107.817  23.142  19.723  1.00 35.87           C  
ANISOU 5503  CA  LYS A 719     4993   4343   4292    315    329    201       C  
ATOM   5504  C   LYS A 719     108.891  22.298  19.060  1.00 28.62           C  
ANISOU 5504  C   LYS A 719     4084   3422   3370    300    319    191       C  
ATOM   5505  O   LYS A 719     108.649  21.690  18.025  1.00 29.14           O  
ANISOU 5505  O   LYS A 719     4151   3498   3424    293    305    202       O  
ATOM   5506  CB  LYS A 719     106.844  22.265  20.515  1.00 27.12           C  
ANISOU 5506  CB  LYS A 719     3859   3255   3192    311    316    202       C  
ATOM   5507  CG  LYS A 719     105.773  23.059  21.262  1.00 25.64           C  
ANISOU 5507  CG  LYS A 719     3662   3071   3009    327    327    213       C  
ATOM   5508  CD  LYS A 719     104.947  22.151  22.144  1.00 32.40           C  
ANISOU 5508  CD  LYS A 719     4492   3948   3873    320    313    214       C  
ATOM   5509  CE  LYS A 719     103.945  22.909  23.012  1.00 30.13           C  
ANISOU 5509  CE  LYS A 719     4193   3665   3591    336    326    224       C  
ATOM   5510  NZ  LYS A 719     102.955  23.644  22.179  1.00 40.69           N  
ANISOU 5510  NZ  LYS A 719     5533   5009   4918    352    332    249       N  
ATOM   5511  N   MET A 720     110.084  22.292  19.634  1.00 20.72           N  
ANISOU 5511  N   MET A 720     3089   2406   2378    295    326    171       N  
ATOM   5512  CA  MET A 720     111.206  21.603  19.022  1.00 18.97           C  
ANISOU 5512  CA  MET A 720     2875   2179   2153    283    320    163       C  
ATOM   5513  C   MET A 720     112.004  20.818  20.065  1.00 33.86           C  
ANISOU 5513  C   MET A 720     4751   4061   4053    274    315    143       C  
ATOM   5514  O   MET A 720     112.192  21.263  21.198  1.00 19.41           O  
ANISOU 5514  O   MET A 720     2918   2224   2234    275    323    134       O  
ATOM   5515  CB  MET A 720     112.110  22.587  18.253  1.00 29.80           C  
ANISOU 5515  CB  MET A 720     4272   3536   3516    283    334    167       C  
ATOM   5516  CG  MET A 720     113.439  21.988  17.755  1.00 20.00           C  
ANISOU 5516  CG  MET A 720     3039   2288   2272    271    331    158       C  
ATOM   5517  SD  MET A 720     114.491  23.141  16.870  1.00 27.04           S  
ANISOU 5517  SD  MET A 720     3958   3166   3152    267    347    167       S  
ATOM   5518  CE  MET A 720     113.487  23.493  15.434  1.00 35.18           C  
ANISOU 5518  CE  MET A 720     4999   4209   4161    269    341    197       C  
ATOM   5519  N   ARG A 721     112.417  19.614  19.687  1.00 27.76           N  
ANISOU 5519  N   ARG A 721     3975   3295   3279    264    301    138       N  
ATOM   5520  CA  ARG A 721     113.312  18.809  20.496  1.00 23.99           C  
ANISOU 5520  CA  ARG A 721     3489   2814   2812    253    295    123       C  
ATOM   5521  C   ARG A 721     114.523  18.516  19.628  1.00 24.29           C  
ANISOU 5521  C   ARG A 721     3541   2842   2844    249    297    119       C  
ATOM   5522  O   ARG A 721     114.378  18.097  18.489  1.00 22.08           O  
ANISOU 5522  O   ARG A 721     3269   2567   2552    249    292    126       O  
ATOM   5523  CB  ARG A 721     112.616  17.504  20.903  1.00 25.27           C  
ANISOU 5523  CB  ARG A 721     3633   2993   2977    244    275    123       C  
ATOM   5524  CG  ARG A 721     113.483  16.522  21.694  1.00 37.30           C  
ANISOU 5524  CG  ARG A 721     5147   4517   4509    231    266    111       C  
ATOM   5525  CD  ARG A 721     112.695  15.269  22.083  1.00 33.56           C  
ANISOU 5525  CD  ARG A 721     4656   4061   4035    219    247    114       C  
