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***  SH2  ***

elNémo ID: 21120308551182204

Job options:

ID        	=	 21120308551182204
JOBID     	=	 SH2
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER SH2

HEADER    PROTEIN BINDING                         04-JUN-18   6DM4              
TITLE     CRYSTAL STRUCTURE OF THE SH2 DOMAIN FROM RAVO (LPG1129) FROM          
TITLE    2 LEGIONELLA PNEUMOPHILA IN COMPLEX WITH HOMO SAPIENS SHC1 PHOSPHO-    
TITLE    3 TYR317 PEPTIDE                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAVO;                                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: SHC1 PHOSPHO-TYR317 PEPTIDE;                               
COMPND   7 CHAIN: E, G, H;                                                      
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LEGIONELLA PNEUMOPHILA SUBSP. PNEUMOPHILA       
SOURCE   3 (STRAIN PHILADELPHIA 1 / ATCC 33152 / DSM 7513);                     
SOURCE   4 ORGANISM_TAXID: 272624;                                              
SOURCE   5 STRAIN: PHILADELPHIA 1 / ATCC 33152 / DSM 7513;                      
SOURCE   6 GENE: LPG1129;                                                       
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL;                   
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PMCSG53;                                  
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 SYNTHETIC: YES;                                                      
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606                                                 
KEYWDS    SH2 DOMAIN, SRC HOMOLOG 2 DOMAIN, SHC1, PHOSPHOPEPTIDE BINDING,       
KEYWDS   2 LEGIONELLA PNEUMOPHILA, STRUCTURAL GENOMICS, APC108076, MIDWEST      
KEYWDS   3 CENTER FOR STRUCTURAL GENOMICS, MCSG, PSI-BIOLOGY, PROTEIN BINDING   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.J.STOGIOS,E.EVDOKIMOVA,R.DI LEO,T.KANEKO,S.LI,A.SAVCHENKO,MIDWEST   
AUTHOR   2 CENTER FOR STRUCTURAL GENOMICS (MCSG)                                
REVDAT   2   01-JAN-20 6DM4    1       REMARK                                   
REVDAT   1   27-JUN-18 6DM4    0                                                
JRNL        AUTH   T.KANEKO                                                     
JRNL        TITL   CRYSTAL STRUCTURE OF THE SH2 DOMAIN FROM RAVO (LPG1129) FROM 
JRNL        TITL 2 LEGIONELLA PNEUMOPHILA IN COMPLEX WITH HOMO SAPIENS SHC1     
JRNL        TITL 3 PHOSPHO-TYR317 PEPTIDE                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_3092: ???)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.82                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.980                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 41046                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.820                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1977                            
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 14.8150 -  4.5382    0.91     2624   136  0.1626 0.2002        
REMARK   3     2  4.5382 -  3.6194    0.98     2815   145  0.1435 0.1799        
REMARK   3     3  3.6194 -  3.1670    0.98     2792   145  0.1725 0.2367        
REMARK   3     4  3.1670 -  2.8797    0.98     2856   140  0.1912 0.2337        
REMARK   3     5  2.8797 -  2.6746    0.98     2797   150  0.1994 0.2514        
REMARK   3     6  2.6746 -  2.5177    0.98     2817   143  0.2124 0.2663        
REMARK   3     7  2.5177 -  2.3922    0.98     2842   137  0.2099 0.2937        
REMARK   3     8  2.3922 -  2.2885    0.97     2789   139  0.1998 0.2507        
REMARK   3     9  2.2885 -  2.2007    0.97     2819   136  0.2102 0.2610        
REMARK   3    10  2.2007 -  2.1249    0.97     2780   149  0.2129 0.2664        
REMARK   3    11  2.1249 -  2.0587    0.97     2806   129  0.2166 0.2827        
REMARK   3    12  2.0587 -  2.0000    0.96     2785   137  0.2252 0.2474        
REMARK   3    13  2.0000 -  1.9474    0.97     2784   144  0.2444 0.2696        
REMARK   3    14  1.9474 -  1.9000    0.96     2763   147  0.2711 0.3397        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.910           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           4158                                  
REMARK   3   ANGLE     :  0.616           5618                                  
REMARK   3   CHIRALITY :  0.051            620                                  
REMARK   3   PLANARITY :  0.003            708                                  
REMARK   3   DIHEDRAL  : 20.564           1555                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 30                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 226 THROUGH 237 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -20.8667  25.3806 -48.3250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4038 T22:   0.8257                                     
REMARK   3      T33:   0.3626 T12:   0.2287                                     
REMARK   3      T13:   0.0007 T23:   0.0820                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6731 L22:   6.8369                                     
REMARK   3      L33:   3.6047 L12:   0.0179                                     
REMARK   3      L13:   3.2348 L23:  -2.9888                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4959 S12:  -2.0394 S13:  -0.2183                       
REMARK   3      S21:   1.0309 S22:   0.3554 S23:  -0.0271                       
REMARK   3      S31:  -0.2193 S32:  -0.2266 S33:   0.0773                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 238 THROUGH 258 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -21.5299  26.5171 -69.4737              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2626 T22:   0.3504                                     
REMARK   3      T33:   0.3027 T12:   0.0555                                     
REMARK   3      T13:  -0.0958 T23:   0.0293                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5181 L22:   4.5238                                     
REMARK   3      L33:   7.9255 L12:  -0.0004                                     
REMARK   3      L13:  -3.8357 L23:   1.7422                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0525 S12:   0.0519 S13:   0.1446                       
REMARK   3      S21:  -0.4198 S22:   0.1567 S23:   0.3064                       
REMARK   3      S31:   0.2220 S32:  -0.5301 S33:  -0.1000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 259 THROUGH 273 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -18.7434  22.2354 -64.8750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4299 T22:   0.3531                                     
REMARK   3      T33:   0.2697 T12:   0.0231                                     
REMARK   3      T13:  -0.1013 T23:  -0.0228                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4708 L22:   4.7449                                     
REMARK   3      L33:   5.3763 L12:   0.9026                                     
REMARK   3      L13:  -2.1904 L23:  -3.8498                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3195 S12:   0.2719 S13:  -0.3114                       
REMARK   3      S21:  -1.1394 S22:   0.6728 S23:   0.2623                       
REMARK   3      S31:   1.1259 S32:  -0.0957 S33:  -0.4233                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 274 THROUGH 278 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -20.9686   7.8996 -53.2084              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2034 T22:   1.0117                                     
REMARK   3      T33:   1.8900 T12:   0.0570                                     
REMARK   3      T13:   0.0360 T23:  -0.1527                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4836 L22:   5.4665                                     
REMARK   3      L33:   5.2645 L12:   5.4712                                     
REMARK   3      L13:   5.3330 L23:   5.3302                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2178 S12:   0.9575 S13:  -5.0721                       
REMARK   3      S21:  -0.8990 S22:   0.3262 S23:   0.6357                       
REMARK   3      S31:   2.4855 S32:   0.8146 S33:   0.0185                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 279 THROUGH 300 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.2118  19.6858 -63.9521              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3039 T22:   0.4166                                     
REMARK   3      T33:   0.3025 T12:   0.1421                                     
REMARK   3      T13:  -0.0616 T23:  -0.0475                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7469 L22:   5.1431                                     
REMARK   3      L33:   6.9919 L12:  -0.8340                                     
REMARK   3      L13:  -0.4405 L23:  -2.4100                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0155 S12:   0.1203 S13:  -0.1646                       
REMARK   3      S21:  -0.3846 S22:   0.0745 S23:  -0.0546                       
REMARK   3      S31:   1.0092 S32:   0.6724 S33:  -0.0178                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 301 THROUGH 308 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.1044  17.1693 -50.0415              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5849 T22:   0.7967                                     
REMARK   3      T33:   0.4278 T12:   0.2410                                     
REMARK   3      T13:  -0.0862 T23:   0.0651                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4224 L22:   6.0500                                     
REMARK   3      L33:   4.9256 L12:  -0.5612                                     
REMARK   3      L13:  -0.8617 L23:   1.2083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2701 S12:  -1.1134 S13:  -0.7514                       
REMARK   3      S21:   0.8505 S22:  -0.0359 S23:  -0.0753                       
REMARK   3      S31:   0.8221 S32:   0.3183 S33:   0.2337                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 309 THROUGH 324 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.9391  18.1238 -54.6820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4423 T22:   0.7421                                     
REMARK   3      T33:   0.3731 T12:   0.2357                                     
REMARK   3      T13:  -0.0208 T23:  -0.0031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1728 L22:   8.5776                                     
REMARK   3      L33:   5.4603 L12:   0.0431                                     
REMARK   3      L13:   0.8629 L23:   2.1541                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2679 S12:  -0.5723 S13:  -0.4831                       
REMARK   3      S21:   0.2292 S22:   0.2842 S23:  -1.2144                       
REMARK   3      S31:   1.0413 S32:   0.9630 S33:  -0.5590                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 325 THROUGH 344 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.8923  26.5231 -63.7874              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2565 T22:   0.5999                                     
REMARK   3      T33:   0.3658 T12:   0.1170                                     
REMARK   3      T13:  -0.0435 T23:  -0.0448                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8882 L22:   9.2239                                     
REMARK   3      L33:   9.1671 L12:  -4.1172                                     
REMARK   3      L13:  -6.7805 L23:   6.4970                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5227 S12:   0.2164 S13:   0.7876                       
REMARK   3      S21:  -0.6034 S22:  -0.0698 S23:  -0.6169                       
REMARK   3      S31:  -0.4562 S32:   0.3438 S33:  -0.3897                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 902 THROUGH 908 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.9177  14.9499 -67.1267              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9625 T22:   0.7846                                     
REMARK   3      T33:   0.5328 T12:   0.1485                                     
REMARK   3      T13:  -0.0744 T23:  -0.0621                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2625 L22:   9.7123                                     
REMARK   3      L33:   1.4155 L12:   6.9108                                     
REMARK   3      L13:  -2.9598 L23:  -3.1684                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4722 S12:   0.9794 S13:  -1.2707                       
REMARK   3      S21:  -0.4627 S22:  -0.4150 S23:  -0.8181                       
REMARK   3      S31:   0.5393 S32:   1.1573 S33:  -0.0032                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 226 THROUGH 237 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -29.1887  21.1075 -52.9190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5608 T22:   0.3523                                     
REMARK   3      T33:   0.6911 T12:  -0.0343                                     
REMARK   3      T13:  -0.0410 T23:   0.0153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8097 L22:   8.9827                                     
REMARK   3      L33:   2.4801 L12:   0.3280                                     
REMARK   3      L13:  -0.7878 L23:  -1.7581                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0761 S12:   0.1907 S13:  -2.0135                       
REMARK   3      S21:  -0.7321 S22:  -0.0332 S23:  -0.4945                       
REMARK   3      S31:   1.5969 S32:   0.0060 S33:   0.0155                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 238 THROUGH 258 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -28.3847  41.7457 -48.8773              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3937 T22:   0.2684                                     
REMARK   3      T33:   0.3239 T12:  -0.0869                                     
REMARK   3      T13:   0.0629 T23:   0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2639 L22:   7.2301                                     
REMARK   3      L33:   7.1661 L12:   2.9704                                     
REMARK   3      L13:   1.1098 L23:   3.5854                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1572 S12:  -0.0238 S13:   0.4579                       
REMARK   3      S21:  -0.2233 S22:   0.0568 S23:  -0.2374                       
REMARK   3      S31:  -1.3044 S32:   0.5651 S33:  -0.1786                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 259 THROUGH 273 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -31.2828  36.1488 -45.6667              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4009 T22:   0.2331                                     
REMARK   3      T33:   0.2681 T12:  -0.0382                                     
REMARK   3      T13:  -0.0334 T23:  -0.0241                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0575 L22:   2.9893                                     
REMARK   3      L33:   5.7237 L12:  -1.0077                                     
REMARK   3      L13:   1.0324 L23:  -3.9177                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3547 S12:  -0.0039 S13:   0.1373                       
REMARK   3      S21:   0.9264 S22:  -0.0167 S23:  -0.3626                       
REMARK   3      S31:  -1.1361 S32:  -0.0059 S33:   0.4601                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 274 THROUGH 279 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -31.2497  20.1181 -36.7066              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0294 T22:   0.8884                                     
REMARK   3      T33:   0.5961 T12:  -0.0539                                     
REMARK   3      T13:  -0.1731 T23:   0.2393                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6066 L22:   4.0088                                     
REMARK   3      L33:   4.4265 L12:   0.5703                                     
REMARK   3      L13:   1.4936 L23:   3.9214                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5354 S12:  -2.5109 S13:  -2.2350                       
REMARK   3      S21:   1.9344 S22:  -0.4902 S23:  -1.0447                       
REMARK   3      S31:   1.4673 S32:  -0.1921 S33:  -0.2867                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 280 THROUGH 299 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -37.3756  36.6136 -43.9379              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2215 T22:   0.3617                                     
REMARK   3      T33:   0.2127 T12:   0.0476                                     
REMARK   3      T13:  -0.0008 T23:  -0.0188                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7857 L22:   8.0885                                     
REMARK   3      L33:   7.3382 L12:  -0.4481                                     
REMARK   3      L13:   0.9718 L23:   0.4170                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1459 S12:  -0.0990 S13:   0.2791                       
REMARK   3      S21:  -0.1705 S22:  -0.2807 S23:   0.2271                       
REMARK   3      S31:  -0.6164 S32:  -0.9631 S33:   0.1180                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 300 THROUGH 324 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -40.3662  23.4716 -45.0661              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4032 T22:   0.3968                                     
REMARK   3      T33:   0.3301 T12:  -0.1849                                     
REMARK   3      T13:  -0.0029 T23:  -0.0183                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3744 L22:   3.9882                                     
REMARK   3      L33:   7.7870 L12:   0.2075                                     
REMARK   3      L13:  -0.0637 L23:   2.5974                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2604 S12:  -0.1370 S13:  -0.6046                       
REMARK   3      S21:   0.6106 S22:  -0.4071 S23:   0.0458                       
REMARK   3      S31:   1.1205 S32:  -0.9134 S33:   0.1426                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 325 THROUGH 344 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -45.3257  36.8568 -50.1645              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3162 T22:   0.6278                                     
REMARK   3      T33:   0.3286 T12:   0.1076                                     
REMARK   3      T13:  -0.0468 T23:  -0.0634                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.8332 L22:   5.5567                                     
REMARK   3      L33:   7.3545 L12:  -0.1189                                     
REMARK   3      L13:   0.0126 L23:   1.0497                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0384 S12:  -0.2114 S13:   0.2285                       
REMARK   3      S21:  -0.1292 S22:  -0.3213 S23:   0.7628                       
REMARK   3      S31:  -0.9293 S32:  -1.0998 S33:   0.3221                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 226 THROUGH 237 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -30.3225  36.9576 -92.2565              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0089 T22:   0.4837                                     
REMARK   3      T33:   0.4133 T12:   0.1884                                     
REMARK   3      T13:  -0.1652 T23:  -0.0460                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7648 L22:   4.0259                                     
REMARK   3      L33:   5.8139 L12:  -0.0284                                     
REMARK   3      L13:   0.0711 L23:  -4.8339                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0902 S12:   1.0309 S13:  -0.6703                       
REMARK   3      S21:  -1.9278 S22:   0.1839 S23:   0.8306                       
REMARK   3      S31:  -0.0949 S32:  -0.6255 S33:  -0.2499                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 238 THROUGH 263 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.8877  37.3722 -71.1903              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3252 T22:   0.2822                                     
REMARK   3      T33:   0.2002 T12:   0.0160                                     
REMARK   3      T13:  -0.0503 T23:   0.0518                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5672 L22:   6.0285                                     
REMARK   3      L33:   3.3586 L12:  -0.7495                                     
REMARK   3      L13:  -4.4424 L23:   0.9008                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1065 S12:  -0.1746 S13:  -0.0586                       
REMARK   3      S21:  -0.2746 S22:  -0.0315 S23:   0.0696                       
REMARK   3      S31:   0.0227 S32:  -0.1703 S33:  -0.0513                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 264 THROUGH 299 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -36.7729  43.0333 -78.3492              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3773 T22:   0.3483                                     
REMARK   3      T33:   0.3572 T12:   0.0955                                     
REMARK   3      T13:   0.0158 T23:   0.0556                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8618 L22:   6.3996                                     
REMARK   3      L33:   8.4368 L12:  -0.7296                                     
REMARK   3      L13:   1.8092 L23:  -0.7577                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0123 S12:  -0.0528 S13:   0.0678                       
REMARK   3      S21:  -0.0766 S22:  -0.0082 S23:   0.7588                       
REMARK   3      S31:  -0.1487 S32:  -1.0964 S33:   0.0375                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 300 THROUGH 324 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -35.3687  49.3222 -87.9055              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7644 T22:   0.3713                                     
REMARK   3      T33:   0.3982 T12:   0.1698                                     
REMARK   3      T13:  -0.0656 T23:   0.0539                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1075 L22:   2.2462                                     
REMARK   3      L33:   6.1595 L12:   0.9823                                     
REMARK   3      L13:  -0.8182 L23:  -1.7629                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1444 S12:   0.1815 S13:   0.5115                       
REMARK   3      S21:  -0.5534 S22:   0.2325 S23:   0.5667                       
REMARK   3      S31:  -0.5849 S32:  -0.9371 S33:  -0.4260                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 325 THROUGH 344 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -25.4539  52.3199 -77.3140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6030 T22:   0.2616                                     
REMARK   3      T33:   0.3165 T12:   0.0771                                     
REMARK   3      T13:   0.0361 T23:   0.0401                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2716 L22:   8.2369                                     
REMARK   3      L33:   7.5502 L12:  -4.2403                                     
REMARK   3      L13:  -5.5453 L23:   6.8488                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1029 S12:  -0.3112 S13:   0.5773                       
REMARK   3      S21:  -0.2411 S22:   0.2695 S23:  -0.6290                       
REMARK   3      S31:  -0.9357 S32:   0.2844 S33:  -0.2781                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 902 THROUGH 907 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -36.5982  50.8439 -72.2247              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9796 T22:   0.7821                                     
REMARK   3      T33:   0.7475 T12:   0.0885                                     
REMARK   3      T13:  -0.0069 T23:  -0.0882                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7781 L22:   1.8415                                     
REMARK   3      L33:   5.6796 L12:   1.9971                                     
REMARK   3      L13:   5.7316 L23:   1.9948                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3838 S12:  -0.1436 S13:   1.1198                       
REMARK   3      S21:   0.9647 S22:   0.2141 S23:  -0.1451                       
REMARK   3      S31:  -1.3482 S32:  -0.0729 S33:   0.1983                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 226 THROUGH 237 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -36.1429  29.6532 -87.4896              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5144 T22:   0.5880                                     
REMARK   3      T33:   0.5484 T12:   0.0687                                     
REMARK   3      T13:  -0.1112 T23:  -0.0535                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2543 L22:   7.4902                                     
REMARK   3      L33:   2.7592 L12:   1.8857                                     
REMARK   3      L13:  -0.1960 L23:   2.0060                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1366 S12:  -0.4835 S13:   0.2178                       
REMARK   3      S21:  -0.3571 S22:  -0.2991 S23:   1.2770                       
REMARK   3      S31:  -0.2806 S32:  -1.3308 S33:   0.1756                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 238 THROUGH 258 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.5755  26.0194 -92.6640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4028 T22:   0.5195                                     
REMARK   3      T33:   0.5675 T12:  -0.0717                                     
REMARK   3      T13:   0.0364 T23:  -0.1090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9846 L22:   4.3827                                     
REMARK   3      L33:   7.1470 L12:  -0.7830                                     
REMARK   3      L13:  -2.7994 L23:   2.5404                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0276 S12:   0.0856 S13:   0.2502                       
REMARK   3      S21:  -0.4084 S22:   0.5427 S23:  -1.3014                       
REMARK   3      S31:  -0.5296 S32:   1.3522 S33:  -0.4786                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 259 THROUGH 273 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -22.4652  24.2268 -95.3732              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3790 T22:   0.2849                                     
REMARK   3      T33:   0.3079 T12:  -0.0225                                     
REMARK   3      T13:   0.0066 T23:  -0.0636                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.3792 L22:   4.1742                                     
REMARK   3      L33:   8.8306 L12:   1.0300                                     
REMARK   3      L13:   0.1786 L23:   0.3829                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0425 S12:   0.1644 S13:   0.2901                       
REMARK   3      S21:  -0.1890 S22:  -0.0062 S23:  -0.4259                       
REMARK   3      S31:  -0.0290 S32:   0.6033 S33:  -0.0130                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 274 THROUGH 278 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -37.8181  29.3517-104.7804              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4489 T22:   1.0890                                     
REMARK   3      T33:   0.7011 T12:   0.2643                                     
REMARK   3      T13:  -0.2432 T23:   0.2027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8186 L22:   0.0604                                     
REMARK   3      L33:   3.3870 L12:  -0.6287                                     
REMARK   3      L13:  -4.5552 L23:   0.4657                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2503 S12:   2.3374 S13:   0.7688                       
REMARK   3      S21:  -2.0692 S22:  -0.3574 S23:   0.7246                       
REMARK   3      S31:  -2.0909 S32:  -0.4903 S33:   0.3528                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 279 THROUGH 300 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -25.2080  19.0980 -97.0186              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3491 T22:   0.2233                                     
REMARK   3      T33:   0.2315 T12:   0.0146                                     
REMARK   3      T13:  -0.0241 T23:   0.0142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.7886 L22:   5.0854                                     
REMARK   3      L33:   8.3471 L12:  -1.8006                                     
REMARK   3      L13:   0.6963 L23:   2.0262                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1373 S12:   0.0954 S13:  -0.4087                       
REMARK   3      S21:  -0.0428 S22:   0.1436 S23:  -0.2695                       
REMARK   3      S31:   0.4160 S32:   0.5308 S33:   0.0234                       
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 301 THROUGH 324 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -36.6656  18.0479 -95.3781              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3434 T22:   0.3737                                     
REMARK   3      T33:   0.2361 T12:  -0.0534                                     
REMARK   3      T13:   0.0116 T23:  -0.0505                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8875 L22:   2.9823                                     
REMARK   3      L33:   3.4752 L12:  -0.4019                                     
REMARK   3      L13:  -0.4734 L23:   1.5978                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1835 S12:  -0.0634 S13:  -0.1700                       
REMARK   3      S21:   0.3942 S22:  -0.2977 S23:   0.3076                       
REMARK   3      S31:   0.5410 S32:  -1.4222 S33:   0.4425                       
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 325 THROUGH 344 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -25.2332  10.8996 -90.1505              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6386 T22:   0.3034                                     
REMARK   3      T33:   0.3009 T12:   0.0819                                     
REMARK   3      T13:  -0.0504 T23:   0.0387                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1177 L22:   5.4020                                     
REMARK   3      L33:   6.8648 L12:  -0.9189                                     
REMARK   3      L13:  -0.8878 L23:   0.0836                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2534 S12:  -0.2552 S13:  -0.6638                       
REMARK   3      S21:   0.3580 S22:   0.0970 S23:  -0.1636                       
REMARK   3      S31:   1.4913 S32:   0.6965 S33:   0.0948                       
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 902 THROUGH 908 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -24.3129  13.3716-101.7459              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7894 T22:   0.5453                                     
REMARK   3      T33:   0.4240 T12:   0.0978                                     
REMARK   3      T13:  -0.0407 T23:  -0.1164                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1585 L22:   4.9651                                     
REMARK   3      L33:   5.6399 L12:  -3.8186                                     
REMARK   3      L13:   1.9850 L23:  -3.4633                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0326 S12:   0.3535 S13:  -0.7253                       
REMARK   3      S21:  -0.2051 S22:  -0.1319 S23:  -0.0435                       
REMARK   3      S31:   1.3943 S32:   0.0927 S33:   0.2256                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6DM4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000234907.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-FEB-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97932                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41529                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 33.1900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.220                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 MM PTYR317 SHC1 PEPTIDE, 0.2 M       
REMARK 280  AMMONIUM SULFATE, 0.1 M TRIS PH 8.5, 25% (W/V) PEG 5K MME, VAPOR    
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G, D, H                            
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     GLU A   225                                                      
REMARK 465     GLU B   225                                                      
REMARK 465     GLU C   225                                                      
REMARK 465     GLN G   908                                                      
REMARK 465     GLU D   225                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     THR C 275    OG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 273      -82.00    -77.28                                   
REMARK 500    THR A 275     -178.40     59.41                                   
REMARK 500    VAL E 907      -65.01    -99.42                                   
REMARK 500    ASN B 277       -9.83     79.01                                   
REMARK 500    ALA B 343        0.86    -67.69                                   
REMARK 500    SER H 903       89.63     57.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues PTR E 904         
REMARK 800  through VAL E 905 bound to SER E 903                                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues PTR G 904         
REMARK 800  through VAL G 905 bound to SER G 903                                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues PTR H 904         
REMARK 800  through VAL H 905 bound to SER H 903                                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: MCSG-APC108076   RELATED DB: TARGETTRACK                 
DBREF  6DM4 A  225   344  UNP    Q5ZWF6   Q5ZWF6_LEGPH   225    344             
DBREF  6DM4 E  902   908  PDB    6DM4     6DM4           902    908             
DBREF  6DM4 B  225   344  UNP    Q5ZWF6   Q5ZWF6_LEGPH   225    344             
DBREF  6DM4 C  225   344  UNP    Q5ZWF6   Q5ZWF6_LEGPH   225    344             
DBREF  6DM4 G  902   908  PDB    6DM4     6DM4           902    908             
DBREF  6DM4 D  225   344  UNP    Q5ZWF6   Q5ZWF6_LEGPH   225    344             
DBREF  6DM4 H  902   908  PDB    6DM4     6DM4           902    908             
SEQRES   1 A  120  GLU SER GLU LYS ILE TYR LYS VAL MET GLU GLU ILE PHE          
SEQRES   2 A  120  VAL ASP ARG HIS TYR LYS GLU ASN ILE ARG THR GLY GLU          
SEQRES   3 A  120  GLU VAL LYS GLN TYR PHE SER LYS SER LYS ALA GLU PHE          
SEQRES   4 A  120  ILE LEU ARG TRP SER SER ALA ASN GLU SER ASP THR GLU          
SEQRES   5 A  120  ASN LYS TYR VAL PHE ILE ALA ALA SER PHE GLN ALA SER          
SEQRES   6 A  120  ASP GLY ILE HIS SER ILE ARG TYR GLY ILE ASN LYS ASN          
SEQRES   7 A  120  GLY GLU LEU PHE SER ILE ASN THR ALA SER ASN LYS VAL          
SEQRES   8 A  120  THR PRO ILE ASP ILE LEU PRO LEU GLY VAL MET ALA THR          
SEQRES   9 A  120  LEU THR GLN HIS ILE THR GLN ASN LYS GLU LEU ILE GLU          
SEQRES  10 A  120  LYS ALA LEU                                                  
SEQRES   1 E    7  PRO SER PTR VAL ASN VAL GLN                                  
SEQRES   1 B  120  GLU SER GLU LYS ILE TYR LYS VAL MET GLU GLU ILE PHE          
SEQRES   2 B  120  VAL ASP ARG HIS TYR LYS GLU ASN ILE ARG THR GLY GLU          
SEQRES   3 B  120  GLU VAL LYS GLN TYR PHE SER LYS SER LYS ALA GLU PHE          
SEQRES   4 B  120  ILE LEU ARG TRP SER SER ALA ASN GLU SER ASP THR GLU          
SEQRES   5 B  120  ASN LYS TYR VAL PHE ILE ALA ALA SER PHE GLN ALA SER          
SEQRES   6 B  120  ASP GLY ILE HIS SER ILE ARG TYR GLY ILE ASN LYS ASN          
SEQRES   7 B  120  GLY GLU LEU PHE SER ILE ASN THR ALA SER ASN LYS VAL          
SEQRES   8 B  120  THR PRO ILE ASP ILE LEU PRO LEU GLY VAL MET ALA THR          
SEQRES   9 B  120  LEU THR GLN HIS ILE THR GLN ASN LYS GLU LEU ILE GLU          
SEQRES  10 B  120  LYS ALA LEU                                                  
SEQRES   1 C  120  GLU SER GLU LYS ILE TYR LYS VAL MET GLU GLU ILE PHE          
SEQRES   2 C  120  VAL ASP ARG HIS TYR LYS GLU ASN ILE ARG THR GLY GLU          
SEQRES   3 C  120  GLU VAL LYS GLN TYR PHE SER LYS SER LYS ALA GLU PHE          
SEQRES   4 C  120  ILE LEU ARG TRP SER SER ALA ASN GLU SER ASP THR GLU          
SEQRES   5 C  120  ASN LYS TYR VAL PHE ILE ALA ALA SER PHE GLN ALA SER          
SEQRES   6 C  120  ASP GLY ILE HIS SER ILE ARG TYR GLY ILE ASN LYS ASN          
SEQRES   7 C  120  GLY GLU LEU PHE SER ILE ASN THR ALA SER ASN LYS VAL          
SEQRES   8 C  120  THR PRO ILE ASP ILE LEU PRO LEU GLY VAL MET ALA THR          
SEQRES   9 C  120  LEU THR GLN HIS ILE THR GLN ASN LYS GLU LEU ILE GLU          
SEQRES  10 C  120  LYS ALA LEU                                                  
SEQRES   1 G    7  PRO SER PTR VAL ASN VAL GLN                                  
SEQRES   1 D  120  GLU SER GLU LYS ILE TYR LYS VAL MET GLU GLU ILE PHE          
SEQRES   2 D  120  VAL ASP ARG HIS TYR LYS GLU ASN ILE ARG THR GLY GLU          
SEQRES   3 D  120  GLU VAL LYS GLN TYR PHE SER LYS SER LYS ALA GLU PHE          
SEQRES   4 D  120  ILE LEU ARG TRP SER SER ALA ASN GLU SER ASP THR GLU          
SEQRES   5 D  120  ASN LYS TYR VAL PHE ILE ALA ALA SER PHE GLN ALA SER          
SEQRES   6 D  120  ASP GLY ILE HIS SER ILE ARG TYR GLY ILE ASN LYS ASN          
SEQRES   7 D  120  GLY GLU LEU PHE SER ILE ASN THR ALA SER ASN LYS VAL          
SEQRES   8 D  120  THR PRO ILE ASP ILE LEU PRO LEU GLY VAL MET ALA THR          
SEQRES   9 D  120  LEU THR GLN HIS ILE THR GLN ASN LYS GLU LEU ILE GLU          
SEQRES  10 D  120  LYS ALA LEU                                                  
SEQRES   1 H    7  PRO SER PTR VAL ASN VAL GLN                                  
HET    PTR  E 904      16                                                       
HET    PTR  G 904      16                                                       
HET    PTR  H 904      16                                                       
HET    SO4  A1001       5                                                       
HET    SO4  A1002       5                                                       
HET    SO4  B 401       5                                                       
HET    SO4  B 402       5                                                       
HET    SO4  C1001       5                                                       
HET    SO4  D1001       5                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     SO4 SULFATE ION                                                      
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   2  PTR    3(C9 H12 N O6 P)                                             
FORMUL   8  SO4    6(O4 S 2-)                                                   
FORMUL  14  HOH   *442(H2 O)                                                    
HELIX    1 AA1 GLU A  227  VAL A  238  1                                  12    
HELIX    2 AA2 THR A  248  SER A  259  1                                  12    
HELIX    3 AA3 SER A  269  ASP A  274  1                                   6    
HELIX    4 AA4 GLY A  324  LEU A  344  1                                  21    
HELIX    5 AA5 GLU B  227  VAL B  238  1                                  12    
HELIX    6 AA6 THR B  248  SER B  259  1                                  12    
HELIX    7 AA7 SER B  269  ASP B  274  1                                   6    
HELIX    8 AA8 GLY B  324  ALA B  343  1                                  20    
HELIX    9 AA9 GLU C  227  VAL C  238  1                                  12    
HELIX   10 AB1 THR C  248  SER C  257  1                                  10    
HELIX   11 AB2 SER C  269  SER C  273  5                                   5    
HELIX   12 AB3 GLY C  324  LEU C  344  1                                  21    
HELIX   13 AB4 LYS D  228  ASP D  239  1                                  12    
HELIX   14 AB5 THR D  248  SER D  259  1                                  12    
HELIX   15 AB6 SER D  269  ASP D  274  1                                   6    
HELIX   16 AB7 GLY D  324  LEU D  344  1                                  21    
SHEET    1 AA1 5 ILE A 264  TRP A 267  0                                        
SHEET    2 AA1 5 TYR A 279  ALA A 288 -1  O  SER A 285   N  ILE A 264           
SHEET    3 AA1 5 GLY A 291  ASN A 300 -1  O  TYR A 297   N  ILE A 282           
SHEET    4 AA1 5 LEU A 305  ILE A 308 -1  O  ILE A 308   N  ARG A 296           
SHEET    5 AA1 5 VAL A 315  ILE A 318 -1  O  THR A 316   N  SER A 307           
SHEET    1 AA2 5 ILE B 264  TRP B 267  0                                        
SHEET    2 AA2 5 VAL B 280  GLN B 287 -1  O  ALA B 283   N  ARG B 266           
SHEET    3 AA2 5 ILE B 292  ILE B 299 -1  O  TYR B 297   N  ILE B 282           
SHEET    4 AA2 5 LEU B 305  ILE B 308 -1  O  ILE B 308   N  ARG B 296           
SHEET    5 AA2 5 VAL B 315  ILE B 318 -1  O  THR B 316   N  SER B 307           
SHEET    1 AA3 5 ILE C 264  TRP C 267  0                                        
SHEET    2 AA3 5 VAL C 280  ALA C 288 -1  O  ALA C 283   N  ARG C 266           
SHEET    3 AA3 5 GLY C 291  ILE C 299 -1  O  TYR C 297   N  ILE C 282           
SHEET    4 AA3 5 LEU C 305  ILE C 308 -1  O  PHE C 306   N  GLY C 298           
SHEET    5 AA3 5 VAL C 315  ILE C 318 -1  O  ILE C 318   N  LEU C 305           
SHEET    1 AA4 5 ILE D 264  TRP D 267  0                                        
SHEET    2 AA4 5 TYR D 279  GLN D 287 -1  O  ALA D 283   N  ARG D 266           
SHEET    3 AA4 5 ILE D 292  ASN D 300 -1  O  TYR D 297   N  ILE D 282           
SHEET    4 AA4 5 LEU D 305  ILE D 308 -1  O  PHE D 306   N  GLY D 298           
SHEET    5 AA4 5 VAL D 315  ILE D 318 -1  O  ILE D 318   N  LEU D 305           
LINK         C   SER E 903                 N   PTR E 904     1555   1555  1.33  
LINK         C   PTR E 904                 N   VAL E 905     1555   1555  1.33  
LINK         C   SER G 903                 N   PTR G 904     1555   1555  1.33  
LINK         C   PTR G 904                 N   VAL G 905     1555   1555  1.33  
LINK         C   SER H 903                 N   PTR H 904     1555   1555  1.33  
LINK         C   PTR H 904                 N   VAL H 905     1555   1555  1.33  
SITE     1 AC1  4 ARG A 240  HIS A 241  GLU A 262  HOH A1150                    
SITE     1 AC2  7 LYS A 243  TYR A 255  SER A 259  HOH A1109                    
SITE     2 AC2  7 HOH A1174  LYS C 243  TYR C 255                               
SITE     1 AC3  8 ARG B 266  SER B 268  SER B 269  ARG B 296                    
SITE     2 AC3  8 HOH B 515  ASN D 309  SER D 312  HOH D1108                    
SITE     1 AC4  7 ARG B 240  HIS B 241  ALA B 261  GLU B 262                    
SITE     2 AC4  7 HOH B 501  HOH B 535  LYS C 253                               
SITE     1 AC5  6 ARG C 240  HIS C 241  ALA C 261  GLU C 262                    
SITE     2 AC5  6 PHE C 263  HOH C1162                                          
SITE     1 AC6  5 LYS A 253  ARG D 240  HIS D 241  ALA D 261                    
SITE     2 AC6  5 GLU D 262                                                     
SITE     1 AC7 12 ARG A 266  SER A 268  SER A 269  SER A 294                    
SITE     2 AC7 12 ILE A 295  ARG A 296  THR A 310  HOH A1144                    
SITE     3 AC7 12 PRO E 902  SER E 903  ASN E 906  HOH E1002                    
SITE     1 AC8 14 ARG C 266  SER C 268  SER C 269  ALA C 283                    
SITE     2 AC8 14 SER C 294  ILE C 295  ARG C 296  THR C 310                    
SITE     3 AC8 14 HOH C1125  PRO G 902  SER G 903  ASN G 906                    
SITE     4 AC8 14 HOH G1001  HOH G1002                                          
SITE     1 AC9 11 ARG D 266  SER D 268  SER D 269  SER D 294                    
SITE     2 AC9 11 ARG D 296  THR D 310  SER H 903  ASN H 906                    
SITE     3 AC9 11 HOH H1102  HOH H1104  HOH H1105                               
CRYST1   44.454   45.035   74.748  72.60  90.14  77.55 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022495 -0.004966  0.001659        0.00000                         
SCALE2      0.000000  0.022740 -0.007331        0.00000                         
SCALE3      0.000000  0.000000  0.014056        0.00000                         
ATOM      1  N   SER A 226     -19.706  20.554 -38.969  1.00 99.41           N  
ANISOU    1  N   SER A 226    11330  18220   8222   2643     -7   2973       N  
ATOM      2  CA  SER A 226     -20.576  19.582 -39.620  1.00 97.96           C  
ANISOU    2  CA  SER A 226    10862  17908   8449   2540    263   3363       C  
ATOM      3  C   SER A 226     -21.347  20.220 -40.776  1.00 93.13           C  
ANISOU    3  C   SER A 226    10183  17122   8079   2616    454   3135       C  
ATOM      4  O   SER A 226     -21.939  19.527 -41.605  1.00 91.32           O  
ANISOU    4  O   SER A 226     9765  16641   8292   2495    594   3402       O  
ATOM      5  CB  SER A 226     -21.547  18.974 -38.605  1.00104.08           C  
ANISOU    5  CB  SER A 226    11524  19073   8949   2560    502   3716       C  
ATOM      6  OG  SER A 226     -22.426  18.051 -39.222  1.00103.27           O  
ANISOU    6  OG  SER A 226    11132  18809   9296   2432    693   4102       O  
ATOM      7  N   GLU A 227     -21.331  21.551 -40.831  1.00 90.11           N  
ANISOU    7  N   GLU A 227     9987  16829   7424   2800    415   2627       N  
ATOM      8  CA  GLU A 227     -22.022  22.296 -41.873  1.00 83.25           C  
ANISOU    8  CA  GLU A 227     9089  15800   6741   2877    553   2367       C  
ATOM      9  C   GLU A 227     -21.060  23.032 -42.794  1.00 73.73           C  
ANISOU    9  C   GLU A 227     8015  14263   5737   2841    257   1995       C  
ATOM     10  O   GLU A 227     -21.499  23.837 -43.624  1.00 68.22           O  
ANISOU   10  O   GLU A 227     7347  13413   5160   2893    299   1688       O  
ATOM     11  CB  GLU A 227     -23.013  23.285 -41.252  1.00 89.07           C  
ANISOU   11  CB  GLU A 227     9904  16861   7077   3131    765   2048       C  
ATOM     12  CG  GLU A 227     -22.368  24.515 -40.627  1.00 93.60           C  
ANISOU   12  CG  GLU A 227    10796  17534   7234   3302    522   1476       C  
ATOM     13  CD  GLU A 227     -23.382  25.411 -39.940  1.00 99.85           C  
ANISOU   13  CD  GLU A 227    11685  18582   7670   3576    743   1160       C  
ATOM     14  OE1 GLU A 227     -24.463  24.908 -39.567  1.00103.29           O  
ANISOU   14  OE1 GLU A 227    11929  19244   8073   3633   1085   1483       O  
ATOM     15  OE2 GLU A 227     -23.099  26.617 -39.775  1.00101.53           O  
ANISOU   15  OE2 GLU A 227    12162  18730   7685   3726    546    602       O  
ATOM     16  N   LYS A 228     -19.757  22.770 -42.676  1.00 70.39           N  
ANISOU   16  N   LYS A 228     7640  13678   5428   2724    -58   2021       N  
ATOM     17  CA  LYS A 228     -18.790  23.498 -43.487  1.00 65.14           C  
ANISOU   17  CA  LYS A 228     7035  12684   5032   2671   -362   1689       C  
ATOM     18  C   LYS A 228     -18.931  23.174 -44.969  1.00 56.98           C  
ANISOU   18  C   LYS A 228     5861  11198   4591   2539   -257   1758       C  
ATOM     19  O   LYS A 228     -18.514  23.974 -45.813  1.00 55.52           O  
ANISOU   19  O   LYS A 228     5717  10687   4692   2462   -384   1396       O  
ATOM     20  CB  LYS A 228     -17.373  23.210 -42.994  1.00 66.43           C  
ANISOU   20  CB  LYS A 228     7220  12749   5272   2555   -697   1774       C  
ATOM     21  CG  LYS A 228     -17.173  23.591 -41.536  1.00 73.14           C  
ANISOU   21  CG  LYS A 228     8281  13944   5565   2638   -864   1669       C  
ATOM     22  CD  LYS A 228     -17.503  25.062 -41.370  1.00 75.19           C  
ANISOU   22  CD  LYS A 228     8775  14289   5506   2797   -960   1103       C  
ATOM     23  CE  LYS A 228     -17.817  25.413 -39.931  1.00 81.35           C  
ANISOU   23  CE  LYS A 228     9814  15432   5664   2946   -964    976       C  
ATOM     24  NZ  LYS A 228     -18.142  24.234 -39.096  1.00 84.46           N  
ANISOU   24  NZ  LYS A 228    10124  16114   5852   2921   -748   1465       N  
ATOM     25  N   ILE A 229     -19.534  22.032 -45.311  1.00 54.15           N  
ANISOU   25  N   ILE A 229     5368  10740   4464   2464    -29   2192       N  
ATOM     26  CA  ILE A 229     -19.754  21.717 -46.722  1.00 51.28           C  
ANISOU   26  CA  ILE A 229     4961   9858   4665   2309     74   2198       C  
ATOM     27  C   ILE A 229     -20.680  22.743 -47.361  1.00 49.71           C  
ANISOU   27  C   ILE A 229     4828   9534   4524   2298    194   1820       C  
ATOM     28  O   ILE A 229     -20.478  23.151 -48.511  1.00 46.59           O  
ANISOU   28  O   ILE A 229     4485   8720   4495   2171    146   1578       O  
ATOM     29  CB  ILE A 229     -20.297  20.285 -46.884  1.00 52.17           C  
ANISOU   29  CB  ILE A 229     4982   9814   5028   2188    239   2693       C  
ATOM     30  CG1 ILE A 229     -20.557  19.984 -48.365  1.00 48.71           C  
ANISOU   30  CG1 ILE A 229     4591   8811   5107   2038    296   2663       C  
ATOM     31  CG2 ILE A 229     -21.560  20.085 -46.055  1.00 54.69           C  
ANISOU   31  CG2 ILE A 229     5210  10527   5042   2245    456   2949       C  
ATOM     32  CD1 ILE A 229     -20.936  18.552 -48.633  1.00 49.80           C  
ANISOU   32  CD1 ILE A 229     4717   8648   5558   1856    370   3025       C  
ATOM     33  N   TYR A 230     -21.708  23.182 -46.633  1.00 51.76           N  
ANISOU   33  N   TYR A 230     5080  10161   4425   2440    360   1776       N  
ATOM     34  CA  TYR A 230     -22.632  24.153 -47.207  1.00 50.93           C  
ANISOU   34  CA  TYR A 230     5002   9922   4427   2453    462   1435       C  
ATOM     35  C   TYR A 230     -21.971  25.511 -47.397  1.00 48.59           C  
ANISOU   35  C   TYR A 230     4861   9510   4090   2485    210    858       C  
ATOM     36  O   TYR A 230     -22.315  26.239 -48.332  1.00 46.35           O  
ANISOU   36  O   TYR A 230     4612   8893   4104   2389    176    575       O  
ATOM     37  CB  TYR A 230     -23.878  24.271 -46.333  1.00 57.33           C  
ANISOU   37  CB  TYR A 230     5720  11182   4882   2651    745   1550       C  
ATOM     38  CG  TYR A 230     -24.577  22.950 -46.127  1.00 61.31           C  
ANISOU   38  CG  TYR A 230     6025  11811   5460   2582    964   2197       C  
ATOM     39  CD1 TYR A 230     -25.200  22.300 -47.186  1.00 59.96           C  
ANISOU   39  CD1 TYR A 230     5754  11208   5819   2364   1011   2474       C  
ATOM     40  CD2 TYR A 230     -24.605  22.346 -44.879  1.00 67.54           C  
ANISOU   40  CD2 TYR A 230     6749  13128   5787   2712   1074   2558       C  
ATOM     41  CE1 TYR A 230     -25.838  21.088 -47.001  1.00 63.56           C  
ANISOU   41  CE1 TYR A 230     6031  11729   6390   2274   1133   3100       C  
ATOM     42  CE2 TYR A 230     -25.238  21.135 -44.686  1.00 71.01           C  
ANISOU   42  CE2 TYR A 230     6973  13554   6453   2580   1181   3115       C  
ATOM     43  CZ  TYR A 230     -25.853  20.511 -45.750  1.00 68.80           C  
ANISOU   43  CZ  TYR A 230     6580  12852   6707   2373   1208   3404       C  
ATOM     44  OH  TYR A 230     -26.486  19.305 -45.556  1.00 72.59           O  
ANISOU   44  OH  TYR A 230     6845  13259   7478   2213   1233   3889       O  
ATOM     45  N   LYS A 231     -21.015  25.866 -46.537  1.00 50.30           N  
ANISOU   45  N   LYS A 231     5179   9968   3966   2590    -25    708       N  
ATOM     46  CA  LYS A 231     -20.305  27.124 -46.737  1.00 51.48           C  
ANISOU   46  CA  LYS A 231     5469   9955   4137   2579   -352    212       C  
ATOM     47  C   LYS A 231     -19.384  27.050 -47.951  1.00 46.29           C  
ANISOU   47  C   LYS A 231     4754   8830   4006   2326   -508    220       C  
ATOM     48  O   LYS A 231     -19.233  28.038 -48.680  1.00 43.58           O  
ANISOU   48  O   LYS A 231     4466   8207   3884   2226   -677   -121       O  
ATOM     49  CB  LYS A 231     -19.522  27.501 -45.481  1.00 58.75           C  
ANISOU   49  CB  LYS A 231     6537  11221   4564   2735   -633     82       C  
ATOM     50  CG  LYS A 231     -20.385  27.669 -44.238  1.00 66.97           C  
ANISOU   50  CG  LYS A 231     7700  12771   4975   3028   -455     23       C  
ATOM     51  CD  LYS A 231     -21.631  28.495 -44.525  1.00 69.73           C  
ANISOU   51  CD  LYS A 231     8068  13094   5333   3173   -232   -302       C  
ATOM     52  CE  LYS A 231     -21.302  29.953 -44.817  1.00 71.32           C  
ANISOU   52  CE  LYS A 231     8462  13030   5608   3199   -594   -904       C  
ATOM     53  NZ  LYS A 231     -22.485  30.655 -45.384  1.00 71.55           N  
ANISOU   53  NZ  LYS A 231     8445  12902   5837   3284   -398  -1166       N  
ATOM     54  N   VAL A 232     -18.764  25.890 -48.190  1.00 43.35           N  
ANISOU   54  N   VAL A 232     4267   8367   3839   2233   -447    614       N  
ATOM     55  CA  VAL A 232     -17.937  25.730 -49.383  1.00 40.91           C  
ANISOU   55  CA  VAL A 232     3899   7641   4004   2045   -500    638       C  
ATOM     56  C   VAL A 232     -18.805  25.736 -50.635  1.00 39.65           C  
ANISOU   56  C   VAL A 232     3785   7119   4161   1906   -301    585       C  
ATOM     57  O   VAL A 232     -18.446  26.340 -51.653  1.00 37.19           O  
ANISOU   57  O   VAL A 232     3511   6492   4125   1754   -382    382       O  
ATOM     58  CB  VAL A 232     -17.092  24.446 -49.286  1.00 42.82           C  
ANISOU   58  CB  VAL A 232     4015   7865   4391   2044   -465   1056       C  
ATOM     59  CG1 VAL A 232     -16.235  24.272 -50.534  1.00 41.00           C  
ANISOU   59  CG1 VAL A 232     3724   7231   4625   1911   -445   1066       C  
ATOM     60  CG2 VAL A 232     -16.213  24.478 -48.041  1.00 45.69           C  
ANISOU   60  CG2 VAL A 232     4337   8564   4461   2147   -729   1137       C  
ATOM     61  N   MET A 233     -19.962  25.070 -50.579  1.00 40.28           N  
ANISOU   61  N   MET A 233     3858   7238   4211   1934    -66    805       N  
ATOM     62  CA  MET A 233     -20.883  25.083 -51.710  1.00 38.72           C  
ANISOU   62  CA  MET A 233     3721   6677   4315   1782     57    783       C  
ATOM     63  C   MET A 233     -21.395  26.488 -51.980  1.00 38.94           C  
ANISOU   63  C   MET A 233     3812   6639   4346   1757    -51    360       C  
ATOM     64  O   MET A 233     -21.523  26.896 -53.140  1.00 37.96           O  
ANISOU   64  O   MET A 233     3772   6129   4521   1566   -100    220       O  
ATOM     65  CB  MET A 233     -22.053  24.139 -51.449  1.00 41.36           C  
ANISOU   65  CB  MET A 233     3988   7087   4639   1807    268   1159       C  
ATOM     66  CG  MET A 233     -21.692  22.673 -51.541  1.00 47.45           C  
ANISOU   66  CG  MET A 233     4736   7744   5551   1771    324   1596       C  
ATOM     67  SD  MET A 233     -23.010  21.648 -50.875  1.00 55.33           S  
ANISOU   67  SD  MET A 233     5595   8945   6481   1799    496   2117       S  
ATOM     68  CE  MET A 233     -24.446  22.424 -51.605  1.00 54.08           C  
ANISOU   68  CE  MET A 233     5443   8583   6522   1692    569   1965       C  
ATOM     69  N   GLU A 234     -21.704  27.237 -50.919  1.00 35.31           N  
ANISOU   69  N   GLU A 234     3337   6538   3540   1957   -101    151       N  
ATOM     70  CA  GLU A 234     -22.107  28.631 -51.076  1.00 38.16           C  
ANISOU   70  CA  GLU A 234     3770   6817   3911   1979   -257   -294       C  
ATOM     71  C   GLU A 234     -21.052  29.416 -51.840  1.00 36.82           C  
ANISOU   71  C   GLU A 234     3675   6349   3964   1794   -559   -549       C  
ATOM     72  O   GLU A 234     -21.368  30.148 -52.785  1.00 37.41           O  
ANISOU   72  O   GLU A 234     3804   6093   4316   1628   -661   -747       O  
ATOM     73  CB  GLU A 234     -22.360  29.264 -49.702  1.00 40.84           C  
ANISOU   73  CB  GLU A 234     4143   7602   3773   2286   -288   -520       C  
ATOM     74  CG  GLU A 234     -23.007  30.652 -49.744  1.00 40.20           C  
ANISOU   74  CG  GLU A 234     4142   7436   3696   2389   -421   -993       C  
ATOM     75  CD  GLU A 234     -22.826  31.428 -48.439  1.00 47.26           C  
ANISOU   75  CD  GLU A 234     5180   8699   4078   2706   -569  -1336       C  
ATOM     76  OE1 GLU A 234     -21.709  31.400 -47.884  1.00 53.19           O  
ANISOU   76  OE1 GLU A 234     6026   9574   4608   2708   -815  -1356       O  
ATOM     77  OE2 GLU A 234     -23.791  32.061 -47.962  1.00 47.34           O  
ANISOU   77  OE2 GLU A 234     5217   8864   3904   2966   -450  -1584       O  
ATOM     78  N   GLU A 235     -19.785  29.268 -51.445  1.00 39.11           N  
ANISOU   78  N   GLU A 235     3945   6753   4163   1801   -722   -499       N  
ATOM     79  CA  GLU A 235     -18.708  30.015 -52.084  1.00 39.02           C  
ANISOU   79  CA  GLU A 235     3938   6508   4380   1621  -1013   -666       C  
ATOM     80  C   GLU A 235     -18.623  29.693 -53.571  1.00 35.61           C  
ANISOU   80  C   GLU A 235     3504   5682   4345   1369   -878   -537       C  
ATOM     81  O   GLU A 235     -18.377  30.582 -54.392  1.00 33.00           O  
ANISOU   81  O   GLU A 235     3209   5098   4232   1179  -1061   -724       O  
ATOM     82  CB  GLU A 235     -17.380  29.703 -51.390  1.00 43.84           C  
ANISOU   82  CB  GLU A 235     4462   7314   4883   1670  -1185   -519       C  
ATOM     83  CG  GLU A 235     -16.842  30.842 -50.535  1.00 52.70           C  
ANISOU   83  CG  GLU A 235     5656   8575   5793   1741  -1623   -824       C  
ATOM     84  CD  GLU A 235     -15.557  30.479 -49.809  1.00 60.07           C  
ANISOU   84  CD  GLU A 235     6493   9683   6647   1765  -1846   -620       C  
ATOM     85  OE1 GLU A 235     -15.612  29.675 -48.854  1.00 63.72           O  
ANISOU   85  OE1 GLU A 235     6963  10447   6803   1933  -1742   -420       O  
ATOM     86  OE2 GLU A 235     -14.488  31.001 -50.192  1.00 62.33           O  
ANISOU   86  OE2 GLU A 235     6709   9751   7221   1553  -2086   -600       O  
ATOM     87  N   ILE A 236     -18.837  28.429 -53.936  1.00 29.34           N  
ANISOU   87  N   ILE A 236     2699   4820   3630   1362   -582   -214       N  
ATOM     88  CA  ILE A 236     -18.733  28.029 -55.338  1.00 32.88           C  
ANISOU   88  CA  ILE A 236     3225   4886   4383   1157   -448   -110       C  
ATOM     89  C   ILE A 236     -19.964  28.470 -56.118  1.00 32.35           C  
ANISOU   89  C   ILE A 236     3298   4547   4448   1010   -436   -234       C  
ATOM     90  O   ILE A 236     -19.854  29.068 -57.195  1.00 31.88           O  
ANISOU   90  O   ILE A 236     3338   4189   4586    791   -525   -358       O  
ATOM     91  CB  ILE A 236     -18.514  26.506 -55.445  1.00 32.85           C  
ANISOU   91  CB  ILE A 236     3215   4844   4424   1226   -196    249       C  
ATOM     92  CG1 ILE A 236     -17.173  26.109 -54.826  1.00 34.85           C  
ANISOU   92  CG1 ILE A 236     3298   5305   4640   1349   -237    391       C  
ATOM     93  CG2 ILE A 236     -18.581  26.030 -56.909  1.00 32.78           C  
ANISOU   93  CG2 ILE A 236     3386   4408   4662   1054    -45    316       C  
ATOM     94  CD1 ILE A 236     -16.903  24.620 -54.881  1.00 35.22           C  
ANISOU   94  CD1 ILE A 236     3326   5286   4770   1448    -27    733       C  
ATOM     95  N   PHE A 237     -21.155  28.188 -55.587  1.00 32.62           N  
ANISOU   95  N   PHE A 237     3318   4686   4388   1117   -333   -162       N  
ATOM     96  CA  PHE A 237     -22.373  28.348 -56.373  1.00 30.62           C  
ANISOU   96  CA  PHE A 237     3160   4136   4339    967   -313   -170       C  
ATOM     97  C   PHE A 237     -22.762  29.806 -56.580  1.00 31.64           C  
ANISOU   97  C   PHE A 237     3305   4162   4555    895   -549   -528       C  
ATOM     98  O   PHE A 237     -23.514  30.101 -57.517  1.00 29.11           O  
ANISOU   98  O   PHE A 237     3081   3499   4481    693   -612   -552       O  
ATOM     99  CB  PHE A 237     -23.527  27.593 -55.715  1.00 31.03           C  
ANISOU   99  CB  PHE A 237     3116   4349   4324   1100   -130     91       C  
ATOM    100  CG  PHE A 237     -23.375  26.097 -55.760  1.00 32.63           C  
ANISOU  100  CG  PHE A 237     3339   4513   4547   1102     37    492       C  
ATOM    101  CD1 PHE A 237     -22.595  25.495 -56.733  1.00 33.11           C  
ANISOU  101  CD1 PHE A 237     3569   4255   4756    965     44    563       C  
ATOM    102  CD2 PHE A 237     -24.016  25.293 -54.830  1.00 37.03           C  
ANISOU  102  CD2 PHE A 237     3748   5349   4975   1252    185    807       C  
ATOM    103  CE1 PHE A 237     -22.455  24.117 -56.775  1.00 35.52           C  
ANISOU  103  CE1 PHE A 237     3923   4470   5105   1000    160    898       C  
ATOM    104  CE2 PHE A 237     -23.881  23.913 -54.866  1.00 37.79           C  
ANISOU  104  CE2 PHE A 237     3864   5363   5131   1237    272   1197       C  
ATOM    105  CZ  PHE A 237     -23.101  23.324 -55.837  1.00 36.46           C  
ANISOU  105  CZ  PHE A 237     3891   4825   5136   1121    241   1221       C  
ATOM    106  N   VAL A 238     -22.286  30.728 -55.738  1.00 31.68           N  
ANISOU  106  N   VAL A 238     2701   5763   3572    763     93   -743       N  
ATOM    107  CA  VAL A 238     -22.581  32.142 -55.970  1.00 38.70           C  
ANISOU  107  CA  VAL A 238     3512   6488   4704    708    272   -931       C  
ATOM    108  C   VAL A 238     -21.622  32.780 -56.961  1.00 36.38           C  
ANISOU  108  C   VAL A 238     3222   6064   4535    680    232  -1034       C  
ATOM    109  O   VAL A 238     -21.870  33.908 -57.405  1.00 34.81           O  
ANISOU  109  O   VAL A 238     3035   5631   4561    663    411  -1128       O  
ATOM    110  CB  VAL A 238     -22.555  32.987 -54.677  1.00 34.56           C  
ANISOU  110  CB  VAL A 238     2968   6110   4054    616    480  -1221       C  
ATOM    111  CG1 VAL A 238     -23.421  32.366 -53.589  1.00 35.87           C  
ANISOU  111  CG1 VAL A 238     3162   6423   4044    625    561  -1137       C  
ATOM    112  CG2 VAL A 238     -21.126  33.160 -54.182  1.00 39.68           C  
ANISOU  112  CG2 VAL A 238     3597   7036   4446    525    394  -1482       C  
ATOM    113  N   ASP A 239     -20.535  32.104 -57.313  1.00 30.45           N  
ANISOU  113  N   ASP A 239     2482   5442   3646    691     43  -1014       N  
ATOM    114  CA  ASP A 239     -19.511  32.716 -58.143  1.00 33.42           C  
ANISOU  114  CA  ASP A 239     2846   5734   4118    619     52  -1164       C  
ATOM    115  C   ASP A 239     -19.966  32.749 -59.598  1.00 32.60           C  
ANISOU  115  C   ASP A 239     2831   5305   4249    681     34   -945       C  
ATOM    116  O   ASP A 239     -20.653  31.841 -60.074  1.00 30.28           O  
ANISOU  116  O   ASP A 239     2572   4964   3968    771   -100   -684       O  
ATOM    117  CB  ASP A 239     -18.192  31.954 -58.019  1.00 32.09           C  
ANISOU  117  CB  ASP A 239     2605   5865   3722    643   -137  -1227       C  
ATOM    118  CG  ASP A 239     -17.046  32.648 -58.727  1.00 35.40           C  
ANISOU  118  CG  ASP A 239     2957   6262   4233    511    -78  -1462       C  
ATOM    119  OD1 ASP A 239     -16.349  33.457 -58.081  1.00 38.44           O  
ANISOU  119  OD1 ASP A 239     3219   6841   4544    335     34  -1819       O  
ATOM    120  OD2 ASP A 239     -16.854  32.400 -59.937  1.00 35.36           O  
ANISOU  120  OD2 ASP A 239     3027   6048   4362    546   -116  -1317       O  
ATOM    121  N   ARG A 240     -19.572  33.811 -60.306  1.00 35.51           N  
ANISOU  121  N   ARG A 240     3259   5453   4779    610    192  -1069       N  
ATOM    122  CA  ARG A 240     -20.010  33.981 -61.689  1.00 34.71           C  
ANISOU  122  CA  ARG A 240     3281   5058   4850    699    185   -850       C  
ATOM    123  C   ARG A 240     -19.493  32.884 -62.608  1.00 33.30           C  
ANISOU  123  C   ARG A 240     3136   4924   4591    724    -34   -691       C  
ATOM    124  O   ARG A 240     -20.094  32.642 -63.663  1.00 30.07           O  
ANISOU  124  O   ARG A 240     2814   4363   4248    806   -116   -467       O  
ATOM    125  CB  ARG A 240     -19.579  35.349 -62.221  1.00 38.91           C  
ANISOU  125  CB  ARG A 240     3950   5301   5533    623    461  -1002       C  
ATOM    126  CG  ARG A 240     -18.079  35.577 -62.255  1.00 43.50           C  
ANISOU  126  CG  ARG A 240     4513   5963   6050    404    545  -1293       C  
ATOM    127  CD  ARG A 240     -17.754  36.962 -62.800  1.00 49.42           C  
ANISOU  127  CD  ARG A 240     5464   6348   6966    279    907  -1449       C  
ATOM    128  NE  ARG A 240     -16.322  37.157 -62.996  1.00 52.93           N  
ANISOU  128  NE  ARG A 240     5864   6875   7371     14   1018  -1752       N  
ATOM    129  CZ  ARG A 240     -15.665  36.795 -64.093  1.00 53.49           C  
ANISOU  129  CZ  ARG A 240     5999   6883   7442     -4    972  -1665       C  
ATOM    130  NH1 ARG A 240     -16.311  36.215 -65.098  1.00 52.52           N  
ANISOU  130  NH1 ARG A 240     6016   6612   7326    218    799  -1288       N  
ATOM    131  NH2 ARG A 240     -14.360  37.011 -64.186  1.00 54.48           N  
ANISOU  131  NH2 ARG A 240     6026   7126   7546   -267   1109  -1988       N  
ATOM    132  N   HIS A 241     -18.399  32.213 -62.239  1.00 30.66           N  
ANISOU  132  N   HIS A 241     2730   4819   4100    676   -128   -808       N  
ATOM    133  CA  HIS A 241     -17.888  31.126 -63.062  1.00 31.14           C  
ANISOU  133  CA  HIS A 241     2844   4895   4094    730   -291   -666       C  
ATOM    134  C   HIS A 241     -18.777  29.892 -63.020  1.00 30.22           C  
ANISOU  134  C   HIS A 241     2781   4793   3908    825   -443   -414       C  
ATOM    135  O   HIS A 241     -18.679  29.051 -63.922  1.00 30.95           O  
ANISOU  135  O   HIS A 241     2978   4798   3982    848   -534   -275       O  
ATOM    136  CB  HIS A 241     -16.473  30.735 -62.631  1.00 34.09           C  
ANISOU  136  CB  HIS A 241     3091   5540   4322    723   -339   -854       C  
ATOM    137  CG  HIS A 241     -15.436  31.771 -62.933  1.00 37.19           C  
ANISOU  137  CG  HIS A 241     3409   5932   4790    553   -171  -1146       C  
ATOM    138  ND1 HIS A 241     -15.104  32.770 -62.044  1.00 40.09           N  
ANISOU  138  ND1 HIS A 241     3649   6437   5147    394    -21  -1459       N  
ATOM    139  CD2 HIS A 241     -14.652  31.959 -64.021  1.00 38.39           C  
ANISOU  139  CD2 HIS A 241     3611   5956   5021    473    -85  -1206       C  
ATOM    140  CE1 HIS A 241     -14.161  33.530 -62.571  1.00 41.60           C  
ANISOU  140  CE1 HIS A 241     3806   6576   5423    198    163  -1712       C  
ATOM    141  NE2 HIS A 241     -13.868  33.059 -63.770  1.00 40.43           N  
ANISOU  141  NE2 HIS A 241     3765   6265   5332    251    132  -1552       N  
ATOM    142  N   TYR A 242     -19.635  29.757 -62.010  1.00 28.13           N  
ANISOU  142  N   TYR A 242     2465   4621   3601    845   -430   -376       N  
ATOM    143  CA  TYR A 242     -20.492  28.581 -61.917  1.00 28.73           C  
ANISOU  143  CA  TYR A 242     2606   4693   3617    870   -506   -172       C  
ATOM    144  C   TYR A 242     -21.682  28.708 -62.862  1.00 30.98           C  
ANISOU  144  C   TYR A 242     2889   4828   4057    827   -527    -43       C  
ATOM    145  O   TYR A 242     -22.434  29.684 -62.797  1.00 29.08           O  
ANISOU  145  O   TYR A 242     2548   4556   3946    847   -453    -68       O  
ATOM    146  CB  TYR A 242     -20.987  28.366 -60.488  1.00 30.18           C  
ANISOU  146  CB  TYR A 242     2751   5039   3679    883   -443   -184       C  
ATOM    147  CG  TYR A 242     -21.704  27.047 -60.347  1.00 29.59           C  
ANISOU  147  CG  TYR A 242     2795   4925   3521    868   -453      9       C  
ATOM    148  CD1 TYR A 242     -20.991  25.855 -60.304  1.00 31.29           C  
ANISOU  148  CD1 TYR A 242     3187   5137   3565    955   -499    117       C  
ATOM    149  CD2 TYR A 242     -23.091  26.986 -60.308  1.00 27.72           C  
ANISOU  149  CD2 TYR A 242     2500   4643   3389    764   -382     73       C  
ATOM    150  CE1 TYR A 242     -21.637  24.639 -60.200  1.00 30.72           C  
ANISOU  150  CE1 TYR A 242     3300   4948   3424    909   -431    284       C  
ATOM    151  CE2 TYR A 242     -23.745  25.775 -60.204  1.00 29.69           C  
ANISOU  151  CE2 TYR A 242     2868   4840   3574    671   -333    202       C  
ATOM    152  CZ  TYR A 242     -23.012  24.605 -60.154  1.00 30.31           C  
ANISOU  152  CZ  TYR A 242     3192   4844   3479    728   -337    308       C  
ATOM    153  OH  TYR A 242     -23.652  23.392 -60.050  1.00 32.52           O  
ANISOU  153  OH  TYR A 242     3665   4995   3698    606   -212    427       O  
ATOM    154  N   LYS A 243     -21.868  27.699 -63.712  1.00 29.79           N  
ANISOU  154  N   LYS A 243     2839   4606   3874    782   -623     84       N  
ATOM    155  CA  LYS A 243     -22.908  27.685 -64.743  1.00 30.88           C  
ANISOU  155  CA  LYS A 243     2943   4693   4096    722   -698    179       C  
ATOM    156  C   LYS A 243     -23.921  26.596 -64.407  1.00 31.49           C  
ANISOU  156  C   LYS A 243     2996   4832   4135    590   -695    241       C  
ATOM    157  O   LYS A 243     -23.721  25.429 -64.755  1.00 32.68           O  
ANISOU  157  O   LYS A 243     3314   4909   4193    490   -707    281       O  
ATOM    158  CB  LYS A 243     -22.289  27.451 -66.119  1.00 28.86           C  
ANISOU  158  CB  LYS A 243     2836   4324   3806    702   -784    213       C  
ATOM    159  CG  LYS A 243     -21.169  28.410 -66.462  1.00 28.53           C  
ANISOU  159  CG  LYS A 243     2849   4196   3794    777   -723    130       C  
ATOM    160  CD  LYS A 243     -21.690  29.835 -66.536  1.00 31.60           C  
ANISOU  160  CD  LYS A 243     3165   4534   4309    860   -650    128       C  
ATOM    161  CE  LYS A 243     -20.562  30.818 -66.785  1.00 34.27           C  
ANISOU  161  CE  LYS A 243     3600   4736   4685    867   -502      7       C  
ATOM    162  NZ  LYS A 243     -21.076  32.200 -66.986  1.00 37.50           N  
ANISOU  162  NZ  LYS A 243     4039   4994   5215    968   -365     35       N  
ATOM    163  N   GLU A 244     -25.023  26.982 -63.749  1.00 29.14           N  
ANISOU  163  N   GLU A 244     2504   4649   3919    574   -634    229       N  
ATOM    164  CA  GLU A 244     -25.997  25.992 -63.301  1.00 31.47           C  
ANISOU  164  CA  GLU A 244     2759   5011   4187    394   -564    247       C  
ATOM    165  C   GLU A 244     -26.769  25.353 -64.449  1.00 34.07           C  
ANISOU  165  C   GLU A 244     3030   5384   4532    209   -672    257       C  
ATOM    166  O   GLU A 244     -27.334  24.270 -64.266  1.00 37.04           O  
ANISOU  166  O   GLU A 244     3452   5759   4863    -26   -580    235       O  
ATOM    167  CB  GLU A 244     -26.984  26.616 -62.308  1.00 34.19           C  
ANISOU  167  CB  GLU A 244     2870   5496   4626    412   -437    200       C  
ATOM    168  CG  GLU A 244     -27.869  27.705 -62.884  1.00 39.25           C  
ANISOU  168  CG  GLU A 244     3221   6252   5441    529   -507    193       C  
ATOM    169  CD  GLU A 244     -27.284  29.091 -62.697  1.00 42.65           C  
ANISOU  169  CD  GLU A 244     3667   6592   5945    765   -457    164       C  
ATOM    170  OE1 GLU A 244     -26.040  29.211 -62.645  1.00 42.35           O  
ANISOU  170  OE1 GLU A 244     3839   6428   5825    794   -454    131       O  
ATOM    171  OE2 GLU A 244     -28.070  30.057 -62.591  1.00 44.75           O  
ANISOU  171  OE2 GLU A 244     3731   6913   6358    916   -393    157       O  
ATOM    172  N   ASN A 245     -26.818  25.984 -65.618  1.00 32.93           N  
ANISOU  172  N   ASN A 245     2805   5285   4423    290   -844    278       N  
ATOM    173  CA  ASN A 245     -27.594  25.454 -66.729  1.00 38.14           C  
ANISOU  173  CA  ASN A 245     3368   6079   5044    112   -988    259       C  
ATOM    174  C   ASN A 245     -26.743  24.686 -67.733  1.00 38.93           C  
ANISOU  174  C   ASN A 245     3765   6018   5008      6  -1048    258       C  
ATOM    175  O   ASN A 245     -27.236  24.345 -68.815  1.00 38.82           O  
ANISOU  175  O   ASN A 245     3708   6127   4916   -145  -1187    218       O  
ATOM    176  CB  ASN A 245     -28.351  26.583 -67.430  1.00 41.89           C  
ANISOU  176  CB  ASN A 245     3563   6769   5586    307  -1158    309       C  
ATOM    177  CG  ASN A 245     -29.380  27.243 -66.525  1.00 46.69           C  
ANISOU  177  CG  ASN A 245     3836   7557   6347    416  -1074    292       C  
ATOM    178  OD1 ASN A 245     -29.421  28.470 -66.404  1.00 48.99           O  
ANISOU  178  OD1 ASN A 245     4042   7834   6738    716  -1057    359       O  
ATOM    179  ND2 ASN A 245     -30.219  26.431 -65.887  1.00 47.17           N  
ANISOU  179  ND2 ASN A 245     3730   7760   6434    162   -970    192       N  
ATOM    180  N   ILE A 246     -25.488  24.395 -67.399  1.00 36.67           N  
ANISOU  180  N   ILE A 246     3756   5499   4676     86   -945    281       N  
ATOM    181  CA  ILE A 246     -24.587  23.655 -68.276  1.00 37.06           C  
ANISOU  181  CA  ILE A 246     4092   5374   4617     25   -951    271       C  
ATOM    182  C   ILE A 246     -24.331  22.305 -67.627  1.00 40.46           C  
ANISOU  182  C   ILE A 246     4761   5626   4988    -97   -761    263       C  
ATOM    183  O   ILE A 246     -23.615  22.211 -66.622  1.00 41.31           O  
ANISOU  183  O   ILE A 246     4966   5650   5082     75   -650    318       O  
ATOM    184  CB  ILE A 246     -23.278  24.412 -68.526  1.00 34.82           C  
ANISOU  184  CB  ILE A 246     3915   4981   4334    253   -960    297       C  
ATOM    185  CG1 ILE A 246     -23.557  25.733 -69.242  1.00 34.52           C  
ANISOU  185  CG1 ILE A 246     3741   5034   4339    374  -1079    334       C  
ATOM    186  CG2 ILE A 246     -22.324  23.566 -69.354  1.00 36.59           C  
ANISOU  186  CG2 ILE A 246     4417   5028   4457    203   -920    273       C  
ATOM    187  CD1 ILE A 246     -22.307  26.490 -69.613  1.00 33.77           C  
ANISOU  187  CD1 ILE A 246     3781   4800   4249    518  -1024    328       C  
ATOM    188  N   ARG A 247     -24.915  21.250 -68.186  1.00 45.25           N  
ANISOU  188  N   ARG A 247     5482   6176   5534   -391   -705    191       N  
ATOM    189  CA  ARG A 247     -24.758  19.924 -67.597  1.00 51.16           C  
ANISOU  189  CA  ARG A 247     6539   6673   6228   -513   -449    199       C  
ATOM    190  C   ARG A 247     -24.145  18.853 -68.497  1.00 51.87           C  
ANISOU  190  C   ARG A 247     6991   6492   6226   -629   -338    150       C  
ATOM    191  O   ARG A 247     -23.319  18.063 -68.040  1.00 54.76           O  
ANISOU  191  O   ARG A 247     7679   6580   6545   -481   -138    234       O  
ATOM    192  CB  ARG A 247     -26.102  19.429 -67.052  1.00 58.38           C  
ANISOU  192  CB  ARG A 247     7335   7671   7176   -830   -315    122       C  
ATOM    193  CG  ARG A 247     -26.732  20.351 -66.021  1.00 63.79           C  
ANISOU  193  CG  ARG A 247     7694   8589   7956   -712   -348    161       C  
ATOM    194  CD  ARG A 247     -25.998  20.278 -64.692  1.00 67.04           C  
ANISOU  194  CD  ARG A 247     8297   8858   8317   -458   -188    298       C  
ATOM    195  NE  ARG A 247     -26.905  20.006 -63.581  1.00 72.71           N  
ANISOU  195  NE  ARG A 247     8966   9616   9044   -605     23    295       N  
ATOM    196  CZ  ARG A 247     -27.580  18.872 -63.428  1.00 78.73           C  
ANISOU  196  CZ  ARG A 247     9916  10223   9775   -936    286    248       C  
ATOM    197  NH1 ARG A 247     -27.451  17.896 -64.316  1.00 81.26           N  
ANISOU  197  NH1 ARG A 247    10493  10327  10053  -1158    367    183       N  
ATOM    198  NH2 ARG A 247     -28.384  18.711 -62.386  1.00 81.87           N  
ANISOU  198  NH2 ARG A 247    10269  10660  10178  -1077    514    242       N  
ATOM    199  N   THR A 248     -24.539  18.814 -69.766  1.00 47.33           N  
ANISOU  199  N   THR A 248     6375   6006   5601   -866   -459     17       N  
ATOM    200  CA  THR A 248     -24.017  17.787 -70.648  1.00 45.56           C  
ANISOU  200  CA  THR A 248     6517   5514   5279  -1020   -316    -71       C  
ATOM    201  C   THR A 248     -22.722  18.243 -71.311  1.00 40.67           C  
ANISOU  201  C   THR A 248     6004   4820   4628   -728   -396    -14       C  
ATOM    202  O   THR A 248     -22.388  19.431 -71.334  1.00 38.06           O  
ANISOU  202  O   THR A 248     5445   4677   4340   -494   -587     58       O  
ATOM    203  CB  THR A 248     -25.047  17.440 -71.720  1.00 49.09           C  
ANISOU  203  CB  THR A 248     6886   6133   5635  -1470   -394   -292       C  
ATOM    204  OG1 THR A 248     -25.236  18.576 -72.574  1.00 45.79           O  
ANISOU  204  OG1 THR A 248     6173   6062   5163  -1373   -732   -288       O  
ATOM    205  CG2 THR A 248     -26.377  17.063 -71.071  1.00 51.62           C  
ANISOU  205  CG2 THR A 248     7010   6598   6007  -1807   -303   -400       C  
ATOM    206  N   GLY A 249     -21.987  17.271 -71.858  1.00 40.82           N  
ANISOU  206  N   GLY A 249     6393   4534   4582   -759   -196    -64       N  
ATOM    207  CA  GLY A 249     -20.812  17.601 -72.647  1.00 38.44           C  
ANISOU  207  CA  GLY A 249     6186   4172   4247   -546   -229    -58       C  
ATOM    208  C   GLY A 249     -21.142  18.436 -73.867  1.00 36.55           C  
ANISOU  208  C   GLY A 249     5798   4177   3914   -686   -467   -140       C  
ATOM    209  O   GLY A 249     -20.364  19.314 -74.254  1.00 32.88           O  
ANISOU  209  O   GLY A 249     5268   3773   3453   -470   -554    -88       O  
ATOM    210  N   GLU A 250     -22.299  18.177 -74.484  1.00 38.85           N  
ANISOU  210  N   GLU A 250     6032   4631   4098  -1052   -563   -275       N  
ATOM    211  CA  GLU A 250     -22.749  18.991 -75.610  1.00 41.15           C  
ANISOU  211  CA  GLU A 250     6165   5230   4238  -1134   -836   -316       C  
ATOM    212  C   GLU A 250     -22.934  20.443 -75.196  1.00 37.56           C  
ANISOU  212  C   GLU A 250     5376   5021   3873   -839  -1056   -143       C  
ATOM    213  O   GLU A 250     -22.539  21.360 -75.925  1.00 35.40           O  
ANISOU  213  O   GLU A 250     5102   4826   3523   -676  -1174    -70       O  
ATOM    214  CB  GLU A 250     -24.054  18.424 -76.171  1.00 47.96           C  
ANISOU  214  CB  GLU A 250     6935   6335   4954  -1572   -933   -515       C  
ATOM    215  CG  GLU A 250     -24.651  19.198 -77.349  1.00 54.00           C  
ANISOU  215  CG  GLU A 250     7512   7516   5491  -1625  -1265   -545       C  
ATOM    216  CD  GLU A 250     -23.724  19.279 -78.549  1.00 56.80           C  
ANISOU  216  CD  GLU A 250     8182   7752   5646  -1576  -1247   -559       C  
ATOM    217  OE1 GLU A 250     -23.673  20.350 -79.192  1.00 57.20           O  
ANISOU  217  OE1 GLU A 250     8151   8013   5571  -1362  -1462   -424       O  
ATOM    218  OE2 GLU A 250     -23.051  18.271 -78.856  1.00 58.21           O  
ANISOU  218  OE2 GLU A 250     8723   7605   5790  -1740   -981   -700       O  
ATOM    219  N   GLU A 251     -23.521  20.672 -74.019  1.00 37.92           N  
ANISOU  219  N   GLU A 251     5179   5153   4076   -772  -1063    -78       N  
ATOM    220  CA  GLU A 251     -23.754  22.043 -73.577  1.00 36.23           C  
ANISOU  220  CA  GLU A 251     4672   5132   3960   -501  -1219     62       C  
ATOM    221  C   GLU A 251     -22.443  22.762 -73.287  1.00 32.53           C  
ANISOU  221  C   GLU A 251     4301   4480   3577   -198  -1127    155       C  
ATOM    222  O   GLU A 251     -22.326  23.968 -73.538  1.00 30.60           O  
ANISOU  222  O   GLU A 251     3963   4312   3351    -13  -1214    239       O  
ATOM    223  CB  GLU A 251     -24.677  22.048 -72.359  1.00 36.46           C  
ANISOU  223  CB  GLU A 251     4437   5286   4131   -527  -1200     74       C  
ATOM    224  CG  GLU A 251     -26.123  21.749 -72.738  1.00 41.08           C  
ANISOU  224  CG  GLU A 251     4773   6188   4650   -814  -1336    -41       C  
ATOM    225  CD  GLU A 251     -27.040  21.531 -71.548  1.00 44.71           C  
ANISOU  225  CD  GLU A 251     4992   6746   5251   -919  -1238    -74       C  
ATOM    226  OE1 GLU A 251     -26.537  21.225 -70.445  1.00 44.42           O  
ANISOU  226  OE1 GLU A 251     5099   6466   5312   -838  -1023    -16       O  
ATOM    227  OE2 GLU A 251     -28.274  21.648 -71.726  1.00 48.44           O  
ANISOU  227  OE2 GLU A 251     5118   7574   5714  -1079  -1374   -164       O  
ATOM    228  N   VAL A 252     -21.446  22.037 -72.759  1.00 31.66           N  
ANISOU  228  N   VAL A 252     4378   4137   3515   -140   -931    133       N  
ATOM    229  CA  VAL A 252     -20.118  22.610 -72.541  1.00 28.45           C  
ANISOU  229  CA  VAL A 252     4006   3632   3173    107   -845    159       C  
ATOM    230  C   VAL A 252     -19.495  23.046 -73.862  1.00 27.97           C  
ANISOU  230  C   VAL A 252     4091   3521   3015     98   -848    130       C  
ATOM    231  O   VAL A 252     -18.968  24.158 -73.984  1.00 28.27           O  
ANISOU  231  O   VAL A 252     4067   3576   3097    232   -840    158       O  
ATOM    232  CB  VAL A 252     -19.203  21.605 -71.810  1.00 29.20           C  
ANISOU  232  CB  VAL A 252     4244   3554   3296    219   -660    148       C  
ATOM    233  CG1 VAL A 252     -17.799  22.173 -71.686  1.00 29.25           C  
ANISOU  233  CG1 VAL A 252     4201   3557   3353    452   -594    122       C  
ATOM    234  CG2 VAL A 252     -19.757  21.264 -70.435  1.00 31.34           C  
ANISOU  234  CG2 VAL A 252     4423   3866   3619    260   -630    211       C  
ATOM    235  N   LYS A 253     -19.509  22.158 -74.861  1.00 29.24           N  
ANISOU  235  N   LYS A 253     4485   3594   3031    -86   -812     55       N  
ATOM    236  CA  LYS A 253     -18.975  22.522 -76.170  1.00 31.08           C  
ANISOU  236  CA  LYS A 253     4898   3789   3123   -117   -796     25       C  
ATOM    237  C   LYS A 253     -19.699  23.729 -76.748  1.00 31.40           C  
ANISOU  237  C   LYS A 253     4837   4022   3070    -82   -990    130       C  
ATOM    238  O   LYS A 253     -19.067  24.638 -77.299  1.00 30.60           O  
ANISOU  238  O   LYS A 253     4826   3864   2935     29   -930    180       O  
ATOM    239  CB  LYS A 253     -19.084  21.346 -77.143  1.00 33.19           C  
ANISOU  239  CB  LYS A 253     5440   3960   3209   -366   -731   -102       C  
ATOM    240  CG  LYS A 253     -18.306  20.110 -76.746  1.00 35.04           C  
ANISOU  240  CG  LYS A 253     5868   3925   3521   -348   -475   -184       C  
ATOM    241  CD  LYS A 253     -18.478  19.035 -77.808  1.00 39.34           C  
ANISOU  241  CD  LYS A 253     6732   4335   3880   -635   -364   -345       C  
ATOM    242  CE  LYS A 253     -17.943  17.689 -77.360  1.00 43.21           C  
ANISOU  242  CE  LYS A 253     7471   4494   4453   -609    -64   -408       C  
ATOM    243  NZ  LYS A 253     -18.279  16.627 -78.357  1.00 47.62           N  
ANISOU  243  NZ  LYS A 253     8371   4891   4833   -962     86   -610       N  
ATOM    244  N   GLN A 254     -21.027  23.746 -76.646  1.00 30.76           N  
ANISOU  244  N   GLN A 254     4575   4171   2943   -161  -1197    167       N  
ATOM    245  CA  GLN A 254     -21.792  24.879 -77.153  1.00 32.07           C  
ANISOU  245  CA  GLN A 254     4622   4552   3010    -33  -1396    305       C  
ATOM    246  C   GLN A 254     -21.421  26.166 -76.426  1.00 30.46           C  
ANISOU  246  C   GLN A 254     4315   4258   2999    242  -1313    427       C  
ATOM    247  O   GLN A 254     -21.336  27.232 -77.045  1.00 32.53           O  
ANISOU  247  O   GLN A 254     4677   4497   3186    405  -1315    554       O  
ATOM    248  CB  GLN A 254     -23.289  24.595 -77.026  1.00 35.91           C  
ANISOU  248  CB  GLN A 254     4834   5368   3443   -147  -1630    290       C  
ATOM    249  CG  GLN A 254     -24.183  25.685 -77.614  1.00 38.51           C  
ANISOU  249  CG  GLN A 254     5003   5991   3637     61  -1873    455       C  
ATOM    250  CD  GLN A 254     -23.991  25.888 -79.108  1.00 41.06           C  
ANISOU  250  CD  GLN A 254     5588   6388   3624     68  -1973    508       C  
ATOM    251  OE1 GLN A 254     -23.758  24.937 -79.859  1.00 39.95           O  
ANISOU  251  OE1 GLN A 254     5643   6250   3288   -210  -1961    348       O  
ATOM    252  NE2 GLN A 254     -24.093  27.136 -79.545  1.00 43.47           N  
ANISOU  252  NE2 GLN A 254     5941   6732   3842    394  -2038    738       N  
ATOM    253  N   TYR A 255     -21.179  26.086 -75.114  1.00 28.45           N  
ANISOU  253  N   TYR A 255     3903   3936   2972    288  -1209    383       N  
ATOM    254  CA  TYR A 255     -20.829  27.285 -74.357  1.00 30.78           C  
ANISOU  254  CA  TYR A 255     4099   4157   3440    488  -1104    434       C  
ATOM    255  C   TYR A 255     -19.537  27.910 -74.877  1.00 29.13           C  
ANISOU  255  C   TYR A 255     4100   3740   3227    528   -902    401       C  
ATOM    256  O   TYR A 255     -19.484  29.110 -75.166  1.00 29.14           O  
ANISOU  256  O   TYR A 255     4176   3654   3240    649   -821    486       O  
ATOM    257  CB  TYR A 255     -20.705  26.960 -72.865  1.00 27.85           C  
ANISOU  257  CB  TYR A 255     3541   3795   3246    498  -1032    357       C  
ATOM    258  CG  TYR A 255     -20.271  28.170 -72.075  1.00 30.56           C  
ANISOU  258  CG  TYR A 255     3791   4080   3742    645   -901    342       C  
ATOM    259  CD1 TYR A 255     -21.182  29.165 -71.742  1.00 33.53           C  
ANISOU  259  CD1 TYR A 255     4032   4511   4196    775   -932    429       C  
ATOM    260  CD2 TYR A 255     -18.945  28.348 -71.709  1.00 28.15           C  
ANISOU  260  CD2 TYR A 255     3521   3677   3497    646   -727    213       C  
ATOM    261  CE1 TYR A 255     -20.788  30.289 -71.045  1.00 33.57           C  
ANISOU  261  CE1 TYR A 255     4003   4413   4339    871   -756    379       C  
ATOM    262  CE2 TYR A 255     -18.546  29.469 -71.023  1.00 30.18           C  
ANISOU  262  CE2 TYR A 255     3693   3896   3876    704   -583    135       C  
ATOM    263  CZ  TYR A 255     -19.470  30.434 -70.692  1.00 33.27           C  
ANISOU  263  CZ  TYR A 255     4015   4282   4346    801   -580    214       C  
ATOM    264  OH  TYR A 255     -19.072  31.555 -70.004  1.00 35.51           O  
ANISOU  264  OH  TYR A 255     4261   4480   4753    823   -380    100       O  
ATOM    265  N   PHE A 256     -18.483  27.106 -75.013  1.00 28.16           N  
ANISOU  265  N   PHE A 256     4086   3521   3092    431   -779    274       N  
ATOM    266  CA  PHE A 256     -17.193  27.638 -75.431  1.00 28.54           C  
ANISOU  266  CA  PHE A 256     4268   3414   3162    433   -552    191       C  
ATOM    267  C   PHE A 256     -17.130  27.964 -76.911  1.00 33.80           C  
ANISOU  267  C   PHE A 256     5230   3988   3624    386   -511    264       C  
ATOM    268  O   PHE A 256     -16.120  28.520 -77.358  1.00 36.84           O  
ANISOU  268  O   PHE A 256     5757   4221   4018    359   -273    199       O  
ATOM    269  CB  PHE A 256     -16.098  26.650 -75.042  1.00 28.87           C  
ANISOU  269  CB  PHE A 256     4271   3436   3264    405   -435     32       C  
ATOM    270  CG  PHE A 256     -15.758  26.706 -73.582  1.00 28.03           C  
ANISOU  270  CG  PHE A 256     3896   3434   3319    503   -420    -44       C  
ATOM    271  CD1 PHE A 256     -15.986  25.618 -72.757  1.00 29.60           C  
ANISOU  271  CD1 PHE A 256     4016   3705   3525    556   -501    -31       C  
ATOM    272  CD2 PHE A 256     -15.216  27.858 -73.033  1.00 29.57           C  
ANISOU  272  CD2 PHE A 256     3952   3651   3633    526   -298   -138       C  
ATOM    273  CE1 PHE A 256     -15.677  25.679 -71.390  1.00 30.09           C  
ANISOU  273  CE1 PHE A 256     3856   3905   3674    675   -502    -80       C  
ATOM    274  CE2 PHE A 256     -14.894  27.923 -71.665  1.00 30.06           C  
ANISOU  274  CE2 PHE A 256     3755   3875   3792    596   -303   -242       C  
ATOM    275  CZ  PHE A 256     -15.134  26.832 -70.852  1.00 30.51           C  
ANISOU  275  CZ  PHE A 256     3729   4046   3816    691   -427   -196       C  
ATOM    276  N   SER A 257     -18.176  27.648 -77.675  1.00 33.55           N  
ANISOU  276  N   SER A 257     5286   4076   3387    361   -726    381       N  
ATOM    277  CA  SER A 257     -18.214  28.063 -79.071  1.00 37.93           C  
ANISOU  277  CA  SER A 257     6139   4596   3677    357   -720    484       C  
ATOM    278  C   SER A 257     -18.234  29.580 -79.195  1.00 40.95           C  
ANISOU  278  C   SER A 257     6627   4854   4077    546   -604    650       C  
ATOM    279  O   SER A 257     -17.668  30.131 -80.145  1.00 43.77           O  
ANISOU  279  O   SER A 257     7304   5047   4281    545   -418    707       O  
ATOM    280  CB  SER A 257     -19.434  27.453 -79.760  1.00 40.89           C  
ANISOU  280  CB  SER A 257     6513   5231   3793    298  -1028    551       C  
ATOM    281  OG  SER A 257     -19.570  27.942 -81.078  1.00 50.48           O  
ANISOU  281  OG  SER A 257     8013   6483   4686    345  -1070    684       O  
ATOM    282  N   LYS A 258     -18.870  30.269 -78.248  1.00 39.12           N  
ANISOU  282  N   LYS A 258     6176   4660   4028    705   -659    726       N  
ATOM    283  CA ALYS A 258     -19.002  31.721 -78.263  0.50 42.01           C  
ANISOU  283  CA ALYS A 258     6672   4851   4437    913   -503    888       C  
ATOM    284  CA BLYS A 258     -18.968  31.720 -78.284  0.50 42.00           C  
ANISOU  284  CA BLYS A 258     6680   4845   4434    908   -496    886       C  
ATOM    285  C   LYS A 258     -18.297  32.416 -77.109  1.00 40.19           C  
ANISOU  285  C   LYS A 258     6321   4434   4514    882   -228    733       C  
ATOM    286  O   LYS A 258     -17.888  33.571 -77.253  1.00 43.38           O  
ANISOU  286  O   LYS A 258     6945   4570   4969    936     65    772       O  
ATOM    287  CB ALYS A 258     -20.486  32.126 -78.228  0.50 44.71           C  
ANISOU  287  CB ALYS A 258     6876   5402   4711   1179   -774   1118       C  
ATOM    288  CB BLYS A 258     -20.443  32.153 -78.343  0.50 44.94           C  
ANISOU  288  CB BLYS A 258     6940   5419   4717   1180   -765   1128       C  
ATOM    289  CG ALYS A 258     -21.365  31.438 -79.262  0.50 47.92           C  
ANISOU  289  CG ALYS A 258     7291   6128   4787   1194  -1115   1230       C  
ATOM    290  CG BLYS A 258     -21.286  31.397 -79.374  0.50 47.94           C  
ANISOU  290  CG BLYS A 258     7327   6122   4765   1178  -1107   1226       C  
ATOM    291  CD ALYS A 258     -21.136  32.006 -80.648  0.50 50.94           C  
ANISOU  291  CD ALYS A 258     8099   6415   4840   1312  -1052   1424       C  
ATOM    292  CD BLYS A 258     -20.872  31.730 -80.800  0.50 50.64           C  
ANISOU  292  CD BLYS A 258     8106   6363   4773   1217  -1030   1366       C  
ATOM    293  CE ALYS A 258     -21.987  31.286 -81.682  0.50 54.08           C  
ANISOU  293  CE ALYS A 258     8484   7214   4850   1296  -1424   1490       C  
ATOM    294  CE BLYS A 258     -21.811  31.094 -81.828  0.50 53.88           C  
ANISOU  294  CE BLYS A 258     8504   7177   4790   1227  -1407   1451       C  
ATOM    295  NZ ALYS A 258     -21.501  31.544 -83.062  0.50 55.51           N  
ANISOU  295  NZ ALYS A 258     9135   7305   4653   1318  -1335   1618       N  
ATOM    296  NZ BLYS A 258     -21.610  29.621 -81.969  0.50 52.40           N  
ANISOU  296  NZ BLYS A 258     8231   7136   4543    848  -1506   1176       N  
ATOM    297  N   SER A 259     -18.156  31.755 -75.968  1.00 50.27           N  
ANISOU  297  N   SER A 259     6344   8246   4510  -1065  -1005   2190       N  
ATOM    298  CA  SER A 259     -17.615  32.412 -74.788  1.00 46.31           C  
ANISOU  298  CA  SER A 259     5541   7390   4664   -748   -742   2025       C  
ATOM    299  C   SER A 259     -16.098  32.539 -74.858  1.00 45.49           C  
