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***  OXIDOREDUCTASE 08-NOV-18 6N1F  ***

elNémo ID: 210812113332114885

Job options:

ID        	=	 210812113332114885
JOBID     	=	 OXIDOREDUCTASE 08-NOV-18 6N1F
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    OXIDOREDUCTASE                          08-NOV-18   6N1F              
TITLE     CRYSTAL STRUCTURE OF OXIDOREDUCTASE, 2OG-FE(II) OXYGENASE FAMILY, FROM
TITLE    2 BURKHOLDERIA PSEUDOMALLEI                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OXIDOREDUCTASE, 2OG-FE(II) OXYGENASE FAMILY;               
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI;                      
SOURCE   3 ORGANISM_TAXID: 320372;                                              
SOURCE   4 STRAIN: 1710B;                                                       
SOURCE   5 GENE: BURPS1710B_A2398;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: BUPSA.17629.A.A1                          
KEYWDS    SSGCID, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR   
KEYWDS   2 INFECTIOUS DISEASE, OXIDOREDUCTASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)    
REVDAT   1   19-DEC-18 6N1F    0                                                
JRNL        AUTH   J.ABENDROTH,P.S.HORANYI,D.LORIMER,T.E.EDWARDS                
JRNL        TITL   CRYSTAL STRUCTURE OF OXIDOREDUCTASE, 2OG-FE(II) OXYGENASE    
JRNL        TITL 2 FAMILY, FROM BURKHOLDERIA PSEUDOMALLEI                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_3304)                                    
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) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.35                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.980                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 59870                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.380                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2024                            
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 27.3530 -  4.9319    0.93     4003   139  0.1904 0.1760        
REMARK   3     2  4.9319 -  3.9183    0.97     4143   124  0.1541 0.1692        
REMARK   3     3  3.9183 -  3.4240    0.97     4142   192  0.1858 0.2171        
REMARK   3     4  3.4240 -  3.1114    0.97     4202   129  0.2055 0.2489        
REMARK   3     5  3.1114 -  2.8887    0.97     4202   127  0.2211 0.2720        
REMARK   3     6  2.8887 -  2.7185    0.98     4189   154  0.2424 0.2886        
REMARK   3     7  2.7185 -  2.5825    0.98     4182   164  0.2395 0.2888        
REMARK   3     8  2.5825 -  2.4702    0.98     4153   149  0.2420 0.2819        
REMARK   3     9  2.4702 -  2.3751    0.98     4208   130  0.2373 0.2913        
REMARK   3    10  2.3751 -  2.2932    0.98     4185   161  0.2446 0.3051        
REMARK   3    11  2.2932 -  2.2215    0.97     4166   149  0.2382 0.3101        
REMARK   3    12  2.2215 -  2.1581    0.97     4174   134  0.2473 0.2949        
REMARK   3    13  2.1581 -  2.1013    0.97     4179   146  0.2576 0.2800        
REMARK   3    14  2.1013 -  2.0500    0.87     3718   126  0.2632 0.2981        
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)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.510           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.44                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.04                          
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      :  0.006           6626                                  
REMARK   3   ANGLE     :  0.859           8993                                  
REMARK   3   CHIRALITY :  0.052            978                                  
REMARK   3   PLANARITY :  0.004           1206                                  
REMARK   3   DIHEDRAL  : 13.274           3935                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 31                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 16 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.6259  10.3530  41.9165              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2111 T22:   0.2351                                     
REMARK   3      T33:   0.2290 T12:   0.0055                                     
REMARK   3      T13:   0.0107 T23:  -0.0289                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9399 L22:   8.3683                                     
REMARK   3      L33:   4.2165 L12:   2.1422                                     
REMARK   3      L13:   0.5748 L23:   1.9192                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1726 S12:  -0.2562 S13:   0.2533                       
REMARK   3      S21:   0.1112 S22:   0.0795 S23:   0.4452                       
REMARK   3      S31:  -0.1093 S32:   0.2293 S33:   0.1167                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 17 THROUGH 50 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -14.2922   3.4171  43.9761              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2249 T22:   0.1041                                     
REMARK   3      T33:   0.2541 T12:  -0.0067                                     
REMARK   3      T13:  -0.0082 T23:  -0.0185                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4969 L22:   3.2267                                     
REMARK   3      L33:   3.2399 L12:   1.0271                                     
REMARK   3      L13:  -0.2504 L23:   0.9242                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0451 S12:   0.1607 S13:  -0.0291                       
REMARK   3      S21:   0.3896 S22:  -0.0847 S23:   0.2917                       
REMARK   3      S31:   0.1241 S32:  -0.0921 S33:   0.1035                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 51 THROUGH 76 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -27.0527  14.3226  55.8109              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4756 T22:   0.3048                                     
REMARK   3      T33:   0.6345 T12:  -0.0233                                     
REMARK   3      T13:   0.2338 T23:  -0.0907                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4360 L22:   5.7106                                     
REMARK   3      L33:   2.4991 L12:   1.0018                                     
REMARK   3      L13:  -0.0054 L23:  -2.0327                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0717 S12:  -0.1504 S13:   0.2487                       
REMARK   3      S21:   1.3852 S22:   0.0053 S23:   1.0528                       
REMARK   3      S31:  -0.0660 S32:  -0.3038 S33:   0.0245                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 77 THROUGH 144 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -17.5211   5.4981  55.5291              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4539 T22:   0.2332                                     
REMARK   3      T33:   0.2597 T12:  -0.0723                                     
REMARK   3      T13:   0.0422 T23:  -0.0179                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1816 L22:   3.9207                                     
REMARK   3      L33:   1.6884 L12:  -0.6389                                     
REMARK   3      L13:  -0.0738 L23:   0.4142                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0170 S12:  -0.1599 S13:   0.0883                       
REMARK   3      S21:   0.8068 S22:  -0.1156 S23:   0.2242                       
REMARK   3      S31:   0.2790 S32:  -0.1115 S33:   0.1347                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 145 THROUGH 159 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -15.5714  13.0715  44.3902              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2622 T22:   0.2541                                     
REMARK   3      T33:   0.2399 T12:  -0.0157                                     
REMARK   3      T13:  -0.0652 T23:  -0.0367                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7435 L22:   5.0869                                     
REMARK   3      L33:   2.9023 L12:   1.9177                                     
REMARK   3      L13:   0.4244 L23:   2.3967                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2794 S12:   0.6216 S13:   0.5922                       
REMARK   3      S21:  -0.3646 S22:  -0.0385 S23:   0.0021                       
REMARK   3      S31:  -0.1671 S32:  -0.2268 S33:   0.1670                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 160 THROUGH 178 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.7079  15.3311  46.9608              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2162 T22:   0.2104                                     
REMARK   3      T33:   0.2423 T12:  -0.0314                                     
REMARK   3      T13:  -0.1361 T23:   0.0230                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1150 L22:   4.0285                                     
REMARK   3      L33:   2.4769 L12:   0.8156                                     
REMARK   3      L13:  -1.9102 L23:   0.9479                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1983 S12:  -0.4728 S13:  -0.2358                       
REMARK   3      S21:   0.4206 S22:  -0.0960 S23:  -0.5399                       
REMARK   3      S31:  -0.0383 S32:   0.2532 S33:   0.0268                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 179 THROUGH 190 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.7245  13.0520  53.3925              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3615 T22:   0.2989                                     
REMARK   3      T33:   0.2191 T12:  -0.0745                                     
REMARK   3      T13:  -0.0943 T23:   0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3824 L22:   3.9259                                     
REMARK   3      L33:   2.0871 L12:   0.4212                                     
REMARK   3      L13:  -0.4155 L23:   0.5656                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0020 S12:  -0.6717 S13:   0.2203                       
REMARK   3      S21:   1.2221 S22:  -0.1749 S23:   0.0446                       
REMARK   3      S31:   0.0374 S32:   0.3912 S33:   0.0827                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 191 THROUGH 216 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.3920  11.2744  55.7205              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3021 T22:   0.2017                                     
REMARK   3      T33:   0.2706 T12:  -0.0437                                     
REMARK   3      T13:   0.0315 T23:  -0.0492                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3513 L22:   4.9849                                     
REMARK   3      L33:   3.2469 L12:  -1.2825                                     
REMARK   3      L13:   1.2801 L23:  -0.6321                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0519 S12:  -0.2637 S13:   0.0096                       
REMARK   3      S21:   0.7539 S22:   0.0223 S23:   0.0673                       
REMARK   3      S31:   0.1829 S32:  -0.4911 S33:   0.0613                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 16 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -16.8916 -21.9106  41.8178              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1872 T22:   0.1453                                     
REMARK   3      T33:   0.2788 T12:  -0.0156                                     
REMARK   3      T13:  -0.0064 T23:  -0.0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7671 L22:   6.3716                                     
REMARK   3      L33:   3.4296 L12:   0.6182                                     
REMARK   3      L13:   0.0684 L23:  -1.2417                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0896 S12:   0.0388 S13:  -0.4198                       
REMARK   3      S21:  -0.0894 S22:   0.1683 S23:  -0.0251                       
REMARK   3      S31:  -0.0172 S32:  -0.1415 S33:  -0.1242                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 17 THROUGH 50 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -12.9210 -11.4797  33.5220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1738 T22:   0.1732                                     
REMARK   3      T33:   0.1985 T12:  -0.0145                                     
REMARK   3      T13:  -0.0337 T23:  -0.0348                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7070 L22:   2.6609                                     
REMARK   3      L33:   2.4596 L12:  -1.1049                                     
REMARK   3      L13:   0.5488 L23:  -2.0500                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0800 S12:   0.0339 S13:  -0.0001                       
REMARK   3      S21:   0.0014 S22:   0.0222 S23:   0.0176                       
REMARK   3      S31:  -0.0358 S32:  -0.1051 S33:   0.0313                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 51 THROUGH 109 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.4755 -13.0532  21.3362              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2014 T22:   0.3209                                     
REMARK   3      T33:   0.2407 T12:   0.0076                                     
REMARK   3      T13:   0.0069 T23:  -0.0340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1532 L22:   2.7929                                     
REMARK   3      L33:   2.9364 L12:  -0.5126                                     
REMARK   3      L13:  -0.0498 L23:   0.0438                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0968 S12:   0.4967 S13:  -0.0786                       
REMARK   3      S21:  -0.3709 S22:  -0.1312 S23:  -0.2080                       
REMARK   3      S31:   0.3045 S32:   0.1956 S33:  -0.0137                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 110 THROUGH 144 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.7897 -22.0734  24.7419              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2627 T22:   0.3363                                     
REMARK   3      T33:   0.2509 T12:   0.0624                                     
REMARK   3      T13:   0.0284 T23:  -0.0950                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4735 L22:   3.3697                                     
REMARK   3      L33:   2.0022 L12:   1.4912                                     
REMARK   3      L13:  -0.6679 L23:  -0.7915                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0898 S12:  -0.0191 S13:  -0.3620                       
REMARK   3      S21:  -0.3005 S22:  -0.0459 S23:  -0.3721                       
REMARK   3      S31:   0.3623 S32:   0.0818 S33:   0.1311                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 145 THROUGH 192 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -15.1358 -23.7106  31.2582              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1870 T22:   0.2172                                     
REMARK   3      T33:   0.2249 T12:  -0.0234                                     
REMARK   3      T13:  -0.0043 T23:  -0.0723                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8119 L22:   4.3926                                     
REMARK   3      L33:   3.4629 L12:   0.6868                                     
REMARK   3      L13:  -0.2966 L23:  -0.6531                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0265 S12:   0.3400 S13:  -0.3586                       
REMARK   3      S21:  -0.2624 S22:  -0.1048 S23:   0.1416                       
REMARK   3      S31:   0.4523 S32:  -0.1781 S33:   0.0312                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 193 THROUGH 214 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.7353 -19.5085  24.4347              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2337 T22:   0.2537                                     
REMARK   3      T33:   0.2103 T12:   0.0357                                     
REMARK   3      T13:   0.0251 T23:  -0.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2030 L22:   2.1241                                     
REMARK   3      L33:   3.5126 L12:  -0.0861                                     
REMARK   3      L13:  -0.0303 L23:  -0.5831                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0872 S12:   0.0806 S13:   0.2455                       
REMARK   3      S21:  -0.2670 S22:  -0.1054 S23:  -0.2016                       
REMARK   3      S31:   0.3634 S32:   0.1884 S33:   0.1426                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 3 THROUGH 37 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  18.8826  -4.4766  87.2359              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2078 T22:   0.1806                                     
REMARK   3      T33:   0.2907 T12:   0.0085                                     
REMARK   3      T13:   0.0683 T23:   0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0652 L22:   3.1062                                     
REMARK   3      L33:   1.6879 L12:  -0.8028                                     
REMARK   3      L13:   0.4152 L23:   0.5030                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0287 S12:   0.2000 S13:   0.0944                       
REMARK   3      S21:  -0.1989 S22:   0.0169 S23:  -0.3365                       
REMARK   3      S31:  -0.0224 S32:   0.0589 S33:   0.0091                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 38 THROUGH 50 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.0157  -1.3564  87.3809              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2212 T22:   0.3151                                     
REMARK   3      T33:   0.4243 T12:   0.0167                                     
REMARK   3      T13:  -0.0408 T23:  -0.0929                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3040 L22:   0.1936                                     
REMARK   3      L33:   0.9129 L12:  -1.0300                                     
REMARK   3      L13:   1.8631 L23:  -0.4027                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2084 S12:  -0.1677 S13:  -0.1066                       
REMARK   3      S21:  -0.5729 S22:  -0.2249 S23:   0.5094                       
REMARK   3      S31:  -0.3839 S32:  -0.6682 S33:   0.0498                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 51 THROUGH 71 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.8339 -15.6314  77.4441              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4434 T22:   0.4077                                     
REMARK   3      T33:   0.5415 T12:  -0.0321                                     
REMARK   3      T13:  -0.0790 T23:  -0.0969                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6794 L22:   8.1633                                     
REMARK   3      L33:   3.1103 L12:  -1.3827                                     
REMARK   3      L13:   1.3356 L23:  -1.4642                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2113 S12:  -0.1021 S13:  -0.3634                       
REMARK   3      S21:  -0.9406 S22:  -0.4721 S23:   1.1476                       
REMARK   3      S31:   0.4066 S32:  -0.3900 S33:   0.1670                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 72 THROUGH 144 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   5.4625  -3.7715  74.5521              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4440 T22:   0.2250                                     
REMARK   3      T33:   0.2322 T12:   0.0609                                     
REMARK   3      T13:   0.0072 T23:  -0.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5510 L22:   3.8151                                     
REMARK   3      L33:   1.3257 L12:   0.4738                                     
REMARK   3      L13:   0.2294 L23:   0.2816                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0327 S12:   0.1770 S13:  -0.0761                       
REMARK   3      S21:  -0.8119 S22:  -0.1374 S23:  -0.0162                       
REMARK   3      S31:  -0.1995 S32:  -0.1380 S33:   0.1501                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 145 THROUGH 159 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.9231 -10.9677  85.9288              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2615 T22:   0.2372                                     
REMARK   3      T33:   0.2391 T12:  -0.0315                                     
REMARK   3      T13:   0.0897 T23:  -0.0408                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2148 L22:   7.4119                                     
REMARK   3      L33:   1.3435 L12:  -0.5495                                     
REMARK   3      L13:   1.6116 L23:  -0.1739                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0643 S12:  -0.2627 S13:  -0.2828                       
REMARK   3      S21:   0.4022 S22:  -0.0704 S23:   0.1438                       
REMARK   3      S31:   0.1696 S32:  -0.2995 S33:   0.0765                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 160 THROUGH 178 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.0628 -13.7090  83.3557              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2125 T22:   0.2144                                     
REMARK   3      T33:   0.2108 T12:  -0.0156                                     
REMARK   3      T13:   0.0977 T23:   0.0165                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3543 L22:   5.3687                                     
REMARK   3      L33:   2.8536 L12:  -0.7492                                     
REMARK   3      L13:   2.3006 L23:   0.9024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1113 S12:   0.4440 S13:   0.1808                       
REMARK   3      S21:  -0.3692 S22:   0.1891 S23:  -0.3824                       
REMARK   3      S31:   0.2848 S32:   0.4530 S33:   0.0232                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 179 THROUGH 199 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.1980 -15.1936  82.0941              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2063 T22:   0.1385                                     
REMARK   3      T33:   0.1999 T12:   0.0131                                     
REMARK   3      T13:   0.0316 T23:  -0.0188                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8821 L22:   6.9786                                     
REMARK   3      L33:   3.6950 L12:   0.1043                                     
REMARK   3      L13:   1.1931 L23:   0.8729                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1309 S12:   0.0904 S13:  -0.2709                       
REMARK   3      S21:  -0.4189 S22:  -0.1779 S23:  -0.1704                       
REMARK   3      S31:   0.1610 S32:  -0.0257 S33:   0.0489                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 200 THROUGH 215 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.3031  -3.0949  68.5450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5196 T22:   0.2543                                     
REMARK   3      T33:   0.2892 T12:   0.0760                                     
REMARK   3      T13:  -0.0177 T23:  -0.0436                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9358 L22:   4.8877                                     
REMARK   3      L33:   4.3661 L12:   1.9045                                     
REMARK   3      L13:  -0.9399 L23:   0.1926                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0964 S12:   0.7401 S13:  -0.0551                       
REMARK   3      S21:  -1.2880 S22:  -0.1236 S23:   0.0844                       
REMARK   3      S31:  -0.5932 S32:  -0.1426 S33:   0.1297                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 3 THROUGH 16 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -17.0033 -25.6558  88.9104              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2798 T22:   0.1876                                     
REMARK   3      T33:   0.3895 T12:   0.0519                                     
REMARK   3      T13:   0.0387 T23:   0.0408                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4222 L22:   5.5102                                     
REMARK   3      L33:   4.0738 L12:  -3.8779                                     
REMARK   3      L13:  -2.2092 L23:   2.9922                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1701 S12:   0.0270 S13:   0.6100                       
REMARK   3      S21:  -0.0114 S22:   0.0976 S23:  -0.5644                       
REMARK   3      S31:  -0.1039 S32:   0.0070 S33:  -0.2632                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 17 THROUGH 50 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -13.0441 -36.7260  97.5713              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1651 T22:   0.1805                                     
REMARK   3      T33:   0.2630 T12:   0.0356                                     
REMARK   3      T13:   0.0515 T23:  -0.0212                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3926 L22:   2.0651                                     
REMARK   3      L33:   2.6953 L12:   1.2110                                     
REMARK   3      L13:  -0.5246 L23:  -0.9773                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0960 S12:  -0.0237 S13:   0.0668                       
REMARK   3      S21:  -0.0875 S22:   0.0697 S23:  -0.0787                       
REMARK   3      S31:   0.1665 S32:  -0.0590 S33:   0.0718                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 51 THROUGH 109 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.4076 -33.7404 109.7281              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1973 T22:   0.3134                                     
REMARK   3      T33:   0.2852 T12:   0.0090                                     
REMARK   3      T13:  -0.0501 T23:  -0.0366                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6891 L22:   2.0894                                     
REMARK   3      L33:   3.4277 L12:   0.1861                                     
REMARK   3      L13:  -0.7907 L23:  -0.1366                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1017 S12:  -0.5226 S13:   0.0777                       
REMARK   3      S21:   0.3358 S22:  -0.0373 S23:  -0.2487                       
REMARK   3      S31:  -0.1789 S32:   0.4951 S33:   0.1593                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 110 THROUGH 124 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.6698 -32.2969 104.1102              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1257 T22:   0.4071                                     
REMARK   3      T33:   0.3323 T12:  -0.0440                                     
REMARK   3      T13:  -0.0087 T23:  -0.0225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4987 L22:   2.0554                                     
REMARK   3      L33:   1.8036 L12:   0.2997                                     
REMARK   3      L13:  -0.0482 L23:  -0.6187                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2238 S12:   0.2409 S13:   0.2883                       
REMARK   3      S21:   0.2548 S22:  -0.1020 S23:  -0.5515                       
REMARK   3      S31:  -0.2436 S32:   0.4306 S33:  -0.0106                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 125 THROUGH 135 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -17.4004 -20.1712 109.3374              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2857 T22:   0.3496                                     
REMARK   3      T33:   0.3125 T12:  -0.0237                                     
REMARK   3      T13:  -0.0190 T23:  -0.1187                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0444 L22:   4.3182                                     
REMARK   3      L33:   4.2038 L12:   1.1192                                     
REMARK   3      L13:  -1.5200 L23:  -0.5781                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1835 S12:  -0.0722 S13:   0.1331                       
REMARK   3      S21:  -0.0560 S22:   0.2264 S23:  -0.0673                       
REMARK   3      S31:  -0.3163 S32:   0.2279 S33:  -0.0117                       
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 136 THROUGH 150 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.7538 -26.1894 102.9782              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2114 T22:   0.3910                                     
REMARK   3      T33:   0.4851 T12:  -0.0831                                     
REMARK   3      T13:  -0.0269 T23:  -0.0751                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3774 L22:   2.3908                                     
REMARK   3      L33:   2.0012 L12:   0.5909                                     
REMARK   3      L13:   1.6446 L23:   0.4482                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1668 S12:  -0.6574 S13:   1.0929                       
REMARK   3      S21:   0.2266 S22:  -0.0338 S23:   0.0033                       
REMARK   3      S31:  -0.4975 S32:   0.5330 S33:  -0.0181                       
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 151 THROUGH 178 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -18.6480 -24.3736  98.8660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1375 T22:   0.2324                                     
REMARK   3      T33:   0.3009 T12:   0.0073                                     
REMARK   3      T13:   0.0218 T23:  -0.0363                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5527 L22:   3.4441                                     
REMARK   3      L33:   2.5937 L12:  -1.8642                                     
REMARK   3      L13:   1.1979 L23:  -0.0360                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0104 S12:  -0.3115 S13:   0.1860                       
REMARK   3      S21:   0.1041 S22:  -0.0241 S23:   0.2355                       
REMARK   3      S31:  -0.1651 S32:  -0.0832 S33:   0.0156                       
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 179 THROUGH 199 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.4484 -24.0131 103.0844              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1982 T22:   0.2626                                     
REMARK   3      T33:   0.1986 T12:   0.0498                                     
REMARK   3      T13:   0.0115 T23:  -0.0223                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2555 L22:   3.6029                                     
REMARK   3      L33:   3.6060 L12:  -0.0721                                     
REMARK   3      L13:  -1.6535 L23:  -0.1095                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0256 S12:  -0.3383 S13:   0.1500                       
REMARK   3      S21:   0.3516 S22:  -0.0850 S23:   0.2797                       
REMARK   3      S31:  -0.3764 S32:  -0.4312 S33:   0.0450                       
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 200 THROUGH 215 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   0.9760 -28.7742 105.6471              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2382 T22:   0.4391                                     
REMARK   3      T33:   0.5128 T12:  -0.1579                                     
REMARK   3      T13:  -0.0403 T23:   0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9177 L22:   1.8731                                     
REMARK   3      L33:   1.4475 L12:   0.5399                                     
REMARK   3      L13:   1.3994 L23:   0.3143                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2147 S12:  -0.3002 S13:   0.4956                       
REMARK   3      S21:   0.2073 S22:  -0.2859 S23:  -0.4977                       
REMARK   3      S31:  -0.5165 S32:   0.7075 S33:   0.0674                       
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 6N1F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-NOV-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000237993.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-G                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97856                            
REMARK 200  MONOCHROMATOR                  : C(111)                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59902                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.351                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 3.814                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.6400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.34                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.170                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HAMPTON RESEARCH PACT SCREEN F12:        
REMARK 280  200MM SODIUM MALONATE DIBASIC, 20% PEG 3350, 100MM BISTRIS          
REMARK 280  PROPANE/HCL PH 6.5: BUPSA.17629.A.A1.PD38303 AT 10.9MG/ML: CRYO:    
REMARK 280  20% EG: TRAY 299888F12: PUCK WTM5-3, VAPOR DIFFUSION, SITTING       
REMARK 280  DROP, TEMPERATURE 290K                                              
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, 3, 4, 5, 6                                        
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       23.47437            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       49.72780            
REMARK 350   BIOMT3   2  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     MSE A   -20                                                      
REMARK 465     ALA A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     MSE A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     THR A   -10                                                      
REMARK 465     LEU A    -9                                                      
REMARK 465     GLU A    -8                                                      
REMARK 465     ALA A    -7                                                      
REMARK 465     GLN A    -6                                                      
REMARK 465     THR A    -5                                                      
REMARK 465     GLN A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MSE A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     THR A    57                                                      
REMARK 465     ALA A    58                                                      
REMARK 465     GLY A    59                                                      
REMARK 465     ASP A    60                                                      
REMARK 465     ALA A    61                                                      
REMARK 465     GLY A    62                                                      
REMARK 465     ASP A    63                                                      
REMARK 465     THR A    64                                                      
REMARK 465     MSE B   -20                                                      
REMARK 465     ALA B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     MSE B   -12                                                      
REMARK 465     GLY B   -11                                                      
REMARK 465     THR B   -10                                                      
REMARK 465     LEU B    -9                                                      
REMARK 465     GLU B    -8                                                      
REMARK 465     ALA B    -7                                                      
REMARK 465     GLN B    -6                                                      
REMARK 465     THR B    -5                                                      
REMARK 465     GLN B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     PRO B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     ASP B    60                                                      
REMARK 465     ALA B    61                                                      
REMARK 465     GLY B    62                                                      
REMARK 465     ASP B    63                                                      
REMARK 465     ALA B   215                                                      
REMARK 465     ALA B   216                                                      
REMARK 465     MSE C   -20                                                      
REMARK 465     ALA C   -19                                                      
REMARK 465     HIS C   -18                                                      
REMARK 465     HIS C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     MSE C   -12                                                      
REMARK 465     GLY C   -11                                                      
REMARK 465     THR C   -10                                                      
REMARK 465     LEU C    -9                                                      
REMARK 465     GLU C    -8                                                      
REMARK 465     ALA C    -7                                                      
REMARK 465     GLN C    -6                                                      
REMARK 465     THR C    -5                                                      
REMARK 465     GLN C    -4                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     PRO C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     THR C    57                                                      
REMARK 465     ALA C    58                                                      
REMARK 465     GLY C    59                                                      
REMARK 465     ASP C    60                                                      
REMARK 465     ALA C    61                                                      
REMARK 465     GLY C    62                                                      
REMARK 465     ASP C    63                                                      
REMARK 465     THR C    64                                                      
REMARK 465     ALA C   216                                                      
REMARK 465     MSE D   -20                                                      
REMARK 465     ALA D   -19                                                      
REMARK 465     HIS D   -18                                                      
REMARK 465     HIS D   -17                                                      
REMARK 465     HIS D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     MSE D   -12                                                      
REMARK 465     GLY D   -11                                                      
REMARK 465     THR D   -10                                                      
REMARK 465     LEU D    -9                                                      
REMARK 465     GLU D    -8                                                      
REMARK 465     ALA D    -7                                                      
REMARK 465     GLN D    -6                                                      
REMARK 465     THR D    -5                                                      
REMARK 465     GLN D    -4                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     PRO D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     ALA D   216                                                      
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     ARG A   9    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  80    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  90    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 112    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 153    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 165    CG   CD   OE1  NE2                                  
REMARK 470     THR B   3    OG1  CG2                                            
REMARK 470     ARG B   9    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  50    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  54    CG   CD   OE1  OE2                                  
REMARK 470     THR B  64    OG1  CG2                                            
REMARK 470     ARG B 112    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 114    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 153    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 165    CG   CD   OE1  NE2                                  
REMARK 470     ARG C   9    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C  24    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  54    CG   CD   OE1  OE2                                  
REMARK 470     ARG C  80    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 112    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 153    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 156    CG   OD1  OD2                                       
REMARK 470     ARG C 214    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D   9    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D  60    CG   OD1  OD2                                       
REMARK 470     GLN D  82    CG   CD   OE1  NE2                                  
REMARK 470     ARG D 112    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 114    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 153    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN D 165    CG   CD   OE1  NE2                                  
REMARK 470     ARG D 167    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 187    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 213    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP B   136     O    HOH B   401              2.11            
REMARK 500   OG1  THR A    91     O    HOH A   401              2.11            
REMARK 500   O    HOH D   469     O    HOH D   501              2.18            
REMARK 500   O    HOH A   490     O    HOH A   498              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 196     -108.13     37.59                                   
REMARK 500    ASP B 128       -7.72     84.50                                   
REMARK 500    HIS B 163       73.66   -119.84                                   
REMARK 500    ASN B 196     -152.75     60.67                                   
REMARK 500    ASN C 196     -120.20     35.75                                   
REMARK 500    ASP D 128       -6.60     80.85                                   
REMARK 500    ASN D 196     -151.71     63.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR B  111     ARG B  112                  146.10                    
REMARK 500 THR D  111     ARG D  112                  144.15                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 513        DISTANCE =  6.85 ANGSTROMS                       
REMARK 525    HOH B 514        DISTANCE =  8.97 ANGSTROMS                       
REMARK 525    HOH C 509        DISTANCE =  5.86 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 300  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 134   NE2                                                    
REMARK 620 2 ASP A 136   OD1  84.9                                              
REMARK 620 3 HIS A 188   NE2  88.4 104.5                                        
REMARK 620 4 HOH A 500   O    92.9 158.0  97.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 300  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 134   NE2                                                    
REMARK 620 2 ASP B 136   OD1  98.4                                              
REMARK 620 3 HIS B 188   NE2  94.3 112.3                                        
REMARK 620 4 HOH B 491   O    85.9  90.7 156.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE C 300  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 134   NE2                                                    
REMARK 620 2 ASP C 136   OD1  88.3                                              
REMARK 620 3 HIS C 188   NE2  87.9  99.1                                        
REMARK 620 4 HOH C 463   O   166.4 104.0  95.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE D 300  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 134   NE2                                                    
REMARK 620 2 ASP D 136   OD1 104.2                                              
REMARK 620 3 ASP D 136   OD2 146.8  52.8                                        
REMARK 620 4 HIS D 188   NE2  91.9 110.7  78.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE A 300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE B 300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE C 300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE D 300                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: SSGCID-BUPSA.17629.A   RELATED DB: TARGETTRACK           
DBREF  6N1F A    1   216  UNP    Q3JFV4   Q3JFV4_BURP1     1    216             
DBREF  6N1F B    1   216  UNP    Q3JFV4   Q3JFV4_BURP1     1    216             
DBREF  6N1F C    1   216  UNP    Q3JFV4   Q3JFV4_BURP1     1    216             
DBREF  6N1F D    1   216  UNP    Q3JFV4   Q3JFV4_BURP1     1    216             
SEQADV 6N1F MSE A  -20  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F ALA A  -19  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS A  -18  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS A  -17  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS A  -16  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS A  -15  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS A  -14  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS A  -13  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F MSE A  -12  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLY A  -11  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F THR A  -10  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F LEU A   -9  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLU A   -8  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F ALA A   -7  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLN A   -6  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F THR A   -5  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLN A   -4  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLY A   -3  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F PRO A   -2  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLY A   -1  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F SER A    0  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F MSE B  -20  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F ALA B  -19  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS B  -18  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS B  -17  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS B  -16  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS B  -15  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS B  -14  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS B  -13  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F MSE B  -12  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLY B  -11  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F THR B  -10  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F LEU B   -9  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLU B   -8  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F ALA B   -7  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLN B   -6  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F THR B   -5  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLN B   -4  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLY B   -3  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F PRO B   -2  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLY B   -1  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F SER B    0  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F MSE C  -20  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F ALA C  -19  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS C  -18  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS C  -17  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS C  -16  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS C  -15  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS C  -14  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS C  -13  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F MSE C  -12  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLY C  -11  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F THR C  -10  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F LEU C   -9  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLU C   -8  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F ALA C   -7  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLN C   -6  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F THR C   -5  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLN C   -4  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLY C   -3  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F PRO C   -2  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLY C   -1  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F SER C    0  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F MSE D  -20  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F ALA D  -19  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS D  -18  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS D  -17  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS D  -16  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS D  -15  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS D  -14  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F HIS D  -13  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F MSE D  -12  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLY D  -11  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F THR D  -10  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F LEU D   -9  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLU D   -8  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F ALA D   -7  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLN D   -6  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F THR D   -5  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLN D   -4  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLY D   -3  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F PRO D   -2  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F GLY D   -1  UNP  Q3JFV4              EXPRESSION TAG                 
SEQADV 6N1F SER D    0  UNP  Q3JFV4              EXPRESSION TAG                 
SEQRES   1 A  237  MSE ALA HIS HIS HIS HIS HIS HIS MSE GLY THR LEU GLU          
SEQRES   2 A  237  ALA GLN THR GLN GLY PRO GLY SER MSE GLU THR ALA GLU          
SEQRES   3 A  237  LEU HIS PHE ARG CYS ASN GLU GLY GLY MSE ALA ASP TYR          
SEQRES   4 A  237  ALA ALA GLN LEU ARG GLU VAL GLY THR VAL MSE LEU PRO          
SEQRES   5 A  237  ALA TYR VAL ALA PHE ASP ALA HIS GLU LEU ALA ARG ILE          
SEQRES   6 A  237  ASP ALA LEU GLN ALA ARG LEU PRO GLU GLU PRO VAL THR          
SEQRES   7 A  237  ALA GLY ASP ALA GLY ASP THR HIS ASP ILE TYR VAL ARG          
SEQRES   8 A  237  ARG ILE MSE VAL ASP ARG ALA GLY GLU ARG PRO GLN LEU          
SEQRES   9 A  237  VAL ASN LEU PRO HIS SER GLU THR ILE LEU ASN LEU LEU          
SEQRES  10 A  237  GLY ASP ALA ARG ARG THR ARG PHE PHE GLY ASP MSE PHE          
SEQRES  11 A  237  GLY THR ARG ALA GLU TYR PHE ILE ARG ARG CYS GLN ILE          
SEQRES  12 A  237  ASN ARG MSE LEU LYS ASP SER PHE ILE GLY MSE HIS LEU          
SEQRES  13 A  237  ASP ALA ALA SER ASN PRO ASP TYR GLU PHE SER VAL VAL          
SEQRES  14 A  237  ILE GLN LEU GLY ARG ALA PHE ASP GLY GLY GLU PHE VAL          
SEQRES  15 A  237  VAL HIS PRO GLN GLY ARG PRO PRO ASN VAL PHE ALA PRO          
SEQRES  16 A  237  ALA TYR GLY THR VAL ILE VAL THR SER CYS ALA HIS ARG          
SEQRES  17 A  237  HIS GLU VAL ARG THR VAL ARG ALA ASN GLU ARG THR SER          
SEQRES  18 A  237  LEU VAL TYR PHE TYR SER ARG HIS ASN GLY ALA ASN ARG          
SEQRES  19 A  237  ARG ALA ALA                                                  
SEQRES   1 B  237  MSE ALA HIS HIS HIS HIS HIS HIS MSE GLY THR LEU GLU          
SEQRES   2 B  237  ALA GLN THR GLN GLY PRO GLY SER MSE GLU THR ALA GLU          
SEQRES   3 B  237  LEU HIS PHE ARG CYS ASN GLU GLY GLY MSE ALA ASP TYR          
SEQRES   4 B  237  ALA ALA GLN LEU ARG GLU VAL GLY THR VAL MSE LEU PRO          
SEQRES   5 B  237  ALA TYR VAL ALA PHE ASP ALA HIS GLU LEU ALA ARG ILE          
SEQRES   6 B  237  ASP ALA LEU GLN ALA ARG LEU PRO GLU GLU PRO VAL THR          
SEQRES   7 B  237  ALA GLY ASP ALA GLY ASP THR HIS ASP ILE TYR VAL ARG          
SEQRES   8 B  237  ARG ILE MSE VAL ASP ARG ALA GLY GLU ARG PRO GLN LEU          
SEQRES   9 B  237  VAL ASN LEU PRO HIS SER GLU THR ILE LEU ASN LEU LEU          
SEQRES  10 B  237  GLY ASP ALA ARG ARG THR ARG PHE PHE GLY ASP MSE PHE          
SEQRES  11 B  237  GLY THR ARG ALA GLU TYR PHE ILE ARG ARG CYS GLN ILE          
SEQRES  12 B  237  ASN ARG MSE LEU LYS ASP SER PHE ILE GLY MSE HIS LEU          
SEQRES  13 B  237  ASP ALA ALA SER ASN PRO ASP TYR GLU PHE SER VAL VAL          
SEQRES  14 B  237  ILE GLN LEU GLY ARG ALA PHE ASP GLY GLY GLU PHE VAL          
SEQRES  15 B  237  VAL HIS PRO GLN GLY ARG PRO PRO ASN VAL PHE ALA PRO          
SEQRES  16 B  237  ALA TYR GLY THR VAL ILE VAL THR SER CYS ALA HIS ARG          
SEQRES  17 B  237  HIS GLU VAL ARG THR VAL ARG ALA ASN GLU ARG THR SER          
SEQRES  18 B  237  LEU VAL TYR PHE TYR SER ARG HIS ASN GLY ALA ASN ARG          
SEQRES  19 B  237  ARG ALA ALA                                                  
SEQRES   1 C  237  MSE ALA HIS HIS HIS HIS HIS HIS MSE GLY THR LEU GLU          
SEQRES   2 C  237  ALA GLN THR GLN GLY PRO GLY SER MSE GLU THR ALA GLU          
SEQRES   3 C  237  LEU HIS PHE ARG CYS ASN GLU GLY GLY MSE ALA ASP TYR          
SEQRES   4 C  237  ALA ALA GLN LEU ARG GLU VAL GLY THR VAL MSE LEU PRO          
SEQRES   5 C  237  ALA TYR VAL ALA PHE ASP ALA HIS GLU LEU ALA ARG ILE          
SEQRES   6 C  237  ASP ALA LEU GLN ALA ARG LEU PRO GLU GLU PRO VAL THR          
SEQRES   7 C  237  ALA GLY ASP ALA GLY ASP THR HIS ASP ILE TYR VAL ARG          
SEQRES   8 C  237  ARG ILE MSE VAL ASP ARG ALA GLY GLU ARG PRO GLN LEU          
SEQRES   9 C  237  VAL ASN LEU PRO HIS SER GLU THR ILE LEU ASN LEU LEU          
SEQRES  10 C  237  GLY ASP ALA ARG ARG THR ARG PHE PHE GLY ASP MSE PHE          
SEQRES  11 C  237  GLY THR ARG ALA GLU TYR PHE ILE ARG ARG CYS GLN ILE          
SEQRES  12 C  237  ASN ARG MSE LEU LYS ASP SER PHE ILE GLY MSE HIS LEU          
SEQRES  13 C  237  ASP ALA ALA SER ASN PRO ASP TYR GLU PHE SER VAL VAL          
SEQRES  14 C  237  ILE GLN LEU GLY ARG ALA PHE ASP GLY GLY GLU PHE VAL          
SEQRES  15 C  237  VAL HIS PRO GLN GLY ARG PRO PRO ASN VAL PHE ALA PRO          
SEQRES  16 C  237  ALA TYR GLY THR VAL ILE VAL THR SER CYS ALA HIS ARG          
SEQRES  17 C  237  HIS GLU VAL ARG THR VAL ARG ALA ASN GLU ARG THR SER          
SEQRES  18 C  237  LEU VAL TYR PHE TYR SER ARG HIS ASN GLY ALA ASN ARG          
SEQRES  19 C  237  ARG ALA ALA                                                  
SEQRES   1 D  237  MSE ALA HIS HIS HIS HIS HIS HIS MSE GLY THR LEU GLU          
SEQRES   2 D  237  ALA GLN THR GLN GLY PRO GLY SER MSE GLU THR ALA GLU          
SEQRES   3 D  237  LEU HIS PHE ARG CYS ASN GLU GLY GLY MSE ALA ASP TYR          
SEQRES   4 D  237  ALA ALA GLN LEU ARG GLU VAL GLY THR VAL MSE LEU PRO          
SEQRES   5 D  237  ALA TYR VAL ALA PHE ASP ALA HIS GLU LEU ALA ARG ILE          
SEQRES   6 D  237  ASP ALA LEU GLN ALA ARG LEU PRO GLU GLU PRO VAL THR          
SEQRES   7 D  237  ALA GLY ASP ALA GLY ASP THR HIS ASP ILE TYR VAL ARG          
SEQRES   8 D  237  ARG ILE MSE VAL ASP ARG ALA GLY GLU ARG PRO GLN LEU          
SEQRES   9 D  237  VAL ASN LEU PRO HIS SER GLU THR ILE LEU ASN LEU LEU          
SEQRES  10 D  237  GLY ASP ALA ARG ARG THR ARG PHE PHE GLY ASP MSE PHE          
SEQRES  11 D  237  GLY THR ARG ALA GLU TYR PHE ILE ARG ARG CYS GLN ILE          
SEQRES  12 D  237  ASN ARG MSE LEU LYS ASP SER PHE ILE GLY MSE HIS LEU          
SEQRES  13 D  237  ASP ALA ALA SER ASN PRO ASP TYR GLU PHE SER VAL VAL          
SEQRES  14 D  237  ILE GLN LEU GLY ARG ALA PHE ASP GLY GLY GLU PHE VAL          