ATOM   5526  NE  ARG A 721     112.505  14.357  20.962  1.00 31.50           N  
ANISOU 5526  NE  ARG A 721     4401   3804   3763    216    236    118       N  
ATOM   5527  CZ  ARG A 721     111.503  13.491  20.863  1.00 29.30           C  
ANISOU 5527  CZ  ARG A 721     4113   3541   3479    206    220    127       C  
ATOM   5528  NH1 ARG A 721     110.596  13.415  21.821  1.00 25.41           N  
ANISOU 5528  NH1 ARG A 721     3601   3063   2991    198    212    134       N  
ATOM   5529  NH2 ARG A 721     111.418  12.696  19.809  1.00 33.96           N  
ANISOU 5529  NH2 ARG A 721     4712   4132   4058    203    211    129       N  
ATOM   5530  N   ILE A 722     115.716  18.757  20.143  1.00 20.24           N  
ANISOU 5530  N   ILE A 722     3033   2318   2339    245    304    109       N  
ATOM   5531  CA  ILE A 722     116.918  18.430  19.381  1.00 28.00           C  
ANISOU 5531  CA  ILE A 722     4027   3295   3318    240    307    107       C  
ATOM   5532  C   ILE A 722     117.578  17.231  20.043  1.00 36.72           C  
ANISOU 5532  C   ILE A 722     5118   4402   4431    232    296     97       C  
ATOM   5533  O   ILE A 722     118.138  17.349  21.137  1.00 26.63           O  
ANISOU 5533  O   ILE A 722     3832   3122   3163    225    296     90       O  
ATOM   5534  CB  ILE A 722     117.896  19.620  19.299  1.00 20.05           C  
ANISOU 5534  CB  ILE A 722     3034   2273   2309    238    324    108       C  
ATOM   5535  CG1 ILE A 722     117.230  20.807  18.596  1.00 30.91           C  
ANISOU 5535  CG1 ILE A 722     4424   3646   3673    245    335    121       C  
ATOM   5536  CG2 ILE A 722     119.167  19.239  18.561  1.00 15.71           C  
ANISOU 5536  CG2 ILE A 722     2494   1721   1754    231    326    109       C  
ATOM   5537  CD1 ILE A 722     118.155  21.975  18.366  1.00 22.99           C  
ANISOU 5537  CD1 ILE A 722     3439   2630   2665    240    351    125       C  
ATOM   5538  N   ASP A 723     117.495  16.072  19.394  1.00 26.63           N  
ANISOU 5538  N   ASP A 723     3839   3131   3147    230    285     97       N  
ATOM   5539  CA  ASP A 723     118.000  14.843  19.991  1.00 25.53           C  
ANISOU 5539  CA  ASP A 723     3689   2996   3015    223    274     90       C  
ATOM   5540  C   ASP A 723     119.514  14.854  19.942  1.00 28.78           C  
ANISOU 5540  C   ASP A 723     4106   3399   3430    221    282     86       C  
ATOM   5541  O   ASP A 723     120.178  14.558  20.935  1.00 26.10           O  
ANISOU 5541  O   ASP A 723     3756   3062   3099    214    278     81       O  
ATOM   5542  CB  ASP A 723     117.425  13.610  19.267  1.00 24.42           C  
ANISOU 5542  CB  ASP A 723     3549   2863   2865    222    261     91       C  
ATOM   5543  CG  ASP A 723     115.899  13.608  19.233  1.00 24.61           C  
ANISOU 5543  CG  ASP A 723     3567   2899   2885    221    252     98       C  
ATOM   5544  OD1 ASP A 723     115.275  13.739  20.309  1.00 31.37           O  
ANISOU 5544  OD1 ASP A 723     4408   3763   3750    217    247     98       O  
ATOM   5545  OD2 ASP A 723     115.321  13.492  18.129  1.00 49.48           O  
ANISOU 5545  OD2 ASP A 723     6728   6052   6022    224    249    106       O  
ATOM   5546  N   LYS A 724     120.050  15.226  18.786  1.00 34.71           N  
ANISOU 5546  N   LYS A 724     4874   4144   4171    224    292     92       N  
ATOM   5547  CA  LYS A 724     121.494  15.324  18.582  1.00 49.40           C  
ANISOU 5547  CA  LYS A 724     6740   5999   6032    221    301     93       C  
ATOM   5548  C   LYS A 724     121.823  16.636  17.881  1.00 45.02           C  
ANISOU 5548  C   LYS A 724     6201   5438   5468    219    316    102       C  