ANISOU  299  C   SER A 259     5503   7240   4542   -530   -396   1727       C  
ATOM    300  O   SER A 259     -15.399  31.650 -75.355  1.00 45.67           O  
ANISOU  300  O   SER A 259     5911   7382   4062   -518   -315   1421       O  
ATOM    301  CB  SER A 259     -18.015  31.643 -73.533  1.00 43.04           C  
ANISOU  301  CB  SER A 259     5213   6733   4407   -669   -832   1663       C  
ATOM    302  OG  SER A 259     -17.390  32.178 -72.374  1.00 40.38           O  
ANISOU  302  OG  SER A 259     4639   6125   4578   -394   -585   1422       O  
ATOM    303  N   LYS A 260     -15.594  33.666 -74.358  1.00 45.09           N  
ANISOU  303  N   LYS A 260     5064   6998   5071   -365   -170   1826       N  
ATOM    304  CA  LYS A 260     -14.170  33.881 -74.157  1.00 44.18           C  
ANISOU  304  CA  LYS A 260     4898   6812   5075   -173    137   1564       C  
ATOM    305  C   LYS A 260     -13.765  33.727 -72.691  1.00 39.02           C  
ANISOU  305  C   LYS A 260     4158   5897   4772     -2    213   1121       C  
ATOM    306  O   LYS A 260     -12.679  34.170 -72.306  1.00 38.21           O  
ANISOU  306  O   LYS A 260     3879   5723   4918    118    432    962       O  
ATOM    307  CB  LYS A 260     -13.771  35.261 -74.679  1.00 48.00           C  
ANISOU  307  CB  LYS A 260     5002   7280   5955   -174    330   1986       C  
ATOM    308  CG  LYS A 260     -14.212  35.524 -76.119  1.00 55.60           C  
ANISOU  308  CG  LYS A 260     5976   8578   6573   -343    249   2535       C  
ATOM    309  CD  LYS A 260     -13.066  36.065 -76.962  1.00 59.88           C  
ANISOU  309  CD  LYS A 260     6409   9285   7058   -283    532   2734       C  
ATOM    310  CE  LYS A 260     -13.268  35.773 -78.445  1.00 65.22           C  
ANISOU  310  CE  LYS A 260     7292  10449   7041   -440    457   3090       C  
ATOM    311  NZ  LYS A 260     -11.966  35.586 -79.151  1.00 67.58           N  
ANISOU  311  NZ  LYS A 260     7719  10974   6986   -323    763   3003       N  
ATOM    312  N   ALA A 261     -14.619  33.113 -71.873  1.00 37.43           N  
ANISOU  312  N   ALA A 261     4051   5598   4573    -12     22    954       N  
ATOM    313  CA  ALA A 261     -14.311  32.916 -70.461  1.00 35.45           C  
ANISOU  313  CA  ALA A 261     3717   5183   4571    140     75    568       C  
ATOM    314  C   ALA A 261     -13.094  32.014 -70.294  1.00 34.95           C  
ANISOU  314  C   ALA A 261     3842   5212   4225    293    207    219       C  
ATOM    315  O   ALA A 261     -12.842  31.120 -71.104  1.00 35.23           O  
ANISOU  315  O   ALA A 261     4206   5372   3809    295    219    184       O  
ATOM    316  CB  ALA A 261     -15.509  32.305 -69.737  1.00 34.81           C  
ANISOU  316  CB  ALA A 261     3711   5038   4477    105   -146    532       C  
ATOM    317  N   GLU A 262     -12.335  32.243 -69.217  1.00 33.37           N  
ANISOU  317  N   GLU A 262     3429   4959   4291    420    320    -38       N  
ATOM    318  CA  GLU A 262     -11.144  31.428 -68.996  1.00 36.27           C  
ANISOU  318  CA  GLU A 262     3881   5450   4449    593    457   -274       C  
ATOM    319  C   GLU A 262     -11.510  30.028 -68.521  1.00 32.18           C  
ANISOU  319  C   GLU A 262     3653   4929   3647    690    352   -453       C  
ATOM    320  O   GLU A 262     -10.841  29.054 -68.881  1.00 34.44           O  
ANISOU  320  O   GLU A 262     4172   5268   3646    831    476   -547       O  
ATOM    321  CB  GLU A 262     -10.202  32.107 -68.001  1.00 41.60           C  
ANISOU  321  CB  GLU A 262     4193   6150   5465    644    563   -443       C  
ATOM    322  CG  GLU A 262      -9.389  33.255 -68.592  1.00 48.55           C  
ANISOU  322  CG  GLU A 262     4808   7030   6608    564    733   -282       C  
ATOM    323  CD  GLU A 262      -8.480  32.821 -69.737  1.00 55.14           C  
ANISOU  323  CD  GLU A 262     5765   8041   7146    667    921   -126       C  
ATOM    324  OE1 GLU A 262      -7.919  31.704 -69.679  1.00 56.59           O  
ANISOU  324  OE1 GLU A 262     6128   8350   7025    856    998   -257       O  
ATOM    325  OE2 GLU A 262      -8.328  33.604 -70.701  1.00 58.34           O  
ANISOU  325  OE2 GLU A 262     6078   8454   7636    580   1027    154       O  
ATOM    326  N   PHE A 263     -12.554  29.903 -67.707  1.00 29.05           N  
ANISOU  326  N   PHE A 263     3234   4446   3359    636    163   -482       N  
ATOM    327  CA  PHE A 263     -13.032  28.586 -67.308  1.00 28.78           C  
ANISOU  327  CA  PHE A 263     3458   4376   3100    694     51   -580       C  
ATOM    328  C   PHE A 263     -14.455  28.718 -66.800  1.00 27.08           C  
ANISOU  328  C   PHE A 263     3189   4081   3021    563   -171   -463       C  
ATOM    329  O   PHE A 263     -14.929  29.818 -66.512  1.00 28.20           O  
ANISOU  329  O   PHE A 263     3064   4188   3464    499   -184   -359       O  
ATOM    330  CB  PHE A 263     -12.136  27.943 -66.232  1.00 27.48           C  
ANISOU  330  CB  PHE A 263     3190   4298   2952    924    156   -778       C  
ATOM    331  CG  PHE A 263     -12.203  28.620 -64.885  1.00 30.15           C  
ANISOU  331  CG  PHE A 263     3172   4725   3557    938    108   -872       C  
ATOM    332  CD1 PHE A 263     -11.379  29.697 -64.592  1.00 33.33           C  
ANISOU  332  CD1 PHE A 263     3263   5223   4177    913    211   -957       C  
ATOM    333  CD2 PHE A 263     -13.073  28.163 -63.905  1.00 30.12           C  
ANISOU  333  CD2 PHE A 263     3155   4721   3568    956    -29   -890       C  
ATOM    334  CE1 PHE A 263     -11.432  30.316 -63.345  1.00 34.26           C  
ANISOU  334  CE1 PHE A 263     3108   5426   4482    880    174  -1126       C  
ATOM    335  CE2 PHE A 263     -13.135  28.782 -62.654  1.00 32.76           C  
ANISOU  335  CE2 PHE A 263     3197   5181   4071    969    -42  -1018       C  
ATOM    336  CZ  PHE A 263     -12.314  29.858 -62.378  1.00 35.07           C  
ANISOU  336  CZ  PHE A 263     3227   5560   4536    919     58  -1171       C  
ATOM    337  N   ILE A 264     -15.136  27.578 -66.703  1.00 27.86           N  
ANISOU  337  N   ILE A 264     3537   4120   2929    530   -315   -462       N  
ATOM    338  CA  ILE A 264     -16.406  27.508 -65.995  1.00 28.41           C  
ANISOU  338  CA  ILE A 264     3508   4147   3139    449   -506   -330       C  
ATOM    339  C   ILE A 264     -16.332  26.426 -64.930  1.00 29.14           C  
ANISOU  339  C   ILE A 264     3644   4237   3191    603   -511   -457       C  
ATOM    340  O   ILE A 264     -15.510  25.510 -64.986  1.00 29.37           O  
ANISOU  340  O   ILE A 264     3864   4240   3055    735   -404   -597       O  
ATOM    341  CB  ILE A 264     -17.594  27.236 -66.933  1.00 29.05           C  
ANISOU  341  CB  ILE A 264     3778   4184   3078    175   -744    -72       C  
ATOM    342  CG1 ILE A 264     -17.439  25.876 -67.631  1.00 30.09           C  
ANISOU  342  CG1 ILE A 264     4366   4235   2833     81   -801   -201       C  
ATOM    343  CG2 ILE A 264     -17.732  28.373 -67.905  1.00 29.93           C  
ANISOU  343  CG2 ILE A 264     3766   4358   3250     41   -743    160       C  
ATOM    344  CD1 ILE A 264     -18.646  25.467 -68.480  1.00 34.38           C  
ANISOU  344  CD1 ILE A 264     5118   4770   3175   -279  -1101     10       C  
ATOM    345  N   LEU A 265     -17.221  26.547 -63.956  1.00 27.89           N  
ANISOU  345  N   LEU A 265     3286   4109   3204    609   -605   -361       N  
ATOM    346  CA  LEU A 265     -17.528  25.487 -63.013  1.00 27.35           C  
ANISOU  346  CA  LEU A 265     3240   4052   3099    705   -659   -349       C  
ATOM    347  C   LEU A 265     -18.948  25.003 -63.273  1.00 29.17           C  
ANISOU  347  C   LEU A 265     3567   4174   3343    491   -889    -84       C  
ATOM    348  O   LEU A 265     -19.802  25.759 -63.752  1.00 28.28           O  
ANISOU  348  O   LEU A 265     3348   4061   3335    321   -997    123       O  
ATOM    349  CB  LEU A 265     -17.388  25.973 -61.570  1.00 25.65           C  
ANISOU  349  CB  LEU A 265     2687   4039   3021    884   -567   -432       C  
ATOM    350  CG  LEU A 265     -15.980  26.430 -61.189  1.00 29.22           C  
ANISOU  350  CG  LEU A 265     2992   4661   3450   1033   -393   -682       C  
ATOM    351  CD1 LEU A 265     -15.978  27.080 -59.830  1.00 30.36           C  
ANISOU  351  CD1 LEU A 265     2825   5040   3672   1113   -339   -811       C  
ATOM    352  CD2 LEU A 265     -15.036  25.249 -61.205  1.00 31.02           C  
ANISOU  352  CD2 LEU A 265     3362   4917   3506   1192   -327   -711       C  
ATOM    353  N   ARG A 266     -19.195  23.732 -62.977  1.00 30.02           N  
ANISOU  353  N   ARG A 266     3846   4185   3375    488   -964    -42       N  
ATOM    354  CA  ARG A 266     -20.481  23.149 -63.329  1.00 29.83           C  
ANISOU  354  CA  ARG A 266     3933   4044   3357    214  -1215    213       C  
ATOM    355  C   ARG A 266     -20.744  21.955 -62.436  1.00 30.10           C  
ANISOU  355  C   ARG A 266     3989   3999   3447    292  -1238    297       C  
ATOM    356  O   ARG A 266     -19.835  21.416 -61.798  1.00 30.15           O  
ANISOU  356  O   ARG A 266     4006   4014   3436    551  -1058    160       O  
ATOM    357  CB  ARG A 266     -20.527  22.720 -64.803  1.00 32.30           C  
ANISOU  357  CB  ARG A 266     4648   4198   3428    -84  -1348    160       C  
ATOM    358  CG  ARG A 266     -19.377  21.817 -65.206  1.00 31.41           C  
ANISOU  358  CG  ARG A 266     4911   3904   3118     34  -1161   -152       C  
ATOM    359  CD  ARG A 266     -19.430  21.468 -66.679  1.00 34.40           C  
ANISOU  359  CD  ARG A 266     5730   4156   3185   -271  -1253   -270       C  
ATOM    360  NE  ARG A 266     -18.298  20.644 -67.092  1.00 35.99           N  
ANISOU  360  NE  ARG A 266     6311   4153   3211   -106   -986   -590       N  
ATOM    361  CZ  ARG A 266     -18.208  19.339 -66.866  1.00 39.26           C  
ANISOU  361  CZ  ARG A 266     7016   4252   3649    -68   -909   -707       C  
ATOM    362  NH1 ARG A 266     -19.188  18.709 -66.229  1.00 38.54           N  
ANISOU  362  NH1 ARG A 266     6869   4036   3740   -219  -1115   -519       N  
ATOM    363  NH2 ARG A 266     -17.146  18.658 -67.285  1.00 42.71           N  
ANISOU  363  NH2 ARG A 266     7787   4474   3966    133   -595   -980       N  
ATOM    364  N   TRP A 267     -22.005  21.540 -62.414  1.00 32.19           N  
ANISOU  364  N   TRP A 267     4225   4206   3801     56  -1465    589       N  
ATOM    365  CA  TRP A 267     -22.398  20.356 -61.663  1.00 37.32           C  
ANISOU  365  CA  TRP A 267     4890   4742   4547     75  -1508    746       C  
ATOM    366  C   TRP A 267     -21.861  19.107 -62.364  1.00 37.12           C  
ANISOU  366  C   TRP A 267     5341   4358   4406    -32  -1494    549       C  
ATOM    367  O   TRP A 267     -22.183  18.854 -63.526  1.00 36.38           O  
ANISOU  367  O   TRP A 267     5580   4079   4164   -378  -1661    467       O  
ATOM    368  CB  TRP A 267     -23.918  20.326 -61.536  1.00 39.99           C  
ANISOU  368  CB  TRP A 267     5031   5121   5044   -187  -1760   1155       C  
ATOM    369  CG  TRP A 267     -24.496  19.295 -60.605  1.00 43.62           C  
ANISOU  369  CG  TRP A 267     5384   5519   5669   -164  -1799   1427       C  
ATOM    370  CD1 TRP A 267     -25.076  18.114 -60.963  1.00 46.96           C  
ANISOU  370  CD1 TRP A 267     6040   5648   6155   -476  -1997   1567       C  
ATOM    371  CD2 TRP A 267     -24.597  19.374 -59.174  1.00 44.69           C  
ANISOU  371  CD2 TRP A 267     5151   5906   5924    156  -1622   1598       C  
ATOM    372  NE1 TRP A 267     -25.519  17.448 -59.851  1.00 49.73           N  
ANISOU  372  NE1 TRP A 267     6156   6027   6712   -351  -1960   1880       N  
ATOM    373  CE2 TRP A 267     -25.232  18.194 -58.738  1.00 47.70           C  
ANISOU  373  CE2 TRP A 267     5532   6137   6454     47  -1697   1882       C  
ATOM    374  CE3 TRP A 267     -24.199  20.317 -58.219  1.00 42.81           C  
ANISOU  374  CE3 TRP A 267     4658   5974   5635    477  -1320   1412       C  
ATOM    375  CZ2 TRP A 267     -25.483  17.934 -57.391  1.00 49.07           C  
ANISOU  375  CZ2 TRP A 267     5436   6513   6694    270  -1450   1997       C  
ATOM    376  CZ3 TRP A 267     -24.449  20.057 -56.881  1.00 43.41           C  
ANISOU  376  CZ3 TRP A 267     4545   6214   5735    646  -1128   1479       C  
ATOM    377  CH2 TRP A 267     -25.084  18.875 -56.480  1.00 47.05           C  
ANISOU  377  CH2 TRP A 267     4989   6577   6309    558  -1179   1778       C  
ATOM    378  N   SER A 268     -21.026  18.344 -61.663  1.00 36.50           N  
ANISOU  378  N   SER A 268     5291   4193   4383    269  -1274    475       N  
ATOM    379  CA  SER A 268     -20.311  17.221 -62.257  1.00 37.35           C  
ANISOU  379  CA  SER A 268     5843   3909   4439    281  -1136    261       C  
ATOM    380  C   SER A 268     -21.226  16.028 -62.498  1.00 41.98           C  
ANISOU  380  C   SER A 268     6705   4101   5143    -49  -1313    385       C  
ATOM    381  O   SER A 268     -22.178  15.784 -61.749  1.00 43.71           O  
ANISOU  381  O   SER A 268     6668   4378   5562   -140  -1473    732       O  
ATOM    382  CB  SER A 268     -19.149  16.797 -61.352  1.00 36.35           C  
ANISOU  382  CB  SER A 268     5573   3837   4402    745   -825    256       C  
ATOM    383  OG  SER A 268     -18.652  15.515 -61.704  1.00 38.49           O  
ANISOU  383  OG  SER A 268     6225   3651   4749    807   -643    164       O  
ATOM    384  N   SER A 269     -20.900  15.260 -63.543  1.00 44.49           N  
ANISOU  384  N   SER A 269     7561   4006   5339   -234  -1258     86       N  
ATOM    385  CA  SER A 269     -21.633  14.038 -63.851  1.00 48.59           C  
ANISOU  385  CA  SER A 269     8432   4054   5977   -597  -1399    105       C  
ATOM    386  C   SER A 269     -21.534  13.001 -62.740  1.00 49.92           C  
ANISOU  386  C   SER A 269     8470   3979   6519   -335  -1226    362       C  
ATOM    387  O   SER A 269     -22.406  12.130 -62.639  1.00 52.23           O  
ANISOU  387  O   SER A 269     8866   3951   7026   -643  -1395    541       O  
ATOM    388  CB  SER A 269     -21.113  13.432 -65.156  1.00 54.35           C  
ANISOU  388  CB  SER A 269     9824   4365   6462   -797  -1279   -372       C  
ATOM    389  OG  SER A 269     -19.871  12.777 -64.951  1.00 56.18           O  
ANISOU  389  OG  SER A 269    10236   4306   6804   -342   -824   -553       O  
ATOM    390  N   ALA A 270     -20.491  13.066 -61.909  1.00 48.68           N  
ANISOU  390  N   ALA A 270     8059   3986   6450    204   -906    428       N  
ATOM    391  CA  ALA A 270     -20.297  12.062 -60.869  1.00 51.11           C  
ANISOU  391  CA  ALA A 270     8210   4109   7099    491   -715    743       C  
ATOM    392  C   ALA A 270     -21.353  12.125 -59.776  1.00 51.69           C  
ANISOU  392  C   ALA A 270     7815   4469   7356    429   -935   1234       C  
ATOM    393  O   ALA A 270     -21.453  11.180 -58.987  1.00 52.25           O  
ANISOU  393  O   ALA A 270     7767   4354   7731    569   -832   1575       O  
ATOM    394  CB  ALA A 270     -18.909  12.210 -60.245  1.00 48.61           C  
ANISOU  394  CB  ALA A 270     7657   4033   6779   1065   -358    763       C  
ATOM    395  N   ASN A 271     -22.137  13.203 -59.706  1.00 52.09           N  
ANISOU  395  N   ASN A 271     7581   4958   7253    250  -1194   1319       N  
ATOM    396  CA  ASN A 271     -23.134  13.319 -58.646  1.00 56.22           C  
ANISOU  396  CA  ASN A 271     7637   5789   7934    242  -1340   1797       C  
ATOM    397  C   ASN A 271     -24.255  12.299 -58.820  1.00 66.77           C  
ANISOU  397  C   ASN A 271     9109   6716   9545   -174  -1557   2068       C  
ATOM    398  O   ASN A 271     -24.709  11.696 -57.841  1.00 66.38           O  
ANISOU  398  O   ASN A 271     8771   6695   9756    -78  -1533   2518       O  
ATOM    399  CB  ASN A 271     -23.684  14.743 -58.605  1.00 51.53           C  
ANISOU  399  CB  ASN A 271     6728   5695   7154    183  -1494   1808       C  
ATOM    400  CG  ASN A 271     -22.687  15.728 -58.030  1.00 46.95           C  
ANISOU  400  CG  ASN A 271     5900   5556   6382    597  -1273   1628       C  
ATOM    401  OD1 ASN A 271     -22.240  15.580 -56.893  1.00 47.78           O  
ANISOU  401  OD1 ASN A 271     5714   5936   6506    941  -1102   1799       O  
ATOM    402  ND2 ASN A 271     -22.319  16.730 -58.817  1.00 43.17           N  
ANISOU  402  ND2 ASN A 271     5525   5170   5709    539  -1286   1300       N  
ATOM    403  N   GLU A 272     -24.709  12.089 -60.055  1.00 78.54           N  
ANISOU  403  N   GLU A 272    11025   7852  10965   -668  -1780   1817       N  
ATOM    404  CA  GLU A 272     -25.709  11.074 -60.358  1.00 86.28           C  
ANISOU  404  CA  GLU A 272    12198   8392  12192  -1166  -2022   2000       C  
ATOM    405  C   GLU A 272     -25.094   9.735 -60.747  1.00 91.60           C  
ANISOU  405  C   GLU A 272    13406   8343  13057  -1206  -1812   1743       C  
ATOM    406  O   GLU A 272     -25.808   8.727 -60.779  1.00 96.65           O  
ANISOU  406  O   GLU A 272    14195   8526  14000  -1574  -1946   1916       O  
ATOM    407  CB  GLU A 272     -26.620  11.558 -61.493  1.00 89.99           C  
ANISOU  407  CB  GLU A 272    12826   8919  12445  -1765  -2427   1885       C  
ATOM    408  CG  GLU A 272     -28.063  11.812 -61.084  1.00 95.09           C  
ANISOU  408  CG  GLU A 272    13005   9861  13265  -2070  -2767   2446       C  
ATOM    409  CD  GLU A 272     -28.854  12.537 -62.160  1.00 98.96           C  
ANISOU  409  CD  GLU A 272    13523  10572  13505  -2576  -3155   2419       C  
ATOM    410  OE1 GLU A 272     -28.635  13.754 -62.344  1.00 96.22           O  
ANISOU  410  OE1 GLU A 272    12985  10648  12926  -2371  -3115   2351       O  
ATOM    411  OE2 GLU A 272     -29.696  11.893 -62.822  1.00104.66           O  
ANISOU  411  OE2 GLU A 272    14434  11069  14264  -3183  -3497   2482       O  
ATOM    412  N   SER A 273     -23.789   9.699 -61.018  1.00 92.27           N  
ANISOU  412  N   SER A 273    13760   8288  13010   -828  -1459   1361       N  
ATOM    413  CA  SER A 273     -23.148   8.540 -61.626  1.00 98.03           C  
ANISOU  413  CA  SER A 273    15081   8280  13888   -853  -1192   1022       C  
ATOM    414  C   SER A 273     -22.912   7.400 -60.642  1.00101.53           C  
ANISOU  414  C   SER A 273    15396   8339  14841   -539   -910   1408       C  
ATOM    415  O   SER A 273     -23.693   6.445 -60.592  1.00107.01           O  
ANISOU  415  O   SER A 273    16227   8545  15888   -894  -1027   1595       O  
ATOM    416  CB  SER A 273     -21.822   8.955 -62.267  1.00 96.44           C  
ANISOU  416  CB  SER A 273    15152   8107  13383   -507   -866    545       C  
ATOM    417  OG  SER A 273     -20.986   7.834 -62.494  1.00101.04           O  
ANISOU  417  OG  SER A 273    16171   8022  14199   -291   -447    333       O  
ATOM    418  N   ASP A 274     -21.834   7.479 -59.867  1.00160.36           N  
ANISOU  418  N   ASP A 274    19568  17091  24270   -984   -553  -7383       N  
ATOM    419  CA  ASP A 274     -21.371   6.342 -59.081  1.00165.38           C  
ANISOU  419  CA  ASP A 274    19896  16819  26122   -339   -241  -7061       C  
ATOM    420  C   ASP A 274     -21.130   6.796 -57.641  1.00159.48           C  
ANISOU  420  C   ASP A 274    18990  16278  25325     -3    -84  -5690       C  
ATOM    421  O   ASP A 274     -21.619   7.844 -57.200  1.00152.13           O  
ANISOU  421  O   ASP A 274    18129  15990  23685   -304   -223  -4987       O  
ATOM    422  CB  ASP A 274     -20.130   5.733 -59.752  1.00171.73           C  
ANISOU  422  CB  ASP A 274    20564  17716  26970     77     28  -8114       C  
ATOM    423  CG  ASP A 274     -19.778   4.360 -59.207  1.00180.30           C  
ANISOU  423  CG  ASP A 274    21370  17588  29549    717    149  -8084       C  
ATOM    424  OD1 ASP A 274     -18.706   4.227 -58.580  1.00181.14           O  
ANISOU  424  OD1 ASP A 274    21249  17802  29776   1339    366  -7817       O  
ATOM    425  OD2 ASP A 274     -20.578   3.419 -59.394  1.00186.71           O  
ANISOU  425  OD2 ASP A 274    22209  17303  31430    590    -32  -8315       O  
ATOM    426  N   THR A 275     -20.367   5.992 -56.893  1.00163.09           N  
ANISOU  426  N   THR A 275    19232  16155  26581    623    158  -5332       N  
ATOM    427  CA  THR A 275     -20.090   6.176 -55.469  1.00158.19           C  
ANISOU  427  CA  THR A 275    18479  15519  26105    952    305  -4018       C  
ATOM    428  C   THR A 275     -21.374   6.169 -54.648  1.00153.83           C  
ANISOU  428  C   THR A 275    17947  14460  26043    508    164  -3083       C  
ATOM    429  O   THR A 275     -22.468   5.976 -55.189  1.00155.97           O  
ANISOU  429  O   THR A 275    18303  14336  26620      3    -58  -3491       O  
ATOM    430  CB  THR A 275     -19.305   7.468 -55.213  1.00151.21           C  
ANISOU  430  CB  THR A 275    17588  15989  23877   1067    462  -3626       C  
ATOM    431  OG1 THR A 275     -20.161   8.603 -55.398  1.00145.75           O  
ANISOU  431  OG1 THR A 275    17057  16035  22285    470    235  -3414       O  
ATOM    432  CG2 THR A 275     -18.110   7.572 -56.152  1.00154.77           C  
ANISOU  432  CG2 THR A 275    18013  17120  23672   1327    627  -4708       C  
ATOM    433  N   GLU A 276     -21.253   6.362 -53.332  1.00147.80           N  
ANISOU  433  N   GLU A 276    17082  13721  25355    650    302  -1868       N  
ATOM    434  CA  GLU A 276     -22.406   6.398 -52.437  1.00142.38           C  
ANISOU  434  CA  GLU A 276    16348  12700  25048    152    246   -983       C  
ATOM    435  C   GLU A 276     -22.269   7.595 -51.494  1.00132.87           C  
ANISOU  435  C   GLU A 276    15024  12519  22942    112    385    -11       C  
ATOM    436  O   GLU A 276     -22.068   7.440 -50.288  1.00133.60           O  
ANISOU  436  O   GLU A 276    15038  12427  23298    211    556   1023       O  
ATOM    437  CB  GLU A 276     -22.558   5.084 -51.671  1.00146.63           C  
ANISOU  437  CB  GLU A 276    16914  11923  26876    206    247   -452       C  
ATOM    438  CG  GLU A 276     -22.989   3.911 -52.545  1.00152.14           C  
ANISOU  438  CG  GLU A 276    17721  11523  28562    122     43  -1366       C  
ATOM    439  CD  GLU A 276     -24.275   4.177 -53.317  1.00148.82           C  
ANISOU  439  CD  GLU A 276    17318  11188  28040   -531   -125  -1972       C  
ATOM    440  OE1 GLU A 276     -24.456   3.567 -54.391  1.00154.03           O  
ANISOU  440  OE1 GLU A 276    18069  11352  29105   -555   -279  -3002       O  
ATOM    441  OE2 GLU A 276     -25.113   4.977 -52.849  1.00142.28           O  
ANISOU  441  OE2 GLU A 276    16385  10900  26775  -1016   -130  -1472       O  
ATOM    442  N   ASN A 277     -22.364   8.790 -52.072  1.00125.04           N  
ANISOU  442  N   ASN A 277    14052  12591  20867    -65    260   -361       N  
ATOM    443  CA  ASN A 277     -22.565  10.040 -51.340  1.00117.32           C  
ANISOU  443  CA  ASN A 277    12942  12584  19048   -236    262    393       C  
ATOM    444  C   ASN A 277     -21.501  10.260 -50.264  1.00112.80           C  
ANISOU  444  C   ASN A 277    12279  12390  18188    246    589   1348       C  
ATOM    445  O   ASN A 277     -21.790  10.356 -49.070  1.00108.94           O  
ANISOU  445  O   ASN A 277    11628  11880  17886    114    738   2340       O  
ATOM    446  CB  ASN A 277     -23.971  10.085 -50.735  1.00118.71           C  
ANISOU  446  CB  ASN A 277    12920  12480  19702   -838    151    789       C  
ATOM    447  CG  ASN A 277     -24.472  11.503 -50.533  1.00112.83           C  
ANISOU  447  CG  ASN A 277    12015  12780  18073  -1121    -61    988       C  
ATOM    448  OD1 ASN A 277     -24.439  12.034 -49.422  1.00109.48           O  
ANISOU  448  OD1 ASN A 277    11362  12823  17414  -1132    125   1870       O  
ATOM    449  ND2 ASN A 277     -24.939  12.125 -51.610  1.00112.15           N  
ANISOU  449  ND2 ASN A 277    12062  13042  17507  -1368   -511    149       N  
ATOM    450  N   LYS A 278     -20.250  10.346 -50.709  1.00103.27           N  
ANISOU  450  N   LYS A 278    11165  11577  16496    767    706    988       N  
ATOM    451  CA  LYS A 278     -19.177  10.831 -49.853  1.00 97.94           C  
ANISOU  451  CA  LYS A 278    10405  11510  15296   1234    967   1767       C  
ATOM    452  C   LYS A 278     -18.693  12.217 -50.244  1.00 85.65           C  
ANISOU  452  C   LYS A 278     8905  11301  12339   1238    921   1621       C  
ATOM    453  O   LYS A 278     -18.216  12.959 -49.383  1.00 81.67           O  
ANISOU  453  O   LYS A 278     8301  11476  11253   1426   1077   2452       O  
ATOM    454  CB  LYS A 278     -17.990   9.856 -49.863  1.00112.29           C  
ANISOU  454  CB  LYS A 278    12221  12750  17692   1890   1136   1543       C  
ATOM    455  CG  LYS A 278     -16.868  10.241 -48.902  1.00 85.45           C  
ANISOU  455  CG  LYS A 278     8720   9849  13897   2412   1377   2375       C  
ATOM    456  CD  LYS A 278     -15.939   9.078 -48.588  1.00 95.25           C  
ANISOU  456  CD  LYS A 278     9920  10167  16102   3038   1416   2361       C  
ATOM    457  CE  LYS A 278     -14.591   9.577 -48.080  1.00 90.28           C  
ANISOU  457  CE  LYS A 278     9173  10245  14883   3646   1624   2725       C  
ATOM    458  NZ  LYS A 278     -14.738  10.667 -47.070  1.00 81.79           N  
ANISOU  458  NZ  LYS A 278     8075  10016  12988   3455   1767   3901       N  
ATOM    459  N   TYR A 279     -18.827  12.590 -51.513  1.00 50.02           N  
ANISOU  459  N   TYR A 279     7115   6093   5796   1568   -149   1526       N  
ATOM    460  CA  TYR A 279     -18.458  13.914 -51.983  1.00 45.79           C  
ANISOU  460  CA  TYR A 279     6321   5837   5240   1570   -207   1218       C  
ATOM    461  C   TYR A 279     -19.619  14.534 -52.743  1.00 45.65           C  
ANISOU  461  C   TYR A 279     6111   5766   5470   1233   -183   1197       C  
ATOM    462  O   TYR A 279     -20.460  13.832 -53.309  1.00 49.50           O  
ANISOU  462  O   TYR A 279     6669   5974   6164    975   -211   1342       O  
ATOM    463  CB  TYR A 279     -17.237  13.881 -52.913  1.00 45.89           C  
ANISOU  463  CB  TYR A 279     6375   5833   5229   1731   -366    963       C  
ATOM    464  CG  TYR A 279     -15.996  13.266 -52.319  1.00 47.97           C  
ANISOU  464  CG  TYR A 279     6766   6185   5275   2105   -411    999       C  
ATOM    465  CD1 TYR A 279     -15.756  11.903 -52.423  1.00 51.07           C  
ANISOU  465  CD1 TYR A 279     7472   6249   5685   2256   -417   1159       C  
ATOM    466  CD2 TYR A 279     -15.055  14.050 -51.673  1.00 47.72           C  
ANISOU  466  CD2 TYR A 279     6547   6558   5027   2305   -464    882       C  
ATOM    467  CE1 TYR A 279     -14.618  11.335 -51.884  1.00 53.18           C  
ANISOU  467  CE1 TYR A 279     7831   6614   5760   2657   -450   1236       C  
ATOM    468  CE2 TYR A 279     -13.911  13.491 -51.128  1.00 49.57           C  
ANISOU  468  CE2 TYR A 279     6837   6937   5062   2655   -537    953       C  
ATOM    469  CZ  TYR A 279     -13.698  12.134 -51.237  1.00 51.99           C  
ANISOU  469  CZ  TYR A 279     7424   6938   5391   2859   -519   1147       C  
ATOM    470  OH  TYR A 279     -12.560  11.578 -50.697  1.00 56.13           O  
ANISOU  470  OH  TYR A 279     7969   7619   5738   3218   -570   1238       O  
ATOM    471  N   VAL A 280     -19.652  15.858 -52.752  1.00 41.67           N  
ANISOU  471  N   VAL A 280     5366   5522   4943   1232   -148   1026       N  
ATOM    472  CA  VAL A 280     -20.372  16.605 -53.777  1.00 39.94           C  
ANISOU  472  CA  VAL A 280     4951   5280   4946    996   -179    943       C  
ATOM    473  C   VAL A 280     -19.362  16.963 -54.856  1.00 39.20           C  
ANISOU  473  C   VAL A 280     4863   5188   4845   1048   -339    661       C  
ATOM    474  O   VAL A 280     -18.292  17.506 -54.556  1.00 38.34           O  
ANISOU  474  O   VAL A 280     4722   5270   4576   1245   -362    487       O  
ATOM    475  CB  VAL A 280     -21.037  17.862 -53.192  1.00 39.30           C  
ANISOU  475  CB  VAL A 280     4636   5432   4864   1002     -9    949       C  
ATOM    476  CG1 VAL A 280     -21.629  18.723 -54.304  1.00 36.96           C  
ANISOU  476  CG1 VAL A 280     4129   5126   4788    823    -53    873       C  
ATOM    477  CG2 VAL A 280     -22.112  17.471 -52.190  1.00 41.67           C  
ANISOU  477  CG2 VAL A 280     4903   5763   5168    969    202   1270       C  
ATOM    478  N   PHE A 281     -19.686  16.647 -56.106  1.00 38.15           N  
ANISOU  478  N   PHE A 281     4766   4862   4865    860   -457    628       N  
ATOM    479  CA  PHE A 281     -18.725  16.738 -57.195  1.00 37.26           C  
ANISOU  479  CA  PHE A 281     4715   4733   4711    935   -578    399       C  
ATOM    480  C   PHE A 281     -18.978  17.993 -58.022  1.00 36.35           C  
ANISOU  480  C   PHE A 281     4369   4753   4689    811   -597    288       C  
ATOM    481  O   PHE A 281     -20.117  18.273 -58.411  1.00 34.88           O  
ANISOU  481  O   PHE A 281     4062   4530   4661    589   -608    400       O  
ATOM    482  CB  PHE A 281     -18.795  15.495 -58.082  1.00 38.42           C  
ANISOU  482  CB  PHE A 281     5152   4555   4893    852   -696    402       C  
ATOM    483  CG  PHE A 281     -18.398  14.223 -57.380  1.00 42.52           C  
ANISOU  483  CG  PHE A 281     5957   4870   5328   1021   -670    513       C  
ATOM    484  CD1 PHE A 281     -17.070  13.847 -57.302  1.00 42.78           C  
ANISOU  484  CD1 PHE A 281     6120   4937   5196   1368   -665    410       C  
ATOM    485  CD2 PHE A 281     -19.358  13.395 -56.817  1.00 44.54           C  
ANISOU  485  CD2 PHE A 281     6335   4902   5686    838   -642    760       C  
ATOM    486  CE1 PHE A 281     -16.703  12.668 -56.662  1.00 45.35           C  
ANISOU  486  CE1 PHE A 281     6723   5060   5449   1573   -634    548       C  
ATOM    487  CE2 PHE A 281     -18.998  12.223 -56.181  1.00 46.51           C  
ANISOU  487  CE2 PHE A 281     6881   4923   5868    999   -606    898       C  
ATOM    488  CZ  PHE A 281     -17.669  11.860 -56.101  1.00 47.57           C  
ANISOU  488  CZ  PHE A 281     7174   5074   5828   1388   -604    791       C  
ATOM    489  N   ILE A 282     -17.909  18.739 -58.286  1.00 36.28           N  
ANISOU  489  N   ILE A 282     4278   4911   4594    952   -604    104       N  
ATOM    490  CA  ILE A 282     -17.946  19.939 -59.112  1.00 34.92           C  
ANISOU  490  CA  ILE A 282     3923   4843   4503    859   -611     12       C  
ATOM    491  C   ILE A 282     -16.864  19.806 -60.169  1.00 32.97           C  
ANISOU  491  C   ILE A 282     3736   4620   4172    949   -677   -132       C  
ATOM    492  O   ILE A 282     -15.718  19.478 -59.846  1.00 32.59           O  
ANISOU  492  O   ILE A 282     3721   4663   3999   1154   -668   -206       O  
ATOM    493  CB  ILE A 282     -17.722  21.218 -58.283  1.00 35.41           C  
ANISOU  493  CB  ILE A 282     3808   5087   4557    910   -512    -52       C  
ATOM    494  CG1 ILE A 282     -18.690  21.276 -57.100  1.00 37.14           C  
ANISOU  494  CG1 ILE A 282     4009   5310   4792    906   -392     82       C  
ATOM    495  CG2 ILE A 282     -17.860  22.449 -59.173  1.00 35.81           C  
ANISOU  495  CG2 ILE A 282     3706   5172   4729    804   -504   -105       C  
ATOM    496  CD1 ILE A 282     -20.129  21.353 -57.504  1.00 38.34           C  
ANISOU  496  CD1 ILE A 282     4059   5377   5133    737   -351    268       C  
ATOM    497  N   ALA A 283     -17.217  20.061 -61.427  1.00 30.15           N  
ANISOU  497  N   ALA A 283     3375   4217   3863    818   -735   -148       N  
ATOM    498  CA  ALA A 283     -16.245  20.004 -62.504  1.00 30.15           C  
ANISOU  498  CA  ALA A 283     3436   4269   3751    922   -753   -266       C  
ATOM    499  C   ALA A 283     -15.897  21.407 -62.978  1.00 29.99           C  
ANISOU  499  C   ALA A 283     3181   4431   3784    874   -699   -292       C  
ATOM    500  O   ALA A 283     -16.737  22.310 -62.976  1.00 31.17           O  
ANISOU  500  O   ALA A 283     3196   4580   4068    723   -689   -215       O  
ATOM    501  CB  ALA A 283     -16.761  19.175 -63.689  1.00 28.71           C  
ANISOU  501  CB  ALA A 283     3500   3900   3509    827   -864   -282       C  
ATOM    502  N   ALA A 284     -14.639  21.582 -63.364  1.00 28.06           N  
ANISOU  502  N   ALA A 284     2877   4339   3446   1016   -648   -373       N  
ATOM    503  CA  ALA A 284     -14.211  22.750 -64.115  1.00 29.06           C  
ANISOU  503  CA  ALA A 284     2822   4608   3613    948   -592   -368       C  
ATOM    504  C   ALA A 284     -14.029  22.367 -65.578  1.00 29.71           C  
ANISOU  504  C   ALA A 284     3040   4695   3555    995   -590   -374       C  
ATOM    505  O   ALA A 284     -13.702  21.224 -65.895  1.00 31.48           O  
ANISOU  505  O   ALA A 284     3484   4855   3622   1157   -601   -441       O  
ATOM    506  CB  ALA A 284     -12.903  23.309 -63.559  1.00 29.18           C  
ANISOU  506  CB  ALA A 284     2622   4836   3629   1028   -529   -418       C  
ATOM    507  N   SER A 285     -14.252  23.328 -66.469  1.00 29.73           N  
ANISOU  507  N   SER A 285     2948   4757   3593    874   -567   -302       N  
ATOM    508  CA  SER A 285     -14.012  23.131 -67.891  1.00 31.80           C  
ANISOU  508  CA  SER A 285     3338   5077   3667    928   -548   -296       C  
ATOM    509  C   SER A 285     -13.343  24.373 -68.454  1.00 31.87           C  
ANISOU  509  C   SER A 285     3119   5271   3720    890   -417   -197       C  
ATOM    510  O   SER A 285     -13.638  25.492 -68.024  1.00 29.39           O  
ANISOU  510  O   SER A 285     2621   4935   3611    736   -403   -116       O  
ATOM    511  CB  SER A 285     -15.311  22.840 -68.659  1.00 34.62           C  
ANISOU  511  CB  SER A 285     3886   5297   3969    777   -709   -253       C  
ATOM    512  OG  SER A 285     -15.836  21.573 -68.301  1.00 35.29           O  
ANISOU  512  OG  SER A 285     4215   5189   4006    773   -833   -338       O  
ATOM    513  N   PHE A 286     -12.429  24.174 -69.400  1.00 33.57           N  
ANISOU  513  N   PHE A 286     3364   5649   3741   1041   -299   -195       N  
ATOM    514  CA  PHE A 286     -11.816  25.285 -70.109  1.00 33.39           C  
ANISOU  514  CA  PHE A 286     3137   5807   3742    985   -154    -50       C  
ATOM    515  C   PHE A 286     -11.451  24.813 -71.507  1.00 36.85           C  
ANISOU  515  C   PHE A 286     3759   6379   3865   1154    -56    -30       C  
ATOM    516  O   PHE A 286     -11.518  23.623 -71.821  1.00 38.01           O  
ANISOU  516  O   PHE A 286     4200   6461   3781   1331    -96   -173       O  
ATOM    517  CB  PHE A 286     -10.591  25.838 -69.371  1.00 34.30           C  
ANISOU  517  CB  PHE A 286     2927   6093   4010    985    -36    -30       C  
ATOM    518  CG  PHE A 286      -9.544  24.806 -69.065  1.00 36.76           C  
ANISOU  518  CG  PHE A 286     3212   6563   4193   1253     31   -120       C  
ATOM    519  CD1 PHE A 286      -8.570  24.488 -69.997  1.00 39.60           C  
ANISOU  519  CD1 PHE A 286     3532   7157   4358   1476    222    -62       C  
ATOM    520  CD2 PHE A 286      -9.528  24.160 -67.838  1.00 36.29           C  
ANISOU  520  CD2 PHE A 286     3163   6433   4195   1320    -75   -233       C  
ATOM    521  CE1 PHE A 286      -7.601  23.540 -69.720  1.00 43.34           C  
ANISOU  521  CE1 PHE A 286     3961   7784   4723   1789    311   -115       C  
ATOM    522  CE2 PHE A 286      -8.562  23.210 -67.558  1.00 39.50           C  
ANISOU  522  CE2 PHE A 286     3537   6986   4486   1613    -14   -275       C  
ATOM    523  CZ  PHE A 286      -7.601  22.901 -68.499  1.00 41.28           C  
ANISOU  523  CZ  PHE A 286     3707   7435   4542   1860    181   -216       C  
ATOM    524  N   GLN A 287     -11.069  25.763 -72.352  1.00 37.59           N  
ANISOU  524  N   GLN A 287     3713   6636   3934   1101     85    150       N  
ATOM    525  CA  GLN A 287     -10.769  25.480 -73.748  1.00 40.30           C  
ANISOU  525  CA  GLN A 287     4239   7143   3931   1264    208    202       C  
ATOM    526  C   GLN A 287      -9.339  25.886 -74.067  1.00 44.38           C  
ANISOU  526  C   GLN A 287     4480   7960   4422   1391    503    338       C  
ATOM    527  O   GLN A 287      -8.902  26.980 -73.697  1.00 44.27           O  
ANISOU  527  O   GLN A 287     4126   8015   4680   1199    579    503       O  
ATOM    528  CB  GLN A 287     -11.743  26.210 -74.677  1.00 41.08           C  
ANISOU  528  CB  GLN A 287     4442   7209   3957   1101    116    367       C  
ATOM    529  CG  GLN A 287     -11.584  25.838 -76.143  1.00 47.57           C  
ANISOU  529  CG  GLN A 287     5534   8205   4335   1271    201    398       C  
ATOM    530  CD  GLN A 287     -12.672  26.434 -77.013  1.00 50.73           C  
ANISOU  530  CD  GLN A 287     6060   8591   4626   1115     37    566       C  
ATOM    531  OE1 GLN A 287     -13.276  25.742 -77.829  1.00 55.78           O  
ANISOU  531  OE1 GLN A 287     7044   9233   4916   1160   -125    469       O  
ATOM    532  NE2 GLN A 287     -12.920  27.728 -76.848  1.00 50.77           N  
ANISOU  532  NE2 GLN A 287     5798   8574   4918    935     66    822       N  
ATOM    533  N   ALA A 288      -8.621  24.999 -74.745  1.00 48.27           N  
ANISOU  533  N   ALA A 288     5125   8622   4595   1712    673    272       N  
ATOM    534  CA  ALA A 288      -7.341  25.286 -75.376  1.00 51.65           C  
ANISOU  534  CA  ALA A 288     5310   9402   4913   1890   1004    450       C  
ATOM    535  C   ALA A 288      -7.466  25.008 -76.871  1.00 55.01           C  
ANISOU  535  C   ALA A 288     6077   9945   4881   2085   1142    485       C  
ATOM    536  O   ALA A 288      -8.543  24.673 -77.371  1.00 53.93           O  
ANISOU  536  O   ALA A 288     6341   9615   4536   2031    931    366       O  
ATOM    537  CB  ALA A 288      -6.217  24.458 -74.747  1.00 53.70           C  
ANISOU  537  CB  ALA A 288     5397   9822   5186   2190   1143    366       C  
ATOM    538  N   SER A 289      -6.348  25.134 -77.592  1.00 60.10           N  
ANISOU  538  N   SER A 289     6552  10938   5346   2313   1496    659       N  
ATOM    539  CA  SER A 289      -6.399  24.985 -79.042  1.00 63.75           C  
ANISOU  539  CA  SER A 289     7344  11559   5322   2515   1669    717       C  
ATOM    540  C   SER A 289      -6.703  23.555 -79.473  1.00 64.72           C  
ANISOU  540  C   SER A 289     8046  11536   5010   2851   1610    376       C  
ATOM    541  O   SER A 289      -7.124  23.344 -80.617  1.00 68.86           O  
ANISOU  541  O   SER A 289     8989  12074   5102   2938   1607    330       O  
ATOM    542  CB  SER A 289      -5.086  25.453 -79.674  1.00 68.85           C  
ANISOU  542  CB  SER A 289     7656  12577   5927   2664   2067   1009       C  
ATOM    543  OG  SER A 289      -3.988  24.699 -79.198  1.00 72.66           O  
ANISOU  543  OG  SER A 289     7983  13085   6539   2897   2158    929       O  
ATOM    544  N   ASP A 290      -6.514  22.572 -78.595  1.00 61.89           N  
ANISOU  544  N   ASP A 290     7757  10999   4761   3021   1539    136       N  
ATOM    545  CA  ASP A 290      -6.826  21.187 -78.921  1.00 64.73           C  
ANISOU  545  CA  ASP A 290     8706  11061   4827   3258   1430   -190       C  
ATOM    546  C   ASP A 290      -8.198  20.756 -78.420  1.00 60.85           C  
ANISOU  546  C   ASP A 290     8555  10193   4372   3000   1016   -426       C  
ATOM    547  O   ASP A 290      -8.551  19.580 -78.553  1.00 63.07           O  
ANISOU  547  O   ASP A 290     9346  10178   4440   3136    891   -713       O  
ATOM    548  CB  ASP A 290      -5.739  20.252 -78.372  1.00 66.09           C  
ANISOU  548  CB  ASP A 290     8792  11167   5151   3573   1571   -246       C  
ATOM    549  CG  ASP A 290      -5.845  20.036 -76.874  1.00 61.54           C  
ANISOU  549  CG  ASP A 290     7997  10454   4932   3496   1404   -311       C  
ATOM    550  OD1 ASP A 290      -6.359  20.933 -76.171  1.00 57.52           O  
ANISOU  550  OD1 ASP A 290     7175  10009   4673   3188   1273   -230       O  
ATOM    551  OD2 ASP A 290      -5.405  18.967 -76.400  1.00 62.02           O  
ANISOU  551  OD2 ASP A 290     8202  10323   5037   3731   1399   -422       O  
ATOM    552  N   GLY A 291      -8.981  21.672 -77.857  1.00 55.12           N  
ANISOU  552  N   GLY A 291     7545   9394   4003   2571    772   -285       N  
ATOM    553  CA  GLY A 291     -10.327  21.342 -77.438  1.00 51.36           C  
ANISOU  553  CA  GLY A 291     7305   8572   3639   2272    371   -434       C  
ATOM    554  C   GLY A 291     -10.623  21.664 -75.989  1.00 47.25           C  
ANISOU  554  C   GLY A 291     6432   7904   3619   2040    225   -388       C  
ATOM    555  O   GLY A 291      -9.883  22.406 -75.337  1.00 44.72           O  
ANISOU  555  O   GLY A 291     5661   7752   3577   2027    382   -227       O  
ATOM    556  N   ILE A 292     -11.705  21.109 -75.476  1.00 44.83           N  
ANISOU  556  N   ILE A 292     6332   7290   3412   1842    -78   -524       N  
ATOM    557  CA  ILE A 292     -12.147  21.381 -74.116  1.00 41.25           C  
ANISOU  557  CA  ILE A 292     5596   6695   3380   1631   -213   -479       C  
ATOM    558  C   ILE A 292     -11.505  20.372 -73.182  1.00 42.64           C  
ANISOU  558  C   ILE A 292     5831   6749   3620   1862   -146   -623       C  
ATOM    559  O   ILE A 292     -11.389  19.182 -73.508  1.00 40.76           O  
ANISOU  559  O   ILE A 292     6006   6340   3140   2076   -144   -812       O  
ATOM    560  CB  ILE A 292     -13.682  21.346 -74.028  1.00 39.20           C  
ANISOU  560  CB  ILE A 292     5463   6217   3213   1302   -543   -484       C  
ATOM    561  CG1 ILE A 292     -14.262  22.534 -74.791  1.00 38.15           C  
ANISOU  561  CG1 ILE A 292     5169   6246   3079   1110   -598   -267       C  
ATOM    562  CG2 ILE A 292     -14.155  21.381 -72.585  1.00 36.62           C  
ANISOU  562  CG2 ILE A 292     4920   5731   3262   1150   -641   -461       C  
ATOM    563  CD1 ILE A 292     -15.494  22.198 -75.547  1.00 42.18           C  
ANISOU  563  CD1 ILE A 292     5950   6669   3407    913   -903   -290       C  
ATOM    564  N   HIS A 293     -11.047  20.865 -72.037  1.00 36.16           N  
ANISOU  564  N   HIS A 293     4623   6012   3105   1833    -91   -531       N  
ATOM    565  CA  HIS A 293     -10.502  20.051 -70.962  1.00 39.04           C  
ANISOU  565  CA  HIS A 293     4971   6297   3563   2030    -64   -609       C  
ATOM    566  C   HIS A 293     -11.321  20.277 -69.701  1.00 35.62           C  
ANISOU  566  C   HIS A 293     4407   5705   3423   1770   -252   -580       C  
ATOM    567  O   HIS A 293     -11.864  21.365 -69.477  1.00 35.45           O  
ANISOU  567  O   HIS A 293     4148   5731   3592   1501   -315   -474       O  
ATOM    568  CB  HIS A 293      -9.028  20.387 -70.701  1.00 40.78           C  
ANISOU  568  CB  HIS A 293     4817   6851   3825   2273    175   -509       C  
ATOM    569  CG  HIS A 293      -8.161  20.263 -71.914  1.00 43.12           C  
ANISOU  569  CG  HIS A 293     5170   7371   3841   2561    430   -485       C  
ATOM    570  ND1 HIS A 293      -7.385  19.153 -72.163  1.00 46.99           N  
ANISOU  570  ND1 HIS A 293     5876   7869   4108   3008    605   -578       N  
ATOM    571  CD2 HIS A 293      -7.959  21.104 -72.955  1.00 43.93           C  
ANISOU  571  CD2 HIS A 293     5162   7698   3831   2499    570   -357       C  
ATOM    572  CE1 HIS A 293      -6.736  19.316 -73.303  1.00 49.46           C  
ANISOU  572  CE1 HIS A 293     6199   8425   4168   3222    859   -522       C  
ATOM    573  NE2 HIS A 293      -7.068  20.493 -73.804  1.00 48.00           N  
ANISOU  573  NE2 HIS A 293     5813   8385   4040   2903    838   -378       N  
ATOM    574  N   SER A 294     -11.413  19.242 -68.874  1.00 34.21           N  
ANISOU  574  N   SER A 294     4406   5325   3269   1880   -317   -662       N  
ATOM    575  CA  SER A 294     -12.167  19.331 -67.638  1.00 33.18           C  
ANISOU  575  CA  SER A 294     4179   5061   3368   1677   -458   -619       C  
ATOM    576  C   SER A 294     -11.342  18.784 -66.480  1.00 34.66           C  
ANISOU  576  C   SER A 294     4276   5294   3599   1914   -401   -613       C  
ATOM    577  O   SER A 294     -10.408  18.002 -66.667  1.00 38.78           O  
ANISOU  577  O   SER A 294     4902   5854   3978   2253   -287   -651       O  
ATOM    578  CB  SER A 294     -13.508  18.587 -67.749  1.00 35.97           C  
ANISOU  578  CB  SER A 294     4864   5085   3719   1474   -649   -662       C  
ATOM    579  OG  SER A 294     -14.412  19.285 -68.591  1.00 35.74           O  
ANISOU  579  OG  SER A 294     4811   5076   3693   1210   -755   -613       O  
ATOM    580  N   ILE A 295     -11.677  19.246 -65.278  1.00 33.11           N  
ANISOU  580  N   ILE A 295     3878   5118   3582   1762   -473   -551       N  
ATOM    581  CA  ILE A 295     -11.082  18.772 -64.032  1.00 36.07           C  
ANISOU  581  CA  ILE A 295     4177   5552   3978   1945   -471   -522       C  
ATOM    582  C   ILE A 295     -12.224  18.499 -63.068  1.00 35.44           C  
ANISOU  582  C   ILE A 295     4220   5250   3996   1765   -581   -481       C  
ATOM    583  O   ILE A 295     -13.134  19.323 -62.937  1.00 32.94           O  
ANISOU  583  O   ILE A 295     3799   4912   3805   1491   -627   -450       O  
ATOM    584  CB  ILE A 295     -10.113  19.803 -63.422  1.00 38.60           C  
ANISOU  584  CB  ILE A 295     4072   6224   4370   1939   -440   -481       C  
ATOM    585  CG1 ILE A 295      -9.077  20.268 -64.441  1.00 41.75           C  
ANISOU  585  CG1 ILE A 295     4266   6879   4716   2040   -308   -464       C  
ATOM    586  CG2 ILE A 295      -9.426  19.229 -62.180  1.00 39.82           C  
ANISOU  586  CG2 ILE A 295     4149   6494   4487   2156   -477   -440       C  
ATOM    587  CD1 ILE A 295      -8.322  21.500 -63.985  1.00 43.24           C  
ANISOU  587  CD1 ILE A 295     4058   7341   5031   1844   -306   -407       C  
ATOM    588  N   ARG A 296     -12.189  17.355 -62.394  1.00 38.34           N  
ANISOU  588  N   ARG A 296     4802   5453   4312   1941   -596   -449       N  
ATOM    589  CA  ARG A 296     -13.237  17.018 -61.439  1.00 37.76           C  
ANISOU  589  CA  ARG A 296     4836   5188   4324   1779   -664   -361       C  
ATOM    590  C   ARG A 296     -12.761  17.287 -60.017  1.00 36.12           C  
ANISOU  590  C   ARG A 296     4432   5189   4102   1884   -656   -290       C  
ATOM    591  O   ARG A 296     -11.657  16.880 -59.640  1.00 38.11           O  
ANISOU  591  O   ARG A 296     4635   5593   4251   2176   -636   -273       O  
ATOM    592  CB  ARG A 296     -13.676  15.561 -61.580  1.00 40.72           C  
ANISOU  592  CB  ARG A 296     5627   5186   4658   1842   -695   -337       C  
ATOM    593  CG  ARG A 296     -14.857  15.223 -60.680  1.00 41.32           C  
ANISOU  593  CG  ARG A 296     5780   5071   4849   1618   -746   -193       C  
ATOM    594  CD  ARG A 296     -15.242  13.768 -60.782  1.00 42.56           C  
ANISOU  594  CD  ARG A 296     6365   4811   4997   1632   -784   -148       C  
ATOM    595  NE  ARG A 296     -15.725  13.435 -62.118  1.00 41.50           N  
ANISOU  595  NE  ARG A 296     6481   4439   4849   1454   -879   -279       N  
ATOM    596  CZ  ARG A 296     -15.857  12.192 -62.566  1.00 44.18           C  
ANISOU  596  CZ  ARG A 296     7279   4366   5140   1472   -931   -332       C  
ATOM    597  NH1 ARG A 296     -15.539  11.172 -61.779  1.00 45.89           N  
ANISOU  597  NH1 ARG A 296     7739   4345   5350   1684   -872   -231       N  
ATOM    598  NH2 ARG A 296     -16.304  11.966 -63.798  1.00 45.28           N  
ANISOU  598  NH2 ARG A 296     7669   4315   5221   1280  -1052   -487       N  
ATOM    599  N   TYR A 297     -13.599  17.970 -59.237  1.00 34.18           N  
ANISOU  599  N   TYR A 297     4077   4971   3939   1669   -670   -243       N  
ATOM    600  CA  TYR A 297     -13.325  18.265 -57.838  1.00 35.57           C  
ANISOU  600  CA  TYR A 297     4133   5334   4047   1739   -674   -199       C  
ATOM    601  C   TYR A 297     -14.406  17.654 -56.958  1.00 36.63           C  
ANISOU  601  C   TYR A 297     4440   5286   4192   1674   -646    -48       C  
ATOM    602  O   TYR A 297     -15.535  17.423 -57.401  1.00 35.98           O  
ANISOU  602  O   TYR A 297     4458   4978   4234   1473   -632     18       O  
ATOM    603  CB  TYR A 297     -13.252  19.779 -57.586  1.00 33.93           C  
ANISOU  603  CB  TYR A 297     3663   5342   3887   1572   -675   -297       C  
ATOM    604  CG  TYR A 297     -12.140  20.449 -58.353  1.00 35.79           C  
ANISOU  604  CG  TYR A 297     3687   5778   4134   1590   -694   -399       C  
ATOM    605  CD1 TYR A 297     -10.825  20.393 -57.904  1.00 37.26           C  
ANISOU  605  CD1 TYR A 297     3703   6240   4214   1766   -749   -414       C  
ATOM    606  CD2 TYR A 297     -12.402  21.126 -59.531  1.00 33.81           C  
ANISOU  606  CD2 TYR A 297     3377   5471   3999   1430   -656   -439       C  
ATOM    607  CE1 TYR A 297      -9.808  21.001 -58.608  1.00 39.32           C  
ANISOU  607  CE1 TYR A 297     3768   6658   4513   1692   -716   -452       C  
ATOM    608  CE2 TYR A 297     -11.394  21.733 -60.245  1.00 34.96           C  
ANISOU  608  CE2 TYR A 297     3320   5808   4157   1435   -638   -485       C  
ATOM    609  CZ  TYR A 297     -10.103  21.666 -59.787  1.00 37.03           C  
ANISOU  609  CZ  TYR A 297     3420   6309   4339   1553   -658   -486       C  
ATOM    610  OH  TYR A 297      -9.103  22.275 -60.509  1.00 39.55           O  
ANISOU  610  OH  TYR A 297     3539   6792   4695   1485   -603   -478       O  
ATOM    611  N   GLY A 298     -14.053  17.405 -55.704  1.00 37.34           N  
ANISOU  611  N   GLY A 298     4540   5507   4141   1833   -644     31       N  
ATOM    612  CA  GLY A 298     -14.997  16.863 -54.745  1.00 37.97           C  
ANISOU  612  CA  GLY A 298     4767   5463   4198   1796   -578    216       C  
ATOM    613  C   GLY A 298     -14.887  17.582 -53.418  1.00 38.73           C  
ANISOU  613  C   GLY A 298     4759   5833   4126   1847   -555    213       C  
ATOM    614  O   GLY A 298     -13.805  18.004 -53.006  1.00 39.61           O  
ANISOU  614  O   GLY A 298     4753   6213   4085   1982   -646    105       O  
ATOM    615  N   ILE A 299     -16.032  17.719 -52.751  1.00 38.61           N  
ANISOU  615  N   ILE A 299     4784   5763   4124   1732   -433    336       N  
ATOM    616  CA  ILE A 299     -16.122  18.298 -51.414  1.00 40.07           C  
ANISOU  616  CA  ILE A 299     4956   6175   4094   1805   -368    341       C  
ATOM    617  C   ILE A 299     -16.713  17.246 -50.487  1.00 42.45           C  
ANISOU  617  C   ILE A 299     5442   6401   4286   1898   -257    634       C  
ATOM    618  O   ILE A 299     -17.801  16.724 -50.756  1.00 42.89           O  
ANISOU  618  O   ILE A 299     5542   6229   4524   1746   -144    829       O  
ATOM    619  CB  ILE A 299     -16.990  19.572 -51.397  1.00 39.03           C  
ANISOU  619  CB  ILE A 299     4707   6073   4051   1639   -248    237       C  
ATOM    620  CG1 ILE A 299     -16.572  20.538 -52.505  1.00 38.67           C  
ANISOU  620  CG1 ILE A 299     4502   6017   4173   1510   -335     12       C  
ATOM    621  CG2 ILE A 299     -16.925  20.250 -50.026  1.00 40.66           C  
ANISOU  621  CG2 ILE A 299     4970   6508   3971   1750   -182    165       C  
ATOM    622  CD1 ILE A 299     -17.632  21.591 -52.811  1.00 40.08           C  
ANISOU  622  CD1 ILE A 299     4584   6118   4526   1361   -200    -15       C  
ATOM    623  N   ASN A 300     -16.016  16.944 -49.393  1.00 43.65           N  
ANISOU  623  N   ASN A 300     5685   6759   4140   2127   -299    695       N  
ATOM    624  CA  ASN A 300     -16.524  15.933 -48.480  1.00 44.89           C  
ANISOU  624  CA  ASN A 300     6036   6850   4170   2235   -177   1019       C  
ATOM    625  C   ASN A 300     -17.451  16.575 -47.446  1.00 46.45           C  
ANISOU  625  C   ASN A 300     6235   7207   4207   2203     28   1090       C  
ATOM    626  O   ASN A 300     -17.646  17.791 -47.425  1.00 45.29           O  
ANISOU  626  O   ASN A 300     5974   7193   4042   2127     65    859       O  
ATOM    627  CB  ASN A 300     -15.374  15.140 -47.840  1.00 47.19           C  
ANISOU  627  CB  ASN A 300     6447   7279   4204   2544   -311   1123       C  
ATOM    628  CG  ASN A 300     -14.540  15.944 -46.833  1.00 47.78           C  
ANISOU  628  CG  ASN A 300     6450   7791   3912   2694   -436    967       C  
ATOM    629  OD1 ASN A 300     -14.949  16.984 -46.316  1.00 47.84           O  
ANISOU  629  OD1 ASN A 300     6420   7965   3792   2593   -374    808       O  
ATOM    630  ND2 ASN A 300     -13.356  15.424 -46.535  1.00 49.54           N  
ANISOU  630  ND2 ASN A 300     6670   8199   3952   2951   -623   1019       N  
ATOM    631  N   LYS A 301     -18.020  15.739 -46.568  1.00 62.25           N  
ANISOU  631  N   LYS A 301     8166   9865   5619   1791    320   1110       N  
ATOM    632  CA  LYS A 301     -19.042  16.203 -45.629  1.00 65.05           C  
ANISOU  632  CA  LYS A 301     8513  10466   5735   1654    572   1047       C  
ATOM    633  C   LYS A 301     -18.517  17.281 -44.688  1.00 65.29           C  
ANISOU  633  C   LYS A 301     8576  10940   5290   1796    391    940       C  
ATOM    634  O   LYS A 301     -19.290  18.129 -44.227  1.00 65.78           O  
ANISOU  634  O   LYS A 301     8545  11235   5215   1706    517    685       O  
ATOM    635  CB  LYS A 301     -19.588  15.030 -44.812  1.00 71.92           C  
ANISOU  635  CB  LYS A 301     9606  11202   6516   1555    954   1451       C  
ATOM    636  CG  LYS A 301     -20.172  13.891 -45.632  1.00 74.91           C  
ANISOU  636  CG  LYS A 301     9963  11099   7400   1367   1172   1536       C  
ATOM    637  CD  LYS A 301     -21.535  14.249 -46.198  1.00 75.36           C  
ANISOU  637  CD  LYS A 301     9722  11120   7794   1085   1362   1168       C  
ATOM    638  CE  LYS A 301     -21.653  13.831 -47.656  1.00 74.65           C  
ANISOU  638  CE  LYS A 301     9473  10672   8218    993   1235    949       C  
ATOM    639  NZ  LYS A 301     -23.071  13.607 -48.057  1.00 77.05           N  
ANISOU  639  NZ  LYS A 301     9528  10846   8903    678   1490    722       N  
ATOM    640  N   ASN A 302     -17.224  17.260 -44.374  1.00 64.89           N  
ANISOU  640  N   ASN A 302     8638  11016   5002   2018     94   1099       N  
ATOM    641  CA  ASN A 302     -16.638  18.257 -43.492  1.00 65.31           C  
ANISOU  641  CA  ASN A 302     8709  11496   4611   2137   -129    952       C  
ATOM    642  C   ASN A 302     -15.988  19.412 -44.252  1.00 60.74           C  
ANISOU  642  C   ASN A 302     7896  10964   4218   2167   -461    563       C  
ATOM    643  O   ASN A 302     -15.184  20.148 -43.672  1.00 58.70           O  
ANISOU  643  O   ASN A 302     7627  11000   3674   2270   -724    435       O  
ATOM    644  CB  ASN A 302     -15.639  17.595 -42.538  1.00 71.10           C  
ANISOU  644  CB  ASN A 302     9681  12409   4927   2363   -285   1350       C  
ATOM    645  CG  ASN A 302     -16.278  16.501 -41.693  1.00 76.95           C  
ANISOU  645  CG  ASN A 302    10711  13094   5431   2337     74   1798       C  
ATOM    646  OD1 ASN A 302     -17.207  16.764 -40.924  1.00 79.96           O  
ANISOU  646  OD1 ASN A 302    11173  13675   5534   2205    370   1751       O  
ATOM    647  ND2 ASN A 302     -15.774  15.278 -41.815  1.00 79.17           N  
ANISOU  647  ND2 ASN A 302    11158  13091   5831   2468     76   2241       N  
ATOM    648  N   GLY A 303     -16.329  19.592 -45.528  1.00 56.48           N  
ANISOU  648  N   GLY A 303     7179  10143   4139   2067   -450    373       N  
ATOM    649  CA  GLY A 303     -15.938  20.772 -46.273  1.00 53.70           C  
ANISOU  649  CA  GLY A 303     6633   9801   3968   2060   -683     26       C  
ATOM    650  C   GLY A 303     -14.567  20.748 -46.909  1.00 52.78           C  
ANISOU  650  C   GLY A 303     6448   9627   3978   2178   -966     74       C  
ATOM    651  O   GLY A 303     -14.130  21.781 -47.428  1.00 50.81           O  
ANISOU  651  O   GLY A 303     6053   9399   3855   2154  -1140   -186       O  
ATOM    652  N   GLU A 304     -13.873  19.612 -46.890  1.00 54.50           N  
ANISOU  652  N   GLU A 304     6757   9754   4196   2309   -995    400       N  
ATOM    653  CA  GLU A 304     -12.543  19.518 -47.475  1.00 50.16           C  
ANISOU  653  CA  GLU A 304     6097   9168   3795   2446  -1233    440       C  
ATOM    654  C   GLU A 304     -12.633  19.360 -48.989  1.00 47.06           C  
ANISOU  654  C   GLU A 304     5609   8456   3817   2381  -1163    342       C  
ATOM    655  O   GLU A 304     -13.500  18.644 -49.499  1.00 46.54           O  
ANISOU  655  O   GLU A 304     5619   8141   3924   2300   -952    398       O  
ATOM    656  CB  GLU A 304     -11.791  18.331 -46.880  1.00 53.40           C  
ANISOU  656  CB  GLU A 304     6632   9585   4071   2663  -1289    829       C  
ATOM    657  CG  GLU A 304     -11.629  18.389 -45.376  1.00 67.81           C  
ANISOU  657  CG  GLU A 304     8595  11760   5410   2758  -1386    975       C  
ATOM    658  CD  GLU A 304     -10.607  17.387 -44.888  1.00 70.94           C  
ANISOU  658  CD  GLU A 304     9066  12090   5798   2944  -1495   1312       C  
ATOM    659  OE1 GLU A 304      -9.512  17.813 -44.466  1.00 72.40           O  
ANISOU  659  OE1 GLU A 304     9117  12406   5985   2949  -1731   1199       O  
ATOM    660  OE2 GLU A 304     -10.898  16.174 -44.942  1.00 72.04           O  
ANISOU  660  OE2 GLU A 304     9396  12026   5951   3092  -1345   1695       O  
ATOM    661  N   LEU A 305     -11.722  20.022 -49.701  1.00 45.56           N  
ANISOU  661  N   LEU A 305     5249   8286   3774   2404  -1333    187       N  
ATOM    662  CA  LEU A 305     -11.680  20.014 -51.158  1.00 44.68           C  
ANISOU  662  CA  LEU A 305     5066   7935   3976   2354  -1274     84       C  
ATOM    663  C   LEU A 305     -10.655  19.005 -51.663  1.00 44.07           C  
ANISOU  663  C   LEU A 305     4962   7729   4053   2523  -1285    259       C  
ATOM    664  O   LEU A 305      -9.614  18.780 -51.037  1.00 46.20           O  
ANISOU  664  O   LEU A 305     5163   8146   4245   2682  -1430    392       O  
ATOM    665  CB  LEU A 305     -11.347  21.408 -51.698  1.00 44.00           C  
ANISOU  665  CB  LEU A 305     4831   7921   3965   2259  -1387   -173       C  
ATOM    666  CG  LEU A 305     -11.382  21.625 -53.214  1.00 44.02           C  
ANISOU  666  CG  LEU A 305     4799   7721   4207   2199  -1319   -273       C  
ATOM    667  CD1 LEU A 305     -12.764  21.326 -53.791  1.00 42.51           C  
ANISOU  667  CD1 LEU A 305     4715   7356   4080   2113  -1180   -325       C  
ATOM    668  CD2 LEU A 305     -10.945  23.043 -53.558  1.00 44.49           C  
ANISOU  668  CD2 LEU A 305     4743   7837   4324   2106  -1414   -456       C  
ATOM    669  N   PHE A 306     -10.969  18.387 -52.801  1.00 42.96           N  
ANISOU  669  N   PHE A 306     4868   7318   4137   2497  -1137    232       N  
ATOM    670  CA  PHE A 306     -10.115  17.373 -53.404  1.00 44.14           C  
ANISOU  670  CA  PHE A 306     5007   7295   4471   2665  -1093    345       C  
ATOM    671  C   PHE A 306     -10.207  17.470 -54.919  1.00 42.40           C  
ANISOU  671  C   PHE A 306     4766   6910   4435   2589   -992    146       C  
ATOM    672  O   PHE A 306     -11.280  17.740 -55.463  1.00 40.87           O  
ANISOU  672  O   PHE A 306     4646   6636   4248   2425   -927      1       O  
ATOM    673  CB  PHE A 306     -10.515  15.953 -52.978  1.00 46.40           C  
ANISOU  673  CB  PHE A 306     5482   7343   4807   2753   -959    584       C  
ATOM    674  CG  PHE A 306     -10.552  15.744 -51.489  1.00 48.84           C  
ANISOU  674  CG  PHE A 306     5883   7807   4866   2835  -1022    842       C  
ATOM    675  CD1 PHE A 306     -11.663  16.116 -50.748  1.00 52.41           C  
ANISOU  675  CD1 PHE A 306     6434   8360   5119   2664   -946    833       C  
ATOM    676  CD2 PHE A 306      -9.483  15.162 -50.835  1.00 51.85           C  
ANISOU  676  CD2 PHE A 306     6250   8255   5195   3104  -1153   1098       C  
ATOM    677  CE1 PHE A 306     -11.699  15.922 -49.377  1.00 51.51           C  
ANISOU  677  CE1 PHE A 306     6442   8424   4703   2740   -972   1077       C  
ATOM    678  CE2 PHE A 306      -9.510  14.966 -49.460  1.00 58.25           C  
ANISOU  678  CE2 PHE A 306     7186   9247   5699   3202  -1234   1365       C  
ATOM    679  CZ  PHE A 306     -10.619  15.345 -48.732  1.00 54.59           C  
ANISOU  679  CZ  PHE A 306     6861   8895   4985   3010  -1128   1356       C  
ATOM    680  N   SER A 307      -9.083  17.246 -55.592  1.00 43.16           N  
ANISOU  680  N   SER A 307     4751   6985   4663   2723   -980    135       N  
ATOM    681  CA  SER A 307      -9.091  16.964 -57.019  1.00 45.03           C  
ANISOU  681  CA  SER A 307     5026   7050   5034   2701   -835    -22       C  
ATOM    682  C   SER A 307      -9.237  15.460 -57.199  1.00 47.96           C  
ANISOU  682  C   SER A 307     5538   7121   5563   2820   -697     46       C  
ATOM    683  O   SER A 307      -8.711  14.677 -56.403  1.00 46.85           O  
ANISOU  683  O   SER A 307     5398   6917   5487   3008   -716    259       O  
ATOM    684  CB  SER A 307      -7.809  17.463 -57.688  1.00 43.14           C  
ANISOU  684  CB  SER A 307     4590   6935   4864   2774   -821    -87       C  
ATOM    685  OG  SER A 307      -6.700  16.672 -57.305  1.00 45.72           O  
ANISOU  685  OG  SER A 307     4785   7259   5327   3017   -827     44       O  
ATOM    686  N   ILE A 308      -9.962  15.052 -58.236  1.00 44.27           N  
ANISOU  686  N   ILE A 308     5201   6458   5163   2718   -576   -139       N  
ATOM    687  CA  ILE A 308     -10.366  13.658 -58.366  1.00 46.41           C  
ANISOU  687  CA  ILE A 308     5633   6384   5618   2760   -439   -130       C  
ATOM    688  C   ILE A 308      -9.938  13.131 -59.727  1.00 51.35           C  
ANISOU  688  C   ILE A 308     6296   6857   6359   2829   -304   -361       C  
ATOM    689  O   ILE A 308     -10.310  13.693 -60.762  1.00 46.37           O  
ANISOU  689  O   ILE A 308     5689   6319   5610   2700   -302   -594       O  
ATOM    690  CB  ILE A 308     -11.877  13.483 -58.151  1.00 51.80           C  
ANISOU  690  CB  ILE A 308     6437   6950   6297   2524   -415   -184       C  
ATOM    691  CG1 ILE A 308     -12.193  13.720 -56.670  1.00 52.57           C  
ANISOU  691  CG1 ILE A 308     6527   7168   6280   2501   -471     75       C  
ATOM    692  CG2 ILE A 308     -12.314  12.089 -58.576  1.00 48.57           C  
ANISOU  692  CG2 ILE A 308     6184   6137   6134   2503   -253   -262       C  
ATOM    693  CD1 ILE A 308     -13.630  13.989 -56.381  1.00 51.07           C  
ANISOU  693  CD1 ILE A 308     6364   6992   6047   2255   -444      1       C  
ATOM    694  N   ASN A 309      -9.146  12.062 -59.718  1.00 51.11           N  
ANISOU  694  N   ASN A 309     7514   6742   5163   3138   -163    -51       N  
ATOM    695  CA  ASN A 309      -8.792  11.355 -60.943  1.00 52.32           C  
ANISOU  695  CA  ASN A 309     7876   6630   5375   3368    -32   -286       C  
ATOM    696  C   ASN A 309     -10.009  10.594 -61.457  1.00 52.64           C  
ANISOU  696  C   ASN A 309     8426   6288   5288   3188   -173   -182       C  
ATOM    697  O   ASN A 309     -10.475   9.654 -60.809  1.00 53.44           O  
ANISOU  697  O   ASN A 309     8769   6112   5424   3179   -467     25       O  
ATOM    698  CB  ASN A 309      -7.633  10.400 -60.666  1.00 57.84           C  
ANISOU  698  CB  ASN A 309     8467   7190   6320   3838   -176   -403       C  
ATOM    699  CG  ASN A 309      -7.049   9.808 -61.928  1.00 60.42           C  
ANISOU  699  CG  ASN A 309     8917   7307   6732   4129     48   -733       C  
ATOM    700  OD1 ASN A 309      -7.720   9.070 -62.649  1.00 60.49           O  
ANISOU  700  OD1 ASN A 309     9390   6959   6634   4099      3   -753       O  
ATOM    701  ND2 ASN A 309      -5.790  10.122 -62.199  1.00 63.76           N  
ANISOU  701  ND2 ASN A 309     8912   7952   7361   4402    303  -1021       N  
ATOM    702  N   THR A 310     -10.521  10.983 -62.627  1.00 52.23           N  
ANISOU  702  N   THR A 310     8562   6198   5085   3035     16   -324       N  
ATOM    703  CA  THR A 310     -11.781  10.419 -63.097  1.00 52.12           C  
ANISOU  703  CA  THR A 310     8973   5860   4971   2811   -172   -249       C  
ATOM    704  C   THR A 310     -11.653   8.985 -63.597  1.00 56.35           C  
ANISOU  704  C   THR A 310     9899   5928   5582   3050   -329   -360       C  
ATOM    705  O   THR A 310     -12.673   8.300 -63.724  1.00 57.70           O  
ANISOU  705  O   THR A 310    10407   5772   5743   2853   -563   -269       O  
ATOM    706  CB  THR A 310     -12.373  11.296 -64.203  1.00 51.32           C  
ANISOU  706  CB  THR A 310     8993   5845   4661   2605     -8   -375       C  
ATOM    707  OG1 THR A 310     -11.494  11.309 -65.332  1.00 54.96           O  
ANISOU  707  OG1 THR A 310     9569   6289   5025   2848    273   -666       O  
ATOM    708  CG2 THR A 310     -12.561  12.716 -63.699  1.00 48.01           C  
ANISOU  708  CG2 THR A 310     8225   5823   4194   2376    119   -265       C  
ATOM    709  N   ALA A 311     -10.439   8.515 -63.888  1.00 58.68           N  
ANISOU  709  N   ALA A 311    10136   6170   5990   3465   -207   -582       N  
ATOM    710  CA  ALA A 311     -10.262   7.145 -64.353  1.00 63.10           C  
ANISOU  710  CA  ALA A 311    11078   6252   6647   3743   -359   -726       C  
ATOM    711  C   ALA A 311     -10.145   6.150 -63.210  1.00 66.05           C  
ANISOU  711  C   ALA A 311    11510   6355   7231   3888   -708   -490       C  
ATOM    712  O   ALA A 311     -10.531   4.986 -63.366  1.00 68.90           O  
ANISOU  712  O   ALA A 311    12300   6219   7661   3941   -947   -474       O  
ATOM    713  CB  ALA A 311      -9.020   7.039 -65.244  1.00 65.13           C  
ANISOU  713  CB  ALA A 311    11249   6545   6952   4163    -40  -1119       C  
ATOM    714  N   SER A 312      -9.621   6.586 -62.066  1.00 64.71           N  
ANISOU  714  N   SER A 312    10966   6475   7145   3946   -763   -304       N  
ATOM    715  CA  SER A 312      -9.413   5.727 -60.913  1.00 67.69           C  
ANISOU  715  CA  SER A 312    11443   6618   7659   4110  -1116    -50       C  
ATOM    716  C   SER A 312     -10.246   6.127 -59.707  1.00 66.16           C  
ANISOU  716  C   SER A 312    11232   6579   7327   3711  -1259    354       C  
ATOM    717  O   SER A 312     -10.356   5.336 -58.763  1.00 69.18           O  
ANISOU  717  O   SER A 312    11860   6695   7732   3742  -1554    636       O  
ATOM    718  CB  SER A 312      -7.932   5.736 -60.519  1.00 69.03           C  
ANISOU  718  CB  SER A 312    11223   6961   8044   4611  -1137   -206       C  
ATOM    719  OG  SER A 312      -7.536   7.041 -60.127  1.00 64.57           O  
ANISOU  719  OG  SER A 312    10139   6958   7436   4493   -943   -222       O  
ATOM    720  N   ASN A 313     -10.813   7.331 -59.713  1.00 61.69           N  
ANISOU  720  N   ASN A 313    10414   6418   6606   3353  -1045    381       N  
ATOM    721  CA  ASN A 313     -11.605   7.908 -58.631  1.00 61.23           C  
ANISOU  721  CA  ASN A 313    10272   6584   6407   2973  -1088    691       C  
ATOM    722  C   ASN A 313     -10.809   8.092 -57.344  1.00 62.23           C  
ANISOU  722  C   ASN A 313    10190   6937   6519   3155  -1236    849       C  
ATOM    723  O   ASN A 313     -11.403   8.327 -56.284  1.00 61.01           O  
ANISOU  723  O   ASN A 313    10076   6903   6203   2883  -1305   1130       O  
ATOM    724  CB  ASN A 313     -12.876   7.094 -58.372  1.00 64.44           C  
ANISOU  724  CB  ASN A 313    11090   6616   6776   2623  -1240    949       C  
ATOM    725  CG  ASN A 313     -13.950   7.362 -59.411  1.00 65.32           C  
ANISOU  725  CG  ASN A 313    11276   6669   6875   2302  -1121    812       C  
ATOM    726  OD1 ASN A 313     -15.010   6.736 -59.402  1.00 68.20           O  
ANISOU  726  OD1 ASN A 313    11906   6729   7277   1991  -1232    945       O  
ATOM    727  ND2 ASN A 313     -13.679   8.298 -60.315  1.00 63.12           N  
ANISOU  727  ND2 ASN A 313    10770   6666   6547   2365   -912    546       N  
ATOM    728  N   LYS A 314      -9.481   8.016 -57.411  1.00 65.09           N  
ANISOU  728  N   LYS A 314    10314   7373   7043   3608  -1287    649       N  
ATOM    729  CA  LYS A 314      -8.654   8.386 -56.271  1.00 67.39           C  
ANISOU  729  CA  LYS A 314    10323   7946   7336   3792  -1467    731       C  
ATOM    730  C   LYS A 314      -8.665   9.899 -56.081  1.00 63.62           C  
ANISOU  730  C   LYS A 314     9405   8005   6762   3541  -1223    645       C  
ATOM    731  O   LYS A 314      -8.683  10.666 -57.050  1.00 52.50           O  
ANISOU  731  O   LYS A 314     7784   6769   5394   3434   -897    410       O  
ATOM    732  CB  LYS A 314      -7.221   7.881 -56.451  1.00 73.01           C  
ANISOU  732  CB  LYS A 314    10817   8588   8336   4366  -1616    485       C  
ATOM    733  CG  LYS A 314      -7.072   6.362 -56.389  1.00 79.13           C  
ANISOU  733  CG  LYS A 314    12014   8814   9236   4630  -1924    574       C  
ATOM    734  CD  LYS A 314      -5.642   5.921 -56.703  1.00 85.41           C  
ANISOU  734  CD  LYS A 314    12470   9595  10388   5088  -1979    241       C  
ATOM    735  CE  LYS A 314      -5.368   5.899 -58.196  1.00 87.28           C  
ANISOU  735  CE  LYS A 314    12605   9775  10784   5252  -1616   -155       C  
ATOM    736  NZ  LYS A 314      -4.243   6.786 -58.580  1.00 88.71           N  
ANISOU  736  NZ  LYS A 314    12130  10397  11177   5409  -1328   -512       N  
ATOM    737  N   VAL A 315      -8.666  10.328 -54.821  1.00 61.38           N  
ANISOU  737  N   VAL A 315     9043   7958   6323   3445  -1390    840       N  
ATOM    738  CA  VAL A 315      -8.797  11.739 -54.481  1.00 55.19           C  
ANISOU  738  CA  VAL A 315     7905   7636   5430   3180  -1197    775       C  
ATOM    739  C   VAL A 315      -7.441  12.285 -54.058  1.00 54.96           C  
ANISOU  739  C   VAL A 315     7412   7913   5560   3472  -1313    569       C  
ATOM    740  O   VAL A 315      -6.555  11.555 -53.605  1.00 59.36           O  
ANISOU  740  O   VAL A 315     7953   8356   6243   3858  -1645    568       O  
ATOM    741  CB  VAL A 315      -9.851  11.973 -53.379  1.00 54.13           C  
ANISOU  741  CB  VAL A 315     7995   7587   4985   2814  -1246   1081       C  
ATOM    742  CG1 VAL A 315     -11.204  11.455 -53.826  1.00 54.41           C  
ANISOU  742  CG1 VAL A 315     8388   7335   4950   2492  -1115   1243       C  
ATOM    743  CG2 VAL A 315      -9.420  11.301 -52.075  1.00 59.07           C  
ANISOU  743  CG2 VAL A 315     8850   8141   5454   3001  -1635   1324       C  
ATOM    744  N   THR A 316      -7.283  13.599 -54.219  1.00 51.43           N  
ANISOU  744  N   THR A 316     6570   7835   5137   3284  -1062    380       N  
ATOM    745  CA  THR A 316      -6.068  14.303 -53.829  1.00 53.16           C  
ANISOU  745  CA  THR A 316     6280   8375   5543   3463  -1138    150       C  
ATOM    746  C   THR A 316      -6.434  15.604 -53.126  1.00 50.72           C  
ANISOU  746  C   THR A 316     5803   8414   5055   3127  -1062    158       C  
ATOM    747  O   THR A 316      -7.082  16.473 -53.724  1.00 47.86           O  
ANISOU  747  O   THR A 316     5405   8136   4643   2818   -720    101       O  
ATOM    748  CB  THR A 316      -5.177  14.588 -55.040  1.00 54.27           C  
ANISOU  748  CB  THR A 316     6032   8570   6017   3612   -820   -203       C  
ATOM    749  OG1 THR A 316      -4.645  13.356 -55.544  1.00 57.84           O  
ANISOU  749  OG1 THR A 316     6589   8720   6667   4008   -928   -273       O  
ATOM    750  CG2 THR A 316      -4.025  15.505 -54.643  1.00 55.61           C  
ANISOU  750  CG2 THR A 316     5598   9104   6427   3680   -837   -463       C  
ATOM    751  N   PRO A 317      -6.026  15.778 -51.871  1.00 52.82           N  
ANISOU  751  N   PRO A 317     5991   8865   5211   3199  -1401    210       N  
ATOM    752  CA  PRO A 317      -6.495  16.932 -51.096  1.00 50.78           C  
ANISOU  752  CA  PRO A 317     5666   8901   4725   2880  -1347    217       C  
ATOM    753  C   PRO A 317      -5.928  18.245 -51.610  1.00 49.81           C  
ANISOU  753  C   PRO A 317     5041   9040   4844   2748  -1082   -107       C  
ATOM    754  O   PRO A 317      -4.795  18.321 -52.092  1.00 52.27           O  
ANISOU  754  O   PRO A 317     4942   9416   5504   2947  -1063   -360       O  
ATOM    755  CB  PRO A 317      -5.999  16.631 -49.675  1.00 53.94           C  
ANISOU  755  CB  PRO A 317     6156   9403   4933   3064  -1840    321       C  
ATOM    756  CG  PRO A 317      -4.827  15.725 -49.868  1.00 61.01           C  
ANISOU  756  CG  PRO A 317     6907  10105   6168   3450  -2099    216       C  
ATOM    757  CD  PRO A 317      -5.148  14.895 -51.084  1.00 57.02           C  
ANISOU  757  CD  PRO A 317     6548   9320   5798   3601  -1895    262       C  
ATOM    758  N   ILE A 318      -6.748  19.286 -51.498  1.00 45.21           N  
ANISOU  758  N   ILE A 318     4494   8590   4094   2398   -857   -104       N  
ATOM    759  CA  ILE A 318      -6.397  20.645 -51.892  1.00 52.70           C  
ANISOU  759  CA  ILE A 318     5067   9733   5222   2203   -603   -367       C  
ATOM    760  C   ILE A 318      -6.591  21.540 -50.677  1.00 51.45           C  
ANISOU  760  C   ILE A 318     4872   9817   4859   2032   -762   -404       C  
ATOM    761  O   ILE A 318      -7.704  21.633 -50.144  1.00 50.51           O  
ANISOU  761  O   ILE A 318     5074   9693   4426   1856   -730   -233       O  
ATOM    762  CB  ILE A 318      -7.261  21.140 -53.063  1.00 48.79           C  
ANISOU  762  CB  ILE A 318     4705   9101   4731   1964   -185   -354       C  
ATOM    763  CG1 ILE A 318      -6.920  20.395 -54.353  1.00 49.17           C  
ANISOU  763  CG1 ILE A 318     4790   8934   4960   2128     -1   -389       C  
ATOM    764  CG2 ILE A 318      -7.088  22.628 -53.253  1.00 46.89           C  
ANISOU  764  CG2 ILE A 318     4199   9017   4601   1720     40   -561       C  
ATOM    765  CD1 ILE A 318      -7.814  20.783 -55.523  1.00 46.62           C  
ANISOU  765  CD1 ILE A 318     4697   8448   4569   1919    332   -356       C  
ATOM    766  N   ASP A 319      -5.522  22.198 -50.240  1.00 53.67           N  
ANISOU  766  N   ASP A 319     4750  10312   5329   2076   -921   -657       N  
ATOM    767  CA  ASP A 319      -5.627  23.137 -49.130  1.00 55.38           C  
ANISOU  767  CA  ASP A 319     4934  10752   5354   1911  -1082   -758       C  
ATOM    768  C   ASP A 319      -6.097  24.490 -49.643  1.00 49.42           C  
ANISOU  768  C   ASP A 319     4072  10021   4683   1583   -707   -909       C  
ATOM    769  O   ASP A 319      -5.650  24.959 -50.692  1.00 47.43           O  
ANISOU  769  O   ASP A 319     3568   9704   4751   1505   -423  -1050       O  
ATOM    770  CB  ASP A 319      -4.284  23.290 -48.416  1.00 63.98           C  
ANISOU  770  CB  ASP A 319     5645  12028   6638   2079  -1474   -996       C  
ATOM    771  CG  ASP A 319      -3.230  23.944 -49.292  1.00 70.94           C  
ANISOU  771  CG  ASP A 319     6013  12899   8042   2000  -1240  -1297       C  
ATOM    772  OD1 ASP A 319      -2.632  23.242 -50.134  1.00 73.92           O  
ANISOU  772  OD1 ASP A 319     6249  13129   8707   2167  -1125  -1309       O  
ATOM    773  OD2 ASP A 319      -3.005  25.165 -49.147  1.00 73.29           O  
ANISOU  773  OD2 ASP A 319     6101  13288   8458   1736  -1136  -1517       O  
ATOM    774  N   ILE A 320      -6.997  25.120 -48.895  1.00 47.70           N  
ANISOU  774  N   ILE A 320     4075   9880   4169   1397   -694   -882       N  
ATOM    775  CA  ILE A 320      -7.621  26.362 -49.342  1.00 47.10           C  
ANISOU  775  CA  ILE A 320     3970   9768   4159   1125   -374  -1003       C  
ATOM    776  C   ILE A 320      -6.644  27.518 -49.173  1.00 49.52           C  
ANISOU  776  C   ILE A 320     3895  10197   4723   1006   -415  -1330       C  
ATOM    777  O   ILE A 320      -6.112  27.747 -48.080  1.00 45.64           O  
ANISOU  777  O   ILE A 320     3299   9900   4143   1039   -738  -1484       O  
ATOM    778  CB  ILE A 320      -8.927  26.624 -48.576  1.00 46.77           C  
ANISOU  778  CB  ILE A 320     4249   9764   3758    998   -327   -910       C  
ATOM    779  CG1 ILE A 320      -9.918  25.478 -48.801  1.00 44.03           C  
ANISOU  779  CG1 ILE A 320     4233   9274   3223   1053   -251   -596       C  
ATOM    780  CG2 ILE A 320      -9.534  27.952 -48.997  1.00 44.79           C  
ANISOU  780  CG2 ILE A 320     3948   9447   3622    776    -56  -1070       C  
ATOM    781  CD1 ILE A 320     -10.120  25.126 -50.255  1.00 40.82           C  
ANISOU  781  CD1 ILE A 320     3829   8628   3054   1066    -30   -505       C  
ATOM    782  N   LEU A 321      -6.429  28.266 -50.253  1.00 41.62           N  
ANISOU  782  N   LEU A 321     2725   9066   4024    844    -95  -1436       N  
ATOM    783  CA  LEU A 321      -5.538  29.416 -50.234  1.00 46.38           C  
ANISOU  783  CA  LEU A 321     2970   9725   4926    657    -61  -1738       C  
ATOM    784  C   LEU A 321      -6.148  30.538 -49.391  1.00 44.78           C  
ANISOU  784  C   LEU A 321     2891   9564   4559    473   -123  -1882       C  
ATOM    785  O   LEU A 321      -7.348  30.520 -49.100  1.00 42.02           O  
ANISOU  785  O   LEU A 321     2882   9175   3908    475    -74  -1747       O  
ATOM    786  CB  LEU A 321      -5.275  29.885 -51.667  1.00 47.49           C  
ANISOU  786  CB  LEU A 321     3112   9572   5360    479    344  -1718       C  
ATOM    787  CG  LEU A 321      -4.609  28.846 -52.570  1.00 48.77           C  
ANISOU  787  CG  LEU A 321     3237   9604   5687    634    450  -1602       C  
ATOM    788  CD1 LEU A 321      -4.315  29.408 -53.958  1.00 49.44           C  
ANISOU  788  CD1 LEU A 321     3404   9379   6001    426    861  -1568       C  
ATOM    789  CD2 LEU A 321      -3.343  28.347 -51.936  1.00 52.54           C  
ANISOU  789  CD2 LEU A 321     3328  10256   6379    797    170  -1770       C  
ATOM    790  N   PRO A 322      -5.342  31.530 -48.989  1.00 46.69           N  
ANISOU  790  N   PRO A 322     2840   9878   5023    307   -221  -2190       N  
ATOM    791  CA  PRO A 322      -5.837  32.522 -48.012  1.00 47.47           C  
ANISOU  791  CA  PRO A 322     3073  10026   4937    174   -346  -2382       C  
ATOM    792  C   PRO A 322      -7.112  33.245 -48.422  1.00 50.15           C  
ANISOU  792  C   PRO A 322     3731  10151   5172     54    -46  -2308       C  
ATOM    793  O   PRO A 322      -7.926  33.570 -47.549  1.00 48.66           O  
ANISOU  793  O   PRO A 322     3763  10029   4697     64   -124  -2374       O  
ATOM    794  CB  PRO A 322      -4.660  33.498 -47.885  1.00 51.26           C  
ANISOU  794  CB  PRO A 322     3146  10530   5801    -35   -439  -2735       C  
ATOM    795  CG  PRO A 322      -3.462  32.670 -48.179  1.00 56.98           C  
ANISOU  795  CG  PRO A 322     3574  11288   6789     98   -538  -2705       C  
ATOM    796  CD  PRO A 322      -3.899  31.702 -49.252  1.00 50.26           C  
ANISOU  796  CD  PRO A 322     2868  10330   5898    243   -259  -2388       C  
ATOM    797  N   LEU A 323      -7.317  33.518 -49.708  1.00 47.59           N  
ANISOU  797  N   LEU A 323     3450   9570   5060    -44    285  -2190       N  
ATOM    798  CA  LEU A 323      -8.481  34.284 -50.139  1.00 47.44           C  
ANISOU  798  CA  LEU A 323     3719   9314   4993   -125    493  -2141       C  
ATOM    799  C   LEU A 323      -9.716  33.420 -50.377  1.00 47.52           C  
ANISOU  799  C   LEU A 323     4007   9300   4750     48    554  -1867       C  
ATOM    800  O   LEU A 323     -10.747  33.942 -50.818  1.00 46.98           O  
ANISOU  800  O   LEU A 323     4164   8990   4699     19    665  -1796       O  
ATOM    801  CB  LEU A 323      -8.155  35.088 -51.399  1.00 47.95           C  
ANISOU  801  CB  LEU A 323     3782   9071   5364   -323    777  -2135       C  
ATOM    802  CG  LEU A 323      -7.311  36.348 -51.199  1.00 50.63           C  
ANISOU  802  CG  LEU A 323     3926   9318   5994   -592    789  -2428       C  
ATOM    803  CD1 LEU A 323      -7.143  37.089 -52.518  1.00 51.07           C  
ANISOU  803  CD1 LEU A 323     4102   9015   6288   -812   1129  -2345       C  
ATOM    804  CD2 LEU A 323      -7.932  37.253 -50.147  1.00 52.46           C  
ANISOU  804  CD2 LEU A 323     4273   9546   6115   -620    617  -2662       C  
ATOM    805  N   GLY A 324      -9.646  32.128 -50.103  1.00 46.59           N  
ANISOU  805  N   GLY A 324     3899   9350   4453    219    434  -1692       N  
ATOM    806  CA  GLY A 324     -10.841  31.313 -50.064  1.00 45.20           C  
ANISOU  806  CA  GLY A 324     4007   9073   4094    314    418  -1422       C  
ATOM    807  C   GLY A 324     -10.909  30.294 -51.188  1.00 40.97           C  
ANISOU  807  C   GLY A 324     3591   8331   3646    393    479  -1148       C  
ATOM    808  O   GLY A 324      -9.957  30.074 -51.947  1.00 39.35           O  
ANISOU  808  O   GLY A 324     3267   8091   3595    410    547  -1152       O  
ATOM    809  N   VAL A 325     -12.083  29.668 -51.282  1.00 41.15           N  
ANISOU  809  N   VAL A 325     4486   6143   5008    262   -214  -1821       N  
ATOM    810  CA  VAL A 325     -12.238  28.489 -52.126  1.00 39.75           C  
ANISOU  810  CA  VAL A 325     4360   5975   4769    371   -216  -1662       C  
ATOM    811  C   VAL A 325     -12.147  28.864 -53.599  1.00 36.86           C  
ANISOU  811  C   VAL A 325     3660   5696   4650    375   -343  -1540       C  
ATOM    812  O   VAL A 325     -11.445  28.207 -54.377  1.00 35.96           O  
ANISOU  812  O   VAL A 325     3511   5732   4419    489   -478  -1421       O  
ATOM    813  CB  VAL A 325     -13.563  27.773 -51.808  1.00 41.40           C  
ANISOU  813  CB  VAL A 325     4766   5915   5050    284    123  -1744       C  
ATOM    814  CG1 VAL A 325     -13.796  26.630 -52.785  1.00 41.03           C  
ANISOU  814  CG1 VAL A 325     4683   5870   5038    317    180  -1707       C  
ATOM    815  CG2 VAL A 325     -13.558  27.268 -50.374  1.00 46.08           C  
ANISOU  815  CG2 VAL A 325     5867   6350   5290    358    359  -1789       C  
ATOM    816  N   MET A 326     -12.860  29.915 -54.010  1.00 35.49           N  
ANISOU  816  N   MET A 326     3293   5417   4775    317   -274  -1549       N  
ATOM    817  CA  MET A 326     -12.825  30.290 -55.421  1.00 36.49           C  
ANISOU  817  CA  MET A 326     3233   5614   5017    459   -359  -1383       C  
ATOM    818  C   MET A 326     -11.432  30.756 -55.820  1.00 36.81           C  
ANISOU  818  C   MET A 326     3241   5718   5028    454   -398  -1275       C  
ATOM    819  O   MET A 326     -10.961  30.458 -56.923  1.00 35.29           O  
ANISOU  819  O   MET A 326     3011   5627   4772    583   -465  -1118       O  
ATOM    820  CB  MET A 326     -13.857  31.377 -55.721  1.00 37.39           C  
ANISOU  820  CB  MET A 326     3232   5593   5380    550   -255  -1381       C  
ATOM    821  CG  MET A 326     -15.248  30.878 -56.117  1.00 38.03           C  
ANISOU  821  CG  MET A 326     3142   5764   5545    676   -298  -1541       C  
ATOM    822  SD  MET A 326     -15.290  29.535 -57.335  1.00 37.42           S  
ANISOU  822  SD  MET A 326     2940   5986   5291    818   -503  -1585       S  
ATOM    823  CE  MET A 326     -14.229  30.186 -58.632  1.00 37.49           C  
ANISOU  823  CE  MET A 326     3033   6089   5124   1106   -634  -1206       C  
ATOM    824  N   ALA A 327     -10.752  31.483 -54.929  1.00 37.34           N  
ANISOU  824  N   ALA A 327     3291   5737   5161    284   -321  -1437       N  
ATOM    825  CA  ALA A 327      -9.364  31.848 -55.192  1.00 38.91           C  
ANISOU  825  CA  ALA A 327     3349   6024   5409    203   -305  -1512       C  
ATOM    826  C   ALA A 327      -8.493  30.615 -55.355  1.00 38.49           C  
ANISOU  826  C   ALA A 327     3273   6263   5087    329   -551  -1508       C  
ATOM    827  O   ALA A 327      -7.534  30.630 -56.137  1.00 41.32           O  
ANISOU  827  O   ALA A 327     3490   6703   5507    331   -531  -1488       O  
ATOM    828  CB  ALA A 327      -8.819  32.733 -54.071  1.00 41.77           C  
ANISOU  828  CB  ALA A 327     3596   6377   5898    -31   -209  -1876       C  
ATOM    829  N   THR A 328      -8.825  29.533 -54.646  1.00 37.92           N  
ANISOU  829  N   THR A 328     3388   6294   4724    456   -703  -1516       N  
ATOM    830  CA  THR A 328      -8.050  28.301 -54.744  1.00 37.76           C  
ANISOU  830  CA  THR A 328     3437   6496   4416    665   -884  -1474       C  
ATOM    831  C   THR A 328      -8.319  27.590 -56.062  1.00 36.70           C  
ANISOU  831  C   THR A 328     3320   6321   4305    737   -855  -1239       C  
ATOM    832  O   THR A 328      -7.384  27.243 -56.797  1.00 35.48           O  
ANISOU  832  O   THR A 328     3053   6309   4118    817   -926  -1188       O  
ATOM    833  CB  THR A 328      -8.377  27.381 -53.567  1.00 38.18           C  
ANISOU  833  CB  THR A 328     3843   6554   4111    847   -910  -1504       C  
ATOM    834  OG1 THR A 328      -8.091  28.056 -52.335  1.00 42.90           O  
ANISOU  834  OG1 THR A 328     4442   7264   4594    843   -984  -1761       O  
ATOM    835  CG2 THR A 328      -7.553  26.108 -53.647  1.00 36.27           C  
ANISOU  835  CG2 THR A 328     3757   6488   3535   1170  -1042  -1416       C  
ATOM    836  N   LEU A 329      -9.598  27.354 -56.368  1.00 33.75           N  
ANISOU  836  N   LEU A 329     3039   5788   3995    709   -748  -1171       N  
ATOM    837  CA  LEU A 329      -9.966  26.691 -57.614  1.00 34.27           C  
ANISOU  837  CA  LEU A 329     3067   5894   4060    786   -755  -1072       C  
ATOM    838  C   LEU A 329      -9.438  27.453 -58.820  1.00 33.65           C  
ANISOU  838  C   LEU A 329     2840   5879   4067    848   -780   -927       C  
ATOM    839  O   LEU A 329      -8.935  26.845 -59.773  1.00 36.22           O  
ANISOU  839  O   LEU A 329     3158   6317   4287    948   -822   -838       O  
ATOM    840  CB  LEU A 329     -11.485  26.543 -57.688  1.00 34.39           C  
ANISOU  840  CB  LEU A 329     3057   5814   4196    735   -657  -1201       C  
ATOM    841  CG  LEU A 329     -12.073  25.446 -56.802  1.00 34.76           C  
ANISOU  841  CG  LEU A 329     3323   5701   4183    643   -446  -1362       C  
ATOM    842  CD1 LEU A 329     -13.592  25.573 -56.722  1.00 35.74           C  
ANISOU  842  CD1 LEU A 329     3299   5724   4557    507   -281  -1631       C  
ATOM    843  CD2 LEU A 329     -11.659  24.072 -57.318  1.00 35.43           C  
ANISOU  843  CD2 LEU A 329     3542   5806   4115    710   -381  -1345       C  
ATOM    844  N   THR A 330      -9.515  28.785 -58.784  1.00 32.38           N  
ANISOU  844  N   THR A 330     2626   5589   4087    800   -669   -896       N  
ATOM    845  CA  THR A 330      -9.013  29.586 -59.896  1.00 34.86           C  
ANISOU  845  CA  THR A 330     2944   5836   4466    891   -522   -716       C  
ATOM    846  C   THR A 330      -7.538  29.298 -60.159  1.00 35.50           C  
ANISOU  846  C   THR A 330     2946   5999   4542    811   -475   -743       C  
ATOM    847  O   THR A 330      -7.121  29.135 -61.313  1.00 34.77           O  
ANISOU  847  O   THR A 330     2909   5926   4375    932   -392   -585       O  
ATOM    848  CB  THR A 330      -9.234  31.071 -59.617  1.00 35.19           C  
ANISOU  848  CB  THR A 330     3025   5605   4740    831   -260   -696       C  
ATOM    849  OG1 THR A 330     -10.641  31.334 -59.544  1.00 36.49           O  
ANISOU  849  OG1 THR A 330     3227   5727   4909    994   -318   -671       O  
ATOM    850  CG2 THR A 330      -8.629  31.919 -60.727  1.00 37.89           C  
ANISOU  850  CG2 THR A 330     3511   5742   5143    941     77   -478       C  
ATOM    851  N   GLN A 331      -6.734  29.219 -59.097  1.00 33.78           N  
ANISOU  851  N   GLN A 331     2580   5876   4379    653   -539   -990       N  
ATOM    852  CA  GLN A 331      -5.317  28.915 -59.276  1.00 35.33           C  
ANISOU  852  CA  GLN A 331     2580   6240   4604    617   -542  -1135       C  
ATOM    853  C   GLN A 331      -5.109  27.497 -59.793  1.00 35.41           C  
ANISOU  853  C   GLN A 331     2662   6435   4358    825   -732  -1014       C  
ATOM    854  O   GLN A 331      -4.279  27.274 -60.678  1.00 38.50           O  
ANISOU  854  O   GLN A 331     2973   6878   4779    853   -640   -978       O  
ATOM    855  CB  GLN A 331      -4.560  29.122 -57.962  1.00 36.42           C  
ANISOU  855  CB  GLN A 331     2474   6574   4790    513   -673  -1535       C  
ATOM    856  CG  GLN A 331      -4.467  30.575 -57.547  1.00 38.46           C  
ANISOU  856  CG  GLN A 331     2580   6643   5389    218   -391  -1785       C  
ATOM    857  CD  GLN A 331      -3.776  31.423 -58.596  1.00 41.49           C  
ANISOU  857  CD  GLN A 331     2869   6777   6118     25     80  -1796       C  
ATOM    858  OE1 GLN A 331      -2.729  31.045 -59.121  1.00 42.69           O  
ANISOU  858  OE1 GLN A 331     2812   7074   6336      8    128  -1928       O  
ATOM    859  NE2 GLN A 331      -4.351  32.581 -58.897  1.00 43.55           N  
ANISOU  859  NE2 GLN A 331     3326   6616   6603    -93    504  -1656       N  
ATOM    860  N   HIS A 332      -5.847  26.525 -59.257  1.00 33.99           N  
ANISOU  860  N   HIS A 332     2663   6296   3955    949   -902   -971       N  
ATOM    861  CA AHIS A 332      -5.681  25.140 -59.694  0.50 33.24           C  
ANISOU  861  CA AHIS A 332     2730   6241   3657   1101   -941   -872       C  
ATOM    862  CA BHIS A 332      -5.661  25.147 -59.698  0.50 33.26           C  
ANISOU  862  CA BHIS A 332     2731   6246   3662   1101   -941   -873       C  
ATOM    863  C   HIS A 332      -6.077  24.972 -61.154  1.00 32.13           C  
ANISOU  863  C   HIS A 332     2606   6089   3514   1131   -869   -725       C  
ATOM    864  O   HIS A 332      -5.439  24.216 -61.897  1.00 31.75           O  
ANISOU  864  O   HIS A 332     2579   6102   3382   1209   -844   -677       O  
ATOM    865  CB AHIS A 332      -6.509  24.209 -58.805  0.50 33.19           C  
ANISOU  865  CB AHIS A 332     2956   6195   3459   1208   -981   -899       C  
ATOM    866  CB BHIS A 332      -6.441  24.193 -58.790  0.50 33.27           C  
ANISOU  866  CB BHIS A 332     2963   6214   3463   1216   -986   -900       C  
ATOM    867  CG AHIS A 332      -6.176  22.757 -58.962  0.50 33.42           C  
ANISOU  867  CG AHIS A 332     3187   6228   3281   1409   -941   -842       C  
ATOM    868  CG BHIS A 332      -5.735  23.863 -57.510  0.50 34.70           C  
ANISOU  868  CG BHIS A 332     3256   6493   3436   1409  -1089   -994       C  
ATOM    869  ND1AHIS A 332      -6.790  21.948 -59.893  0.50 32.90           N  
ANISOU  869  ND1AHIS A 332     3208   6067   3226   1363   -798   -814       N  
ATOM    870  ND1BHIS A 332      -4.822  22.836 -57.407  0.50 36.35           N  
ANISOU  870  ND1BHIS A 332     3594   6781   3435   1688  -1119   -959       N  
ATOM    871  CD2AHIS A 332      -5.308  21.964 -58.290  0.50 35.49           C  
ANISOU  871  CD2AHIS A 332     3603   6579   3304   1707  -1002   -836       C  
ATOM    872  CD2BHIS A 332      -5.809  24.425 -56.280  0.50 36.01           C  
ANISOU  872  CD2BHIS A 332     3454   6708   3522   1432  -1172  -1136       C  
ATOM    873  CE1AHIS A 332      -6.307  20.722 -59.797  0.50 33.58           C  
ANISOU  873  CE1AHIS A 332     3519   6100   3142   1555   -695   -774       C  
ATOM    874  CE1BHIS A 332      -4.365  22.778 -56.169  0.50 39.25           C  
ANISOU  874  CE1BHIS A 332     4085   7248   3580   1925  -1221  -1059       C  
ATOM    875  NE2AHIS A 332      -5.406  20.705 -58.831  0.50 36.05           N  
ANISOU  875  NE2AHIS A 332     3906   6516   3276   1818   -822   -745       N  
ATOM    876  NE2BHIS A 332      -4.949  23.731 -55.465  0.50 38.65           N  