SEQRES  15 D  237  VAL HIS PRO GLN GLY ARG PRO PRO ASN VAL PHE ALA PRO          
SEQRES  16 D  237  ALA TYR GLY THR VAL ILE VAL THR SER CYS ALA HIS ARG          
SEQRES  17 D  237  HIS GLU VAL ARG THR VAL ARG ALA ASN GLU ARG THR SER          
SEQRES  18 D  237  LEU VAL TYR PHE TYR SER ARG HIS ASN GLY ALA ASN ARG          
SEQRES  19 D  237  ARG ALA ALA                                                  
MODRES 6N1F MSE A   15  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE A   29  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE A   73  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE A  108  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE A  125  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE A  133  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE B   15  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE B   29  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE B   73  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE B  108  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE B  125  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE B  133  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE C   15  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE C   29  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE C   73  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE C  108  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE C  125  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE C  133  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE D   15  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE D   29  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE D   73  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE D  108  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE D  125  MET  MODIFIED RESIDUE                                   
MODRES 6N1F MSE D  133  MET  MODIFIED RESIDUE                                   
HET    MSE  A  15       8                                                       
HET    MSE  A  29       8                                                       
HET    MSE  A  73       8                                                       
HET    MSE  A 108       8                                                       
HET    MSE  A 125       8                                                       
HET    MSE  A 133       8                                                       
HET    MSE  B  15       8                                                       
HET    MSE  B  29       8                                                       
HET    MSE  B  73       8                                                       
HET    MSE  B 108       8                                                       
HET    MSE  B 125       8                                                       
HET    MSE  B 133       8                                                       
HET    MSE  C  15       8                                                       
HET    MSE  C  29       8                                                       
HET    MSE  C  73       8                                                       
HET    MSE  C 108       8                                                       
HET    MSE  C 125       8                                                       
HET    MSE  C 133       8                                                       
HET    MSE  D  15       8                                                       
HET    MSE  D  29       8                                                       
HET    MSE  D  73       8                                                       
HET    MSE  D 108       8                                                       
HET    MSE  D 125       8                                                       
HET    MSE  D 133       8                                                       
HET     FE  A 300       1                                                       
HET     CL  A 301       1                                                       
HET     FE  B 300       1                                                       
HET     FE  C 300       1                                                       
HET     CL  C 301       1                                                       
HET     FE  D 300       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      FE FE (III) ION                                                     
HETNAM      CL CHLORIDE ION                                                     
FORMUL   1  MSE    24(C5 H11 N O2 SE)                                           
FORMUL   5   FE    4(FE 3+)                                                     
FORMUL   6   CL    2(CL 1-)                                                     
FORMUL  11  HOH   *442(H2 O)                                                    
HELIX    1 AA1 GLY A   14  VAL A   25  1                                  12    
HELIX    2 AA2 ASP A   37  ARG A   50  1                                  14    
HELIX    3 AA3 PRO A   87  GLY A   97  1                                  11    
HELIX    4 AA4 ASP A   98  GLY A  110  1                                  13    
HELIX    5 AA5 LEU A  135  SER A  139  5                                   5    
HELIX    6 AA6 GLY B   14  GLY B   26  1                                  13    
HELIX    7 AA7 ASP B   37  ARG B   50  1                                  14    
HELIX    8 AA8 PRO B   87  GLY B   97  1                                  11    
HELIX    9 AA9 ASP B   98  PHE B  109  1                                  12    
HELIX   10 AB1 LEU B  135  SER B  139  5                                   5    
HELIX   11 AB2 GLY C   14  GLY C   26  1                                  13    
HELIX   12 AB3 ASP C   37  ARG C   50  1                                  14    
HELIX   13 AB4 PRO C   87  GLY C   97  1                                  11    
HELIX   14 AB5 ASP C   98  GLY C  110  1                                  13    
HELIX   15 AB6 LEU C  135  SER C  139  5                                   5    
HELIX   16 AB7 GLY D   14  GLY D   26  1                                  13    
HELIX   17 AB8 ASP D   37  ARG D   50  1                                  14    
HELIX   18 AB9 PRO D   87  GLY D   97  1                                  11    
HELIX   19 AC1 ASP D   98  GLY D  110  1                                  13    
HELIX   20 AC2 LEU D  135  ASN D  140  1                                   6    
SHEET    1 AA1 5 LEU A   6  PHE A   8  0                                        
SHEET    2 AA1 5 ASN A 170  PHE A 172  1  O  VAL A 171   N  LEU A   6           
SHEET    3 AA1 5 PHE A 160  HIS A 163 -1  N  VAL A 162   O  ASN A 170           
SHEET    4 AA1 5 ARG A 187  VAL A 190 -1  O  GLU A 189   N  VAL A 161           
SHEET    5 AA1 5 ILE A 131  HIS A 134 -1  N  ILE A 131   O  VAL A 190           
SHEET    1 AA2 7 THR A  27  LEU A  30  0                                        
SHEET    2 AA2 7 VAL A 179  SER A 183 -1  O  VAL A 179   N  LEU A  30           
SHEET    3 AA2 7 PHE A 145  GLN A 150 -1  N  VAL A 148   O  ILE A 180           
SHEET    4 AA2 7 GLU A 197  SER A 206 -1  O  LEU A 201   N  ILE A 149           
SHEET    5 AA2 7 PHE A 116  LEU A 126 -1  N  MSE A 125   O  ARG A 198           
SHEET    6 AA2 7 ILE A  67  VAL A  74 -1  N  TYR A  68   O  ARG A 124           
SHEET    7 AA2 7 GLU A  54  VAL A  56 -1  N  GLU A  54   O  VAL A  69           
SHEET    1 AA3 7 THR A  27  LEU A  30  0                                        
SHEET    2 AA3 7 VAL A 179  SER A 183 -1  O  VAL A 179   N  LEU A  30           
SHEET    3 AA3 7 PHE A 145  GLN A 150 -1  N  VAL A 148   O  ILE A 180           
SHEET    4 AA3 7 GLU A 197  SER A 206 -1  O  LEU A 201   N  ILE A 149           
SHEET    5 AA3 7 PHE A 116  LEU A 126 -1  N  MSE A 125   O  ARG A 198           
SHEET    6 AA3 7 ILE A  67  VAL A  74 -1  N  TYR A  68   O  ARG A 124           
SHEET    7 AA3 7 GLN A  82  LEU A  83 -1  O  GLN A  82   N  VAL A  74           
SHEET    1 AA4 5 LEU B   6  HIS B   7  0                                        
SHEET    2 AA4 5 ASN B 170  PHE B 172  1  O  VAL B 171   N  LEU B   6           
SHEET    3 AA4 5 PHE B 160  VAL B 162 -1  N  VAL B 162   O  ASN B 170           
SHEET    4 AA4 5 HIS B 188  VAL B 190 -1  O  GLU B 189   N  VAL B 161           
SHEET    5 AA4 5 ILE B 131  HIS B 134 -1  N  ILE B 131   O  VAL B 190           
SHEET    1 AA5 7 THR B  27  LEU B  30  0                                        
SHEET    2 AA5 7 VAL B 179  SER B 183 -1  O  VAL B 179   N  LEU B  30           
SHEET    3 AA5 7 PHE B 145  GLN B 150 -1  N  VAL B 148   O  ILE B 180           
SHEET    4 AA5 7 ARG B 198  SER B 206 -1  O  TYR B 203   N  VAL B 147           
SHEET    5 AA5 7 PHE B 116  MSE B 125 -1  N  PHE B 116   O  SER B 206           
SHEET    6 AA5 7 HIS B  65  VAL B  74 -1  N  ARG B  70   O  ILE B 122           
SHEET    7 AA5 7 GLU B  54  ALA B  58 -1  N  VAL B  56   O  ILE B  67           
SHEET    1 AA6 7 THR B  27  LEU B  30  0                                        
SHEET    2 AA6 7 VAL B 179  SER B 183 -1  O  VAL B 179   N  LEU B  30           
SHEET    3 AA6 7 PHE B 145  GLN B 150 -1  N  VAL B 148   O  ILE B 180           
SHEET    4 AA6 7 ARG B 198  SER B 206 -1  O  TYR B 203   N  VAL B 147           
SHEET    5 AA6 7 PHE B 116  MSE B 125 -1  N  PHE B 116   O  SER B 206           
SHEET    6 AA6 7 HIS B  65  VAL B  74 -1  N  ARG B  70   O  ILE B 122           
SHEET    7 AA6 7 GLN B  82  LEU B  83 -1  O  GLN B  82   N  VAL B  74           
SHEET    1 AA7 2 PHE B 155  GLY B 157  0                                        
SHEET    2 AA7 2 VAL B 193  ASN B 196 -1  O  ARG B 194   N  ASP B 156           
SHEET    1 AA8 5 LEU C   6  PHE C   8  0                                        
SHEET    2 AA8 5 ASN C 170  PHE C 172  1  O  VAL C 171   N  LEU C   6           
SHEET    3 AA8 5 PHE C 160  HIS C 163 -1  N  PHE C 160   O  PHE C 172           
SHEET    4 AA8 5 ARG C 187  VAL C 190 -1  O  GLU C 189   N  VAL C 161           
SHEET    5 AA8 5 ILE C 131  HIS C 134 -1  N  ILE C 131   O  VAL C 190           
SHEET    1 AA9 7 THR C  27  LEU C  30  0                                        
SHEET    2 AA9 7 VAL C 179  SER C 183 -1  O  VAL C 179   N  LEU C  30           
SHEET    3 AA9 7 PHE C 145  GLN C 150 -1  N  SER C 146   O  THR C 182           
SHEET    4 AA9 7 GLU C 197  SER C 206 -1  O  TYR C 205   N  PHE C 145           
SHEET    5 AA9 7 PHE C 116  LEU C 126 -1  N  MSE C 125   O  ARG C 198           
SHEET    6 AA9 7 ILE C  67  VAL C  74 -1  N  ARG C  70   O  ILE C 122           
SHEET    7 AA9 7 GLU C  54  PRO C  55 -1  N  GLU C  54   O  VAL C  69           
SHEET    1 AB1 7 THR C  27  LEU C  30  0                                        
SHEET    2 AB1 7 VAL C 179  SER C 183 -1  O  VAL C 179   N  LEU C  30           
SHEET    3 AB1 7 PHE C 145  GLN C 150 -1  N  SER C 146   O  THR C 182           
SHEET    4 AB1 7 GLU C 197  SER C 206 -1  O  TYR C 205   N  PHE C 145           
SHEET    5 AB1 7 PHE C 116  LEU C 126 -1  N  MSE C 125   O  ARG C 198           
SHEET    6 AB1 7 ILE C  67  VAL C  74 -1  N  ARG C  70   O  ILE C 122           
SHEET    7 AB1 7 GLN C  82  LEU C  83 -1  O  GLN C  82   N  VAL C  74           
SHEET    1 AB2 5 LEU D   6  PHE D   8  0                                        
SHEET    2 AB2 5 ASN D 170  PHE D 172  1  O  VAL D 171   N  LEU D   6           
SHEET    3 AB2 5 PHE D 160  HIS D 163 -1  N  PHE D 160   O  PHE D 172           
SHEET    4 AB2 5 ARG D 187  VAL D 190 -1  O  ARG D 187   N  HIS D 163           
SHEET    5 AB2 5 ILE D 131  HIS D 134 -1  N  ILE D 131   O  VAL D 190           
SHEET    1 AB3 7 THR D  27  LEU D  30  0                                        
SHEET    2 AB3 7 VAL D 179  SER D 183 -1  O  VAL D 179   N  LEU D  30           
SHEET    3 AB3 7 PHE D 145  GLN D 150 -1  N  SER D 146   O  THR D 182           
SHEET    4 AB3 7 ARG D 198  SER D 206 -1  O  TYR D 205   N  PHE D 145           
SHEET    5 AB3 7 PHE D 116  MSE D 125 -1  N  PHE D 116   O  SER D 206           
SHEET    6 AB3 7 THR D  64  VAL D  74 -1  N  MSE D  73   O  CYS D 120           
SHEET    7 AB3 7 GLU D  54  GLY D  59 -1  N  ALA D  58   O  HIS D  65           
SHEET    1 AB4 7 THR D  27  LEU D  30  0                                        
SHEET    2 AB4 7 VAL D 179  SER D 183 -1  O  VAL D 179   N  LEU D  30           
SHEET    3 AB4 7 PHE D 145  GLN D 150 -1  N  SER D 146   O  THR D 182           
SHEET    4 AB4 7 ARG D 198  SER D 206 -1  O  TYR D 205   N  PHE D 145           
SHEET    5 AB4 7 PHE D 116  MSE D 125 -1  N  PHE D 116   O  SER D 206           
SHEET    6 AB4 7 THR D  64  VAL D  74 -1  N  MSE D  73   O  CYS D 120           
SHEET    7 AB4 7 GLN D  82  LEU D  83 -1  O  GLN D  82   N  VAL D  74           
SHEET    1 AB5 2 PHE D 155  GLY D 157  0                                        
SHEET    2 AB5 2 VAL D 193  ASN D 196 -1  O  ARG D 194   N  ASP D 156           
LINK         C   GLY A  14                 N   MSE A  15     1555   1555  1.34  
LINK         C   MSE A  15                 N   ALA A  16     1555   1555  1.34  
LINK         C   VAL A  28                 N   MSE A  29     1555   1555  1.33  
LINK         C   MSE A  29                 N   LEU A  30     1555   1555  1.32  
LINK         C   ILE A  72                 N   MSE A  73     1555   1555  1.32  
LINK         C   MSE A  73                 N   VAL A  74     1555   1555  1.34  
LINK         C   ASP A 107                 N   MSE A 108     1555   1555  1.33  
LINK         C   MSE A 108                 N   PHE A 109     1555   1555  1.33  
LINK         C   ARG A 124                 N   MSE A 125     1555   1555  1.33  
LINK         C   MSE A 125                 N   LEU A 126     1555   1555  1.33  
LINK         C   GLY A 132                 N   MSE A 133     1555   1555  1.32  
LINK         C   MSE A 133                 N   HIS A 134     1555   1555  1.34  
LINK         NE2 HIS A 134                FE    FE A 300     1555   1555  2.52  
LINK         OD1 ASP A 136                FE    FE A 300     1555   1555  2.18  
LINK         NE2 HIS A 188                FE    FE A 300     1555   1555  2.16  
LINK         C   GLY B  14                 N   MSE B  15     1555   1555  1.33  
LINK         C   MSE B  15                 N   ALA B  16     1555   1555  1.34  
LINK         C   VAL B  28                 N   MSE B  29     1555   1555  1.33  
LINK         C   MSE B  29                 N   LEU B  30     1555   1555  1.34  
LINK         C   ILE B  72                 N   MSE B  73     1555   1555  1.33  
LINK         C   MSE B  73                 N   VAL B  74     1555   1555  1.33  
LINK         C   ASP B 107                 N   MSE B 108     1555   1555  1.33  
LINK         C   MSE B 108                 N   PHE B 109     1555   1555  1.33  
LINK         C   ARG B 124                 N   MSE B 125     1555   1555  1.33  
LINK         C   MSE B 125                 N   LEU B 126     1555   1555  1.33  
LINK         C   GLY B 132                 N   MSE B 133     1555   1555  1.33  
LINK         C   MSE B 133                 N   HIS B 134     1555   1555  1.33  
LINK         NE2 HIS B 134                FE    FE B 300     1555   1555  2.11  
LINK         OD1 ASP B 136                FE    FE B 300     1555   1555  1.97  
LINK         NE2 HIS B 188                FE    FE B 300     1555   1555  1.90  
LINK         C   GLY C  14                 N   MSE C  15     1555   1555  1.33  
LINK         C   MSE C  15                 N   ALA C  16     1555   1555  1.33  
LINK         C   VAL C  28                 N   MSE C  29     1555   1555  1.34  
LINK         C   MSE C  29                 N   LEU C  30     1555   1555  1.32  
LINK         C   ILE C  72                 N   MSE C  73     1555   1555  1.32  
LINK         C   MSE C  73                 N   VAL C  74     1555   1555  1.33  
LINK         C   ASP C 107                 N   MSE C 108     1555   1555  1.32  
LINK         C   MSE C 108                 N   PHE C 109     1555   1555  1.33  
LINK         C   ARG C 124                 N   MSE C 125     1555   1555  1.33  
LINK         C   MSE C 125                 N   LEU C 126     1555   1555  1.33  
LINK         C   GLY C 132                 N   MSE C 133     1555   1555  1.33  
LINK         C   MSE C 133                 N   HIS C 134     1555   1555  1.34  
LINK         NE2 HIS C 134                FE    FE C 300     1555   1555  2.54  
LINK         OD1 ASP C 136                FE    FE C 300     1555   1555  2.10  
LINK         NE2 HIS C 188                FE    FE C 300     1555   1555  2.19  
LINK         C   GLY D  14                 N   MSE D  15     1555   1555  1.33  
LINK         C   MSE D  15                 N   ALA D  16     1555   1555  1.34  
LINK         C   VAL D  28                 N   MSE D  29     1555   1555  1.33  
LINK         C   MSE D  29                 N   LEU D  30     1555   1555  1.33  
LINK         C   ILE D  72                 N   MSE D  73     1555   1555  1.34  
LINK         C   MSE D  73                 N   VAL D  74     1555   1555  1.33  
LINK         C   ASP D 107                 N   MSE D 108     1555   1555  1.33  
LINK         C   MSE D 108                 N   PHE D 109     1555   1555  1.33  
LINK         C   ARG D 124                 N   MSE D 125     1555   1555  1.33  
LINK         C   MSE D 125                 N   LEU D 126     1555   1555  1.33  
LINK         C   GLY D 132                 N   MSE D 133     1555   1555  1.33  
LINK         C   MSE D 133                 N   HIS D 134     1555   1555  1.33  
LINK         NE2 HIS D 134                FE    FE D 300     1555   1555  2.30  
LINK         OD1 ASP D 136                FE    FE D 300     1555   1555  1.97  
LINK         OD2 ASP D 136                FE    FE D 300     1555   1555  2.74  
LINK         NE2 HIS D 188                FE    FE D 300     1555   1555  2.14  
LINK        FE    FE A 300                 O   HOH A 500     1555   1555  2.52  
LINK        FE    FE B 300                 O   HOH B 491     1555   1555  2.40  
LINK        FE    FE C 300                 O   HOH C 463     1555   1555  2.42  
CISPEP   1 ALA A   32    TYR A   33          0         4.93                     
CISPEP   2 LEU A   86    PRO A   87          0         1.83                     
CISPEP   3 ALA B   32    TYR B   33          0        -0.28                     
CISPEP   4 LEU B   86    PRO B   87          0         1.60                     
CISPEP   5 ALA C   32    TYR C   33          0         0.64                     
CISPEP   6 LEU C   86    PRO C   87          0         1.51                     
CISPEP   7 ALA D   32    TYR D   33          0         4.73                     
CISPEP   8 LEU D   86    PRO D   87          0         1.76                     
SITE     1 AC1  5 HIS A 134  ASP A 136  HIS A 188  HOH A 496                    
SITE     2 AC1  5 HOH A 500                                                     
SITE     1 AC2  3 ALA A  38  ASP B  37  ALA B  38                               
SITE     1 AC3  4 HIS B 134  ASP B 136  HIS B 188  HOH B 491                    
SITE     1 AC4  5 HIS C 134  ASP C 136  HIS C 188  HOH C 463                    
SITE     2 AC4  5 HOH C 499                                                     
SITE     1 AC5  4 ALA C  38  HOH C 473  ASP D  37  ALA D  38                    
SITE     1 AC6  5 HIS D 134  ASP D 136  HIS D 188  HOH D 456                    
SITE     2 AC6  5 HOH D 496                                                     
CRYST1   47.030   54.990  112.100  77.66  87.03  64.73 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      0.021263 -0.010036  0.001049        0.00000                         
SCALE2      0.000000  0.020109 -0.004364        0.00000                         
SCALE3      0.000000  0.000000  0.009141        0.00000                         
ATOM      1  N   THR A   3       2.871  27.662  46.745  1.00 53.77           N  
ANISOU    1  N   THR A   3     7497   4781   8152  -1365   -484  -2306       N  
ATOM      2  CA  THR A   3       3.518  28.045  45.494  1.00 60.26           C  
ANISOU    2  CA  THR A   3     8393   5435   9070  -1609   -605  -2015       C  
ATOM      3  C   THR A   3       3.602  26.847  44.548  1.00 60.51           C  
ANISOU    3  C   THR A   3     8330   5735   8925  -1586   -595  -1703       C  
ATOM      4  O   THR A   3       3.649  27.013  43.323  1.00 58.52           O  
ANISOU    4  O   THR A   3     8193   5310   8732  -1708   -668  -1397       O  
ATOM      5  CB  THR A   3       4.934  28.621  45.738  1.00 72.38           C  
ANISOU    5  CB  THR A   3     9930   7086  10483  -1932   -649  -2083       C  
ATOM      6  OG1 THR A   3       5.423  29.248  44.542  1.00 77.52           O  
ANISOU    6  OG1 THR A   3    10702   7486  11265  -2192   -723  -1808       O  
ATOM      7  CG2 THR A   3       5.902  27.521  46.181  1.00 69.25           C  
ANISOU    7  CG2 THR A   3     9306   7232   9773  -1993   -615  -2148       C  
ATOM      8  N   ALA A   4       3.598  25.641  45.126  1.00 53.07           N  
ANISOU    8  N   ALA A   4     7227   5219   7717  -1424   -504  -1751       N  
ATOM      9  CA  ALA A   4       3.668  24.404  44.364  1.00 45.78           C  
ANISOU    9  CA  ALA A   4     6211   4580   6606  -1359   -474  -1480       C  
ATOM     10  C   ALA A   4       2.696  23.383  44.941  1.00 38.44           C  
ANISOU   10  C   ALA A   4     5199   3819   5586  -1053   -391  -1514       C  
ATOM     11  O   ALA A   4       2.575  23.237  46.160  1.00 34.84           O  
ANISOU   11  O   ALA A   4     4720   3502   5018   -967   -315  -1758       O  
ATOM     12  CB  ALA A   4       5.086  23.835  44.364  1.00 40.81           C  
ANISOU   12  CB  ALA A   4     5430   4326   5750  -1553   -451  -1479       C  
ATOM     13  N   GLU A   5       2.000  22.681  44.067  1.00 32.44           N  
ANISOU   13  N   GLU A   5     4425   3044   4855   -925   -399  -1274       N  
ATOM     14  CA  GLU A   5       1.072  21.650  44.511  1.00 30.68           C  
ANISOU   14  CA  GLU A   5     4111   2969   4578   -678   -300  -1287       C  
ATOM     15  C   GLU A   5       1.216  20.433  43.611  1.00 28.16           C  
ANISOU   15  C   GLU A   5     3740   2860   4101   -657   -306  -1031       C  
ATOM     16  O   GLU A   5       1.393  20.562  42.397  1.00 28.11           O  
ANISOU   16  O   GLU A   5     3807   2751   4122   -770   -395   -824       O  
ATOM     17  CB  GLU A   5      -0.373  22.183  44.539  1.00 32.02           C  
ANISOU   17  CB  GLU A   5     4275   2798   5094   -489   -302  -1360       C  
ATOM     18  CG  GLU A   5      -0.592  23.189  45.673  1.00 34.84           C  
ANISOU   18  CG  GLU A   5     4659   2982   5598   -469   -212  -1710       C  
ATOM     19  CD  GLU A   5      -1.983  23.787  45.715  1.00 37.01           C  
ANISOU   19  CD  GLU A   5     4860   2885   6315   -260   -191  -1845       C  
ATOM     20  OE1 GLU A   5      -2.745  23.638  44.738  1.00 36.71           O  
ANISOU   20  OE1 GLU A   5     4761   2662   6523   -145   -339  -1629       O  
ATOM     21  OE2 GLU A   5      -2.308  24.422  46.734  1.00 41.60           O  
ANISOU   21  OE2 GLU A   5     5437   3354   7016   -212    -35  -2194       O  
ATOM     22  N   LEU A   6       1.169  19.252  44.219  1.00 26.58           N  
ANISOU   22  N   LEU A   6     3453   2938   3709   -534   -205  -1051       N  
ATOM     23  CA  LEU A   6       1.376  18.000  43.503  1.00 25.71           C  
ANISOU   23  CA  LEU A   6     3288   3020   3460   -501   -193   -858       C  
ATOM     24  C   LEU A   6       0.019  17.479  43.031  1.00 26.95           C  
ANISOU   24  C   LEU A   6     3433   3045   3760   -347   -184   -756       C  
ATOM     25  O   LEU A   6      -0.838  17.121  43.848  1.00 25.79           O  
ANISOU   25  O   LEU A   6     3234   2904   3660   -207    -75   -857       O  
ATOM     26  CB  LEU A   6       2.098  17.001  44.410  1.00 25.60           C  
ANISOU   26  CB  LEU A   6     3203   3320   3203   -448   -141   -915       C  
ATOM     27  CG  LEU A   6       2.577  15.683  43.786  1.00 26.03           C  
ANISOU   27  CG  LEU A   6     3180   3561   3148   -404   -131   -763       C  
ATOM     28  CD1 LEU A   6       3.534  15.943  42.617  1.00 25.77           C  
ANISOU   28  CD1 LEU A   6     3104   3547   3139   -582   -151   -699       C  
ATOM     29  CD2 LEU A   6       3.239  14.799  44.843  1.00 23.69           C  
ANISOU   29  CD2 LEU A   6     2833   3503   2664   -315   -153   -809       C  
ATOM     30  N   HIS A   7      -0.200  17.463  41.717  1.00 23.60           N  
ANISOU   30  N   HIS A   7     3066   2499   3402   -400   -297   -570       N  
ATOM     31  CA  HIS A   7      -1.462  16.979  41.171  1.00 27.61           C  
ANISOU   31  CA  HIS A   7     3542   2877   4069   -273   -361   -477       C  
ATOM     32  C   HIS A   7      -1.325  15.505  40.795  1.00 27.54           C  
ANISOU   32  C   HIS A   7     3500   3090   3875   -247   -292   -383       C  
ATOM     33  O   HIS A   7      -0.320  15.096  40.207  1.00 27.98           O  
ANISOU   33  O   HIS A   7     3606   3298   3729   -361   -271   -314       O  
ATOM     34  CB  HIS A   7      -1.895  17.803  39.957  1.00 24.65           C  
ANISOU   34  CB  HIS A   7     3301   2211   3854   -346   -603   -317       C  
ATOM     35  CG  HIS A   7      -2.277  19.220  40.282  1.00 29.51           C  
ANISOU   35  CG  HIS A   7     3947   2508   4758   -322   -712   -403       C  
ATOM     36  ND1 HIS A   7      -3.440  19.797  39.825  1.00 29.08           N  
ANISOU   36  ND1 HIS A   7     3878   2113   5057   -201   -941   -351       N  
ATOM     37  CD2 HIS A   7      -1.642  20.178  41.001  1.00 28.20           C  
ANISOU   37  CD2 HIS A   7     3817   2280   4616   -398   -649   -553       C  
ATOM     38  CE1 HIS A   7      -3.510  21.045  40.251  1.00 39.49           C  
ANISOU   38  CE1 HIS A   7     5227   3152   6627   -183   -996   -466       C  
ATOM     39  NE2 HIS A   7      -2.436  21.298  40.976  1.00 30.83           N  
ANISOU   39  NE2 HIS A   7     4174   2221   5319   -315   -806   -599       N  
ATOM     40  N   PHE A   8      -2.329  14.714  41.153  1.00 25.32           N  
ANISOU   40  N   PHE A   8     3117   2810   3694   -107   -228   -407       N  
ATOM     41  CA  PHE A   8      -2.334  13.273  40.936  1.00 23.75           C  
ANISOU   41  CA  PHE A   8     2892   2765   3366    -72   -155   -337       C  
ATOM     42  C   PHE A   8      -3.424  12.917  39.939  1.00 24.05           C  
ANISOU   42  C   PHE A   8     2911   2653   3573    -55   -293   -248       C  
ATOM     43  O   PHE A   8      -4.526  13.472  39.993  1.00 28.73           O  
ANISOU   43  O   PHE A   8     3407   3053   4457     15   -382   -289       O  
ATOM     44  CB  PHE A   8      -2.607  12.505  42.239  1.00 22.50           C  
ANISOU   44  CB  PHE A   8     2666   2722   3160     27     43   -424       C  
ATOM     45  CG  PHE A   8      -1.441  12.453  43.190  1.00 30.04           C  
ANISOU   45  CG  PHE A   8     3672   3867   3873     14    111   -477       C  
ATOM     46  CD1 PHE A   8      -0.586  11.366  43.199  1.00 25.68           C  
ANISOU   46  CD1 PHE A   8     3135   3478   3143     37    118   -404       C  
ATOM     47  CD2 PHE A   8      -1.216  13.481  44.096  1.00 32.02           C  
ANISOU   47  CD2 PHE A   8     3949   4115   4104    -13    135   -620       C  
ATOM     48  CE1 PHE A   8       0.489  11.320  44.083  1.00 27.28           C  
ANISOU   48  CE1 PHE A   8     3357   3843   3165     45     96   -448       C  
ATOM     49  CE2 PHE A   8      -0.147  13.435  44.979  1.00 28.52           C  
ANISOU   49  CE2 PHE A   8     3555   3853   3428    -39    129   -676       C  
ATOM     50  CZ  PHE A   8       0.708  12.353  44.967  1.00 22.35           C  
ANISOU   50  CZ  PHE A   8     2767   3239   2486     -4     84   -577       C  
ATOM     51  N   ARG A   9      -3.112  11.998  39.032  1.00 22.92           N  
ANISOU   51  N   ARG A   9     2843   2591   3274   -116   -324   -157       N  
ATOM     52  CA  ARG A   9      -4.117  11.356  38.203  1.00 26.55           C  
ANISOU   52  CA  ARG A   9     3289   2950   3848   -112   -456   -100       C  
ATOM     53  C   ARG A   9      -4.535  10.058  38.895  1.00 26.28           C  
ANISOU   53  C   ARG A   9     3137   2994   3853    -28   -271   -154       C  
ATOM     54  O   ARG A   9      -3.983   9.695  39.934  1.00 20.77           O  
ANISOU   54  O   ARG A   9     2422   2421   3048     23    -73   -197       O  
ATOM     55  CB  ARG A   9      -3.564  11.112  36.799  1.00 28.03           C  
ANISOU   55  CB  ARG A   9     3683   3166   3803   -265   -576     -3       C  
ATOM     56  N   CYS A  10      -5.508   9.341  38.321  1.00 19.81           N  
ANISOU   56  N   CYS A  10     2262   2086   3181    -36   -361   -139       N  
ATOM     57  CA  CYS A  10      -5.861   8.022  38.848  1.00 19.74           C  
ANISOU   57  CA  CYS A  10     2182   2116   3205     -6   -178   -170       C  
ATOM     58  C   CYS A  10      -4.682   7.069  38.735  1.00 21.34           C  
ANISOU   58  C   CYS A  10     2526   2448   3133    -15    -69   -140       C  
ATOM     59  O   CYS A  10      -3.971   7.050  37.726  1.00 24.33           O  
ANISOU   59  O   CYS A  10     3030   2870   3347    -85   -154   -125       O  
ATOM     60  CB  CYS A  10      -7.060   7.429  38.098  1.00 20.67           C  
ANISOU   60  CB  CYS A  10     2203   2100   3550    -51   -327   -180       C  
ATOM     61  SG  CYS A  10      -8.559   8.380  38.217  1.00 28.04           S  
ANISOU   61  SG  CYS A  10     2857   2849   4949      1   -488   -254       S  
ATOM     62  N   ASN A  11      -4.486   6.254  39.771  1.00 19.54           N  
ANISOU   62  N   ASN A  11     2288   2269   2867     50    126   -138       N  
ATOM     63  CA  ASN A  11      -3.439   5.244  39.729  1.00 17.75           C  
ANISOU   63  CA  ASN A  11     2158   2110   2476     90    189   -114       C  
ATOM     64  C   ASN A  11      -3.800   4.177  38.697  1.00 25.13           C  
ANISOU   64  C   ASN A  11     3136   2945   3465     37    148   -134       C  
ATOM     65  O   ASN A  11      -4.875   3.578  38.774  1.00 22.03           O  
ANISOU   65  O   ASN A  11     2697   2431   3242     -1    167   -132       O  
ATOM     66  CB  ASN A  11      -3.252   4.622  41.105  1.00 21.37           C  
ANISOU   66  CB  ASN A  11     2649   2591   2879    171    335    -62       C  
ATOM     67  CG  ASN A  11      -2.014   3.769  41.183  1.00 28.40           C  
ANISOU   67  CG  ASN A  11     3609   3526   3654    267    326    -31       C  
ATOM     68  OD1 ASN A  11      -1.827   2.857  40.381  1.00 24.26           O  
ANISOU   68  OD1 ASN A  11     3108   2927   3181    278    317    -56       O  
ATOM     69  ND2 ASN A  11      -1.135   4.085  42.129  1.00 31.53           N  
ANISOU   69  ND2 ASN A  11     4024   4035   3920    343    306     -3       N  
ATOM     70  N   GLU A  12      -2.913   3.943  37.727  1.00 25.50           N  
ANISOU   70  N   GLU A  12     3268   3042   3378     10    118   -185       N  
ATOM     71  CA  GLU A  12      -3.205   3.061  36.604  1.00 27.85           C  
ANISOU   71  CA  GLU A  12     3652   3252   3680    -72     76   -255       C  
ATOM     72  C   GLU A  12      -2.632   1.658  36.778  1.00 20.09           C  
ANISOU   72  C   GLU A  12     2702   2203   2727     20    209   -305       C  
ATOM     73  O   GLU A  12      -2.547   0.914  35.801  1.00 24.93           O  
ANISOU   73  O   GLU A  12     3404   2751   3315    -41    215   -421       O  
ATOM     74  CB  GLU A  12      -2.680   3.671  35.301  1.00 33.69           C  
ANISOU   74  CB  GLU A  12     4516   4067   4216   -207     -3   -315       C  
ATOM     75  CG  GLU A  12      -3.326   4.988  34.913  1.00 43.89           C  
ANISOU   75  CG  GLU A  12     5839   5345   5491   -308   -211   -233       C  
ATOM     76  CD  GLU A  12      -2.722   5.589  33.650  1.00 58.23           C  
ANISOU   76  CD  GLU A  12     7870   7224   7032   -488   -276   -245       C  
ATOM     77  OE1 GLU A  12      -3.476   6.217  32.881  1.00 64.22           O  
ANISOU   77  OE1 GLU A  12     8757   7899   7747   -610   -535   -169       O  
ATOM     78  OE2 GLU A  12      -1.500   5.435  33.424  1.00 60.18           O  
ANISOU   78  OE2 GLU A  12     8158   7594   7112   -520    -74   -330       O  
ATOM     79  N   GLY A  13      -2.235   1.288  37.981  1.00 19.96           N  
ANISOU   79  N   GLY A  13     2646   2179   2757    161    293   -225       N  
ATOM     80  CA  GLY A  13      -1.613   0.013  38.260  1.00 24.91           C  
ANISOU   80  CA  GLY A  13     3316   2695   3453    288    362   -235       C  
ATOM     81  C   GLY A  13      -2.592  -0.964  38.871  1.00 22.19           C  
ANISOU   81  C   GLY A  13     3040   2142   3248    269    403   -137       C  
ATOM     82  O   GLY A  13      -3.777  -0.981  38.525  1.00 25.08           O  
ANISOU   82  O   GLY A  13     3392   2433   3706    122    393   -153       O  
ATOM     83  N   GLY A  14      -2.095  -1.771  39.808  1.00 24.86           N  
ANISOU   83  N   GLY A  14     3453   2374   3618    405    432    -25       N  
ATOM     84  CA  GLY A  14      -2.925  -2.747  40.488  1.00 26.38           C  
ANISOU   84  CA  GLY A  14     3770   2341   3913    353    502    107       C  
ATOM     85  C   GLY A  14      -2.872  -2.607  41.995  1.00 34.92           C  
ANISOU   85  C   GLY A  14     4958   3447   4863    391    534    317       C  
ATOM     86  O   GLY A  14      -2.428  -1.572  42.509  1.00 29.56           O  
ANISOU   86  O   GLY A  14     4226   2983   4020    433    494    332       O  
HETATM   87  N   MSE A  15      -3.305  -3.647  42.712  1.00 28.00           N  
ANISOU   87  N   MSE A  15     4272   2338   4028    349    606    481       N  
HETATM   88  CA  MSE A  15      -3.397  -3.581  44.168  1.00 33.38           C  
ANISOU   88  CA  MSE A  15     5148   3032   4504    317    664    701       C  
HETATM   89  C   MSE A  15      -2.071  -3.213  44.825  1.00 32.28           C  
ANISOU   89  C   MSE A  15     5065   3027   4173    525    459    782       C  
HETATM   90  O   MSE A  15      -2.042  -2.367  45.719  1.00 29.66           O  
ANISOU   90  O   MSE A  15     4786   2883   3600    483    473    836       O  
HETATM   91  CB  MSE A  15      -3.895  -4.907  44.752  1.00 33.94           C  
ANISOU   91  CB  MSE A  15     5489   2781   4625    223    755    902       C  
HETATM   92  CG  MSE A  15      -4.106  -4.831  46.271  1.00 43.05           C  
ANISOU   92  CG  MSE A  15     6928   3953   5477    115    858   1145       C  
HETATM   93 SE   MSE A  15      -5.292  -3.355  46.861  1.00 44.48          SE  
ANISOU   93 SE   MSE A  15     6951   4444   5503   -139   1183   1007      SE  
HETATM   94  CE  MSE A  15      -6.989  -4.202  46.375  1.00 43.43           C  
ANISOU   94  CE  MSE A  15     6707   4064   5731   -450   1504    940       C  
ATOM     95  N   ALA A  16      -0.980  -3.849  44.384  1.00 30.62           N  
ANISOU   95  N   ALA A  16     4821   2714   4100    746    269    757       N  
ATOM     96  CA  ALA A  16       0.337  -3.517  44.921  1.00 36.19           C  
ANISOU   96  CA  ALA A  16     5493   3546   4712    957     27    798       C  
ATOM     97  C   ALA A  16       0.633  -2.028  44.780  1.00 37.14           C  
ANISOU   97  C   ALA A  16     5399   4010   4702    915     32    640       C  
ATOM     98  O   ALA A  16       1.218  -1.416  45.682  1.00 29.47           O  
ANISOU   98  O   ALA A  16     4467   3195   3535    960   -110    708       O  
ATOM     99  CB  ALA A  16       1.416  -4.335  44.220  1.00 32.90           C  
ANISOU   99  CB  ALA A  16     4942   2974   4584   1207   -130    695       C  
ATOM    100  N   ASP A  17       0.223  -1.432  43.655  1.00 26.35           N  
ANISOU  100  N   ASP A  17     2941   2967   4103    852  -1066   -345       N  
ATOM    101  CA  ASP A  17       0.425   0.001  43.438  1.00 26.75           C  
ANISOU  101  CA  ASP A  17     2897   3191   4074    672  -1055   -343       C  
ATOM    102  C   ASP A  17      -0.526   0.832  44.289  1.00 24.18           C  
ANISOU  102  C   ASP A  17     2792   2776   3618    551  -1063   -227       C  
ATOM    103  O   ASP A  17      -0.114   1.838  44.881  1.00 25.99           O  
ANISOU  103  O   ASP A  17     3015   3079   3782    464  -1143   -192       O  
ATOM    104  CB  ASP A  17       0.246   0.340  41.952  1.00 25.80           C  
ANISOU  104  CB  ASP A  17     2645   3199   3960    554   -889   -438       C  
ATOM    105  CG  ASP A  17       1.075  -0.559  41.048  1.00 32.26           C  
ANISOU  105  CG  ASP A  17     3258   4099   4900    663   -835   -584       C  
ATOM    106  OD1 ASP A  17       2.324  -0.550  41.175  1.00 33.34           O  
ANISOU  106  OD1 ASP A  17     3191   4359   5116    735   -914   -645       O  
ATOM    107  OD2 ASP A  17       0.474  -1.291  40.228  1.00 35.91           O  
ANISOU  107  OD2 ASP A  17     3755   4505   5386    676   -712   -651       O  
ATOM    108  N   TYR A  18      -1.809   0.451  44.343  1.00 20.57           N  
ANISOU  108  N   TYR A  18     2521   2165   3130    532   -967   -187       N  
ATOM    109  CA  TYR A  18      -2.761   1.198  45.163  1.00 23.96           C  
ANISOU  109  CA  TYR A  18     3143   2507   3453    428   -949   -101       C  
ATOM    110  C   TYR A  18      -2.299   1.284  46.618  1.00 25.78           C  
ANISOU  110  C   TYR A  18     3503   2685   3606    465  -1095    -26       C  
ATOM    111  O   TYR A  18      -2.271   2.371  47.209  1.00 23.02           O  
ANISOU  111  O   TYR A  18     3202   2374   3170    358  -1130      2       O  
ATOM    112  CB  TYR A  18      -4.146   0.565  45.108  1.00 20.90           C  
ANISOU  112  CB  TYR A  18     2910   1967   3064    416   -825    -87       C  
ATOM    113  CG  TYR A  18      -4.734   0.363  43.738  1.00 28.12           C  
ANISOU  113  CG  TYR A  18     3721   2930   4034    374   -701   -161       C  
ATOM    114  CD1 TYR A  18      -4.327   1.129  42.660  1.00 27.29           C  
ANISOU  114  CD1 TYR A  18     3445   2993   3933    302   -678   -209       C  
ATOM    115  CD2 TYR A  18      -5.706  -0.608  43.531  1.00 25.46           C  
ANISOU  115  CD2 TYR A  18     3473   2472   3729    386   -607   -185       C  
ATOM    116  CE1 TYR A  18      -4.874   0.947  41.424  1.00 26.86           C  
ANISOU  116  CE1 TYR A  18     3319   2992   3893    252   -581   -270       C  
ATOM    117  CE2 TYR A  18      -6.255  -0.810  42.298  1.00 20.05           C  
ANISOU  117  CE2 TYR A  18     2697   1845   3078    334   -512   -263       C  
ATOM    118  CZ  TYR A  18      -5.844  -0.031  41.249  1.00 23.89           C  
ANISOU  118  CZ  TYR A  18     3023   2507   3548    272   -507   -301       C  
ATOM    119  OH  TYR A  18      -6.399  -0.226  40.023  1.00 22.08           O  
ANISOU  119  OH  TYR A  18     2724   2347   3318    209   -427   -372       O  
ATOM    120  N   ALA A  19      -1.952   0.140  47.220  1.00 24.11           N  
ANISOU  120  N   ALA A  19     3369   2374   3417    612  -1188     10       N  
ATOM    121  CA  ALA A  19      -1.576   0.137  48.634  1.00 23.33           C  
ANISOU  121  CA  ALA A  19     3430   2222   3211    646  -1348    101       C  
ATOM    122  C   ALA A  19      -0.269   0.887  48.868  1.00 27.03           C  
ANISOU  122  C   ALA A  19     3722   2874   3673    640  -1517     76       C  
ATOM    123  O   ALA A  19      -0.097   1.538  49.904  1.00 26.01           O  
ANISOU  123  O   ALA A  19     3705   2763   3415    568  -1622    125       O  
ATOM    124  CB  ALA A  19      -1.466  -1.298  49.146  1.00 35.16           C  
ANISOU  124  CB  ALA A  19     5065   3557   4737    818  -1428    165       C  
ATOM    125  N   ALA A  20       0.673   0.796  47.923  1.00 27.94           N  
ANISOU  125  N   ALA A  20     3558   3137   3922    701  -1536    -15       N  
ATOM    126  CA  ALA A  20       1.945   1.495  48.081  1.00 29.42           C  
ANISOU  126  CA  ALA A  20     3536   3520   4121    675  -1683    -60       C  
ATOM    127  C   ALA A  20       1.764   3.012  48.031  1.00 26.58           C  
ANISOU  127  C   ALA A  20     3176   3252   3671    444  -1618    -79       C  
ATOM    128  O   ALA A  20       2.420   3.742  48.781  1.00 26.17           O  
ANISOU  128  O   ALA A  20     3107   3289   3548    366  -1752    -77       O  
ATOM    129  CB  ALA A  20       2.931   1.031  47.013  1.00 27.31           C  
ANISOU  129  CB  ALA A  20     2953   3395   4027    777  -1674   -177       C  
ATOM    130  N   GLN A  21       0.881   3.511  47.158  1.00 30.93           N  
ANISOU  130  N   GLN A  21     3753   3775   4226    331  -1424    -99       N  
ATOM    131  CA  GLN A  21       0.650   4.956  47.116  1.00 25.90           C  
ANISOU  131  CA  GLN A  21     3146   3178   3516    131  -1364   -103       C  
ATOM    132  C   GLN A  21      -0.045   5.432  48.378  1.00 28.30           C  
ANISOU  132  C   GLN A  21     3711   3353   3687     70  -1393    -37       C  
ATOM    133  O   GLN A  21       0.279   6.503  48.907  1.00 24.77           O  
ANISOU  133  O   GLN A  21     3296   2949   3167    -65  -1440    -51       O  
ATOM    134  CB  GLN A  21      -0.179   5.357  45.894  1.00 21.19           C  
ANISOU  134  CB  GLN A  21     2531   2568   2952     49  -1177   -118       C  
ATOM    135  CG  GLN A  21      -0.094   6.862  45.623  1.00 25.09           C  
ANISOU  135  CG  GLN A  21     3013   3116   3404   -145  -1134   -123       C  
ATOM    136  CD  GLN A  21      -0.986   7.331  44.500  1.00 27.81           C  
ANISOU  136  CD  GLN A  21     3377   3428   3761   -216   -983   -106       C  
ATOM    137  OE1 GLN A  21      -1.232   6.616  43.540  1.00 22.62           O  
ANISOU  137  OE1 GLN A  21     2642   2802   3152   -157   -913   -128       O  
ATOM    138  NE2 GLN A  21      -1.483   8.556  44.621  1.00 32.55           N  
ANISOU  138  NE2 GLN A  21     4091   3960   4317   -341   -942    -69       N  
ATOM    139  N   LEU A  22      -1.026   4.660  48.852  1.00 25.29           N  
ANISOU  139  N   LEU A  22     3528   2812   3270    147  -1343     20       N  
ATOM    140  CA  LEU A  22      -1.671   4.970  50.119  1.00 31.93           C  
ANISOU  140  CA  LEU A  22     4627   3537   3970     89  -1350     69       C  
ATOM    141  C   LEU A  22      -0.644   4.998  51.238  1.00 30.52           C  
ANISOU  141  C   LEU A  22     4485   3424   3688     96  -1564     89       C  
ATOM    142  O   LEU A  22      -0.677   5.882  52.107  1.00 30.61           O  
ANISOU  142  O   LEU A  22     4627   3431   3570    -30  -1595     82       O  
ATOM    143  CB  LEU A  22      -2.767   3.941  50.410  1.00 26.32           C  
ANISOU  143  CB  LEU A  22     4101   2658   3241    164  -1255    122       C  
ATOM    144  CG  LEU A  22      -3.555   4.119  51.705  1.00 30.40           C  
ANISOU  144  CG  LEU A  22     4901   3051   3599     92  -1217    164       C  
ATOM    145  CD1 LEU A  22      -4.337   5.402  51.632  1.00 20.93           C  
ANISOU  145  CD1 LEU A  22     3733   1832   2387    -47  -1072    111       C  
ATOM    146  CD2 LEU A  22      -4.501   2.949  51.957  1.00 28.93           C  
ANISOU  146  CD2 LEU A  22     4883   2708   3400    151  -1119    216       C  
ATOM    147  N   ARG A  23       0.292   4.043  51.209  1.00 33.39           N  
ANISOU  147  N   ARG A  23     4724   3851   4112    249  -1721    105       N  
ATOM    148  CA  ARG A  23       1.366   3.981  52.196  1.00 38.22           C  
ANISOU  148  CA  ARG A  23     5328   4551   4642    285  -1971    129       C  
ATOM    149  C   ARG A  23       2.286   5.197  52.105  1.00 38.33           C  
ANISOU  149  C   ARG A  23     5157   4753   4655    135  -2043     42       C  
ATOM    150  O   ARG A  23       2.528   5.876  53.109  1.00 40.16           O  
ANISOU  150  O   ARG A  23     5504   5016   4737     20  -2154     42       O  
ATOM    151  CB  ARG A  23       2.162   2.687  52.006  1.00 40.21           C  
ANISOU  151  CB  ARG A  23     5443   4824   5011    516  -2120    156       C  
ATOM    152  CG  ARG A  23       2.527   1.973  53.302  1.00 46.40           C  
ANISOU  152  CG  ARG A  23     6402   5552   5674    619  -2318    261       C  
ATOM    153  CD  ARG A  23       3.321   0.691  53.048  1.00 53.38           C  
ANISOU  153  CD  ARG A  23     7133   6437   6713    849  -2390    278       C  
ATOM    154  NE  ARG A  23       2.600  -0.245  52.185  1.00 56.12           N  
ANISOU  154  NE  ARG A  23     7512   6625   7185    963  -2247    280       N  
ATOM    155  CZ  ARG A  23       3.029  -0.675  50.998  1.00 51.06           C  
ANISOU  155  CZ  ARG A  23     6610   6041   6751   1072  -2187    185       C  
ATOM    156  NH1 ARG A  23       4.198  -0.270  50.511  1.00 45.72           N  
ANISOU  156  NH1 ARG A  23     5607   5583   6181   1082  -2245     84       N  
ATOM    157  NH2 ARG A  23       2.284  -1.523  50.299  1.00 42.35           N  
ANISOU  157  NH2 ARG A  23     5573   4779   5739   1154  -2047    179       N  
ATOM    158  N   GLU A  24       2.817   5.489  50.914  1.00 33.27           N  
ANISOU  158  N   GLU A  24     4238   4239   4166    112  -1974    -40       N  
ATOM    159  CA  GLU A  24       3.860   6.510  50.812  1.00 29.30           C  
ANISOU  159  CA  GLU A  24     3533   3925   3675    -38  -2050   -127       C  
ATOM    160  C   GLU A  24       3.272   7.911  50.761  1.00 27.71           C  
ANISOU  160  C   GLU A  24     3457   3673   3399   -272  -1906   -155       C  
ATOM    161  O   GLU A  24       3.739   8.811  51.464  1.00 31.43           O  
ANISOU  161  O   GLU A  24     3964   4202   3778   -427  -1996   -195       O  
ATOM    162  CB  GLU A  24       4.730   6.259  49.579  1.00 33.94           C  
ANISOU  162  CB  GLU A  24     3775   4676   4443      8  -2016   -212       C  
ATOM    163  CG  GLU A  24       5.564   4.983  49.679  1.00 47.13           C  
ANISOU  163  CG  GLU A  24     5274   6414   6220    250  -2171   -214       C  
ATOM    164  CD  GLU A  24       6.258   4.622  48.378  1.00 56.36           C  
ANISOU  164  CD  GLU A  24     6117   7724   7575    309  -2072   -320       C  
ATOM    165  OE1 GLU A  24       5.725   4.969  47.294  1.00 53.60           O  
ANISOU  165  OE1 GLU A  24     5746   7362   7259    211  -1869   -358       O  
ATOM    166  OE2 GLU A  24       7.338   3.990  48.450  1.00 56.37           O  
ANISOU  166  OE2 GLU A  24     5910   7843   7666    439  -2147   -352       O  
ATOM    167  N   VAL A  25       2.246   8.102  49.932  1.00 32.06           N  
ANISOU  167  N   VAL A  25     4079   4110   3994   -294  -1692   -137       N  
ATOM    168  CA  VAL A  25       1.622   9.405  49.739  1.00 31.64           C  
ANISOU  168  CA  VAL A  25     4139   3979   3905   -478  -1551   -153       C  
ATOM    169  C   VAL A  25       0.587   9.682  50.824  1.00 36.31           C  
ANISOU  169  C   VAL A  25     5033   4393   4371   -504  -1511   -119       C  
ATOM    170  O   VAL A  25       0.475  10.809  51.316  1.00 29.73           O  
ANISOU  170  O   VAL A  25     4319   3511   3467   -661  -1484   -158       O  
ATOM    171  CB  VAL A  25       0.996   9.477  48.331  1.00 30.32           C  
ANISOU  171  CB  VAL A  25     3901   3780   3841   -475  -1368   -142       C  
ATOM    172  CG1 VAL A  25       0.161  10.722  48.178  1.00 33.14           C  
ANISOU  172  CG1 VAL A  25     4411   4009   4173   -615  -1237   -130       C  
ATOM    173  CG2 VAL A  25       2.068   9.423  47.266  1.00 27.64           C  
ANISOU  173  CG2 VAL A  25     3279   3628   3596   -506  -1373   -198       C  
ATOM    174  N   GLY A  26      -0.191   8.674  51.211  1.00 23.76           N  
ANISOU  174  N   GLY A  26     3578   2698   2752   -364  -1487    -59       N  
ATOM    175  CA  GLY A  26      -1.260   8.869  52.164  1.00 23.55           C  
ANISOU  175  CA  GLY A  26     3827   2512   2609   -398  -1404    -41       C  
ATOM    176  C   GLY A  26      -2.631   8.965  51.538  1.00 22.65           C  
ANISOU  176  C   GLY A  26     3774   2261   2570   -378  -1189    -30       C  
ATOM    177  O   GLY A  26      -3.626   8.980  52.270  1.00 28.25           O  
ANISOU  177  O   GLY A  26     4684   2841   3207   -391  -1089    -27       O  
ATOM    178  N   THR A  27      -2.705   8.996  50.208  1.00 20.67           N  
ANISOU  178  N   THR A  27     3348   2050   2456   -352  -1118    -29       N  
ATOM    179  CA  THR A  27      -3.940   9.156  49.457  1.00 19.27           C  
ANISOU  179  CA  THR A  27     3189   1774   2360   -333   -949    -17       C  
ATOM    180  C   THR A  27      -3.745   8.505  48.098  1.00 22.33           C  
ANISOU  180  C   THR A  27     3379   2250   2855   -261   -935     -4       C  
ATOM    181  O   THR A  27      -2.663   8.583  47.519  1.00 26.38           O  
ANISOU  181  O   THR A  27     3727   2899   3397   -286  -1008    -24       O  
ATOM    182  CB  THR A  27      -4.298  10.640  49.281  1.00 25.54           C  
ANISOU  182  CB  THR A  27     4030   2500   3173   -451   -870    -43       C  
ATOM    183  OG1 THR A  27      -4.311  11.269  50.562  1.00 26.04           O  
ANISOU  183  OG1 THR A  27     4274   2491   3128   -533   -881    -86       O  
ATOM    184  CG2 THR A  27      -5.677  10.792  48.651  1.00 23.70           C  
ANISOU  184  CG2 THR A  27     3818   2158   3030   -402   -722    -25       C  
ATOM    185  N   VAL A  28      -4.786   7.851  47.596  1.00 21.88           N  
ANISOU  185  N   VAL A  28     3333   2128   2853   -187   -833     13       N  
ATOM    186  CA  VAL A  28      -4.757   7.274  46.261  1.00 16.91           C  
ANISOU  186  CA  VAL A  28     2541   1577   2307   -139   -803      9       C  
ATOM    187  C   VAL A  28      -6.148   7.405  45.653  1.00 15.99           C  
ANISOU  187  C   VAL A  28     2451   1382   2241   -134   -682     21       C  
ATOM    188  O   VAL A  28      -7.156   7.293  46.359  1.00 24.31           O  
ANISOU  188  O   VAL A  28     3628   2321   3287   -116   -613     22       O  
ATOM    189  CB  VAL A  28      -4.271   5.813  46.312  1.00 25.26           C  
ANISOU  189  CB  VAL A  28     3549   2664   3384    -20   -858     -1       C  
ATOM    190  CG1 VAL A  28      -5.266   4.940  47.088  1.00 23.32           C  
ANISOU  190  CG1 VAL A  28     3473   2273   3114     41   -804     23       C  
ATOM    191  CG2 VAL A  28      -4.054   5.286  44.925  1.00 30.78           C  
ANISOU  191  CG2 VAL A  28     4074   3459   4161     13   -820    -37       C  
HETATM  192  N   MSE A  29      -6.197   7.683  44.350  1.00 15.63           N  
ANISOU  192  N   MSE A  29     2287   1412   2239   -159   -657     26       N  
HETATM  193  CA  MSE A  29      -7.452   7.759  43.586  1.00 15.07           C  
ANISOU  193  CA  MSE A  29     2205   1302   2217   -146   -580     41       C  
HETATM  194  C   MSE A  29      -7.530   6.594  42.611  1.00 20.91           C  
ANISOU  194  C   MSE A  29     2839   2123   2983   -100   -563      9       C  
HETATM  195  O   MSE A  29      -6.643   6.406  41.775  1.00 22.90           O  
ANISOU  195  O   MSE A  29     2982   2497   3221   -121   -589    -11       O  
HETATM  196  CB  MSE A  29      -7.564   9.084  42.807  1.00 17.53           C  
ANISOU  196  CB  MSE A  29     2500   1623   2536   -220   -583     89       C  
HETATM  197  CG  MSE A  29      -8.856   9.239  42.053  1.00 22.37           C  
ANISOU  197  CG  MSE A  29     3094   2204   3204   -187   -544    117       C  
HETATM  198 SE   MSE A  29      -9.144  11.118  41.574  1.00 32.38          SE  
ANISOU  198 SE   MSE A  29     4425   3387   4492   -245   -569    209      SE  
HETATM  199  CE  MSE A  29      -7.588  11.395  40.393  1.00 20.87           C  
ANISOU  199  CE  MSE A  29     2898   2098   2935   -383   -618    247       C  
ATOM    200  N   LEU A  30      -8.595   5.819  42.716  1.00 19.72           N  
ANISOU  200  N   LEU A  30     2718   1906   2869    -54   -502    -12       N  
ATOM    201  CA  LEU A  30      -8.727   4.663  41.845  1.00 16.94           C  
ANISOU  201  CA  LEU A  30     2286   1611   2541    -26   -478    -62       C  
ATOM    202  C   LEU A  30      -9.582   5.019  40.633  1.00 22.50           C  
ANISOU  202  C   LEU A  30     2913   2380   3258    -66   -460    -57       C  
ATOM    203  O   LEU A  30     -10.531   5.801  40.756  1.00 21.24           O  
ANISOU  203  O   LEU A  30     2776   2168   3127    -74   -450    -20       O  
ATOM    204  CB  LEU A  30      -9.362   3.503  42.606  1.00 14.62           C  
ANISOU  204  CB  LEU A  30     2078   1203   2274     22   -422    -94       C  
ATOM    205  CG  LEU A  30      -8.775   3.263  44.001  1.00 23.64           C  
ANISOU  205  CG  LEU A  30     3350   2254   3376     59   -455    -67       C  
ATOM    206  CD1 LEU A  30      -9.626   2.259  44.790  1.00 23.00           C  
ANISOU  206  CD1 LEU A  30     3401   2038   3302     73   -377    -77       C  
ATOM    207  CD2 LEU A  30      -7.326   2.804  43.925  1.00 25.76           C  
ANISOU  207  CD2 LEU A  30     3563   2589   3635    116   -547    -76       C  
ATOM    208  N   PRO A  31      -9.287   4.504  39.444  1.00 20.36           N  
ANISOU  208  N   PRO A  31     2549   2225   2963    -88   -462    -98       N  
ATOM    209  CA  PRO A  31     -10.088   4.866  38.271  1.00 18.09           C  
ANISOU  209  CA  PRO A  31     2203   2017   2655   -136   -474    -82       C  
ATOM    210  C   PRO A  31     -11.401   4.105  38.254  1.00 22.30           C  
ANISOU  210  C   PRO A  31     2721   2507   3244   -119   -434   -133       C  
ATOM    211  O   PRO A  31     -11.543   3.026  38.838  1.00 20.65           O  
ANISOU  211  O   PRO A  31     2546   2224   3076    -91   -376   -199       O  
ATOM    212  CB  PRO A  31      -9.198   4.456  37.092  1.00 18.54           C  
ANISOU  212  CB  PRO A  31     2182   2224   2639   -186   -472   -132       C  
ATOM    213  CG  PRO A  31      -8.362   3.317  37.625  1.00 20.33           C  
ANISOU  213  CG  PRO A  31     2399   2420   2904   -123   -435   -219       C  
ATOM    214  CD  PRO A  31      -8.195   3.568  39.117  1.00 24.33           C  
ANISOU  214  CD  PRO A  31     2995   2796   3455    -65   -457   -170       C  
ATOM    215  N   ALA A  32     -12.378   4.692  37.576  1.00 17.28           N  
ANISOU  215  N   ALA A  32     2036   1916   2614   -141   -474    -98       N  
ATOM    216  CA  ALA A  32     -13.616   3.970  37.294  1.00 21.50           C  
ANISOU  216  CA  ALA A  32     2509   2461   3201   -151   -451   -166       C  
ATOM    217  C   ALA A  32     -13.325   2.853  36.291  1.00 21.01           C  
ANISOU  217  C   ALA A  32     2403   2504   3078   -206   -436   -262       C  
ATOM    218  O   ALA A  32     -12.680   3.098  35.269  1.00 23.19           O  
ANISOU  218  O   ALA A  32     2654   2904   3254   -251   -479   -250       O  
ATOM    219  CB  ALA A  32     -14.661   4.939  36.740  1.00 16.44           C  
ANISOU  219  CB  ALA A  32     1798   1863   2585   -143   -532   -101       C  
ATOM    220  N   TYR A  33     -13.779   1.622  36.555  1.00 17.24           N  
ANISOU  220  N   TYR A  33     1929   1970   2653   -218   -361   -367       N  
ATOM    221  CA  TYR A  33     -14.617   1.234  37.660  1.00 16.29           C  
ANISOU  221  CA  TYR A  33     1846   1714   2629   -202   -286   -390       C  
ATOM    222  C   TYR A  33     -13.994   0.060  38.407  1.00 16.50           C  
ANISOU  222  C   TYR A  33     1983   1614   2673   -182   -202   -443       C  
ATOM    223  O   TYR A  33     -14.590  -1.014  38.481  1.00 17.33           O  
ANISOU  223  O   TYR A  33     2109   1655   2820   -228   -127   -529       O  
ATOM    224  CB  TYR A  33     -15.995   0.829  37.128  1.00 17.19           C  
ANISOU  224  CB  TYR A  33     1857   1883   2792   -269   -277   -466       C  
ATOM    225  CG  TYR A  33     -16.705   1.956  36.412  1.00 25.96           C  
ANISOU  225  CG  TYR A  33     2852   3111   3900   -261   -391   -401       C  
ATOM    226  CD1 TYR A  33     -17.550   2.803  37.107  1.00 17.86           C  
ANISOU  226  CD1 TYR A  33     1785   2029   2973   -208   -392   -352       C  
ATOM    227  CD2 TYR A  33     -16.535   2.168  35.042  1.00 24.27           C  
ANISOU  227  CD2 TYR A  33     2582   3059   3582   -303   -499   -388       C  
ATOM    228  CE1 TYR A  33     -18.206   3.833  36.482  1.00 18.66           C  
ANISOU  228  CE1 TYR A  33     1783   2210   3097   -168   -512   -284       C  
ATOM    229  CE2 TYR A  33     -17.191   3.210  34.398  1.00 22.92           C  
ANISOU  229  CE2 TYR A  33     2330   2979   3401   -283   -631   -300       C  