ATOM   5549  O   LYS A 724     121.373  16.874  16.753  1.00 28.01           O  
ANISOU 5549  O   LYS A 724     4059   3284   3299    222    319    111       O  
ATOM   5550  CB  LYS A 724     122.019  14.152  17.739  1.00 49.23           C  
ANISOU 5550  CB  LYS A 724     6724   5978   6003    223    297     94       C  
ATOM   5551  CG  LYS A 724     121.840  12.778  18.364  1.00 81.38           C  
ANISOU 5551  CG  LYS A 724    10784  10056  10082    223    283     87       C  
ATOM   5552  CD  LYS A 724     122.616  11.707  17.609  1.00 93.48           C  
ANISOU 5552  CD  LYS A 724    12324  11587  11608    227    283     88       C  
ATOM   5553  CE  LYS A 724     124.121  11.933  17.701  1.00103.29           C  
ANISOU 5553  CE  LYS A 724    13565  12827  12853    225    294     91       C  
ATOM   5554  NZ  LYS A 724     124.886  10.795  17.104  1.00109.09           N  
ANISOU 5554  NZ  LYS A 724    14305  13561  13582    231    294     93       N  
ATOM   5555  N   ALA A 725     122.616  17.476  18.546  1.00 26.56           N  
ANISOU 5555  N   ALA A 725     3861   3094   3136    212    325    101       N  
ATOM   5556  CA  ALA A 725     123.026  18.763  17.988  1.00 38.73           C  
ANISOU 5556  CA  ALA A 725     5418   4630   4668    206    340    111       C  
ATOM   5557  C   ALA A 725     123.816  18.587  16.699  1.00 37.73           C  
ANISOU 5557  C   ALA A 725     5303   4508   4526    201    347    122       C  
ATOM   5558  O   ALA A 725     124.650  17.696  16.596  1.00 42.80           O  
ANISOU 5558  O   ALA A 725     5940   5154   5169    199    344    121       O  
ATOM   5559  CB  ALA A 725     123.840  19.534  18.991  1.00 36.10           C  
ANISOU 5559  CB  ALA A 725     5082   4292   4343    196    347    107       C  
ATOM   5560  N   PRO A 726     123.556  19.449  15.708  1.00 42.48           N  
ANISOU 5560  N   PRO A 726     5921   5109   5110    198    355    134       N  
ATOM   5561  CA  PRO A 726     124.217  19.340  14.407  1.00 40.93           C  
ANISOU 5561  CA  PRO A 726     5736   4921   4894    190    362    148       C  
ATOM   5562  C   PRO A 726     125.710  19.644  14.481  1.00 45.70           C  
ANISOU 5562  C   PRO A 726     6339   5528   5496    175    374    152       C  
ATOM   5563  O   PRO A 726     126.094  20.759  14.825  1.00 45.76           O  
ANISOU 5563  O   PRO A 726     6351   5532   5503    164    383    156       O  
ATOM   5564  CB  PRO A 726     123.490  20.381  13.555  1.00 43.49           C  
ANISOU 5564  CB  PRO A 726     6077   5246   5201    187    367    163       C  
ATOM   5565  CG  PRO A 726     122.981  21.365  14.528  1.00 40.74           C  
ANISOU 5565  CG  PRO A 726     5728   4888   4866    191    371    157       C  
ATOM   5566  CD  PRO A 726     122.675  20.623  15.786  1.00 23.91           C  
ANISOU 5566  CD  PRO A 726     3578   2752   2756    201    360    139       C  
ATOM   5567  N   GLU A 727     126.534  18.650  14.157  1.00 57.69           N  
ANISOU 5567  N   GLU A 727     7853   7056   7012    173    373    153       N  
ATOM   5568  CA  GLU A 727     127.986  18.791  14.202  1.00 63.10           C  
ANISOU 5568  CA  GLU A 727     8532   7750   7693    158    384    158       C  
ATOM   5569  C   GLU A 727     128.491  19.797  13.171  1.00 71.00           C  
ANISOU 5569  C   GLU A 727     9547   8762   8669    139    400    176       C  
ATOM   5570  O   GLU A 727     129.392  20.586  13.451  1.00 79.22           O  
ANISOU 5570  O   GLU A 727    10586   9807   9706    122    411    181       O  
ATOM   5571  CB  GLU A 727     128.655  17.438  13.966  0.50 65.29           C  
ANISOU 5571  CB  GLU A 727     8801   8037   7969    163    381    157       C  