ANISOU  876  NE2BHIS A 332     3957   7165   3564   1761  -1260  -1176       N  
ATOM    877  N   ILE A 333      -7.128  25.674 -61.584  1.00 30.90           N  
ANISOU  877  N   ILE A 333     2462   5868   3412   1120   -838   -671       N  
ATOM    878  CA  ILE A 333      -7.629  25.527 -62.947  1.00 33.57           C  
ANISOU  878  CA  ILE A 333     2849   6275   3633   1266   -834   -577       C  
ATOM    879  C   ILE A 333      -6.760  26.293 -63.937  1.00 34.88           C  
ANISOU  879  C   ILE A 333     3059   6394   3801   1341   -654   -394       C  
ATOM    880  O   ILE A 333      -6.375  25.761 -64.984  1.00 36.98           O  
ANISOU  880  O   ILE A 333     3391   6751   3907   1460   -619   -322       O  
ATOM    881  CB  ILE A 333      -9.100  25.982 -63.022  1.00 33.28           C  
ANISOU  881  CB  ILE A 333     2815   6225   3605   1332   -893   -637       C  
ATOM    882  CG1 ILE A 333      -9.994  25.036 -62.226  1.00 33.73           C  
ANISOU  882  CG1 ILE A 333     2857   6249   3711   1182   -910   -885       C  
ATOM    883  CG2 ILE A 333      -9.573  26.030 -64.473  1.00 34.90           C  
ANISOU  883  CG2 ILE A 333     3093   6564   3604   1585   -934   -579       C  
ATOM    884  CD1 ILE A 333     -11.249  25.688 -61.671  1.00 34.81           C  
ANISOU  884  CD1 ILE A 333     2892   6343   3990   1160   -926  -1033       C  
ATOM    885  N   THR A 334      -6.457  27.561 -63.642  1.00 33.61           N  
ANISOU  885  N   THR A 334     2900   6036   3833   1256   -445   -340       N  
ATOM    886  CA  THR A 334      -5.740  28.375 -64.619  1.00 36.48           C  
ANISOU  886  CA  THR A 334     3407   6219   4233   1311    -81   -166       C  
ATOM    887  C   THR A 334      -4.288  27.939 -64.760  1.00 35.62           C  
ANISOU  887  C   THR A 334     3132   6151   4251   1143     66   -290       C  
ATOM    888  O   THR A 334      -3.738  27.979 -65.866  1.00 37.61           O  
ANISOU  888  O   THR A 334     3535   6323   4431   1228    340   -152       O  
ATOM    889  CB  THR A 334      -5.815  29.857 -64.253  1.00 39.63           C  
ANISOU  889  CB  THR A 334     3892   6290   4877   1221    261   -123       C  
ATOM    890  OG1 THR A 334      -5.235  30.067 -62.966  1.00 38.79           O  
ANISOU  890  OG1 THR A 334     3488   6179   5072    877    250   -439       O  
ATOM    891  CG2 THR A 334      -7.265  30.337 -64.242  1.00 39.62           C  
ANISOU  891  CG2 THR A 334     4055   6261   4738   1490    126     15       C  
ATOM    892  N   GLN A 335      -3.653  27.512 -63.666  1.00 34.74           N  
ANISOU  892  N   GLN A 335     2720   6188   4291    966   -111   -571       N  
ATOM    893  CA  GLN A 335      -2.306  26.967 -63.782  1.00 36.04           C  
ANISOU  893  CA  GLN A 335     2640   6496   4558    905    -62   -762       C  
ATOM    894  C   GLN A 335      -2.315  25.667 -64.573  1.00 38.09           C  
ANISOU  894  C   GLN A 335     3025   6903   4545   1113   -205   -620       C  
ATOM    895  O   GLN A 335      -1.404  25.414 -65.369  1.00 38.69           O  
ANISOU  895  O   GLN A 335     3046   6991   4664   1117     -5   -635       O  
ATOM    896  CB  GLN A 335      -1.697  26.753 -62.393  1.00 36.46           C  
ANISOU  896  CB  GLN A 335     2351   6787   4716    843   -323  -1125       C  
ATOM    897  CG  GLN A 335      -1.372  28.040 -61.642  1.00 38.94           C  
ANISOU  897  CG  GLN A 335     2419   7014   5364    568   -137  -1440       C  
ATOM    898  CD  GLN A 335      -0.615  27.791 -60.341  1.00 43.73           C  
ANISOU  898  CD  GLN A 335     2671   7967   5979    588   -462  -1891       C  
ATOM    899  OE1 GLN A 335       0.161  26.840 -60.226  1.00 43.81           O  
ANISOU  899  OE1 GLN A 335     2713   8130   5804    770   -658  -1939       O  
ATOM    900  NE2 GLN A 335      -0.837  28.656 -59.355  1.00 45.79           N  
ANISOU  900  NE2 GLN A 335     2847   8196   6357    417   -468  -2138       N  
ATOM    901  N   ASN A 336      -3.344  24.833 -64.378  1.00 37.33           N  
ANISOU  901  N   ASN A 336     3090   6885   4208   1248   -476   -537       N  
ATOM    902  CA  ASN A 336      -3.455  23.605 -65.161  1.00 39.17           C  
ANISOU  902  CA  ASN A 336     3446   7216   4222   1392   -535   -479       C  
ATOM    903  C   ASN A 336      -3.687  23.915 -66.634  1.00 39.74           C  
ANISOU  903  C   ASN A 336     3704   7258   4136   1493   -365   -313       C  
ATOM    904  O   ASN A 336      -3.125  23.249 -67.513  1.00 42.89           O  
ANISOU  904  O   ASN A 336     4154   7718   4425   1565   -267   -294       O  
ATOM    905  CB  ASN A 336      -4.582  22.730 -64.613  1.00 38.32           C  
ANISOU  905  CB  ASN A 336     3453   7127   3979   1430   -718   -539       C  
ATOM    906  CG  ASN A 336      -4.069  21.621 -63.720  1.00 39.62           C  
ANISOU  906  CG  ASN A 336     3668   7280   4106   1495   -756   -618       C  
ATOM    907  OD1 ASN A 336      -3.139  20.908 -64.078  1.00 42.73           O  
ANISOU  907  OD1 ASN A 336     4026   7750   4460   1620   -718   -622       O  
ATOM    908  ND2 ASN A 336      -4.659  21.487 -62.538  1.00 39.17           N  
ANISOU  908  ND2 ASN A 336     3715   7141   4026   1493   -813   -670       N  
ATOM    909  N   LYS A 337      -4.517  24.920 -66.922  1.00 39.19           N  
ANISOU  909  N   LYS A 337     3781   7105   4004   1574   -320   -184       N  
ATOM    910  CA  LYS A 337      -4.686  25.360 -68.301  1.00 41.29           C  
ANISOU  910  CA  LYS A 337     4331   7353   4005   1826   -142     20       C  
ATOM    911  C   LYS A 337      -3.365  25.853 -68.879  1.00 42.84           C  
ANISOU  911  C   LYS A 337     4615   7333   4331   1745    324    125       C  
ATOM    912  O   LYS A 337      -3.076  25.646 -70.066  1.00 44.03           O  
ANISOU  912  O   LYS A 337     5011   7491   4229   1927    518    255       O  
ATOM    913  CB  LYS A 337      -5.750  26.456 -68.371  1.00 43.42           C  
ANISOU  913  CB  LYS A 337     4783   7551   4162   2050   -157    165       C  
ATOM    914  CG  LYS A 337      -5.980  27.031 -69.760  1.00 49.31           C  
ANISOU  914  CG  LYS A 337     5948   8284   4503   2498     29    435       C  
ATOM    915  CD  LYS A 337      -7.177  27.980 -69.761  1.00 53.01           C  
ANISOU  915  CD  LYS A 337     6586   8759   4799   2873    -81    557       C  
ATOM    916  CE  LYS A 337      -7.314  28.695 -71.087  1.00 61.04           C  
ANISOU  916  CE  LYS A 337     8154   9721   5315   3480    161    902       C  
ATOM    917  NZ  LYS A 337      -7.208  27.725 -72.207  1.00 63.91           N  
ANISOU  917  NZ  LYS A 337     8603  10440   5241   3715    -14    828       N  
ATOM    918  N   GLU A 338      -2.550  26.511 -68.052  1.00 42.30           N  
ANISOU  918  N   GLU A 338     4325   7079   4667   1456    548     -3       N  
ATOM    919  CA  GLU A 338      -1.257  27.002 -68.516  1.00 46.56           C  
ANISOU  919  CA  GLU A 338     4833   7392   5464   1279   1089    -58       C  
ATOM    920  C   GLU A 338      -0.346  25.853 -68.927  1.00 45.23           C  
ANISOU  920  C   GLU A 338     4479   7419   5286   1263   1045   -197       C  
ATOM    921  O   GLU A 338       0.330  25.929 -69.960  1.00 46.65           O  
ANISOU  921  O   GLU A 338     4833   7449   5442   1279   1484   -120       O  
ATOM    922  CB  GLU A 338      -0.603  27.850 -67.426  1.00 51.93           C  
ANISOU  922  CB  GLU A 338     5154   7934   6642    923   1282   -370       C  
ATOM    923  CG  GLU A 338       0.747  28.429 -67.803  1.00 60.58           C  
ANISOU  923  CG  GLU A 338     6085   8784   8150    634   1935   -608       C  
ATOM    924  CD  GLU A 338       1.059  29.707 -67.048  1.00 67.46           C  
ANISOU  924  CD  GLU A 338     6755   9374   9502    277   2344   -909       C  
ATOM    925  OE1 GLU A 338       0.235  30.111 -66.199  1.00 66.81           O  
ANISOU  925  OE1 GLU A 338     6680   9313   9390    289   2061   -888       O  
ATOM    926  OE2 GLU A 338       2.127  30.304 -67.302  1.00 73.69           O  
ANISOU  926  OE2 GLU A 338     7358   9901  10738    -52   3006  -1227       O  
ATOM    927  N   LEU A 339      -0.317  24.778 -68.131  1.00 41.55           N  
ANISOU  927  N   LEU A 339     3724   7242   4822   1270    585   -382       N  
ATOM    928  CA  LEU A 339       0.495  23.615 -68.484  1.00 42.44           C  
ANISOU  928  CA  LEU A 339     3697   7519   4910   1333    547   -493       C  
ATOM    929  C   LEU A 339       0.053  23.020 -69.814  1.00 42.15           C  
ANISOU  929  C   LEU A 339     4030   7488   4496   1523    621   -278       C  
ATOM    930  O   LEU A 339       0.889  22.654 -70.649  1.00 44.92           O  
ANISOU  930  O   LEU A 339     4403   7812   4850   1533    902   -297       O  
ATOM    931  CB  LEU A 339       0.410  22.555 -67.386  1.00 41.09           C  
ANISOU  931  CB  LEU A 339     3331   7578   4704   1436    101   -640       C  
ATOM    932  CG  LEU A 339       1.208  22.760 -66.098  1.00 43.42           C  
ANISOU  932  CG  LEU A 339     3209   8030   5259   1399    -60   -949       C  
ATOM    933  CD1 LEU A 339       0.994  21.577 -65.173  1.00 43.29           C  
ANISOU  933  CD1 LEU A 339     3276   8150   5023   1652   -430   -954       C  
ATOM    934  CD2 LEU A 339       2.686  22.948 -66.394  1.00 46.54           C  
ANISOU  934  CD2 LEU A 339     3196   8508   5981   1309    201  -1257       C  
ATOM    935  N   ILE A 340      -1.261  22.913 -70.021  1.00 40.05           N  
ANISOU  935  N   ILE A 340     4013   7299   3907   1683    367   -149       N  
ATOM    936  CA  ILE A 340      -1.788  22.367 -71.270  1.00 43.64           C  
ANISOU  936  CA  ILE A 340     4758   7876   3948   1907    354    -70       C  
ATOM    937  C   ILE A 340      -1.362  23.228 -72.452  1.00 48.57           C  
ANISOU  937  C   ILE A 340     5739   8328   4390   2054    804    160       C  
ATOM    938  O   ILE A 340      -0.857  22.723 -73.463  1.00 51.30           O  
ANISOU  938  O   ILE A 340     6256   8700   4538   2148   1015    181       O  
ATOM    939  CB  ILE A 340      -3.322  22.246 -71.197  1.00 44.21           C  
ANISOU  939  CB  ILE A 340     4897   8141   3759   2059    -26   -126       C  
ATOM    940  CG1 ILE A 340      -3.740  21.269 -70.096  1.00 44.07           C  
ANISOU  940  CG1 ILE A 340     4633   8185   3925   1886   -291   -362       C  
ATOM    941  CG2 ILE A 340      -3.896  21.836 -72.563  1.00 47.06           C  
ANISOU  941  CG2 ILE A 340     5498   8746   3638   2353    -93   -162       C  
ATOM    942  CD1 ILE A 340      -3.460  19.826 -70.422  1.00 45.98           C  
ANISOU  942  CD1 ILE A 340     4860   8494   4117   1858   -264   -541       C  
ATOM    943  N   GLU A 341      -1.555  24.546 -72.339  1.00 51.25           N  
ANISOU  943  N   GLU A 341     6263   8429   4780   2095   1040    348       N  
ATOM    944  CA AGLU A 341      -1.276  25.451 -73.451  0.50 56.82           C  
ANISOU  944  CA AGLU A 341     7487   8855   5247   2320   1602    640       C  
ATOM    945  CA BGLU A 341      -1.282  25.412 -73.479  0.50 56.82           C  
ANISOU  945  CA BGLU A 341     7488   8865   5233   2327   1593    638       C  
ATOM    946  C   GLU A 341       0.206  25.473 -73.803  1.00 58.92           C  
ANISOU  946  C   GLU A 341     7697   8845   5843   2043   2221    564       C  
ATOM    947  O   GLU A 341       0.572  25.598 -74.977  1.00 62.01           O  
ANISOU  947  O   GLU A 341     8542   9071   5946   2235   2693    753       O  
ATOM    948  CB AGLU A 341      -1.750  26.863 -73.108  0.50 59.48           C  
ANISOU  948  CB AGLU A 341     8066   8883   5649   2409   1843    852       C  
ATOM    949  CB BGLU A 341      -1.836  26.815 -73.231  0.50 59.65           C  
ANISOU  949  CB BGLU A 341     8132   8934   5598   2465   1818    873       C  
ATOM    950  CG AGLU A 341      -3.254  27.035 -73.067  0.50 59.24           C  
ANISOU  950  CG AGLU A 341     8178   9113   5216   2823   1332    957       C  
ATOM    951  CG BGLU A 341      -3.203  27.066 -73.873  0.50 62.24           C  
ANISOU  951  CG BGLU A 341     8871   9486   5292   3072   1492   1099       C  
ATOM    952  CD AGLU A 341      -3.655  28.476 -72.837  0.50 62.66           C  
ANISOU  952  CD AGLU A 341     8937   9178   5693   2993   1665   1218       C  
ATOM    953  CD BGLU A 341      -3.163  27.064 -75.398  0.50 68.41           C  
ANISOU  953  CD BGLU A 341    10272  10297   5424   3598   1756   1357       C  
ATOM    954  OE1AGLU A 341      -2.839  29.236 -72.274  0.50 63.89           O  
ANISOU  954  OE1AGLU A 341     9024   8894   6357   2600   2197   1186       O  
ATOM    955  OE1BGLU A 341      -2.056  27.111 -75.977  0.50 71.56           O  
ANISOU  955  OE1BGLU A 341    10900  10380   5911   3450   2377   1450       O  
ATOM    956  OE2AGLU A 341      -4.783  28.850 -73.222  0.50 64.84           O  
ANISOU  956  OE2AGLU A 341     9511   9617   5509   3540   1409   1397       O  
ATOM    957  OE2BGLU A 341      -4.247  27.020 -76.022  0.50 71.05           O  
ANISOU  957  OE2BGLU A 341    10853  11005   5137   4192   1344   1421       O  
ATOM    958  N   LYS A 342       1.076  25.378 -72.796  1.00 57.28           N  
ANISOU  958  N   LYS A 342     6927   8611   6224   1627   2241    242       N  
ATOM    959  CA  LYS A 342       2.508  25.412 -73.080  1.00 62.90           C  
ANISOU  959  CA  LYS A 342     7433   9125   7341   1347   2821     24       C  
ATOM    960  C   LYS A 342       2.982  24.121 -73.735  1.00 62.31           C  
ANISOU  960  C   LYS A 342     7290   9284   7099   1442   2702    -54       C  
ATOM    961  O   LYS A 342       3.950  24.137 -74.504  1.00 65.01           O  
ANISOU  961  O   LYS A 342     7697   9430   7575   1344   3285   -116       O  
ATOM    962  CB  LYS A 342       3.297  25.687 -71.799  1.00 65.97           C  
ANISOU  962  CB  LYS A 342     7135   9554   8377    956   2786   -430       C  
ATOM    963  CG  LYS A 342       3.540  27.169 -71.543  1.00 72.94           C  
ANISOU  963  CG  LYS A 342     8059  10001   9653    674   3414   -516       C  
ATOM    964  CD  LYS A 342       3.587  27.486 -70.056  1.00 73.49           C  
ANISOU  964  CD  LYS A 342     7540  10259  10126    423   3046   -916       C  
ATOM    965  CE  LYS A 342       3.698  28.986 -69.812  1.00 79.41           C  
ANISOU  965  CE  LYS A 342     8364  10530  11278    108   3722  -1039       C  
ATOM    966  NZ  LYS A 342       2.540  29.742 -70.369  1.00 80.32           N  
ANISOU  966  NZ  LYS A 342     9268  10278  10973    411   3932   -448       N  
ATOM    967  N   ALA A 343       2.314  23.000 -73.454  1.00 59.28           N  
ANISOU  967  N   ALA A 343     6801   9264   6461   1606   2048    -79       N  
ATOM    968  CA  ALA A 343       2.686  21.737 -74.080  1.00 59.33           C  
ANISOU  968  CA  ALA A 343     6789   9442   6310   1699   1985   -164       C  
ATOM    969  C   ALA A 343       2.243  21.669 -75.536  1.00 62.89           C  
ANISOU  969  C   ALA A 343     7824   9876   6194   1970   2196     69       C  
ATOM    970  O   ALA A 343       2.857  20.953 -76.333  1.00 64.34           O  
ANISOU  970  O   ALA A 343     8081  10078   6289   1997   2425      4       O  
ATOM    971  CB  ALA A 343       2.094  20.564 -73.295  1.00 54.26           C  
ANISOU  971  CB  ALA A 343     5921   9085   5610   1766   1375   -295       C  
ATOM    972  N   LEU A 344       1.191  22.397 -75.897  1.00 92.06           N  
ANISOU  972  N   LEU A 344    12191  16206   6580   1644   2766   -971       N  
ATOM    973  CA  LEU A 344       0.705  22.419 -77.270  1.00 96.06           C  
ANISOU  973  CA  LEU A 344    13122  16678   6700   1347   2872  -1266       C  
ATOM    974  C   LEU A 344       1.634  23.238 -78.161  1.00100.73           C  
ANISOU  974  C   LEU A 344    13681  17379   7214   1176   3207  -1262       C  
ATOM    975  O   LEU A 344       1.693  23.038 -79.376  1.00106.57           O  
ANISOU  975  O   LEU A 344    14762  18081   7649    993   3497  -1576       O  
ATOM    976  CB  LEU A 344      -0.716  22.982 -77.321  1.00 91.81           C  
ANISOU  976  CB  LEU A 344    12903  16012   5967    985   2366   -992       C  
ATOM    977  CG  LEU A 344      -1.784  22.074 -76.710  1.00 89.41           C  
ANISOU  977  CG  LEU A 344    12748  15544   5681   1092   2057  -1074       C  
ATOM    978  CD1 LEU A 344      -3.102  22.813 -76.534  1.00 85.42           C  
ANISOU  978  CD1 LEU A 344    12401  14897   5157    776   1609   -681       C  
ATOM    979  CD2 LEU A 344      -1.970  20.831 -77.567  1.00 94.07           C  
ANISOU  979  CD2 LEU A 344    13645  16068   6027   1136   2258  -1637       C  
TER     980      LEU A 344                                                      
ATOM    981  N   PRO E 902     -16.119  13.671 -72.373  1.00101.51           N  
ANISOU  981  N   PRO E 902    16283  12536   9752    683  -1994  -1183       N  
ATOM    982  CA  PRO E 902     -15.323  14.736 -71.756  1.00 97.42           C  
ANISOU  982  CA  PRO E 902    15528  12162   9327    750  -1709   -929       C  
ATOM    983  C   PRO E 902     -13.908  14.289 -71.399  1.00 95.46           C  
ANISOU  983  C   PRO E 902    15225  12041   9004   1042  -1411  -1260       C  
ATOM    984  O   PRO E 902     -13.732  13.244 -70.773  1.00 95.66           O  
ANISOU  984  O   PRO E 902    15293  11758   9295   1264  -1417  -1520       O  
ATOM    985  CB  PRO E 902     -16.122  15.075 -70.497  1.00 94.53           C  
ANISOU  985  CB  PRO E 902    15069  11285   9561    712  -1731   -610       C  
ATOM    986  CG  PRO E 902     -17.535  14.799 -70.886  1.00 97.10           C  
ANISOU  986  CG  PRO E 902    15460  11337  10095    534  -2070   -451       C  
ATOM    987  CD  PRO E 902     -17.485  13.614 -71.819  1.00101.02           C  
ANISOU  987  CD  PRO E 902    16203  11998  10182    572  -2274   -893       C  
ATOM    988  N   SER E 903     -12.913  15.076 -71.798  1.00 89.73           N  
ANISOU  988  N   SER E 903    14364  11744   7986   1036  -1166  -1198       N  
ATOM    989  CA  SER E 903     -11.522  14.771 -71.483  1.00 85.51           C  
ANISOU  989  CA  SER E 903    13684  11325   7481   1296   -884  -1407       C  
ATOM    990  C   SER E 903     -11.088  15.450 -70.187  1.00 76.97           C  
ANISOU  990  C   SER E 903    12405  10140   6701   1289   -819  -1067       C  
ATOM    991  O   SER E 903     -11.008  16.678 -70.111  1.00 73.18           O  
ANISOU  991  O   SER E 903    11827   9864   6112   1100   -711   -747       O  
ATOM    992  CB  SER E 903     -10.603  15.198 -72.625  1.00 88.70           C  
ANISOU  992  CB  SER E 903    14053  12234   7413   1270   -612  -1553       C  
ATOM    993  OG  SER E 903      -9.244  15.000 -72.276  1.00 89.19           O  
ANISOU  993  OG  SER E 903    13883  12364   7639   1526   -318  -1671       O  
HETATM  994  N   PTR E 904     -10.796  14.643 -69.173  1.00 72.71           N  
ANISOU  994  N   PTR E 904    11823   9278   6526   1438   -882  -1123       N  
HETATM  995  CA  PTR E 904     -10.442  15.177 -67.866  1.00 67.36           C  
ANISOU  995  CA  PTR E 904    11051   8487   6057   1290   -874   -794       C  
HETATM  996  C   PTR E 904      -8.938  15.174 -67.612  1.00 70.78           C  
ANISOU  996  C   PTR E 904    11210   9162   6523   1411   -751   -729       C  
HETATM  997  O   PTR E 904      -8.205  14.321 -68.116  1.00 73.97           O  
ANISOU  997  O   PTR E 904    11459   9606   7041   1708   -678   -972       O  
HETATM  998  CB  PTR E 904     -11.171  14.394 -66.771  1.00 62.96           C  
ANISOU  998  CB  PTR E 904    10647   7411   5863   1238  -1094   -775       C  
HETATM  999  CG  PTR E 904     -12.600  14.846 -66.567  1.00 57.77           C  
ANISOU  999  CG  PTR E 904    10197   6451   5300    996  -1140   -654       C  
HETATM 1000  CD1 PTR E 904     -13.629  14.348 -67.356  1.00 57.70           C  
ANISOU 1000  CD1 PTR E 904    10304   6306   5315   1075  -1294   -822       C  
HETATM 1001  CD2 PTR E 904     -12.919  15.780 -65.589  1.00 53.14           C  
ANISOU 1001  CD2 PTR E 904     9684   5681   4826    639   -990   -357       C  
HETATM 1002  CE1 PTR E 904     -14.935  14.764 -67.175  1.00 56.57           C  
ANISOU 1002  CE1 PTR E 904    10259   5837   5400    860  -1343   -631       C  
HETATM 1003  CE2 PTR E 904     -14.222  16.199 -65.396  1.00 52.06           C  
ANISOU 1003  CE2 PTR E 904     9674   5166   4938    428   -927   -233       C  
HETATM 1004  CZ  PTR E 904     -15.228  15.687 -66.190  1.00 55.49           C  
ANISOU 1004  CZ  PTR E 904    10136   5456   5492    568  -1126   -336       C  
HETATM 1005  OH  PTR E 904     -16.454  16.090 -66.023  1.00 56.33           O  
ANISOU 1005  OH  PTR E 904    10279   5169   5956    376  -1075   -145       O  
HETATM 1006  P   PTR E 904     -17.487  15.326 -65.058  1.00 47.50           P  
ANISOU 1006  P   PTR E 904     9362   3393   5292    297  -1140   -210       P  
HETATM 1007  O1P PTR E 904     -17.560  13.838 -65.441  1.00 48.80           O  
ANISOU 1007  O1P PTR E 904     9615   3536   5391    609  -1517   -545       O  
HETATM 1008  O2P PTR E 904     -18.815  15.956 -65.240  1.00 47.50           O  
ANISOU 1008  O2P PTR E 904     9277   3008   5764    117  -1038     65       O  
HETATM 1009  O3P PTR E 904     -17.031  15.475 -63.594  1.00 50.41           O  
ANISOU 1009  O3P PTR E 904     9916   3527   5711     26   -896   -185       O  
ATOM   1010  N   VAL E 905      -8.488  16.154 -66.833  1.00 72.41           N  
ANISOU 1010  N   VAL E 905    11344   9493   6675   1142   -689   -386       N  
ATOM   1011  CA  VAL E 905      -7.091  16.250 -66.428  1.00 76.68           C  
ANISOU 1011  CA  VAL E 905    11596  10253   7284   1163   -650   -200       C  
ATOM   1012  C   VAL E 905      -6.869  15.391 -65.190  1.00 78.96           C  
ANISOU 1012  C   VAL E 905    11848  10212   7940   1086   -940    -17       C  
ATOM   1013  O   VAL E 905      -7.345  15.720 -64.103  1.00 77.96           O  
ANISOU 1013  O   VAL E 905    11946   9887   7789    683  -1060    208       O  
ATOM   1014  CB  VAL E 905      -6.680  17.712 -66.166  1.00 76.41           C  
ANISOU 1014  CB  VAL E 905    11529  10531   6971    825   -470    100       C  
ATOM   1015  CG1 VAL E 905      -5.261  17.780 -65.619  1.00 79.26           C  
ANISOU 1015  CG1 VAL E 905    11585  11102   7429    773   -512    367       C  
ATOM   1016  CG2 VAL E 905      -6.814  18.538 -67.441  1.00 77.74           C  
ANISOU 1016  CG2 VAL E 905    11682  11045   6812    907   -214    -18       C  
ATOM   1017  N   ASN E 906      -6.148  14.287 -65.360  1.00 81.53           N  
ANISOU 1017  N   ASN E 906    11895  10446   8638   1432  -1017   -103       N  
ATOM   1018  CA  ASN E 906      -5.938  13.309 -64.303  1.00 83.30           C  
ANISOU 1018  CA  ASN E 906    12015  10329   9305   1399  -1347    122       C  
ATOM   1019  C   ASN E 906      -4.459  13.236 -63.952  1.00 90.93           C  
ANISOU 1019  C   ASN E 906    12498  11457  10593   1422  -1432    510       C  
ATOM   1020  O   ASN E 906      -3.602  13.197 -64.840  1.00 93.32           O  
ANISOU 1020  O   ASN E 906    12458  11948  11049   1755  -1160    388       O  
ATOM   1021  CB  ASN E 906      -6.451  11.930 -64.727  1.00 81.45           C  
ANISOU 1021  CB  ASN E 906    11795   9720   9431   1791  -1379   -240       C  
ATOM   1022  CG  ASN E 906      -7.962  11.887 -64.866  1.00 74.27           C  
ANISOU 1022  CG  ASN E 906    11336   8593   8290   1705  -1413   -517       C  
ATOM   1023  OD1 ASN E 906      -8.689  12.451 -64.050  1.00 69.05           O  
ANISOU 1023  OD1 ASN E 906    10951   7817   7467   1325  -1531   -329       O  
ATOM   1024  ND2 ASN E 906      -8.441  11.215 -65.907  1.00 73.99           N  
ANISOU 1024  ND2 ASN E 906    11381   8470   8262   2009  -1276   -963       N  
ATOM   1025  N   VAL E 907      -4.165  13.213 -62.653  1.00 95.66           N  
ANISOU 1025  N   VAL E 907    13072  11966  11307   1011  -1811   1005       N  
ATOM   1026  CA  VAL E 907      -2.787  13.212 -62.176  1.00104.76           C  
ANISOU 1026  CA  VAL E 907    13737  13278  12789    907  -2017   1534       C  
ATOM   1027  C   VAL E 907      -2.362  11.797 -61.811  1.00117.60           C  
ANISOU 1027  C   VAL E 907    14960  14523  15199   1168  -2314   1763       C  
ATOM   1028  O   VAL E 907      -1.463  11.223 -62.436  1.00122.16           O  
ANISOU 1028  O   VAL E 907    14990  15043  16383   1625  -2144   1775       O  
ATOM   1029  CB  VAL E 907      -2.614  14.154 -60.972  1.00101.81           C  
ANISOU 1029  CB  VAL E 907    13588  13096  11997    142  -2291   2030       C  
ATOM   1030  CG1 VAL E 907      -1.156  14.194 -60.538  1.00105.91           C  
ANISOU 1030  CG1 VAL E 907    13567  13828  12847    -23  -2577   2654       C  
ATOM   1031  CG2 VAL E 907      -3.118  15.546 -61.313  1.00 96.74           C  
ANISOU 1031  CG2 VAL E 907    13331  12734  10692   -108  -1909   1788       C  
ATOM   1032  N   GLN E 908      -2.999  11.232 -60.793  1.00126.70           N  
ANISOU 1032  N   GLN E 908    16366  15371  16404    864  -2711   1959       N  
ATOM   1033  CA  GLN E 908      -2.606   9.928 -60.281  1.00135.09           C  
ANISOU 1033  CA  GLN E 908    17029  16055  18244   1027  -3072   2305       C  
ATOM   1034  C   GLN E 908      -3.602   8.844 -60.676  1.00134.74           C  
ANISOU 1034  C   GLN E 908    17173  15570  18451   1450  -2943   1790       C  
ATOM   1035  O   GLN E 908      -3.314   7.999 -61.525  1.00139.30           O  
ANISOU 1035  O   GLN E 908    17396  15928  19604   2034  -2653   1500       O  
ATOM   1036  CB  GLN E 908      -2.462   9.984 -58.761  1.00138.88           C  
ANISOU 1036  CB  GLN E 908    17626  16519  18624    284  -3698   3011       C  
ATOM   1037  CG  GLN E 908      -1.733   8.796 -58.170  1.00148.79           C  
ANISOU 1037  CG  GLN E 908    18298  17465  20770    361  -4183   3630       C  
ATOM   1038  CD  GLN E 908      -0.248   8.801 -58.482  1.00156.91           C  
ANISOU 1038  CD  GLN E 908    18510  18640  22469    580  -4212   4127       C  
ATOM   1039  OE1 GLN E 908       0.278   7.852 -59.064  1.00161.99           O  
ANISOU 1039  OE1 GLN E 908    18534  18961  24054   1202  -4034   4121       O  
ATOM   1040  NE2 GLN E 908       0.435   9.872 -58.094  1.00157.94           N  
ANISOU 1040  NE2 GLN E 908    18625  19213  22171     49  -4385   4555       N  
TER    1041      GLN E 908                                                      
ATOM   1042  N   SER B 226     -29.769  11.198 -48.067  1.00104.39           N  
ANISOU 1042  N   SER B 226    13882   7520  18262   -465   -759   2223       N  
ATOM   1043  CA  SER B 226     -29.337  12.556 -47.759  1.00 98.55           C  
ANISOU 1043  CA  SER B 226    12995   7358  17093   -364   -817   2363       C  
ATOM   1044  C   SER B 226     -28.594  13.170 -48.937  1.00 95.09           C  
ANISOU 1044  C   SER B 226    12586   6877  16665   -153   -718   1858       C  
ATOM   1045  O   SER B 226     -27.620  13.900 -48.755  1.00 93.54           O  
ANISOU 1045  O   SER B 226    12224   6961  16358    124   -713   1968       O  
ATOM   1046  CB  SER B 226     -28.447  12.568 -46.515  1.00100.65           C  
ANISOU 1046  CB  SER B 226    13087   7864  17291   -120   -903   2911       C  
ATOM   1047  OG  SER B 226     -29.092  11.947 -45.416  1.00104.14           O  
ANISOU 1047  OG  SER B 226    13547   8327  17695   -288   -953   3359       O  
ATOM   1048  N   GLU B 227     -29.059  12.872 -50.147  1.00 94.38           N  
ANISOU 1048  N   GLU B 227    12717   6464  16679   -287   -636   1277       N  
ATOM   1049  CA  GLU B 227     -28.395  13.320 -51.365  1.00 91.95           C  
ANISOU 1049  CA  GLU B 227    12512   6084  16340    -76   -467    704       C  
ATOM   1050  C   GLU B 227     -29.011  14.577 -51.959  1.00 83.33           C  
ANISOU 1050  C   GLU B 227    11443   5639  14579   -283   -508    406       C  
ATOM   1051  O   GLU B 227     -28.284  15.436 -52.468  1.00 80.60           O  
ANISOU 1051  O   GLU B 227    11039   5670  13917    -51   -360    191       O  
ATOM   1052  CB  GLU B 227     -28.418  12.206 -52.416  1.00100.47           C  
ANISOU 1052  CB  GLU B 227    13897   6602  17674    -67   -312    140       C  
ATOM   1053  CG  GLU B 227     -28.331  10.805 -51.836  1.00109.27           C  
ANISOU 1053  CG  GLU B 227    15020   7259  19240    -25   -304    410       C  
ATOM   1054  CD  GLU B 227     -27.839   9.789 -52.846  1.00116.76           C  
ANISOU 1054  CD  GLU B 227    16236   7656  20473    147    -79   -123       C  
ATOM   1055  OE1 GLU B 227     -28.009   8.576 -52.601  1.00122.69           O  
ANISOU 1055  OE1 GLU B 227    17055   7951  21609    100    -86    -25       O  
ATOM   1056  OE2 GLU B 227     -27.284  10.204 -53.885  1.00116.73           O  
ANISOU 1056  OE2 GLU B 227    16384   7686  20282    334    128   -639       O  
ATOM   1057  N   LYS B 228     -30.340  14.628 -51.973  1.00 78.79           N  
ANISOU 1057  N   LYS B 228    10935   5162  13840   -712   -689    387       N  
ATOM   1058  CA  LYS B 228     -31.095  15.721 -52.589  1.00 73.05           C  
ANISOU 1058  CA  LYS B 228    10215   5009  12534   -945   -764    124       C  
ATOM   1059  C   LYS B 228     -30.917  17.128 -52.024  1.00 68.12           C  
ANISOU 1059  C   LYS B 228     9329   5119  11434   -874   -751    410       C  
ATOM   1060  O   LYS B 228     -31.168  18.109 -52.724  1.00 52.07           O  
ANISOU 1060  O   LYS B 228     7293   3534   8959   -937   -742    143       O  
ATOM   1061  CB  LYS B 228     -32.587  15.371 -52.618  1.00 71.55           C  
ANISOU 1061  CB  LYS B 228    10071   4689  12425  -1428   -989    123       C  
ATOM   1062  CG  LYS B 228     -32.946  14.260 -53.591  1.00 76.07           C  
ANISOU 1062  CG  LYS B 228    10953   4628  13323  -1590  -1064   -384       C  
ATOM   1063  CD  LYS B 228     -34.357  13.750 -53.352  1.00 78.49           C  
ANISOU 1063  CD  LYS B 228    11194   4897  13733  -2010  -1233   -247       C  
ATOM   1064  CE  LYS B 228     -34.568  12.386 -53.989  1.00 84.92           C  
ANISOU 1064  CE  LYS B 228    12274   5135  14857  -2097  -1228   -620       C  
ATOM   1065  NZ  LYS B 228     -34.825  12.492 -55.452  1.00 85.96           N  
ANISOU 1065  NZ  LYS B 228    12711   5274  14676  -2240  -1338  -1321       N  
ATOM   1066  N   ILE B 229     -30.492  17.240 -50.773  1.00 54.19           N  
ANISOU 1066  N   ILE B 229     7366   3472   9751   -751   -765    947       N  
ATOM   1067  CA  ILE B 229     -30.340  18.563 -50.173  1.00 49.11           C  
ANISOU 1067  CA  ILE B 229     6505   3489   8666   -710   -768   1177       C  
ATOM   1068  C   ILE B 229     -29.270  19.365 -50.896  1.00 46.89           C  
ANISOU 1068  C   ILE B 229     6160   3472   8185   -399   -624    879       C  
ATOM   1069  O   ILE B 229     -29.357  20.594 -50.979  1.00 42.67           O  
ANISOU 1069  O   ILE B 229     5493   3470   7249   -427   -602    838       O  
ATOM   1070  CB  ILE B 229     -30.033  18.458 -48.665  1.00 55.81           C  
ANISOU 1070  CB  ILE B 229     7222   4398   9585   -646   -848   1790       C  
ATOM   1071  CG1 ILE B 229     -30.119  19.846 -48.018  1.00 52.59           C  
ANISOU 1071  CG1 ILE B 229     6645   4661   8675   -688   -862   1960       C  
ATOM   1072  CG2 ILE B 229     -28.666  17.827 -48.422  1.00 52.54           C  
ANISOU 1072  CG2 ILE B 229     6764   3657   9541   -264   -844   1937       C  
ATOM   1073  CD1 ILE B 229     -29.556  19.916 -46.613  1.00 54.80           C  
ANISOU 1073  CD1 ILE B 229     6849   5087   8887   -577   -969   2483       C  
ATOM   1074  N   TYR B 230     -28.260  18.693 -51.451  1.00 50.13           N  
ANISOU 1074  N   TYR B 230     6644   3485   8918    -94   -483    672       N  
ATOM   1075  CA  TYR B 230     -27.157  19.411 -52.079  1.00 48.75           C  
ANISOU 1075  CA  TYR B 230     6365   3525   8634    228   -281    450       C  
ATOM   1076  C   TYR B 230     -27.608  20.141 -53.338  1.00 50.58           C  
ANISOU 1076  C   TYR B 230     6744   4047   8428    120   -163    -21       C  
ATOM   1077  O   TYR B 230     -27.162  21.265 -53.604  1.00 47.94           O  
ANISOU 1077  O   TYR B 230     6253   4152   7808    239    -52    -64       O  
ATOM   1078  CB  TYR B 230     -26.020  18.440 -52.384  1.00 53.59           C  
ANISOU 1078  CB  TYR B 230     7005   3584   9772    590    -92    352       C  
ATOM   1079  CG  TYR B 230     -25.410  17.857 -51.136  1.00 55.72           C  
ANISOU 1079  CG  TYR B 230     7069   3618  10483    747   -248    898       C  
ATOM   1080  CD1 TYR B 230     -24.985  18.684 -50.106  1.00 56.13           C  
ANISOU 1080  CD1 TYR B 230     6839   4110  10377    799   -428   1326       C  
ATOM   1081  CD2 TYR B 230     -25.272  16.485 -50.976  1.00 62.49           C  
ANISOU 1081  CD2 TYR B 230     8030   3805  11908    830   -242    995       C  
ATOM   1082  CE1 TYR B 230     -24.427  18.162 -48.951  1.00 58.83           C  
ANISOU 1082  CE1 TYR B 230     7026   4276  11051    928   -638   1858       C  
ATOM   1083  CE2 TYR B 230     -24.712  15.954 -49.824  1.00 66.51           C  
ANISOU 1083  CE2 TYR B 230     8346   4107  12816    979   -420   1569       C  
ATOM   1084  CZ  TYR B 230     -24.294  16.798 -48.815  1.00 64.52           C  
ANISOU 1084  CZ  TYR B 230     7836   4349  12331   1024   -638   2009       C  
ATOM   1085  OH  TYR B 230     -23.739  16.280 -47.666  1.00 68.14           O  
ANISOU 1085  OH  TYR B 230     8157   4865  12868   1091   -830   2461       O  
ATOM   1086  N   LYS B 231     -28.516  19.510 -54.076  1.00 52.91           N  
ANISOU 1086  N   LYS B 231     7333   4091   8680   -126   -222   -342       N  
ATOM   1087  CA  LYS B 231     -29.071  20.092 -55.288  1.00 54.45           C  
ANISOU 1087  CA  LYS B 231     7719   4548   8420   -273   -198   -763       C  
ATOM   1088  C   LYS B 231     -29.950  21.274 -54.903  1.00 49.27           C  
ANISOU 1088  C   LYS B 231     6850   4470   7403   -528   -374   -526       C  
ATOM   1089  O   LYS B 231     -29.798  22.370 -55.444  1.00 47.56           O  
ANISOU 1089  O   LYS B 231     6560   4690   6821   -468   -281   -620       O  
ATOM   1090  CB  LYS B 231     -29.886  19.054 -56.061  1.00 63.03           C  
ANISOU 1090  CB  LYS B 231     9174   5197   9579   -524   -322  -1151       C  
ATOM   1091  CG  LYS B 231     -29.971  19.320 -57.555  1.00 69.70           C  
ANISOU 1091  CG  LYS B 231    10351   6158   9973   -542   -238  -1703       C  
ATOM   1092  CD  LYS B 231     -28.955  20.365 -57.988  1.00 71.14           C  
ANISOU 1092  CD  LYS B 231    10429   6752   9851   -208     80  -1732       C  
ATOM   1093  CE  LYS B 231     -29.094  20.691 -59.466  1.00 76.47           C  
ANISOU 1093  CE  LYS B 231    11473   7601   9981   -237    179  -2219       C  
ATOM   1094  NZ  LYS B 231     -30.403  21.330 -59.774  1.00 76.11           N  
ANISOU 1094  NZ  LYS B 231    11447   7944   9529   -637   -197  -2198       N  
ATOM   1095  N   VAL B 232     -30.871  21.054 -53.966  1.00 47.49           N  
ANISOU 1095  N   VAL B 232     6513   4218   7312   -804   -584   -198       N  
ATOM   1096  CA  VAL B 232     -31.744  22.138 -53.515  1.00 42.02           C  
ANISOU 1096  CA  VAL B 232     5596   4020   6351  -1032   -689     38       C  
ATOM   1097  C   VAL B 232     -30.910  23.350 -53.120  1.00 38.35           C  
ANISOU 1097  C   VAL B 232     4890   4004   5677   -793   -543    195       C  
ATOM   1098  O   VAL B 232     -31.250  24.494 -53.448  1.00 33.33           O  
ANISOU 1098  O   VAL B 232     4129   3795   4741   -860   -524    161       O  
ATOM   1099  CB  VAL B 232     -32.640  21.667 -52.353  1.00 41.99           C  
ANISOU 1099  CB  VAL B 232     5487   3886   6580  -1293   -823    436       C  
ATOM   1100  CG1 VAL B 232     -33.327  22.862 -51.702  1.00 36.70           C  
ANISOU 1100  CG1 VAL B 232     4559   3722   5664  -1447   -821    706       C  
ATOM   1101  CG2 VAL B 232     -33.666  20.663 -52.840  1.00 43.41           C  
ANISOU 1101  CG2 VAL B 232     5837   3658   7000  -1605   -999    276       C  
ATOM   1102  N   MET B 233     -29.789  23.115 -52.431  1.00 38.23           N  
ANISOU 1102  N   MET B 233     4788   3871   5868   -514   -462    376       N  
ATOM   1103  CA  MET B 233     -28.919  24.216 -52.030  1.00 37.07           C  
ANISOU 1103  CA  MET B 233     4391   4100   5592   -303   -373    510       C  
ATOM   1104  C   MET B 233     -28.293  24.897 -53.238  1.00 35.93           C  
ANISOU 1104  C   MET B 233     4245   4122   5285   -113   -166    186       C  
ATOM   1105  O   MET B 233     -28.087  26.116 -53.233  1.00 32.42           O  
ANISOU 1105  O   MET B 233     3594   4078   4646    -72   -100    233       O  
ATOM   1106  CB  MET B 233     -27.842  23.709 -51.071  1.00 41.21           C  
ANISOU 1106  CB  MET B 233     4808   4426   6425    -61   -409    791       C  
ATOM   1107  CG  MET B 233     -28.371  23.290 -49.700  1.00 46.41           C  
ANISOU 1107  CG  MET B 233     5462   5041   7130   -234   -601   1212       C  
ATOM   1108  SD  MET B 233     -29.367  24.559 -48.884  1.00 46.39           S  
ANISOU 1108  SD  MET B 233     5337   5588   6703   -515   -644   1398       S  
ATOM   1109  CE  MET B 233     -31.001  23.991 -49.266  1.00 47.65           C  
ANISOU 1109  CE  MET B 233     5643   5581   6880   -885   -657   1341       C  
ATOM   1110  N   GLU B 234     -27.995  24.133 -54.291  1.00 38.06           N  
ANISOU 1110  N   GLU B 234     4763   4073   5627      2    -33   -147       N  
ATOM   1111  CA  GLU B 234     -27.486  24.752 -55.508  1.00 38.09           C  
ANISOU 1111  CA  GLU B 234     4831   4248   5396    169    217   -447       C  
ATOM   1112  C   GLU B 234     -28.525  25.679 -56.126  1.00 34.93           C  
ANISOU 1112  C   GLU B 234     4466   4249   4557    -89    124   -526       C  
ATOM   1113  O   GLU B 234     -28.192  26.785 -56.569  1.00 34.85           O  
ANISOU 1113  O   GLU B 234     4318   4589   4333     11    276   -525       O  
ATOM   1114  CB  GLU B 234     -27.069  23.681 -56.512  1.00 43.63           C  
ANISOU 1114  CB  GLU B 234     5874   4509   6195    322    410   -833       C  
ATOM   1115  CG  GLU B 234     -26.205  24.198 -57.651  1.00 45.66           C  
ANISOU 1115  CG  GLU B 234     6203   4888   6258    594    789  -1097       C  
ATOM   1116  CD  GLU B 234     -26.684  23.704 -58.995  1.00 51.10           C  
ANISOU 1116  CD  GLU B 234     7379   5445   6590    501    870  -1570       C  
ATOM   1117  OE1 GLU B 234     -25.862  23.355 -59.863  1.00 54.92           O  
ANISOU 1117  OE1 GLU B 234     8081   5726   7060    770   1250  -1876       O  
ATOM   1118  OE2 GLU B 234     -27.910  23.691 -59.183  1.00 51.65           O  
ANISOU 1118  OE2 GLU B 234     7614   5624   6387    147    549  -1636       O  
ATOM   1119  N   GLU B 235     -29.791  25.247 -56.170  1.00 35.09           N  
ANISOU 1119  N   GLU B 235     4636   4199   4498   -423   -133   -562       N  
ATOM   1120  CA  GLU B 235     -30.843  26.101 -56.720  1.00 34.74           C  
ANISOU 1120  CA  GLU B 235     4568   4515   4117   -677   -277   -579       C  
ATOM   1121  C   GLU B 235     -30.941  27.412 -55.965  1.00 29.92           C  
ANISOU 1121  C   GLU B 235     3580   4322   3467   -689   -251   -258       C  
ATOM   1122  O   GLU B 235     -31.199  28.458 -56.567  1.00 28.86           O  
ANISOU 1122  O   GLU B 235     3354   4529   3084   -718   -218   -260       O  
ATOM   1123  CB  GLU B 235     -32.202  25.396 -56.694  1.00 41.15           C  
ANISOU 1123  CB  GLU B 235     5497   5146   4992  -1054   -594   -599       C  
ATOM   1124  CG  GLU B 235     -32.368  24.331 -57.768  1.00 50.10           C  
ANISOU 1124  CG  GLU B 235     7053   5925   6057  -1132   -688  -1020       C  
ATOM   1125  CD  GLU B 235     -33.709  23.613 -57.710  1.00 57.97           C  
ANISOU 1125  CD  GLU B 235     8115   6698   7214  -1539  -1051  -1032       C  
ATOM   1126  OE1 GLU B 235     -34.759  24.283 -57.636  1.00 59.11           O  
ANISOU 1126  OE1 GLU B 235     8046   7125   7289  -1803  -1264   -844       O  
ATOM   1127  OE2 GLU B 235     -33.685  22.355 -57.699  1.00 63.18           O  
ANISOU 1127  OE2 GLU B 235     9001   6855   8148  -1588  -1106  -1211       O  
ATOM   1128  N   ILE B 236     -30.770  27.372 -54.643  1.00 27.49           N  
ANISOU 1128  N   ILE B 236     3073   3982   3391   -675   -271     22       N  
ATOM   1129  CA  ILE B 236     -30.916  28.572 -53.823  1.00 26.98           C  
ANISOU 1129  CA  ILE B 236     2698   4275   3278   -711   -244    275       C  
ATOM   1130  C   ILE B 236     -29.695  29.473 -53.963  1.00 25.93           C  
ANISOU 1130  C   ILE B 236     2393   4334   3127   -424    -43    259       C  
ATOM   1131  O   ILE B 236     -29.824  30.677 -54.218  1.00 25.53           O  
ANISOU 1131  O   ILE B 236     2158   4597   2946   -436     37    291       O  
ATOM   1132  CB  ILE B 236     -31.172  28.176 -52.356  1.00 28.28           C  
ANISOU 1132  CB  ILE B 236     2788   4348   3608   -812   -336    560       C  
ATOM   1133  CG1 ILE B 236     -32.540  27.495 -52.228  1.00 30.39           C  
ANISOU 1133  CG1 ILE B 236     3144   4458   3945  -1134   -485    632       C  
ATOM   1134  CG2 ILE B 236     -31.042  29.396 -51.412  1.00 28.61           C  
ANISOU 1134  CG2 ILE B 236     2571   4731   3568   -799   -269    755       C  
ATOM   1135  CD1 ILE B 236     -32.776  26.853 -50.878  1.00 34.33           C  
ANISOU 1135  CD1 ILE B 236     3643   4798   4602  -1226   -524    935       C  
ATOM   1136  N   PHE B 237     -28.496  28.899 -53.822  1.00 23.94           N  
ANISOU 1136  N   PHE B 237     2160   3860   3075   -163     45    229       N  
ATOM   1137  CA  PHE B 237     -27.276  29.703 -53.813  1.00 25.75           C  
ANISOU 1137  CA  PHE B 237     2149   4229   3406    100    218    259       C  
ATOM   1138  C   PHE B 237     -27.022  30.408 -55.144  1.00 28.80           C  
ANISOU 1138  C   PHE B 237     2547   4778   3618    211    463     78       C  
ATOM   1139  O   PHE B 237     -26.446  31.503 -55.165  1.00 28.45           O  
ANISOU 1139  O   PHE B 237     2325   4861   3624    299    567    141       O  
ATOM   1140  CB  PHE B 237     -26.084  28.825 -53.452  1.00 28.21           C  
ANISOU 1140  CB  PHE B 237     2441   4220   4059    361    249    295       C  
ATOM   1141  CG  PHE B 237     -26.044  28.434 -52.005  1.00 28.92           C  
ANISOU 1141  CG  PHE B 237     2451   4235   4303    302     -1    574       C  
ATOM   1142  CD1 PHE B 237     -26.696  29.199 -51.054  1.00 28.85           C  
ANISOU 1142  CD1 PHE B 237     2340   4513   4110     90   -147    750       C  
ATOM   1143  CD2 PHE B 237     -25.355  27.307 -51.597  1.00 34.30           C  
ANISOU 1143  CD2 PHE B 237     3177   4550   5304    465    -71    674       C  
ATOM   1144  CE1 PHE B 237     -26.660  28.844 -49.712  1.00 32.06           C  
ANISOU 1144  CE1 PHE B 237     2743   4883   4555     31   -361   1014       C  
ATOM   1145  CE2 PHE B 237     -25.309  26.948 -50.250  1.00 36.68           C  
ANISOU 1145  CE2 PHE B 237     3434   4808   5694    410   -331    992       C  
ATOM   1146  CZ  PHE B 237     -25.966  27.719 -49.312  1.00 34.93           C  
ANISOU 1146  CZ  PHE B 237     3165   4916   5192    186   -476   1156       C  
ATOM   1147  N   VAL B 238     -27.391  29.784 -56.268  1.00 30.19           N  
ANISOU 1147  N   VAL B 238     2230   4534   4709    198    547   -812       N  
ATOM   1148  CA  VAL B 238     -27.120  30.406 -57.564  1.00 31.63           C  
ANISOU 1148  CA  VAL B 238     2495   4908   4615    -43    846   -933       C  
ATOM   1149  C   VAL B 238     -28.111  31.515 -57.879  1.00 30.41           C  
ANISOU 1149  C   VAL B 238     2765   4707   4084   -152    853   -630       C  
ATOM   1150  O   VAL B 238     -27.849  32.338 -58.767  1.00 32.74           O  
ANISOU 1150  O   VAL B 238     3261   5100   4079   -408   1055   -626       O  
ATOM   1151  CB  VAL B 238     -27.146  29.396 -58.728  1.00 33.00           C  
ANISOU 1151  CB  VAL B 238     2559   5186   4792    -27    972  -1220       C  
ATOM   1152  CG1 VAL B 238     -26.158  28.255 -58.508  1.00 32.76           C  
ANISOU 1152  CG1 VAL B 238     2271   5061   5116    124    858  -1462       C  
ATOM   1153  CG2 VAL B 238     -28.556  28.868 -58.940  1.00 33.49           C  
ANISOU 1153  CG2 VAL B 238     2837   5139   4746    109    803  -1059       C  
ATOM   1154  N   ASP B 239     -29.234  31.563 -57.171  1.00 28.06           N  
ANISOU 1154  N   ASP B 239     2614   4251   3796     25    633   -394       N  
ATOM   1155  CA  ASP B 239     -30.294  32.501 -57.500  1.00 29.94           C  
ANISOU 1155  CA  ASP B 239     3189   4424   3762     20    576   -162       C  
ATOM   1156  C   ASP B 239     -29.854  33.941 -57.260  1.00 30.43           C  
ANISOU 1156  C   ASP B 239     3477   4407   3679   -148    654    -21       C  
ATOM   1157  O   ASP B 239     -29.096  34.234 -56.329  1.00 28.10           O  
ANISOU 1157  O   ASP B 239     3063   4080   3532   -208    681    -47       O  
ATOM   1158  CB  ASP B 239     -31.541  32.186 -56.677  1.00 27.53           C  
ANISOU 1158  CB  ASP B 239     2882   4007   3572    241    363    -37       C  
ATOM   1159  CG  ASP B 239     -32.738  32.960 -57.151  1.00 31.14           C  
ANISOU 1159  CG  ASP B 239     3582   4420   3832    318    254    116       C  
ATOM   1160  OD1 ASP B 239     -32.967  34.052 -56.600  1.00 30.55           O  
ANISOU 1160  OD1 ASP B 239     3667   4215   3727    346    215    253       O  
ATOM   1161  OD2 ASP B 239     -33.420  32.494 -58.097  1.00 30.53           O  
ANISOU 1161  OD2 ASP B 239     3531   4427   3641    361    184     76       O  
ATOM   1162  N   ARG B 240     -30.335  34.843 -58.122  1.00 28.72           N  
ANISOU 1162  N   ARG B 240     3622   4133   3157   -237    655    134       N  
ATOM   1163  CA  ARG B 240     -29.974  36.251 -58.012  1.00 26.60           C  
ANISOU 1163  CA  ARG B 240     3667   3709   2731   -423    717    286       C  
ATOM   1164  C   ARG B 240     -30.388  36.850 -56.674  1.00 25.51           C  
ANISOU 1164  C   ARG B 240     3538   3375   2780   -258    584    387       C  
ATOM   1165  O   ARG B 240     -29.797  37.843 -56.239  1.00 27.14           O  
ANISOU 1165  O   ARG B 240     3902   3456   2956   -434    666    432       O  
ATOM   1166  CB  ARG B 240     -30.610  37.042 -59.156  1.00 29.24           C  
ANISOU 1166  CB  ARG B 240     4476   3932   2702   -490    637    489       C  
ATOM   1167  CG  ARG B 240     -32.129  37.008 -59.151  1.00 28.47           C  
ANISOU 1167  CG  ARG B 240     4455   3721   2642   -127    313    622       C  
ATOM   1168  CD  ARG B 240     -32.705  37.677 -60.404  1.00 33.02           C  
ANISOU 1168  CD  ARG B 240     5504   4195   2847   -166    138    826       C  
ATOM   1169  NE  ARG B 240     -34.165  37.625 -60.384  1.00 35.10           N  
ANISOU 1169  NE  ARG B 240     5741   4383   3211    224   -219    897       N  
ATOM   1170  CZ  ARG B 240     -34.936  38.604 -59.918  1.00 38.54           C  
ANISOU 1170  CZ  ARG B 240     6346   4538   3761    481   -460   1034       C  
ATOM   1171  NH1 ARG B 240     -34.389  39.715 -59.446  1.00 38.49           N  
ANISOU 1171  NH1 ARG B 240     6614   4257   3752    372   -383   1144       N  
ATOM   1172  NH2 ARG B 240     -36.255  38.474 -59.930  1.00 39.55           N  
ANISOU 1172  NH2 ARG B 240     6339   4658   4029    844   -775   1017       N  
ATOM   1173  N   HIS B 241     -31.412  36.288 -56.023  1.00 21.92           N  
ANISOU 1173  N   HIS B 241     2932   2900   2496     29    410    393       N  
ATOM   1174  CA  HIS B 241     -31.895  36.842 -54.767  1.00 23.03           C  
ANISOU 1174  CA  HIS B 241     3085   2892   2773    151    331    435       C  
ATOM   1175  C   HIS B 241     -31.000  36.479 -53.588  1.00 24.55           C  
ANISOU 1175  C   HIS B 241     3056   3148   3124     45    391    337       C  
ATOM   1176  O   HIS B 241     -31.081  37.135 -52.545  1.00 23.98           O  
ANISOU 1176  O   HIS B 241     3053   2967   3093     36    376    351       O  
ATOM   1177  CB  HIS B 241     -33.318  36.359 -54.461  1.00 22.95           C  
ANISOU 1177  CB  HIS B 241     2962   2889   2869    423    177    423       C  
ATOM   1178  CG  HIS B 241     -34.349  36.838 -55.437  1.00 27.37           C  
ANISOU 1178  CG  HIS B 241     3704   3374   3320    596     18    505       C  
ATOM   1179  ND1 HIS B 241     -34.744  36.087 -56.522  1.00 29.36           N  
ANISOU 1179  ND1 HIS B 241     3912   3771   3474    634    -63    491       N  
ATOM   1180  CD2 HIS B 241     -35.074  37.980 -55.484  1.00 30.45           C  
ANISOU 1180  CD2 HIS B 241     4324   3547   3699    763   -123    587       C  
ATOM   1181  CE1 HIS B 241     -35.664  36.750 -57.204  1.00 30.90           C  
ANISOU 1181  CE1 HIS B 241     4303   3865   3574    808   -279    586       C  
ATOM   1182  NE2 HIS B 241     -35.882  37.903 -56.596  1.00 32.91           N  
ANISOU 1182  NE2 HIS B 241     4722   3878   3903    916   -334    649       N  
ATOM   1183  N   TYR B 242     -30.173  35.449 -53.719  1.00 23.92           N  
ANISOU 1183  N   TYR B 242     2717   3232   3140    -16    426    220       N  
ATOM   1184  CA  TYR B 242     -29.347  35.022 -52.596  1.00 25.43           C  
ANISOU 1184  CA  TYR B 242     2697   3467   3499    -65    375    144       C  
ATOM   1185  C   TYR B 242     -28.153  35.958 -52.452  1.00 27.14           C  
ANISOU 1185  C   TYR B 242     2929   3699   3683   -314    489     84       C  
ATOM   1186  O   TYR B 242     -27.405  36.174 -53.410  1.00 27.87           O  
ANISOU 1186  O   TYR B 242     2996   3884   3711   -493    656     -5       O  
ATOM   1187  CB  TYR B 242     -28.874  33.578 -52.769  1.00 25.66           C  
ANISOU 1187  CB  TYR B 242     2432   3605   3711     20    306     17       C  
ATOM   1188  CG  TYR B 242     -28.162  33.108 -51.526  1.00 23.04           C  
ANISOU 1188  CG  TYR B 242     1937   3267   3552     28    135    -12       C  
ATOM   1189  CD1 TYR B 242     -26.784  33.185 -51.419  1.00 24.65           C  
ANISOU 1189  CD1 TYR B 242     1908   3570   3887    -75    131   -167       C  
ATOM   1190  CD2 TYR B 242     -28.881  32.658 -50.430  1.00 25.47           C  
ANISOU 1190  CD2 TYR B 242     2336   3480   3861    103    -34    109       C  
ATOM   1191  CE1 TYR B 242     -26.132  32.784 -50.260  1.00 28.07           C  
ANISOU 1191  CE1 TYR B 242     2202   3992   4471    -43   -118   -179       C  
ATOM   1192  CE2 TYR B 242     -28.239  32.256 -49.264  1.00 25.47           C  
ANISOU 1192  CE2 TYR B 242     2277   3455   3946     81   -249    129       C  
ATOM   1193  CZ  TYR B 242     -26.875  32.325 -49.187  1.00 25.17           C  
ANISOU 1193  CZ  TYR B 242     2011   3498   4053     36   -328     -1       C  
ATOM   1194  OH  TYR B 242     -26.246  31.927 -48.029  1.00 27.51           O  
ANISOU 1194  OH  TYR B 242     2258   3767   4429     41   -629     31       O  
ATOM   1195  N   LYS B 243     -27.968  36.510 -51.254  1.00 25.82           N  
ANISOU 1195  N   LYS B 243     2808   3466   3538   -378    423    104       N  
ATOM   1196  CA  LYS B 243     -26.918  37.497 -51.008  1.00 29.38           C  
ANISOU 1196  CA  LYS B 243     3288   3920   3955   -655    521     31       C  
ATOM   1197  C   LYS B 243     -25.938  36.939 -49.978  1.00 31.48           C  
ANISOU 1197  C   LYS B 243     3249   4325   4388   -699    359    -92       C  
ATOM   1198  O   LYS B 243     -26.189  37.006 -48.772  1.00 28.86           O  
ANISOU 1198  O   LYS B 243     2990   3940   4036   -676    204    -40       O  
ATOM   1199  CB  LYS B 243     -27.531  38.816 -50.545  1.00 29.22           C  
ANISOU 1199  CB  LYS B 243     3634   3667   3799   -715    561    127       C  
ATOM   1200  CG  LYS B 243     -28.572  39.374 -51.509  1.00 28.66           C  
ANISOU 1200  CG  LYS B 243     3877   3409   3603   -592    609    264       C  
ATOM   1201  CD  LYS B 243     -27.995  39.586 -52.913  1.00 30.51           C  
ANISOU 1201  CD  LYS B 243     4216   3680   3697   -791    760    285       C  
ATOM   1202  CE  LYS B 243     -29.022  40.233 -53.849  1.00 32.10           C  
ANISOU 1202  CE  LYS B 243     4818   3653   3725   -672    713    471       C  
ATOM   1203  NZ  LYS B 243     -28.548  40.287 -55.273  1.00 37.42           N  
ANISOU 1203  NZ  LYS B 243     5659   4392   4167   -908    850    515       N  
ATOM   1204  N   GLU B 244     -24.813  36.401 -50.456  1.00 33.34           N  
ANISOU 1204  N   GLU B 244     3138   4749   4782   -766    383   -281       N  
ATOM   1205  CA  GLU B 244     -23.850  35.763 -49.563  1.00 35.87           C  
ANISOU 1205  CA  GLU B 244     3113   5195   5321   -732    135   -415       C  
ATOM   1206  C   GLU B 244     -23.152  36.752 -48.638  1.00 38.68           C  
ANISOU 1206  C   GLU B 244     3491   5582   5624   -993     91   -473       C  
ATOM   1207  O   GLU B 244     -22.593  36.335 -47.618  1.00 39.24           O  
ANISOU 1207  O   GLU B 244     3377   5724   5808   -950   -211   -519       O  
ATOM   1208  CB  GLU B 244     -22.800  34.999 -50.373  1.00 37.53           C  
ANISOU 1208  CB  GLU B 244     2867   5609   5785   -704    181   -692       C  
ATOM   1209  CG  GLU B 244     -21.856  35.884 -51.177  1.00 41.37           C  
ANISOU 1209  CG  GLU B 244     3221   6271   6227  -1068    518   -917       C  
ATOM   1210  CD  GLU B 244     -22.423  36.279 -52.535  1.00 42.61           C  
ANISOU 1210  CD  GLU B 244     3666   6390   6134  -1203    863   -853       C  
ATOM   1211  OE1 GLU B 244     -23.634  36.073 -52.770  1.00 40.84           O  
ANISOU 1211  OE1 GLU B 244     3755   5993   5770   -999    812   -619       O  
ATOM   1212  OE2 GLU B 244     -21.649  36.790 -53.372  1.00 46.98           O  
ANISOU 1212  OE2 GLU B 244     4178   7077   6594  -1509   1151  -1027       O  
ATOM   1213  N   ASN B 245     -23.164  38.043 -48.964  1.00 39.00           N  
ANISOU 1213  N   ASN B 245     3787   5547   5486  -1273    352   -467       N  
ATOM   1214  CA  ASN B 245     -22.451  39.041 -48.181  1.00 42.75           C  
ANISOU 1214  CA  ASN B 245     4293   6039   5912  -1581    348   -566       C  
ATOM   1215  C   ASN B 245     -23.353  39.801 -47.216  1.00 41.28           C  
ANISOU 1215  C   ASN B 245     4529   5623   5533  -1583    297   -415       C  
ATOM   1216  O   ASN B 245     -22.901  40.770 -46.602  1.00 43.61           O  
ANISOU 1216  O   ASN B 245     4939   5880   5752  -1863    329   -505       O  
ATOM   1217  CB  ASN B 245     -21.736  40.022 -49.107  1.00 47.93           C  
ANISOU 1217  CB  ASN B 245     4984   6726   6500  -1974    688   -700       C  
ATOM   1218  CG  ASN B 245     -20.656  39.355 -49.936  1.00 52.40           C  
ANISOU 1218  CG  ASN B 245     5049   7600   7262  -2062    801   -970       C  
ATOM   1219  OD1 ASN B 245     -20.592  39.535 -51.151  1.00 54.99           O  
ANISOU 1219  OD1 ASN B 245     5498   7929   7468  -2163   1081   -983       O  
ATOM   1220  ND2 ASN B 245     -19.804  38.575 -49.280  1.00 54.25           N  
ANISOU 1220  ND2 ASN B 245     4841   8024   7747  -1883    514  -1140       N  
ATOM   1221  N   ILE B 246     -24.605  39.382 -47.057  1.00 36.62           N  
ANISOU 1221  N   ILE B 246     4143   4898   4875  -1303    241   -239       N  
ATOM   1222  CA  ILE B 246     -25.554  40.055 -46.173  1.00 37.16           C  
ANISOU 1222  CA  ILE B 246     4554   4779   4786  -1288    246   -174       C  
ATOM   1223  C   ILE B 246     -25.840  39.126 -45.001  1.00 37.01           C  
ANISOU 1223  C   ILE B 246     4471   4860   4731  -1175     -7   -130       C  
ATOM   1224  O   ILE B 246     -26.494  38.087 -45.162  1.00 35.76           O  
ANISOU 1224  O   ILE B 246     4255   4720   4610   -947    -87    -22       O  
ATOM   1225  CB  ILE B 246     -26.839  40.446 -46.916  1.00 33.70           C  
ANISOU 1225  CB  ILE B 246     4390   4118   4295  -1094    406    -59       C  
ATOM   1226  CG1 ILE B 246     -26.525  41.472 -48.007  1.00 33.91           C  
ANISOU 1226  CG1 ILE B 246     4617   3983   4284  -1260    604    -47       C  
ATOM   1227  CG2 ILE B 246     -27.862  41.009 -45.957  1.00 33.89           C  
ANISOU 1227  CG2 ILE B 246     4662   3985   4228  -1026    422    -81       C  
ATOM   1228  CD1 ILE B 246     -27.743  41.919 -48.803  1.00 33.23           C  
ANISOU 1228  CD1 ILE B 246     4833   3642   4150  -1036    662     89       C  
ATOM   1229  N   ARG B 247     -25.360  39.500 -43.817  1.00 40.45           N  
ANISOU 1229  N   ARG B 247     4964   5350   5057  -1380   -139   -210       N  
ATOM   1230  CA  ARG B 247     -25.477  38.671 -42.623  1.00 42.15           C  
ANISOU 1230  CA  ARG B 247     5201   5662   5151  -1363   -420   -144       C  
ATOM   1231  C   ARG B 247     -26.163  39.368 -41.458  1.00 41.50           C  
ANISOU 1231  C   ARG B 247     5454   5519   4794  -1533   -345   -198       C  
ATOM   1232  O   ARG B 247     -26.888  38.719 -40.701  1.00 41.40           O  
ANISOU 1232  O   ARG B 247     5586   5537   4609  -1511   -421   -114       O  
ATOM   1233  CB  ARG B 247     -24.084  38.199 -42.176  1.00 48.35           C  
ANISOU 1233  CB  ARG B 247     5701   6636   6032  -1455   -770   -206       C  
ATOM   1234  CG  ARG B 247     -23.314  37.440 -43.247  1.00 52.77           C  
ANISOU 1234  CG  ARG B 247     5851   7289   6911  -1278   -835   -249       C  
ATOM   1235  CD  ARG B 247     -23.939  36.079 -43.530  1.00 54.69           C  
ANISOU 1235  CD  ARG B 247     6068   7470   7243   -968   -968    -84       C  
ATOM   1236  NE  ARG B 247     -22.920  35.051 -43.715  1.00 60.07           N  
ANISOU 1236  NE  ARG B 247     6361   8248   8215   -795  -1291   -153       N  
ATOM   1237  CZ  ARG B 247     -22.761  34.341 -44.827  1.00 63.05           C  
ANISOU 1237  CZ  ARG B 247     6468   8631   8856   -582  -1213   -228       C  
ATOM   1238  NH1 ARG B 247     -23.559  34.537 -45.869  1.00 60.02           N  
ANISOU 1238  NH1 ARG B 247     6193   8182   8428   -547   -846   -201       N  
ATOM   1239  NH2 ARG B 247     -21.799  33.431 -44.898  1.00 67.43           N  
ANISOU 1239  NH2 ARG B 247     6637   9255   9726   -392  -1526   -356       N  
ATOM   1240  N   THR B 248     -25.961  40.668 -41.294  1.00 41.35           N  
ANISOU 1240  N   THR B 248     5583   5409   4720  -1738   -172   -362       N  
ATOM   1241  CA  THR B 248     -26.513  41.409 -40.171  1.00 43.53           C  
ANISOU 1241  CA  THR B 248     6161   5627   4751  -1919    -73   -499       C  
ATOM   1242  C   THR B 248     -27.737  42.209 -40.600  1.00 39.83           C  
ANISOU 1242  C   THR B 248     5891   4910   4332  -1762    261   -581       C  
ATOM   1243  O   THR B 248     -27.957  42.470 -41.785  1.00 35.86           O  
ANISOU 1243  O   THR B 248     5351   4248   4027  -1574    380   -516       O  
ATOM   1244  CB  THR B 248     -25.464  42.351 -39.582  1.00 47.67           C  
ANISOU 1244  CB  THR B 248     6733   6182   5196  -2262   -132   -685       C  
ATOM   1245  OG1 THR B 248     -25.277  43.461 -40.468  1.00 47.42           O  
ANISOU 1245  OG1 THR B 248     6763   5928   5328  -2315    116   -778       O  
ATOM   1246  CG2 THR B 248     -24.137  41.627 -39.391  1.00 49.54           C  
ANISOU 1246  CG2 THR B 248     6660   6674   5488  -2358   -509   -645       C  
ATOM   1247  N   GLY B 249     -28.541  42.598 -39.609  1.00 39.88           N  
ANISOU 1247  N   GLY B 249     6112   4892   4151  -1844    394   -747       N  
ATOM   1248  CA  GLY B 249     -29.705  43.417 -39.896  1.00 39.77           C  
ANISOU 1248  CA  GLY B 249     6233   4635   4245  -1651    677   -907       C  
ATOM   1249  C   GLY B 249     -29.344  44.773 -40.462  1.00 40.30           C  
ANISOU 1249  C   GLY B 249     6467   4379   4467  -1676    785  -1011       C  
ATOM   1250  O   GLY B 249     -30.103  45.340 -41.255  1.00 38.34           O  
ANISOU 1250  O   GLY B 249     6302   3852   4414  -1407    904  -1024       O  
ATOM   1251  N   GLU B 250     -28.188  45.311 -40.067  1.00 41.97           N  
ANISOU 1251  N   GLU B 250     6749   4604   4592  -2013    714  -1084       N  
ATOM   1252  CA  GLU B 250     -27.713  46.557 -40.656  1.00 44.60           C  
ANISOU 1252  CA  GLU B 250     7285   4609   5054  -2129    820  -1157       C  
ATOM   1253  C   GLU B 250     -27.440  46.389 -42.149  1.00 41.91           C  
ANISOU 1253  C   GLU B 250     6858   4174   4891  -1990    806   -910       C  
ATOM   1254  O   GLU B 250     -27.772  47.268 -42.953  1.00 40.76           O  
ANISOU 1254  O   GLU B 250     6969   3655   4863  -1898    915   -880       O  
ATOM   1255  CB  GLU B 250     -26.461  47.035 -39.922  1.00 48.26           C  
ANISOU 1255  CB  GLU B 250     7780   5178   5380  -2585    742  -1308       C  
ATOM   1256  CG  GLU B 250     -26.702  47.439 -38.464  1.00 53.52           C  
ANISOU 1256  CG  GLU B 250     8630   5896   5809  -2795    778  -1596       C  
ATOM   1257  CD  GLU B 250     -26.612  46.275 -37.474  1.00 56.46           C  
ANISOU 1257  CD  GLU B 250     8844   6695   5913  -2876    560  -1536       C  
ATOM   1258  OE1 GLU B 250     -26.680  45.102 -37.897  1.00 54.81           O  
ANISOU 1258  OE1 GLU B 250     8399   6675   5751  -2668    404  -1276       O  
ATOM   1259  OE2 GLU B 250     -26.480  46.536 -36.257  1.00 60.52           O  
ANISOU 1259  OE2 GLU B 250     9511   7335   6147  -3156    531  -1738       O  
ATOM   1260  N   GLU B 251     -26.841  45.261 -42.541  1.00 39.88           N  
ANISOU 1260  N   GLU B 251     6275   4234   4645  -1978    658   -740       N  
ATOM   1261  CA  GLU B 251     -26.571  45.028 -43.958  1.00 38.46           C  
ANISOU 1261  CA  GLU B 251     6002   4020   4590  -1889    687   -557       C  
ATOM   1262  C   GLU B 251     -27.851  44.761 -44.739  1.00 35.58           C  
ANISOU 1262  C   GLU B 251     5708   3507   4305  -1484    725   -416       C  
ATOM   1263  O   GLU B 251     -27.924  45.089 -45.930  1.00 36.69           O  
ANISOU 1263  O   GLU B 251     5980   3464   4497  -1420    780   -284       O  
ATOM   1264  CB  GLU B 251     -25.585  43.872 -44.121  1.00 37.80           C  
ANISOU 1264  CB  GLU B 251     5506   4315   4543  -1955    527   -498       C  
ATOM   1265  CG  GLU B 251     -24.179  44.228 -43.651  1.00 43.82           C  
ANISOU 1265  CG  GLU B 251     6119   5239   5290  -2354    464   -664       C  
ATOM   1266  CD  GLU B 251     -23.302  43.014 -43.395  1.00 45.07           C  
ANISOU 1266  CD  GLU B 251     5820   5777   5528  -2332    196   -673       C  
ATOM   1267  OE1 GLU B 251     -23.844  41.905 -43.205  1.00 41.61           O  
ANISOU 1267  OE1 GLU B 251     5275   5437   5100  -2041     30   -543       O  
ATOM   1268  OE2 GLU B 251     -22.062  43.177 -43.383  1.00 49.12           O  
ANISOU 1268  OE2 GLU B 251     6074   6474   6117  -2611    139   -832       O  
ATOM   1269  N   VAL B 252     -28.862  44.173 -44.096  1.00 32.35           N  
ANISOU 1269  N   VAL B 252     5222   3190   3881  -1251    692   -453       N  
ATOM   1270  CA  VAL B 252     -30.157  44.001 -44.750  1.00 32.50           C  
ANISOU 1270  CA  VAL B 252     5255   3089   4005   -876    720   -389       C  
ATOM   1271  C   VAL B 252     -30.800  45.360 -44.998  1.00 36.19           C  
ANISOU 1271  C   VAL B 252     6050   3130   4571   -744    802   -484       C  
ATOM   1272  O   VAL B 252     -31.325  45.632 -46.085  1.00 37.60           O  
ANISOU 1272  O   VAL B 252     6347   3090   4849   -506    754   -352       O  
ATOM   1273  CB  VAL B 252     -31.075  43.091 -43.910  1.00 31.02           C  
ANISOU 1273  CB  VAL B 252     4887   3126   3772   -744    715   -465       C  
ATOM   1274  CG1 VAL B 252     -32.463  43.014 -44.524  1.00 33.18           C  
ANISOU 1274  CG1 VAL B 252     5110   3305   4192   -376    751   -479       C  
ATOM   1275  CG2 VAL B 252     -30.498  41.702 -43.782  1.00 28.57           C  
ANISOU 1275  CG2 VAL B 252     4334   3133   3390   -828    569   -320       C  
ATOM   1276  N   LYS B 253     -30.754  46.238 -43.997  1.00 37.61           N  
ANISOU 1276  N   LYS B 253     6409   3160   4721   -894    894   -720       N  
ATOM   1277  CA  LYS B 253     -31.324  47.571 -44.156  1.00 41.48           C  
ANISOU 1277  CA  LYS B 253     7237   3168   5355   -744    949   -851       C  
ATOM   1278  C   LYS B 253     -30.578  48.368 -45.214  1.00 43.60           C  
ANISOU 1278  C   LYS B 253     7834   3101   5632   -897    911   -650       C  
ATOM   1279  O   LYS B 253     -31.195  49.088 -46.007  1.00 45.35           O  
ANISOU 1279  O   LYS B 253     8346   2903   5982   -645    837   -564       O  
ATOM   1280  CB  LYS B 253     -31.307  48.313 -42.820  1.00 45.15           C  
ANISOU 1280  CB  LYS B 253     7834   3550   5772   -930   1084  -1200       C  
ATOM   1281  CG  LYS B 253     -32.077  49.620 -42.832  1.00 51.16           C  
ANISOU 1281  CG  LYS B 253     8908   3778   6750   -690   1140  -1424       C  
ATOM   1282  CD  LYS B 253     -32.236  50.171 -41.419  1.00 55.95           C  
ANISOU 1282  CD  LYS B 253     9578   4379   7302   -850   1323  -1858       C  
ATOM   1283  CE  LYS B 253     -30.963  50.851 -40.931  1.00 58.99           C  
ANISOU 1283  CE  LYS B 253    10189   4709   7518  -1342   1343  -1895       C  
ATOM   1284  NZ  LYS B 253     -31.199  52.268 -40.527  1.00 64.67           N  
ANISOU 1284  NZ  LYS B 253    11133   5062   8378  -1273   1377  -2122       N  
ATOM   1285  N   GLN B 254     -29.248  48.251 -45.242  1.00 42.87           N  
ANISOU 1285  N   GLN B 254     7706   3185   5396  -1329    945   -582       N  
ATOM   1286  CA AGLN B 254     -28.460  48.983 -46.227  0.50 46.13           C  
ANISOU 1286  CA AGLN B 254     8431   3331   5765  -1601    980   -420       C  
ATOM   1287  CA BGLN B 254     -28.472  48.993 -46.228  0.50 46.15           C  
ANISOU 1287  CA BGLN B 254     8438   3328   5769  -1598    980   -420       C  
ATOM   1288  C   GLN B 254     -28.807  48.550 -47.645  1.00 44.99           C  
ANISOU 1288  C   GLN B 254     8321   3163   5610  -1394    902   -128       C  
ATOM   1289  O   GLN B 254     -28.807  49.372 -48.570  1.00 47.20           O  
ANISOU 1289  O   GLN B 254     9020   3063   5850  -1445    881     41       O  
ATOM   1290  CB AGLN B 254     -26.968  48.785 -45.960  0.50 46.62           C  
ANISOU 1290  CB AGLN B 254     8302   3706   5706  -2117   1056   -480       C  
ATOM   1291  CB BGLN B 254     -26.975  48.835 -45.946  0.50 46.77           C  
ANISOU 1291  CB BGLN B 254     8337   3708   5726  -2121   1058   -484       C  
ATOM   1292  CG AGLN B 254     -26.065  49.553 -46.909  0.50 49.91           C  
ANISOU 1292  CG AGLN B 254     8919   4013   6034  -2428   1136   -362       C  
ATOM   1293  CG BGLN B 254     -26.445  49.818 -44.902  0.50 50.19           C  
ANISOU 1293  CG BGLN B 254     8912   4038   6121  -2412   1115   -730       C  
ATOM   1294  CD AGLN B 254     -24.603  49.208 -46.723  0.50 50.78           C  
ANISOU 1294  CD AGLN B 254     8659   4563   6070  -2838   1197   -478       C  
ATOM   1295  CD BGLN B 254     -25.204  49.315 -44.181  0.50 50.36           C  
ANISOU 1295  CD BGLN B 254     8559   4528   6048  -2781   1088   -867       C  
ATOM   1296  OE1AGLN B 254     -24.224  48.035 -46.742  0.50 48.45           O  
ANISOU 1296  OE1AGLN B 254     7941   4660   5808  -2847   1157   -489       O  
ATOM   1297  OE1BGLN B 254     -24.560  48.360 -44.615  0.50 49.43           O  
ANISOU 1297  OE1BGLN B 254     8088   4761   5931  -2864   1043   -787       O  
ATOM   1298  NE2AGLN B 254     -23.771  50.228 -46.544  0.50 54.20           N  
ANISOU 1298  NE2AGLN B 254     9227   4931   6435  -3156   1276   -585       N  
ATOM   1299  NE2BGLN B 254     -24.866  49.960 -43.071  0.50 51.97           N  
ANISOU 1299  NE2BGLN B 254     8814   4747   6186  -2970   1088  -1091       N  
ATOM   1300  N   TYR B 255     -29.108  47.263 -47.832  1.00 42.84           N  
ANISOU 1300  N   TYR B 255     7640   3294   5343  -1178    837    -61       N  
ATOM   1301  CA  TYR B 255     -29.447  46.770 -49.162  1.00 42.86           C  
ANISOU 1301  CA  TYR B 255     7658   3322   5307  -1004    762    177       C  
ATOM   1302  C   TYR B 255     -30.765  47.358 -49.650  1.00 44.79           C  
ANISOU 1302  C   TYR B 255     8191   3172   5654   -576    600    260       C  
ATOM   1303  O   TYR B 255     -30.842  47.901 -50.758  1.00 46.39           O  
ANISOU 1303  O   TYR B 255     8780   3076   5769   -574    510    481       O  
ATOM   1304  CB  TYR B 255     -29.514  45.243 -49.162  1.00 39.71           C  
ANISOU 1304  CB  TYR B 255     6762   3406   4920   -866    723    183       C  
ATOM   1305  CG  TYR B 255     -29.995  44.682 -50.482  1.00 39.83           C  
ANISOU 1305  CG  TYR B 255     6779   3465   4888   -672    643    377       C  
ATOM   1306  CD1 TYR B 255     -29.106  44.444 -51.521  1.00 41.73           C  
ANISOU 1306  CD1 TYR B 255     7045   3834   4978   -949    733    483       C  
ATOM   1307  CD2 TYR B 255     -31.341  44.413 -50.697  1.00 39.37           C  
ANISOU 1307  CD2 TYR B 255     6684   3350   4926   -243    490    408       C  
ATOM   1308  CE1 TYR B 255     -29.546  43.940 -52.744  1.00 42.22           C  
ANISOU 1308  CE1 TYR B 255     7149   3954   4939   -813    666    638       C  
ATOM   1309  CE2 TYR B 255     -31.789  43.923 -51.914  1.00 40.57           C  
ANISOU 1309  CE2 TYR B 255     6853   3555   5007    -87    379    572       C  
ATOM   1310  CZ  TYR B 255     -30.888  43.677 -52.928  1.00 41.85           C  
ANISOU 1310  CZ  TYR B 255     7093   3835   4973   -377    465    696       C  
ATOM   1311  OH  TYR B 255     -31.336  43.176 -54.132  1.00 44.52           O  
ANISOU 1311  OH  TYR B 255     7479   4250   5188   -260    362    835       O  
ATOM   1312  N   PHE B 256     -31.821  47.243 -48.843  1.00 44.16           N  
ANISOU 1312  N   PHE B 256     7927   3099   5753   -218    546     70       N  
ATOM   1313  CA  PHE B 256     -33.127  47.741 -49.256  1.00 47.25           C  
ANISOU 1313  CA  PHE B 256     8469   3161   6325    257    356     70       C  
ATOM   1314  C   PHE B 256     -33.205  49.261 -49.266  1.00 55.36           C  
ANISOU 1314  C   PHE B 256    10025   3562   7449    294    290     45       C  
ATOM   1315  O   PHE B 256     -34.195  49.806 -49.766  1.00 58.03           O  
ANISOU 1315  O   PHE B 256    10425   3660   7964    695     49     74       O  
ATOM   1316  CB  PHE B 256     -34.220  47.158 -48.358  1.00 43.26           C  
ANISOU 1316  CB  PHE B 256     7537   2897   6003    580    379   -209       C  
ATOM   1317  CG  PHE B 256     -34.511  45.712 -48.637  1.00 38.45           C  
ANISOU 1317  CG  PHE B 256     6505   2764   5340    647    360   -137       C  
ATOM   1318  CD1 PHE B 256     -35.130  45.330 -49.818  1.00 37.63           C  
ANISOU 1318  CD1 PHE B 256     6374   2668   5256    907    160     42       C  
ATOM   1319  CD2 PHE B 256     -34.153  44.733 -47.727  1.00 33.61           C  
ANISOU 1319  CD2 PHE B 256     5570   2561   4639    433    509   -239       C  
ATOM   1320  CE1 PHE B 256     -35.390  43.996 -50.081  1.00 34.26           C  
ANISOU 1320  CE1 PHE B 256     5579   2651   4787    939    152     78       C  
ATOM   1321  CE2 PHE B 256     -34.407  43.403 -47.982  1.00 31.77           C  
ANISOU 1321  CE2 PHE B 256     5011   2689   4372    480    479   -166       C  
ATOM   1322  CZ  PHE B 256     -35.025  43.029 -49.158  1.00 32.20           C  
ANISOU 1322  CZ  PHE B 256     5014   2748   4471    725    322    -27       C  
ATOM   1323  N   SER B 257     -32.196  49.956 -48.738  1.00 59.53           N  
ANISOU 1323  N   SER B 257    10760   3973   7885   -131    454    -23       N  
ATOM   1324  CA  SER B 257     -32.150  51.405 -48.890  1.00 67.82           C  
ANISOU 1324  CA  SER B 257    12160   4605   9002   -158    362     -6       C  
ATOM   1325  C   SER B 257     -31.714  51.810 -50.292  1.00 71.81           C  
ANISOU 1325  C   SER B 257    12983   4993   9310   -324    239    356       C  
ATOM   1326  O   SER B 257     -32.138  52.859 -50.789  1.00 77.09           O  
ANISOU 1326  O   SER B 257    13966   5266  10059   -166     50    457       O  
ATOM   1327  CB  SER B 257     -31.210  52.021 -47.851  1.00 69.97           C  
ANISOU 1327  CB  SER B 257    12508   4856   9221   -581    574   -224       C  
ATOM   1328  OG  SER B 257     -29.851  51.864 -48.227  1.00 69.04           O  
ANISOU 1328  OG  SER B 257    12426   4964   8843  -1113    710    -76       O  
ATOM   1329  N   LYS B 258     -30.888  50.992 -50.947  1.00 71.29           N  
ANISOU 1329  N   LYS B 258    12835   5269   8983   -650    351    528       N  
ATOM   1330  CA  LYS B 258     -30.360  51.310 -52.266  1.00 76.82           C  
ANISOU 1330  CA  LYS B 258    13825   5943   9420   -900    312    805       C  
ATOM   1331  C   LYS B 258     -30.937  50.454 -53.386  1.00 77.46           C  
ANISOU 1331  C   LYS B 258    13834   6205   9391   -680    152   1015       C  
ATOM   1332  O   LYS B 258     -30.749  50.798 -54.559  1.00 80.71           O  
ANISOU 1332  O   LYS B 258    14547   6553   9567   -830     72   1234       O  
ATOM   1333  CB  LYS B 258     -28.829  51.174 -52.271  1.00 78.81           C  
ANISOU 1333  CB  LYS B 258    14006   6493   9444  -1514    606    759       C  
ATOM   1334  CG  LYS B 258     -28.106  52.232 -51.446  1.00 85.37           C  
ANISOU 1334  CG  LYS B 258    14989   7142  10307  -1823    737    587       C  
ATOM   1335  CD  LYS B 258     -26.797  52.651 -52.102  1.00 90.22           C  
ANISOU 1335  CD  LYS B 258    15746   7884  10649  -2386    927    629       C  
ATOM   1336  CE  LYS B 258     -26.053  53.677 -51.258  1.00 93.75           C  
ANISOU 1336  CE  LYS B 258    16321   8177  11123  -2712   1054    442       C  
ATOM   1337  NZ  LYS B 258     -26.905  54.847 -50.915  1.00 97.69           N  
ANISOU 1337  NZ  LYS B 258    17223   8099  11794  -2437    875    460       N  
ATOM   1338  N   SER B 259     -31.626  49.360 -53.071  1.00 75.56           N  
ANISOU 1338  N   SER B 259    11450   6875  10385   -828  -1702   1987       N  
ATOM   1339  CA  SER B 259     -32.181  48.473 -54.081  1.00 72.39           C  
ANISOU 1339  CA  SER B 259    10439   7256   9809   -693  -1314   2073       C  
ATOM   1340  C   SER B 259     -33.695  48.408 -53.951  1.00 71.53           C  
ANISOU 1340  C   SER B 259    10454   7217   9507   -211   -964   1885       C  
ATOM   1341  O   SER B 259     -34.267  48.716 -52.901  1.00 73.88           O  
ANISOU 1341  O   SER B 259    11292   7050   9730     67   -953   1599       O  
ATOM   1342  CB  SER B 259     -31.591  47.060 -53.976  1.00 68.39           C  
ANISOU 1342  CB  SER B 259     9622   7223   9138   -845  -1221   1862       C  
ATOM   1343  OG  SER B 259     -32.303  46.147 -54.796  1.00 64.27           O  
ANISOU 1343  OG  SER B 259     8637   7364   8420   -672   -856   1816       O  
ATOM   1344  N   LYS B 260     -34.340  47.988 -55.041  1.00 68.96           N  
ANISOU 1344  N   LYS B 260     9601   7529   9071   -107   -676   2065       N  
ATOM   1345  CA  LYS B 260     -35.793  47.880 -55.103  1.00 68.74           C  
ANISOU 1345  CA  LYS B 260     9551   7702   8865    308   -344   1998       C  
ATOM   1346  C   LYS B 260     -36.253  46.458 -55.404  1.00 62.70           C  
ANISOU 1346  C   LYS B 260     8375   7599   7848    331    -76   1792       C  
ATOM   1347  O   LYS B 260     -37.412  46.252 -55.779  1.00 62.29           O  
ANISOU 1347  O   LYS B 260     8121   7896   7649    580    184   1839       O  
ATOM   1348  CB  LYS B 260     -36.356  48.851 -56.141  1.00 74.90           C  
ANISOU 1348  CB  LYS B 260    10098   8603   9758    427   -275   2460       C  
ATOM   1349  CG  LYS B 260     -36.263  50.307 -55.723  1.00 83.58           C  
ANISOU 1349  CG  LYS B 260    11695   8924  11138    521   -495   2635       C  
ATOM   1350  CD  LYS B 260     -37.282  50.650 -54.649  1.00 87.63           C  
ANISOU 1350  CD  LYS B 260    12768   8975  11552   1004   -348   2349       C  
ATOM   1351  CE  LYS B 260     -37.155  52.104 -54.221  1.00 94.52           C  
ANISOU 1351  CE  LYS B 260    14215   8987  12712   1124   -586   2453       C  
ATOM   1352  NZ  LYS B 260     -35.874  52.362 -53.505  1.00 96.88           N  
ANISOU 1352  NZ  LYS B 260    14927   8705  13177    740  -1027   2264       N  
ATOM   1353  N   ALA B 261     -35.369  45.473 -55.254  1.00 56.40           N  
ANISOU 1353  N   ALA B 261     7446   6967   7018     70   -150   1587       N  
ATOM   1354  CA  ALA B 261     -35.774  44.082 -55.382  1.00 48.64           C  
ANISOU 1354  CA  ALA B 261     6166   6469   5847     91     68   1334       C  
ATOM   1355  C   ALA B 261     -36.836  43.746 -54.336  1.00 43.15           C  
ANISOU 1355  C   ALA B 261     5760   5605   5029    400    235   1089       C  
ATOM   1356  O   ALA B 261     -36.927  44.376 -53.280  1.00 43.53           O  
ANISOU 1356  O   ALA B 261     6300   5141   5099    574    160   1003       O  
ATOM   1357  CB  ALA B 261     -34.562  43.161 -55.244  1.00 45.53           C  
ANISOU 1357  CB  ALA B 261     5654   6158   5488   -193    -47   1165       C  
ATOM   1358  N   GLU B 262     -37.658  42.742 -54.647  1.00 38.47           N  
ANISOU 1358  N   GLU B 262     4855   5470   4293    470    455    988       N  
ATOM   1359  CA  GLU B 262     -38.782  42.417 -53.775  1.00 39.14           C  
ANISOU 1359  CA  GLU B 262     5104   5507   4261    769    637    871       C  
ATOM   1360  C   GLU B 262     -38.350  41.663 -52.523  1.00 34.94           C  
ANISOU 1360  C   GLU B 262     4837   4715   3723    747    588    579       C  
ATOM   1361  O   GLU B 262     -38.995  41.792 -51.475  1.00 35.51           O  
ANISOU 1361  O   GLU B 262     5212   4582   3698   1035    677    512       O  
ATOM   1362  CB  GLU B 262     -39.828  41.609 -54.543  1.00 41.47           C  
ANISOU 1362  CB  GLU B 262     4939   6381   4435    792    838    923       C  
ATOM   1363  CG  GLU B 262     -40.676  42.467 -55.476  1.00 47.72           C  
ANISOU 1363  CG  GLU B 262     5516   7445   5173    944    939   1270       C  
ATOM   1364  CD  GLU B 262     -41.284  43.671 -54.770  1.00 53.83           C  
ANISOU 1364  CD  GLU B 262     6676   7813   5963   1336   1007   1445       C  
ATOM   1365  OE1 GLU B 262     -42.101  43.477 -53.845  1.00 55.26           O  
ANISOU 1365  OE1 GLU B 262     7036   7914   6047   1631   1159   1382       O  
ATOM   1366  OE2 GLU B 262     -40.939  44.814 -55.138  1.00 57.64           O  
ANISOU 1366  OE2 GLU B 262     7286   8054   6561   1368    910   1660       O  
ATOM   1367  N   PHE B 263     -37.279  40.880 -52.599  1.00 30.99           N  
ANISOU 1367  N   PHE B 263     4212   4256   3307    446    465    434       N  
ATOM   1368  CA  PHE B 263     -36.803  40.174 -51.417  1.00 30.21           C  
ANISOU 1368  CA  PHE B 263     4330   3930   3218    415    408    214       C  
ATOM   1369  C   PHE B 263     -35.357  39.768 -51.643  1.00 30.99           C  
ANISOU 1369  C   PHE B 263     4318   4005   3451     85    223    166       C  
ATOM   1370  O   PHE B 263     -34.837  39.835 -52.759  1.00 31.46           O  
ANISOU 1370  O   PHE B 263     4081   4304   3567    -92    186    280       O  
ATOM   1371  CB  PHE B 263     -37.671  38.953 -51.092  1.00 27.76           C  
ANISOU 1371  CB  PHE B 263     3821   3875   2850    509    607    106       C  
ATOM   1372  CG  PHE B 263     -37.616  37.870 -52.136  1.00 28.37           C  
ANISOU 1372  CG  PHE B 263     3437   4347   2995    289    663     42       C  
ATOM   1373  CD1 PHE B 263     -38.459  37.914 -53.241  1.00 29.30           C  
ANISOU 1373  CD1 PHE B 263     3242   4849   3040    302    769    149       C  
ATOM   1374  CD2 PHE B 263     -36.736  36.807 -52.012  1.00 28.88           C  
ANISOU 1374  CD2 PHE B 263     3392   4400   3181     86    605   -131       C  
ATOM   1375  CE1 PHE B 263     -38.418  36.922 -54.198  1.00 30.49           C  
ANISOU 1375  CE1 PHE B 263     3022   5353   3208    103    791     25       C  
ATOM   1376  CE2 PHE B 263     -36.685  35.807 -52.976  1.00 28.43           C  
ANISOU 1376  CE2 PHE B 263     2972   4655   3175    -74    655   -252       C  
ATOM   1377  CZ  PHE B 263     -37.529  35.869 -54.072  1.00 29.72           C  
ANISOU 1377  CZ  PHE B 263     2869   5189   3233    -72    737   -203       C  
ATOM   1378  N   ILE B 264     -34.706  39.352 -50.555  1.00 24.55           N  
ANISOU 1378  N   ILE B 264     3721   2944   2661     27    117     33       N  
ATOM   1379  CA  ILE B 264     -33.409  38.695 -50.636  1.00 27.19           C  
ANISOU 1379  CA  ILE B 264     3891   3315   3125   -247    -12      9       C  
ATOM   1380  C   ILE B 264     -33.495  37.386 -49.872  1.00 27.08           C  
ANISOU 1380  C   ILE B 264     3812   3346   3130   -215     92   -157       C  
ATOM   1381  O   ILE B 264     -34.390  37.175 -49.051  1.00 25.87           O  
ANISOU 1381  O   ILE B 264     3814   3134   2881    -10    202   -223       O  
ATOM   1382  CB  ILE B 264     -32.251  39.543 -50.076  1.00 28.22           C  
ANISOU 1382  CB  ILE B 264     4311   3095   3318   -428   -319    107       C  
ATOM   1383  CG1 ILE B 264     -32.414  39.752 -48.564  1.00 27.55           C  
ANISOU 1383  CG1 ILE B 264     4696   2653   3118   -300   -415    -33       C  
ATOM   1384  CG2 ILE B 264     -32.165  40.865 -50.764  1.00 29.39           C  
ANISOU 1384  CG2 ILE B 264     4536   3124   3509   -480   -454    318       C  
ATOM   1385  CD1 ILE B 264     -31.254  40.471 -47.940  1.00 29.97           C  
ANISOU 1385  CD1 ILE B 264     5303   2616   3471   -534   -772     25       C  
ATOM   1386  N   LEU B 265     -32.548  36.501 -50.166  1.00 24.75           N  
ANISOU 1386  N   LEU B 265     3261   3173   2971   -399     68   -184       N  
ATOM   1387  CA  LEU B 265     -32.302  35.301 -49.383  1.00 24.21           C  
ANISOU 1387  CA  LEU B 265     3135   3070   2993   -408    116   -284       C  
ATOM   1388  C   LEU B 265     -30.925  35.428 -48.757  1.00 25.45           C  
ANISOU 1388  C   LEU B 265     3391   3058   3221   -582   -101   -186       C  
ATOM   1389  O   LEU B 265     -30.014  35.996 -49.367  1.00 26.98           O  
ANISOU 1389  O   LEU B 265     3503   3288   3461   -749   -243    -45       O  
ATOM   1390  CB  LEU B 265     -32.382  34.040 -50.251  1.00 23.14           C  
ANISOU 1390  CB  LEU B 265     2614   3192   2986   -442    284   -405       C  
ATOM   1391  CG  LEU B 265     -33.733  33.794 -50.914  1.00 24.71           C  
ANISOU 1391  CG  LEU B 265     2672   3596   3119   -339    451   -495       C  
ATOM   1392  CD1 LEU B 265     -33.676  32.547 -51.801  1.00 28.76           C  
ANISOU 1392  CD1 LEU B 265     2860   4311   3757   -414    552   -678       C  
ATOM   1393  CD2 LEU B 265     -34.826  33.674 -49.864  1.00 24.52           C  
ANISOU 1393  CD2 LEU B 265     2812   3463   3041   -173    527   -470       C  
ATOM   1394  N   ARG B 266     -30.781  34.939 -47.525  1.00 23.10           N  
ANISOU 1394  N   ARG B 266     3242   2615   2920   -553   -140   -206       N  
ATOM   1395  CA  ARG B 266     -29.515  35.086 -46.827  1.00 24.62           C  
ANISOU 1395  CA  ARG B 266     3528   2676   3150   -737   -378    -81       C  
ATOM   1396  C   ARG B 266     -29.302  33.882 -45.924  1.00 25.56           C  
ANISOU 1396  C   ARG B 266     3544   2812   3355   -706   -311    -77       C  
ATOM   1397  O   ARG B 266     -30.238  33.149 -45.602  1.00 26.01           O  
ANISOU 1397  O   ARG B 266     3555   2910   3417   -535   -118   -162       O  
ATOM   1398  CB  ARG B 266     -29.467  36.389 -46.018  1.00 25.56           C  
ANISOU 1398  CB  ARG B 266     4115   2515   3081   -762   -635    -65       C  
ATOM   1399  CG  ARG B 266     -30.413  36.418 -44.821  1.00 25.19           C  
ANISOU 1399  CG  ARG B 266     4402   2354   2814   -514   -573   -200       C  
ATOM   1400  CD  ARG B 266     -30.577  37.845 -44.278  1.00 29.00           C  
ANISOU 1400  CD  ARG B 266     5409   2529   3080   -457   -791   -271       C  
ATOM   1401  NE  ARG B 266     -31.773  38.004 -43.447  1.00 29.93           N  
ANISOU 1401  NE  ARG B 266     5825   2611   2938    -95   -633   -413       N  
ATOM   1402  CZ  ARG B 266     -31.962  37.419 -42.266  1.00 33.98           C  
ANISOU 1402  CZ  ARG B 266     6436   3195   3277     46   -588   -452       C  
ATOM   1403  NH1 ARG B 266     -31.026  36.634 -41.736  1.00 32.30           N  
ANISOU 1403  NH1 ARG B 266     6065   3064   3145   -161   -703   -361       N  
ATOM   1404  NH2 ARG B 266     -33.087  37.637 -41.595  1.00 37.49           N  
ANISOU 1404  NH2 ARG B 266     7120   3669   3454    422   -415   -539       N  
ATOM   1405  N   TRP B 267     -28.043  33.679 -45.543  1.00 27.10           N  
ANISOU 1405  N   TRP B 267     3660   2996   3642   -886   -479     83       N  
ATOM   1406  CA  TRP B 267     -27.676  32.613 -44.619  1.00 27.14           C  
ANISOU 1406  CA  TRP B 267     3551   3017   3743   -870   -446    164       C  
ATOM   1407  C   TRP B 267     -28.260  32.920 -43.246  1.00 27.25           C  
ANISOU 1407  C   TRP B 267     3917   2924   3513   -766   -526    132       C  
ATOM   1408  O   TRP B 267     -27.952  33.958 -42.656  1.00 29.72           O  
ANISOU 1408  O   TRP B 267     4575   3106   3610   -852   -785    135       O  
ATOM   1409  CB  TRP B 267     -26.152  32.494 -44.555  1.00 29.63           C  
ANISOU 1409  CB  TRP B 267     3684   3389   4185  -1088   -629    408       C  
ATOM   1410  CG  TRP B 267     -25.638  31.322 -43.750  1.00 30.80           C  
ANISOU 1410  CG  TRP B 267     3631   3586   4486  -1065   -575    559       C  
ATOM   1411  CD1 TRP B 267     -25.003  31.377 -42.543  1.00 31.66           C  
ANISOU 1411  CD1 TRP B 267     3845   3684   4500  -1176   -790    750       C  
ATOM   1412  CD2 TRP B 267     -25.706  29.934 -44.106  1.00 31.21           C  
ANISOU 1412  CD2 TRP B 267     3344   3692   4821   -925   -305    548       C  
ATOM   1413  NE1 TRP B 267     -24.675  30.109 -42.123  1.00 31.59           N  
ANISOU 1413  NE1 TRP B 267     3543   3750   4709  -1102   -648    910       N  
ATOM   1414  CE2 TRP B 267     -25.096  29.205 -43.063  1.00 33.36           C  
ANISOU 1414  CE2 TRP B 267     3509   3974   5193   -941   -350    782       C  
ATOM   1415  CE3 TRP B 267     -26.224  29.236 -45.203  1.00 33.69           C  
ANISOU 1415  CE3 TRP B 267     3454   4035   5313   -792    -50    353       C  
ATOM   1416  CZ2 TRP B 267     -24.991  27.813 -43.085  1.00 34.94           C  
ANISOU 1416  CZ2 TRP B 267     3402   4158   5715   -812   -133    850       C  
ATOM   1417  CZ3 TRP B 267     -26.122  27.848 -45.220  1.00 34.16           C  
ANISOU 1417  CZ3 TRP B 267     3253   4051   5674   -679    140    360       C  
ATOM   1418  CH2 TRP B 267     -25.510  27.156 -44.168  1.00 36.09           C  
ANISOU 1418  CH2 TRP B 267     3395   4254   6063   -681    105    618       C  
ATOM   1419  N   SER B 268     -29.108  32.029 -42.741  1.00 25.04           N  
ANISOU 1419  N   SER B 268     3553   2703   3258   -576   -316    107       N  
ATOM   1420  CA  SER B 268     -29.858  32.333 -41.531  1.00 25.11           C  
ANISOU 1420  CA  SER B 268     3866   2699   2977   -397   -329     88       C  
ATOM   1421  C   SER B 268     -28.949  32.328 -40.311  1.00 30.63           C  
ANISOU 1421  C   SER B 268     4692   3405   3541   -503   -557    230       C  
ATOM   1422  O   SER B 268     -28.002  31.540 -40.223  1.00 27.28           O  
ANISOU 1422  O   SER B 268     3983   3044   3337   -653   -597    420       O  
ATOM   1423  CB  SER B 268     -30.991  31.325 -41.348  1.00 28.23           C  
ANISOU 1423  CB  SER B 268     4052   3212   3461   -189    -47    120       C  
ATOM   1424  OG  SER B 268     -31.556  31.417 -40.049  1.00 30.34           O  
ANISOU 1424  OG  SER B 268     4524   3560   3442      8    -36    191       O  
ATOM   1425  N   SER B 269     -29.243  33.225 -39.366  1.00 31.74           N  
ANISOU 1425  N   SER B 269     5270   3493   3297   -403   -708    136       N  
ATOM   1426  CA  SER B 269     -28.516  33.274 -38.102  1.00 34.46           C  
ANISOU 1426  CA  SER B 269     5785   3891   3416   -491   -951    237       C  
ATOM   1427  C   SER B 269     -28.711  32.023 -37.258  1.00 32.55           C  
ANISOU 1427  C   SER B 269     5257   3888   3222   -365   -777    460       C  
ATOM   1428  O   SER B 269     -27.985  31.837 -36.268  1.00 34.30           O  
ANISOU 1428  O   SER B 269     5500   4230   3303   -464   -962    622       O  
ATOM   1429  CB  SER B 269     -28.963  34.500 -37.307  1.00 40.55           C  
ANISOU 1429  CB  SER B 269     7147   4546   3714   -344  -1127      6       C  
ATOM   1430  OG  SER B 269     -30.243  34.278 -36.739  1.00 42.05           O  
ANISOU 1430  OG  SER B 269     7416   4889   3670     52   -851    -46       O  
ATOM   1431  N   ALA B 270     -29.671  31.170 -37.609  1.00 31.15           N  
ANISOU 1431  N   ALA B 270     4798   3790   3246   -173   -451    507       N  
ATOM   1432  CA  ALA B 270     -29.938  29.972 -36.827  1.00 34.83           C  
ANISOU 1432  CA  ALA B 270     4967   4452   3816    -62   -290    776       C  
ATOM   1433  C   ALA B 270     -28.972  28.838 -37.128  1.00 34.98           C  
ANISOU 1433  C   ALA B 270     4552   4449   4292   -257   -276   1008       C  
ATOM   1434  O   ALA B 270     -28.942  27.862 -36.374  1.00 36.39           O  
ANISOU 1434  O   ALA B 270     4478   4758   4592   -205   -197   1294       O  
ATOM   1435  CB  ALA B 270     -31.374  29.493 -37.056  1.00 35.64           C  
ANISOU 1435  CB  ALA B 270     4920   4628   3993    183     16    788       C  
ATOM   1436  N   ASN B 271     -28.178  28.937 -38.196  1.00 32.67           N  
ANISOU 1436  N   ASN B 271     4150   4012   4252   -449   -337    927       N  
ATOM   1437  CA  ASN B 271     -27.212  27.880 -38.484  1.00 33.97           C  
ANISOU 1437  CA  ASN B 271     3913   4162   4830   -564   -296   1148       C  
ATOM   1438  C   ASN B 271     -26.098  27.826 -37.439  1.00 39.89           C  
ANISOU 1438  C   ASN B 271     4626   5054   5475   -697   -520   1445       C  
ATOM   1439  O   ASN B 271     -25.667  26.735 -37.050  1.00 40.35           O  
ANISOU 1439  O   ASN B 271     4348   5173   5809   -680   -434   1745       O  
ATOM   1440  CB  ASN B 271     -26.621  28.073 -39.876  1.00 31.33           C  
ANISOU 1440  CB  ASN B 271     3467   3721   4715   -683   -289   1005       C  
ATOM   1441  CG  ASN B 271     -27.643  27.857 -40.966  1.00 29.87           C  
ANISOU 1441  CG  ASN B 271     3228   3445   4675   -568    -62    748       C  
ATOM   1442  OD1 ASN B 271     -28.127  26.744 -41.162  1.00 30.31           O  
ANISOU 1442  OD1 ASN B 271     3043   3442   5031   -475    139    764       O  
ATOM   1443  ND2 ASN B 271     -27.990  28.925 -41.671  1.00 29.36           N  
ANISOU 1443  ND2 ASN B 271     3386   3362   4409   -591   -116    526       N  
ATOM   1444  N   GLU B 272     -25.614  28.984 -36.982  1.00 45.12           N  
ANISOU 1444  N   GLU B 272     5628   5758   5757   -845   -827   1382       N  
ATOM   1445  CA  GLU B 272     -24.413  29.011 -36.147  1.00 54.77           C  
ANISOU 1445  CA  GLU B 272     6795   7135   6879  -1051  -1105   1670       C  
ATOM   1446  C   GLU B 272     -24.613  28.243 -34.845  1.00 60.25           C  
ANISOU 1446  C   GLU B 272     7375   8058   7458   -926  -1058   1940       C  
ATOM   1447  O   GLU B 272     -23.815  27.365 -34.501  1.00 61.83           O  
ANISOU 1447  O   GLU B 272     7206   8388   7899   -990  -1053   2315       O  
ATOM   1448  CB  GLU B 272     -23.997  30.453 -35.844  1.00 59.43           C  
ANISOU 1448  CB  GLU B 272     7839   7682   7060  -1263  -1499   1507       C  
ATOM   1449  CG  GLU B 272     -22.963  30.540 -34.720  1.00 66.71           C  
ANISOU 1449  CG  GLU B 272     8773   8813   7759  -1490  -1844   1784       C  
ATOM   1450  CD  GLU B 272     -22.434  31.943 -34.485  1.00 72.03           C  
ANISOU 1450  CD  GLU B 272     9903   9380   8086  -1777  -2308   1618       C  
ATOM   1451  OE1 GLU B 272     -22.810  32.864 -35.239  1.00 72.41           O  
ANISOU 1451  OE1 GLU B 272    10240   9162   8112  -1793  -2349   1320       O  
ATOM   1452  OE2 GLU B 272     -21.635  32.123 -33.539  1.00 76.87           O  
ANISOU 1452  OE2 GLU B 272    10582  10167   8458  -2005  -2655   1804       O  
ATOM   1453  N   SER B 273     -25.673  28.562 -34.106  1.00 66.47           N  
ANISOU 1453  N   SER B 273     8449   8932   7873   -718  -1006   1796       N  