ATOM    230  CZ  TYR A  33     -18.031   4.030  35.126  1.00 21.22           C  
ANISOU  230  CZ  TYR A  33     2065   2684   3312   -202   -645   -245       C  
ATOM    231  OH  TYR A  33     -18.692   5.062  34.513  1.00 26.03           O  
ANISOU  231  OH  TYR A  33     2595   3359   3938   -150   -791   -152       O  
ATOM    232  N   VAL A  34     -12.798   0.269  38.945  1.00 16.84           N  
ANISOU  232  N   VAL A  34     2097   1617   2686   -116   -225   -389       N  
ATOM    233  CA  VAL A  34     -12.055  -0.802  39.608  1.00 22.42           C  
ANISOU  233  CA  VAL A  34     2906   2203   3408    -64   -187   -419       C  
ATOM    234  C   VAL A  34     -12.765  -1.259  40.879  1.00 25.01           C  
ANISOU  234  C   VAL A  34     3366   2362   3774    -71   -112   -401       C  
ATOM    235  O   VAL A  34     -13.088  -2.439  41.033  1.00 20.45           O  
ANISOU  235  O   VAL A  34     2863   1676   3230    -95    -39   -460       O  
ATOM    236  CB  VAL A  34     -10.618  -0.341  39.901  1.00 24.79           C  
ANISOU  236  CB  VAL A  34     3216   2530   3673     11   -257   -364       C  
ATOM    237  CG1 VAL A  34      -9.934  -1.277  40.875  1.00 24.13           C  
ANISOU  237  CG1 VAL A  34     3249   2304   3615     96   -255   -360       C  
ATOM    238  CG2 VAL A  34      -9.828  -0.201  38.587  1.00 24.30           C  
ANISOU  238  CG2 VAL A  34     3029   2632   3570     -5   -287   -414       C  
ATOM    239  N   ALA A  35     -13.023  -0.335  41.813  1.00 20.89           N  
ANISOU  239  N   ALA A  35     2893   1805   3239    -66   -114   -325       N  
ATOM    240  CA  ALA A  35     -13.532  -0.768  43.115  1.00 18.85           C  
ANISOU  240  CA  ALA A  35     2790   1392   2981    -87    -27   -307       C  
ATOM    241  C   ALA A  35     -15.020  -1.109  43.075  1.00 23.85           C  
ANISOU  241  C   ALA A  35     3384   2002   3676   -186     91   -377       C  
ATOM    242  O   ALA A  35     -15.462  -2.056  43.741  1.00 25.05           O  
ANISOU  242  O   ALA A  35     3660   2023   3834   -242    195   -401       O  
ATOM    243  CB  ALA A  35     -13.277   0.310  44.168  1.00 16.03           C  
ANISOU  243  CB  ALA A  35     2509   1009   2572    -64    -51   -228       C  
ATOM    244  N   PHE A  36     -15.811  -0.323  42.344  1.00 19.70           N  
ANISOU  244  N   PHE A  36     2689   1599   3197   -211     74   -404       N  
ATOM    245  CA  PHE A  36     -17.245  -0.533  42.214  1.00 17.86           C  
ANISOU  245  CA  PHE A  36     2358   1385   3045   -298    165   -485       C  
ATOM    246  C   PHE A  36     -17.603  -0.490  40.740  1.00 18.36           C  
ANISOU  246  C   PHE A  36     2234   1607   3134   -319     80   -538       C  
ATOM    247  O   PHE A  36     -17.228   0.455  40.041  1.00 20.59           O  
ANISOU  247  O   PHE A  36     2436   1998   3388   -262    -38   -481       O  
ATOM    248  CB  PHE A  36     -18.016   0.534  42.969  1.00 20.22           C  
ANISOU  248  CB  PHE A  36     2620   1675   3389   -288    217   -468       C  
ATOM    249  CG  PHE A  36     -17.771   0.511  44.431  1.00 27.13           C  
ANISOU  249  CG  PHE A  36     3692   2409   4207   -296    313   -431       C  
ATOM    250  CD1 PHE A  36     -18.592  -0.233  45.264  1.00 28.84           C  
ANISOU  250  CD1 PHE A  36     3993   2530   4437   -400    482   -487       C  
ATOM    251  CD2 PHE A  36     -16.721   1.217  44.985  1.00 29.81           C  
ANISOU  251  CD2 PHE A  36     4145   2718   4465   -223    238   -344       C  
ATOM    252  CE1 PHE A  36     -18.373  -0.265  46.630  1.00 24.62           C  
ANISOU  252  CE1 PHE A  36     3673   1871   3812   -426    572   -445       C  
ATOM    253  CE2 PHE A  36     -16.495   1.186  46.352  1.00 29.86           C  
ANISOU  253  CE2 PHE A  36     4349   2608   4388   -244    310   -311       C  
ATOM    254  CZ  PHE A  36     -17.322   0.442  47.175  1.00 22.67           C  
ANISOU  254  CZ  PHE A  36     3543   1602   3470   -343    476   -356       C  
ATOM    255  N   ASP A  37     -18.293  -1.523  40.269  1.00 18.72           N  
ANISOU  255  N   ASP A  37     2231   1663   3217   -418    138   -645       N  
ATOM    256  CA  ASP A  37     -18.637  -1.603  38.863  1.00 22.05           C  
ANISOU  256  CA  ASP A  37     2493   2248   3636   -461     49   -710       C  
ATOM    257  C   ASP A  37     -19.629  -0.493  38.523  1.00 25.13           C  
ANISOU  257  C   ASP A  37     2696   2766   4086   -441    -26   -689       C  
ATOM    258  O   ASP A  37     -20.228   0.124  39.408  1.00 21.86           O  
ANISOU  258  O   ASP A  37     2260   2299   3748   -410     34   -666       O  
ATOM    259  CB  ASP A  37     -19.191  -2.994  38.532  1.00 26.03           C  
ANISOU  259  CB  ASP A  37     3000   2721   4170   -593    137   -849       C  
ATOM    260  CG  ASP A  37     -18.142  -4.102  38.703  1.00 29.38           C  
ANISOU  260  CG  ASP A  37     3614   2998   4552   -581    190   -868       C  
ATOM    261  OD1 ASP A  37     -16.932  -3.795  38.682  1.00 25.75           O  
ANISOU  261  OD1 ASP A  37     3220   2531   4033   -469    124   -794       O  
ATOM    262  OD2 ASP A  37     -18.522  -5.286  38.851  1.00 29.63           O  
ANISOU  262  OD2 ASP A  37     3723   2914   4621   -682    299   -963       O  
ATOM    263  N   ALA A  38     -19.761  -0.196  37.226  1.00 21.13           N  
ANISOU  263  N   ALA A  38     2062   2429   3539   -449   -164   -694       N  
ATOM    264  CA  ALA A  38     -20.623   0.918  36.843  1.00 27.21           C  
ANISOU  264  CA  ALA A  38     2662   3310   4366   -397   -277   -647       C  
ATOM    265  C   ALA A  38     -22.081   0.620  37.179  1.00 31.33           C  
ANISOU  265  C   ALA A  38     3019   3853   5031   -459   -206   -756       C  
ATOM    266  O   ALA A  38     -22.801   1.489  37.685  1.00 22.80           O  
ANISOU  266  O   ALA A  38     1834   2765   4064   -383   -204   -730       O  
ATOM    267  CB  ALA A  38     -20.465   1.237  35.356  1.00 23.09           C  
ANISOU  267  CB  ALA A  38     2065   2968   3740   -406   -457   -615       C  
ATOM    268  N   HIS A  39     -22.539  -0.609  36.916  1.00 23.25           N  
ANISOU  268  N   HIS A  39     1965   2853   4017   -603   -135   -893       N  
ATOM    269  CA  HIS A  39     -23.931  -0.901  37.233  1.00 24.84           C  
ANISOU  269  CA  HIS A  39     1986   3091   4360   -691    -54  -1012       C  
ATOM    270  C   HIS A  39     -24.179  -0.855  38.737  1.00 24.68           C  
ANISOU  270  C   HIS A  39     2045   2905   4426   -688    148  -1017       C  
ATOM    271  O   HIS A  39     -25.294  -0.554  39.157  1.00 27.15           O  
ANISOU  271  O   HIS A  39     2181   3257   4877   -705    216  -1086       O  
ATOM    272  CB  HIS A  39     -24.358  -2.246  36.634  1.00 31.15           C  
ANISOU  272  CB  HIS A  39     2748   3939   5146   -880     -9  -1171       C  
ATOM    273  CG  HIS A  39     -23.769  -3.432  37.322  1.00 31.27           C  
ANISOU  273  CG  HIS A  39     2999   3755   5125   -973    174  -1217       C  
ATOM    274  ND1 HIS A  39     -22.573  -3.996  36.933  1.00 31.38           N  
ANISOU  274  ND1 HIS A  39     3202   3699   5021   -954    154  -1193       N  
ATOM    275  CD2 HIS A  39     -24.218  -4.172  38.365  1.00 31.94           C  
ANISOU  275  CD2 HIS A  39     3169   3688   5280  -1083    381  -1282       C  
ATOM    276  CE1 HIS A  39     -22.306  -5.032  37.712  1.00 35.15           C  
ANISOU  276  CE1 HIS A  39     3872   3976   5509  -1023    320  -1231       C  
ATOM    277  NE2 HIS A  39     -23.289  -5.163  38.585  1.00 35.61           N  
ANISOU  277  NE2 HIS A  39     3889   3976   5666  -1114    459  -1276       N  
ATOM    278  N   GLU A  40     -23.153  -1.116  39.551  1.00 23.29           N  
ANISOU  278  N   GLU A  40     2126   2558   4166   -664    240   -948       N  
ATOM    279  CA  GLU A  40     -23.293  -1.012  41.000  1.00 27.35           C  
ANISOU  279  CA  GLU A  40     2757   2920   4713   -668    419   -936       C  
ATOM    280  C   GLU A  40     -23.397   0.441  41.441  1.00 30.25           C  
ANISOU  280  C   GLU A  40     3062   3300   5132   -523    379   -861       C  
ATOM    281  O   GLU A  40     -24.184   0.774  42.337  1.00 27.56           O  
ANISOU  281  O   GLU A  40     2669   2920   4884   -536    521   -915       O  
ATOM    282  CB  GLU A  40     -22.106  -1.682  41.689  1.00 22.18           C  
ANISOU  282  CB  GLU A  40     2401   2090   3937   -670    482   -867       C  
ATOM    283  CG  GLU A  40     -21.961  -3.179  41.379  1.00 30.28           C  
ANISOU  283  CG  GLU A  40     3530   3045   4931   -798    542   -942       C  
ATOM    284  CD  GLU A  40     -20.746  -3.797  42.053  1.00 30.20           C  
ANISOU  284  CD  GLU A  40     3806   2849   4819   -756    572   -858       C  
ATOM    285  OE1 GLU A  40     -19.641  -3.231  41.921  1.00 30.52           O  
ANISOU  285  OE1 GLU A  40     3902   2903   4791   -619    449   -759       O  
ATOM    286  OE2 GLU A  40     -20.895  -4.832  42.740  1.00 28.44           O  
ANISOU  286  OE2 GLU A  40     3754   2464   4589   -861    713   -886       O  
ATOM    287  N   LEU A  41     -22.595   1.319  40.840  1.00 21.86           N  
ANISOU  287  N   LEU A  41     2016   2279   4009   -393    204   -746       N  
ATOM    288  CA  LEU A  41     -22.725   2.738  41.150  1.00 26.80           C  
ANISOU  288  CA  LEU A  41     2590   2894   4697   -257    157   -679       C  
ATOM    289  C   LEU A  41     -24.076   3.261  40.701  1.00 28.02           C  
ANISOU  289  C   LEU A  41     2463   3164   5020   -218    113   -746       C  
ATOM    290  O   LEU A  41     -24.687   4.075  41.396  1.00 28.92           O  
ANISOU  290  O   LEU A  41     2502   3232   5254   -140    186   -771       O  
ATOM    291  CB  LEU A  41     -21.596   3.540  40.507  1.00 24.79           C  
ANISOU  291  CB  LEU A  41     2421   2656   4342   -156    -18   -539       C  
ATOM    292  CG  LEU A  41     -20.253   3.271  41.188  1.00 30.52           C  
ANISOU  292  CG  LEU A  41     3394   3268   4936   -166     27   -478       C  
ATOM    293  CD1 LEU A  41     -19.204   4.264  40.739  1.00 22.98           C  
ANISOU  293  CD1 LEU A  41     2500   2326   3904    -82   -114   -356       C  
ATOM    294  CD2 LEU A  41     -20.394   3.279  42.711  1.00 22.79           C  
ANISOU  294  CD2 LEU A  41     2544   2146   3970   -184    200   -506       C  
ATOM    295  N   ALA A  42     -24.550   2.810  39.539  1.00 24.53           N  
ANISOU  295  N   ALA A  42     1854   2878   4589   -265    -13   -787       N  
ATOM    296  CA  ALA A  42     -25.902   3.147  39.105  1.00 26.69           C  
ANISOU  296  CA  ALA A  42     1825   3285   5031   -236    -75   -867       C  
ATOM    297  C   ALA A  42     -26.939   2.757  40.158  1.00 29.59           C  
ANISOU  297  C   ALA A  42     2081   3615   5548   -319    161  -1021       C  
ATOM    298  O   ALA A  42     -27.842   3.541  40.466  1.00 33.68           O  
ANISOU  298  O   ALA A  42     2396   4158   6241   -222    184  -1070       O  
ATOM    299  CB  ALA A  42     -26.205   2.467  37.770  1.00 34.20           C  
ANISOU  299  CB  ALA A  42     2641   4419   5935   -326   -234   -911       C  
ATOM    300  N   ARG A  43     -26.813   1.566  40.737  1.00 27.80           N  
ANISOU  300  N   ARG A  43     1992   3314   5256   -498    349  -1100       N  
ATOM    301  CA  ARG A  43     -27.749   1.156  41.776  1.00 36.14           C  
ANISOU  301  CA  ARG A  43     2979   4328   6424   -615    605  -1241       C  
ATOM    302  C   ARG A  43     -27.650   2.070  42.992  1.00 34.77           C  
ANISOU  302  C   ARG A  43     2905   4026   6281   -516    745  -1213       C  
ATOM    303  O   ARG A  43     -28.664   2.574  43.494  1.00 31.01           O  
ANISOU  303  O   ARG A  43     2227   3581   5973   -490    865  -1321       O  
ATOM    304  CB  ARG A  43     -27.494  -0.296  42.172  1.00 29.15           C  
ANISOU  304  CB  ARG A  43     2295   3348   5434   -832    773  -1297       C  
ATOM    305  CG  ARG A  43     -28.572  -0.881  43.071  1.00 36.65           C  
ANISOU  305  CG  ARG A  43     3166   4275   6484  -1014   1047  -1455       C  
ATOM    306  CD  ARG A  43     -28.228  -2.310  43.483  1.00 41.09           C  
ANISOU  306  CD  ARG A  43     3990   4696   6926  -1229   1207  -1477       C  
ATOM    307  NE  ARG A  43     -29.287  -2.932  44.279  1.00 44.88           N  
ANISOU  307  NE  ARG A  43     4447   5162   7442  -1400   1458  -1604       N  
ATOM    308  CZ  ARG A  43     -29.089  -3.944  45.122  1.00 51.66           C  
ANISOU  308  CZ  ARG A  43     5609   5863   8157  -1536   1641  -1583       C  
ATOM    309  NH1 ARG A  43     -27.869  -4.443  45.283  1.00 55.69           N  
ANISOU  309  NH1 ARG A  43     6441   6211   8509  -1512   1594  -1446       N  
ATOM    310  NH2 ARG A  43     -30.104  -4.450  45.814  1.00 51.27           N  
ANISOU  310  NH2 ARG A  43     5546   5820   8114  -1678   1856  -1693       N  
ATOM    311  N   ILE A  44     -26.430   2.284  43.488  1.00 32.64           N  
ANISOU  311  N   ILE A  44     2936   3616   5852   -465    737  -1084       N  
ATOM    312  CA  ILE A  44     -26.229   3.162  44.640  1.00 31.98           C  
ANISOU  312  CA  ILE A  44     2979   3408   5764   -388    858  -1062       C  
ATOM    313  C   ILE A  44     -26.870   4.517  44.392  1.00 28.18           C  
ANISOU  313  C   ILE A  44     2269   2977   5461   -204    776  -1077       C  
ATOM    314  O   ILE A  44     -27.543   5.074  45.270  1.00 29.62           O  
ANISOU  314  O   ILE A  44     2384   3114   5757   -175    950  -1175       O  
ATOM    315  CB  ILE A  44     -24.728   3.302  44.951  1.00 33.04           C  
ANISOU  315  CB  ILE A  44     3430   3422   5701   -345    784   -912       C  
ATOM    316  CG1 ILE A  44     -24.160   1.974  45.449  1.00 33.12           C  
ANISOU  316  CG1 ILE A  44     3680   3346   5558   -501    886   -901       C  
ATOM    317  CG2 ILE A  44     -24.489   4.453  45.947  1.00 24.89           C  
ANISOU  317  CG2 ILE A  44     2509   2284   4665   -251    856   -891       C  
ATOM    318  CD1 ILE A  44     -22.651   1.973  45.497  1.00 35.19           C  
ANISOU  318  CD1 ILE A  44     4191   3529   5650   -442    762   -759       C  
ATOM    319  N   ASP A  45     -26.709   5.045  43.178  1.00 31.84           N  
ANISOU  319  N   ASP A  45     2613   3530   5954    -78    516   -986       N  
ATOM    320  CA  ASP A  45     -27.275   6.349  42.845  1.00 40.10           C  
ANISOU  320  CA  ASP A  45     3464   4598   7174    122    399   -969       C  
ATOM    321  C   ASP A  45     -28.798   6.339  42.928  1.00 43.73           C  
ANISOU  321  C   ASP A  45     3580   5162   7874    133    490  -1140       C  
ATOM    322  O   ASP A  45     -29.401   7.271  43.477  1.00 50.84           O  
ANISOU  322  O   ASP A  45     4361   6009   8949    268    570  -1205       O  
ATOM    323  CB  ASP A  45     -26.819   6.777  41.453  1.00 47.95           C  
ANISOU  323  CB  ASP A  45     4427   5675   8118    224     92   -819       C  
ATOM    324  CG  ASP A  45     -26.408   8.225  41.408  1.00 56.93           C  
ANISOU  324  CG  ASP A  45     5636   6704   9291    417    -26   -694       C  
ATOM    325  OD1 ASP A  45     -26.656   8.935  42.409  1.00 52.36           O  
ANISOU  325  OD1 ASP A  45     5081   5995   8816    492    124   -753       O  
ATOM    326  OD2 ASP A  45     -25.828   8.649  40.385  1.00 63.05           O  
ANISOU  326  OD2 ASP A  45     6462   7514   9982    478   -255   -544       O  
ATOM    327  N   ALA A  46     -29.441   5.304  42.379  1.00 42.20           N  
ANISOU  327  N   ALA A  46     3208   5120   7707     -9    485  -1233       N  
ATOM    328  CA  ALA A  46     -30.896   5.210  42.477  1.00 39.08           C  
ANISOU  328  CA  ALA A  46     2451   4850   7549    -28    582  -1419       C  
ATOM    329  C   ALA A  46     -31.338   5.082  43.928  1.00 40.54           C  
ANISOU  329  C   ALA A  46     2687   4936   7780   -127    934  -1565       C  
ATOM    330  O   ALA A  46     -32.353   5.659  44.331  1.00 47.68           O  
ANISOU  330  O   ALA A  46     3436   5861   8818    -51   1007  -1659       O  
ATOM    331  CB  ALA A  46     -31.409   4.023  41.659  1.00 36.61           C  
ANISOU  331  CB  ALA A  46     2032   4703   7175   -210    512  -1479       C  
ATOM    332  N   LEU A  47     -30.578   4.344  44.732  1.00 40.48           N  
ANISOU  332  N   LEU A  47     3001   4804   7576   -298   1117  -1544       N  
ATOM    333  CA  LEU A  47     -30.981   4.112  46.114  1.00 44.65           C  
ANISOU  333  CA  LEU A  47     3611   5247   8107   -433   1464  -1677       C  
ATOM    334  C   LEU A  47     -30.815   5.362  46.968  1.00 43.56           C  
ANISOU  334  C   LEU A  47     3557   4985   8010   -269   1551  -1677       C  
ATOM    335  O   LEU A  47     -31.699   5.689  47.767  1.00 50.33           O  
ANISOU  335  O   LEU A  47     4316   5837   8970   -285   1756  -1822       O  
ATOM    336  CB  LEU A  47     -30.184   2.951  46.704  1.00 43.09           C  
ANISOU  336  CB  LEU A  47     3778   4938   7657   -655   1595  -1622       C  
ATOM    337  CG  LEU A  47     -30.540   1.544  46.226  1.00 37.86           C  
ANISOU  337  CG  LEU A  47     3068   4350   6969   -880   1629  -1683       C  
ATOM    338  CD1 LEU A  47     -29.500   0.550  46.711  1.00 33.63           C  
ANISOU  338  CD1 LEU A  47     2944   3653   6181  -1026   1693  -1575       C  
ATOM    339  CD2 LEU A  47     -31.909   1.164  46.743  1.00 44.36           C  
ANISOU  339  CD2 LEU A  47     3725   5241   7889  -1017   1842  -1869       C  
ATOM    340  N   GLN A  48     -29.692   6.074  46.828  1.00 37.38           N  
ANISOU  340  N   GLN A  48     3009   4092   7103   -129   1375  -1504       N  
ATOM    341  CA  GLN A  48     -29.473   7.229  47.699  1.00 39.83           C  
ANISOU  341  CA  GLN A  48     3437   4262   7434     -2   1472  -1517       C  
ATOM    342  C   GLN A  48     -30.494   8.333  47.433  1.00 45.73           C  
ANISOU  342  C   GLN A  48     3854   5045   8475    213   1438  -1614       C  
ATOM    343  O   GLN A  48     -30.883   9.060  48.361  1.00 43.62           O  
ANISOU  343  O   GLN A  48     3635   4697   8243    246   1597  -1698       O  
ATOM    344  CB  GLN A  48     -28.033   7.742  47.551  1.00 32.12           C  
ANISOU  344  CB  GLN A  48     2771   3168   6266     77   1281  -1317       C  
ATOM    345  CG  GLN A  48     -27.625   8.127  46.146  1.00 36.60           C  
ANISOU  345  CG  GLN A  48     3249   3796   6861    221    948  -1162       C  
ATOM    346  CD  GLN A  48     -27.977   9.559  45.828  1.00 38.68           C  
ANISOU  346  CD  GLN A  48     3370   4007   7319    461    832  -1144       C  
ATOM    347  OE1 GLN A  48     -28.051  10.398  46.727  1.00 35.81           O  
ANISOU  347  OE1 GLN A  48     3081   3511   7016    531    980  -1214       O  
ATOM    348  NE2 GLN A  48     -28.217   9.846  44.552  1.00 42.71           N  
ANISOU  348  NE2 GLN A  48     3691   4612   7926    588    568  -1054       N  
ATOM    349  N   ALA A  49     -30.972   8.445  46.191  1.00 42.12           N  
ANISOU  349  N   ALA A  49     3143   4719   8141    325   1173  -1557       N  
ATOM    350  CA  ALA A  49     -32.010   9.420  45.876  1.00 46.86           C  
ANISOU  350  CA  ALA A  49     3511   5365   8930    511   1061  -1585       C  
ATOM    351  C   ALA A  49     -33.226   9.269  46.790  1.00 46.96           C  
ANISOU  351  C   ALA A  49     3381   5422   9040    420   1321  -1789       C  
ATOM    352  O   ALA A  49     -33.836  10.265  47.195  1.00 51.91           O  
ANISOU  352  O   ALA A  49     3926   5999   9799    565   1363  -1849       O  
ATOM    353  CB  ALA A  49     -32.416   9.281  44.407  1.00 49.60           C  
ANISOU  353  CB  ALA A  49     3631   5880   9334    592    746  -1495       C  
ATOM    354  N   ARG A  50     -33.584   8.028  47.137  1.00 50.40           N  
ANISOU  354  N   ARG A  50     3801   5942   9407    171   1504  -1899       N  
ATOM    355  CA  ARG A  50     -34.743   7.747  47.983  1.00 49.65           C  
ANISOU  355  CA  ARG A  50     3582   5897   9385     43   1760  -2095       C  
ATOM    356  C   ARG A  50     -34.559   8.197  49.425  1.00 47.44           C  
ANISOU  356  C   ARG A  50     3520   5466   9039    -15   2047  -2176       C  
ATOM    357  O   ARG A  50     -35.533   8.197  50.182  1.00 50.38           O  
ANISOU  357  O   ARG A  50     3789   5869   9484    -95   2261  -2343       O  
ATOM    358  CB  ARG A  50     -35.056   6.248  47.974  1.00 47.03           C  
ANISOU  358  CB  ARG A  50     3247   5664   8958   -238   1877  -2169       C  
ATOM    359  CG  ARG A  50     -35.343   5.651  46.595  1.00 53.14           C  
ANISOU  359  CG  ARG A  50     3818   6607   9767   -233   1615  -2117       C  
ATOM    360  CD  ARG A  50     -36.061   4.313  46.730  1.00 59.76           C  
ANISOU  360  CD  ARG A  50     4609   7541  10556   -506   1770  -2246       C  
ATOM    361  NE  ARG A  50     -36.508   3.766  45.448  1.00 64.90           N  
ANISOU  361  NE  ARG A  50     5052   8369  11238   -515   1532  -2225       N  
ATOM    362  CZ  ARG A  50     -37.626   4.126  44.817  1.00 70.46           C  
ANISOU  362  CZ  ARG A  50     5426   9237  12109   -408   1393  -2286       C  
ATOM    363  NH1 ARG A  50     -38.435   5.049  45.333  1.00 69.39           N  
ANISOU  363  NH1 ARG A  50     5110   9104  12149   -266   1469  -2375       N  
ATOM    364  NH2 ARG A  50     -37.933   3.562  43.656  1.00 75.83           N  
ANISOU  364  NH2 ARG A  50     5959  10080  12774   -442   1174  -2256       N  
ATOM    365  N   LEU A  51     -33.351   8.568  49.822  1.00 41.78           N  
ANISOU  365  N   LEU A  51     3314   4044   8518   -982   1903   -445       N  
ATOM    366  CA  LEU A  51     -33.048   8.906  51.200  1.00 41.85           C  
ANISOU  366  CA  LEU A  51     3512   3919   8470   -865   2267   -502       C  
ATOM    367  C   LEU A  51     -33.499  10.324  51.537  1.00 44.38           C  
ANISOU  367  C   LEU A  51     3721   4196   8946   -717   2370   -466       C  
ATOM    368  O   LEU A  51     -33.622  11.177  50.652  1.00 47.07           O  
ANISOU  368  O   LEU A  51     3869   4632   9383   -687   2112   -412       O  
ATOM    369  CB  LEU A  51     -31.549   8.763  51.447  1.00 39.27           C  
ANISOU  369  CB  LEU A  51     3448   3607   7865   -859   2268   -612       C  
ATOM    370  CG  LEU A  51     -31.028   7.341  51.295  1.00 47.29           C  
ANISOU  370  CG  LEU A  51     4633   4601   8736   -988   2232   -651       C  
ATOM    371  CD1 LEU A  51     -29.534   7.295  51.571  1.00 47.18           C  
ANISOU  371  CD1 LEU A  51     4948   4616   8361   -887   2129   -716       C  
ATOM    372  CD2 LEU A  51     -31.761   6.437  52.248  1.00 49.96           C  
ANISOU  372  CD2 LEU A  51     5083   4793   9108  -1031   2524   -616       C  
ATOM    373  N   PRO A  52     -33.766  10.596  52.817  1.00 45.07           N  
ANISOU  373  N   PRO A  52     3959   4123   9041   -627   2759   -490       N  
ATOM    374  CA  PRO A  52     -34.066  11.974  53.230  1.00 48.38           C  
ANISOU  374  CA  PRO A  52     4341   4456   9585   -483   2902   -483       C  
ATOM    375  C   PRO A  52     -32.817  12.849  53.246  1.00 47.06           C  
ANISOU  375  C   PRO A  52     4324   4332   9223   -419   2817   -582       C  
ATOM    376  O   PRO A  52     -31.736  12.435  53.676  1.00 42.43           O  
ANISOU  376  O   PRO A  52     4000   3765   8357   -443   2866   -674       O  
ATOM    377  CB  PRO A  52     -34.645  11.805  54.640  1.00 48.25           C  
ANISOU  377  CB  PRO A  52     4533   4244   9554   -428   3367   -495       C  
ATOM    378  CG  PRO A  52     -34.049  10.543  55.127  1.00 51.91           C  
ANISOU  378  CG  PRO A  52     5260   4709   9753   -526   3453   -547       C  
ATOM    379  CD  PRO A  52     -33.952   9.640  53.924  1.00 47.19           C  
ANISOU  379  CD  PRO A  52     4460   4264   9208   -660   3094   -509       C  
ATOM    380  N   GLU A  53     -32.990  14.083  52.792  1.00 45.56           N  
ANISOU  380  N   GLU A  53     3965   4149   9196   -334   2691   -546       N  
ATOM    381  CA  GLU A  53     -31.909  15.037  52.639  1.00 41.75           C  
ANISOU  381  CA  GLU A  53     3555   3715   8594   -273   2558   -616       C  
ATOM    382  C   GLU A  53     -32.056  16.134  53.687  1.00 51.60           C  
ANISOU  382  C   GLU A  53     4982   4770   9853   -130   2877   -679       C  
ATOM    383  O   GLU A  53     -33.168  16.590  53.964  1.00 55.83           O  
ANISOU  383  O   GLU A  53     5415   5176  10624    -75   3064   -609       O  
ATOM    384  CB  GLU A  53     -31.943  15.622  51.227  1.00 45.29           C  
ANISOU  384  CB  GLU A  53     3719   4313   9176   -295   2127   -516       C  
ATOM    385  CG  GLU A  53     -30.645  16.202  50.739  1.00 49.55           C  
ANISOU  385  CG  GLU A  53     4300   4968   9557   -288   1869   -559       C  
ATOM    386  CD  GLU A  53     -30.643  16.427  49.236  1.00 53.68           C  
ANISOU  386  CD  GLU A  53     4635   5675  10087   -341   1424   -443       C  
ATOM    387  OE1 GLU A  53     -29.694  15.960  48.562  1.00 46.00           O  
ANISOU  387  OE1 GLU A  53     3723   4860   8897   -410   1180   -457       O  
ATOM    388  OE2 GLU A  53     -31.589  17.073  48.731  1.00 60.74           O  
ANISOU  388  OE2 GLU A  53     5347   6550  11181   -311   1341   -329       O  
ATOM    389  N   GLU A  54     -30.939  16.542  54.283  1.00 56.34           N  
ANISOU  389  N   GLU A  54     5927   5336  10142    -69   2883   -803       N  
ATOM    390  CA  GLU A  54     -30.940  17.620  55.260  1.00 55.87           C  
ANISOU  390  CA  GLU A  54     6152   5071  10004     63   3134   -897       C  
ATOM    391  C   GLU A  54     -29.798  18.580  54.963  1.00 53.31           C  
ANISOU  391  C   GLU A  54     5979   4787   9490     86   2765   -930       C  
ATOM    392  O   GLU A  54     -28.738  18.169  54.478  1.00 48.13           O  
ANISOU  392  O   GLU A  54     5386   4298   8604      3   2393   -905       O  
ATOM    393  CB  GLU A  54     -30.816  17.088  56.698  1.00 60.58           C  
ANISOU  393  CB  GLU A  54     7262   5523  10232     59   3454   -989       C  
ATOM    394  CG  GLU A  54     -29.488  16.417  57.021  1.00 64.16           C  
ANISOU  394  CG  GLU A  54     8107   6053  10217    -25   3189  -1031       C  
ATOM    395  CD  GLU A  54     -29.623  15.301  58.046  1.00 75.82           C  
ANISOU  395  CD  GLU A  54     9910   7455  11442    -82   3469  -1049       C  
ATOM    396  OE1 GLU A  54     -30.617  14.542  57.983  1.00 79.19           O  
ANISOU  396  OE1 GLU A  54    10105   7877  12106   -111   3735   -993       O  
ATOM    397  OE2 GLU A  54     -28.732  15.183  58.914  1.00 79.22           O  
ANISOU  397  OE2 GLU A  54    10827   7827  11445   -112   3401  -1100       O  
ATOM    398  N   PRO A  55     -29.995  19.868  55.222  1.00 52.16           N  
ANISOU  398  N   PRO A  55     5877   4477   9465    200   2869   -974       N  
ATOM    399  CA  PRO A  55     -28.941  20.841  54.940  1.00 49.34           C  
ANISOU  399  CA  PRO A  55     5652   4137   8959    204   2508   -991       C  
ATOM    400  C   PRO A  55     -27.864  20.818  56.012  1.00 55.21           C  
ANISOU  400  C   PRO A  55     6981   4791   9205    165   2455  -1100       C  
ATOM    401  O   PRO A  55     -28.124  20.552  57.187  1.00 61.48           O  
ANISOU  401  O   PRO A  55     8158   5415   9787    183   2794  -1202       O  
ATOM    402  CB  PRO A  55     -29.696  22.174  54.931  1.00 44.62           C  
ANISOU  402  CB  PRO A  55     4908   3341   8704    344   2694  -1001       C  
ATOM    403  CG  PRO A  55     -30.815  21.956  55.887  1.00 47.96           C  
ANISOU  403  CG  PRO A  55     5432   3631   9158    384   3169  -1014       C  
ATOM    404  CD  PRO A  55     -31.197  20.499  55.793  1.00 47.21           C  
ANISOU  404  CD  PRO A  55     5201   3671   9066    288   3253   -957       C  
ATOM    405  N   VAL A  56     -26.633  21.079  55.578  1.00 55.00           N  
ANISOU  405  N   VAL A  56     7020   4885   8994     97   2011  -1057       N  
ATOM    406  CA  VAL A  56     -25.475  21.114  56.470  1.00 57.05           C  
ANISOU  406  CA  VAL A  56     7785   5078   8815     29   1844  -1111       C  
ATOM    407  C   VAL A  56     -24.481  22.189  56.011  1.00 58.84           C  
ANISOU  407  C   VAL A  56     8012   5324   9021      0   1435  -1064       C  
ATOM    408  O   VAL A  56     -24.845  23.167  55.343  1.00 58.26           O  
ANISOU  408  O   VAL A  56     7674   5221   9240     62   1391  -1037       O  
ATOM    409  CB  VAL A  56     -24.783  19.728  56.553  1.00 56.91           C  
ANISOU  409  CB  VAL A  56     7855   5224   8546    -68   1703  -1049       C  
ATOM    410  CG1 VAL A  56     -23.385  19.861  57.133  1.00 57.62           C  
ANISOU  410  CG1 VAL A  56     8329   5296   8268   -154   1374  -1027       C  
ATOM    411  CG2 VAL A  56     -25.609  18.745  57.383  1.00 56.52           C  
ANISOU  411  CG2 VAL A  56     7972   5088   8417    -64   2114  -1107       C  
ATOM    412  N   HIS A  65     -27.082  27.506  53.235  1.00 64.51           N  
ANISOU  412  N   HIS A  65     7473   5606  11434    415   1455   -889       N  
ATOM    413  CA  HIS A  65     -27.369  26.127  52.841  1.00 63.32           C  
ANISOU  413  CA  HIS A  65     7089   5709  11262    353   1486   -827       C  
ATOM    414  C   HIS A  65     -26.842  25.799  51.445  1.00 56.64           C  
ANISOU  414  C   HIS A  65     5866   5182  10471    245   1059   -647       C  
ATOM    415  O   HIS A  65     -27.550  25.987  50.460  1.00 56.99           O  
ANISOU  415  O   HIS A  65     5475   5311  10867    261    995   -513       O  
ATOM    416  CB  HIS A  65     -28.875  25.864  52.871  1.00 68.99           C  
ANISOU  416  CB  HIS A  65     7511   6343  12358    462   1896   -812       C  
ATOM    417  CG  HIS A  65     -29.478  25.894  54.240  1.00 74.32           C  
ANISOU  417  CG  HIS A  65     8550   6750  12939    562   2400   -977       C  
ATOM    418  ND1 HIS A  65     -30.840  25.842  54.451  1.00 77.19           N  
ANISOU  418  ND1 HIS A  65     8701   7088  13540    614   2747   -904       N  
ATOM    419  CD2 HIS A  65     -28.910  25.962  55.467  1.00 75.19           C  
ANISOU  419  CD2 HIS A  65     9250   6710  12608    545   2526  -1143       C  
ATOM    420  CE1 HIS A  65     -31.085  25.882  55.748  1.00 80.32           C  
ANISOU  420  CE1 HIS A  65     9527   7325  13667    651   3106  -1027       C  
ATOM    421  NE2 HIS A  65     -29.931  25.954  56.386  1.00 79.76           N  
ANISOU  421  NE2 HIS A  65     9960   7189  13157    608   2969  -1177       N  
ATOM    422  N   ASP A  66     -25.611  25.298  51.345  1.00 50.91           N  
ANISOU  422  N   ASP A  66     5310   4629   9406    132    771   -629       N  
ATOM    423  CA  ASP A  66     -25.086  24.907  50.045  1.00 47.39           C  
ANISOU  423  CA  ASP A  66     4552   4477   8978     40    432   -471       C  
ATOM    424  C   ASP A  66     -24.536  23.485  50.012  1.00 37.15           C  
ANISOU  424  C   ASP A  66     3330   3376   7410    -41    394   -480       C  
ATOM    425  O   ASP A  66     -24.008  23.065  48.974  1.00 31.79           O  
ANISOU  425  O   ASP A  66     2452   2929   6698   -111    151   -370       O  
ATOM    426  CB  ASP A  66     -24.012  25.903  49.572  1.00 53.01           C  
ANISOU  426  CB  ASP A  66     5277   5224   9642     -6     71   -372       C  
ATOM    427  CG  ASP A  66     -22.919  26.107  50.590  1.00 60.38           C  
ANISOU  427  CG  ASP A  66     6647   6042  10254    -45    -16   -449       C  
ATOM    428  OD1 ASP A  66     -22.929  25.387  51.612  1.00 59.77           O  
ANISOU  428  OD1 ASP A  66     6877   5884   9950    -43    182   -574       O  
ATOM    429  OD2 ASP A  66     -22.056  26.990  50.364  1.00 62.09           O  
ANISOU  429  OD2 ASP A  66     6899   6244  10449    -95   -303   -367       O  
ATOM    430  N   ILE A  67     -24.661  22.728  51.098  1.00 40.72           N  
ANISOU  430  N   ILE A  67     4075   3727   7669    -28    643   -602       N  
ATOM    431  CA  ILE A  67     -24.350  21.304  51.108  1.00 41.49           C  
ANISOU  431  CA  ILE A  67     4227   3969   7567    -89    657   -607       C  
ATOM    432  C   ILE A  67     -25.529  20.566  51.722  1.00 42.78           C  
ANISOU  432  C   ILE A  67     4410   4029   7815    -59   1040   -692       C  
ATOM    433  O   ILE A  67     -26.007  20.940  52.799  1.00 35.24           O  
ANISOU  433  O   ILE A  67     3696   2855   6837      5   1324   -793       O  
ATOM    434  CB  ILE A  67     -23.053  21.005  51.882  1.00 35.35           C  
ANISOU  434  CB  ILE A  67     3821   3181   6430   -130    517   -623       C  
ATOM    435  CG1 ILE A  67     -21.880  21.659  51.178  1.00 33.08           C  
ANISOU  435  CG1 ILE A  67     3443   3015   6111   -171    138   -499       C  
ATOM    436  CG2 ILE A  67     -22.828  19.528  51.962  1.00 33.60           C  
ANISOU  436  CG2 ILE A  67     3653   3066   6045   -169    570   -622       C  
ATOM    437  CD1 ILE A  67     -20.562  21.314  51.768  1.00 33.36           C  
ANISOU  437  CD1 ILE A  67     3745   3066   5863   -223    -52   -456       C  
ATOM    438  N   TYR A  68     -26.008  19.535  51.028  1.00 43.13           N  
ANISOU  438  N   TYR A  68     4213   4218   7955   -112   1059   -648       N  
ATOM    439  CA  TYR A  68     -27.121  18.714  51.484  1.00 40.90           C  
ANISOU  439  CA  TYR A  68     3894   3859   7789   -114   1393   -693       C  
ATOM    440  C   TYR A  68     -26.635  17.284  51.684  1.00 40.01           C  
ANISOU  440  C   TYR A  68     3953   3828   7422   -186   1393   -714       C  
ATOM    441  O   TYR A  68     -25.967  16.722  50.808  1.00 35.15           O  
ANISOU  441  O   TYR A  68     3245   3387   6724   -247   1140   -661       O  
ATOM    442  CB  TYR A  68     -28.281  18.769  50.487  1.00 37.66           C  
ANISOU  442  CB  TYR A  68     3023   3510   7778   -139   1398   -600       C  
ATOM    443  CG  TYR A  68     -29.027  20.084  50.520  1.00 40.40           C  
ANISOU  443  CG  TYR A  68     3188   3713   8450    -39   1501   -567       C  
ATOM    444  CD1 TYR A  68     -30.140  20.254  51.329  1.00 41.33           C  
ANISOU  444  CD1 TYR A  68     3278   3627   8798     50   1910   -602       C  
ATOM    445  CD2 TYR A  68     -28.600  21.162  49.760  1.00 41.66           C  
ANISOU  445  CD2 TYR A  68     3206   3923   8700    -22   1212   -489       C  
ATOM    446  CE1 TYR A  68     -30.821  21.457  51.370  1.00 45.94           C  
ANISOU  446  CE1 TYR A  68     3730   4053   9672    157   2011   -558       C  
ATOM    447  CE2 TYR A  68     -29.265  22.369  49.794  1.00 46.43           C  
ANISOU  447  CE2 TYR A  68     3649   4368   9626     82   1305   -450       C  
ATOM    448  CZ  TYR A  68     -30.375  22.513  50.600  1.00 50.92           C  
ANISOU  448  CZ  TYR A  68     4222   4724  10402    177   1703   -486       C  
ATOM    449  OH  TYR A  68     -31.037  23.716  50.627  1.00 57.93           O  
ANISOU  449  OH  TYR A  68     5020   5439  11551    271   1777   -426       O  
ATOM    450  N   VAL A  69     -26.974  16.704  52.834  1.00 38.93           N  
ANISOU  450  N   VAL A  69     4080   3549   7163   -174   1696   -787       N  
ATOM    451  CA  VAL A  69     -26.400  15.447  53.301  1.00 33.60           C  
ANISOU  451  CA  VAL A  69     3652   2897   6215   -229   1707   -802       C  
ATOM    452  C   VAL A  69     -27.514  14.415  53.450  1.00 34.88           C  
ANISOU  452  C   VAL A  69     3710   3016   6527   -278   1994   -805       C  
ATOM    453  O   VAL A  69     -28.562  14.704  54.043  1.00 37.98           O  
ANISOU  453  O   VAL A  69     4070   3270   7091   -240   2324   -829       O  
ATOM    454  CB  VAL A  69     -25.639  15.650  54.627  1.00 34.40           C  
ANISOU  454  CB  VAL A  69     4232   2862   5977   -203   1759   -856       C  
ATOM    455  CG1 VAL A  69     -25.137  14.333  55.181  1.00 34.23           C  
ANISOU  455  CG1 VAL A  69     4458   2843   5706   -256   1780   -840       C  
ATOM    456  CG2 VAL A  69     -24.461  16.593  54.406  1.00 34.43           C  
ANISOU  456  CG2 VAL A  69     4311   2913   5857   -189   1416   -824       C  
ATOM    457  N   ARG A  70     -27.287  13.221  52.901  1.00 33.81           N  
ANISOU  457  N   ARG A  70     3520   2984   6344   -360   1883   -775       N  
ATOM    458  CA  ARG A  70     -28.176  12.070  53.058  1.00 40.98           C  
ANISOU  458  CA  ARG A  70     4371   3840   7358   -438   2108   -769       C  
ATOM    459  C   ARG A  70     -27.449  11.023  53.886  1.00 38.18           C  
ANISOU  459  C   ARG A  70     4386   3429   6692   -455   2158   -785       C  
ATOM    460  O   ARG A  70     -26.537  10.358  53.389  1.00 44.44           O  
ANISOU  460  O   ARG A  70     5231   4309   7343   -476   1928   -765       O  
ATOM    461  CB  ARG A  70     -28.582  11.507  51.700  1.00 39.24           C  
ANISOU  461  CB  ARG A  70     3813   3750   7348   -543   1920   -723       C  
ATOM    462  CG  ARG A  70     -29.705  12.265  51.061  1.00 35.58           C  
ANISOU  462  CG  ARG A  70     2957   3301   7262   -564   1933   -665       C  
ATOM    463  CD  ARG A  70     -29.680  12.128  49.557  1.00 45.38           C  
ANISOU  463  CD  ARG A  70     3963   4709   8571   -653   1577   -611       C  
ATOM    464  NE  ARG A  70     -30.959  12.518  48.972  1.00 52.59           N  
ANISOU  464  NE  ARG A  70     4652   5637   9694   -650   1479   -502       N  
ATOM    465  CZ  ARG A  70     -31.181  12.632  47.669  1.00 50.63           C  
ANISOU  465  CZ  ARG A  70     4263   5534   9440   -710   1149   -418       C  
ATOM    466  NH1 ARG A  70     -30.205  12.392  46.814  1.00 45.77           N  
ANISOU  466  NH1 ARG A  70     3720   5056   8616   -764    912   -446       N  
ATOM    467  NH2 ARG A  70     -32.381  12.982  47.221  1.00 55.11           N  
ANISOU  467  NH2 ARG A  70     4630   6104  10205   -723   1076   -297       N  
ATOM    468  N   ARG A  71     -27.841  10.880  55.142  1.00 36.85           N  
ANISOU  468  N   ARG A  71     4480   3105   6418   -440   2470   -807       N  
ATOM    469  CA  ARG A  71     -27.112  10.007  56.045  1.00 37.10           C  
ANISOU  469  CA  ARG A  71     4900   3067   6129   -460   2495   -797       C  
ATOM    470  C   ARG A  71     -27.495   8.546  55.832  1.00 37.44           C  
ANISOU  470  C   ARG A  71     4885   3098   6242   -553   2573   -759       C  
ATOM    471  O   ARG A  71     -28.659   8.209  55.607  1.00 38.93           O  
ANISOU  471  O   ARG A  71     4844   3255   6694   -618   2774   -747       O  
ATOM    472  CB  ARG A  71     -27.363  10.420  57.492  1.00 39.43           C  
ANISOU  472  CB  ARG A  71     5562   3191   6228   -428   2798   -833       C  
ATOM    473  CG  ARG A  71     -27.074  11.868  57.726  1.00 39.58           C  
ANISOU  473  CG  ARG A  71     5676   3178   6184   -348   2740   -891       C  
ATOM    474  CD  ARG A  71     -26.841  12.179  59.184  1.00 46.29           C  
ANISOU  474  CD  ARG A  71     7048   3855   6686   -339   2927   -938       C  
ATOM    475  NE  ARG A  71     -26.656  13.616  59.358  1.00 56.71           N  
ANISOU  475  NE  ARG A  71     8469   5110   7969   -272   2881  -1014       N  
ATOM    476  CZ  ARG A  71     -25.514  14.252  59.123  1.00 54.78           C  
ANISOU  476  CZ  ARG A  71     8309   4924   7581   -274   2488  -1000       C  
ATOM    477  NH1 ARG A  71     -24.448  13.574  58.716  1.00 54.16           N  
ANISOU  477  NH1 ARG A  71     8206   4978   7396   -321   2134   -904       N  
ATOM    478  NH2 ARG A  71     -25.438  15.562  59.298  1.00 52.54           N  
ANISOU  478  NH2 ARG A  71     8127   4550   7284   -226   2461  -1072       N  
ATOM    479  N   ILE A  72     -26.486   7.690  55.863  1.00 36.50           N  
ANISOU  479  N   ILE A  72     4959   2993   5916   -562   2393   -724       N  
ATOM    480  CA  ILE A  72     -26.656   6.248  55.827  1.00 37.07           C  
ANISOU  480  CA  ILE A  72     5072   3008   6005   -641   2460   -689       C  
ATOM    481  C   ILE A  72     -26.307   5.628  57.173  1.00 38.59           C  
ANISOU  481  C   ILE A  72     5675   3059   5927   -646   2605   -635       C  
ATOM    482  O   ILE A  72     -27.064   4.824  57.721  1.00 42.60           O  
ANISOU  482  O   ILE A  72     6263   3454   6471   -722   2866   -606       O  
ATOM    483  CB  ILE A  72     -25.804   5.637  54.693  1.00 35.25           C  
ANISOU  483  CB  ILE A  72     4731   2878   5786   -635   2162   -683       C  
ATOM    484  CG1 ILE A  72     -26.452   5.933  53.332  1.00 39.82           C  
ANISOU  484  CG1 ILE A  72     4933   3572   6625   -689   2061   -729       C  
ATOM    485  CG2 ILE A  72     -25.621   4.140  54.900  1.00 37.29           C  
ANISOU  485  CG2 ILE A  72     5156   3027   5986   -685   2213   -644       C  
ATOM    486  CD1 ILE A  72     -25.463   6.307  52.199  1.00 33.45           C  
ANISOU  486  CD1 ILE A  72     4012   2919   5777   -632   1751   -739       C  
HETATM  487  N   MSE A  73     -25.173   6.021  57.732  1.00 38.14           N  
ANISOU  487  N   MSE A  73     5885   3004   5602   -583   2423   -601       N  
HETATM  488  CA  MSE A  73     -24.763   5.602  59.057  1.00 39.88           C  
ANISOU  488  CA  MSE A  73     6536   3094   5524   -603   2500   -529       C  
HETATM  489  C   MSE A  73     -24.184   6.765  59.862  1.00 40.42           C  
ANISOU  489  C   MSE A  73     6882   3141   5334   -568   2411   -540       C  
HETATM  490  O   MSE A  73     -23.354   7.512  59.338  1.00 39.07           O  
ANISOU  490  O   MSE A  73     6609   3071   5164   -515   2113   -538       O  
HETATM  491  CB  MSE A  73     -23.741   4.499  58.930  1.00 39.37           C  
ANISOU  491  CB  MSE A  73     6562   3017   5381   -595   2277   -422       C  
HETATM  492  CG  MSE A  73     -23.088   4.121  60.202  1.00 48.27           C  
ANISOU  492  CG  MSE A  73     8119   4024   6197   -618   2245   -304       C  
HETATM  493 SE   MSE A  73     -22.560   2.278  59.996  1.00 60.94          SE  
ANISOU  493 SE   MSE A  73     9749   5538   7869   -624   2168   -167      SE  
HETATM  494  CE  MSE A  73     -24.264   1.424  60.344  1.00 56.10           C  
ANISOU  494  CE  MSE A  73     9141   4793   7381   -754   2635   -214       C  
ATOM    495  N   VAL A  74     -24.608   6.912  61.123  1.00 44.70           N  
ANISOU  495  N   VAL A  74     7795   3543   5646   -610   2669   -548       N  
ATOM    496  CA  VAL A  74     -24.148   7.991  61.990  1.00 44.16           C  
ANISOU  496  CA  VAL A  74     8083   3413   5285   -606   2607   -580       C  
ATOM    497  C   VAL A  74     -23.246   7.412  63.075  1.00 46.03           C  
ANISOU  497  C   VAL A  74     8794   3554   5139   -676   2448   -453       C  
ATOM    498  O   VAL A  74     -23.331   6.234  63.429  1.00 46.78           O  
ANISOU  498  O   VAL A  74     8998   3590   5186   -724   2539   -355       O  
ATOM    499  CB  VAL A  74     -25.321   8.774  62.621  1.00 50.73           C  
ANISOU  499  CB  VAL A  74     9036   4131   6108   -596   3044   -703       C  
ATOM    500  CG1 VAL A  74     -26.247   9.327  61.553  1.00 48.26           C  
ANISOU  500  CG1 VAL A  74     8213   3901   6224   -528   3176   -785       C  
ATOM    501  CG2 VAL A  74     -26.086   7.898  63.589  1.00 53.37           C  
ANISOU  501  CG2 VAL A  74     9636   4330   6313   -663   3444   -666       C  
ATOM    502  N   ASP A  75     -22.383   8.275  63.634  1.00 46.50           N  
ANISOU  502  N   ASP A  75     9156   3585   4927   -699   2188   -440       N  
ATOM    503  CA  ASP A  75     -21.347   7.861  64.585  1.00 51.23           C  
ANISOU  503  CA  ASP A  75    10186   4106   5170   -786   1912   -281       C  
ATOM    504  C   ASP A  75     -21.096   8.983  65.603  1.00 50.62           C  
ANISOU  504  C   ASP A  75    10605   3914   4716   -863   1849   -342       C  
ATOM    505  O   ASP A  75     -20.030   9.598  65.650  1.00 50.48           O  
ANISOU  505  O   ASP A  75    10682   3916   4580   -902   1424   -273       O  
ATOM    506  CB  ASP A  75     -20.059   7.482  63.849  1.00 46.16           C  
ANISOU  506  CB  ASP A  75     9284   3582   4671   -748   1440   -118       C  
ATOM    507  CG  ASP A  75     -19.026   6.860  64.764  1.00 49.39           C  
ANISOU  507  CG  ASP A  75    10057   3908   4801   -833   1140    101       C  
ATOM    508  OD1 ASP A  75     -19.405   6.430  65.871  1.00 50.93           O  
ANISOU  508  OD1 ASP A  75    10690   3964   4698   -928   1322    132       O  
ATOM    509  OD2 ASP A  75     -17.838   6.809  64.381  1.00 47.31           O  
ANISOU  509  OD2 ASP A  75     9637   3715   4625   -807    725    262       O  
ATOM    510  N   ARG A  76     -22.082   9.231  66.467  1.00 53.47           N  
ANISOU  510  N   ARG A  76    11311   4133   4873   -897   2287   -465       N  
ATOM    511  CA  ARG A  76     -22.044  10.381  67.366  1.00 55.98           C  
ANISOU  511  CA  ARG A  76    12129   4307   4835   -959   2322   -581       C  
ATOM    512  C   ARG A  76     -21.050  10.198  68.510  1.00 59.01           C  
ANISOU  512  C   ARG A  76    13120   4584   4718  -1124   1987   -441       C  
ATOM    513  O   ARG A  76     -20.784   9.080  68.965  1.00 59.73           O  
ANISOU  513  O   ARG A  76    13360   4660   4675  -1193   1925   -266       O  
ATOM    514  CB  ARG A  76     -23.427  10.649  67.953  1.00 62.26           C  
ANISOU  514  CB  ARG A  76    13124   4963   5571   -926   2962   -752       C  
ATOM    515  CG  ARG A  76     -24.461  10.992  66.918  1.00 61.15           C  
ANISOU  515  CG  ARG A  76    12400   4901   5933   -778   3273   -870       C  
ATOM    516  CD  ARG A  76     -25.752  11.415  67.565  1.00 65.65           C  
ANISOU  516  CD  ARG A  76    13125   5324   6496   -734   3877   -992       C  
ATOM    517  NE  ARG A  76     -26.865  11.206  66.649  1.00 71.19           N  
ANISOU  517  NE  ARG A  76    13198   6117   7736   -628   4170   -999       N  
ATOM    518  CZ  ARG A  76     -27.588  10.094  66.601  1.00 73.63           C  
ANISOU  518  CZ  ARG A  76    13315   6442   8219   -649   4438   -914       C  
ATOM    519  NH1 ARG A  76     -27.321   9.088  67.425  1.00 78.08           N  
ANISOU  519  NH1 ARG A  76    14268   6940   8458   -756   4482   -815       N  
ATOM    520  NH2 ARG A  76     -28.583   9.987  65.731  1.00 73.50           N  
ANISOU  520  NH2 ARG A  76    12718   6499   8708   -581   4628   -906       N  
ATOM    521  N   ALA A  77     -20.529  11.331  68.995  1.00 47.79           N  
ANISOU  521  N   ALA A  77    10197   4305   3655   -607   1497   -840       N  
ATOM    522  CA  ALA A  77     -19.543  11.331  70.071  1.00 48.67           C  
ANISOU  522  CA  ALA A  77    10626   4335   3529   -531   1240   -804       C  
ATOM    523  C   ALA A  77     -20.068  10.579  71.283  1.00 56.69           C  
ANISOU  523  C   ALA A  77    11960   5240   4341   -524   1456   -735       C  
ATOM    524  O   ALA A  77     -21.178  10.834  71.758  1.00 59.18           O  
ANISOU  524  O   ALA A  77    12308   5513   4666   -545   1783   -767       O  
ATOM    525  CB  ALA A  77     -19.180  12.766  70.461  1.00 49.14           C  
ANISOU  525  CB  ALA A  77    10712   4373   3585   -467   1071   -907       C  
ATOM    526  N   GLY A  78     -19.265   9.642  71.775  1.00 65.19           N  
ANISOU  526  N   GLY A  78    13265   6255   5250   -490   1273   -643       N  
ATOM    527  CA  GLY A  78     -19.657   8.812  72.893  1.00 70.51           C  
ANISOU  527  CA  GLY A  78    14265   6793   5733   -480   1454   -571       C  
ATOM    528  C   GLY A  78     -20.554   7.645  72.546  1.00 70.80           C  
ANISOU  528  C   GLY A  78    14233   6814   5855   -575   1768   -503       C  
ATOM    529  O   GLY A  78     -20.910   6.873  73.447  1.00 75.48           O  
ANISOU  529  O   GLY A  78    15097   7273   6309   -575   1935   -444       O  
ATOM    530  N   GLU A  79     -20.919   7.474  71.277  1.00 59.16           N  
ANISOU  530  N   GLU A  79    12412   5457   4608   -656   1848   -515       N  
ATOM    531  CA  GLU A  79     -21.880   6.456  70.891  1.00 57.10           C  
ANISOU  531  CA  GLU A  79    12039   5183   4472   -759   2156   -471       C  
ATOM    532  C   GLU A  79     -21.256   5.467  69.917  1.00 60.26           C  
ANISOU  532  C   GLU A  79    12311   5645   4939   -791   1988   -403       C  
ATOM    533  O   GLU A  79     -20.199   5.713  69.330  1.00 58.17           O  
ANISOU  533  O   GLU A  79    11970   5461   4673   -741   1664   -402       O  
ATOM    534  CB  GLU A  79     -23.132   7.086  70.265  1.00 56.83           C  
ANISOU  534  CB  GLU A  79    11683   5223   4686   -834   2460   -557       C  
ATOM    535  CG  GLU A  79     -23.911   7.995  71.209  1.00 65.28           C  
ANISOU  535  CG  GLU A  79    12860   6225   5718   -804   2679   -625       C  
ATOM    536  CD  GLU A  79     -25.141   8.609  70.557  1.00 67.05           C  
ANISOU  536  CD  GLU A  79    12731   6522   6225   -863   2962   -715       C  
ATOM    537  OE1 GLU A  79     -25.484   8.195  69.428  1.00 67.06           O  
ANISOU  537  OE1 GLU A  79    12416   6614   6451   -937   3013   -719       O  
ATOM    538  OE2 GLU A  79     -25.769   9.501  71.173  1.00 65.31           O  
ANISOU  538  OE2 GLU A  79    12542   6262   6008   -827   3126   -783       O  
ATOM    539  N   ARG A  80     -21.920   4.340  69.765  1.00 62.02           N  
ANISOU  539  N   ARG A  80    12511   5821   5234   -873   2210   -351       N  
ATOM    540  CA  ARG A  80     -21.531   3.338  68.790  1.00 56.53           C  
ANISOU  540  CA  ARG A  80    11675   5179   4625   -914   2104   -290       C  
ATOM    541  C   ARG A  80     -22.188   3.644  67.451  1.00 50.41           C  
ANISOU  541  C   ARG A  80    10490   4545   4116  -1003   2222   -343       C  
ATOM    542  O   ARG A  80     -23.186   4.369  67.396  1.00 50.93           O  
ANISOU  542  O   ARG A  80    10385   4640   4325  -1045   2457   -424       O  
ATOM    543  CB  ARG A  80     -21.927   1.950  69.289  1.00 58.25           C  
ANISOU  543  CB  ARG A  80    12072   5262   4800   -959   2273   -223       C  
ATOM    544  N   PRO A  81     -21.635   3.134  66.347  1.00 46.85           N  
ANISOU  544  N   PRO A  81     9871   4184   3745  -1021   2056   -301       N  
ATOM    545  CA  PRO A  81     -22.218   3.423  65.024  1.00 42.16           C  
ANISOU  545  CA  PRO A  81     8822   3721   3477  -1082   2093   -343       C  
ATOM    546  C   PRO A  81     -23.643   2.901  64.899  1.00 45.22           C  
ANISOU  546  C   PRO A  81     9075   4076   4029  -1211   2472   -368       C  
ATOM    547  O   PRO A  81     -23.962   1.805  65.355  1.00 50.17           O  
ANISOU  547  O   PRO A  81     9856   4596   4612  -1262   2610   -320       O  
ATOM    548  CB  PRO A  81     -21.277   2.699  64.052  1.00 39.10           C  
ANISOU  548  CB  PRO A  81     8300   3394   3163  -1055   1801   -267       C  
ATOM    549  CG  PRO A  81     -19.995   2.494  64.814  1.00 46.28           C  
ANISOU  549  CG  PRO A  81     9553   4239   3794   -955   1552   -210       C  
ATOM    550  CD  PRO A  81     -20.393   2.343  66.255  1.00 49.59           C  
ANISOU  550  CD  PRO A  81    10367   4513   3963   -956   1754   -211       C  
ATOM    551  N   GLN A  82     -24.497   3.683  64.246  1.00 42.59           N  
ANISOU  551  N   GLN A  82     8379   3830   3974  -1239   2566   -454       N  
ATOM    552  CA  GLN A  82     -25.914   3.356  64.133  1.00 42.04           C  
ANISOU  552  CA  GLN A  82     8125   3735   4116  -1357   2918   -502       C  
ATOM    553  C   GLN A  82     -26.368   3.465  62.689  1.00 41.89           C  
ANISOU  553  C   GLN A  82     7627   3838   4450  -1386   2809   -543       C  
ATOM    554  O   GLN A  82     -26.111   4.480  62.033  1.00 41.16           O  
ANISOU  554  O   GLN A  82     7313   3852   4473  -1305   2604   -586       O  
ATOM    555  CB  GLN A  82     -26.760   4.298  64.992  1.00 45.01           C  
ANISOU  555  CB  GLN A  82     8532   4068   4501  -1339   3169   -591       C  
ATOM    556  CG  GLN A  82     -26.507   4.179  66.480  1.00 49.20           C  
ANISOU  556  CG  GLN A  82     9486   4453   4754  -1283   3216   -557       C  
ATOM    557  CD  GLN A  82     -27.174   5.273  67.260  1.00 48.08           C  
ANISOU  557  CD  GLN A  82     9371   4276   4620  -1240   3394   -638       C  
ATOM    558  OE1 GLN A  82     -27.433   6.367  66.737  1.00 57.80           O  
ANISOU  558  OE1 GLN A  82    10361   5603   5996  -1210   3390   -723       O  
ATOM    559  NE2 GLN A  82     -27.454   5.000  68.521  1.00 52.82           N  
ANISOU  559  NE2 GLN A  82    10274   4730   5064  -1229   3553   -614       N  
ATOM    560  N   LEU A  83     -27.054   2.434  62.204  1.00 47.40           N  
ANISOU  560  N   LEU A  83     8184   4510   5317  -1501   2944   -533       N  
ATOM    561  CA  LEU A  83     -27.759   2.526  60.930  1.00 44.73           C  
ANISOU  561  CA  LEU A  83     7402   4269   5327  -1538   2885   -597       C  
ATOM    562  C   LEU A  83     -28.929   3.491  61.059  1.00 50.49           C  
ANISOU  562  C   LEU A  83     7892   5022   6272  -1548   3102   -709       C  
ATOM    563  O   LEU A  83     -29.627   3.509  62.078  1.00 55.44           O  
ANISOU  563  O   LEU A  83     8652   5556   6858  -1594   3422   -740       O  
ATOM    564  CB  LEU A  83     -28.283   1.151  60.504  1.00 46.68           C  
ANISOU  564  CB  LEU A  83     7576   4455   5704  -1673   2990   -575       C  
ATOM    565  CG  LEU A  83     -27.552   0.319  59.456  1.00 45.61           C  
ANISOU  565  CG  LEU A  83     7385   4359   5586  -1662   2705   -518       C  
ATOM    566  CD1 LEU A  83     -28.287  -0.991  59.233  1.00 46.56           C  
ANISOU  566  CD1 LEU A  83     7446   4399   5847  -1792   2845   -525       C  
ATOM    567  CD2 LEU A  83     -27.449   1.097  58.158  1.00 51.02           C  
ANISOU  567  CD2 LEU A  83     7728   5194   6464  -1579   2431   -569       C  
ATOM    568  N   VAL A  84     -29.145   4.300  60.018  1.00 47.81           N  
ANISOU  568  N   VAL A  84     7202   4800   6164  -1487   2917   -771       N  
ATOM    569  CA  VAL A  84     -30.241   5.261  59.984  1.00 40.90           C  
ANISOU  569  CA  VAL A  84     6057   3954   5530  -1472   3076   -883       C  
ATOM    570  C   VAL A  84     -30.821   5.282  58.580  1.00 41.43           C  
ANISOU  570  C   VAL A  84     5701   4114   5924  -1475   2909   -939       C  
ATOM    571  O   VAL A  84     -30.187   4.849  57.618  1.00 41.53           O  
ANISOU  571  O   VAL A  84     5662   4185   5932  -1455   2633   -890       O  
ATOM    572  CB  VAL A  84     -29.811   6.694  60.388  1.00 41.76           C  
ANISOU  572  CB  VAL A  84     6244   4095   5526  -1337   2995   -912       C  
ATOM    573  CG1 VAL A  84     -29.230   6.718  61.790  1.00 44.79           C  
ANISOU  573  CG1 VAL A  84     7070   4381   5569  -1322   3127   -871       C  
ATOM    574  CG2 VAL A  84     -28.816   7.261  59.380  1.00 37.63           C  
ANISOU  574  CG2 VAL A  84     5628   3676   4993  -1230   2599   -873       C  
ATOM    575  N   ASN A  85     -32.045   5.803  58.475  1.00 43.94           N  
ANISOU  575  N   ASN A  85     5723   4441   6529  -1490   3078  -1047       N  
ATOM    576  CA  ASN A  85     -32.757   5.931  57.199  1.00 45.53           C  
ANISOU  576  CA  ASN A  85     5512   4723   7063  -1478   2916  -1121       C  
ATOM    577  C   ASN A  85     -32.990   4.580  56.527  1.00 45.95           C  
ANISOU  577  C   ASN A  85     5467   4756   7235  -1602   2867  -1111       C  
ATOM    578  O   ASN A  85     -32.883   4.452  55.308  1.00 45.79           O  
ANISOU  578  O   ASN A  85     5261   4809   7329  -1566   2583  -1121       O  
ATOM    579  CB  ASN A  85     -32.030   6.880  56.254  1.00 42.21           C  
ANISOU  579  CB  ASN A  85     5016   4411   6612  -1325   2556  -1102       C  
ATOM    580  CG  ASN A  85     -32.082   8.297  56.740  1.00 47.82           C  
ANISOU  580  CG  ASN A  85     5735   5132   7303  -1209   2601  -1143       C  
ATOM    581  OD1 ASN A  85     -32.984   8.654  57.491  1.00 52.17           O  