ATOM   5572  CG  GLU A 727     128.166  16.345  14.888  0.50 69.04           C  
ANISOU 5572  CG  GLU A 727     9263   8503   8465    179    365    142       C  
ATOM   5573  CD  GLU A 727     128.743  14.995  14.533  0.50 67.70           C  
ANISOU 5573  CD  GLU A 727     9089   8341   8293    186    363    142       C  
ATOM   5574  OE1 GLU A 727     129.547  14.925  13.578  0.50 61.49           O  
ANISOU 5574  OE1 GLU A 727     8308   7568   7487    178    375    153       O  
ATOM   5575  OE2 GLU A 727     128.390  14.005  15.209  0.50 61.18           O  
ANISOU 5575  OE2 GLU A 727     8255   7509   7482    199    350    132       O  
ATOM   5576  N   GLN A 728     127.908  19.755  11.976  1.00 60.33           N  
ANISOU 5576  N   GLN A 728     8209   7417   7297    139    400    186       N  
ATOM   5577  CA  GLN A 728     128.327  20.623  10.883  1.00 55.50           C  
ANISOU 5577  CA  GLN A 728     7611   6821   6657    119    414    207       C  
ATOM   5578  C   GLN A 728     127.457  21.873  10.819  1.00 56.34           C  
ANISOU 5578  C   GLN A 728     7731   6917   6759    117    415    215       C  
ATOM   5579  O   GLN A 728     127.371  22.526   9.783  1.00 53.35           O  
ANISOU 5579  O   GLN A 728     7366   6550   6354    103    421    235       O  
ATOM   5580  CB  GLN A 728     128.260  19.869   9.550  0.50 47.36           C  
ANISOU 5580  CB  GLN A 728     6587   5809   5599    117    414    216       C  
ATOM   5581  CG  GLN A 728     129.567  19.817   8.784  0.50 42.54           C  
ANISOU 5581  CG  GLN A 728     5974   5227   4963     95    431    228       C  
ATOM   5582  CD  GLN A 728     130.540  18.811   9.356  0.50 54.63           C  
ANISOU 5582  CD  GLN A 728     7488   6764   6507    100    433    216       C  
ATOM   5583  OE1 GLN A 728     130.726  18.729  10.568  0.50 45.94           O  
ANISOU 5583  OE1 GLN A 728     6374   5647   5433    108    427    204       O  
ATOM   5584  NE2 GLN A 728     131.169  18.035   8.481  0.50 71.73           N  
ANISOU 5584  NE2 GLN A 728     9651   8955   8648     94    442    219       N  
ATOM   5585  N   GLY A 729     126.807  22.200  11.930  1.00 54.85           N  
ANISOU 5585  N   GLY A 729     7538   6709   6594    130    408    202       N  
ATOM   5586  CA  GLY A 729     125.917  23.343  11.969  1.00 51.48           C  
ANISOU 5586  CA  GLY A 729     7124   6272   6165    131    410    209       C  
ATOM   5587  C   GLY A 729     124.610  23.098  11.240  1.00 50.78           C  
ANISOU 5587  C   GLY A 729     7042   6185   6067    144    399    216       C  
ATOM   5588  O   GLY A 729     124.456  22.107  10.520  1.00 57.45           O  
ANISOU 5588  O   GLY A 729     7886   7041   6902    147    392    217       O  
ATOM   5589  N   ALA A 730     123.662  24.005  11.438  1.00 38.61           N  
ANISOU 5589  N   ALA A 730     5508   4634   4527    150    398    221       N  
ATOM   5590  CA  ALA A 730     122.347  23.879  10.837  1.00 36.28           C  
ANISOU 5590  CA  ALA A 730     5218   4344   4223    161    388    230       C  
ATOM   5591  C   ALA A 730     121.671  25.239  10.803  1.00 38.43           C  
ANISOU 5591  C   ALA A 730     5503   4610   4490    160    393    247       C  
ATOM   5592  O   ALA A 730     121.996  26.127  11.596  1.00 39.44           O  
ANISOU 5592  O   ALA A 730     5634   4724   4628    157    403    243       O  
ATOM   5593  CB  ALA A 730     121.493  22.881  11.601  1.00 22.21           C  
ANISOU 5593  CB  ALA A 730     3419   2557   2461    181    374    210       C  
ATOM   5594  N   ASN A 731     120.710  25.383   9.899  1.00 35.14           N  
ANISOU 5594  N   ASN A 731     5094   4202   4056    161    384    267       N  