ATOM   1454  CA  SER B 273     -25.860  28.038 -32.760  1.00 70.07           C  
ANISOU 1454  CA  SER B 273     8835   9694   8094   -590   -998   2071       C  
ATOM   1455  C   SER B 273     -26.800  26.842 -32.710  1.00 68.22           C  
ANISOU 1455  C   SER B 273     8244   9509   8167   -346   -633   2282       C  
ATOM   1456  O   SER B 273     -27.132  26.376 -31.616  1.00 72.81           O  
ANISOU 1456  O   SER B 273     8724  10380   8560   -201   -582   2561       O  
ATOM   1457  CB  SER B 273     -26.377  29.141 -31.835  1.00 74.26           C  
ANISOU 1457  CB  SER B 273     9906  10363   7948   -474  -1179   1820       C  
ATOM   1458  OG  SER B 273     -27.689  29.537 -32.196  1.00 75.79           O  
ANISOU 1458  OG  SER B 273    10323  10454   8021   -193   -951   1530       O  
ATOM   1459  N   ASP B 274     -27.235  26.328 -33.857  1.00 86.27           N  
ANISOU 1459  N   ASP B 274    12447  13504   6826    232  -2592    691       N  
ATOM   1460  CA  ASP B 274     -28.151  25.195 -33.845  1.00 86.55           C  
ANISOU 1460  CA  ASP B 274    12528  13639   6719     86  -2491   1167       C  
ATOM   1461  C   ASP B 274     -27.407  23.918 -33.471  1.00 89.51           C  
ANISOU 1461  C   ASP B 274    12900  13844   7265    110  -3030   1952       C  
ATOM   1462  O   ASP B 274     -26.340  23.621 -34.018  1.00 88.25           O  
ANISOU 1462  O   ASP B 274    12557  13369   7607    338  -3449   2009       O  
ATOM   1463  CB  ASP B 274     -28.835  25.033 -35.202  1.00 82.46           C  
ANISOU 1463  CB  ASP B 274    11970  12926   6433     -5  -2196    872       C  
ATOM   1464  CG  ASP B 274     -29.508  23.679 -35.363  1.00 85.66           C  
ANISOU 1464  CG  ASP B 274    12530  13047   6969   -251  -2207   1465       C  
ATOM   1465  OD1 ASP B 274     -30.671  23.536 -34.926  1.00 86.94           O  
ANISOU 1465  OD1 ASP B 274    12854  13449   6730   -546  -1895   1572       O  
ATOM   1466  OD2 ASP B 274     -28.891  22.770 -35.955  1.00 87.00           O  
ANISOU 1466  OD2 ASP B 274    12590  12539   7926    -35  -2371   1663       O  
ATOM   1467  N   THR B 275     -27.987  23.158 -32.543  1.00 92.02           N  
ANISOU 1467  N   THR B 275    13469  14189   7306   -107  -3035   2517       N  
ATOM   1468  CA  THR B 275     -27.426  21.913 -32.040  1.00 96.78           C  
ANISOU 1468  CA  THR B 275    14217  14426   8131    -70  -3509   3266       C  
ATOM   1469  C   THR B 275     -28.010  20.682 -32.733  1.00 97.40           C  
ANISOU 1469  C   THR B 275    14475  13916   8618   -244  -3512   3727       C  
ATOM   1470  O   THR B 275     -27.469  19.582 -32.570  1.00101.93           O  
ANISOU 1470  O   THR B 275    15153  13961   9616   -113  -3901   4258       O  
ATOM   1471  CB  THR B 275     -27.670  21.827 -30.518  1.00101.41           C  
ANISOU 1471  CB  THR B 275    15051  15332   8149   -206  -3507   3587       C  
ATOM   1472  OG1 THR B 275     -27.209  23.032 -29.895  1.00 99.79           O  
ANISOU 1472  OG1 THR B 275    14721  15550   7643    -15  -3479   3113       O  
ATOM   1473  CG2 THR B 275     -26.925  20.656 -29.891  1.00109.59           C  
ANISOU 1473  CG2 THR B 275    16270  15989   9379    -92  -4028   4272       C  
ATOM   1474  N   GLU B 276     -29.063  20.847 -33.542  1.00 92.69           N  
ANISOU 1474  N   GLU B 276    13892  13322   8005   -466  -3036   3429       N  
ATOM   1475  CA  GLU B 276     -29.974  19.744 -33.836  1.00 94.55           C  
ANISOU 1475  CA  GLU B 276    14316  13107   8503   -707  -2776   3766       C  
ATOM   1476  C   GLU B 276     -29.598  18.870 -35.030  1.00 93.36           C  
ANISOU 1476  C   GLU B 276    13988  12085   9402   -411  -2790   3696       C  
ATOM   1477  O   GLU B 276     -30.100  17.740 -35.104  1.00 96.93           O  
ANISOU 1477  O   GLU B 276    14634  12066  10130   -574  -2740   4144       O  
ATOM   1478  CB  GLU B 276     -31.399  20.260 -34.065  1.00 90.80           C  
ANISOU 1478  CB  GLU B 276    13873  13039   7587  -1060  -2143   3347       C  
ATOM   1479  CG  GLU B 276     -32.250  20.306 -32.818  1.00 95.39           C  
ANISOU 1479  CG  GLU B 276    14672  14171   7402  -1461  -1951   3587       C  
ATOM   1480  CD  GLU B 276     -33.627  19.742 -33.080  1.00 95.80           C  
ANISOU 1480  CD  GLU B 276    14856  14178   7367  -1885  -1469   3620       C  
ATOM   1481  OE1 GLU B 276     -33.888  19.384 -34.247  1.00 92.17           O  
ANISOU 1481  OE1 GLU B 276    14293  13237   7490  -1802  -1266   3393       O  
ATOM   1482  OE2 GLU B 276     -34.425  19.605 -32.128  1.00100.79           O  
ANISOU 1482  OE2 GLU B 276    15589  15120   7586  -2191  -1229   3719       O  
ATOM   1483  N   ASN B 277     -28.785  19.350 -35.982  1.00 90.08           N  
ANISOU 1483  N   ASN B 277    13223  11441   9561    -20  -2821   3129       N  
ATOM   1484  CA  ASN B 277     -28.340  18.614 -37.165  1.00 90.13           C  
ANISOU 1484  CA  ASN B 277    13017  10660  10570    284  -2827   2973       C  
ATOM   1485  C   ASN B 277     -29.386  18.550 -38.293  1.00 83.69           C  
ANISOU 1485  C   ASN B 277    12159   9584  10057    181  -2235   2534       C  
ATOM   1486  O   ASN B 277     -29.025  18.196 -39.417  1.00 79.46           O  
ANISOU 1486  O   ASN B 277    11412   8465  10314    448  -2168   2237       O  
ATOM   1487  CB  ASN B 277     -27.883  17.178 -36.815  1.00100.68           C  
ANISOU 1487  CB  ASN B 277    14503  11387  12365    375  -3298   3718       C  
ATOM   1488  CG  ASN B 277     -28.028  16.191 -37.975  1.00103.17           C  
ANISOU 1488  CG  ASN B 277    14710  10894  13598    523  -3148   3657       C  
ATOM   1489  OD1 ASN B 277     -29.124  15.671 -38.231  1.00104.54           O  
ANISOU 1489  OD1 ASN B 277    15058  10890  13773    245  -2773   3777       O  
ATOM   1490  ND2 ASN B 277     -26.920  15.830 -38.579  1.00105.02           N  
ANISOU 1490  ND2 ASN B 277    14662  10634  14606    945  -3478   3517       N  
ATOM   1491  N   LYS B 278     -30.636  18.962 -38.068  1.00 75.63           N  
ANISOU 1491  N   LYS B 278    11302   9003   8432   -173  -1809   2400       N  
ATOM   1492  CA ALYS B 278     -31.729  18.558 -38.951  0.50 77.79           C  
ANISOU 1492  CA ALYS B 278    11584   8963   9011   -302  -1327   2150       C  
ATOM   1493  CA BLYS B 278     -31.714  18.545 -38.961  0.50 77.81           C  
ANISOU 1493  CA BLYS B 278    11584   8954   9027   -297  -1332   2152       C  
ATOM   1494  C   LYS B 278     -31.860  19.438 -40.192  1.00 73.39           C  
ANISOU 1494  C   LYS B 278    10823   8351   8710    -84   -977   1274       C  
ATOM   1495  O   LYS B 278     -32.092  18.930 -41.297  1.00 51.42           O  
ANISOU 1495  O   LYS B 278     7949   4995   6593     48   -762   1034       O  
ATOM   1496  CB ALYS B 278     -33.044  18.555 -38.170  0.50 64.30           C  
ANISOU 1496  CB ALYS B 278    10111   7752   6568   -788  -1022   2336       C  
ATOM   1497  CB BLYS B 278     -33.036  18.488 -38.194  0.50 64.44           C  
ANISOU 1497  CB BLYS B 278    10130   7730   6623   -785  -1027   2357       C  
ATOM   1498  CG ALYS B 278     -34.247  18.012 -38.938  0.50 62.40           C  
ANISOU 1498  CG ALYS B 278     9875   7214   6621   -970   -544   2123       C  
ATOM   1499  CG BLYS B 278     -33.952  17.346 -38.641  0.50 69.79           C  
ANISOU 1499  CG BLYS B 278    10900   7910   7710   -998   -747   2573       C  
ATOM   1500  CD ALYS B 278     -34.866  16.845 -38.187  0.50 73.11           C  
ANISOU 1500  CD ALYS B 278    11499   8440   7839  -1387   -536   2853       C  
ATOM   1501  CD BLYS B 278     -35.417  17.669 -38.402  0.50 69.03           C  
ANISOU 1501  CD BLYS B 278    10883   8324   7021  -1424   -247   2312       C  
ATOM   1502  CE ALYS B 278     -35.854  16.103 -39.062  0.50 71.59           C  
ANISOU 1502  CE ALYS B 278    11270   7794   8139  -1517   -122   2680       C  
ATOM   1503  CE BLYS B 278     -35.714  17.811 -36.923  0.50 71.09           C  
ANISOU 1503  CE BLYS B 278    11390   9254   6367  -1846   -330   2781       C  
ATOM   1504  NZ ALYS B 278     -35.270  15.790 -40.397  0.50 63.76           N  
ANISOU 1504  NZ ALYS B 278    10056   6069   8100  -1061   -170   2372       N  
ATOM   1505  NZ BLYS B 278     -37.061  17.271 -36.603  0.50 74.28           N  
ANISOU 1505  NZ BLYS B 278    11939   9826   6458  -2373     91   2902       N  
ATOM   1506  N   TYR B 279     -31.746  20.754 -40.046  1.00 50.61           N  
ANISOU 1506  N   TYR B 279     7906   6033   5290    -52   -920    782       N  
ATOM   1507  CA  TYR B 279     -32.015  21.641 -41.172  1.00 47.70           C  
ANISOU 1507  CA  TYR B 279     7461   5621   5041    107   -582    -48       C  
ATOM   1508  C   TYR B 279     -30.825  22.529 -41.503  1.00 46.33           C  
ANISOU 1508  C   TYR B 279     7157   5486   4962    379   -765   -446       C  
ATOM   1509  O   TYR B 279     -30.019  22.872 -40.635  1.00 43.65           O  
ANISOU 1509  O   TYR B 279     6780   5499   4305    393  -1105   -208       O  
ATOM   1510  CB  TYR B 279     -33.226  22.553 -40.904  1.00 44.50           C  
ANISOU 1510  CB  TYR B 279     7192   5841   3874   -125   -255   -469       C  
ATOM   1511  CG  TYR B 279     -34.490  21.821 -40.526  1.00 47.48           C  
ANISOU 1511  CG  TYR B 279     7669   6307   4065   -460    -10   -192       C  
ATOM   1512  CD1 TYR B 279     -34.933  21.800 -39.212  1.00 53.63           C  
ANISOU 1512  CD1 TYR B 279     8572   7681   4122   -813    -67    239       C  
ATOM   1513  CD2 TYR B 279     -35.243  21.156 -41.482  1.00 46.20           C  
ANISOU 1513  CD2 TYR B 279     7475   5645   4435   -450    297   -386       C  
ATOM   1514  CE1 TYR B 279     -36.088  21.135 -38.858  1.00 56.56           C  
ANISOU 1514  CE1 TYR B 279     9033   8156   4301  -1186    203    459       C  
ATOM   1515  CE2 TYR B 279     -36.402  20.484 -41.136  1.00 49.42           C  
ANISOU 1515  CE2 TYR B 279     7949   6147   4681   -796    549   -173       C  
ATOM   1516  CZ  TYR B 279     -36.819  20.477 -39.824  1.00 54.47           C  
ANISOU 1516  CZ  TYR B 279     8710   7391   4594  -1182    516    243       C  
ATOM   1517  OH  TYR B 279     -37.971  19.811 -39.476  1.00 58.77           O  
ANISOU 1517  OH  TYR B 279     9322   8050   4960  -1589    811    423       O  
ATOM   1518  N   VAL B 280     -30.739  22.906 -42.777  1.00 33.68           N  
ANISOU 1518  N   VAL B 280     4503   3418   4875   -631   -630    370       N  
ATOM   1519  CA  VAL B 280     -30.000  24.092 -43.196  1.00 32.15           C  
ANISOU 1519  CA  VAL B 280     4067   3403   4745   -433   -486    313       C  
ATOM   1520  C   VAL B 280     -30.992  25.242 -43.265  1.00 30.42           C  
ANISOU 1520  C   VAL B 280     3755   3492   4310   -567   -383    278       C  
ATOM   1521  O   VAL B 280     -32.043  25.129 -43.910  1.00 29.82           O  
ANISOU 1521  O   VAL B 280     3736   3505   4087   -662   -341    183       O  
ATOM   1522  CB  VAL B 280     -29.306  23.867 -44.551  1.00 34.49           C  
ANISOU 1522  CB  VAL B 280     4351   3594   5159   -173   -317    153       C  
ATOM   1523  CG1 VAL B 280     -28.678  25.159 -45.063  1.00 33.99           C  
ANISOU 1523  CG1 VAL B 280     4054   3728   5132    -47   -107    130       C  
ATOM   1524  CG2 VAL B 280     -28.247  22.794 -44.420  1.00 37.26           C  
ANISOU 1524  CG2 VAL B 280     4747   3643   5769     41   -408    166       C  
ATOM   1525  N   PHE B 281     -30.679  26.345 -42.593  1.00 30.10           N  
ANISOU 1525  N   PHE B 281     3574   3600   4263   -561   -377    338       N  
ATOM   1526  CA  PHE B 281     -31.620  27.449 -42.467  1.00 26.50           C  
ANISOU 1526  CA  PHE B 281     3060   3394   3614   -641   -301    303       C  
ATOM   1527  C   PHE B 281     -31.271  28.574 -43.429  1.00 25.46           C  
ANISOU 1527  C   PHE B 281     2839   3324   3509   -481   -146    232       C  
ATOM   1528  O   PHE B 281     -30.125  29.031 -43.480  1.00 25.05           O  
ANISOU 1528  O   PHE B 281     2692   3191   3634   -390   -105    263       O  
ATOM   1529  CB  PHE B 281     -31.650  27.963 -41.031  1.00 26.76           C  
ANISOU 1529  CB  PHE B 281     3091   3516   3560   -745   -399    391       C  
ATOM   1530  CG  PHE B 281     -32.077  26.936 -40.039  1.00 29.56           C  
ANISOU 1530  CG  PHE B 281     3594   3827   3811   -930   -514    508       C  
ATOM   1531  CD1 PHE B 281     -33.408  26.597 -39.910  1.00 31.97           C  
ANISOU 1531  CD1 PHE B 281     3927   4278   3941  -1123   -435    506       C  
ATOM   1532  CD2 PHE B 281     -31.145  26.303 -39.232  1.00 31.57           C  
ANISOU 1532  CD2 PHE B 281     3952   3893   4150   -918   -708    641       C  
ATOM   1533  CE1 PHE B 281     -33.804  25.647 -38.986  1.00 34.48           C  
ANISOU 1533  CE1 PHE B 281     4407   4542   4153  -1350   -494    655       C  
ATOM   1534  CE2 PHE B 281     -31.539  25.361 -38.321  1.00 36.13           C  
ANISOU 1534  CE2 PHE B 281     4744   4393   4590  -1096   -813    795       C  
ATOM   1535  CZ  PHE B 281     -32.869  25.033 -38.197  1.00 35.65           C  
ANISOU 1535  CZ  PHE B 281     4743   4465   4338  -1335   -678    813       C  
ATOM   1536  N   ILE B 282     -32.269  29.011 -44.193  1.00 26.74           N  
ANISOU 1536  N   ILE B 282     3027   3628   3505   -461    -71    152       N  
ATOM   1537  CA  ILE B 282     -32.147  30.114 -45.136  1.00 27.07           C  
ANISOU 1537  CA  ILE B 282     3072   3712   3501   -313     64    122       C  
ATOM   1538  C   ILE B 282     -33.237  31.116 -44.797  1.00 25.55           C  
ANISOU 1538  C   ILE B 282     2854   3701   3154   -311     34     96       C  
ATOM   1539  O   ILE B 282     -34.394  30.733 -44.601  1.00 27.01           O  
ANISOU 1539  O   ILE B 282     2995   4041   3225   -383    -38     45       O  
ATOM   1540  CB  ILE B 282     -32.288  29.639 -46.597  1.00 28.78           C  
ANISOU 1540  CB  ILE B 282     3413   3903   3620   -205    144     41       C  
ATOM   1541  CG1 ILE B 282     -31.227  28.585 -46.919  1.00 30.86           C  
ANISOU 1541  CG1 ILE B 282     3709   3976   4039   -150    207     24       C  
ATOM   1542  CG2 ILE B 282     -32.220  30.825 -47.564  1.00 27.95           C  
ANISOU 1542  CG2 ILE B 282     3385   3836   3397    -59    286     60       C  
ATOM   1543  CD1 ILE B 282     -29.801  29.099 -46.823  1.00 31.59           C  
ANISOU 1543  CD1 ILE B 282     3662   3984   4356    -67    358    104       C  
ATOM   1544  N   ALA B 283     -32.868  32.384 -44.686  1.00 23.33           N  
ANISOU 1544  N   ALA B 283     2582   3386   2894   -232     90    125       N  
ATOM   1545  CA  ALA B 283     -33.827  33.411 -44.323  1.00 24.37           C  
ANISOU 1545  CA  ALA B 283     2717   3641   2901   -160     64     78       C  
ATOM   1546  C   ALA B 283     -34.135  34.276 -45.530  1.00 23.11           C  
ANISOU 1546  C   ALA B 283     2670   3463   2648     30    118     82       C  
ATOM   1547  O   ALA B 283     -33.260  34.564 -46.347  1.00 24.18           O  
ANISOU 1547  O   ALA B 283     2914   3445   2829     66    230    159       O  
ATOM   1548  CB  ALA B 283     -33.314  34.290 -43.178  1.00 25.76           C  
ANISOU 1548  CB  ALA B 283     2911   3739   3140   -198     37     83       C  
ATOM   1549  N   ALA B 284     -35.389  34.685 -45.626  1.00 23.32           N  
ANISOU 1549  N   ALA B 284     2663   3658   2540    158     43     13       N  
ATOM   1550  CA  ALA B 284     -35.810  35.675 -46.599  1.00 25.49           C  
ANISOU 1550  CA  ALA B 284     3081   3903   2702    392     27     33       C  
ATOM   1551  C   ALA B 284     -36.076  36.981 -45.869  1.00 25.83           C  
ANISOU 1551  C   ALA B 284     3167   3882   2766    531     18      7       C  
ATOM   1552  O   ALA B 284     -36.573  36.976 -44.742  1.00 27.43           O  
ANISOU 1552  O   ALA B 284     3226   4213   2983    503      1    -91       O  
ATOM   1553  CB  ALA B 284     -37.065  35.219 -47.334  1.00 26.39           C  
ANISOU 1553  CB  ALA B 284     3108   4248   2672    499   -122    -45       C  
ATOM   1554  N   SER B 285     -35.710  38.091 -46.491  1.00 27.36           N  
ANISOU 1554  N   SER B 285     3602   3849   2944    672     50     96       N  
ATOM   1555  CA  SER B 285     -35.991  39.409 -45.944  1.00 29.00           C  
ANISOU 1555  CA  SER B 285     3935   3911   3172    845     17     57       C  
ATOM   1556  C   SER B 285     -36.624  40.265 -47.030  1.00 29.14           C  
ANISOU 1556  C   SER B 285     4168   3845   3060   1154    -64    130       C  
ATOM   1557  O   SER B 285     -36.300  40.133 -48.212  1.00 30.49           O  
ANISOU 1557  O   SER B 285     4512   3948   3124   1160    -36    273       O  
ATOM   1558  CB  SER B 285     -34.724  40.081 -45.400  1.00 29.71           C  
ANISOU 1558  CB  SER B 285     4179   3684   3425    660     99    113       C  
ATOM   1559  OG  SER B 285     -34.227  39.383 -44.262  1.00 29.09           O  
ANISOU 1559  OG  SER B 285     3921   3691   3442    428     93     36       O  
ATOM   1560  N   PHE B 286     -37.546  41.133 -46.620  1.00 31.45           N  
ANISOU 1560  N   PHE B 286     4470   4143   3335   1445   -166     26       N  
ATOM   1561  CA  PHE B 286     -38.189  42.055 -47.544  1.00 34.62           C  
ANISOU 1561  CA  PHE B 286     5103   4424   3628   1809   -303    103       C  
ATOM   1562  C   PHE B 286     -38.627  43.293 -46.776  1.00 38.01           C  
ANISOU 1562  C   PHE B 286     5653   4659   4131   2091   -349    -11       C  
ATOM   1563  O   PHE B 286     -38.733  43.284 -45.548  1.00 32.82           O  
ANISOU 1563  O   PHE B 286     4832   4084   3554   2040   -281   -198       O  
ATOM   1564  CB  PHE B 286     -39.375  41.403 -48.261  1.00 36.18           C  
ANISOU 1564  CB  PHE B 286     5065   4988   3696   2007   -494     52       C  
ATOM   1565  CG  PHE B 286     -40.435  40.865 -47.336  1.00 38.15           C  
ANISOU 1565  CG  PHE B 286     4840   5628   4026   2049   -532   -171       C  
ATOM   1566  CD1 PHE B 286     -41.431  41.693 -46.843  1.00 42.40           C  
ANISOU 1566  CD1 PHE B 286     5248   6246   4614   2425   -606   -311       C  
ATOM   1567  CD2 PHE B 286     -40.445  39.526 -46.975  1.00 37.64           C  
ANISOU 1567  CD2 PHE B 286     4468   5841   3992   1720   -468   -235       C  
ATOM   1568  CE1 PHE B 286     -42.407  41.204 -45.988  1.00 43.89           C  
ANISOU 1568  CE1 PHE B 286     4958   6839   4876   2449   -563   -509       C  
ATOM   1569  CE2 PHE B 286     -41.424  39.029 -46.121  1.00 38.17           C  
ANISOU 1569  CE2 PHE B 286     4108   6268   4127   1701   -450   -402       C  
ATOM   1570  CZ  PHE B 286     -42.405  39.870 -45.632  1.00 41.69           C  
ANISOU 1570  CZ  PHE B 286     4378   6847   4616   2055   -473   -538       C  
ATOM   1571  N   GLN B 287     -38.883  44.362 -47.519  1.00 41.15           N  
ANISOU 1571  N   GLN B 287     6392   4774   4469   2410   -467    103       N  
ATOM   1572  CA  GLN B 287     -39.213  45.656 -46.946  1.00 46.82           C  
ANISOU 1572  CA  GLN B 287     7339   5186   5264   2728   -526      5       C  
ATOM   1573  C   GLN B 287     -40.672  45.968 -47.226  1.00 50.58           C  
ANISOU 1573  C   GLN B 287     7652   5877   5687   3274   -741   -100       C  
ATOM   1574  O   GLN B 287     -41.109  45.930 -48.381  1.00 53.87           O  
ANISOU 1574  O   GLN B 287     8129   6364   5977   3416   -913     51       O  
ATOM   1575  CB  GLN B 287     -38.313  46.749 -47.527  1.00 51.91           C  
ANISOU 1575  CB  GLN B 287     8558   5239   5925   2674   -508    241       C  
ATOM   1576  CG  GLN B 287     -38.369  48.074 -46.797  1.00 57.01           C  
ANISOU 1576  CG  GLN B 287     9532   5437   6691   2894   -557    120       C  
ATOM   1577  CD  GLN B 287     -37.562  49.146 -47.501  1.00 61.55           C  
ANISOU 1577  CD  GLN B 287    10626   5463   7296   2722   -537    383       C  
ATOM   1578  OE1 GLN B 287     -37.724  49.374 -48.698  1.00 63.52           O  
ANISOU 1578  OE1 GLN B 287    11050   5679   7404   2792   -589    619       O  
ATOM   1579  NE2 GLN B 287     -36.673  49.799 -46.762  1.00 63.49           N  
ANISOU 1579  NE2 GLN B 287    11098   5305   7721   2441   -462    333       N  
ATOM   1580  N   ALA B 288     -41.424  46.246 -46.172  1.00 51.52           N  
ANISOU 1580  N   ALA B 288     7526   6155   5896   3486   -709   -372       N  
ATOM   1581  CA  ALA B 288     -42.755  46.821 -46.281  1.00 57.08           C  
ANISOU 1581  CA  ALA B 288     8039   7032   6616   3845   -844   -487       C  
ATOM   1582  C   ALA B 288     -42.699  48.273 -45.819  1.00 62.74           C  
ANISOU 1582  C   ALA B 288     9146   7293   7399   4055   -842   -554       C  
ATOM   1583  O   ALA B 288     -41.662  48.762 -45.364  1.00 62.35           O  
ANISOU 1583  O   ALA B 288     9480   6823   7386   3864   -745   -534       O  
ATOM   1584  CB  ALA B 288     -43.764  46.009 -45.465  1.00 56.97           C  
ANISOU 1584  CB  ALA B 288     7400   7590   6654   3857   -751   -728       C  
ATOM   1585  N   SER B 289     -43.821  48.981 -45.960  1.00 70.18           N  
ANISOU 1585  N   SER B 289     9992   8298   8377   4439   -970   -640       N  
ATOM   1586  CA  SER B 289     -43.916  50.292 -45.327  1.00 76.63           C  
ANISOU 1586  CA  SER B 289    11113   8733   9271   4676   -953   -767       C  
ATOM   1587  C   SER B 289     -43.758  50.169 -43.818  1.00 77.93           C  
ANISOU 1587  C   SER B 289    11152   8989   9469   4575   -716  -1048       C  
ATOM   1588  O   SER B 289     -43.267  51.094 -43.161  1.00 81.61           O  
ANISOU 1588  O   SER B 289    12005   9035   9967   4584   -670  -1150       O  
ATOM   1589  CB  SER B 289     -45.246  50.955 -45.684  1.00 83.07           C  
ANISOU 1589  CB  SER B 289    11766   9656  10139   5155  -1122   -833       C  
ATOM   1590  OG  SER B 289     -46.305  50.016 -45.641  1.00 83.00           O  
ANISOU 1590  OG  SER B 289    11113  10262  10162   5224  -1120   -947       O  
ATOM   1591  N   ASP B 290     -44.166  49.025 -43.266  1.00 78.22           N  
ANISOU 1591  N   ASP B 290    10674   9566   9480   4444   -568  -1172       N  
ATOM   1592  CA  ASP B 290     -43.933  48.700 -41.863  1.00 79.39           C  
ANISOU 1592  CA  ASP B 290    10721   9857   9587   4273   -318  -1403       C  
ATOM   1593  C   ASP B 290     -42.453  48.783 -41.503  1.00 75.62           C  
ANISOU 1593  C   ASP B 290    10695   8961   9074   3934   -286  -1366       C  
ATOM   1594  O   ASP B 290     -42.086  49.320 -40.452  1.00 77.82           O  
ANISOU 1594  O   ASP B 290    11218   9028   9320   3887   -196  -1563       O  
ATOM   1595  CB  ASP B 290     -44.471  47.290 -41.599  1.00 79.75           C  
ANISOU 1595  CB  ASP B 290    10173  10532   9597   4076   -175  -1439       C  
ATOM   1596  CG  ASP B 290     -44.628  46.974 -40.130  1.00 82.70           C  
ANISOU 1596  CG  ASP B 290    10382  11154   9884   3953    113  -1670       C  
ATOM   1597  OD1 ASP B 290     -43.755  47.358 -39.325  1.00 83.91           O  
ANISOU 1597  OD1 ASP B 290    10923  11008   9950   3827    186  -1772       O  
ATOM   1598  OD2 ASP B 290     -45.631  46.317 -39.783  1.00 85.16           O  
ANISOU 1598  OD2 ASP B 290    10192  11958  10207   3947    263  -1740       O  
ATOM   1599  N   GLY B 291     -41.596  48.262 -42.361  1.00 67.07           N  
ANISOU 1599  N   GLY B 291     9731   7751   8002   3685   -365  -1125       N  
ATOM   1600  CA  GLY B 291     -40.197  48.046 -42.077  1.00 61.60           C  
ANISOU 1600  CA  GLY B 291     9341   6747   7320   3303   -322  -1075       C  
ATOM   1601  C   GLY B 291     -39.774  46.735 -42.693  1.00 52.51           C  
ANISOU 1601  C   GLY B 291     7891   5911   6148   2921   -288   -856       C  
ATOM   1602  O   GLY B 291     -40.499  46.148 -43.492  1.00 49.37           O  
ANISOU 1602  O   GLY B 291     7197   5843   5718   3058   -343   -761       O  
ATOM   1603  N   ILE B 292     -38.595  46.255 -42.305  1.00 46.03           N  
ANISOU 1603  N   ILE B 292     7131   5002   5357   2417   -223   -786       N  
ATOM   1604  CA  ILE B 292     -38.034  45.035 -42.870  1.00 43.77           C  
ANISOU 1604  CA  ILE B 292     6600   4953   5076   2034   -181   -580       C  
ATOM   1605  C   ILE B 292     -38.556  43.831 -42.100  1.00 42.41           C  
ANISOU 1605  C   ILE B 292     5997   5296   4819   1911    -86   -705       C  
ATOM   1606  O   ILE B 292     -38.497  43.795 -40.863  1.00 39.39           O  
ANISOU 1606  O   ILE B 292     5606   4986   4376   1829    -13   -885       O  
ATOM   1607  CB  ILE B 292     -36.499  45.078 -42.855  1.00 41.13           C  
ANISOU 1607  CB  ILE B 292     6477   4287   4864   1588   -161   -437       C  
ATOM   1608  CG1 ILE B 292     -36.008  46.171 -43.801  1.00 46.47           C  
ANISOU 1608  CG1 ILE B 292     7565   4466   5626   1637   -203   -243       C  
ATOM   1609  CG2 ILE B 292     -35.924  43.732 -43.251  1.00 35.19           C  
ANISOU 1609  CG2 ILE B 292     5440   3804   4127   1250    -92   -284       C  
ATOM   1610  CD1 ILE B 292     -34.550  46.425 -43.702  1.00 46.92           C  
ANISOU 1610  CD1 ILE B 292     7786   4178   5862   1192   -165   -126       C  
ATOM   1611  N   HIS B 293     -39.061  42.841 -42.829  1.00 38.38           N  
ANISOU 1611  N   HIS B 293     5177   5123   4282   1876    -93   -604       N  
ATOM   1612  CA  HIS B 293     -39.537  41.602 -42.239  1.00 38.91           C  
ANISOU 1612  CA  HIS B 293     4856   5634   4296   1686     -3   -670       C  
ATOM   1613  C   HIS B 293     -38.678  40.445 -42.728  1.00 35.64           C  
ANISOU 1613  C   HIS B 293     4389   5235   3915   1295     -8   -490       C  
ATOM   1614  O   HIS B 293     -38.100  40.493 -43.820  1.00 31.75           O  
ANISOU 1614  O   HIS B 293     4052   4551   3461   1261    -64   -328       O  
ATOM   1615  CB  HIS B 293     -41.010  41.342 -42.588  1.00 41.71           C  
ANISOU 1615  CB  HIS B 293     4830   6387   4630   1960    -29   -753       C  
ATOM   1616  CG  HIS B 293     -41.952  42.369 -42.043  1.00 45.56           C  
ANISOU 1616  CG  HIS B 293     5275   6926   5111   2409     10   -963       C  
ATOM   1617  ND1 HIS B 293     -42.955  42.059 -41.149  1.00 47.59           N  
ANISOU 1617  ND1 HIS B 293     5149   7603   5328   2499    184  -1152       N  
ATOM   1618  CD2 HIS B 293     -42.046  43.702 -42.265  1.00 48.47           C  
ANISOU 1618  CD2 HIS B 293     5945   6963   5510   2814    -81  -1018       C  
ATOM   1619  CE1 HIS B 293     -43.627  43.156 -40.846  1.00 51.72           C  
ANISOU 1619  CE1 HIS B 293     5730   8051   5869   2910    199  -1312       C  
ATOM   1620  NE2 HIS B 293     -43.094  44.167 -41.507  1.00 52.10           N  
ANISOU 1620  NE2 HIS B 293     6201   7634   5961   3141     22  -1250       N  
ATOM   1621  N   SER B 294     -38.598  39.397 -41.916  1.00 34.14           N  
ANISOU 1621  N   SER B 294     4012   5265   3695   1020     68   -514       N  
ATOM   1622  CA  SER B 294     -37.862  38.206 -42.302  1.00 32.81           C  
ANISOU 1622  CA  SER B 294     3790   5100   3575    702     53   -370       C  
ATOM   1623  C   SER B 294     -38.731  36.971 -42.119  1.00 34.09           C  
ANISOU 1623  C   SER B 294     3643   5616   3692    560     84   -391       C  
ATOM   1624  O   SER B 294     -39.659  36.946 -41.306  1.00 36.53           O  
ANISOU 1624  O   SER B 294     3761   6190   3929    603    175   -501       O  
ATOM   1625  CB  SER B 294     -36.561  38.045 -41.492  1.00 32.42           C  
ANISOU 1625  CB  SER B 294     3891   4847   3580    442     58   -324       C  
ATOM   1626  OG  SER B 294     -35.560  38.941 -41.939  1.00 33.38           O  
ANISOU 1626  OG  SER B 294     4242   4624   3819    452     24   -258       O  
ATOM   1627  N   ILE B 295     -38.400  35.941 -42.891  1.00 31.81           N  
ANISOU 1627  N   ILE B 295     3320   5317   3450    378     29   -289       N  
ATOM   1628  CA  ILE B 295     -38.995  34.618 -42.777  1.00 31.49           C  
ANISOU 1628  CA  ILE B 295     3057   5504   3405    148     28   -285       C  
ATOM   1629  C   ILE B 295     -37.854  33.614 -42.744  1.00 29.54           C  
ANISOU 1629  C   ILE B 295     2949   5054   3219   -107     14   -172       C  
ATOM   1630  O   ILE B 295     -36.911  33.723 -43.533  1.00 30.19           O  
ANISOU 1630  O   ILE B 295     3194   4913   3364    -63    -13   -111       O  
ATOM   1631  CB  ILE B 295     -39.948  34.318 -43.957  1.00 32.29           C  
ANISOU 1631  CB  ILE B 295     2986   5775   3509    236    -99   -325       C  
ATOM   1632  CG1 ILE B 295     -41.060  35.369 -44.039  1.00 34.34           C  
ANISOU 1632  CG1 ILE B 295     3067   6233   3747    569   -132   -434       C  
ATOM   1633  CG2 ILE B 295     -40.542  32.925 -43.829  1.00 34.67           C  
ANISOU 1633  CG2 ILE B 295     3069   6261   3845    -74   -121   -331       C  
ATOM   1634  CD1 ILE B 295     -41.924  35.249 -45.297  1.00 38.34           C  
ANISOU 1634  CD1 ILE B 295     3425   6892   4249    714   -352   -471       C  
ATOM   1635  N   ARG B 296     -37.922  32.647 -41.833  1.00 29.95           N  
ANISOU 1635  N   ARG B 296     2946   5180   3255   -357     48   -132       N  
ATOM   1636  CA  ARG B 296     -36.910  31.600 -41.759  1.00 27.62           C  
ANISOU 1636  CA  ARG B 296     2784   4675   3038   -552     -4    -23       C  
ATOM   1637  C   ARG B 296     -37.410  30.335 -42.447  1.00 27.64           C  
ANISOU 1637  C   ARG B 296     2722   4700   3081   -716    -64    -17       C  
ATOM   1638  O   ARG B 296     -38.523  29.868 -42.175  1.00 30.20           O  
ANISOU 1638  O   ARG B 296     2870   5238   3365   -872    -44    -43       O  
ATOM   1639  CB  ARG B 296     -36.528  31.290 -40.309  1.00 28.05           C  
ANISOU 1639  CB  ARG B 296     2924   4711   3023   -715     12     52       C  
ATOM   1640  CG  ARG B 296     -35.359  30.310 -40.212  1.00 27.36           C  
ANISOU 1640  CG  ARG B 296     2978   4368   3049   -835    -99    175       C  
ATOM   1641  CD  ARG B 296     -34.986  29.995 -38.763  1.00 28.13           C  
ANISOU 1641  CD  ARG B 296     3213   4442   3033   -975   -152    276       C  
ATOM   1642  NE  ARG B 296     -34.562  31.183 -38.030  1.00 28.71           N  
ANISOU 1642  NE  ARG B 296     3360   4527   3023   -864   -173    212       N  
ATOM   1643  CZ  ARG B 296     -34.564  31.281 -36.703  1.00 29.59           C  
ANISOU 1643  CZ  ARG B 296     3623   4704   2916   -943   -199    236       C  
ATOM   1644  NH1 ARG B 296     -34.993  30.270 -35.957  1.00 30.79           N  
ANISOU 1644  NH1 ARG B 296     3868   4930   2901  -1142   -170    366       N  
ATOM   1645  NH2 ARG B 296     -34.162  32.402 -36.123  1.00 29.37           N  
ANISOU 1645  NH2 ARG B 296     3699   4650   2809   -839   -254    130       N  
ATOM   1646  N   TYR B 297     -36.584  29.786 -43.330  1.00 24.97           N  
ANISOU 1646  N   TYR B 297     2521   4138   2829   -693   -124      1       N  
ATOM   1647  CA  TYR B 297     -36.859  28.525 -43.996  1.00 27.43           C  
ANISOU 1647  CA  TYR B 297     2869   4377   3177   -840   -209    -27       C  
ATOM   1648  C   TYR B 297     -35.812  27.502 -43.589  1.00 27.79           C  
ANISOU 1648  C   TYR B 297     3085   4141   3331   -940   -238     66       C  
ATOM   1649  O   TYR B 297     -34.694  27.855 -43.214  1.00 27.18           O  
ANISOU 1649  O   TYR B 297     3066   3933   3328   -829   -212    134       O  
ATOM   1650  CB  TYR B 297     -36.854  28.695 -45.518  1.00 26.56           C  
ANISOU 1650  CB  TYR B 297     2835   4233   3023   -662   -258   -130       C  
ATOM   1651  CG  TYR B 297     -37.962  29.596 -45.993  1.00 28.37           C  
ANISOU 1651  CG  TYR B 297     2912   4722   3144   -530   -310   -209       C  
ATOM   1652  CD1 TYR B 297     -39.265  29.125 -46.105  1.00 30.12           C  
ANISOU 1652  CD1 TYR B 297     2925   5166   3356   -675   -435   -295       C  
ATOM   1653  CD2 TYR B 297     -37.719  30.932 -46.279  1.00 28.68           C  
ANISOU 1653  CD2 TYR B 297     2999   4774   3124   -264   -253   -190       C  
ATOM   1654  CE1 TYR B 297     -40.294  29.959 -46.520  1.00 32.28           C  
ANISOU 1654  CE1 TYR B 297     2997   5702   3568   -501   -525   -373       C  
ATOM   1655  CE2 TYR B 297     -38.738  31.772 -46.701  1.00 30.82           C  
ANISOU 1655  CE2 TYR B 297     3154   5249   3307    -78   -339   -251       C  
ATOM   1656  CZ  TYR B 297     -40.023  31.279 -46.821  1.00 30.90           C  
ANISOU 1656  CZ  TYR B 297     2913   5513   3316   -171   -486   -349       C  
ATOM   1657  OH  TYR B 297     -41.040  32.108 -47.234  1.00 32.88           O  
ANISOU 1657  OH  TYR B 297     2991   5988   3516     63   -613   -416       O  
ATOM   1658  N   GLY B 298     -36.189  26.235 -43.667  1.00 31.88           N  
ANISOU 1658  N   GLY B 298     3675   4551   3886  -1149   -320     67       N  
ATOM   1659  CA  GLY B 298     -35.270  25.152 -43.391  1.00 31.86           C  
ANISOU 1659  CA  GLY B 298     3877   4226   4003  -1195   -385    149       C  
ATOM   1660  C   GLY B 298     -35.412  24.064 -44.432  1.00 31.02           C  
ANISOU 1660  C   GLY B 298     3929   3910   3947  -1240   -475     29       C  
ATOM   1661  O   GLY B 298     -36.503  23.792 -44.935  1.00 34.56           O  
ANISOU 1661  O   GLY B 298     4325   4470   4337  -1411   -543    -74       O  
ATOM   1662  N   ILE B 299     -34.284  23.443 -44.753  1.00 30.34           N  
ANISOU 1662  N   ILE B 299     4027   3519   3983  -1070   -491     18       N  
ATOM   1663  CA  ILE B 299     -34.222  22.376 -45.743  1.00 34.65           C  
ANISOU 1663  CA  ILE B 299     4803   3796   4566  -1045   -565   -138       C  
ATOM   1664  C   ILE B 299     -33.584  21.170 -45.076  1.00 36.87           C  
ANISOU 1664  C   ILE B 299     5301   3692   5016  -1086   -668    -32       C  
ATOM   1665  O   ILE B 299     -32.462  21.264 -44.562  1.00 35.02           O  
ANISOU 1665  O   ILE B 299     5045   3351   4910   -876   -646     75       O  
ATOM   1666  CB  ILE B 299     -33.432  22.798 -46.990  1.00 35.53           C  
ANISOU 1666  CB  ILE B 299     4967   3894   4639   -704   -433   -294       C  
ATOM   1667  CG1 ILE B 299     -34.072  24.031 -47.637  1.00 35.84           C  
ANISOU 1667  CG1 ILE B 299     4863   4273   4481   -649   -364   -349       C  
ATOM   1668  CG2 ILE B 299     -33.361  21.646 -47.989  1.00 37.42           C  
ANISOU 1668  CG2 ILE B 299     5511   3841   4867   -646   -499   -501       C  
ATOM   1669  CD1 ILE B 299     -33.489  25.356 -47.188  1.00 34.59           C  
ANISOU 1669  CD1 ILE B 299     4509   4288   4346   -508   -212   -218       C  
ATOM   1670  N   ASN B 300     -34.298  20.046 -45.068  1.00 42.56           N  
ANISOU 1670  N   ASN B 300     6656   3913   5600   -715   -906    198       N  
ATOM   1671  CA  ASN B 300     -33.799  18.838 -44.432  1.00 46.72           C  
ANISOU 1671  CA  ASN B 300     7602   3998   6150   -622  -1105    345       C  
ATOM   1672  C   ASN B 300     -32.914  18.059 -45.408  1.00 49.05           C  
ANISOU 1672  C   ASN B 300     7899   4050   6686   -278  -1215    167       C  
ATOM   1673  O   ASN B 300     -32.737  18.441 -46.567  1.00 47.03           O  
ANISOU 1673  O   ASN B 300     7319   4008   6542   -167  -1109    -68       O  
ATOM   1674  CB  ASN B 300     -34.958  17.987 -43.907  1.00 49.29           C  
ANISOU 1674  CB  ASN B 300     8320   4083   6323  -1047  -1014    476       C  
ATOM   1675  CG  ASN B 300     -35.867  17.460 -45.013  1.00 49.33           C  
ANISOU 1675  CG  ASN B 300     8290   4050   6403  -1290   -838    252       C  
ATOM   1676  OD1 ASN B 300     -35.602  17.641 -46.199  1.00 49.52           O  
ANISOU 1676  OD1 ASN B 300     8038   4202   6573  -1101   -805     12       O  
ATOM   1677  ND2 ASN B 300     -36.949  16.799 -44.617  1.00 50.91           N  
ANISOU 1677  ND2 ASN B 300     8765   4102   6476  -1743   -715    316       N  
ATOM   1678  N   LYS B 301     -32.359  16.939 -44.936  1.00 54.56           N  
ANISOU 1678  N   LYS B 301     8991   4293   7446    -90  -1430    278       N  
ATOM   1679  CA  LYS B 301     -31.435  16.167 -45.763  1.00 58.93           C  
ANISOU 1679  CA  LYS B 301     9547   4601   8241    311  -1559     76       C  
ATOM   1680  C   LYS B 301     -32.113  15.593 -47.002  1.00 59.89           C  
ANISOU 1680  C   LYS B 301     9678   4616   8459    145  -1379   -187       C  
ATOM   1681  O   LYS B 301     -31.447  15.348 -48.015  1.00 60.73           O  
ANISOU 1681  O   LYS B 301     9602   4732   8741    444  -1390   -462       O  
ATOM   1682  CB  LYS B 301     -30.800  15.052 -44.935  1.00 65.72           C  
ANISOU 1682  CB  LYS B 301    10893   4937   9140    585  -1854    267       C  
ATOM   1683  CG  LYS B 301     -29.371  15.343 -44.523  1.00 68.23           C  
ANISOU 1683  CG  LYS B 301    10997   5392   9534   1110  -2128    268       C  
ATOM   1684  CD  LYS B 301     -29.293  15.955 -43.144  1.00 69.63           C  
ANISOU 1684  CD  LYS B 301    11236   5748   9471   1038  -2258    566       C  
ATOM   1685  CE  LYS B 301     -27.851  16.044 -42.688  1.00 72.79           C  
ANISOU 1685  CE  LYS B 301    11452   6262   9944   1578  -2589    542       C  
ATOM   1686  NZ  LYS B 301     -27.764  16.659 -41.351  1.00 72.54           N  
ANISOU 1686  NZ  LYS B 301    11467   6449   9645   1500  -2733    794       N  
ATOM   1687  N   ASN B 302     -33.426  15.379 -46.948  1.00 59.91           N  
ANISOU 1687  N   ASN B 302     9860   4569   8335   -339  -1208   -145       N  
ATOM   1688  CA  ASN B 302     -34.183  14.929 -48.110  1.00 60.56           C  
ANISOU 1688  CA  ASN B 302     9897   4643   8472   -554  -1041   -432       C  
ATOM   1689  C   ASN B 302     -34.442  16.043 -49.116  1.00 55.03           C  
ANISOU 1689  C   ASN B 302     8661   4532   7714   -565   -867   -637       C  
ATOM   1690  O   ASN B 302     -35.148  15.814 -50.102  1.00 55.50           O  
ANISOU 1690  O   ASN B 302     8627   4699   7760   -746   -739   -882       O  
ATOM   1691  CB  ASN B 302     -35.516  14.318 -47.668  1.00 64.84           C  
ANISOU 1691  CB  ASN B 302    10769   4980   8888  -1112   -915   -345       C  
ATOM   1692  CG  ASN B 302     -35.336  13.039 -46.881  1.00 72.78           C  
ANISOU 1692  CG  ASN B 302    12414   5295   9945  -1150  -1058   -145       C  
ATOM   1693  OD1 ASN B 302     -34.398  12.278 -47.122  1.00 76.74           O  
ANISOU 1693  OD1 ASN B 302    13126   5390  10639   -745  -1241   -208       O  
ATOM   1694  ND2 ASN B 302     -36.237  12.790 -45.937  1.00 75.90           N  
ANISOU 1694  ND2 ASN B 302    13052   5639  10148  -1594   -944     96       N  
ATOM   1695  N   GLY B 303     -33.894  17.236 -48.894  1.00 51.05           N  
ANISOU 1695  N   GLY B 303     7832   4400   7164   -384   -869   -542       N  
ATOM   1696  CA  GLY B 303     -34.175  18.362 -49.758  1.00 47.04           C  
ANISOU 1696  CA  GLY B 303     6902   4392   6578   -404   -705   -665       C  
ATOM   1697  C   GLY B 303     -35.573  18.923 -49.636  1.00 44.56           C  
ANISOU 1697  C   GLY B 303     6502   4349   6079   -778   -556   -625       C  
ATOM   1698  O   GLY B 303     -35.993  19.696 -50.502  1.00 42.57           O  
ANISOU 1698  O   GLY B 303     5955   4474   5747   -781   -440   -743       O  
ATOM   1699  N   GLU B 304     -36.311  18.554 -48.594  1.00 44.37           N  
ANISOU 1699  N   GLU B 304     6725   4166   5966  -1080   -556   -465       N  
ATOM   1700  CA  GLU B 304     -37.666  19.048 -48.413  1.00 43.05           C  
ANISOU 1700  CA  GLU B 304     6424   4309   5625  -1434   -403   -473       C  
ATOM   1701  C   GLU B 304     -37.642  20.411 -47.731  1.00 38.09           C  
ANISOU 1701  C   GLU B 304     5578   4000   4896  -1359   -373   -323       C  
ATOM   1702  O   GLU B 304     -36.771  20.702 -46.909  1.00 36.88           O  
ANISOU 1702  O   GLU B 304     5508   3737   4767  -1192   -476   -152       O  
ATOM   1703  CB  GLU B 304     -38.487  18.042 -47.606  1.00 47.70           C  
ANISOU 1703  CB  GLU B 304     7360   4622   6142  -1854   -366   -394       C  
ATOM   1704  CG  GLU B 304     -38.369  16.621 -48.160  1.00 52.95           C  
ANISOU 1704  CG  GLU B 304     8343   4829   6946  -1925   -414   -532       C  
ATOM   1705  CD  GLU B 304     -39.188  15.603 -47.392  1.00 59.40           C  
ANISOU 1705  CD  GLU B 304     9566   5309   7693  -2411   -346   -437       C  
ATOM   1706  OE1 GLU B 304     -39.659  14.632 -48.020  1.00 64.23           O  
ANISOU 1706  OE1 GLU B 304    10337   5686   8380  -2655   -296   -646       O  
ATOM   1707  OE2 GLU B 304     -39.351  15.763 -46.164  1.00 61.60           O  
ANISOU 1707  OE2 GLU B 304    10022   5555   7827  -2577   -331   -162       O  
ATOM   1708  N   LEU B 305     -38.607  21.250 -48.090  1.00 36.35           N  
ANISOU 1708  N   LEU B 305     5072   4178   4560  -1463   -246   -416       N  
ATOM   1709  CA  LEU B 305     -38.633  22.648 -47.682  1.00 35.50           C  
ANISOU 1709  CA  LEU B 305     4747   4358   4383  -1343   -206   -333       C  
ATOM   1710  C   LEU B 305     -39.655  22.862 -46.573  1.00 35.22           C  
ANISOU 1710  C   LEU B 305     4725   4472   4186  -1631   -119   -278       C  
ATOM   1711  O   LEU B 305     -40.725  22.245 -46.571  1.00 36.96           O  
ANISOU 1711  O   LEU B 305     4950   4776   4317  -1947    -29   -378       O  
ATOM   1712  CB  LEU B 305     -38.957  23.541 -48.884  1.00 36.63           C  
ANISOU 1712  CB  LEU B 305     4585   4833   4501  -1172   -143   -466       C  
ATOM   1713  CG  LEU B 305     -39.044  25.052 -48.680  1.00 36.91           C  
ANISOU 1713  CG  LEU B 305     4432   5107   4486  -1012    -96   -398       C  
ATOM   1714  CD1 LEU B 305     -37.757  25.605 -48.084  1.00 35.76           C  
ANISOU 1714  CD1 LEU B 305     4359   4784   4444   -846   -153   -255       C  
ATOM   1715  CD2 LEU B 305     -39.361  25.727 -50.016  1.00 37.99           C  
ANISOU 1715  CD2 LEU B 305     4359   5503   4571   -823    -59   -491       C  
ATOM   1716  N   PHE B 306     -39.316  23.739 -45.629  1.00 35.00           N  
ANISOU 1716  N   PHE B 306     4683   4505   4110  -1547   -131   -154       N  
ATOM   1717  CA  PHE B 306     -40.158  24.031 -44.478  1.00 34.86           C  
ANISOU 1717  CA  PHE B 306     4671   4663   3912  -1790    -36   -120       C  
ATOM   1718  C   PHE B 306     -40.063  25.516 -44.165  1.00 31.86           C  
ANISOU 1718  C   PHE B 306     4083   4510   3513  -1582    -10   -138       C  
ATOM   1719  O   PHE B 306     -38.993  26.111 -44.299  1.00 32.73           O  
ANISOU 1719  O   PHE B 306     4188   4507   3740  -1327    -99    -80       O  
ATOM   1720  CB  PHE B 306     -39.734  23.227 -43.230  1.00 36.00           C  
ANISOU 1720  CB  PHE B 306     5183   4534   3963  -1967   -103     83       C  
ATOM   1721  CG  PHE B 306     -39.778  21.735 -43.415  1.00 38.42           C  
ANISOU 1721  CG  PHE B 306     5799   4499   4299  -2172   -134    135       C  
ATOM   1722  CD1 PHE B 306     -40.880  21.005 -43.006  1.00 41.25           C  
ANISOU 1722  CD1 PHE B 306     6287   4881   4506  -2623     14    124       C  
ATOM   1723  CD2 PHE B 306     -38.708  21.061 -43.985  1.00 38.54           C  
ANISOU 1723  CD2 PHE B 306     5982   4160   4501  -1926   -299    172       C  
ATOM   1724  CE1 PHE B 306     -40.923  19.632 -43.180  1.00 45.05           C  
ANISOU 1724  CE1 PHE B 306     7112   4970   5032  -2850     -3    169       C  
ATOM   1725  CE2 PHE B 306     -38.746  19.692 -44.161  1.00 39.54           C  
ANISOU 1725  CE2 PHE B 306     6439   3904   4680  -2083   -335    197       C  
ATOM   1726  CZ  PHE B 306     -39.851  18.977 -43.759  1.00 43.82           C  
ANISOU 1726  CZ  PHE B 306     7164   4403   5081  -2557   -189    207       C  
ATOM   1727  N   SER B 307     -41.180  26.118 -43.775  1.00 30.94           N  
ANISOU 1727  N   SER B 307     3784   4712   3261  -1696    119   -250       N  
ATOM   1728  CA  SER B 307     -41.119  27.400 -43.089  1.00 33.46           C  
ANISOU 1728  CA  SER B 307     4001   5173   3541  -1546    147   -273       C  
ATOM   1729  C   SER B 307     -41.040  27.140 -41.590  1.00 32.99           C  
ANISOU 1729  C   SER B 307     4138   5093   3303  -1771    163   -182       C  
ATOM   1730  O   SER B 307     -41.564  26.141 -41.089  1.00 33.93           O  
ANISOU 1730  O   SER B 307     4408   5211   3274  -2095    224   -130       O  
ATOM   1731  CB  SER B 307     -42.330  28.277 -43.415  1.00 36.44           C  
ANISOU 1731  CB  SER B 307     4067   5916   3863  -1464    263   -474       C  
ATOM   1732  OG  SER B 307     -43.534  27.688 -42.959  1.00 37.91           O  
ANISOU 1732  OG  SER B 307     4152   6373   3877  -1782    393   -594       O  
ATOM   1733  N   ILE B 308     -40.377  28.045 -40.875  1.00 34.34           N  
ANISOU 1733  N   ILE B 308     4331   5248   3467  -1624    112   -165       N  
ATOM   1734  CA  ILE B 308     -40.063  27.834 -39.466  1.00 36.43           C  
ANISOU 1734  CA  ILE B 308     4810   5501   3532  -1789     79    -67       C  
ATOM   1735  C   ILE B 308     -40.539  29.030 -38.656  1.00 37.82           C  
ANISOU 1735  C   ILE B 308     4837   5948   3583  -1762    185   -240       C  
ATOM   1736  O   ILE B 308     -40.107  30.163 -38.899  1.00 38.04           O  
ANISOU 1736  O   ILE B 308     4744   5949   3760  -1511    154   -342       O  
ATOM   1737  CB  ILE B 308     -38.560  27.602 -39.254  1.00 37.42           C  
ANISOU 1737  CB  ILE B 308     5127   5342   3747  -1634   -143     93       C  
ATOM   1738  CG1 ILE B 308     -38.168  26.265 -39.876  1.00 41.12           C  
ANISOU 1738  CG1 ILE B 308     5783   5530   4310  -1654   -246    241       C  
ATOM   1739  CG2 ILE B 308     -38.218  27.617 -37.778  1.00 38.52           C  
ANISOU 1739  CG2 ILE B 308     5460   5538   3639  -1744   -215    172       C  
ATOM   1740  CD1 ILE B 308     -36.805  26.248 -40.423  1.00 42.34           C  
ANISOU 1740  CD1 ILE B 308     5933   5472   4683  -1371   -430    282       C  
ATOM   1741  N   ASN B 309     -41.430  28.779 -37.703  1.00 40.26           N  
ANISOU 1741  N   ASN B 309     5171   6508   3618  -2039    329   -288       N  
ATOM   1742  CA  ASN B 309     -41.768  29.778 -36.699  1.00 42.95           C  
ANISOU 1742  CA  ASN B 309     5418   7114   3789  -2030    426   -471       C  
ATOM   1743  C   ASN B 309     -40.596  29.915 -35.737  1.00 41.96           C  
ANISOU 1743  C   ASN B 309     5528   6850   3564  -2002    258   -360       C  
ATOM   1744  O   ASN B 309     -40.223  28.948 -35.067  1.00 44.05           O  
ANISOU 1744  O   ASN B 309     6075   7033   3628  -2194    173   -141       O  
ATOM   1745  CB  ASN B 309     -43.039  29.370 -35.958  1.00 47.13           C  
ANISOU 1745  CB  ASN B 309     5885   8010   4011  -2374    657   -569       C  
ATOM   1746  CG  ASN B 309     -43.516  30.429 -34.985  1.00 49.62           C  
ANISOU 1746  CG  ASN B 309     6051   8660   4143  -2339    791   -832       C  
ATOM   1747  OD1 ASN B 309     -42.838  30.740 -34.010  1.00 50.31           O  
ANISOU 1747  OD1 ASN B 309     6317   8725   4074  -2345    717   -806       O  
ATOM   1748  ND2 ASN B 309     -44.696  30.979 -35.241  1.00 52.17           N  
ANISOU 1748  ND2 ASN B 309     6027   9322   4472  -2284    977  -1120       N  
ATOM   1749  N   THR B 310     -40.005  31.107 -35.677  1.00 39.97           N  
ANISOU 1749  N   THR B 310     5178   6562   3449  -1763    196   -513       N  
ATOM   1750  CA  THR B 310     -38.775  31.299 -34.922  1.00 39.85           C  
ANISOU 1750  CA  THR B 310     5320   6438   3383  -1720      2   -458       C  
ATOM   1751  C   THR B 310     -39.004  31.478 -33.426  1.00 43.27           C  
ANISOU 1751  C   THR B 310     5860   7146   3435  -1899     42   -547       C  
ATOM   1752  O   THR B 310     -38.031  31.471 -32.663  1.00 44.68           O  
ANISOU 1752  O   THR B 310     6186   7299   3489  -1892   -149   -492       O  
ATOM   1753  CB  THR B 310     -38.005  32.501 -35.475  1.00 37.91           C  
ANISOU 1753  CB  THR B 310     4934   6030   3442  -1467    -61   -610       C  
ATOM   1754  OG1 THR B 310     -38.743  33.700 -35.216  1.00 39.23           O  
ANISOU 1754  OG1 THR B 310     4960   6343   3604  -1397    100   -894       O  
ATOM   1755  CG2 THR B 310     -37.800  32.352 -36.972  1.00 32.76           C  
ANISOU 1755  CG2 THR B 310     4190   5152   3106  -1306    -73   -513       C  
ATOM   1756  N   ALA B 311     -40.253  31.635 -32.984  1.00 45.73           N  
ANISOU 1756  N   ALA B 311     6074   7768   3534  -2055    283   -706       N  
ATOM   1757  CA  ALA B 311     -40.519  31.724 -31.553  1.00 49.55           C  
ANISOU 1757  CA  ALA B 311     6668   8567   3593  -2261    357   -796       C  
ATOM   1758  C   ALA B 311     -40.679  30.351 -30.915  1.00 54.50           C  
ANISOU 1758  C   ALA B 311     7599   9250   3860  -2591    361   -481       C  
ATOM   1759  O   ALA B 311     -40.303  30.163 -29.751  1.00 58.53           O  
ANISOU 1759  O   ALA B 311     8327   9866   4045  -2701    281   -393       O  
ATOM   1760  CB  ALA B 311     -41.771  32.564 -31.302  1.00 50.74           C  
ANISOU 1760  CB  ALA B 311     6549   9073   3657  -2272    640  -1158       C  
ATOM   1761  N   SER B 312     -41.229  29.387 -31.656  1.00 54.60           N  
ANISOU 1761  N   SER B 312     7639   9146   3959  -2736    444   -303       N  
ATOM   1762  CA  SER B 312     -41.496  28.049 -31.147  1.00 57.56           C  
ANISOU 1762  CA  SER B 312     8335   9464   4073  -3071    477      2       C  
ATOM   1763  C   SER B 312     -40.644  26.965 -31.789  1.00 56.74           C  
ANISOU 1763  C   SER B 312     8532   8918   4110  -3020    244    346       C  
ATOM   1764  O   SER B 312     -40.579  25.858 -31.244  1.00 58.21           O  
ANISOU 1764  O   SER B 312     9079   8929   4108  -3215    193    635       O  
ATOM   1765  CB  SER B 312     -42.972  27.688 -31.364  1.00 58.89           C  
ANISOU 1765  CB  SER B 312     8285   9813   4279  -3327    764   -126       C  
ATOM   1766  OG  SER B 312     -43.244  27.567 -32.755  1.00 56.24           O  
ANISOU 1766  OG  SER B 312     7762   9381   4227  -3257    800   -179       O  
ATOM   1767  N   ASN B 313     -40.008  27.254 -32.926  1.00 53.06           N  
ANISOU 1767  N   ASN B 313     7888   8197   4076  -2690     94    292       N  
ATOM   1768  CA  ASN B 313     -39.216  26.330 -33.738  1.00 54.38           C  
ANISOU 1768  CA  ASN B 313     8232   7944   4488  -2550   -115    522       C  
ATOM   1769  C   ASN B 313     -40.061  25.260 -34.420  1.00 55.35           C  
ANISOU 1769  C   ASN B 313     8442   7928   4661  -2807     36    617       C  
ATOM   1770  O   ASN B 313     -39.506  24.284 -34.943  1.00 55.44           O  
ANISOU 1770  O   ASN B 313     8685   7560   4818  -2745   -119    814       O  
ATOM   1771  CB  ASN B 313     -38.091  25.673 -32.929  1.00 57.12           C  
ANISOU 1771  CB  ASN B 313     8959   8089   4656  -2466   -409    803       C  
ATOM   1772  CG  ASN B 313     -37.007  26.662 -32.538  1.00 56.30           C  
ANISOU 1772  CG  ASN B 313     8706   8086   4601  -2171   -623    669       C  
ATOM   1773  OD1 ASN B 313     -36.628  27.534 -33.325  1.00 52.29           O  
ANISOU 1773  OD1 ASN B 313     7878   7565   4426  -1947   -633    454       O  
ATOM   1774  ND2 ASN B 313     -36.508  26.536 -31.315  1.00 59.38           N  
ANISOU 1774  ND2 ASN B 313     9339   8587   4634  -2196   -792    792       N  
ATOM   1775  N   LYS B 314     -41.383  25.418 -34.445  1.00 55.24           N  
ANISOU 1775  N   LYS B 314     8224   8224   4541  -3089    332    440       N  
ATOM   1776  CA  LYS B 314     -42.242  24.487 -35.163  1.00 56.36           C  
ANISOU 1776  CA  LYS B 314     8373   8293   4750  -3373    487    453       C  
ATOM   1777  C   LYS B 314     -42.097  24.681 -36.669  1.00 51.34           C  
ANISOU 1777  C   LYS B 314     7463   7525   4520  -3085    413    308       C  
ATOM   1778  O   LYS B 314     -42.011  25.809 -37.162  1.00 48.83           O  
ANISOU 1778  O   LYS B 314     6812   7366   4375  -2774    396    105       O  
ATOM   1779  CB  LYS B 314     -43.698  24.684 -34.744  1.00 60.76           C  
ANISOU 1779  CB  LYS B 314     8664   9271   5150  -3650    765    200       C  
ATOM   1780  CG  LYS B 314     -44.686  23.779 -35.463  1.00 65.58           C  
ANISOU 1780  CG  LYS B 314     9198   9849   5869  -3878    876    101       C  
ATOM   1781  CD  LYS B 314     -46.070  24.409 -35.510  1.00 68.56           C  
ANISOU 1781  CD  LYS B 314     9109  10728   6212  -3948   1082   -272       C  
ATOM   1782  CE  LYS B 314     -47.120  23.417 -35.989  1.00 72.31           C  
ANISOU 1782  CE  LYS B 314     9545  11234   6697  -4238   1192   -383       C  
ATOM   1783  NZ  LYS B 314     -48.487  24.009 -35.960  1.00 74.64           N  
ANISOU 1783  NZ  LYS B 314     9379  12055   6927  -4294   1360   -758       N  
ATOM   1784  N   VAL B 315     -42.074  23.571 -37.406  1.00 50.99           N  
ANISOU 1784  N   VAL B 315     7594   7171   4611  -3196    374    414       N  
ATOM   1785  CA  VAL B 315     -41.867  23.603 -38.849  1.00 48.93           C  
ANISOU 1785  CA  VAL B 315     7121   6785   4684  -2940    295    288       C  
ATOM   1786  C   VAL B 315     -43.191  23.364 -39.560  1.00 50.11           C  
ANISOU 1786  C   VAL B 315     7004   7190   4845  -3209    504     64       C  
ATOM   1787  O   VAL B 315     -44.099  22.703 -39.035  1.00 52.89           O  
ANISOU 1787  O   VAL B 315     7440   7648   5009  -3575    662     42       O  
ATOM   1788  CB  VAL B 315     -40.805  22.573 -39.286  1.00 48.38           C  
ANISOU 1788  CB  VAL B 315     7392   6205   4783  -2801     77    488       C  
ATOM   1789  CG1 VAL B 315     -39.509  22.806 -38.526  1.00 46.53           C  
ANISOU 1789  CG1 VAL B 315     7359   5802   4519  -2518   -157    675       C  
ATOM   1790  CG2 VAL B 315     -41.314  21.156 -39.064  1.00 51.70           C  
ANISOU 1790  CG2 VAL B 315     8193   6357   5092  -3220    152    631       C  
ATOM   1791  N   THR B 316     -43.302  23.921 -40.762  1.00 46.64           N  
ANISOU 1791  N   THR B 316     6230   6871   4621  -2934    471   -131       N  
ATOM   1792  CA  THR B 316     -44.474  23.754 -41.620  1.00 47.91           C  
ANISOU 1792  CA  THR B 316     6077   7322   4805  -3101    605   -381       C  
ATOM   1793  C   THR B 316     -43.992  23.364 -43.009  1.00 44.69           C  
ANISOU 1793  C   THR B 316     5658   6691   4632  -2886    465   -419       C  
ATOM   1794  O   THR B 316     -43.306  24.171 -43.670  1.00 40.70           O  
ANISOU 1794  O   THR B 316     5031   6163   4272  -2460    343   -423       O  
ATOM   1795  CB  THR B 316     -45.307  25.031 -41.687  1.00 47.25           C  
ANISOU 1795  CB  THR B 316     5533   7743   4676  -2918    701   -630       C  
ATOM   1796  OG1 THR B 316     -45.838  25.331 -40.391  1.00 48.65           O  
ANISOU 1796  OG1 THR B 316     5714   8154   4617  -3094    844   -657       O  
ATOM   1797  CG2 THR B 316     -46.456  24.861 -42.664  1.00 47.62           C  
ANISOU 1797  CG2 THR B 316     5258   8093   4742  -2924    754   -896       C  
ATOM   1798  N   PRO B 317     -44.314  22.165 -43.491  1.00 48.03           N  
ANISOU 1798  N   PRO B 317     6219   6943   5085  -3167    491   -460       N  
ATOM   1799  CA  PRO B 317     -43.812  21.747 -44.803  1.00 46.02           C  
ANISOU 1799  CA  PRO B 317     5966   6487   5031  -2977    364   -535       C  
ATOM   1800  C   PRO B 317     -44.366  22.614 -45.922  1.00 45.08           C  
ANISOU 1800  C   PRO B 317     5394   6790   4943  -2723    359   -776       C  
ATOM   1801  O   PRO B 317     -45.495  23.106 -45.866  1.00 45.46           O  
ANISOU 1801  O   PRO B 317     5116   7285   4873  -2800    467   -957       O  
ATOM   1802  CB  PRO B 317     -44.295  20.298 -44.926  1.00 49.69           C  
ANISOU 1802  CB  PRO B 317     6673   6717   5490  -3318    426   -572       C  
ATOM   1803  CG  PRO B 317     -45.438  20.198 -43.984  1.00 52.41           C  
ANISOU 1803  CG  PRO B 317     6968   7332   5612  -3609    614   -600       C  
ATOM   1804  CD  PRO B 317     -45.122  21.115 -42.849  1.00 51.30           C  
ANISOU 1804  CD  PRO B 317     6839   7309   5344  -3532    626   -445       C  
ATOM   1805  N   ILE B 318     -43.540  22.802 -46.946  1.00 42.48           N  
ANISOU 1805  N   ILE B 318     5061   6324   4755  -2363    226   -769       N  
ATOM   1806  CA  ILE B 318     -43.893  23.571 -48.131  1.00 41.24           C  
ANISOU 1806  CA  ILE B 318     4566   6507   4596  -2078    190   -936       C  
ATOM   1807  C   ILE B 318     -43.632  22.682 -49.337  1.00 43.06           C  
ANISOU 1807  C   ILE B 318     4857   6605   4900  -2079    122  -1062       C  
ATOM   1808  O   ILE B 318     -42.485  22.300 -49.591  1.00 41.43           O  
ANISOU 1808  O   ILE B 318     4886   6035   4819  -1920     44   -954       O  
ATOM   1809  CB  ILE B 318     -43.082  24.873 -48.234  1.00 38.28           C  
ANISOU 1809  CB  ILE B 318     4147   6125   4275  -1635    125   -793       C  
ATOM   1810  CG1 ILE B 318     -43.422  25.825 -47.081  1.00 37.62           C  
ANISOU 1810  CG1 ILE B 318     3988   6187   4117  -1619    193   -738       C  
ATOM   1811  CG2 ILE B 318     -43.320  25.537 -49.574  1.00 38.41           C  
ANISOU 1811  CG2 ILE B 318     3925   6406   4263  -1333     75   -900       C  
ATOM   1812  CD1 ILE B 318     -42.479  27.008 -46.974  1.00 33.30           C  
ANISOU 1812  CD1 ILE B 318     3486   5514   3653  -1268    141   -594       C  
ATOM   1813  N   ASP B 319     -44.684  22.338 -50.069  1.00 46.52           N  
ANISOU 1813  N   ASP B 319     5056   7368   5253  -2253    148  -1329       N  
ATOM   1814  CA  ASP B 319     -44.490  21.528 -51.261  1.00 49.81           C  
ANISOU 1814  CA  ASP B 319     5511   7703   5710  -2258     83  -1506       C  
ATOM   1815  C   ASP B 319     -43.922  22.380 -52.388  1.00 45.94           C  
ANISOU 1815  C   ASP B 319     4887   7375   5192  -1787    -11  -1488       C  
ATOM   1816  O   ASP B 319     -44.147  23.591 -52.455  1.00 44.52           O  
ANISOU 1816  O   ASP B 319     4506   7482   4929  -1511    -27  -1412       O  
ATOM   1817  CB  ASP B 319     -45.798  20.867 -51.695  1.00 57.82           C  
ANISOU 1817  CB  ASP B 319     6337   9002   6631  -2533    150  -1773       C  
ATOM   1818  CG  ASP B 319     -46.374  19.958 -50.625  1.00 65.76           C  
ANISOU 1818  CG  ASP B 319     7547   9796   7643  -2944    297  -1716       C  
ATOM   1819  OD1 ASP B 319     -47.448  20.284 -50.073  1.00 69.78           O  
ANISOU 1819  OD1 ASP B 319     7846  10646   8021  -3060    415  -1767       O  
ATOM   1820  OD2 ASP B 319     -45.743  18.923 -50.322  1.00 68.60           O  
ANISOU 1820  OD2 ASP B 319     8297   9646   8122  -3132    294  -1624       O  
ATOM   1821  N   ILE B 320     -43.179  21.734 -53.281  1.00 45.11           N  
ANISOU 1821  N   ILE B 320     4923   7070   5149  -1698    -62  -1563       N  
ATOM   1822  CA  ILE B 320     -42.483  22.429 -54.356  1.00 41.54           C  
ANISOU 1822  CA  ILE B 320     4398   6743   4642  -1300   -114  -1525       C  
ATOM   1823  C   ILE B 320     -43.429  22.623 -55.534  1.00 41.08           C  
ANISOU 1823  C   ILE B 320     4055   7188   4366  -1243   -167  -1763       C  
ATOM   1824  O   ILE B 320     -44.043  21.663 -56.019  1.00 41.61           O  
ANISOU 1824  O   ILE B 320     4065   7356   4390  -1499   -185  -2058       O  
ATOM   1825  CB  ILE B 320     -41.223  21.658 -54.780  1.00 42.23           C  
ANISOU 1825  CB  ILE B 320     4726   6452   4868  -1208   -129  -1537       C  
ATOM   1826  CG1 ILE B 320     -40.302  21.460 -53.574  1.00 40.13           C  
ANISOU 1826  CG1 ILE B 320     4717   5733   4798  -1216   -127  -1307       C  
ATOM   1827  CG2 ILE B 320     -40.501  22.402 -55.888  1.00 41.95           C  
ANISOU 1827  CG2 ILE B 320     4599   6601   4737   -853   -132  -1501       C  
ATOM   1828  CD1 ILE B 320     -39.982  22.748 -52.828  1.00 39.83           C  
ANISOU 1828  CD1 ILE B 320     4615   5762   4758  -1041   -109  -1042       C  
ATOM   1829  N   LEU B 321     -43.544  23.867 -55.998  1.00 38.92           N  
ANISOU 1829  N   LEU B 321     3623   7220   3947   -904   -205  -1640       N  
ATOM   1830  CA  LEU B 321     -44.414  24.186 -57.119  1.00 40.24           C  
ANISOU 1830  CA  LEU B 321     3529   7901   3859   -758   -301  -1820       C  
ATOM   1831  C   LEU B 321     -43.783  23.656 -58.407  1.00 40.97           C  
ANISOU 1831  C   LEU B 321     3704   8014   3846   -670   -329  -1948       C  
ATOM   1832  O   LEU B 321     -42.605  23.289 -58.422  1.00 41.84           O  
ANISOU 1832  O   LEU B 321     4046   7755   4097   -646   -260  -1865       O  
ATOM   1833  CB  LEU B 321     -44.657  25.695 -57.172  1.00 40.47           C  
ANISOU 1833  CB  LEU B 321     3452   8160   3764   -374   -347  -1599       C  
ATOM   1834  CG  LEU B 321     -45.519  26.225 -56.014  1.00 41.76           C  
ANISOU 1834  CG  LEU B 321     3455   8422   3988   -429   -328  -1580       C  
ATOM   1835  CD1 LEU B 321     -45.547  27.743 -55.970  1.00 41.92           C  
ANISOU 1835  CD1 LEU B 321     3463   8516   3947     -5   -367  -1346       C  
ATOM   1836  CD2 LEU B 321     -46.925  25.673 -56.113  1.00 45.44           C  
ANISOU 1836  CD2 LEU B 321     3601   9314   4351   -638   -363  -1907       C  
ATOM   1837  N   PRO B 322     -44.550  23.582 -59.501  1.00 42.39           N  
ANISOU 1837  N   PRO B 322     3675   8668   3764   -611   -435  -2187       N  
ATOM   1838  CA  PRO B 322     -44.022  22.945 -60.724  1.00 45.46           C  
ANISOU 1838  CA  PRO B 322     4140   9106   4028   -569   -444  -2369       C  
ATOM   1839  C   PRO B 322     -42.706  23.514 -61.236  1.00 43.73           C  
ANISOU 1839  C   PRO B 322     4122   8732   3762   -280   -369  -2125       C  
ATOM   1840  O   PRO B 322     -41.907  22.758 -61.801  1.00 41.57           O  
ANISOU 1840  O   PRO B 322     3970   8311   3513   -316   -310  -2279       O  
ATOM   1841  CB  PRO B 322     -45.156  23.159 -61.734  1.00 48.94           C  
ANISOU 1841  CB  PRO B 322     4329  10015   4250   -431   -525  -2468       C  
ATOM   1842  CG  PRO B 322     -46.393  23.138 -60.888  1.00 46.82           C  
ANISOU 1842  CG  PRO B 322     3851   9849   4091   -609   -515  -2529       C  
ATOM   1843  CD  PRO B 322     -46.005  23.815 -59.592  1.00 43.83           C  
ANISOU 1843  CD  PRO B 322     3564   9234   3856   -602   -478  -2287       C  
ATOM   1844  N   LEU B 323     -42.444  24.807 -61.064  1.00 42.42           N  
ANISOU 1844  N   LEU B 323     3996   8578   3545     -8   -348  -1767       N  
ATOM   1845  CA  LEU B 323     -41.247  25.409 -61.640  1.00 43.26           C  
ANISOU 1845  CA  LEU B 323     4278   8579   3581    207   -240  -1534       C  
ATOM   1846  C   LEU B 323     -40.038  25.343 -60.712  1.00 39.46           C  
ANISOU 1846  C   LEU B 323     3960   7598   3434    132   -103  -1372       C  
ATOM   1847  O   LEU B 323     -38.987  25.905 -61.042  1.00 39.38           O  
ANISOU 1847  O   LEU B 323     4054   7502   3404    262     15  -1187       O  
ATOM   1848  CB  LEU B 323     -41.520  26.858 -62.048  1.00 44.48           C  
ANISOU 1848  CB  LEU B 323     4449   8960   3490    520   -278  -1223       C  
ATOM   1849  CG  LEU B 323     -42.385  26.997 -63.306  1.00 48.65           C  
ANISOU 1849  CG  LEU B 323     4858  10036   3590    705   -432  -1342       C  
ATOM   1850  CD1 LEU B 323     -42.424  28.435 -63.795  1.00 50.59           C  
ANISOU 1850  CD1 LEU B 323     5238  10409   3576   1065   -464   -962       C  
ATOM   1851  CD2 LEU B 323     -41.899  26.068 -64.418  1.00 50.75           C  
ANISOU 1851  CD2 LEU B 323     5141  10462   3679    620   -389  -1606       C  
ATOM   1852  N   GLY B 324     -40.153  24.676 -59.576  1.00 37.31           N  
ANISOU 1852  N   GLY B 324     3710   7026   3441    -85   -115  -1438       N  
ATOM   1853  CA  GLY B 324     -38.996  24.367 -58.758  1.00 34.89           C  
ANISOU 1853  CA  GLY B 324     3552   6281   3423   -137    -37  -1343       C  
ATOM   1854  C   GLY B 324     -38.937  25.155 -57.461  1.00 32.39           C  
ANISOU 1854  C   GLY B 324     3276   5757   3272   -147    -26  -1079       C  
ATOM   1855  O   GLY B 324     -39.869  25.871 -57.073  1.00 32.04           O  
ANISOU 1855  O   GLY B 324     3149   5871   3154   -132    -66   -994       O  
ATOM   1856  N   VAL B 325     -37.787  25.014 -56.788  1.00 35.71           N  
ANISOU 1856  N   VAL B 325     3072   5422   5075   -233    169  -1314       N  
ATOM   1857  CA  VAL B 325     -37.625  25.512 -55.423  1.00 32.72           C  
ANISOU 1857  CA  VAL B 325     2689   5009   4734   -251    174   -873       C  
ATOM   1858  C   VAL B 325     -37.686  27.034 -55.385  1.00 31.44           C  
ANISOU 1858  C   VAL B 325     2652   5150   4144   -225    105   -710       C  
ATOM   1859  O   VAL B 325     -38.378  27.623 -54.546  1.00 31.06           O  
ANISOU 1859  O   VAL B 325     2610   5157   4033   -258     39   -527       O  
ATOM   1860  CB  VAL B 325     -36.306  24.995 -54.814  1.00 34.49           C  
ANISOU 1860  CB  VAL B 325     2860   5050   5194   -161    283   -671       C  
ATOM   1861  CG1 VAL B 325     -36.069  25.622 -53.434  1.00 33.74           C  
ANISOU 1861  CG1 VAL B 325     2770   5023   5027   -182    248   -244       C  
ATOM   1862  CG2 VAL B 325     -36.323  23.485 -54.711  1.00 36.62           C  
ANISOU 1862  CG2 VAL B 325     3042   4907   5964   -150    338   -774       C  
ATOM   1863  N   MET B 326     -36.942  27.702 -56.269  1.00 30.32           N  
ANISOU 1863  N   MET B 326     2619   5190   3713   -168    142   -769       N  
ATOM   1864  CA  MET B 326     -36.934  29.163 -56.213  1.00 31.99           C  
ANISOU 1864  CA  MET B 326     2992   5581   3581   -164     84   -572       C  
ATOM   1865  C   MET B 326     -38.296  29.740 -56.584  1.00 32.25           C  
ANISOU 1865  C   MET B 326     3095   5737   3422   -120    -84   -652       C  
ATOM   1866  O   MET B 326     -38.724  30.751 -56.014  1.00 31.01           O  
ANISOU 1866  O   MET B 326     3026   5607   3148    -84   -163   -478       O  
ATOM   1867  CB  MET B 326     -35.850  29.735 -57.123  1.00 31.70           C  
ANISOU 1867  CB  MET B 326     3060   5701   3286   -164    195   -566       C  
ATOM   1868  CG  MET B 326     -34.496  29.927 -56.460  1.00 32.80           C  
ANISOU 1868  CG  MET B 326     3122   5811   3529   -220    316   -367       C  
ATOM   1869  SD  MET B 326     -34.525  30.677 -54.812  1.00 32.61           S  
ANISOU 1869  SD  MET B 326     3114   5696   3580   -289    211    -67       S  
ATOM   1870  CE  MET B 326     -35.392  32.219 -55.116  1.00 33.53           C  
ANISOU 1870  CE  MET B 326     3515   5856   3370   -296     95     -2       C  
ATOM   1871  N   ALA B 327     -38.984  29.124 -57.551  1.00 33.84           N  
ANISOU 1871  N   ALA B 327     3240   6026   3590   -101   -158   -950       N  
ATOM   1872  CA  ALA B 327     -40.335  29.572 -57.882  1.00 35.07           C  
ANISOU 1872  CA  ALA B 327     3379   6351   3594    -36   -363  -1044       C  
ATOM   1873  C   ALA B 327     -41.271  29.420 -56.693  1.00 36.44           C  
ANISOU 1873  C   ALA B 327     3374   6436   4037    -78   -397   -967       C  
ATOM   1874  O   ALA B 327     -42.204  30.216 -56.529  1.00 39.55           O  
ANISOU 1874  O   ALA B 327     3748   6969   4311     27   -530   -926       O  
ATOM   1875  CB  ALA B 327     -40.878  28.794 -59.080  1.00 35.02           C  
ANISOU 1875  CB  ALA B 327     3291   6497   3517    -45   -466  -1436       C  
ATOM   1876  N   THR B 328     -41.036  28.405 -55.858  1.00 34.83           N  
ANISOU 1876  N   THR B 328     3032   6011   4190   -213   -264   -931       N  
ATOM   1877  CA  THR B 328     -41.861  28.191 -54.674  1.00 36.14           C  
ANISOU 1877  CA  THR B 328     3029   6130   4572   -295   -236   -808       C  
ATOM   1878  C   THR B 328     -41.545  29.218 -53.597  1.00 35.02           C  
ANISOU 1878  C   THR B 328     2997   6030   4280   -223   -193   -513       C  
ATOM   1879  O   THR B 328     -42.453  29.800 -52.992  1.00 35.29           O  
ANISOU 1879  O   THR B 328     2956   6199   4255   -173   -226   -480       O  
ATOM   1880  CB  THR B 328     -41.644  26.775 -54.135  1.00 37.63           C  
ANISOU 1880  CB  THR B 328     3092   6034   5173   -468   -102   -782       C  
ATOM   1881  OG1 THR B 328     -41.969  25.822 -55.152  1.00 38.63           O  
ANISOU 1881  OG1 THR B 328     3130   6069   5477   -553   -149  -1141       O  
ATOM   1882  CG2 THR B 328     -42.519  26.527 -52.915  1.00 38.31           C  
ANISOU 1882  CG2 THR B 328     3008   6114   5434   -597    -29   -597       C  
ATOM   1883  N   LEU B 329     -40.257  29.445 -53.338  1.00 32.16           N  
ANISOU 1883  N   LEU B 329     2782   5576   3861   -217   -119   -342       N  
ATOM   1884  CA  LEU B 329     -39.869  30.457 -52.366  1.00 31.29           C  
ANISOU 1884  CA  LEU B 329     2785   5509   3594   -182   -108   -132       C  
ATOM   1885  C   LEU B 329     -40.357  31.835 -52.789  1.00 32.09           C  
ANISOU 1885  C   LEU B 329     3044   5711   3436    -44   -221   -183       C  
ATOM   1886  O   LEU B 329     -40.861  32.601 -51.960  1.00 32.73           O  
ANISOU 1886  O   LEU B 329     3151   5842   3445     25   -239   -141       O  
ATOM   1887  CB  LEU B 329     -38.352  30.449 -52.180  1.00 30.57           C  
ANISOU 1887  CB  LEU B 329     2770   5341   3503   -227    -45     12       C  
ATOM   1888  CG  LEU B 329     -37.801  29.268 -51.376  1.00 31.13           C  
ANISOU 1888  CG  LEU B 329     2699   5296   3832   -290     34    162       C  
ATOM   1889  CD1 LEU B 329     -36.285  29.178 -51.517  1.00 31.91           C  
ANISOU 1889  CD1 LEU B 329     2796   5366   3964   -280     69    239       C  
ATOM   1890  CD2 LEU B 329     -38.205  29.384 -49.900  1.00 29.50           C  
ANISOU 1890  CD2 LEU B 329     2457   5168   3583   -328     44    366       C  
ATOM   1891  N   THR B 330     -40.221  32.166 -54.076  1.00 32.69           N  
ANISOU 1891  N   THR B 330     3243   5817   3359     20   -294   -268       N  
ATOM   1892  CA  THR B 330     -40.711  33.450 -54.571  1.00 32.98           C  
ANISOU 1892  CA  THR B 330     3467   5900   3165    186   -426   -249       C  
ATOM   1893  C   THR B 330     -42.186  33.643 -54.228  1.00 34.46           C  
ANISOU 1893  C   THR B 330     3495   6203   3396    342   -536   -358       C  
ATOM   1894  O   THR B 330     -42.590  34.700 -53.728  1.00 35.28           O  
ANISOU 1894  O   THR B 330     3695   6276   3435    500   -588   -314       O  
ATOM   1895  CB  THR B 330     -40.478  33.540 -56.081  1.00 34.10           C  
ANISOU 1895  CB  THR B 330     3742   6126   3088    227   -489   -292       C  
ATOM   1896  OG1 THR B 330     -39.070  33.600 -56.345  1.00 34.30           O  
ANISOU 1896  OG1 THR B 330     3897   6085   3051     89   -342   -177       O  
ATOM   1897  CG2 THR B 330     -41.155  34.766 -56.670  1.00 36.40           C  
ANISOU 1897  CG2 THR B 330     4233   6456   3143    444   -668   -213       C  
ATOM   1898  N   GLN B 331     -43.005  32.618 -54.470  1.00 33.36           N  
ANISOU 1898  N   GLN B 331     3084   6192   3400    295   -564   -535       N  
ATOM   1899  CA  GLN B 331     -44.430  32.734 -54.171  1.00 34.37           C  
ANISOU 1899  CA  GLN B 331     2963   6499   3597    415   -652   -661       C  
ATOM   1900  C   GLN B 331     -44.673  32.849 -52.669  1.00 36.77           C  
ANISOU 1900  C   GLN B 331     3158   6802   4011    381   -493   -579       C  
ATOM   1901  O   GLN B 331     -45.418  33.726 -52.217  1.00 37.94           O  
ANISOU 1901  O   GLN B 331     3264   7051   4100    587   -531   -620       O  
ATOM   1902  CB  GLN B 331     -45.183  31.542 -54.753  1.00 36.91           C  
ANISOU 1902  CB  GLN B 331     2982   6956   4088    283   -707   -894       C  
ATOM   1903  CG  GLN B 331     -45.299  31.595 -56.264  1.00 37.51           C  
ANISOU 1903  CG  GLN B 331     3127   7170   3956    380   -924  -1057       C  
ATOM   1904  CD  GLN B 331     -45.930  32.890 -56.746  1.00 43.74           C  
ANISOU 1904  CD  GLN B 331     4014   8120   4485    713  -1152  -1002       C  
ATOM   1905  OE1 GLN B 331     -47.049  33.224 -56.360  1.00 46.82           O  
ANISOU 1905  OE1 GLN B 331     4157   8674   4958    873  -1249  -1076       O  
ATOM   1906  NE2 GLN B 331     -45.214  33.624 -57.591  1.00 44.63           N  
ANISOU 1906  NE2 GLN B 331     4477   8185   4294    831  -1226   -851       N  
ATOM   1907  N   HIS B 332     -44.045  31.977 -51.875  1.00 33.88           N  
ANISOU 1907  N   HIS B 332     2750   6340   3784    151   -314   -462       N  
ATOM   1908  CA  HIS B 332     -44.263  32.028 -50.430  1.00 36.04           C  
ANISOU 1908  CA  HIS B 332     2934   6688   4072    104   -157   -357       C  
ATOM   1909  C   HIS B 332     -43.824  33.368 -49.854  1.00 34.77           C  
ANISOU 1909  C   HIS B 332     3020   6499   3692    266   -175   -317       C  
ATOM   1910  O   HIS B 332     -44.497  33.927 -48.981  1.00 36.47           O  
ANISOU 1910  O   HIS B 332     3159   6862   3835    379   -111   -384       O  
ATOM   1911  CB  HIS B 332     -43.527  30.882 -49.737  1.00 36.66           C  
ANISOU 1911  CB  HIS B 332     2981   6653   4295   -140     -3   -159       C  
ATOM   1912  CG  HIS B 332     -44.017  30.606 -48.350  1.00 44.17           C  
ANISOU 1912  CG  HIS B 332     3782   7761   5239   -234    174    -21       C  
ATOM   1913  ND1 HIS B 332     -43.412  31.129 -47.226  1.00 45.43           N  
ANISOU 1913  ND1 HIS B 332     4084   7998   5180   -213    239    127       N  
ATOM   1914  CD2 HIS B 332     -45.067  29.876 -47.905  1.00 48.21           C  
ANISOU 1914  CD2 HIS B 332     4004   8413   5900   -374    312    -12       C  
ATOM   1915  CE1 HIS B 332     -44.062  30.726 -46.149  1.00 47.15           C  
ANISOU 1915  CE1 HIS B 332     4131   8424   5359   -309    418    238       C  
ATOM   1916  NE2 HIS B 332     -45.072  29.965 -46.532  1.00 48.53           N  
ANISOU 1916  NE2 HIS B 332     4036   8631   5773   -421    486    179       N  
ATOM   1917  N   ILE B 333     -42.715  33.914 -50.354  1.00 31.36           N  
ANISOU 1917  N   ILE B 333     2872   5880   3164    268   -246   -244       N  
ATOM   1918  CA  ILE B 333     -42.198  35.169 -49.813  1.00 32.29           C  
ANISOU 1918  CA  ILE B 333     3241   5898   3129    349   -269   -230       C  
ATOM   1919  C   ILE B 333     -43.058  36.348 -50.257  1.00 35.30           C  
ANISOU 1919  C   ILE B 333     3726   6234   3453    640   -394   -359       C  
ATOM   1920  O   ILE B 333     -43.496  37.155 -49.431  1.00 36.80           O  
ANISOU 1920  O   ILE B 333     3951   6435   3598    793   -371   -474       O  
ATOM   1921  CB  ILE B 333     -40.725  35.361 -50.218  1.00 31.72           C  
ANISOU 1921  CB  ILE B 333     3390   5643   3017    199   -285    -99       C  
ATOM   1922  CG1 ILE B 333     -39.858  34.294 -49.549  1.00 30.29           C  
ANISOU 1922  CG1 ILE B 333     3079   5517   2911     -8   -186     31       C  
ATOM   1923  CG2 ILE B 333     -40.251  36.751 -49.820  1.00 31.91           C  
ANISOU 1923  CG2 ILE B 333     3686   5506   2933    233   -332   -122       C  
ATOM   1924  CD1 ILE B 333     -38.537  34.060 -50.237  1.00 29.55           C  
ANISOU 1924  CD1 ILE B 333     3053   5320   2853   -134   -183    126       C  
ATOM   1925  N   THR B 334     -43.307  36.477 -51.567  1.00 33.68           N  
ANISOU 1925  N   THR B 334     3578   5986   3233    754   -537   -350       N  
ATOM   1926  CA  THR B 334     -44.035  37.650 -52.054  1.00 37.24           C  
ANISOU 1926  CA  THR B 334     4166   6354   3629   1083   -700   -398       C  
ATOM   1927  C   THR B 334     -45.493  37.643 -51.606  1.00 38.89           C  
ANISOU 1927  C   THR B 334     4051   6804   3922   1330   -722   -595       C  
ATOM   1928  O   THR B 334     -46.073  38.711 -51.376  1.00 42.98           O  
ANISOU 1928  O   THR B 334     4647   7239   4446   1648   -794   -684       O  
ATOM   1929  CB  THR B 334     -43.958  37.750 -53.584  1.00 38.33           C  
ANISOU 1929  CB  THR B 334     4448   6463   3653   1156   -870   -290       C  
ATOM   1930  OG1 THR B 334     -44.429  36.534 -54.174  1.00 38.25           O  
ANISOU 1930  OG1 THR B 334     4139   6723   3672   1068   -900   -391       O  
ATOM   1931  CG2 THR B 334     -42.525  38.011 -54.041  1.00 38.85           C  
ANISOU 1931  CG2 THR B 334     4837   6310   3616    933   -805    -89       C  
ATOM   1932  N   GLN B 335     -46.107  36.466 -51.485  1.00 37.34           N  
ANISOU 1932  N   GLN B 335     3472   6889   3825   1190   -651   -676       N  
ATOM   1933  CA  GLN B 335     -47.479  36.422 -50.995  1.00 37.23           C  
ANISOU 1933  CA  GLN B 335     3072   7166   3909   1368   -624   -866       C  
ATOM   1934  C   GLN B 335     -47.542  36.817 -49.524  1.00 37.85           C  
ANISOU 1934  C   GLN B 335     3128   7297   3956   1390   -406   -936       C  
ATOM   1935  O   GLN B 335     -48.486  37.488 -49.097  1.00 40.86           O  
ANISOU 1935  O   GLN B 335     3343   7825   4356   1692   -390  -1124       O  
ATOM   1936  CB  GLN B 335     -48.073  35.033 -51.213  1.00 40.33           C  
ANISOU 1936  CB  GLN B 335     3058   7813   4452   1121   -576   -928       C  
ATOM   1937  CG  GLN B 335     -48.377  34.716 -52.682  1.00 41.48           C  
ANISOU 1937  CG  GLN B 335     3140   8025   4596   1165   -834   -994       C  
ATOM   1938  CD  GLN B 335     -49.211  33.463 -52.842  1.00 43.60           C  
ANISOU 1938  CD  GLN B 335     2949   8548   5071    928   -814  -1160       C  
ATOM   1939  OE1 GLN B 335     -49.993  33.108 -51.961  1.00 44.03           O  
ANISOU 1939  OE1 GLN B 335     2725   8728   5276    819   -622  -1208       O  
ATOM   1940  NE2 GLN B 335     -49.051  32.785 -53.974  1.00 46.34           N  
ANISOU 1940  NE2 GLN B 335     3328   8866   5413    791   -961  -1231       N  
ATOM   1941  N   ASN B 336     -46.537  36.426 -48.741  1.00 38.00           N  
ANISOU 1941  N   ASN B 336     3300   7234   3903   1103   -245   -806       N  
ATOM   1942  CA  ASN B 336     -46.480  36.869 -47.351  1.00 40.68           C  
ANISOU 1942  CA  ASN B 336     3671   7670   4115   1120    -65   -888       C  
ATOM   1943  C   ASN B 336     -46.289  38.379 -47.263  1.00 42.52           C  
ANISOU 1943  C   ASN B 336     4230   7648   4279   1408   -168  -1041       C  
ATOM   1944  O   ASN B 336     -46.951  39.047 -46.462  1.00 44.44           O  
ANISOU 1944  O   ASN B 336     4401   8011   4473   1643    -77  -1280       O  
ATOM   1945  CB  ASN B 336     -45.365  36.134 -46.609  1.00 39.21           C  
ANISOU 1945  CB  ASN B 336     3589   7475   3833    772     58   -684       C  
ATOM   1946  CG  ASN B 336     -45.844  34.842 -45.980  1.00 40.59           C  
ANISOU 1946  CG  ASN B 336     3435   7937   4052    543    260   -561       C  
ATOM   1947  OD1 ASN B 336     -46.832  34.826 -45.248  1.00 44.54           O  
ANISOU 1947  OD1 ASN B 336     3673   8747   4503    604    432   -670       O  
ATOM   1948  ND2 ASN B 336     -45.154  33.748 -46.274  1.00 39.61           N  
ANISOU 1948  ND2 ASN B 336     3315   7694   4040    279    261   -329       N  
ATOM   1949  N   LYS B 337     -45.394  38.937 -48.086  1.00 42.13           N  
ANISOU 1949  N   LYS B 337     4540   7228   4241   1388   -337   -918       N  
ATOM   1950  CA  LYS B 337     -45.211  40.387 -48.100  1.00 43.22           C  
ANISOU 1950  CA  LYS B 337     5029   7011   4383   1627   -442  -1029       C  
ATOM   1951  C   LYS B 337     -46.508  41.106 -48.451  1.00 45.78           C  
ANISOU 1951  C   LYS B 337     5240   7338   4815   2106   -547  -1199       C  
ATOM   1952  O   LYS B 337     -46.856  42.119 -47.828  1.00 47.74           O  
ANISOU 1952  O   LYS B 337     5601   7441   5096   2391   -528  -1440       O  
ATOM   1953  CB  LYS B 337     -44.105  40.775 -49.084  1.00 41.46           C  
ANISOU 1953  CB  LYS B 337     5176   6408   4170   1475   -578   -795       C  
ATOM   1954  CG  LYS B 337     -44.155  42.244 -49.492  1.00 45.29           C  
ANISOU 1954  CG  LYS B 337     6034   6441   4733   1749   -722   -822       C  
ATOM   1955  CD  LYS B 337     -42.904  42.704 -50.235  1.00 44.85           C  
ANISOU 1955  CD  LYS B 337     6364   6007   4670   1492   -782   -566       C  
ATOM   1956  CE  LYS B 337     -43.049  44.171 -50.643  1.00 49.95           C  
ANISOU 1956  CE  LYS B 337     7416   6125   5437   1758   -918   -535       C  
ATOM   1957  NZ  LYS B 337     -41.774  44.774 -51.122  1.00 50.91           N  
ANISOU 1957  NZ  LYS B 337     7927   5837   5578   1426   -918   -299       N  
ATOM   1958  N   GLU B 338     -47.239  40.599 -49.446  1.00 46.77           N  
ANISOU 1958  N   GLU B 338     5126   7639   5005   2226   -677  -1112       N  
ATOM   1959  CA  GLU B 338     -48.504  41.221 -49.820  1.00 52.82           C  
ANISOU 1959  CA  GLU B 338     5708   8480   5881   2720   -824  -1259       C  
ATOM   1960  C   GLU B 338     -49.534  41.076 -48.708  1.00 55.25           C  
ANISOU 1960  C   GLU B 338     5583   9178   6232   2876   -618  -1568       C  
ATOM   1961  O   GLU B 338     -50.320  41.997 -48.455  1.00 59.47           O  
ANISOU 1961  O   GLU B 338     6057   9678   6859   3338   -652  -1799       O  
ATOM   1962  CB  GLU B 338     -49.021  40.610 -51.123  1.00 54.79           C  
ANISOU 1962  CB  GLU B 338     5748   8928   6141   2766  -1043  -1122       C  
ATOM   1963  CG  GLU B 338     -50.264  41.285 -51.667  1.00 61.82           C  
ANISOU 1963  CG  GLU B 338     6438   9921   7130   3316  -1281  -1227       C  
ATOM   1964  CD  GLU B 338     -50.730  40.677 -52.972  1.00 65.17           C  
ANISOU 1964  CD  GLU B 338     6655  10608   7500   3338  -1549  -1116       C  
ATOM   1965  OE1 GLU B 338     -49.887  40.103 -53.697  1.00 63.72           O  
ANISOU 1965  OE1 GLU B 338     6683  10356   7172   3001  -1583   -919       O  
ATOM   1966  OE2 GLU B 338     -51.940  40.772 -53.272  1.00 69.86           O  
ANISOU 1966  OE2 GLU B 338     6958  11410   8178   3542  -1647  -1231       O  
ATOM   1967  N   LEU B 339     -49.534  39.928 -48.026  1.00 54.67           N  
ANISOU 1967  N   LEU B 339     5208   9471   6095   2505   -383  -1563       N  
ATOM   1968  CA  LEU B 339     -50.421  39.732 -46.883  1.00 58.06           C  
ANISOU 1968  CA  LEU B 339     5232  10327   6502   2572   -113  -1808       C  
ATOM   1969  C   LEU B 339     -50.156  40.766 -45.794  1.00 60.35           C  
ANISOU 1969  C   LEU B 339     5780  10483   6667   2757     23  -2054       C  
ATOM   1970  O   LEU B 339     -51.093  41.278 -45.171  1.00 63.21           O  
ANISOU 1970  O   LEU B 339     5891  11080   7047   3103    157  -2373       O  
ATOM   1971  CB  LEU B 339     -50.245  38.314 -46.340  1.00 55.81           C  
ANISOU 1971  CB  LEU B 339     4697  10361   6149   2071    122  -1646       C  
ATOM   1972  CG  LEU B 339     -51.329  37.706 -45.455  1.00 60.89           C  
ANISOU 1972  CG  LEU B 339     4865  11480   6791   1970    406  -1749       C  
ATOM   1973  CD1 LEU B 339     -52.683  37.769 -46.140  1.00 64.57           C  
ANISOU 1973  CD1 LEU B 339     5018  12041   7474   2151    266  -1855       C  
ATOM   1974  CD2 LEU B 339     -50.959  36.268 -45.119  1.00 59.34           C  
ANISOU 1974  CD2 LEU B 339     4565  11406   6576   1433    583  -1462       C  
ATOM   1975  N   ILE B 340     -48.882  41.091 -45.561  1.00 59.30           N  
ANISOU 1975  N   ILE B 340     6121   9995   6414   2532     -8  -1956       N  
ATOM   1976  CA  ILE B 340     -48.527  42.073 -44.540  1.00 62.34           C  
ANISOU 1976  CA  ILE B 340     6784  10230   6674   2648     86  -2247       C  
ATOM   1977  C   ILE B 340     -48.964  43.471 -44.963  1.00 67.98           C  
ANISOU 1977  C   ILE B 340     7720  10513   7595   3169    -88  -2480       C  
ATOM   1978  O   ILE B 340     -49.565  44.216 -44.179  1.00 72.28           O  
ANISOU 1978  O   ILE B 340     8214  11112   8138   3513     34  -2883       O  
ATOM   1979  CB  ILE B 340     -47.014  42.017 -44.254  1.00 59.90           C  
ANISOU 1979  CB  ILE B 340     6871   9675   6214   2226     51  -2087       C  
ATOM   1980  CG1 ILE B 340     -46.696  40.886 -43.274  1.00 58.56           C  
ANISOU 1980  CG1 ILE B 340     6493   9977   5781   1843    270  -1970       C  
ATOM   1981  CG2 ILE B 340     -46.516  43.354 -43.721  1.00 62.18           C  
ANISOU 1981  CG2 ILE B 340     7570   9569   6485   2364      0  -2400       C  
ATOM   1982  CD1 ILE B 340     -45.273  40.382 -43.363  1.00 54.67           C  
ANISOU 1982  CD1 ILE B 340     6231   9328   5212   1423    179  -1674       C  
ATOM   1983  N   GLU B 341     -48.676  43.845 -46.213  1.00 68.57           N  
ANISOU 1983  N   GLU B 341     8056  10152   7846   3255   -366  -2222       N  
ATOM   1984  CA  GLU B 341     -48.948  45.207 -46.665  1.00 75.05           C  
ANISOU 1984  CA  GLU B 341     9187  10443   8885   3736   -559  -2337       C  
ATOM   1985  C   GLU B 341     -50.438  45.526 -46.628  1.00 80.10           C  
ANISOU 1985  C   GLU B 341     9422  11333   9679   4336   -565  -2606       C  
ATOM   1986  O   GLU B 341     -50.828  46.663 -46.335  1.00 85.38           O  
ANISOU 1986  O   GLU B 341    10260  11666  10514   4769   -597  -2880       O  
ATOM   1987  CB  GLU B 341     -48.394  45.413 -48.075  1.00 75.59           C  
ANISOU 1987  CB  GLU B 341     9590  10086   9043   3683   -838  -1907       C  
ATOM   1988  CG  GLU B 341     -46.966  45.940 -48.107  1.00 76.39           C  
ANISOU 1988  CG  GLU B 341    10241   9658   9127   3309   -863  -1757       C  
ATOM   1989  CD  GLU B 341     -46.858  47.374 -47.615  1.00 83.16           C  
ANISOU 1989  CD  GLU B 341    11509   9916  10171   3570   -893  -2034       C  
ATOM   1990  OE1 GLU B 341     -45.732  47.811 -47.298  1.00 83.48           O  
ANISOU 1990  OE1 GLU B 341    11926   9583  10209   3203   -867  -2046       O  
ATOM   1991  OE2 GLU B 341     -47.895  48.068 -47.550  1.00 88.71           O  
ANISOU 1991  OE2 GLU B 341    12143  10507  11055   4143   -951  -2266       O  
ATOM   1992  N   LYS B 342     -51.286  44.540 -46.930  1.00 79.36           N  
ANISOU 1992  N   LYS B 342     8775  11809   9568   4327   -537  -2532       N  
ATOM   1993  CA  LYS B 342     -52.727  44.769 -46.873  1.00 85.32           C  
ANISOU 1993  CA  LYS B 342     9136  12822  10460   4603   -536  -2667       C  
ATOM   1994  C   LYS B 342     -53.177  45.085 -45.455  1.00 90.60           C  
ANISOU 1994  C   LYS B 342     9663  13696  11063   4624   -221  -3037       C  
ATOM   1995  O   LYS B 342     -54.018  45.967 -45.243  1.00 94.35           O  
ANISOU 1995  O   LYS B 342    10079  14071  11699   5013   -230  -3254       O  
ATOM   1996  CB  LYS B 342     -53.479  43.550 -47.405  1.00 84.64           C  
ANISOU 1996  CB  LYS B 342     8535  13265  10360   4356   -551  -2495       C  
ATOM   1997  CG  LYS B 342     -53.329  43.311 -48.898  1.00 84.66           C  
ANISOU 1997  CG  LYS B 342     8626  13138  10405   4373   -895  -2177       C  
ATOM   1998  CD  LYS B 342     -53.648  41.863 -49.248  1.00 83.25           C  
ANISOU 1998  CD  LYS B 342     8033  13424  10174   3930   -848  -2060       C  
ATOM   1999  CE  LYS B 342     -54.821  41.339 -48.428  1.00 86.81           C  
ANISOU 1999  CE  LYS B 342     7968  14336  10679   3805   -596  -2260       C  
ATOM   2000  NZ  LYS B 342     -55.087  39.897 -48.684  1.00 85.15           N  
ANISOU 2000  NZ  LYS B 342     7419  14460  10475   3314   -523  -2148       N  
ATOM   2001  N   ALA B 343     -52.620  44.382 -44.468  1.00 90.99           N  
ANISOU 2001  N   ALA B 343     9668  14048  10856   4212     59  -3094       N  
ATOM   2002  CA  ALA B 343     -52.991  44.570 -43.071  1.00 95.90           C  
ANISOU 2002  CA  ALA B 343    10172  14947  11320   4167    369  -3399       C  
ATOM   2003  C   ALA B 343     -52.572  45.925 -42.513  1.00 99.97           C  
ANISOU 2003  C   ALA B 343    11133  14983  11869   4433    357  -3739       C  
ATOM   2004  O   ALA B 343     -52.823  46.187 -41.331  1.00103.79           O  
ANISOU 2004  O   ALA B 343    11562  15681  12192   4414    605  -4037       O  
ATOM   2005  CB  ALA B 343     -52.387  43.452 -42.219  1.00 92.50           C  
ANISOU 2005  CB  ALA B 343     9653  14934  10558   3625    626  -3272       C  
ATOM   2006  N   LEU B 344     -51.951  46.783 -43.315  1.00 99.79           N  
ANISOU 2006  N   LEU B 344    11567  14297  12050   4653     83  -3693       N  
ATOM   2007  CA  LEU B 344     -51.527  48.098 -42.853  1.00106.33           C  
ANISOU 2007  CA  LEU B 344    12867  14545  12988   4848     55  -4010       C  
ATOM   2008  C   LEU B 344     -52.512  49.176 -43.294  1.00115.46           C  
ANISOU 2008  C   LEU B 344    14020  15343  14507   5410    -79  -4114       C  
ATOM   2009  O   LEU B 344     -52.456  50.316 -42.830  1.00122.05           O  
ANISOU 2009  O   LEU B 344    15165  15709  15498   5630    -59  -4423       O  
ATOM   2010  CB  LEU B 344     -50.123  48.419 -43.370  1.00103.53           C  
ANISOU 2010  CB  LEU B 344    13093  13582  12662   4652   -143  -3875       C  
ATOM   2011  CG  LEU B 344     -49.063  47.350 -43.100  1.00 98.78           C  
ANISOU 2011  CG  LEU B 344    12506  13308  11719   4116    -54  -3734       C  
ATOM   2012  CD1 LEU B 344     -47.689  47.828 -43.542  1.00 97.26           C  
ANISOU 2012  CD1 LEU B 344    12887  12471  11596   3788   -251  -3552       C  
ATOM   2013  CD2 LEU B 344     -49.052  46.957 -41.629  1.00100.48           C  
ANISOU 2013  CD2 LEU B 344    12527  14069  11583   3818    244  -3983       C  
TER    2014      LEU B 344                                                      
ATOM   2015  N   SER C 226     -35.408  38.243-101.341  1.00112.31           N  
ANISOU 2015  N   SER C 226    19231  14235   9207   1249  -4501   -242       N  
ATOM   2016  CA  SER C 226     -36.309  37.601-100.390  1.00110.46           C  
ANISOU 2016  CA  SER C 226    18635  13868   9466   1166  -4859   -174       C  
ATOM   2017  C   SER C 226     -35.528  36.986 -99.234  1.00102.44           C  
ANISOU 2017  C   SER C 226    17645  12482   8798   1262  -4566   -433       C  
ATOM   2018  O   SER C 226     -36.060  36.800 -98.138  1.00 98.75           O  
ANISOU 2018  O   SER C 226    16784  11915   8821   1314  -4698   -251       O  
ATOM   2019  CB  SER C 226     -37.152  36.529-101.088  1.00117.86           C  
ANISOU 2019  CB  SER C 226    19577  14898  10305    789  -5438   -379       C  
ATOM   2020  OG  SER C 226     -38.233  37.107-101.800  1.00123.60           O  
ANISOU 2020  OG  SER C 226    20058  16031  10871    694  -5809     28       O  
ATOM   2021  N   GLU C 227     -34.257  36.673 -99.487  1.00 99.07           N  
ANISOU 2021  N   GLU C 227    17611  11897   8135   1298  -4130   -806       N  
ATOM   2022  CA  GLU C 227     -33.387  36.043 -98.504  1.00 91.68           C  
ANISOU 2022  CA  GLU C 227    16704  10652   7479   1373  -3789  -1050       C  
ATOM   2023  C   GLU C 227     -32.501  37.050 -97.777  1.00 82.91           C  
ANISOU 2023  C   GLU C 227    15554   9508   6439   1638  -3236   -813       C  
ATOM   2024  O   GLU C 227     -31.519  36.656 -97.139  1.00 78.48           O  
ANISOU 2024  O   GLU C 227    15048   8760   6012   1690  -2829   -987       O  
ATOM   2025  CB  GLU C 227     -32.529  34.970 -99.177  1.00 94.47           C  
ANISOU 2025  CB  GLU C 227    17410  10847   7638   1248  -3568  -1552       C  
ATOM   2026  CG  GLU C 227     -33.337  33.871 -99.855  1.00101.40           C  
ANISOU 2026  CG  GLU C 227    18373  11677   8478    940  -4090  -1853       C  
ATOM   2027  CD  GLU C 227     -32.932  33.647-101.302  1.00108.66           C  
ANISOU 2027  CD  GLU C 227    19686  12745   8853    858  -3989  -2130       C  
ATOM   2028  OE1 GLU C 227     -33.412  32.668-101.911  1.00114.72           O  
ANISOU 2028  OE1 GLU C 227    20605  13440   9544    597  -4336  -2456       O  
ATOM   2029  OE2 GLU C 227     -32.136  34.450-101.833  1.00108.82           O  
ANISOU 2029  OE2 GLU C 227    19851  12966   8531   1043  -3578  -2011       O  
ATOM   2030  N   LYS C 228     -32.828  38.342 -97.862  1.00 79.45           N  
ANISOU 2030  N   LYS C 228    14995   9234   5959   1779  -3194   -407       N  
ATOM   2031  CA  LYS C 228     -32.023  39.350 -97.183  1.00 72.47           C  