ANISOU  581  OD1 ASN A  85     6225   5632   7965  -1230   2885  -1221       O  
ATOM    582  ND2 ASN A  85     -31.118   9.115  56.333  1.00 41.95           N  
ANISOU  582  ND2 ASN A  85     5070   4443   6426  -1089   2340  -1093       N  
ATOM    583  N   LEU A  86     -33.325   3.567  57.325  1.00 43.48           N  
ANISOU  583  N   LEU A  86     5306   4334   6879  -1729   3129  -1091       N  
ATOM    584  CA  LEU A  86     -33.684   2.264  56.782  1.00 52.12           C  
ANISOU  584  CA  LEU A  86     6322   5395   8087  -1819   3067  -1091       C  
ATOM    585  C   LEU A  86     -34.904   2.384  55.864  1.00 53.94           C  
ANISOU  585  C   LEU A  86     6116   5674   8706  -1820   2986  -1214       C  
ATOM    586  O   LEU A  86     -35.700   3.317  55.995  1.00 53.35           O  
ANISOU  586  O   LEU A  86     5831   5623   8815  -1762   3068  -1299       O  
ATOM    587  CB  LEU A  86     -33.968   1.289  57.925  1.00 57.26           C  
ANISOU  587  CB  LEU A  86     7227   5917   8612  -1893   3331  -1052       C  
ATOM    588  CG  LEU A  86     -32.748   0.914  58.768  1.00 55.98           C  
ANISOU  588  CG  LEU A  86     7523   5693   8053  -1882   3354   -927       C  
ATOM    589  CD1 LEU A  86     -33.155   0.281  60.088  1.00 58.91           C  
ANISOU  589  CD1 LEU A  86     8157   5927   8298  -1923   3644   -905       C  
ATOM    590  CD2 LEU A  86     -31.855  -0.018  57.982  1.00 51.56           C  
ANISOU  590  CD2 LEU A  86     7049   5145   7396  -1909   3116   -850       C  
ATOM    591  N   PRO A  87     -35.084   1.438  54.920  1.00 55.91           N  
ANISOU  591  N   PRO A  87     6233   5928   9084  -1877   2809  -1230       N  
ATOM    592  CA  PRO A  87     -34.285   0.241  54.639  1.00 51.10           C  
ANISOU  592  CA  PRO A  87     5836   5278   8300  -1942   2700  -1146       C  
ATOM    593  C   PRO A  87     -33.196   0.434  53.580  1.00 48.38           C  
ANISOU  593  C   PRO A  87     5518   5007   7855  -1889   2384  -1104       C  
ATOM    594  O   PRO A  87     -32.282  -0.383  53.496  1.00 47.88           O  
ANISOU  594  O   PRO A  87     5698   4905   7589  -1917   2304  -1017       O  
ATOM    595  CB  PRO A  87     -35.337  -0.744  54.131  1.00 54.60           C  
ANISOU  595  CB  PRO A  87     6059   5681   9004  -2027   2689  -1221       C  
ATOM    596  CG  PRO A  87     -36.253   0.134  53.333  1.00 55.04           C  
ANISOU  596  CG  PRO A  87     5722   5818   9371  -1963   2557  -1344       C  
ATOM    597  CD  PRO A  87     -36.278   1.486  54.056  1.00 52.60           C  
ANISOU  597  CD  PRO A  87     5415   5543   9026  -1874   2703  -1353       C  
ATOM    598  N   HIS A  88     -33.290   1.497  52.777  1.00 55.00           N  
ANISOU  598  N   HIS A  88     6133   5952   8815  -1779   2183  -1160       N  
ATOM    599  CA  HIS A  88     -32.389   1.622  51.635  1.00 49.93           C  
ANISOU  599  CA  HIS A  88     5527   5398   8047  -1653   1820  -1114       C  
ATOM    600  C   HIS A  88     -30.953   1.880  52.071  1.00 46.43           C  
ANISOU  600  C   HIS A  88     5418   4975   7249  -1559   1758   -981       C  
ATOM    601  O   HIS A  88     -30.016   1.500  51.360  1.00 41.54           O  
ANISOU  601  O   HIS A  88     4915   4388   6482  -1499   1535   -914       O  
ATOM    602  CB  HIS A  88     -32.891   2.716  50.697  1.00 45.45           C  
ANISOU  602  CB  HIS A  88     4671   4930   7668  -1526   1612  -1193       C  
ATOM    603  CG  HIS A  88     -34.299   2.499  50.237  1.00 52.05           C  
ANISOU  603  CG  HIS A  88     5151   5748   8878  -1603   1630  -1337       C  
ATOM    604  ND1 HIS A  88     -34.676   1.407  49.484  1.00 57.06           N  
ANISOU  604  ND1 HIS A  88     5685   6344   9652  -1699   1513  -1393       N  
ATOM    605  CD2 HIS A  88     -35.428   3.215  50.451  1.00 57.79           C  
ANISOU  605  CD2 HIS A  88     5590   6481   9889  -1600   1749  -1445       C  
ATOM    606  CE1 HIS A  88     -35.973   1.468  49.242  1.00 58.12           C  
ANISOU  606  CE1 HIS A  88     5515   6477  10090  -1709   1515  -1508       C  
ATOM    607  NE2 HIS A  88     -36.453   2.557  49.815  1.00 58.12           N  
ANISOU  607  NE2 HIS A  88     5396   6505  10183  -1642   1655  -1540       N  
ATOM    608  N   SER A  89     -30.756   2.493  53.238  1.00 39.34           N  
ANISOU  608  N   SER A  89     4678   4052   6219  -1544   1951   -947       N  
ATOM    609  CA  SER A  89     -29.405   2.656  53.767  1.00 37.85           C  
ANISOU  609  CA  SER A  89     4807   3865   5709  -1469   1885   -832       C  
ATOM    610  C   SER A  89     -28.679   1.315  53.863  1.00 36.34           C  
ANISOU  610  C   SER A  89     4856   3605   5346  -1532   1864   -749       C  
ATOM    611  O   SER A  89     -27.511   1.198  53.475  1.00 37.03           O  
ANISOU  611  O   SER A  89     5087   3728   5256  -1447   1657   -667       O  
ATOM    612  CB  SER A  89     -29.463   3.321  55.140  1.00 39.85           C  
ANISOU  612  CB  SER A  89     5225   4071   5846  -1468   2122   -827       C  
ATOM    613  OG  SER A  89     -30.053   2.454  56.106  1.00 41.54           O  
ANISOU  613  OG  SER A  89     5564   4167   6051  -1607   2429   -832       O  
ATOM    614  N   GLU A  90     -29.360   0.293  54.387  1.00 37.54           N  
ANISOU  614  N   GLU A  90     5053   3649   5563  -1680   2091   -767       N  
ATOM    615  CA  GLU A  90     -28.726  -1.007  54.591  1.00 39.05           C  
ANISOU  615  CA  GLU A  90     5500   3748   5588  -1741   2097   -686       C  
ATOM    616  C   GLU A  90     -28.364  -1.662  53.266  1.00 36.38           C  
ANISOU  616  C   GLU A  90     5071   3450   5304  -1714   1832   -686       C  
ATOM    617  O   GLU A  90     -27.343  -2.352  53.159  1.00 33.90           O  
ANISOU  617  O   GLU A  90     4973   3109   4798  -1674   1714   -600       O  
ATOM    618  CB  GLU A  90     -29.652  -1.921  55.396  1.00 44.66           C  
ANISOU  618  CB  GLU A  90     6267   4317   6386  -1917   2423   -708       C  
ATOM    619  N   THR A  91     -29.206  -1.481  52.254  1.00 44.79           N  
ANISOU  619  N   THR A  91     5824   4568   6626  -1727   1734   -787       N  
ATOM    620  CA  THR A  91     -28.899  -2.029  50.942  1.00 44.90           C  
ANISOU  620  CA  THR A  91     5770   4618   6673  -1686   1472   -800       C  
ATOM    621  C   THR A  91     -27.612  -1.431  50.398  1.00 38.41           C  
ANISOU  621  C   THR A  91     5053   3892   5647  -1512   1234   -717       C  
ATOM    622  O   THR A  91     -26.750  -2.155  49.886  1.00 36.56           O  
ANISOU  622  O   THR A  91     4963   3648   5282  -1470   1097   -658       O  
ATOM    623  CB  THR A  91     -30.065  -1.769  49.992  1.00 52.35           C  
ANISOU  623  CB  THR A  91     6365   5604   7921  -1711   1380   -933       C  
ATOM    624  OG1 THR A  91     -31.285  -2.137  50.642  1.00 56.24           O  
ANISOU  624  OG1 THR A  91     6718   6007   8642  -1875   1638  -1015       O  
ATOM    625  CG2 THR A  91     -29.911  -2.575  48.705  1.00 50.80           C  
ANISOU  625  CG2 THR A  91     6136   5409   7756  -1696   1134   -964       C  
ATOM    626  N   ILE A  92     -27.453  -0.111  50.516  1.00 31.86           N  
ANISOU  626  N   ILE A  92     4156   3150   4801  -1411   1199   -711       N  
ATOM    627  CA  ILE A  92     -26.216   0.528  50.078  1.00 32.72           C  
ANISOU  627  CA  ILE A  92     4355   3337   4738  -1260   1004   -628       C  
ATOM    628  C   ILE A  92     -25.043  -0.019  50.873  1.00 34.17           C  
ANISOU  628  C   ILE A  92     4834   3468   4681  -1249   1034   -520       C  
ATOM    629  O   ILE A  92     -24.025  -0.449  50.313  1.00 28.43           O  
ANISOU  629  O   ILE A  92     4209   2756   3838  -1176    880   -454       O  
ATOM    630  CB  ILE A  92     -26.319   2.056  50.231  1.00 28.83           C  
ANISOU  630  CB  ILE A  92     3752   2918   4284  -1174    992   -643       C  
ATOM    631  CG1 ILE A  92     -27.460   2.606  49.378  1.00 31.17           C  
ANISOU  631  CG1 ILE A  92     3755   3264   4824  -1159    930   -748       C  
ATOM    632  CG2 ILE A  92     -24.981   2.710  49.914  1.00 26.85           C  
ANISOU  632  CG2 ILE A  92     3606   2727   3868  -1040    823   -551       C  
ATOM    633  CD1 ILE A  92     -27.559   4.116  49.417  1.00 35.94           C  
ANISOU  633  CD1 ILE A  92     4255   3929   5472  -1057    901   -761       C  
ATOM    634  N   LEU A  93     -25.185  -0.012  52.200  1.00 33.50           N  
ANISOU  634  N   LEU A  93     4896   3313   4518  -1314   1235   -505       N  
ATOM    635  CA  LEU A  93     -24.145  -0.511  53.087  1.00 34.10           C  
ANISOU  635  CA  LEU A  93     5274   3326   4357  -1297   1253   -409       C  
ATOM    636  C   LEU A  93     -23.775  -1.959  52.779  1.00 40.13           C  
ANISOU  636  C   LEU A  93     6171   4014   5062  -1334   1216   -367       C  
ATOM    637  O   LEU A  93     -22.602  -2.330  52.901  1.00 44.95           O  
ANISOU  637  O   LEU A  93     6969   4609   5500  -1257   1103   -282       O  
ATOM    638  CB  LEU A  93     -24.625  -0.367  54.525  1.00 33.48           C  
ANISOU  638  CB  LEU A  93     5348   3165   4208  -1371   1500   -416       C  
ATOM    639  CG  LEU A  93     -23.598  -0.401  55.643  1.00 40.51           C  
ANISOU  639  CG  LEU A  93     6562   4000   4832  -1321   1499   -330       C  
ATOM    640  CD1 LEU A  93     -22.331   0.285  55.224  1.00 32.68           C  
ANISOU  640  CD1 LEU A  93     5569   3093   3756  -1181   1241   -281       C  
ATOM    641  CD2 LEU A  93     -24.187   0.302  56.848  1.00 47.76           C  
ANISOU  641  CD2 LEU A  93     7572   4875   5701  -1356   1716   -365       C  
ATOM    642  N   ASN A  94     -24.758  -2.787  52.386  1.00 34.04           N  
ANISOU  642  N   ASN A  94     5299   3186   4447  -1449   1303   -430       N  
ATOM    643  CA  ASN A  94     -24.485  -4.188  52.059  1.00 37.70           C  
ANISOU  643  CA  ASN A  94     5894   3560   4870  -1492   1272   -401       C  
ATOM    644  C   ASN A  94     -23.469  -4.299  50.934  1.00 30.34           C  
ANISOU  644  C   ASN A  94     4953   2699   3877  -1359   1017   -365       C  
ATOM    645  O   ASN A  94     -22.594  -5.172  50.961  1.00 36.08           O  
ANISOU  645  O   ASN A  94     5877   3366   4467  -1319    958   -296       O  
ATOM    646  CB  ASN A  94     -25.773  -4.922  51.653  1.00 41.84           C  
ANISOU  646  CB  ASN A  94     6259   4016   5621  -1643   1377   -499       C  
ATOM    647  CG  ASN A  94     -26.646  -5.325  52.841  1.00 46.00           C  
ANISOU  647  CG  ASN A  94     6867   4418   6194  -1801   1686   -511       C  
ATOM    648  OD1 ASN A  94     -26.172  -5.490  53.966  1.00 46.73           O  
ANISOU  648  OD1 ASN A  94     7231   4436   6089  -1802   1818   -427       O  
ATOM    649  ND2 ASN A  94     -27.939  -5.499  52.580  1.00 46.82           N  
ANISOU  649  ND2 ASN A  94     6736   4489   6564  -1935   1802   -617       N  
ATOM    650  N   LEU A  95     -23.590  -3.442  49.921  1.00 28.42           N  
ANISOU  650  N   LEU A  95     4490   2573   3735  -1282    873   -411       N  
ATOM    651  CA  LEU A  95     -22.611  -3.418  48.843  1.00 33.76           C  
ANISOU  651  CA  LEU A  95     5168   3317   4344  -1146    663   -371       C  
ATOM    652  C   LEU A  95     -21.247  -2.989  49.358  1.00 34.06           C  
ANISOU  652  C   LEU A  95     5352   3383   4207  -1035    606   -266       C  
ATOM    653  O   LEU A  95     -20.220  -3.589  49.014  1.00 25.40           O  
ANISOU  653  O   LEU A  95     4371   2271   3008   -954    509   -204       O  
ATOM    654  CB  LEU A  95     -23.078  -2.472  47.738  1.00 37.53           C  
ANISOU  654  CB  LEU A  95     5408   3902   4948  -1084    540   -434       C  
ATOM    655  CG  LEU A  95     -23.838  -3.123  46.596  1.00 42.36           C  
ANISOU  655  CG  LEU A  95     5908   4501   5686  -1116    449   -524       C  
ATOM    656  CD1 LEU A  95     -24.657  -2.088  45.850  1.00 44.91           C  
ANISOU  656  CD1 LEU A  95     5993   4911   6160  -1077    360   -602       C  
ATOM    657  CD2 LEU A  95     -22.852  -3.781  45.666  1.00 44.14           C  
ANISOU  657  CD2 LEU A  95     6257   4727   5789  -1013    305   -478       C  
ATOM    658  N   LEU A  96     -21.218  -1.922  50.162  1.00 27.59           N  
ANISOU  658  N   LEU A  96     4517   2599   3366  -1024    659   -255       N  
ATOM    659  CA  LEU A  96     -19.944  -1.402  50.639  1.00 26.98           C  
ANISOU  659  CA  LEU A  96     4552   2547   3153   -923    577   -172       C  
ATOM    660  C   LEU A  96     -19.207  -2.442  51.465  1.00 31.81           C  
ANISOU  660  C   LEU A  96     5419   3059   3609   -925    594   -104       C  
ATOM    661  O   LEU A  96     -17.971  -2.498  51.441  1.00 28.31           O  
ANISOU  661  O   LEU A  96     5056   2626   3076   -821    467    -35       O  
ATOM    662  CB  LEU A  96     -20.172  -0.127  51.459  1.00 26.64           C  
ANISOU  662  CB  LEU A  96     4471   2536   3115   -928    635   -190       C  
ATOM    663  CG  LEU A  96     -20.784   1.065  50.728  1.00 26.36           C  
ANISOU  663  CG  LEU A  96     4197   2592   3226   -900    604   -246       C  
ATOM    664  CD1 LEU A  96     -20.755   2.304  51.640  1.00 30.34           C  
ANISOU  664  CD1 LEU A  96     4711   3109   3708   -886    650   -255       C  
ATOM    665  CD2 LEU A  96     -20.043   1.339  49.423  1.00 25.60           C  
ANISOU  665  CD2 LEU A  96     4003   2571   3154   -789    431   -210       C  
ATOM    666  N   GLY A  97     -19.949  -3.295  52.167  1.00 28.89           N  
ANISOU  666  N   GLY A  97     5177   2583   3218  -1039    751   -122       N  
ATOM    667  CA  GLY A  97     -19.323  -4.235  53.061  1.00 29.34           C  
ANISOU  667  CA  GLY A  97     5513   2526   3108  -1036    777    -51       C  
ATOM    668  C   GLY A  97     -19.388  -5.667  52.592  1.00 31.30           C  
ANISOU  668  C   GLY A  97     5850   2682   3361  -1072    786    -41       C  
ATOM    669  O   GLY A  97     -19.220  -6.581  53.403  1.00 33.26           O  
ANISOU  669  O   GLY A  97     6346   2802   3487  -1102    859     10       O  
ATOM    670  N   ASP A  98     -19.645  -5.894  51.305  1.00 27.67           N  
ANISOU  670  N   ASP A  98     5218   2270   3027  -1065    712    -90       N  
ATOM    671  CA  ASP A  98     -19.737  -7.270  50.857  1.00 32.63           C  
ANISOU  671  CA  ASP A  98     5943   2794   3661  -1102    717    -94       C  
ATOM    672  C   ASP A  98     -18.337  -7.879  50.781  1.00 28.74           C  
ANISOU  672  C   ASP A  98     5620   2271   3030   -963    585     -7       C  
ATOM    673  O   ASP A  98     -17.324  -7.201  50.972  1.00 33.78           O  
ANISOU  673  O   ASP A  98     6259   2979   3597   -843    479     48       O  
ATOM    674  CB  ASP A  98     -20.475  -7.362  49.521  1.00 31.00           C  
ANISOU  674  CB  ASP A  98     5526   2634   3619  -1134    661   -188       C  
ATOM    675  CG  ASP A  98     -19.759  -6.635  48.385  1.00 35.59           C  
ANISOU  675  CG  ASP A  98     5968   3348   4205   -985    482   -183       C  
ATOM    676  OD1 ASP A  98     -18.581  -6.240  48.528  1.00 32.21           O  
ANISOU  676  OD1 ASP A  98     5596   2967   3676   -860    402   -104       O  
ATOM    677  OD2 ASP A  98     -20.393  -6.463  47.324  1.00 33.85           O  
ANISOU  677  OD2 ASP A  98     5583   3179   4099   -992    421   -260       O  
ATOM    678  N   ALA A  99     -18.291  -9.179  50.492  1.00 28.90           N  
ANISOU  678  N   ALA A  99     5774   2177   3031   -980    589     -2       N  
ATOM    679  CA  ALA A  99     -17.026  -9.908  50.532  1.00 33.34           C  
ANISOU  679  CA  ALA A  99     6516   2683   3471   -845    482     78       C  
ATOM    680  C   ALA A  99     -16.017  -9.329  49.548  1.00 29.05           C  
ANISOU  680  C   ALA A  99     5825   2268   2946   -682    319     93       C  
ATOM    681  O   ALA A  99     -14.828  -9.200  49.866  1.00 27.26           O  
ANISOU  681  O   ALA A  99     5659   2057   2643   -552    224    165       O  
ATOM    682  CB  ALA A  99     -17.267 -11.393  50.240  1.00 32.56           C  
ANISOU  682  CB  ALA A  99     6573   2429   3370   -894    521     67       C  
ATOM    683  N   ARG A 100     -16.470  -8.987  48.343  1.00 26.88           N  
ANISOU  683  N   ARG A 100     5359   2078   2777   -684    287     24       N  
ATOM    684  CA  ARG A 100     -15.569  -8.391  47.362  1.00 30.01           C  
ANISOU  684  CA  ARG A 100     5630   2588   3186   -534    169     43       C  
ATOM    685  C   ARG A 100     -14.929  -7.114  47.903  1.00 26.36           C  
ANISOU  685  C   ARG A 100     5074   2225   2716   -476    131     94       C  
ATOM    686  O   ARG A 100     -13.711  -6.937  47.808  1.00 26.02           O  
ANISOU  686  O   ARG A 100     5026   2214   2647   -346     48    156       O  
ATOM    687  CB  ARG A 100     -16.325  -8.112  46.064  1.00 32.38           C  
ANISOU  687  CB  ARG A 100     5770   2955   3578   -552    144    -41       C  
ATOM    688  CG  ARG A 100     -15.546  -7.307  45.050  1.00 24.51           C  
ANISOU  688  CG  ARG A 100     4651   2076   2586   -408     59    -17       C  
ATOM    689  CD  ARG A 100     -16.378  -7.097  43.791  1.00 26.06           C  
ANISOU  689  CD  ARG A 100     4740   2321   2842   -418     21   -102       C  
ATOM    690  NE  ARG A 100     -15.698  -6.207  42.859  1.00 31.45           N  
ANISOU  690  NE  ARG A 100     5328   3108   3513   -284    -34    -66       N  
ATOM    691  CZ  ARG A 100     -16.195  -5.795  41.697  1.00 26.29           C  
ANISOU  691  CZ  ARG A 100     4602   2510   2879   -249    -86   -119       C  
ATOM    692  NH1 ARG A 100     -17.396  -6.194  41.289  1.00 25.26           N  
ANISOU  692  NH1 ARG A 100     4456   2345   2798   -337   -121   -223       N  
ATOM    693  NH2 ARG A 100     -15.478  -4.975  40.944  1.00 27.94           N  
ANISOU  693  NH2 ARG A 100     4756   2798   3062   -124   -107    -66       N  
ATOM    694  N   ARG A 101     -15.724  -6.228  48.504  1.00 24.95           N  
ANISOU  694  N   ARG A 101     4819   2086   2575   -573    195     63       N  
ATOM    695  CA  ARG A 101     -15.150  -4.979  49.000  1.00 26.21           C  
ANISOU  695  CA  ARG A 101     4899   2328   2732   -523    151     99       C  
ATOM    696  C   ARG A 101     -14.311  -5.200  50.250  1.00 29.83           C  
ANISOU  696  C   ARG A 101     5534   2719   3079   -487    118    164       C  
ATOM    697  O   ARG A 101     -13.286  -4.536  50.428  1.00 24.23           O  
ANISOU  697  O   ARG A 101     4779   2058   2368   -394     15    208       O  
ATOM    698  CB  ARG A 101     -16.249  -3.960  49.276  1.00 27.70           C  
ANISOU  698  CB  ARG A 101     4966   2568   2990   -623    230     40       C  
ATOM    699  CG  ARG A 101     -16.310  -2.833  48.245  1.00 22.89           C  
ANISOU  699  CG  ARG A 101     4141   2077   2478   -571    174     17       C  
ATOM    700  CD  ARG A 101     -16.501  -3.348  46.835  1.00 22.76           C  
ANISOU  700  CD  ARG A 101     4063   2080   2504   -531    132    -13       C  
ATOM    701  NE  ARG A 101     -17.803  -3.969  46.688  1.00 23.55           N  
ANISOU  701  NE  ARG A 101     4154   2132   2661   -646    194    -98       N  
ATOM    702  CZ  ARG A 101     -18.408  -4.172  45.527  1.00 25.98           C  
ANISOU  702  CZ  ARG A 101     4380   2460   3032   -642    146   -162       C  
ATOM    703  NH1 ARG A 101     -17.830  -3.794  44.393  1.00 23.16           N  
ANISOU  703  NH1 ARG A 101     3972   2170   2658   -520     53   -141       N  
ATOM    704  NH2 ARG A 101     -19.598  -4.751  45.501  1.00 31.28           N  
ANISOU  704  NH2 ARG A 101     5024   3076   3786   -762    191   -249       N  
ATOM    705  N   THR A 102     -14.713  -6.140  51.109  1.00 31.84           N  
ANISOU  705  N   THR A 102     5999   2852   3245   -558    195    172       N  
ATOM    706  CA  THR A 102     -13.949  -6.418  52.321  1.00 34.25           C  
ANISOU  706  CA  THR A 102     6519   3078   3415   -510    145    236       C  
ATOM    707  C   THR A 102     -12.558  -6.947  51.990  1.00 32.83           C  
ANISOU  707  C   THR A 102     6370   2886   3218   -353    -10    296       C  
ATOM    708  O   THR A 102     -11.564  -6.547  52.608  1.00 31.39           O  
ANISOU  708  O   THR A 102     6218   2712   2996   -261   -135    339       O  
ATOM    709  CB  THR A 102     -14.707  -7.418  53.193  1.00 38.46           C  
ANISOU  709  CB  THR A 102     7301   3464   3847   -615    283    242       C  
ATOM    710  OG1 THR A 102     -16.023  -6.917  53.444  1.00 37.95           O  
ANISOU  710  OG1 THR A 102     7170   3413   3836   -762    452    179       O  
ATOM    711  CG2 THR A 102     -13.977  -7.642  54.518  1.00 34.57           C  
ANISOU  711  CG2 THR A 102     7076   2880   3181   -555    223    311       C  
ATOM    712  N   ARG A 103     -12.468  -7.875  51.036  1.00 33.43           N  
ANISOU  712  N   ARG A 103     6439   2932   3329   -315     -7    293       N  
ATOM    713  CA  ARG A 103     -11.155  -8.332  50.595  1.00 28.77           C  
ANISOU  713  CA  ARG A 103     5845   2337   2749   -152   -132    343       C  
ATOM    714  C   ARG A 103     -10.373  -7.198  49.946  1.00 28.59           C  
ANISOU  714  C   ARG A 103     5576   2450   2835    -65   -211    349       C  
ATOM    715  O   ARG A 103      -9.169  -7.053  50.185  1.00 26.15           O  
ANISOU  715  O   ARG A 103     5238   2150   2549     55   -330    396       O  
ATOM    716  CB  ARG A 103     -11.295  -9.488  49.616  1.00 27.12           C  
ANISOU  716  CB  ARG A 103     5682   2068   2556   -128    -95    325       C  
ATOM    717  CG  ARG A 103     -11.763 -10.793  50.221  1.00 28.46           C  
ANISOU  717  CG  ARG A 103     6114   2069   2630   -189    -33    334       C  
ATOM    718  CD  ARG A 103     -10.738 -11.339  51.195  1.00 42.56           C  
ANISOU  718  CD  ARG A 103     8098   3758   4314    -76   -134    414       C  
ATOM    719  NE  ARG A 103     -10.930 -12.769  51.412  1.00 52.12           N  
ANISOU  719  NE  ARG A 103     9564   4794   5446    -86    -90    434       N  
ATOM    720  CZ  ARG A 103     -10.231 -13.497  52.276  1.00 49.95           C  
ANISOU  720  CZ  ARG A 103     9524   4392   5061      7   -167    505       C  
ATOM    721  NH1 ARG A 103      -9.288 -12.927  53.019  1.00 45.43           N  
ANISOU  721  NH1 ARG A 103     8954   3856   4449    118   -313    553       N  
ATOM    722  NH2 ARG A 103     -10.484 -14.794  52.401  1.00 46.58           N  
ANISOU  722  NH2 ARG A 103     9314   3811   4572    -10   -109    515       N  
ATOM    723  N   PHE A 104     -11.046  -6.398  49.111  1.00 24.79           N  
ANISOU  723  N   PHE A 104     4917   2066   2434   -122   -148    303       N  
ATOM    724  CA  PHE A 104     -10.383  -5.343  48.345  1.00 25.66           C  
ANISOU  724  CA  PHE A 104     4809   2291   2648    -47   -192    316       C  
ATOM    725  C   PHE A 104      -9.758  -4.304  49.265  1.00 27.68           C  
ANISOU  725  C   PHE A 104     5008   2580   2928    -35   -273    342       C  
ATOM    726  O   PHE A 104      -8.603  -3.918  49.083  1.00 26.32           O  
ANISOU  726  O   PHE A 104     4724   2442   2836     65   -358    381       O  
ATOM    727  CB  PHE A 104     -11.394  -4.697  47.395  1.00 23.13           C  
ANISOU  727  CB  PHE A 104     4356   2048   2383   -115   -114    261       C  
ATOM    728  CG  PHE A 104     -10.832  -3.592  46.529  1.00 31.09           C  
ANISOU  728  CG  PHE A 104     5171   3159   3484    -43   -133    283       C  
ATOM    729  CD1 PHE A 104     -10.274  -3.876  45.293  1.00 29.97           C  
ANISOU  729  CD1 PHE A 104     4978   3040   3368     62   -121    302       C  
ATOM    730  CD2 PHE A 104     -10.914  -2.264  46.930  1.00 28.33           C  
ANISOU  730  CD2 PHE A 104     4707   2869   3188    -83   -145    283       C  
ATOM    731  CE1 PHE A 104      -9.772  -2.870  44.488  1.00 32.68           C  
ANISOU  731  CE1 PHE A 104     5166   3462   3788    123   -107    333       C  
ATOM    732  CE2 PHE A 104     -10.424  -1.241  46.120  1.00 23.92           C  
ANISOU  732  CE2 PHE A 104     3984   2385   2720    -27   -146    310       C  
ATOM    733  CZ  PHE A 104      -9.847  -1.546  44.897  1.00 27.14           C  
ANISOU  733  CZ  PHE A 104     4347   2812   3151     75   -119    341       C  
ATOM    734  N   PHE A 105     -10.501  -3.842  50.268  1.00 30.32           N  
ANISOU  734  N   PHE A 105     5419   2898   3204   -139   -246    314       N  
ATOM    735  CA  PHE A 105      -9.915  -2.860  51.170  1.00 30.62           C  
ANISOU  735  CA  PHE A 105     5431   2955   3251   -126   -341    325       C  
ATOM    736  C   PHE A 105      -9.026  -3.500  52.226  1.00 33.63           C  
ANISOU  736  C   PHE A 105     5989   3247   3543    -55   -469    365       C  
ATOM    737  O   PHE A 105      -8.099  -2.843  52.708  1.00 33.04           O  
ANISOU  737  O   PHE A 105     5856   3186   3513      3   -609    378       O  
ATOM    738  CB  PHE A 105     -11.015  -2.000  51.791  1.00 23.96           C  
ANISOU  738  CB  PHE A 105     4601   2127   2375   -247   -258    274       C  
ATOM    739  CG  PHE A 105     -11.574  -1.000  50.809  1.00 23.38           C  
ANISOU  739  CG  PHE A 105     4313   2151   2420   -279   -194    241       C  
ATOM    740  CD1 PHE A 105     -10.827   0.111  50.447  1.00 29.75           C  
ANISOU  740  CD1 PHE A 105     4947   3022   3333   -228   -265    259       C  
ATOM    741  CD2 PHE A 105     -12.803  -1.207  50.200  1.00 22.51           C  
ANISOU  741  CD2 PHE A 105     4171   2056   2326   -354    -75    194       C  
ATOM    742  CE1 PHE A 105     -11.304   1.016  49.524  1.00 25.32           C  
ANISOU  742  CE1 PHE A 105     4219   2535   2866   -244   -208    241       C  
ATOM    743  CE2 PHE A 105     -13.288  -0.305  49.282  1.00 21.73           C  
ANISOU  743  CE2 PHE A 105     3892   2039   2327   -362    -45    166       C  
ATOM    744  CZ  PHE A 105     -12.536   0.808  48.944  1.00 26.83           C  
ANISOU  744  CZ  PHE A 105     4398   2743   3052   -302   -108    196       C  
ATOM    745  N   GLY A 106      -9.242  -4.775  52.544  1.00 35.15           N  
ANISOU  745  N   GLY A 106     6394   3339   3623    -52   -441    383       N  
ATOM    746  CA  GLY A 106      -8.302  -5.477  53.404  1.00 38.24           C  
ANISOU  746  CA  GLY A 106     6962   3637   3931     48   -585    429       C  
ATOM    747  C   GLY A 106      -6.903  -5.524  52.818  1.00 38.94           C  
ANISOU  747  C   GLY A 106     6884   3759   4153    199   -726    463       C  
ATOM    748  O   GLY A 106      -5.916  -5.272  53.510  1.00 42.71           O  
ANISOU  748  O   GLY A 106     7362   4216   4649    283   -904    481       O  
ATOM    749  N   ASP A 107      -6.798  -5.860  51.532  1.00 27.24           N  
ANISOU  749  N   ASP A 107     5259   2321   2771    240   -649    466       N  
ATOM    750  CA  ASP A 107      -5.501  -5.795  50.870  1.00 27.56           C  
ANISOU  750  CA  ASP A 107     5109   2400   2965    381   -734    496       C  
ATOM    751  C   ASP A 107      -4.995  -4.358  50.794  1.00 39.39           C  
ANISOU  751  C   ASP A 107     6367   3993   4608    370   -786    489       C  
ATOM    752  O   ASP A 107      -3.795  -4.101  50.951  1.00 44.27           O  
ANISOU  752  O   ASP A 107     6855   4615   5353    467   -920    510       O  
ATOM    753  CB  ASP A 107      -5.604  -6.390  49.471  1.00 31.94           C  
ANISOU  753  CB  ASP A 107     5591   2977   3569    423   -608    496       C  
ATOM    754  CG  ASP A 107      -5.912  -7.875  49.500  1.00 43.09           C  
ANISOU  754  CG  ASP A 107     7232   4274   4864    448   -576    501       C  
ATOM    755  OD1 ASP A 107      -6.070  -8.419  50.614  1.00 39.38           O  
ANISOU  755  OD1 ASP A 107     6981   3707   4274    428   -638    515       O  
ATOM    756  OD2 ASP A 107      -5.992  -8.487  48.417  1.00 40.54           O  
ANISOU  756  OD2 ASP A 107     6892   3950   4563    490   -488    490       O  
HETATM  757  N   MSE A 108      -5.899  -3.418  50.560  1.00 25.97           N  
ANISOU  757  N   MSE A 108     4600   2359   2909    253   -686    456       N  
HETATM  758  CA  MSE A 108      -5.564  -2.019  50.332  1.00 36.37           C  
ANISOU  758  CA  MSE A 108     5696   3755   4366    230   -703    449       C  
HETATM  759  C   MSE A 108      -4.920  -1.455  51.582  1.00 36.19           C  
ANISOU  759  C   MSE A 108     5698   3699   4354    235   -884    439       C  
HETATM  760  O   MSE A 108      -3.931  -0.734  51.512  1.00 34.78           O  
ANISOU  760  O   MSE A 108     5328   3546   4341    279   -981    448       O  
HETATM  761  CB  MSE A 108      -6.825  -1.233  49.941  1.00 28.84           C  
ANISOU  761  CB  MSE A 108     4714   2860   3385    110   -567    411       C  
HETATM  762  CG  MSE A 108      -6.729   0.269  50.041  1.00 38.79           C  
ANISOU  762  CG  MSE A 108     5817   4173   4748     63   -589    397       C  
HETATM  763 SE   MSE A 108      -6.166   1.077  48.368  1.00 41.54          SE  
ANISOU  763 SE   MSE A 108     5888   4604   5290    115   -491    439      SE  
HETATM  764  CE  MSE A 108      -7.490   0.346  47.137  1.00 36.02           C  
ANISOU  764  CE  MSE A 108     5274   3934   4478     96   -322    421       C  
ATOM    765  N   PHE A 109      -5.483  -1.820  52.733  1.00 36.34           N  
ANISOU  765  N   PHE A 109     5965   3649   4194    190   -928    418       N  
ATOM    766  CA  PHE A 109      -4.959  -1.358  54.005  1.00 33.97           C  
ANISOU  766  CA  PHE A 109     5752   3301   3854    202  -1117    400       C  
ATOM    767  C   PHE A 109      -3.750  -2.164  54.450  1.00 41.99           C  
ANISOU  767  C   PHE A 109     6817   4249   4890    341  -1318    431       C  
ATOM    768  O   PHE A 109      -3.000  -1.705  55.318  1.00 46.29           O  
ANISOU  768  O   PHE A 109     7367   4760   5459    381  -1529    412       O  
ATOM    769  CB  PHE A 109      -6.058  -1.397  55.079  1.00 30.36           C  
ANISOU  769  CB  PHE A 109     5576   2788   3174    108  -1063    368       C  
ATOM    770  CG  PHE A 109      -7.276  -0.556  54.749  1.00 28.31           C  
ANISOU  770  CG  PHE A 109     5253   2588   2913    -20   -877    326       C  
ATOM    771  CD1 PHE A 109      -7.215   0.453  53.799  1.00 32.23           C  
ANISOU  771  CD1 PHE A 109     5482   3178   3588    -41   -829    316       C  
ATOM    772  CD2 PHE A 109      -8.483  -0.784  55.392  1.00 30.25           C  
ANISOU  772  CD2 PHE A 109     5711   2790   2991   -113   -742    299       C  
ATOM    773  CE1 PHE A 109      -8.338   1.216  53.486  1.00 29.81           C  
ANISOU  773  CE1 PHE A 109     5121   2919   3285   -139   -678    277       C  
ATOM    774  CE2 PHE A 109      -9.615  -0.027  55.089  1.00 26.11           C  
ANISOU  774  CE2 PHE A 109     5106   2320   2495   -218   -576    253       C  
ATOM    775  CZ  PHE A 109      -9.537   0.974  54.129  1.00 28.18           C  
ANISOU  775  CZ  PHE A 109     5101   2676   2931   -224   -559    241       C  
ATOM    776  N   GLY A 110      -3.541  -3.345  53.880  1.00 42.17           N  
ANISOU  776  N   GLY A 110     6875   4241   4907    423  -1272    472       N  
ATOM    777  CA  GLY A 110      -2.380  -4.142  54.229  1.00 39.60           C  
ANISOU  777  CA  GLY A 110     6579   3847   4621    575  -1462    503       C  
ATOM    778  C   GLY A 110      -2.392  -4.726  55.626  1.00 45.91           C  
ANISOU  778  C   GLY A 110     7706   4530   5210    611  -1625    507       C  
ATOM    779  O   GLY A 110      -1.341  -4.768  56.279  1.00 47.40           O  
ANISOU  779  O   GLY A 110     7892   4671   5448    725  -1875    508       O  
ATOM    780  N   THR A 111      -3.551  -5.185  56.104  1.00 42.34           N  
ANISOU  780  N   THR A 111     7539   4020   4527    519  -1490    509       N  
ATOM    781  CA  THR A 111      -3.629  -5.841  57.402  1.00 47.59           C  
ANISOU  781  CA  THR A 111     8569   4554   4957    555  -1604    528       C  
ATOM    782  C   THR A 111      -4.662  -6.956  57.345  1.00 46.02           C  
ANISOU  782  C   THR A 111     8626   4274   4586    494  -1395    561       C  
ATOM    783  O   THR A 111      -5.571  -6.955  56.510  1.00 44.21           O  
ANISOU  783  O   THR A 111     8302   4099   4397    384  -1166    545       O  
ATOM    784  CB  THR A 111      -3.983  -4.859  58.536  1.00 51.01           C  
ANISOU  784  CB  THR A 111     9145   4978   5260    480  -1675    483       C  
ATOM    785  OG1 THR A 111      -3.732  -5.464  59.809  1.00 44.22           O  
ANISOU  785  OG1 THR A 111     8645   3982   4173    559  -1843    506       O  
ATOM    786  CG2 THR A 111      -5.433  -4.505  58.470  1.00 57.43           C  
ANISOU  786  CG2 THR A 111    10028   5819   5972    310  -1401    458       C  
ATOM    787  N   ARG A 112      -4.499  -7.921  58.238  1.00 45.74           N  
ANISOU  787  N   ARG A 112     8919   4096   4363    569  -1486    605       N  
ATOM    788  CA  ARG A 112      -5.498  -8.966  58.385  1.00 49.44           C  
ANISOU  788  CA  ARG A 112     9615   4485   4685    482  -1261    610       C  
ATOM    789  C   ARG A 112      -6.620  -8.547  59.317  1.00 50.71           C  
ANISOU  789  C   ARG A 112     9987   4616   4666    335  -1109    580       C  
ATOM    790  O   ARG A 112      -7.658  -9.219  59.358  1.00 49.53           O  
ANISOU  790  O   ARG A 112     9979   4409   4433    226   -878    577       O  
ATOM    791  CB  ARG A 112      -4.844 -10.248  58.899  1.00 46.81           C  
ANISOU  791  CB  ARG A 112     9447   4053   4286    602  -1353    620       C  
ATOM    792  N   ALA A 113      -6.445  -7.444  60.038  1.00 49.45           N  
ANISOU  792  N   ALA A 113     9839   4489   4462    329  -1225    550       N  
ATOM    793  CA  ALA A 113      -7.398  -7.058  61.063  1.00 49.28           C  
ANISOU  793  CA  ALA A 113    10043   4423   4257    217  -1085    514       C  
ATOM    794  C   ALA A 113      -8.748  -6.708  60.451  1.00 47.36           C  
ANISOU  794  C   ALA A 113     9734   4224   4038     46   -795    509       C  
ATOM    795  O   ALA A 113      -8.847  -6.246  59.312  1.00 41.31           O  
ANISOU  795  O   ALA A 113     8655   3573   3470      9   -748    490       O  
ATOM    796  CB  ALA A 113      -6.867  -5.879  61.875  1.00 43.27           C  
ANISOU  796  CB  ALA A 113     9297   3687   3456    256  -1288    470       C  
ATOM    797  N   GLU A 114      -9.795  -6.957  61.228  1.00 46.49           N  
ANISOU  797  N   GLU A 114     9837   4042   3784    -60   -577    484       N  
ATOM    798  CA  GLU A 114     -11.152  -6.661  60.804  1.00 44.55           C  
ANISOU  798  CA  GLU A 114     9526   3826   3575   -230   -289    465       C  
ATOM    799  C   GLU A 114     -11.406  -5.160  60.875  1.00 34.86           C  
ANISOU  799  C   GLU A 114     8152   2702   2392   -280   -288    410       C  
ATOM    800  O   GLU A 114     -11.144  -4.520  61.898  1.00 35.98           O  
ANISOU  800  O   GLU A 114     8470   2812   2388   -244   -384    392       O  
ATOM    801  CB  GLU A 114     -12.130  -7.419  61.700  1.00 49.57           C  
ANISOU  801  CB  GLU A 114    10407   4347   4079   -315    -52    443       C  
ATOM    802  CG  GLU A 114     -13.583  -6.997  61.605  1.00 50.73           C  
ANISOU  802  CG  GLU A 114    10499   4513   4265   -491    254    403       C  
ATOM    803  CD  GLU A 114     -14.502  -7.983  62.313  1.00 55.14           C  
ANISOU  803  CD  GLU A 114    11262   4948   4741   -571    498    387       C  
ATOM    804  OE1 GLU A 114     -15.570  -8.298  61.750  1.00 57.06           O  
ANISOU  804  OE1 GLU A 114    11384   5196   5101   -706    729    365       O  
ATOM    805  OE2 GLU A 114     -14.153  -8.459  63.421  1.00 53.60           O  
ANISOU  805  OE2 GLU A 114    11344   4644   4377   -498    452    396       O  
ATOM    806  N   TYR A 115     -11.916  -4.600  59.793  1.00 32.98           N  
ANISOU  806  N   TYR A 115     7573   2589   2369   -354   -187    361       N  
ATOM    807  CA  TYR A 115     -12.299  -3.198  59.762  1.00 40.78           C  
ANISOU  807  CA  TYR A 115     8373   3679   3441   -406   -153    290       C  
ATOM    808  C   TYR A 115     -13.816  -3.077  59.705  1.00 42.15           C  
ANISOU  808  C   TYR A 115     8520   3854   3641   -557    149    245       C  
ATOM    809  O   TYR A 115     -14.511  -3.957  59.184  1.00 44.48           O  
ANISOU  809  O   TYR A 115     8795   4118   3989   -629    308    257       O  
ATOM    810  CB  TYR A 115     -11.664  -2.471  58.579  1.00 33.45           C  
ANISOU  810  CB  TYR A 115     7071   2890   2748   -359   -286    270       C  
ATOM    811  CG  TYR A 115     -10.252  -1.993  58.836  1.00 35.34           C  
ANISOU  811  CG  TYR A 115     7272   3146   3009   -235   -572    282       C  
ATOM    812  CD1 TYR A 115      -9.985  -0.657  59.096  1.00 40.03           C  
ANISOU  812  CD1 TYR A 115     7753   3796   3660   -235   -667    230       C  
ATOM    813  CD2 TYR A 115      -9.184  -2.878  58.823  1.00 35.91           C  
ANISOU  813  CD2 TYR A 115     7410   3168   3065   -116   -751    339       C  
ATOM    814  CE1 TYR A 115      -8.693  -0.216  59.327  1.00 42.49           C  
ANISOU  814  CE1 TYR A 115     8005   4113   4027   -135   -938    230       C  
ATOM    815  CE2 TYR A 115      -7.896  -2.445  59.055  1.00 32.76           C  
ANISOU  815  CE2 TYR A 115     6940   2781   2726     -3  -1021    340       C  
ATOM    816  CZ  TYR A 115      -7.647  -1.122  59.307  1.00 37.34           C  
ANISOU  816  CZ  TYR A 115     7395   3416   3376    -19  -1117    284       C  
ATOM    817  OH  TYR A 115      -6.349  -0.698  59.538  1.00 37.03           O  
ANISOU  817  OH  TYR A 115     7261   3378   3429     81  -1398    276       O  
ATOM    818  N   PHE A 116     -14.319  -1.992  60.285  1.00 35.23           N  
ANISOU  818  N   PHE A 116     7646   3003   2737   -600    222    186       N  
ATOM    819  CA  PHE A 116     -15.741  -1.702  60.369  1.00 34.54           C  
ANISOU  819  CA  PHE A 116     7517   2916   2690   -730    509    132       C  
ATOM    820  C   PHE A 116     -16.024  -0.373  59.694  1.00 35.13           C  
ANISOU  820  C   PHE A 116     7269   3122   2955   -744    497     60       C  
ATOM    821  O   PHE A 116     -15.248   0.576  59.832  1.00 40.96           O  
ANISOU  821  O   PHE A 116     7956   3908   3700   -672    315     44       O  
ATOM    822  CB  PHE A 116     -16.208  -1.630  61.826  1.00 34.43           C  
ANISOU  822  CB  PHE A 116     7854   2787   2442   -760    658    125       C  
ATOM    823  CG  PHE A 116     -15.826  -2.829  62.640  1.00 36.22           C  
ANISOU  823  CG  PHE A 116     8462   2865   2437   -726    648    206       C  
ATOM    824  CD1 PHE A 116     -16.686  -3.903  62.746  1.00 37.29           C  
ANISOU  824  CD1 PHE A 116     8703   2904   2561   -818    893    228       C  
ATOM    825  CD2 PHE A 116     -14.607  -2.881  63.292  1.00 37.05           C  
ANISOU  825  CD2 PHE A 116     8786   2922   2370   -592    376    246       C  
ATOM    826  CE1 PHE A 116     -16.344  -5.017  63.494  1.00 45.29           C  
ANISOU  826  CE1 PHE A 116     9966   3794   3447   -757    859    257       C  
ATOM    827  CE2 PHE A 116     -14.255  -3.990  64.038  1.00 46.07           C  
ANISOU  827  CE2 PHE A 116    10171   3938   3395   -527    334    278       C  
ATOM    828  CZ  PHE A 116     -15.128  -5.061  64.139  1.00 45.19           C  
ANISOU  828  CZ  PHE A 116    10140   3741   3290   -609    583    285       C  
ATOM    829  N   ILE A 117     -17.142  -0.301  58.980  1.00 34.15           N  
ANISOU  829  N   ILE A 117     6933   3046   2995   -836    683     16       N  
ATOM    830  CA  ILE A 117     -17.624   0.971  58.448  1.00 37.51           C  
ANISOU  830  CA  ILE A 117     7089   3575   3588   -850    703    -54       C  
ATOM    831  C   ILE A 117     -18.411   1.656  59.566  1.00 39.42           C  
ANISOU  831  C   ILE A 117     7473   3766   3737   -898    886   -112       C  
ATOM    832  O   ILE A 117     -19.489   1.198  59.944  1.00 40.86           O  
ANISOU  832  O   ILE A 117     7725   3889   3913   -991   1140   -134       O  
ATOM    833  CB  ILE A 117     -18.484   0.770  57.193  1.00 28.29           C  
ANISOU  833  CB  ILE A 117     5636   2476   2636   -909    791    -85       C  
ATOM    834  CG1 ILE A 117     -17.657   0.157  56.057  1.00 28.42           C  
ANISOU  834  CG1 ILE A 117     5537   2540   2721   -845    615    -34       C  
ATOM    835  CG2 ILE A 117     -19.093   2.083  56.737  1.00 27.59           C  
ANISOU  835  CG2 ILE A 117     5299   2477   2707   -913    820   -156       C  
ATOM    836  CD1 ILE A 117     -18.481  -0.268  54.836  1.00 26.47           C  
ANISOU  836  CD1 ILE A 117     5072   2337   2647   -898    679    -67       C  
ATOM    837  N   ARG A 118     -17.871   2.756  60.101  1.00 32.76           N  
ANISOU  837  N   ARG A 118     6675   2938   2834   -836    768   -140       N  
ATOM    838  CA  ARG A 118     -18.491   3.417  61.242  1.00 33.33           C  
ANISOU  838  CA  ARG A 118     6932   2948   2783   -860    929   -199       C  
ATOM    839  C   ARG A 118     -19.412   4.563  60.855  1.00 32.74           C  
ANISOU  839  C   ARG A 118     6608   2941   2891   -891   1053   -284       C  
ATOM    840  O   ARG A 118     -20.316   4.903  61.622  1.00 33.29           O  
ANISOU  840  O   ARG A 118     6779   2959   2911   -933   1282   -342       O  
ATOM    841  CB  ARG A 118     -17.418   3.960  62.191  1.00 38.18           C  
ANISOU  841  CB  ARG A 118     7788   3515   3205   -772    720   -199       C  
ATOM    842  CG  ARG A 118     -16.760   2.917  63.083  1.00 39.54           C  
ANISOU  842  CG  ARG A 118     8323   3576   3122   -734    646   -132       C  
ATOM    843  CD  ARG A 118     -15.894   3.588  64.140  1.00 39.70           C  
ANISOU  843  CD  ARG A 118     8599   3539   2947   -648    441   -159       C  
ATOM    844  NE  ARG A 118     -16.674   4.267  65.169  1.00 43.13           N  
ANISOU  844  NE  ARG A 118     9249   3906   3231   -673    637   -231       N  
ATOM    845  CZ  ARG A 118     -17.004   3.716  66.336  1.00 46.48           C  
ANISOU  845  CZ  ARG A 118    10080   4203   3377   -675    789   -215       C  
ATOM    846  NH1 ARG A 118     -16.626   2.474  66.618  1.00 44.16           N  
ANISOU  846  NH1 ARG A 118     9985   3830   2962   -653    747   -123       N  
ATOM    847  NH2 ARG A 118     -17.709   4.404  67.224  1.00 41.26           N  
ANISOU  847  NH2 ARG A 118     9576   3484   2618   -686    977   -280       N  
ATOM    848  N   ARG A 119     -19.186   5.193  59.710  1.00 32.47           N  
ANISOU  848  N   ARG A 119     6265   3011   3060   -859    914   -293       N  
ATOM    849  CA  ARG A 119     -19.949   6.364  59.319  1.00 33.00           C  
ANISOU  849  CA  ARG A 119     6107   3134   3297   -863    991   -368       C  
ATOM    850  C   ARG A 119     -20.023   6.363  57.807  1.00 29.62           C  
ANISOU  850  C   ARG A 119     5358   2806   3090   -854    902   -350       C  
ATOM    851  O   ARG A 119     -19.086   5.928  57.143  1.00 30.52           O  
ANISOU  851  O   ARG A 119     5432   2954   3211   -814    722   -284       O  
ATOM    852  CB  ARG A 119     -19.301   7.658  59.853  1.00 34.37           C  
ANISOU  852  CB  ARG A 119     6345   3298   3418   -798    855   -405       C  
ATOM    853  CG  ARG A 119     -19.902   8.933  59.310  1.00 35.35           C  
ANISOU  853  CG  ARG A 119     6228   3473   3728   -782    890   -471       C  
ATOM    854  CD  ARG A 119     -19.392  10.158  60.044  1.00 41.32           C  
ANISOU  854  CD  ARG A 119     7100   4186   4415   -732    794   -522       C  
ATOM    855  NE  ARG A 119     -19.925  11.384  59.461  1.00 43.33           N  
ANISOU  855  NE  ARG A 119     7129   4478   4858   -708    819   -577       N  
ATOM    856  CZ  ARG A 119     -19.932  12.564  60.075  1.00 48.03           C  
ANISOU  856  CZ  ARG A 119     7797   5022   5430   -674    813   -649       C  
ATOM    857  NH1 ARG A 119     -19.439  12.674  61.301  1.00 48.81           N  
ANISOU  857  NH1 ARG A 119     8196   5035   5316   -664    776   -681       N  
ATOM    858  NH2 ARG A 119     -20.440  13.632  59.467  1.00 43.29           N  
ANISOU  858  NH2 ARG A 119     6989   4448   5013   -644    835   -692       N  
ATOM    859  N   CYS A 120     -21.145   6.835  57.268  1.00 29.63           N  
ANISOU  859  N   CYS A 120     5140   2848   3269   -881   1031   -412       N  
ATOM    860  CA  CYS A 120     -21.388   6.767  55.834  1.00 26.82           C  
ANISOU  860  CA  CYS A 120     4509   2576   3104   -868    953   -404       C  
ATOM    861  C   CYS A 120     -22.500   7.737  55.465  1.00 27.12           C  
ANISOU  861  C   CYS A 120     4329   2650   3326   -863   1046   -485       C  
ATOM    862  O   CYS A 120     -23.562   7.726  56.094  1.00 31.51           O  
ANISOU  862  O   CYS A 120     4887   3165   3919   -918   1259   -553       O  
ATOM    863  CB  CYS A 120     -21.759   5.340  55.426  1.00 36.10           C  
ANISOU  863  CB  CYS A 120     5681   3739   4297   -934   1015   -380       C  
ATOM    864  SG  CYS A 120     -22.129   5.143  53.671  1.00 37.00           S  
ANISOU  864  SG  CYS A 120     5499   3942   4616   -913    906   -386       S  
ATOM    865  N   GLN A 121     -22.261   8.574  54.456  1.00 27.86           N  
ANISOU  865  N   GLN A 121     4238   2809   3539   -791    897   -477       N  
ATOM    866  CA  GLN A 121     -23.253   9.559  54.043  1.00 28.73           C  
ANISOU  866  CA  GLN A 121     4144   2946   3825   -762    949   -549       C  
ATOM    867  C   GLN A 121     -22.966  10.018  52.616  1.00 32.76           C  
ANISOU  867  C   GLN A 121     4472   3526   4449   -684    767   -512       C  
ATOM    868  O   GLN A 121     -21.852   9.874  52.103  1.00 37.91           O  
ANISOU  868  O   GLN A 121     5170   4200   5036   -647    616   -430       O  
ATOM    869  CB  GLN A 121     -23.279  10.760  55.001  1.00 27.15           C  
ANISOU  869  CB  GLN A 121     4030   2699   3588   -731   1012   -598       C  
ATOM    870  CG  GLN A 121     -22.014  11.626  54.910  1.00 26.21           C  
ANISOU  870  CG  GLN A 121     3975   2578   3407   -665    819   -546       C  
ATOM    871  CD  GLN A 121     -21.874  12.588  56.051  1.00 32.19           C  
ANISOU  871  CD  GLN A 121     4885   3265   4081   -651    863   -600       C  
ATOM    872  OE1 GLN A 121     -21.900  12.190  57.216  1.00 41.14           O  
ANISOU  872  OE1 GLN A 121     6234   4338   5058   -691    969   -625       O  
ATOM    873  NE2 GLN A 121     -21.724  13.879  55.730  1.00 29.74           N  
ANISOU  873  NE2 GLN A 121     4489   2949   3863   -588    781   -617       N  
ATOM    874  N   ILE A 122     -24.001  10.567  51.981  1.00 29.71           N  
ANISOU  874  N   ILE A 122     3884   3168   4237   -652    788   -572       N  
ATOM    875  CA  ILE A 122     -23.901  11.184  50.663  1.00 25.94           C  
ANISOU  875  CA  ILE A 122     3258   2741   3857   -561    626   -543       C  
ATOM    876  C   ILE A 122     -23.854  12.693  50.871  1.00 31.23           C  
ANISOU  876  C   ILE A 122     3906   3386   4573   -490    611   -560       C  
ATOM    877  O   ILE A 122     -24.756  13.260  51.505  1.00 35.74           O  
ANISOU  877  O   ILE A 122     4430   3927   5224   -491    737   -645       O  
ATOM    878  CB  ILE A 122     -25.089  10.805  49.761  1.00 28.05           C  
ANISOU  878  CB  ILE A 122     3324   3045   4289   -556    617   -604       C  
ATOM    879  CG1 ILE A 122     -25.325   9.295  49.729  1.00 32.22           C  
ANISOU  879  CG1 ILE A 122     3873   3572   4795   -649    663   -613       C  
ATOM    880  CG2 ILE A 122     -24.850  11.291  48.357  1.00 36.46           C  
ANISOU  880  CG2 ILE A 122     4299   4154   5399   -450    429   -559       C  
ATOM    881  CD1 ILE A 122     -24.397   8.581  48.823  1.00 40.21           C  
ANISOU  881  CD1 ILE A 122     4952   4615   5711   -623    512   -530       C  
ATOM    882  N   ASN A 123     -22.805  13.343  50.353  1.00 26.98           N  
ANISOU  882  N   ASN A 123     3406   2851   3996   -430    473   -480       N  
ATOM    883  CA  ASN A 123     -22.663  14.795  50.411  1.00 24.44           C  
ANISOU  883  CA  ASN A 123     3069   2488   3727   -364    441   -485       C  
ATOM    884  C   ASN A 123     -22.958  15.371  49.041  1.00 26.03           C  
ANISOU  884  C   ASN A 123     3133   2718   4039   -267    334   -454       C  
ATOM    885  O   ASN A 123     -22.267  15.047  48.070  1.00 30.24           O  
ANISOU  885  O   ASN A 123     3672   3283   4535   -238    228   -367       O  
ATOM    886  CB  ASN A 123     -21.260  15.209  50.838  1.00 24.10           C  
ANISOU  886  CB  ASN A 123     3166   2406   3586   -374    366   -419       C  
ATOM    887  CG  ASN A 123     -20.989  14.906  52.274  1.00 30.86           C  
ANISOU  887  CG  ASN A 123     4190   3215   4319   -443    441   -461       C  
ATOM    888  OD1 ASN A 123     -21.914  14.729  53.067  1.00 34.02           O  
ANISOU  888  OD1 ASN A 123     4619   3596   4710   -476    586   -544       O  
ATOM    889  ND2 ASN A 123     -19.717  14.853  52.633  1.00 33.41           N  
ANISOU  889  ND2 ASN A 123     4631   3514   4550   -462    344   -407       N  
ATOM    890  N   ARG A 124     -23.956  16.243  48.965  1.00 25.28           N  
ANISOU  890  N   ARG A 124     2930   2603   4073   -206    362   -522       N  
ATOM    891  CA  ARG A 124     -24.326  16.898  47.718  1.00 25.51           C  
ANISOU  891  CA  ARG A 124     2850   2642   4200    -93    247   -496       C  
ATOM    892  C   ARG A 124     -23.925  18.369  47.809  1.00 25.75           C  
ANISOU  892  C   ARG A 124     2925   2598   4260    -27    222   -469       C  
ATOM    893  O   ARG A 124     -24.570  19.161  48.510  1.00 26.72           O  
ANISOU  893  O   ARG A 124     3022   2669   4460     -4    300   -550       O  
ATOM    894  CB  ARG A 124     -25.815  16.720  47.452  1.00 31.80           C  
ANISOU  894  CB  ARG A 124     3470   3465   5148    -59    268   -597       C  
ATOM    895  CG  ARG A 124     -26.298  17.381  46.181  1.00 37.63           C  
ANISOU  895  CG  ARG A 124     4108   4208   5982     77    119   -580       C  
ATOM    896  CD  ARG A 124     -27.734  16.987  45.914  1.00 43.85           C  
ANISOU  896  CD  ARG A 124     4696   5028   6937    101    108   -693       C  
ATOM    897  NE  ARG A 124     -28.425  17.993  45.122  1.00 37.34           N  
ANISOU  897  NE  ARG A 124     3768   4180   6240    252    -15   -712       N  
ATOM    898  CZ  ARG A 124     -29.206  18.934  45.635  1.00 48.54           C  
ANISOU  898  CZ  ARG A 124     5086   5550   7805    313     50   -791       C  
ATOM    899  NH1 ARG A 124     -29.402  19.000  46.949  1.00 59.18           N  
ANISOU  899  NH1 ARG A 124     6435   6871   9179    232    254   -862       N  
ATOM    900  NH2 ARG A 124     -29.792  19.812  44.834  1.00 51.98           N  
ANISOU  900  NH2 ARG A 124     5439   5958   8351    468    -87   -800       N  
HETATM  901  N   MSE A 125     -22.860  18.729  47.102  1.00 25.05           N  
ANISOU  901  N   MSE A 125     2907   2491   4118      3    129   -356       N  
HETATM  902  CA  MSE A 125     -22.260  20.047  47.241  1.00 25.30           C  
ANISOU  902  CA  MSE A 125     3001   2434   4178     37    112   -318       C  
HETATM  903  C   MSE A 125     -22.629  20.916  46.056  1.00 25.91           C  
ANISOU  903  C   MSE A 125     3032   2481   4333    165     29   -268       C  
HETATM  904  O   MSE A 125     -22.369  20.550  44.902  1.00 25.60           O  
ANISOU  904  O   MSE A 125     2997   2478   4253    213    -49   -183       O  
HETATM  905  CB  MSE A 125     -20.730  19.940  47.369  1.00 24.45           C  
ANISOU  905  CB  MSE A 125     2999   2305   3987    -30     83   -225       C  
HETATM  906  CG  MSE A 125     -20.246  19.114  48.559  1.00 24.24           C  
ANISOU  906  CG  MSE A 125     3048   2295   3867   -140    130   -266       C  
HETATM  907 SE   MSE A 125     -18.293  19.043  48.596  1.00 34.13          SE  
ANISOU  907 SE   MSE A 125     4386   3517   5066   -203     53   -155      SE  
HETATM  908  CE  MSE A 125     -17.880  20.931  48.836  1.00 24.33           C  
ANISOU  908  CE  MSE A 125     3171   2135   3938   -183     27   -154       C  
ATOM    909  N   LEU A 126     -23.246  22.054  46.344  1.00 26.96           N  
ANISOU  909  N   LEU A 126     3140   2538   4565    231     47   -323       N  
ATOM    910  CA  LEU A 126     -23.730  22.939  45.304  1.00 27.86           C  
ANISOU  910  CA  LEU A 126     3223   2606   4755    371    -38   -283       C  
ATOM    911  C   LEU A 126     -22.645  23.942  44.919  1.00 39.21           C  
ANISOU  911  C   LEU A 126     4781   3942   6175    387    -64   -166       C  
ATOM    912  O   LEU A 126     -21.597  24.036  45.564  1.00 27.29           O  
ANISOU  912  O   LEU A 126     3346   2395   4629    285    -21   -138       O  
ATOM    913  CB  LEU A 126     -24.991  23.653  45.781  1.00 29.24           C  
ANISOU  913  CB  LEU A 126     3302   2740   5066    448     -4   -404       C  
ATOM    914  CG  LEU A 126     -26.064  22.711  46.306  1.00 29.57           C  
ANISOU  914  CG  LEU A 126     3205   2866   5162    412     64   -528       C  
ATOM    915  CD1 LEU A 126     -27.253  23.509  46.795  1.00 31.20           C  
ANISOU  915  CD1 LEU A 126     3301   3023   5530    496    123   -648       C  
ATOM    916  CD2 LEU A 126     -26.477  21.739  45.233  1.00 29.43           C  
ANISOU  916  CD2 LEU A 126     3102   2941   5140    442    -44   -508       C  
ATOM    917  N   LYS A 127     -22.911  24.701  43.849  1.00 28.72           N  
ANISOU  917  N   LYS A 127     3471   2558   4882    517   -140    -97       N  
ATOM    918  CA  LYS A 127     -21.951  25.685  43.366  1.00 35.75           C  
ANISOU  918  CA  LYS A 127     4480   3333   5770    534   -144     27       C  
ATOM    919  C   LYS A 127     -21.572  26.648  44.478  1.00 36.99           C  
ANISOU  919  C   LYS A 127     4676   3377   6000    469    -79    -22       C  
ATOM    920  O   LYS A 127     -22.441  27.145  45.199  1.00 30.16           O  
ANISOU  920  O   LYS A 127     3770   2478   5211    506    -55   -138       O  
ATOM    921  CB  LYS A 127     -22.533  26.462  42.191  1.00 32.75           C  
ANISOU  921  CB  LYS A 127     4139   2890   5417    704   -229     93       C  
ATOM    922  CG  LYS A 127     -21.543  27.363  41.491  1.00 34.41           C  
ANISOU  922  CG  LYS A 127     4494   2974   5609    724   -212    247       C  
ATOM    923  CD  LYS A 127     -22.172  27.981  40.246  1.00 45.24           C  
ANISOU  923  CD  LYS A 127     5941   4283   6965    910   -306    322       C  
ATOM    924  CE  LYS A 127     -21.316  29.113  39.690  1.00 50.96           C  
ANISOU  924  CE  LYS A 127     6827   4840   7694    933   -257    473       C  
ATOM    925  NZ  LYS A 127     -20.820  30.000  40.772  1.00 50.99           N  
ANISOU  925  NZ  LYS A 127     6828   4729   7818    829   -175    433       N  
ATOM    926  N   ASP A 128     -20.267  26.884  44.624  1.00 29.04           N  
ANISOU  926  N   ASP A 128     3746   2310   4979    371    -51     58       N  
ATOM    927  CA  ASP A 128     -19.637  27.809  45.569  1.00 29.55           C  
ANISOU  927  CA  ASP A 128     3866   2248   5112    292    -19     24       C  
ATOM    928  C   ASP A 128     -19.558  27.222  46.973  1.00 36.15           C  
ANISOU  928  C   ASP A 128     4692   3134   5911    182     11   -102       C  
ATOM    929  O   ASP A 128     -19.076  27.899  47.882  1.00 39.75           O  
ANISOU  929  O   ASP A 128     5210   3489   6404    115     17   -156       O  
ATOM    930  CB  ASP A 128     -20.342  29.173  45.629  1.00 35.98           C  
ANISOU  930  CB  ASP A 128     4718   2923   6029    393    -22    -15       C  
ATOM    931  CG  ASP A 128     -20.335  29.878  44.299  1.00 46.06           C  
ANISOU  931  CG  ASP A 128     6051   4119   7332    507    -55    121       C  
ATOM    932  OD1 ASP A 128     -19.239  30.034  43.715  1.00 49.76           O  