ATOM   5595  CA  ASN A 731     120.110  26.670   9.611  1.00 35.43           C  
ANISOU 5595  CA  ASN A 731     5145   4234   4082    158    387    292       C  
ATOM   5596  C   ASN A 731     118.597  26.570   9.714  1.00 42.32           C  
ANISOU 5596  C   ASN A 731     6012   5108   4960    176    375    295       C  
ATOM   5597  O   ASN A 731     117.997  25.652   9.158  1.00 32.05           O  
ANISOU 5597  O   ASN A 731     4705   3820   3651    180    361    297       O  
ATOM   5598  CB  ASN A 731     120.518  27.094   8.203  1.00 43.19           C  
ANISOU 5598  CB  ASN A 731     6144   5232   5032    134    388    325       C  
ATOM   5599  CG  ASN A 731     120.278  28.556   7.940  1.00 59.40           C  
ANISOU 5599  CG  ASN A 731     8215   7279   7075    124    393    355       C  
ATOM   5600  OD1 ASN A 731     119.186  29.063   8.159  1.00 79.41           O  
ANISOU 5600  OD1 ASN A 731    10752   9805   9616    137    387    364       O  
ATOM   5601  ND2 ASN A 731     121.301  29.244   7.457  1.00 91.26           N  
ANISOU 5601  ND2 ASN A 731    12263  11318  11094     99    404    374       N  
ATOM   5602  N   LEU A 732     117.998  27.515  10.435  1.00 44.09           N  
ANISOU 5602  N   LEU A 732     6239   5319   5195    186    380    297       N  
ATOM   5603  CA  LEU A 732     116.552  27.616  10.600  1.00 23.58           C  
ANISOU 5603  CA  LEU A 732     3634   2723   2601    203    371    304       C  
ATOM   5604  C   LEU A 732     116.036  28.911   9.955  1.00 38.40           C  
ANISOU 5604  C   LEU A 732     5530   4597   4464    198    371    341       C  
ATOM   5605  O   LEU A 732     116.262  30.000  10.469  1.00 36.58           O  
ANISOU 5605  O   LEU A 732     5310   4349   4239    197    384    345       O  
ATOM   5606  CB  LEU A 732     116.208  27.577  12.094  1.00 23.02           C  
ANISOU 5606  CB  LEU A 732     3549   2640   2557    222    378    275       C  
ATOM   5607  CG  LEU A 732     114.865  28.110  12.584  1.00 33.64           C  
ANISOU 5607  CG  LEU A 732     4889   3984   3909    240    377    283       C  
ATOM   5608  CD1 LEU A 732     113.758  27.340  11.956  1.00 33.67           C  
ANISOU 5608  CD1 LEU A 732     4881   4005   3905    245    358    295       C  
ATOM   5609  CD2 LEU A 732     114.780  28.048  14.100  1.00 33.66           C  
ANISOU 5609  CD2 LEU A 732     4878   3977   3935    254    387    253       C  
ATOM   5610  N   GLN A 733     115.369  28.792   8.815  1.00 32.17           N  
ANISOU 5610  N   GLN A 733     4745   3822   3654    191    355    371       N  
ATOM   5611  CA  GLN A 733     114.805  29.951   8.132  1.00 30.89           C  
ANISOU 5611  CA  GLN A 733     4600   3658   3478    184    349    413       C  
ATOM   5612  C   GLN A 733     113.293  30.007   8.317  1.00 31.89           C  
ANISOU 5612  C   GLN A 733     4718   3787   3613    203    336    425       C  
ATOM   5613  O   GLN A 733     112.643  28.980   8.460  1.00 32.86           O  
ANISOU 5613  O   GLN A 733     4823   3923   3740    214    326    409       O  
ATOM   5614  CB  GLN A 733     115.171  29.931   6.652  1.00 27.92           C  
ANISOU 5614  CB  GLN A 733     4238   3299   3072    159    338    448       C  
ATOM   5615  CG  GLN A 733     116.612  30.310   6.398  1.00 21.23           C  
ANISOU 5615  CG  GLN A 733     3404   2450   2214    137    353    449       C  
ATOM   5616  CD  GLN A 733     117.117  29.857   5.029  1.00 50.62           C  
ANISOU 5616  CD  GLN A 733     7133   6196   5904    112    345    472       C  
ATOM   5617  OE1 GLN A 733     116.877  28.725   4.611  1.00 29.88           O  