ANISOU 2031  CA  LYS C 228    14079   8263   5192   1969  -2695   -193       C  
ATOM   2032  C   LYS C 228     -32.176  39.251 -95.672  1.00 65.15           C  
ANISOU 2032  C   LYS C 228    12856   7179   4720   2081  -2623    -91       C  
ATOM   2033  O   LYS C 228     -31.208  39.452 -94.929  1.00 60.18           O  
ANISOU 2033  O   LYS C 228    12238   6418   4209   2131  -2176   -104       O  
ATOM   2034  CB  LYS C 228     -32.411  40.747 -97.663  1.00 75.14           C  
ANISOU 2034  CB  LYS C 228    14353   8753   5444   2070  -2685    188       C  
ATOM   2035  CG  LYS C 228     -31.262  41.741 -97.676  1.00 74.25           C  
ANISOU 2035  CG  LYS C 228    14378   8568   5267   2140  -2190    300       C  
ATOM   2036  CD  LYS C 228     -30.570  41.749 -99.031  1.00 79.00           C  
ANISOU 2036  CD  LYS C 228    15240   9352   5424   2049  -2097    219       C  
ATOM   2037  CE  LYS C 228     -31.518  42.199-100.135  1.00 84.99           C  
ANISOU 2037  CE  LYS C 228    15990  10399   5903   2020  -2469    417       C  
ATOM   2038  NZ  LYS C 228     -31.893  43.635-100.008  1.00 85.78           N  
ANISOU 2038  NZ  LYS C 228    15931  10512   6150   2151  -2426    859       N  
ATOM   2039  N   ILE C 229     -33.388  38.940 -95.200  1.00 62.64           N  
ANISOU 2039  N   ILE C 229    12140   6907   4753   2078  -3005     54       N  
ATOM   2040  CA  ILE C 229     -33.635  38.851 -93.763  1.00 58.88           C  
ANISOU 2040  CA  ILE C 229    11173   6341   4857   2159  -2834    188       C  
ATOM   2041  C   ILE C 229     -32.800  37.743 -93.142  1.00 56.02           C  
ANISOU 2041  C   ILE C 229    10711   5821   4755   1999  -2562   -120       C  
ATOM   2042  O   ILE C 229     -32.353  37.859 -91.995  1.00 52.12           O  
ANISOU 2042  O   ILE C 229     9965   5261   4577   2061  -2207    -49       O  
ATOM   2043  CB  ILE C 229     -35.138  38.644 -93.489  1.00 61.14           C  
ANISOU 2043  CB  ILE C 229    10982   6772   5476   2184  -3297    467       C  
ATOM   2044  CG1 ILE C 229     -35.407  38.547 -91.987  1.00 65.26           C  
ANISOU 2044  CG1 ILE C 229    10973   7264   6557   2310  -3087    634       C  
ATOM   2045  CG2 ILE C 229     -35.652  37.401 -94.193  1.00 72.73           C  
ANISOU 2045  CG2 ILE C 229    12432   8274   6927   1879  -3789    254       C  
ATOM   2046  CD1 ILE C 229     -36.874  38.492 -91.637  1.00 68.19           C  
ANISOU 2046  CD1 ILE C 229    10739   7859   7312   2324  -3350    987       C  
ATOM   2047  N   TYR C 230     -32.554  36.666 -93.887  1.00 58.99           N  
ANISOU 2047  N   TYR C 230    11300   6128   4986   1798  -2712   -461       N  
ATOM   2048  CA  TYR C 230     -31.836  35.535 -93.313  1.00 57.22           C  
ANISOU 2048  CA  TYR C 230    10950   5713   5077   1676  -2457   -715       C  
ATOM   2049  C   TYR C 230     -30.355  35.838 -93.127  1.00 54.43           C  
ANISOU 2049  C   TYR C 230    10825   5300   4557   1748  -1861   -780       C  
ATOM   2050  O   TYR C 230     -29.735  35.314 -92.197  1.00 50.37           O  
ANISOU 2050  O   TYR C 230    10040   4694   4407   1713  -1537   -789       O  
ATOM   2051  CB  TYR C 230     -32.049  34.297 -94.182  1.00 60.78           C  
ANISOU 2051  CB  TYR C 230    11619   6035   5439   1462  -2791  -1087       C  
ATOM   2052  CG  TYR C 230     -33.507  33.914 -94.279  1.00 64.68           C  
ANISOU 2052  CG  TYR C 230    11819   6596   6159   1307  -3434   -965       C  
ATOM   2053  CD1 TYR C 230     -34.161  33.324 -93.206  1.00 64.20           C  
ANISOU 2053  CD1 TYR C 230    11153   6493   6749   1236  -3565   -769       C  
ATOM   2054  CD2 TYR C 230     -34.235  34.162 -95.435  1.00 70.40           C  
ANISOU 2054  CD2 TYR C 230    12829   7479   6441   1218  -3923   -978       C  
ATOM   2055  CE1 TYR C 230     -35.496  32.983 -93.283  1.00 68.44           C  
ANISOU 2055  CE1 TYR C 230    11358   7127   7517   1078  -4166   -567       C  
ATOM   2056  CE2 TYR C 230     -35.571  33.824 -95.521  1.00 74.71           C  
ANISOU 2056  CE2 TYR C 230    13057   8127   7200   1035  -4546   -789       C  
ATOM   2057  CZ  TYR C 230     -36.195  33.234 -94.443  1.00 73.23           C  
ANISOU 2057  CZ  TYR C 230    12253   7881   7690    965  -4665   -572       C  
ATOM   2058  OH  TYR C 230     -37.525  32.894 -94.526  1.00 77.98           O  
ANISOU 2058  OH  TYR C 230    12483   8618   8527    766  -5298   -302       O  
ATOM   2059  N   LYS C 231     -29.771  36.690 -93.975  1.00 55.59           N  
ANISOU 2059  N   LYS C 231    11418   5532   4171   1835  -1719   -758       N  
ATOM   2060  CA  LYS C 231     -28.373  37.056 -93.766  1.00 55.78           C  
ANISOU 2060  CA  LYS C 231    11599   5537   4058   1878  -1175   -715       C  
ATOM   2061  C   LYS C 231     -28.224  38.048 -92.615  1.00 52.16           C  
ANISOU 2061  C   LYS C 231    10879   5090   3849   1933   -953   -400       C  
ATOM   2062  O   LYS C 231     -27.231  38.007 -91.879  1.00 48.28           O  
ANISOU 2062  O   LYS C 231    10273   4568   3501   1879   -553   -341       O  
ATOM   2063  CB  LYS C 231     -27.769  37.614 -95.052  1.00 61.02           C  
ANISOU 2063  CB  LYS C 231    12710   6314   4162   1922  -1076   -714       C  
ATOM   2064  CG  LYS C 231     -27.445  36.538 -96.081  1.00 69.12           C  
ANISOU 2064  CG  LYS C 231    13919   7329   5013   1851  -1067  -1032       C  
ATOM   2065  CD  LYS C 231     -25.977  36.126 -96.002  1.00 70.51           C  
ANISOU 2065  CD  LYS C 231    14062   7482   5247   1858   -511  -1028       C  
ATOM   2066  CE  LYS C 231     -25.678  34.901 -96.859  1.00 74.94           C  
ANISOU 2066  CE  LYS C 231    14794   7989   5691   1840   -461  -1372       C  
ATOM   2067  NZ  LYS C 231     -25.203  35.267 -98.225  1.00 79.70           N  
ANISOU 2067  NZ  LYS C 231    15658   8796   5830   1891   -372  -1365       N  
ATOM   2068  N   VAL C 232     -29.193  38.950 -92.441  1.00 52.22           N  
ANISOU 2068  N   VAL C 232    10801   5142   3899   2043  -1203   -186       N  
ATOM   2069  CA  VAL C 232     -29.191  39.797 -91.250  1.00 45.63           C  
ANISOU 2069  CA  VAL C 232     9746   4271   3323   2119  -1008     39       C  
ATOM   2070  C   VAL C 232     -29.344  38.939 -90.001  1.00 44.20           C  
ANISOU 2070  C   VAL C 232     9062   4093   3639   2056   -927      5       C  
ATOM   2071  O   VAL C 232     -28.642  39.140 -89.001  1.00 42.53           O  
ANISOU 2071  O   VAL C 232     8706   3876   3579   2005   -598     75       O  
ATOM   2072  CB  VAL C 232     -30.291  40.871 -91.342  1.00 47.46           C  
ANISOU 2072  CB  VAL C 232     9991   4518   3524   2324  -1266    275       C  
ATOM   2073  CG1 VAL C 232     -30.363  41.685 -90.040  1.00 48.12           C  
ANISOU 2073  CG1 VAL C 232     9816   4554   3912   2391  -1013    398       C  
ATOM   2074  CG2 VAL C 232     -30.049  41.777 -92.536  1.00 50.26           C  
ANISOU 2074  CG2 VAL C 232    10693   4897   3506   2317  -1265    332       C  
ATOM   2075  N   MET C 233     -30.248  37.955 -90.046  1.00 44.26           N  
ANISOU 2075  N   MET C 233     8782   4131   3903   2025  -1246    -73       N  
ATOM   2076  CA  MET C 233     -30.399  37.045 -88.916  1.00 42.89           C  
ANISOU 2076  CA  MET C 233     8087   3979   4231   1955  -1185    -53       C  
ATOM   2077  C   MET C 233     -29.124  36.248 -88.683  1.00 41.54           C  
ANISOU 2077  C   MET C 233     7911   3735   4138   1798   -816   -192       C  
ATOM   2078  O   MET C 233     -28.735  36.015 -87.535  1.00 38.87           O  
ANISOU 2078  O   MET C 233     7205   3458   4107   1750   -563    -76       O  
ATOM   2079  CB  MET C 233     -31.579  36.101 -89.142  1.00 46.18           C  
ANISOU 2079  CB  MET C 233     8210   4412   4924   1901  -1645    -70       C  
ATOM   2080  CG  MET C 233     -32.938  36.751 -88.957  1.00 50.65           C  
ANISOU 2080  CG  MET C 233     8534   5128   5582   2077  -1969    214       C  
ATOM   2081  SD  MET C 233     -34.277  35.736 -89.615  1.00 56.15           S  
ANISOU 2081  SD  MET C 233     8982   5869   6482   1928  -2620    244       S  
ATOM   2082  CE  MET C 233     -34.034  34.197 -88.735  1.00 55.43           C  
ANISOU 2082  CE  MET C 233     8417   5674   6971   1712  -2557    159       C  
ATOM   2083  N   GLU C 234     -28.459  35.823 -89.761  1.00 43.18           N  
ANISOU 2083  N   GLU C 234     8512   3843   4050   1739   -761   -412       N  
ATOM   2084  CA  GLU C 234     -27.203  35.097 -89.605  1.00 44.41           C  
ANISOU 2084  CA  GLU C 234     8666   3936   4273   1653   -352   -491       C  
ATOM   2085  C   GLU C 234     -26.186  35.928 -88.828  1.00 42.51           C  
ANISOU 2085  C   GLU C 234     8374   3806   3972   1626     60   -252       C  
ATOM   2086  O   GLU C 234     -25.559  35.435 -87.884  1.00 42.06           O  
ANISOU 2086  O   GLU C 234     7963   3797   4219   1533    339   -135       O  
ATOM   2087  CB  GLU C 234     -26.645  34.695 -90.973  1.00 47.30           C  
ANISOU 2087  CB  GLU C 234     9538   4206   4228   1675   -309   -754       C  
ATOM   2088  CG  GLU C 234     -25.354  33.882 -90.891  1.00 47.49           C  
ANISOU 2088  CG  GLU C 234     9558   4156   4329   1659    162   -804       C  
ATOM   2089  CD  GLU C 234     -24.645  33.744 -92.226  1.00 52.35           C  
ANISOU 2089  CD  GLU C 234    10725   4740   4426   1761    323  -1015       C  
ATOM   2090  OE1 GLU C 234     -24.303  32.608 -92.610  1.00 54.45           O  
ANISOU 2090  OE1 GLU C 234    11028   4862   4798   1769    442  -1232       O  
ATOM   2091  OE2 GLU C 234     -24.430  34.774 -92.900  1.00 55.95           O  
ANISOU 2091  OE2 GLU C 234    11456   5366   4438   1797    323   -887       O  
ATOM   2092  N   GLU C 235     -26.028  37.202 -89.202  1.00 42.76           N  
ANISOU 2092  N   GLU C 235     8745   3879   3623   1679     75   -146       N  
ATOM   2093  CA  GLU C 235     -25.064  38.070 -88.529  1.00 42.43           C  
ANISOU 2093  CA  GLU C 235     8719   3902   3501   1590    401     77       C  
ATOM   2094  C   GLU C 235     -25.382  38.208 -87.047  1.00 40.42           C  
ANISOU 2094  C   GLU C 235     8037   3723   3599   1540    438    204       C  
ATOM   2095  O   GLU C 235     -24.475  38.249 -86.209  1.00 38.49           O  
ANISOU 2095  O   GLU C 235     7616   3573   3435   1378    729    354       O  
ATOM   2096  CB  GLU C 235     -25.043  39.452 -89.184  1.00 46.57           C  
ANISOU 2096  CB  GLU C 235     9686   4390   3620   1650    334    180       C  
ATOM   2097  CG  GLU C 235     -24.377  39.502 -90.555  1.00 54.75           C  
ANISOU 2097  CG  GLU C 235    11073   5438   4291   1657    401    150       C  
ATOM   2098  CD  GLU C 235     -24.272  40.918 -91.094  1.00 59.63           C  
ANISOU 2098  CD  GLU C 235    11807   6027   4821   1623    344    276       C  
ATOM   2099  OE1 GLU C 235     -23.497  41.718 -90.526  1.00 59.12           O  
ANISOU 2099  OE1 GLU C 235    11606   5964   4892   1451    523    408       O  
ATOM   2100  OE2 GLU C 235     -24.963  41.231 -92.087  1.00 63.13           O  
ANISOU 2100  OE2 GLU C 235    12464   6469   5053   1745    100    236       O  
ATOM   2101  N   ILE C 236     -26.669  38.280 -86.706  1.00 38.25           N  
ANISOU 2101  N   ILE C 236     7570   3451   3511   1679    145    180       N  
ATOM   2102  CA  ILE C 236     -27.054  38.475 -85.314  1.00 35.14           C  
ANISOU 2102  CA  ILE C 236     6789   3176   3388   1694    198    304       C  
ATOM   2103  C   ILE C 236     -26.876  37.183 -84.522  1.00 34.44           C  
ANISOU 2103  C   ILE C 236     6160   3215   3710   1578    305    347       C  
ATOM   2104  O   ILE C 236     -26.274  37.179 -83.440  1.00 33.80           O  
ANISOU 2104  O   ILE C 236     5808   3290   3742   1451    551    486       O  
ATOM   2105  CB  ILE C 236     -28.497  39.008 -85.232  1.00 36.17           C  
ANISOU 2105  CB  ILE C 236     6859   3306   3577   1945   -103    337       C  
ATOM   2106  CG1 ILE C 236     -28.558  40.417 -85.828  1.00 36.58           C  
ANISOU 2106  CG1 ILE C 236     7421   3210   3267   2071   -140    362       C  
ATOM   2107  CG2 ILE C 236     -28.992  39.013 -83.770  1.00 34.65           C  
ANISOU 2107  CG2 ILE C 236     6208   3293   3665   2021    -24    463       C  
ATOM   2108  CD1 ILE C 236     -29.946  40.994 -85.906  1.00 39.66           C  
ANISOU 2108  CD1 ILE C 236     7696   3652   3721   2289   -384    418       C  
ATOM   2109  N   PHE C 237     -27.388  36.064 -85.045  1.00 32.23           N  
ANISOU 2109  N   PHE C 237     5719   2866   3662   1594    104    246       N  
ATOM   2110  CA  PHE C 237     -27.443  34.845 -84.243  1.00 32.52           C  
ANISOU 2110  CA  PHE C 237     5192   2982   4182   1507    151    335       C  
ATOM   2111  C   PHE C 237     -26.080  34.191 -84.053  1.00 33.71           C  
ANISOU 2111  C   PHE C 237     5257   3137   4414   1343    535    390       C  
ATOM   2112  O   PHE C 237     -25.894  33.470 -83.068  1.00 34.26           O  
ANISOU 2112  O   PHE C 237     4809   3345   4865   1255    677    576       O  
ATOM   2113  CB  PHE C 237     -28.415  33.835 -84.858  1.00 35.76           C  
ANISOU 2113  CB  PHE C 237     5477   3251   4861   1530   -222    219       C  
ATOM   2114  CG  PHE C 237     -29.849  34.284 -84.835  1.00 37.63           C  
ANISOU 2114  CG  PHE C 237     5592   3568   5138   1677   -611    301       C  
ATOM   2115  CD1 PHE C 237     -30.289  35.201 -83.890  1.00 37.32           C  
ANISOU 2115  CD1 PHE C 237     5362   3742   5078   1829   -541    503       C  
ATOM   2116  CD2 PHE C 237     -30.758  33.792 -85.753  1.00 41.88           C  
ANISOU 2116  CD2 PHE C 237     6211   3981   5722   1669  -1043    194       C  
ATOM   2117  CE1 PHE C 237     -31.605  35.623 -83.868  1.00 39.96           C  
ANISOU 2117  CE1 PHE C 237     5552   4169   5461   2029   -845    640       C  
ATOM   2118  CE2 PHE C 237     -32.083  34.213 -85.740  1.00 44.78           C  
ANISOU 2118  CE2 PHE C 237     6402   4473   6141   1804  -1405    366       C  
ATOM   2119  CZ  PHE C 237     -32.505  35.126 -84.792  1.00 44.72           C  
ANISOU 2119  CZ  PHE C 237     6165   4686   6141   2014  -1279    613       C  
ATOM   2120  N   VAL C 238     -25.126  34.417 -84.962  1.00 42.48           N  
ANISOU 2120  N   VAL C 238     8364   5082   2693    277     70   -192       N  
ATOM   2121  CA  VAL C 238     -23.782  33.874 -84.763  1.00 41.74           C  
ANISOU 2121  CA  VAL C 238     8317   4590   2952    172    460   -220       C  
ATOM   2122  C   VAL C 238     -22.952  34.692 -83.787  1.00 40.32           C  
ANISOU 2122  C   VAL C 238     7971   4191   3156    274    622     12       C  
ATOM   2123  O   VAL C 238     -21.880  34.236 -83.369  1.00 41.30           O  
ANISOU 2123  O   VAL C 238     8012   4032   3647    198    876      2       O  
ATOM   2124  CB  VAL C 238     -23.000  33.773 -86.084  1.00 42.49           C  
ANISOU 2124  CB  VAL C 238     8825   4541   2779    193    778   -296       C  
ATOM   2125  CG1 VAL C 238     -23.776  32.954 -87.105  1.00 44.65           C  
ANISOU 2125  CG1 VAL C 238     9277   5077   2611     62    617   -600       C  
ATOM   2126  CG2 VAL C 238     -22.672  35.167 -86.619  1.00 43.36           C  
ANISOU 2126  CG2 VAL C 238     9180   4632   2662    467    925    -29       C  
ATOM   2127  N   ASP C 239     -23.404  35.883 -83.418  1.00 37.51           N  
ANISOU 2127  N   ASP C 239     7543   3962   2745    441    494    200       N  
ATOM   2128  CA  ASP C 239     -22.595  36.773 -82.600  1.00 37.71           C  
ANISOU 2128  CA  ASP C 239     7427   3789   3112    510    683    346       C  
ATOM   2129  C   ASP C 239     -22.590  36.303 -81.151  1.00 35.61           C  
ANISOU 2129  C   ASP C 239     6786   3540   3204    385    541    315       C  
ATOM   2130  O   ASP C 239     -23.586  35.773 -80.649  1.00 34.80           O  
ANISOU 2130  O   ASP C 239     6526   3637   3059    316    266    270       O  
ATOM   2131  CB  ASP C 239     -23.122  38.204 -82.689  1.00 39.66           C  
ANISOU 2131  CB  ASP C 239     7729   4127   3212    721    661    539       C  
ATOM   2132  CG  ASP C 239     -22.194  39.208 -82.046  1.00 39.97           C  
ANISOU 2132  CG  ASP C 239     7661   3914   3612    761    951    617       C  
ATOM   2133  OD1 ASP C 239     -22.274  39.389 -80.813  1.00 38.73           O  
ANISOU 2133  OD1 ASP C 239     7192   3800   3722    684    836    587       O  
ATOM   2134  OD2 ASP C 239     -21.380  39.815 -82.774  1.00 41.73           O  
ANISOU 2134  OD2 ASP C 239     8111   3895   3851    858   1319    682       O  
ATOM   2135  N   ARG C 240     -21.453  36.494 -80.480  1.00 34.29           N  
ANISOU 2135  N   ARG C 240     6467   3176   3384    364    739    337       N  
ATOM   2136  CA  ARG C 240     -21.342  36.030 -79.102  1.00 35.89           C  
ANISOU 2136  CA  ARG C 240     6335   3444   3857    284    600    335       C  
ATOM   2137  C   ARG C 240     -22.293  36.766 -78.169  1.00 31.53           C  
ANISOU 2137  C   ARG C 240     5611   3113   3255    314    365    387       C  
ATOM   2138  O   ARG C 240     -22.662  36.218 -77.129  1.00 32.92           O  
ANISOU 2138  O   ARG C 240     5574   3415   3519    254    195    393       O  
ATOM   2139  CB  ARG C 240     -19.900  36.166 -78.606  1.00 38.71           C  
ANISOU 2139  CB  ARG C 240     6523   3620   4565    275    813    329       C  
ATOM   2140  CG  ARG C 240     -19.376  37.588 -78.541  1.00 42.79           C  
ANISOU 2140  CG  ARG C 240     7014   4055   5188    332    981    322       C  
ATOM   2141  CD  ARG C 240     -17.965  37.615 -77.961  1.00 45.40           C  
ANISOU 2141  CD  ARG C 240     7082   4258   5908    288   1143    249       C  
ATOM   2142  NE  ARG C 240     -17.502  38.976 -77.715  1.00 47.83           N  
ANISOU 2142  NE  ARG C 240     7293   4492   6388    289   1316    166       N  
ATOM   2143  CZ  ARG C 240     -17.754  39.657 -76.601  1.00 47.32           C  
ANISOU 2143  CZ  ARG C 240     6985   4616   6379    246   1159     93       C  
ATOM   2144  NH1 ARG C 240     -18.466  39.103 -75.629  1.00 45.90           N  
ANISOU 2144  NH1 ARG C 240     6657   4721   6061    223    821    133       N  
ATOM   2145  NH2 ARG C 240     -17.297  40.893 -76.461  1.00 48.81           N  
ANISOU 2145  NH2 ARG C 240     7089   4685   6772    214   1390    -38       N  
ATOM   2146  N   HIS C 241     -22.724  37.976 -78.530  1.00 29.42           N  
ANISOU 2146  N   HIS C 241     5449   2874   2856    423    395    445       N  
ATOM   2147  CA  HIS C 241     -23.668  38.712 -77.695  1.00 29.12           C  
ANISOU 2147  CA  HIS C 241     5252   3005   2805    455    227    490       C  
ATOM   2148  C   HIS C 241     -25.071  38.114 -77.713  1.00 29.46           C  
ANISOU 2148  C   HIS C 241     5262   3270   2662    442    -62    496       C  
ATOM   2149  O   HIS C 241     -25.838  38.347 -76.774  1.00 29.79           O  
ANISOU 2149  O   HIS C 241     5116   3442   2762    425   -200    512       O  
ATOM   2150  CB  HIS C 241     -23.740  40.175 -78.132  1.00 33.25           C  
ANISOU 2150  CB  HIS C 241     5895   3442   3298    603    412    580       C  
ATOM   2151  CG  HIS C 241     -22.482  40.952 -77.888  1.00 35.73           C  
ANISOU 2151  CG  HIS C 241     6164   3522   3891    579    735    519       C  
ATOM   2152  ND1 HIS C 241     -21.460  41.022 -78.807  1.00 37.47           N  
ANISOU 2152  ND1 HIS C 241     6572   3499   4168    612   1036    517       N  
ATOM   2153  CD2 HIS C 241     -22.095  41.717 -76.838  1.00 36.27           C  
ANISOU 2153  CD2 HIS C 241     6005   3562   4214    506    825    416       C  
ATOM   2154  CE1 HIS C 241     -20.491  41.786 -78.333  1.00 38.09           C  
ANISOU 2154  CE1 HIS C 241     6507   3394   4572    557   1300    413       C  
ATOM   2155  NE2 HIS C 241     -20.851  42.219 -77.139  1.00 37.23           N  
ANISOU 2155  NE2 HIS C 241     6141   3432   4575    483   1162    331       N  
ATOM   2156  N   TYR C 242     -25.438  37.359 -78.749  1.00 29.71           N  
ANISOU 2156  N   TYR C 242     5455   3349   2483    430   -138    446       N  
ATOM   2157  CA  TYR C 242     -26.787  36.810 -78.810  1.00 29.91           C  
ANISOU 2157  CA  TYR C 242     5392   3599   2372    389   -413    387       C  
ATOM   2158  C   TYR C 242     -26.894  35.590 -77.906  1.00 32.56           C  
ANISOU 2158  C   TYR C 242     5535   3916   2918    214   -460    293       C  
ATOM   2159  O   TYR C 242     -26.105  34.649 -78.023  1.00 33.10           O  
ANISOU 2159  O   TYR C 242     5653   3831   3093    122   -318    230       O  
ATOM   2160  CB  TYR C 242     -27.179  36.458 -80.250  1.00 33.52           C  
ANISOU 2160  CB  TYR C 242     6068   4172   2497    419   -499    304       C  
ATOM   2161  CG  TYR C 242     -28.614  35.993 -80.342  1.00 36.13           C  
ANISOU 2161  CG  TYR C 242     6238   4779   2710    365   -815    189       C  
ATOM   2162  CD1 TYR C 242     -29.649  36.917 -80.438  1.00 37.69           C  
ANISOU 2162  CD1 TYR C 242     6346   5201   2773    537  -1017    310       C  
ATOM   2163  CD2 TYR C 242     -28.940  34.641 -80.333  1.00 32.01           C  
ANISOU 2163  CD2 TYR C 242     5624   4272   2266    145   -875    -48       C  
ATOM   2164  CE1 TYR C 242     -30.971  36.509 -80.503  1.00 40.01           C  
ANISOU 2164  CE1 TYR C 242     6425   5765   3014    488  -1319    184       C  
ATOM   2165  CE2 TYR C 242     -30.266  34.223 -80.397  1.00 40.48           C  
ANISOU 2165  CE2 TYR C 242     6496   5587   3298     64  -1142   -209       C  
ATOM   2166  CZ  TYR C 242     -31.275  35.165 -80.484  1.00 40.94           C  
ANISOU 2166  CZ  TYR C 242     6432   5903   3220    235  -1386    -99       C  
ATOM   2167  OH  TYR C 242     -32.590  34.770 -80.559  1.00 42.76           O  
ANISOU 2167  OH  TYR C 242     6403   6391   3452    156  -1664   -278       O  
ATOM   2168  N   LYS C 243     -27.871  35.611 -77.002  1.00 31.82           N  
ANISOU 2168  N   LYS C 243     5229   3951   2910    187   -608    308       N  
ATOM   2169  CA  LYS C 243     -28.052  34.580 -75.985  1.00 33.23           C  
ANISOU 2169  CA  LYS C 243     5236   4095   3296     61   -595    279       C  
ATOM   2170  C   LYS C 243     -29.335  33.813 -76.288  1.00 36.32           C  
ANISOU 2170  C   LYS C 243     5529   4591   3678    -47   -738    130       C  
ATOM   2171  O   LYS C 243     -30.424  34.210 -75.867  1.00 39.01           O  
ANISOU 2171  O   LYS C 243     5707   5072   4042    -31   -875    136       O  
ATOM   2172  CB  LYS C 243     -28.110  35.196 -74.578  1.00 33.04           C  
ANISOU 2172  CB  LYS C 243     5050   4117   3387    100   -589    395       C  
ATOM   2173  CG  LYS C 243     -26.939  36.093 -74.243  1.00 34.05           C  
ANISOU 2173  CG  LYS C 243     5211   4187   3539    173   -472    461       C  
ATOM   2174  CD  LYS C 243     -25.642  35.319 -74.270  1.00 36.87           C  
ANISOU 2174  CD  LYS C 243     5601   4410   4000    147   -340    469       C  
ATOM   2175  CE  LYS C 243     -24.465  36.199 -73.881  1.00 39.81           C  
ANISOU 2175  CE  LYS C 243     5929   4751   4448    194   -239    480       C  
ATOM   2176  NZ  LYS C 243     -23.202  35.412 -73.766  1.00 41.60           N  
ANISOU 2176  NZ  LYS C 243     6106   4876   4825    190   -134    506       N  
ATOM   2177  N   GLU C 244     -29.195  32.686 -76.995  1.00 36.00           N  
ANISOU 2177  N   GLU C 244     5562   4466   3651   -177   -672    -38       N  
ATOM   2178  CA  GLU C 244     -30.361  31.917 -77.416  1.00 38.37           C  
ANISOU 2178  CA  GLU C 244     5745   4868   3966   -329   -790   -275       C  
ATOM   2179  C   GLU C 244     -31.143  31.325 -76.246  1.00 38.83           C  
ANISOU 2179  C   GLU C 244     5560   4873   4321   -422   -735   -270       C  
ATOM   2180  O   GLU C 244     -32.328  31.009 -76.405  1.00 40.78           O  
ANISOU 2180  O   GLU C 244     5627   5234   4634   -533   -856   -461       O  
ATOM   2181  CB  GLU C 244     -29.932  30.799 -78.371  1.00 42.47           C  
ANISOU 2181  CB  GLU C 244     6405   5261   4472   -488   -652   -511       C  
ATOM   2182  CG  GLU C 244     -28.998  29.767 -77.765  1.00 43.33           C  
ANISOU 2182  CG  GLU C 244     6535   5044   4884   -556   -319   -444       C  
ATOM   2183  CD  GLU C 244     -27.531  30.046 -78.059  1.00 46.01           C  
ANISOU 2183  CD  GLU C 244     7076   5230   5176   -444   -152   -298       C  
ATOM   2184  OE1 GLU C 244     -27.144  31.230 -78.178  1.00 45.74           O  
ANISOU 2184  OE1 GLU C 244     7122   5298   4958   -288   -251   -159       O  
ATOM   2185  OE2 GLU C 244     -26.759  29.069 -78.181  1.00 49.40           O  
ANISOU 2185  OE2 GLU C 244     7567   5402   5799   -513    123   -329       O  
ATOM   2186  N   ASN C 245     -30.526  31.168 -75.076  1.00 38.03           N  
ANISOU 2186  N   ASN C 245     5439   4619   4392   -372   -550    -59       N  
ATOM   2187  CA  ASN C 245     -31.180  30.510 -73.953  1.00 40.31           C  
ANISOU 2187  CA  ASN C 245     5556   4826   4933   -435   -422    -12       C  
ATOM   2188  C   ASN C 245     -31.830  31.488 -72.978  1.00 41.31           C  
ANISOU 2188  C   ASN C 245     5560   5097   5037   -340   -521    126       C  
ATOM   2189  O   ASN C 245     -32.320  31.061 -71.930  1.00 40.91           O  
ANISOU 2189  O   ASN C 245     5403   4980   5162   -366   -379    203       O  
ATOM   2190  CB  ASN C 245     -30.180  29.623 -73.209  1.00 42.13           C  
ANISOU 2190  CB  ASN C 245     5846   4832   5331   -402   -142    172       C  
ATOM   2191  CG  ASN C 245     -29.722  28.436 -74.038  1.00 45.02           C  
ANISOU 2191  CG  ASN C 245     6297   4971   5839   -523     63     23       C  
ATOM   2192  OD1 ASN C 245     -28.522  28.206 -74.204  1.00 46.05           O  
ANISOU 2192  OD1 ASN C 245     6547   4972   5978   -449    195    134       O  
ATOM   2193  ND2 ASN C 245     -30.677  27.677 -74.564  1.00 47.23           N  
ANISOU 2193  ND2 ASN C 245     6491   5192   6262   -725    114   -263       N  
ATOM   2194  N   ILE C 246     -31.860  32.776 -73.297  1.00 41.82           N  
ANISOU 2194  N   ILE C 246     5655   5327   4908   -226   -704    163       N  
ATOM   2195  CA  ILE C 246     -32.400  33.793 -72.402  1.00 43.23           C  
ANISOU 2195  CA  ILE C 246     5732   5604   5090   -140   -740    275       C  
ATOM   2196  C   ILE C 246     -33.705  34.285 -73.012  1.00 49.41           C  
ANISOU 2196  C   ILE C 246     6357   6535   5879   -134   -931    165       C  
ATOM   2197  O   ILE C 246     -33.707  35.118 -73.925  1.00 50.23           O  
ANISOU 2197  O   ILE C 246     6520   6761   5805    -21  -1088    172       O  
ATOM   2198  CB  ILE C 246     -31.405  34.936 -72.175  1.00 38.62           C  
ANISOU 2198  CB  ILE C 246     5267   5047   4358    -11   -726    403       C  
ATOM   2199  CG1 ILE C 246     -30.196  34.424 -71.394  1.00 37.93           C  
ANISOU 2199  CG1 ILE C 246     5246   4880   4286     -8   -583    503       C  
ATOM   2200  CG2 ILE C 246     -32.063  36.075 -71.422  1.00 36.58           C  
ANISOU 2200  CG2 ILE C 246     4910   4871   4118     54   -727    457       C  
ATOM   2201  CD1 ILE C 246     -29.190  35.487 -71.072  1.00 36.05           C  
ANISOU 2201  CD1 ILE C 246     5059   4686   3951     74   -565    553       C  
ATOM   2202  N   ARG C 247     -34.831  33.787 -72.512  1.00 56.83           N  
ANISOU 2202  N   ARG C 247     7083   7470   7039   -231   -902     81       N  
ATOM   2203  CA  ARG C 247     -36.122  34.164 -73.088  1.00 61.75           C  
ANISOU 2203  CA  ARG C 247     7478   8265   7720   -223  -1111    -42       C  
ATOM   2204  C   ARG C 247     -37.062  35.035 -72.249  1.00 60.49           C  
ANISOU 2204  C   ARG C 247     7126   8141   7717   -144  -1080     55       C  
ATOM   2205  O   ARG C 247     -37.758  35.889 -72.797  1.00 63.94           O  
ANISOU 2205  O   ARG C 247     7427   8741   8124    -17  -1269     72       O  
ATOM   2206  CB  ARG C 247     -36.872  32.909 -73.552  1.00 67.97           C  
ANISOU 2206  CB  ARG C 247     8084   9046   8697   -433  -1137   -326       C  
ATOM   2207  CG  ARG C 247     -36.405  32.366 -74.892  1.00 74.04           C  
ANISOU 2207  CG  ARG C 247     8975   9895   9262   -502  -1279   -522       C  
ATOM   2208  CD  ARG C 247     -37.141  33.031 -76.044  1.00 80.48           C  
ANISOU 2208  CD  ARG C 247     9671  11050   9858   -408  -1650   -632       C  
ATOM   2209  NE  ARG C 247     -37.369  32.108 -77.152  1.00 87.16           N  
ANISOU 2209  NE  ARG C 247    10473  12027  10617   -589  -1794   -990       N  
ATOM   2210  CZ  ARG C 247     -38.543  31.551 -77.431  1.00 93.63           C  
ANISOU 2210  CZ  ARG C 247    10950  13008  11617   -759  -1949  -1317       C  
ATOM   2211  NH1 ARG C 247     -39.602  31.822 -76.680  1.00 95.26           N  
ANISOU 2211  NH1 ARG C 247    10826  13234  12135   -751  -1962  -1293       N  
ATOM   2212  NH2 ARG C 247     -38.660  30.722 -78.459  1.00 98.07           N  
ANISOU 2212  NH2 ARG C 247    11485  13709  12068   -957  -2071  -1706       N  
ATOM   2213  N   THR C 248     -37.093  34.832 -70.936  1.00 52.05           N  
ANISOU 2213  N   THR C 248     6051   6923   6802   -194   -825    137       N  
ATOM   2214  CA  THR C 248     -38.007  35.598 -70.109  1.00 46.72           C  
ANISOU 2214  CA  THR C 248     5210   6249   6293   -144   -733    199       C  
ATOM   2215  C   THR C 248     -37.287  36.738 -69.395  1.00 40.59           C  
ANISOU 2215  C   THR C 248     4610   5458   5356    -23   -617    365       C  
ATOM   2216  O   THR C 248     -36.057  36.799 -69.338  1.00 36.17           O  
ANISOU 2216  O   THR C 248     4272   4884   4586     -1   -592    425       O  
ATOM   2217  CB  THR C 248     -38.672  34.684 -69.084  1.00 43.77           C  
ANISOU 2217  CB  THR C 248     4720   5718   6194   -285   -472    157       C  
ATOM   2218  OG1 THR C 248     -37.679  34.234 -68.154  1.00 37.49           O  
ANISOU 2218  OG1 THR C 248     4169   4812   5263   -291   -249    298       O  
ATOM   2219  CG2 THR C 248     -39.294  33.477 -69.773  1.00 44.28           C  
ANISOU 2219  CG2 THR C 248     4597   5748   6481   -454   -519    -73       C  
ATOM   2220  N   GLY C 249     -38.083  37.650 -68.834  1.00 39.02           N  
ANISOU 2220  N   GLY C 249     4279   5252   5297     38   -521    406       N  
ATOM   2221  CA  GLY C 249     -37.509  38.730 -68.049  1.00 36.10           C  
ANISOU 2221  CA  GLY C 249     4051   4847   4819    103   -348    488       C  
ATOM   2222  C   GLY C 249     -36.786  38.226 -66.813  1.00 34.63           C  
ANISOU 2222  C   GLY C 249     4032   4625   4502      9   -153    504       C  
ATOM   2223  O   GLY C 249     -35.764  38.785 -66.407  1.00 33.41           O  
ANISOU 2223  O   GLY C 249     4039   4508   4146     27   -104    515       O  
ATOM   2224  N   GLU C 250     -37.299  37.156 -66.205  1.00 35.12           N  
ANISOU 2224  N   GLU C 250     4043   4624   4676    -82    -30    505       N  
ATOM   2225  CA  GLU C 250     -36.602  36.565 -65.065  1.00 36.37           C  
ANISOU 2225  CA  GLU C 250     4380   4783   4656   -111    148    588       C  
ATOM   2226  C   GLU C 250     -35.240  36.026 -65.481  1.00 34.04           C  
ANISOU 2226  C   GLU C 250     4241   4543   4149    -84     12    640       C  
ATOM   2227  O   GLU C 250     -34.255  36.171 -64.748  1.00 32.90           O  
ANISOU 2227  O   GLU C 250     4236   4501   3762    -47     44    702       O  
ATOM   2228  CB  GLU C 250     -37.448  35.454 -64.443  1.00 40.08           C  
ANISOU 2228  CB  GLU C 250     4782   5119   5326   -182    375    625       C  
ATOM   2229  CG  GLU C 250     -36.739  34.679 -63.333  1.00 42.16           C  
ANISOU 2229  CG  GLU C 250     5254   5391   5374   -151    572    792       C  
ATOM   2230  CD  GLU C 250     -36.374  35.555 -62.141  1.00 43.22           C  
ANISOU 2230  CD  GLU C 250     5532   5680   5209   -104    678    828       C  
ATOM   2231  OE1 GLU C 250     -37.113  36.521 -61.862  1.00 42.87           O  
ANISOU 2231  OE1 GLU C 250     5413   5621   5256   -136    771    725       O  
ATOM   2232  OE2 GLU C 250     -35.346  35.278 -61.484  1.00 43.17           O  
ANISOU 2232  OE2 GLU C 250     5698   5825   4880    -33    669    945       O  
ATOM   2233  N   GLU C 251     -35.159  35.415 -66.668  1.00 32.30           N  
ANISOU 2233  N   GLU C 251     3981   4274   4015   -105   -143    593       N  
ATOM   2234  CA  GLU C 251     -33.872  34.900 -67.128  1.00 31.28           C  
ANISOU 2234  CA  GLU C 251     3994   4155   3736    -79   -226    638       C  
ATOM   2235  C   GLU C 251     -32.898  36.030 -67.442  1.00 28.97           C  
ANISOU 2235  C   GLU C 251     3789   3960   3260    -10   -341    619       C  
ATOM   2236  O   GLU C 251     -31.691  35.879 -67.228  1.00 28.10           O  
ANISOU 2236  O   GLU C 251     3776   3893   3010     22   -348    669       O  
ATOM   2237  CB  GLU C 251     -34.070  33.991 -68.348  1.00 32.15           C  
ANISOU 2237  CB  GLU C 251     4058   4174   3981   -147   -315    541       C  
ATOM   2238  CG  GLU C 251     -34.592  32.600 -67.994  1.00 37.33           C  
ANISOU 2238  CG  GLU C 251     4657   4669   4859   -241   -112    544       C  
ATOM   2239  CD  GLU C 251     -35.079  31.815 -69.205  1.00 43.57           C  
ANISOU 2239  CD  GLU C 251     5343   5381   5829   -371   -184    333       C  
ATOM   2240  OE1 GLU C 251     -35.086  32.376 -70.320  1.00 43.99           O  
ANISOU 2240  OE1 GLU C 251     5382   5559   5774   -362   -434    206       O  
ATOM   2241  OE2 GLU C 251     -35.468  30.639 -69.036  1.00 46.96           O  
ANISOU 2241  OE2 GLU C 251     5712   5628   6504   -482     34    282       O  
ATOM   2242  N   VAL C 252     -33.400  37.167 -67.936  1.00 28.49           N  
ANISOU 2242  N   VAL C 252     3672   3917   3235     27   -399    555       N  
ATOM   2243  CA  VAL C 252     -32.543  38.331 -68.164  1.00 26.77           C  
ANISOU 2243  CA  VAL C 252     3535   3727   2911     86   -406    530       C  
ATOM   2244  C   VAL C 252     -31.957  38.828 -66.845  1.00 27.67           C  
ANISOU 2244  C   VAL C 252     3680   3920   2913     53   -276    497       C  
ATOM   2245  O   VAL C 252     -30.748  39.075 -66.734  1.00 27.79           O  
ANISOU 2245  O   VAL C 252     3755   3991   2814     50   -289    454       O  
ATOM   2246  CB  VAL C 252     -33.325  39.441 -68.893  1.00 27.21           C  
ANISOU 2246  CB  VAL C 252     3525   3751   3064    174   -424    524       C  
ATOM   2247  CG1 VAL C 252     -32.465  40.696 -69.039  1.00 27.92           C  
ANISOU 2247  CG1 VAL C 252     3706   3794   3109    232   -318    501       C  
ATOM   2248  CG2 VAL C 252     -33.773  38.965 -70.268  1.00 28.31           C  
ANISOU 2248  CG2 VAL C 252     3639   3907   3211    225   -618    538       C  
ATOM   2249  N   LYS C 253     -32.806  38.974 -65.820  1.00 27.50           N  
ANISOU 2249  N   LYS C 253     3605   3923   2920     17   -144    490       N  
ATOM   2250  CA  LYS C 253     -32.325  39.419 -64.513  1.00 28.56           C  
ANISOU 2250  CA  LYS C 253     3786   4189   2876    -29    -25    420       C  
ATOM   2251  C   LYS C 253     -31.301  38.447 -63.943  1.00 28.79           C  
ANISOU 2251  C   LYS C 253     3884   4370   2685    -11   -102    503       C  
ATOM   2252  O   LYS C 253     -30.260  38.865 -63.426  1.00 29.80           O  
ANISOU 2252  O   LYS C 253     4028   4668   2627    -25   -143    412       O  
ATOM   2253  CB  LYS C 253     -33.487  39.568 -63.535  1.00 30.40           C  
ANISOU 2253  CB  LYS C 253     3985   4406   3160    -66    172    414       C  
ATOM   2254  CG  LYS C 253     -34.469  40.669 -63.866  1.00 34.14           C  
ANISOU 2254  CG  LYS C 253     4356   4740   3877    -59    293    344       C  
ATOM   2255  CD  LYS C 253     -35.602  40.678 -62.854  1.00 35.74           C  
ANISOU 2255  CD  LYS C 253     4513   4898   4167   -102    530    338       C  
ATOM   2256  CE  LYS C 253     -36.653  41.730 -63.182  1.00 38.30           C  
ANISOU 2256  CE  LYS C 253     4690   5060   4802    -65    674    302       C  
ATOM   2257  NZ  LYS C 253     -37.768  41.727 -62.187  1.00 40.14           N  
ANISOU 2257  NZ  LYS C 253     4865   5215   5172   -115    954    285       N  
ATOM   2258  N   GLN C 254     -31.585  37.147 -64.031  1.00 28.89           N  
ANISOU 2258  N   GLN C 254     3911   4321   2745     24   -107    670       N  
ATOM   2259  CA  GLN C 254     -30.647  36.142 -63.542  1.00 30.29           C  
ANISOU 2259  CA  GLN C 254     4146   4606   2756     97   -142    824       C  
ATOM   2260  C   GLN C 254     -29.306  36.232 -64.266  1.00 29.16           C  
ANISOU 2260  C   GLN C 254     3992   4500   2588    127   -302    787       C  
ATOM   2261  O   GLN C 254     -28.247  36.100 -63.640  1.00 30.98           O  
ANISOU 2261  O   GLN C 254     4211   4929   2630    187   -374    828       O  
ATOM   2262  CB  GLN C 254     -31.259  34.747 -63.691  1.00 30.60           C  
ANISOU 2262  CB  GLN C 254     4198   4470   2957    123    -29   1001       C  
ATOM   2263  CG  GLN C 254     -30.402  33.625 -63.103  1.00 31.34           C  
ANISOU 2263  CG  GLN C 254     4359   4629   2921    252     15   1242       C  
ATOM   2264  CD  GLN C 254     -30.188  33.770 -61.609  1.00 33.84           C  
ANISOU 2264  CD  GLN C 254     4745   5213   2901    345     71   1357       C  
ATOM   2265  OE1 GLN C 254     -31.089  34.173 -60.872  1.00 34.97           O  
ANISOU 2265  OE1 GLN C 254     4927   5380   2982    299    216   1314       O  
ATOM   2266  NE2 GLN C 254     -28.985  33.434 -61.150  1.00 35.62           N  
ANISOU 2266  NE2 GLN C 254     4979   5662   2893    488    -44   1503       N  
ATOM   2267  N   TYR C 255     -29.331  36.473 -65.581  1.00 27.60           N  
ANISOU 2267  N   TYR C 255     3786   4133   2567     98   -357    710       N  
ATOM   2268  CA  TYR C 255     -28.091  36.560 -66.348  1.00 28.07           C  
ANISOU 2268  CA  TYR C 255     3854   4173   2639    121   -443    672       C  
ATOM   2269  C   TYR C 255     -27.215  37.705 -65.852  1.00 29.91           C  
ANISOU 2269  C   TYR C 255     4032   4560   2771     93   -463    509       C  
ATOM   2270  O   TYR C 255     -26.031  37.514 -65.544  1.00 30.45           O  
ANISOU 2270  O   TYR C 255     4040   4762   2768    124   -534    504       O  
ATOM   2271  CB  TYR C 255     -28.395  36.736 -67.845  1.00 27.79           C  
ANISOU 2271  CB  TYR C 255     3866   3945   2750    105   -464    617       C  
ATOM   2272  CG  TYR C 255     -27.123  36.909 -68.623  1.00 29.44           C  
ANISOU 2272  CG  TYR C 255     4111   4096   2978    128   -481    575       C  
ATOM   2273  CD1 TYR C 255     -26.346  35.808 -68.958  1.00 30.44           C  
ANISOU 2273  CD1 TYR C 255     4259   4157   3151    159   -480    665       C  
ATOM   2274  CD2 TYR C 255     -26.653  38.173 -68.954  1.00 28.74           C  
ANISOU 2274  CD2 TYR C 255     4028   3983   2909    120   -434    447       C  
ATOM   2275  CE1 TYR C 255     -25.158  35.958 -69.636  1.00 31.50           C  
ANISOU 2275  CE1 TYR C 255     4411   4214   3344    178   -454    622       C  
ATOM   2276  CE2 TYR C 255     -25.463  38.332 -69.629  1.00 29.92           C  
ANISOU 2276  CE2 TYR C 255     4202   4046   3122    133   -391    400       C  
ATOM   2277  CZ  TYR C 255     -24.719  37.220 -69.966  1.00 31.40           C  
ANISOU 2277  CZ  TYR C 255     4401   4182   3347    161   -412    485       C  
ATOM   2278  OH  TYR C 255     -23.531  37.361 -70.637  1.00 35.21           O  
ANISOU 2278  OH  TYR C 255     4894   4552   3934    172   -332    434       O  
ATOM   2279  N   PHE C 256     -27.781  38.909 -65.763  1.00 28.12           N  
ANISOU 2279  N   PHE C 256     3797   4311   2575     30   -380    355       N  
ATOM   2280  CA  PHE C 256     -26.987  40.065 -65.373  1.00 29.58           C  
ANISOU 2280  CA  PHE C 256     3920   4587   2733    -41   -331    128       C  
ATOM   2281  C   PHE C 256     -26.626  40.070 -63.893  1.00 33.15           C  
ANISOU 2281  C   PHE C 256     4306   5354   2937    -84   -374     35       C  
ATOM   2282  O   PHE C 256     -25.773  40.865 -63.488  1.00 35.19           O  
ANISOU 2282  O   PHE C 256     4466   5753   3153   -172   -372   -214       O  
ATOM   2283  CB  PHE C 256     -27.726  41.344 -65.754  1.00 30.46           C  
ANISOU 2283  CB  PHE C 256     4050   4524   3001    -81   -153      8       C  
ATOM   2284  CG  PHE C 256     -27.593  41.685 -67.207  1.00 29.28           C  
ANISOU 2284  CG  PHE C 256     3963   4137   3026    -12   -109     61       C  
ATOM   2285  CD1 PHE C 256     -26.384  42.135 -67.716  1.00 31.61           C  
ANISOU 2285  CD1 PHE C 256     4251   4358   3403    -31    -45    -49       C  
ATOM   2286  CD2 PHE C 256     -28.661  41.526 -68.072  1.00 27.77           C  
ANISOU 2286  CD2 PHE C 256     3830   3820   2903     79   -131    217       C  
ATOM   2287  CE1 PHE C 256     -26.251  42.441 -69.073  1.00 30.21           C  
ANISOU 2287  CE1 PHE C 256     4182   3952   3346     56     44     30       C  
ATOM   2288  CE2 PHE C 256     -28.533  41.831 -69.421  1.00 28.95           C  
ANISOU 2288  CE2 PHE C 256     4069   3809   3123    175   -107    287       C  
ATOM   2289  CZ  PHE C 256     -27.324  42.287 -69.917  1.00 30.22           C  
ANISOU 2289  CZ  PHE C 256     4279   3868   3335    171      3    211       C  
ATOM   2290  N   SER C 257     -27.237  39.205 -63.086  1.00 32.16           N  
ANISOU 2290  N   SER C 257     4230   5349   2640    -26   -397    213       N  
ATOM   2291  CA ASER C 257     -26.843  39.092 -61.686  0.50 35.62           C  
ANISOU 2291  CA ASER C 257     4644   6144   2747    -19   -457    178       C  
ATOM   2292  CA BSER C 257     -26.841  39.102 -61.686  0.50 35.63           C  
ANISOU 2292  CA BSER C 257     4644   6145   2747    -20   -457    175       C  
ATOM   2293  C   SER C 257     -25.419  38.580 -61.525  1.00 38.83           C  
ANISOU 2293  C   SER C 257     4934   6794   3024     64   -666    216       C  
ATOM   2294  O   SER C 257     -24.807  38.801 -60.476  1.00 43.44           O  
ANISOU 2294  O   SER C 257     5437   7758   3312     58   -781     93       O  
ATOM   2295  CB ASER C 257     -27.808  38.171 -60.943  0.50 35.98           C  
ANISOU 2295  CB ASER C 257     4805   6216   2648     68   -374    431       C  
ATOM   2296  CB BSER C 257     -27.815  38.202 -60.923  0.50 36.01           C  
ANISOU 2296  CB BSER C 257     4809   6225   2649     65   -372    424       C  
ATOM   2297  OG ASER C 257     -27.327  37.879 -59.643  0.50 38.41           O  
ANISOU 2297  OG ASER C 257     5128   6907   2559    140   -447    480       O  
ATOM   2298  OG BSER C 257     -27.540  36.829 -61.146  0.50 35.23           O  
ANISOU 2298  OG BSER C 257     4735   6084   2568    220   -429    738       O  
ATOM   2299  N   LYS C 258     -24.887  37.888 -62.525  1.00 38.65           N  
ANISOU 2299  N   LYS C 258     4889   6585   3211    146   -717    373       N  
ATOM   2300  CA  LYS C 258     -23.526  37.374 -62.463  1.00 44.50           C  
ANISOU 2300  CA  LYS C 258     5482   7512   3914    246   -887    434       C  
ATOM   2301  C   LYS C 258     -22.627  37.886 -63.577  1.00 42.42           C  
ANISOU 2301  C   LYS C 258     5119   7055   3945    175   -875    258       C  
ATOM   2302  O   LYS C 258     -21.413  37.970 -63.379  1.00 47.50           O  
ANISOU 2302  O   LYS C 258     5561   7896   4591    191  -1002    154       O  
ATOM   2303  CB  LYS C 258     -23.532  35.835 -62.494  1.00 48.67           C  
ANISOU 2303  CB  LYS C 258     6069   7977   4445    449   -888    840       C  
ATOM   2304  CG  LYS C 258     -24.386  35.195 -61.402  1.00 53.61           C  
ANISOU 2304  CG  LYS C 258     6817   8742   4808    553   -822   1075       C  
ATOM   2305  CD  LYS C 258     -23.549  34.384 -60.432  1.00 60.92           C  
ANISOU 2305  CD  LYS C 258     7687   9862   5599    735   -904   1258       C  
ATOM   2306  CE  LYS C 258     -24.386  33.860 -59.267  1.00 64.03           C  
ANISOU 2306  CE  LYS C 258     8242  10309   5778    818   -770   1439       C  
ATOM   2307  NZ  LYS C 258     -24.473  34.828 -58.136  1.00 66.66           N  
ANISOU 2307  NZ  LYS C 258     8583  10975   5770    732   -850   1200       N  
ATOM   2308  N   SER C 259     -23.181  38.262 -64.720  1.00 36.39           N  
ANISOU 2308  N   SER C 259     4477   5932   3418    108   -720    219       N  
ATOM   2309  CA  SER C 259     -22.359  38.601 -65.869  1.00 34.79           C  
ANISOU 2309  CA  SER C 259     4241   5503   3474     78   -650    119       C  
ATOM   2310  C   SER C 259     -21.865  40.043 -65.807  1.00 35.27           C  
ANISOU 2310  C   SER C 259     4193   5572   3635    -70   -552   -233       C  
ATOM   2311  O   SER C 259     -22.536  40.936 -65.281  1.00 34.72           O  
ANISOU 2311  O   SER C 259     4147   5546   3500   -168   -466   -401       O  
ATOM   2312  CB  SER C 259     -23.147  38.388 -67.158  1.00 34.24           C  
ANISOU 2312  CB  SER C 259     4373   5088   3550     97   -527    240       C  
ATOM   2313  OG  SER C 259     -22.489  38.997 -68.253  1.00 34.39           O  
ANISOU 2313  OG  SER C 259     4418   4882   3767     68   -399    127       O  
ATOM   2314  N   LYS C 260     -20.679  40.263 -66.372  1.00 35.97           N  
ANISOU 2314  N   LYS C 260     4155   5576   3937    -94   -506   -358       N  
ATOM   2315  CA  LYS C 260     -20.126  41.596 -66.564  1.00 38.65           C  
ANISOU 2315  CA  LYS C 260     4390   5806   4487   -247   -313   -705       C  
ATOM   2316  C   LYS C 260     -20.286  42.095 -67.997  1.00 37.13           C  
ANISOU 2316  C   LYS C 260     4394   5170   4545   -227    -30   -653       C  
ATOM   2317  O   LYS C 260     -19.734  43.146 -68.340  1.00 38.71           O  
ANISOU 2317  O   LYS C 260     4534   5184   4990   -326    222   -893       O  
ATOM   2318  CB  LYS C 260     -18.650  41.613 -66.167  1.00 44.35           C  
ANISOU 2318  CB  LYS C 260     4791   6737   5321   -302   -414   -927       C  
ATOM   2319  CG  LYS C 260     -18.414  41.421 -64.677  1.00 51.28           C  
ANISOU 2319  CG  LYS C 260     5449   8145   5892   -322   -707  -1045       C  
ATOM   2320  CD  LYS C 260     -19.438  42.206 -63.869  1.00 54.37           C  
ANISOU 2320  CD  LYS C 260     5945   8647   6067   -443   -644  -1217       C  
ATOM   2321  CE  LYS C 260     -18.968  42.461 -62.448  1.00 59.79           C  
ANISOU 2321  CE  LYS C 260     6389   9870   6459   -541   -866  -1516       C  
ATOM   2322  NZ  LYS C 260     -20.035  43.128 -61.650  1.00 61.06           N  
ANISOU 2322  NZ  LYS C 260     6697  10112   6391   -659   -757  -1670       N  
ATOM   2323  N   ALA C 261     -21.031  41.372 -68.829  1.00 34.47           N  
ANISOU 2323  N   ALA C 261     4287   4668   4141   -102    -46   -358       N  
ATOM   2324  CA  ALA C 261     -21.180  41.735 -70.235  1.00 34.94           C  
ANISOU 2324  CA  ALA C 261     4561   4380   4337    -42    179   -274       C  
ATOM   2325  C   ALA C 261     -21.809  43.114 -70.394  1.00 35.89           C  
ANISOU 2325  C   ALA C 261     4759   4337   4540    -68    423   -372       C  
ATOM   2326  O   ALA C 261     -22.707  43.500 -69.642  1.00 35.70           O  
ANISOU 2326  O   ALA C 261     4713   4430   4422   -100    385   -404       O  
ATOM   2327  CB  ALA C 261     -22.032  40.694 -70.960  1.00 34.23           C  
ANISOU 2327  CB  ALA C 261     4675   4238   4093     71     62     -1       C  
ATOM   2328  N   GLU C 262     -21.342  43.858 -71.401  1.00 37.35           N  
ANISOU 2328  N   GLU C 262     5052   4215   4925    -35    728   -393       N  
ATOM   2329  CA  GLU C 262     -21.886  45.192 -71.620  1.00 39.96           C  
ANISOU 2329  CA  GLU C 262     5468   4332   5385    -14   1039   -431       C  
ATOM   2330  C   GLU C 262     -23.310  45.139 -72.160  1.00 35.98           C  
ANISOU 2330  C   GLU C 262     5167   3812   4694    161    964   -142       C  
ATOM   2331  O   GLU C 262     -24.130  45.992 -71.809  1.00 36.00           O  
ANISOU 2331  O   GLU C 262     5160   3771   4748    182   1092   -145       O  
ATOM   2332  CB  GLU C 262     -20.978  45.994 -72.552  1.00 45.79           C  
ANISOU 2332  CB  GLU C 262     6284   4710   6404      5   1454   -492       C  
ATOM   2333  CG  GLU C 262     -19.749  46.565 -71.848  1.00 53.44           C  
ANISOU 2333  CG  GLU C 262     6966   5658   7683   -215   1632   -892       C  
ATOM   2334  CD  GLU C 262     -20.101  47.519 -70.709  1.00 59.87           C  
ANISOU 2334  CD  GLU C 262     7601   6561   8585   -382   1728  -1188       C  
ATOM   2335  OE1 GLU C 262     -21.131  48.220 -70.801  1.00 61.65           O  
ANISOU 2335  OE1 GLU C 262     7973   6647   8804   -299   1905  -1068       O  
ATOM   2336  OE2 GLU C 262     -19.345  47.561 -69.713  1.00 63.12           O  
ANISOU 2336  OE2 GLU C 262     7714   7202   9066   -593   1625  -1551       O  
ATOM   2337  N   PHE C 263     -23.633  44.150 -72.994  1.00 34.50           N  
ANISOU 2337  N   PHE C 263     5133   3668   4309    279    764     83       N  
ATOM   2338  CA  PHE C 263     -25.013  43.962 -73.426  1.00 34.18           C  
ANISOU 2338  CA  PHE C 263     5206   3701   4079    421    608    303       C  
ATOM   2339  C   PHE C 263     -25.187  42.551 -73.968  1.00 32.05           C  
ANISOU 2339  C   PHE C 263     5013   3560   3606    441    329    407       C  
ATOM   2340  O   PHE C 263     -24.213  41.845 -74.245  1.00 33.65           O  
ANISOU 2340  O   PHE C 263     5241   3719   3825    389    331    362       O  
ATOM   2341  CB  PHE C 263     -25.441  45.013 -74.472  1.00 34.64           C  
ANISOU 2341  CB  PHE C 263     5451   3549   4162    627    863    483       C  
ATOM   2342  CG  PHE C 263     -24.812  44.829 -75.838  1.00 36.22           C  
ANISOU 2342  CG  PHE C 263     5895   3599   4266    751    982    609       C  
ATOM   2343  CD1 PHE C 263     -23.618  45.458 -76.156  1.00 38.84           C  
ANISOU 2343  CD1 PHE C 263     6288   3654   4816    726   1358    522       C  
ATOM   2344  CD2 PHE C 263     -25.428  44.045 -76.806  1.00 35.68           C  
ANISOU 2344  CD2 PHE C 263     5992   3667   3897    877    745    781       C  
ATOM   2345  CE1 PHE C 263     -23.037  45.297 -77.413  1.00 42.16           C  
ANISOU 2345  CE1 PHE C 263     6967   3910   5143    845   1528    646       C  
ATOM   2346  CE2 PHE C 263     -24.851  43.874 -78.061  1.00 39.85           C  
ANISOU 2346  CE2 PHE C 263     6783   4077   4280    984    877    875       C  
ATOM   2347  CZ  PHE C 263     -23.655  44.502 -78.364  1.00 42.16           C  
ANISOU 2347  CZ  PHE C 263     7172   4068   4780    979   1284    830       C  
ATOM   2348  N   ILE C 264     -26.451  42.137 -74.081  1.00 29.77           N  
ANISOU 2348  N   ILE C 264     4694   3024   3595    656     25    709       N  
ATOM   2349  CA  ILE C 264     -26.818  40.901 -74.760  1.00 29.48           C  
ANISOU 2349  CA  ILE C 264     4655   2957   3588    726    105    755       C  
ATOM   2350  C   ILE C 264     -27.874  41.215 -75.812  1.00 29.39           C  
ANISOU 2350  C   ILE C 264     4660   2924   3583    720    197    703       C  
ATOM   2351  O   ILE C 264     -28.595  42.210 -75.727  1.00 29.31           O  
ANISOU 2351  O   ILE C 264     4671   2918   3546    703    211    659       O  
ATOM   2352  CB  ILE C 264     -27.356  39.818 -73.803  1.00 30.44           C  
ANISOU 2352  CB  ILE C 264     4877   3056   3635    724     87    831       C  
ATOM   2353  CG1 ILE C 264     -28.640  40.301 -73.118  1.00 28.67           C  
ANISOU 2353  CG1 ILE C 264     4706   2909   3278    658    164    803       C  
ATOM   2354  CG2 ILE C 264     -26.292  39.412 -72.790  1.00 28.81           C  
ANISOU 2354  CG2 ILE C 264     4674   2886   3388    769    -52    928       C  
ATOM   2355  CD1 ILE C 264     -29.337  39.234 -72.312  1.00 30.13           C  
ANISOU 2355  CD1 ILE C 264     4957   3114   3377    591    207    946       C  
ATOM   2356  N   LEU C 265     -27.957  40.339 -76.810  1.00 28.76           N  
ANISOU 2356  N   LEU C 265     4580   2816   3531    767    231    686       N  
ATOM   2357  CA  LEU C 265     -29.086  40.283 -77.724  1.00 30.03           C  
ANISOU 2357  CA  LEU C 265     4762   2982   3665    751    253    629       C  
ATOM   2358  C   LEU C 265     -29.866  39.000 -77.457  1.00 32.37           C  
ANISOU 2358  C   LEU C 265     5112   3188   3998    685    219    616       C  
ATOM   2359  O   LEU C 265     -29.302  37.989 -77.016  1.00 31.86           O  
ANISOU 2359  O   LEU C 265     5117   3000   3988    704    187    652       O  
ATOM   2360  CB  LEU C 265     -28.626  40.336 -79.180  1.00 29.97           C  
ANISOU 2360  CB  LEU C 265     4751   3032   3606    825    287    590       C  
ATOM   2361  CG  LEU C 265     -27.860  41.599 -79.579  1.00 31.40           C  
ANISOU 2361  CG  LEU C 265     4869   3295   3765    821    338    685       C  
ATOM   2362  CD1 LEU C 265     -27.298  41.434 -80.973  1.00 32.39           C  
ANISOU 2362  CD1 LEU C 265     4981   3556   3770    898    429    687       C  
ATOM   2363  CD2 LEU C 265     -28.753  42.824 -79.519  1.00 31.07           C  
ANISOU 2363  CD2 LEU C 265     4859   3218   3727    781    295    731       C  
ATOM   2364  N   ARG C 266     -31.171  39.046 -77.716  1.00 31.07           N  
ANISOU 2364  N   ARG C 266     4900   3073   3833    598    205    591       N  
ATOM   2365  CA  ARG C 266     -32.029  37.935 -77.337  1.00 30.13           C  
ANISOU 2365  CA  ARG C 266     4785   2875   3788    437    171    626       C  
ATOM   2366  C   ARG C 266     -33.291  37.952 -78.181  1.00 29.52           C  
ANISOU 2366  C   ARG C 266     4594   2889   3735    341    101    553       C  
ATOM   2367  O   ARG C 266     -33.652  38.971 -78.775  1.00 30.76           O  
ANISOU 2367  O   ARG C 266     4660   3200   3828    437     92    515       O  
ATOM   2368  CB  ARG C 266     -32.388  37.993 -75.846  1.00 30.80           C  
ANISOU 2368  CB  ARG C 266     4825   3038   3840    355    259    776       C  
ATOM   2369  CG  ARG C 266     -33.003  39.319 -75.428  1.00 30.93           C  
ANISOU 2369  CG  ARG C 266     4708   3278   3766    430    350    749       C  
ATOM   2370  CD  ARG C 266     -33.358  39.344 -73.942  1.00 33.09           C  
ANISOU 2370  CD  ARG C 266     4958   3697   3918    388    473    853       C  
ATOM   2371  NE  ARG C 266     -33.963  40.621 -73.572  1.00 34.41           N  
ANISOU 2371  NE  ARG C 266     5023   4058   3995    534    569    750       N  
ATOM   2372  CZ  ARG C 266     -35.246  40.914 -73.752  1.00 37.07           C  
ANISOU 2372  CZ  ARG C 266     5134   4583   4367    554    648    727       C  
ATOM   2373  NH1 ARG C 266     -36.061  40.015 -74.291  1.00 38.34           N  
ANISOU 2373  NH1 ARG C 266     5130   4784   4654    363    622    812       N  
ATOM   2374  NH2 ARG C 266     -35.718  42.102 -73.391  1.00 37.70           N  
ANISOU 2374  NH2 ARG C 266     5143   4801   4379    775    732    602       N  
ATOM   2375  N   TRP C 267     -33.966  36.807 -78.200  1.00 29.55           N  
ANISOU 2375  N   TRP C 267     4603   2775   3850    134     18    556       N  
ATOM   2376  CA  TRP C 267     -35.226  36.662 -78.917  1.00 34.05           C  
ANISOU 2376  CA  TRP C 267     5014   3449   4476    -26   -107    489       C  
ATOM   2377  C   TRP C 267     -36.316  37.473 -78.222  1.00 34.82           C  
ANISOU 2377  C   TRP C 267     4802   3845   4582    -60      1    609       C  
ATOM   2378  O   TRP C 267     -36.642  37.214 -77.060  1.00 36.33           O  
ANISOU 2378  O   TRP C 267     4904   4094   4807   -185    142    769       O  
ATOM   2379  CB  TRP C 267     -35.600  35.184 -78.978  1.00 37.40           C  
ANISOU 2379  CB  TRP C 267     5530   3609   5071   -308   -247    472       C  
ATOM   2380  CG  TRP C 267     -36.737  34.855 -79.882  1.00 41.63           C  
ANISOU 2380  CG  TRP C 267     5925   4211   5682   -523   -463    348       C  
ATOM   2381  CD1 TRP C 267     -38.031  34.612 -79.518  1.00 44.54           C  
ANISOU 2381  CD1 TRP C 267     5988   4726   6209   -838   -504    469       C  
ATOM   2382  CD2 TRP C 267     -36.686  34.708 -81.307  1.00 42.75           C  
ANISOU 2382  CD2 TRP C 267     6200   4322   5723   -455   -687     74       C  
ATOM   2383  NE1 TRP C 267     -38.787  34.327 -80.628  1.00 47.63           N  
ANISOU 2383  NE1 TRP C 267     6293   5160   6642   -990   -788    282       N  
ATOM   2384  CE2 TRP C 267     -37.986  34.381 -81.740  1.00 46.70           C  
ANISOU 2384  CE2 TRP C 267     6477   4931   6335   -749   -915     24       C  
ATOM   2385  CE3 TRP C 267     -35.667  34.825 -82.259  1.00 40.52           C  
ANISOU 2385  CE3 TRP C 267     6179   3983   5232   -176   -706   -128       C  
ATOM   2386  CZ2 TRP C 267     -38.295  34.172 -83.082  1.00 49.09           C  
ANISOU 2386  CZ2 TRP C 267     6861   5267   6524   -766  -1212   -248       C  
ATOM   2387  CZ3 TRP C 267     -35.977  34.615 -83.592  1.00 44.01           C  
ANISOU 2387  CZ3 TRP C 267     6717   4482   5522   -171   -942   -387       C  
ATOM   2388  CH2 TRP C 267     -37.278  34.293 -83.990  1.00 47.61           C  
ANISOU 2388  CH2 TRP C 267     6997   5024   6068   -461  -1217   -459       C  
ATOM   2389  N   SER C 268     -36.886  38.445 -78.930  1.00 35.32           N  
ANISOU 2389  N   SER C 268     4706   4119   4596     84    -58    544       N  
ATOM   2390  CA  SER C 268     -37.843  39.360 -78.320  1.00 36.02           C  
ANISOU 2390  CA  SER C 268     4496   4491   4699    179     54    615       C  
ATOM   2391  C   SER C 268     -39.184  38.677 -78.068  1.00 41.23           C  
ANISOU 2391  C   SER C 268     4807   5354   5506    -91     37    693       C  
ATOM   2392  O   SER C 268     -39.605  37.786 -78.811  1.00 44.79           O  
ANISOU 2392  O   SER C 268     5219   5738   6063   -345   -173    647       O  
ATOM   2393  CB  SER C 268     -38.037  40.590 -79.208  1.00 35.51           C  
ANISOU 2393  CB  SER C 268     4384   4535   4574    455    -46    555       C  
ATOM   2394  OG  SER C 268     -39.197  41.317 -78.846  1.00 38.88           O  
ANISOU 2394  OG  SER C 268     4472   5235   5067    587      3    589       O  
ATOM   2395  N   SER C 269     -39.858  39.107 -76.997  1.00 44.12           N  
ANISOU 2395  N   SER C 269     4906   5988   5870    -47    264    799       N  
ATOM   2396  CA  SER C 269     -41.185  38.582 -76.695  1.00 47.12           C  
ANISOU 2396  CA  SER C 269     4844   6666   6394   -310    309    920       C  
ATOM   2397  C   SER C 269     -42.219  39.014 -77.725  1.00 48.22           C  
ANISOU 2397  C   SER C 269     4623   7052   6646   -242     88    838       C  
ATOM   2398  O   SER C 269     -43.272  38.377 -77.837  1.00 50.44           O  
ANISOU 2398  O   SER C 269     4511   7550   7102   -551      6    917       O  
ATOM   2399  CB  SER C 269     -41.630  39.028 -75.300  1.00 49.48           C  
ANISOU 2399  CB  SER C 269     4920   7289   6593   -208    668   1040       C  
ATOM   2400  OG  SER C 269     -42.164  40.341 -75.337  1.00 50.48           O  
ANISOU 2400  OG  SER C 269     4817   7684   6680    209    738    918       O  
ATOM   2401  N   ALA C 270     -41.939  40.074 -78.483  1.00 47.49           N  
ANISOU 2401  N   ALA C 270     4647   6933   6465    131    -35    716       N  
ATOM   2402  CA  ALA C 270     -42.867  40.552 -79.498  1.00 51.42           C  
ANISOU 2402  CA  ALA C 270     4837   7668   7031    257   -295    673       C  
ATOM   2403  C   ALA C 270     -43.035  39.578 -80.657  1.00 54.53           C  
ANISOU 2403  C   ALA C 270     5272   7982   7465    -69   -657    597       C  
ATOM   2404  O   ALA C 270     -43.976  39.740 -81.441  1.00 56.44           O  
ANISOU 2404  O   ALA C 270     5187   8490   7769    -60   -929    575       O  
ATOM   2405  CB  ALA C 270     -42.401  41.906 -80.032  1.00 50.21           C  
ANISOU 2405  CB  ALA C 270     4898   7425   6754    724   -354    624       C  
ATOM   2406  N   ASN C 271     -42.158  38.576 -80.782  1.00 55.35           N  
ANISOU 2406  N   ASN C 271     5771   7730   7529   -323   -694    532       N  
ATOM   2407  CA  ASN C 271     -42.233  37.657 -81.913  1.00 60.02           C  
ANISOU 2407  CA  ASN C 271     6495   8190   8122   -584  -1052    372       C  
ATOM   2408  C   ASN C 271     -43.506  36.822 -81.891  1.00 72.47           C  
ANISOU 2408  C   ASN C 271     7635   9949   9953  -1026  -1242    405       C  
ATOM   2409  O   ASN C 271     -43.976  36.384 -82.947  1.00 73.52           O  
ANISOU 2409  O   ASN C 271     7727  10115  10092  -1205  -1634    244       O  
ATOM   2410  CB  ASN C 271     -41.004  36.752 -81.932  1.00 55.12           C  
ANISOU 2410  CB  ASN C 271     6391   7117   7436   -689  -1016    268       C  
ATOM   2411  CG  ASN C 271     -39.788  37.443 -82.509  1.00 48.89           C  
ANISOU 2411  CG  ASN C 271     5983   6211   6380   -317   -957    183       C  
ATOM   2412  OD1 ASN C 271     -39.814  37.921 -83.641  1.00 48.70           O  
ANISOU 2412  OD1 ASN C 271     6025   6313   6165   -150  -1152     87       O  
ATOM   2413  ND2 ASN C 271     -38.716  37.508 -81.727  1.00 43.06           N  
ANISOU 2413  ND2 ASN C 271     5477   5269   5615   -202   -694    252       N  
ATOM   2414  N   GLU C 272     -44.077  36.582 -80.711  1.00 85.07           N  
ANISOU 2414  N   GLU C 272     8891  11690  11741  -1235   -980    617       N  
ATOM   2415  CA  GLU C 272     -45.318  35.825 -80.604  1.00 94.80           C  
ANISOU 2415  CA  GLU C 272     9618  13147  13256  -1721  -1116    719       C  
ATOM   2416  C   GLU C 272     -46.439  36.620 -79.947  1.00 98.40           C  
ANISOU 2416  C   GLU C 272     9385  14193  13810  -1582   -895    904       C  
ATOM   2417  O   GLU C 272     -47.451  36.031 -79.547  1.00103.81           O  
ANISOU 2417  O   GLU C 272     9549  15151  14744  -2005   -875   1073       O  
ATOM   2418  CB  GLU C 272     -45.084  34.513 -79.848  1.00 99.05           C  
ANISOU 2418  CB  GLU C 272    10338  13326  13970  -2227  -1011    862       C  
ATOM   2419  CG  GLU C 272     -44.431  33.434 -80.703  1.00103.26           C  
ANISOU 2419  CG  GLU C 272    11403  13297  14535  -2468  -1363    626       C  
ATOM   2420  CD  GLU C 272     -45.087  32.076 -80.539  1.00111.59           C  
ANISOU 2420  CD  GLU C 272    12349  14111  15939  -3158  -1555    723       C  
ATOM   2421  OE1 GLU C 272     -45.548  31.765 -79.420  1.00114.63           O  
ANISOU 2421  OE1 GLU C 272    12445  14611  16497  -3463  -1272   1079       O  
ATOM   2422  OE2 GLU C 272     -45.150  31.324 -81.535  1.00115.10           O  
ANISOU 2422  OE2 GLU C 272    13013  14251  16470  -3411  -1995    445       O  
ATOM   2423  N   SER C 273     -46.292  37.940 -79.829  1.00 97.12           N  
ANISOU 2423  N   SER C 273     9195  14227  13478   -999   -726    878       N  
ATOM   2424  CA  SER C 273     -47.359  38.797 -79.330  1.00100.98           C  
ANISOU 2424  CA  SER C 273     9043  15269  14054   -728   -540    982       C  
ATOM   2425  C   SER C 273     -47.949  39.712 -80.392  1.00101.70           C  
ANISOU 2425  C   SER C 273     8882  15611  14148   -343   -878    882       C  
ATOM   2426  O   SER C 273     -49.106  40.117 -80.261  1.00106.83           O  
ANISOU 2426  O   SER C 273     8855  16771  14965   -216   -871    960       O  
ATOM   2427  CB  SER C 273     -46.857  39.650 -78.155  1.00 98.34           C  
ANISOU 2427  CB  SER C 273     8861  14958  13547   -307    -63   1020       C  
ATOM   2428  OG  SER C 273     -46.051  40.727 -78.600  1.00 93.99           O  
ANISOU 2428  OG  SER C 273     8740  14157  12815    204   -132    871       O  
ATOM   2429  N   ASP C 274     -47.193  40.044 -81.436  1.00 96.81           N  
ANISOU 2429  N   ASP C 274     8764  14683  13335   -138  -1168    742       N  
ATOM   2430  CA  ASP C 274     -47.717  40.868 -82.515  1.00 98.41           C  
ANISOU 2430  CA  ASP C 274     8793  15106  13492    214  -1536    707       C  
ATOM   2431  C   ASP C 274     -48.469  40.008 -83.524  1.00102.56           C  
ANISOU 2431  C   ASP C 274     9047  15816  14104   -205  -2040    638       C  
ATOM   2432  O   ASP C 274     -48.189  38.818 -83.691  1.00101.56           O  
ANISOU 2432  O   ASP C 274     9143  15442  14004   -726  -2162    541       O  
ATOM   2433  CB  ASP C 274     -46.590  41.633 -83.211  1.00 94.01           C  
ANISOU 2433  CB  ASP C 274     8891  14185  12643    586  -1610    648       C  
ATOM   2434  CG  ASP C 274     -47.059  42.954 -83.798  1.00 96.61           C  
ANISOU 2434  CG  ASP C 274     9068  14704  12933   1145  -1797    727       C  
ATOM   2435  OD1 ASP C 274     -48.261  43.270 -83.667  1.00101.53           O  
ANISOU 2435  OD1 ASP C 274     9055  15758  13763   1303  -1882    792       O  
ATOM   2436  OD2 ASP C 274     -46.228  43.677 -84.388  1.00 94.12           O  
ANISOU 2436  OD2 ASP C 274     9252  14112  12398   1430  -1859    753       O  
ATOM   2437  N   THR C 275     -49.430  40.629 -84.207  1.00107.32           N  
ANISOU 2437  N   THR C 275     9183  16836  14760     46  -2373    674       N  
ATOM   2438  CA  THR C 275     -50.364  39.900 -85.057  1.00112.02           C  
ANISOU 2438  CA  THR C 275     9363  17727  15470   -356  -2898    609       C  
ATOM   2439  C   THR C 275     -50.085  40.038 -86.547  1.00110.84           C  
ANISOU 2439  C   THR C 275     9612  17508  14995   -235  -3438    469       C  
ATOM   2440  O   THR C 275     -50.472  39.152 -87.316  1.00115.01           O  
ANISOU 2440  O   THR C 275    10077  18105  15515   -679  -3902    308       O  
ATOM   2441  CB  THR C 275     -51.799  40.359 -84.778  1.00118.77           C  
ANISOU 2441  CB  THR C 275     9265  19232  16630   -212  -2956    762       C  
ATOM   2442  N   GLU C 276     -49.432  41.119 -86.982  1.00106.25           N  
ANISOU 2442  N   GLU C 276     9454  16793  14125    330  -3404    531       N  
ATOM   2443  CA  GLU C 276     -49.252  41.352 -88.412  1.00108.05           C  
ANISOU 2443  CA  GLU C 276    10021  17057  13975    483  -3896    472       C  
ATOM   2444  C   GLU C 276     -48.083  40.570 -89.003  1.00102.71           C  
ANISOU 2444  C   GLU C 276    10101  15973  12953    219  -3917    249       C  
ATOM   2445  O   GLU C 276     -48.051  40.369 -90.223  1.00105.37           O  
ANISOU 2445  O   GLU C 276    10689  16409  12939    187  -4363    117       O  
ATOM   2446  CB  GLU C 276     -49.069  42.847 -88.686  1.00110.30           C  
ANISOU 2446  CB  GLU C 276    10450  17358  14100   1172  -3864    704       C  
ATOM   2447  CG  GLU C 276     -49.453  43.274 -90.101  1.00118.11           C  
ANISOU 2447  CG  GLU C 276    11546  18536  14796   1367  -4415    771       C  
ATOM   2448  CD  GLU C 276     -50.850  42.822 -90.501  1.00126.83           C  
ANISOU 2448  CD  GLU C 276    12069  19971  16148   1126  -4848    698       C  
ATOM   2449  OE1 GLU C 276     -50.971  42.029 -91.461  1.00130.22           O  
ANISOU 2449  OE1 GLU C 276    12653  20472  16354    776  -5298    513       O  
ATOM   2450  OE2 GLU C 276     -51.828  43.262 -89.860  1.00130.34           O  
ANISOU 2450  OE2 GLU C 276    11919  20595  17010   1301  -4735    794       O  
ATOM   2451  N   ASN C 277     -47.132  40.131 -88.176  1.00 94.80           N  
ANISOU 2451  N   ASN C 277     9454  14553  12012     68  -3454    196       N  
ATOM   2452  CA  ASN C 277     -46.005  39.305 -88.620  1.00 89.27           C  
ANISOU 2452  CA  ASN C 277     9412  13465  11043   -140  -3426    -36       C  
ATOM   2453  C   ASN C 277     -45.213  39.991 -89.733  1.00 83.40           C  
ANISOU 2453  C   ASN C 277     9179  12714   9795    230  -3532    -25       C  
ATOM   2454  O   ASN C 277     -44.940  39.407 -90.785  1.00 84.19           O  
ANISOU 2454  O   ASN C 277     9624  12822   9541    115  -3830   -258       O  
ATOM   2455  CB  ASN C 277     -46.477  37.918 -89.068  1.00 95.32           C  
ANISOU 2455  CB  ASN C 277    10136  14200  11880   -691  -3815   -331       C  
ATOM   2456  CG  ASN C 277     -47.390  37.255 -88.058  1.00 99.19           C  
ANISOU 2456  CG  ASN C 277    10054  14751  12883  -1136  -3746   -258       C  
ATOM   2457  OD1 ASN C 277     -48.609  37.220 -88.237  1.00105.15           O  
ANISOU 2457  OD1 ASN C 277    10202  15909  13842  -1319  -4081   -216       O  
ATOM   2458  ND2 ASN C 277     -46.804  36.717 -86.994  1.00 96.17           N  
ANISOU 2458  ND2 ASN C 277     9834  14006  12701  -1323  -3317   -210       N  
ATOM   2459  N   LYS C 278     -44.842  41.248 -89.495  1.00 77.66           N  
ANISOU 2459  N   LYS C 278     8518  11967   9021    671  -3280    252       N  
ATOM   2460  CA  LYS C 278     -44.062  42.003 -90.465  1.00 75.05           C  
ANISOU 2460  CA  LYS C 278     8656  11622   8238    989  -3320    372       C  
ATOM   2461  C   LYS C 278     -42.574  42.030 -90.149  1.00 69.88           C  
ANISOU 2461  C   LYS C 278     8497  10596   7456   1023  -2865    375       C  
ATOM   2462  O   LYS C 278     -41.776  42.373 -91.029  1.00 56.89           O  
ANISOU 2462  O   LYS C 278     7263   8958   5395   1176  -2856    443       O  
ATOM   2463  CB  LYS C 278     -44.580  43.445 -90.563  1.00 74.54           C  
ANISOU 2463  CB  LYS C 278     8394  11717   8211   1447  -3404    722       C  
ATOM   2464  CG  LYS C 278     -44.250  44.127 -91.884  1.00 75.69           C  
ANISOU 2464  CG  LYS C 278     8916  11993   7850   1709  -3659    914       C  
ATOM   2465  CD  LYS C 278     -44.401  45.641 -91.803  1.00 75.81           C  
ANISOU 2465  CD  LYS C 278     8911  11900   7993   2129  -3585   1318       C  
ATOM   2466  CE  LYS C 278     -45.849  46.050 -91.597  1.00 80.31           C  
ANISOU 2466  CE  LYS C 278     8900  12676   8937   2274  -3835   1396       C  
ATOM   2467  NZ  LYS C 278     -46.223  47.178 -92.498  1.00 84.78           N  
ANISOU 2467  NZ  LYS C 278     9581  13211   9419   2523  -4042   1728       N  
ATOM   2468  N   TYR C 279     -42.185  41.666 -88.928  1.00 62.65           N  
ANISOU 2468  N   TYR C 279     7528   9407   6868    878  -2495    324       N  
ATOM   2469  CA  TYR C 279     -40.802  41.762 -88.491  1.00 54.88           C  
ANISOU 2469  CA  TYR C 279     6922   8105   5824    927  -2089    351       C  
ATOM   2470  C   TYR C 279     -40.400  40.499 -87.746  1.00 49.63           C  
ANISOU 2470  C   TYR C 279     6312   7198   5347    611  -1916    123       C  
ATOM   2471  O   TYR C 279     -41.236  39.779 -87.197  1.00 50.51           O  
ANISOU 2471  O   TYR C 279     6125   7332   5736    348  -2009     36       O  
ATOM   2472  CB  TYR C 279     -40.576  42.966 -87.563  1.00 51.41           C  
ANISOU 2472  CB  TYR C 279     6411   7524   5598   1179  -1799    605       C  
ATOM   2473  CG  TYR C 279     -40.968  44.295 -88.154  1.00 53.86           C  
ANISOU 2473  CG  TYR C 279     6700   7950   5812   1527  -1964    873       C  
ATOM   2474  CD1 TYR C 279     -42.275  44.753 -88.077  1.00 57.34           C  
ANISOU 2474  CD1 TYR C 279     6722   8619   6445   1700  -2200    950       C  
ATOM   2475  CD2 TYR C 279     -40.025  45.100 -88.776  1.00 54.26           C  
ANISOU 2475  CD2 TYR C 279     7133   7881   5605   1690  -1882   1086       C  
ATOM   2476  CE1 TYR C 279     -42.637  45.972 -88.619  1.00 61.30           C  
ANISOU 2476  CE1 TYR C 279     7230   9174   6886   2079  -2387   1219       C  
ATOM   2477  CE2 TYR C 279     -40.374  46.316 -89.315  1.00 57.11           C  
ANISOU 2477  CE2 TYR C 279     7528   8273   5898   1998  -2055   1392       C  
ATOM   2478  CZ  TYR C 279     -41.680  46.747 -89.236  1.00 61.06           C  
ANISOU 2478  CZ  TYR C 279     7655   8948   6598   2218  -2325   1451       C  
ATOM   2479  OH  TYR C 279     -42.021  47.961 -89.773  1.00 65.02           O  
ANISOU 2479  OH  TYR C 279     8213   9397   7094   2515  -2491   1756       O  
ATOM   2480  N   VAL C 280     -39.100  40.241 -87.734  1.00 45.57           N  
ANISOU 2480  N   VAL C 280     6166   6456   4692    638  -1666     63       N  
ATOM   2481  CA  VAL C 280     -38.479  39.406 -86.718  1.00 41.72           C  
ANISOU 2481  CA  VAL C 280     5748   5672   4433    467  -1416    -31       C  
ATOM   2482  C   VAL C 280     -37.945  40.350 -85.657  1.00 40.10           C  
ANISOU 2482  C   VAL C 280     5493   5363   4379    625  -1091    198       C  
ATOM   2483  O   VAL C 280     -37.209  41.294 -85.975  1.00 40.26           O  
ANISOU 2483  O   VAL C 280     5673   5383   4239    836   -976    341       O  
ATOM   2484  CB  VAL C 280     -37.357  38.529 -87.300  1.00 41.26           C  
ANISOU 2484  CB  VAL C 280     6079   5442   4155    461  -1358   -259       C  
ATOM   2485  CG1 VAL C 280     -36.583  37.854 -86.177  1.00 38.63           C  
ANISOU 2485  CG1 VAL C 280     5820   4785   4073    376  -1098   -277       C  
ATOM   2486  CG2 VAL C 280     -37.931  37.496 -88.244  1.00 47.27           C  
ANISOU 2486  CG2 VAL C 280     6943   6239   4780    290  -1713   -576       C  
ATOM   2487  N   PHE C 281     -38.341  40.124 -84.410  1.00 37.69           N  
ANISOU 2487  N   PHE C 281     4973   4983   4363    501   -956    241       N  
ATOM   2488  CA  PHE C 281     -38.050  41.041 -83.319  1.00 36.63           C  
ANISOU 2488  CA  PHE C 281     4779   4791   4349    655   -697    399       C  
ATOM   2489  C   PHE C 281     -36.864  40.527 -82.515  1.00 36.11           C  
ANISOU 2489  C   PHE C 281     4928   4478   4314    582   -468    378       C  
ATOM   2490  O   PHE C 281     -36.864  39.377 -82.066  1.00 37.81           O  
ANISOU 2490  O   PHE C 281     5158   4576   4631    368   -457    309       O  
ATOM   2491  CB  PHE C 281     -39.269  41.216 -82.411  1.00 37.57           C  
ANISOU 2491  CB  PHE C 281     4505   5084   4688    624   -662    459       C  
ATOM   2492  CG  PHE C 281     -40.475  41.790 -83.109  1.00 41.85           C  
ANISOU 2492  CG  PHE C 281     4743   5911   5246    755   -902    497       C  
ATOM   2493  CD1 PHE C 281     -40.592  43.153 -83.310  1.00 41.21           C  
ANISOU 2493  CD1 PHE C 281     4654   5873   5133   1115   -917    614       C  
ATOM   2494  CD2 PHE C 281     -41.498  40.964 -83.548  1.00 45.53           C  
ANISOU 2494  CD2 PHE C 281     4927   6581   5791    512  -1149    426       C  
ATOM   2495  CE1 PHE C 281     -41.708  43.684 -83.947  1.00 45.83           C  
ANISOU 2495  CE1 PHE C 281     4944   6722   5747   1296  -1173    677       C  
ATOM   2496  CE2 PHE C 281     -42.612  41.489 -84.184  1.00 50.15           C  
ANISOU 2496  CE2 PHE C 281     5172   7482   6400    647  -1416    472       C  
ATOM   2497  CZ  PHE C 281     -42.714  42.852 -84.384  1.00 50.90           C  
ANISOU 2497  CZ  PHE C 281     5252   7640   6446   1073  -1426    606       C  
ATOM   2498  N   ILE C 282     -35.859  41.380 -82.349  1.00 34.22           N  
ANISOU 2498  N   ILE C 282     4849   4146   4008    749   -320    462       N  
ATOM   2499  CA  ILE C 282     -34.682  41.093 -81.543  1.00 32.15           C  
ANISOU 2499  CA  ILE C 282     4732   3704   3779    718   -138    467       C  
ATOM   2500  C   ILE C 282     -34.582  42.173 -80.478  1.00 31.93           C  
ANISOU 2500  C   ILE C 282     4657   3644   3830    821    -10    558       C  
ATOM   2501  O   ILE C 282     -34.768  43.358 -80.769  1.00 35.01           O  
ANISOU 2501  O   ILE C 282     5045   4045   4210    977    -41    625       O  
ATOM   2502  CB  ILE C 282     -33.400  41.048 -82.398  1.00 31.67           C  
ANISOU 2502  CB  ILE C 282     4879   3595   3560    787    -97    451       C  
ATOM   2503  CG1 ILE C 282     -33.556  40.047 -83.546  1.00 35.75           C  
ANISOU 2503  CG1 ILE C 282     5492   4160   3929    750   -232    283       C  
ATOM   2504  CG2 ILE C 282     -32.204  40.671 -81.543  1.00 31.84           C  
ANISOU 2504  CG2 ILE C 282     4969   3473   3655    772     51    459       C  
ATOM   2505  CD1 ILE C 282     -33.655  38.616 -83.081  1.00 37.35           C  
ANISOU 2505  CD1 ILE C 282     5737   4183   4270    599   -274    133       C  
ATOM   2506  N   ALA C 283     -34.299  41.770 -79.247  1.00 31.14           N  
ANISOU 2506  N   ALA C 283     4556   3483   3792    746    107    554       N  
ATOM   2507  CA  ALA C 283     -34.175  42.705 -78.141  1.00 30.71           C  
ANISOU 2507  CA  ALA C 283     4503   3410   3756    845    210    569       C  
ATOM   2508  C   ALA C 283     -32.728  42.766 -77.673  1.00 31.04           C  
ANISOU 2508  C   ALA C 283     4712   3309   3771    818    250    583       C  
ATOM   2509  O   ALA C 283     -32.008  41.763 -77.719  1.00 31.47           O  
ANISOU 2509  O   ALA C 283     4821   3316   3819    732    250    595       O  
ATOM   2510  CB  ALA C 283     -35.080  42.308 -76.974  1.00 31.58           C  
ANISOU 2510  CB  ALA C 283     4455   3664   3880    793    317    566       C  
ATOM   2511  N   ALA C 284     -32.305  43.951 -77.244  1.00 31.07           N  
ANISOU 2511  N   ALA C 284     4789   3229   3786    903    254    571       N  
ATOM   2512  CA  ALA C 284     -31.037  44.128 -76.558  1.00 31.40           C  
ANISOU 2512  CA  ALA C 284     4931   3177   3823    842    249    569       C  
ATOM   2513  C   ALA C 284     -31.299  44.427 -75.086  1.00 29.66           C  
ANISOU 2513  C   ALA C 284     4749   2988   3532    880    280    471       C  
ATOM   2514  O   ALA C 284     -32.306  45.044 -74.742  1.00 32.05           O  
ANISOU 2514  O   ALA C 284     5024   3339   3814   1012    328    384       O  
ATOM   2515  CB  ALA C 284     -30.230  45.264 -77.180  1.00 31.90           C  
ANISOU 2515  CB  ALA C 284     5070   3095   3956    833    190    626       C  
ATOM   2516  N   SER C 285     -30.394  43.981 -74.220  1.00 27.79           N  
ANISOU 2516  N   SER C 285     4568   2764   3229    800    252    478       N  
ATOM   2517  CA  SER C 285     -30.510  44.249 -72.791  1.00 30.47           C  
ANISOU 2517  CA  SER C 285     4989   3183   3406    836    262    376       C  
ATOM   2518  C   SER C 285     -29.148  44.616 -72.228  1.00 31.19           C  
ANISOU 2518  C   SER C 285     5174   3197   3479    757    102    339       C  
ATOM   2519  O   SER C 285     -28.122  44.077 -72.648  1.00 29.43           O  
ANISOU 2519  O   SER C 285     4881   2953   3348    669     30    455       O  
ATOM   2520  CB  SER C 285     -31.073  43.048 -72.024  1.00 32.00           C  
ANISOU 2520  CB  SER C 285     5139   3568   3451    792    368    478       C  
ATOM   2521  OG  SER C 285     -32.457  42.887 -72.267  1.00 33.88           O  
ANISOU 2521  OG  SER C 285     5236   3935   3702    827    512    491       O  
ATOM   2522  N   PHE C 286     -29.148  45.542 -71.267  1.00 34.24           N  
ANISOU 2522  N   PHE C 286     5701   3561   3747    805     34    148       N  
ATOM   2523  CA  PHE C 286     -27.918  45.920 -70.591  1.00 33.48           C  
ANISOU 2523  CA  PHE C 286     5687   3417   3617    692   -182     76       C  
ATOM   2524  C   PHE C 286     -28.255  46.390 -69.183  1.00 33.91           C  
ANISOU 2524  C   PHE C 286     5938   3574   3373    785   -223   -163       C  
ATOM   2525  O   PHE C 286     -29.411  46.663 -68.849  1.00 33.84           O  
ANISOU 2525  O   PHE C 286     5988   3648   3223    967    -50   -294       O  
ATOM   2526  CB  PHE C 286     -27.142  46.996 -71.369  1.00 33.52           C  
ANISOU 2526  CB  PHE C 286     5693   3155   3889    564   -324     56       C  
ATOM   2527  CG  PHE C 286     -27.933  48.241 -71.657  1.00 35.74           C  
ANISOU 2527  CG  PHE C 286     6129   3186   4265    671   -309    -97       C  
ATOM   2528  CD1 PHE C 286     -28.001  49.267 -70.728  1.00 38.03           C  
ANISOU 2528  CD1 PHE C 286     6656   3311   4483    725   -447   -393       C  
ATOM   2529  CD2 PHE C 286     -28.587  48.398 -72.872  1.00 34.76           C  
ANISOU 2529  CD2 PHE C 286     5940   2972   4296    746   -191     40       C  
ATOM   2530  CE1 PHE C 286     -28.717  50.415 -70.990  1.00 41.18           C  
ANISOU 2530  CE1 PHE C 286     7228   3409   5009    887   -453   -549       C  
ATOM   2531  CE2 PHE C 286     -29.307  49.542 -73.141  1.00 36.79           C  
ANISOU 2531  CE2 PHE C 286     6343   2972   4663    897   -213    -63       C  
ATOM   2532  CZ  PHE C 286     -29.373  50.553 -72.203  1.00 40.35           C  
ANISOU 2532  CZ  PHE C 286     7033   3206   5090    984   -337   -356       C  
ATOM   2533  N   GLN C 287     -27.224  46.468 -68.356  1.00 34.53           N  
ANISOU 2533  N   GLN C 287     6093   3696   3330    677   -459   -230       N  
ATOM   2534  CA  GLN C 287     -27.367  46.827 -66.954  1.00 42.75           C  
ANISOU 2534  CA  GLN C 287     7361   4890   3993    759   -544   -480       C  
ATOM   2535  C   GLN C 287     -26.729  48.183 -66.701  1.00 47.95           C  
ANISOU 2535  C   GLN C 287     8204   5278   4737    671   -830   -801       C  
ATOM   2536  O   GLN C 287     -25.631  48.461 -67.187  1.00 48.68           O  
ANISOU 2536  O   GLN C 287     8190   5196   5112    434  -1061   -726       O  
ATOM   2537  CB  GLN C 287     -26.724  45.762 -66.065  1.00 39.03           C  
ANISOU 2537  CB  GLN C 287     6874   4713   3244    703   -658   -301       C  
ATOM   2538  CG  GLN C 287     -27.072  45.858 -64.597  1.00 65.20           C  
ANISOU 2538  CG  GLN C 287    10434   8312   6028    817   -677   -485       C  
ATOM   2539  CD  GLN C 287     -26.615  44.629 -63.851  1.00 64.07           C  
ANISOU 2539  CD  GLN C 287    10277   8464   5603    783   -756   -177       C  
ATOM   2540  OE1 GLN C 287     -27.383  44.018 -63.112  1.00 65.85           O  
ANISOU 2540  OE1 GLN C 287    10594   8977   5449    876   -545    -50       O  
ATOM   2541  NE2 GLN C 287     -25.362  44.240 -64.064  1.00 62.57           N  
ANISOU 2541  NE2 GLN C 287     9948   8216   5612    658  -1050    -15       N  
ATOM   2542  N   ALA C 288     -27.430  49.027 -65.952  1.00 53.38           N  
ANISOU 2542  N   ALA C 288     9160   5928   5195    860   -809  -1167       N  
ATOM   2543  CA  ALA C 288     -26.910  50.306 -65.489  1.00 60.22           C  
ANISOU 2543  CA  ALA C 288    10301   6488   6093    792  -1124  -1559       C  
ATOM   2544  C   ALA C 288     -27.093  50.383 -63.979  1.00 65.80           C  
ANISOU 2544  C   ALA C 288    11287   7479   6234    951  -1197  -1906       C  
ATOM   2545  O   ALA C 288     -27.643  49.470 -63.357  1.00 65.96           O  
ANISOU 2545  O   ALA C 288    11264   7948   5851   1102   -963  -1774       O  
ATOM   2546  CB  ALA C 288     -27.608  51.479 -66.188  1.00 61.85           C  
ANISOU 2546  CB  ALA C 288    10649   6244   6606    938  -1058  -1747       C  
ATOM   2547  N   SER C 289     -26.618  51.482 -63.383  1.00 74.21           N  
ANISOU 2547  N   SER C 289    12664   8280   7252    894  -1535  -2347       N  
ATOM   2548  CA  SER C 289     -26.914  51.751 -61.977  1.00 81.08           C  
ANISOU 2548  CA  SER C 289    13881   9406   7520   1110  -1598  -2790       C  
ATOM   2549  C   SER C 289     -28.414  51.721 -61.739  1.00 82.00           C  
ANISOU 2549  C   SER C 289    13990   9766   7400   1533  -1096  -2869       C  
ATOM   2550  O   SER C 289     -28.885  51.297 -60.676  1.00 85.34           O  
ANISOU 2550  O   SER C 289    14420  10687   7317   1682   -894  -2903       O  
ATOM   2551  CB  SER C 289     -26.350  53.114 -61.575  1.00 87.48           C  
ANISOU 2551  CB  SER C 289    14920   9805   8512    964  -1959  -3218       C  
ATOM   2552  OG  SER C 289     -25.125  53.372 -62.233  1.00 88.45           O  
ANISOU 2552  OG  SER C 289    14963   9562   9081    530  -2376  -3100       O  
ATOM   2553  N   ASP C 290     -29.171  52.181 -62.736  1.00 80.82           N  
ANISOU 2553  N   ASP C 290    13753   9298   7657   1697   -887  -2839       N  
ATOM   2554  CA  ASP C 290     -30.628  52.169 -62.706  1.00 81.45           C  
ANISOU 2554  CA  ASP C 290    13677   9621   7649   2072   -424  -2845       C  
ATOM   2555  C   ASP C 290     -31.194  50.763 -62.555  1.00 73.09           C  
ANISOU 2555  C   ASP C 290    12377   9146   6246   2121    -70  -2479       C  
ATOM   2556  O   ASP C 290     -32.301  50.594 -62.032  1.00 73.39           O  
ANISOU 2556  O   ASP C 290    12255   9579   6050   2349    303  -2484       O  
ATOM   2557  CB  ASP C 290     -31.141  52.804 -64.002  1.00 81.89           C  
ANISOU 2557  CB  ASP C 290    13627   9220   8269   2178   -364  -2765       C  
ATOM   2558  CG  ASP C 290     -32.499  53.437 -63.854  1.00 87.67           C  
ANISOU 2558  CG  ASP C 290    14248  10036   9025   2572    -62  -2936       C  
ATOM   2559  OD1 ASP C 290     -33.480  52.697 -63.643  1.00 88.11           O  
ANISOU 2559  OD1 ASP C 290    14039  10594   8844   2761    314  -2794       O  
ATOM   2560  OD2 ASP C 290     -32.585  54.679 -63.959  1.00 92.90           O  
ANISOU 2560  OD2 ASP C 290    15071  10261   9966   2674   -208  -3188       O  
ATOM   2561  N   GLY C 291     -30.464  49.748 -63.015  1.00 66.37           N  
ANISOU 2561  N   GLY C 291    11345   8354   5519   1800   -169  -2039       N  
ATOM   2562  CA  GLY C 291     -31.016  48.430 -63.225  1.00 60.85           C  
ANISOU 2562  CA  GLY C 291    10334   8030   4758   1743    142  -1570       C  
ATOM   2563  C   GLY C 291     -30.888  48.012 -64.677  1.00 54.01           C  
ANISOU 2563  C   GLY C 291     9183   6885   4452   1558    137  -1216       C  
ATOM   2564  O   GLY C 291     -29.978  48.473 -65.394  1.00 45.00           O  
ANISOU 2564  O   GLY C 291     8067   5358   3674   1382   -141  -1216       O  
ATOM   2565  N   ILE C 292     -31.796  47.160 -65.118  1.00 44.73           N  
ANISOU 2565  N   ILE C 292     7736   5926   3334   1579    442   -919       N  
ATOM   2566  CA  ILE C 292     -31.725  46.579 -66.452  1.00 46.17           C  
ANISOU 2566  CA  ILE C 292     7675   5912   3955   1409    436   -601       C  
ATOM   2567  C   ILE C 292     -32.584  47.395 -67.407  1.00 39.72           C  
ANISOU 2567  C   ILE C 292     6750   4895   3445   1596    529   -715       C  
ATOM   2568  O   ILE C 292     -33.686  47.833 -67.063  1.00 42.48           O  
ANISOU 2568  O   ILE C 292     7046   5421   3672   1874    747   -891       O  
ATOM   2569  CB  ILE C 292     -32.155  45.103 -66.423  1.00 47.02           C  
ANISOU 2569  CB  ILE C 292     7581   6305   3981   1268    631   -213       C  
ATOM   2570  CG1 ILE C 292     -31.138  44.286 -65.622  1.00 48.39           C  
ANISOU 2570  CG1 ILE C 292     7887   6583   3914   1104    464    -32       C  
ATOM   2571  CG2 ILE C 292     -32.283  44.555 -67.829  1.00 43.02           C  
ANISOU 2571  CG2 ILE C 292     6854   5599   3890   1142    630     16       C  
ATOM   2572  CD1 ILE C 292     -31.529  42.854 -65.425  1.00 49.17           C  
ANISOU 2572  CD1 ILE C 292     7875   6885   3922    965    625    371       C  
ATOM   2573  N   HIS C 293     -32.082  47.588 -68.617  1.00 36.82           N  
ANISOU 2573  N   HIS C 293     6334   4198   3458   1471    370   -593       N  
ATOM   2574  CA  HIS C 293     -32.793  48.314 -69.655  1.00 36.55           C  
ANISOU 2574  CA  HIS C 293     6217   3956   3713   1633    399   -617       C  
ATOM   2575  C   HIS C 293     -32.780  47.472 -70.914  1.00 32.95           C  
ANISOU 2575  C   HIS C 293     5541   3499   3481   1455    407   -292       C  
ATOM   2576  O   HIS C 293     -31.848  46.729 -71.148  1.00 30.79           O  
ANISOU 2576  O   HIS C 293     5257   3206   3236   1221    320   -120       O  
ATOM   2577  CB  HIS C 293     -32.124  49.650 -69.941  1.00 40.95           C  
ANISOU 2577  CB  HIS C 293     7028   4052   4480   1654    154   -801       C  
ATOM   2578  CG  HIS C 293     -32.068  50.563 -68.761  1.00 44.06           C  
ANISOU 2578  CG  HIS C 293     7713   4355   4674   1827     78  -1207       C  
ATOM   2579  ND1 HIS C 293     -33.030  51.514 -68.513  1.00 46.04           N  
ANISOU 2579  ND1 HIS C 293     8070   4504   4918   2220    162  -1509       N  
ATOM   2580  CD2 HIS C 293     -31.166  50.671 -67.761  1.00 46.14           C  
ANISOU 2580  CD2 HIS C 293     8193   4620   4717   1691   -101  -1396       C  
ATOM   2581  CE1 HIS C 293     -32.722  52.170 -67.411  1.00 52.45           C  
ANISOU 2581  CE1 HIS C 293     9195   5234   5500   2323     55  -1905       C  
ATOM   2582  NE2 HIS C 293     -31.595  51.678 -66.936  1.00 49.00           N  
ANISOU 2582  NE2 HIS C 293     8832   4869   4917   1981   -123  -1841       N  
ATOM   2583  N   SER C 294     -33.820  47.591 -71.716  1.00 36.37           N  
ANISOU 2583  N   SER C 294     5795   3969   4057   1601    494   -236       N  
ATOM   2584  CA  SER C 294     -33.897  46.835 -72.953  1.00 33.81           C  
ANISOU 2584  CA  SER C 294     5296   3657   3892   1450    469     12       C  
ATOM   2585  C   SER C 294     -34.289  47.749 -74.105  1.00 34.57           C  
ANISOU 2585  C   SER C 294     5386   3551   4197   1603    367     40       C  
ATOM   2586  O   SER C 294     -34.858  48.823 -73.913  1.00 37.32           O  
ANISOU 2586  O   SER C 294     5796   3781   4602   1878    354   -113       O  
ATOM   2587  CB  SER C 294     -34.884  45.664 -72.829  1.00 35.78           C  
ANISOU 2587  CB  SER C 294     5279   4246   4069   1386    636    132       C  
ATOM   2588  OG  SER C 294     -34.359  44.630 -72.011  1.00 36.18           O  
ANISOU 2588  OG  SER C 294     5377   4414   3957   1186    690    226       O  
ATOM   2589  N   ILE C 295     -33.939  47.318 -75.313  1.00 34.77           N  
ANISOU 2589  N   ILE C 295     5368   3529   4315   1451    284    237       N  
ATOM   2590  CA  ILE C 295     -34.338  47.983 -76.547  1.00 35.56           C  
ANISOU 2590  CA  ILE C 295     5459   3510   4544   1569    175    347       C  
ATOM   2591  C   ILE C 295     -34.861  46.910 -77.484  1.00 36.04           C  
ANISOU 2591  C   ILE C 295     5316   3809   4570   1470    169    476       C  
ATOM   2592  O   ILE C 295     -34.270  45.831 -77.585  1.00 35.15           O  
ANISOU 2592  O   ILE C 295     5195   3768   4391   1252    199    520       O  
ATOM   2593  CB  ILE C 295     -33.172  48.749 -77.209  1.00 37.26           C  
ANISOU 2593  CB  ILE C 295     5900   3410   4846   1452     51    470       C  
ATOM   2594  CG1 ILE C 295     -32.508  49.705 -76.220  1.00 41.36           C  
ANISOU 2594  CG1 ILE C 295     6640   3646   5427   1450     -4    310       C  
ATOM   2595  CG2 ILE C 295     -33.665  49.515 -78.453  1.00 39.86           C  
ANISOU 2595  CG2 ILE C 295     6264   3618   5261   1595    -66    649       C  
ATOM   2596  CD1 ILE C 295     -31.171  50.226 -76.694  1.00 42.28           C  
ANISOU 2596  CD1 ILE C 295     6905   3505   5653   1195   -113    462       C  
ATOM   2597  N   ARG C 296     -35.956  47.197 -78.176  1.00 38.13           N  
ANISOU 2597  N   ARG C 296     5423   4179   4887   1647     96    518       N  
ATOM   2598  CA  ARG C 296     -36.521  46.249 -79.124  1.00 37.33           C  
ANISOU 2598  CA  ARG C 296     5138   4301   4745   1534     18    600       C  
ATOM   2599  C   ARG C 296     -36.155  46.656 -80.544  1.00 34.65           C  
ANISOU 2599  C   ARG C 296     4941   3873   4352   1553   -148    755       C  
ATOM   2600  O   ARG C 296     -36.294  47.825 -80.919  1.00 35.55           O  
ANISOU 2600  O   ARG C 296     5153   3830   4523   1760   -243    853       O  
ATOM   2601  CB  ARG C 296     -38.039  46.153 -78.976  1.00 40.57           C  
ANISOU 2601  CB  ARG C 296     5197   4994   5224   1677     11    560       C  
ATOM   2602  CG  ARG C 296     -38.652  45.126 -79.914  1.00 42.24           C  
ANISOU 2602  CG  ARG C 296     5206   5428   5413   1492   -134    612       C  
ATOM   2603  CD  ARG C 296     -40.154  45.050 -79.757  1.00 45.03           C  
ANISOU 2603  CD  ARG C 296     5119   6113   5878   1587   -161    598       C  
ATOM   2604  NE  ARG C 296     -40.533  44.543 -78.442  1.00 44.72           N  
ANISOU 2604  NE  ARG C 296     4875   6243   5872   1487     94    544       N  
ATOM   2605  CZ  ARG C 296     -41.752  44.657 -77.931  1.00 50.20           C  
ANISOU 2605  CZ  ARG C 296     5138   7278   6657   1611    194    533       C  
ATOM   2606  NH1 ARG C 296     -42.707  45.268 -78.624  1.00 53.53           N  
ANISOU 2606  NH1 ARG C 296     5268   7883   7189   1872     21    553       N  
ATOM   2607  NH2 ARG C 296     -42.016  44.170 -76.727  1.00 52.60           N  
ANISOU 2607  NH2 ARG C 296     5280   7781   6926   1492    474    528       N  