ANISOU  932  OD1 ASP A 128     6583   4532   7792    453    -35    253       O  
ATOM    933  OD2 ASP A 128     -21.424  30.257  43.826  1.00 49.44           O  
ANISOU  933  OD2 ASP A 128     6462   4533   7789    656    -98     98       O  
ATOM    934  N   SER A 129     -20.001  25.992  47.182  1.00 28.11           N  
ANISOU  934  N   SER A 129     3616   2254   4810    160     26   -151       N  
ATOM    935  CA  SER A 129     -19.717  25.324  48.439  1.00 27.65           C  
ANISOU  935  CA  SER A 129     3588   2234   4683     51     57   -239       C  
ATOM    936  C   SER A 129     -18.260  24.853  48.476  1.00 27.34           C  
ANISOU  936  C   SER A 129     3584   2202   4602    -53     15   -159       C  
ATOM    937  O   SER A 129     -17.577  24.760  47.453  1.00 26.62           O  
ANISOU  937  O   SER A 129     3468   2118   4527    -44     -9    -35       O  
ATOM    938  CB  SER A 129     -20.663  24.136  48.633  1.00 29.58           C  
ANISOU  938  CB  SER A 129     3768   2608   4865     55    104   -308       C  
ATOM    939  OG  SER A 129     -20.492  23.185  47.594  1.00 26.28           O  
ANISOU  939  OG  SER A 129     3296   2287   4402     67     64   -219       O  
ATOM    940  N   PHE A 130     -17.793  24.551  49.684  1.00 26.91           N  
ANISOU  940  N   PHE A 130     3593   2140   4493   -145      7   -234       N  
ATOM    941  CA  PHE A 130     -16.462  24.003  49.911  1.00 26.46           C  
ANISOU  941  CA  PHE A 130     3555   2093   4407   -238    -55   -183       C  
ATOM    942  C   PHE A 130     -16.458  23.314  51.267  1.00 27.13           C  
ANISOU  942  C   PHE A 130     3727   2204   4376   -302    -62   -288       C  
ATOM    943  O   PHE A 130     -17.379  23.479  52.071  1.00 27.02           O  
ANISOU  943  O   PHE A 130     3776   2176   4314   -283      0   -397       O  
ATOM    944  CB  PHE A 130     -15.380  25.087  49.851  1.00 27.67           C  
ANISOU  944  CB  PHE A 130     3720   2114   4681   -283   -112   -137       C  
ATOM    945  CG  PHE A 130     -15.563  26.188  50.858  1.00 38.08           C  
ANISOU  945  CG  PHE A 130     5127   3302   6039   -300   -132   -248       C  
ATOM    946  CD1 PHE A 130     -15.062  26.064  52.144  1.00 44.08           C  
ANISOU  946  CD1 PHE A 130     5980   4026   6741   -377   -200   -347       C  
ATOM    947  CD2 PHE A 130     -16.222  27.355  50.511  1.00 38.03           C  
ANISOU  947  CD2 PHE A 130     5132   3198   6120   -229    -93   -257       C  
ATOM    948  CE1 PHE A 130     -15.231  27.080  53.070  1.00 46.32           C  
ANISOU  948  CE1 PHE A 130     6375   4181   7044   -387   -222   -460       C  
ATOM    949  CE2 PHE A 130     -16.398  28.374  51.432  1.00 43.50           C  
ANISOU  949  CE2 PHE A 130     5920   3759   6848   -237   -106   -367       C  
ATOM    950  CZ  PHE A 130     -15.902  28.237  52.711  1.00 45.64           C  
ANISOU  950  CZ  PHE A 130     6291   3997   7053   -318   -168   -472       C  
ATOM    951  N   ILE A 131     -15.409  22.535  51.515  1.00 28.41           N  
ANISOU  951  N   ILE A 131     3903   2399   4492   -369   -132   -252       N  
ATOM    952  CA  ILE A 131     -15.142  21.971  52.833  1.00 32.08           C  
ANISOU  952  CA  ILE A 131     4491   2862   4837   -426   -175   -338       C  
ATOM    953  C   ILE A 131     -13.804  22.520  53.286  1.00 33.22           C  
ANISOU  953  C   ILE A 131     4661   2912   5050   -490   -315   -337       C  
ATOM    954  O   ILE A 131     -12.759  22.110  52.771  1.00 30.93           O  
ANISOU  954  O   ILE A 131     4284   2645   4823   -519   -382   -250       O  
ATOM    955  CB  ILE A 131     -15.108  20.443  52.836  1.00 32.26           C  
ANISOU  955  CB  ILE A 131     4519   2997   4740   -439   -162   -308       C  
ATOM    956  CG1 ILE A 131     -16.386  19.876  52.237  1.00 50.22           C  
ANISOU  956  CG1 ILE A 131     6735   5360   6987   -388    -38   -308       C  
ATOM    957  CG2 ILE A 131     -14.925  19.952  54.265  1.00 26.14           C  
ANISOU  957  CG2 ILE A 131     3914   2199   3818   -484   -201   -395       C  
ATOM    958  CD1 ILE A 131     -17.587  20.193  53.055  1.00 56.88           C  
ANISOU  958  CD1 ILE A 131     7646   6178   7788   -372     67   -423       C  
ATOM    959  N   GLY A 132     -13.829  23.427  54.253  1.00 33.01           N  
ANISOU  959  N   GLY A 132     4747   2774   5022   -510   -359   -441       N  
ATOM    960  CA  GLY A 132     -12.599  23.988  54.770  1.00 31.45           C  
ANISOU  960  CA  GLY A 132     4573   2471   4905   -579   -520   -464       C  
ATOM    961  C   GLY A 132     -11.739  22.941  55.451  1.00 30.12           C  
ANISOU  961  C   GLY A 132     4458   2346   4641   -620   -647   -473       C  
ATOM    962  O   GLY A 132     -12.162  21.823  55.754  1.00 33.94           O  
ANISOU  962  O   GLY A 132     5012   2922   4962   -597   -601   -478       O  
HETATM  963  N   MSE A 133     -10.496  23.330  55.686  1.00 34.76           N  
ANISOU  963  N   MSE A 133     5006   2853   5350   -680   -816   -478       N  
HETATM  964  CA  MSE A 133      -9.484  22.475  56.308  1.00 41.20           C  
ANISOU  964  CA  MSE A 133     5849   3687   6120   -710   -986   -489       C  
HETATM  965  C   MSE A 133      -9.948  21.794  57.604  1.00 37.15           C  
ANISOU  965  C   MSE A 133     5584   3186   5344   -687  -1027   -590       C  
HETATM  966  O   MSE A 133     -10.519  22.454  58.474  1.00 36.82           O  
ANISOU  966  O   MSE A 133     5722   3065   5203   -682  -1020   -703       O  
HETATM  967  CB  MSE A 133      -8.242  23.310  56.602  1.00 48.89           C  
ANISOU  967  CB  MSE A 133     6755   4534   7286   -783  -1184   -525       C  
HETATM  968  CG  MSE A 133      -7.034  22.477  56.876  1.00 61.85           C  
ANISOU  968  CG  MSE A 133     8334   6200   8967   -805  -1369   -508       C  
HETATM  969 SE   MSE A 133      -6.331  21.808  55.207  1.00 70.40          SE  
ANISOU  969 SE   MSE A 133     9108   7387  10254   -797  -1249   -318      SE  
HETATM  970  CE  MSE A 133      -5.183  23.349  54.803  1.00 64.49           C  
ANISOU  970  CE  MSE A 133     8152   6470   9882   -902  -1328   -309       C  
ATOM    971  N   HIS A 134      -9.697  20.488  57.744  1.00 39.07           N  
ANISOU  971  N   HIS A 134     5859   3517   5469   -668  -1057   -550       N  
ATOM    972  CA  HIS A 134     -10.096  19.788  58.961  1.00 41.70           C  
ANISOU  972  CA  HIS A 134     6457   3848   5540   -644  -1082   -629       C  
ATOM    973  C   HIS A 134      -9.414  18.428  59.036  1.00 40.33           C  
ANISOU  973  C   HIS A 134     6293   3741   5290   -627  -1178   -568       C  
ATOM    974  O   HIS A 134      -8.750  17.983  58.096  1.00 33.64           O  
ANISOU  974  O   HIS A 134     5235   2953   4592   -626  -1197   -468       O  
ATOM    975  CB  HIS A 134     -11.610  19.607  59.029  1.00 45.30           C  
ANISOU  975  CB  HIS A 134     7014   4349   5847   -611   -835   -652       C  
ATOM    976  CG  HIS A 134     -12.134  18.628  58.032  1.00 45.82           C  
ANISOU  976  CG  HIS A 134     6944   4540   5924   -590   -678   -548       C  
ATOM    977  ND1 HIS A 134     -12.321  18.950  56.705  1.00 44.35           N  
ANISOU  977  ND1 HIS A 134     6530   4405   5915   -581   -590   -466       N  
ATOM    978  CD2 HIS A 134     -12.488  17.328  58.161  1.00 43.22           C  
ANISOU  978  CD2 HIS A 134     6692   4284   5446   -576   -605   -515       C  
ATOM    979  CE1 HIS A 134     -12.779  17.891  56.061  1.00 43.86           C  
ANISOU  979  CE1 HIS A 134     6410   4446   5810   -560   -483   -398       C  
ATOM    980  NE2 HIS A 134     -12.894  16.896  56.923  1.00 45.23           N  
ANISOU  980  NE2 HIS A 134     6756   4633   5798   -563   -485   -427       N  
ATOM    981  N   LEU A 135      -9.617  17.765  60.176  1.00 44.60           N  
ANISOU  981  N   LEU A 135     7102   4260   5583   -603  -1223   -628       N  
ATOM    982  CA  LEU A 135      -9.135  16.412  60.439  1.00 45.37           C  
ANISOU  982  CA  LEU A 135     7279   4402   5558   -571  -1305   -579       C  
ATOM    983  C   LEU A 135     -10.325  15.519  60.748  1.00 43.99           C  
ANISOU  983  C   LEU A 135     7290   4272   5151   -550  -1085   -571       C  
ATOM    984  O   LEU A 135     -11.092  15.809  61.672  1.00 39.91           O  
ANISOU  984  O   LEU A 135     7010   3699   4455   -547   -999   -655       O  
ATOM    985  CB  LEU A 135      -8.160  16.388  61.616  1.00 45.74           C  
ANISOU  985  CB  LEU A 135     7515   4355   5509   -555  -1597   -654       C  
ATOM    986  CG  LEU A 135      -6.664  16.484  61.352  1.00 47.18           C  
ANISOU  986  CG  LEU A 135     7497   4515   5917   -563  -1868   -634       C  
ATOM    987  CD1 LEU A 135      -5.940  16.844  62.648  1.00 53.11           C  
ANISOU  987  CD1 LEU A 135     8460   5145   6575   -552  -2173   -754       C  
ATOM    988  CD2 LEU A 135      -6.148  15.171  60.789  1.00 42.95           C  
ANISOU  988  CD2 LEU A 135     6851   4064   5405   -519  -1880   -525       C  
ATOM    989  N   ASP A 136     -10.472  14.435  59.984  1.00 49.57           N  
ANISOU  989  N   ASP A 136     7894   5071   5871   -537   -985   -473       N  
ATOM    990  CA  ASP A 136     -11.544  13.483  60.252  1.00 50.92           C  
ANISOU  990  CA  ASP A 136     8224   5273   5851   -533   -779   -462       C  
ATOM    991  C   ASP A 136     -11.410  12.881  61.639  1.00 48.69           C  
ANISOU  991  C   ASP A 136     8288   4914   5300   -509   -857   -507       C  
ATOM    992  O   ASP A 136     -12.417  12.622  62.305  1.00 51.54           O  
ANISOU  992  O   ASP A 136     8862   5248   5474   -517   -667   -543       O  
ATOM    993  CB  ASP A 136     -11.550  12.384  59.192  1.00 52.52           C  
ANISOU  993  CB  ASP A 136     8264   5569   6122   -525   -703   -357       C  
ATOM    994  CG  ASP A 136     -12.080  12.867  57.856  1.00 60.79           C  
ANISOU  994  CG  ASP A 136     9040   6691   7367   -538   -567   -318       C  
ATOM    995  OD1 ASP A 136     -12.854  13.854  57.845  1.00 66.05           O  
ANISOU  995  OD1 ASP A 136     9677   7341   8079   -554   -464   -373       O  
ATOM    996  OD2 ASP A 136     -11.730  12.252  56.821  1.00 58.49           O  
ANISOU  996  OD2 ASP A 136     8583   6465   7174   -522   -566   -234       O  
ATOM    997  N   ALA A 137     -10.178  12.679  62.099  1.00 46.70           N  
ANISOU  997  N   ALA A 137     8099   4615   5027   -476  -1132   -506       N  
ATOM    998  CA  ALA A 137      -9.951  12.164  63.441  1.00 52.32           C  
ANISOU  998  CA  ALA A 137     9174   5239   5464   -435  -1253   -549       C  
ATOM    999  C   ALA A 137     -10.616  13.014  64.521  1.00 50.90           C  
ANISOU  999  C   ALA A 137     9266   4970   5104   -442  -1190   -664       C  
ATOM   1000  O   ALA A 137     -10.842  12.518  65.630  1.00 49.60           O  
ANISOU 1000  O   ALA A 137     9462   4732   4653   -408  -1180   -695       O  
ATOM   1001  CB  ALA A 137      -8.448  12.061  63.697  1.00 56.34           C  
ANISOU 1001  CB  ALA A 137     9661   5710   6038   -389  -1612   -550       C  
ATOM   1002  N   ALA A 138     -10.938  14.277  64.230  1.00 56.82           N  
ANISOU 1002  N   ALA A 138     9872   5712   6003   -476  -1136   -727       N  
ATOM   1003  CA  ALA A 138     -11.601  15.117  65.223  1.00 55.55           C  
ANISOU 1003  CA  ALA A 138     9969   5461   5678   -473  -1058   -845       C  
ATOM   1004  C   ALA A 138     -13.012  14.626  65.532  1.00 52.26           C  
ANISOU 1004  C   ALA A 138     9716   5056   5085   -479   -706   -844       C  
ATOM   1005  O   ALA A 138     -13.488  14.786  66.662  1.00 51.65           O  
ANISOU 1005  O   ALA A 138     9975   4889   4761   -456   -624   -924       O  
ATOM   1006  CB  ALA A 138     -11.640  16.568  64.748  1.00 55.22           C  
ANISOU 1006  CB  ALA A 138     9719   5400   5861   -504  -1071   -907       C  
ATOM   1007  N   SER A 139     -13.699  14.042  64.546  1.00 45.31           N  
ANISOU 1007  N   SER A 139     8606   4277   4333   -509   -490   -761       N  
ATOM   1008  CA  SER A 139     -15.014  13.463  64.811  1.00 50.88           C  
ANISOU 1008  CA  SER A 139     9430   4990   4912   -528   -158   -760       C  
ATOM   1009  C   SER A 139     -14.895  12.168  65.603  1.00 56.10           C  
ANISOU 1009  C   SER A 139    10399   5606   5309   -513   -142   -713       C  
ATOM   1010  O   SER A 139     -15.746  11.869  66.449  1.00 63.41           O  
ANISOU 1010  O   SER A 139    11595   6470   6027   -518     90   -743       O  
ATOM   1011  CB  SER A 139     -15.755  13.211  63.500  1.00 45.26           C  
ANISOU 1011  CB  SER A 139     8374   4390   4433   -567     27   -697       C  
ATOM   1012  OG  SER A 139     -16.007  14.426  62.827  1.00 51.62           O  
ANISOU 1012  OG  SER A 139     8939   5222   5454   -568     38   -737       O  
ATOM   1013  N   ASN A 140     -13.850  11.390  65.342  1.00 50.54           N  
ANISOU 1013  N   ASN A 140     9664   4922   4615   -490   -372   -636       N  
ATOM   1014  CA  ASN A 140     -13.632  10.111  66.001  1.00 45.05           C  
ANISOU 1014  CA  ASN A 140     9257   4177   3683   -463   -389   -577       C  
ATOM   1015  C   ASN A 140     -12.152   9.770  65.885  1.00 37.82           C  
ANISOU 1015  C   ASN A 140     8302   3260   2808   -406   -757   -534       C  
ATOM   1016  O   ASN A 140     -11.656   9.536  64.777  1.00 36.09           O  
ANISOU 1016  O   ASN A 140     7761   3129   2824   -413   -834   -469       O  
ATOM   1017  CB  ASN A 140     -14.516   9.032  65.372  1.00 37.40           C  
ANISOU 1017  CB  ASN A 140     8190   3263   2756   -514   -113   -496       C  
ATOM   1018  CG  ASN A 140     -14.438   7.690  66.098  1.00 42.22           C  
ANISOU 1018  CG  ASN A 140     9132   3797   3111   -494    -80   -430       C  
ATOM   1019  OD1 ASN A 140     -13.409   7.330  66.669  1.00 39.77           O  
ANISOU 1019  OD1 ASN A 140     9026   3429   2656   -423   -346   -410       O  
ATOM   1020  ND2 ASN A 140     -15.533   6.943  66.069  1.00 38.14           N  
ANISOU 1020  ND2 ASN A 140     8665   3272   2552   -555    241   -397       N  
ATOM   1021  N   PRO A 141     -11.417   9.736  67.001  1.00 39.98           N  
ANISOU 1021  N   PRO A 141     8898   3431   2861   -340   -994   -574       N  
ATOM   1022  CA  PRO A 141      -9.967   9.499  66.929  1.00 40.37           C  
ANISOU 1022  CA  PRO A 141     8879   3474   2986   -278  -1376   -550       C  
ATOM   1023  C   PRO A 141      -9.585   8.122  66.423  1.00 45.04           C  
ANISOU 1023  C   PRO A 141     9414   4103   3597   -247  -1398   -432       C  
ATOM   1024  O   PRO A 141      -8.393   7.879  66.209  1.00 53.31           O  
ANISOU 1024  O   PRO A 141    10342   5156   4757   -189  -1693   -406       O  
ATOM   1025  CB  PRO A 141      -9.517   9.682  68.385  1.00 45.14           C  
ANISOU 1025  CB  PRO A 141     9810   3965   3375   -195  -1553   -586       C  
ATOM   1026  CG  PRO A 141     -10.718   9.298  69.178  1.00 44.34           C  
ANISOU 1026  CG  PRO A 141    10001   3813   3033   -202  -1218   -562       C  
ATOM   1027  CD  PRO A 141     -11.886   9.830  68.394  1.00 42.44           C  
ANISOU 1027  CD  PRO A 141     9594   3640   2892   -302   -901   -608       C  
ATOM   1028  N   ASP A 142     -10.540   7.216  66.230  1.00 39.00           N  
ANISOU 1028  N   ASP A 142     8721   3354   2743   -283  -1099   -365       N  
ATOM   1029  CA  ASP A 142     -10.247   5.861  65.782  1.00 40.47           C  
ANISOU 1029  CA  ASP A 142     8889   3556   2933   -254  -1105   -258       C  
ATOM   1030  C   ASP A 142     -10.480   5.658  64.290  1.00 39.77           C  
ANISOU 1030  C   ASP A 142     8388   3590   3132   -307   -969   -202       C  
ATOM   1031  O   ASP A 142     -10.281   4.548  63.795  1.00 42.42           O  
ANISOU 1031  O   ASP A 142     8687   3941   3491   -286   -957   -119       O  
ATOM   1032  CB  ASP A 142     -11.080   4.849  66.582  1.00 41.74           C  
ANISOU 1032  CB  ASP A 142     9436   3626   2796   -262   -877   -217       C  
ATOM   1033  CG  ASP A 142     -10.783   4.895  68.067  1.00 55.62           C  
ANISOU 1033  CG  ASP A 142    11541   5253   4339   -181   -986   -230       C  
ATOM   1034  OD1 ASP A 142      -9.595   4.823  68.448  1.00 58.35           O  
ANISOU 1034  OD1 ASP A 142    11915   5558   4696    -81  -1319   -225       O  
ATOM   1035  OD2 ASP A 142     -11.737   5.021  68.865  1.00 61.58           O  
ANISOU 1035  OD2 ASP A 142    12506   5942   4951   -210   -730   -243       O  
ATOM   1036  N   TYR A 143     -10.895   6.688  63.558  1.00 38.29           N  
ANISOU 1036  N   TYR A 143     7914   3481   3153   -366   -872   -244       N  
ATOM   1037  CA  TYR A 143     -10.992   6.559  62.108  1.00 38.10           C  
ANISOU 1037  CA  TYR A 143     7521   3567   3387   -397   -785   -191       C  
ATOM   1038  C   TYR A 143      -9.594   6.427  61.521  1.00 37.52           C  
ANISOU 1038  C   TYR A 143     7249   3526   3482   -331  -1053   -147       C  
ATOM   1039  O   TYR A 143      -8.746   7.298  61.737  1.00 37.03           O  
ANISOU 1039  O   TYR A 143     7111   3447   3510   -308  -1269   -192       O  
ATOM   1040  CB  TYR A 143     -11.687   7.771  61.503  1.00 35.09           C  
ANISOU 1040  CB  TYR A 143     6907   3247   3177   -455   -650   -245       C  
ATOM   1041  CG  TYR A 143     -13.164   7.894  61.755  1.00 31.29           C  
ANISOU 1041  CG  TYR A 143     6514   2759   2618   -519   -349   -286       C  
ATOM   1042  CD1 TYR A 143     -13.903   6.839  62.248  1.00 35.41           C  
ANISOU 1042  CD1 TYR A 143     7254   3235   2965   -545   -161   -261       C  
ATOM   1043  CD2 TYR A 143     -13.819   9.082  61.477  1.00 32.75           C  
ANISOU 1043  CD2 TYR A 143     6545   2973   2926   -552   -245   -350       C  
ATOM   1044  CE1 TYR A 143     -15.261   6.971  62.465  1.00 38.88           C  
ANISOU 1044  CE1 TYR A 143     7736   3664   3374   -610    134   -304       C  
ATOM   1045  CE2 TYR A 143     -15.162   9.221  61.682  1.00 33.52           C  
ANISOU 1045  CE2 TYR A 143     6684   3064   2987   -600     30   -395       C  
ATOM   1046  CZ  TYR A 143     -15.881   8.173  62.176  1.00 39.38           C  
ANISOU 1046  CZ  TYR A 143     7619   3766   3576   -632    224   -375       C  
ATOM   1047  OH  TYR A 143     -17.229   8.342  62.372  1.00 42.05           O  
ANISOU 1047  OH  TYR A 143     7964   4096   3919   -686    515   -426       O  
ATOM   1048  N   GLU A 144      -9.346   5.352  60.770  1.00 32.92           N  
ANISOU 1048  N   GLU A 144     6571   2980   2959   -304  -1032    -66       N  
ATOM   1049  CA  GLU A 144      -8.047   5.154  60.132  1.00 31.08           C  
ANISOU 1049  CA  GLU A 144     6126   2777   2905   -234  -1245    -22       C  
ATOM   1050  C   GLU A 144      -8.042   5.519  58.660  1.00 33.37           C  
ANISOU 1050  C   GLU A 144     6057   3170   3452   -259  -1145     11       C  
ATOM   1051  O   GLU A 144      -7.035   6.007  58.142  1.00 32.26           O  
ANISOU 1051  O   GLU A 144     5689   3057   3512   -227  -1289     22       O  
ATOM   1052  CB  GLU A 144      -7.602   3.704  60.253  1.00 31.71           C  
ANISOU 1052  CB  GLU A 144     6348   2817   2883   -160  -1308     47       C  
ATOM   1053  CG  GLU A 144      -6.973   3.331  61.548  1.00 43.58           C  
ANISOU 1053  CG  GLU A 144     8159   4213   4186    -84  -1532     34       C  
ATOM   1054  CD  GLU A 144      -6.458   1.921  61.490  1.00 47.42           C  
ANISOU 1054  CD  GLU A 144     8747   4658   4613      4  -1602    111       C  
ATOM   1055  OE1 GLU A 144      -6.827   1.121  62.372  1.00 51.32           O  
ANISOU 1055  OE1 GLU A 144     9596   5057   4848     26  -1572    132       O  
ATOM   1056  OE2 GLU A 144      -5.710   1.614  60.534  1.00 45.57           O  
ANISOU 1056  OE2 GLU A 144     8246   4479   4589     54  -1667    153       O  
ATOM   1057  N   PHE A 145      -9.125   5.245  57.957  1.00 30.69           N  
ANISOU 1057  N   PHE A 145     5383   3010   3268   -213  -1844    106       N  
ATOM   1058  CA  PHE A 145      -9.172   5.505  56.534  1.00 27.81           C  
ANISOU 1058  CA  PHE A 145     4769   2590   3207   -118  -1620    -65       C  
ATOM   1059  C   PHE A 145     -10.535   6.051  56.195  1.00 28.58           C  
ANISOU 1059  C   PHE A 145     4872   2870   3119   -260  -1322   -217       C  
ATOM   1060  O   PHE A 145     -11.523   5.798  56.887  1.00 32.57           O  
ANISOU 1060  O   PHE A 145     5571   3480   3326   -438  -1230   -191       O  
ATOM   1061  CB  PHE A 145      -8.897   4.260  55.686  1.00 28.20           C  
ANISOU 1061  CB  PHE A 145     4787   2382   3545    -30  -1584      8       C  
ATOM   1062  CG  PHE A 145      -7.528   3.690  55.874  1.00 35.24           C  
ANISOU 1062  CG  PHE A 145     5601   3048   4739    151  -1883    111       C  
ATOM   1063  CD1 PHE A 145      -6.427   4.273  55.260  1.00 30.02           C  
ANISOU 1063  CD1 PHE A 145     4637   2368   4400    308  -1935    -45       C  
ATOM   1064  CD2 PHE A 145      -7.340   2.568  56.665  1.00 33.81           C  
ANISOU 1064  CD2 PHE A 145     5640   2659   4548    158  -2121    369       C  
ATOM   1065  CE1 PHE A 145      -5.159   3.739  55.437  1.00 36.49           C  
ANISOU 1065  CE1 PHE A 145     5328   2978   5557    487  -2219     -1       C  
ATOM   1066  CE2 PHE A 145      -6.080   2.031  56.845  1.00 40.80           C  
ANISOU 1066  CE2 PHE A 145     6423   3306   5775    358  -2450    460       C  
ATOM   1067  CZ  PHE A 145      -4.987   2.618  56.234  1.00 35.89           C  
ANISOU 1067  CZ  PHE A 145     5453   2681   5504    532  -2499    248       C  
ATOM   1068  N   SER A 146     -10.560   6.809  55.121  1.00 28.63           N  
ANISOU 1068  N   SER A 146     4653   2914   3312   -190  -1182   -373       N  
ATOM   1069  CA  SER A 146     -11.761   7.367  54.552  1.00 25.69           C  
ANISOU 1069  CA  SER A 146     4224   2678   2858   -270   -950   -516       C  
ATOM   1070  C   SER A 146     -11.845   6.895  53.108  1.00 23.76           C  
ANISOU 1070  C   SER A 146     3864   2365   2798   -217   -803   -542       C  
ATOM   1071  O   SER A 146     -10.820   6.766  52.435  1.00 26.10           O  
ANISOU 1071  O   SER A 146     4036   2560   3319   -107   -848   -525       O  
ATOM   1072  CB  SER A 146     -11.714   8.905  54.637  1.00 27.17           C  
ANISOU 1072  CB  SER A 146     4257   2977   3088   -242   -970   -660       C  
ATOM   1073  OG  SER A 146     -12.798   9.475  53.944  1.00 38.16           O  
ANISOU 1073  OG  SER A 146     5558   4454   4486   -275   -798   -780       O  
ATOM   1074  N   VAL A 147     -13.059   6.609  52.641  1.00 23.20           N  
ANISOU 1074  N   VAL A 147     3817   2372   2626   -311   -621   -615       N  
ATOM   1075  CA  VAL A 147     -13.310   6.199  51.266  1.00 28.03           C  
ANISOU 1075  CA  VAL A 147     4323   2983   3344   -293   -481   -678       C  
ATOM   1076  C   VAL A 147     -14.366   7.126  50.690  1.00 27.01           C  
ANISOU 1076  C   VAL A 147     4089   3029   3143   -324   -388   -794       C  
ATOM   1077  O   VAL A 147     -15.365   7.423  51.352  1.00 26.43           O  
ANISOU 1077  O   VAL A 147     4055   3047   2942   -407   -349   -872       O  
ATOM   1078  CB  VAL A 147     -13.771   4.728  51.155  1.00 20.05           C  
ANISOU 1078  CB  VAL A 147     3423   1868   2329   -374   -383   -672       C  
ATOM   1079  CG1 VAL A 147     -13.982   4.372  49.718  1.00 19.53           C  
ANISOU 1079  CG1 VAL A 147     3222   1843   2355   -366   -243   -797       C  
ATOM   1080  CG2 VAL A 147     -12.732   3.813  51.764  1.00 23.09           C  
ANISOU 1080  CG2 VAL A 147     3909   2018   2844   -317   -529   -525       C  
ATOM   1081  N   VAL A 148     -14.142   7.589  49.462  1.00 29.38           N  
ANISOU 1081  N   VAL A 148     4252   3380   3530   -267   -358   -808       N  
ATOM   1082  CA  VAL A 148     -15.025   8.548  48.811  1.00 23.05           C  
ANISOU 1082  CA  VAL A 148     3349   2714   2695   -267   -343   -861       C  
ATOM   1083  C   VAL A 148     -15.275   8.095  47.394  1.00 21.08           C  
ANISOU 1083  C   VAL A 148     3039   2562   2410   -289   -257   -889       C  
ATOM   1084  O   VAL A 148     -14.333   7.988  46.601  1.00 24.03           O  
ANISOU 1084  O   VAL A 148     3370   2928   2833   -269   -230   -842       O  
ATOM   1085  CB  VAL A 148     -14.436   9.964  48.807  1.00 25.63           C  
ANISOU 1085  CB  VAL A 148     3588   3013   3136   -192   -450   -793       C  
ATOM   1086  CG1 VAL A 148     -15.459  10.919  48.251  1.00 25.88           C  
ANISOU 1086  CG1 VAL A 148     3526   3128   3180   -176   -482   -820       C  
ATOM   1087  CG2 VAL A 148     -14.044  10.343  50.196  1.00 23.46           C  
ANISOU 1087  CG2 VAL A 148     3359   2666   2887   -182   -538   -813       C  
ATOM   1088  N   ILE A 149     -16.539   7.866  47.064  1.00 17.28           N  
ANISOU 1088  N   ILE A 149     2532   2199   1836   -346   -209   -998       N  
ATOM   1089  CA  ILE A 149     -16.964   7.449  45.737  1.00 20.89           C  
ANISOU 1089  CA  ILE A 149     2925   2802   2209   -386   -153  -1062       C  
ATOM   1090  C   ILE A 149     -17.596   8.648  45.063  1.00 26.30           C  
ANISOU 1090  C   ILE A 149     3516   3618   2861   -341   -276  -1007       C  
ATOM   1091  O   ILE A 149     -18.519   9.252  45.620  1.00 27.09           O  
ANISOU 1091  O   ILE A 149     3560   3721   3011   -312   -349  -1065       O  
ATOM   1092  CB  ILE A 149     -17.972   6.300  45.810  1.00 23.37           C  
ANISOU 1092  CB  ILE A 149     3248   3142   2489   -467    -45  -1193       C  
ATOM   1093  CG1 ILE A 149     -17.429   5.188  46.696  1.00 23.52           C  
ANISOU 1093  CG1 ILE A 149     3389   2969   2579   -508     32  -1183       C  
ATOM   1094  CG2 ILE A 149     -18.315   5.785  44.410  1.00 21.30           C  
ANISOU 1094  CG2 ILE A 149     2903   3038   2151   -503      6  -1264       C  
ATOM   1095  CD1 ILE A 149     -18.393   4.035  46.807  1.00 25.11           C  
ANISOU 1095  CD1 ILE A 149     3593   3158   2791   -593    144  -1246       C  
ATOM   1096  N   GLN A 150     -17.128   8.990  43.865  1.00 27.69           N  
ANISOU 1096  N   GLN A 150     3666   3898   2957   -345   -301   -901       N  
ATOM   1097  CA  GLN A 150     -17.626  10.181  43.183  1.00 28.78           C  
ANISOU 1097  CA  GLN A 150     3748   4122   3066   -301   -467   -764       C  
ATOM   1098  C   GLN A 150     -18.824   9.792  42.338  1.00 21.44           C  
ANISOU 1098  C   GLN A 150     2754   3407   1984   -340   -518   -875       C  
ATOM   1099  O   GLN A 150     -18.701   9.008  41.390  1.00 22.28           O  
ANISOU 1099  O   GLN A 150     2874   3687   1904   -434   -431   -943       O  
ATOM   1100  CB  GLN A 150     -16.559  10.848  42.315  1.00 31.46           C  
ANISOU 1100  CB  GLN A 150     4120   4482   3352   -328   -479   -542       C  
ATOM   1101  CG  GLN A 150     -17.007  12.183  41.687  1.00 33.40           C  
ANISOU 1101  CG  GLN A 150     4346   4747   3597   -287   -690   -313       C  
ATOM   1102  CD  GLN A 150     -17.408  13.231  42.726  1.00 36.15           C  
ANISOU 1102  CD  GLN A 150     4633   4869   4232   -159   -837   -293       C  
ATOM   1103  OE1 GLN A 150     -18.323  14.031  42.503  1.00 38.88           O  
ANISOU 1103  OE1 GLN A 150     4908   5196   4667    -80  -1039   -230       O  
ATOM   1104  NE2 GLN A 150     -16.729  13.223  43.863  1.00 20.85           N  
ANISOU 1104  NE2 GLN A 150     2704   2763   2455   -136   -753   -373       N  
ATOM   1105  N   LEU A 151     -19.975  10.339  42.690  1.00 23.04           N  
ANISOU 1105  N   LEU A 151     2859   3607   2288   -271   -659   -939       N  
ATOM   1106  CA  LEU A 151     -21.201  10.120  41.961  1.00 23.61           C  
ANISOU 1106  CA  LEU A 151     2823   3880   2269   -284   -763  -1063       C  
ATOM   1107  C   LEU A 151     -21.589  11.322  41.135  1.00 25.78           C  
ANISOU 1107  C   LEU A 151     3042   4211   2543   -193  -1051   -848       C  
ATOM   1108  O   LEU A 151     -22.639  11.299  40.475  1.00 35.34           O  
ANISOU 1108  O   LEU A 151     4141   5595   3691   -175  -1219   -923       O  
ATOM   1109  CB  LEU A 151     -22.332   9.772  42.933  1.00 35.18           C  
ANISOU 1109  CB  LEU A 151     4169   5309   3888   -284   -715  -1341       C  
ATOM   1110  CG  LEU A 151     -22.147   8.469  43.715  1.00 39.43           C  
ANISOU 1110  CG  LEU A 151     4803   5737   4441   -384   -420  -1423       C  
ATOM   1111  CD1 LEU A 151     -23.285   8.267  44.710  1.00 38.06           C  
ANISOU 1111  CD1 LEU A 151     4535   5509   4417   -399   -320  -1555       C  
ATOM   1112  CD2 LEU A 151     -22.031   7.277  42.764  1.00 41.58           C  
ANISOU 1112  CD2 LEU A 151     5108   6103   4588   -468   -300  -1445       C  
ATOM   1113  N   GLY A 152     -20.782  12.367  41.152  1.00 31.06           N  
ANISOU 1113  N   GLY A 152     3781   4722   3299   -137  -1133   -574       N  
ATOM   1114  CA  GLY A 152     -21.135  13.583  40.445  1.00 43.22           C  
ANISOU 1114  CA  GLY A 152     5292   6239   4892    -49  -1434   -310       C  
ATOM   1115  C   GLY A 152     -20.831  13.453  38.972  1.00 55.14           C  
ANISOU 1115  C   GLY A 152     6916   8003   6033   -165  -1497    -88       C  
ATOM   1116  O   GLY A 152     -19.682  13.200  38.594  1.00 46.01           O  
ANISOU 1116  O   GLY A 152     5894   6897   4692   -295  -1306     21       O  
ATOM   1117  N   ARG A 153     -21.858  13.625  38.135  1.00 75.91           N  
ANISOU 1117  N   ARG A 153     9479  10816   8546   -130  -1767    -43       N  
ATOM   1118  CA  ARG A 153     -21.702  13.381  36.704  1.00 84.73           C  
ANISOU 1118  CA  ARG A 153    10713  12262   9218   -277  -1835    127       C  
ATOM   1119  C   ARG A 153     -20.734  14.368  36.062  1.00 85.54           C  
ANISOU 1119  C   ARG A 153    11003  12304   9195   -352  -1899    583       C  
ATOM   1120  O   ARG A 153     -19.892  13.974  35.246  1.00 95.00           O  
ANISOU 1120  O   ARG A 153    12344  13730  10023   -556  -1714    667       O  
ATOM   1121  CB  ARG A 153     -23.063  13.442  36.013  1.00 88.92           C  
ANISOU 1121  CB  ARG A 153    11120  13004   9663   -208  -2182     91       C  
ATOM   1122  N   ALA A 154     -20.834  15.650  36.410  1.00 65.50           N  
ANISOU 1122  N   ALA A 154     8454   9454   6981   -209  -2137    859       N  
ATOM   1123  CA  ALA A 154     -20.004  16.664  35.770  1.00 53.92           C  
ANISOU 1123  CA  ALA A 154     7172   7889   5426   -303  -2218   1334       C  
ATOM   1124  C   ALA A 154     -20.012  17.918  36.620  1.00 53.51           C  
ANISOU 1124  C   ALA A 154     7053   7370   5910   -122  -2385   1489       C  
ATOM   1125  O   ALA A 154     -21.085  18.442  36.933  1.00 60.48           O  
ANISOU 1125  O   ALA A 154     7775   8090   7113     88  -2690   1446       O  
ATOM   1126  CB  ALA A 154     -20.507  16.985  34.359  1.00 53.66           C  
ANISOU 1126  CB  ALA A 154     7255   8111   5021   -373  -2495   1651       C  
ATOM   1127  N   PHE A 155     -18.825  18.403  36.972  1.00 50.95           N  
ANISOU 1127  N   PHE A 155     6818   6829   5713   -206  -2186   1630       N  
ATOM   1128  CA  PHE A 155     -18.696  19.645  37.725  1.00 52.51           C  
ANISOU 1128  CA  PHE A 155     6953   6569   6428    -69  -2323   1765       C  
ATOM   1129  C   PHE A 155     -17.296  20.207  37.512  1.00 59.09           C  
ANISOU 1129  C   PHE A 155     7943   7267   7241   -258  -2134   2051       C  
ATOM   1130  O   PHE A 155     -16.394  19.516  37.028  1.00 51.54           O  
ANISOU 1130  O   PHE A 155     7096   6569   5919   -475  -1842   2040       O  
ATOM   1131  CB  PHE A 155     -18.978  19.430  39.219  1.00 44.04           C  
ANISOU 1131  CB  PHE A 155     5673   5309   5749     97  -2209   1311       C  
ATOM   1132  CG  PHE A 155     -18.072  18.420  39.865  1.00 39.52           C  
ANISOU 1132  CG  PHE A 155     5123   4857   5037    -13  -1822   1026       C  
ATOM   1133  CD1 PHE A 155     -16.917  18.825  40.527  1.00 40.91           C  
ANISOU 1133  CD1 PHE A 155     5319   4816   5410    -62  -1648   1037       C  
ATOM   1134  CD2 PHE A 155     -18.363  17.067  39.792  1.00 35.25           C  
ANISOU 1134  CD2 PHE A 155     4571   4624   4200    -66  -1656    749       C  
ATOM   1135  CE1 PHE A 155     -16.069  17.899  41.117  1.00 43.09           C  
ANISOU 1135  CE1 PHE A 155     5600   5186   5585   -139  -1353    793       C  
ATOM   1136  CE2 PHE A 155     -17.523  16.132  40.375  1.00 38.38           C  
ANISOU 1136  CE2 PHE A 155     4988   5075   4519   -148  -1346    521       C  
ATOM   1137  CZ  PHE A 155     -16.374  16.548  41.041  1.00 42.16           C  
ANISOU 1137  CZ  PHE A 155     5485   5343   5192   -174  -1212    553       C  
ATOM   1138  N   ASP A 156     -17.136  21.479  37.874  1.00 66.95           N  
ANISOU 1138  N   ASP A 156     8920   7842   8677   -181  -2296   2272       N  
ATOM   1139  CA  ASP A 156     -15.851  22.163  37.882  1.00 65.39           C  
ANISOU 1139  CA  ASP A 156     8819   7429   8595   -351  -2119   2497       C  
ATOM   1140  C   ASP A 156     -15.401  22.396  39.318  1.00 54.05           C  
ANISOU 1140  C   ASP A 156     7208   5697   7633   -238  -1979   2148       C  
ATOM   1141  O   ASP A 156     -16.208  22.384  40.253  1.00 48.01           O  
ANISOU 1141  O   ASP A 156     6265   4817   7161    -22  -2086   1827       O  
ATOM   1142  CB  ASP A 156     -15.932  23.498  37.135  1.00 78.28           C  
ANISOU 1142  CB  ASP A 156    10565   8800  10377   -388  -2356   2975       C  
ATOM   1143  CG  ASP A 156     -16.261  23.324  35.670  1.00 84.72           C  
ANISOU 1143  CG  ASP A 156    11568   9964  10658   -530  -2431   3267       C  
ATOM   1144  OD1 ASP A 156     -16.228  22.171  35.195  1.00 85.52           O  
ANISOU 1144  OD1 ASP A 156    11732  10503  10259   -651  -2300   3162       O  
ATOM   1145  OD2 ASP A 156     -16.561  24.330  34.997  1.00 91.47           O  
ANISOU 1145  OD2 ASP A 156    12501  10662  11591   -522  -2619   3574       O  
ATOM   1146  N   GLY A 157     -14.098  22.613  39.484  1.00 46.50           N  
ANISOU 1146  N   GLY A 157     6289   4645   6734   -407  -1731   2189       N  
ATOM   1147  CA  GLY A 157     -13.553  22.787  40.819  1.00 41.08           C  
ANISOU 1147  CA  GLY A 157     5441   3731   6438   -327  -1607   1848       C  
ATOM   1148  C   GLY A 157     -13.763  21.551  41.673  1.00 37.28           C  
ANISOU 1148  C   GLY A 157     4861   3493   5812   -233  -1461   1387       C  
ATOM   1149  O   GLY A 157     -13.754  20.413  41.190  1.00 33.42           O  
ANISOU 1149  O   GLY A 157     4436   3346   4918   -305  -1322   1315       O  
ATOM   1150  N   GLY A 158     -13.958  21.774  42.973  1.00 37.59           N  
ANISOU 1150  N   GLY A 158     4748   3348   6186    -88  -1489   1063       N  
ATOM   1151  CA  GLY A 158     -14.263  20.669  43.871  1.00 29.85           C  
ANISOU 1151  CA  GLY A 158     3704   2573   5065    -16  -1375    670       C  
ATOM   1152  C   GLY A 158     -13.139  19.674  44.079  1.00 27.63           C  
ANISOU 1152  C   GLY A 158     3464   2472   4562   -131  -1125    548       C  
ATOM   1153  O   GLY A 158     -13.403  18.487  44.335  1.00 27.22           O  
ANISOU 1153  O   GLY A 158     3427   2642   4273   -114  -1031    347       O  
ATOM   1154  N   GLU A 159     -11.888  20.116  43.987  1.00 28.45           N  
ANISOU 1154  N   GLU A 159     3567   2464   4779   -248  -1020    652       N  
ATOM   1155  CA  GLU A 159     -10.784  19.195  44.200  1.00 26.86           C  
ANISOU 1155  CA  GLU A 159     3353   2409   4444   -330   -813    504       C  
ATOM   1156  C   GLU A 159     -10.693  18.765  45.662  1.00 26.09           C  
ANISOU 1156  C   GLU A 159     3173   2282   4457   -221   -827    172       C  
ATOM   1157  O   GLU A 159     -10.916  19.547  46.590  1.00 24.99           O  
ANISOU 1157  O   GLU A 159     2958   1960   4579   -146   -940     46       O  
ATOM   1158  CB  GLU A 159      -9.464  19.808  43.754  1.00 28.76           C  
ANISOU 1158  CB  GLU A 159     3566   2544   4816   -496   -689    656       C  
ATOM   1159  CG  GLU A 159      -9.387  20.136  42.266  1.00 31.51           C  
ANISOU 1159  CG  GLU A 159     4035   2977   4962   -675   -625   1012       C  
ATOM   1160  CD  GLU A 159      -9.908  21.520  41.963  1.00 43.39           C  
ANISOU 1160  CD  GLU A 159     5591   4205   6691   -675   -823   1321       C  
ATOM   1161  OE1 GLU A 159     -10.464  22.143  42.897  1.00 42.02           O  
ANISOU 1161  OE1 GLU A 159     5329   3785   6851   -506  -1002   1192       O  
ATOM   1162  OE2 GLU A 159      -9.757  21.988  40.806  1.00 44.57           O  
ANISOU 1162  OE2 GLU A 159     5867   4376   6690   -852   -801   1687       O  
ATOM   1163  N   PHE A 160     -10.378  17.497  45.856  1.00 14.60           N  
ANISOU 1163  N   PHE A 160     2093   1741   1713   -219   -872     35       N  
ATOM   1164  CA  PHE A 160     -10.057  16.976  47.170  1.00 18.07           C  
ANISOU 1164  CA  PHE A 160     2565   2218   2085   -319   -968     90       C  
ATOM   1165  C   PHE A 160      -8.565  17.209  47.402  1.00 24.53           C  
ANISOU 1165  C   PHE A 160     3340   3037   2944   -369  -1072     96       C  
ATOM   1166  O   PHE A 160      -7.733  16.676  46.661  1.00 23.14           O  
ANISOU 1166  O   PHE A 160     3059   2820   2913   -320  -1120    117       O  
ATOM   1167  CB  PHE A 160     -10.432  15.494  47.230  1.00 15.49           C  
ANISOU 1167  CB  PHE A 160     2204   1884   1797   -301  -1018    170       C  
ATOM   1168  CG  PHE A 160     -10.131  14.865  48.518  1.00 21.61           C  
ANISOU 1168  CG  PHE A 160     3046   2679   2485   -381  -1118    257       C  
ATOM   1169  CD1 PHE A 160     -10.974  15.050  49.596  1.00 27.61           C  
ANISOU 1169  CD1 PHE A 160     3936   3466   3088   -466  -1064    249       C  
ATOM   1170  CD2 PHE A 160      -8.986  14.101  48.677  1.00 19.88           C  
ANISOU 1170  CD2 PHE A 160     2769   2443   2340   -367  -1263    351       C  
ATOM   1171  CE1 PHE A 160     -10.678  14.484  50.814  1.00 26.66           C  
ANISOU 1171  CE1 PHE A 160     3924   3361   2844   -546  -1161    342       C  
ATOM   1172  CE2 PHE A 160      -8.699  13.521  49.887  1.00 21.54           C  
ANISOU 1172  CE2 PHE A 160     3059   2675   2450   -417  -1369    454       C  
ATOM   1173  CZ  PHE A 160      -9.543  13.721  50.960  1.00 27.44           C  
ANISOU 1173  CZ  PHE A 160     3976   3456   2995   -515  -1336    457       C  
ATOM   1174  N   VAL A 161      -8.223  18.033  48.398  1.00 20.50           N  
ANISOU 1174  N   VAL A 161     2900   2570   2318   -477  -1093     56       N  
ATOM   1175  CA  VAL A 161      -6.840  18.421  48.646  1.00 18.07           C  
ANISOU 1175  CA  VAL A 161     2527   2287   2050   -546  -1193     24       C  
ATOM   1176  C   VAL A 161      -6.415  17.956  50.029  1.00 25.38           C  
ANISOU 1176  C   VAL A 161     3480   3302   2863   -626  -1339     91       C  
ATOM   1177  O   VAL A 161      -7.054  18.304  51.028  1.00 26.06           O  
ANISOU 1177  O   VAL A 161     3707   3428   2765   -718  -1307     79       O  
ATOM   1178  CB  VAL A 161      -6.647  19.936  48.515  1.00 18.21           C  
ANISOU 1178  CB  VAL A 161     2600   2282   2036   -610  -1050   -112       C  
ATOM   1179  CG1 VAL A 161      -5.185  20.269  48.667  1.00 25.00           C  
ANISOU 1179  CG1 VAL A 161     3358   3171   2971   -696  -1142   -176       C  
ATOM   1180  CG2 VAL A 161      -7.184  20.412  47.170  1.00 16.91           C  
ANISOU 1180  CG2 VAL A 161     2449   2021   1957   -490   -871   -149       C  
ATOM   1181  N   VAL A 162      -5.302  17.216  50.082  1.00 20.68           N  
ANISOU 1181  N   VAL A 162     2749   2723   2384   -577  -1454    153       N  
ATOM   1182  CA  VAL A 162      -4.674  16.753  51.314  1.00 22.76           C  
ANISOU 1182  CA  VAL A 162     3016   3069   2563   -608  -1586    222       C  
ATOM   1183  C   VAL A 162      -3.437  17.591  51.585  1.00 30.11           C  
ANISOU 1183  C   VAL A 162     3843   4080   3519   -682  -1654    119       C  
ATOM   1184  O   VAL A 162      -2.647  17.866  50.669  1.00 26.27           O  
ANISOU 1184  O   VAL A 162     3207   3559   3216   -660  -1638     48       O  
ATOM   1185  CB  VAL A 162      -4.290  15.263  51.216  1.00 28.73           C  
ANISOU 1185  CB  VAL A 162     3690   3785   3441   -490  -1678    367       C  
ATOM   1186  CG1 VAL A 162      -3.717  14.770  52.535  1.00 31.17           C  
ANISOU 1186  CG1 VAL A 162     4031   4177   3637   -507  -1835    456       C  
ATOM   1187  CG2 VAL A 162      -5.469  14.430  50.775  1.00 24.82           C  
ANISOU 1187  CG2 VAL A 162     3275   3204   2952   -435  -1594    436       C  
ATOM   1188  N   HIS A 163      -3.244  17.961  52.855  1.00 28.56           N  
ANISOU 1188  N   HIS A 163     3724   3988   3142   -782  -1728    101       N  
ATOM   1189  CA  HIS A 163      -2.145  18.812  53.307  1.00 30.41           C  
ANISOU 1189  CA  HIS A 163     3866   4325   3365   -881  -1798    -26       C  
ATOM   1190  C   HIS A 163      -1.280  18.084  54.334  1.00 33.72           C  
ANISOU 1190  C   HIS A 163     4220   4860   3732   -855  -2015     60       C  
ATOM   1191  O   HIS A 163      -1.307  18.408  55.530  1.00 38.42           O  
ANISOU 1191  O   HIS A 163     4930   5551   4119   -955  -2085     43       O  
ATOM   1192  CB  HIS A 163      -2.685  20.110  53.902  1.00 30.10           C  
ANISOU 1192  CB  HIS A 163     3990   4306   3141  -1047  -1678   -161       C  
ATOM   1193  CG  HIS A 163      -3.408  20.968  52.912  1.00 28.06           C  
ANISOU 1193  CG  HIS A 163     3796   3934   2934  -1072  -1467   -256       C  
ATOM   1194  ND1 HIS A 163      -2.849  22.103  52.374  1.00 31.17           N  
ANISOU 1194  ND1 HIS A 163     4141   4294   3409  -1160  -1361   -426       N  
ATOM   1195  CD2 HIS A 163      -4.633  20.851  52.355  1.00 28.45           C  
ANISOU 1195  CD2 HIS A 163     3958   3887   2964  -1019  -1342   -211       C  
ATOM   1196  CE1 HIS A 163      -3.700  22.655  51.530  1.00 27.42           C  
ANISOU 1196  CE1 HIS A 163     3773   3696   2948  -1154  -1174   -466       C  
ATOM   1197  NE2 HIS A 163      -4.792  21.916  51.500  1.00 26.17           N  
ANISOU 1197  NE2 HIS A 163     3702   3511   2730  -1063  -1177   -340       N  
ATOM   1198  N   PRO A 164      -0.475  17.120  53.898  1.00 35.77           N  
ANISOU 1198  N   PRO A 164     4304   5110   4176   -725  -2124    150       N  
ATOM   1199  CA  PRO A 164       0.427  16.444  54.838  1.00 40.51           C  
ANISOU 1199  CA  PRO A 164     4827   5828   4738   -681  -2347    237       C  
ATOM   1200  C   PRO A 164       1.470  17.407  55.383  1.00 43.43           C  
ANISOU 1200  C   PRO A 164     5072   6358   5069   -795  -2451     70       C  
ATOM   1201  O   PRO A 164       1.959  18.288  54.672  1.00 41.20           O  
ANISOU 1201  O   PRO A 164     4658   6074   4922   -867  -2360   -103       O  
ATOM   1202  CB  PRO A 164       1.070  15.348  53.987  1.00 42.27           C  
ANISOU 1202  CB  PRO A 164     4865   5969   5226   -516  -2389    342       C  
ATOM   1203  CG  PRO A 164       1.001  15.874  52.602  1.00 43.75           C  
ANISOU 1203  CG  PRO A 164     4968   6045   5609   -526  -2209    231       C  
ATOM   1204  CD  PRO A 164      -0.241  16.706  52.506  1.00 35.16           C  
ANISOU 1204  CD  PRO A 164     4082   4913   4363   -621  -2044    161       C  
ATOM   1205  N   GLN A 165       1.806  17.228  56.661  1.00 48.39           N  
ANISOU 1205  N   GLN A 165     5751   7126   5509   -823  -2641    114       N  
ATOM   1206  CA  GLN A 165       2.776  18.099  57.312  1.00 46.95           C  
ANISOU 1206  CA  GLN A 165     5453   7118   5267   -941  -2767    -60       C  
ATOM   1207  C   GLN A 165       4.091  18.105  56.540  1.00 51.67           C  
ANISOU 1207  C   GLN A 165     5716   7775   6142   -896  -2827   -154       C  
ATOM   1208  O   GLN A 165       4.632  17.047  56.199  1.00 50.66           O  
ANISOU 1208  O   GLN A 165     5439   7629   6178   -739  -2924     -8       O  
ATOM   1209  CB  GLN A 165       3.004  17.647  58.753  1.00 46.68           C  
ANISOU 1209  CB  GLN A 165     5514   7231   4992   -942  -3005     38       C  
ATOM   1210  N   GLY A 166       4.579  19.305  56.237  1.00 44.16           N  
ANISOU 1210  N   GLY A 166     4652   6866   5260  -1045  -2739   -404       N  
ATOM   1211  CA  GLY A 166       5.884  19.459  55.612  1.00 50.25           C  
ANISOU 1211  CA  GLY A 166     5096   7721   6278  -1062  -2768   -530       C  
ATOM   1212  C   GLY A 166       5.997  18.858  54.228  1.00 48.44           C  
ANISOU 1212  C   GLY A 166     4752   7326   6328   -955  -2632   -433       C  
ATOM   1213  O   GLY A 166       7.026  18.257  53.896  1.00 54.00           O  
ANISOU 1213  O   GLY A 166     5211   8062   7245   -876  -2726   -383       O  
ATOM   1214  N   ARG A 167       4.963  19.006  53.413  1.00 39.73           N  
ANISOU 1214  N   ARG A 167     3823   6028   5243   -942  -2417   -407       N  
ATOM   1215  CA  ARG A 167       4.955  18.521  52.041  1.00 44.28           C  
ANISOU 1215  CA  ARG A 167     4332   6411   6080   -843  -2276   -343       C  
ATOM   1216  C   ARG A 167       4.073  19.450  51.230  1.00 37.39           C  
ANISOU 1216  C   ARG A 167     3620   5396   5189   -935  -2027   -451       C  
ATOM   1217  O   ARG A 167       3.222  20.151  51.794  1.00 38.23           O  
ANISOU 1217  O   ARG A 167     3924   5525   5075  -1023  -1974   -509       O  
ATOM   1218  CB  ARG A 167       4.419  17.082  51.945  1.00 46.15           C  
ANISOU 1218  CB  ARG A 167     4643   6540   6353   -637  -2337    -99       C  
ATOM   1219  CG  ARG A 167       5.383  15.971  52.327  1.00 52.21           C  
ANISOU 1219  CG  ARG A 167     5229   7364   7245   -499  -2540     33       C  
ATOM   1220  CD  ARG A 167       4.722  14.615  52.067  1.00 59.24           C  
ANISOU 1220  CD  ARG A 167     6226   8096   8186   -324  -2528    249       C  
ATOM   1221  NE  ARG A 167       4.594  13.804  53.279  1.00 69.51           N  
ANISOU 1221  NE  ARG A 167     7622   9488   9301   -248  -2722    418       N  
ATOM   1222  CZ  ARG A 167       3.746  12.784  53.429  1.00 65.10           C  
ANISOU 1222  CZ  ARG A 167     7237   8821   8677   -149  -2703    596       C  
ATOM   1223  NH1 ARG A 167       3.718  12.112  54.573  1.00 67.07           N  
ANISOU 1223  NH1 ARG A 167     7582   9150   8751    -90  -2876    743       N  
ATOM   1224  NH2 ARG A 167       2.919  12.436  52.450  1.00 49.77           N  
ANISOU 1224  NH2 ARG A 167     5378   6696   6835   -118  -2511    620       N  
ATOM   1225  N   PRO A 168       4.230  19.473  49.908  1.00 40.39           N  
ANISOU 1225  N   PRO A 168     3937   5602   5808   -903  -1866   -483       N  
ATOM   1226  CA  PRO A 168       3.255  20.174  49.085  1.00 33.90           C  
ANISOU 1226  CA  PRO A 168     3297   4622   4961   -944  -1649   -547       C  
ATOM   1227  C   PRO A 168       1.883  19.566  49.272  1.00 33.11           C  
ANISOU 1227  C   PRO A 168     3403   4483   4695   -838  -1667   -387       C  
ATOM   1228  O   PRO A 168       1.752  18.366  49.579  1.00 28.40           O  
ANISOU 1228  O   PRO A 168     2793   3901   4096   -704  -1791   -212       O  
ATOM   1229  CB  PRO A 168       3.777  19.958  47.656  1.00 29.33           C  
ANISOU 1229  CB  PRO A 168     2599   3853   4691   -875  -1502   -587       C  
ATOM   1230  CG  PRO A 168       5.226  19.659  47.833  1.00 39.07           C  
ANISOU 1230  CG  PRO A 168     3572   5162   6112   -878  -1600   -623       C  
ATOM   1231  CD  PRO A 168       5.328  18.909  49.107  1.00 37.53           C  
ANISOU 1231  CD  PRO A 168     3338   5160   5761   -822  -1862   -483       C  
ATOM   1232  N   PRO A 169       0.825  20.355  49.105  1.00 32.88           N  
ANISOU 1232  N   PRO A 169     3576   4387   4529   -901  -1530   -440       N  
ATOM   1233  CA  PRO A 169      -0.523  19.779  49.042  1.00 24.51           C  
ANISOU 1233  CA  PRO A 169     2692   3272   3350   -803  -1513   -297       C  
ATOM   1234  C   PRO A 169      -0.639  18.779  47.896  1.00 33.95           C  
ANISOU 1234  C   PRO A 169     3819   4339   4741   -653  -1486   -201       C  
ATOM   1235  O   PRO A 169      -0.038  18.954  46.833  1.00 22.85           O  
ANISOU 1235  O   PRO A 169     2306   2824   3551   -645  -1395   -286       O  
ATOM   1236  CB  PRO A 169      -1.423  20.999  48.807  1.00 25.42           C  
ANISOU 1236  CB  PRO A 169     3003   3313   3343   -903  -1342   -407       C  
ATOM   1237  CG  PRO A 169      -0.609  22.183  49.196  1.00 31.32           C  
ANISOU 1237  CG  PRO A 169     3719   4102   4079  -1074  -1282   -596       C  
ATOM   1238  CD  PRO A 169       0.821  21.819  48.959  1.00 35.61           C  
ANISOU 1238  CD  PRO A 169     4005   4690   4837  -1069  -1365   -641       C  
ATOM   1239  N   ASN A 170      -1.423  17.719  48.128  1.00 27.07           N  
ANISOU 1239  N   ASN A 170     3019   3468   3799   -550  -1537    -42       N  
ATOM   1240  CA  ASN A 170      -1.749  16.709  47.119  1.00 23.35           C  
ANISOU 1240  CA  ASN A 170     2515   2880   3479   -426  -1494     41       C  
ATOM   1241  C   ASN A 170      -3.164  16.945  46.601  1.00 23.12           C  
ANISOU 1241  C   ASN A 170     2648   2801   3338   -414  -1391     38       C  
ATOM   1242  O   ASN A 170      -4.134  16.823  47.357  1.00 22.84           O  
ANISOU 1242  O   ASN A 170     2745   2821   3113   -423  -1398     98       O  
ATOM   1243  CB  ASN A 170      -1.621  15.300  47.711  1.00 22.20           C  
ANISOU 1243  CB  ASN A 170     2335   2749   3350   -335  -1601    202       C  
ATOM   1244  CG  ASN A 170      -0.255  15.054  48.313  1.00 25.89           C  
ANISOU 1244  CG  ASN A 170     2642   3281   3913   -328  -1735    216       C  
ATOM   1245  OD1 ASN A 170       0.740  15.590  47.836  1.00 33.46           O  
ANISOU 1245  OD1 ASN A 170     3448   4231   5035   -360  -1718    106       O  
ATOM   1246  ND2 ASN A 170      -0.198  14.261  49.369  1.00 28.59           N  
ANISOU 1246  ND2 ASN A 170     3016   3690   4158   -289  -1866    343       N  
ATOM   1247  N   VAL A 171      -3.284  17.252  45.312  1.00 22.52           N  
ANISOU 1247  N   VAL A 171     2583   2619   3352   -365  -1207    -33       N  
ATOM   1248  CA  VAL A 171      -4.540  17.684  44.708  1.00 23.18           C  
ANISOU 1248  CA  VAL A 171     2822   2673   3313   -320  -1052    -50       C  
ATOM   1249  C   VAL A 171      -5.114  16.548  43.874  1.00 24.01           C  
ANISOU 1249  C   VAL A 171     2913   2727   3483   -225  -1026     16       C  
ATOM   1250  O   VAL A 171      -4.427  16.010  42.996  1.00 23.11           O  
ANISOU 1250  O   VAL A 171     2712   2529   3539   -193   -985      4       O  
ATOM   1251  CB  VAL A 171      -4.336  18.936  43.835  1.00 22.64           C  
ANISOU 1251  CB  VAL A 171     2823   2525   3256   -330   -864   -170       C  
ATOM   1252  CG1 VAL A 171      -5.660  19.355  43.187  1.00 17.03           C  
ANISOU 1252  CG1 VAL A 171     2261   1790   2419   -247   -739   -161       C  
ATOM   1253  CG2 VAL A 171      -3.764  20.057  44.655  1.00 18.77           C  
ANISOU 1253  CG2 VAL A 171     2349   2071   2711   -449   -854   -262       C  
ATOM   1254  N   PHE A 172      -6.386  16.220  44.111  1.00 17.82           N  
ANISOU 1254  N   PHE A 172     2211   1987   2571   -197  -1023     64       N  
ATOM   1255  CA  PHE A 172      -7.076  15.155  43.391  1.00 22.44           C  
ANISOU 1255  CA  PHE A 172     2785   2543   3198   -136   -991    101       C  
ATOM   1256  C   PHE A 172      -8.354  15.723  42.806  1.00 16.42           C  
ANISOU 1256  C   PHE A 172     2112   1809   2317    -94   -896     53       C  
ATOM   1257  O   PHE A 172      -9.220  16.186  43.553  1.00 20.71           O  
ANISOU 1257  O   PHE A 172     2715   2415   2739   -108   -896     54       O  
ATOM   1258  CB  PHE A 172      -7.408  13.969  44.307  1.00 29.29           C  
ANISOU 1258  CB  PHE A 172     3637   3439   4054   -149  -1087    201       C  
ATOM   1259  CG  PHE A 172      -6.203  13.291  44.873  1.00 27.34           C  
ANISOU 1259  CG  PHE A 172     3295   3165   3930   -153  -1210    282       C  
ATOM   1260  CD1 PHE A 172      -5.725  12.121  44.315  1.00 16.60           C  
ANISOU 1260  CD1 PHE A 172     1845   1711   2750   -103  -1198    331       C  
ATOM   1261  CD2 PHE A 172      -5.548  13.829  45.969  1.00 25.64           C  
ANISOU 1261  CD2 PHE A 172     3075   3016   3650   -207  -1336    304       C  
ATOM   1262  CE1 PHE A 172      -4.606  11.510  44.847  1.00 18.04           C  
ANISOU 1262  CE1 PHE A 172     1919   1863   3075    -77  -1322    420       C  
ATOM   1263  CE2 PHE A 172      -4.439  13.234  46.496  1.00 23.23           C  
ANISOU 1263  CE2 PHE A 172     2677   2705   3442   -189  -1426    371       C  
ATOM   1264  CZ  PHE A 172      -3.960  12.063  45.931  1.00 22.64           C  
ANISOU 1264  CZ  PHE A 172     2500   2533   3570   -113  -1426    437       C  
ATOM   1265  N   ALA A 173      -8.467  15.675  41.478  1.00 14.16           N  
ANISOU 1265  N   ALA A 173     1836   1476   2068    -42   -816     12       N  
ATOM   1266  CA  ALA A 173      -9.675  16.044  40.753  1.00 22.43           C  
ANISOU 1266  CA  ALA A 173     2946   2566   3011     23   -766    -19       C  
ATOM   1267  C   ALA A 173     -10.447  14.776  40.418  1.00 25.17           C  
ANISOU 1267  C   ALA A 173     3237   2948   3377     21   -788    -15       C  
ATOM   1268  O   ALA A 173      -9.972  13.978  39.604  1.00 30.72           O  
ANISOU 1268  O   ALA A 173     3913   3593   4166      7   -759    -29       O  
ATOM   1269  CB  ALA A 173      -9.320  16.797  39.475  1.00 22.81           C  
ANISOU 1269  CB  ALA A 173     3073   2547   3046     73   -676    -64       C  
ATOM   1270  N   PRO A 174     -11.592  14.533  41.007  1.00 27.93           N  
ANISOU 1270  N   PRO A 174     3568   3378   3665     17   -811    -13       N  
ATOM   1271  CA  PRO A 174     -12.230  13.230  40.816  1.00 32.11           C  
ANISOU 1271  CA  PRO A 174     4038   3928   4233    -18   -808    -28       C  
ATOM   1272  C   PRO A 174     -13.278  13.302  39.731  1.00 36.24           C  
ANISOU 1272  C   PRO A 174     4542   4529   4698     25   -798   -105       C  
ATOM   1273  O   PRO A 174     -13.900  14.347  39.532  1.00 37.52           O  
ANISOU 1273  O   PRO A 174     4728   4752   4778    101   -811   -122       O  
ATOM   1274  CB  PRO A 174     -12.851  12.949  42.188  1.00 36.45           C  
ANISOU 1274  CB  PRO A 174     4586   4513   4751    -68   -820      3       C  
ATOM   1275  CG  PRO A 174     -13.268  14.321  42.646  1.00 42.33           C  
ANISOU 1275  CG  PRO A 174     5377   5305   5402    -32   -814    -12       C  
ATOM   1276  CD  PRO A 174     -12.286  15.325  42.034  1.00 36.51           C  
ANISOU 1276  CD  PRO A 174     4686   4520   4665     17   -812    -10       C  
ATOM   1277  N   ALA A 175     -13.468  12.206  39.014  1.00 32.00           N  
ANISOU 1277  N   ALA A 175     3963   3990   4204    -22   -775   -152       N  
ATOM   1278  CA  ALA A 175     -14.517  12.103  38.019  1.00 26.87           C  
ANISOU 1278  CA  ALA A 175     3278   3446   3486     -6   -794   -242       C  
ATOM   1279  C   ALA A 175     -15.527  11.064  38.480  1.00 21.82           C  
ANISOU 1279  C   ALA A 175     2539   2865   2885    -89   -770   -304       C  
ATOM   1280  O   ALA A 175     -15.325  10.357  39.474  1.00 19.49           O  
ANISOU 1280  O   ALA A 175     2241   2501   2662   -154   -720   -263       O  
ATOM   1281  CB  ALA A 175     -13.935  11.747  36.645  1.00 24.07           C  
ANISOU 1281  CB  ALA A 175     2977   3046   3123    -27   -763   -284       C  
ATOM   1282  N   TYR A 176     -16.633  10.989  37.754  1.00 20.27           N  
ANISOU 1282  N   TYR A 176     2267   2800   2636    -87   -808   -407       N  
ATOM   1283  CA  TYR A 176     -17.652   9.998  38.065  1.00 23.07           C  
ANISOU 1283  CA  TYR A 176     2509   3216   3041   -188   -763   -507       C  