ANISOU 5617  OE1 GLN A 733     4497   3587   3269    115    335    461       O  
ATOM   5618  NE2 GLN A 733     117.819  30.753   4.323  1.00 44.94           N  
ANISOU 5618  NE2 GLN A 733     6431   5480   5163     87    350    505       N  
ATOM   5619  N   VAL A 734     112.738  31.215   8.349  1.00 34.25           N  
ANISOU 5619  N   VAL A 734     5028   4073   3913    207    337    454       N  
ATOM   5620  CA  VAL A 734     111.314  31.382   8.614  1.00 32.35           C  
ANISOU 5620  CA  VAL A 734     4778   3833   3682    226    326    467       C  
ATOM   5621  C   VAL A 734     110.676  32.331   7.609  1.00 32.89           C  
ANISOU 5621  C   VAL A 734     4862   3898   3736    217    307    523       C  
ATOM   5622  O   VAL A 734     111.216  33.409   7.346  1.00 42.99           O  
ANISOU 5622  O   VAL A 734     6162   5160   5011    204    312    547       O  
ATOM   5623  CB  VAL A 734     111.066  31.877  10.057  1.00 38.08           C  
ANISOU 5623  CB  VAL A 734     5496   4541   4433    248    345    442       C  
ATOM   5624  CG1 VAL A 734     109.591  32.127  10.299  1.00 31.36           C  
ANISOU 5624  CG1 VAL A 734     4634   3691   3590    267    335    460       C  
ATOM   5625  CG2 VAL A 734     111.590  30.862  11.055  1.00 34.83           C  
ANISOU 5625  CG2 VAL A 734     5066   4133   4035    255    358    392       C  
ATOM   5626  N   MET A 735     109.535  31.918   7.051  1.00 31.70           N  
ANISOU 5626  N   MET A 735     4703   3763   3579    221    283    545       N  
ATOM   5627  CA  MET A 735     108.768  32.731   6.105  1.00 33.66           C  
ANISOU 5627  CA  MET A 735     4964   4008   3817    213    259    602       C  
ATOM   5628  C   MET A 735     109.601  33.138   4.906  1.00 45.72           C  
ANISOU 5628  C   MET A 735     6513   5539   5318    183    251    637       C  
ATOM   5629  O   MET A 735     110.064  34.271   4.823  1.00 40.73           O  
ANISOU 5629  O   MET A 735     5901   4886   4688    173    256    662       O  
ATOM   5630  CB  MET A 735     108.195  33.979   6.787  1.00 43.05           C  
ANISOU 5630  CB  MET A 735     6161   5169   5028    230    264    620       C  
ATOM   5631  CG  MET A 735     107.160  33.670   7.838  1.00 51.04           C  
ANISOU 5631  CG  MET A 735     7150   6182   6061    259    269    597       C  
ATOM   5632  SD  MET A 735     105.834  32.665   7.160  1.00 36.89           S  
ANISOU 5632  SD  MET A 735     5338   4418   4259    261    236    615       S  
ATOM   5633  CE  MET A 735     104.843  32.438   8.636  1.00 33.60           C  
ANISOU 5633  CE  MET A 735     4895   4001   3869    294    250    584       C  
ATOM   5634  N   CYS A 736     109.770  32.208   3.976  1.00 35.09           N  
ANISOU 5634  N   CYS A 736     5164   4221   3948    166    238    641       N  
ATOM   5635  CA  CYS A 736     110.632  32.402   2.819  1.00 39.08           C  
ANISOU 5635  CA  CYS A 736     5688   4738   4424    135    234    670       C  
ATOM   5636  C   CYS A 736     109.848  32.487   1.513  1.00 57.53           C  
ANISOU 5636  C   CYS A 736     8030   7093   6735    118    200    727       C  
ATOM   5637  O   CYS A 736     108.687  32.093   1.447  1.00 58.36           O  
ANISOU 5637  O   CYS A 736     8123   7207   6843    128    179    736       O  
ATOM   5638  CB  CYS A 736     111.658  31.267   2.741  1.00 26.57           C  
ANISOU 5638  CB  CYS A 736     4096   3171   2828    126    249    630       C  
ATOM   5639  SG  CYS A 736     112.632  31.025   4.250  1.00 30.28           S  
ANISOU 5639  SG  CYS A 736     4556   3621   3327    144    283    566       S  
ATOM   5640  N   SER A 737     110.493  32.994   0.469  1.00 46.95           N  