ATOM   2608  N   TYR C 297     -35.679  45.694 -81.326  1.00 33.08           N  
ANISOU 2608  N   TYR C 297     4783   3762   4025   1356   -179    783       N  
ATOM   2609  CA  TYR C 297     -35.382  45.921 -82.731  1.00 35.16           C  
ANISOU 2609  CA  TYR C 297     5175   4051   4132   1371   -304    925       C  
ATOM   2610  C   TYR C 297     -36.243  45.010 -83.594  1.00 35.06           C  
ANISOU 2610  C   TYR C 297     5023   4298   4000   1322   -471    861       C  
ATOM   2611  O   TYR C 297     -36.803  44.014 -83.125  1.00 35.45           O  
ANISOU 2611  O   TYR C 297     4897   4449   4124   1186   -470    715       O  
ATOM   2612  CB  TYR C 297     -33.895  45.690 -83.027  1.00 33.79           C  
ANISOU 2612  CB  TYR C 297     5199   3792   3849   1221   -182    977       C  
ATOM   2613  CG  TYR C 297     -33.004  46.647 -82.285  1.00 33.46           C  
ANISOU 2613  CG  TYR C 297     5271   3500   3942   1203    -85   1053       C  
ATOM   2614  CD1 TYR C 297     -32.755  47.922 -82.777  1.00 34.54           C  
ANISOU 2614  CD1 TYR C 297     5555   3457   4111   1263   -143   1269       C  
ATOM   2615  CD2 TYR C 297     -32.429  46.284 -81.073  1.00 31.22           C  
ANISOU 2615  CD2 TYR C 297     4965   3138   3757   1107     24    921       C  
ATOM   2616  CE1 TYR C 297     -31.947  48.803 -82.092  1.00 36.17           C  
ANISOU 2616  CE1 TYR C 297     5881   3379   4484   1186   -104   1315       C  
ATOM   2617  CE2 TYR C 297     -31.622  47.155 -80.384  1.00 31.92           C  
ANISOU 2617  CE2 TYR C 297     5158   3008   3961   1059     49    948       C  
ATOM   2618  CZ  TYR C 297     -31.385  48.407 -80.886  1.00 35.32           C  
ANISOU 2618  CZ  TYR C 297     5729   3230   4463   1080    -20   1123       C  
ATOM   2619  OH  TYR C 297     -30.577  49.265 -80.187  1.00 38.95           O  
ANISOU 2619  OH  TYR C 297     6304   3419   5076    972    -41   1125       O  
ATOM   2620  N   GLY C 298     -36.340  45.366 -84.869  1.00 38.04           N  
ANISOU 2620  N   GLY C 298     5495   4779   4179   1405   -637    988       N  
ATOM   2621  CA  GLY C 298     -37.101  44.576 -85.812  1.00 38.17           C  
ANISOU 2621  CA  GLY C 298     5421   5055   4027   1354   -865    897       C  
ATOM   2622  C   GLY C 298     -36.434  44.532 -87.168  1.00 38.15           C  
ANISOU 2622  C   GLY C 298     5677   5166   3653   1359   -927    973       C  
ATOM   2623  O   GLY C 298     -35.808  45.507 -87.591  1.00 39.23           O  
ANISOU 2623  O   GLY C 298     5992   5237   3676   1460   -861   1226       O  
ATOM   2624  N   ILE C 299     -36.554  43.399 -87.851  1.00 39.31           N  
ANISOU 2624  N   ILE C 299     5862   5479   3595   1238  -1049    753       N  
ATOM   2625  CA  ILE C 299     -36.029  43.213 -89.199  1.00 41.25           C  
ANISOU 2625  CA  ILE C 299     6360   5921   3392   1275  -1107    750       C  
ATOM   2626  C   ILE C 299     -37.204  42.861 -90.097  1.00 45.14           C  
ANISOU 2626  C   ILE C 299     6779   6686   3687   1280  -1508    637       C  
ATOM   2627  O   ILE C 299     -37.866  41.840 -89.879  1.00 45.72           O  
ANISOU 2627  O   ILE C 299     6712   6764   3897   1105  -1674    355       O  
ATOM   2628  CB  ILE C 299     -34.960  42.108 -89.246  1.00 42.44           C  
ANISOU 2628  CB  ILE C 299     6681   6015   3428   1178   -902    495       C  
ATOM   2629  CG1 ILE C 299     -33.921  42.314 -88.143  1.00 40.69           C  
ANISOU 2629  CG1 ILE C 299     6433   5544   3481   1148   -572    581       C  
ATOM   2630  CG2 ILE C 299     -34.293  42.051 -90.613  1.00 46.50           C  
ANISOU 2630  CG2 ILE C 299     7456   6796   3417   1280   -870    492       C  
ATOM   2631  CD1 ILE C 299     -33.161  41.048 -87.790  1.00 39.47           C  
ANISOU 2631  CD1 ILE C 299     6345   5269   3382   1080   -432    306       C  
ATOM   2632  N   ASN C 300     -37.473  43.698 -91.097  1.00 47.47           N  
ANISOU 2632  N   ASN C 300     8331   5303   4402    610  -1663    496       N  
ATOM   2633  CA  ASN C 300     -38.552  43.378 -92.018  1.00 51.11           C  
ANISOU 2633  CA  ASN C 300     8680   6051   4687    450  -1941    574       C  
ATOM   2634  C   ASN C 300     -38.050  42.381 -93.059  1.00 54.90           C  
ANISOU 2634  C   ASN C 300     9431   6434   4993    165  -2023    324       C  
ATOM   2635  O   ASN C 300     -36.897  41.942 -93.030  1.00 47.42           O  
ANISOU 2635  O   ASN C 300     8735   5189   4095    141  -1847    115       O  
ATOM   2636  CB  ASN C 300     -39.141  44.653 -92.636  1.00 51.28           C  
ANISOU 2636  CB  ASN C 300     8615   6298   4570    698  -2009    823       C  
ATOM   2637  CG  ASN C 300     -38.250  45.293 -93.701  1.00 50.63           C  
ANISOU 2637  CG  ASN C 300     8843   6106   4289    777  -1940    796       C  
ATOM   2638  OD1 ASN C 300     -37.098  44.914 -93.900  1.00 50.16           O  
ANISOU 2638  OD1 ASN C 300     9058   5806   4195    689  -1801    575       O  
ATOM   2639  ND2 ASN C 300     -38.796  46.295 -94.382  1.00 52.36           N  
ANISOU 2639  ND2 ASN C 300     8989   6526   4379    965  -2029   1065       N  
ATOM   2640  N   LYS C 301     -38.920  42.010 -93.998  1.00 57.87           N  
ANISOU 2640  N   LYS C 301     9747   7092   5151    -55  -2288    333       N  
ATOM   2641  CA  LYS C 301     -38.580  40.898 -94.875  1.00 61.18           C  
ANISOU 2641  CA  LYS C 301    10418   7415   5412   -379  -2368     20       C  
ATOM   2642  C   LYS C 301     -37.529  41.255 -95.918  1.00 59.61           C  
ANISOU 2642  C   LYS C 301    10550   7141   4957   -298  -2247   -137       C  
ATOM   2643  O   LYS C 301     -36.937  40.346 -96.508  1.00 60.32           O  
ANISOU 2643  O   LYS C 301    10901   7067   4948   -493  -2211   -463       O  
ATOM   2644  CB  LYS C 301     -39.833  40.349 -95.560  1.00 67.43           C  
ANISOU 2644  CB  LYS C 301    11042   8573   6006   -714  -2703     36       C  
ATOM   2645  CG  LYS C 301     -39.725  38.856 -95.830  1.00 73.55           C  
ANISOU 2645  CG  LYS C 301    12014   9128   6804  -1127  -2772   -325       C  
ATOM   2646  CD  LYS C 301     -40.973  38.280 -96.466  1.00 81.86           C  
ANISOU 2646  CD  LYS C 301    12897  10552   7653  -1542  -3122   -339       C  
ATOM   2647  CE  LYS C 301     -40.674  36.920 -97.077  1.00 87.48           C  
ANISOU 2647  CE  LYS C 301    13935  10989   8315  -1961  -3166   -800       C  
ATOM   2648  NZ  LYS C 301     -39.371  36.925 -97.800  1.00 88.42           N  
ANISOU 2648  NZ  LYS C 301    14473  10844   8278  -1816  -2936  -1119       N  
ATOM   2649  N   ASN C 302     -37.268  42.537 -96.149  1.00 58.06           N  
ANISOU 2649  N   ASN C 302    10352   7045   4663    -14  -2166     86       N  
ATOM   2650  CA  ASN C 302     -36.174  42.954 -97.013  1.00 58.85           C  
ANISOU 2650  CA  ASN C 302    10739   7082   4541     70  -2017     -7       C  
ATOM   2651  C   ASN C 302     -34.852  43.075 -96.264  1.00 54.44           C  
ANISOU 2651  C   ASN C 302    10331   6146   4208    239  -1701   -101       C  
ATOM   2652  O   ASN C 302     -33.867  43.546 -96.841  1.00 54.20           O  
ANISOU 2652  O   ASN C 302    10497   6072   4024    329  -1544   -129       O  
ATOM   2653  CB  ASN C 302     -36.512  44.286 -97.693  1.00 62.29           C  
ANISOU 2653  CB  ASN C 302    11102   7796   4768    262  -2089    334       C  
ATOM   2654  CG  ASN C 302     -37.674  44.172 -98.664  1.00 70.25           C  
ANISOU 2654  CG  ASN C 302    11956   9278   5459     85  -2413    455       C  
ATOM   2655  OD1 ASN C 302     -37.863  43.140 -99.312  1.00 73.18           O  
ANISOU 2655  OD1 ASN C 302    12409   9786   5609   -241  -2559    181       O  
ATOM   2656  ND2 ASN C 302     -38.459  45.239 -98.772  1.00 72.83           N  
ANISOU 2656  ND2 ASN C 302    12051   9860   5760    297  -2524    869       N  
ATOM   2657  N   GLY C 303     -34.809  42.665 -94.996  1.00 50.94           N  
ANISOU 2657  N   GLY C 303     9769   5486   4100    266  -1610   -121       N  
ATOM   2658  CA  GLY C 303     -33.597  42.751 -94.211  1.00 46.79           C  
ANISOU 2658  CA  GLY C 303     9330   4679   3767    401  -1336   -179       C  
ATOM   2659  C   GLY C 303     -33.306  44.109 -93.618  1.00 45.08           C  
ANISOU 2659  C   GLY C 303     9049   4440   3638    640  -1201     35       C  
ATOM   2660  O   GLY C 303     -32.213  44.306 -93.077  1.00 45.55           O  
ANISOU 2660  O   GLY C 303     9183   4323   3801    715   -982    -11       O  
ATOM   2661  N   GLU C 304     -34.241  45.052 -93.699  1.00 44.70           N  
ANISOU 2661  N   GLU C 304     8861   4561   3561    758  -1318    265       N  
ATOM   2662  CA  GLU C 304     -34.024  46.382 -93.146  1.00 45.27           C  
ANISOU 2662  CA  GLU C 304     8910   4537   3754    990  -1175    436       C  
ATOM   2663  C   GLU C 304     -34.256  46.384 -91.641  1.00 42.87           C  
ANISOU 2663  C   GLU C 304     8409   4159   3721   1061  -1085    426       C  
ATOM   2664  O   GLU C 304     -35.151  45.706 -91.130  1.00 43.39           O  
ANISOU 2664  O   GLU C 304     8259   4357   3870    993  -1206    437       O  
ATOM   2665  CB  GLU C 304     -34.949  47.397 -93.814  1.00 50.23           C  
ANISOU 2665  CB  GLU C 304     9464   5338   4283   1145  -1310    711       C  
ATOM   2666  CG  GLU C 304     -34.934  47.323 -95.324  1.00 55.80           C  
ANISOU 2666  CG  GLU C 304    10302   6242   4655   1044  -1449    765       C  
ATOM   2667  CD  GLU C 304     -35.785  48.399 -95.957  1.00 63.18           C  
ANISOU 2667  CD  GLU C 304    11135   7368   5503   1228  -1577   1122       C  
ATOM   2668  OE1 GLU C 304     -35.316  49.553 -96.049  1.00 65.51           O  
ANISOU 2668  OE1 GLU C 304    11543   7490   5859   1413  -1438   1308       O  
ATOM   2669  OE2 GLU C 304     -36.926  48.090 -96.355  1.00 67.45           O  
ANISOU 2669  OE2 GLU C 304    11470   8231   5925   1179  -1820   1243       O  
ATOM   2670  N   LEU C 305     -33.452  47.179 -90.936  1.00 41.31           N  
ANISOU 2670  N   LEU C 305     8277   3783   3637   1169   -873    410       N  
ATOM   2671  CA  LEU C 305     -33.422  47.191 -89.480  1.00 40.41           C  
ANISOU 2671  CA  LEU C 305     8001   3636   3716   1205   -753    354       C  
ATOM   2672  C   LEU C 305     -34.179  48.392 -88.927  1.00 40.61           C  
ANISOU 2672  C   LEU C 305     7918   3664   3849   1430   -708    461       C  
ATOM   2673  O   LEU C 305     -34.093  49.501 -89.467  1.00 41.70           O  
ANISOU 2673  O   LEU C 305     8199   3671   3975   1572   -659    557       O  
ATOM   2674  CB  LEU C 305     -31.981  47.217 -88.969  1.00 40.63           C  
ANISOU 2674  CB  LEU C 305     8153   3512   3772   1135   -545    228       C  
ATOM   2675  CG  LEU C 305     -31.805  47.070 -87.455  1.00 42.74           C  
ANISOU 2675  CG  LEU C 305     8238   3825   4176   1116   -430    164       C  
ATOM   2676  CD1 LEU C 305     -32.288  45.704 -86.985  1.00 41.44           C  
ANISOU 2676  CD1 LEU C 305     7877   3792   4076   1005   -533    174       C  
ATOM   2677  CD2 LEU C 305     -30.352  47.291 -87.075  1.00 43.28           C  
ANISOU 2677  CD2 LEU C 305     8410   3805   4228   1037   -243     77       C  
ATOM   2678  N   PHE C 306     -34.903  48.169 -87.833  1.00 40.88           N  
ANISOU 2678  N   PHE C 306     7697   3838   3996   1473   -703    451       N  
ATOM   2679  CA  PHE C 306     -35.688  49.214 -87.194  1.00 41.84           C  
ANISOU 2679  CA  PHE C 306     7687   3984   4227   1723   -625    508       C  
ATOM   2680  C   PHE C 306     -35.554  49.112 -85.683  1.00 39.27           C  
ANISOU 2680  C   PHE C 306     7201   3738   3982   1704   -472    363       C  
ATOM   2681  O   PHE C 306     -35.431  48.016 -85.130  1.00 39.60           O  
ANISOU 2681  O   PHE C 306     7099   3936   4011   1518   -512    335       O  
ATOM   2682  CB  PHE C 306     -37.171  49.119 -87.561  1.00 45.38           C  
ANISOU 2682  CB  PHE C 306     7884   4688   4671   1850   -812    710       C  
ATOM   2683  CG  PHE C 306     -37.435  49.130 -89.040  1.00 47.77           C  
ANISOU 2683  CG  PHE C 306     8286   5030   4835   1835  -1003    879       C  
ATOM   2684  CD1 PHE C 306     -37.772  50.308 -89.685  1.00 50.76           C  
ANISOU 2684  CD1 PHE C 306     8729   5329   5228   2093   -994   1073       C  
ATOM   2685  CD2 PHE C 306     -37.352  47.963 -89.782  1.00 48.17           C  
ANISOU 2685  CD2 PHE C 306     8367   5201   4735   1561  -1185    845       C  
ATOM   2686  CE1 PHE C 306     -38.017  50.324 -91.040  1.00 52.91           C  
ANISOU 2686  CE1 PHE C 306     9061   5718   5326   2067  -1180   1270       C  
ATOM   2687  CE2 PHE C 306     -37.594  47.973 -91.139  1.00 50.20           C  
ANISOU 2687  CE2 PHE C 306     8709   5565   4801   1517  -1361    968       C  
ATOM   2688  CZ  PHE C 306     -37.927  49.155 -91.769  1.00 53.64           C  
ANISOU 2688  CZ  PHE C 306     9174   5998   5210   1765  -1368   1201       C  
ATOM   2689  N   SER C 307     -35.569  50.264 -85.023  1.00 40.44           N  
ANISOU 2689  N   SER C 307     7382   3773   4211   1891   -289    273       N  
ATOM   2690  CA  SER C 307     -35.852  50.311 -83.597  1.00 43.02           C  
ANISOU 2690  CA  SER C 307     7493   4282   4569   1929   -155    142       C  
ATOM   2691  C   SER C 307     -37.357  50.447 -83.418  1.00 46.43           C  
ANISOU 2691  C   SER C 307     7633   4955   5055   2171   -211    277       C  
ATOM   2692  O   SER C 307     -38.052  51.007 -84.271  1.00 48.04           O  
ANISOU 2692  O   SER C 307     7853   5090   5309   2385   -286    442       O  
ATOM   2693  CB  SER C 307     -35.121  51.470 -82.916  1.00 44.46           C  
ANISOU 2693  CB  SER C 307     7865   4237   4789   1982     89    -94       C  
ATOM   2694  OG  SER C 307     -35.538  52.718 -83.436  1.00 48.01           O  
ANISOU 2694  OG  SER C 307     8477   4401   5362   2256    161    -63       O  
ATOM   2695  N   ILE C 308     -37.867  49.903 -82.317  1.00 46.36           N  
ANISOU 2695  N   ILE C 308     7317   5279   5019   2134   -178    250       N  
ATOM   2696  CA  ILE C 308     -39.306  49.793 -82.116  1.00 50.40           C  
ANISOU 2696  CA  ILE C 308     7472   6124   5555   2316   -246    417       C  
ATOM   2697  C   ILE C 308     -39.672  50.397 -80.770  1.00 52.13           C  
ANISOU 2697  C   ILE C 308     7503   6531   5771   2503     -7    247       C  
ATOM   2698  O   ILE C 308     -39.092  50.031 -79.742  1.00 46.51           O  
ANISOU 2698  O   ILE C 308     6739   5965   4967   2318     97     94       O  
ATOM   2699  CB  ILE C 308     -39.785  48.333 -82.203  1.00 51.85           C  
ANISOU 2699  CB  ILE C 308     7398   6618   5685   2044   -474    609       C  
ATOM   2700  CG1 ILE C 308     -39.377  47.740 -83.552  1.00 52.85           C  
ANISOU 2700  CG1 ILE C 308     7751   6541   5787   1850   -686    694       C  
ATOM   2701  CG2 ILE C 308     -41.292  48.256 -81.994  1.00 54.97           C  
ANISOU 2701  CG2 ILE C 308     7377   7417   6091   2200   -551    812       C  
ATOM   2702  CD1 ILE C 308     -40.259  46.643 -84.035  1.00 54.30           C  
ANISOU 2702  CD1 ILE C 308     7708   6979   5945   1655   -943    893       C  
ATOM   2703  N   ASN C 309     -40.621  51.329 -80.786  1.00 55.34           N  
ANISOU 2703  N   ASN C 309     7803   6957   6267   2883     89    279       N  
ATOM   2704  CA  ASN C 309     -41.226  51.828 -79.559  1.00 56.49           C  
ANISOU 2704  CA  ASN C 309     7711   7357   6396   3111    323    118       C  
ATOM   2705  C   ASN C 309     -42.182  50.772 -79.014  1.00 54.25           C  
ANISOU 2705  C   ASN C 309     6941   7659   6011   3009    208    330       C  
ATOM   2706  O   ASN C 309     -43.189  50.453 -79.652  1.00 55.66           O  
ANISOU 2706  O   ASN C 309     6871   8049   6230   3093     28    625       O  
ATOM   2707  CB  ASN C 309     -41.958  53.141 -79.839  1.00 57.80           C  
ANISOU 2707  CB  ASN C 309     7915   7316   6731   3605    480    111       C  
ATOM   2708  CG  ASN C 309     -42.377  53.867 -78.571  1.00 61.21           C  
ANISOU 2708  CG  ASN C 309     8208   7896   7154   3882    801   -176       C  
ATOM   2709  OD1 ASN C 309     -43.022  53.293 -77.697  1.00 62.09           O  
ANISOU 2709  OD1 ASN C 309     7927   8535   7129   3862    834   -153       O  
ATOM   2710  ND2 ASN C 309     -42.013  55.142 -78.471  1.00 63.63           N  
ANISOU 2710  ND2 ASN C 309     8844   7731   7602   4132   1050   -455       N  
ATOM   2711  N   THR C 310     -41.870  50.216 -77.841  1.00 53.47           N  
ANISOU 2711  N   THR C 310     6687   7862   5769   2797    301    212       N  
ATOM   2712  CA  THR C 310     -42.687  49.127 -77.319  1.00 54.06           C  
ANISOU 2712  CA  THR C 310     6304   8481   5754   2635    183    463       C  
ATOM   2713  C   THR C 310     -44.045  49.602 -76.813  1.00 58.58           C  
ANISOU 2713  C   THR C 310     6467   9477   6312   2986    309    536       C  
ATOM   2714  O   THR C 310     -44.956  48.780 -76.660  1.00 60.11           O  
ANISOU 2714  O   THR C 310     6241  10137   6461   2879    173    828       O  
ATOM   2715  CB  THR C 310     -41.939  48.388 -76.206  1.00 53.24           C  
ANISOU 2715  CB  THR C 310     6128   8610   5492   2311    244    387       C  
ATOM   2716  OG1 THR C 310     -41.744  49.264 -75.090  1.00 55.09           O  
ANISOU 2716  OG1 THR C 310     6357   8982   5594   2478    545     61       O  
ATOM   2717  CG2 THR C 310     -40.583  47.900 -76.710  1.00 49.25           C  
ANISOU 2717  CG2 THR C 310     5985   7712   5015   2008    135    347       C  
ATOM   2718  N   ALA C 311     -44.211  50.902 -76.563  1.00 61.11           N  
ANISOU 2718  N   ALA C 311     6895   9639   6686   3404    576    284       N  
ATOM   2719  CA  ALA C 311     -45.501  51.398 -76.095  1.00 65.78           C  
ANISOU 2719  CA  ALA C 311     7085  10629   7279   3812    738    343       C  
ATOM   2720  C   ALA C 311     -46.455  51.679 -77.252  1.00 70.96           C  
ANISOU 2720  C   ALA C 311     7614  11236   8111   4101    579    670       C  
ATOM   2721  O   ALA C 311     -47.654  51.395 -77.152  1.00 70.77           O  
ANISOU 2721  O   ALA C 311     7101  11727   8061   4242    528    948       O  
ATOM   2722  CB  ALA C 311     -45.305  52.655 -75.246  1.00 68.82           C  
ANISOU 2722  CB  ALA C 311     7637  10856   7657   4164   1132   -106       C  
ATOM   2723  N   SER C 312     -45.946  52.227 -78.356  1.00 66.68           N  
ANISOU 2723  N   SER C 312     7472  10138   7725   4176    491    678       N  
ATOM   2724  CA  SER C 312     -46.779  52.610 -79.486  1.00 72.15           C  
ANISOU 2724  CA  SER C 312     8058  10795   8560   4468    342   1011       C  
ATOM   2725  C   SER C 312     -46.650  51.685 -80.688  1.00 69.08           C  
ANISOU 2725  C   SER C 312     7719  10398   8130   4086    -52   1307       C  
ATOM   2726  O   SER C 312     -47.484  51.767 -81.596  1.00 71.03           O  
ANISOU 2726  O   SER C 312     7766  10803   8418   4240   -237   1641       O  
ATOM   2727  CB  SER C 312     -46.447  54.045 -79.923  1.00 73.42           C  
ANISOU 2727  CB  SER C 312     8607  10354   8935   4896    547    863       C  
ATOM   2728  OG  SER C 312     -45.125  54.122 -80.432  1.00 69.12           O  
ANISOU 2728  OG  SER C 312     8587   9269   8406   4607    492    695       O  
ATOM   2729  N   ASN C 313     -45.635  50.819 -80.721  1.00 64.13           N  
ANISOU 2729  N   ASN C 313     7342   9613   7412   3604   -176   1188       N  
ATOM   2730  CA  ASN C 313     -45.317  49.891 -81.805  1.00 63.68           C  
ANISOU 2730  CA  ASN C 313     7414   9475   7304   3212   -505   1360       C  
ATOM   2731  C   ASN C 313     -44.845  50.592 -83.074  1.00 63.18           C  
ANISOU 2731  C   ASN C 313     7728   8971   7307   3334   -578   1399       C  
ATOM   2732  O   ASN C 313     -44.635  49.917 -84.092  1.00 61.68           O  
ANISOU 2732  O   ASN C 313     7650   8743   7041   3044   -841   1523       O  
ATOM   2733  CB  ASN C 313     -46.490  48.960 -82.150  1.00 68.07           C  
ANISOU 2733  CB  ASN C 313     7515  10555   7793   3036   -784   1705       C  
ATOM   2734  CG  ASN C 313     -46.617  47.802 -81.179  1.00 69.72           C  
ANISOU 2734  CG  ASN C 313     7451  11116   7923   2676   -814   1719       C  
ATOM   2735  OD1 ASN C 313     -45.664  47.453 -80.479  1.00 66.79           O  
ANISOU 2735  OD1 ASN C 313     7279  10570   7529   2476   -699   1505       O  
ATOM   2736  ND2 ASN C 313     -47.800  47.201 -81.128  1.00 73.80           N  
ANISOU 2736  ND2 ASN C 313     7483  12161   8397   2580   -976   2013       N  
ATOM   2737  N   LYS C 314     -44.661  51.911 -83.054  1.00 64.98           N  
ANISOU 2737  N   LYS C 314     8164   8857   7669   3736   -346   1293       N  
ATOM   2738  CA  LYS C 314     -44.098  52.609 -84.201  1.00 65.19           C  
ANISOU 2738  CA  LYS C 314     8567   8440   7764   3824   -395   1361       C  
ATOM   2739  C   LYS C 314     -42.638  52.215 -84.394  1.00 60.92           C  
ANISOU 2739  C   LYS C 314     8451   7544   7150   3436   -409   1131       C  
ATOM   2740  O   LYS C 314     -41.918  51.910 -83.437  1.00 54.32           O  
ANISOU 2740  O   LYS C 314     7695   6663   6280   3245   -269    854       O  
ATOM   2741  CB  LYS C 314     -44.206  54.125 -84.019  1.00 69.45           C  
ANISOU 2741  CB  LYS C 314     9251   8619   8516   4334   -112   1303       C  
ATOM   2742  CG  LYS C 314     -45.565  54.611 -83.533  1.00 75.91           C  
ANISOU 2742  CG  LYS C 314     9638   9768   9438   4807      6   1460       C  
ATOM   2743  CD  LYS C 314     -45.524  56.090 -83.165  1.00 80.69           C  
ANISOU 2743  CD  LYS C 314    10457   9906  10298   5315    356   1297       C  
ATOM   2744  CE  LYS C 314     -46.678  56.860 -83.791  1.00 87.05           C  
ANISOU 2744  CE  LYS C 314    11004  10794  11275   5691    343   1650       C  
ATOM   2745  NZ  LYS C 314     -47.055  58.062 -82.989  1.00 92.51           N  
ANISOU 2745  NZ  LYS C 314    11713  11228  12209   6059    709   1415       N  
ATOM   2746  N   VAL C 315     -42.199  52.228 -85.647  1.00 59.04           N  
ANISOU 2746  N   VAL C 315     8458   7107   6867   3328   -575   1268       N  
ATOM   2747  CA  VAL C 315     -40.851  51.805 -85.999  1.00 55.85           C  
ANISOU 2747  CA  VAL C 315     8421   6423   6378   2982   -597   1092       C  
ATOM   2748  C   VAL C 315     -40.065  53.001 -86.514  1.00 57.36           C  
ANISOU 2748  C   VAL C 315     8997   6133   6665   3141   -451   1062       C  
ATOM   2749  O   VAL C 315     -40.625  53.955 -87.069  1.00 56.37           O  
ANISOU 2749  O   VAL C 315     8877   5891   6649   3474   -434   1282       O  
ATOM   2750  CB  VAL C 315     -40.868  50.666 -87.040  1.00 54.37           C  
ANISOU 2750  CB  VAL C 315     8215   6429   6013   2651   -899   1231       C  
ATOM   2751  CG1 VAL C 315     -41.697  49.499 -86.528  1.00 55.01           C  
ANISOU 2751  CG1 VAL C 315     7923   6938   6040   2455  -1049   1282       C  
ATOM   2752  CG2 VAL C 315     -41.410  51.166 -88.374  1.00 56.81           C  
ANISOU 2752  CG2 VAL C 315     8533   6789   6263   2804  -1072   1533       C  
ATOM   2753  N   THR C 316     -38.748  52.943 -86.323  1.00 53.22           N  
ANISOU 2753  N   THR C 316     8777   5335   6108   2896   -344    824       N  
ATOM   2754  CA  THR C 316     -37.836  53.975 -86.788  1.00 53.67           C  
ANISOU 2754  CA  THR C 316     9211   4939   6243   2941   -211    790       C  
ATOM   2755  C   THR C 316     -36.698  53.289 -87.537  1.00 50.66           C  
ANISOU 2755  C   THR C 316     9047   4510   5690   2585   -312    763       C  
ATOM   2756  O   THR C 316     -36.052  52.385 -86.983  1.00 48.36           O  
ANISOU 2756  O   THR C 316     8732   4331   5312   2316   -305    571       O  
ATOM   2757  CB  THR C 316     -37.286  54.811 -85.624  1.00 54.84           C  
ANISOU 2757  CB  THR C 316     9506   4802   6529   3000     83    475       C  
ATOM   2758  OG1 THR C 316     -38.356  55.538 -85.013  1.00 58.29           O  
ANISOU 2758  OG1 THR C 316     9767   5250   7130   3389    216    475       O  
ATOM   2759  CG2 THR C 316     -36.242  55.799 -86.126  1.00 56.41           C  
ANISOU 2759  CG2 THR C 316    10081   4541   6812   2921    203    438       C  
ATOM   2760  N   PRO C 317     -36.428  53.673 -88.781  1.00 51.84           N  
ANISOU 2760  N   PRO C 317     9390   4526   5783   2593   -395    971       N  
ATOM   2761  CA  PRO C 317     -35.411  52.956 -89.556  1.00 49.94           C  
ANISOU 2761  CA  PRO C 317     9324   4308   5344   2280   -478    937       C  
ATOM   2762  C   PRO C 317     -34.016  53.194 -89.002  1.00 47.93           C  
ANISOU 2762  C   PRO C 317     9296   3799   5118   2093   -275    700       C  
ATOM   2763  O   PRO C 317     -33.687  54.289 -88.538  1.00 49.95           O  
ANISOU 2763  O   PRO C 317     9643   3802   5533   2143    -86    618       O  
ATOM   2764  CB  PRO C 317     -35.565  53.536 -90.967  1.00 51.04           C  
ANISOU 2764  CB  PRO C 317     9563   4428   5403   2357   -583   1238       C  
ATOM   2765  CG  PRO C 317     -36.166  54.882 -90.754  1.00 54.80           C  
ANISOU 2765  CG  PRO C 317     9965   4719   6140   2632   -453   1365       C  
ATOM   2766  CD  PRO C 317     -37.073  54.740 -89.564  1.00 54.52           C  
ANISOU 2766  CD  PRO C 317     9726   4760   6229   2862   -409   1262       C  
ATOM   2767  N   ILE C 318     -33.204  52.144 -89.047  1.00 44.91           N  
ANISOU 2767  N   ILE C 318     8928   3545   4590   1823   -309    573       N  
ATOM   2768  CA  ILE C 318     -31.798  52.193 -88.667  1.00 45.09           C  
ANISOU 2768  CA  ILE C 318     9111   3430   4592   1617   -148    401       C  
ATOM   2769  C   ILE C 318     -30.977  51.820 -89.889  1.00 47.50           C  
ANISOU 2769  C   ILE C 318     9579   3756   4712   1469   -199    486       C  
ATOM   2770  O   ILE C 318     -31.058  50.683 -90.372  1.00 48.13           O  
ANISOU 2770  O   ILE C 318     9592   4039   4658   1379   -324    470       O  
ATOM   2771  CB  ILE C 318     -31.483  51.241 -87.506  1.00 42.16           C  
ANISOU 2771  CB  ILE C 318     8562   3237   4220   1470   -106    202       C  
ATOM   2772  CG1 ILE C 318     -32.209  51.676 -86.233  1.00 42.48           C  
ANISOU 2772  CG1 ILE C 318     8436   3316   4390   1600    -22     94       C  
ATOM   2773  CG2 ILE C 318     -29.982  51.174 -87.271  1.00 41.99           C  
ANISOU 2773  CG2 ILE C 318     8657   3159   4139   1251     31     84       C  
ATOM   2774  CD1 ILE C 318     -31.959  50.750 -85.071  1.00 41.12           C  
ANISOU 2774  CD1 ILE C 318     8052   3386   4185   1449      8    -39       C  
ATOM   2775  N   ASP C 319     -30.185  52.765 -90.385  1.00 48.84           N  
ANISOU 2775  N   ASP C 319     9902   3772   4881   1403    -87    544       N  
ATOM   2776  CA  ASP C 319     -29.300  52.476 -91.504  1.00 49.76           C  
ANISOU 2776  CA  ASP C 319    10162   3951   4794   1264    -97    622       C  
ATOM   2777  C   ASP C 319     -28.061  51.748 -91.002  1.00 46.86           C  
ANISOU 2777  C   ASP C 319     9833   3615   4357   1080     16    453       C  
ATOM   2778  O   ASP C 319     -27.564  52.015 -89.900  1.00 45.37           O  
ANISOU 2778  O   ASP C 319     9597   3357   4284   1000    141    316       O  
ATOM   2779  CB  ASP C 319     -28.919  53.763 -92.237  1.00 54.11           C  
ANISOU 2779  CB  ASP C 319    10824   4359   5378   1248    -21    799       C  
ATOM   2780  CG  ASP C 319     -30.136  54.556 -92.694  1.00 58.94           C  
ANISOU 2780  CG  ASP C 319    11363   4926   6106   1467   -114   1022       C  
ATOM   2781  OD1 ASP C 319     -31.049  53.952 -93.299  1.00 60.07           O  
ANISOU 2781  OD1 ASP C 319    11421   5278   6124   1575   -298   1141       O  
ATOM   2782  OD2 ASP C 319     -30.188  55.782 -92.442  1.00 61.83           O  
ANISOU 2782  OD2 ASP C 319    11752   5050   6692   1528     -8   1089       O  
ATOM   2783  N   ILE C 320     -27.579  50.805 -91.803  1.00 45.14           N  
ANISOU 2783  N   ILE C 320     9630   3575   3947   1000    -20    437       N  
ATOM   2784  CA  ILE C 320     -26.480  49.941 -91.388  1.00 44.69           C  
ANISOU 2784  CA  ILE C 320     9511   3618   3852    870     91    289       C  
ATOM   2785  C   ILE C 320     -25.159  50.662 -91.616  1.00 44.85           C  
ANISOU 2785  C   ILE C 320     9638   3602   3802    735    260    347       C  
ATOM   2786  O   ILE C 320     -24.883  51.150 -92.718  1.00 45.80           O  
ANISOU 2786  O   ILE C 320     9901   3729   3773    716    271    494       O  
ATOM   2787  CB  ILE C 320     -26.526  48.602 -92.138  1.00 44.13           C  
ANISOU 2787  CB  ILE C 320     9427   3704   3636    871     15    212       C  
ATOM   2788  CG1 ILE C 320     -27.830  47.858 -91.833  1.00 42.76           C  
ANISOU 2788  CG1 ILE C 320     9130   3568   3551    934   -165    162       C  
ATOM   2789  CG2 ILE C 320     -25.336  47.742 -91.764  1.00 42.88           C  
ANISOU 2789  CG2 ILE C 320     9202   3614   3474    801    162     99       C  
ATOM   2790  CD1 ILE C 320     -28.071  47.617 -90.360  1.00 39.70           C  
ANISOU 2790  CD1 ILE C 320     8549   3160   3374    937   -140    101       C  
ATOM   2791  N   LEU C 321     -24.347  50.741 -90.564  1.00 41.11           N  
ANISOU 2791  N   LEU C 321     9068   3138   3413    616    385    257       N  
ATOM   2792  CA  LEU C 321     -23.053  51.392 -90.634  1.00 42.06           C  
ANISOU 2792  CA  LEU C 321     9239   3272   3469    431    539    312       C  
ATOM   2793  C   LEU C 321     -22.077  50.530 -91.438  1.00 41.91           C  
ANISOU 2793  C   LEU C 321     9184   3484   3257    408    614    340       C  
ATOM   2794  O   LEU C 321     -22.316  49.336 -91.643  1.00 41.97           O  
ANISOU 2794  O   LEU C 321     9124   3596   3228    527    569    255       O  
ATOM   2795  CB  LEU C 321     -22.529  51.648 -89.218  1.00 43.16           C  
ANISOU 2795  CB  LEU C 321     9245   3435   3717    280    625    191       C  
ATOM   2796  CG  LEU C 321     -23.349  52.635 -88.377  1.00 43.76           C  
ANISOU 2796  CG  LEU C 321     9383   3279   3965    292    607    102       C  
ATOM   2797  CD1 LEU C 321     -22.908  52.613 -86.916  1.00 44.55           C  
ANISOU 2797  CD1 LEU C 321     9312   3513   4100    132    677    -72       C  
ATOM   2798  CD2 LEU C 321     -23.259  54.046 -88.936  1.00 45.77           C  
ANISOU 2798  CD2 LEU C 321     9883   3231   4277    221    661    206       C  
ATOM   2799  N   PRO C 322     -20.962  51.113 -91.899  1.00 42.16           N  
ANISOU 2799  N   PRO C 322     9257   3590   3172    253    745    454       N  
ATOM   2800  CA  PRO C 322     -20.120  50.408 -92.887  1.00 44.30           C  
ANISOU 2800  CA  PRO C 322     9506   4106   3222    278    840    494       C  
ATOM   2801  C   PRO C 322     -19.642  49.024 -92.472  1.00 45.33           C  
ANISOU 2801  C   PRO C 322     9447   4414   3363    381    905    361       C  
ATOM   2802  O   PRO C 322     -19.378  48.197 -93.354  1.00 46.27           O  
ANISOU 2802  O   PRO C 322     9587   4661   3331    499    962    314       O  
ATOM   2803  CB  PRO C 322     -18.938  51.367 -93.075  1.00 45.84           C  
ANISOU 2803  CB  PRO C 322     9704   4383   3331     47    985    659       C  
ATOM   2804  CG  PRO C 322     -19.505  52.705 -92.805  1.00 46.18           C  
ANISOU 2804  CG  PRO C 322     9909   4115   3524    -64    922    741       C  
ATOM   2805  CD  PRO C 322     -20.510  52.503 -91.700  1.00 44.06           C  
ANISOU 2805  CD  PRO C 322     9595   3676   3468     46    814    559       C  
ATOM   2806  N   LEU C 323     -19.514  48.731 -91.179  1.00 44.36           N  
ANISOU 2806  N   LEU C 323     9139   4307   3407    350    910    303       N  
ATOM   2807  CA  LEU C 323     -18.937  47.454 -90.771  1.00 44.77           C  
ANISOU 2807  CA  LEU C 323     8989   4523   3500    461    989    258       C  
ATOM   2808  C   LEU C 323     -19.973  46.362 -90.514  1.00 44.62           C  
ANISOU 2808  C   LEU C 323     8966   4366   3622    633    868    141       C  
ATOM   2809  O   LEU C 323     -19.594  45.266 -90.088  1.00 44.66           O  
ANISOU 2809  O   LEU C 323     8814   4432   3720    739    929    130       O  
ATOM   2810  CB  LEU C 323     -18.062  47.633 -89.527  1.00 44.00           C  
ANISOU 2810  CB  LEU C 323     8637   4615   3467    314   1066    328       C  
ATOM   2811  CG  LEU C 323     -16.721  48.341 -89.737  1.00 45.57           C  
ANISOU 2811  CG  LEU C 323     8748   5047   3519    117   1214    461       C  
ATOM   2812  CD1 LEU C 323     -15.945  48.414 -88.424  1.00 43.68           C  
ANISOU 2812  CD1 LEU C 323     8217   5062   3319    -59   1253    521       C  
ATOM   2813  CD2 LEU C 323     -15.904  47.655 -90.822  1.00 48.71           C  
ANISOU 2813  CD2 LEU C 323     9114   5626   3766    269   1368    518       C  
ATOM   2814  N   GLY C 324     -21.252  46.617 -90.751  1.00 44.16           N  
ANISOU 2814  N   GLY C 324     9055   4128   3596    659    701     85       N  
ATOM   2815  CA  GLY C 324     -22.256  45.571 -90.742  1.00 43.35           C  
ANISOU 2815  CA  GLY C 324     8958   3917   3594    774    574    -16       C  
ATOM   2816  C   GLY C 324     -23.294  45.759 -89.651  1.00 39.49           C  
ANISOU 2816  C   GLY C 324     8369   3360   3277    751    439     -9       C  
ATOM   2817  O   GLY C 324     -23.309  46.750 -88.921  1.00 39.70           O  
ANISOU 2817  O   GLY C 324     8349   3398   3337    668    449     31       O  
ATOM   2818  N   VAL C 325     -24.161  44.747 -89.540  1.00 38.99           N  
ANISOU 2818  N   VAL C 325     6395   4835   3586    842   1095    183       N  
ATOM   2819  CA  VAL C 325     -25.326  44.840 -88.658  1.00 39.61           C  
ANISOU 2819  CA  VAL C 325     6328   5010   3712   1012    857     91       C  
ATOM   2820  C   VAL C 325     -24.907  44.829 -87.190  1.00 38.05           C  
ANISOU 2820  C   VAL C 325     6029   4546   3884    758    889    236       C  
ATOM   2821  O   VAL C 325     -25.411  45.619 -86.382  1.00 36.90           O  
ANISOU 2821  O   VAL C 325     6032   4311   3678    867    780    338       O  
ATOM   2822  CB  VAL C 325     -26.320  43.706 -88.970  1.00 40.60           C  
ANISOU 2822  CB  VAL C 325     5982   5491   3953   1099    748   -355       C  
ATOM   2823  CG1 VAL C 325     -27.369  43.581 -87.869  1.00 38.91           C  
ANISOU 2823  CG1 VAL C 325     5535   5282   3967   1128    655   -509       C  
ATOM   2824  CG2 VAL C 325     -26.980  43.942 -90.329  1.00 45.77           C  
ANISOU 2824  CG2 VAL C 325     6729   6553   4110   1524    576   -598       C  
ATOM   2825  N   MET C 326     -24.008  43.918 -86.808  1.00 35.77           N  
ANISOU 2825  N   MET C 326     5491   4159   3941    485   1020    224       N  
ATOM   2826  CA  MET C 326     -23.601  43.865 -85.406  1.00 35.78           C  
ANISOU 2826  CA  MET C 326     5427   3989   4178    390    999    339       C  
ATOM   2827  C   MET C 326     -22.856  45.129 -85.003  1.00 35.69           C  
ANISOU 2827  C   MET C 326     5667   3802   4091    322    989    484       C  
ATOM   2828  O   MET C 326     -23.010  45.613 -83.875  1.00 37.99           O  
ANISOU 2828  O   MET C 326     6003   4028   4405    369    880    537       O  
ATOM   2829  CB  MET C 326     -22.738  42.631 -85.140  1.00 36.42           C  
ANISOU 2829  CB  MET C 326     5238   4026   4575    253   1121    297       C  
ATOM   2830  CG  MET C 326     -23.516  41.381 -84.747  1.00 38.45           C  
ANISOU 2830  CG  MET C 326     5286   4283   5041    308   1241    192       C  
ATOM   2831  SD  MET C 326     -24.792  41.625 -83.490  1.00 39.48           S  
ANISOU 2831  SD  MET C 326     5510   4350   5139    468   1213    230       S  
ATOM   2832  CE  MET C 326     -23.852  42.297 -82.112  1.00 39.80           C  
ANISOU 2832  CE  MET C 326     5757   4279   5087    561   1057    501       C  
ATOM   2833  N   ALA C 327     -22.046  45.678 -85.909  1.00 36.04           N  
ANISOU 2833  N   ALA C 327     5881   3745   4069    193   1167    500       N  
ATOM   2834  CA  ALA C 327     -21.383  46.946 -85.630  1.00 39.17           C  
ANISOU 2834  CA  ALA C 327     6516   3893   4473     66   1303    546       C  
ATOM   2835  C   ALA C 327     -22.399  48.065 -85.436  1.00 39.45           C  
ANISOU 2835  C   ALA C 327     6915   3836   4239    296   1239    688       C  
ATOM   2836  O   ALA C 327     -22.195  48.963 -84.611  1.00 39.40           O  
ANISOU 2836  O   ALA C 327     7003   3650   4320    222   1263    681       O  
ATOM   2837  CB  ALA C 327     -20.411  47.293 -86.756  1.00 41.85           C  
ANISOU 2837  CB  ALA C 327     7033   4055   4815   -139   1672    522       C  
ATOM   2838  N   THR C 328     -23.500  48.030 -86.195  1.00 39.31           N  
ANISOU 2838  N   THR C 328     7068   3973   3895    612   1142    752       N  
ATOM   2839  CA  THR C 328     -24.542  49.045 -86.057  1.00 40.01           C  
ANISOU 2839  CA  THR C 328     7483   4017   3704    936   1037    860       C  
ATOM   2840  C   THR C 328     -25.276  48.900 -84.728  1.00 39.15           C  
ANISOU 2840  C   THR C 328     7123   3998   3755    964    789    779       C  
ATOM   2841  O   THR C 328     -25.420  49.873 -83.973  1.00 37.39           O  
ANISOU 2841  O   THR C 328     7083   3592   3531    988    785    845       O  
ATOM   2842  CB  THR C 328     -25.519  48.948 -87.231  1.00 42.31           C  
ANISOU 2842  CB  THR C 328     7936   4572   3568   1374    916    838       C  
ATOM   2843  OG1 THR C 328     -24.789  49.011 -88.457  1.00 43.32           O  
ANISOU 2843  OG1 THR C 328     8356   4622   3481   1379   1187    936       O  
ATOM   2844  CG2 THR C 328     -26.513  50.093 -87.211  1.00 45.04           C  
ANISOU 2844  CG2 THR C 328     8670   4872   3571   1822    803    949       C  
ATOM   2845  N   LEU C 329     -25.756  47.689 -84.429  1.00 35.60           N  
ANISOU 2845  N   LEU C 329     6283   3788   3457    953    657    620       N  
ATOM   2846  CA  LEU C 329     -26.461  47.469 -83.172  1.00 35.45           C  
ANISOU 2846  CA  LEU C 329     6093   3800   3577    979    544    559       C  
ATOM   2847  C   LEU C 329     -25.575  47.810 -81.984  1.00 34.22           C  
ANISOU 2847  C   LEU C 329     5960   3473   3568    804    563    647       C  
ATOM   2848  O   LEU C 329     -26.040  48.406 -81.007  1.00 35.26           O  
ANISOU 2848  O   LEU C 329     6170   3556   3670    878    483    658       O  
ATOM   2849  CB  LEU C 329     -26.941  46.022 -83.080  1.00 35.39           C  
ANISOU 2849  CB  LEU C 329     5721   3951   3777    938    590    371       C  
ATOM   2850  CG  LEU C 329     -28.049  45.587 -84.038  1.00 36.74           C  
ANISOU 2850  CG  LEU C 329     5697   4386   3875   1115    539     71       C  
ATOM   2851  CD1 LEU C 329     -28.163  44.067 -84.045  1.00 35.56           C  
ANISOU 2851  CD1 LEU C 329     5168   4286   4059    940    743   -166       C  
ATOM   2852  CD2 LEU C 329     -29.366  46.239 -83.643  1.00 36.96           C  
ANISOU 2852  CD2 LEU C 329     5727   4517   3800   1364    389    -86       C  
ATOM   2853  N   THR C 330     -24.288  47.457 -82.061  1.00 33.90           N  
ANISOU 2853  N   THR C 330     5814   3387   3679    600    650    641       N  
ATOM   2854  CA  THR C 330     -23.377  47.748 -80.958  1.00 35.36           C  
ANISOU 2854  CA  THR C 330     5923   3525   3986    503    599    583       C  
ATOM   2855  C   THR C 330     -23.334  49.241 -80.664  1.00 35.80           C  
ANISOU 2855  C   THR C 330     6204   3404   3993    453    632    548       C  
ATOM   2856  O   THR C 330     -23.340  49.651 -79.498  1.00 37.33           O  
ANISOU 2856  O   THR C 330     6363   3622   4196    491    512    462       O  
ATOM   2857  CB  THR C 330     -21.977  47.220 -81.277  1.00 35.77           C  
ANISOU 2857  CB  THR C 330     5757   3602   4232    323    673    466       C  
ATOM   2858  OG1 THR C 330     -22.012  45.790 -81.343  1.00 34.29           O  
ANISOU 2858  OG1 THR C 330     5378   3535   4117    408    666    505       O  
ATOM   2859  CG2 THR C 330     -20.978  47.656 -80.207  1.00 38.32           C  
ANISOU 2859  CG2 THR C 330     5916   3974   4672    277    563    248       C  
ATOM   2860  N   GLN C 331     -23.320  50.071 -81.709  1.00 34.40           N  
ANISOU 2860  N   GLN C 331     6310   3023   3739    403    840    615       N  
ATOM   2861  CA  GLN C 331     -23.306  51.515 -81.494  1.00 38.21           C  
ANISOU 2861  CA  GLN C 331     7085   3219   4213    360   1000    600       C  
ATOM   2862  C   GLN C 331     -24.632  52.001 -80.923  1.00 39.21           C  
ANISOU 2862  C   GLN C 331     7373   3372   4155    640    821    693       C  
ATOM   2863  O   GLN C 331     -24.648  52.801 -79.979  1.00 39.53           O  
ANISOU 2863  O   GLN C 331     7447   3305   4268    597    810    589       O  
ATOM   2864  CB  GLN C 331     -22.979  52.241 -82.798  1.00 40.83           C  
ANISOU 2864  CB  GLN C 331     7821   3234   4460    313   1392    722       C  
ATOM   2865  CG  GLN C 331     -21.526  52.097 -83.208  1.00 41.99           C  
ANISOU 2865  CG  GLN C 331     7814   3250   4890    -68   1701    530       C  
ATOM   2866  CD  GLN C 331     -20.574  52.563 -82.115  1.00 43.14           C  
ANISOU 2866  CD  GLN C 331     7638   3342   5411   -377   1742    137       C  
ATOM   2867  OE1 GLN C 331     -20.738  53.649 -81.557  1.00 44.44           O  
ANISOU 2867  OE1 GLN C 331     7966   3275   5644   -423   1871     42       O  
ATOM   2868  NE2 GLN C 331     -19.576  51.742 -81.807  1.00 41.56           N  
ANISOU 2868  NE2 GLN C 331     6952   3388   5452   -547   1618   -153       N  
ATOM   2869  N   HIS C 332     -25.752  51.525 -81.474  1.00 38.59           N  
ANISOU 2869  N   HIS C 332     7334   3464   3864    926    681    802       N  
ATOM   2870  CA AHIS C 332     -27.058  51.950 -80.981  0.50 39.12           C  
ANISOU 2870  CA AHIS C 332     7477   3590   3796   1204    515    801       C  
ATOM   2871  CA BHIS C 332     -27.059  51.951 -80.981  0.50 39.12           C  
ANISOU 2871  CA BHIS C 332     7477   3590   3796   1204    515    801       C  
ATOM   2872  C   HIS C 332     -27.247  51.574 -79.518  1.00 36.82           C  
ANISOU 2872  C   HIS C 332     6934   3410   3645   1123    383    688       C  
ATOM   2873  O   HIS C 332     -27.826  52.343 -78.739  1.00 35.89           O  
ANISOU 2873  O   HIS C 332     6918   3223   3497   1214    334    650       O  
ATOM   2874  CB AHIS C 332     -28.165  51.331 -81.831  0.50 39.16           C  
ANISOU 2874  CB AHIS C 332     7405   3860   3615   1513    368    758       C  
ATOM   2875  CB BHIS C 332     -28.165  51.335 -81.839  0.50 39.18           C  
ANISOU 2875  CB BHIS C 332     7409   3862   3616   1514    369    759       C  
ATOM   2876  CG AHIS C 332     -28.806  52.290 -82.785  0.50 41.72           C  
ANISOU 2876  CG AHIS C 332     8034   4168   3649   1868    361    796       C  
ATOM   2877  CG BHIS C 332     -29.483  52.042 -81.736  0.50 39.97           C  
ANISOU 2877  CG BHIS C 332     7628   4020   3538   1892    216    698       C  
ATOM   2878  ND1AHIS C 332     -28.124  52.856 -83.840  0.50 45.08           N  
ANISOU 2878  ND1AHIS C 332     8742   4437   3950   1870    585    906       N  
ATOM   2879  ND1BHIS C 332     -30.400  51.768 -80.744  0.50 38.05           N  
ANISOU 2879  ND1BHIS C 332     7124   3912   3421   1917     96    514       N  
ATOM   2880  CD2AHIS C 332     -30.067  52.780 -82.846  0.50 43.31           C  
ANISOU 2880  CD2AHIS C 332     8272   4514   3671   2259    183    685       C  
ATOM   2881  CD2BHIS C 332     -30.045  53.000 -82.513  0.50 42.74           C  
ANISOU 2881  CD2BHIS C 332     8213   4377   3649   2205    203    694       C  
ATOM   2882  CE1AHIS C 332     -28.937  53.654 -84.510  0.50 47.60           C  
ANISOU 2882  CE1AHIS C 332     9300   4794   3990   2282    551    898       C  
ATOM   2883  CE1BHIS C 332     -31.465  52.532 -80.907  0.50 40.18           C  
ANISOU 2883  CE1BHIS C 332     7515   4232   3519   2297    -38    431       C  
ATOM   2884  NE2AHIS C 332     -30.122  53.625 -83.927  0.50 47.46           N  
ANISOU 2884  NE2AHIS C 332     9114   4984   3933   2528    280    748       N  
ATOM   2885  NE2BHIS C 332     -31.277  53.288 -81.975  0.50 43.21           N  
ANISOU 2885  NE2BHIS C 332     8192   4566   3661   2487      9    539       N  
ATOM   2886  N   ILE C 333     -26.763  50.396 -79.129  1.00 34.31           N  
ANISOU 2886  N   ILE C 333     6343   3248   3446   1002    356    649       N  
ATOM   2887  CA  ILE C 333     -26.950  49.919 -77.764  1.00 35.14           C  
ANISOU 2887  CA  ILE C 333     6326   3447   3579   1037    290    605       C  
ATOM   2888  C   ILE C 333     -26.007  50.632 -76.803  1.00 36.13           C  
ANISOU 2888  C   ILE C 333     6466   3542   3720    950    228    504       C  
ATOM   2889  O   ILE C 333     -26.433  51.137 -75.757  1.00 34.99           O  
ANISOU 2889  O   ILE C 333     6384   3414   3498   1038    161    439       O  
ATOM   2890  CB  ILE C 333     -26.770  48.391 -77.708  1.00 33.98           C  
ANISOU 2890  CB  ILE C 333     5984   3413   3513   1037    359    637       C  
ATOM   2891  CG1 ILE C 333     -27.865  47.702 -78.522  1.00 33.18           C  
ANISOU 2891  CG1 ILE C 333     5773   3366   3467   1088    457    573       C  
ATOM   2892  CG2 ILE C 333     -26.798  47.905 -76.271  1.00 34.65           C  
ANISOU 2892  CG2 ILE C 333     6092   3539   3535   1166    371    669       C  
ATOM   2893  CD1 ILE C 333     -27.471  46.343 -79.048  1.00 33.43           C  
ANISOU 2893  CD1 ILE C 333     5617   3434   3651   1006    604    563       C  
ATOM   2894  N   THR C 334     -24.711  50.675 -77.129  1.00 35.37           N  
ANISOU 2894  N   THR C 334     6259   3434   3745    773    256    403       N  
ATOM   2895  CA  THR C 334     -23.747  51.209 -76.170  1.00 36.33           C  
ANISOU 2895  CA  THR C 334     6245   3631   3927    703    164    129       C  
ATOM   2896  C   THR C 334     -23.868  52.721 -76.027  1.00 36.26           C  
ANISOU 2896  C   THR C 334     6392   3392   3992    570    278    -29       C  
ATOM   2897  O   THR C 334     -23.660  53.259 -74.930  1.00 37.72           O  
ANISOU 2897  O   THR C 334     6484   3676   4170    586    167   -291       O  
ATOM   2898  CB  THR C 334     -22.317  50.826 -76.565  1.00 38.77           C  
ANISOU 2898  CB  THR C 334     6286   4022   4423    537    182    -76       C  
ATOM   2899  OG1 THR C 334     -22.033  51.310 -77.881  1.00 39.78           O  
ANISOU 2899  OG1 THR C 334     6528   3877   4711    279    470    -43       O  
ATOM   2900  CG2 THR C 334     -22.132  49.315 -76.531  1.00 37.69           C  
ANISOU 2900  CG2 THR C 334     6011   4093   4215    732     75     70       C  
ATOM   2901  N   GLN C 335     -24.208  53.424 -77.107  1.00 36.03           N  
ANISOU 2901  N   GLN C 335     6636   3050   4005    489    522    117       N  
ATOM   2902  CA  GLN C 335     -24.441  54.859 -76.985  1.00 39.02           C  
ANISOU 2902  CA  GLN C 335     7266   3108   4452    424    722     29       C  
ATOM   2903  C   GLN C 335     -25.685  55.139 -76.149  1.00 38.02           C  
ANISOU 2903  C   GLN C 335     7243   3052   4153    674    542     97       C  
ATOM   2904  O   GLN C 335     -25.719  56.109 -75.383  1.00 39.20           O  
ANISOU 2904  O   GLN C 335     7437   3080   4378    619    592   -109       O  
ATOM   2905  CB  GLN C 335     -24.554  55.498 -78.369  1.00 40.27           C  
ANISOU 2905  CB  GLN C 335     7830   2875   4594    421   1076    255       C  
ATOM   2906  CG  GLN C 335     -23.230  55.573 -79.116  1.00 40.42           C  
ANISOU 2906  CG  GLN C 335     7814   2692   4854     84   1428    113       C  
ATOM   2907  CD  GLN C 335     -23.286  56.481 -80.333  1.00 46.30           C  
ANISOU 2907  CD  GLN C 335     9125   2923   5545    108   1936    349       C  
ATOM   2908  OE1 GLN C 335     -24.028  57.463 -80.360  1.00 45.62           O  
ANISOU 2908  OE1 GLN C 335     9361   2647   5326    313   2051    482       O  
ATOM   2909  NE2 GLN C 335     -22.493  56.155 -81.348  1.00 48.89           N  
ANISOU 2909  NE2 GLN C 335     9516   3132   5929    -59   2232    390       N  
ATOM   2910  N   ASN C 336     -26.712  54.296 -76.275  1.00 36.79           N  
ANISOU 2910  N   ASN C 336     7082   3083   3812    917    378    311       N  
ATOM   2911  CA  ASN C 336     -27.896  54.449 -75.438  1.00 37.12           C  
ANISOU 2911  CA  ASN C 336     7159   3204   3739   1120    261    304       C  
ATOM   2912  C   ASN C 336     -27.585  54.153 -73.973  1.00 38.38           C  
ANISOU 2912  C   ASN C 336     7149   3579   3854   1107    132    131       C  
ATOM   2913  O   ASN C 336     -28.150  54.795 -73.075  1.00 38.73           O  
ANISOU 2913  O   ASN C 336     7261   3613   3842   1181    103     18       O  
ATOM   2914  CB  ASN C 336     -29.017  53.542 -75.954  1.00 37.96           C  
ANISOU 2914  CB  ASN C 336     7210   3463   3752   1326    198    432       C  
ATOM   2915  CG  ASN C 336     -30.019  54.291 -76.815  1.00 42.14           C  
ANISOU 2915  CG  ASN C 336     7941   3880   4191   1579    200    480       C  
ATOM   2916  OD1 ASN C 336     -30.474  55.374 -76.448  1.00 45.56           O  
ANISOU 2916  OD1 ASN C 336     8561   4145   4605   1691    221    441       O  
ATOM   2917  ND2 ASN C 336     -30.360  53.725 -77.968  1.00 42.79           N  
ANISOU 2917  ND2 ASN C 336     7989   4080   4191   1730    164    534       N  
ATOM   2918  N   LYS C 337     -26.679  53.209 -73.712  1.00 38.33           N  
ANISOU 2918  N   LYS C 337     6953   3784   3827   1078     48    101       N  
ATOM   2919  CA  LYS C 337     -26.274  52.950 -72.333  1.00 41.04           C  
ANISOU 2919  CA  LYS C 337     7200   4386   4007   1212   -110    -65       C  
ATOM   2920  C   LYS C 337     -25.489  54.123 -71.760  1.00 42.83           C  
ANISOU 2920  C   LYS C 337     7318   4628   4326   1075   -171   -471       C  
ATOM   2921  O   LYS C 337     -25.689  54.502 -70.597  1.00 44.03           O  
ANISOU 2921  O   LYS C 337     7476   4939   4315   1210   -285   -664       O  
ATOM   2922  CB  LYS C 337     -25.455  51.660 -72.249  1.00 43.27           C  
ANISOU 2922  CB  LYS C 337     7343   4896   4203   1339   -199      1       C  
ATOM   2923  CG  LYS C 337     -24.994  51.348 -70.830  1.00 47.75           C  
ANISOU 2923  CG  LYS C 337     7890   5786   4468   1654   -399   -147       C  
ATOM   2924  CD  LYS C 337     -24.178  50.071 -70.736  1.00 49.78           C  
ANISOU 2924  CD  LYS C 337     8077   6253   4586   1915   -488    -49       C  
ATOM   2925  CE  LYS C 337     -23.646  49.893 -69.321  1.00 54.62           C  
ANISOU 2925  CE  LYS C 337     8721   7251   4780   2384   -746   -226       C  
ATOM   2926  NZ  LYS C 337     -22.984  48.577 -69.126  1.00 57.51           N  
ANISOU 2926  NZ  LYS C 337     9139   7796   4914   2809   -812    -51       N  
ATOM   2927  N   GLU C 338     -24.589  54.713 -72.556  1.00 43.82           N  
ANISOU 2927  N   GLU C 338     7337   4577   4737    787    -37   -661       N  
ATOM   2928  CA  GLU C 338     -23.880  55.908 -72.105  1.00 50.13           C  
ANISOU 2928  CA  GLU C 338     7990   5302   5755    563     41  -1162       C  
ATOM   2929  C   GLU C 338     -24.855  57.018 -71.743  1.00 49.10           C  
ANISOU 2929  C   GLU C 338     8111   4910   5634    565    174  -1160       C  
ATOM   2930  O   GLU C 338     -24.659  57.724 -70.748  1.00 52.90           O  
ANISOU 2930  O   GLU C 338     8459   5497   6145    531    116  -1582       O  
ATOM   2931  CB  GLU C 338     -22.908  56.393 -73.181  1.00 56.32           C  
ANISOU 2931  CB  GLU C 338     8699   5779   6921    190    368  -1341       C  
ATOM   2932  CG  GLU C 338     -21.707  55.489 -73.395  1.00 61.73           C  
ANISOU 2932  CG  GLU C 338     9013   6753   7688    137    240  -1544       C  
ATOM   2933  CD  GLU C 338     -20.825  55.948 -74.542  1.00 67.30           C  
ANISOU 2933  CD  GLU C 338     9679   7095   8797   -274    673  -1713       C  
ATOM   2934  OE1 GLU C 338     -21.059  55.507 -75.690  1.00 66.25           O  
ANISOU 2934  OE1 GLU C 338     9797   6752   8623   -285    850  -1274       O  
ATOM   2935  OE2 GLU C 338     -19.893  56.744 -74.295  1.00 73.19           O  
ANISOU 2935  OE2 GLU C 338    10131   7765   9911   -593    881  -2340       O  
ATOM   2936  N   LEU C 339     -25.912  57.185 -72.540  1.00 47.50           N  
ANISOU 2936  N   LEU C 339     8245   4405   5397    650    330   -746       N  
ATOM   2937  CA  LEU C 339     -26.930  58.190 -72.243  1.00 50.56           C  
ANISOU 2937  CA  LEU C 339     8879   4550   5780    740    434   -725       C  
ATOM   2938  C   LEU C 339     -27.574  57.931 -70.888  1.00 49.35           C  
ANISOU 2938  C   LEU C 339     8637   4721   5392    939    192   -829       C  
ATOM   2939  O   LEU C 339     -27.747  58.852 -70.080  1.00 50.59           O  
ANISOU 2939  O   LEU C 339     8805   4821   5595    907    227  -1114       O  
ATOM   2940  CB  LEU C 339     -27.988  58.191 -73.346  1.00 53.09           C  
ANISOU 2940  CB  LEU C 339     9516   4638   6018    951    529   -302       C  
ATOM   2941  CG  LEU C 339     -28.435  59.507 -73.982  1.00 58.48           C  
ANISOU 2941  CG  LEU C 339    10593   4825   6801   1022    832   -216       C  
ATOM   2942  CD1 LEU C 339     -27.253  60.412 -74.283  1.00 62.30           C  
ANISOU 2942  CD1 LEU C 339    11172   4902   7597    676   1247   -436       C  
ATOM   2943  CD2 LEU C 339     -29.216  59.212 -75.255  1.00 58.25           C  
ANISOU 2943  CD2 LEU C 339    10825   4734   6575   1352    821    170       C  
ATOM   2944  N   ILE C 340     -27.945  56.675 -70.627  1.00 46.49           N  
ANISOU 2944  N   ILE C 340     8225   4657   4783   1143     19   -606       N  
ATOM   2945  CA  ILE C 340     -28.578  56.323 -69.358  1.00 47.92           C  
ANISOU 2945  CA  ILE C 340     8427   5088   4693   1362    -90   -644       C  
ATOM   2946  C   ILE C 340     -27.625  56.579 -68.198  1.00 50.89           C  
ANISOU 2946  C   ILE C 340     8637   5772   4928   1396   -269  -1052       C  
ATOM   2947  O   ILE C 340     -28.001  57.170 -67.178  1.00 51.29           O  
ANISOU 2947  O   ILE C 340     8727   5915   4846   1483   -304  -1280       O  
ATOM   2948  CB  ILE C 340     -29.043  54.855 -69.381  1.00 46.74           C  
ANISOU 2948  CB  ILE C 340     8316   5088   4356   1550    -77   -326       C  
ATOM   2949  CG1 ILE C 340     -30.043  54.611 -70.514  1.00 44.53           C  
ANISOU 2949  CG1 ILE C 340     8082   4599   4237   1529     63    -98       C  
ATOM   2950  CG2 ILE C 340     -29.643  54.471 -68.043  1.00 47.89           C  
ANISOU 2950  CG2 ILE C 340     8591   5410   4196   1788    -47   -334       C  
ATOM   2951  CD1 ILE C 340     -31.446  55.071 -70.203  1.00 46.92           C  
ANISOU 2951  CD1 ILE C 340     8465   4808   4555   1632    157   -147       C  
ATOM   2952  N   GLU C 341     -26.371  56.142 -68.339  1.00 52.01           N  
ANISOU 2952  N   GLU C 341     8548   6125   5087   1361   -409  -1220       N  
ATOM   2953  CA  GLU C 341     -25.435  56.210 -67.220  1.00 57.64           C  
ANISOU 2953  CA  GLU C 341     9023   7283   5595   1523   -678  -1703       C  
ATOM   2954  C   GLU C 341     -25.034  57.648 -66.907  1.00 59.68           C  
ANISOU 2954  C   GLU C 341     9072   7460   6143   1242   -621  -2310       C  
ATOM   2955  O   GLU C 341     -24.846  58.002 -65.737  1.00 61.17           O  
ANISOU 2955  O   GLU C 341     9127   8004   6111   1413   -822  -2756       O  
ATOM   2956  CB  GLU C 341     -24.201  55.357 -67.517  1.00 62.55           C  
ANISOU 2956  CB  GLU C 341     9382   8187   6199   1606   -867  -1806       C  
ATOM   2957  CG  GLU C 341     -24.473  53.858 -67.517  1.00 64.75           C  
ANISOU 2957  CG  GLU C 341     9877   8586   6141   1970   -910  -1283       C  
ATOM   2958  CD  GLU C 341     -24.457  53.251 -66.124  1.00 72.75           C  
ANISOU 2958  CD  GLU C 341    11046  10030   6566   2540  -1129  -1300       C  
ATOM   2959  OE1 GLU C 341     -23.671  52.306 -65.901  1.00 76.66           O  
ANISOU 2959  OE1 GLU C 341    11499  10837   6791   2922  -1327  -1273       O  
ATOM   2960  OE2 GLU C 341     -25.222  53.718 -65.250  1.00 75.59           O  
ANISOU 2960  OE2 GLU C 341    11610  10414   6696   2660  -1086  -1332       O  
ATOM   2961  N   LYS C 342     -24.902  58.493 -67.932  1.00 59.36           N  
ANISOU 2961  N   LYS C 342     9038   6934   6582    835   -297  -2355       N  
ATOM   2962  CA  LYS C 342     -24.509  59.877 -67.684  1.00 63.82           C  
ANISOU 2962  CA  LYS C 342     9442   7288   7517    515    -84  -2954       C  
ATOM   2963  C   LYS C 342     -25.632  60.674 -67.031  1.00 62.04           C  
ANISOU 2963  C   LYS C 342     9464   6894   7215    595      2  -2923       C  
ATOM   2964  O   LYS C 342     -25.364  61.662 -66.336  1.00 65.29           O  
ANISOU 2964  O   LYS C 342     9694   7306   7807    437     77  -3521       O  
ATOM   2965  CB  LYS C 342     -24.062  60.539 -68.987  1.00 65.91           C  
ANISOU 2965  CB  LYS C 342     9783   6962   8298     96    392  -2939       C  
ATOM   2966  CG  LYS C 342     -22.787  59.933 -69.559  1.00 68.67           C  
ANISOU 2966  CG  LYS C 342     9795   7470   8824    -73    375  -3159       C  
ATOM   2967  CD  LYS C 342     -21.891  60.978 -70.198  1.00 74.98           C  
ANISOU 2967  CD  LYS C 342    10458   7788  10242   -601    926  -3663       C  
ATOM   2968  CE  LYS C 342     -20.423  60.616 -70.014  1.00 80.03           C  
ANISOU 2968  CE  LYS C 342    10452   8845  11112   -779    789  -4397       C  
ATOM   2969  NZ  LYS C 342     -20.148  59.200 -70.386  1.00 77.58           N  
ANISOU 2969  NZ  LYS C 342    10071   8920  10486   -494    418  -4000       N  
ATOM   2970  N   ALA C 343     -26.885  60.265 -67.233  1.00 56.90           N  
ANISOU 2970  N   ALA C 343     9168   6112   6339    823     10  -2324       N  
ATOM   2971  CA  ALA C 343     -28.011  60.956 -66.620  1.00 56.47           C  
ANISOU 2971  CA  ALA C 343     9315   5917   6223    925     88  -2315       C  
ATOM   2972  C   ALA C 343     -28.183  60.600 -65.150  1.00 57.74           C  
ANISOU 2972  C   ALA C 343     9395   6591   5954   1196   -183  -2544       C  
ATOM   2973  O   ALA C 343     -28.772  61.385 -64.399  1.00 60.38           O  
ANISOU 2973  O   ALA C 343     9786   6881   6274   1213   -121  -2782       O  
ATOM   2974  CB  ALA C 343     -29.301  60.645 -67.381  1.00 52.97           C  
ANISOU 2974  CB  ALA C 343     9189   5205   5734   1091    193  -1726       C  
ATOM   2975  N   LEU C 344     -27.684  59.444 -64.727  1.00102.71           N  
ANISOU 2975  N   LEU C 344    17760   8581  12684   -457  -3398  -2505       N  
ATOM   2976  CA  LEU C 344     -27.755  59.044 -63.329  1.00103.14           C  
ANISOU 2976  CA  LEU C 344    18007   8676  12504   -148  -3306  -2909       C  
ATOM   2977  C   LEU C 344     -26.695  59.773 -62.512  1.00101.39           C  
ANISOU 2977  C   LEU C 344    18123   8054  12345   -323  -3711  -3074       C  
ATOM   2978  O   LEU C 344     -26.887  60.915 -62.091  1.00105.67           O  
ANISOU 2978  O   LEU C 344    19038   8084  13028   -152  -4041  -3253       O  
ATOM   2979  CB  LEU C 344     -27.583  57.531 -63.198  1.00 93.64           C  
ANISOU 2979  CB  LEU C 344    16479   8043  11055   -200  -2965  -2892       C  
ATOM   2980  CG  LEU C 344     -28.622  56.701 -63.955  1.00 90.33           C  
ANISOU 2980  CG  LEU C 344    15725   8034  10561    -32  -2577  -2729       C  
ATOM   2981  CD1 LEU C 344     -28.161  55.259 -64.113  1.00 86.34           C  
ANISOU 2981  CD1 LEU C 344    14876   8013   9918   -201  -2401  -2640       C  
ATOM   2982  CD2 LEU C 344     -29.971  56.768 -63.250  1.00 91.42           C  
ANISOU 2982  CD2 LEU C 344    16018   8203  10513    458  -2368  -2991       C  
TER    2983      LEU C 344                                                      
ATOM   2984  N   PRO G 902     -40.622  44.259 -68.314  1.00108.22           N  
ANISOU 2984  N   PRO G 902    14999  15055  11066   1059    481   -729       N  
ATOM   2985  CA  PRO G 902     -39.310  44.869 -68.532  1.00107.13           C  
ANISOU 2985  CA  PRO G 902    14938  14541  11224   1023    269   -868       C  
ATOM   2986  C   PRO G 902     -39.393  46.334 -68.953  1.00105.47           C  
ANISOU 2986  C   PRO G 902    14762  14095  11216   1230    438  -1010       C  
ATOM   2987  O   PRO G 902     -40.344  46.736 -69.624  1.00105.45           O  
ANISOU 2987  O   PRO G 902    14615  14166  11286   1432    682   -947       O  
ATOM   2988  CB  PRO G 902     -38.715  44.013 -69.656  1.00105.38           C  
ANISOU 2988  CB  PRO G 902    14430  14314  11296    935     80   -696       C  
ATOM   2989  CG  PRO G 902     -39.448  42.679 -69.574  1.00104.84           C  
ANISOU 2989  CG  PRO G 902    14270  14523  11043    859     21   -482       C  
ATOM   2990  CD  PRO G 902     -40.603  42.818 -68.610  1.00107.38           C  
ANISOU 2990  CD  PRO G 902    14755  15096  10947    872    265   -470       C  
ATOM   2991  N   SER G 903     -38.398  47.118 -68.552  1.00 98.27           N  
ANISOU 2991  N   SER G 903    14059  12873  10406   1167    253  -1195       N  
ATOM   2992  CA  SER G 903     -38.323  48.523 -68.927  1.00 90.46           C  
ANISOU 2992  CA  SER G 903    13159  11570   9642   1302    278  -1303       C  
ATOM   2993  C   SER G 903     -37.573  48.684 -70.244  1.00 80.28           C  
ANISOU 2993  C   SER G 903    11654  10152   8697   1147    170  -1113       C  
ATOM   2994  O   SER G 903     -36.410  48.296 -70.356  1.00 79.36           O  
ANISOU 2994  O   SER G 903    11472  10016   8666    909    -49  -1108       O  
ATOM   2995  CB  SER G 903     -37.643  49.339 -67.826  1.00 91.14           C  
ANISOU 2995  CB  SER G 903    13592  11383   9656   1282     97  -1587       C  
ATOM   2996  OG  SER G 903     -37.048  50.512 -68.351  1.00 89.48           O  
ANISOU 2996  OG  SER G 903    13470  10780   9749   1264    -58  -1614       O  
HETATM 2997  N   PTR G 904     -38.240  49.254 -71.241  1.00 71.69           N  
ANISOU 2997  N   PTR G 904    10434   9020   7786   1266    308   -975       N  
HETATM 2998  CA  PTR G 904     -37.624  49.420 -72.550  1.00 65.96           C  
ANISOU 2998  CA  PTR G 904     9475   8268   7320   1059    224   -762       C  
HETATM 2999  C   PTR G 904     -37.244  50.866 -72.834  1.00 66.89           C  
ANISOU 2999  C   PTR G 904     9786   7990   7637    974     51   -759       C  
HETATM 3000  O   PTR G 904     -37.851  51.801 -72.312  1.00 69.52           O  
ANISOU 3000  O   PTR G 904    10395   8034   7987   1203     28   -908       O  
HETATM 3001  CB  PTR G 904     -38.552  48.896 -73.650  1.00 63.25           C  
ANISOU 3001  CB  PTR G 904     8819   8181   7034   1158    443   -528       C  
HETATM 3002  CG  PTR G 904     -38.441  47.403 -73.849  1.00 57.26           C  
ANISOU 3002  CG  PTR G 904     7781   7787   6187   1095    464   -454       C  
HETATM 3003  CD1 PTR G 904     -39.124  46.522 -73.024  1.00 56.75           C  
ANISOU 3003  CD1 PTR G 904     7777   7896   5890   1221    544   -495       C  
HETATM 3004  CD2 PTR G 904     -37.638  46.874 -74.853  1.00 55.51           C  
ANISOU 3004  CD2 PTR G 904     7227   7761   6104    890    355   -363       C  
HETATM 3005  CE1 PTR G 904     -39.018  45.153 -73.195  1.00 56.21           C  
ANISOU 3005  CE1 PTR G 904     7501   8082   5776   1147    452   -409       C  
HETATM 3006  CE2 PTR G 904     -37.528  45.506 -75.035  1.00 53.29           C  
ANISOU 3006  CE2 PTR G 904     6692   7767   5788    886    284   -359       C  
HETATM 3007  CZ  PTR G 904     -38.223  44.648 -74.207  1.00 54.41           C  
ANISOU 3007  CZ  PTR G 904     6956   7972   5746   1018    301   -364       C  
HETATM 3008  OH  PTR G 904     -38.107  43.357 -74.361  1.00 51.18           O  
ANISOU 3008  OH  PTR G 904     6354   7759   5334    997    132   -344       O  
HETATM 3009  P   PTR G 904     -38.979  42.501 -75.408  1.00 48.90           P  
ANISOU 3009  P   PTR G 904     5736   7734   5109   1111    243   -142       P  
HETATM 3010  O1P PTR G 904     -38.704  43.027 -76.829  1.00 48.09           O  
ANISOU 3010  O1P PTR G 904     5305   7755   5213   1074    355    -84       O  
HETATM 3011  O2P PTR G 904     -40.480  42.614 -75.093  1.00 49.03           O  
ANISOU 3011  O2P PTR G 904     5888   7793   4950   1271    545     33       O  
HETATM 3012  O3P PTR G 904     -38.553  41.086 -75.276  1.00 48.11           O  
ANISOU 3012  O3P PTR G 904     5513   7740   5027   1072   -118   -204       O  
ATOM   3013  N   VAL G 905     -36.214  51.034 -73.658  1.00 68.24           N  
ANISOU 3013  N   VAL G 905     9799   8179   7951    626   -114   -608       N  
ATOM   3014  CA  VAL G 905     -35.831  52.346 -74.152  1.00 73.56           C  
ANISOU 3014  CA  VAL G 905    10628   8511   8809    420   -336   -491       C  
ATOM   3015  C   VAL G 905     -36.695  52.671 -75.362  1.00 75.92           C  
ANISOU 3015  C   VAL G 905    10778   8825   9242    449   -245   -215       C  
ATOM   3016  O   VAL G 905     -36.557  52.053 -76.416  1.00 65.90           O  
ANISOU 3016  O   VAL G 905     9139   7925   7975    256   -141     -5       O  
ATOM   3017  CB  VAL G 905     -34.333  52.406 -74.510  1.00 73.18           C  
ANISOU 3017  CB  VAL G 905    10439   8573   8792    -53   -557   -430       C  
ATOM   3018  CG1 VAL G 905     -34.021  53.671 -75.302  1.00 75.21           C  
ANISOU 3018  CG1 VAL G 905    10797   8570   9210   -390   -802   -180       C  
ATOM   3019  CG2 VAL G 905     -33.477  52.329 -73.253  1.00 69.62           C  
ANISOU 3019  CG2 VAL G 905    10211   7989   8251    -71   -713   -714       C  
ATOM   3020  N   ASN G 906     -37.602  53.628 -75.203  1.00 80.05           N  
ANISOU 3020  N   ASN G 906    11579   8958   9880    714   -313   -253       N  
ATOM   3021  CA  ASN G 906     -38.470  54.066 -76.284  1.00 82.28           C  
ANISOU 3021  CA  ASN G 906    11783   9157  10322    765   -302     -5       C  
ATOM   3022  C   ASN G 906     -38.055  55.460 -76.735  1.00 90.29           C  
ANISOU 3022  C   ASN G 906    13069   9681  11558    485   -732    171       C  
ATOM   3023  O   ASN G 906     -37.618  56.283 -75.924  1.00 93.50           O  
ANISOU 3023  O   ASN G 906    13826   9672  12027    493  -1023    -14       O  
ATOM   3024  CB  ASN G 906     -39.938  54.050 -75.851  1.00 81.33           C  
ANISOU 3024  CB  ASN G 906    11732   8981  10189   1309   -108   -204       C  
ATOM   3025  CG  ASN G 906     -40.451  52.643 -75.597  1.00 75.70           C  
ANISOU 3025  CG  ASN G 906    10734   8787   9242   1486    283   -264       C  
ATOM   3026  OD1 ASN G 906     -40.151  51.717 -76.351  1.00 71.49           O  
ANISOU 3026  OD1 ASN G 906     9877   8618   8666   1278    413    -49       O  
ATOM   3027  ND2 ASN G 906     -41.220  52.475 -74.526  1.00 75.45           N  
ANISOU 3027  ND2 ASN G 906    10812   8817   9039   1851    435   -568       N  
ATOM   3028  N   VAL G 907     -38.212  55.710 -78.036  1.00 95.58           N  
ANISOU 3028  N   VAL G 907    13585  10396  12336    214   -806    546       N  
ATOM   3029  CA  VAL G 907     -37.625  56.853 -78.748  1.00101.64           C  
ANISOU 3029  CA  VAL G 907    14536  10823  13258   -273  -1255    867       C  
ATOM   3030  C   VAL G 907     -36.234  57.183 -78.211  1.00103.87           C  
ANISOU 3030  C   VAL G 907    14945  11045  13476   -678  -1497    820       C  
ATOM   3031  O   VAL G 907     -35.320  56.360 -78.289  1.00102.56           O  
ANISOU 3031  O   VAL G 907    14453  11395  13120   -955  -1312    810       O  
ATOM   3032  CB  VAL G 907     -38.541  58.108 -78.704  1.00107.52           C  
ANISOU 3032  CB  VAL G 907    15704  10861  14289      2  -1643    853       C  
ATOM   3033  CG1 VAL G 907     -39.966  57.755 -79.114  1.00106.45           C  
ANISOU 3033  CG1 VAL G 907    15422  10806  14217    470  -1390    821       C  
ATOM   3034  CG2 VAL G 907     -38.497  58.801 -77.345  1.00111.73           C  
ANISOU 3034  CG2 VAL G 907    16652  10895  14906    348  -1888    424       C  
TER    3035      VAL G 907                                                      
ATOM   3036  N   SER D 226     -46.711  30.411 -91.205  1.00107.75           N  
ANISOU 3036  N   SER D 226     9624  14831  16485   1893  -3563  -1742       N  
ATOM   3037  CA  SER D 226     -45.692  30.730 -92.197  1.00104.32           C  
ANISOU 3037  CA  SER D 226     9981  14061  15596   2000  -3878  -1474       C  
ATOM   3038  C   SER D 226     -44.612  31.613 -91.588  1.00 99.64           C  
ANISOU 3038  C   SER D 226     9812  13334  14713   2129  -3500  -1400       C  
ATOM   3039  O   SER D 226     -44.038  32.467 -92.264  1.00 99.52           O  
ANISOU 3039  O   SER D 226    10310  13012  14493   2385  -3749  -1286       O  
ATOM   3040  CB  SER D 226     -46.314  31.423 -93.410  1.00108.78           C  
ANISOU 3040  CB  SER D 226    10607  14386  16338   2371  -4616  -1482       C  
ATOM   3041  OG  SER D 226     -46.822  32.699 -93.061  1.00112.20           O  
ANISOU 3041  OG  SER D 226    10803  14746  17083   2765  -4607  -1636       O  
ATOM   3042  N   GLU D 227     -44.344  31.399 -90.300  1.00 95.47           N  
ANISOU 3042  N   GLU D 227     9094  13025  14154   1927  -2897  -1472       N  
ATOM   3043  CA  GLU D 227     -43.352  32.188 -89.584  1.00 89.64           C  
ANISOU 3043  CA  GLU D 227     8704  12192  13161   2012  -2523  -1433       C  
ATOM   3044  C   GLU D 227     -42.481  31.358 -88.652  1.00 81.01           C  
ANISOU 3044  C   GLU D 227     7789  11238  11753   1611  -2018  -1328       C  
ATOM   3045  O   GLU D 227     -41.571  31.918 -88.032  1.00 80.94           O  
ANISOU 3045  O   GLU D 227     8088  11153  11513   1641  -1728  -1290       O  
ATOM   3046  CB  GLU D 227     -44.035  33.309 -88.780  1.00 95.63           C  
ANISOU 3046  CB  GLU D 227     9025  13030  14278   2319  -2336  -1702       C  
ATOM   3047  CG  GLU D 227     -44.760  32.854 -87.514  1.00100.32           C  
ANISOU 3047  CG  GLU D 227     9020  13976  15122   2088  -1837  -1934       C  
ATOM   3048  CD  GLU D 227     -45.885  31.865 -87.779  1.00105.51           C  
ANISOU 3048  CD  GLU D 227     9128  14839  16122   1898  -1991  -2042       C  
ATOM   3049  OE1 GLU D 227     -46.403  31.826 -88.916  1.00108.27           O  
ANISOU 3049  OE1 GLU D 227     9407  15070  16661   2070  -2565  -2015       O  
ATOM   3050  OE2 GLU D 227     -46.256  31.126 -86.843  1.00106.90           O  
ANISOU 3050  OE2 GLU D 227     8967  15285  16366   1558  -1540  -2158       O  
ATOM   3051  N   LYS D 228     -42.725  30.051 -88.533  1.00 75.61           N  
ANISOU 3051  N   LYS D 228     6936  10733  11059   1239  -1932  -1280       N  
ATOM   3052  CA  LYS D 228     -41.871  29.189 -87.723  1.00 68.82           C  
ANISOU 3052  CA  LYS D 228     6303   9953   9894    863  -1533  -1143       C  
ATOM   3053  C   LYS D 228     -40.458  29.072 -88.281  1.00 61.84           C  
ANISOU 3053  C   LYS D 228     6071   8790   8635    820  -1615   -902       C  
ATOM   3054  O   LYS D 228     -39.566  28.596 -87.567  1.00 52.05           O  
ANISOU 3054  O   LYS D 228     5059   7556   7163    586  -1321   -791       O  
ATOM   3055  CB  LYS D 228     -42.496  27.796 -87.606  1.00 67.75           C  
ANISOU 3055  CB  LYS D 228     5871  10019   9851    481  -1467  -1136       C  
ATOM   3056  CG  LYS D 228     -43.834  27.763 -86.883  1.00 71.41           C  
ANISOU 3056  CG  LYS D 228     5660  10773  10699    426  -1257  -1407       C  
ATOM   3057  CD  LYS D 228     -44.330  26.335 -86.717  1.00 72.63           C  
ANISOU 3057  CD  LYS D 228     5590  11103  10903    -10  -1133  -1388       C  
ATOM   3058  CE  LYS D 228     -45.627  26.288 -85.929  1.00 77.99           C  
ANISOU 3058  CE  LYS D 228     5593  12062  11976   -118   -831  -1692       C  
ATOM   3059  NZ  LYS D 228     -46.199  24.913 -85.861  1.00 79.33           N  
ANISOU 3059  NZ  LYS D 228     5530  12384  12229   -557   -721  -1694       N  
ATOM   3060  N   ILE D 229     -40.230  29.503 -89.524  1.00 59.02           N  
ANISOU 3060  N   ILE D 229     6030   8171   8224   1029  -2004   -831       N  
ATOM   3061  CA  ILE D 229     -38.920  29.328 -90.149  1.00 50.80           C  
ANISOU 3061  CA  ILE D 229     5596   6844   6863    946  -2035   -641       C  
ATOM   3062  C   ILE D 229     -37.850  30.106 -89.399  1.00 48.12           C  
ANISOU 3062  C   ILE D 229     5522   6405   6356   1027  -1730   -630       C  
ATOM   3063  O   ILE D 229     -36.705  29.655 -89.279  1.00 44.87           O  
ANISOU 3063  O   ILE D 229     5441   5865   5742    839  -1569   -508       O  
ATOM   3064  CB  ILE D 229     -38.973  29.737 -91.633  1.00 56.39           C  
ANISOU 3064  CB  ILE D 229     6641   7271   7513   1135  -2483   -591       C  
ATOM   3065  CG1 ILE D 229     -37.572  29.669 -92.249  1.00 52.68           C  
ANISOU 3065  CG1 ILE D 229     6813   6478   6725   1034  -2418   -443       C  
ATOM   3066  CG2 ILE D 229     -39.572  31.132 -91.789  1.00 54.74           C  
ANISOU 3066  CG2 ILE D 229     6343   6991   7466   1556  -2693   -713       C  
ATOM   3067  CD1 ILE D 229     -37.575  29.659 -93.756  1.00 54.93           C  
ANISOU 3067  CD1 ILE D 229     7520   6483   6867   1064  -2803   -373       C  
ATOM   3068  N   TYR D 230     -38.198  31.286 -88.882  1.00 49.75           N  
ANISOU 3068  N   TYR D 230     5572   6652   6677   1309  -1655   -777       N  
ATOM   3069  CA  TYR D 230     -37.189  32.130 -88.251  1.00 54.23           C  
ANISOU 3069  CA  TYR D 230     6419   7101   7084   1396  -1400   -787       C  
ATOM   3070  C   TYR D 230     -36.646  31.493 -86.978  1.00 51.53           C  
ANISOU 3070  C   TYR D 230     6019   6939   6622   1104  -1030   -759       C  
ATOM   3071  O   TYR D 230     -35.442  31.569 -86.705  1.00 42.89           O  
ANISOU 3071  O   TYR D 230     5261   5696   5338   1026   -896   -681       O  
ATOM   3072  CB  TYR D 230     -37.773  33.513 -87.969  1.00 58.00           C  
ANISOU 3072  CB  TYR D 230     6729   7575   7732   1757  -1396   -969       C  
ATOM   3073  CG  TYR D 230     -38.297  34.187 -89.214  1.00 59.95           C  
ANISOU 3073  CG  TYR D 230     7086   7600   8094   2069  -1828   -973       C  
ATOM   3074  CD1 TYR D 230     -39.634  34.543 -89.325  1.00 64.89           C  
ANISOU 3074  CD1 TYR D 230     7253   8339   9064   2302  -2049  -1125       C  
ATOM   3075  CD2 TYR D 230     -37.456  34.449 -90.288  1.00 57.99           C  
ANISOU 3075  CD2 TYR D 230     7412   7004   7616   2116  -2025   -832       C  
ATOM   3076  CE1 TYR D 230     -40.118  35.155 -90.469  1.00 67.98           C  
ANISOU 3076  CE1 TYR D 230     7776   8496   9557   2601  -2529  -1109       C  
ATOM   3077  CE2 TYR D 230     -37.930  35.061 -91.437  1.00 61.70           C  
ANISOU 3077  CE2 TYR D 230     8080   7238   8127   2378  -2453   -811       C  
ATOM   3078  CZ  TYR D 230     -39.262  35.410 -91.521  1.00 66.76           C  
ANISOU 3078  CZ  TYR D 230     8276   7989   9100   2632  -2741   -936       C  
ATOM   3079  OH  TYR D 230     -39.744  36.019 -92.659  1.00 71.28           O  
ANISOU 3079  OH  TYR D 230     9069   8300   9715   2908  -3247   -898       O  
ATOM   3080  N   LYS D 231     -37.514  30.852 -86.193  1.00 52.50           N  
ANISOU 3080  N   LYS D 231     5731   7360   6857    926   -874   -827       N  
ATOM   3081  CA  LYS D 231     -37.057  30.164 -84.989  1.00 49.71           C  
ANISOU 3081  CA  LYS D 231     5394   7157   6338    614   -557   -773       C  
ATOM   3082  C   LYS D 231     -36.183  28.962 -85.332  1.00 45.43           C  
ANISOU 3082  C   LYS D 231     5129   6488   5645    338   -637   -552       C  
ATOM   3083  O   LYS D 231     -35.190  28.692 -84.646  1.00 42.43           O  
ANISOU 3083  O   LYS D 231     4985   6048   5087    180   -497   -455       O  
ATOM   3084  CB  LYS D 231     -38.258  29.735 -84.149  1.00 57.48           C  
ANISOU 3084  CB  LYS D 231     5916   8461   7465    450   -338   -909       C  
ATOM   3085  CG  LYS D 231     -37.897  28.957 -82.899  1.00 61.59           C  
ANISOU 3085  CG  LYS D 231     6518   9121   7762     84    -22   -836       C  
ATOM   3086  CD  LYS D 231     -37.295  29.860 -81.835  1.00 64.60           C  
ANISOU 3086  CD  LYS D 231     7085   9502   7956    139    229   -913       C  
ATOM   3087  CE  LYS D 231     -36.623  29.040 -80.745  1.00 66.24           C  
ANISOU 3087  CE  LYS D 231     7544   9761   7865   -226    416   -770       C  
ATOM   3088  NZ  LYS D 231     -35.309  28.501 -81.184  1.00 63.79           N  
ANISOU 3088  NZ  LYS D 231     7614   9204   7422   -285    184   -533       N  
ATOM   3089  N   VAL D 232     -36.532  28.225 -86.389  1.00 45.76           N  
ANISOU 3089  N   VAL D 232     5145   6469   5773    277   -879   -480       N  
ATOM   3090  CA  VAL D 232     -35.687  27.112 -86.814  1.00 44.29           C  
ANISOU 3090  CA  VAL D 232     5228   6119   5481     33   -942   -296       C  
ATOM   3091  C   VAL D 232     -34.326  27.624 -87.267  1.00 41.92           C  
ANISOU 3091  C   VAL D 232     5360   5503   5066    143   -972   -238       C  
ATOM   3092  O   VAL D 232     -33.290  27.009 -86.987  1.00 36.71           O  
ANISOU 3092  O   VAL D 232     4904   4712   4331    -34   -893   -129       O  
ATOM   3093  CB  VAL D 232     -36.386  26.294 -87.916  1.00 44.84           C  
ANISOU 3093  CB  VAL D 232     5202   6176   5658    -57  -1190   -265       C  
ATOM   3094  CG1 VAL D 232     -35.399  25.339 -88.587  1.00 40.39           C  
ANISOU 3094  CG1 VAL D 232     4985   5362   5001   -256  -1254   -108       C  
ATOM   3095  CG2 VAL D 232     -37.561  25.526 -87.334  1.00 46.47           C  
ANISOU 3095  CG2 VAL D 232     4973   6683   5998   -264  -1100   -319       C  
ATOM   3096  N   MET D 233     -34.303  28.763 -87.966  1.00 42.50           N  
ANISOU 3096  N   MET D 233     5574   5425   5148    433  -1087   -321       N  
ATOM   3097  CA  MET D 233     -33.027  29.322 -88.401  1.00 40.52           C  
ANISOU 3097  CA  MET D 233     5737   4859   4799    513  -1059   -298       C  
ATOM   3098  C   MET D 233     -32.181  29.776 -87.219  1.00 39.94           C  
ANISOU 3098  C   MET D 233     5708   4804   4664    503   -827   -326       C  
ATOM   3099  O   MET D 233     -30.948  29.696 -87.274  1.00 37.90           O  
ANISOU 3099  O   MET D 233     5710   4319   4371    431   -765   -286       O  
ATOM   3100  CB  MET D 233     -33.255  30.483 -89.373  1.00 42.37           C  
ANISOU 3100  CB  MET D 233     6165   4907   5025    809  -1226   -373       C  
ATOM   3101  CG  MET D 233     -33.895  30.088 -90.701  1.00 47.70           C  
ANISOU 3101  CG  MET D 233     6929   5487   5708    811  -1527   -331       C  
ATOM   3102  SD  MET D 233     -33.318  28.504 -91.347  1.00 48.96           S  
ANISOU 3102  SD  MET D 233     7261   5525   5817    448  -1536   -203       S  
ATOM   3103  CE  MET D 233     -31.597  28.867 -91.686  1.00 45.12           C  
ANISOU 3103  CE  MET D 233     7270   4645   5227    411  -1328   -199       C  
ATOM   3104  N   GLU D 234     -32.814  30.249 -86.144  1.00 41.72           N  
ANISOU 3104  N   GLU D 234     5681   5283   4889    560   -693   -416       N  
ATOM   3105  CA  GLU D 234     -32.055  30.611 -84.953  1.00 40.70           C  
ANISOU 3105  CA  GLU D 234     5625   5184   4655    508   -495   -444       C  
ATOM   3106  C   GLU D 234     -31.318  29.401 -84.393  1.00 39.10           C  
ANISOU 3106  C   GLU D 234     5493   4972   4390    204   -473   -293       C  
ATOM   3107  O   GLU D 234     -30.116  29.468 -84.115  1.00 38.96           O  
ANISOU 3107  O   GLU D 234     5689   4773   4340    161   -458   -262       O  
ATOM   3108  CB  GLU D 234     -32.980  31.218 -83.896  1.00 44.12           C  
ANISOU 3108  CB  GLU D 234     5791   5899   5075    573   -317   -586       C  
ATOM   3109  CG  GLU D 234     -32.249  31.700 -82.649  1.00 44.75           C  
ANISOU 3109  CG  GLU D 234     5999   6008   4995    511   -122   -635       C  
ATOM   3110  CD  GLU D 234     -33.025  31.436 -81.370  1.00 47.89           C  
ANISOU 3110  CD  GLU D 234     6190   6713   5295    331    101   -695       C  
ATOM   3111  OE1 GLU D 234     -33.099  32.340 -80.515  1.00 48.38           O  
ANISOU 3111  OE1 GLU D 234     6254   6855   5273    402    297   -849       O  
ATOM   3112  OE2 GLU D 234     -33.565  30.322 -81.221  1.00 49.85           O  
ANISOU 3112  OE2 GLU D 234     6296   7104   5539     95    109   -599       O  
ATOM   3113  N   GLU D 235     -32.026  28.278 -84.232  1.00 39.90           N  
ANISOU 3113  N   GLU D 235     5411   5244   4504    -11   -489   -203       N  
ATOM   3114  CA  GLU D 235     -31.407  27.074 -83.681  1.00 40.85           C  
ANISOU 3114  CA  GLU D 235     5620   5329   4571   -298   -495    -39       C  
ATOM   3115  C   GLU D 235     -30.225  26.620 -84.525  1.00 36.47           C  
ANISOU 3115  C   GLU D 235     5299   4441   4117   -320   -625     45       C  
ATOM   3116  O   GLU D 235     -29.234  26.103 -83.997  1.00 35.51           O  
ANISOU 3116  O   GLU D 235     5306   4184   4001   -451   -651    136       O  
ATOM   3117  CB  GLU D 235     -32.436  25.949 -83.580  1.00 47.55           C  
ANISOU 3117  CB  GLU D 235     6255   6376   5435   -527   -483     35       C  
ATOM   3118  CG  GLU D 235     -33.707  26.324 -82.851  1.00 56.37           C  
ANISOU 3118  CG  GLU D 235     7084   7814   6520   -535   -301    -94       C  
ATOM   3119  CD  GLU D 235     -34.635  25.139 -82.659  1.00 63.04           C  
ANISOU 3119  CD  GLU D 235     7723   8836   7391   -822   -242    -34       C  
ATOM   3120  OE1 GLU D 235     -34.172  23.988 -82.826  1.00 63.18           O  
ANISOU 3120  OE1 GLU D 235     7881   8729   7396  -1039   -335    142       O  
ATOM   3121  OE2 GLU D 235     -35.824  25.358 -82.339  1.00 67.08           O  
ANISOU 3121  OE2 GLU D 235     7922   9596   7969   -836    -87   -181       O  
ATOM   3122  N   ILE D 236     -30.319  26.793 -85.842  1.00 32.39           N  
ANISOU 3122  N   ILE D 236     4847   3768   3691   -202   -712      4       N  
ATOM   3123  CA  ILE D 236     -29.245  26.366 -86.726  1.00 30.68           C  
ANISOU 3123  CA  ILE D 236     4862   3215   3579   -251   -764     40       C  
ATOM   3124  C   ILE D 236     -28.087  27.353 -86.683  1.00 29.43           C  
ANISOU 3124  C   ILE D 236     4901   2832   3448   -110   -689    -57       C  
ATOM   3125  O   ILE D 236     -26.920  26.960 -86.563  1.00 31.05           O  
ANISOU 3125  O   ILE D 236     5208   2815   3775   -203   -675    -38       O  
ATOM   3126  CB  ILE D 236     -29.791  26.186 -88.156  1.00 30.98           C  
ANISOU 3126  CB  ILE D 236     4971   3154   3645   -223   -867     22       C  
ATOM   3127  CG1 ILE D 236     -30.725  24.976 -88.222  1.00 32.22           C  
ANISOU 3127  CG1 ILE D 236     4932   3486   3824   -425   -948    114       C  
ATOM   3128  CG2 ILE D 236     -28.653  26.054 -89.157  1.00 32.83           C  
ANISOU 3128  CG2 ILE D 236     5508   3005   3960   -258   -838     -4       C  
ATOM   3129  CD1 ILE D 236     -31.373  24.779 -89.606  1.00 39.12           C  
ANISOU 3129  CD1 ILE D 236     5874   4285   4704   -416  -1103     88       C  
ATOM   3130  N   PHE D 237     -28.388  28.649 -86.766  1.00 29.79           N  
ANISOU 3130  N   PHE D 237     4985   2916   3419    116   -642   -178       N  
ATOM   3131  CA  PHE D 237     -27.328  29.647 -86.851  1.00 35.06           C  
ANISOU 3131  CA  PHE D 237     5862   3344   4116    238   -549   -290       C  
ATOM   3132  C   PHE D 237     -26.525  29.757 -85.553  1.00 36.64           C  
ANISOU 3132  C   PHE D 237     6016   3584   4323    177   -499   -302       C  
ATOM   3133  O   PHE D 237     -25.330  30.069 -85.595  1.00 33.68           O  
ANISOU 3133  O   PHE D 237     5773   2959   4063    176   -453   -375       O  
ATOM   3134  CB  PHE D 237     -27.921  31.005 -87.223  1.00 34.57           C  
ANISOU 3134  CB  PHE D 237     5874   3295   3966    497   -525   -406       C  
ATOM   3135  CG  PHE D 237     -28.310  31.124 -88.682  1.00 34.44           C  
ANISOU 3135  CG  PHE D 237     6054   3100   3931    575   -622   -406       C  
ATOM   3136  CD1 PHE D 237     -27.780  30.260 -89.627  1.00 34.03           C  
ANISOU 3136  CD1 PHE D 237     6180   2820   3929    404   -639   -355       C  
ATOM   3137  CD2 PHE D 237     -29.198  32.103 -89.098  1.00 37.66           C  
ANISOU 3137  CD2 PHE D 237     6493   3544   4271    814   -709   -463       C  
ATOM   3138  CE1 PHE D 237     -28.137  30.367 -90.979  1.00 36.92           C  
ANISOU 3138  CE1 PHE D 237     6806   3006   4214    439   -736   -355       C  
ATOM   3139  CE2 PHE D 237     -29.559  32.223 -90.444  1.00 38.98           C  
ANISOU 3139  CE2 PHE D 237     6909   3521   4381    879   -864   -443       C  
ATOM   3140  CZ  PHE D 237     -29.026  31.351 -91.384  1.00 38.25           C  
ANISOU 3140  CZ  PHE D 237     7046   3213   4276    675   -874   -387       C  
ATOM   3141  N   VAL D 238     -27.152  29.524 -84.397  1.00 32.21           N  
ANISOU 3141  N   VAL D 238     5441   2942   3855    303  -1053   -138       N  
ATOM   3142  CA  VAL D 238     -26.409  29.623 -83.140  1.00 35.48           C  
ANISOU 3142  CA  VAL D 238     5800   3379   4304    260  -1188   -275       C  
ATOM   3143  C   VAL D 238     -25.565  28.385 -82.866  1.00 35.30           C  
ANISOU 3143  C   VAL D 238     5572   3540   4302    344  -1297   -338       C  
ATOM   3144  O   VAL D 238     -24.664  28.440 -82.023  1.00 36.35           O  
ANISOU 3144  O   VAL D 238     5586   3777   4450    330  -1437   -471       O  
ATOM   3145  CB  VAL D 238     -27.334  29.864 -81.934  1.00 38.43           C  
ANISOU 3145  CB  VAL D 238     6355   3670   4576    368  -1264   -283       C  
ATOM   3146  CG1 VAL D 238     -28.178  31.108 -82.143  1.00 39.76           C  
ANISOU 3146  CG1 VAL D 238     6732   3646   4729    350  -1153   -228       C  
ATOM   3147  CG2 VAL D 238     -28.207  28.644 -81.678  1.00 39.11           C  
ANISOU 3147  CG2 VAL D 238     6471   3816   4574    550  -1277   -214       C  
ATOM   3148  N   ASP D 239     -25.823  27.274 -83.552  1.00 34.79           N  
ANISOU 3148  N   ASP D 239     5464   3528   4227    450  -1236   -262       N  
ATOM   3149  CA  ASP D 239     -25.142  26.028 -83.231  1.00 34.73           C  
ANISOU 3149  CA  ASP D 239     5336   3634   4228    600  -1310   -295       C  
ATOM   3150  C   ASP D 239     -23.652  26.132 -83.527  1.00 34.92           C  
ANISOU 3150  C   ASP D 239     5080   3818   4370    528  -1351   -419       C  
ATOM   3151  O   ASP D 239     -23.236  26.797 -84.480  1.00 34.48           O  
ANISOU 3151  O   ASP D 239     4926   3768   4405    326  -1226   -452       O  
ATOM   3152  CB  ASP D 239     -25.749  24.863 -84.012  1.00 35.32           C  
ANISOU 3152  CB  ASP D 239     5452   3682   4285    684  -1176   -222       C  
ATOM   3153  CG  ASP D 239     -25.226  23.525 -83.541  1.00 36.42           C  
ANISOU 3153  CG  ASP D 239     5577   3845   4417    892  -1209   -227       C  
ATOM   3154  OD1 ASP D 239     -24.207  23.062 -84.089  1.00 37.33           O  
ANISOU 3154  OD1 ASP D 239     5503   4060   4621    934  -1196   -278       O  
ATOM   3155  OD2 ASP D 239     -25.822  22.944 -82.607  1.00 37.65           O  
ANISOU 3155  OD2 ASP D 239     5932   3904   4469   1031  -1225   -174       O  
ATOM   3156  N   ARG D 240     -22.845  25.473 -82.689  1.00 32.95           N  
ANISOU 3156  N   ARG D 240     4702   3713   4103    710  -1518   -494       N  
ATOM   3157  CA  ARG D 240     -21.397  25.512 -82.846  1.00 35.14           C  
ANISOU 3157  CA  ARG D 240     4632   4223   4494    679  -1588   -663       C  
ATOM   3158  C   ARG D 240     -20.936  24.956 -84.186  1.00 33.71           C  
ANISOU 3158  C   ARG D 240     4291   4084   4436    642  -1402   -660       C  
ATOM   3159  O   ARG D 240     -19.832  25.292 -84.628  1.00 35.06           O  
ANISOU 3159  O   ARG D 240     4156   4430   4735    506  -1369   -819       O  
ATOM   3160  CB  ARG D 240     -20.724  24.732 -81.710  1.00 37.44           C  
ANISOU 3160  CB  ARG D 240     4825   4706   4694    999  -1833   -720       C  
ATOM   3161  CG  ARG D 240     -21.116  23.260 -81.664  1.00 36.98           C  
ANISOU 3161  CG  ARG D 240     4955   4543   4553   1337  -1792   -552       C  
ATOM   3162  CD  ARG D 240     -20.652  22.597 -80.363  1.00 39.39           C  
ANISOU 3162  CD  ARG D 240     5300   4978   4687   1720  -2034   -542       C  
ATOM   3163  NE  ARG D 240     -21.063  21.196 -80.318  1.00 39.78           N  
ANISOU 3163  NE  ARG D 240     5617   4837   4659   1990  -1878   -361       N  
ATOM   3164  CZ  ARG D 240     -20.348  20.193 -80.820  1.00 44.38           C  
ANISOU 3164  CZ  ARG D 240     6087   5464   5312   2210  -1809   -354       C  
ATOM   3165  NH1 ARG D 240     -19.181  20.436 -81.402  1.00 46.83           N  
ANISOU 3165  NH1 ARG D 240     5969   6049   5776   2258  -1934   -527       N  
ATOM   3166  NH2 ARG D 240     -20.798  18.946 -80.740  1.00 46.30           N  
ANISOU 3166  NH2 ARG D 240     6624   5485   5483   2352  -1586   -201       N  
ATOM   3167  N   HIS D 241     -21.744  24.102 -84.830  1.00 31.93           N  
ANISOU 3167  N   HIS D 241     4247   3716   4167    739  -1262   -518       N  
ATOM   3168  CA  HIS D 241     -21.375  23.519 -86.117  1.00 32.91           C  
ANISOU 3168  CA  HIS D 241     4251   3877   4375    706  -1073   -534       C  
ATOM   3169  C   HIS D 241     -21.565  24.474 -87.287  1.00 31.41           C  
ANISOU 3169  C   HIS D 241     4077   3650   4207    409   -886   -520       C  
ATOM   3170  O   HIS D 241     -20.999  24.230 -88.358  1.00 29.00           O  
ANISOU 3170  O   HIS D 241     3636   3421   3963    333   -720   -568       O  
ATOM   3171  CB  HIS D 241     -22.195  22.256 -86.395  1.00 32.66           C  
ANISOU 3171  CB  HIS D 241     4425   3707   4276    877   -969   -436       C  
ATOM   3172  CG  HIS D 241     -21.893  21.119 -85.472  1.00 36.97           C  
ANISOU 3172  CG  HIS D 241     5024   4230   4793   1208  -1064   -417       C  
ATOM   3173  ND1 HIS D 241     -22.654  20.846 -84.356  1.00 37.13           N  
ANISOU 3173  ND1 HIS D 241     5311   4113   4685   1349  -1148   -319       N  
ATOM   3174  CD2 HIS D 241     -20.920  20.179 -85.504  1.00 39.71           C  
ANISOU 3174  CD2 HIS D 241     5226   4658   5203   1462  -1066   -468       C  
ATOM   3175  CE1 HIS D 241     -22.159  19.790 -83.736  1.00 38.92           C  
ANISOU 3175  CE1 HIS D 241     5599   4315   4874   1680  -1193   -286       C  
ATOM   3176  NE2 HIS D 241     -21.106  19.365 -84.412  1.00 40.87           N  
ANISOU 3176  NE2 HIS D 241     5593   4694   5240   1779  -1158   -373       N  
ATOM   3177  N   TYR D 242     -22.356  25.532 -87.127  1.00 31.66           N  
ANISOU 3177  N   TYR D 242     4305   3555   4169    271   -889   -445       N  
ATOM   3178  CA  TYR D 242     -22.618  26.434 -88.240  1.00 31.88           C  
ANISOU 3178  CA  TYR D 242     4434   3510   4167     63   -701   -381       C  
ATOM   3179  C   TYR D 242     -21.441  27.382 -88.443  1.00 33.78           C  
ANISOU 3179  C   TYR D 242     4509   3795   4532   -189   -600   -503       C  
ATOM   3180  O   TYR D 242     -20.979  28.028 -87.495  1.00 35.56           O  
ANISOU 3180  O   TYR D 242     4655   4029   4825   -278   -708   -619       O  
ATOM   3181  CB  TYR D 242     -23.903  27.230 -88.013  1.00 30.53           C  
ANISOU 3181  CB  TYR D 242     4551   3176   3873     71   -726   -249       C  
ATOM   3182  CG  TYR D 242     -24.271  28.040 -89.229  1.00 29.26           C  
ANISOU 3182  CG  TYR D 242     4552   2943   3623    -37   -542   -135       C  
ATOM   3183  CD1 TYR D 242     -24.931  27.455 -90.305  1.00 28.82           C  
ANISOU 3183  CD1 TYR D 242     4554   2962   3435     45   -465    -61       C  
ATOM   3184  CD2 TYR D 242     -23.905  29.375 -89.330  1.00 30.54           C  
ANISOU 3184  CD2 TYR D 242     4830   2960   3812   -222   -425   -115       C  
ATOM   3185  CE1 TYR D 242     -25.244  28.186 -91.432  1.00 27.87           C  
ANISOU 3185  CE1 TYR D 242     4607   2812   3170      3   -318     61       C  