ATOM   1284  C   TYR A 176     -17.034   8.615  38.147  1.00 23.07           C  
ANISOU 1284  C   TYR A 176     2539   3088   3138   -312   -648   -512       C  
ATOM   1285  O   TYR A 176     -16.248   8.221  37.284  1.00 27.83           O  
ANISOU 1285  O   TYR A 176     3197   3621   3756   -336   -619   -516       O  
ATOM   1286  CB  TYR A 176     -18.757   9.997  37.003  1.00 20.64           C  
ANISOU 1286  CB  TYR A 176     2092   3082   2669   -185   -841   -641       C  
ATOM   1287  CG  TYR A 176     -19.815   8.960  37.319  1.00 22.19           C  
ANISOU 1287  CG  TYR A 176     2148   3344   2941   -316   -772   -781       C  
ATOM   1288  CD1 TYR A 176     -20.774   9.209  38.283  1.00 22.01           C  
ANISOU 1288  CD1 TYR A 176     2020   3373   2970   -311   -747   -815       C  
ATOM   1289  CD2 TYR A 176     -19.827   7.725  36.685  1.00 24.92           C  
ANISOU 1289  CD2 TYR A 176     2476   3677   3317   -464   -695   -893       C  
ATOM   1290  CE1 TYR A 176     -21.736   8.277  38.587  1.00 29.81           C  
ANISOU 1290  CE1 TYR A 176     2880   4404   4041   -448   -650   -962       C  
ATOM   1291  CE2 TYR A 176     -20.793   6.778  36.981  1.00 27.94           C  
ANISOU 1291  CE2 TYR A 176     2733   4104   3777   -605   -599  -1042       C  
ATOM   1292  CZ  TYR A 176     -21.742   7.063  37.938  1.00 26.76           C  
ANISOU 1292  CZ  TYR A 176     2475   4011   3683   -597   -577  -1076       C  
ATOM   1293  OH  TYR A 176     -22.700   6.139  38.253  1.00 27.78           O  
ANISOU 1293  OH  TYR A 176     2489   4164   3901   -746   -446  -1232       O  
ATOM   1294  N   GLY A 177     -17.390   7.871  39.185  1.00 18.43           N  
ANISOU 1294  N   GLY A 177     1932   2450   2621   -390   -557   -511       N  
ATOM   1295  CA  GLY A 177     -16.913   6.517  39.285  1.00 17.36           C  
ANISOU 1295  CA  GLY A 177     1835   2174   2587   -492   -428   -505       C  
ATOM   1296  C   GLY A 177     -15.543   6.353  39.902  1.00 20.47           C  
ANISOU 1296  C   GLY A 177     2330   2400   3047   -447   -416   -338       C  
ATOM   1297  O   GLY A 177     -15.175   5.220  40.232  1.00 20.35           O  
ANISOU 1297  O   GLY A 177     2353   2246   3134   -505   -304   -298       O  
ATOM   1298  N   THR A 178     -14.765   7.427  40.062  1.00 16.02           N  
ANISOU 1298  N   THR A 178     1805   1839   2442   -345   -522   -241       N  
ATOM   1299  CA  THR A 178     -13.510   7.285  40.780  1.00 15.64           C  
ANISOU 1299  CA  THR A 178     1817   1661   2467   -307   -538    -93       C  
ATOM   1300  C   THR A 178     -13.768   7.180  42.278  1.00 17.47           C  
ANISOU 1300  C   THR A 178     2101   1875   2660   -322   -548     -3       C  
ATOM   1301  O   THR A 178     -14.822   7.560  42.791  1.00 16.11           O  
ANISOU 1301  O   THR A 178     1927   1791   2401   -352   -537    -57       O  
ATOM   1302  CB  THR A 178     -12.548   8.457  40.524  1.00 30.22           C  
ANISOU 1302  CB  THR A 178     3679   3514   4290   -222   -633    -44       C  
ATOM   1303  OG1 THR A 178     -13.084   9.663  41.086  1.00 26.60           O  
ANISOU 1303  OG1 THR A 178     3239   3161   3708   -182   -705    -43       O  
ATOM   1304  CG2 THR A 178     -12.269   8.646  39.033  1.00 30.78           C  
ANISOU 1304  CG2 THR A 178     3744   3584   4368   -212   -603   -129       C  
ATOM   1305  N   VAL A 179     -12.763   6.664  42.979  1.00 13.77           N  
ANISOU 1305  N   VAL A 179     1034   1608   2592   -299   -166    167       N  
ATOM   1306  CA  VAL A 179     -12.821   6.385  44.405  1.00 19.77           C  
ANISOU 1306  CA  VAL A 179     1865   2254   3394   -362    -84    224       C  
ATOM   1307  C   VAL A 179     -11.507   6.852  45.013  1.00 23.77           C  
ANISOU 1307  C   VAL A 179     2467   2844   3721   -338   -240    323       C  
ATOM   1308  O   VAL A 179     -10.428   6.461  44.553  1.00 22.53           O  
ANISOU 1308  O   VAL A 179     2255   2775   3530   -285   -364    396       O  
ATOM   1309  CB  VAL A 179     -13.039   4.880  44.678  1.00 22.08           C  
ANISOU 1309  CB  VAL A 179     2238   2446   3706   -336     63    245       C  
ATOM   1310  CG1 VAL A 179     -12.990   4.591  46.160  1.00 24.28           C  
ANISOU 1310  CG1 VAL A 179     2761   2637   3828   -340    166    317       C  
ATOM   1311  CG2 VAL A 179     -14.359   4.410  44.069  1.00 15.73           C  
ANISOU 1311  CG2 VAL A 179     1326   1563   3088   -373    210    120       C  
ATOM   1312  N   ILE A 180     -11.590   7.693  46.034  1.00 18.63           N  
ANISOU 1312  N   ILE A 180     1946   2167   2966   -379   -234    307       N  
ATOM   1313  CA  ILE A 180     -10.414   8.174  46.744  1.00 19.13           C  
ANISOU 1313  CA  ILE A 180     2108   2307   2853   -374   -396    377       C  
ATOM   1314  C   ILE A 180     -10.341   7.419  48.065  1.00 20.96           C  
ANISOU 1314  C   ILE A 180     2582   2483   2898   -357   -321    437       C  
ATOM   1315  O   ILE A 180     -11.364   7.215  48.730  1.00 16.74           O  
ANISOU 1315  O   ILE A 180     2175   1841   2344   -394   -118    387       O  
ATOM   1316  CB  ILE A 180     -10.468   9.709  46.939  1.00 16.77           C  
ANISOU 1316  CB  ILE A 180     1797   2020   2555   -444   -463    302       C  
ATOM   1317  CG1 ILE A 180     -10.423  10.405  45.571  1.00 20.74           C  
ANISOU 1317  CG1 ILE A 180     2076   2575   3228   -454   -554    292       C  
ATOM   1318  CG2 ILE A 180      -9.307  10.225  47.840  1.00 14.67           C  
ANISOU 1318  CG2 ILE A 180     1649   1827   2099   -463   -632    341       C  
ATOM   1319  CD1 ILE A 180     -10.724  11.933  45.564  1.00 19.62           C  
ANISOU 1319  CD1 ILE A 180     1940   2396   3118   -481   -555    210       C  
ATOM   1320  N   VAL A 181      -9.154   6.925  48.401  1.00 22.74           N  
ANISOU 1320  N   VAL A 181     2864   2779   2998   -296   -478    555       N  
ATOM   1321  CA  VAL A 181      -8.887   6.305  49.692  1.00 24.35           C  
ANISOU 1321  CA  VAL A 181     3319   2951   2982   -269   -471    651       C  
ATOM   1322  C   VAL A 181      -7.803   7.134  50.344  1.00 22.82           C  
ANISOU 1322  C   VAL A 181     3181   2877   2614   -284   -708    673       C  
ATOM   1323  O   VAL A 181      -6.794   7.449  49.705  1.00 27.03           O  
ANISOU 1323  O   VAL A 181     3534   3516   3221   -258   -905    695       O  
ATOM   1324  CB  VAL A 181      -8.446   4.836  49.557  1.00 23.80           C  
ANISOU 1324  CB  VAL A 181     3266   2837   2940   -162   -471    790       C  
ATOM   1325  CG1 VAL A 181      -8.272   4.218  50.936  1.00 24.20           C  
ANISOU 1325  CG1 VAL A 181     3609   2839   2748   -133   -463    921       C  
ATOM   1326  CG2 VAL A 181      -9.460   4.038  48.740  1.00 17.53           C  
ANISOU 1326  CG2 VAL A 181     2379   1924   2358   -163   -254    736       C  
ATOM   1327  N   THR A 182      -8.027   7.548  51.580  1.00 26.87           N  
ANISOU 1327  N   THR A 182     3931   3378   2901   -341   -681    645       N  
ATOM   1328  CA  THR A 182      -7.050   8.429  52.196  1.00 27.70           C  
ANISOU 1328  CA  THR A 182     4083   3600   2842   -378   -920    627       C  
ATOM   1329  C   THR A 182      -6.939   8.115  53.678  1.00 30.15           C  
ANISOU 1329  C   THR A 182     4715   3922   2820   -384   -942    687       C  
ATOM   1330  O   THR A 182      -7.901   7.666  54.308  1.00 25.47           O  
ANISOU 1330  O   THR A 182     4329   3230   2118   -407   -704    687       O  
ATOM   1331  CB  THR A 182      -7.396   9.919  51.937  1.00 21.80           C  
ANISOU 1331  CB  THR A 182     3244   2851   2187   -486   -909    449       C  
ATOM   1332  OG1 THR A 182      -6.425  10.746  52.584  1.00 28.05           O  
ANISOU 1332  OG1 THR A 182     4087   3743   2827   -540  -1142    413       O  
ATOM   1333  CG2 THR A 182      -8.767  10.278  52.459  1.00 24.46           C  
ANISOU 1333  CG2 THR A 182     3725   3068   2501   -554   -639    319       C  
ATOM   1334  N   SER A 183      -5.725   8.291  54.207  1.00 32.17           N  
ANISOU 1334  N   SER A 183     5005   4305   2915   -364  -1234    748       N  
ATOM   1335  CA ASER A 183      -5.479   8.130  55.632  0.29 30.81           C  
ANISOU 1335  CA ASER A 183     5149   4179   2378   -377  -1321    805       C  
ATOM   1336  CA BSER A 183      -5.475   8.135  55.633  0.71 28.74           C  
ANISOU 1336  CA BSER A 183     4887   3918   2116   -377  -1322    805       C  
ATOM   1337  C   SER A 183      -5.963   9.359  56.392  1.00 32.39           C  
ANISOU 1337  C   SER A 183     5508   4391   2406   -521  -1257    601       C  
ATOM   1338  O   SER A 183      -5.699  10.496  55.995  1.00 43.58           O  
ANISOU 1338  O   SER A 183     6764   5845   3952   -595  -1351    450       O  
ATOM   1339  CB ASER A 183      -3.989   7.905  55.893  0.29 31.77           C  
ANISOU 1339  CB ASER A 183     5105   4428   2537   -255  -1543    851       C  
ATOM   1340  CB BSER A 183      -3.986   7.935  55.907  0.71 31.79           C  
ANISOU 1340  CB BSER A 183     5110   4433   2537   -258  -1545    847       C  
ATOM   1341  OG ASER A 183      -3.545   6.678  55.336  0.29 30.57           O  
ANISOU 1341  OG ASER A 183     4816   4249   2549   -101  -1535    999       O  
ATOM   1342  OG BSER A 183      -3.737   7.925  57.308  0.71 36.78           O  
ANISOU 1342  OG BSER A 183     5985   5132   2858   -262  -1611    863       O  
ATOM   1343  N   CYS A 184      -6.659   9.124  57.496  1.00 34.84           N  
ANISOU 1343  N   CYS A 184     6146   4663   2430   -563  -1082    595       N  
ATOM   1344  CA  CYS A 184      -7.231  10.201  58.299  1.00 42.78           C  
ANISOU 1344  CA  CYS A 184     7335   5664   3256   -698   -964    377       C  
ATOM   1345  C   CYS A 184      -6.188  10.945  59.129  1.00 47.86           C  
ANISOU 1345  C   CYS A 184     8061   6457   3668   -746  -1263    303       C  
ATOM   1346  O   CYS A 184      -6.556  11.800  59.947  1.00 51.20           O  
ANISOU 1346  O   CYS A 184     8672   6885   3896   -859  -1184    110       O  
ATOM   1347  CB  CYS A 184      -8.335   9.644  59.205  1.00 46.68           C  
ANISOU 1347  CB  CYS A 184     8147   6071   3519   -733   -631    388       C  
ATOM   1348  SG  CYS A 184      -9.690   8.833  58.294  1.00 46.18           S  
ANISOU 1348  SG  CYS A 184     7930   5815   3802   -695   -235    423       S  
ATOM   1349  N   ALA A 185      -4.906  10.642  58.933  1.00 44.80           N  
ANISOU 1349  N   ALA A 185     7437   6173   3412   -628  -1523    413       N  
ATOM   1350  CA  ALA A 185      -3.821  11.311  59.638  1.00 44.43           C  
ANISOU 1350  CA  ALA A 185     7334   6264   3284   -633  -1751    327       C  
ATOM   1351  C   ALA A 185      -3.510  12.693  59.085  1.00 39.68           C  
ANISOU 1351  C   ALA A 185     6524   5664   2890   -733  -1832    125       C  
ATOM   1352  O   ALA A 185      -2.803  13.457  59.747  1.00 42.26           O  
ANISOU 1352  O   ALA A 185     6842   6082   3133   -776  -1979      3       O  
ATOM   1353  CB  ALA A 185      -2.551  10.458  59.580  1.00 43.73           C  
ANISOU 1353  CB  ALA A 185     7051   6282   3283   -468  -1950    500       C  
ATOM   1354  N   HIS A 186      -3.993  13.026  57.893  1.00 34.61           N  
ANISOU 1354  N   HIS A 186     5704   4921   2523   -770  -1742     92       N  
ATOM   1355  CA  HIS A 186      -3.648  14.275  57.235  1.00 37.72           C  
ANISOU 1355  CA  HIS A 186     5865   5296   3171   -847  -1800    -60       C  
ATOM   1356  C   HIS A 186      -4.860  15.181  57.158  1.00 37.39           C  
ANISOU 1356  C   HIS A 186     5953   5117   3137   -995  -1629   -252       C  
ATOM   1357  O   HIS A 186      -5.968  14.727  56.858  1.00 38.30           O  
ANISOU 1357  O   HIS A 186     6142   5129   3280   -985  -1398   -231       O  
ATOM   1358  CB  HIS A 186      -3.121  14.040  55.825  1.00 37.56           C  
ANISOU 1358  CB  HIS A 186     5495   5270   3508   -759  -1812     48       C  
ATOM   1359  CG  HIS A 186      -1.886  13.204  55.775  1.00 45.84           C  
ANISOU 1359  CG  HIS A 186     6388   6430   4597   -612  -1928    183       C  
ATOM   1360  ND1 HIS A 186      -0.707  13.584  56.376  1.00 48.98           N  
ANISOU 1360  ND1 HIS A 186     6720   6948   4943   -600  -2096    131       N  
ATOM   1361  CD2 HIS A 186      -1.647  12.004  55.196  1.00 47.15           C  
ANISOU 1361  CD2 HIS A 186     6452   6603   4859   -476  -1894    344       C  
ATOM   1362  CE1 HIS A 186       0.207  12.653  56.170  1.00 50.36           C  
ANISOU 1362  CE1 HIS A 186     6758   7201   5177   -460  -2162    257       C  
ATOM   1363  NE2 HIS A 186      -0.337  11.683  55.457  1.00 48.13           N  
ANISOU 1363  NE2 HIS A 186     6457   6844   4988   -380  -2034    382       N  
ATOM   1364  N   ARG A 187      -4.630  16.461  57.435  1.00 40.31           N  
ANISOU 1364  N   ARG A 187     6290   5464   3562  -1091  -1669   -452       N  
ATOM   1365  CA  ARG A 187      -5.631  17.479  57.169  1.00 35.23           C  
ANISOU 1365  CA  ARG A 187     5679   4652   3053  -1211  -1498   -657       C  
ATOM   1366  C   ARG A 187      -6.002  17.457  55.692  1.00 30.87           C  
ANISOU 1366  C   ARG A 187     4849   4005   2877  -1166  -1421   -562       C  
ATOM   1367  O   ARG A 187      -5.161  17.180  54.833  1.00 30.90           O  
ANISOU 1367  O   ARG A 187     4599   4084   3060  -1088  -1549   -404       O  
ATOM   1368  CB  ARG A 187      -5.081  18.850  57.576  1.00 38.20           C  
ANISOU 1368  CB  ARG A 187     5997   5012   3503  -1288  -1577   -857       C  
ATOM   1369  CG  ARG A 187      -4.777  18.981  59.062  1.00 48.38           C  
ANISOU 1369  CG  ARG A 187     7541   6403   4440  -1325  -1635   -981       C  
ATOM   1370  CD  ARG A 187      -4.074  20.304  59.413  1.00 59.92           C  
ANISOU 1370  CD  ARG A 187     8910   7862   5994  -1404  -1753  -1186       C  
ATOM   1371  NE  ARG A 187      -4.937  21.487  59.315  1.00 70.80           N  
ANISOU 1371  NE  ARG A 187    10315   9034   7550  -1498  -1570  -1424       N  
ATOM   1372  CZ  ARG A 187      -5.858  21.830  60.218  1.00 72.74           C  
ANISOU 1372  CZ  ARG A 187    10826   9197   7615  -1555  -1370  -1632       C  
ATOM   1373  NH1 ARG A 187      -6.060  21.071  61.286  1.00 77.24           N  
ANISOU 1373  NH1 ARG A 187    11678   9886   7784  -1541  -1320  -1618       N  
ATOM   1374  NH2 ARG A 187      -6.590  22.928  60.049  1.00 68.55           N  
ANISOU 1374  NH2 ARG A 187    10269   8455   7324  -1607  -1195  -1842       N  
ATOM   1375  N   HIS A 188      -7.273  17.723  55.390  1.00 30.29           N  
ANISOU 1375  N   HIS A 188     4766   3770   2971  -1151  -1131   -642       N  
ATOM   1376  CA  HIS A 188      -7.720  17.731  53.999  1.00 25.95           C  
ANISOU 1376  CA  HIS A 188     3947   3136   2777  -1087  -1048   -548       C  
ATOM   1377  C   HIS A 188      -8.946  18.623  53.842  1.00 29.61           C  
ANISOU 1377  C   HIS A 188     4390   3403   3458  -1108   -808   -712       C  
ATOM   1378  O   HIS A 188      -9.565  19.049  54.820  1.00 27.89           O  
ANISOU 1378  O   HIS A 188     4369   3108   3120  -1158   -650   -900       O  
ATOM   1379  CB  HIS A 188      -8.031  16.323  53.490  1.00 25.26           C  
ANISOU 1379  CB  HIS A 188     3809   3099   2690   -967   -962   -355       C  
ATOM   1380  CG  HIS A 188      -9.101  15.629  54.262  1.00 48.69           C  
ANISOU 1380  CG  HIS A 188     6986   6012   5501   -940   -700   -390       C  
ATOM   1381  ND1 HIS A 188      -8.839  14.567  55.101  1.00 54.89           N  
ANISOU 1381  ND1 HIS A 188     7982   6889   5986   -908   -711   -288       N  
ATOM   1382  CD2 HIS A 188     -10.436  15.844  54.327  1.00 51.78           C  
ANISOU 1382  CD2 HIS A 188     7402   6261   6009   -942   -410   -508       C  
ATOM   1383  CE1 HIS A 188      -9.968  14.154  55.645  1.00 57.10           C  
ANISOU 1383  CE1 HIS A 188     8422   7083   6191   -907   -419   -337       C  
ATOM   1384  NE2 HIS A 188     -10.953  14.911  55.193  1.00 60.86           N  
ANISOU 1384  NE2 HIS A 188     8775   7422   6927   -928   -228   -483       N  
ATOM   1385  N   GLU A 189      -9.308  18.875  52.584  1.00 23.98           N  
ANISOU 1385  N   GLU A 189     3434   2610   3067  -1062   -780   -638       N  
ATOM   1386  CA  GLU A 189     -10.336  19.851  52.262  1.00 24.13           C  
ANISOU 1386  CA  GLU A 189     3380   2432   3358  -1065   -615   -766       C  
ATOM   1387  C   GLU A 189     -10.843  19.587  50.859  1.00 28.39           C  
ANISOU 1387  C   GLU A 189     3676   2940   4173   -977   -590   -616       C  
ATOM   1388  O   GLU A 189     -10.161  18.976  50.030  1.00 20.34           O  
ANISOU 1388  O   GLU A 189     2530   2043   3154   -944   -731   -437       O  
ATOM   1389  CB  GLU A 189      -9.785  21.279  52.329  1.00 25.47           C  
ANISOU 1389  CB  GLU A 189     3528   2503   3648  -1166   -739   -889       C  
ATOM   1390  CG  GLU A 189      -8.883  21.570  51.149  1.00 25.97           C  
ANISOU 1390  CG  GLU A 189     3362   2642   3864  -1145   -899   -707       C  
ATOM   1391  CD  GLU A 189      -8.404  23.019  51.071  1.00 39.55           C  
ANISOU 1391  CD  GLU A 189     5039   4292   5697  -1202   -910   -774       C  
ATOM   1392  OE1 GLU A 189      -9.158  23.928  51.475  1.00 43.46           O  
ANISOU 1392  OE1 GLU A 189     5620   4596   6299  -1244   -797   -930       O  
ATOM   1393  OE2 GLU A 189      -7.271  23.240  50.592  1.00 33.07           O  
ANISOU 1393  OE2 GLU A 189     4110   3592   4863  -1198  -1017   -664       O  
ATOM   1394  N   VAL A 190     -12.030  20.103  50.583  1.00 23.65           N  
ANISOU 1394  N   VAL A 190     3002   2171   3811   -938   -417   -701       N  
ATOM   1395  CA  VAL A 190     -12.568  20.129  49.234  1.00 21.66           C  
ANISOU 1395  CA  VAL A 190     2524   1886   3819   -854   -421   -571       C  
ATOM   1396  C   VAL A 190     -12.637  21.587  48.804  1.00 26.80           C  
ANISOU 1396  C   VAL A 190     3119   2445   4618   -827   -441   -570       C  
ATOM   1397  O   VAL A 190     -13.213  22.418  49.515  1.00 27.02           O  
ANISOU 1397  O   VAL A 190     3219   2313   4734   -847   -332   -742       O  
ATOM   1398  CB  VAL A 190     -13.943  19.444  49.168  1.00 20.47           C  
ANISOU 1398  CB  VAL A 190     2319   1670   3788   -782   -206   -616       C  
ATOM   1399  CG1 VAL A 190     -14.457  19.432  47.735  1.00 18.95           C  
ANISOU 1399  CG1 VAL A 190     1926   1534   3741   -649   -245   -450       C  
ATOM   1400  CG2 VAL A 190     -13.866  18.011  49.739  1.00 21.07           C  
ANISOU 1400  CG2 VAL A 190     2523   1881   3603   -772   -123   -572       C  
ATOM   1401  N   ARG A 191     -12.020  21.908  47.668  1.00 31.26           N  
ANISOU 1401  N   ARG A 191     3257   2913   5708     37   -167    268       N  
ATOM   1402  CA  ARG A 191     -12.003  23.290  47.218  1.00 26.49           C  
ANISOU 1402  CA  ARG A 191     2612   2165   5286     57   -232    406       C  
ATOM   1403  C   ARG A 191     -13.313  23.644  46.523  1.00 28.49           C  
ANISOU 1403  C   ARG A 191     2888   2539   5397    167   -169    397       C  
ATOM   1404  O   ARG A 191     -14.140  22.781  46.199  1.00 21.75           O  
ANISOU 1404  O   ARG A 191     2044   1898   4323    210    -69    310       O  
ATOM   1405  CB  ARG A 191     -10.807  23.559  46.302  1.00 24.59           C  
ANISOU 1405  CB  ARG A 191     2221   1886   5236    -10   -175    680       C  
ATOM   1406  CG  ARG A 191      -9.493  23.377  47.027  1.00 34.12           C  
ANISOU 1406  CG  ARG A 191     3356   2949   6660   -118   -277    700       C  
ATOM   1407  CD  ARG A 191      -8.300  23.784  46.200  1.00 37.47           C  
ANISOU 1407  CD  ARG A 191     3578   3323   7337   -193   -209    996       C  
ATOM   1408  NE  ARG A 191      -7.106  23.872  47.037  1.00 38.60           N  
ANISOU 1408  NE  ARG A 191     3628   3324   7714   -286   -377    986       N  
ATOM   1409  CZ  ARG A 191      -5.861  23.917  46.572  1.00 39.17           C  
ANISOU 1409  CZ  ARG A 191     3492   3425   7966   -326   -323   1186       C  
ATOM   1410  NH1 ARG A 191      -5.629  23.856  45.264  1.00 38.63           N  
ANISOU 1410  NH1 ARG A 191     3295   3492   7891   -302    -69   1437       N  
ATOM   1411  NH2 ARG A 191      -4.847  24.003  47.419  1.00 30.56           N  
ANISOU 1411  NH2 ARG A 191     2332   2238   7042   -368   -517   1138       N  
ATOM   1412  N   THR A 192     -13.488  24.947  46.309  1.00 24.35           N  
ANISOU 1412  N   THR A 192     2369   1854   5031    210   -259    490       N  
ATOM   1413  CA  THR A 192     -14.758  25.510  45.879  1.00 24.83           C  
ANISOU 1413  CA  THR A 192     2457   1972   5007    341   -261    460       C  
ATOM   1414  C   THR A 192     -15.316  24.771  44.676  1.00 27.76           C  
ANISOU 1414  C   THR A 192     2777   2610   5162    385   -123    534       C  
ATOM   1415  O   THR A 192     -14.600  24.508  43.707  1.00 27.49           O  
ANISOU 1415  O   THR A 192     2696   2647   5101    350    -30    727       O  
ATOM   1416  CB  THR A 192     -14.567  26.993  45.536  1.00 26.99           C  
ANISOU 1416  CB  THR A 192     2739   2003   5513    370   -379    629       C  
ATOM   1417  OG1 THR A 192     -13.874  27.622  46.609  1.00 40.49           O  
ANISOU 1417  OG1 THR A 192     4506   3433   7445    307   -546    557       O  
ATOM   1418  CG2 THR A 192     -15.905  27.675  45.350  1.00 27.80           C  
ANISOU 1418  CG2 THR A 192     2883   2119   5562    537   -427    559       C  
ATOM   1419  N   VAL A 193     -16.604  24.442  44.749  1.00 31.83           N  
ANISOU 1419  N   VAL A 193     3297   3273   5523    473   -114    375       N  
ATOM   1420  CA  VAL A 193     -17.313  23.864  43.616  1.00 27.26           C  
ANISOU 1420  CA  VAL A 193     2681   2922   4755    527    -54    416       C  
ATOM   1421  C   VAL A 193     -17.644  24.992  42.655  1.00 25.59           C  
ANISOU 1421  C   VAL A 193     2469   2660   4592    636   -117    599       C  
ATOM   1422  O   VAL A 193     -18.274  25.979  43.041  1.00 29.40           O  
ANISOU 1422  O   VAL A 193     2959   3015   5197    728   -219    559       O  
ATOM   1423  CB  VAL A 193     -18.580  23.126  44.062  1.00 24.69           C  
ANISOU 1423  CB  VAL A 193     2320   2758   4304    557    -48    198       C  
ATOM   1424  CG1 VAL A 193     -19.330  22.624  42.852  1.00 23.56           C  
ANISOU 1424  CG1 VAL A 193     2136   2817   3999    610    -52    234       C  
ATOM   1425  CG2 VAL A 193     -18.213  21.950  44.971  1.00 25.34           C  
ANISOU 1425  CG2 VAL A 193     2428   2877   4324    439     21     58       C  
ATOM   1426  N   ARG A 194     -17.223  24.849  41.402  1.00 26.31           N  
ANISOU 1426  N   ARG A 194     2573   2849   4575    646    -55    801       N  
ATOM   1427  CA  ARG A 194     -17.293  25.951  40.460  1.00 40.93           C  
ANISOU 1427  CA  ARG A 194     4455   4628   6468    735   -102   1040       C  
ATOM   1428  C   ARG A 194     -18.417  25.808  39.447  1.00 52.39           C  
ANISOU 1428  C   ARG A 194     5927   6271   7709    873   -159   1043       C  
ATOM   1429  O   ARG A 194     -18.735  26.789  38.765  1.00 66.18           O  
ANISOU 1429  O   ARG A 194     7714   7950   9482    979   -240   1219       O  
ATOM   1430  CB  ARG A 194     -15.946  26.121  39.736  1.00 42.40           C  
ANISOU 1430  CB  ARG A 194     4649   4773   6688    664     21   1329       C  
ATOM   1431  CG  ARG A 194     -14.857  26.722  40.633  1.00 37.69           C  
ANISOU 1431  CG  ARG A 194     4004   3914   6400    531      3   1391       C  
ATOM   1432  CD  ARG A 194     -13.658  27.256  39.868  1.00 44.51           C  
ANISOU 1432  CD  ARG A 194     4826   4697   7389    460    110   1743       C  
ATOM   1433  NE  ARG A 194     -12.499  26.382  39.991  1.00 51.17           N  
ANISOU 1433  NE  ARG A 194     5578   5617   8247    354    259   1768       N  
ATOM   1434  CZ  ARG A 194     -11.994  25.653  38.998  1.00 66.47           C  
ANISOU 1434  CZ  ARG A 194     7499   7776   9981    390    464   1906       C  
ATOM   1435  NH1 ARG A 194     -12.540  25.706  37.786  1.00 70.95           N  
ANISOU 1435  NH1 ARG A 194     8163   8511  10286    521    534   2036       N  
ATOM   1436  NH2 ARG A 194     -10.936  24.873  39.213  1.00 68.73           N  
ANISOU 1436  NH2 ARG A 194     7684   8114  10316    318    591   1907       N  
ATOM   1437  N   ALA A 195     -19.043  24.639  39.343  1.00 49.59           N  
ANISOU 1437  N   ALA A 195     5551   6130   7163    873   -151    857       N  
ATOM   1438  CA  ALA A 195     -20.191  24.524  38.456  1.00 58.84           C  
ANISOU 1438  CA  ALA A 195     6724   7464   8169    998   -266    833       C  
ATOM   1439  C   ALA A 195     -21.056  23.351  38.891  1.00 53.12           C  
ANISOU 1439  C   ALA A 195     5916   6897   7370    951   -298    565       C  
ATOM   1440  O   ALA A 195     -20.592  22.428  39.564  1.00 47.86           O  
ANISOU 1440  O   ALA A 195     5242   6245   6699    825   -202    442       O  
ATOM   1441  CB  ALA A 195     -19.762  24.376  36.990  1.00 59.67           C  
ANISOU 1441  CB  ALA A 195     6954   7691   8028   1064   -232   1041       C  
ATOM   1442  N   ASN A 196     -22.323  23.412  38.469  1.00 44.21           N  
ANISOU 1442  N   ASN A 196     4718   5877   6204   1052   -451    496       N  
ATOM   1443  CA  ASN A 196     -23.402  22.492  38.815  1.00 43.55           C  
ANISOU 1443  CA  ASN A 196     4500   5932   6115   1008   -518    272       C  
ATOM   1444  C   ASN A 196     -23.340  22.021  40.264  1.00 43.86           C  
ANISOU 1444  C   ASN A 196     4454   5921   6290    879   -393    109       C  
ATOM   1445  O   ASN A 196     -23.632  22.793  41.184  1.00 45.93           O  
ANISOU 1445  O   ASN A 196     4644   6083   6722    925   -367     67       O  
ATOM   1446  CB  ASN A 196     -23.409  21.291  37.866  1.00 40.96           C  
ANISOU 1446  CB  ASN A 196     4250   5764   5550    968   -573    225       C  
ATOM   1447  CG  ASN A 196     -24.752  20.565  37.858  1.00 47.31           C  
ANISOU 1447  CG  ASN A 196     4896   6700   6379    941   -733     42       C  
ATOM   1448  OD1 ASN A 196     -25.783  21.131  38.231  1.00 44.54           O  
ANISOU 1448  OD1 ASN A 196     4362   6362   6199   1003   -816     -1       O  
ATOM   1449  ND2 ASN A 196     -24.742  19.306  37.434  1.00 56.73           N  
ANISOU 1449  ND2 ASN A 196     6148   7980   7425    851   -782    -66       N  
ATOM   1450  N   GLU A 197     -22.975  20.759  40.477  1.00 33.34           N  
ANISOU 1450  N   GLU A 197     3152   4647   4868    736   -322     13       N  
ATOM   1451  CA  GLU A 197     -23.011  20.177  41.811  1.00 33.58           C  
ANISOU 1451  CA  GLU A 197     3121   4647   4990    613   -213   -128       C  
ATOM   1452  C   GLU A 197     -22.076  18.979  41.849  1.00 28.88           C  
ANISOU 1452  C   GLU A 197     2640   4048   4284    478   -136   -156       C  
ATOM   1453  O   GLU A 197     -21.759  18.385  40.819  1.00 24.22           O  
ANISOU 1453  O   GLU A 197     2138   3523   3541    486   -179   -125       O  
ATOM   1454  CB  GLU A 197     -24.434  19.761  42.204  1.00 42.71           C  
ANISOU 1454  CB  GLU A 197     4082   5924   6223    591   -258   -265       C  
ATOM   1455  CG  GLU A 197     -24.949  18.548  41.462  1.00 49.22           C  
ANISOU 1455  CG  GLU A 197     4871   6876   6953    499   -364   -333       C  
ATOM   1456  CD  GLU A 197     -26.335  18.119  41.924  1.00 63.57           C  
ANISOU 1456  CD  GLU A 197     6442   8802   8909    438   -402   -443       C  
ATOM   1457  OE1 GLU A 197     -27.186  18.997  42.178  1.00 67.34           O  
ANISOU 1457  OE1 GLU A 197     6746   9316   9523    556   -416   -442       O  
ATOM   1458  OE2 GLU A 197     -26.574  16.898  42.035  1.00 67.28           O  
ANISOU 1458  OE2 GLU A 197     6878   9311   9372    272   -414   -523       O  
ATOM   1459  N   ARG A 198     -21.634  18.637  43.055  1.00 24.71           N  
ANISOU 1459  N   ARG A 198     2129   3440   3821    379    -29   -221       N  
ATOM   1460  CA  ARG A 198     -20.664  17.572  43.264  1.00 25.71           C  
ANISOU 1460  CA  ARG A 198     2363   3529   3876    269     37   -243       C  
ATOM   1461  C   ARG A 198     -21.236  16.653  44.330  1.00 25.70           C  
ANISOU 1461  C   ARG A 198     2318   3543   3904    141     81   -373       C  
ATOM   1462  O   ARG A 198     -21.549  17.104  45.441  1.00 25.23           O  
ANISOU 1462  O   ARG A 198     2215   3445   3925    139    145   -411       O  
ATOM   1463  CB  ARG A 198     -19.302  18.153  43.673  1.00 29.38           C  
ANISOU 1463  CB  ARG A 198     2912   3848   4402    278    104   -145       C  
ATOM   1464  CG  ARG A 198     -18.198  17.165  44.095  1.00 26.54           C  
ANISOU 1464  CG  ARG A 198     2641   3429   4013    185    167   -164       C  
ATOM   1465  CD  ARG A 198     -17.226  17.940  44.986  1.00 23.25           C  
ANISOU 1465  CD  ARG A 198     2249   2851   3735    177    185   -107       C  
ATOM   1466  NE  ARG A 198     -15.868  17.411  45.050  1.00 26.09           N  
ANISOU 1466  NE  ARG A 198     2657   3141   4115    136    222    -52       N  
ATOM   1467  CZ  ARG A 198     -15.421  16.598  46.007  1.00 27.27           C  
ANISOU 1467  CZ  ARG A 198     2864   3228   4271     58    223   -133       C  
ATOM   1468  NH1 ARG A 198     -16.230  16.191  46.989  1.00 23.51           N  
ANISOU 1468  NH1 ARG A 198     2421   2756   3753      2    215   -256       N  
ATOM   1469  NH2 ARG A 198     -14.159  16.209  45.995  1.00 26.53           N  
ANISOU 1469  NH2 ARG A 198     2784   3069   4226     46    238    -72       N  
ATOM   1470  N   THR A 199     -21.401  15.378  43.981  1.00 23.52           N  
ANISOU 1470  N   THR A 199     2067   3316   3554     43     47   -437       N  
ATOM   1471  CA  THR A 199     -22.075  14.392  44.820  1.00 24.45           C  
ANISOU 1471  CA  THR A 199     2132   3447   3711   -105     79   -526       C  
ATOM   1472  C   THR A 199     -21.134  13.230  45.085  1.00 22.43           C  
ANISOU 1472  C   THR A 199     2033   3095   3393   -203    105   -548       C  
ATOM   1473  O   THR A 199     -20.593  12.646  44.145  1.00 23.45           O  
ANISOU 1473  O   THR A 199     2260   3216   3433   -179     40   -557       O  
ATOM   1474  CB  THR A 199     -23.344  13.876  44.148  1.00 30.15           C  
ANISOU 1474  CB  THR A 199     2713   4281   4460   -156    -38   -585       C  
ATOM   1475  OG1 THR A 199     -24.143  14.990  43.735  1.00 34.94           O  
ANISOU 1475  OG1 THR A 199     3173   4977   5127    -28    -93   -557       O  
ATOM   1476  CG2 THR A 199     -24.132  12.987  45.100  1.00 30.29           C  
ANISOU 1476  CG2 THR A 199     2629   4310   4571   -333     22   -634       C  
ATOM   1477  N   SER A 200     -20.947  12.888  46.352  1.00 20.79           N  
ANISOU 1477  N   SER A 200     1866   2818   3217   -291    197   -557       N  
ATOM   1478  CA  SER A 200     -19.980  11.861  46.700  1.00 29.05           C  
ANISOU 1478  CA  SER A 200     3070   3749   4217   -363    205   -564       C  
ATOM   1479  C   SER A 200     -20.492  11.028  47.863  1.00 22.31           C  
ANISOU 1479  C   SER A 200     2232   2860   3383   -514    267   -582       C  
ATOM   1480  O   SER A 200     -21.119  11.556  48.784  1.00 22.83           O  
ANISOU 1480  O   SER A 200     2228   2972   3475   -523    364   -569       O  
ATOM   1481  CB  SER A 200     -18.621  12.489  47.049  1.00 33.83           C  
ANISOU 1481  CB  SER A 200     3769   4259   4824   -274    237   -505       C  
ATOM   1482  OG  SER A 200     -18.719  13.376  48.150  1.00 37.63           O  
ANISOU 1482  OG  SER A 200     4238   4711   5348   -253    290   -494       O  
ATOM   1483  N   LEU A 201     -20.225   9.724  47.811  1.00 22.95           N  
ANISOU 1483  N   LEU A 201     2420   2854   3446   -620    220   -604       N  
ATOM   1484  CA  LEU A 201     -20.476   8.824  48.934  1.00 20.82           C  
ANISOU 1484  CA  LEU A 201     2214   2512   3187   -773    279   -580       C  
ATOM   1485  C   LEU A 201     -19.208   8.736  49.779  1.00 25.37           C  
ANISOU 1485  C   LEU A 201     2976   2960   3705   -728    300   -545       C  
ATOM   1486  O   LEU A 201     -18.154   8.318  49.283  1.00 24.15           O  
ANISOU 1486  O   LEU A 201     2926   2714   3537   -668    223   -559       O  
ATOM   1487  CB  LEU A 201     -20.888   7.436  48.429  1.00 22.11           C  
ANISOU 1487  CB  LEU A 201     2408   2604   3391   -921    178   -616       C  
ATOM   1488  CG  LEU A 201     -21.571   6.492  49.408  1.00 29.43           C  
ANISOU 1488  CG  LEU A 201     3340   3469   4374  -1129    239   -555       C  
ATOM   1489  CD1 LEU A 201     -22.104   5.306  48.636  1.00 38.41           C  
ANISOU 1489  CD1 LEU A 201     4471   4520   5602  -1277     84   -606       C  
ATOM   1490  CD2 LEU A 201     -20.649   6.011  50.485  1.00 31.41           C  
ANISOU 1490  CD2 LEU A 201     3805   3580   4551  -1142    292   -492       C  
ATOM   1491  N   VAL A 202     -19.320   9.077  51.060  1.00 21.71           N  
ANISOU 1491  N   VAL A 202     2555   2493   3201   -745    399   -503       N  
ATOM   1492  CA  VAL A 202     -18.176   9.163  51.957  1.00 20.54           C  
ANISOU 1492  CA  VAL A 202     2583   2229   2993   -688    378   -477       C  
ATOM   1493  C   VAL A 202     -18.390   8.175  53.098  1.00 20.78           C  
ANISOU 1493  C   VAL A 202     2759   2187   2950   -813    431   -419       C  
ATOM   1494  O   VAL A 202     -19.471   8.136  53.691  1.00 27.44           O  
ANISOU 1494  O   VAL A 202     3545   3119   3762   -898    564   -381       O  
ATOM   1495  CB  VAL A 202     -17.998  10.597  52.494  1.00 21.89           C  
ANISOU 1495  CB  VAL A 202     2735   2436   3144   -560    407   -491       C  
ATOM   1496  CG1 VAL A 202     -16.889  10.645  53.515  1.00 24.85           C  
ANISOU 1496  CG1 VAL A 202     3300   2680   3463   -516    340   -477       C  
ATOM   1497  CG2 VAL A 202     -17.709  11.557  51.358  1.00 31.12           C  
ANISOU 1497  CG2 VAL A 202     3778   3646   4401   -449    351   -507       C  
ATOM   1498  N   TYR A 203     -17.374   7.377  53.408  1.00 22.87           N  
ANISOU 1498  N   TYR A 203     3203   2295   3192   -819    337   -394       N  
ATOM   1499  CA  TYR A 203     -17.486   6.526  54.588  1.00 23.31           C  
ANISOU 1499  CA  TYR A 203     3438   2265   3154   -922    376   -310       C  
ATOM   1500  C   TYR A 203     -16.131   6.346  55.249  1.00 30.89           C  
ANISOU 1500  C   TYR A 203     4603   3072   4062   -835    246   -292       C  
ATOM   1501  O   TYR A 203     -15.082   6.605  54.655  1.00 28.00           O  
ANISOU 1501  O   TYR A 203     4208   2652   3779   -722    125   -339       O  
ATOM   1502  CB  TYR A 203     -18.125   5.158  54.290  1.00 24.44           C  
ANISOU 1502  CB  TYR A 203     3591   2336   3359  -1103    375   -262       C  
ATOM   1503  CG  TYR A 203     -17.559   4.286  53.174  1.00 27.57           C  
ANISOU 1503  CG  TYR A 203     4012   2605   3859  -1098    218   -326       C  
ATOM   1504  CD1 TYR A 203     -16.907   3.088  53.462  1.00 23.99           C  
ANISOU 1504  CD1 TYR A 203     3760   1943   3412  -1137    114   -288       C  
ATOM   1505  CD2 TYR A 203     -17.755   4.613  51.836  1.00 25.77           C  
ANISOU 1505  CD2 TYR A 203     3627   2460   3704  -1042    172   -426       C  
ATOM   1506  CE1 TYR A 203     -16.426   2.258  52.443  1.00 25.01           C  
ANISOU 1506  CE1 TYR A 203     3930   1946   3625  -1100    -25   -372       C  
ATOM   1507  CE2 TYR A 203     -17.274   3.792  50.809  1.00 24.94           C  
ANISOU 1507  CE2 TYR A 203     3580   2249   3649  -1006     40   -505       C  
ATOM   1508  CZ  TYR A 203     -16.615   2.625  51.116  1.00 23.37           C  
ANISOU 1508  CZ  TYR A 203     3576   1840   3462  -1028    -53   -489       C  
ATOM   1509  OH  TYR A 203     -16.147   1.840  50.089  1.00 31.36           O  
ANISOU 1509  OH  TYR A 203     4659   2744   4512   -954   -178   -594       O  
ATOM   1510  N   PHE A 204     -16.175   5.867  56.493  1.00 25.52           N  
ANISOU 1510  N   PHE A 204     4124   2329   3246   -886    275   -206       N  
ATOM   1511  CA  PHE A 204     -15.026   5.872  57.384  1.00 29.03           C  
ANISOU 1511  CA  PHE A 204     4779   2645   3605   -791    133   -186       C  
ATOM   1512  C   PHE A 204     -14.820   4.490  57.987  1.00 25.27           C  
ANISOU 1512  C   PHE A 204     4524   2005   3071   -881     79    -75       C  
ATOM   1513  O   PHE A 204     -15.774   3.840  58.421  1.00 34.76           O  
ANISOU 1513  O   PHE A 204     5784   3223   4199  -1027    218     28       O  
ATOM   1514  CB  PHE A 204     -15.219   6.926  58.481  1.00 24.36           C  
ANISOU 1514  CB  PHE A 204     4281   2136   2838   -710    189   -202       C  
ATOM   1515  CG  PHE A 204     -15.388   8.327  57.939  1.00 34.53           C  
ANISOU 1515  CG  PHE A 204     5376   3541   4202   -610    215   -310       C  
ATOM   1516  CD1 PHE A 204     -14.297   9.164  57.798  1.00 28.74           C  
ANISOU 1516  CD1 PHE A 204     4627   2735   3560   -489     36   -376       C  
ATOM   1517  CD2 PHE A 204     -16.633   8.785  57.542  1.00 35.38           C  
ANISOU 1517  CD2 PHE A 204     5304   3815   4324   -645    403   -330       C  
ATOM   1518  CE1 PHE A 204     -14.444  10.438  57.292  1.00 33.84           C  
ANISOU 1518  CE1 PHE A 204     5111   3451   4294   -412     48   -451       C  
ATOM   1519  CE2 PHE A 204     -16.789  10.053  57.035  1.00 34.65           C  
ANISOU 1519  CE2 PHE A 204     5054   3804   4308   -541    408   -418       C  
ATOM   1520  CZ  PHE A 204     -15.694  10.884  56.912  1.00 38.25           C  
ANISOU 1520  CZ  PHE A 204     5526   4165   4841   -428    232   -474       C  
ATOM   1521  N   TYR A 205     -13.566   4.053  58.005  1.00 32.35           N  
ANISOU 1521  N   TYR A 205     5528   2739   4024   -791   -125    -81       N  
ATOM   1522  CA  TYR A 205     -13.172   2.729  58.462  1.00 29.75           C  
ANISOU 1522  CA  TYR A 205     5418   2212   3674   -838   -229     18       C  
ATOM   1523  C   TYR A 205     -12.392   2.838  59.768  1.00 33.85           C  
ANISOU 1523  C   TYR A 205     6187   2644   4031   -747   -368     79       C  
ATOM   1524  O   TYR A 205     -11.501   3.685  59.904  1.00 35.41           O  
ANISOU 1524  O   TYR A 205     6348   2848   4256   -605   -511      2       O  
ATOM   1525  CB  TYR A 205     -12.293   2.026  57.418  1.00 28.04           C  
ANISOU 1525  CB  TYR A 205     5135   1860   3659   -766   -377    -46       C  
ATOM   1526  CG  TYR A 205     -12.987   1.236  56.334  1.00 26.12           C  
ANISOU 1526  CG  TYR A 205     4802   1592   3531   -870   -318    -83       C  
ATOM   1527  CD1 TYR A 205     -13.652   0.054  56.626  1.00 28.03           C  
ANISOU 1527  CD1 TYR A 205     5194   1694   3764  -1037   -305     15       C  
ATOM   1528  CD2 TYR A 205     -12.932   1.640  55.006  1.00 29.02           C  
ANISOU 1528  CD2 TYR A 205     4954   2056   4016   -799   -298   -210       C  
ATOM   1529  CE1 TYR A 205     -14.260  -0.701  55.635  1.00 36.38           C  
ANISOU 1529  CE1 TYR A 205     6152   2721   4947  -1119   -300    -38       C  
ATOM   1530  CE2 TYR A 205     -13.549   0.888  54.002  1.00 35.55           C  
ANISOU 1530  CE2 TYR A 205     5737   2845   4924   -876   -291   -270       C  
ATOM   1531  CZ  TYR A 205     -14.209  -0.277  54.328  1.00 34.84           C  
ANISOU 1531  CZ  TYR A 205     5775   2616   4845  -1038   -308   -195       C  
ATOM   1532  OH  TYR A 205     -14.827  -1.031  53.359  1.00 42.80           O  
ANISOU 1532  OH  TYR A 205     6715   3594   5953  -1100   -337   -267       O  
ATOM   1533  N   SER A 206     -12.726   1.972  60.718  1.00 30.24           N  
ANISOU 1533  N   SER A 206     5986   2094   3410   -835   -345    229       N  
ATOM   1534  CA  SER A 206     -12.012   1.846  61.979  1.00 32.06           C  
ANISOU 1534  CA  SER A 206     6516   2218   3448   -746   -506    308       C  
ATOM   1535  C   SER A 206     -11.926   0.368  62.338  1.00 35.00           C  
ANISOU 1535  C   SER A 206     7122   2375   3802   -829   -576    475       C  
ATOM   1536  O   SER A 206     -12.795  -0.419  61.961  1.00 34.86           O  
ANISOU 1536  O   SER A 206     7072   2326   3847  -1004   -426    559       O  
ATOM   1537  CB  SER A 206     -12.717   2.621  63.102  1.00 33.41           C  
ANISOU 1537  CB  SER A 206     6838   2545   3312   -740   -352    347       C  
ATOM   1538  OG  SER A 206     -12.078   2.441  64.362  1.00 37.40           O  
ANISOU 1538  OG  SER A 206     7689   2947   3576   -646   -524    427       O  
ATOM   1539  N   ARG A 207     -10.866  -0.009  63.057  1.00 40.94           N  
ANISOU 1539  N   ARG A 207     8107   2958   4492   -707   -834    525       N  
ATOM   1540  CA  ARG A 207     -10.822  -1.332  63.672  1.00 42.28           C  
ANISOU 1540  CA  ARG A 207     8571   2908   4585   -772   -910    718       C  
ATOM   1541  C   ARG A 207     -11.605  -1.384  64.975  1.00 40.96           C  
ANISOU 1541  C   ARG A 207     8698   2804   4062   -858   -749    912       C  
ATOM   1542  O   ARG A 207     -11.861  -2.474  65.488  1.00 43.56           O  
ANISOU 1542  O   ARG A 207     9198   3029   4323   -947   -725   1091       O  
ATOM   1543  CB  ARG A 207      -9.379  -1.761  63.938  1.00 39.14           C  
ANISOU 1543  CB  ARG A 207     8217   2390   4266   -571  -1242    678       C  
ATOM   1544  CG  ARG A 207      -8.512  -1.891  62.708  1.00 38.38           C  
ANISOU 1544  CG  ARG A 207     7780   2300   4501   -450  -1349    511       C  
ATOM   1545  CD  ARG A 207      -7.068  -2.127  63.110  1.00 40.95           C  
ANISOU 1545  CD  ARG A 207     8124   2539   4894   -250  -1656    486       C  
ATOM   1546  NE  ARG A 207      -6.569  -1.050  63.963  1.00 39.62           N  
ANISOU 1546  NE  ARG A 207     8064   2399   4592   -162  -1824    461       N  
ATOM   1547  CZ  ARG A 207      -6.315  -1.165  65.265  1.00 43.54           C  
ANISOU 1547  CZ  ARG A 207     8888   2816   4840   -118  -2002    556       C  
ATOM   1548  NH1 ARG A 207      -6.483  -2.323  65.896  1.00 43.91           N  
ANISOU 1548  NH1 ARG A 207     9174   2757   4754   -160  -2014    702       N  
ATOM   1549  NH2 ARG A 207      -5.873  -0.114  65.938  1.00 51.29           N  
ANISOU 1549  NH2 ARG A 207     9961   3819   5706    -24  -2183    496       N  
ATOM   1550  N   HIS A 208     -11.989  -0.240  65.519  1.00 40.75           N  
ANISOU 1550  N   HIS A 208     8669   3000   3816   -803   -619    850       N  
ATOM   1551  CA  HIS A 208     -12.777  -0.192  66.741  1.00 48.11           C  
ANISOU 1551  CA  HIS A 208     9877   4036   4366   -847   -412   1020       C  
ATOM   1552  C   HIS A 208     -14.250  -0.152  66.381  1.00 43.67           C  
ANISOU 1552  C   HIS A 208     9104   3659   3829  -1043    -12   1087       C  
ATOM   1553  O   HIS A 208     -14.678   0.697  65.595  1.00 41.27           O  
ANISOU 1553  O   HIS A 208     8479   3525   3676  -1041    106    916       O  
ATOM   1554  CB  HIS A 208     -12.408   1.037  67.578  1.00 44.00           C  
ANISOU 1554  CB  HIS A 208     9498   3649   3571   -646   -497    891       C  
ATOM   1555  CG  HIS A 208     -13.131   1.123  68.885  1.00 49.66           C  
ANISOU 1555  CG  HIS A 208    10549   4490   3831   -632   -283   1046       C  
ATOM   1556  ND1 HIS A 208     -13.110   0.106  69.818  1.00 54.08           N  
ANISOU 1556  ND1 HIS A 208    11463   4932   4154   -668   -294   1296       N  
ATOM   1557  CD2 HIS A 208     -13.879   2.114  69.426  1.00 51.83           C  
ANISOU 1557  CD2 HIS A 208    10855   5004   3834   -559    -39    980       C  
ATOM   1558  CE1 HIS A 208     -13.819   0.466  70.874  1.00 56.43           C  
ANISOU 1558  CE1 HIS A 208    11920   5430   4090   -614    -46   1356       C  
ATOM   1559  NE2 HIS A 208     -14.299   1.678  70.660  1.00 52.37           N  
ANISOU 1559  NE2 HIS A 208    11302   5114   3484   -547    116   1194       N  
ATOM   1560  N   ASN A 209     -15.025  -1.070  66.951  1.00 49.37           N  
ANISOU 1560  N   ASN A 209     9992   4342   4425  -1217    190   1352       N  
ATOM   1561  CA  ASN A 209     -16.467  -1.043  66.780  1.00 47.58           C  
ANISOU 1561  CA  ASN A 209     9551   4303   4223  -1413    582   1454       C  
ATOM   1562  C   ASN A 209     -17.198  -0.661  68.060  1.00 52.82           C  
ANISOU 1562  C   ASN A 209    10397   5185   4487  -1370    880   1602       C  
ATOM   1563  O   ASN A 209     -18.432  -0.648  68.070  1.00 55.47           O  
ANISOU 1563  O   ASN A 209    10502   5718   4857  -1502   1228   1701       O  
ATOM   1564  CB  ASN A 209     -16.969  -2.395  66.263  1.00 48.87           C  
ANISOU 1564  CB  ASN A 209     9563   4320   4685  -1643    605   1601       C  
ATOM   1565  CG  ASN A 209     -18.196  -2.260  65.370  1.00 52.73           C  
ANISOU 1565  CG  ASN A 209     9658   4955   5424  -1840    852   1579       C  
ATOM   1566  OD1 ASN A 209     -18.404  -1.228  64.720  1.00 56.03           O  
ANISOU 1566  OD1 ASN A 209     9861   5530   5897  -1793    920   1391       O  
ATOM   1567  ND2 ASN A 209     -19.009  -3.308  65.326  1.00 51.04           N  
ANISOU 1567  ND2 ASN A 209     9297   4695   5399  -2036    951   1756       N  
ATOM   1568  N   GLY A 210     -16.479  -0.335  69.129  1.00 52.42           N  
ANISOU 1568  N   GLY A 210    10692   5133   4094  -1156    735   1588       N  
ATOM   1569  CA  GLY A 210     -17.118   0.173  70.320  1.00 55.71           C  
ANISOU 1569  CA  GLY A 210    11247   5792   4129  -1042    999   1652       C  
ATOM   1570  C   GLY A 210     -17.532   1.625  70.146  1.00 60.14           C  
ANISOU 1570  C   GLY A 210    11689   6588   4573   -908   1164   1433       C  
ATOM   1571  O   GLY A 210     -17.573   2.177  69.044  1.00 59.51           O  
ANISOU 1571  O   GLY A 210    11291   6531   4790   -937   1126   1247       O  
ATOM   1572  N   ALA A 211     -17.834   2.257  71.273  1.00 57.01           N  
ANISOU 1572  N   ALA A 211    11462   6388   3811   -714   1310   1409       N  
ATOM   1573  CA  ALA A 211     -18.334   3.620  71.223  1.00 56.22           C  
ANISOU 1573  CA  ALA A 211    11239   6517   3606   -551   1481   1188       C  
ATOM   1574  C   ALA A 211     -17.250   4.587  70.753  1.00 56.54           C  
ANISOU 1574  C   ALA A 211    11361   6433   3687   -384   1103    890       C  
ATOM   1575  O   ALA A 211     -16.049   4.360  70.941  1.00 54.85           O  
ANISOU 1575  O   ALA A 211    11372   6004   3465   -314    697    846       O  
ATOM   1576  CB  ALA A 211     -18.868   4.050  72.586  1.00 60.74           C  
ANISOU 1576  CB  ALA A 211    11978   7311   3788   -352   1692   1211       C  
ATOM   1577  N   ASN A 212     -17.693   5.670  70.118  1.00 52.84           N  
ANISOU 1577  N   ASN A 212    10580   6110   3387   -314   1199    669       N  
ATOM   1578  CA  ASN A 212     -16.808   6.744  69.686  1.00 52.83           C  
ANISOU 1578  CA  ASN A 212    10515   6022   3537   -150    850    369       C  
ATOM   1579  C   ASN A 212     -16.109   7.358  70.892  1.00 59.94           C  
ANISOU 1579  C   ASN A 212    11873   6874   4027    103    621    249       C  
ATOM   1580  O   ASN A 212     -16.754   7.995  71.730  1.00 66.39           O  
ANISOU 1580  O   ASN A 212    12807   7864   4553    269    830    191       O  
ATOM   1581  CB  ASN A 212     -17.606   7.804  68.920  1.00 46.23           C  
ANISOU 1581  CB  ASN A 212     9304   5359   2902   -111   1047    194       C  
ATOM   1582  CG  ASN A 212     -16.722   8.819  68.225  1.00 49.17           C  
ANISOU 1582  CG  ASN A 212     9540   5611   3532     -5    698    -67       C  
ATOM   1583  OD1 ASN A 212     -15.615   9.108  68.676  1.00 54.32           O  
ANISOU 1583  OD1 ASN A 212    10436   6098   4105    113    338   -171       O  
ATOM   1584  ND2 ASN A 212     -17.213   9.375  67.120  1.00 40.69           N  
ANISOU 1584  ND2 ASN A 212     8067   4613   2779    -53    794   -159       N  
ATOM   1585  N   ARG A 213     -14.793   7.178  70.990  1.00 58.65           N  
ANISOU 1585  N   ARG A 213    11879   6477   3927    145    163    196       N  
ATOM   1586  CA  ARG A 213     -14.114   7.729  72.161  1.00 65.02           C  
ANISOU 1586  CA  ARG A 213    13043   7219   4442    375   -113     71       C  
ATOM   1587  C   ARG A 213     -13.975   9.253  72.120  1.00 61.35           C  
ANISOU 1587  C   ARG A 213    12494   6775   4041    559   -253   -236       C  
ATOM   1588  O   ARG A 213     -13.307   9.804  73.010  1.00 60.37           O  
ANISOU 1588  O   ARG A 213    12577   6557   3806    735   -542   -361       O  
ATOM   1589  CB  ARG A 213     -12.736   7.088  72.336  1.00 69.63           C  
ANISOU 1589  CB  ARG A 213    13795   7540   5119    371   -586    111       C  
ATOM   1590  CG  ARG A 213     -12.778   5.647  72.825  1.00 69.97           C  
ANISOU 1590  CG  ARG A 213    14013   7526   5046    259   -507    404       C  
ATOM   1591  CD  ARG A 213     -11.473   5.231  73.514  1.00 65.58           C  
ANISOU 1591  CD  ARG A 213    13696   6740   4481    357   -972    401       C  
ATOM   1592  NE  ARG A 213     -10.279   5.728  72.833  1.00 57.79           N  
ANISOU 1592  NE  ARG A 213    12559   5573   3826    398  -1420    218       N  
ATOM   1593  CZ  ARG A 213      -9.887   5.327  71.630  1.00 57.43           C  
ANISOU 1593  CZ  ARG A 213    12268   5432   4121    269  -1528    253       C  
ATOM   1594  NH1 ARG A 213     -10.602   4.436  70.969  1.00 66.66           N  
ANISOU 1594  NH1 ARG A 213    13260   6644   5423     82  -1210    435       N  
ATOM   1595  NH2 ARG A 213      -8.789   5.823  71.079  1.00 56.89           N  
ANISOU 1595  NH2 ARG A 213    11994   5226   4397    317  -1909     91       N  
ATOM   1596  N   ARG A 214     -14.544   9.970  71.155  1.00 59.24           N  
ANISOU 1596  N   ARG A 214    11933   6602   3973    528    -84   -360       N  
ATOM   1597  CA  ARG A 214     -14.592  11.422  71.255  1.00 58.25           C  
ANISOU 1597  CA  ARG A 214    11730   6495   3906    713   -171   -621       C  
ATOM   1598  C   ARG A 214     -15.622  11.817  72.306  1.00 62.53           C  
ANISOU 1598  C   ARG A 214    12398   7250   4109    880    157   -626       C  
ATOM   1599  O   ARG A 214     -16.777  11.383  72.252  1.00 64.10           O  
ANISOU 1599  O   ARG A 214    12480   7670   4206    816    608   -480       O  
ATOM   1600  CB  ARG A 214     -14.936  12.047  69.908  1.00 58.74           C  
ANISOU 1600  CB  ARG A 214    11408   6587   4321    637    -82   -733       C  
ATOM   1601  CG  ARG A 214     -14.548  13.516  69.790  1.00 61.74           C  
ANISOU 1601  CG  ARG A 214    11700   6873   4885    789   -333   -989       C  
ATOM   1602  CD  ARG A 214     -15.751  14.371  69.449  1.00 65.01           C  
ANISOU 1602  CD  ARG A 214    11914   7471   5317    876      6  -1088       C  
ATOM   1603  NE  ARG A 214     -16.549  13.770  68.385  1.00 70.50           N  
ANISOU 1603  NE  ARG A 214    12257   8307   6223    693    332   -944       N  
ATOM   1604  CZ  ARG A 214     -17.609  14.349  67.832  1.00 72.88           C  
ANISOU 1604  CZ  ARG A 214    12280   8772   6639    728    623   -989       C  
ATOM   1605  NH1 ARG A 214     -17.994  15.551  68.245  1.00 74.08           N  
ANISOU 1605  NH1 ARG A 214    12537   8954   6657    968    650  -1201       N  
ATOM   1606  NH2 ARG A 214     -18.281  13.729  66.867  1.00 66.82           N  
ANISOU 1606  NH2 ARG A 214    11137   8123   6127    536    858   -834       N  
ATOM   1607  N   ALA A 215     -15.197  12.630  73.268  1.00 63.13           N  
ANISOU 1607  N   ALA A 215    12693   7260   4034   1088    -74   -784       N  
ATOM   1608  CA  ALA A 215     -16.068  13.000  74.374  1.00 66.85           C  
ANISOU 1608  CA  ALA A 215    13330   7922   4145   1274    201   -806       C  
ATOM   1609  C   ALA A 215     -17.296  13.749  73.874  1.00 64.21           C  
ANISOU 1609  C   ALA A 215    12709   7804   3885   1326    579   -891       C  
ATOM   1610  O   ALA A 215     -17.193  14.663  73.050  1.00 62.76           O  
ANISOU 1610  O   ALA A 215    12308   7546   3990   1346    452  -1068       O  
ATOM   1611  CB  ALA A 215     -15.299  13.855  75.381  1.00 73.73           C  
ANISOU 1611  CB  ALA A 215    14494   8642   4876   1492   -172   -998       C  
ATOM   1612  N   ALA A 216     -18.460  13.352  74.374  1.00 72.40           N  
ANISOU 1612  N   ALA A 216    13718   9106   4686   1345   1039   -748       N  
ATOM   1613  CA  ALA A 216     -19.716  14.002  74.021  1.00 77.29           C  
ANISOU 1613  CA  ALA A 216    14037   9956   5374   1410   1420   -810       C  
ATOM   1614  C   ALA A 216     -19.963  15.217  74.907  1.00 80.05           C  
ANISOU 1614  C   ALA A 216    14549  10347   5521   1702   1392  -1042       C  
ATOM   1615  O   ALA A 216     -19.541  16.327  74.583  1.00 79.66           O  
ANISOU 1615  O   ALA A 216    14477  10142   5651   1812   1115  -1282       O  
ATOM   1616  CB  ALA A 216     -20.872  13.019  74.134  1.00 83.76           C  
ANISOU 1616  CB  ALA A 216    14682  11046   6097   1276   1920   -532       C  
TER    1617      ALA A 216                                                      
ATOM   1618  N   THR B   3     -21.576 -39.435  36.505  1.00 54.61           N  
ANISOU 1618  N   THR B   3     7899   4386   8465  -1362  -1477   -485       N  
ATOM   1619  CA  THR B   3     -21.925 -39.930  37.836  1.00 60.08           C  
ANISOU 1619  CA  THR B   3     8400   5096   9332  -1385  -1504   -277       C  
ATOM   1620  C   THR B   3     -22.291 -38.765  38.759  1.00 56.06           C  
ANISOU 1620  C   THR B   3     7584   4839   8876  -1350  -1475    -88       C  
ATOM   1621  O   THR B   3     -23.408 -38.687  39.281  1.00 52.83           O  
ANISOU 1621  O   THR B   3     6986   4549   8540  -1476  -1563    107       O  
ATOM   1622  CB  THR B   3     -20.766 -40.736  38.464  1.00 56.78           C  
ANISOU 1622  CB  THR B   3     8073   4488   9013  -1224  -1368   -325       C  
ATOM   1623  N   ALA B   4     -21.333 -37.859  38.943  1.00 45.65           N  
ANISOU 1623  N   ALA B   4     6221   3591   7532  -1175  -1331   -148       N  
ATOM   1624  CA  ALA B   4     -21.528 -36.660  39.743  1.00 33.24           C  
ANISOU 1624  CA  ALA B   4     4406   2235   5988  -1125  -1277     -2       C  
ATOM   1625  C   ALA B   4     -20.615 -35.583  39.192  1.00 33.10           C  
ANISOU 1625  C   ALA B   4     4424   2273   5880   -988  -1167   -150       C  
ATOM   1626  O   ALA B   4     -19.445 -35.853  38.912  1.00 32.45           O  
ANISOU 1626  O   ALA B   4     4472   2062   5794   -857  -1061   -307       O  
ATOM   1627  CB  ALA B   4     -21.218 -36.915  41.218  1.00 39.12           C  
ANISOU 1627  CB  ALA B   4     5038   2978   6850  -1054  -1209    155       C  
ATOM   1628  N   GLU B   5     -21.147 -34.377  39.031  1.00 30.04           N  
ANISOU 1628  N   GLU B   5     3911   2067   5435  -1012  -1179    -94       N  
ATOM   1629  CA  GLU B   5     -20.384 -33.236  38.542  1.00 28.37           C  
ANISOU 1629  CA  GLU B   5     3730   1917   5134   -903  -1076   -218       C  
ATOM   1630  C   GLU B   5     -20.470 -32.109  39.554  1.00 26.27           C  
ANISOU 1630  C   GLU B   5     3242   1819   4922   -844  -1001    -68       C  
ATOM   1631  O   GLU B   5     -21.509 -31.916  40.194  1.00 28.84           O  
ANISOU 1631  O   GLU B   5     3398   2257   5303   -920  -1043    128       O  
ATOM   1632  CB  GLU B   5     -20.901 -32.755  37.182  1.00 29.19           C  
ANISOU 1632  CB  GLU B   5     3968   2051   5071   -994  -1172   -316       C  
ATOM   1633  CG  GLU B   5     -20.903 -33.859  36.144  1.00 34.52           C  
ANISOU 1633  CG  GLU B   5     4914   2550   5650  -1073  -1242   -466       C  
ATOM   1634  CD  GLU B   5     -21.409 -33.380  34.804  1.00 42.22           C  
ANISOU 1634  CD  GLU B   5     6068   3555   6419  -1169  -1358   -550       C  
ATOM   1635  OE1 GLU B   5     -22.190 -32.405  34.764  1.00 43.16           O  
ANISOU 1635  OE1 GLU B   5     6043   3840   6516  -1219  -1470   -426       O  