ANISOU 5640  N   SER A 737     6707   5763   5368     89    195    768       N  
ATOM   5641  CA  SER A 737     109.796  33.249  -0.781  1.00 50.39           C  
ANISOU 5641  CA  SER A 737     7150   6218   5779     70    162    830       C  
ATOM   5642  C   SER A 737     110.702  33.067  -1.979  1.00 61.64           C  
ANISOU 5642  C   SER A 737     8583   7673   7162     37    163    855       C  
ATOM   5643  O   SER A 737     110.652  33.858  -2.914  1.00 84.64           O  
ANISOU 5643  O   SER A 737    11510  10595  10056     16    146    916       O  
ATOM   5644  CB  SER A 737     109.261  34.683  -0.784  1.00 72.10           C  
ANISOU 5644  CB  SER A 737     9914   8938   8545     71    145    883       C  
ATOM   5645  OG  SER A 737     110.332  35.623  -0.785  1.00 60.67           O  
ANISOU 5645  OG  SER A 737     8484   7473   7096     56    163    897       O  
ATOM   5646  N   GLU A 738     111.534  32.033  -1.943  1.00 68.18           N  
ANISOU 5646  N   GLU A 738     9405   8521   7979     34    184    809       N  
ATOM   5647  CA  GLU A 738     112.536  31.780  -2.987  1.00 86.22           C  
ANISOU 5647  CA  GLU A 738    11698  10839  10224      5    192    824       C  
ATOM   5648  C   GLU A 738     113.654  32.821  -3.000  1.00 87.44           C  
ANISOU 5648  C   GLU A 738    11867  10980  10375    -12    211    842       C  
ATOM   5649  O   GLU A 738     114.827  32.473  -3.124  1.00 85.97           O  
ANISOU 5649  O   GLU A 738    11682  10808  10174    -25    234    820       O  
ATOM   5650  CB  GLU A 738     111.916  31.686  -4.387  0.50 75.44           C  
ANISOU 5650  CB  GLU A 738    10335   9511   8819    -15    165    882       C  
ATOM   5651  CG  GLU A 738     110.789  30.685  -4.526  0.50 73.78           C  
ANISOU 5651  CG  GLU A 738    10109   9316   8606     -3    143    872       C  
ATOM   5652  CD  GLU A 738     110.134  30.760  -5.892  0.50 70.50           C  
ANISOU 5652  CD  GLU A 738     9695   8939   8152    -22    115    936       C  
ATOM   5653  OE1 GLU A 738     110.711  31.409  -6.792  0.50 57.64           O  
ANISOU 5653  OE1 GLU A 738     8077   7330   6493    -44    118    983       O  
ATOM   5654  OE2 GLU A 738     109.042  30.178  -6.066  0.50 69.27           O  
ANISOU 5654  OE2 GLU A 738     9529   8796   7995    -15     90    943       O  
ATOM   5655  N   SER A 739     113.291  34.095  -2.874  1.00 92.36           N  
ANISOU 5655  N   SER A 739    12502  11577  11014    -13    201    884       N  
ATOM   5656  CA  SER A 739     114.266  35.184  -2.952  1.00 97.18           C  
ANISOU 5656  CA  SER A 739    13127  12175  11621    -33    216    911       C  
ATOM   5657  C   SER A 739     114.929  35.497  -1.611  1.00 85.76           C  
ANISOU 5657  C   SER A 739    11682  10692  10210    -18    242    861       C  
ATOM   5658  O   SER A 739     116.107  35.846  -1.571  1.00 70.12           O  
ANISOU 5658  O   SER A 739     9709   8711   8222    -35    264    857       O  
ATOM   5659  CB  SER A 739     113.636  36.445  -3.570  1.00 94.23           C  
ANISOU 5659  CB  SER A 739    12767  11788  11247    -44    190    988       C  
ATOM   5660  OG  SER A 739     112.532  36.911  -2.809  1.00 95.52           O  
ANISOU 5660  OG  SER A 739    12929  11915  11447    -19    173    989       O  
ATOM   5661  N   ASN A 740     114.168  35.373  -0.525  1.00 86.59           N  
ANISOU 5661  N   ASN A 740    11779  10771  10351     14    241    826       N  
ATOM   5662  CA  ASN A 740     114.695  35.557   0.831  1.00 77.50           C  
ANISOU 5662  CA  ASN A 740    10626   9590   9232     32    268    776       C  
ATOM   5663  C   ASN A 740     113.683  35.199   1.925  1.00 48.70           C  