ATOM   3186  CE2 TYR D 242     -24.215  30.114 -90.456  1.00 30.72           C  
ANISOU 3186  CE2 TYR D 242     5078   2883   3713   -272   -229     31       C  
ATOM   3187  CZ  TYR D 242     -24.878  29.515 -91.499  1.00 30.26           C  
ANISOU 3187  CZ  TYR D 242     5074   2938   3484   -133   -196    132       C  
ATOM   3188  OH  TYR D 242     -25.185  30.259 -92.614  1.00 32.87           O  
ANISOU 3188  OH  TYR D 242     5656   3200   3632   -127    -24    297       O  
ATOM   3189  N   LYS D 243     -20.961  27.466 -89.683  1.00 31.80           N  
ANISOU 3189  N   LYS D 243     4206   3577   4299   -335   -369   -504       N  
ATOM   3190  CA  LYS D 243     -19.799  28.280 -90.039  1.00 35.93           C  
ANISOU 3190  CA  LYS D 243     4561   4139   4953   -632   -183   -645       C  
ATOM   3191  C   LYS D 243     -20.238  29.367 -91.017  1.00 39.05           C  
ANISOU 3191  C   LYS D 243     5283   4316   5237   -825     82   -487       C  
ATOM   3192  O   LYS D 243     -20.388  29.113 -92.217  1.00 40.67           O  
ANISOU 3192  O   LYS D 243     5588   4535   5330   -818    264   -384       O  
ATOM   3193  CB  LYS D 243     -18.691  27.413 -90.631  1.00 36.28           C  
ANISOU 3193  CB  LYS D 243     4256   4417   5112   -631    -85   -801       C  
ATOM   3194  CG  LYS D 243     -18.274  26.245 -89.745  1.00 36.99           C  
ANISOU 3194  CG  LYS D 243     4074   4703   5276   -338   -339   -915       C  
ATOM   3195  CD  LYS D 243     -17.787  26.719 -88.380  1.00 40.62           C  
ANISOU 3195  CD  LYS D 243     4358   5264   5810   -347   -576  -1071       C  
ATOM   3196  CE  LYS D 243     -17.354  25.538 -87.523  1.00 42.50           C  
ANISOU 3196  CE  LYS D 243     4373   5711   6063     26   -836  -1146       C  
ATOM   3197  NZ  LYS D 243     -17.056  25.933 -86.115  1.00 44.77           N  
ANISOU 3197  NZ  LYS D 243     4545   6130   6338     82  -1121  -1276       N  
ATOM   3198  N   GLU D 244     -20.430  30.586 -90.505  1.00 38.85           N  
ANISOU 3198  N   GLU D 244     5459   4081   5222   -977    117   -469       N  
ATOM   3199  CA  GLU D 244     -20.896  31.679 -91.351  1.00 38.93           C  
ANISOU 3199  CA  GLU D 244     5866   3821   5102  -1093    382   -277       C  
ATOM   3200  C   GLU D 244     -19.846  32.139 -92.355  1.00 42.42           C  
ANISOU 3200  C   GLU D 244     6279   4236   5603  -1416    755   -340       C  
ATOM   3201  O   GLU D 244     -20.203  32.769 -93.354  1.00 43.24           O  
ANISOU 3201  O   GLU D 244     6750   4144   5534  -1450   1014   -131       O  
ATOM   3202  CB  GLU D 244     -21.339  32.864 -90.489  1.00 40.19           C  
ANISOU 3202  CB  GLU D 244     6287   3708   5277  -1161    363   -256       C  
ATOM   3203  CG  GLU D 244     -20.201  33.596 -89.809  1.00 44.61           C  
ANISOU 3203  CG  GLU D 244     6668   4229   6054  -1533    466   -537       C  
ATOM   3204  CD  GLU D 244     -19.810  32.954 -88.493  1.00 45.53           C  
ANISOU 3204  CD  GLU D 244     6405   4610   6286  -1460    124   -780       C  
ATOM   3205  OE1 GLU D 244     -20.329  31.859 -88.187  1.00 42.98           O  
ANISOU 3205  OE1 GLU D 244     5983   4461   5886  -1130   -140   -704       O  
ATOM   3206  OE2 GLU D 244     -18.987  33.546 -87.765  1.00 49.25           O  
ANISOU 3206  OE2 GLU D 244     6692   5115   6904  -1736    133  -1055       O  
ATOM   3207  N   ASN D 245     -18.571  31.833 -92.125  1.00 44.85           N  
ANISOU 3207  N   ASN D 245     6161   4753   6128  -1632    800   -625       N  
ATOM   3208  CA  ASN D 245     -17.496  32.310 -92.986  1.00 50.87           C  
ANISOU 3208  CA  ASN D 245     6842   5506   6981  -2002   1201   -745       C  
ATOM   3209  C   ASN D 245     -17.137  31.338 -94.103  1.00 51.19           C  
ANISOU 3209  C   ASN D 245     6723   5763   6963  -1922   1329   -730       C  
ATOM   3210  O   ASN D 245     -16.229  31.630 -94.887  1.00 53.28           O  
ANISOU 3210  O   ASN D 245     6903   6051   7292  -2224   1695   -837       O  
ATOM   3211  CB  ASN D 245     -16.245  32.606 -92.153  1.00 57.57           C  
ANISOU 3211  CB  ASN D 245     7243   6519   8114  -2325   1209  -1135       C  
ATOM   3212  CG  ASN D 245     -16.355  33.901 -91.373  1.00 63.44           C  
ANISOU 3212  CG  ASN D 245     8209   6978   8918  -2587   1273  -1208       C  
ATOM   3213  OD1 ASN D 245     -16.965  34.868 -91.833  1.00 65.81           O  
ANISOU 3213  OD1 ASN D 245     9032   6879   9094  -2675   1529   -982       O  
ATOM   3214  ND2 ASN D 245     -15.763  33.927 -90.183  1.00 65.21           N  
ANISOU 3214  ND2 ASN D 245     8056   7408   9314  -2688   1041  -1533       N  
ATOM   3215  N   ILE D 246     -17.817  30.204 -94.201  1.00 48.53           N  
ANISOU 3215  N   ILE D 246     6356   5573   6508  -1554   1080   -625       N  
ATOM   3216  CA  ILE D 246     -17.482  29.161 -95.163  1.00 50.46           C  
ANISOU 3216  CA  ILE D 246     6437   6027   6707  -1462   1185   -658       C  
ATOM   3217  C   ILE D 246     -18.590  29.129 -96.209  1.00 48.82           C  
ANISOU 3217  C   ILE D 246     6658   5714   6175  -1302   1255   -378       C  
ATOM   3218  O   ILE D 246     -19.679  28.601 -95.962  1.00 45.38           O  
ANISOU 3218  O   ILE D 246     6344   5291   5609  -1015    990   -261       O  
ATOM   3219  CB  ILE D 246     -17.301  27.801 -94.481  1.00 48.31           C  
ANISOU 3219  CB  ILE D 246     5798   5999   6559  -1177    884   -807       C  
ATOM   3220  CG1 ILE D 246     -16.153  27.871 -93.474  1.00 49.86           C  
ANISOU 3220  CG1 ILE D 246     5543   6375   7027  -1279    779  -1094       C  
ATOM   3221  CG2 ILE D 246     -17.036  26.727 -95.507  1.00 48.67           C  
ANISOU 3221  CG2 ILE D 246     5733   6207   6554  -1070   1026   -847       C  
ATOM   3222  CD1 ILE D 246     -15.875  26.565 -92.772  1.00 49.35           C  
ANISOU 3222  CD1 ILE D 246     5154   6541   7056   -929    492  -1212       C  
ATOM   3223  N   ARG D 247     -18.315  29.681 -97.389  1.00 53.18           N  
ANISOU 3223  N   ARG D 247     7436   6192   6578  -1487   1622   -286       N  
ATOM   3224  CA  ARG D 247     -19.306  29.786 -98.457  1.00 55.23           C  
ANISOU 3224  CA  ARG D 247     8122   6397   6464  -1317   1688    -19       C  
ATOM   3225  C   ARG D 247     -18.956  28.980 -99.698  1.00 57.40           C  
ANISOU 3225  C   ARG D 247     8340   6879   6589  -1317   1890    -70       C  
ATOM   3226  O   ARG D 247     -19.846  28.385-100.314  1.00 56.61           O  
ANISOU 3226  O   ARG D 247     8389   6900   6220  -1078   1767     27       O  
ATOM   3227  CB  ARG D 247     -19.497  31.259 -98.853  1.00 59.32           C  
ANISOU 3227  CB  ARG D 247     9126   6596   6816  -1458   1959    213       C  
ATOM   3228  CG  ARG D 247     -19.847  32.181 -97.694  1.00 61.51           C  
ANISOU 3228  CG  ARG D 247     9524   6618   7231  -1478   1820    252       C  
ATOM   3229  CD  ARG D 247     -21.346  32.193 -97.414  1.00 60.29           C  
ANISOU 3229  CD  ARG D 247     9619   6429   6861  -1085   1493    468       C  
ATOM   3230  NE  ARG D 247     -21.772  33.431 -96.762  1.00 61.48           N  
ANISOU 3230  NE  ARG D 247    10093   6240   7026  -1091   1514    597       N  
ATOM   3231  CZ  ARG D 247     -22.413  33.485 -95.597  1.00 58.14           C  
ANISOU 3231  CZ  ARG D 247     9604   5776   6710   -942   1211    561       C  
ATOM   3232  NH1 ARG D 247     -22.709  32.368 -94.945  1.00 51.38           N  
ANISOU 3232  NH1 ARG D 247     8393   5185   5945   -783    876    421       N  
ATOM   3233  NH2 ARG D 247     -22.760  34.658 -95.085  1.00 61.59           N  
ANISOU 3233  NH2 ARG D 247    10368   5879   7153   -953   1281    665       N  
ATOM   3234  N   THR D 248     -17.686  28.938-100.083  1.00 59.41           N  
ANISOU 3234  N   THR D 248     8359   7206   7008  -1591   2208   -256       N  
ATOM   3235  CA  THR D 248     -17.260  28.268-101.301  1.00 61.77           C  
ANISOU 3235  CA  THR D 248     8621   7686   7161  -1621   2467   -321       C  
ATOM   3236  C   THR D 248     -16.772  26.854-101.006  1.00 60.06           C  
ANISOU 3236  C   THR D 248     7925   7727   7169  -1484   2315   -595       C  
ATOM   3237  O   THR D 248     -16.420  26.511 -99.875  1.00 57.10           O  
ANISOU 3237  O   THR D 248     7203   7399   7095  -1421   2081   -751       O  
ATOM   3238  CB  THR D 248     -16.148  29.062-101.988  1.00 66.26           C  
ANISOU 3238  CB  THR D 248     9232   8178   7767  -2012   2981   -375       C  
ATOM   3239  OG1 THR D 248     -14.902  28.791-101.337  1.00 67.41           O  
ANISOU 3239  OG1 THR D 248     8818   8468   8328  -2218   3042   -713       O  
ATOM   3240  CG2 THR D 248     -16.436  30.554-101.911  1.00 68.87           C  
ANISOU 3240  CG2 THR D 248    10024   8155   7989  -2182   3158   -137       C  
ATOM   3241  N   GLY D 249     -16.753  26.030-102.058  1.00 61.50           N  
ANISOU 3241  N   GLY D 249     8126   8069   7173  -1413   2464   -649       N  
ATOM   3242  CA  GLY D 249     -16.197  24.695-101.928  1.00 61.07           C  
ANISOU 3242  CA  GLY D 249     7670   8208   7325  -1277   2411   -912       C  
ATOM   3243  C   GLY D 249     -14.721  24.707-101.589  1.00 63.97           C  
ANISOU 3243  C   GLY D 249     7568   8687   8049  -1452   2601  -1170       C  
ATOM   3244  O   GLY D 249     -14.223  23.793-100.925  1.00 64.58           O  
ANISOU 3244  O   GLY D 249     7255   8897   8386  -1261   2436  -1371       O  
ATOM   3245  N   GLU D 250     -14.003  25.742-102.027  1.00 67.20           N  
ANISOU 3245  N   GLU D 250     8009   9052   8471  -1805   2961  -1179       N  
ATOM   3246  CA  GLU D 250     -12.590  25.861-101.688  1.00 72.03           C  
ANISOU 3246  CA  GLU D 250     8107   9823   9438  -2028   3156  -1483       C  
ATOM   3247  C   GLU D 250     -12.400  26.124-100.200  1.00 69.33           C  
ANISOU 3247  C   GLU D 250     7462   9493   9386  -1988   2808  -1584       C  
ATOM   3248  O   GLU D 250     -11.433  25.645 -99.596  1.00 70.26           O  
ANISOU 3248  O   GLU D 250     7032   9861   9805  -1935   2729  -1877       O  
ATOM   3249  CB  GLU D 250     -11.946  26.969-102.521  1.00 80.39           C  
ANISOU 3249  CB  GLU D 250     9321  10794  10430  -2487   3687  -1481       C  
ATOM   3250  CG  GLU D 250     -12.060  26.765-104.028  1.00 86.69           C  
ANISOU 3250  CG  GLU D 250    10452  11601  10885  -2531   4067  -1377       C  
ATOM   3251  CD  GLU D 250     -13.369  27.289-104.597  1.00 87.86           C  
ANISOU 3251  CD  GLU D 250    11289  11520  10574  -2416   4003   -981       C  
ATOM   3252  OE1 GLU D 250     -14.395  26.584-104.485  1.00 84.67           O  
ANISOU 3252  OE1 GLU D 250    11011  11155  10006  -2064   3625   -872       O  
ATOM   3253  OE2 GLU D 250     -13.373  28.406-105.157  1.00 91.60           O  
ANISOU 3253  OE2 GLU D 250    12182  11778  10844  -2669   4346   -787       O  
ATOM   3254  N   GLU D 251     -13.316  26.878 -99.589  1.00 66.51           N  
ANISOU 3254  N   GLU D 251     7450   8897   8923  -1980   2586  -1356       N  
ATOM   3255  CA  GLU D 251     -13.203  27.162 -98.163  1.00 64.66           C  
ANISOU 3255  CA  GLU D 251     6976   8674   8917  -1947   2254  -1455       C  
ATOM   3256  C   GLU D 251     -13.596  25.959 -97.313  1.00 59.58           C  
ANISOU 3256  C   GLU D 251     6155   8151   8332  -1495   1810  -1475       C  
ATOM   3257  O   GLU D 251     -13.110  25.817 -96.184  1.00 58.48           O  
ANISOU 3257  O   GLU D 251     5662   8154   8404  -1395   1550  -1645       O  
ATOM   3258  CB  GLU D 251     -14.058  28.377 -97.802  1.00 63.26           C  
ANISOU 3258  CB  GLU D 251     7257   8174   8605  -2080   2206  -1217       C  
ATOM   3259  CG  GLU D 251     -13.572  29.675 -98.425  1.00 67.24           C  
ANISOU 3259  CG  GLU D 251     7978   8482   9087  -2545   2678  -1204       C  
ATOM   3260  CD  GLU D 251     -14.566  30.805 -98.260  1.00 67.51           C  
ANISOU 3260  CD  GLU D 251     8588   8133   8930  -2582   2669   -906       C  
ATOM   3261  OE1 GLU D 251     -15.781  30.524 -98.238  1.00 64.69           O  
ANISOU 3261  OE1 GLU D 251     8542   7694   8343  -2232   2390   -646       O  
ATOM   3262  OE2 GLU D 251     -14.133  31.972 -98.152  1.00 71.83           O  
ANISOU 3262  OE2 GLU D 251     9270   8459   9564  -2963   2963   -954       O  
ATOM   3263  N   VAL D 252     -14.471  25.091 -97.825  1.00 56.66           N  
ANISOU 3263  N   VAL D 252     6041   7726   7760  -1225   1733  -1317       N  
ATOM   3264  CA  VAL D 252     -14.792  23.858 -97.109  1.00 54.34           C  
ANISOU 3264  CA  VAL D 252     5627   7492   7526   -826   1410  -1347       C  
ATOM   3265  C   VAL D 252     -13.571  22.951 -97.053  1.00 57.98           C  
ANISOU 3265  C   VAL D 252     5598   8208   8221   -677   1467  -1622       C  
ATOM   3266  O   VAL D 252     -13.232  22.400 -95.999  1.00 57.79           O  
ANISOU 3266  O   VAL D 252     5310   8291   8358   -403   1190  -1719       O  
ATOM   3267  CB  VAL D 252     -15.986  23.140 -97.764  1.00 51.49           C  
ANISOU 3267  CB  VAL D 252     5641   7015   6906   -649   1382  -1178       C  
ATOM   3268  CG1 VAL D 252     -16.261  21.822 -97.050  1.00 49.89           C  
ANISOU 3268  CG1 VAL D 252     5358   6812   6786   -285   1140  -1229       C  
ATOM   3269  CG2 VAL D 252     -17.227  24.025 -97.748  1.00 48.65           C  
ANISOU 3269  CG2 VAL D 252     5706   6466   6312   -719   1278   -922       C  
ATOM   3270  N   LYS D 253     -12.894  22.782 -98.193  1.00 61.59           N  
ANISOU 3270  N   LYS D 253     5940   8781   8680   -821   1833  -1748       N  
ATOM   3271  CA  LYS D 253     -11.699  21.948 -98.229  1.00 67.21           C  
ANISOU 3271  CA  LYS D 253     6156   9758   9623   -658   1925  -2033       C  
ATOM   3272  C   LYS D 253     -10.610  22.508 -97.325  1.00 70.47           C  
ANISOU 3272  C   LYS D 253     6051  10417  10306   -750   1824  -2269       C  
ATOM   3273  O   LYS D 253      -9.896  21.751 -96.658  1.00 73.12           O  
ANISOU 3273  O   LYS D 253     5965  10988  10829   -417   1634  -2458       O  
ATOM   3274  CB  LYS D 253     -11.195  21.815 -99.667  1.00 71.41           C  
ANISOU 3274  CB  LYS D 253     6675  10369  10088   -852   2389  -2139       C  
ATOM   3275  CG  LYS D 253     -10.868  20.388-100.076  1.00 74.61           C  
ANISOU 3275  CG  LYS D 253     6928  10872  10550   -506   2462  -2288       C  
ATOM   3276  CD  LYS D 253     -10.439  20.305-101.534  1.00 78.54           C  
ANISOU 3276  CD  LYS D 253     7456  11447  10939   -721   2943  -2398       C  
ATOM   3277  CE  LYS D 253     -11.500  20.878-102.460  1.00 77.18           C  
ANISOU 3277  CE  LYS D 253     7864  11075  10386   -965   3081  -2145       C  
ATOM   3278  NZ  LYS D 253     -11.168  20.648-103.892  1.00 80.43           N  
ANISOU 3278  NZ  LYS D 253     8369  11570  10620  -1118   3531  -2244       N  
ATOM   3279  N   GLN D 254     -10.476  23.834 -97.278  1.00 71.19           N  
ANISOU 3279  N   GLN D 254     6176  10463  10409  -1187   1950  -2276       N  
ATOM   3280  CA  GLN D 254      -9.466  24.433 -96.415  1.00 75.19           C  
ANISOU 3280  CA  GLN D 254     6170  11230  11168  -1351   1864  -2566       C  
ATOM   3281  C   GLN D 254      -9.811  24.259 -94.941  1.00 72.94           C  
ANISOU 3281  C   GLN D 254     5826  10977  10911  -1035   1344  -2530       C  
ATOM   3282  O   GLN D 254      -8.906  24.157 -94.105  1.00 76.48           O  
ANISOU 3282  O   GLN D 254     5743  11767  11548   -922   1140  -2810       O  
ATOM   3283  CB  GLN D 254      -9.294  25.913 -96.754  1.00 78.25           C  
ANISOU 3283  CB  GLN D 254     6688  11484  11558  -1949   2194  -2595       C  
ATOM   3284  CG  GLN D 254      -7.845  26.365 -96.799  1.00 85.35           C  
ANISOU 3284  CG  GLN D 254     6967  12724  12738  -2309   2465  -3028       C  
ATOM   3285  CD  GLN D 254      -7.640  27.585 -97.673  1.00 89.46           C  
ANISOU 3285  CD  GLN D 254     7805  12998  13187  -2884   2965  -2996       C  
ATOM   3286  OE1 GLN D 254      -7.957  28.707 -97.277  1.00 90.32           O  
ANISOU 3286  OE1 GLN D 254     8189  12861  13269  -3198   2999  -2928       O  
ATOM   3287  NE2 GLN D 254      -7.107  27.372 -98.871  1.00 92.66           N  
ANISOU 3287  NE2 GLN D 254     8260  13418  13528  -2975   3340  -3020       N  
ATOM   3288  N   TYR D 255     -11.101  24.218 -94.601  1.00 67.64           N  
ANISOU 3288  N   TYR D 255     5674   9991  10034   -879   1126  -2208       N  
ATOM   3289  CA  TYR D 255     -11.484  24.025 -93.206  1.00 64.64           C  
ANISOU 3289  CA  TYR D 255     5296   9621   9645   -579    670  -2156       C  
ATOM   3290  C   TYR D 255     -11.112  22.629 -92.725  1.00 65.63           C  
ANISOU 3290  C   TYR D 255     5173   9937   9827    -29    438  -2221       C  
ATOM   3291  O   TYR D 255     -10.438  22.473 -91.701  1.00 68.19           O  
ANISOU 3291  O   TYR D 255     5118  10540  10250    200    149  -2396       O  
ATOM   3292  CB  TYR D 255     -12.981  24.269 -93.022  1.00 59.49           C  
ANISOU 3292  CB  TYR D 255     5244   8594   8765   -549    546  -1815       C  
ATOM   3293  CG  TYR D 255     -13.465  23.954 -91.622  1.00 57.38           C  
ANISOU 3293  CG  TYR D 255     5037   8310   8457   -227    122  -1742       C  
ATOM   3294  CD1 TYR D 255     -13.407  24.908 -90.616  1.00 57.83           C  
ANISOU 3294  CD1 TYR D 255     5037   8398   8538   -387    -68  -1816       C  
ATOM   3295  CD2 TYR D 255     -13.965  22.697 -91.302  1.00 55.42           C  
ANISOU 3295  CD2 TYR D 255     4932   7995   8132    221    -51  -1613       C  
ATOM   3296  CE1 TYR D 255     -13.841  24.623 -89.338  1.00 56.87           C  
ANISOU 3296  CE1 TYR D 255     4995   8276   8338    -89   -438  -1751       C  
ATOM   3297  CE2 TYR D 255     -14.391  22.401 -90.026  1.00 53.80           C  
ANISOU 3297  CE2 TYR D 255     4829   7755   7858    513   -391  -1530       C  
ATOM   3298  CZ  TYR D 255     -14.333  23.368 -89.049  1.00 55.32           C  
ANISOU 3298  CZ  TYR D 255     4959   8013   8047    367   -594  -1592       C  
ATOM   3299  OH  TYR D 255     -14.768  23.076 -87.774  1.00 55.45           O  
ANISOU 3299  OH  TYR D 255     5109   8006   7954    662   -919  -1507       O  
ATOM   3300  N   PHE D 256     -11.554  21.598 -93.445  1.00 64.53           N  
ANISOU 3300  N   PHE D 256     5269   9645   9605    210    562  -2087       N  
ATOM   3301  CA  PHE D 256     -11.269  20.230 -93.036  1.00 66.91           C  
ANISOU 3301  CA  PHE D 256     5444  10027   9952    758    404  -2117       C  
ATOM   3302  C   PHE D 256      -9.807  19.852 -93.230  1.00 75.72           C  
ANISOU 3302  C   PHE D 256     5946  11542  11284    907    494  -2439       C  
ATOM   3303  O   PHE D 256      -9.390  18.786 -92.762  1.00 77.03           O  
ANISOU 3303  O   PHE D 256     5950  11819  11501   1437    335  -2483       O  
ATOM   3304  CB  PHE D 256     -12.178  19.262 -93.794  1.00 62.49           C  
ANISOU 3304  CB  PHE D 256     5333   9157   9254    906    567  -1930       C  
ATOM   3305  CG  PHE D 256     -13.617  19.342 -93.376  1.00 56.53           C  
ANISOU 3305  CG  PHE D 256     5101   8076   8302    889    413  -1656       C  
ATOM   3306  CD1 PHE D 256     -14.053  18.702 -92.228  1.00 54.72           C  
ANISOU 3306  CD1 PHE D 256     5030   7732   8029   1258    129  -1539       C  
ATOM   3307  CD2 PHE D 256     -14.530  20.068 -94.122  1.00 53.34           C  
ANISOU 3307  CD2 PHE D 256     5029   7498   7741    527    562  -1519       C  
ATOM   3308  CE1 PHE D 256     -15.375  18.777 -91.832  1.00 50.64           C  
ANISOU 3308  CE1 PHE D 256     4958   6937   7346   1214     25  -1322       C  
ATOM   3309  CE2 PHE D 256     -15.855  20.148 -93.732  1.00 49.65           C  
ANISOU 3309  CE2 PHE D 256     4972   6788   7104    531    415  -1306       C  
ATOM   3310  CZ  PHE D 256     -16.278  19.501 -92.584  1.00 48.57           C  
ANISOU 3310  CZ  PHE D 256     4953   6544   6957    849    161  -1223       C  
ATOM   3311  N   SER D 257      -9.021  20.697 -93.899  1.00 82.13           N  
ANISOU 3311  N   SER D 257     6421  12565  12222    469    769  -2666       N  
ATOM   3312  CA  SER D 257      -7.586  20.458 -93.982  1.00 90.00           C  
ANISOU 3312  CA  SER D 257     6731  14017  13450    572    849  -3035       C  
ATOM   3313  C   SER D 257      -6.900  20.691 -92.642  1.00 95.32           C  
ANISOU 3313  C   SER D 257     7053  14998  14165    753    423  -3173       C  
ATOM   3314  O   SER D 257      -5.850  20.098 -92.374  1.00100.67           O  
ANISOU 3314  O   SER D 257     7422  15942  14886   1061    301  -3304       O  
ATOM   3315  CB  SER D 257      -6.970  21.351 -95.059  1.00 92.54           C  
ANISOU 3315  CB  SER D 257     6868  14431  13861    -25   1308  -3227       C  
ATOM   3316  OG  SER D 257      -5.565  21.184 -95.121  1.00 98.41           O  
ANISOU 3316  OG  SER D 257     7169  15498  14725     16   1332  -3479       O  
ATOM   3317  N   LYS D 258      -7.475  21.539 -91.789  1.00 96.14           N  
ANISOU 3317  N   LYS D 258     7261  15053  14216    568    190  -3127       N  
ATOM   3318  CA  LYS D 258      -6.854  21.925 -90.530  1.00101.78           C  
ANISOU 3318  CA  LYS D 258     7741  16035  14897    647   -191  -3260       C  
ATOM   3319  C   LYS D 258      -7.699  21.575 -89.316  1.00100.70           C  
ANISOU 3319  C   LYS D 258     7913  15771  14580   1055   -622  -3029       C  
ATOM   3320  O   LYS D 258      -7.241  21.770 -88.184  1.00103.85           O  
ANISOU 3320  O   LYS D 258     8186  16388  14886   1189   -953  -3109       O  
ATOM   3321  CB  LYS D 258      -6.557  23.431 -90.527  1.00105.52           C  
ANISOU 3321  CB  LYS D 258     8079  16568  15444    -29    -41  -3473       C  
ATOM   3322  CG  LYS D 258      -6.156  23.980 -91.884  1.00110.27           C  
ANISOU 3322  CG  LYS D 258     8625  17103  16170   -553    497  -3591       C  
ATOM   3323  CD  LYS D 258      -5.569  25.374 -91.766  1.00115.57           C  
ANISOU 3323  CD  LYS D 258     9177  17827  16908  -1160    663  -3832       C  
ATOM   3324  CE  LYS D 258      -5.117  25.897 -93.120  1.00118.73           C  
ANISOU 3324  CE  LYS D 258     9612  18114  17387  -1653   1230  -3916       C  
ATOM   3325  NZ  LYS D 258      -4.223  24.932 -93.818  1.00122.41           N  
ANISOU 3325  NZ  LYS D 258     9764  18822  17924  -1392   1356  -4038       N  
ATOM   3326  N   SER D 259      -8.918  21.081 -89.515  1.00 93.82           N  
ANISOU 3326  N   SER D 259     8342  15422  11883   1110  -1088   -556       N  
ATOM   3327  CA  SER D 259      -9.794  20.684 -88.424  1.00 91.14           C  
ANISOU 3327  CA  SER D 259     8410  14827  11391   1171  -1338   -389       C  
ATOM   3328  C   SER D 259     -10.439  19.347 -88.760  1.00 88.27           C  
ANISOU 3328  C   SER D 259     8458  13939  11143   1689  -1290   -204       C  
ATOM   3329  O   SER D 259     -10.809  19.095 -89.910  1.00 87.19           O  
ANISOU 3329  O   SER D 259     8537  13436  11154   1785  -1008   -312       O  
ATOM   3330  CB  SER D 259     -10.875  21.741 -88.152  1.00 86.76           C  
ANISOU 3330  CB  SER D 259     8260  13988  10716    616  -1280   -531       C  
ATOM   3331  OG  SER D 259     -12.044  21.158 -87.597  1.00 83.03           O  
ANISOU 3331  OG  SER D 259     8290  13125  10134    732  -1358   -381       O  
ATOM   3332  N   LYS D 260     -10.567  18.491 -87.749  1.00 87.19           N  
ANISOU 3332  N   LYS D 260     8438  13771  10918   1990  -1575     82       N  
ATOM   3333  CA  LYS D 260     -11.202  17.189 -87.897  1.00 84.71           C  
ANISOU 3333  CA  LYS D 260     8564  12883  10739   2422  -1570    300       C  
ATOM   3334  C   LYS D 260     -12.494  17.097 -87.086  1.00 78.67           C  
ANISOU 3334  C   LYS D 260     8323  11794   9776   2166  -1666    480       C  
ATOM   3335  O   LYS D 260     -12.787  16.066 -86.474  1.00 79.72           O  
ANISOU 3335  O   LYS D 260     8707  11685   9900   2447  -1840    821       O  
ATOM   3336  CB  LYS D 260     -10.229  16.074 -87.513  1.00 92.03           C  
ANISOU 3336  CB  LYS D 260     9209  13960  11798   3072  -1803    571       C  
ATOM   3337  CG  LYS D 260      -8.833  16.235 -88.136  1.00 97.20           C  
ANISOU 3337  CG  LYS D 260     9190  15133  12607   3336  -1730    382       C  
ATOM   3338  CD  LYS D 260      -8.333  14.940 -88.779  1.00102.24           C  
ANISOU 3338  CD  LYS D 260     9791  15475  13581   4095  -1663    427       C  
ATOM   3339  CE  LYS D 260      -8.527  14.964 -90.298  1.00 99.91           C  
ANISOU 3339  CE  LYS D 260     9618  14890  13456   4086  -1223     36       C  
ATOM   3340  NZ  LYS D 260      -8.556  13.600 -90.908  1.00103.10           N  
ANISOU 3340  NZ  LYS D 260    10279  14718  14174   4746  -1126      4       N  
ATOM   3341  N   ALA D 261     -13.265  18.184 -87.059  1.00 71.91           N  
ANISOU 3341  N   ALA D 261     7619  10940   8764   1635  -1547    267       N  
ATOM   3342  CA  ALA D 261     -14.618  18.143 -86.527  1.00 66.15           C  
ANISOU 3342  CA  ALA D 261     7358   9909   7867   1392  -1544    357       C  
ATOM   3343  C   ALA D 261     -15.466  17.154 -87.322  1.00 60.53           C  
ANISOU 3343  C   ALA D 261     7081   8561   7357   1579  -1379    436       C  
ATOM   3344  O   ALA D 261     -15.175  16.829 -88.476  1.00 61.83           O  
ANISOU 3344  O   ALA D 261     7230   8497   7765   1791  -1200    288       O  
ATOM   3345  CB  ALA D 261     -15.251  19.534 -86.568  1.00 62.50           C  
ANISOU 3345  CB  ALA D 261     6943   9516   7286    877  -1404     46       C  
ATOM   3346  N   GLU D 262     -16.531  16.666 -86.687  1.00 55.84           N  
ANISOU 3346  N   GLU D 262     6864   7721   6631   1462  -1433    648       N  
ATOM   3347  CA  GLU D 262     -17.346  15.645 -87.337  1.00 53.74           C  
ANISOU 3347  CA  GLU D 262     7012   6848   6560   1574  -1311    729       C  
ATOM   3348  C   GLU D 262     -18.097  16.215 -88.537  1.00 45.81           C  
ANISOU 3348  C   GLU D 262     6137   5624   5644   1339  -1036    382       C  
ATOM   3349  O   GLU D 262     -18.164  15.573 -89.593  1.00 44.54           O  
ANISOU 3349  O   GLU D 262     6125   5097   5699   1514   -898    265       O  
ATOM   3350  CB  GLU D 262     -18.318  15.018 -86.338  1.00 58.17           C  
ANISOU 3350  CB  GLU D 262     7909   7254   6939   1417  -1424   1074       C  
ATOM   3351  CG  GLU D 262     -17.932  13.603 -85.898  1.00 68.05           C  
ANISOU 3351  CG  GLU D 262     9332   8195   8328   1800  -1615   1516       C  
ATOM   3352  CD  GLU D 262     -18.126  12.558 -86.993  1.00 72.39           C  
ANISOU 3352  CD  GLU D 262    10188   8041   9275   2042  -1477   1440       C  
ATOM   3353  OE1 GLU D 262     -19.290  12.262 -87.346  1.00 71.48           O  
ANISOU 3353  OE1 GLU D 262    10429   7537   9191   1748  -1338   1389       O  
ATOM   3354  OE2 GLU D 262     -17.112  12.028 -87.497  1.00 75.91           O  
ANISOU 3354  OE2 GLU D 262    10493   8353   9996   2525  -1505   1395       O  
ATOM   3355  N   PHE D 263     -18.654  17.418 -88.407  1.00 39.59           N  
ANISOU 3355  N   PHE D 263     5295   5060   4687    965   -962    203       N  
ATOM   3356  CA  PHE D 263     -19.330  18.043 -89.539  1.00 36.58           C  
ANISOU 3356  CA  PHE D 263     5008   4512   4378    778   -739    -60       C  
ATOM   3357  C   PHE D 263     -19.439  19.545 -89.307  1.00 33.60           C  
ANISOU 3357  C   PHE D 263     4466   4416   3886    473   -701   -243       C  
ATOM   3358  O   PHE D 263     -19.185  20.053 -88.211  1.00 34.71           O  
ANISOU 3358  O   PHE D 263     4465   4859   3864    356   -834   -228       O  
ATOM   3359  CB  PHE D 263     -20.711  17.420 -89.786  1.00 34.30           C  
ANISOU 3359  CB  PHE D 263     5084   3862   4088    650   -668    -17       C  
ATOM   3360  CG  PHE D 263     -21.737  17.747 -88.733  1.00 34.11           C  
ANISOU 3360  CG  PHE D 263     5152   3967   3843    368   -718     79       C  
ATOM   3361  CD1 PHE D 263     -21.913  16.912 -87.641  1.00 39.54           C  
ANISOU 3361  CD1 PHE D 263     5962   4659   4403    372   -857    386       C  
ATOM   3362  CD2 PHE D 263     -22.536  18.876 -88.838  1.00 32.20           C  
ANISOU 3362  CD2 PHE D 263     4870   3851   3513    120   -615   -123       C  
ATOM   3363  CE1 PHE D 263     -22.854  17.201 -86.671  1.00 39.43           C  
ANISOU 3363  CE1 PHE D 263     5998   4860   4124     95   -863    461       C  
ATOM   3364  CE2 PHE D 263     -23.480  19.174 -87.868  1.00 31.61           C  
ANISOU 3364  CE2 PHE D 263     4834   3949   3226    -95   -625    -95       C  
ATOM   3365  CZ  PHE D 263     -23.641  18.334 -86.784  1.00 35.70           C  
ANISOU 3365  CZ  PHE D 263     5445   4556   3565   -128   -734    182       C  
ATOM   3366  N   ILE D 264     -19.805  20.254 -90.373  1.00 31.32           N  
ANISOU 3366  N   ILE D 264     4208   4013   3679    348   -525   -422       N  
ATOM   3367  CA  ILE D 264     -20.146  21.666 -90.298  1.00 31.48           C  
ANISOU 3367  CA  ILE D 264     4171   4123   3665     76   -471   -580       C  
ATOM   3368  C   ILE D 264     -21.460  21.872 -91.030  1.00 29.92           C  
ANISOU 3368  C   ILE D 264     4202   3683   3485    -15   -350   -626       C  
ATOM   3369  O   ILE D 264     -21.840  21.092 -91.903  1.00 27.80           O  
ANISOU 3369  O   ILE D 264     4074   3236   3254     84   -284   -589       O  
ATOM   3370  CB  ILE D 264     -19.069  22.588 -90.904  1.00 31.46           C  
ANISOU 3370  CB  ILE D 264     3916   4267   3770     -6   -401   -687       C  
ATOM   3371  CG1 ILE D 264     -18.894  22.294 -92.403  1.00 31.90           C  
ANISOU 3371  CG1 ILE D 264     3993   4207   3919    103   -227   -682       C  
ATOM   3372  CG2 ILE D 264     -17.768  22.465 -90.137  1.00 33.66           C  
ANISOU 3372  CG2 ILE D 264     3880   4888   4020     53   -546   -666       C  
ATOM   3373  CD1 ILE D 264     -18.063  23.326 -93.135  1.00 33.59           C  
ANISOU 3373  CD1 ILE D 264     3990   4569   4203    -70   -104   -735       C  
ATOM   3374  N   LEU D 265     -22.152  22.938 -90.653  1.00 30.29           N  
ANISOU 3374  N   LEU D 265     4265   3740   3504   -191   -332   -736       N  
ATOM   3375  CA  LEU D 265     -23.284  23.448 -91.407  1.00 29.82           C  
ANISOU 3375  CA  LEU D 265     4333   3510   3489   -244   -235   -778       C  
ATOM   3376  C   LEU D 265     -22.891  24.793 -92.000  1.00 29.44           C  
ANISOU 3376  C   LEU D 265     4215   3391   3579   -341   -167   -848       C  
ATOM   3377  O   LEU D 265     -22.047  25.501 -91.447  1.00 31.74           O  
ANISOU 3377  O   LEU D 265     4377   3761   3921   -452   -200   -939       O  
ATOM   3378  CB  LEU D 265     -24.522  23.585 -90.515  1.00 31.21           C  
ANISOU 3378  CB  LEU D 265     4573   3729   3557   -311   -253   -837       C  
ATOM   3379  CG  LEU D 265     -25.037  22.260 -89.948  1.00 31.77           C  
ANISOU 3379  CG  LEU D 265     4737   3852   3482   -301   -302   -698       C  
ATOM   3380  CD1 LEU D 265     -26.033  22.511 -88.814  1.00 33.62           C  
ANISOU 3380  CD1 LEU D 265     4953   4280   3543   -415   -295   -762       C  
ATOM   3381  CD2 LEU D 265     -25.641  21.387 -91.041  1.00 30.00           C  
ANISOU 3381  CD2 LEU D 265     4647   3442   3309   -271   -258   -619       C  
ATOM   3382  N   ARG D 266     -23.485  25.137 -93.142  1.00 28.62           N  
ANISOU 3382  N   ARG D 266     4200   3146   3529   -326    -87   -785       N  
ATOM   3383  CA  ARG D 266     -23.065  26.334 -93.853  1.00 27.57           C  
ANISOU 3383  CA  ARG D 266     4042   2902   3532   -429    -20   -745       C  
ATOM   3384  C   ARG D 266     -24.188  26.778 -94.780  1.00 28.94           C  
ANISOU 3384  C   ARG D 266     4342   2933   3722   -373      9   -637       C  
ATOM   3385  O   ARG D 266     -25.116  26.023 -95.074  1.00 27.74           O  
ANISOU 3385  O   ARG D 266     4248   2840   3451   -276    -15   -615       O  
ATOM   3386  CB  ARG D 266     -21.784  26.081 -94.650  1.00 27.99           C  
ANISOU 3386  CB  ARG D 266     3969   3090   3576   -464     58   -660       C  
ATOM   3387  CG  ARG D 266     -21.882  24.845 -95.544  1.00 27.81           C  
ANISOU 3387  CG  ARG D 266     3990   3164   3413   -301    107   -611       C  
ATOM   3388  CD  ARG D 266     -20.640  24.652 -96.392  1.00 29.78           C  
ANISOU 3388  CD  ARG D 266     4076   3609   3631   -296    231   -579       C  
ATOM   3389  NE  ARG D 266     -20.752  23.469 -97.247  1.00 29.82           N  
ANISOU 3389  NE  ARG D 266     4145   3683   3501   -117    295   -627       N  
ATOM   3390  CZ  ARG D 266     -21.368  23.442 -98.427  1.00 30.59           C  
ANISOU 3390  CZ  ARG D 266     4363   3808   3451   -130    367   -591       C  
ATOM   3391  NH1 ARG D 266     -21.934  24.538 -98.918  1.00 31.19           N  
ANISOU 3391  NH1 ARG D 266     4502   3843   3505   -277    372   -426       N  
ATOM   3392  NH2 ARG D 266     -21.412  22.315 -99.120  1.00 30.73           N  
ANISOU 3392  NH2 ARG D 266     4446   3890   3341     13    421   -727       N  
ATOM   3393  N   TRP D 267     -24.079  28.017 -95.243  1.00 29.91           N  
ANISOU 3393  N   TRP D 267     4499   2867   3998   -452     44   -547       N  
ATOM   3394  CA  TRP D 267     -25.053  28.579 -96.171  1.00 29.47           C  
ANISOU 3394  CA  TRP D 267     4548   2682   3968   -361     39   -366       C  
ATOM   3395  C   TRP D 267     -24.918  27.889 -97.525  1.00 30.66           C  
ANISOU 3395  C   TRP D 267     4706   3044   3900   -350     86   -180       C  
ATOM   3396  O   TRP D 267     -23.844  27.903 -98.130  1.00 34.98           O  
ANISOU 3396  O   TRP D 267     5202   3690   4397   -470    182    -88       O  
ATOM   3397  CB  TRP D 267     -24.831  30.087 -96.290  1.00 33.09           C  
ANISOU 3397  CB  TRP D 267     5084   2804   4687   -452     57   -263       C  
ATOM   3398  CG  TRP D 267     -25.884  30.827 -97.068  1.00 36.40           C  
ANISOU 3398  CG  TRP D 267     5615   3030   5186   -289     11    -32       C  
ATOM   3399  CD1 TRP D 267     -25.774  31.319 -98.337  1.00 38.56           C  
ANISOU 3399  CD1 TRP D 267     5969   3256   5427   -326     29    340       C  
ATOM   3400  CD2 TRP D 267     -27.197  31.172 -96.616  1.00 37.73           C  
ANISOU 3400  CD2 TRP D 267     5794   3079   5462    -40    -69   -128       C  
ATOM   3401  NE1 TRP D 267     -26.942  31.945 -98.706  1.00 40.93           N  
ANISOU 3401  NE1 TRP D 267     6343   3390   5820    -88    -71    517       N  
ATOM   3402  CE2 TRP D 267     -27.832  31.867 -97.666  1.00 41.49           C  
ANISOU 3402  CE2 TRP D 267     6350   3416   5999    109   -127    210       C  
ATOM   3403  CE3 TRP D 267     -27.899  30.957 -95.425  1.00 38.59           C  
ANISOU 3403  CE3 TRP D 267     5823   3245   5594     79    -89   -456       C  
ATOM   3404  CZ2 TRP D 267     -29.137  32.350 -97.559  1.00 43.82           C  
ANISOU 3404  CZ2 TRP D 267     6615   3610   6423    423   -220    214       C  
ATOM   3405  CZ3 TRP D 267     -29.192  31.434 -95.320  1.00 39.79           C  
ANISOU 3405  CZ3 TRP D 267     5937   3329   5854    354   -140   -488       C  
ATOM   3406  CH2 TRP D 267     -29.798  32.122 -96.380  1.00 43.60           C  
ANISOU 3406  CH2 TRP D 267     6469   3656   6441    548   -213   -164       C  
ATOM   3407  N   SER D 268     -25.999  27.273 -97.991  1.00 29.53           N  
ANISOU 3407  N   SER D 268     4596   3025   3601   -231     25   -162       N  
ATOM   3408  CA  SER D 268     -25.955  26.495 -99.220  1.00 30.40           C  
ANISOU 3408  CA  SER D 268     4722   3380   3450   -236     58    -85       C  
ATOM   3409  C   SER D 268     -25.904  27.388-100.455  1.00 33.34           C  
ANISOU 3409  C   SER D 268     5136   3798   3736   -274     83    224       C  
ATOM   3410  O   SER D 268     -26.455  28.492-100.476  1.00 35.74           O  
ANISOU 3410  O   SER D 268     5488   3899   4193   -222     15    423       O  
ATOM   3411  CB  SER D 268     -27.167  25.572 -99.316  1.00 29.34           C  
ANISOU 3411  CB  SER D 268     4600   3382   3167   -169    -38   -193       C  
ATOM   3412  OG  SER D 268     -27.278  25.042-100.627  1.00 32.32           O  
ANISOU 3412  OG  SER D 268     5008   4006   3268   -195    -31   -149       O  
ATOM   3413  N   SER D 269     -25.240  26.884-101.502  1.00 33.89           N  
ANISOU 3413  N   SER D 269     5190   4142   3545   -347    187    270       N  
ATOM   3414  CA  SER D 269     -25.167  27.611-102.767  1.00 39.57           C  
ANISOU 3414  CA  SER D 269     5948   5016   4072   -420    223    613       C  
ATOM   3415  C   SER D 269     -26.516  27.692-103.465  1.00 40.39           C  
ANISOU 3415  C   SER D 269     6100   5258   3988   -305     54    771       C  
ATOM   3416  O   SER D 269     -26.687  28.522-104.367  1.00 42.53           O  
ANISOU 3416  O   SER D 269     6421   5606   4133   -322     19   1156       O  
ATOM   3417  CB  SER D 269     -24.152  26.957-103.707  1.00 42.43           C  
ANISOU 3417  CB  SER D 269     6243   5758   4122   -523    408    561       C  
ATOM   3418  OG  SER D 269     -24.678  25.770-104.282  1.00 40.70           O  
ANISOU 3418  OG  SER D 269     6044   5818   3603   -442    377    318       O  
ATOM   3419  N   ALA D 270     -27.478  26.857-103.068  1.00 37.92           N  
ANISOU 3419  N   ALA D 270     5756   5006   3645   -208    -64    518       N  
ATOM   3420  CA  ALA D 270     -28.792  26.867-103.697  1.00 40.15           C  
ANISOU 3420  CA  ALA D 270     6005   5513   3738   -118   -250    631       C  
ATOM   3421  C   ALA D 270     -29.605  28.108-103.353  1.00 40.43           C  
ANISOU 3421  C   ALA D 270     6017   5307   4037     66   -385    905       C  
ATOM   3422  O   ALA D 270     -30.603  28.375-104.032  1.00 42.62           O  
ANISOU 3422  O   ALA D 270     6228   5805   4160    189   -559   1115       O  
ATOM   3423  CB  ALA D 270     -29.575  25.616-103.299  1.00 39.23           C  
ANISOU 3423  CB  ALA D 270     5829   5526   3548   -139   -324    269       C  
ATOM   3424  N   ASN D 271     -29.210  28.870-102.329  1.00 38.01           N  
ANISOU 3424  N   ASN D 271     5751   4568   4122    108   -322    884       N  
ATOM   3425  CA  ASN D 271     -29.975  30.060-101.970  1.00 43.65           C  
ANISOU 3425  CA  ASN D 271     6467   4978   5142    334   -432   1070       C  
ATOM   3426  C   ASN D 271     -29.902  31.126-103.058  1.00 51.43           C  
ANISOU 3426  C   ASN D 271     7563   5879   6099    385   -492   1591       C  
ATOM   3427  O   ASN D 271     -30.897  31.809-103.328  1.00 53.13           O  
ANISOU 3427  O   ASN D 271     7745   6040   6403    654   -665   1844       O  
ATOM   3428  CB  ASN D 271     -29.489  30.620-100.637  1.00 37.48           C  
ANISOU 3428  CB  ASN D 271     5732   3751   4759    328   -337    846       C  
ATOM   3429  CG  ASN D 271     -29.902  29.761 -99.472  1.00 34.29           C  
ANISOU 3429  CG  ASN D 271     5206   3453   4370    343   -322    426       C  
ATOM   3430  OD1 ASN D 271     -31.085  29.644 -99.162  1.00 36.94           O  
ANISOU 3430  OD1 ASN D 271     5406   3917   4714    519   -412    333       O  
ATOM   3431  ND2 ASN D 271     -28.926  29.145 -98.820  1.00 32.32           N  
ANISOU 3431  ND2 ASN D 271     4977   3194   4107    154   -210    201       N  
ATOM   3432  N   GLU D 272     -28.742  31.289-103.690  1.00 56.70           N  
ANISOU 3432  N   GLU D 272     8343   6560   6640    139   -353   1792       N  
ATOM   3433  CA  GLU D 272     -28.616  32.263-104.765  1.00 68.77           C  
ANISOU 3433  CA  GLU D 272    10000   8042   8089    119   -393   2368       C  
ATOM   3434  C   GLU D 272     -29.025  31.703-106.122  1.00 75.95           C  
ANISOU 3434  C   GLU D 272    10850   9582   8427    108   -485   2597       C  
ATOM   3435  O   GLU D 272     -29.352  32.481-107.024  1.00 78.14           O  
ANISOU 3435  O   GLU D 272    11203   9913   8575    185   -607   3139       O  
ATOM   3436  CB  GLU D 272     -27.180  32.794-104.839  1.00 71.98           C  
ANISOU 3436  CB  GLU D 272    10523   8228   8597   -209   -177   2522       C  
ATOM   3437  CG  GLU D 272     -26.921  34.002-103.940  1.00 75.19           C  
ANISOU 3437  CG  GLU D 272    11073   7913   9582   -218   -161   2567       C  
ATOM   3438  CD  GLU D 272     -27.346  35.319-104.576  1.00 82.88           C  
ANISOU 3438  CD  GLU D 272    12254   8482  10755   -102   -280   3173       C  
ATOM   3439  OE1 GLU D 272     -26.463  36.137-104.912  1.00 87.14           O  
ANISOU 3439  OE1 GLU D 272    12959   8725  11427   -399   -167   3530       O  
ATOM   3440  OE2 GLU D 272     -28.566  35.538-104.738  1.00 84.96           O  
ANISOU 3440  OE2 GLU D 272    12503   8723  11055    285   -493   3319       O  
ATOM   3441  N   SER D 273     -29.029  30.378-106.282  1.00 82.98           N  
ANISOU 3441  N   SER D 273    11622  10937   8971     13   -444   2196       N  
ATOM   3442  CA  SER D 273     -29.444  29.761-107.536  1.00 84.62           C  
ANISOU 3442  CA  SER D 273    11770  11782   8598    -31   -536   2286       C  
ATOM   3443  C   SER D 273     -30.957  29.672-107.679  1.00 84.31           C  
ANISOU 3443  C   SER D 273    11589  11973   8474    204   -834   2320       C  
ATOM   3444  O   SER D 273     -31.454  29.572-108.805  1.00 89.64           O  
ANISOU 3444  O   SER D 273    12208  13172   8677    200   -991   2554       O  
ATOM   3445  CB  SER D 273     -28.852  28.353-107.654  1.00 81.91           C  
ANISOU 3445  CB  SER D 273    11382  11777   7964   -223   -372   1769       C  
ATOM   3446  OG  SER D 273     -27.437  28.381-107.694  1.00 83.08           O  
ANISOU 3446  OG  SER D 273    11581  11867   8120   -409    -98   1747       O  
ATOM   3447  N   ASP D 274     -31.690  29.717-106.571  1.00110.09           N  
ANISOU 3447  N   ASP D 274    18940  14372   8516    445   -490   3388       N  
ATOM   3448  CA  ASP D 274     -33.103  29.363-106.562  1.00104.14           C  
ANISOU 3448  CA  ASP D 274    17904  13718   7945    950   -954   3049       C  
ATOM   3449  C   ASP D 274     -33.983  30.541-106.968  1.00106.74           C  
ANISOU 3449  C   ASP D 274    18677  13754   8127   1372  -1469   3437       C  
ATOM   3450  O   ASP D 274     -33.695  31.694-106.640  1.00109.76           O  
ANISOU 3450  O   ASP D 274    19392  13624   8690   1308  -1411   3835       O  
ATOM   3451  CB  ASP D 274     -33.497  28.864-105.170  1.00 96.22           C  
ANISOU 3451  CB  ASP D 274    16329  12530   7700   1048   -847   2610       C  
ATOM   3452  CG  ASP D 274     -34.926  28.377-105.103  1.00 95.72           C  
ANISOU 3452  CG  ASP D 274    15887  12588   7896   1534  -1273   2182       C  
ATOM   3453  OD1 ASP D 274     -35.238  27.346-105.736  1.00 96.16           O  
ANISOU 3453  OD1 ASP D 274    15636  13132   7770   1572  -1275   1798       O  
ATOM   3454  OD2 ASP D 274     -35.734  29.021-104.400  1.00 95.65           O  
ANISOU 3454  OD2 ASP D 274    15868  12186   8289   1857  -1581   2196       O  
ATOM   3455  N   THR D 275     -35.066  30.237-107.688  1.00105.66           N  
ANISOU 3455  N   THR D 275    18416  13986   7743   1784  -1918   3266       N  
ATOM   3456  CA  THR D 275     -36.059  31.235-108.071  1.00108.00           C  
ANISOU 3456  CA  THR D 275    18984  14112   7939   2265  -2411   3602       C  
ATOM   3457  C   THR D 275     -37.347  31.138-107.265  1.00104.94           C  
ANISOU 3457  C   THR D 275    18255  13555   8061   2733  -2789   3250       C  
ATOM   3458  O   THR D 275     -38.062  32.138-107.139  1.00107.99           O  
ANISOU 3458  O   THR D 275    18781  13585   8665   3049  -3056   3528       O  
ATOM   3459  CB  THR D 275     -36.412  31.109-109.561  1.00112.93           C  
ANISOU 3459  CB  THR D 275    19605  15387   7915   2391  -2655   3694       C  
ATOM   3460  OG1 THR D 275     -37.099  29.873-109.794  1.00111.22           O  
ANISOU 3460  OG1 THR D 275    19001  15782   7476   2593  -2873   3088       O  
ATOM   3461  CG2 THR D 275     -35.161  31.155-110.423  1.00114.58           C  
ANISOU 3461  CG2 THR D 275    20004  15822   7711   1902  -2274   3985       C  
ATOM   3462  N   GLU D 276     -37.656  29.961-106.716  1.00 99.31           N  
ANISOU 3462  N   GLU D 276    16920  13091   7722   2694  -2702   2586       N  
ATOM   3463  CA  GLU D 276     -38.945  29.745-106.066  1.00 97.58           C  
ANISOU 3463  CA  GLU D 276    16290  12801   7985   3128  -3058   2182       C  
ATOM   3464  C   GLU D 276     -39.029  30.408-104.697  1.00 89.15           C  
ANISOU 3464  C   GLU D 276    15211  11041   7619   3185  -3003   2256       C  
ATOM   3465  O   GLU D 276     -40.112  30.853-104.299  1.00 90.02           O  
ANISOU 3465  O   GLU D 276    15258  10918   8029   3624  -3399   2215       O  
ATOM   3466  CB  GLU D 276     -39.216  28.245-105.939  1.00 93.00           C  
ANISOU 3466  CB  GLU D 276    15042  12682   7613   3051  -2901   1441       C  
ATOM   3467  CG  GLU D 276     -38.897  27.456-107.199  1.00 96.30           C  
ANISOU 3467  CG  GLU D 276    15411  13787   7391   2850  -2800   1266       C  
ATOM   3468  CD  GLU D 276     -39.587  26.108-107.233  1.00 94.19           C  
ANISOU 3468  CD  GLU D 276    14483  13974   7332   2905  -2757    477       C  
ATOM   3469  OE1 GLU D 276     -40.365  25.817-106.298  1.00 90.90           O  
ANISOU 3469  OE1 GLU D 276    13663  13330   7545   3141  -2839    106       O  
ATOM   3470  OE2 GLU D 276     -39.361  25.346-108.199  1.00 95.57           O  
ANISOU 3470  OE2 GLU D 276    14533  14726   7053   2703  -2617    208       O  
ATOM   3471  N   ASN D 277     -37.911  30.474-103.969  1.00 85.14           N  
ANISOU 3471  N   ASN D 277    14733  10255   7361   2747  -2515   2342       N  
ATOM   3472  CA  ASN D 277     -37.864  31.067-102.630  1.00 85.93           C  
ANISOU 3472  CA  ASN D 277    14762   9790   8097   2724  -2400   2355       C  
ATOM   3473  C   ASN D 277     -38.836  30.385-101.673  1.00 76.90           C  
ANISOU 3473  C   ASN D 277    13003   8652   7564   3025  -2553   1812       C  
ATOM   3474  O   ASN D 277     -39.413  31.028-100.793  1.00 75.92           O  
ANISOU 3474  O   ASN D 277    12845   8089   7913   3250  -2731   1814       O  
ATOM   3475  CB  ASN D 277     -38.131  32.575-102.677  1.00 90.73           C  
ANISOU 3475  CB  ASN D 277    15942   9832   8698   2917  -2632   2881       C  
ATOM   3476  CG  ASN D 277     -37.021  33.339-103.365  1.00 90.60           C  
ANISOU 3476  CG  ASN D 277    16525   9678   8222   2561  -2348   3433       C  
ATOM   3477  OD1 ASN D 277     -35.850  32.969-103.274  1.00 92.02           O  
ANISOU 3477  OD1 ASN D 277    16670  10002   8292   2065  -1892   3408       O  
ATOM   3478  ND2 ASN D 277     -37.382  34.411-104.056  1.00 97.60           N  
ANISOU 3478  ND2 ASN D 277    17729  10378   8977   2723  -2498   3847       N  
ATOM   3479  N   LYS D 278     -39.038  29.081-101.849  1.00 74.30           N  
ANISOU 3479  N   LYS D 278    12179   8801   7250   3029  -2457   1334       N  
ATOM   3480  CA  LYS D 278     -39.889  28.346-100.925  1.00 76.97           C  
ANISOU 3480  CA  LYS D 278    11903   9138   8203   3290  -2516    811       C  
ATOM   3481  C   LYS D 278     -39.094  27.811 -99.741  1.00 71.22           C  
ANISOU 3481  C   LYS D 278    10758   8344   7959   3009  -1973    651       C  
ATOM   3482  O   LYS D 278     -39.653  27.648 -98.650  1.00 65.50           O  
ANISOU 3482  O   LYS D 278     9620   7441   7827   3221  -1997    390       O  
ATOM   3483  CB  LYS D 278     -40.603  27.203-101.655  1.00 76.57           C  
ANISOU 3483  CB  LYS D 278    11480   9606   8007   3455  -2634    324       C  
ATOM   3484  CG  LYS D 278     -41.508  26.366-100.757  1.00 70.74           C  
ANISOU 3484  CG  LYS D 278    10089   8859   7929   3722  -2643   -247       C  
ATOM   3485  CD  LYS D 278     -41.821  25.001-101.342  1.00 70.07           C  
ANISOU 3485  CD  LYS D 278     9549   9277   7797   3698  -2473   -811       C  
ATOM   3486  CE  LYS D 278     -42.967  25.041-102.325  1.00 74.93           C  
ANISOU 3486  CE  LYS D 278    10202  10225   8042   4018  -3023  -1030       C  
ATOM   3487  NZ  LYS D 278     -44.103  24.206-101.831  1.00 73.23           N  
ANISOU 3487  NZ  LYS D 278     9378  10089   8358   4308  -3112  -1681       N  
ATOM   3488  N   TYR D 279     -37.799  27.554 -99.931  1.00 41.95           N  
ANISOU 3488  N   TYR D 279     5863   5428   4647   1233  -1633   -266       N  
ATOM   3489  CA  TYR D 279     -36.932  27.029 -98.889  1.00 38.08           C  
ANISOU 3489  CA  TYR D 279     5394   4820   4256    956  -1388   -276       C  
ATOM   3490  C   TYR D 279     -35.739  27.946 -98.675  1.00 38.56           C  
ANISOU 3490  C   TYR D 279     5761   4481   4409    941  -1375    -94       C  
ATOM   3491  O   TYR D 279     -35.234  28.568 -99.614  1.00 40.11           O  
ANISOU 3491  O   TYR D 279     6203   4468   4571    973  -1455    146       O  
ATOM   3492  CB  TYR D 279     -36.400  25.625 -99.235  1.00 36.38           C  
ANISOU 3492  CB  TYR D 279     5151   4696   3977    627  -1216   -247       C  
ATOM   3493  CG  TYR D 279     -37.459  24.611 -99.571  1.00 39.36           C  
ANISOU 3493  CG  TYR D 279     5238   5388   4328    537  -1227   -449       C  
ATOM   3494  CD1 TYR D 279     -37.864  24.408-100.887  1.00 41.36           C  
ANISOU 3494  CD1 TYR D 279     5465   5813   4437    595  -1396   -501       C  
ATOM   3495  CD2 TYR D 279     -38.061  23.858 -98.576  1.00 39.53           C  
ANISOU 3495  CD2 TYR D 279     4998   5561   4460    372  -1068   -591       C  
ATOM   3496  CE1 TYR D 279     -38.838  23.481-101.198  1.00 43.07           C  
ANISOU 3496  CE1 TYR D 279     5372   6320   4673    473  -1438   -766       C  
ATOM   3497  CE2 TYR D 279     -39.043  22.928 -98.879  1.00 40.68           C  
ANISOU 3497  CE2 TYR D 279     4844   5959   4655    205  -1063   -787       C  
ATOM   3498  CZ  TYR D 279     -39.428  22.747-100.188  1.00 43.52           C  
ANISOU 3498  CZ  TYR D 279     5151   6460   4923    248  -1265   -912       C  
ATOM   3499  OH  TYR D 279     -40.401  21.824-100.485  1.00 46.57           O  
ANISOU 3499  OH  TYR D 279     5198   7097   5399     44  -1289  -1182       O  
ATOM   3500  N   VAL D 280     -35.288  28.009 -97.426  1.00 36.58           N  
ANISOU 3500  N   VAL D 280     5479   4159   4261    871  -1268   -207       N  
ATOM   3501  CA  VAL D 280     -33.933  28.431 -97.110  1.00 36.54           C  
ANISOU 3501  CA  VAL D 280     5670   3860   4354    717  -1211   -102       C  
ATOM   3502  C   VAL D 280     -33.064  27.182 -97.111  1.00 34.54           C  
ANISOU 3502  C   VAL D 280     5375   3733   4017    440  -1018    -21       C  
ATOM   3503  O   VAL D 280     -33.434  26.154 -96.528  1.00 34.18           O  
ANISOU 3503  O   VAL D 280     5163   3915   3908    379   -907   -112       O  
ATOM   3504  CB  VAL D 280     -33.881  29.151 -95.753  1.00 38.71           C  
ANISOU 3504  CB  VAL D 280     5910   4051   4748    832  -1248   -341       C  
ATOM   3505  CG1 VAL D 280     -32.445  29.363 -95.306  1.00 38.71           C  
ANISOU 3505  CG1 VAL D 280     6020   3844   4846    619  -1197   -312       C  
ATOM   3506  CG2 VAL D 280     -34.620  30.482 -95.841  1.00 40.38           C  
ANISOU 3506  CG2 VAL D 280     6209   4028   5104   1158  -1465   -451       C  
ATOM   3507  N   PHE D 281     -31.922  27.252 -97.781  1.00 34.28           N  
ANISOU 3507  N   PHE D 281     5485   3547   3991    279   -966    162       N  
ATOM   3508  CA  PHE D 281     -31.095  26.075 -97.999  1.00 31.38           C  
ANISOU 3508  CA  PHE D 281     5072   3303   3546     95   -807    214       C  
ATOM   3509  C   PHE D 281     -29.878  26.095 -97.082  1.00 29.32           C  
ANISOU 3509  C   PHE D 281     4784   2981   3375    -13   -741    184       C  
ATOM   3510  O   PHE D 281     -29.167  27.100 -96.988  1.00 31.32           O  
ANISOU 3510  O   PHE D 281     5102   3045   3754    -76   -786    211       O  
ATOM   3511  CB  PHE D 281     -30.671  25.981 -99.461  1.00 30.15           C  
ANISOU 3511  CB  PHE D 281     5019   3169   3268     27   -772    390       C  
ATOM   3512  CG  PHE D 281     -31.809  25.688-100.401  1.00 31.72           C  
ANISOU 3512  CG  PHE D 281     5204   3539   3309    150   -866    364       C  
ATOM   3513  CD1 PHE D 281     -32.390  24.428-100.431  1.00 30.79           C  
ANISOU 3513  CD1 PHE D 281     4938   3614   3148    113   -833    184       C  
ATOM   3514  CD2 PHE D 281     -32.297  26.665-101.257  1.00 35.38           C  
ANISOU 3514  CD2 PHE D 281     5800   3961   3680    302  -1010    519       C  
ATOM   3515  CE1 PHE D 281     -33.439  24.141-101.309  1.00 33.91           C  
ANISOU 3515  CE1 PHE D 281     5261   4212   3413    199   -955     81       C  
ATOM   3516  CE2 PHE D 281     -33.344  26.381-102.133  1.00 37.47           C  
ANISOU 3516  CE2 PHE D 281     6011   4470   3755    458  -1146    460       C  
ATOM   3517  CZ  PHE D 281     -33.913  25.117-102.155  1.00 34.60           C  
ANISOU 3517  CZ  PHE D 281     5442   4351   3353    392  -1126    202       C  
ATOM   3518  N   ILE D 282     -29.646  24.975 -96.415  1.00 27.52           N  
ANISOU 3518  N   ILE D 282     4458   2903   3097    -35   -649    131       N  
ATOM   3519  CA  ILE D 282     -28.520  24.803 -95.512  1.00 28.01           C  
ANISOU 3519  CA  ILE D 282     4458   2999   3185    -69   -623     95       C  
ATOM   3520  C   ILE D 282     -27.828  23.508 -95.888  1.00 28.07           C  
ANISOU 3520  C   ILE D 282     4435   3083   3147   -104   -509    166       C  
ATOM   3521  O   ILE D 282     -28.485  22.471 -96.010  1.00 31.19           O  
ANISOU 3521  O   ILE D 282     4843   3504   3504    -82   -450    183       O  
ATOM   3522  CB  ILE D 282     -28.978  24.756 -94.043  1.00 27.19           C  
ANISOU 3522  CB  ILE D 282     4288   3028   3014     51   -657    -26       C  
ATOM   3523  CG1 ILE D 282     -29.598  26.091 -93.634  1.00 30.48           C  
ANISOU 3523  CG1 ILE D 282     4721   3369   3492    147   -786   -193       C  
ATOM   3524  CG2 ILE D 282     -27.823  24.367 -93.138  1.00 28.26           C  
ANISOU 3524  CG2 ILE D 282     4354   3285   3100     72   -663    -50       C  
ATOM   3525  CD1 ILE D 282     -28.676  27.279 -93.797  1.00 32.91           C  
ANISOU 3525  CD1 ILE D 282     5084   3438   3984     59   -894   -260       C  
ATOM   3526  N   ALA D 283     -26.511  23.559 -96.050  1.00 28.02           N  
ANISOU 3526  N   ALA D 283     4363   3103   3179   -160   -481    175       N  
ATOM   3527  CA  ALA D 283     -25.733  22.376 -96.373  1.00 26.76           C  
ANISOU 3527  CA  ALA D 283     4149   3025   2994   -116   -390    190       C  
ATOM   3528  C   ALA D 283     -24.905  21.918 -95.179  1.00 26.53           C  
ANISOU 3528  C   ALA D 283     4018   3102   2962      8   -439    156       C  
ATOM   3529  O   ALA D 283     -24.410  22.726 -94.386  1.00 25.66           O  
ANISOU 3529  O   ALA D 283     3811   3070   2869     -5   -537     76       O  
ATOM   3530  CB  ALA D 283     -24.808  22.627 -97.566  1.00 28.23           C  
ANISOU 3530  CB  ALA D 283     4271   3278   3178   -218   -297    212       C  
ATOM   3531  N   ALA D 284     -24.773  20.607 -95.061  1.00 26.09           N  
ANISOU 3531  N   ALA D 284     3992   3032   2887    150   -395    203       N  
ATOM   3532  CA  ALA D 284     -23.832  19.990 -94.145  1.00 27.16           C  
ANISOU 3532  CA  ALA D 284     4046   3280   2995    348   -456    219       C  
ATOM   3533  C   ALA D 284     -22.641  19.494 -94.945  1.00 29.43           C  
ANISOU 3533  C   ALA D 284     4192   3642   3347    430   -410    138       C  
ATOM   3534  O   ALA D 284     -22.780  19.109 -96.104  1.00 29.46           O  
ANISOU 3534  O   ALA D 284     4239   3569   3384    384   -301     95       O  
ATOM   3535  CB  ALA D 284     -24.476  18.824 -93.403  1.00 26.97           C  
ANISOU 3535  CB  ALA D 284     4187   3134   2925    493   -437    388       C  
ATOM   3536  N   SER D 285     -21.465  19.524 -94.335  1.00 32.16           N  
ANISOU 3536  N   SER D 285     4330   4204   3685    573   -502     71       N  
ATOM   3537  CA  SER D 285     -20.278  18.979 -94.973  1.00 33.54           C  
ANISOU 3537  CA  SER D 285     4296   4529   3917    715   -456    -42       C  
ATOM   3538  C   SER D 285     -19.497  18.195 -93.933  1.00 34.21           C  
ANISOU 3538  C   SER D 285     4292   4739   3967   1082   -614    -28       C  
ATOM   3539  O   SER D 285     -19.487  18.548 -92.751  1.00 33.49           O  
ANISOU 3539  O   SER D 285     4180   4777   3768   1147   -772     15       O  
ATOM   3540  CB  SER D 285     -19.395  20.076 -95.597  1.00 35.19           C  
ANISOU 3540  CB  SER D 285     4206   4987   4177    468   -390   -175       C  
ATOM   3541  OG  SER D 285     -20.058  20.717 -96.678  1.00 34.51           O  
ANISOU 3541  OG  SER D 285     4248   4781   4084    187   -240   -113       O  
ATOM   3542  N   PHE D 286     -18.864  17.114 -94.381  1.00 34.87           N  
ANISOU 3542  N   PHE D 286     4332   4800   4118   1370   -589    -79       N  
ATOM   3543  CA  PHE D 286     -18.030  16.300 -93.511  1.00 38.44           C  
ANISOU 3543  CA  PHE D 286     4700   5360   4545   1811   -765    -48       C  
ATOM   3544  C   PHE D 286     -16.946  15.642 -94.350  1.00 41.67           C  
ANISOU 3544  C   PHE D 286     4860   5908   5065   2078   -719   -269       C  
ATOM   3545  O   PHE D 286     -16.979  15.667 -95.583  1.00 41.14           O  
ANISOU 3545  O   PHE D 286     4746   5829   5056   1923   -524   -423       O  
ATOM   3546  CB  PHE D 286     -18.852  15.248 -92.753  1.00 41.26           C  
ANISOU 3546  CB  PHE D 286     5463   5338   4877   2028   -819    256       C  
ATOM   3547  CG  PHE D 286     -19.721  14.390 -93.639  1.00 39.52           C  
ANISOU 3547  CG  PHE D 286     5542   4645   4828   1946   -658    294       C  
ATOM   3548  CD1 PHE D 286     -19.205  13.258 -94.253  1.00 42.65           C  
ANISOU 3548  CD1 PHE D 286     5980   4824   5401   2260   -650    179       C  
ATOM   3549  CD2 PHE D 286     -21.053  14.707 -93.840  1.00 37.14           C  
ANISOU 3549  CD2 PHE D 286     5452   4132   4526   1581   -541    386       C  
ATOM   3550  CE1 PHE D 286     -19.996  12.464 -95.067  1.00 41.80           C  
ANISOU 3550  CE1 PHE D 286     6136   4267   5478   2170   -536    124       C  
ATOM   3551  CE2 PHE D 286     -21.855  13.916 -94.656  1.00 39.10           C  
ANISOU 3551  CE2 PHE D 286     5922   3988   4948   1481   -429    352       C  
ATOM   3552  CZ  PHE D 286     -21.323  12.792 -95.267  1.00 40.27           C  
ANISOU 3552  CZ  PHE D 286     6126   3891   5282   1756   -431    208       C  
ATOM   3553  N   GLN D 287     -15.974  15.057 -93.662  1.00 45.20           N  
ANISOU 3553  N   GLN D 287     5127   6546   5501   2528   -908   -298       N  
ATOM   3554  CA  GLN D 287     -14.843  14.405 -94.300  1.00 48.93           C  
ANISOU 3554  CA  GLN D 287     5292   7223   6075   2891   -898   -553       C  
ATOM   3555  C   GLN D 287     -14.930  12.906 -94.061  1.00 52.87           C  
ANISOU 3555  C   GLN D 287     6116   7290   6681   3426  -1007   -426       C  
ATOM   3556  O   GLN D 287     -15.034  12.462 -92.912  1.00 56.34           O  
ANISOU 3556  O   GLN D 287     6766   7593   7049   3706  -1213   -140       O  
ATOM   3557  CB  GLN D 287     -13.523  14.955 -93.758  1.00 54.42           C  
ANISOU 3557  CB  GLN D 287     5428   8532   6717   3034  -1064   -751       C  
ATOM   3558  CG  GLN D 287     -12.310  14.627 -94.613  1.00 59.87           C  
ANISOU 3558  CG  GLN D 287     5633   9611   7505   3281   -976  -1096       C  
ATOM   3559  CD  GLN D 287     -11.133  15.530 -94.314  1.00 63.35           C  
ANISOU 3559  CD  GLN D 287     5411  10730   7931   3163  -1055  -1343       C  
ATOM   3560  OE1 GLN D 287     -10.722  15.671 -93.163  1.00 67.19           O  
ANISOU 3560  OE1 GLN D 287     5832  11368   8331   3266  -1320  -1302       O  
ATOM   3561  NE2 GLN D 287     -10.590  16.156 -95.350  1.00 64.67           N  
ANISOU 3561  NE2 GLN D 287     5167  11248   8156   2811   -778  -1567       N  
ATOM   3562  N   ALA D 288     -14.897  12.137 -95.141  1.00 53.88           N  
ANISOU 3562  N   ALA D 288     6309   7194   6970   3568   -867   -634       N  
ATOM   3563  CA  ALA D 288     -14.753  10.691 -95.086  1.00 60.02           C  
ANISOU 3563  CA  ALA D 288     7351   7519   7934   4021   -953   -605       C  
ATOM   3564  C   ALA D 288     -13.371  10.309 -95.604  1.00 65.87           C  
ANISOU 3564  C   ALA D 288     7669   8641   8716   4341   -955   -959       C  
ATOM   3565  O   ALA D 288     -12.589  11.158 -96.040  1.00 65.82           O  
ANISOU 3565  O   ALA D 288     7147   9262   8599   4248   -873  -1225       O  
ATOM   3566  CB  ALA D 288     -15.859  10.005 -95.892  1.00 59.13           C  
ANISOU 3566  CB  ALA D 288     7672   6787   8007   3870   -809   -634       C  
ATOM   3567  N   SER D 289     -13.063   9.011 -95.539  1.00 72.53           N  
ANISOU 3567  N   SER D 289     8714   9103   9742   4694  -1034   -947       N  
ATOM   3568  CA  SER D 289     -11.855   8.516 -96.193  1.00 79.48           C  
ANISOU 3568  CA  SER D 289     9237  10286  10677   5030  -1017  -1325       C  
ATOM   3569  C   SER D 289     -11.915   8.775 -97.692  1.00 80.05           C  
ANISOU 3569  C   SER D 289     9124  10568  10724   4853   -752  -1740       C  
ATOM   3570  O   SER D 289     -10.894   9.075 -98.324  1.00 84.10           O  
ANISOU 3570  O   SER D 289     9147  11675  11133   4920   -647  -2065       O  
ATOM   3571  CB  SER D 289     -11.678   7.025 -95.910  1.00 85.92           C  
ANISOU 3571  CB  SER D 289    10364  10541  11739   5452  -1148  -1232       C  
ATOM   3572  OG  SER D 289     -12.088   6.706 -94.590  1.00 86.58           O  
ANISOU 3572  OG  SER D 289    10783  10274  11838   5502  -1327   -731       O  
ATOM   3573  N   ASP D 290     -13.109   8.640 -98.274  1.00 77.88           N  
ANISOU 3573  N   ASP D 290     9231   9843  10517   4603   -631  -1732       N  
ATOM   3574  CA  ASP D 290     -13.372   9.084 -99.639  1.00 79.31           C  
ANISOU 3574  CA  ASP D 290     9277  10287  10570   4358   -377  -2077       C  
ATOM   3575  C   ASP D 290     -12.887  10.510 -99.858  1.00 75.12           C  
ANISOU 3575  C   ASP D 290     8245  10523   9776   4082   -216  -2128       C  
ATOM   3576  O   ASP D 290     -12.241  10.813-100.868  1.00 76.49           O  
ANISOU 3576  O   ASP D 290     8046  11228   9788   4008      5  -2418       O  
ATOM   3577  CB  ASP D 290     -14.879   8.979 -99.907  1.00 78.89           C  
ANISOU 3577  CB  ASP D 290     9715   9671  10589   4053   -334  -1981       C  
ATOM   3578  CG  ASP D 290     -15.258   9.219-101.359  1.00 83.32           C  
ANISOU 3578  CG  ASP D 290    10219  10456  10981   3831   -108  -2350       C  
ATOM   3579  OD1 ASP D 290     -14.594  10.012-102.059  1.00 85.54           O  
ANISOU 3579  OD1 ASP D 290    10077  11434  10991   3742     86  -2532       O  
ATOM   3580  OD2 ASP D 290     -16.259   8.614-101.796  1.00 85.23           O  
ANISOU 3580  OD2 ASP D 290    10838  10198  11346   3694   -118  -2432       O  
ATOM   3581  N   GLY D 291     -13.182  11.391 -98.922  1.00 69.78           N  
ANISOU 3581  N   GLY D 291     7543   9917   9053   3891   -309  -1831       N  
ATOM   3582  CA  GLY D 291     -12.951  12.807 -99.054  1.00 65.94           C  
ANISOU 3582  CA  GLY D 291     6701   9974   8380   3376   -154  -1764       C  
ATOM   3583  C   GLY D 291     -14.124  13.556 -98.474  1.00 57.24           C  
ANISOU 3583  C   GLY D 291     5976   8534   7238   2884   -202  -1384       C  
ATOM   3584  O   GLY D 291     -14.853  13.031 -97.636  1.00 55.95           O  
ANISOU 3584  O   GLY D 291     6217   7877   7165   2998   -383  -1145       O  
ATOM   3585  N   ILE D 292     -14.316  14.781 -98.947  1.00 52.61           N  
ANISOU 3585  N   ILE D 292     5259   8215   6517   2346    -20  -1317       N  
ATOM   3586  CA  ILE D 292     -15.363  15.650 -98.422  1.00 48.44           C  
ANISOU 3586  CA  ILE D 292     5025   7425   5956   1910    -70  -1011       C  
ATOM   3587  C   ILE D 292     -16.675  15.368 -99.142  1.00 44.18           C  
ANISOU 3587  C   ILE D 292     4925   6482   5379   1746     19   -948       C  
ATOM   3588  O   ILE D 292     -16.716  15.276-100.374  1.00 43.60           O  
ANISOU 3588  O   ILE D 292     4823   6547   5195   1691    207  -1123       O  
ATOM   3589  CB  ILE D 292     -14.958  17.124 -98.562  1.00 50.64           C  
ANISOU 3589  CB  ILE D 292     4987   8081   6171   1434     48   -964       C  
ATOM   3590  CG1 ILE D 292     -13.730  17.409 -97.696  1.00 55.65           C  
ANISOU 3590  CG1 ILE D 292     5147   9113   6884   1553    -97  -1080       C  
ATOM   3591  CG2 ILE D 292     -16.109  18.037 -98.180  1.00 46.51           C  
ANISOU 3591  CG2 ILE D 292     4795   7246   5631   1038      1   -706       C  
ATOM   3592  CD1 ILE D 292     -13.319  18.847 -97.685  1.00 57.12           C  
ANISOU 3592  CD1 ILE D 292     5021   9576   7105   1030    -12  -1061       C  
ATOM   3593  N   HIS D 293     -17.747  15.218 -98.371  1.00 40.42           N  
ANISOU 3593  N   HIS D 293     4821   5573   4964   1676   -116   -720       N  
ATOM   3594  CA  HIS D 293     -19.098  15.068 -98.890  1.00 37.82           C  
ANISOU 3594  CA  HIS D 293     4846   4897   4625   1462    -66   -663       C  
ATOM   3595  C   HIS D 293     -19.983  16.145 -98.283  1.00 34.63           C  
ANISOU 3595  C   HIS D 293     4560   4434   4162   1105   -107   -410       C  
ATOM   3596  O   HIS D 293     -19.720  16.627 -97.175  1.00 32.70           O  
ANISOU 3596  O   HIS D 293     4241   4263   3922   1106   -222   -275       O  
ATOM   3597  CB  HIS D 293     -19.690  13.694 -98.559  1.00 36.27           C  
ANISOU 3597  CB  HIS D 293     4975   4187   4620   1708   -164   -655       C  
ATOM   3598  CG  HIS D 293     -18.878  12.545 -99.064  1.00 44.25           C  
ANISOU 3598  CG  HIS D 293     5925   5133   5753   2139   -168   -942       C  
ATOM   3599  ND1 HIS D 293     -19.174  11.882-100.236  1.00 47.33           N  
ANISOU 3599  ND1 HIS D 293     6409   5399   6175   2188    -86  -1268       N  
ATOM   3600  CD2 HIS D 293     -17.782  11.936 -98.553  1.00 44.15           C  
ANISOU 3600  CD2 HIS D 293     5759   5180   5836   2592   -271   -999       C  
ATOM   3601  CE1 HIS D 293     -18.293  10.915-100.426  1.00 52.46           C  
ANISOU 3601  CE1 HIS D 293     6976   5997   6957   2655   -121  -1535       C  
ATOM   3602  NE2 HIS D 293     -17.437  10.927 -99.420  1.00 48.00           N  
ANISOU 3602  NE2 HIS D 293     6258   5539   6441   2922   -235  -1358       N  
ATOM   3603  N   SER D 294     -21.042  16.509 -99.005  1.00 31.13           N  
ANISOU 3603  N   SER D 294     4289   3889   3651    847    -38   -389       N  
ATOM   3604  CA  SER D 294     -22.026  17.453 -98.498  1.00 30.22           C  
ANISOU 3604  CA  SER D 294     4296   3686   3500    578    -89   -194       C  
ATOM   3605  C   SER D 294     -23.431  16.875 -98.625  1.00 30.86           C  
ANISOU 3605  C   SER D 294     4635   3461   3628    507   -112   -174       C  
ATOM   3606  O   SER D 294     -23.684  15.943 -99.394  1.00 34.70           O  
ANISOU 3606  O   SER D 294     5208   3812   4164    579    -82   -348       O  
ATOM   3607  CB  SER D 294     -21.949  18.809 -99.225  1.00 30.99           C  
ANISOU 3607  CB  SER D 294     4290   4010   3474    309     -5   -152       C  
ATOM   3608  OG  SER D 294     -20.724  19.477 -98.959  1.00 30.88           O  
ANISOU 3608  OG  SER D 294     4000   4253   3481    264     24   -158       O  
ATOM   3609  N   ILE D 295     -24.343  17.435 -97.834  1.00 29.26           N  
ANISOU 3609  N   ILE D 295     4520   3174   3424    362   -170    -10       N  
ATOM   3610  CA  ILE D 295     -25.769  17.139 -97.903  1.00 29.06           C  
ANISOU 3610  CA  ILE D 295     4645   2956   3441    226   -178      7       C  
ATOM   3611  C   ILE D 295     -26.503  18.470 -97.891  1.00 27.34           C  
ANISOU 3611  C   ILE D 295     4399   2871   3118     59   -212     72       C  
ATOM   3612  O   ILE D 295     -26.205  19.331 -97.057  1.00 26.73           O  
ANISOU 3612  O   ILE D 295     4266   2882   3010     56   -254    163       O  
ATOM   3613  CB  ILE D 295     -26.237  16.259 -96.727  1.00 31.38           C  
ANISOU 3613  CB  ILE D 295     5059   3007   3856    271   -188    169       C  
ATOM   3614  CG1 ILE D 295     -25.384  14.990 -96.599  1.00 33.14           C  
ANISOU 3614  CG1 ILE D 295     5357   3015   4219    513   -189    162       C  
ATOM   3615  CG2 ILE D 295     -27.707  15.910 -96.872  1.00 30.77           C  
ANISOU 3615  CG2 ILE D 295     5058   2768   3864     61   -158    159       C  
ATOM   3616  CD1 ILE D 295     -25.591  14.268 -95.275  1.00 35.63           C  
ANISOU 3616  CD1 ILE D 295     5824   3114   4600    599   -197    454       C  
ATOM   3617  N   ARG D 296     -27.434  18.656 -98.828  1.00 28.23           N  
ANISOU 3617  N   ARG D 296     4544   3003   3178    -44   -224    -10       N  
ATOM   3618  CA  ARG D 296     -28.215  19.884 -98.917  1.00 27.16           C  
ANISOU 3618  CA  ARG D 296     4402   2959   2959   -126   -289     51       C  
ATOM   3619  C   ARG D 296     -29.536  19.700 -98.186  1.00 27.56           C  
ANISOU 3619  C   ARG D 296     4444   2949   3078   -178   -324     54       C  
ATOM   3620  O   ARG D 296     -30.233  18.704 -98.400  1.00 29.02           O  
ANISOU 3620  O   ARG D 296     4628   3050   3348   -246   -303    -37       O  
ATOM   3621  CB  ARG D 296     -28.475  20.275-100.379  1.00 27.86           C  
ANISOU 3621  CB  ARG D 296     4513   3185   2888   -146   -310     -9       C  
ATOM   3622  CG  ARG D 296     -29.100  21.663-100.503  1.00 27.89           C  
ANISOU 3622  CG  ARG D 296     4549   3230   2817   -160   -402    116       C  
ATOM   3623  CD  ARG D 296     -29.378  22.045-101.944  1.00 29.87           C  
ANISOU 3623  CD  ARG D 296     4859   3649   2842   -130   -441    136       C  
ATOM   3624  NE  ARG D 296     -28.139  22.249-102.688  1.00 31.63           N  
ANISOU 3624  NE  ARG D 296     5098   3994   2926   -161   -306    236       N  
ATOM   3625  CZ  ARG D 296     -28.054  22.267-104.015  1.00 34.14           C  
ANISOU 3625  CZ  ARG D 296     5458   4555   2957   -123   -270    253       C  
ATOM   3626  NH1 ARG D 296     -29.144  22.102-104.760  1.00 36.60           N  
ANISOU 3626  NH1 ARG D 296     5810   5007   3090    -29   -412    149       N  
ATOM   3627  NH2 ARG D 296     -26.876  22.457-104.596  1.00 33.29           N  
ANISOU 3627  NH2 ARG D 296     5320   4619   2710   -176    -89    362       N  
ATOM   3628  N   TYR D 297     -29.872  20.653 -97.318  1.00 24.15           N  
ANISOU 3628  N   TYR D 297     3980   2570   2626   -159   -367    125       N  
ATOM   3629  CA  TYR D 297     -31.142  20.653 -96.613  1.00 25.28           C  
ANISOU 3629  CA  TYR D 297     4051   2766   2787   -187   -368    110       C  
ATOM   3630  C   TYR D 297     -31.939  21.887 -97.004  1.00 26.07           C  
ANISOU 3630  C   TYR D 297     4108   2962   2836   -124   -487     46       C  
ATOM   3631  O   TYR D 297     -31.378  22.912 -97.397  1.00 27.01           O  
ANISOU 3631  O   TYR D 297     4302   3034   2925    -63   -561     86       O  
ATOM   3632  CB  TYR D 297     -30.935  20.630 -95.078  1.00 24.93           C  
ANISOU 3632  CB  TYR D 297     3991   2771   2710   -135   -314    207       C  
ATOM   3633  CG  TYR D 297     -30.222  19.381 -94.619  1.00 26.93           C  
ANISOU 3633  CG  TYR D 297     4321   2910   3003   -132   -224    337       C  
ATOM   3634  CD1 TYR D 297     -30.917  18.194 -94.436  1.00 28.66           C  
ANISOU 3634  CD1 TYR D 297     4563   3006   3320   -249   -113    421       C  
ATOM   3635  CD2 TYR D 297     -28.851  19.378 -94.395  1.00 27.28           C  
ANISOU 3635  CD2 TYR D 297     4402   2945   3020    -10   -261    376       C  
ATOM   3636  CE1 TYR D 297     -30.267  17.038 -94.027  1.00 30.35           C  
ANISOU 3636  CE1 TYR D 297     4906   3016   3608   -206    -49    585       C  
ATOM   3637  CE2 TYR D 297     -28.194  18.227 -93.989  1.00 27.71           C  
ANISOU 3637  CE2 TYR D 297     4532   2883   3114     81   -217    501       C  
ATOM   3638  CZ  TYR D 297     -28.908  17.060 -93.808  1.00 28.89           C  
ANISOU 3638  CZ  TYR D 297     4775   2836   3366      1   -116    626       C  
ATOM   3639  OH  TYR D 297     -28.267  15.901 -93.409  1.00 31.73           O  
ANISOU 3639  OH  TYR D 297     5269   2983   3804    127    -88    794       O  
ATOM   3640  N   GLY D 298     -33.251  21.780 -96.879  1.00 27.79           N  
ANISOU 3640  N   GLY D 298     4190   3300   3067   -137   -502    -43       N  
ATOM   3641  CA  GLY D 298     -34.132  22.924 -97.059  1.00 29.99           C  
ANISOU 3641  CA  GLY D 298     4395   3689   3310     12   -640   -125       C  
ATOM   3642  C   GLY D 298     -35.120  23.049 -95.922  1.00 32.78           C  
ANISOU 3642  C   GLY D 298     4554   4232   3668     58   -587   -213       C  
ATOM   3643  O   GLY D 298     -35.605  22.048 -95.389  1.00 34.03           O  
ANISOU 3643  O   GLY D 298     4582   4493   3855   -102   -435   -203       O  
ATOM   3644  N   ILE D 299     -35.427  24.291 -95.556  1.00 32.95           N  
ANISOU 3644  N   ILE D 299     4558   4291   3671    280   -700   -301       N  
ATOM   3645  CA  ILE D 299     -36.439  24.587 -94.548  1.00 36.30           C  
ANISOU 3645  CA  ILE D 299     4755   4981   4056    402   -656   -458       C  
ATOM   3646  C   ILE D 299     -37.464  25.525 -95.168  1.00 38.55           C  
ANISOU 3646  C   ILE D 299     4921   5353   4374    658   -855   -622       C  
ATOM   3647  O   ILE D 299     -37.099  26.581 -95.697  1.00 38.99           O  
ANISOU 3647  O   ILE D 299     5176   5163   4476    850  -1042   -598       O  
ATOM   3648  CB  ILE D 299     -35.826  25.220 -93.285  1.00 37.21           C  
ANISOU 3648  CB  ILE D 299     4939   5098   4100    524   -628   -509       C  
ATOM   3649  CG1 ILE D 299     -34.682  24.359 -92.749  1.00 37.42           C  
ANISOU 3649  CG1 ILE D 299     5095   5056   4066    345   -496   -325       C  
ATOM   3650  CG2 ILE D 299     -36.896  25.441 -92.212  1.00 39.27           C  
ANISOU 3650  CG2 ILE D 299     4935   5740   4246    675   -540   -705       C  
ATOM   3651  CD1 ILE D 299     -33.370  25.092 -92.686  1.00 38.69           C  
ANISOU 3651  CD1 ILE D 299     5447   4987   4266    394   -616   -331       C  
ATOM   3652  N   ASN D 300     -38.742  25.150 -95.095  1.00 41.41           N  
ANISOU 3652  N   ASN D 300     4947   6058   4728    664   -815   -774       N  
ATOM   3653  CA  ASN D 300     -39.789  26.000 -95.638  1.00 44.59           C  
ANISOU 3653  CA  ASN D 300     5174   6616   5151    981  -1036   -962       C  
ATOM   3654  C   ASN D 300     -40.265  26.998 -94.582  1.00 48.55           C  
ANISOU 3654  C   ASN D 300     5549   7260   5640   1312  -1053  -1183       C  
ATOM   3655  O   ASN D 300     -39.762  27.044 -93.456  1.00 48.01           O  
ANISOU 3655  O   ASN D 300     5535   7201   5507   1278   -899  -1203       O  
ATOM   3656  CB  ASN D 300     -40.942  25.159 -96.197  1.00 46.69           C  
ANISOU 3656  CB  ASN D 300     5063   7242   5436    842  -1030  -1094       C  
ATOM   3657  CG  ASN D 300     -41.651  24.314 -95.140  1.00 47.15           C  
ANISOU 3657  CG  ASN D 300     4754   7657   5505    591   -734  -1180       C  
ATOM   3658  OD1 ASN D 300     -41.617  24.609 -93.947  1.00 46.47           O  
ANISOU 3658  OD1 ASN D 300     4621   7699   5337    670   -569  -1200       O  
ATOM   3659  ND2 ASN D 300     -42.322  23.261 -95.595  1.00 47.24           N  
ANISOU 3659  ND2 ASN D 300     4490   7852   5609    272   -663  -1241       N  
ATOM   3660  N   LYS D 301     -41.263  27.808 -94.952  1.00 47.99           N  
ANISOU 3660  N   LYS D 301     4744   8244   5245   1844   -718  -1276       N  
ATOM   3661  CA  LYS D 301     -41.758  28.852 -94.059  1.00 51.70           C  
ANISOU 3661  CA  LYS D 301     5198   8744   5701   1995   -717  -1378       C  
ATOM   3662  C   LYS D 301     -42.449  28.290 -92.823  1.00 52.95           C  
ANISOU 3662  C   LYS D 301     5101   9281   5736   1896   -568  -1598       C  
ATOM   3663  O   LYS D 301     -42.544  28.992 -91.809  1.00 53.34           O  
ANISOU 3663  O   LYS D 301     5189   9305   5774   2004   -555  -1666       O  
ATOM   3664  CB  LYS D 301     -42.707  29.776 -94.820  1.00 56.24           C  
ANISOU 3664  CB  LYS D 301     5695   9423   6252   2138   -791  -1437       C  
ATOM   3665  CG  LYS D 301     -42.087  30.394 -96.061  1.00 56.89           C  
ANISOU 3665  CG  LYS D 301     6010   9169   6437   2211   -877  -1225       C  
ATOM   3666  CD  LYS D 301     -43.126  31.143 -96.880  1.00 62.00           C  
ANISOU 3666  CD  LYS D 301     6542   9986   7029   2368   -949  -1296       C  
ATOM   3667  CE  LYS D 301     -44.070  30.187 -97.599  1.00 64.58           C  
ANISOU 3667  CE  LYS D 301     6602  10714   7221   2287   -941  -1444       C  
ATOM   3668  NZ  LYS D 301     -43.591  29.832 -98.967  1.00 63.48           N  
ANISOU 3668  NZ  LYS D 301     6573  10451   7095   2252   -984  -1294       N  
ATOM   3669  N   ASN D 302     -42.929  27.049 -92.880  1.00 53.38           N  
ANISOU 3669  N   ASN D 302     5025   9578   5681   1555   -406  -1670       N  
ATOM   3670  CA  ASN D 302     -43.499  26.383 -91.716  1.00 56.01           C  
ANISOU 3670  CA  ASN D 302     5295  10121   5866   1271   -171  -1800       C  
ATOM   3671  C   ASN D 302     -42.435  25.732 -90.837  1.00 52.81           C  
ANISOU 3671  C   ASN D 302     5277   9356   5434   1055    -70  -1612       C  
ATOM   3672  O   ASN D 302     -42.780  25.026 -89.883  1.00 54.24           O  
ANISOU 3672  O   ASN D 302     5487   9657   5465    781    143  -1667       O  
ATOM   3673  CB  ASN D 302     -44.526  25.336 -92.162  1.00 59.61           C  
ANISOU 3673  CB  ASN D 302     5487  10941   6219    931    -17  -1952       C  
ATOM   3674  CG  ASN D 302     -45.520  24.987 -91.069  1.00 65.26           C  
ANISOU 3674  CG  ASN D 302     6002  12009   6783    711    232  -2167       C  
ATOM   3675  OD1 ASN D 302     -45.609  25.673 -90.049  1.00 67.46           O  
ANISOU 3675  OD1 ASN D 302     6283  12332   7017    874    268  -2237       O  
ATOM   3676  ND2 ASN D 302     -46.274  23.912 -91.276  1.00 68.06           N  
ANISOU 3676  ND2 ASN D 302     6184  12619   7057    323    421  -2286       N  
ATOM   3677  N   GLY D 303     -41.157  25.947 -91.140  1.00 48.99           N  
ANISOU 3677  N   GLY D 303     5088   8441   5084   1175   -215  -1395       N  
ATOM   3678  CA  GLY D 303     -40.094  25.387 -90.334  1.00 46.54           C  
ANISOU 3678  CA  GLY D 303     5130   7796   4759   1024   -162  -1228       C  
ATOM   3679  C   GLY D 303     -39.898  23.897 -90.474  1.00 44.81           C  
ANISOU 3679  C   GLY D 303     5067   7488   4472    626    -11  -1120       C  
ATOM   3680  O   GLY D 303     -39.223  23.294 -89.639  1.00 44.36           O  
ANISOU 3680  O   GLY D 303     5291   7210   4353    480     62   -999       O  
ATOM   3681  N   GLU D 304     -40.467  23.279 -91.503  1.00 44.73           N  
ANISOU 3681  N   GLU D 304     4892   7636   4466    457     30  -1166       N  
ATOM   3682  CA  GLU D 304     -40.269  21.853 -91.705  1.00 44.56           C  
ANISOU 3682  CA  GLU D 304     5031   7495   4404     74    177  -1078       C  
ATOM   3683  C   GLU D 304     -38.959  21.609 -92.445  1.00 39.19           C  
ANISOU 3683  C   GLU D 304     4618   6395   3877    124     45   -866       C  
ATOM   3684  O   GLU D 304     -38.507  22.438 -93.239  1.00 35.29           O  
ANISOU 3684  O   GLU D 304     4091   5801   3516    398   -139   -823       O  
ATOM   3685  CB  GLU D 304     -41.451  21.249 -92.463  1.00 49.68           C  
ANISOU 3685  CB  GLU D 304     5375   8504   4995   -158    286  -1259       C  
ATOM   3686  CG  GLU D 304     -42.759  21.344 -91.680  1.00 55.40           C  
ANISOU 3686  CG  GLU D 304     5812   9663   5574   -262    459  -1491       C  
ATOM   3687  CD  GLU D 304     -43.972  20.916 -92.484  1.00 61.88           C  
ANISOU 3687  CD  GLU D 304     6257  10890   6365   -452    533  -1721       C  
ATOM   3688  OE1 GLU D 304     -43.881  20.845 -93.731  1.00 61.85           O  
ANISOU 3688  OE1 GLU D 304     6177  10878   6444   -401    392  -1718       O  
ATOM   3689  OE2 GLU D 304     -45.024  20.654 -91.863  1.00 66.51           O  
ANISOU 3689  OE2 GLU D 304     6614  11821   6838   -657    737  -1919       O  
ATOM   3690  N   LEU D 305     -38.336  20.470 -92.152  1.00 38.80           N  
ANISOU 3690  N   LEU D 305     4846   6088   3809   -136    151   -733       N  
ATOM   3691  CA  LEU D 305     -37.002  20.144 -92.639  1.00 35.00           C  
ANISOU 3691  CA  LEU D 305     4636   5191   3473    -96     47   -541       C  
ATOM   3692  C   LEU D 305     -37.078  19.133 -93.774  1.00 33.50           C  
ANISOU 3692  C   LEU D 305     4438   4969   3321   -333    108   -540       C  
ATOM   3693  O   LEU D 305     -37.895  18.208 -93.744  1.00 35.62           O  
ANISOU 3693  O   LEU D 305     4641   5407   3487   -647    287   -632       O  
ATOM   3694  CB  LEU D 305     -36.135  19.587 -91.506  1.00 35.78           C  
ANISOU 3694  CB  LEU D 305     5071   4992   3530   -168     90   -392       C  
ATOM   3695  CG  LEU D 305     -34.665  19.282 -91.799  1.00 36.69           C  
ANISOU 3695  CG  LEU D 305     5459   4675   3805    -92    -29   -211       C  
ATOM   3696  CD1 LEU D 305     -33.886  20.552 -92.125  1.00 35.18           C  
ANISOU 3696  CD1 LEU D 305     5222   4360   3786    257   -240   -188       C  
ATOM   3697  CD2 LEU D 305     -34.049  18.570 -90.601  1.00 40.20           C  
ANISOU 3697  CD2 LEU D 305     6220   4894   4158   -182     22    -86       C  
ATOM   3698  N   PHE D 306     -36.213  19.315 -94.770  1.00 30.13           N  
ANISOU 3698  N   PHE D 306     4081   4322   3045   -194    -28   -448       N  
ATOM   3699  CA  PHE D 306     -36.170  18.461 -95.947  1.00 32.22           C  
ANISOU 3699  CA  PHE D 306     4348   4546   3350   -376      8   -458       C  
ATOM   3700  C   PHE D 306     -34.722  18.224 -96.343  1.00 29.84           C  
ANISOU 3700  C   PHE D 306     4308   3823   3207   -299    -71   -286       C  
ATOM   3701  O   PHE D 306     -33.888  19.127 -96.240  1.00 30.91           O  
ANISOU 3701  O   PHE D 306     4506   3787   3453    -28   -207   -195       O  
ATOM   3702  CB  PHE D 306     -36.923  19.087 -97.138  1.00 29.99           C  
ANISOU 3702  CB  PHE D 306     3770   4572   3053   -254    -83   -588       C  
ATOM   3703  CG  PHE D 306     -38.376  19.383 -96.860  1.00 33.99           C  
ANISOU 3703  CG  PHE D 306     3959   5533   3424   -292    -30   -793       C  
ATOM   3704  CD1 PHE D 306     -39.367  18.509 -97.276  1.00 36.73           C  
ANISOU 3704  CD1 PHE D 306     4122   6152   3681   -593     95   -966       C  
ATOM   3705  CD2 PHE D 306     -38.750  20.539 -96.194  1.00 35.98           C  
ANISOU 3705  CD2 PHE D 306     4076   5944   3652    -29   -103   -838       C  
ATOM   3706  CE1 PHE D 306     -40.702  18.776 -97.023  1.00 39.57           C  
ANISOU 3706  CE1 PHE D 306     4147   6955   3932   -633    149  -1183       C  
ATOM   3707  CE2 PHE D 306     -40.082  20.809 -95.926  1.00 38.51           C  
ANISOU 3707  CE2 PHE D 306     4079   6696   3857    -48    -49  -1048       C  
ATOM   3708  CZ  PHE D 306     -41.059  19.927 -96.347  1.00 41.26           C  
ANISOU 3708  CZ  PHE D 306     4222   7334   4120   -351     77  -1223       C  
ATOM   3709  N   SER D 307     -34.424  17.012 -96.794  1.00 28.29           N  
ANISOU 3709  N   SER D 307     4255   3459   3036   -541     23   -261       N  
ATOM   3710  CA  SER D 307     -33.193  16.800 -97.533  1.00 27.15           C  
ANISOU 3710  CA  SER D 307     4281   2987   3050   -461    -48   -150       C  
ATOM   3711  C   SER D 307     -33.496  17.007 -99.014  1.00 27.98           C  
ANISOU 3711  C   SER D 307     4211   3259   3162   -431    -91   -233       C  
ATOM   3712  O   SER D 307     -34.627  16.807 -99.463  1.00 29.85           O  
ANISOU 3712  O   SER D 307     4244   3820   3280   -568    -40   -386       O  
ATOM   3713  CB  SER D 307     -32.615  15.406 -97.285  1.00 27.58           C  
ANISOU 3713  CB  SER D 307     4601   2740   3140   -696     64    -81       C  
ATOM   3714  OG  SER D 307     -33.506  14.385 -97.698  1.00 31.00           O  
ANISOU 3714  OG  SER D 307     4979   3314   3484  -1017    218   -201       O  
ATOM   3715  N   ILE D 308     -32.485  17.438 -99.762  1.00 26.58           N  
ANISOU 3715  N   ILE D 308     4109   2877   3115   -245   -185   -142       N  
ATOM   3716  CA  ILE D 308     -32.663  17.882-101.142  1.00 27.74           C  
ANISOU 3716  CA  ILE D 308     4123   3175   3243   -148   -244   -187       C  
ATOM   3717  C   ILE D 308     -31.824  16.999-102.052  1.00 28.28           C  
ANISOU 3717  C   ILE D 308     4341   3012   3393   -263   -192   -162       C  
ATOM   3718  O   ILE D 308     -30.630  16.804-101.808  1.00 30.07           O  
ANISOU 3718  O   ILE D 308     4758   2896   3773   -215   -192    -51       O  
ATOM   3719  CB  ILE D 308     -32.267  19.361-101.321  1.00 27.89           C  
ANISOU 3719  CB  ILE D 308     4095   3174   3327    192   -380    -99       C  
ATOM   3720  CG1 ILE D 308     -32.848  20.227-100.198  1.00 30.28           C  
ANISOU 3720  CG1 ILE D 308     4298   3616   3592    330   -431   -121       C  
ATOM   3721  CG2 ILE D 308     -32.688  19.868-102.710  1.00 28.69           C  
ANISOU 3721  CG2 ILE D 308     4065   3487   3347    306   -441   -136       C  
ATOM   3722  CD1 ILE D 308     -34.338  20.471-100.304  1.00 33.09           C  
ANISOU 3722  CD1 ILE D 308     4392   4404   3776    317   -435   -277       C  
ATOM   3723  N   ASN D 309     -32.442  16.480-103.107  1.00 27.53           N  
ANISOU 3723  N   ASN D 309     4146   3118   3197   -403   -154   -286       N  
ATOM   3724  CA  ASN D 309     -31.690  15.837-104.172  1.00 29.29           C  
ANISOU 3724  CA  ASN D 309     4485   3167   3477   -467   -115   -287       C  
ATOM   3725  C   ASN D 309     -31.126  16.935-105.065  1.00 30.21           C  
ANISOU 3725  C   ASN D 309     4582   3278   3617   -190   -210   -196       C  
ATOM   3726  O   ASN D 309     -31.891  17.681-105.680  1.00 33.00           O  
ANISOU 3726  O   ASN D 309     4774   3931   3834    -65   -289   -239       O  
ATOM   3727  CB  ASN D 309     -32.595  14.891-104.959  1.00 32.11           C  
ANISOU 3727  CB  ASN D 309     4741   3759   3702   -727    -43   -481       C  
ATOM   3728  CG  ASN D 309     -31.848  14.107-106.030  1.00 31.89           C  
ANISOU 3728  CG  ASN D 309     4844   3550   3724   -815     15   -514       C  
ATOM   3729  OD1 ASN D 309     -31.302  14.679-106.975  1.00 33.49           O  
ANISOU 3729  OD1 ASN D 309     5057   3747   3923   -635    -39   -464       O  
ATOM   3730  ND2 ASN D 309     -31.848  12.783-105.897  1.00 29.57           N  
ANISOU 3730  ND2 ASN D 309     4661   3106   3469  -1098    140   -605       N  
ATOM   3731  N   THR D 310     -29.799  17.049-105.138  1.00 27.38           N  
ANISOU 3731  N   THR D 310     4389   2584   3431    -90   -199    -73       N  
ATOM   3732  CA  THR D 310     -29.219  18.177-105.862  1.00 28.32           C  
ANISOU 3732  CA  THR D 310     4508   2666   3589    157   -258     31       C  
ATOM   3733  C   THR D 310     -29.221  18.004-107.379  1.00 27.82           C  
ANISOU 3733  C   THR D 310     4440   2717   3413    142   -226    -13       C  
ATOM   3734  O   THR D 310     -28.783  18.920-108.086  1.00 29.61           O  
ANISOU 3734  O   THR D 310     4692   2920   3639    334   -251     88       O  
ATOM   3735  CB  THR D 310     -27.794  18.453-105.373  1.00 26.69           C  
ANISOU 3735  CB  THR D 310     4268   2261   3611    224   -201    139       C  
ATOM   3736  OG1 THR D 310     -26.924  17.391-105.772  1.00 28.10           O  
ANISOU 3736  OG1 THR D 310     4395   2389   3894     96    -94    106       O  
ATOM   3737  CG2 THR D 310     -27.785  18.589-103.858  1.00 27.09           C  
ANISOU 3737  CG2 THR D 310     4216   2355   3724    218   -198    154       C  
ATOM   3738  N   ALA D 311     -29.701  16.877-107.907  1.00 26.55           N  
ANISOU 3738  N   ALA D 311     4262   2678   3148    -84   -163   -163       N  
ATOM   3739  CA  ALA D 311     -29.860  16.735-109.353  1.00 27.17           C  
ANISOU 3739  CA  ALA D 311     4322   2932   3071    -94   -149   -237       C  
ATOM   3740  C   ALA D 311     -31.264  17.108-109.812  1.00 30.75           C  
ANISOU 3740  C   ALA D 311     4574   3832   3277    -59   -253   -347       C  
ATOM   3741  O   ALA D 311     -31.429  17.853-110.784  1.00 34.36           O  
ANISOU 3741  O   ALA D 311     5004   4467   3583    124   -324   -307       O  
ATOM   3742  CB  ALA D 311     -29.533  15.301-109.790  1.00 28.07           C  
ANISOU 3742  CB  ALA D 311     4528   2923   3216   -350    -29   -374       C  
ATOM   3743  N   SER D 312     -32.283  16.597-109.123  1.00 29.33           N  
ANISOU 3743  N   SER D 312     4255   3842   3048   -229   -260   -487       N  
ATOM   3744  CA  SER D 312     -33.673  16.834-109.476  1.00 30.80           C  
ANISOU 3744  CA  SER D 312     4200   4483   3020   -220   -359   -640       C  
ATOM   3745  C   SER D 312     -34.301  17.990-108.710  1.00 31.41           C  
ANISOU 3745  C   SER D 312     4137   4719   3080      6   -471   -573       C  
ATOM   3746  O   SER D 312     -35.361  18.475-109.124  1.00 30.93           O  
ANISOU 3746  O   SER D 312     3866   5042   2843    116   -588   -676       O  
ATOM   3747  CB  SER D 312     -34.497  15.577-109.207  1.00 32.91           C  
ANISOU 3747  CB  SER D 312     4361   4893   3252   -571   -275   -872       C  
ATOM   3748  OG  SER D 312     -34.562  15.354-107.804  1.00 35.88           O  
ANISOU 3748  OG  SER D 312     4758   5119   3757   -682   -204   -833       O  
ATOM   3749  N   ASN D 313     -33.691  18.410-107.596  1.00 32.07           N  
ANISOU 3749  N   ASN D 313     4319   4526   3338     82   -445   -428       N  
ATOM   3750  CA  ASN D 313     -34.202  19.392-106.635  1.00 33.35           C  
ANISOU 3750  CA  ASN D 313     4370   4785   3517    264   -524   -386       C  
ATOM   3751  C   ASN D 313     -35.427  18.895-105.875  1.00 31.37           C  
ANISOU 3751  C   ASN D 313     3910   4823   3186     76   -496   -572       C  
ATOM   3752  O   ASN D 313     -36.045  19.676-105.137  1.00 32.32           O  
ANISOU 3752  O   ASN D 313     3893   5099   3288    223   -556   -584       O  
ATOM   3753  CB  ASN D 313     -34.514  20.741-107.297  1.00 37.70           C  
ANISOU 3753  CB  ASN D 313     4844   5509   3969    610   -673   -313       C  
ATOM   3754  CG  ASN D 313     -33.300  21.349-107.977  1.00 37.59           C  
ANISOU 3754  CG  ASN D 313     5050   5192   4040    785   -669   -111       C  
ATOM   3755  OD1 ASN D 313     -32.234  21.465-107.378  1.00 36.36           O  
ANISOU 3755  OD1 ASN D 313     5053   4677   4085    788   -606     12       O  
ATOM   3756  ND2 ASN D 313     -33.456  21.731-109.238  1.00 39.65           N  
ANISOU 3756  ND2 ASN D 313     5317   5608   4140    927   -732    -84       N  
ATOM   3757  N   LYS D 314     -35.794  17.622-106.021  1.00 27.97           N  
ANISOU 3757  N   LYS D 314     3452   4462   2715   -254   -389   -729       N  
ATOM   3758  CA  LYS D 314     -36.903  17.067-105.259  1.00 29.05           C  
ANISOU 3758  CA  LYS D 314     3402   4842   2794   -488   -315   -908       C  
ATOM   3759  C   LYS D 314     -36.553  17.016-103.773  1.00 31.25           C  
ANISOU 3759  C   LYS D 314     3808   4880   3186   -541   -224   -802       C  
ATOM   3760  O   LYS D 314     -35.399  16.795-103.392  1.00 28.90           O  
ANISOU 3760  O   LYS D 314     3771   4184   3024   -534   -181   -638       O  
ATOM   3761  CB  LYS D 314     -37.255  15.665-105.753  1.00 30.37           C  
ANISOU 3761  CB  LYS D 314     3552   5067   2921   -863   -195  -1095       C  
ATOM   3762  CG  LYS D 314     -37.801  15.597-107.180  1.00 34.87           C  