ATOM   1636  OE2 GLU B   5     -21.018 -33.982  33.790  1.00 47.02           O  
ANISOU 1636  OE2 GLU B   5     6970   4012   6883  -1185  -1333   -735       O  
ATOM   1637  N   LEU B   6     -19.365 -31.379  39.691  1.00 30.46           N  
ANISOU 1637  N   LEU B   6     3777   2409   5386   -680   -839   -152       N  
ATOM   1638  CA  LEU B   6     -19.245 -30.242  40.594  1.00 30.96           C  
ANISOU 1638  CA  LEU B   6     3699   2659   5404   -587   -726    -41       C  
ATOM   1639  C   LEU B   6     -19.576 -28.971  39.817  1.00 28.01           C  
ANISOU 1639  C   LEU B   6     3330   2441   4869   -572   -685    -75       C  
ATOM   1640  O   LEU B   6     -18.856 -28.614  38.880  1.00 27.17           O  
ANISOU 1640  O   LEU B   6     3348   2314   4660   -527   -622   -238       O  
ATOM   1641  CB  LEU B   6     -17.824 -30.187  41.157  1.00 40.39           C  
ANISOU 1641  CB  LEU B   6     4898   3810   6640   -449   -623   -104       C  
ATOM   1642  CG  LEU B   6     -17.571 -29.558  42.520  1.00 40.09           C  
ANISOU 1642  CG  LEU B   6     4769   3870   6592   -387   -574     35       C  
ATOM   1643  CD1 LEU B   6     -18.507 -30.190  43.545  1.00 35.12           C  
ANISOU 1643  CD1 LEU B   6     4101   3221   6023   -469   -636    229       C  
ATOM   1644  CD2 LEU B   6     -16.114 -29.759  42.913  1.00 40.16           C  
ANISOU 1644  CD2 LEU B   6     4773   3794   6692   -280   -555    -28       C  
ATOM   1645  N   HIS B   7     -20.659 -28.290  40.198  1.00 21.98           N  
ANISOU 1645  N   HIS B   7     2438   1821   4094   -601   -701     87       N  
ATOM   1646  CA  HIS B   7     -21.094 -27.074  39.530  1.00 21.57           C  
ANISOU 1646  CA  HIS B   7     2382   1901   3913   -572   -685     90       C  
ATOM   1647  C   HIS B   7     -20.669 -25.871  40.355  1.00 22.65           C  
ANISOU 1647  C   HIS B   7     2477   2152   3975   -442   -513    137       C  
ATOM   1648  O   HIS B   7     -21.018 -25.786  41.536  1.00 24.98           O  
ANISOU 1648  O   HIS B   7     2677   2492   4324   -414   -446    278       O  
ATOM   1649  CB  HIS B   7     -22.611 -27.041  39.350  1.00 32.71           C  
ANISOU 1649  CB  HIS B   7     3650   3381   5399   -668   -820    252       C  
ATOM   1650  CG  HIS B   7     -23.140 -28.045  38.380  1.00 35.00           C  
ANISOU 1650  CG  HIS B   7     4009   3556   5733   -835  -1048    208       C  
ATOM   1651  ND1 HIS B   7     -24.091 -27.726  37.441  1.00 32.84           N  
ANISOU 1651  ND1 HIS B   7     3717   3326   5433   -925  -1239    257       N  
ATOM   1652  CD2 HIS B   7     -22.884 -29.368  38.225  1.00 25.96           C  
ANISOU 1652  CD2 HIS B   7     2973   2234   4656   -938  -1142    128       C  
ATOM   1653  CE1 HIS B   7     -24.383 -28.799  36.731  1.00 34.61           C  
ANISOU 1653  CE1 HIS B   7     4056   3406   5686  -1098  -1455    198       C  
ATOM   1654  NE2 HIS B   7     -23.658 -29.806  37.181  1.00 28.04           N  
ANISOU 1654  NE2 HIS B   7     3315   2431   4909  -1104  -1383    110       N  
ATOM   1655  N   PHE B   8     -19.952 -24.934  39.729  1.00 22.47           N  
ANISOU 1655  N   PHE B   8     2560   2165   3814   -377   -435     24       N  
ATOM   1656  CA  PHE B   8     -19.480 -23.711  40.378  1.00 26.84           C  
ANISOU 1656  CA  PHE B   8     3119   2799   4278   -278   -293     48       C  
ATOM   1657  C   PHE B   8     -20.241 -22.491  39.879  1.00 29.51           C  
ANISOU 1657  C   PHE B   8     3468   3234   4510   -238   -274    106       C  
ATOM   1658  O   PHE B   8     -20.596 -22.404  38.702  1.00 28.17           O  
ANISOU 1658  O   PHE B   8     3361   3061   4281   -280   -366     64       O  
ATOM   1659  CB  PHE B   8     -17.986 -23.457  40.129  1.00 17.39           C  
ANISOU 1659  CB  PHE B   8     2015   1557   3035   -243   -205   -104       C  
ATOM   1660  CG  PHE B   8     -17.094 -24.500  40.691  1.00 28.65           C  
ANISOU 1660  CG  PHE B   8     3405   2882   4597   -242   -221   -146       C  
ATOM   1661  CD1 PHE B   8     -16.420 -24.278  41.875  1.00 28.87           C  
ANISOU 1661  CD1 PHE B   8     3396   2914   4661   -203   -198    -91       C  
ATOM   1662  CD2 PHE B   8     -16.950 -25.722  40.051  1.00 26.50           C  
ANISOU 1662  CD2 PHE B   8     3161   2491   4417   -281   -281   -233       C  
ATOM   1663  CE1 PHE B   8     -15.603 -25.249  42.405  1.00 30.02           C  
ANISOU 1663  CE1 PHE B   8     3497   2956   4952   -193   -253   -104       C  
ATOM   1664  CE2 PHE B   8     -16.138 -26.691  40.568  1.00 25.61           C  
ANISOU 1664  CE2 PHE B   8     3011   2263   4458   -254   -298   -258       C  
ATOM   1665  CZ  PHE B   8     -15.458 -26.455  41.752  1.00 26.01           C  
ANISOU 1665  CZ  PHE B   8     2988   2328   4566   -204   -294   -183       C  
ATOM   1666  N   ARG B   9     -20.465 -21.538  40.782  1.00 33.64           N  
ANISOU 1666  N   ARG B   9     3965   3820   4995   -152   -160    204       N  
ATOM   1667  CA  ARG B   9     -20.920 -20.206  40.424  1.00 28.15           C  
ANISOU 1667  CA  ARG B   9     3313   3186   4197    -74   -105    246       C  
ATOM   1668  C   ARG B   9     -19.702 -19.286  40.357  1.00 25.98           C  
ANISOU 1668  C   ARG B   9     3201   2888   3781    -46     -2    131       C  
ATOM   1669  O   ARG B   9     -18.563 -19.718  40.570  1.00 17.52           O  
ANISOU 1669  O   ARG B   9     2163   1769   2725    -87     16     30       O  
ATOM   1670  CB  ARG B   9     -21.954 -19.705  41.435  1.00 28.12           C  
ANISOU 1670  CB  ARG B   9     3203   3235   4245     18     -5    420       C  
ATOM   1671  N   CYS B  10     -19.937 -18.006  40.057  1.00 22.95           N  
ANISOU 1671  N   CYS B  10     2906   2528   3285     23     58    158       N  
ATOM   1672  CA  CYS B  10     -18.859 -17.030  40.190  1.00 22.14           C  
ANISOU 1672  CA  CYS B  10     2958   2392   3061     30    163     76       C  
ATOM   1673  C   CYS B  10     -18.386 -16.934  41.636  1.00 24.22           C  
ANISOU 1673  C   CYS B  10     3239   2632   3330     46    232     98       C  
ATOM   1674  O   CYS B  10     -19.175 -16.994  42.593  1.00 24.43           O  
ANISOU 1674  O   CYS B  10     3230   2674   3381    107    274    208       O  
ATOM   1675  CB  CYS B  10     -19.282 -15.641  39.706  1.00 16.53           C  
ANISOU 1675  CB  CYS B  10     2372   1682   2227    104    214    119       C  
ATOM   1676  SG  CYS B  10     -19.742 -15.581  37.998  1.00 32.25           S  
ANISOU 1676  SG  CYS B  10     4422   3679   4151     72     95    107       S  
ATOM   1677  N   ASN B  11     -17.080 -16.779  41.783  1.00 21.00           N  
ANISOU 1677  N   ASN B  11     2896   2183   2900    -19    242      1       N  
ATOM   1678  CA  ASN B  11     -16.483 -16.542  43.082  1.00 19.66           C  
ANISOU 1678  CA  ASN B  11     2795   1974   2702    -33    251     18       C  
ATOM   1679  C   ASN B  11     -16.843 -15.134  43.541  1.00 21.99           C  
ANISOU 1679  C   ASN B  11     3279   2238   2836     28    350     60       C  
ATOM   1680  O   ASN B  11     -16.575 -14.161  42.828  1.00 20.60           O  
ANISOU 1680  O   ASN B  11     3204   2041   2582     22    393     16       O  
ATOM   1681  CB  ASN B  11     -14.974 -16.711  42.963  1.00 23.48           C  
ANISOU 1681  CB  ASN B  11     3251   2419   3253   -131    202    -81       C  
ATOM   1682  CG  ASN B  11     -14.299 -16.871  44.288  1.00 25.31           C  
ANISOU 1682  CG  ASN B  11     3513   2602   3501   -175    116    -50       C  
ATOM   1683  OD1 ASN B  11     -14.327 -15.965  45.118  1.00 26.63           O  
ANISOU 1683  OD1 ASN B  11     3860   2732   3526   -179    130    -16       O  
ATOM   1684  ND2 ASN B  11     -13.639 -18.007  44.481  1.00 22.61           N  
ANISOU 1684  ND2 ASN B  11     3027   2241   3324   -209     12    -63       N  
ATOM   1685  N   GLU B  12     -17.461 -15.014  44.715  1.00 23.32           N  
ANISOU 1685  N   GLU B  12     3529   2387   2945     92    407    145       N  
ATOM   1686  CA  GLU B  12     -17.943 -13.723  45.191  1.00 26.42           C  
ANISOU 1686  CA  GLU B  12     4134   2722   3182    184    541    182       C  
ATOM   1687  C   GLU B  12     -16.968 -13.034  46.137  1.00 32.35           C  
ANISOU 1687  C   GLU B  12     5137   3371   3785    104    519    129       C  
ATOM   1688  O   GLU B  12     -17.327 -12.025  46.760  1.00 34.45           O  
ANISOU 1688  O   GLU B  12     5650   3550   3890    175    637    148       O  
ATOM   1689  CB  GLU B  12     -19.297 -13.892  45.876  1.00 28.85           C  
ANISOU 1689  CB  GLU B  12     4410   3049   3502    320    678    309       C  
ATOM   1690  CG  GLU B  12     -20.348 -14.496  44.984  1.00 38.53           C  
ANISOU 1690  CG  GLU B  12     5369   4369   4901    376    660    386       C  
ATOM   1691  CD  GLU B  12     -21.523 -15.048  45.759  1.00 51.64           C  
ANISOU 1691  CD  GLU B  12     6907   6063   6650    459    778    528       C  
ATOM   1692  OE1 GLU B  12     -21.439 -15.127  47.007  1.00 50.60           O  
ANISOU 1692  OE1 GLU B  12     6923   5881   6422    465    885    556       O  
ATOM   1693  OE2 GLU B  12     -22.531 -15.406  45.114  1.00 58.37           O  
ANISOU 1693  OE2 GLU B  12     7523   6986   7669    505    759    621       O  
ATOM   1694  N   GLY B  13     -15.748 -13.545  46.256  1.00 30.60           N  
ANISOU 1694  N   GLY B  13     4863   3140   3624    -40    363     68       N  
ATOM   1695  CA  GLY B  13     -14.796 -13.006  47.209  1.00 32.97           C  
ANISOU 1695  CA  GLY B  13     5378   3340   3809   -150    269     37       C  
ATOM   1696  C   GLY B  13     -13.869 -11.984  46.591  1.00 27.59           C  
ANISOU 1696  C   GLY B  13     4767   2606   3109   -255    240    -41       C  
ATOM   1697  O   GLY B  13     -14.271 -11.242  45.695  1.00 23.21           O  
ANISOU 1697  O   GLY B  13     4242   2053   2522   -197    358    -56       O  
ATOM   1698  N   GLY B  14     -12.622 -11.948  47.054  1.00 29.35           N  
ANISOU 1698  N   GLY B  14     5008   2776   3369   -420     67    -73       N  
ATOM   1699  CA  GLY B  14     -11.610 -11.084  46.481  1.00 33.07           C  
ANISOU 1699  CA  GLY B  14     5491   3199   3876   -561     31   -132       C  
ATOM   1700  C   GLY B  14     -10.430 -11.858  45.929  1.00 32.18           C  
ANISOU 1700  C   GLY B  14     5050   3145   4032   -673    -76   -158       C  
ATOM   1701  O   GLY B  14     -10.515 -13.081  45.748  1.00 30.69           O  
ANISOU 1701  O   GLY B  14     4629   3033   3997   -608    -96   -146       O  
HETATM 1702  N   MSE B  15      -9.325 -11.158  45.667  1.00 26.41           N  
ANISOU 1702  N   MSE B  15     4295   2364   3376   -839   -130   -188       N  
HETATM 1703  CA  MSE B  15      -8.142 -11.743  45.035  1.00 26.51           C  
ANISOU 1703  CA  MSE B  15     3963   2424   3685   -935   -168   -207       C  
HETATM 1704  C   MSE B  15      -7.639 -13.002  45.750  1.00 25.39           C  
ANISOU 1704  C   MSE B  15     3598   2306   3743   -930   -365   -165       C  
HETATM 1705  O   MSE B  15      -7.349 -14.003  45.112  1.00 23.71           O  
ANISOU 1705  O   MSE B  15     3099   2156   3755   -866   -309   -182       O  
HETATM 1706  CB  MSE B  15      -7.011 -10.703  44.952  1.00 23.63           C  
ANISOU 1706  CB  MSE B  15     3610   1983   3386  -1151   -224   -214       C  
HETATM 1707  CG  MSE B  15      -5.742 -11.220  44.301  1.00 32.77           C  
ANISOU 1707  CG  MSE B  15     4370   3187   4896  -1247   -214   -217       C  
HETATM 1708 SE   MSE B  15      -6.019 -12.045  42.543  1.00 41.07          SE  
ANISOU 1708 SE   MSE B  15     5197   4349   6060  -1085    136   -289      SE  
HETATM 1709  CE  MSE B  15      -6.411 -10.450  41.491  1.00 33.78           C  
ANISOU 1709  CE  MSE B  15     4584   3377   4875  -1151    374   -318       C  
ATOM   1710  N   ALA B  16      -7.532 -12.951  47.080  1.00 23.24           N  
ANISOU 1710  N   ALA B  16     3494   1964   3374   -995   -598   -108       N  
ATOM   1711  CA  ALA B  16      -7.051 -14.120  47.808  1.00 24.03           C  
ANISOU 1711  CA  ALA B  16     3415   2067   3650   -992   -823    -44       C  
ATOM   1712  C   ALA B  16      -7.961 -15.319  47.580  1.00 24.57           C  
ANISOU 1712  C   ALA B  16     3395   2202   3738   -805   -709    -37       C  
ATOM   1713  O   ALA B  16      -7.492 -16.460  47.517  1.00 26.69           O  
ANISOU 1713  O   ALA B  16     3402   2487   4253   -764   -793    -12       O  
ATOM   1714  CB  ALA B  16      -6.942 -13.803  49.297  1.00 30.28           C  
ANISOU 1714  CB  ALA B  16     4506   2753   4247  -1100  -1099     22       C  
ATOM   1715  N   ASP B  17      -9.267 -15.073  47.448  1.00 23.05           N  
ANISOU 1715  N   ASP B  17     3274   2902   2581    364   -392   -196       N  
ATOM   1716  CA  ASP B  17     -10.202 -16.143  47.135  1.00 21.33           C  
ANISOU 1716  CA  ASP B  17     2933   2741   2431    377   -227   -128       C  
ATOM   1717  C   ASP B  17     -10.065 -16.576  45.681  1.00 23.70           C  
ANISOU 1717  C   ASP B  17     3112   3010   2884    247   -203   -128       C  
ATOM   1718  O   ASP B  17     -10.122 -17.774  45.380  1.00 25.02           O  
ANISOU 1718  O   ASP B  17     3186   3185   3136    207   -124    -71       O  
ATOM   1719  CB  ASP B  17     -11.629 -15.687  47.432  1.00 23.21           C  
ANISOU 1719  CB  ASP B  17     3206   3023   2590    500   -138   -119       C  
ATOM   1720  CG  ASP B  17     -11.785 -15.139  48.841  1.00 30.03           C  
ANISOU 1720  CG  ASP B  17     4234   3913   3262    673   -151   -128       C  
ATOM   1721  OD1 ASP B  17     -11.472 -15.879  49.796  1.00 24.64           O  
ANISOU 1721  OD1 ASP B  17     3562   3274   2525    728   -125    -69       O  
ATOM   1722  OD2 ASP B  17     -12.198 -13.960  48.994  1.00 29.91           O  
ANISOU 1722  OD2 ASP B  17     4356   3868   3139    766   -191   -195       O  
ATOM   1723  N   TYR B  18      -9.894 -15.620  44.764  1.00 16.87           N  
ANISOU 1723  N   TYR B  18     2263   2100   2045    190   -273   -189       N  
ATOM   1724  CA  TYR B  18      -9.673 -15.986  43.367  1.00 21.72           C  
ANISOU 1724  CA  TYR B  18     2788   2690   2776     90   -252   -190       C  
ATOM   1725  C   TYR B  18      -8.454 -16.884  43.243  1.00 23.22           C  
ANISOU 1725  C   TYR B  18     2924   2869   3029     41   -252   -140       C  
ATOM   1726  O   TYR B  18      -8.520 -17.970  42.658  1.00 28.19           O  
ANISOU 1726  O   TYR B  18     3496   3490   3725     16   -172   -112       O  
ATOM   1727  CB  TYR B  18      -9.476 -14.744  42.498  1.00 21.94           C  
ANISOU 1727  CB  TYR B  18     2843   2679   2815     47   -332   -242       C  
ATOM   1728  CG  TYR B  18     -10.607 -13.741  42.483  1.00 24.26           C  
ANISOU 1728  CG  TYR B  18     3195   2974   3050    105   -332   -286       C  
ATOM   1729  CD1 TYR B  18     -11.921 -14.123  42.727  1.00 21.54           C  
ANISOU 1729  CD1 TYR B  18     2821   2681   2683    171   -233   -260       C  
ATOM   1730  CD2 TYR B  18     -10.357 -12.404  42.186  1.00 25.18           C  
ANISOU 1730  CD2 TYR B  18     3382   3037   3148     95   -429   -333       C  
ATOM   1731  CE1 TYR B  18     -12.961 -13.190  42.692  1.00 20.18           C  
ANISOU 1731  CE1 TYR B  18     2687   2522   2460    246   -217   -275       C  
ATOM   1732  CE2 TYR B  18     -11.389 -11.461  42.154  1.00 26.13           C  
ANISOU 1732  CE2 TYR B  18     3565   3152   3212    168   -419   -369       C  
ATOM   1733  CZ  TYR B  18     -12.679 -11.857  42.402  1.00 22.26           C  
ANISOU 1733  CZ  TYR B  18     3041   2727   2689    252   -307   -338       C  
ATOM   1734  OH  TYR B  18     -13.683 -10.920  42.357  1.00 17.84           O  
ANISOU 1734  OH  TYR B  18     2529   2172   2076    344   -283   -349       O  
ATOM   1735  N   ALA B  19      -7.327 -16.444  43.801  1.00 20.49           N  
ANISOU 1735  N   ALA B  19     2604   2516   2665     32   -350   -121       N  
ATOM   1736  CA  ALA B  19      -6.093 -17.193  43.620  1.00 25.27           C  
ANISOU 1736  CA  ALA B  19     3135   3124   3341     -4   -346    -45       C  
ATOM   1737  C   ALA B  19      -6.150 -18.543  44.325  1.00 21.44           C  
ANISOU 1737  C   ALA B  19     2625   2665   2857     43   -256     10       C  
ATOM   1738  O   ALA B  19      -5.608 -19.529  43.814  1.00 23.22           O  
ANISOU 1738  O   ALA B  19     2789   2879   3152     34   -186     63       O  
ATOM   1739  CB  ALA B  19      -4.910 -16.366  44.124  1.00 25.65           C  
ANISOU 1739  CB  ALA B  19     3195   3164   3387    -41   -498     -8       C  
ATOM   1740  N   ALA B  20      -6.800 -18.606  45.491  1.00 20.66           N  
ANISOU 1740  N   ALA B  20     2581   2597   2672    108   -250      6       N  
ATOM   1741  CA  ALA B  20      -6.944 -19.879  46.195  1.00 21.80           C  
ANISOU 1741  CA  ALA B  20     2694   2767   2821    155   -158     78       C  
ATOM   1742  C   ALA B  20      -7.833 -20.856  45.430  1.00 18.66           C  
ANISOU 1742  C   ALA B  20     2245   2338   2505    133    -41     87       C  
ATOM   1743  O   ALA B  20      -7.558 -22.059  45.412  1.00 19.10           O  
ANISOU 1743  O   ALA B  20     2263   2370   2624    132     26    147       O  
ATOM   1744  CB  ALA B  20      -7.502 -19.644  47.602  1.00 26.35           C  
ANISOU 1744  CB  ALA B  20     3346   3395   3272    253   -166     88       C  
ATOM   1745  N   GLN B  21      -8.920 -20.384  44.811  1.00 23.58           N  
ANISOU 1745  N   GLN B  21     2874   2954   3133    114    -27     36       N  
ATOM   1746  CA  GLN B  21      -9.725 -21.330  44.042  1.00 23.87           C  
ANISOU 1746  CA  GLN B  21     2865   2946   3257     67     42     51       C  
ATOM   1747  C   GLN B  21      -8.956 -21.836  42.826  1.00 24.18           C  
ANISOU 1747  C   GLN B  21     2908   2915   3363     14     42     22       C  
ATOM   1748  O   GLN B  21      -8.987 -23.035  42.513  1.00 19.90           O  
ANISOU 1748  O   GLN B  21     2367   2310   2886     -3     91     50       O  
ATOM   1749  CB  GLN B  21     -11.064 -20.718  43.611  1.00 19.14           C  
ANISOU 1749  CB  GLN B  21     2253   2362   2655     52     42     24       C  
ATOM   1750  CG  GLN B  21     -11.949 -21.755  42.866  1.00 21.94           C  
ANISOU 1750  CG  GLN B  21     2560   2663   3115    -22     74     56       C  
ATOM   1751  CD  GLN B  21     -13.312 -21.220  42.450  1.00 23.72           C  
ANISOU 1751  CD  GLN B  21     2739   2916   3356    -46     63     64       C  
ATOM   1752  OE1 GLN B  21     -13.859 -20.316  43.075  1.00 30.73           O  
ANISOU 1752  OE1 GLN B  21     3619   3881   4177     29     79     83       O  
ATOM   1753  NE2 GLN B  21     -13.861 -21.783  41.381  1.00 27.09           N  
ANISOU 1753  NE2 GLN B  21     3149   3277   3867   -142     30     53       N  
ATOM   1754  N   LEU B  22      -8.251 -20.939  42.134  1.00 21.01           N  
ANISOU 1754  N   LEU B  22     2522   2517   2945     -1    -10    -24       N  
ATOM   1755  CA  LEU B  22      -7.462 -21.354  40.978  1.00 17.67           C  
ANISOU 1755  CA  LEU B  22     2105   2045   2563    -14     13    -30       C  
ATOM   1756  C   LEU B  22      -6.420 -22.384  41.382  1.00 17.96           C  
ANISOU 1756  C   LEU B  22     2127   2068   2630     31     66     47       C  
ATOM   1757  O   LEU B  22      -6.172 -23.349  40.654  1.00 23.39           O  
ANISOU 1757  O   LEU B  22     2847   2688   3350     51    128     53       O  
ATOM   1758  CB  LEU B  22      -6.784 -20.139  40.341  1.00 15.60           C  
ANISOU 1758  CB  LEU B  22     1834   1810   2285    -26    -43    -48       C  
ATOM   1759  CG  LEU B  22      -5.913 -20.468  39.130  1.00 16.64           C  
ANISOU 1759  CG  LEU B  22     1965   1915   2442     -6      4    -26       C  
ATOM   1760  CD1 LEU B  22      -6.758 -21.110  38.023  1.00 17.53           C  
ANISOU 1760  CD1 LEU B  22     2149   1961   2549    -13     44    -96       C  
ATOM   1761  CD2 LEU B  22      -5.256 -19.215  38.602  1.00 22.04           C  
ANISOU 1761  CD2 LEU B  22     2611   2636   3127    -22    -50     -5       C  
ATOM   1762  N   ARG B  23      -5.810 -22.184  42.553  1.00 22.72           N  
ANISOU 1762  N   ARG B  23     2696   2727   3210     57     35    108       N  
ATOM   1763  CA  ARG B  23      -4.745 -23.049  43.053  1.00 23.53           C  
ANISOU 1763  CA  ARG B  23     2764   2836   3340    105     75    205       C  
ATOM   1764  C   ARG B  23      -5.269 -24.435  43.394  1.00 31.92           C  
ANISOU 1764  C   ARG B  23     3848   3844   4435    131    160    234       C  
ATOM   1765  O   ARG B  23      -4.588 -25.439  43.159  1.00 28.38           O  
ANISOU 1765  O   ARG B  23     3404   3350   4030    176    229    290       O  
ATOM   1766  CB  ARG B  23      -4.126 -22.402  44.296  1.00 29.53           C  
ANISOU 1766  CB  ARG B  23     3494   3671   4055    114    -15    258       C  
ATOM   1767  CG  ARG B  23      -2.806 -22.978  44.764  1.00 35.72           C  
ANISOU 1767  CG  ARG B  23     4214   4485   4871    152    -10    381       C  
ATOM   1768  CD  ARG B  23      -2.295 -22.278  46.022  1.00 33.52           C  
ANISOU 1768  CD  ARG B  23     3929   4274   4535    144   -142    423       C  
ATOM   1769  NE  ARG B  23      -2.446 -20.829  45.931  1.00 48.56           N  
ANISOU 1769  NE  ARG B  23     5873   6181   6397     86   -274    350       N  
ATOM   1770  CZ  ARG B  23      -3.184 -20.098  46.764  1.00 50.89           C  
ANISOU 1770  CZ  ARG B  23     6263   6483   6589     95   -353    273       C  
ATOM   1771  NH1 ARG B  23      -3.830 -20.686  47.765  1.00 54.78           N  
ANISOU 1771  NH1 ARG B  23     6803   7002   7008    165   -301    277       N  
ATOM   1772  NH2 ARG B  23      -3.270 -18.781  46.608  1.00 39.82           N  
ANISOU 1772  NH2 ARG B  23     4918   5060   5154     50   -475    205       N  
ATOM   1773  N   GLU B  24      -6.471 -24.501  43.967  1.00 31.86           N  
ANISOU 1773  N   GLU B  24     3851   3840   4414    110    159    215       N  
ATOM   1774  CA  GLU B  24      -7.042 -25.716  44.539  1.00 22.07           C  
ANISOU 1774  CA  GLU B  24     2608   2559   3219    122    224    278       C  
ATOM   1775  C   GLU B  24      -7.899 -26.473  43.537  1.00 23.73           C  
ANISOU 1775  C   GLU B  24     2860   2654   3504     64    245    238       C  
ATOM   1776  O   GLU B  24      -7.776 -27.694  43.403  1.00 27.05           O  
ANISOU 1776  O   GLU B  24     3313   2976   3987     70    291    276       O  
ATOM   1777  CB  GLU B  24      -7.892 -25.369  45.772  1.00 22.95           C  
ANISOU 1777  CB  GLU B  24     2692   2751   3277    146    220    320       C  
ATOM   1778  CG  GLU B  24      -7.098 -24.934  46.994  1.00 41.45           C  
ANISOU 1778  CG  GLU B  24     5032   5187   5531    217    187    368       C  
ATOM   1779  CD  GLU B  24      -7.932 -24.189  48.037  1.00 53.00           C  
ANISOU 1779  CD  GLU B  24     6517   6734   6886    273    172    373       C  
ATOM   1780  OE1 GLU B  24      -9.174 -24.103  47.891  1.00 54.60           O  
ANISOU 1780  OE1 GLU B  24     6705   6939   7102    266    213    372       O  
ATOM   1781  OE2 GLU B  24      -7.331 -23.681  49.009  1.00 55.63           O  
ANISOU 1781  OE2 GLU B  24     6889   7132   7116    334    114    387       O  
ATOM   1782  N   VAL B  25      -8.789 -25.767  42.851  1.00 27.51           N  
ANISOU 1782  N   VAL B  25     3346   3133   3974      5    198    165       N  
ATOM   1783  CA  VAL B  25      -9.682 -26.403  41.893  1.00 18.37           C  
ANISOU 1783  CA  VAL B  25     2232   1866   2883    -70    177    127       C  
ATOM   1784  C   VAL B  25      -9.049 -26.470  40.518  1.00 20.15           C  
ANISOU 1784  C   VAL B  25     2553   2012   3090    -64    164     39       C  
ATOM   1785  O   VAL B  25      -9.295 -27.419  39.762  1.00 19.14           O  
ANISOU 1785  O   VAL B  25     2519   1750   3002    -92    152      7       O  
ATOM   1786  CB  VAL B  25     -11.015 -25.649  41.846  1.00 22.15           C  
ANISOU 1786  CB  VAL B  25     2656   2396   3363   -129    130    118       C  
ATOM   1787  CG1 VAL B  25     -12.002 -26.365  40.928  1.00 25.87           C  
ANISOU 1787  CG1 VAL B  25     3157   2753   3920   -232     74    103       C  
ATOM   1788  CG2 VAL B  25     -11.569 -25.463  43.266  1.00 18.46           C  
ANISOU 1788  CG2 VAL B  25     2101   2030   2881    -85    172    222       C  
ATOM   1789  N   GLY B  26      -8.225 -25.491  40.187  1.00 20.17           N  
ANISOU 1789  N   GLY B  26     2547   2089   3030    -22    163      7       N  
ATOM   1790  CA  GLY B  26      -7.616 -25.430  38.891  1.00 23.88           C  
ANISOU 1790  CA  GLY B  26     3095   2512   3467     10    172    -51       C  
ATOM   1791  C   GLY B  26      -8.388 -24.586  37.922  1.00 23.25           C  
ANISOU 1791  C   GLY B  26     3038   2439   3355    -46    107   -135       C  
ATOM   1792  O   GLY B  26      -7.960 -24.452  36.773  1.00 19.98           O  
ANISOU 1792  O   GLY B  26     2698   1997   2897    -10    116   -182       O  
ATOM   1793  N   THR B  27      -9.521 -24.031  38.354  1.00 17.08           N  
ANISOU 1793  N   THR B  27     2195   1703   2590   -116     53   -140       N  
ATOM   1794  CA  THR B  27     -10.371 -23.157  37.558  1.00 24.50           C  
ANISOU 1794  CA  THR B  27     3136   2666   3508   -168    -11   -200       C  
ATOM   1795  C   THR B  27     -11.091 -22.209  38.510  1.00 26.48           C  
ANISOU 1795  C   THR B  27     3289   3017   3755   -180    -28   -164       C  
ATOM   1796  O   THR B  27     -11.482 -22.614  39.608  1.00 22.25           O  
ANISOU 1796  O   THR B  27     2703   2504   3248   -173     -1    -96       O  
ATOM   1797  CB  THR B  27     -11.392 -23.959  36.745  1.00 21.47           C  
ANISOU 1797  CB  THR B  27     2817   2178   3161   -246    -73   -237       C  
ATOM   1798  OG1 THR B  27     -10.717 -24.984  36.019  1.00 26.23           O  
ANISOU 1798  OG1 THR B  27     3556   2662   3749   -209    -55   -276       O  
ATOM   1799  CG2 THR B  27     -12.117 -23.066  35.740  1.00 17.48           C  
ANISOU 1799  CG2 THR B  27     2319   1700   2621   -291   -146   -295       C  
ATOM   1800  N   VAL B  28     -11.248 -20.948  38.101  1.00 22.47           N  
ANISOU 1800  N   VAL B  28     2768   2567   3204   -179    -63   -203       N  
ATOM   1801  CA  VAL B  28     -12.047 -19.977  38.842  1.00 25.28           C  
ANISOU 1801  CA  VAL B  28     3067   3001   3538   -165    -76   -181       C  
ATOM   1802  C   VAL B  28     -12.852 -19.164  37.832  1.00 27.93           C  
ANISOU 1802  C   VAL B  28     3399   3350   3864   -200   -125   -222       C  
ATOM   1803  O   VAL B  28     -12.413 -18.930  36.702  1.00 24.45           O  
ANISOU 1803  O   VAL B  28     3004   2881   3403   -216   -151   -276       O  
ATOM   1804  CB  VAL B  28     -11.179 -19.064  39.757  1.00 25.36           C  
ANISOU 1804  CB  VAL B  28     3083   3064   3490   -101    -79   -175       C  
ATOM   1805  CG1 VAL B  28     -10.276 -18.168  38.952  1.00 21.33           C  
ANISOU 1805  CG1 VAL B  28     2598   2548   2959   -106   -119   -216       C  
ATOM   1806  CG2 VAL B  28     -12.048 -18.220  40.681  1.00 22.66           C  
ANISOU 1806  CG2 VAL B  28     2727   2783   3099    -50    -81   -157       C  
HETATM 1807  N   MSE B  29     -14.067 -18.787  38.218  1.00 21.31           N  
ANISOU 1807  N   MSE B  29     2499   2561   3037   -201   -129   -179       N  
HETATM 1808  CA  MSE B  29     -14.877 -17.947  37.342  1.00 26.01           C  
ANISOU 1808  CA  MSE B  29     3076   3182   3624   -224   -175   -199       C  
HETATM 1809  C   MSE B  29     -15.103 -16.623  38.036  1.00 20.87           C  
ANISOU 1809  C   MSE B  29     2415   2599   2916   -138   -155   -189       C  
HETATM 1810  O   MSE B  29     -15.677 -16.586  39.136  1.00 19.56           O  
ANISOU 1810  O   MSE B  29     2212   2482   2737    -72   -106   -123       O  
HETATM 1811  CB  MSE B  29     -16.218 -18.604  36.983  1.00 23.21           C  
ANISOU 1811  CB  MSE B  29     2649   2823   3345   -299   -210   -137       C  
HETATM 1812  CG  MSE B  29     -17.081 -17.736  36.055  1.00 27.22           C  
ANISOU 1812  CG  MSE B  29     3125   3369   3846   -323   -267   -141       C  
HETATM 1813 SE   MSE B  29     -18.552 -18.670  35.139  1.00 32.07          SE  
ANISOU 1813 SE   MSE B  29     3664   3953   4570   -470   -384    -69      SE  
HETATM 1814  CE  MSE B  29     -19.450 -19.392  36.713  1.00 22.50           C  
ANISOU 1814  CE  MSE B  29     2294   2793   3461   -457   -309    119       C  
ATOM   1815  N   LEU B  30     -14.622 -15.541  37.403  1.00 17.91           N  
ANISOU 1815  N   LEU B  30     2086   2219   2499   -126   -191   -248       N  
ATOM   1816  CA  LEU B  30     -14.763 -14.205  37.989  1.00 15.19           C  
ANISOU 1816  CA  LEU B  30     1771   1903   2096    -43   -194   -255       C  
ATOM   1817  C   LEU B  30     -16.062 -13.565  37.518  1.00 16.13           C  
ANISOU 1817  C   LEU B  30     1840   2068   2220    -23   -192   -221       C  
ATOM   1818  O   LEU B  30     -16.394 -13.646  36.329  1.00 21.22           O  
ANISOU 1818  O   LEU B  30     2454   2709   2898    -92   -231   -230       O  
ATOM   1819  CB  LEU B  30     -13.590 -13.315  37.611  1.00 14.76           C  
ANISOU 1819  CB  LEU B  30     1784   1807   2018    -50   -246   -310       C  
ATOM   1820  CG  LEU B  30     -12.209 -13.933  37.831  1.00 20.74           C  
ANISOU 1820  CG  LEU B  30     2559   2531   2791    -79   -254   -313       C  
ATOM   1821  CD1 LEU B  30     -11.106 -13.050  37.266  1.00 27.90           C  
ANISOU 1821  CD1 LEU B  30     3489   3406   3705   -102   -310   -322       C  
ATOM   1822  CD2 LEU B  30     -11.981 -14.202  39.302  1.00 18.15           C  
ANISOU 1822  CD2 LEU B  30     2257   2212   2429    -26   -242   -293       C  
ATOM   1823  N   PRO B  31     -16.802 -12.925  38.410  1.00 17.69           N  
ANISOU 1823  N   PRO B  31     2037   2311   2373     85   -147   -176       N  
ATOM   1824  CA  PRO B  31     -18.044 -12.266  38.006  1.00 23.63           C  
ANISOU 1824  CA  PRO B  31     2727   3118   3133    127   -131   -118       C  
ATOM   1825  C   PRO B  31     -17.774 -11.005  37.203  1.00 24.95           C  
ANISOU 1825  C   PRO B  31     2958   3252   3270    137   -183   -181       C  
ATOM   1826  O   PRO B  31     -16.698 -10.404  37.264  1.00 22.42           O  
ANISOU 1826  O   PRO B  31     2738   2866   2915    137   -226   -256       O  
ATOM   1827  CB  PRO B  31     -18.703 -11.917  39.339  1.00 19.41           C  
ANISOU 1827  CB  PRO B  31     2203   2638   2533    287    -42    -47       C  
ATOM   1828  CG  PRO B  31     -17.536 -11.648  40.218  1.00 25.58           C  
ANISOU 1828  CG  PRO B  31     3129   3358   3231    336    -62   -133       C  
ATOM   1829  CD  PRO B  31     -16.505 -12.692  39.831  1.00 20.41           C  
ANISOU 1829  CD  PRO B  31     2456   2660   2640    197   -108   -174       C  
ATOM   1830  N   ALA B  32     -18.789 -10.607  36.445  1.00 16.84           N  
ANISOU 1830  N   ALA B  32     1857   2272   2269    138   -187   -128       N  
ATOM   1831  CA  ALA B  32     -18.779  -9.287  35.833  1.00 25.86           C  
ANISOU 1831  CA  ALA B  32     3052   3393   3381    180   -217   -159       C  
ATOM   1832  C   ALA B  32     -18.969  -8.241  36.928  1.00 28.78           C  
ANISOU 1832  C   ALA B  32     3519   3746   3670    346   -169   -159       C  
ATOM   1833  O   ALA B  32     -19.783  -8.433  37.832  1.00 29.62           O  
ANISOU 1833  O   ALA B  32     3593   3913   3747    456    -85    -82       O  
ATOM   1834  CB  ALA B  32     -19.895  -9.193  34.787  1.00 17.86           C  
ANISOU 1834  CB  ALA B  32     1926   2446   2413    148   -234    -86       C  
ATOM   1835  N   TYR B  33     -18.198  -7.147  36.891  1.00 24.65           N  
ANISOU 1835  N   TYR B  33     3128   3133   3106    372   -223   -235       N  
ATOM   1836  CA  TYR B  33     -17.176  -6.842  35.907  1.00 23.32           C  
ANISOU 1836  CA  TYR B  33     2984   2900   2978    258   -308   -290       C  
ATOM   1837  C   TYR B  33     -15.852  -6.573  36.632  1.00 27.86           C  
ANISOU 1837  C   TYR B  33     3679   3377   3530    241   -373   -356       C  
ATOM   1838  O   TYR B  33     -15.293  -5.473  36.523  1.00 16.88           O  
ANISOU 1838  O   TYR B  33     2383   1896   2136    245   -446   -385       O  
ATOM   1839  CB  TYR B  33     -17.588  -5.619  35.065  1.00 17.03           C  
ANISOU 1839  CB  TYR B  33     2201   2084   2184    292   -331   -275       C  
ATOM   1840  CG  TYR B  33     -18.829  -5.839  34.210  1.00 23.50           C  
ANISOU 1840  CG  TYR B  33     2889   3008   3034    291   -295   -195       C  
ATOM   1841  CD1 TYR B  33     -18.716  -6.203  32.872  1.00 16.84           C  
ANISOU 1841  CD1 TYR B  33     1972   2193   2231    178   -339   -189       C  
ATOM   1842  CD2 TYR B  33     -20.111  -5.709  34.747  1.00 27.41           C  
ANISOU 1842  CD2 TYR B  33     3329   3574   3510    410   -220   -112       C  
ATOM   1843  CE1 TYR B  33     -19.838  -6.415  32.091  1.00 19.52           C  
ANISOU 1843  CE1 TYR B  33     2200   2620   2594    161   -342   -116       C  
ATOM   1844  CE2 TYR B  33     -21.254  -5.937  33.964  1.00 18.64           C  
ANISOU 1844  CE2 TYR B  33     2069   2566   2447    390   -209    -11       C  
ATOM   1845  CZ  TYR B  33     -21.100  -6.282  32.636  1.00 23.06           C  
ANISOU 1845  CZ  TYR B  33     2571   3141   3049    254   -286    -22       C  
ATOM   1846  OH  TYR B  33     -22.203  -6.496  31.835  1.00 27.74           O  
ANISOU 1846  OH  TYR B  33     3029   3827   3684    218   -311     76       O  
ATOM   1847  N   VAL B  34     -15.367  -7.582  37.369  1.00 16.32           N  
ANISOU 1847  N   VAL B  34     2209   1929   2063    215   -359   -365       N  
ATOM   1848  CA  VAL B  34     -14.179  -7.407  38.199  1.00 18.24           C  
ANISOU 1848  CA  VAL B  34     2556   2093   2282    202   -433   -409       C  
ATOM   1849  C   VAL B  34     -12.933  -7.228  37.344  1.00 17.55           C  
ANISOU 1849  C   VAL B  34     2442   1956   2271     78   -512   -407       C  
ATOM   1850  O   VAL B  34     -12.152  -6.299  37.556  1.00 20.90           O  
ANISOU 1850  O   VAL B  34     2951   2287   2704     58   -615   -421       O  
ATOM   1851  CB  VAL B  34     -14.008  -8.591  39.159  1.00 17.57           C  
ANISOU 1851  CB  VAL B  34     2451   2051   2174    211   -389   -399       C  
ATOM   1852  CG1 VAL B  34     -12.700  -8.469  39.873  1.00 24.64           C  
ANISOU 1852  CG1 VAL B  34     3432   2874   3055    176   -485   -431       C  
ATOM   1853  CG2 VAL B  34     -15.123  -8.596  40.164  1.00 20.91           C  
ANISOU 1853  CG2 VAL B  34     2910   2523   2512    360   -306   -375       C  
ATOM   1854  N   ALA B  35     -12.700  -8.145  36.402  1.00 15.34           N  
ANISOU 1854  N   ALA B  35     2051   1731   2046      1   -469   -377       N  
ATOM   1855  CA  ALA B  35     -11.417  -8.145  35.716  1.00 22.89           C  
ANISOU 1855  CA  ALA B  35     2973   2660   3064    -84   -512   -345       C  
ATOM   1856  C   ALA B  35     -11.386  -7.118  34.601  1.00 24.73           C  
ANISOU 1856  C   ALA B  35     3195   2872   3329   -104   -542   -317       C  
ATOM   1857  O   ALA B  35     -10.343  -6.501  34.352  1.00 20.58           O  
ANISOU 1857  O   ALA B  35     2664   2295   2859   -155   -608   -268       O  
ATOM   1858  CB  ALA B  35     -11.113  -9.538  35.167  1.00 21.41           C  
ANISOU 1858  CB  ALA B  35     2708   2530   2898   -122   -442   -325       C  
ATOM   1859  N   PHE B  36     -12.515  -6.942  33.919  1.00 15.24           N  
ANISOU 1859  N   PHE B  36     1973   1714   2103    -69   -499   -324       N  
ATOM   1860  CA  PHE B  36     -12.651  -5.994  32.826  1.00 20.86           C  
ANISOU 1860  CA  PHE B  36     2673   2419   2835    -73   -517   -290       C  
ATOM   1861  C   PHE B  36     -13.964  -5.262  33.024  1.00 24.89           C  
ANISOU 1861  C   PHE B  36     3218   2933   3307      8   -506   -307       C  
ATOM   1862  O   PHE B  36     -14.993  -5.889  33.310  1.00 25.92           O  
ANISOU 1862  O   PHE B  36     3314   3129   3404     49   -451   -315       O  
ATOM   1863  CB  PHE B  36     -12.656  -6.693  31.460  1.00 20.38           C  
ANISOU 1863  CB  PHE B  36     2540   2432   2772   -104   -467   -262       C  
ATOM   1864  CG  PHE B  36     -11.371  -7.373  31.111  1.00 20.01           C  
ANISOU 1864  CG  PHE B  36     2463   2390   2751   -144   -448   -224       C  
ATOM   1865  CD1 PHE B  36     -10.404  -6.713  30.366  1.00 23.92           C  
ANISOU 1865  CD1 PHE B  36     2928   2872   3289   -162   -460   -139       C  
ATOM   1866  CD2 PHE B  36     -11.147  -8.687  31.490  1.00 21.34           C  
ANISOU 1866  CD2 PHE B  36     2624   2580   2905   -151   -407   -251       C  
ATOM   1867  CE1 PHE B  36      -9.212  -7.347  30.028  1.00 29.05           C  
ANISOU 1867  CE1 PHE B  36     3532   3544   3963   -172   -419    -70       C  
ATOM   1868  CE2 PHE B  36      -9.972  -9.322  31.172  1.00 28.02           C  
ANISOU 1868  CE2 PHE B  36     3444   3432   3768   -160   -371   -202       C  
ATOM   1869  CZ  PHE B  36      -8.999  -8.654  30.435  1.00 31.96           C  
ANISOU 1869  CZ  PHE B  36     3904   3934   4306   -163   -371   -106       C  
ATOM   1870  N   ASP B  37     -13.935  -3.945  32.880  1.00 16.39           N  
ANISOU 1870  N   ASP B  37     2200   1784   2243     34   -556   -293       N  
ATOM   1871  CA  ASP B  37     -15.156  -3.196  33.134  1.00 16.95           C  
ANISOU 1871  CA  ASP B  37     2316   1854   2271    142   -533   -299       C  
ATOM   1872  C   ASP B  37     -16.107  -3.307  31.953  1.00 16.84           C  
ANISOU 1872  C   ASP B  37     2199   1939   2258    147   -484   -250       C  
ATOM   1873  O   ASP B  37     -15.703  -3.582  30.827  1.00 17.24           O  
ANISOU 1873  O   ASP B  37     2188   2029   2334     76   -491   -221       O  
ATOM   1874  CB  ASP B  37     -14.834  -1.724  33.404  1.00 21.59           C  
ANISOU 1874  CB  ASP B  37     3031   2303   2868    180   -612   -305       C  
ATOM   1875  CG  ASP B  37     -13.953  -1.559  34.602  1.00 25.36           C  
ANISOU 1875  CG  ASP B  37     3635   2667   3334    168   -700   -358       C  
ATOM   1876  OD1 ASP B  37     -14.046  -2.422  35.499  1.00 27.49           O  
ANISOU 1876  OD1 ASP B  37     3913   2979   3551    197   -665   -396       O  
ATOM   1877  OD2 ASP B  37     -13.166  -0.590  34.644  1.00 23.95           O  
ANISOU 1877  OD2 ASP B  37     3544   2354   3203    123   -816   -352       O  
ATOM   1878  N   ALA B  38     -17.390  -3.064  32.222  1.00 17.34           N  
ANISOU 1878  N   ALA B  38     2250   2050   2289    247   -436   -227       N  
ATOM   1879  CA  ALA B  38     -18.397  -3.179  31.175  1.00 23.77           C  
ANISOU 1879  CA  ALA B  38     2955   2968   3110    246   -413   -164       C  
ATOM   1880  C   ALA B  38     -18.054  -2.324  29.948  1.00 17.60           C  
ANISOU 1880  C   ALA B  38     2173   2165   2349    217   -452   -131       C  
ATOM   1881  O   ALA B  38     -18.153  -2.790  28.806  1.00 18.79           O  
ANISOU 1881  O   ALA B  38     2251   2391   2498    156   -464   -104       O  
ATOM   1882  CB  ALA B  38     -19.774  -2.815  31.739  1.00 20.26           C  
ANISOU 1882  CB  ALA B  38     2483   2575   2641    378   -351   -106       C  
ATOM   1883  N   HIS B  39     -17.651  -1.071  30.147  1.00 18.23           N  
ANISOU 1883  N   HIS B  39     2348   2135   2443    264   -482   -129       N  
ATOM   1884  CA  HIS B  39     -17.360  -0.263  28.957  1.00 18.64           C  
ANISOU 1884  CA  HIS B  39     2384   2173   2526    238   -511    -71       C  
ATOM   1885  C   HIS B  39     -16.144  -0.807  28.215  1.00 22.47           C  
ANISOU 1885  C   HIS B  39     2831   2668   3037    127   -533    -61       C  
ATOM   1886  O   HIS B  39     -16.045  -0.680  26.983  1.00 18.68           O  
ANISOU 1886  O   HIS B  39     2300   2243   2554    107   -529     -1       O  
ATOM   1887  CB  HIS B  39     -17.146   1.202  29.327  1.00 19.24           C  
ANISOU 1887  CB  HIS B  39     2577   2102   2630    300   -553    -60       C  
ATOM   1888  CG  HIS B  39     -15.849   1.469  30.031  1.00 23.21           C  
ANISOU 1888  CG  HIS B  39     3178   2464   3178    234   -633    -99       C  
ATOM   1889  ND1 HIS B  39     -15.691   1.304  31.390  1.00 24.23           N  
ANISOU 1889  ND1 HIS B  39     3415   2518   3273    267   -659   -179       N  
ATOM   1890  CD2 HIS B  39     -14.652   1.897  29.564  1.00 23.54           C  
ANISOU 1890  CD2 HIS B  39     3215   2429   3299    135   -703    -47       C  
ATOM   1891  CE1 HIS B  39     -14.454   1.611  31.731  1.00 23.44           C  
ANISOU 1891  CE1 HIS B  39     3379   2296   3231    177   -762   -186       C  
ATOM   1892  NE2 HIS B  39     -13.802   1.974  30.640  1.00 28.73           N  
ANISOU 1892  NE2 HIS B  39     3970   2965   3983     92   -788    -96       N  
ATOM   1893  N   GLU B  40     -15.234  -1.452  28.942  1.00 21.93           N  
ANISOU 1893  N   GLU B  40     2787   2561   2985     73   -547   -105       N  
ATOM   1894  CA  GLU B  40     -14.075  -2.050  28.292  1.00 26.99           C  
ANISOU 1894  CA  GLU B  40     3382   3225   3648     -5   -543    -73       C  
ATOM   1895  C   GLU B  40     -14.499  -3.206  27.395  1.00 20.80           C  
ANISOU 1895  C   GLU B  40     2541   2562   2801    -14   -495    -84       C  
ATOM   1896  O   GLU B  40     -14.101  -3.277  26.226  1.00 19.22           O  
ANISOU 1896  O   GLU B  40     2315   2410   2578    -20   -477    -32       O  
ATOM   1897  CB  GLU B  40     -13.064  -2.498  29.347  1.00 22.74           C  
ANISOU 1897  CB  GLU B  40     2873   2623   3144    -52   -572   -105       C  
ATOM   1898  CG  GLU B  40     -12.475  -1.329  30.159  1.00 29.91           C  
ANISOU 1898  CG  GLU B  40     3864   3385   4114    -65   -665    -94       C  
ATOM   1899  CD  GLU B  40     -11.398  -1.761  31.151  1.00 29.83           C  
ANISOU 1899  CD  GLU B  40     3878   3317   4139   -127   -722   -110       C  
ATOM   1900  OE1 GLU B  40     -11.658  -2.678  31.967  1.00 29.07           O  
ANISOU 1900  OE1 GLU B  40     3798   3258   3990   -105   -691   -182       O  
ATOM   1901  OE2 GLU B  40     -10.288  -1.176  31.114  1.00 26.79           O  
ANISOU 1901  OE2 GLU B  40     3483   2852   3844   -201   -805    -31       O  
ATOM   1902  N   LEU B  41     -15.325  -4.114  27.923  1.00 25.38           N  
ANISOU 1902  N   LEU B  41     3111   3186   3347    -10   -481   -144       N  
ATOM   1903  CA  LEU B  41     -15.767  -5.250  27.121  1.00 23.05           C  
ANISOU 1903  CA  LEU B  41     2786   2974   2999    -37   -474   -162       C  
ATOM   1904  C   LEU B  41     -16.565  -4.773  25.927  1.00 24.47           C  
ANISOU 1904  C   LEU B  41     2942   3218   3140    -16   -496   -117       C  
ATOM   1905  O   LEU B  41     -16.465  -5.344  24.834  1.00 20.28           O  
ANISOU 1905  O   LEU B  41     2425   2735   2545    -30   -508   -118       O  
ATOM   1906  CB  LEU B  41     -16.592  -6.216  27.963  1.00 18.52           C  
ANISOU 1906  CB  LEU B  41     2189   2421   2426    -52   -473   -204       C  
ATOM   1907  CG  LEU B  41     -15.731  -6.760  29.088  1.00 20.16           C  
ANISOU 1907  CG  LEU B  41     2427   2574   2660    -67   -449   -243       C  
ATOM   1908  CD1 LEU B  41     -16.446  -7.847  29.835  1.00 24.57           C  
ANISOU 1908  CD1 LEU B  41     2956   3158   3223    -84   -437   -266       C  
ATOM   1909  CD2 LEU B  41     -14.433  -7.253  28.487  1.00 18.11           C  
ANISOU 1909  CD2 LEU B  41     2190   2299   2391    -98   -434   -244       C  
ATOM   1910  N   ALA B  42     -17.334  -3.697  26.105  1.00 18.17           N  
ANISOU 1910  N   ALA B  42     2122   2416   2365     34   -504    -75       N  
ATOM   1911  CA  ALA B  42     -18.095  -3.182  24.980  1.00 22.97           C  
ANISOU 1911  CA  ALA B  42     2697   3092   2940     60   -528    -16       C  
ATOM   1912  C   ALA B  42     -17.153  -2.712  23.885  1.00 22.56           C  
ANISOU 1912  C   ALA B  42     2672   3038   2861     65   -520     29       C  
ATOM   1913  O   ALA B  42     -17.408  -2.937  22.693  1.00 21.54           O  
ANISOU 1913  O   ALA B  42     2543   2985   2658     70   -540     54       O  
ATOM   1914  CB  ALA B  42     -19.024  -2.058  25.443  1.00 22.94           C  
ANISOU 1914  CB  ALA B  42     2667   3077   2970    137   -520     36       C  
ATOM   1915  N   ARG B  43     -16.035  -2.093  24.280  1.00 22.34           N  
ANISOU 1915  N   ARG B  43     2669   2925   2893     63   -497     54       N  
ATOM   1916  CA  ARG B  43     -15.028  -1.664  23.323  1.00 26.92           C  
ANISOU 1916  CA  ARG B  43     3247   3509   3472     70   -473    138       C  
ATOM   1917  C   ARG B  43     -14.322  -2.854  22.697  1.00 28.30           C  
ANISOU 1917  C   ARG B  43     3439   3742   3572     63   -435    121       C  
ATOM   1918  O   ARG B  43     -14.119  -2.887  21.478  1.00 26.64           O  
ANISOU 1918  O   ARG B  43     3240   3599   3283    107   -408    177       O  
ATOM   1919  CB  ARG B  43     -14.019  -0.749  24.002  1.00 36.59           C  
ANISOU 1919  CB  ARG B  43     4476   4618   4808     46   -484    193       C  
ATOM   1920  CG  ARG B  43     -12.967  -0.169  23.072  1.00 45.22           C  
ANISOU 1920  CG  ARG B  43     5531   5713   5936     47   -458    331       C  
ATOM   1921  CD  ARG B  43     -11.951   0.627  23.884  1.00 49.85           C  
ANISOU 1921  CD  ARG B  43     6113   6167   6662    -13   -508    393       C  
ATOM   1922  NE  ARG B  43     -10.834   1.111  23.082  1.00 56.76           N  
ANISOU 1922  NE  ARG B  43     6916   7047   7605    -27   -483    567       N  
ATOM   1923  CZ  ARG B  43      -9.674   1.505  23.597  1.00 62.03           C  
ANISOU 1923  CZ  ARG B  43     7541   7623   8404   -103   -531    664       C  
ATOM   1924  NH1 ARG B  43      -9.484   1.460  24.909  1.00 60.62           N  
ANISOU 1924  NH1 ARG B  43     7414   7336   8284   -168   -618    577       N  
ATOM   1925  NH2 ARG B  43      -8.703   1.937  22.802  1.00 62.72           N  
ANISOU 1925  NH2 ARG B  43     7531   7733   8566   -112   -498    863       N  
ATOM   1926  N   ILE B  44     -13.960  -3.851  23.508  1.00 24.84           N  
ANISOU 1926  N   ILE B  44     3017   3277   3143     27   -426     46       N  
ATOM   1927  CA  ILE B  44     -13.367  -5.064  22.953  1.00 26.76           C  
ANISOU 1927  CA  ILE B  44     3301   3561   3305     41   -385     20       C  
ATOM   1928  C   ILE B  44     -14.339  -5.745  22.004  1.00 31.08           C  
ANISOU 1928  C   ILE B  44     3905   4175   3730     59   -424    -35       C  
ATOM   1929  O   ILE B  44     -13.958  -6.165  20.903  1.00 31.74           O  
ANISOU 1929  O   ILE B  44     4055   4303   3701    117   -397    -21       O  
ATOM   1930  CB  ILE B  44     -12.919  -6.015  24.078  1.00 23.71           C  
ANISOU 1930  CB  ILE B  44     2923   3127   2959      1   -374    -47       C  
ATOM   1931  CG1 ILE B  44     -11.666  -5.461  24.762  1.00 19.16           C  
ANISOU 1931  CG1 ILE B  44     2301   2494   2486    -17   -350     29       C  
ATOM   1932  CG2 ILE B  44     -12.709  -7.433  23.524  1.00 20.04           C  
ANISOU 1932  CG2 ILE B  44     2531   2690   2395     25   -345   -104       C  
ATOM   1933  CD1 ILE B  44     -11.278  -6.198  26.028  1.00 21.82           C  
ANISOU 1933  CD1 ILE B  44     2640   2783   2870    -57   -355    -28       C  
ATOM   1934  N   ASP B  45     -15.612  -5.848  22.405  1.00 28.44           N  
ANISOU 1934  N   ASP B  45     3549   3847   3411     15   -496    -87       N  
ATOM   1935  CA  ASP B  45     -16.622  -6.461  21.549  1.00 25.58           C  
ANISOU 1935  CA  ASP B  45     3225   3540   2955      1   -577   -124       C  
ATOM   1936  C   ASP B  45     -16.740  -5.719  20.219  1.00 30.61           C  
ANISOU 1936  C   ASP B  45     3883   4243   3504     62   -588    -56       C  
ATOM   1937  O   ASP B  45     -16.880  -6.338  19.157  1.00 25.33           O  
ANISOU 1937  O   ASP B  45     3309   3613   2702     86   -633    -86       O  
ATOM   1938  CB  ASP B  45     -17.968  -6.483  22.275  1.00 32.31           C  
ANISOU 1938  CB  ASP B  45     3998   4402   3875    -56   -646   -132       C  
ATOM   1939  CG  ASP B  45     -18.908  -7.554  21.739  1.00 44.23           C  
ANISOU 1939  CG  ASP B  45     5538   5939   5327   -120   -761   -174       C  
ATOM   1940  OD1 ASP B  45     -18.514  -8.303  20.820  1.00 45.35           O  
ANISOU 1940  OD1 ASP B  45     5801   6074   5356   -113   -797   -228       O  
ATOM   1941  OD2 ASP B  45     -20.044  -7.655  22.248  1.00 46.86           O  
ANISOU 1941  OD2 ASP B  45     5779   6296   5729   -173   -822   -144       O  
ATOM   1942  N   ALA B  46     -16.657  -4.392  20.256  1.00 28.92           N  
ANISOU 1942  N   ALA B  46     3601   4032   3356     96   -551     36       N  
ATOM   1943  CA  ALA B  46     -16.753  -3.626  19.026  1.00 25.18           C  
ANISOU 1943  CA  ALA B  46     3136   3624   2809    160   -552    121       C  
ATOM   1944  C   ALA B  46     -15.500  -3.784  18.163  1.00 34.35           C  
ANISOU 1944  C   ALA B  46     4361   4807   3883    236   -467    171       C  
ATOM   1945  O   ALA B  46     -15.599  -3.930  16.940  1.00 40.99           O  
ANISOU 1945  O   ALA B  46     5275   5720   4578    305   -477    192       O  
ATOM   1946  CB  ALA B  46     -17.015  -2.164  19.368  1.00 21.76           C  
ANISOU 1946  CB  ALA B  46     2618   3167   2484    177   -537    213       C  
ATOM   1947  N   LEU B  47     -14.312  -3.763  18.775  1.00 28.93           N  
ANISOU 1947  N   LEU B  47     3646   4066   3278    236   -384    206       N  
ATOM   1948  CA  LEU B  47     -13.076  -3.906  18.009  1.00 28.27           C  
ANISOU 1948  CA  LEU B  47     3593   4019   3131    325   -280    297       C  
ATOM   1949  C   LEU B  47     -12.983  -5.271  17.330  1.00 27.96           C  
ANISOU 1949  C   LEU B  47     3696   4015   2913    391   -268    207       C  
ATOM   1950  O   LEU B  47     -12.679  -5.355  16.134  1.00 30.50           O  
ANISOU 1950  O   LEU B  47     4100   4407   3081    510   -217    260       O  
ATOM   1951  CB  LEU B  47     -11.867  -3.679  18.912  1.00 26.03           C  
ANISOU 1951  CB  LEU B  47     3225   3670   2993    293   -215    370       C  
ATOM   1952  CG  LEU B  47     -11.665  -2.199  19.252  1.00 31.84           C  
ANISOU 1952  CG  LEU B  47     3858   4354   3885    251   -230    493       C  
ATOM   1953  CD1 LEU B  47     -10.890  -2.049  20.543  1.00 30.01           C  
ANISOU 1953  CD1 LEU B  47     3568   4022   3813    167   -247    503       C  
ATOM   1954  CD2 LEU B  47     -10.950  -1.488  18.116  1.00 32.10           C  
ANISOU 1954  CD2 LEU B  47     3847   4449   3898    335   -151    683       C  
ATOM   1955  N   GLN B  48     -13.251  -6.350  18.077  1.00 27.63           N  
ANISOU 1955  N   GLN B  48     3702   3917   2879    327   -316     73       N  
ATOM   1956  CA  GLN B  48     -13.115  -7.695  17.522  1.00 29.62           C  
ANISOU 1956  CA  GLN B  48     4119   4165   2971    387   -318    -23       C  
ATOM   1957  C   GLN B  48     -14.047  -7.926  16.336  1.00 35.30           C  
ANISOU 1957  C   GLN B  48     4972   4929   3513    422   -422    -80       C  
ATOM   1958  O   GLN B  48     -13.713  -8.707  15.436  1.00 34.06           O  
ANISOU 1958  O   GLN B  48     4994   4780   3167    532   -406   -124       O  
ATOM   1959  CB  GLN B  48     -13.364  -8.747  18.600  1.00 26.49           C  
ANISOU 1959  CB  GLN B  48     3739   3685   2643    291   -370   -146       C  
ATOM   1960  CG  GLN B  48     -14.817  -8.841  19.092  1.00 32.37           C  
ANISOU 1960  CG  GLN B  48     4446   4408   3446    162   -518   -224       C  
ATOM   1961  CD  GLN B  48     -15.712  -9.834  18.320  1.00 35.69           C  
ANISOU 1961  CD  GLN B  48     5015   4815   3731    137   -658   -327       C  
ATOM   1962  OE1 GLN B  48     -15.260 -10.631  17.468  1.00 27.81           O  
ANISOU 1962  OE1 GLN B  48     4200   3798   2569    224   -654   -382       O  
ATOM   1963  NE2 GLN B  48     -17.004  -9.782  18.628  1.00 36.20           N  
ANISOU 1963  NE2 GLN B  48     5006   4883   3864     22   -792   -344       N  
ATOM   1964  N   ALA B  49     -15.202  -7.249  16.298  1.00 35.08           N  
ANISOU 1964  N   ALA B  49     4871   4929   3529    343   -534    -74       N  
ATOM   1965  CA  ALA B  49     -16.142  -7.458  15.199  1.00 32.20           C  
ANISOU 1965  CA  ALA B  49     4620   4611   3004    357   -666   -117       C  
ATOM   1966  C   ALA B  49     -15.592  -6.957  13.866  1.00 40.04           C  
ANISOU 1966  C   ALA B  49     5699   5689   3823    518   -591    -28       C  
ATOM   1967  O   ALA B  49     -16.066  -7.388  12.805  1.00 37.57           O  
ANISOU 1967  O   ALA B  49     5554   5409   3313    572   -689    -82       O  
ATOM   1968  CB  ALA B  49     -17.477  -6.787  15.521  1.00 29.26           C  
ANISOU 1968  CB  ALA B  49     4112   4267   2740    246   -788    -92       C  
ATOM   1969  N   ARG B  50     -14.594  -6.074  13.904  1.00 37.54           N  
ANISOU 1969  N   ARG B  50     5279   5407   3578    595   -429    117       N  
ATOM   1970  CA  ARG B  50     -13.914  -5.565  12.723  1.00 35.73           C  
ANISOU 1970  CA  ARG B  50     5099   5268   3207    764   -318    247       C  
ATOM   1971  C   ARG B  50     -12.792  -6.486  12.246  1.00 37.94           C  
ANISOU 1971  C   ARG B  50     5532   5554   3331    924   -188    245       C  
ATOM   1972  O   ARG B  50     -12.167  -6.203  11.218  1.00 41.23           O  
ANISOU 1972  O   ARG B  50     6007   6058   3599   1102    -72    366       O  
ATOM   1973  CB  ARG B  50     -13.363  -4.161  13.014  1.00 32.37           C  
ANISOU 1973  CB  ARG B  50     4472   4866   2963    758   -214    438       C  
ATOM   1974  N   LEU B  51     -12.530  -7.594  12.959  1.00 35.96           N  
ANISOU 1974  N   LEU B  51     4368   6077   3217    317   -456     21       N  
ATOM   1975  CA  LEU B  51     -11.497  -8.545  12.562  1.00 34.06           C  
ANISOU 1975  CA  LEU B  51     4204   5850   2888    327   -342    -67       C  
ATOM   1976  C   LEU B  51     -12.030  -9.505  11.499  1.00 35.08           C  
ANISOU 1976  C   LEU B  51     4441   6091   2795    371   -455   -231       C  
ATOM   1977  O   LEU B  51     -13.191  -9.916  11.559  1.00 38.54           O  
ANISOU 1977  O   LEU B  51     4847   6550   3246    328   -637   -346       O  
ATOM   1978  CB  LEU B  51     -11.010  -9.346  13.772  1.00 33.33           C  
ANISOU 1978  CB  LEU B  51     4034   5622   3007    239   -287   -165       C  
ATOM   1979  CG  LEU B  51     -10.289  -8.571  14.875  1.00 31.32           C  
ANISOU 1979  CG  LEU B  51     3683   5257   2962    191   -178    -38       C  
ATOM   1980  CD1 LEU B  51     -10.133  -9.434  16.129  1.00 33.09           C  
ANISOU 1980  CD1 LEU B  51     3842   5359   3373    111   -181   -147       C  
ATOM   1981  CD2 LEU B  51      -8.943  -8.087  14.378  1.00 33.19           C  
ANISOU 1981  CD2 LEU B  51     3943   5525   3143    237      1     85       C  
ATOM   1982  N   PRO B  52     -11.205  -9.877  10.521  1.00 35.95           N  
ANISOU 1982  N   PRO B  52     4679   6281   2700    452   -349   -252       N  
ATOM   1983  CA  PRO B  52     -11.599 -10.946   9.590  1.00 35.01           C  
ANISOU 1983  CA  PRO B  52     4688   6246   2369    490   -452   -448       C  
ATOM   1984  C   PRO B  52     -11.804 -12.271  10.317  1.00 35.68           C  
ANISOU 1984  C   PRO B  52     4746   6211   2602    396   -513   -663       C  
ATOM   1985  O   PRO B  52     -11.074 -12.614  11.250  1.00 37.02           O  
ANISOU 1985  O   PRO B  52     4853   6252   2960    354   -396   -665       O  
ATOM   1986  CB  PRO B  52     -10.422 -11.016   8.610  1.00 36.49           C  
ANISOU 1986  CB  PRO B  52     5008   6519   2336    605   -263   -411       C  
ATOM   1987  CG  PRO B  52      -9.273 -10.397   9.338  1.00 33.94           C  