ANISOU 5663  C   ASN A 740     6964   5925   5617     69    266    738       C  
ATOM   5664  O   ASN A 740     112.511  34.925   1.655  1.00 44.04           O  
ANISOU 5664  O   ASN A 740     6366   5342   5027     81    243    754       O  
ATOM   5665  CB  ASN A 740     115.212  36.988   1.045  1.00 84.13           C  
ANISOU 5665  CB  ASN A 740    11485  10400  10082     19    275    806       C  
ATOM   5666  CG  ASN A 740     114.136  38.030   0.848  1.00 84.39           C  
ANISOU 5666  CG  ASN A 740    11528  10407  10127     25    250    860       C  
ATOM   5667  OD1 ASN A 740     113.312  38.268   1.736  1.00 72.22           O  
ANISOU 5667  OD1 ASN A 740     9983   8840   8616     53    248    844       O  
ATOM   5668  ND2 ASN A 740     114.138  38.664  -0.321  1.00 94.43           N  
ANISOU 5668  ND2 ASN A 740    12814  11689  11377     -3    230    928       N  
ATOM   5669  N   CYS A 741     114.147  35.220   3.168  1.00 45.29           N  
ANISOU 5669  N   CYS A 741     6526   5472   5209     87    291    690       N  
ATOM   5670  CA  CYS A 741     113.328  34.824   4.304  1.00 36.25           C  
ANISOU 5670  CA  CYS A 741     5364   4316   4093    121    295    651       C  
ATOM   5671  C   CYS A 741     113.246  35.958   5.338  1.00 40.71           C  
ANISOU 5671  C   CYS A 741     5938   4845   4684    135    309    649       C  
ATOM   5672  O   CYS A 741     114.167  36.767   5.449  1.00 42.85           O  
ANISOU 5672  O   CYS A 741     6225   5100   4956    119    323    656       O  
ATOM   5673  CB  CYS A 741     113.930  33.586   4.972  1.00 35.40           C  
ANISOU 5673  CB  CYS A 741     5238   4220   3991    130    313    591       C  
ATOM   5674  SG  CYS A 741     114.290  32.145   3.889  1.00 38.12           S  
ANISOU 5674  SG  CYS A 741     5574   4603   4307    114    302    584       S  
ATOM   5675  N   LEU A 742     112.152  36.007   6.094  1.00 31.77           N  
ANISOU 5675  N   LEU A 742     4795   3703   3575    163    306    638       N  
ATOM   5676  CA  LEU A 742     111.998  36.971   7.179  1.00 19.29           C  
ANISOU 5676  CA  LEU A 742     3220   2089   2019    180    322    631       C  
ATOM   5677  C   LEU A 742     113.017  36.759   8.299  1.00 37.70           C  
ANISOU 5677  C   LEU A 742     5547   4415   4361    183    353    577       C  
ATOM   5678  O   LEU A 742     113.472  37.718   8.913  1.00 31.17           O  
ANISOU 5678  O   LEU A 742     4735   3562   3546    181    369    576       O  
ATOM   5679  CB  LEU A 742     110.577  36.931   7.748  1.00 21.73           C  
ANISOU 5679  CB  LEU A 742     3516   2394   2347    210    314    630       C  
ATOM   5680  CG  LEU A 742     109.527  37.845   7.123  1.00 49.69           C  
ANISOU 5680  CG  LEU A 742     7067   5918   5893    213    286    689       C  
ATOM   5681  CD1 LEU A 742     109.512  37.744   5.606  1.00 62.88           C  
ANISOU 5681  CD1 LEU A 742     8748   7605   7538    187    256    738       C  
ATOM   5682  CD2 LEU A 742     108.152  37.533   7.676  1.00 38.93           C  
ANISOU 5682  CD2 LEU A 742     5686   4559   4547    244    278    683       C  
ATOM   5683  N   ARG A 743     113.365  35.503   8.580  1.00 36.64           N  
ANISOU 5683  N   ARG A 743     5394   4303   4224    188    360    534       N  
ATOM   5684  CA  ARG A 743     114.367  35.208   9.609  1.00 34.64           C  
ANISOU 5684  CA  ARG A 743     5134   4044   3981    189    384    486       C  
ATOM   5685  C   ARG A 743     115.329  34.134   9.157  1.00 35.35           C  
ANISOU 5685  C   ARG A 743     5216   4155   4059    174    384    465       C  
ATOM   5686  O   ARG A 743     114.959  33.229   8.416  1.00 45.11