ANISOU 3762  CG  LYS D 314     3958   5955   3338   -849   -290  -1263       C  
ATOM   3763  CD  LYS D 314     -38.197  14.179-107.513  1.00 39.33           C  
ANISOU 3763  CD  LYS D 314     4496   6564   3884  -1256   -157  -1486       C  
ATOM   3764  CE  LYS D 314     -38.681  14.055-108.960  1.00 43.67           C  
ANISOU 3764  CE  LYS D 314     4891   7437   4266  -1249   -264  -1680       C  
ATOM   3765  NZ  LYS D 314     -38.882  12.632-109.332  1.00 49.20           N  
ANISOU 3765  NZ  LYS D 314     5609   8095   4990  -1642   -119  -1886       N  
ATOM   3766  N   VAL D 315     -37.566  17.218-102.932  1.00 33.75           N  
ANISOU 3766  N   VAL D 315     3929   5460   3435   -588   -196   -911       N  
ATOM   3767  CA  VAL D 315     -37.371  17.321-101.490  1.00 34.27           C  
ANISOU 3767  CA  VAL D 315     4099   5366   3558   -604   -120   -821       C  
ATOM   3768  C   VAL D 315     -37.924  16.076-100.815  1.00 36.22           C  
ANISOU 3768  C   VAL D 315     4361   5635   3765  -1006     82   -929       C  
ATOM   3769  O   VAL D 315     -38.834  15.412-101.327  1.00 38.57           O  
ANISOU 3769  O   VAL D 315     4472   6197   3984  -1251    153  -1132       O  
ATOM   3770  CB  VAL D 315     -38.023  18.594-100.906  1.00 35.06           C  
ANISOU 3770  CB  VAL D 315     3997   5715   3608   -330   -218   -850       C  
ATOM   3771  CG1 VAL D 315     -37.673  19.802-101.758  1.00 35.90           C  
ANISOU 3771  CG1 VAL D 315     4077   5825   3738     50   -409   -762       C  
ATOM   3772  CG2 VAL D 315     -39.532  18.430-100.791  1.00 36.78           C  
ANISOU 3772  CG2 VAL D 315     3878   6403   3693   -476   -165  -1098       C  
ATOM   3773  N   THR D 316     -37.359  15.763 -99.647  1.00 33.80           N  
ANISOU 3773  N   THR D 316     4288   5045   3510  -1075    176   -794       N  
ATOM   3774  CA  THR D 316     -37.719  14.572 -98.887  1.00 35.26           C  
ANISOU 3774  CA  THR D 316     4578   5162   3655  -1449    390   -836       C  
ATOM   3775  C   THR D 316     -37.913  15.012 -97.446  1.00 34.77           C  
ANISOU 3775  C   THR D 316     4552   5126   3533  -1395    444   -773       C  
ATOM   3776  O   THR D 316     -36.950  15.495 -96.815  1.00 32.07           O  
ANISOU 3776  O   THR D 316     4419   4515   3251  -1174    359   -592       O  
ATOM   3777  CB  THR D 316     -36.638  13.489 -98.984  1.00 34.51           C  
ANISOU 3777  CB  THR D 316     4832   4613   3666  -1598    460   -702       C  
ATOM   3778  OG1 THR D 316     -36.539  13.019-100.333  1.00 37.70           O  
ANISOU 3778  OG1 THR D 316     5192   5021   4109  -1673    433   -796       O  
ATOM   3779  CG2 THR D 316     -36.974  12.316 -98.074  1.00 35.25           C  
ANISOU 3779  CG2 THR D 316     5095   4584   3715  -1960    687   -703       C  
ATOM   3780  N   PRO D 317     -39.110  14.877 -96.881  1.00 38.64           N  
ANISOU 3780  N   PRO D 317     4836   5941   3903  -1590    585   -933       N  
ATOM   3781  CA  PRO D 317     -39.337  15.376 -95.523  1.00 37.89           C  
ANISOU 3781  CA  PRO D 317     4764   5910   3724  -1520    643   -892       C  
ATOM   3782  C   PRO D 317     -38.520  14.608 -94.498  1.00 38.49           C  
ANISOU 3782  C   PRO D 317     5242   5591   3790  -1650    757   -690       C  
ATOM   3783  O   PRO D 317     -38.277  13.404 -94.630  1.00 38.49           O  
ANISOU 3783  O   PRO D 317     5454   5355   3814  -1933    889   -642       O  
ATOM   3784  CB  PRO D 317     -40.840  15.164 -95.309  1.00 41.55           C  
ANISOU 3784  CB  PRO D 317     4902   6819   4066  -1774    815  -1138       C  
ATOM   3785  CG  PRO D 317     -41.214  14.080 -96.269  1.00 44.10           C  
ANISOU 3785  CG  PRO D 317     5162   7175   4418  -2106    911  -1268       C  
ATOM   3786  CD  PRO D 317     -40.315  14.258 -97.462  1.00 41.26           C  
ANISOU 3786  CD  PRO D 317     4889   6615   4171  -1893    704  -1184       C  
ATOM   3787  N   ILE D 318     -38.085  15.333 -93.470  1.00 37.21           N  
ANISOU 3787  N   ILE D 318     5194   5353   3590  -1422    692   -577       N  
ATOM   3788  CA  ILE D 318     -37.371  14.766 -92.335  1.00 38.11           C  
ANISOU 3788  CA  ILE D 318     5682   5149   3650  -1485    767   -389       C  
ATOM   3789  C   ILE D 318     -38.146  15.155 -91.086  1.00 40.39           C  
ANISOU 3789  C   ILE D 318     5904   5690   3752  -1513    890   -446       C  
ATOM   3790  O   ILE D 318     -38.236  16.343 -90.749  1.00 38.78           O  
ANISOU 3790  O   ILE D 318     5542   5660   3532  -1224    763   -500       O  
ATOM   3791  CB  ILE D 318     -35.921  15.257 -92.251  1.00 34.82           C  
ANISOU 3791  CB  ILE D 318     5492   4379   3359  -1161    547   -206       C  
ATOM   3792  CG1 ILE D 318     -35.122  14.817 -93.477  1.00 32.47           C  
ANISOU 3792  CG1 ILE D 318     5263   3833   3243  -1147    458   -157       C  
ATOM   3793  CG2 ILE D 318     -35.269  14.727 -90.989  1.00 36.76           C  
ANISOU 3793  CG2 ILE D 318     6101   4351   3514  -1190    596    -30       C  
ATOM   3794  CD1 ILE D 318     -33.789  15.522 -93.604  1.00 29.89           C  
ANISOU 3794  CD1 ILE D 318     5051   3234   3071   -812    239    -30       C  
ATOM   3795  N   ASP D 319     -38.718  14.166 -90.408  1.00 44.87           N  
ANISOU 3795  N   ASP D 319     6598   6274   4178  -1866   1151   -443       N  
ATOM   3796  CA  ASP D 319     -39.399  14.429 -89.150  1.00 47.85           C  
ANISOU 3796  CA  ASP D 319     6957   6875   4348  -1922   1308   -483       C  
ATOM   3797  C   ASP D 319     -38.386  14.805 -88.076  1.00 44.85           C  
ANISOU 3797  C   ASP D 319     6903   6242   3896  -1667   1188   -285       C  
ATOM   3798  O   ASP D 319     -37.254  14.315 -88.061  1.00 41.91           O  
ANISOU 3798  O   ASP D 319     6862   5470   3593  -1601   1086    -86       O  
ATOM   3799  CB  ASP D 319     -40.199  13.204 -88.711  1.00 56.25           C  
ANISOU 3799  CB  ASP D 319     8118   7979   5275  -2397   1650   -506       C  
ATOM   3800  CG  ASP D 319     -39.344  11.957 -88.633  1.00 61.69           C  
ANISOU 3800  CG  ASP D 319     9265   8187   5988  -2579   1716   -276       C  
ATOM   3801  OD1 ASP D 319     -38.834  11.526 -89.688  1.00 63.94           O  
ANISOU 3801  OD1 ASP D 319     9577   8261   6455  -2587   1615   -260       O  
ATOM   3802  OD2 ASP D 319     -39.169  11.414 -87.524  1.00 66.50           O  
ANISOU 3802  OD2 ASP D 319    10198   8615   6454  -2661   1835   -119       O  
ATOM   3803  N   ILE D 320     -38.805  15.683 -87.166  1.00 42.39           N  
ANISOU 3803  N   ILE D 320     6481   6181   3444  -1515   1195   -363       N  
ATOM   3804  CA  ILE D 320     -37.925  16.198 -86.127  1.00 41.48           C  
ANISOU 3804  CA  ILE D 320     6625   5891   3244  -1248   1057   -227       C  
ATOM   3805  C   ILE D 320     -37.872  15.198 -84.978  1.00 44.00           C  
ANISOU 3805  C   ILE D 320     7329   6065   3322  -1485   1267    -65       C  
ATOM   3806  O   ILE D 320     -38.913  14.766 -84.467  1.00 46.08           O  
ANISOU 3806  O   ILE D 320     7543   6567   3399  -1778   1555   -140       O  
ATOM   3807  CB  ILE D 320     -38.401  17.578 -85.639  1.00 42.72           C  
ANISOU 3807  CB  ILE D 320     6513   6372   3347   -977    976   -401       C  
ATOM   3808  CG1 ILE D 320     -38.450  18.566 -86.810  1.00 41.36           C  
ANISOU 3808  CG1 ILE D 320     6001   6307   3410   -726    768   -533       C  
ATOM   3809  CG2 ILE D 320     -37.495  18.093 -84.529  1.00 42.59           C  
ANISOU 3809  CG2 ILE D 320     6763   6186   3234   -717    831   -293       C  
ATOM   3810  CD1 ILE D 320     -37.198  18.577 -87.666  1.00 39.14           C  
ANISOU 3810  CD1 ILE D 320     5864   5652   3356   -556    537   -386       C  
ATOM   3811  N   LEU D 321     -36.658  14.829 -84.572  1.00 41.81           N  
ANISOU 3811  N   LEU D 321     7441   5402   3045  -1354   1126    159       N  
ATOM   3812  CA  LEU D 321     -36.481  13.926 -83.450  1.00 44.98           C  
ANISOU 3812  CA  LEU D 321     8267   5630   3196  -1513   1283    351       C  
ATOM   3813  C   LEU D 321     -36.857  14.634 -82.147  1.00 47.36           C  
ANISOU 3813  C   LEU D 321     8585   6190   3221  -1403   1334    299       C  
ATOM   3814  O   LEU D 321     -36.907  15.866 -82.095  1.00 47.44           O  
ANISOU 3814  O   LEU D 321     8330   6415   3281  -1126   1173    139       O  
ATOM   3815  CB  LEU D 321     -35.040  13.423 -83.410  1.00 45.90           C  
ANISOU 3815  CB  LEU D 321     8754   5281   3404  -1334   1065    581       C  
ATOM   3816  CG  LEU D 321     -34.690  12.526 -84.606  1.00 47.36           C  
ANISOU 3816  CG  LEU D 321     8938   5194   3862  -1463   1049    619       C  
ATOM   3817  CD1 LEU D 321     -33.209  12.183 -84.632  1.00 46.98           C  
ANISOU 3817  CD1 LEU D 321     9078   4758   4014  -1184    774    748       C  
ATOM   3818  CD2 LEU D 321     -35.528  11.262 -84.550  1.00 51.50           C  
ANISOU 3818  CD2 LEU D 321     9482   5708   4376  -1823   1313    602       C  
ATOM   3819  N   PRO D 322     -37.139  13.874 -81.082  1.00 49.23           N  
ANISOU 3819  N   PRO D 322     9028   6390   3288  -1553   1502    408       N  
ATOM   3820  CA  PRO D 322     -37.657  14.498 -79.850  1.00 52.93           C  
ANISOU 3820  CA  PRO D 322     9459   7149   3504  -1472   1582    335       C  
ATOM   3821  C   PRO D 322     -36.806  15.628 -79.293  1.00 51.32           C  
ANISOU 3821  C   PRO D 322     9328   6955   3217  -1070   1303    316       C  
ATOM   3822  O   PRO D 322     -37.356  16.520 -78.638  1.00 52.79           O  
ANISOU 3822  O   PRO D 322     9349   7465   3244   -963   1344    149       O  
ATOM   3823  CB  PRO D 322     -37.727  13.319 -78.871  1.00 56.25           C  
ANISOU 3823  CB  PRO D 322    10184   7396   3793  -1651   1742    526       C  
ATOM   3824  CG  PRO D 322     -37.939  12.135 -79.736  1.00 53.20           C  
ANISOU 3824  CG  PRO D 322     9822   6792   3600  -1947   1867    576       C  
ATOM   3825  CD  PRO D 322     -37.158  12.402 -80.994  1.00 51.93           C  
ANISOU 3825  CD  PRO D 322     9594   6454   3684  -1810   1643    563       C  
ATOM   3826  N   LEU D 323     -35.496  15.639 -79.536  1.00 49.00           N  
ANISOU 3826  N   LEU D 323     9242   6320   3057   -833   1012    450       N  
ATOM   3827  CA  LEU D 323     -34.631  16.639 -78.922  1.00 49.42           C  
ANISOU 3827  CA  LEU D 323     9353   6353   3072   -452    723    416       C  
ATOM   3828  C   LEU D 323     -34.397  17.865 -79.799  1.00 46.05           C  
ANISOU 3828  C   LEU D 323     8589   5990   2918   -198    498    225       C  
ATOM   3829  O   LEU D 323     -33.642  18.754 -79.395  1.00 45.74           O  
ANISOU 3829  O   LEU D 323     8550   5907   2921    118    242    167       O  
ATOM   3830  CB  LEU D 323     -33.283  16.021 -78.533  1.00 49.48           C  
ANISOU 3830  CB  LEU D 323     9659   5972   3170   -291    492    625       C  
ATOM   3831  CG  LEU D 323     -33.265  15.169 -77.262  1.00 52.19           C  
ANISOU 3831  CG  LEU D 323    10270   6266   3294   -369    593    778       C  
ATOM   3832  CD1 LEU D 323     -31.860  14.673 -76.954  1.00 53.47           C  
ANISOU 3832  CD1 LEU D 323    10662   6076   3576   -155    328    924       C  
ATOM   3833  CD2 LEU D 323     -33.832  15.936 -76.073  1.00 52.51           C  
ANISOU 3833  CD2 LEU D 323    10264   6648   3038   -296    659    666       C  
ATOM   3834  N   GLY D 324     -35.002  17.941 -80.977  1.00 44.20           N  
ANISOU 3834  N   GLY D 324     8033   5850   2911   -316    570    121       N  
ATOM   3835  CA  GLY D 324     -35.048  19.184 -81.722  1.00 42.15           C  
ANISOU 3835  CA  GLY D 324     7399   5712   2903    -77    397    -71       C  
ATOM   3836  C   GLY D 324     -34.376  19.090 -83.077  1.00 39.03           C  
ANISOU 3836  C   GLY D 324     6918   5067   2843    -25    240    -16       C  
ATOM   3837  O   GLY D 324     -33.954  18.020 -83.530  1.00 38.83           O  
ANISOU 3837  O   GLY D 324     7084   4794   2874   -191    277    144       O  
ATOM   3838  N   VAL D 325     -34.278  20.250 -83.733  1.00 34.69           N  
ANISOU 3838  N   VAL D 325     5588   4239   3355   -572    211     55       N  
ATOM   3839  CA  VAL D 325     -33.821  20.288 -85.122  1.00 36.04           C  
ANISOU 3839  CA  VAL D 325     5613   4349   3731   -632     13     46       C  
ATOM   3840  C   VAL D 325     -32.334  19.964 -85.208  1.00 34.81           C  
ANISOU 3840  C   VAL D 325     5582   4193   3453   -544   -192     43       C  
ATOM   3841  O   VAL D 325     -31.902  19.198 -86.080  1.00 32.83           O  
ANISOU 3841  O   VAL D 325     5332   3880   3263   -571   -273    107       O  
ATOM   3842  CB  VAL D 325     -34.151  21.652 -85.763  1.00 36.80           C  
ANISOU 3842  CB  VAL D 325     5495   4456   4030   -619    -42    -63       C  
ATOM   3843  CG1 VAL D 325     -33.404  21.828 -87.085  1.00 34.43           C  
ANISOU 3843  CG1 VAL D 325     5104   4117   3860   -652   -245    -57       C  
ATOM   3844  CG2 VAL D 325     -35.647  21.779 -86.004  1.00 38.20           C  
ANISOU 3844  CG2 VAL D 325     5467   4666   4381   -676    125    -29       C  
ATOM   3845  N   MET D 326     -31.528  20.524 -84.301  1.00 32.99           N  
ANISOU 3845  N   MET D 326     5442   4052   3040   -430   -283    -50       N  
ATOM   3846  CA  MET D 326     -30.097  20.233 -84.326  1.00 34.98           C  
ANISOU 3846  CA  MET D 326     5734   4368   3188   -335   -496    -56       C  
ATOM   3847  C   MET D 326     -29.823  18.775 -83.973  1.00 34.43           C  
ANISOU 3847  C   MET D 326     5872   4264   2947   -231   -468    118       C  
ATOM   3848  O   MET D 326     -28.922  18.154 -84.545  1.00 34.11           O  
ANISOU 3848  O   MET D 326     5821   4214   2926   -148   -591    168       O  
ATOM   3849  CB  MET D 326     -29.343  21.163 -83.375  1.00 39.63           C  
ANISOU 3849  CB  MET D 326     6348   5093   3616   -268   -638   -224       C  
ATOM   3850  CG  MET D 326     -28.748  22.408 -84.031  1.00 40.84           C  
ANISOU 3850  CG  MET D 326     6301   5242   3975   -366   -778   -385       C  
ATOM   3851  SD  MET D 326     -28.035  22.203 -85.689  1.00 40.54           S  
ANISOU 3851  SD  MET D 326     6046   5171   4187   -433   -863   -296       S  
ATOM   3852  CE  MET D 326     -26.685  21.067 -85.393  1.00 40.83           C  
ANISOU 3852  CE  MET D 326     6103   5370   4040   -264  -1023   -225       C  
ATOM   3853  N   ALA D 327     -30.579  18.211 -83.028  1.00 34.24           N  
ANISOU 3853  N   ALA D 327     6052   4208   2750   -217   -281    224       N  
ATOM   3854  CA  ALA D 327     -30.424  16.788 -82.738  1.00 34.50           C  
ANISOU 3854  CA  ALA D 327     6336   4127   2644   -129   -216    433       C  
ATOM   3855  C   ALA D 327     -30.790  15.941 -83.950  1.00 32.73           C  
ANISOU 3855  C   ALA D 327     6079   3689   2666   -261   -154    500       C  
ATOM   3856  O   ALA D 327     -30.198  14.879 -84.177  1.00 35.99           O  
ANISOU 3856  O   ALA D 327     6664   3968   3043   -150   -190    610       O  
ATOM   3857  CB  ALA D 327     -31.280  16.390 -81.540  1.00 36.25           C  
ANISOU 3857  CB  ALA D 327     6795   4335   2643   -135     32    566       C  
ATOM   3858  N   THR D 328     -31.773  16.392 -84.730  1.00 31.11           N  
ANISOU 3858  N   THR D 328     5667   3452   2700   -475    -71    424       N  
ATOM   3859  CA  THR D 328     -32.190  15.674 -85.935  1.00 30.38           C  
ANISOU 3859  CA  THR D 328     5532   3195   2817   -632    -52    436       C  
ATOM   3860  C   THR D 328     -31.136  15.769 -87.033  1.00 31.28           C  
ANISOU 3860  C   THR D 328     5560   3329   2997   -536   -256    354       C  
ATOM   3861  O   THR D 328     -30.800  14.766 -87.684  1.00 32.09           O  
ANISOU 3861  O   THR D 328     5794   3275   3123   -511   -269    383       O  
ATOM   3862  CB  THR D 328     -33.525  16.238 -86.431  1.00 29.21           C  
ANISOU 3862  CB  THR D 328     5135   3086   2876   -858     43    373       C  
ATOM   3863  OG1 THR D 328     -34.524  16.091 -85.413  1.00 34.64           O  
ANISOU 3863  OG1 THR D 328     5864   3783   3514   -947    285    456       O  
ATOM   3864  CG2 THR D 328     -33.981  15.510 -87.684  1.00 30.17           C  
ANISOU 3864  CG2 THR D 328     5206   3079   3179  -1043     12    349       C  
ATOM   3865  N   LEU D 329     -30.631  16.980 -87.280  1.00 27.91           N  
ANISOU 3865  N   LEU D 329     4923   3075   2608   -491   -386    245       N  
ATOM   3866  CA  LEU D 329     -29.590  17.152 -88.287  1.00 29.88           C  
ANISOU 3866  CA  LEU D 329     5063   3379   2912   -415   -533    189       C  
ATOM   3867  C   LEU D 329     -28.335  16.372 -87.920  1.00 30.66           C  
ANISOU 3867  C   LEU D 329     5290   3492   2866   -183   -609    242       C  
ATOM   3868  O   LEU D 329     -27.723  15.731 -88.785  1.00 31.20           O  
ANISOU 3868  O   LEU D 329     5376   3511   2966    -95   -636    242       O  
ATOM   3869  CB  LEU D 329     -29.267  18.636 -88.467  1.00 29.98           C  
ANISOU 3869  CB  LEU D 329     4849   3540   3001   -445   -625     92       C  
ATOM   3870  CG  LEU D 329     -30.287  19.435 -89.275  1.00 29.85           C  
ANISOU 3870  CG  LEU D 329     4682   3504   3155   -597   -586     62       C  
ATOM   3871  CD1 LEU D 329     -29.951  20.915 -89.249  1.00 30.71           C  
ANISOU 3871  CD1 LEU D 329     4648   3679   3341   -606   -648    -11       C  
ATOM   3872  CD2 LEU D 329     -30.342  18.922 -90.710  1.00 30.85           C  
ANISOU 3872  CD2 LEU D 329     4779   3595   3348   -649   -614     78       C  
ATOM   3873  N   THR D 330     -27.933  16.417 -86.642  1.00 30.30           N  
ANISOU 3873  N   THR D 330     5335   3537   2641    -48   -650    283       N  
ATOM   3874  CA  THR D 330     -26.773  15.646 -86.211  1.00 33.04           C  
ANISOU 3874  CA  THR D 330     5787   3932   2833    227   -754    361       C  
ATOM   3875  C   THR D 330     -26.931  14.166 -86.550  1.00 35.42           C  
ANISOU 3875  C   THR D 330     6360   3966   3132    319   -640    489       C  
ATOM   3876  O   THR D 330     -25.996  13.534 -87.054  1.00 38.17           O  
ANISOU 3876  O   THR D 330     6723   4296   3484    536   -699    505       O  
ATOM   3877  CB  THR D 330     -26.545  15.824 -84.708  1.00 36.50           C  
ANISOU 3877  CB  THR D 330     6338   4514   3018    356   -824    404       C  
ATOM   3878  OG1 THR D 330     -26.382  17.215 -84.407  1.00 35.72           O  
ANISOU 3878  OG1 THR D 330     6021   4620   2930    248   -935    231       O  
ATOM   3879  CG2 THR D 330     -25.302  15.079 -84.268  1.00 40.38           C  
ANISOU 3879  CG2 THR D 330     6897   5109   3338    689   -982    500       C  
ATOM   3880  N   GLN D 331     -28.108  13.594 -86.284  1.00 32.14           N  
ANISOU 3880  N   GLN D 331     6159   3326   2727    153   -457    573       N  
ATOM   3881  CA  GLN D 331     -28.312  12.178 -86.571  1.00 32.83           C  
ANISOU 3881  CA  GLN D 331     6552   3085   2838    184   -334    680       C  
ATOM   3882  C   GLN D 331     -28.299  11.920 -88.072  1.00 34.04           C  
ANISOU 3882  C   GLN D 331     6630   3127   3175     94   -344    541       C  
ATOM   3883  O   GLN D 331     -27.645  10.984 -88.547  1.00 37.33           O  
ANISOU 3883  O   GLN D 331     7225   3372   3587    289   -342    552       O  
ATOM   3884  CB  GLN D 331     -29.626  11.701 -85.955  1.00 34.48           C  
ANISOU 3884  CB  GLN D 331     6963   3087   3049    -56   -112    795       C  
ATOM   3885  CG  GLN D 331     -29.562  11.535 -84.446  1.00 36.96           C  
ANISOU 3885  CG  GLN D 331     7498   3444   3102     97    -46    990       C  
ATOM   3886  CD  GLN D 331     -28.450  10.604 -84.030  1.00 43.69           C  
ANISOU 3886  CD  GLN D 331     8629   4196   3776    477   -128   1154       C  
ATOM   3887  OE1 GLN D 331     -28.348   9.481 -84.529  1.00 46.91           O  
ANISOU 3887  OE1 GLN D 331     9284   4270   4267    538    -52   1228       O  
ATOM   3888  NE2 GLN D 331     -27.602  11.063 -83.114  1.00 44.12           N  
ANISOU 3888  NE2 GLN D 331     8647   4537   3579    752   -298   1199       N  
ATOM   3889  N   HIS D 332     -29.013  12.746 -88.834  1.00 30.69           N  
ANISOU 3889  N   HIS D 332     5964   2808   2891   -166   -355    409       N  
ATOM   3890  CA  HIS D 332     -29.054  12.573 -90.283  1.00 32.65           C  
ANISOU 3890  CA  HIS D 332     6155   3000   3250   -252   -383    273       C  
ATOM   3891  C   HIS D 332     -27.661  12.687 -90.894  1.00 31.58           C  
ANISOU 3891  C   HIS D 332     5927   3007   3066     21   -478    222       C  
ATOM   3892  O   HIS D 332     -27.289  11.897 -91.768  1.00 35.27           O  
ANISOU 3892  O   HIS D 332     6529   3338   3534    119   -449    154       O  
ATOM   3893  CB  HIS D 332     -30.001  13.603 -90.892  1.00 32.55           C  
ANISOU 3893  CB  HIS D 332     5876   3139   3353   -518   -415    181       C  
ATOM   3894  CG  HIS D 332     -30.414  13.293 -92.295  1.00 34.66           C  
ANISOU 3894  CG  HIS D 332     6137   3344   3687   -662   -447     54       C  
ATOM   3895  ND1 HIS D 332     -29.736  13.773 -93.396  1.00 34.28           N  
ANISOU 3895  ND1 HIS D 332     5968   3450   3609   -572   -531    -30       N  
ATOM   3896  CD2 HIS D 332     -31.451  12.568 -92.778  1.00 36.94           C  
ANISOU 3896  CD2 HIS D 332     6527   3457   4053   -910   -412    -16       C  
ATOM   3897  CE1 HIS D 332     -30.332  13.349 -94.496  1.00 35.44           C  
ANISOU 3897  CE1 HIS D 332     6172   3528   3765   -723   -559   -148       C  
ATOM   3898  NE2 HIS D 332     -31.375  12.615 -94.148  1.00 37.16           N  
ANISOU 3898  NE2 HIS D 332     6513   3547   4060   -943   -509   -159       N  
ATOM   3899  N   ILE D 333     -26.873  13.663 -90.438  1.00 30.57           N  
ANISOU 3899  N   ILE D 333     5559   3156   2899    136   -578    236       N  
ATOM   3900  CA  ILE D 333     -25.540  13.882 -90.997  1.00 32.12           C  
ANISOU 3900  CA  ILE D 333     5574   3547   3084    353   -648    194       C  
ATOM   3901  C   ILE D 333     -24.590  12.757 -90.602  1.00 34.86           C  
ANISOU 3901  C   ILE D 333     6092   3815   3337    711   -648    269       C  
ATOM   3902  O   ILE D 333     -23.926  12.160 -91.457  1.00 37.54           O  
ANISOU 3902  O   ILE D 333     6460   4120   3685    901   -602    218       O  
ATOM   3903  CB  ILE D 333     -24.995  15.254 -90.561  1.00 33.07           C  
ANISOU 3903  CB  ILE D 333     5376   3967   3224    310   -761    173       C  
ATOM   3904  CG1 ILE D 333     -25.816  16.375 -91.196  1.00 31.69           C  
ANISOU 3904  CG1 ILE D 333     5053   3827   3162     23   -744    112       C  
ATOM   3905  CG2 ILE D 333     -23.526  15.396 -90.948  1.00 33.37           C  
ANISOU 3905  CG2 ILE D 333     5175   4237   3266    519   -821    150       C  
ATOM   3906  CD1 ILE D 333     -25.810  17.669 -90.395  1.00 31.10           C  
ANISOU 3906  CD1 ILE D 333     4805   3894   3119    -82   -820     87       C  
ATOM   3907  N   THR D 334     -24.494  12.456 -89.299  1.00 36.15           N  
ANISOU 3907  N   THR D 334     6388   3960   3388    849   -694    398       N  
ATOM   3908  CA  THR D 334     -23.500  11.480 -88.860  1.00 38.75           C  
ANISOU 3908  CA  THR D 334     6858   4251   3613   1261   -729    507       C  
ATOM   3909  C   THR D 334     -23.865  10.065 -89.297  1.00 39.99           C  
ANISOU 3909  C   THR D 334     7429   3975   3791   1357   -570    548       C  
ATOM   3910  O   THR D 334     -22.971   9.249 -89.561  1.00 42.51           O  
ANISOU 3910  O   THR D 334     7844   4219   4089   1727   -557    572       O  
ATOM   3911  CB  THR D 334     -23.312  11.544 -87.339  1.00 41.98           C  
ANISOU 3911  CB  THR D 334     7335   4777   3839   1406   -843    656       C  
ATOM   3912  OG1 THR D 334     -24.541  11.222 -86.679  1.00 42.08           O  
ANISOU 3912  OG1 THR D 334     7661   4533   3794   1199   -712    757       O  
ATOM   3913  CG2 THR D 334     -22.867  12.940 -86.910  1.00 41.61           C  
ANISOU 3913  CG2 THR D 334     6901   5136   3771   1298  -1023    557       C  
ATOM   3914  N   GLN D 335     -25.157   9.744 -89.385  1.00 37.06           N  
ANISOU 3914  N   GLN D 335     7297   3307   3478   1032   -443    542       N  
ATOM   3915  CA  GLN D 335     -25.509   8.416 -89.875  1.00 39.04           C  
ANISOU 3915  CA  GLN D 335     7952   3103   3779   1054   -297    536       C  
ATOM   3916  C   GLN D 335     -25.214   8.290 -91.367  1.00 37.98           C  
ANISOU 3916  C   GLN D 335     7757   2954   3721   1064   -274    313       C  
ATOM   3917  O   GLN D 335     -24.828   7.211 -91.831  1.00 40.91           O  
ANISOU 3917  O   GLN D 335     8424   3027   4093   1293   -188    270       O  
ATOM   3918  CB  GLN D 335     -26.976   8.101 -89.579  1.00 39.24           C  
ANISOU 3918  CB  GLN D 335     8199   2839   3872    644   -168    573       C  
ATOM   3919  CG  GLN D 335     -27.276   7.851 -88.106  1.00 39.98           C  
ANISOU 3919  CG  GLN D 335     8495   2850   3847    680   -104    829       C  
ATOM   3920  CD  GLN D 335     -28.657   7.261 -87.881  1.00 42.06           C  
ANISOU 3920  CD  GLN D 335     9008   2767   4205    283     95    890       C  
ATOM   3921  OE1 GLN D 335     -29.175   6.527 -88.722  1.00 43.75           O  
ANISOU 3921  OE1 GLN D 335     9350   2696   4575     72    178    753       O  
ATOM   3922  NE2 GLN D 335     -29.257   7.575 -86.734  1.00 41.70           N  
ANISOU 3922  NE2 GLN D 335     8934   2835   4073    164    177   1048       N  
ATOM   3923  N   ASN D 336     -25.357   9.381 -92.120  1.00 36.09           N  
ANISOU 3923  N   ASN D 336     7171   3021   3521    850   -338    177       N  
ATOM   3924  CA  ASN D 336     -24.959   9.357 -93.525  1.00 37.53           C  
ANISOU 3924  CA  ASN D 336     7291   3263   3707    898   -308    -10       C  
ATOM   3925  C   ASN D 336     -23.450   9.208 -93.660  1.00 39.11           C  
ANISOU 3925  C   ASN D 336     7357   3649   3852   1354   -301      6       C  
ATOM   3926  O   ASN D 336     -22.968   8.488 -94.541  1.00 39.65           O  
ANISOU 3926  O   ASN D 336     7576   3597   3891   1571   -200   -115       O  
ATOM   3927  CB  ASN D 336     -25.442  10.618 -94.236  1.00 34.28           C  
ANISOU 3927  CB  ASN D 336     6556   3144   3324    592   -372    -97       C  
ATOM   3928  CG  ASN D 336     -26.783  10.421 -94.913  1.00 35.66           C  
ANISOU 3928  CG  ASN D 336     6875   3136   3537    226   -364   -219       C  
ATOM   3929  OD1 ASN D 336     -26.974   9.467 -95.668  1.00 37.09           O  
ANISOU 3929  OD1 ASN D 336     7336   3063   3691    217   -310   -364       O  
ATOM   3930  ND2 ASN D 336     -27.725  11.308 -94.628  1.00 34.48           N  
ANISOU 3930  ND2 ASN D 336     6531   3115   3454    -68   -428   -178       N  
ATOM   3931  N   LYS D 337     -22.687   9.860 -92.781  1.00 40.54           N  
ANISOU 3931  N   LYS D 337     7247   4140   4017   1513   -409    136       N  
ATOM   3932  CA  LYS D 337     -21.239   9.697 -92.833  1.00 42.95           C  
ANISOU 3932  CA  LYS D 337     7346   4677   4297   1950   -421    160       C  
ATOM   3933  C   LYS D 337     -20.836   8.274 -92.465  1.00 46.59           C  
ANISOU 3933  C   LYS D 337     8176   4814   4713   2379   -359    241       C  
ATOM   3934  O   LYS D 337     -19.920   7.706 -93.073  1.00 49.06           O  
ANISOU 3934  O   LYS D 337     8473   5146   5022   2761   -272    182       O  
ATOM   3935  CB  LYS D 337     -20.551  10.715 -91.922  1.00 42.42           C  
ANISOU 3935  CB  LYS D 337     6863   5028   4226   1976   -598    253       C  
ATOM   3936  CG  LYS D 337     -19.035  10.575 -91.916  1.00 47.74           C  
ANISOU 3936  CG  LYS D 337     7226   6015   4899   2410   -640    278       C  
ATOM   3937  CD  LYS D 337     -18.348  11.522 -90.944  1.00 49.85           C  
ANISOU 3937  CD  LYS D 337     7075   6703   5162   2399   -863    338       C  
ATOM   3938  CE  LYS D 337     -16.923  11.051 -90.676  1.00 56.71           C  
ANISOU 3938  CE  LYS D 337     7671   7857   6017   2905   -947    398       C  
ATOM   3939  NZ  LYS D 337     -16.115  12.071 -89.959  1.00 58.77           N  
ANISOU 3939  NZ  LYS D 337     7421   8609   6300   2838  -1186    393       N  
ATOM   3940  N   GLU D 338     -21.518   7.671 -91.486  1.00 48.53           N  
ANISOU 3940  N   GLU D 338     8776   4739   4923   2340   -373    390       N  
ATOM   3941  CA  GLU D 338     -21.208   6.288 -91.132  1.00 54.64           C  
ANISOU 3941  CA  GLU D 338     9982   5118   5662   2745   -293    507       C  
ATOM   3942  C   GLU D 338     -21.607   5.334 -92.250  1.00 56.31           C  
ANISOU 3942  C   GLU D 338    10580   4877   5938   2712   -102    319       C  
ATOM   3943  O   GLU D 338     -20.886   4.371 -92.537  1.00 59.01           O  
ANISOU 3943  O   GLU D 338    11147   5000   6275   3158     -6    304       O  
ATOM   3944  CB  GLU D 338     -21.900   5.897 -89.825  1.00 57.96           C  
ANISOU 3944  CB  GLU D 338    10728   5285   6010   2669   -314    747       C  
ATOM   3945  CG  GLU D 338     -21.571   4.478 -89.374  1.00 65.85           C  
ANISOU 3945  CG  GLU D 338    12062   5967   6989   2960   -202    864       C  
ATOM   3946  CD  GLU D 338     -22.065   4.161 -87.974  1.00 69.65           C  
ANISOU 3946  CD  GLU D 338    12709   6376   7380   2852   -200   1097       C  
ATOM   3947  OE1 GLU D 338     -22.317   5.102 -87.191  1.00 67.86           O  
ANISOU 3947  OE1 GLU D 338    12275   6448   7059   2692   -322   1175       O  
ATOM   3948  OE2 GLU D 338     -22.201   2.960 -87.657  1.00 75.12           O  
ANISOU 3948  OE2 GLU D 338    13749   6710   8084   2933    -63   1197       O  
ATOM   3949  N   LEU D 339     -22.755   5.579 -92.884  1.00 53.69           N  
ANISOU 3949  N   LEU D 339    10330   4410   5660   2199    -57    159       N  
ATOM   3950  CA  LEU D 339     -23.160   4.779 -94.035  1.00 55.42           C  
ANISOU 3950  CA  LEU D 339    10889   4256   5912   2107     79    -84       C  
ATOM   3951  C   LEU D 339     -22.096   4.819 -95.123  1.00 56.98           C  
ANISOU 3951  C   LEU D 339    10916   4682   6050   2453    144   -265       C  
ATOM   3952  O   LEU D 339     -21.705   3.777 -95.664  1.00 62.19           O  
ANISOU 3952  O   LEU D 339    11925   5009   6695   2766    283   -391       O  
ATOM   3953  CB  LEU D 339     -24.503   5.278 -94.570  1.00 51.54           C  
ANISOU 3953  CB  LEU D 339    10364   3751   5467   1495     46   -235       C  
ATOM   3954  CG  LEU D 339     -25.252   4.416 -95.589  1.00 54.83           C  
ANISOU 3954  CG  LEU D 339    11172   3750   5910   1255    129   -505       C  
ATOM   3955  CD1 LEU D 339     -25.680   3.086 -94.980  1.00 58.48           C  
ANISOU 3955  CD1 LEU D 339    11964   3787   6469   1184    233   -401       C  
ATOM   3956  CD2 LEU D 339     -26.454   5.176 -96.147  1.00 52.83           C  
ANISOU 3956  CD2 LEU D 339    10717   3676   5682    694     26   -640       C  
ATOM   3957  N   ILE D 340     -21.599   6.018 -95.437  1.00 54.48           N  
ANISOU 3957  N   ILE D 340    10077   4921   5703   2410     72   -274       N  
ATOM   3958  CA  ILE D 340     -20.566   6.165 -96.462  1.00 57.70           C  
ANISOU 3958  CA  ILE D 340    10261   5614   6047   2709    179   -414       C  
ATOM   3959  C   ILE D 340     -19.324   5.368 -96.083  1.00 63.75           C  
ANISOU 3959  C   ILE D 340    11048   6353   6819   3351    251   -327       C  
ATOM   3960  O   ILE D 340     -18.862   4.503 -96.837  1.00 67.46           O  
ANISOU 3960  O   ILE D 340    11765   6618   7248   3697    427   -485       O  
ATOM   3961  CB  ILE D 340     -20.230   7.651 -96.686  1.00 55.02           C  
ANISOU 3961  CB  ILE D 340     9345   5853   5705   2510    105   -376       C  
ATOM   3962  CG1 ILE D 340     -21.347   8.350 -97.464  1.00 53.04           C  
ANISOU 3962  CG1 ILE D 340     9108   5626   5419   1993     74   -495       C  
ATOM   3963  CG2 ILE D 340     -18.895   7.799 -97.406  1.00 56.65           C  
ANISOU 3963  CG2 ILE D 340     9231   6423   5872   2888    243   -429       C  
ATOM   3964  CD1 ILE D 340     -21.765   7.614 -98.707  1.00 57.35           C  
ANISOU 3964  CD1 ILE D 340    10019   5923   5847   1958    194   -750       C  
ATOM   3965  N   GLU D 341     -18.778   5.630 -94.893  1.00 65.02           N  
ANISOU 3965  N   GLU D 341    10962   6726   7015   3549    105    -84       N  
ATOM   3966  CA  GLU D 341     -17.523   4.990 -94.508  1.00 71.58           C  
ANISOU 3966  CA  GLU D 341    11709   7639   7848   4206    125     26       C  
ATOM   3967  C   GLU D 341     -17.674   3.483 -94.328  1.00 74.66           C  
ANISOU 3967  C   GLU D 341    12635   7496   8237   4382    232     54       C  
ATOM   3968  O   GLU D 341     -16.711   2.739 -94.549  1.00 78.99           O  
ANISOU 3968  O   GLU D 341    13143   8080   8788   4800    329     48       O  
ATOM   3969  CB  GLU D 341     -16.971   5.630 -93.235  1.00 73.69           C  
ANISOU 3969  CB  GLU D 341    11574   8308   8116   4308   -118    268       C  
ATOM   3970  CG  GLU D 341     -15.788   6.553 -93.489  1.00 77.15           C  
ANISOU 3970  CG  GLU D 341    11309   9409   8595   4444   -169    242       C  
ATOM   3971  CD  GLU D 341     -15.628   7.621 -92.423  1.00 78.22           C  
ANISOU 3971  CD  GLU D 341    11021   9966   8734   4226   -446    376       C  
ATOM   3972  OE1 GLU D 341     -16.535   7.762 -91.574  1.00 77.08           O  
ANISOU 3972  OE1 GLU D 341    11132   9622   8532   3939   -572    471       O  
ATOM   3973  OE2 GLU D 341     -14.597   8.326 -92.437  1.00 80.57           O  
ANISOU 3973  OE2 GLU D 341    10726  10797   9089   4326   -525    368       O  
ATOM   3974  N   LYS D 342     -18.859   3.010 -93.937  1.00 73.70           N  
ANISOU 3974  N   LYS D 342    12959   6915   8130   4006    230     91       N  
ATOM   3975  CA  LYS D 342     -19.075   1.570 -93.840  1.00 79.92           C  
ANISOU 3975  CA  LYS D 342    14217   7205   8945   4060    353    107       C  
ATOM   3976  C   LYS D 342     -19.149   0.906 -95.208  1.00 83.47           C  
ANISOU 3976  C   LYS D 342    14908   7402   9406   4040    534   -192       C  
ATOM   3977  O   LYS D 342     -18.963  -0.312 -95.302  1.00 87.27           O  
ANISOU 3977  O   LYS D 342    15716   7523   9919   4226    650   -211       O  
ATOM   3978  CB  LYS D 342     -20.347   1.271 -93.045  1.00 80.43           C  
ANISOU 3978  CB  LYS D 342    14614   6904   9043   3606    330    231       C  
ATOM   3979  CG  LYS D 342     -20.135   1.233 -91.538  1.00 83.44           C  
ANISOU 3979  CG  LYS D 342    14945   7387   9371   3750    221    555       C  
ATOM   3980  CD  LYS D 342     -21.416   0.879 -90.801  1.00 84.62           C  
ANISOU 3980  CD  LYS D 342    15413   7190   9550   3297    265    675       C  
ATOM   3981  CE  LYS D 342     -21.116   0.349 -89.407  1.00 89.27           C  
ANISOU 3981  CE  LYS D 342    16102   7757  10057   3529    234    985       C  
ATOM   3982  NZ  LYS D 342     -20.226   1.265 -88.638  1.00 88.37           N  
ANISOU 3982  NZ  LYS D 342    15563   8196   9817   3817     24   1124       N  
ATOM   3983  N   ALA D 343     -19.419   1.671 -96.264  1.00 83.31           N  
ANISOU 3983  N   ALA D 343    14749   7564   9341   3821    559   -432       N  
ATOM   3984  CA  ALA D 343     -19.398   1.147 -97.622  1.00 88.53           C  
ANISOU 3984  CA  ALA D 343    15592   8093   9954   3812    716   -737       C  
ATOM   3985  C   ALA D 343     -18.007   1.169 -98.242  1.00 93.85           C  
ANISOU 3985  C   ALA D 343    15973   9117  10567   4344    847   -799       C  
ATOM   3986  O   ALA D 343     -17.795   0.522 -99.274  1.00 99.86           O  
ANISOU 3986  O   ALA D 343    16917   9751  11275   4445   1008  -1029       O  
ATOM   3987  CB  ALA D 343     -20.363   1.937 -98.512  1.00 85.09           C  
ANISOU 3987  CB  ALA D 343    15142   7742   9447   3309    677   -967       C  
ATOM   3988  N   LEU D 344     -17.080   1.896 -97.627  1.00 96.19           N  
ANISOU 3988  N   LEU D 344    17566   8741  10243   3829    133   -901       N  
ATOM   3989  CA  LEU D 344     -15.716   1.987 -98.134  1.00 98.85           C  
ANISOU 3989  CA  LEU D 344    17793   9366  10401   4408    263   -840       C  
ATOM   3990  C   LEU D 344     -14.827   0.911 -97.522  1.00103.76           C  
ANISOU 3990  C   LEU D 344    18621   9874  10930   4722    341   -700       C  
ATOM   3991  O   LEU D 344     -14.341   0.019 -98.218  1.00108.39           O  
ANISOU 3991  O   LEU D 344    19496  10386  11303   4997    379   -761       O  
ATOM   3992  CB  LEU D 344     -15.132   3.374 -97.855  1.00 96.50           C  
ANISOU 3992  CB  LEU D 344    16812   9637  10217   4403    284   -625       C  
ATOM   3993  CG  LEU D 344     -15.670   4.520 -98.714  1.00 96.01           C  
ANISOU 3993  CG  LEU D 344    16385   9896  10198   4120    231   -699       C  
ATOM   3994  CD1 LEU D 344     -15.642   5.830 -97.940  1.00 93.00           C  
ANISOU 3994  CD1 LEU D 344    15453   9867  10016   3871    143   -508       C  
ATOM   3995  CD2 LEU D 344     -14.879   4.640-100.007  1.00 98.89           C  
ANISOU 3995  CD2 LEU D 344    16673  10523  10377   4551    355   -706       C  
TER    3996      LEU D 344                                                      
ATOM   3997  N   PRO H 902     -19.806  20.199-105.298  1.00112.25           N  
ANISOU 3997  N   PRO H 902    14169  15565  12915   1707   -380   -191       N  
ATOM   3998  CA  PRO H 902     -18.743  19.495-104.574  1.00111.53           C  
ANISOU 3998  CA  PRO H 902    14076  15343  12958   1884   -404    -36       C  
ATOM   3999  C   PRO H 902     -19.227  18.230-103.862  1.00108.26           C  
ANISOU 3999  C   PRO H 902    14077  14637  12421   1877   -386   -281       C  
ATOM   4000  O   PRO H 902     -19.213  18.181-102.632  1.00109.40           O  
ANISOU 4000  O   PRO H 902    14305  14606  12656   1777   -554   -258       O  
ATOM   4001  CB  PRO H 902     -18.269  20.541-103.565  1.00112.64           C  
ANISOU 4001  CB  PRO H 902    13981  15455  13361   1716   -710    192       C  
ATOM   4002  CG  PRO H 902     -18.483  21.837-104.269  1.00112.75           C  
ANISOU 4002  CG  PRO H 902    13730  15675  13436   1585   -761    307       C  
ATOM   4003  CD  PRO H 902     -19.728  21.658-105.106  1.00111.69           C  
ANISOU 4003  CD  PRO H 902    13807  15615  13017   1529   -573      5       C  
ATOM   4004  N   SER H 903     -19.655  17.237-104.640  1.00 96.24           N  
ANISOU 4004  N   SER H 903    12833  13044  10689   1995   -210   -502       N  
ATOM   4005  CA  SER H 903     -20.003  15.908-104.133  1.00 82.95           C  
ANISOU 4005  CA  SER H 903    11557  11043   8918   2005   -192   -696       C  
ATOM   4006  C   SER H 903     -21.096  15.913-103.062  1.00 68.06           C  
ANISOU 4006  C   SER H 903     9824   8972   7062   1662   -334   -804       C  
ATOM   4007  O   SER H 903     -20.806  15.979-101.869  1.00 66.97           O  
ANISOU 4007  O   SER H 903     9679   8734   7033   1639   -438   -684       O  
ATOM   4008  CB  SER H 903     -18.755  15.216-103.580  1.00 82.69           C  
ANISOU 4008  CB  SER H 903    11536  10916   8967   2304   -151   -519       C  
ATOM   4009  OG  SER H 903     -17.882  14.833-104.628  1.00 83.01           O  
ANISOU 4009  OG  SER H 903    11533  11102   8904   2707     45   -430       O  
HETATM 4010  N   PTR H 904     -22.349  15.817-103.494  1.00 55.13           N  
ANISOU 4010  N   PTR H 904     8324   7307   5316   1430   -337  -1005       N  
HETATM 4011  CA  PTR H 904     -23.477  15.764-102.567  1.00 45.72           C  
ANISOU 4011  CA  PTR H 904     7238   5992   4143   1135   -421  -1040       C  
HETATM 4012  C   PTR H 904     -24.069  14.360-102.451  1.00 45.31           C  
ANISOU 4012  C   PTR H 904     7532   5616   4069   1041   -402  -1172       C  
HETATM 4013  O   PTR H 904     -24.038  13.585-103.401  1.00 46.94           O  
ANISOU 4013  O   PTR H 904     7943   5700   4193   1123   -377  -1340       O  
HETATM 4014  CB  PTR H 904     -24.568  16.751-102.995  1.00 41.74           C  
ANISOU 4014  CB  PTR H 904     6572   5714   3574    901   -462  -1092       C  
HETATM 4015  CG  PTR H 904     -24.292  18.169-102.564  1.00 40.36           C  
ANISOU 4015  CG  PTR H 904     6135   5757   3445    912   -550   -932       C  
HETATM 4016  CD1 PTR H 904     -23.361  18.951-103.232  1.00 41.50           C  
ANISOU 4016  CD1 PTR H 904     6041   6084   3642   1061   -553   -832       C  
HETATM 4017  CD2 PTR H 904     -24.955  18.723-101.474  1.00 38.20           C  
ANISOU 4017  CD2 PTR H 904     5872   5487   3156    798   -646   -854       C  
HETATM 4018  CE1 PTR H 904     -23.100  20.252-102.827  1.00 41.47           C  
ANISOU 4018  CE1 PTR H 904     5828   6210   3720   1032   -703   -675       C  
HETATM 4019  CE2 PTR H 904     -24.706  20.021-101.066  1.00 38.07           C  
ANISOU 4019  CE2 PTR H 904     5706   5603   3154    836   -792   -738       C  
HETATM 4020  CZ  PTR H 904     -23.780  20.784-101.749  1.00 39.28           C  
ANISOU 4020  CZ  PTR H 904     5637   5884   3404    920   -848   -659       C  
HETATM 4021  OH  PTR H 904     -23.522  22.000-101.357  1.00 38.30           O  
ANISOU 4021  OH  PTR H 904     5399   5820   3333    922  -1048   -539       O  
HETATM 4022  P   PTR H 904     -24.437  23.272-101.721  1.00 36.79           P  
ANISOU 4022  P   PTR H 904     5136   5820   3020    810  -1109   -565       P  
HETATM 4023  O1P PTR H 904     -24.481  23.461-103.246  1.00 38.96           O  
ANISOU 4023  O1P PTR H 904     5212   6310   3281    778   -944   -606       O  
HETATM 4024  O2P PTR H 904     -23.799  24.449-101.083  1.00 37.66           O  
ANISOU 4024  O2P PTR H 904     5201   5870   3237    853  -1415   -413       O  
HETATM 4025  O3P PTR H 904     -25.867  23.069-101.191  1.00 36.87           O  
ANISOU 4025  O3P PTR H 904     5334   5856   2818    731  -1039   -666       O  
ATOM   4026  N   VAL H 905     -24.608  14.036-101.280  1.00 44.78           N  
ANISOU 4026  N   VAL H 905     7554   5392   4069    891   -431  -1078       N  
ATOM   4027  CA  VAL H 905     -25.325  12.779-101.082  1.00 49.88           C  
ANISOU 4027  CA  VAL H 905     8484   5714   4753    722   -435  -1131       C  
ATOM   4028  C   VAL H 905     -26.778  13.007-101.491  1.00 51.34           C  
ANISOU 4028  C   VAL H 905     8583   5984   4938    368   -493  -1176       C  
ATOM   4029  O   VAL H 905     -27.425  13.901-100.955  1.00 45.35           O  
ANISOU 4029  O   VAL H 905     7602   5457   4170    254   -483  -1040       O  
ATOM   4030  CB  VAL H 905     -25.212  12.299 -99.619  1.00 50.03           C  
ANISOU 4030  CB  VAL H 905     8609   5548   4850    758   -405   -939       C  
ATOM   4031  CG1 VAL H 905     -25.643  10.850 -99.492  1.00 52.95           C  
ANISOU 4031  CG1 VAL H 905     9299   5521   5298    629   -405   -959       C  
ATOM   4032  CG2 VAL H 905     -23.793  12.482 -99.116  1.00 47.06           C  
ANISOU 4032  CG2 VAL H 905     8207   5200   4474   1103   -391   -858       C  
ATOM   4033  N   ASN H 906     -27.309  12.220-102.428  1.00 53.63           N  
ANISOU 4033  N   ASN H 906     9062   6087   5228    217   -580  -1358       N  
ATOM   4034  CA  ASN H 906     -28.542  12.642-103.093  1.00 58.14           C  
ANISOU 4034  CA  ASN H 906     9483   6819   5789    -87   -673  -1419       C  
ATOM   4035  C   ASN H 906     -29.741  11.726-102.879  1.00 69.92           C  
ANISOU 4035  C   ASN H 906    11071   8052   7445   -476   -799  -1353       C  
ATOM   4036  O   ASN H 906     -30.845  12.227-102.632  1.00 66.97           O  
ANISOU 4036  O   ASN H 906    10433   7885   7126   -742   -807  -1192       O  
ATOM   4037  CB  ASN H 906     -28.293  12.805-104.596  1.00 54.96           C  
ANISOU 4037  CB  ASN H 906     9149   6502   5231     46   -737  -1687       C  
ATOM   4038  CG  ASN H 906     -27.478  14.036-104.905  1.00 51.51           C  
ANISOU 4038  CG  ASN H 906     8459   6436   4679    322   -611  -1654       C  
ATOM   4039  OD1 ASN H 906     -27.812  15.132-104.450  1.00 49.43           O  
ANISOU 4039  OD1 ASN H 906     7905   6452   4425    238   -574  -1511       O  
ATOM   4040  ND2 ASN H 906     -26.399  13.869-105.657  1.00 52.31           N  
ANISOU 4040  ND2 ASN H 906     8670   6535   4670    673   -549  -1749       N  
ATOM   4041  N   VAL H 907     -29.575  10.408-102.992  1.00 84.39           N  
ANISOU 4041  N   VAL H 907    13265   9435   9364   -515   -911  -1442       N  
ATOM   4042  CA  VAL H 907     -30.667   9.449-102.816  1.00 96.48           C  
ANISOU 4042  CA  VAL H 907    14893  10646  11119   -935  -1088  -1341       C  
ATOM   4043  C   VAL H 907     -30.456   8.580-101.570  1.00109.31           C  
ANISOU 4043  C   VAL H 907    16661  11966  12908   -943   -996  -1088       C  
ATOM   4044  O   VAL H 907     -30.829   7.409-101.559  1.00113.53           O  
ANISOU 4044  O   VAL H 907    17458  12052  13627  -1177  -1166  -1063       O  
ATOM   4045  CB  VAL H 907     -30.873   8.596-104.083  1.00 95.58           C  
ANISOU 4045  CB  VAL H 907    15141  10182  10995  -1043  -1399  -1661       C  
ATOM   4046  CG1 VAL H 907     -32.250   7.922-104.103  1.00 97.60           C  
ANISOU 4046  CG1 VAL H 907    15368  10185  11532  -1596  -1678  -1534       C  
ATOM   4047  CG2 VAL H 907     -30.772   9.480-105.303  1.00 90.21           C  
ANISOU 4047  CG2 VAL H 907    14372   9830  10075   -872  -1431  -1923       C  
ATOM   4048  N   GLN H 908     -29.841   9.134-100.526  1.00117.79           N  
ANISOU 4048  N   GLN H 908    17594  13248  13912   -679   -759   -902       N  
ATOM   4049  CA  GLN H 908     -29.972   8.602 -99.163  1.00124.44           C  
ANISOU 4049  CA  GLN H 908    18456  13937  14887   -702   -632   -570       C  
ATOM   4050  C   GLN H 908     -29.467   7.169 -98.997  1.00129.17           C  
ANISOU 4050  C   GLN H 908    19482  13999  15599   -670   -698   -604       C  
ATOM   4051  O   GLN H 908     -28.621   6.891 -98.139  1.00129.99           O  
ANISOU 4051  O   GLN H 908    19723  14009  15658   -375   -555   -511       O  
ATOM   4052  CB  GLN H 908     -31.443   8.695 -98.735  1.00131.15           C  
ANISOU 4052  CB  GLN H 908    19009  14910  15910  -1094   -626   -236       C  
ATOM   4053  CG  GLN H 908     -32.036  10.094 -98.926  1.00131.75           C  
ANISOU 4053  CG  GLN H 908    18695  15518  15845  -1098   -562   -196       C  
ATOM   4054  CD  GLN H 908     -33.148  10.162 -99.970  1.00135.31           C  
ANISOU 4054  CD  GLN H 908    18970  16047  16396  -1490   -757   -261       C  
ATOM   4055  OE1 GLN H 908     -33.201   9.362-100.907  1.00139.26           O  
ANISOU 4055  OE1 GLN H 908    19700  16215  16998  -1690  -1006   -496       O  
ATOM   4056  NE2 GLN H 908     -34.044  11.125 -99.804  1.00135.03           N  
ANISOU 4056  NE2 GLN H 908    18554  16445  16305  -1568   -669    -56       N  
TER    4057      GLN H 908                                                      
HETATM 4058  S   SO4 A1001     -13.115  34.814 -66.917  1.00 68.61           S  
HETATM 4059  O1  SO4 A1001     -14.405  35.422 -67.240  1.00 68.10           O  
HETATM 4060  O2  SO4 A1001     -12.237  34.878 -68.083  1.00 68.87           O  
HETATM 4061  O3  SO4 A1001     -13.318  33.419 -66.535  1.00 67.71           O  
HETATM 4062  O4  SO4 A1001     -12.491  35.541 -65.816  1.00 68.91           O  
HETATM 4063  S   SO4 A1002     -21.333  34.316 -70.340  1.00102.95           S  
HETATM 4064  O1  SO4 A1002     -22.435  33.386 -70.569  1.00103.06           O  
HETATM 4065  O2  SO4 A1002     -21.394  35.393 -71.323  1.00103.04           O  
HETATM 4066  O3  SO4 A1002     -20.062  33.612 -70.475  1.00103.26           O  
HETATM 4067  O4  SO4 A1002     -21.438  34.876 -68.994  1.00102.83           O  
HETATM 4068  S   SO4 B 401     -32.919  34.565 -39.150  1.00 29.88           S  
HETATM 4069  O1  SO4 B 401     -33.227  33.216 -39.603  1.00 26.84           O  
HETATM 4070  O2  SO4 B 401     -33.903  35.492 -39.692  1.00 27.49           O  
HETATM 4071  O3  SO4 B 401     -32.942  34.579 -37.682  1.00 32.07           O  
HETATM 4072  O4  SO4 B 401     -31.573  34.945 -39.586  1.00 26.54           O  
HETATM 4073  S   SO4 B 402     -37.392  41.506 -58.162  1.00 80.39           S  
HETATM 4074  O1  SO4 B 402     -38.122  40.250 -58.292  1.00 80.87           O  
HETATM 4075  O2  SO4 B 402     -36.806  41.878 -59.445  1.00 79.76           O  
HETATM 4076  O3  SO4 B 402     -38.309  42.556 -57.731  1.00 80.96           O  
HETATM 4077  O4  SO4 B 402     -36.336  41.341 -57.171  1.00 80.76           O  
HETATM 4078  S   SO4 C1001     -19.212  42.441 -73.802  1.00 73.97           S  
HETATM 4079  O1  SO4 C1001     -18.992  40.999 -73.761  1.00 73.44           O  
HETATM 4080  O2  SO4 C1001     -18.805  42.973 -75.101  1.00 74.48           O  
HETATM 4081  O3  SO4 C1001     -20.632  42.714 -73.605  1.00 74.91           O  
HETATM 4082  O4  SO4 C1001     -18.432  43.085 -72.749  1.00 73.30           O  
HETATM 4083  S   SO4 D1001     -17.692  17.687 -82.967  1.00 98.99           S  
HETATM 4084  O1  SO4 D1001     -16.740  17.306 -84.005  1.00 99.12           O  
HETATM 4085  O2  SO4 D1001     -18.982  17.060 -83.239  1.00 98.60           O  
HETATM 4086  O3  SO4 D1001     -17.196  17.247 -81.665  1.00 98.99           O  
HETATM 4087  O4  SO4 D1001     -17.844  19.139 -82.962  1.00 99.39           O  
HETATM 4088  O   HOH A1101     -24.572  30.729 -61.925  1.00 38.40           O  
HETATM 4089  O   HOH A1102     -16.897   5.595 -58.516  1.00 75.43           O  
HETATM 4090  O   HOH A1103      -7.717  19.285 -44.568  1.00 67.91           O  
HETATM 4091  O   HOH A1104     -14.249  33.190 -49.389  1.00 49.11           O  
HETATM 4092  O   HOH A1105     -14.442  31.665 -52.523  1.00 43.18           O  
HETATM 4093  O   HOH A1106     -19.457  30.570 -47.526  1.00 36.79           O  
HETATM 4094  O   HOH A1107     -11.814  33.276 -60.441  1.00 64.47           O  
HETATM 4095  O   HOH A1108     -26.672  22.137 -62.387  1.00 44.80           O  
HETATM 4096  O   HOH A1109     -23.910  31.872 -69.255  1.00 52.41           O  
HETATM 4097  O   HOH A1110     -29.491  19.630 -70.908  1.00 60.50           O  
HETATM 4098  O   HOH A1111     -22.344  33.152 -65.060  1.00 49.34           O  
HETATM 4099  O   HOH A1112     -12.335  23.392 -48.176  1.00 53.52           O  
HETATM 4100  O   HOH A1113      -1.010  29.382 -76.371  1.00 50.80           O  
HETATM 4101  O   HOH A1114     -11.575  24.399 -79.188  1.00 72.88           O  
HETATM 4102  O   HOH A1115      -6.441  31.114 -67.675  1.00 54.67           O  
HETATM 4103  O   HOH A1116     -26.893  25.245 -71.199  1.00 54.10           O  
HETATM 4104  O   HOH A1117     -16.910  34.554 -55.820  1.00 42.09           O  
HETATM 4105  O   HOH A1118      -4.155  29.806 -67.665  1.00 40.91           O  
HETATM 4106  O   HOH A1119     -12.482  30.191 -73.506  1.00 42.17           O  
HETATM 4107  O   HOH A1120     -24.793  17.549 -44.626  1.00 62.89           O  
HETATM 4108  O   HOH A1121     -13.138  29.801 -47.958  1.00 49.93           O  
HETATM 4109  O   HOH A1122      -2.813  20.603 -66.678  1.00 42.84           O  
HETATM 4110  O   HOH A1123      -3.511  18.718 -74.578  1.00 51.10           O  
HETATM 4111  O   HOH A1124     -25.117  22.585 -79.151  1.00 43.78           O  
HETATM 4112  O   HOH A1125     -23.337  31.039 -60.006  1.00 42.57           O  
HETATM 4113  O   HOH A1126     -30.689  30.088 -61.952  1.00 54.40           O  
HETATM 4114  O   HOH A1127     -17.065  32.846 -53.727  1.00 35.79           O  
HETATM 4115  O   HOH A1128     -12.189  32.925 -52.863  1.00 38.62           O  
HETATM 4116  O   HOH A1129      -8.543  18.667 -48.557  1.00 49.34           O  
HETATM 4117  O   HOH A1130      -1.053  20.045 -73.810  1.00 46.11           O  
HETATM 4118  O   HOH A1131      -9.847  21.629 -48.485  1.00 42.03           O  
HETATM 4119  O   HOH A1132     -13.973  23.175 -78.351  1.00 58.50           O  
HETATM 4120  O   HOH A1133       3.518  22.434 -69.996  1.00 49.15           O  
HETATM 4121  O   HOH A1134     -14.113  34.434 -59.278  1.00 58.71           O  
HETATM 4122  O   HOH A1135     -23.755  14.549 -54.885  1.00 60.41           O  
HETATM 4123  O   HOH A1136     -27.551  18.145 -73.951  1.00 57.72           O  
HETATM 4124  O   HOH A1137     -24.471  25.685 -73.560  1.00 36.84           O  
HETATM 4125  O   HOH A1138     -22.018  19.685 -66.140  1.00 43.13           O  
HETATM 4126  O   HOH A1139     -23.969  22.819 -63.926  1.00 32.77           O  
HETATM 4127  O   HOH A1140     -17.415  12.947 -46.752  1.00 50.59           O  
HETATM 4128  O   HOH A1141      -1.676  18.727 -63.229  1.00 58.35           O  
HETATM 4129  O   HOH A1142     -14.188  17.704 -70.863  1.00 46.55           O  
HETATM 4130  O   HOH A1143     -16.195  34.363 -79.314  1.00 58.20           O  
HETATM 4131  O   HOH A1144      -9.992  15.522 -62.836  1.00 37.57           O  
HETATM 4132  O   HOH A1145     -16.569  24.592 -78.541  1.00 34.78           O  
HETATM 4133  O   HOH A1146      -3.530  34.067 -61.127  1.00 60.98           O  
HETATM 4134  O  AHOH A1147     -23.311  29.416 -39.662  0.50 29.70           O  
HETATM 4135  O  BHOH A1147     -22.584  31.160 -39.609  0.50 33.02           O  
HETATM 4136  O   HOH A1148       6.013  22.915 -75.993  1.00 68.25           O  
HETATM 4137  O   HOH A1149      -3.424  18.875 -54.502  1.00 49.75           O  
HETATM 4138  O   HOH A1150     -10.732  33.706 -64.572  1.00 54.77           O  
HETATM 4139  O   HOH A1151      -3.981  24.986 -52.978  1.00 37.36           O  
HETATM 4140  O   HOH A1152     -11.182  28.677 -71.679  1.00 39.51           O  
HETATM 4141  O   HOH A1153     -29.410  21.729 -74.343  1.00 60.33           O  
HETATM 4142  O   HOH A1154     -21.461  31.109 -74.654  1.00 51.28           O  
HETATM 4143  O   HOH A1155     -16.819  31.971 -66.566  1.00 44.59           O  
HETATM 4144  O   HOH A1156     -12.777  12.724 -47.483  1.00 48.20           O  
HETATM 4145  O   HOH A1157     -23.627  15.624 -74.445  1.00 42.77           O  
HETATM 4146  O   HOH A1158     -15.449  10.090 -58.893  1.00 57.81           O  
HETATM 4147  O   HOH A1159       5.264  19.538 -75.557  1.00 49.41           O  
HETATM 4148  O   HOH A1160     -25.673  28.428 -66.675  1.00 35.66           O  
HETATM 4149  O   HOH A1161     -19.405  10.022 -64.140  1.00 60.40           O  
HETATM 4150  O   HOH A1162     -22.549  14.484 -71.233  1.00 46.75           O  
HETATM 4151  O   HOH A1163     -18.528  33.499 -67.544  1.00 52.21           O  
HETATM 4152  O   HOH A1164     -24.734  14.387 -61.964  1.00 59.87           O  
HETATM 4153  O   HOH A1165      -7.261  16.714 -76.690  1.00 58.08           O  
HETATM 4154  O   HOH A1166     -14.206  28.724 -79.583  1.00 64.80           O  
HETATM 4155  O   HOH A1167     -17.264  35.970 -73.537  1.00 46.11           O  
HETATM 4156  O   HOH A1168     -25.015  31.001 -64.772  1.00 55.17           O  
HETATM 4157  O   HOH A1169     -18.565   9.795 -53.174  1.00 60.25           O  
HETATM 4158  O   HOH A1170      -7.480  23.772 -46.273  1.00 48.50           O  
HETATM 4159  O   HOH A1171     -27.151  14.950 -60.004  1.00 53.56           O  
HETATM 4160  O   HOH A1172     -18.374  36.184 -58.918  1.00 41.40           O  
HETATM 4161  O   HOH A1173      -6.884  33.393 -57.421  1.00 39.72           O  
HETATM 4162  O   HOH A1174     -19.764  37.829 -70.463  1.00 63.03           O  
HETATM 4163  O   HOH A1175      -4.231  29.644 -46.554  1.00 57.65           O  
HETATM 4164  O   HOH A1176     -27.873  29.873 -68.672  1.00 66.20           O  
HETATM 4165  O   HOH A1177     -19.310  35.860 -65.739  1.00 59.45           O  
HETATM 4166  O   HOH A1178     -12.417   8.641 -51.714  1.00 61.91           O  
HETATM 4167  O   HOH A1179     -17.636  35.573 -70.456  1.00 73.81           O  
HETATM 4168  O   HOH A1180     -11.559  33.694 -57.721  1.00 53.19           O  
HETATM 4169  O   HOH A1181     -17.377  18.830 -73.435  1.00 44.11           O  
HETATM 4170  O   HOH A1182      -0.959  32.535 -61.327  1.00 63.44           O  
HETATM 4171  O   HOH A1183     -19.392  17.878 -69.429  1.00 70.69           O  
HETATM 4172  O   HOH A1184       1.099  30.726 -60.971  1.00 55.73           O  
HETATM 4173  O  AHOH A1185     -11.659  37.086 -51.154  0.50 32.82           O  
HETATM 4174  O  BHOH A1185     -11.185  38.343 -52.538  0.50 33.30           O  
HETATM 4175  O   HOH A1186     -19.552  33.153 -49.646  1.00 52.86           O  
HETATM 4176  O   HOH A1187     -20.646   0.828 -57.350  1.00 67.76           O  
HETATM 4177  O   HOH A1188     -11.377   2.086 -62.024  1.00 67.30           O  
HETATM 4178  O   HOH A1189     -13.618  19.128 -77.325  1.00 50.60           O  
HETATM 4179  O   HOH A1190     -14.918  37.373 -59.987  1.00 66.03           O  
HETATM 4180  O   HOH A1191     -14.383   9.823 -56.180  1.00 54.84           O  
HETATM 4181  O   HOH A1192     -13.229  25.425 -81.156  1.00 62.24           O  
HETATM 4182  O   HOH A1193     -28.548   6.882 -61.316  1.00 64.38           O  
HETATM 4183  O   HOH A1194      -3.376  18.809 -60.704  1.00 62.55           O  
HETATM 4184  O   HOH A1195     -33.549  26.926 -66.167  1.00 73.25           O  
HETATM 4185  O   HOH A1196     -15.402  26.314 -80.524  1.00 81.96           O  
HETATM 4186  O   HOH A1197     -17.225  18.257 -70.749  1.00 49.52           O  
HETATM 4187  O   HOH A1198     -20.848  26.909 -37.119  1.00 69.02           O  
HETATM 4188  O   HOH A1199     -16.209   9.748 -66.516  1.00 61.87           O  
HETATM 4189  O   HOH A1200     -20.722  11.615 -68.202  1.00 57.43           O  
HETATM 4190  O   HOH A1201     -26.410  21.928 -39.613  1.00 66.26           O  
HETATM 4191  O   HOH A1202     -32.238  27.526 -68.608  1.00 57.00           O  
HETATM 4192  O   HOH A1203       5.488  22.173 -71.927  1.00 53.88           O  
HETATM 4193  O   HOH A1204     -16.312  38.674 -67.752  1.00 53.07           O  
HETATM 4194  O   HOH A1205     -12.277  13.188 -43.432  1.00 62.43           O  
HETATM 4195  O   HOH A1206     -12.017  34.886 -54.952  1.00 48.83           O  
HETATM 4196  O   HOH A1207     -25.950  22.599 -76.490  1.00 50.82           O  
HETATM 4197  O   HOH A1208       0.195  18.450 -75.889  1.00 53.46           O  
HETATM 4198  O   HOH A1209     -26.274   7.000 -57.391  1.00 64.14           O  
HETATM 4199  O   HOH A1210     -31.801  31.445 -65.798  1.00 44.63           O  
HETATM 4200  O   HOH A1211      -0.658  28.027 -50.281  1.00 58.64           O  
HETATM 4201  O   HOH A1212      -3.144  11.740 -51.740  1.00 60.03           O  
HETATM 4202  O   HOH A1213     -21.823  22.343 -36.169  1.00 74.67           O  
HETATM 4203  O   HOH A1214     -24.550  28.060 -74.510  1.00 58.14           O  
HETATM 4204  O   HOH A1215     -11.894  17.430 -78.541  1.00 53.95           O  
HETATM 4205  O   HOH A1216     -18.531  36.183 -56.145  1.00 45.48           O  
HETATM 4206  O   HOH A1217     -30.027  27.655 -70.274  1.00 48.37           O  
HETATM 4207  O   HOH A1218      -8.843  34.577 -57.973  1.00 50.88           O  
HETATM 4208  O   HOH A1219     -10.641  34.790 -61.937  1.00 65.51           O  
HETATM 4209  O   HOH A1220       3.431  19.904 -68.869  1.00 59.24           O  
HETATM 4210  O   HOH A1221     -24.045  30.791 -73.435  1.00 59.08           O  
HETATM 4211  O   HOH A1222     -25.229  32.583 -67.477  1.00 41.90           O  
HETATM 4212  O   HOH A1223     -19.931  37.902 -59.271  1.00 69.83           O  
HETATM 4213  O   HOH A1224     -17.177  33.405 -47.473  1.00 69.02           O  
HETATM 4214  O   HOH A1225     -15.256  17.793 -75.023  1.00 57.74           O  
HETATM 4215  O   HOH A1226     -12.981  25.930 -46.422  1.00 52.71           O  
HETATM 4216  O   HOH A1227     -27.710  19.866 -76.029  1.00 93.40           O  
HETATM 4217  O   HOH A1228     -18.082  34.055 -51.604  1.00 37.17           O  
HETATM 4218  O   HOH A1229       4.080  33.341 -64.673  1.00 57.40           O  
HETATM 4219  O   HOH A1230     -19.474  21.737 -34.484  1.00 78.97           O  
HETATM 4220  O   HOH A1231       0.493  33.599 -63.086  1.00 66.38           O  
HETATM 4221  O   HOH A1232     -19.435  29.134 -41.339  1.00 67.91           O  
HETATM 4222  O   HOH A1233       6.136  19.705 -73.171  1.00 67.21           O  
HETATM 4223  O   HOH A1234     -27.061  32.275 -71.332  1.00 46.80           O  
HETATM 4224  O   HOH A1235     -34.600  24.464 -67.204  1.00 72.29           O  
HETATM 4225  O   HOH A1236     -24.854  29.110 -69.227  1.00 63.19           O  
HETATM 4226  O   HOH A1237     -26.007   5.912 -47.302  1.00 71.61           O  
HETATM 4227  O   HOH A1238     -13.846  30.468 -43.898  1.00 61.12           O  
HETATM 4228  O   HOH A1239       3.947  31.685 -62.344  1.00 62.08           O  
HETATM 4229  O   HOH A1240     -21.405  19.748 -33.708  1.00 93.03           O  
HETATM 4230  O   HOH E1001      -4.762  14.238 -67.931  1.00 49.54           O  
HETATM 4231  O   HOH E1002     -19.713  15.670 -68.140  1.00 57.45           O  
HETATM 4232  O   HOH E1003      -6.248  17.648 -61.840  1.00 54.05           O  
HETATM 4233  O   HOH E1004      -4.626  11.658 -68.745  1.00 64.80           O  
HETATM 4234  O   HOH B 501     -39.185  38.617 -57.092  1.00 57.41           O  
HETATM 4235  O   HOH B 502     -41.228  15.316 -44.864  1.00 70.43           O  
HETATM 4236  O   HOH B 503     -43.927  26.328 -38.407  1.00 47.64           O  
HETATM 4237  O   HOH B 504     -24.666  36.031 -54.885  1.00 54.61           O  
HETATM 4238  O   HOH B 505     -35.986  27.434 -29.074  1.00 52.31           O  
HETATM 4239  O   HOH B 506     -36.761  16.915 -51.631  1.00 71.34           O  
HETATM 4240  O   HOH B 507     -43.342  41.323 -53.702  1.00 43.28           O  
HETATM 4241  O   HOH B 508     -32.209  17.634 -54.942  1.00 56.58           O  
HETATM 4242  O   HOH B 509     -36.525  22.526 -57.825  1.00 53.61           O  
HETATM 4243  O   HOH B 510     -35.673  30.613 -33.083  1.00 41.69           O  
HETATM 4244  O   HOH B 511     -34.338  19.943 -57.211  1.00 76.06           O  
HETATM 4245  O   HOH B 512     -45.749  40.927 -52.647  1.00 39.96           O  
HETATM 4246  O   HOH B 513     -21.707  39.312 -53.902  1.00 72.15           O  
HETATM 4247  O   HOH B 514     -27.223  37.710 -56.057  1.00 36.92           O  
HETATM 4248  O   HOH B 515     -36.387  35.280 -38.884  1.00 35.76           O  
HETATM 4249  O   HOH B 516     -37.875  46.336 -51.804  1.00 61.00           O  
HETATM 4250  O   HOH B 517     -40.378  32.474 -40.147  1.00 31.22           O  
HETATM 4251  O   HOH B 518     -43.391  39.596 -40.289  1.00 56.88           O  
HETATM 4252  O   HOH B 519     -39.291  44.270 -50.352  1.00 36.29           O  
HETATM 4253  O   HOH B 520     -28.111  36.581 -42.295  1.00 40.66           O  
HETATM 4254  O   HOH B 521     -37.543  27.582 -59.577  1.00 33.53           O  
HETATM 4255  O   HOH B 522     -35.060  26.819 -58.401  1.00 33.33           O  
HETATM 4256  O   HOH B 523     -39.505  22.573 -62.946  1.00 52.32           O  
HETATM 4257  O   HOH B 524     -26.383  34.059 -55.935  1.00 33.93           O  
HETATM 4258  O   HOH B 525     -32.725  44.920 -40.921  1.00 37.76           O  
HETATM 4259  O   HOH B 526     -38.118  34.668 -32.788  1.00 45.86           O  
HETATM 4260  O   HOH B 527     -35.554  33.978 -58.804  1.00 31.54           O  
HETATM 4261  O   HOH B 528     -40.401  20.639 -50.007  1.00 48.83           O  
HETATM 4262  O   HOH B 529     -19.022  36.645 -52.724  1.00 67.78           O  
HETATM 4263  O   HOH B 530     -28.209  24.389 -39.304  1.00 47.60           O  
HETATM 4264  O   HOH B 531     -40.461  44.350 -39.075  1.00 54.71           O  
HETATM 4265  O   HOH B 532     -48.030  22.646 -45.013  1.00 66.10           O  
HETATM 4266  O   HOH B 533     -25.988  35.605 -46.441  1.00 26.88           O  
HETATM 4267  O   HOH B 534     -32.595  28.204 -58.884  1.00 46.01           O  
HETATM 4268  O   HOH B 535     -38.273  45.234 -58.202  1.00 63.47           O  
HETATM 4269  O   HOH B 536     -25.591  18.086 -40.498  1.00 66.81           O  
HETATM 4270  O   HOH B 537     -46.133  25.457 -52.073  1.00 48.16           O  
HETATM 4271  O   HOH B 538     -32.669  30.576 -59.934  1.00 38.34           O  
HETATM 4272  O   HOH B 539     -44.126  28.710 -40.462  1.00 44.92           O  
HETATM 4273  O   HOH B 540     -46.879  16.891 -51.838  1.00 67.26           O  
HETATM 4274  O   HOH B 541     -25.671  45.766 -47.524  1.00 44.12           O  
HETATM 4275  O   HOH B 542     -43.025  33.505 -34.438  1.00 62.06           O  
HETATM 4276  O   HOH B 543     -41.586  19.601 -47.042  1.00 53.81           O  
HETATM 4277  O   HOH B 544     -39.289  39.885 -39.218  1.00 37.18           O  
HETATM 4278  O   HOH B 545     -38.007  26.874 -63.519  1.00 46.37           O  
HETATM 4279  O   HOH B 546     -41.652  33.026 -36.967  1.00 45.19           O  
HETATM 4280  O   HOH B 547     -31.482  21.560 -37.288  1.00 36.99           O  
HETATM 4281  O   HOH B 548     -30.512  23.729 -31.311  1.00 76.36           O  
HETATM 4282  O   HOH B 549     -42.829  31.965 -58.720  1.00 39.96           O  
HETATM 4283  O   HOH B 550     -37.626  16.857 -41.649  1.00 55.36           O  
HETATM 4284  O   HOH B 551     -35.112  27.306 -35.774  1.00 38.69           O  
HETATM 4285  O   HOH B 552     -32.370  40.503 -54.507  1.00 31.78           O  
HETATM 4286  O   HOH B 553     -45.809  27.748 -44.828  1.00 46.81           O  
HETATM 4287  O   HOH B 554     -36.695  48.532 -51.268  1.00 59.76           O  
HETATM 4288  O   HOH B 555     -23.306  45.499 -39.854  1.00 52.62           O  
HETATM 4289  O   HOH B 556     -25.641  38.155 -38.137  1.00 57.33           O  
HETATM 4290  O   HOH B 557     -25.495  31.316 -38.754  1.00 35.30           O  
HETATM 4291  O   HOH B 558     -42.348  37.925 -41.883  1.00 42.79           O  
HETATM 4292  O   HOH B 559     -30.389  19.140 -43.684  1.00 51.18           O  
HETATM 4293  O   HOH B 560     -29.300  43.141 -56.256  1.00 52.16           O  
HETATM 4294  O   HOH B 561     -36.992  32.231 -29.984  1.00 53.10           O  
HETATM 4295  O   HOH B 562     -38.075  32.343 -58.851  1.00 37.56           O  
HETATM 4296  O   HOH B 563     -47.024  37.436 -43.776  1.00 53.62           O  
HETATM 4297  O   HOH B 564     -42.091  19.747 -61.637  1.00 54.59           O  
HETATM 4298  O   HOH B 565     -46.962  25.729 -46.194  1.00 55.72           O  
HETATM 4299  O   HOH B 566     -28.401  47.636 -52.555  1.00 67.42           O  
HETATM 4300  O   HOH B 567     -24.307  39.692 -51.345  1.00 34.00           O  
HETATM 4301  O   HOH B 568     -36.336  49.505 -43.636  1.00 63.95           O  
HETATM 4302  O   HOH B 569     -35.510  24.140 -60.702  1.00 54.26           O  
HETATM 4303  O   HOH B 570     -24.241  34.104 -37.831  1.00 64.03           O  
HETATM 4304  O   HOH B 571     -22.016  32.552 -30.377  1.00 74.18           O  
HETATM 4305  O   HOH B 572     -32.303  40.475 -57.014  1.00 40.56           O  
HETATM 4306  O   HOH B 573     -36.542  24.751 -36.440  1.00 44.99           O  
HETATM 4307  O   HOH B 574     -29.315  40.657 -58.568  1.00 66.72           O  
HETATM 4308  O   HOH B 575     -43.627  32.134 -38.376  1.00 42.86           O  
HETATM 4309  O   HOH B 576     -23.587  44.170 -47.179  1.00 68.56           O  
HETATM 4310  O   HOH B 577     -37.078  29.877 -60.490  1.00 43.86           O  
HETATM 4311  O   HOH B 578     -42.919  31.097 -41.011  1.00 44.63           O  
HETATM 4312  O   HOH B 579     -34.234  22.900 -35.524  1.00 53.32           O  
HETATM 4313  O   HOH B 580     -46.540  28.322 -36.976  1.00 55.83           O  
HETATM 4314  O   HOH B 581     -43.964  32.281 -43.103  1.00 43.85           O  
HETATM 4315  O   HOH B 582     -33.611   9.013 -56.126  1.00 68.33           O  
HETATM 4316  O   HOH B 583     -44.474  36.898 -43.159  1.00 41.50           O  
HETATM 4317  O   HOH B 584     -40.784  32.967 -27.256  1.00 64.17           O  
HETATM 4318  O   HOH B 585     -33.671  24.425 -29.898  1.00 54.85           O  
HETATM 4319  O   HOH B 586     -44.349  34.592 -42.364  1.00 42.27           O  
HETATM 4320  O   HOH B 587     -46.409  43.527 -51.815  1.00 78.80           O  
HETATM 4321  O  AHOH B 588     -36.365  20.190 -55.931  0.50 44.38           O  
HETATM 4322  O  BHOH B 588     -36.871  19.545 -53.722  0.50 50.46           O  
HETATM 4323  O   HOH B 589     -32.837  26.901 -34.162  1.00 47.01           O  
HETATM 4324  O   HOH B 590     -40.141  32.900 -60.065  1.00 39.84           O  
HETATM 4325  O   HOH B 591     -25.894  46.552 -50.034  1.00 49.21           O  
HETATM 4326  O   HOH B 592     -48.546  28.230 -39.618  1.00 61.99           O  
HETATM 4327  O   HOH B 593     -20.691  30.964 -41.487  1.00 71.11           O  
HETATM 4328  O   HOH B 594     -29.860  15.877 -56.429  1.00 61.16           O  
HETATM 4329  O   HOH B 595     -39.784  17.795 -51.136  1.00 57.90           O  
HETATM 4330  O   HOH B 596     -48.808  47.630 -51.792  1.00 61.39           O  
HETATM 4331  O   HOH B 597     -43.937  40.438 -56.384  1.00 71.24           O  
HETATM 4332  O   HOH B 598     -26.118  43.380 -53.292  1.00 66.14           O  
HETATM 4333  O   HOH B 599     -34.746  30.101 -61.554  1.00 58.61           O  
HETATM 4334  O   HOH B 600     -45.885  39.172 -39.445  1.00 55.68           O  
HETATM 4335  O   HOH B 601     -38.513  30.003 -62.800  1.00 57.74           O  
HETATM 4336  O   HOH B 602     -27.413  23.493 -25.398  1.00 74.24           O  
HETATM 4337  O   HOH B 603     -31.333  26.673 -60.913  1.00 40.39           O  
HETATM 4338  O   HOH B 604     -24.821  42.036 -51.288  1.00 49.70           O  
HETATM 4339  O   HOH B 605     -48.515  37.921 -41.766  1.00 58.09           O  
HETATM 4340  O   HOH B 606     -48.718  45.060 -52.007  1.00 65.12           O  
HETATM 4341  O   HOH B 607     -40.217  18.500 -56.763  1.00 64.35           O  
HETATM 4342  O   HOH B 608     -48.636  32.197 -38.421  1.00 67.84           O  
HETATM 4343  O   HOH C1101     -35.654  52.962 -63.967  1.00 61.77           O  
HETATM 4344  O   HOH C1102     -38.914  34.481 -95.407  1.00 65.29           O  
HETATM 4345  O   HOH C1103     -22.490  42.021 -88.341  1.00 40.18           O  
HETATM 4346  O   HOH C1104     -31.593  51.705 -94.068  1.00 75.48           O  
HETATM 4347  O   HOH C1105     -26.793  35.707 -58.655  1.00 61.35           O  
HETATM 4348  O   HOH C1106     -39.054  47.415 -97.394  1.00 64.09           O  
HETATM 4349  O   HOH C1107     -30.401  55.649 -73.720  1.00 45.78           O  
HETATM 4350  O   HOH C1108     -33.687  33.402 -61.631  1.00 38.11           O  
HETATM 4351  O   HOH C1109     -24.963  37.223 -93.071  1.00 52.64           O  
HETATM 4352  O   HOH C1110     -37.733  29.827 -69.760  1.00 66.31           O  
HETATM 4353  O   HOH C1111     -23.337  43.859 -67.221  1.00 43.66           O  
HETATM 4354  O   HOH C1112     -17.583  43.765 -90.479  1.00 53.02           O  
HETATM 4355  O   HOH C1113     -20.243  39.571 -61.768  1.00 57.02           O  
HETATM 4356  O   HOH C1114     -27.129  62.854 -60.396  1.00 69.35           O  
HETATM 4357  O   HOH C1115     -30.324  41.079 -62.078  1.00 43.13           O  
HETATM 4358  O   HOH C1116     -31.375  48.804 -92.133  1.00 40.37           O  
HETATM 4359  O   HOH C1117     -35.681  36.918 -74.644  1.00 44.72           O  
HETATM 4360  O   HOH C1118     -20.674  39.034 -85.195  1.00 48.97           O  
HETATM 4361  O   HOH C1119     -23.066  33.674 -75.758  1.00 50.15           O  
HETATM 4362  O   HOH C1120     -30.585  57.682 -66.908  1.00 53.61           O  
HETATM 4363  O   HOH C1121     -21.858  52.331 -73.209  1.00 42.60           O  
HETATM 4364  O   HOH C1122     -38.277  32.112 -66.661  1.00 46.36           O  
HETATM 4365  O   HOH C1123     -21.334  49.849 -72.915  1.00 42.24           O  
HETATM 4366  O   HOH C1124     -24.248  43.732 -92.720  1.00 58.11           O  
HETATM 4367  O   HOH C1125     -37.428  49.766 -77.661  1.00 40.05           O  
HETATM 4368  O   HOH C1126     -34.159  32.113 -78.031  1.00 45.68           O  
HETATM 4369  O   HOH C1127     -43.848  45.760 -81.511  1.00 52.79           O  
HETATM 4370  O   HOH C1128     -38.908  38.289 -62.813  1.00 44.88           O  
HETATM 4371  O   HOH C1129     -33.208  55.203 -66.561  1.00 58.84           O  
HETATM 4372  O   HOH C1130     -19.473  34.973 -84.439  1.00 65.73           O  
HETATM 4373  O   HOH C1131     -43.597  48.766 -73.123  1.00 60.24           O  
HETATM 4374  O   HOH C1132     -33.397  54.402 -83.799  1.00 50.31           O  
HETATM 4375  O   HOH C1133     -20.985  44.071 -88.032  1.00 38.55           O  
HETATM 4376  O   HOH C1134     -41.166  35.553 -78.387  1.00 52.22           O  
HETATM 4377  O   HOH C1135     -24.561  45.932 -68.837  1.00 36.65           O  
HETATM 4378  O   HOH C1136     -33.042  34.554 -76.671  1.00 32.25           O  
HETATM 4379  O   HOH C1137     -35.744  45.341 -69.712  1.00 46.26           O  
HETATM 4380  O   HOH C1138     -15.255  39.091 -79.377  1.00 59.57           O  
HETATM 4381  O   HOH C1139     -19.671  41.786 -81.733  1.00 45.63           O  
HETATM 4382  O   HOH C1140     -24.637  33.170 -80.498  1.00 45.90           O  
HETATM 4383  O   HOH C1141     -19.068  38.137 -67.330  1.00 48.38           O  
HETATM 4384  O   HOH C1142     -24.769  55.990 -61.206  1.00 56.18           O  
HETATM 4385  O   HOH C1143     -19.270  36.426 -75.142  1.00 48.83           O  
HETATM 4386  O   HOH C1144     -19.058  45.453 -94.040  1.00 45.47           O  
HETATM 4387  O   HOH C1145     -19.534  49.372 -83.659  1.00 48.67           O  
HETATM 4388  O   HOH C1146     -22.225  39.771 -74.263  1.00 51.11           O  
HETATM 4389  O   HOH C1147     -30.590  33.206 -67.140  1.00 31.19           O  
HETATM 4390  O   HOH C1148     -33.968  50.368 -92.233  1.00 39.26           O  
HETATM 4391  O   HOH C1149     -25.338  31.989 -76.026  1.00 51.41           O  
HETATM 4392  O   HOH C1150     -45.037  42.668 -86.948  1.00 57.24           O  
HETATM 4393  O   HOH C1151     -35.581  29.442 -66.361  1.00 54.98           O  
HETATM 4394  O   HOH C1152     -26.998  53.743 -87.587  1.00 38.38           O  
HETATM 4395  O   HOH C1153     -27.670  26.358 -78.880  1.00 53.88           O  
HETATM 4396  O   HOH C1154     -28.788  50.657 -94.488  1.00 41.87           O  
HETATM 4397  O   HOH C1155     -30.059  49.170 -58.997  1.00 62.90           O  
HETATM 4398  O   HOH C1156     -40.999  37.671 -69.353  1.00 50.00           O  
HETATM 4399  O   HOH C1157     -18.859  37.126 -81.808  1.00 40.70           O  
HETATM 4400  O   HOH C1158     -40.170  36.322 -66.480  1.00 43.28           O  
HETATM 4401  O   HOH C1159     -27.768  31.824 -74.071  1.00 36.82           O  
HETATM 4402  O   HOH C1160     -26.799  63.663 -64.248  1.00 56.72           O  
HETATM 4403  O   HOH C1161     -19.536  53.212 -74.454  1.00 67.94           O  
HETATM 4404  O   HOH C1162     -18.281  39.459 -71.232  1.00 58.87           O  
HETATM 4405  O   HOH C1163     -24.331  35.006 -65.877  1.00 51.71           O  
HETATM 4406  O   HOH C1164     -27.330  28.650 -71.398  1.00 69.93           O  
HETATM 4407  O   HOH C1165     -21.828  39.500 -87.175  1.00 42.53           O  
HETATM 4408  O   HOH C1166     -22.563  36.766 -91.375  1.00 58.37           O  
HETATM 4409  O   HOH C1167     -41.926  46.063 -93.976  1.00 60.28           O  
HETATM 4410  O   HOH C1168     -20.018  44.555 -83.724  1.00 54.74           O  
HETATM 4411  O   HOH C1169     -28.945  54.233 -59.282  1.00 59.66           O  
HETATM 4412  O   HOH C1170     -27.082  33.025 -63.760  1.00 57.49           O  
HETATM 4413  O   HOH C1171     -33.010  29.335 -67.300  1.00 51.76           O  
HETATM 4414  O   HOH C1172     -47.108  44.207 -79.799  1.00 63.53           O  
HETATM 4415  O   HOH C1173     -43.965  46.467 -84.188  1.00 53.46           O  
HETATM 4416  O   HOH C1174     -27.330  52.608 -94.847  1.00 44.38           O  
HETATM 4417  O   HOH C1175     -44.329  44.925 -74.125  1.00 75.33           O  
HETATM 4418  O   HOH C1176     -15.996  38.680 -73.010  1.00 49.18           O  
HETATM 4419  O   HOH C1177     -39.202  44.174 -64.457  1.00 57.74           O  
HETATM 4420  O   HOH C1178     -36.142  41.848 -69.792  1.00 39.51           O  
HETATM 4421  O   HOH C1179     -21.364  58.717 -64.956  1.00 61.02           O  
HETATM 4422  O   HOH C1180     -18.934  43.704 -86.007  1.00 43.27           O  
HETATM 4423  O   HOH C1181     -34.022  32.470 -64.360  1.00 38.16           O  
HETATM 4424  O   HOH C1182     -27.705  63.624 -68.680  1.00 64.71           O  
HETATM 4425  O   HOH C1183     -19.501  46.738 -75.587  1.00 63.19           O  
HETATM 4426  O  AHOH C1184     -29.388  62.241 -71.166  0.50 29.92           O  
HETATM 4427  O  BHOH C1184     -27.625  61.777 -70.620  0.50 28.80           O  
HETATM 4428  O   HOH C1185     -20.804  43.425 -93.430  1.00 44.43           O  
HETATM 4429  O   HOH C1186     -26.738  24.669 -75.201  1.00 47.23           O  
HETATM 4430  O   HOH C1187     -28.114  32.744 -66.977  1.00 68.67           O  
HETATM 4431  O   HOH C1188     -34.459  44.473 -63.354  1.00 55.01           O  
HETATM 4432  O   HOH C1189     -18.318  46.947 -83.054  1.00 49.19           O  
HETATM 4433  O   HOH C1190     -15.666  44.185 -88.832  1.00 50.91           O  
HETATM 4434  O   HOH C1191     -29.119  64.698 -67.155  1.00 65.67           O  
HETATM 4435  O   HOH C1192     -17.661  34.730 -81.617  1.00 66.46           O  
HETATM 4436  O   HOH C1193     -36.598  31.320 -64.873  1.00 49.02           O  
HETATM 4437  O   HOH C1194     -16.376  39.725 -81.897  1.00 74.93           O  
HETATM 4438  O   HOH C1195     -18.220  41.141 -89.039  1.00 61.13           O  
HETATM 4439  O   HOH C1196     -20.942  37.602 -89.243  1.00 55.37           O  
HETATM 4440  O   HOH C1197     -30.622  48.825 -94.895  1.00 59.36           O  
HETATM 4441  O   HOH C1198     -29.666  23.281 -77.655  1.00 63.60           O  
HETATM 4442  O   HOH G1001     -40.798  50.256 -70.695  1.00 65.79           O  
HETATM 4443  O   HOH G1002     -39.205  39.512 -72.730  1.00 67.57           O  
HETATM 4444  O   HOH G1003     -34.151  53.176 -78.832  1.00 54.10           O  
HETATM 4445  O   HOH D1101     -17.400   8.149 -89.394  1.00 61.51           O  
HETATM 4446  O   HOH D1102     -41.610  32.336 -85.645  1.00 60.04           O  
HETATM 4447  O   HOH D1103     -32.163  22.707 -82.305  1.00 41.49           O  
HETATM 4448  O   HOH D1104     -35.996  22.305 -82.571  1.00 48.84           O  
HETATM 4449  O   HOH D1105     -16.656   9.615 -86.890  1.00 63.53           O  
HETATM 4450  O   HOH D1106     -26.776   7.497 -84.322  1.00 45.51           O  
HETATM 4451  O   HOH D1107     -36.287  11.814 -94.366  1.00 50.84           O  
HETATM 4452  O   HOH D1108     -34.875  12.845-107.347  1.00 33.55           O  
HETATM 4453  O   HOH D1109     -18.167  21.791 -86.595  1.00 38.75           O  
HETATM 4454  O   HOH D1110     -43.333  18.302 -94.067  1.00 59.32           O  
HETATM 4455  O   HOH D1111     -36.971  19.009 -77.854  1.00 66.15           O  
HETATM 4456  O   HOH D1112     -40.993  12.143-110.853  1.00 62.40           O  
HETATM 4457  O   HOH D1113     -20.604  30.771 -85.783  1.00 50.50           O  
HETATM 4458  O   HOH D1114     -35.779  18.500-111.750  1.00 33.37           O  
HETATM 4459  O   HOH D1115     -33.137  19.290-112.239  1.00 31.69           O  
HETATM 4460  O   HOH D1116     -39.912  18.408 -90.572  1.00 41.53           O  
HETATM 4461  O   HOH D1117     -18.680   7.664-101.211  1.00 49.56           O  
HETATM 4462  O   HOH D1118     -24.842  20.546 -81.956  1.00 44.91           O  
HETATM 4463  O   HOH D1119     -31.820  19.868 -81.012  1.00 37.98           O  
HETATM 4464  O   HOH D1120     -38.365  20.979-105.498  1.00 55.35           O  
HETATM 4465  O   HOH D1121     -15.754  15.108 -90.703  1.00 53.03           O  
HETATM 4466  O   HOH D1122     -33.974  12.447 -95.881  1.00 40.29           O  
HETATM 4467  O   HOH D1123     -40.485  17.889 -93.048  1.00 39.14           O  
HETATM 4468  O   HOH D1124      -4.350  20.687 -97.488  1.00 63.71           O  
HETATM 4469  O   HOH D1125     -35.024  14.221-102.233  1.00 30.11           O  
HETATM 4470  O   HOH D1126     -38.736  29.244 -96.633  1.00 52.77           O  
HETATM 4471  O   HOH D1127     -42.504  22.569 -98.888  1.00 56.29           O  
HETATM 4472  O   HOH D1128     -21.761  29.746 -94.508  1.00 34.97           O  
HETATM 4473  O   HOH D1129     -22.760  29.566 -84.755  1.00 35.61           O  
HETATM 4474  O   HOH D1130     -38.216  25.436 -83.709  1.00 62.42           O  
HETATM 4475  O   HOH D1131     -28.853  21.634-107.516  1.00 38.41           O  
HETATM 4476  O  AHOH D1132     -37.273  25.912-104.411  0.50 48.69           O  
HETATM 4477  O  BHOH D1132     -37.168  27.488-102.802  0.50 31.41           O  
HETATM 4478  O   HOH D1133     -24.596   8.602 -96.942  1.00 35.07           O  
HETATM 4479  O   HOH D1134     -28.279  13.634 -82.117  1.00 43.46           O  
HETATM 4480  O   HOH D1135     -20.510   9.094 -88.150  1.00 41.08           O  
HETATM 4481  O   HOH D1136     -35.796  11.917 -88.689  1.00 51.33           O  
HETATM 4482  O   HOH D1137     -38.143  19.015-108.581  1.00 45.51           O  
HETATM 4483  O   HOH D1138     -42.462  27.388 -97.927  1.00 51.03           O  
HETATM 4484  O   HOH D1139     -11.928  27.957 -94.634  1.00 52.36           O  
HETATM 4485  O   HOH D1140     -36.182  21.879-110.229  1.00 41.47           O  
HETATM 4486  O   HOH D1141     -32.281  22.681-104.739  1.00 37.61           O  
HETATM 4487  O   HOH D1142     -31.807  19.501 -77.255  1.00 49.59           O  
HETATM 4488  O   HOH D1143     -41.627  16.443 -87.483  1.00 45.48           O  
HETATM 4489  O   HOH D1144     -29.582  24.593 -81.479  1.00 60.58           O  
HETATM 4490  O   HOH D1145     -17.202  30.459 -89.882  1.00 45.87           O  
HETATM 4491  O   HOH D1146     -40.145  17.380-104.393  1.00 36.70           O  
HETATM 4492  O   HOH D1147     -34.785  22.060-103.858  1.00 29.69           O  
HETATM 4493  O   HOH D1148     -26.851  18.837 -81.935  1.00 44.59           O  
HETATM 4494  O   HOH D1149     -19.981  35.710 -92.808  1.00 61.66           O  
HETATM 4495  O   HOH D1150     -19.292  28.247 -84.895  1.00 47.65           O  
HETATM 4496  O   HOH D1151     -40.446  26.939 -85.175  1.00 64.35           O  
HETATM 4497  O   HOH D1152     -39.505  22.422 -86.729  1.00 59.47           O  
HETATM 4498  O   HOH D1153     -42.405  37.616 -92.628  1.00 75.89           O  
HETATM 4499  O   HOH D1154     -39.288  28.101-111.174  1.00 66.24           O  
HETATM 4500  O   HOH D1155     -12.483  16.074-101.194  1.00 55.88           O  
HETATM 4501  O   HOH D1156     -17.828  27.588-104.651  1.00 60.24           O  
HETATM 4502  O   HOH D1157     -19.802   5.123 -99.918  1.00 57.70           O  
HETATM 4503  O   HOH D1158     -29.251  19.551 -80.302  1.00 48.73           O  
HETATM 4504  O   HOH D1159     -17.533  23.262 -81.943  1.00 59.67           O  
HETATM 4505  O   HOH D1160     -34.087  24.344-111.344  1.00 52.65           O  
HETATM 4506  O   HOH D1161     -43.613  25.154 -98.566  1.00 57.85           O  
HETATM 4507  O   HOH D1162     -20.728  36.967 -96.965  1.00 61.57           O  
HETATM 4508  O   HOH D1163     -22.324  26.170-106.998  1.00 55.09           O  
HETATM 4509  O   HOH D1164     -32.218  25.128-106.109  1.00 51.52           O  
HETATM 4510  O   HOH D1165     -23.393  18.018-106.934  1.00 57.74           O  
HETATM 4511  O   HOH D1166     -36.505  23.888-104.898  1.00 53.77           O  
HETATM 4512  O  AHOH D1167     -35.464  12.454-104.497  0.50 19.97           O  
HETATM 4513  O  BHOH D1167     -33.769  10.755-104.346  0.50 38.66           O  
HETATM 4514  O   HOH D1168     -40.447  11.986-100.350  1.00 55.95           O  
HETATM 4515  O   HOH D1169     -33.246  25.069 -79.145  1.00 59.09           O  
HETATM 4516  O   HOH D1170     -32.913  25.664-109.022  1.00 68.88           O  
HETATM 4517  O   HOH D1171     -41.607  20.759 -87.548  1.00 77.92           O  
HETATM 4518  O   HOH D1172     -24.155  12.640 -81.457  1.00 48.93           O  
HETATM 4519  O   HOH D1173     -37.472  20.861 -79.324  1.00 62.33           O  
HETATM 4520  O   HOH D1174     -43.982  20.742 -98.551  1.00 62.57           O  
HETATM 4521  O   HOH D1175     -41.696  29.736 -84.043  1.00 62.62           O  
HETATM 4522  O   HOH D1176     -38.426  22.482 -84.312  1.00 68.48           O  
HETATM 4523  O   HOH D1177     -41.585  16.085-109.007  1.00 58.33           O  
HETATM 4524  O   HOH D1178     -15.365  20.973 -78.953  1.00 65.89           O  
HETATM 4525  O   HOH D1179     -41.812  18.760 -89.034  1.00 47.54           O  
HETATM 4526  O   HOH D1180     -14.927  29.031 -90.202  1.00 49.74           O  
HETATM 4527  O   HOH H1101     -31.047  13.805-101.102  1.00 48.03           O  
HETATM 4528  O   HOH H1102     -28.126  16.440-100.703  1.00 28.86           O  
HETATM 4529  O   HOH H1103     -33.271  13.630-100.342  1.00 42.88           O  
HETATM 4530  O   HOH H1104     -22.730  23.123-105.616  1.00 63.95           O  
HETATM 4531  O   HOH H1105     -21.084  24.876-102.268  1.00 46.22           O  
HETATM 4532  O   HOH H1106     -25.567  11.121-106.570  1.00 44.74           O  
HETATM 4533  O   HOH H1107     -23.274  15.154-106.400  1.00 50.70           O  
HETATM 4534  O   HOH H1108     -17.864  16.474-107.294  1.00 66.59           O  
HETATM 4535  O   HOH H1109     -35.774   7.189-100.442  1.00 76.14           O  
CONECT  990  994                                                                
CONECT  994  990  995                                                           
CONECT  995  994  996  998                                                      
CONECT  996  995  997 1010                                                      
CONECT  997  996                                                                
CONECT  998  995  999                                                           
CONECT  999  998 1000 1001                                                      
CONECT 1000  999 1002                                                           
CONECT 1001  999 1003                                                           
CONECT 1002 1000 1004                                                           
CONECT 1003 1001 1004                                                           
CONECT 1004 1002 1003 1005                                                      
CONECT 1005 1004 1006                                                           
CONECT 1006 1005 1007 1008 1009                                                 
CONECT 1007 1006                                                                
CONECT 1008 1006                                                                
CONECT 1009 1006                                                                
CONECT 1010  996                                                                
CONECT 2993 2997                                                                
CONECT 2997 2993 2998                                                           
CONECT 2998 2997 2999 3001                                                      
CONECT 2999 2998 3000 3013                                                      
CONECT 3000 2999                                                                
CONECT 3001 2998 3002                                                           
CONECT 3002 3001 3003 3004                                                      
CONECT 3003 3002 3005                                                           
CONECT 3004 3002 3006                                                           
CONECT 3005 3003 3007                                                           
CONECT 3006 3004 3007                                                           
CONECT 3007 3005 3006 3008                                                      
CONECT 3008 3007 3009                                                           
CONECT 3009 3008 3010 3011 3012                                                 
CONECT 3010 3009                                                                
CONECT 3011 3009                                                                
CONECT 3012 3009                                                                
CONECT 3013 2999                                                                
CONECT 4006 4010                                                                
CONECT 4010 4006 4011                                                           
CONECT 4011 4010 4012 4014                                                      
CONECT 4012 4011 4013 4026                                                      
CONECT 4013 4012                                                                
CONECT 4014 4011 4015                                                           
CONECT 4015 4014 4016 4017                                                      
CONECT 4016 4015 4018                                                           
CONECT 4017 4015 4019                                                           
CONECT 4018 4016 4020                                                           
CONECT 4019 4017 4020                                                           
CONECT 4020 4018 4019 4021                                                      
CONECT 4021 4020 4022                                                           
CONECT 4022 4021 4023 4024 4025                                                 
CONECT 4023 4022                                                                
CONECT 4024 4022                                                                
CONECT 4025 4022                                                                
CONECT 4026 4012                                                                
CONECT 4058 4059 4060 4061 4062                                                 
CONECT 4059 4058                                                                
CONECT 4060 4058                                                                
CONECT 4061 4058                                                                
CONECT 4062 4058                                                                
CONECT 4063 4064 4065 4066 4067                                                 
CONECT 4064 4063                                                                
CONECT 4065 4063                                                                
CONECT 4066 4063                                                                
CONECT 4067 4063                                                                
CONECT 4068 4069 4070 4071 4072                                                 
CONECT 4069 4068                                                                
CONECT 4070 4068                                                                
CONECT 4071 4068                                                                
CONECT 4072 4068                                                                
CONECT 4073 4074 4075 4076 4077                                                 
CONECT 4074 4073                                                                
CONECT 4075 4073                                                                
CONECT 4076 4073                                                                
CONECT 4077 4073                                                                
CONECT 4078 4079 4080 4081 4082                                                 
CONECT 4079 4078                                                                
CONECT 4080 4078                                                                
CONECT 4081 4078                                                                
CONECT 4082 4078                                                                
CONECT 4083 4084 4085 4086 4087                                                 
CONECT 4084 4083                                                                
CONECT 4085 4083                                                                
CONECT 4086 4083                                                                
CONECT 4087 4083                                                                
MASTER      731    0    9   16   20    0   21    6 4481    7   84   43          
END                                                                             



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