ANISOU 1987  CG  PRO B  52     4582   6117   2196    587    -51   -247       C  
ATOM   1988  CD  PRO B  52      -9.878  -9.328  10.211  1.00 32.30           C  
ANISOU 1988  CD  PRO B  52     4246   5837   2189    510   -124   -102       C  
ATOM   1989  N   GLU B  53     -12.808 -13.017   9.873  1.00 36.36           N  
ANISOU 1989  N   GLU B  53     4882   6334   2599    360   -704   -842       N  
ATOM   1990  CA  GLU B  53     -13.247 -14.250  10.511  1.00 38.69           C  
ANISOU 1990  CA  GLU B  53     5161   6501   3039    243   -789  -1043       C  
ATOM   1991  C   GLU B  53     -12.944 -15.448   9.618  1.00 40.16           C  
ANISOU 1991  C   GLU B  53     5533   6692   3033    289   -800  -1255       C  
ATOM   1992  O   GLU B  53     -12.974 -15.343   8.391  1.00 45.34           O  
ANISOU 1992  O   GLU B  53     6320   7495   3413    387   -840  -1289       O  
ATOM   1993  CB  GLU B  53     -14.748 -14.190  10.804  1.00 38.66           C  
ANISOU 1993  CB  GLU B  53     5041   6519   3128    131  -1009  -1095       C  
ATOM   1994  CG  GLU B  53     -15.217 -15.162  11.859  1.00 40.47           C  
ANISOU 1994  CG  GLU B  53     5198   6587   3592    -27  -1054  -1225       C  
ATOM   1995  CD  GLU B  53     -16.661 -14.931  12.252  1.00 41.72           C  
ANISOU 1995  CD  GLU B  53     5193   6786   3874   -141  -1234  -1241       C  
ATOM   1996  OE1 GLU B  53     -17.522 -14.836  11.354  1.00 44.10           O  
ANISOU 1996  OE1 GLU B  53     5494   7232   4030   -130  -1415  -1307       O  
ATOM   1997  OE2 GLU B  53     -16.928 -14.830  13.469  1.00 45.12           O  
ANISOU 1997  OE2 GLU B  53     5489   7114   4540   -235  -1191  -1186       O  
ATOM   1998  N   GLU B  54     -12.653 -16.595  10.237  1.00 39.31           N  
ANISOU 1998  N   GLU B  54     5457   6416   3062    227   -765  -1400       N  
ATOM   1999  CA  GLU B  54     -12.362 -17.800   9.454  1.00 43.93           C  
ANISOU 1999  CA  GLU B  54     6239   6969   3485    275   -774  -1623       C  
ATOM   2000  C   GLU B  54     -13.050 -19.018  10.057  1.00 39.20           C  
ANISOU 2000  C   GLU B  54     5657   6187   3049    121   -897  -1820       C  
ATOM   2001  O   GLU B  54     -13.127 -19.144  11.287  1.00 38.86           O  
ANISOU 2001  O   GLU B  54     5499   6000   3266     19   -866  -1763       O  
ATOM   2002  CB  GLU B  54     -10.851 -18.063   9.359  1.00 44.47           C  
ANISOU 2002  CB  GLU B  54     6388   6999   3510    420   -533  -1596       C  
ATOM   2003  N   PRO B  55     -13.555 -19.924   9.226  1.00 42.75           N  
ANISOU 2003  N   PRO B  55     6261   6628   3356     93  -1033  -2042       N  
ATOM   2004  CA  PRO B  55     -14.152 -21.151   9.763  1.00 44.68           C  
ANISOU 2004  CA  PRO B  55     6540   6646   3791    -80  -1117  -2191       C  
ATOM   2005  C   PRO B  55     -13.073 -22.102  10.247  1.00 45.98           C  
ANISOU 2005  C   PRO B  55     6827   6617   4026    -10   -960  -2281       C  
ATOM   2006  O   PRO B  55     -12.034 -22.270   9.607  1.00 51.01           O  
ANISOU 2006  O   PRO B  55     7598   7284   4499    169   -823  -2311       O  
ATOM   2007  CB  PRO B  55     -14.914 -21.728   8.566  1.00 48.64           C  
ANISOU 2007  CB  PRO B  55     7176   7167   4139   -137  -1264  -2316       C  
ATOM   2008  CG  PRO B  55     -14.146 -21.229   7.379  1.00 49.53           C  
ANISOU 2008  CG  PRO B  55     7413   7451   3956     64  -1176  -2284       C  
ATOM   2009  CD  PRO B  55     -13.649 -19.856   7.757  1.00 43.88           C  
ANISOU 2009  CD  PRO B  55     6550   6899   3225    178  -1076  -2071       C  
ATOM   2010  N   VAL B  56     -13.315 -22.709  11.405  1.00 44.64           N  
ANISOU 2010  N   VAL B  56     6606   6247   4107   -144   -969  -2307       N  
ATOM   2011  CA  VAL B  56     -12.392 -23.662  12.007  1.00 50.03           C  
ANISOU 2011  CA  VAL B  56     7403   6705   4902    -85   -832  -2355       C  
ATOM   2012  C   VAL B  56     -13.185 -24.896  12.403  1.00 56.77           C  
ANISOU 2012  C   VAL B  56     8344   7314   5911   -281   -931  -2486       C  
ATOM   2013  O   VAL B  56     -14.190 -24.788  13.116  1.00 54.66           O  
ANISOU 2013  O   VAL B  56     7942   7010   5814   -478  -1024  -2431       O  
ATOM   2014  CB  VAL B  56     -11.670 -23.069  13.231  1.00 50.49           C  
ANISOU 2014  CB  VAL B  56     7306   6724   5154    -47   -677  -2124       C  
ATOM   2015  CG1 VAL B  56     -10.892 -24.155  13.967  1.00 54.70           C  
ANISOU 2015  CG1 VAL B  56     7951   7008   5824      0   -575  -2172       C  
ATOM   2016  CG2 VAL B  56     -10.746 -21.931  12.809  1.00 49.59           C  
ANISOU 2016  CG2 VAL B  56     7112   6814   4914    128   -542  -1957       C  
ATOM   2017  N   THR B  57     -12.748 -26.062  11.935  1.00 60.04           N  
ANISOU 2017  N   THR B  57     8977   7560   6275   -235   -885  -2629       N  
ATOM   2018  CA  THR B  57     -13.414 -27.300  12.313  1.00 61.57           C  
ANISOU 2018  CA  THR B  57     9275   7498   6620   -431   -944  -2729       C  
ATOM   2019  C   THR B  57     -13.237 -27.550  13.807  1.00 63.25           C  
ANISOU 2019  C   THR B  57     9431   7514   7086   -488   -879  -2639       C  
ATOM   2020  O   THR B  57     -12.174 -27.285  14.378  1.00 64.91           O  
ANISOU 2020  O   THR B  57     9626   7705   7333   -311   -757  -2569       O  
ATOM   2021  CB  THR B  57     -12.868 -28.475  11.499  1.00 62.62           C  
ANISOU 2021  CB  THR B  57     9652   7493   6647   -349   -883  -2908       C  
ATOM   2022  OG1 THR B  57     -11.450 -28.577  11.687  1.00 64.95           O  
ANISOU 2022  OG1 THR B  57    10014   7738   6925    -95   -706  -2885       O  
ATOM   2023  CG2 THR B  57     -13.169 -28.276  10.018  1.00 58.66           C  
ANISOU 2023  CG2 THR B  57     9217   7184   5887   -320   -960  -3005       C  
ATOM   2024  N   ALA B  58     -14.300 -28.028  14.452  1.00 60.69           N  
ANISOU 2024  N   ALA B  58     9072   7056   6933   -737   -961  -2625       N  
ATOM   2025  CA  ALA B  58     -14.267 -28.309  15.881  1.00 58.17           C  
ANISOU 2025  CA  ALA B  58     8715   6544   6845   -817   -898  -2523       C  
ATOM   2026  C   ALA B  58     -15.136 -29.529  16.164  1.00 59.40           C  
ANISOU 2026  C   ALA B  58     8991   6459   7121  -1057   -941  -2583       C  
ATOM   2027  O   ALA B  58     -15.746 -30.108  15.261  1.00 59.03           O  
ANISOU 2027  O   ALA B  58     9025   6412   6993  -1161  -1021  -2714       O  
ATOM   2028  CB  ALA B  58     -14.717 -27.092  16.694  1.00 54.02           C  
ANISOU 2028  CB  ALA B  58     7921   6186   6420   -876   -915  -2354       C  
ATOM   2029  N   GLY B  59     -15.181 -29.924  17.432  1.00 61.50           N  
ANISOU 2029  N   GLY B  59     9251   6528   7586  -1127   -887  -2467       N  
ATOM   2030  CA  GLY B  59     -15.972 -31.068  17.842  1.00 68.19           C  
ANISOU 2030  CA  GLY B  59    10044   7152   8713  -1203  -1011  -2540       C  
ATOM   2031  C   GLY B  59     -15.244 -32.397  17.765  1.00 76.39           C  
ANISOU 2031  C   GLY B  59    11256   7967   9801  -1177   -832  -2711       C  
ATOM   2032  O   GLY B  59     -14.322 -32.657  18.538  1.00 80.36           O  
ANISOU 2032  O   GLY B  59    11879   8299  10354  -1055   -722  -2626       O  
ATOM   2033  N   THR B  64     -18.371 -33.464  14.324  1.00 70.25           N  
ANISOU 2033  N   THR B  64    10515   7493   8685  -1777  -1131  -3186       N  
ATOM   2034  CA  THR B  64     -17.590 -32.377  13.741  1.00 64.43           C  
ANISOU 2034  CA  THR B  64     9888   6923   7670  -1574  -1173  -3080       C  
ATOM   2035  C   THR B  64     -18.498 -31.212  13.338  1.00 68.41           C  
ANISOU 2035  C   THR B  64    10267   7656   8067  -1620  -1404  -2948       C  
ATOM   2036  O   THR B  64     -19.530 -31.411  12.700  1.00 65.64           O  
ANISOU 2036  O   THR B  64     9899   7359   7684  -1778  -1573  -3012       O  
ATOM   2037  CB  THR B  64     -16.785 -32.857  12.512  1.00 61.72           C  
ANISOU 2037  CB  THR B  64     9710   6593   7149  -1396  -1142  -3316       C  
ATOM   2038  N   HIS B  65     -18.112 -29.995  13.717  1.00 74.50           N  
ANISOU 2038  N   HIS B  65    10886   8594   8828  -1477  -1387  -2809       N  
ATOM   2039  CA  HIS B  65     -18.924 -28.816  13.444  1.00 79.01           C  
ANISOU 2039  CA  HIS B  65    11225   9430   9364  -1502  -1529  -2722       C  
ATOM   2040  C   HIS B  65     -18.012 -27.626  13.197  1.00 74.10           C  
ANISOU 2040  C   HIS B  65    10516   9033   8608  -1257  -1438  -2652       C  
ATOM   2041  O   HIS B  65     -16.838 -27.628  13.573  1.00 75.84           O  
ANISOU 2041  O   HIS B  65    10809   9187   8820  -1094  -1282  -2636       O  
ATOM   2042  CB  HIS B  65     -19.891 -28.511  14.597  1.00 82.99           C  
ANISOU 2042  CB  HIS B  65    11492   9915  10127  -1650  -1579  -2564       C  
ATOM   2043  CG  HIS B  65     -20.912 -29.581  14.829  1.00 88.13           C  
ANISOU 2043  CG  HIS B  65    12166  10372  10947  -1868  -1690  -2607       C  
ATOM   2044  ND1 HIS B  65     -22.159 -29.561  14.242  1.00 90.63           N  
ANISOU 2044  ND1 HIS B  65    12366  10798  11271  -2027  -1871  -2646       N  
ATOM   2045  CD2 HIS B  65     -20.869 -30.707  15.580  1.00 88.97           C  
ANISOU 2045  CD2 HIS B  65    12376  10185  11245  -1932  -1652  -2616       C  
ATOM   2046  CE1 HIS B  65     -22.841 -30.626  14.623  1.00 92.14           C  
ANISOU 2046  CE1 HIS B  65    12586  10773  11651  -2199  -1933  -2681       C  
ATOM   2047  NE2 HIS B  65     -22.081 -31.339  15.435  1.00 91.63           N  
ANISOU 2047  NE2 HIS B  65    12650  10456  11710  -2135  -1806  -2666       N  
ATOM   2048  N   ASP B  66     -18.571 -26.600  12.563  1.00 66.22           N  
ANISOU 2048  N   ASP B  66     9358   8297   7507  -1228  -1544  -2601       N  
ATOM   2049  CA  ASP B  66     -17.832 -25.386  12.260  1.00 56.22           C  
ANISOU 2049  CA  ASP B  66     8009   7252   6100  -1011  -1478  -2515       C  
ATOM   2050  C   ASP B  66     -18.051 -24.353  13.358  1.00 55.55           C  
ANISOU 2050  C   ASP B  66     7672   7252   6182  -1022  -1433  -2330       C  
ATOM   2051  O   ASP B  66     -19.189 -24.084  13.752  1.00 56.23           O  
ANISOU 2051  O   ASP B  66     7580   7382   6403  -1168  -1524  -2257       O  
ATOM   2052  CB  ASP B  66     -18.256 -24.810  10.906  1.00 57.14           C  
ANISOU 2052  CB  ASP B  66     8124   7601   5986   -951  -1607  -2550       C  
ATOM   2053  CG  ASP B  66     -17.403 -25.324   9.746  1.00 60.95           C  
ANISOU 2053  CG  ASP B  66     8855   8086   6218   -808  -1560  -2694       C  
ATOM   2054  OD1 ASP B  66     -16.617 -26.278   9.948  1.00 59.48           O  
ANISOU 2054  OD1 ASP B  66     8841   7701   6057   -774  -1441  -2792       O  
ATOM   2055  OD2 ASP B  66     -17.518 -24.763   8.631  1.00 60.73           O  
ANISOU 2055  OD2 ASP B  66     8850   8259   5967   -717  -1632  -2703       O  
ATOM   2056  N   ILE B  67     -16.953 -23.797  13.862  1.00 53.70           N  
ANISOU 2056  N   ILE B  67     7420   7042   5941   -868  -1284  -2258       N  
ATOM   2057  CA  ILE B  67     -16.977 -22.587  14.668  1.00 46.58           C  
ANISOU 2057  CA  ILE B  67     6297   6273   5128   -842  -1233  -2089       C  
ATOM   2058  C   ILE B  67     -16.136 -21.555  13.931  1.00 48.04           C  
ANISOU 2058  C   ILE B  67     6483   6672   5100   -629  -1189  -2046       C  
ATOM   2059  O   ILE B  67     -15.347 -21.888  13.042  1.00 53.08           O  
ANISOU 2059  O   ILE B  67     7295   7323   5551   -490  -1151  -2137       O  
ATOM   2060  CB  ILE B  67     -16.457 -22.815  16.099  1.00 46.15           C  
ANISOU 2060  CB  ILE B  67     6213   6050   5273   -880  -1096  -2024       C  
ATOM   2061  CG1 ILE B  67     -14.936 -22.937  16.095  1.00 45.82           C  
ANISOU 2061  CG1 ILE B  67     6310   5940   5158   -676   -936  -1986       C  
ATOM   2062  CG2 ILE B  67     -17.094 -24.065  16.699  1.00 50.15           C  
ANISOU 2062  CG2 ILE B  67     6794   6310   5950  -1068  -1115  -2071       C  
ATOM   2063  CD1 ILE B  67     -14.361 -23.266  17.431  1.00 49.15           C  
ANISOU 2063  CD1 ILE B  67     6738   6177   5762   -682   -805  -1876       C  
ATOM   2064  N   TYR B  68     -16.310 -20.289  14.302  1.00 39.37           N  
ANISOU 2064  N   TYR B  68     5202   5719   4038   -595  -1165  -1857       N  
ATOM   2065  CA  TYR B  68     -15.785 -19.172  13.523  1.00 39.65           C  
ANISOU 2065  CA  TYR B  68     5231   5949   3886   -418  -1127  -1739       C  
ATOM   2066  C   TYR B  68     -14.850 -18.353  14.395  1.00 43.28           C  
ANISOU 2066  C   TYR B  68     5616   6382   4447   -331   -944  -1528       C  
ATOM   2067  O   TYR B  68     -15.250 -17.868  15.460  1.00 43.22           O  
ANISOU 2067  O   TYR B  68     5460   6339   4621   -409   -926  -1416       O  
ATOM   2068  CB  TYR B  68     -16.937 -18.342  12.956  1.00 40.73           C  
ANISOU 2068  CB  TYR B  68     5239   6286   3952   -446  -1300  -1712       C  
ATOM   2069  CG  TYR B  68     -17.882 -19.261  12.219  1.00 45.46           C  
ANISOU 2069  CG  TYR B  68     5910   6846   4517   -556  -1462  -1863       C  
ATOM   2070  CD1 TYR B  68     -17.514 -19.816  11.000  1.00 50.22           C  
ANISOU 2070  CD1 TYR B  68     6719   7468   4895   -478  -1493  -1983       C  
ATOM   2071  CD2 TYR B  68     -19.096 -19.646  12.775  1.00 40.84           C  
ANISOU 2071  CD2 TYR B  68     5200   6184   4133   -742  -1556  -1869       C  
ATOM   2072  CE1 TYR B  68     -18.339 -20.693  10.331  1.00 51.41           C  
ANISOU 2072  CE1 TYR B  68     6952   7565   5017   -594  -1637  -2116       C  
ATOM   2073  CE2 TYR B  68     -19.932 -20.527  12.110  1.00 47.11           C  
ANISOU 2073  CE2 TYR B  68     6063   6931   4907   -860  -1700  -1992       C  
ATOM   2074  CZ  TYR B  68     -19.545 -21.044  10.886  1.00 52.86           C  
ANISOU 2074  CZ  TYR B  68     7001   7677   5405   -791  -1749  -2121       C  
ATOM   2075  OH  TYR B  68     -20.354 -21.920  10.207  1.00 57.41           O  
ANISOU 2075  OH  TYR B  68     7656   8208   5949   -921  -1899  -2255       O  
ATOM   2076  N   VAL B  69     -13.604 -18.216  13.950  1.00 39.32           N  
ANISOU 2076  N   VAL B  69     5211   5901   3826   -174   -806  -1483       N  
ATOM   2077  CA  VAL B  69     -12.519 -17.728  14.787  1.00 30.51           C  
ANISOU 2077  CA  VAL B  69     4040   4732   2821   -104   -633  -1323       C  
ATOM   2078  C   VAL B  69     -11.974 -16.432  14.208  1.00 29.70           C  
ANISOU 2078  C   VAL B  69     3892   4794   2598     15   -557  -1158       C  
ATOM   2079  O   VAL B  69     -11.778 -16.314  12.995  1.00 34.43           O  
ANISOU 2079  O   VAL B  69     4586   5518   2976    112   -557  -1188       O  
ATOM   2080  CB  VAL B  69     -11.404 -18.786  14.910  1.00 34.16           C  
ANISOU 2080  CB  VAL B  69     4631   5055   3295    -28   -516  -1407       C  
ATOM   2081  CG1 VAL B  69     -10.218 -18.235  15.704  1.00 34.82           C  
ANISOU 2081  CG1 VAL B  69     4631   5114   3484     54   -355  -1243       C  
ATOM   2082  CG2 VAL B  69     -11.952 -20.064  15.542  1.00 30.54           C  
ANISOU 2082  CG2 VAL B  69     4241   4395   2967   -153   -585  -1552       C  
ATOM   2083  N   ARG B  70     -11.733 -15.461  15.081  1.00 28.39           N  
ANISOU 2083  N   ARG B  70     3596   4620   2572      4   -489   -983       N  
ATOM   2084  CA  ARG B  70     -11.058 -14.215  14.733  1.00 31.11           C  
ANISOU 2084  CA  ARG B  70     3897   5072   2851     95   -390   -806       C  
ATOM   2085  C   ARG B  70      -9.751 -14.162  15.510  1.00 28.57           C  
ANISOU 2085  C   ARG B  70     3533   4669   2653    131   -229   -724       C  
ATOM   2086  O   ARG B  70      -9.762 -14.066  16.742  1.00 27.93           O  
ANISOU 2086  O   ARG B  70     3367   4484   2762     61   -227   -679       O  
ATOM   2087  CB  ARG B  70     -11.932 -13.004  15.054  1.00 27.91           C  
ANISOU 2087  CB  ARG B  70     3376   4719   2508     51   -465   -675       C  
ATOM   2088  CG  ARG B  70     -13.070 -12.802  14.072  1.00 32.22           C  
ANISOU 2088  CG  ARG B  70     3945   5396   2901     60   -623   -719       C  
ATOM   2089  CD  ARG B  70     -13.980 -11.703  14.564  1.00 35.45           C  
ANISOU 2089  CD  ARG B  70     4224   5835   3411     31   -698   -600       C  
ATOM   2090  NE  ARG B  70     -14.595 -10.967  13.467  1.00 36.51           N  
ANISOU 2090  NE  ARG B  70     4383   6124   3365    112   -800   -543       N  
ATOM   2091  CZ  ARG B  70     -15.892 -10.992  13.196  1.00 42.73           C  
ANISOU 2091  CZ  ARG B  70     5110   6995   4132     85   -985   -608       C  
ATOM   2092  NH1 ARG B  70     -16.708 -11.716  13.950  1.00 43.46           N  
ANISOU 2092  NH1 ARG B  70     5103   7026   4384    -41  -1068   -729       N  
ATOM   2093  NH2 ARG B  70     -16.372 -10.290  12.178  1.00 42.54           N  
ANISOU 2093  NH2 ARG B  70     5117   7118   3929    184  -1086   -542       N  
ATOM   2094  N   ARG B  71      -8.627 -14.199  14.796  1.00 26.77           N  
ANISOU 2094  N   ARG B  71     3356   4503   2314    244    -96   -703       N  
ATOM   2095  CA  ARG B  71      -7.323 -14.306  15.440  1.00 26.16           C  
ANISOU 2095  CA  ARG B  71     3219   4367   2354    289     46   -649       C  
ATOM   2096  C   ARG B  71      -6.750 -12.935  15.774  1.00 26.43           C  
ANISOU 2096  C   ARG B  71     3128   4448   2467    276    130   -450       C  
ATOM   2097  O   ARG B  71      -6.812 -12.002  14.970  1.00 33.30           O  
ANISOU 2097  O   ARG B  71     4004   5427   3220    300    163   -344       O  
ATOM   2098  CB  ARG B  71      -6.357 -15.085  14.548  1.00 27.92           C  
ANISOU 2098  CB  ARG B  71     3534   4637   2438    423    165   -735       C  
ATOM   2099  CG  ARG B  71      -6.895 -16.466  14.219  1.00 32.92           C  
ANISOU 2099  CG  ARG B  71     4319   5192   2998    434     77   -951       C  
ATOM   2100  CD  ARG B  71      -5.867 -17.430  13.632  1.00 35.08           C  
ANISOU 2100  CD  ARG B  71     4692   5458   3178    584    201  -1063       C  
ATOM   2101  NE  ARG B  71      -6.515 -18.689  13.271  1.00 43.45           N  
ANISOU 2101  NE  ARG B  71     5926   6418   4165    577     96  -1282       N  
ATOM   2102  CZ  ARG B  71      -6.738 -19.694  14.117  1.00 52.97           C  
ANISOU 2102  CZ  ARG B  71     7176   7429   5523    523     32  -1381       C  
ATOM   2103  NH1 ARG B  71      -6.356 -19.612  15.391  1.00 50.42           N  
ANISOU 2103  NH1 ARG B  71     6740   7004   5414    488     58  -1280       N  
ATOM   2104  NH2 ARG B  71      -7.349 -20.790  13.685  1.00 57.78           N  
ANISOU 2104  NH2 ARG B  71     7956   7938   6062    500    -62  -1583       N  
ATOM   2105  N   ILE B  72      -6.213 -12.822  16.983  1.00 23.98           N  
ANISOU 2105  N   ILE B  72     2715   4044   2351    234    156   -399       N  
ATOM   2106  CA  ILE B  72      -5.542 -11.623  17.443  1.00 23.34           C  
ANISOU 2106  CA  ILE B  72     2515   3979   2376    204    228   -235       C  
ATOM   2107  C   ILE B  72      -4.046 -11.853  17.596  1.00 27.19           C  
ANISOU 2107  C   ILE B  72     2922   4482   2928    266    363   -209       C  
ATOM   2108  O   ILE B  72      -3.243 -11.029  17.155  1.00 25.35           O  
ANISOU 2108  O   ILE B  72     2616   4331   2685    279    481    -89       O  
ATOM   2109  CB  ILE B  72      -6.162 -11.129  18.768  1.00 23.73           C  
ANISOU 2109  CB  ILE B  72     2499   3922   2595     99    132   -198       C  
ATOM   2110  CG1 ILE B  72      -7.610 -10.687  18.536  1.00 28.95           C  
ANISOU 2110  CG1 ILE B  72     3199   4598   3201     52     18   -201       C  
ATOM   2111  CG2 ILE B  72      -5.357  -9.998  19.337  1.00 26.60           C  
ANISOU 2111  CG2 ILE B  72     2753   4276   3080     61    195    -59       C  
ATOM   2112  CD1 ILE B  72      -8.341 -10.312  19.802  1.00 25.58           C  
ANISOU 2112  CD1 ILE B  72     2717   4076   2925    -34    -62   -185       C  
HETATM 2113  N   MSE B  73      -3.656 -12.975  18.204  1.00 26.36           N  
ANISOU 2113  N   MSE B  73     2824   4298   2895    308    350   -313       N  
HETATM 2114  CA  MSE B  73      -2.258 -13.395  18.243  1.00 29.41           C  
ANISOU 2114  CA  MSE B  73     3130   4714   3332    405    469   -312       C  
HETATM 2115  C   MSE B  73      -2.118 -14.923  18.051  1.00 30.49           C  
ANISOU 2115  C   MSE B  73     3376   4792   3417    519    469   -474       C  
HETATM 2116  O   MSE B  73      -2.843 -15.714  18.661  1.00 29.16           O  
ANISOU 2116  O   MSE B  73     3299   4493   3288    485    356   -567       O  
HETATM 2117  CB  MSE B  73      -1.624 -12.944  19.555  1.00 23.70           C  
ANISOU 2117  CB  MSE B  73     2260   3932   2811    348    443   -234       C  
HETATM 2118  CG  MSE B  73      -0.236 -13.468  19.814  1.00 48.53           C  
ANISOU 2118  CG  MSE B  73     5293   7105   6043    451    525   -240       C  
HETATM 2119 SE   MSE B  73       0.457 -12.756  21.496  1.00 50.91          SE  
ANISOU 2119 SE   MSE B  73     5411   7350   6583    359    443   -147      SE  
HETATM 2120  CE  MSE B  73       1.220 -11.100  20.787  1.00 52.74           C  
ANISOU 2120  CE  MSE B  73     5473   7722   6845    270    579     20       C  
ATOM   2121  N   VAL B  74      -1.185 -15.322  17.193  1.00 27.41           N  
ANISOU 2121  N   VAL B  74     2981   4492   2941    656    609   -504       N  
ATOM   2122  CA  VAL B  74      -0.925 -16.725  16.913  1.00 28.70           C  
ANISOU 2122  CA  VAL B  74     3260   4594   3050    794    630   -663       C  
ATOM   2123  C   VAL B  74       0.420 -17.137  17.512  1.00 30.91           C  
ANISOU 2123  C   VAL B  74     3407   4869   3471    914    712   -644       C  
ATOM   2124  O   VAL B  74       1.283 -16.309  17.829  1.00 32.15           O  
ANISOU 2124  O   VAL B  74     3367   5117   3732    897    781   -516       O  
ATOM   2125  CB  VAL B  74      -0.969 -17.021  15.402  1.00 30.67           C  
ANISOU 2125  CB  VAL B  74     3638   4950   3063    895    724   -748       C  
ATOM   2126  CG1 VAL B  74      -2.340 -16.692  14.863  1.00 30.21           C  
ANISOU 2126  CG1 VAL B  74     3708   4902   2869    786    604   -776       C  
ATOM   2127  CG2 VAL B  74       0.104 -16.224  14.683  1.00 31.97           C  
ANISOU 2127  CG2 VAL B  74     3673   5301   3174    965    919   -627       C  
ATOM   2128  N   ASP B  75       0.599 -18.448  17.640  1.00 35.31           N  
ANISOU 2128  N   ASP B  75     4072   5312   4033   1038    698   -778       N  
ATOM   2129  CA  ASP B  75       1.696 -19.055  18.376  1.00 31.01           C  
ANISOU 2129  CA  ASP B  75     3427   4723   3632   1173    728   -777       C  
ATOM   2130  C   ASP B  75       2.041 -20.383  17.708  1.00 37.75           C  
ANISOU 2130  C   ASP B  75     4430   5516   4396   1376    799   -939       C  
ATOM   2131  O   ASP B  75       1.869 -21.462  18.269  1.00 33.40           O  
ANISOU 2131  O   ASP B  75     4011   4780   3901   1436    718  -1031       O  
ATOM   2132  CB  ASP B  75       1.290 -19.228  19.838  1.00 29.35           C  
ANISOU 2132  CB  ASP B  75     3222   4352   3577   1080    566   -745       C  
ATOM   2133  CG  ASP B  75       2.438 -19.656  20.714  1.00 36.45           C  
ANISOU 2133  CG  ASP B  75     3996   5226   4626   1213    567   -712       C  
ATOM   2134  OD1 ASP B  75       3.606 -19.498  20.294  1.00 39.05           O  
ANISOU 2134  OD1 ASP B  75     4159   5698   4981   1343    693   -682       O  
ATOM   2135  OD2 ASP B  75       2.166 -20.153  21.824  1.00 31.61           O  
ANISOU 2135  OD2 ASP B  75     3448   4459   4103   1192    443   -711       O  
ATOM   2136  N   ARG B  76       2.512 -20.310  16.463  1.00 40.24           N  
ANISOU 2136  N   ARG B  76     4748   5982   4561   1487    960   -976       N  
ATOM   2137  CA  ARG B  76       2.761 -21.513  15.684  1.00 41.84           C  
ANISOU 2137  CA  ARG B  76     5122   6131   4644   1687   1038  -1152       C  
ATOM   2138  C   ARG B  76       3.985 -22.254  16.219  1.00 43.88           C  
ANISOU 2138  C   ARG B  76     5276   6353   5045   1902   1107  -1166       C  
ATOM   2139  O   ARG B  76       4.842 -21.684  16.901  1.00 40.30           O  
ANISOU 2139  O   ARG B  76     4570   5991   4750   1911   1133  -1031       O  
ATOM   2140  CB  ARG B  76       2.954 -21.165  14.205  1.00 45.66           C  
ANISOU 2140  CB  ARG B  76     5642   6808   4900   1759   1207  -1182       C  
ATOM   2141  CG  ARG B  76       1.844 -20.291  13.608  1.00 42.76           C  
ANISOU 2141  CG  ARG B  76     5355   6512   4380   1571   1139  -1139       C  
ATOM   2142  CD  ARG B  76       2.019 -20.108  12.087  1.00 42.00           C  
ANISOU 2142  CD  ARG B  76     5347   6597   4014   1671   1302  -1181       C  
ATOM   2143  NE  ARG B  76       1.181 -19.021  11.583  1.00 46.76           N  
ANISOU 2143  NE  ARG B  76     5973   7305   4490   1508   1251  -1079       N  
ATOM   2144  CZ  ARG B  76       1.566 -17.748  11.522  1.00 47.86           C  
ANISOU 2144  CZ  ARG B  76     5935   7593   4657   1431   1345   -874       C  
ATOM   2145  NH1 ARG B  76       2.786 -17.404  11.922  1.00 49.43           N  
ANISOU 2145  NH1 ARG B  76     5901   7867   5012   1481   1494   -758       N  
ATOM   2146  NH2 ARG B  76       0.737 -16.817  11.062  1.00 41.40           N  
ANISOU 2146  NH2 ARG B  76     5168   6842   3719   1303   1285   -783       N  
ATOM   2147  N   ALA B  77       4.054 -23.550  15.906  1.00 46.68           N  
ANISOU 2147  N   ALA B  77     5828   6565   5343   2082   1123  -1339       N  
ATOM   2148  CA  ALA B  77       5.123 -24.391  16.428  1.00 48.96           C  
ANISOU 2148  CA  ALA B  77     6050   6786   5766   2319   1169  -1364       C  
ATOM   2149  C   ALA B  77       6.479 -23.896  15.942  1.00 46.11           C  
ANISOU 2149  C   ALA B  77     5419   6673   5427   2471   1374  -1286       C  
ATOM   2150  O   ALA B  77       6.646 -23.550  14.771  1.00 48.66           O  
ANISOU 2150  O   ALA B  77     5746   7143   5599   2462   1521  -1294       O  
ATOM   2151  CB  ALA B  77       4.916 -25.849  16.007  1.00 55.78           C  
ANISOU 2151  CB  ALA B  77     7210   7436   6548   2493   1168  -1577       C  
ATOM   2152  N   GLY B  78       7.447 -23.858  16.855  1.00 44.25           N  
ANISOU 2152  N   GLY B  78     4952   6459   5402   2537   1353  -1179       N  
ATOM   2153  CA  GLY B  78       8.767 -23.357  16.539  1.00 47.71           C  
ANISOU 2153  CA  GLY B  78     5103   7100   5926   2582   1504  -1073       C  
ATOM   2154  C   GLY B  78       8.852 -21.875  16.245  1.00 45.06           C  
ANISOU 2154  C   GLY B  78     4553   6989   5580   2394   1584   -924       C  
ATOM   2155  O   GLY B  78       9.927 -21.403  15.860  1.00 51.06           O  
ANISOU 2155  O   GLY B  78     5086   7908   6407   2399   1725   -840       O  
ATOM   2156  N   GLU B  79       7.766 -21.124  16.411  1.00 42.47           N  
ANISOU 2156  N   GLU B  79     4291   6670   5177   2223   1502   -889       N  
ATOM   2157  CA  GLU B  79       7.755 -19.685  16.196  1.00 42.19           C  
ANISOU 2157  CA  GLU B  79     4080   6809   5140   2022   1560   -730       C  
ATOM   2158  C   GLU B  79       7.528 -18.942  17.505  1.00 42.47           C  
ANISOU 2158  C   GLU B  79     3991   6781   5365   1818   1369   -608       C  
ATOM   2159  O   GLU B  79       7.065 -19.506  18.503  1.00 37.80           O  
ANISOU 2159  O   GLU B  79     3503   6005   4853   1804   1183   -649       O  
ATOM   2160  CB  GLU B  79       6.666 -19.272  15.196  1.00 41.36           C  
ANISOU 2160  CB  GLU B  79     4197   6716   4801   1896   1581   -755       C  
ATOM   2161  CG  GLU B  79       6.901 -19.727  13.758  1.00 43.40           C  
ANISOU 2161  CG  GLU B  79     4588   7064   4839   2044   1770   -851       C  
ATOM   2162  CD  GLU B  79       5.808 -19.238  12.810  1.00 48.06           C  
ANISOU 2162  CD  GLU B  79     5383   7706   5173   1943   1774   -869       C  
ATOM   2163  OE1 GLU B  79       4.981 -18.393  13.230  1.00 40.53           O  
ANISOU 2163  OE1 GLU B  79     4434   6712   4255   1721   1632   -769       O  
ATOM   2164  OE2 GLU B  79       5.773 -19.703  11.647  1.00 48.13           O  
ANISOU 2164  OE2 GLU B  79     5572   7738   4979   2026   1867   -967       O  
ATOM   2165  N   ARG B  80       7.865 -17.658  17.480  1.00 38.79           N  
ANISOU 2165  N   ARG B  80     3314   6462   4963   1659   1428   -457       N  
ATOM   2166  CA  ARG B  80       7.512 -16.750  18.547  1.00 36.61           C  
ANISOU 2166  CA  ARG B  80     2954   6128   4826   1439   1259   -350       C  
ATOM   2167  C   ARG B  80       6.082 -16.262  18.353  1.00 36.53           C  
ANISOU 2167  C   ARG B  80     3171   6023   4687   1258   1166   -346       C  
ATOM   2168  O   ARG B  80       5.561 -16.271  17.235  1.00 34.92           O  
ANISOU 2168  O   ARG B  80     3119   5860   4290   1271   1259   -383       O  
ATOM   2169  CB  ARG B  80       8.479 -15.574  18.576  1.00 37.52           C  
ANISOU 2169  CB  ARG B  80     2759   6421   5078   1334   1358   -199       C  
ATOM   2170  CG  ARG B  80       9.798 -15.914  19.231  1.00 40.90           C  
ANISOU 2170  CG  ARG B  80     2947   6883   5708   1428   1341   -193       C  
ATOM   2171  CD  ARG B  80      10.834 -14.845  19.007  1.00 46.13           C  
ANISOU 2171  CD  ARG B  80     3367   7658   6504   1274   1437    -80       C  
ATOM   2172  NE  ARG B  80      12.133 -15.285  19.502  1.00 55.05           N  
ANISOU 2172  NE  ARG B  80     4282   8817   7819   1371   1416   -104       N  
ATOM   2173  CZ  ARG B  80      12.967 -16.078  18.831  1.00 62.90           C  
ANISOU 2173  CZ  ARG B  80     5230   9868   8800   1557   1558   -167       C  
ATOM   2174  NH1 ARG B  80      12.647 -16.526  17.622  1.00 63.17           N  
ANISOU 2174  NH1 ARG B  80     5438   9931   8632   1664   1733   -222       N  
ATOM   2175  NH2 ARG B  80      14.129 -16.424  19.370  1.00 63.59           N  
ANISOU 2175  NH2 ARG B  80     5100   9986   9075   1643   1520   -182       N  
ATOM   2176  N   PRO B  81       5.413 -15.860  19.433  1.00 32.26           N  
ANISOU 2176  N   PRO B  81     2659   5361   4239   1102    978   -308       N  
ATOM   2177  CA  PRO B  81       4.073 -15.283  19.288  1.00 37.13           C  
ANISOU 2177  CA  PRO B  81     3447   5905   4754    935    894   -294       C  
ATOM   2178  C   PRO B  81       4.131 -14.048  18.406  1.00 39.64           C  
ANISOU 2178  C   PRO B  81     3694   6360   5007    832   1020   -175       C  
ATOM   2179  O   PRO B  81       5.096 -13.282  18.448  1.00 38.95           O  
ANISOU 2179  O   PRO B  81     3389   6382   5029    791   1114    -65       O  
ATOM   2180  CB  PRO B  81       3.679 -14.929  20.723  1.00 28.49           C  
ANISOU 2180  CB  PRO B  81     2327   4691   3806    804    708   -254       C  
ATOM   2181  CG  PRO B  81       4.586 -15.807  21.586  1.00 34.98           C  
ANISOU 2181  CG  PRO B  81     3060   5476   4754    943    658   -293       C  
ATOM   2182  CD  PRO B  81       5.864 -15.892  20.834  1.00 31.66           C  
ANISOU 2182  CD  PRO B  81     2455   5220   4354   1083    834   -278       C  
ATOM   2183  N   GLN B  82       3.105 -13.871  17.578  1.00 36.96           N  
ANISOU 2183  N   GLN B  82     3540   6015   4489    790   1021   -193       N  
ATOM   2184  CA  GLN B  82       3.038 -12.686  16.737  1.00 36.17           C  
ANISOU 2184  CA  GLN B  82     3414   6025   4304    699   1127    -63       C  
ATOM   2185  C   GLN B  82       1.596 -12.222  16.636  1.00 36.41           C  
ANISOU 2185  C   GLN B  82     3619   5978   4235    588    996    -58       C  
ATOM   2186  O   GLN B  82       0.675 -13.037  16.516  1.00 32.31           O  
ANISOU 2186  O   GLN B  82     3275   5387   3616    626    895   -185       O  
ATOM   2187  CB  GLN B  82       3.642 -12.934  15.335  1.00 36.81           C  
ANISOU 2187  CB  GLN B  82     3514   6265   4206    835   1345    -70       C  
ATOM   2188  CG  GLN B  82       2.947 -13.972  14.463  1.00 43.66           C  
ANISOU 2188  CG  GLN B  82     4626   7119   4845    963   1336   -230       C  
ATOM   2189  CD  GLN B  82       3.495 -14.003  13.023  1.00 52.27           C  
ANISOU 2189  CD  GLN B  82     5756   8384   5719   1089   1562   -222       C  
ATOM   2190  OE1 GLN B  82       4.707 -14.113  12.805  1.00 55.74           O  
ANISOU 2190  OE1 GLN B  82     6034   8938   6207   1190   1750   -190       O  
ATOM   2191  NE2 GLN B  82       2.598 -13.906  12.041  1.00 46.11           N  
ANISOU 2191  NE2 GLN B  82     5187   7638   4694   1089   1545   -250       N  
ATOM   2192  N   LEU B  83       1.409 -10.907  16.741  1.00 33.90           N  
ANISOU 2192  N   LEU B  83     3244   5668   3967    449    992     88       N  
ATOM   2193  CA  LEU B  83       0.119 -10.310  16.439  1.00 34.58           C  
ANISOU 2193  CA  LEU B  83     3477   5715   3947    373    896    117       C  
ATOM   2194  C   LEU B  83      -0.210 -10.534  14.972  1.00 36.31           C  
ANISOU 2194  C   LEU B  83     3844   6044   3907    466    981     95       C  
ATOM   2195  O   LEU B  83       0.675 -10.571  14.111  1.00 33.88           O  
ANISOU 2195  O   LEU B  83     3502   5861   3508    547   1165    134       O  
ATOM   2196  CB  LEU B  83       0.122  -8.806  16.741  1.00 30.72           C  
ANISOU 2196  CB  LEU B  83     2908   5203   3560    231    900    287       C  
ATOM   2197  CG  LEU B  83      -0.331  -8.252  18.093  1.00 34.91           C  
ANISOU 2197  CG  LEU B  83     3395   5595   4274    110    745    301       C  
ATOM   2198  CD1 LEU B  83      -0.021  -6.763  18.157  1.00 39.85           C  
ANISOU 2198  CD1 LEU B  83     3945   6203   4993    -13    795    469       C  
ATOM   2199  CD2 LEU B  83      -1.809  -8.483  18.351  1.00 34.43           C  
ANISOU 2199  CD2 LEU B  83     3480   5451   4150     98    584    224       C  
ATOM   2200  N   VAL B  84      -1.502 -10.717  14.706  1.00 34.69           N  
ANISOU 2200  N   VAL B  84     3800   5800   3579    456    843     26       N  
ATOM   2201  CA  VAL B  84      -2.058 -10.814  13.366  1.00 34.57           C  
ANISOU 2201  CA  VAL B  84     3948   5887   3300    528    865      0       C  
ATOM   2202  C   VAL B  84      -3.253  -9.874  13.330  1.00 33.26           C  
ANISOU 2202  C   VAL B  84     3843   5696   3099    442    732     83       C  
ATOM   2203  O   VAL B  84      -3.747  -9.434  14.367  1.00 36.09           O  
ANISOU 2203  O   VAL B  84     4136   5944   3631    344    618    111       O  
ATOM   2204  CB  VAL B  84      -2.478 -12.259  12.999  1.00 35.31           C  
ANISOU 2204  CB  VAL B  84     4185   5965   3267    625    798   -218       C  
ATOM   2205  CG1 VAL B  84      -1.272 -13.191  13.003  1.00 34.74           C  
ANISOU 2205  CG1 VAL B  84     4062   5908   3229    744    938   -300       C  
ATOM   2206  CG2 VAL B  84      -3.539 -12.764  13.958  1.00 28.91           C  
ANISOU 2206  CG2 VAL B  84     3403   5007   2574    541    590   -324       C  
ATOM   2207  N   ASN B  85      -3.689  -9.535  12.120  1.00 30.93           N  
ANISOU 2207  N   ASN B  85     3675   5510   2568    497    751    127       N  
ATOM   2208  CA  ASN B  85      -4.858  -8.674  11.906  1.00 35.43           C  
ANISOU 2208  CA  ASN B  85     4313   6076   3074    455    616    208       C  
ATOM   2209  C   ASN B  85      -4.707  -7.292  12.549  1.00 32.35           C  
ANISOU 2209  C   ASN B  85     3823   5611   2857    357    643    403       C  
ATOM   2210  O   ASN B  85      -5.659  -6.743  13.106  1.00 28.69           O  
ANISOU 2210  O   ASN B  85     3355   5069   2478    302    499    427       O  
ATOM   2211  CB  ASN B  85      -6.139  -9.355  12.393  1.00 31.69           C  
ANISOU 2211  CB  ASN B  85     3878   5532   2630    423    394     47       C  
ATOM   2212  CG  ASN B  85      -6.474 -10.585  11.588  1.00 31.66           C  
ANISOU 2212  CG  ASN B  85     4007   5590   2431    502    340   -146       C  
ATOM   2213  OD1 ASN B  85      -6.167 -10.656  10.398  1.00 32.89           O  
ANISOU 2213  OD1 ASN B  85     4274   5872   2350    599    425   -142       O  
ATOM   2214  ND2 ASN B  85      -7.098 -11.571  12.233  1.00 31.36           N  
ANISOU 2214  ND2 ASN B  85     3973   5457   2487    456    206   -318       N  
ATOM   2215  N   LEU B  86      -3.516  -6.704  12.451  1.00 34.03           N  
ANISOU 2215  N   LEU B  86     3955   5848   3128    335    832    540       N  
ATOM   2216  CA  LEU B  86      -3.377  -5.288  12.767  1.00 33.77           C  
ANISOU 2216  CA  LEU B  86     3869   5743   3219    240    869    738       C  
ATOM   2217  C   LEU B  86      -4.366  -4.469  11.935  1.00 35.46           C  
ANISOU 2217  C   LEU B  86     4233   5984   3256    280    803    851       C  
ATOM   2218  O   LEU B  86      -4.754  -4.879  10.837  1.00 34.17           O  
ANISOU 2218  O   LEU B  86     4203   5944   2836    384    795    819       O  
ATOM   2219  CB  LEU B  86      -1.955  -4.807  12.493  1.00 32.24           C  
ANISOU 2219  CB  LEU B  86     3575   5597   3078    203   1100    876       C  
ATOM   2220  CG  LEU B  86      -0.865  -5.446  13.343  1.00 39.19           C  
ANISOU 2220  CG  LEU B  86     4272   6462   4156    170   1162    791       C  
ATOM   2221  CD1 LEU B  86       0.512  -4.969  12.897  1.00 34.04           C  
ANISOU 2221  CD1 LEU B  86     3495   5893   3544    136   1404    932       C  
ATOM   2222  CD2 LEU B  86      -1.107  -5.131  14.819  1.00 38.96           C  
ANISOU 2222  CD2 LEU B  86     4147   6272   4383     58   1011    759       C  
ATOM   2223  N   PRO B  87      -4.794  -3.296  12.429  1.00 33.46           N  
ANISOU 2223  N   PRO B  87     3971   5614   3129    210    745    982       N  
ATOM   2224  CA  PRO B  87      -4.417  -2.639  13.686  1.00 35.00           C  
ANISOU 2224  CA  PRO B  87     4040   5652   3606     85    740   1022       C  
ATOM   2225  C   PRO B  87      -5.263  -2.998  14.910  1.00 29.91           C  
ANISOU 2225  C   PRO B  87     3346   4905   3112     55    554    875       C  
ATOM   2226  O   PRO B  87      -4.774  -2.871  16.026  1.00 30.22           O  
ANISOU 2226  O   PRO B  87     3278   4843   3362    -35    551    850       O  
ATOM   2227  CB  PRO B  87      -4.603  -1.161  13.354  1.00 35.58           C  
ANISOU 2227  CB  PRO B  87     4189   5648   3683     54    775   1239       C  
ATOM   2228  CG  PRO B  87      -5.760  -1.161  12.428  1.00 35.28           C  
ANISOU 2228  CG  PRO B  87     4305   5689   3411    180    668   1252       C  
ATOM   2229  CD  PRO B  87      -5.651  -2.427  11.606  1.00 33.96           C  
ANISOU 2229  CD  PRO B  87     4178   5697   3028    271    690   1119       C  
ATOM   2230  N   HIS B  88      -6.507  -3.437  14.709  1.00 28.91           N  
ANISOU 2230  N   HIS B  88     3294   4813   2879    124    402    782       N  
ATOM   2231  CA  HIS B  88      -7.436  -3.555  15.828  1.00 30.36           C  
ANISOU 2231  CA  HIS B  88     3430   4900   3203     90    246    680       C  
ATOM   2232  C   HIS B  88      -7.051  -4.659  16.790  1.00 29.66           C  
ANISOU 2232  C   HIS B  88     3256   4779   3233     44    231    521       C  
ATOM   2233  O   HIS B  88      -7.417  -4.589  17.971  1.00 24.93           O  
ANISOU 2233  O   HIS B  88     2603   4078   2792    -13    155    470       O  
ATOM   2234  CB  HIS B  88      -8.845  -3.768  15.298  1.00 33.84           C  
ANISOU 2234  CB  HIS B  88     3942   5409   3508    168     94    624       C  
ATOM   2235  CG  HIS B  88      -9.284  -2.683  14.369  1.00 39.25           C  
ANISOU 2235  CG  HIS B  88     4722   6127   4065    240     86    790       C  
ATOM   2236  ND1 HIS B  88      -9.283  -1.354  14.736  1.00 39.42           N  
ANISOU 2236  ND1 HIS B  88     4751   6027   4202    218    111    946       N  
ATOM   2237  CD2 HIS B  88      -9.701  -2.719  13.082  1.00 42.29           C  
ANISOU 2237  CD2 HIS B  88     5217   6644   4207    341     54    830       C  
ATOM   2238  CE1 HIS B  88      -9.703  -0.619  13.722  1.00 41.95           C  
ANISOU 2238  CE1 HIS B  88     5183   6394   4364    309     97   1088       C  
ATOM   2239  NE2 HIS B  88      -9.965  -1.423  12.706  1.00 42.82           N  
ANISOU 2239  NE2 HIS B  88     5354   6668   4246    387     59   1023       N  
ATOM   2240  N   SER B  89      -6.295  -5.652  16.324  1.00 28.52           N  
ANISOU 2240  N   SER B  89     3111   4715   3011     79    309    447       N  
ATOM   2241  CA  SER B  89      -5.832  -6.695  17.229  1.00 30.62           C  
ANISOU 2241  CA  SER B  89     3308   4935   3392     54    298    314       C  
ATOM   2242  C   SER B  89      -4.905  -6.120  18.291  1.00 28.78           C  
ANISOU 2242  C   SER B  89     2960   4613   3362    -27    347    376       C  
ATOM   2243  O   SER B  89      -4.962  -6.522  19.459  1.00 23.03           O  
ANISOU 2243  O   SER B  89     2184   3801   2764    -68    276    297       O  
ATOM   2244  CB  SER B  89      -5.129  -7.793  16.438  1.00 30.92           C  
ANISOU 2244  CB  SER B  89     3377   5069   3305    134    386    230       C  
ATOM   2245  OG  SER B  89      -4.014  -7.271  15.733  1.00 30.61           O  
ANISOU 2245  OG  SER B  89     3303   5106   3221    156    556    351       O  
ATOM   2246  N   GLU B  90      -4.061  -5.161  17.913  1.00 25.73           N  
ANISOU 2246  N   GLU B  90     2532   4242   3003    -60    465    521       N  
ATOM   2247  CA  GLU B  90      -3.163  -4.573  18.900  1.00 31.69           C  
ANISOU 2247  CA  GLU B  90     3167   4915   3961   -158    493    569       C  
ATOM   2248  C   GLU B  90      -3.932  -3.746  19.920  1.00 32.40           C  
ANISOU 2248  C   GLU B  90     3276   4866   4169   -227    376    580       C  
ATOM   2249  O   GLU B  90      -3.593  -3.760  21.110  1.00 28.15           O  
ANISOU 2249  O   GLU B  90     2669   4249   3780   -288    322    528       O  
ATOM   2250  CB  GLU B  90      -2.086  -3.722  18.230  1.00 36.55           C  
ANISOU 2250  CB  GLU B  90     3723   5572   4594   -204    655    725       C  
ATOM   2251  CG  GLU B  90      -1.190  -3.008  19.241  1.00 41.72           C  
ANISOU 2251  CG  GLU B  90     4242   6134   5474   -332    662    769       C  
ATOM   2252  CD  GLU B  90       0.150  -2.599  18.670  1.00 60.08           C  
ANISOU 2252  CD  GLU B  90     6445   8532   7850   -389    839    886       C  
ATOM   2253  OE1 GLU B  90       1.080  -2.347  19.467  1.00 65.75           O  
ANISOU 2253  OE1 GLU B  90     7009   9215   8756   -488    840    886       O  
ATOM   2254  OE2 GLU B  90       0.277  -2.528  17.428  1.00 67.38           O  
ANISOU 2254  OE2 GLU B  90     7421   9557   8621   -337    978    977       O  
ATOM   2255  N   THR B  91      -4.977  -3.034  19.484  1.00 29.38           N  
ANISOU 2255  N   THR B  91     2990   4458   3714   -203    330    640       N  
ATOM   2256  CA  THR B  91      -5.799  -2.290  20.438  1.00 31.00           C  
ANISOU 2256  CA  THR B  91     3218   4535   4024   -239    227    635       C  
ATOM   2257  C   THR B  91      -6.389  -3.218  21.499  1.00 31.69           C  
ANISOU 2257  C   THR B  91     3285   4598   4156   -235    123    480       C  
ATOM   2258  O   THR B  91      -6.359  -2.905  22.696  1.00 26.87           O  
ANISOU 2258  O   THR B  91     2648   3887   3674   -291     76    446       O  
ATOM   2259  CB  THR B  91      -6.910  -1.528  19.714  1.00 29.13           C  
ANISOU 2259  CB  THR B  91     3082   4296   3690   -174    188    717       C  
ATOM   2260  OG1 THR B  91      -6.351  -0.751  18.655  1.00 28.52           O  
ANISOU 2260  OG1 THR B  91     3051   4242   3545   -171    296    879       O  
ATOM   2261  CG2 THR B  91      -7.623  -0.583  20.674  1.00 23.96           C  
ANISOU 2261  CG2 THR B  91     2446   3497   3159   -196    110    725       C  
ATOM   2262  N   ILE B  92      -6.899  -4.381  21.085  1.00 29.65           N  
ANISOU 2262  N   ILE B  92     3051   4426   3790   -175     90    383       N  
ATOM   2263  CA  ILE B  92      -7.411  -5.345  22.056  1.00 19.35           C  
ANISOU 2263  CA  ILE B  92     1735   3087   2529   -186     12    250       C  
ATOM   2264  C   ILE B  92      -6.287  -5.854  22.946  1.00 20.05           C  
ANISOU 2264  C   ILE B  92     1763   3137   2717   -223     36    210       C  
ATOM   2265  O   ILE B  92      -6.419  -5.900  24.176  1.00 27.27           O  
ANISOU 2265  O   ILE B  92     2666   3972   3723   -262    -20    164       O  
ATOM   2266  CB  ILE B  92      -8.131  -6.504  21.344  1.00 21.23           C  
ANISOU 2266  CB  ILE B  92     2019   3408   2639   -134    -28    153       C  
ATOM   2267  CG1 ILE B  92      -9.340  -5.981  20.589  1.00 19.28           C  
ANISOU 2267  CG1 ILE B  92     1813   3213   2302    -95    -90    184       C  
ATOM   2268  CG2 ILE B  92      -8.550  -7.561  22.351  1.00 17.76           C  
ANISOU 2268  CG2 ILE B  92     1576   2913   2258   -164    -87     31       C  
ATOM   2269  CD1 ILE B  92      -9.996  -7.032  19.730  1.00 26.54           C  
ANISOU 2269  CD1 ILE B  92     2775   4224   3084    -56   -145     83       C  
ATOM   2270  N   LEU B  93      -5.157  -6.236  22.339  1.00 21.03           N  
ANISOU 2270  N   LEU B  93     1845   3328   2819   -199    121    228       N  
ATOM   2271  CA  LEU B  93      -4.031  -6.753  23.116  1.00 29.56           C  
ANISOU 2271  CA  LEU B  93     2845   4391   3997   -211    134    193       C  
ATOM   2272  C   LEU B  93      -3.537  -5.739  24.148  1.00 29.32           C  
ANISOU 2272  C   LEU B  93     2750   4278   4111   -299    103    243       C  
ATOM   2273  O   LEU B  93      -3.137  -6.116  25.258  1.00 23.04           O  
ANISOU 2273  O   LEU B  93     1920   3438   3396   -317     42    187       O  
ATOM   2274  CB  LEU B  93      -2.888  -7.154  22.183  1.00 30.89           C  
ANISOU 2274  CB  LEU B  93     2951   4662   4123   -158    251    219       C  
ATOM   2275  CG  LEU B  93      -1.780  -7.900  22.927  1.00 32.08           C  
ANISOU 2275  CG  LEU B  93     3004   4813   4371   -134    250    168       C  
ATOM   2276  CD1 LEU B  93      -2.368  -9.157  23.529  1.00 35.17           C  
ANISOU 2276  CD1 LEU B  93     3480   5150   4734    -80    165     48       C  
ATOM   2277  CD2 LEU B  93      -0.623  -8.251  22.006  1.00 37.57           C  
ANISOU 2277  CD2 LEU B  93     3612   5625   5038    -65    385    193       C  
ATOM   2278  N   ASN B  94      -3.558  -4.449  23.801  1.00 21.92           N  
ANISOU 2278  N   ASN B  94     1814   3312   3203   -355    137    346       N  
ATOM   2279  CA  ASN B  94      -3.096  -3.416  24.725  1.00 24.26           C  
ANISOU 2279  CA  ASN B  94     2068   3509   3641   -453    102    380       C  
ATOM   2280  C   ASN B  94      -3.911  -3.409  26.019  1.00 22.46           C  
ANISOU 2280  C   ASN B  94     1902   3185   3447   -463    -12    295       C  
ATOM   2281  O   ASN B  94      -3.353  -3.227  27.110  1.00 22.90           O  
ANISOU 2281  O   ASN B  94     1922   3183   3595   -518    -72    258       O  
ATOM   2282  CB  ASN B  94      -3.125  -2.052  24.024  1.00 20.91           C  
ANISOU 2282  CB  ASN B  94     1670   3039   3234   -505    165    510       C  
ATOM   2283  CG  ASN B  94      -1.871  -1.812  23.168  1.00 31.81           C  
ANISOU 2283  CG  ASN B  94     2951   4494   4642   -549    294    611       C  
ATOM   2284  OD1 ASN B  94      -0.987  -2.666  23.103  1.00 33.78           O  
ANISOU 2284  OD1 ASN B  94     3095   4839   4899   -524    335    572       O  
ATOM   2285  ND2 ASN B  94      -1.797  -0.657  22.511  1.00 35.70           N  
ANISOU 2285  ND2 ASN B  94     3476   4938   5149   -606    369    746       N  
ATOM   2286  N   LEU B  95      -5.224  -3.658  25.916  1.00 21.22           N  
ANISOU 2286  N   LEU B  95     1832   3024   3207   -408    -42    260       N  
ATOM   2287  CA  LEU B  95      -6.097  -3.723  27.088  1.00 26.39           C  
ANISOU 2287  CA  LEU B  95     2541   3606   3880   -410   -120    184       C  
ATOM   2288  C   LEU B  95      -5.845  -4.978  27.920  1.00 27.04           C  
ANISOU 2288  C   LEU B  95     2617   3703   3954   -395   -159     95       C  
ATOM   2289  O   LEU B  95      -5.803  -4.912  29.156  1.00 23.46           O  
ANISOU 2289  O   LEU B  95     2187   3187   3542   -421   -216     51       O  
ATOM   2290  CB  LEU B  95      -7.560  -3.668  26.642  1.00 26.43           C  
ANISOU 2290  CB  LEU B  95     2603   3626   3811   -357   -129    179       C  
ATOM   2291  CG  LEU B  95      -8.114  -2.282  26.300  1.00 31.96           C  
ANISOU 2291  CG  LEU B  95     3341   4269   4532   -347   -123    259       C  
ATOM   2292  CD1 LEU B  95      -9.481  -2.410  25.657  1.00 38.12           C  
ANISOU 2292  CD1 LEU B  95     4144   5108   5231   -271   -145    256       C  
ATOM   2293  CD2 LEU B  95      -8.207  -1.430  27.555  1.00 26.73           C  
ANISOU 2293  CD2 LEU B  95     2714   3482   3962   -382   -159    230       C  
ATOM   2294  N   LEU B  96      -5.687  -6.130  27.262  1.00 18.54           N  
ANISOU 2294  N   LEU B  96     1530   2700   2814   -346   -131     69       N  
ATOM   2295  CA  LEU B  96      -5.387  -7.365  27.977  1.00 23.23           C  
ANISOU 2295  CA  LEU B  96     2136   3285   3403   -319   -164     -2       C  
ATOM   2296  C   LEU B  96      -4.039  -7.294  28.670  1.00 21.75           C  
ANISOU 2296  C   LEU B  96     1877   3091   3296   -331   -191      7       C  
ATOM   2297  O   LEU B  96      -3.832  -7.952  29.691  1.00 26.39           O  
ANISOU 2297  O   LEU B  96     2492   3645   3892   -314   -251    -38       O  
ATOM   2298  CB  LEU B  96      -5.398  -8.559  27.010  1.00 20.33           C  
ANISOU 2298  CB  LEU B  96     1787   2979   2960   -256   -124    -38       C  
ATOM   2299  CG  LEU B  96      -6.584  -8.704  26.067  1.00 25.28           C  
ANISOU 2299  CG  LEU B  96     2466   3642   3499   -245   -113    -56       C  
ATOM   2300  CD1 LEU B  96      -6.461  -9.979  25.224  1.00 24.82           C  
ANISOU 2300  CD1 LEU B  96     2444   3624   3361   -188    -88   -121       C  
ATOM   2301  CD2 LEU B  96      -7.880  -8.696  26.879  1.00 25.07           C  
ANISOU 2301  CD2 LEU B  96     2486   3560   3481   -285   -163    -92       C  
ATOM   2302  N   GLY B  97      -3.114  -6.497  28.139  1.00 22.86           N  
ANISOU 2302  N   GLY B  97     1923   3269   3496   -364   -152     69       N  
ATOM   2303  CA  GLY B  97      -1.783  -6.408  28.691  1.00 24.59           C  
ANISOU 2303  CA  GLY B  97     2030   3504   3808   -386   -184     75       C  
ATOM   2304  C   GLY B  97      -1.431  -5.144  29.445  1.00 23.43           C  
ANISOU 2304  C   GLY B  97     1851   3293   3759   -491   -243     95       C  
ATOM   2305  O   GLY B  97      -0.248  -4.942  29.748  1.00 25.88           O  
ANISOU 2305  O   GLY B  97     2038   3632   4163   -531   -275    104       O  
ATOM   2306  N   ASP B  98      -2.394  -4.282  29.767  1.00 24.44           N  
ANISOU 2306  N   ASP B  98     2079   3332   3875   -534   -264     94       N  
ATOM   2307  CA  ASP B  98      -2.039  -3.026  30.402  1.00 22.78           C  
ANISOU 2307  CA  ASP B  98     1860   3037   3760   -634   -316    101       C  
ATOM   2308  C   ASP B  98      -1.666  -3.269  31.865  1.00 26.29           C  
ANISOU 2308  C   ASP B  98     2320   3449   4220   -645   -443     17       C  
ATOM   2309  O   ASP B  98      -1.706  -4.398  32.377  1.00 19.97           O  
ANISOU 2309  O   ASP B  98     1544   2689   3355   -569   -481    -28       O  
ATOM   2310  CB  ASP B  98      -3.158  -1.986  30.249  1.00 25.01           C  
ANISOU 2310  CB  ASP B  98     2255   3223   4026   -651   -292    125       C  
ATOM   2311  CG  ASP B  98      -4.516  -2.441  30.816  1.00 27.40           C  
ANISOU 2311  CG  ASP B  98     2674   3502   4234   -577   -314     62       C  
ATOM   2312  OD1 ASP B  98      -4.576  -3.398  31.625  1.00 21.74           O  
ANISOU 2312  OD1 ASP B  98     1982   2809   3471   -542   -360     -3       O  
ATOM   2313  OD2 ASP B  98      -5.540  -1.813  30.433  1.00 21.71           O  
ANISOU 2313  OD2 ASP B  98     2018   2740   3490   -553   -279     88       O  
ATOM   2314  N   ALA B  99      -1.262  -2.188  32.532  1.00 24.53           N  
ANISOU 2314  N   ALA B  99     2095   3147   4079   -743   -514     -3       N  
ATOM   2315  CA  ALA B  99      -0.736  -2.305  33.887  1.00 22.35           C  
ANISOU 2315  CA  ALA B  99     1829   2854   3809   -761   -655    -87       C  
ATOM   2316  C   ALA B  99      -1.772  -2.910  34.832  1.00 23.69           C  
ANISOU 2316  C   ALA B  99     2161   2993   3845   -676   -689   -152       C  
ATOM   2317  O   ALA B  99      -1.449  -3.785  35.643  1.00 25.37           O  
ANISOU 2317  O   ALA B  99     2390   3248   4002   -622   -768   -191       O  
ATOM   2318  CB  ALA B  99      -0.271  -0.937  34.379  1.00 21.79           C  
ANISOU 2318  CB  ALA B  99     1756   2681   3842   -893   -730   -116       C  
ATOM   2319  N   ARG B 100      -3.028  -2.491  34.711  1.00 20.96           N  
ANISOU 2319  N   ARG B 100     1932   2584   3448   -656   -622   -152       N  
ATOM   2320  CA  ARG B 100      -4.080  -3.026  35.571  1.00 24.72           C  
ANISOU 2320  CA  ARG B 100     2543   3042   3806   -586   -623   -204       C  
ATOM   2321  C   ARG B 100      -4.229  -4.548  35.403  1.00 27.06           C  
ANISOU 2321  C   ARG B 100     2833   3418   4030   -510   -592   -187       C  
ATOM   2322  O   ARG B 100      -4.245  -5.305  36.392  1.00 17.33           O  
ANISOU 2322  O   ARG B 100     1675   2188   2720   -469   -643   -222       O  
ATOM   2323  CB  ARG B 100      -5.385  -2.287  35.254  1.00 17.55           C  
ANISOU 2323  CB  ARG B 100     1712   2073   2881   -569   -540   -198       C  
ATOM   2324  CG  ARG B 100      -6.601  -2.919  35.852  1.00 16.92           C  
ANISOU 2324  CG  ARG B 100     1729   2003   2696   -501   -497   -232       C  
ATOM   2325  CD  ARG B 100      -7.855  -2.104  35.577  1.00 17.90           C  
ANISOU 2325  CD  ARG B 100     1898   2083   2822   -469   -424   -231       C  
ATOM   2326  NE  ARG B 100      -8.973  -2.829  36.151  1.00 23.42           N  
ANISOU 2326  NE  ARG B 100     2652   2815   3431   -416   -369   -260       N  
ATOM   2327  CZ  ARG B 100     -10.253  -2.528  35.976  1.00 24.45           C  
ANISOU 2327  CZ  ARG B 100     2790   2950   3552   -368   -293   -261       C  
ATOM   2328  NH1 ARG B 100     -10.593  -1.491  35.232  1.00 21.02           N  
ANISOU 2328  NH1 ARG B 100     2329   2477   3180   -347   -275   -232       N  
ATOM   2329  NH2 ARG B 100     -11.191  -3.276  36.556  1.00 16.34           N  
ANISOU 2329  NH2 ARG B 100     1790   1965   2454   -340   -233   -285       N  
ATOM   2330  N   ARG B 101      -4.303  -5.020  34.152  1.00 16.70           N  
ANISOU 2330  N   ARG B 101     1448   2161   2736   -487   -511   -134       N  
ATOM   2331  CA  ARG B 101      -4.437  -6.459  33.905  1.00 21.27           C  
ANISOU 2331  CA  ARG B 101     2036   2789   3256   -419   -481   -131       C  
ATOM   2332  C   ARG B 101      -3.153  -7.229  34.235  1.00 24.73           C  
ANISOU 2332  C   ARG B 101     2412   3268   3715   -381   -551   -133       C  
ATOM   2333  O   ARG B 101      -3.215  -8.381  34.681  1.00 25.60           O  
ANISOU 2333  O   ARG B 101     2587   3376   3766   -316   -568   -145       O  
ATOM   2334  CB  ARG B 101      -4.845  -6.707  32.451  1.00 23.40           C  
ANISOU 2334  CB  ARG B 101     2259   3107   3524   -402   -388    -93       C  
ATOM   2335  CG  ARG B 101      -6.301  -7.164  32.268  1.00 22.99           C  
ANISOU 2335  CG  ARG B 101     2284   3046   3405   -385   -336   -111       C  
ATOM   2336  CD  ARG B 101      -7.325  -6.172  32.820  1.00 19.89           C  
ANISOU 2336  CD  ARG B 101     1944   2604   3007   -409   -330   -123       C  
ATOM   2337  NE  ARG B 101      -7.177  -4.843  32.225  1.00 27.18           N  
ANISOU 2337  NE  ARG B 101     2828   3511   3989   -434   -321    -84       N  
ATOM   2338  CZ  ARG B 101      -8.144  -3.930  32.202  1.00 24.92           C  
ANISOU 2338  CZ  ARG B 101     2575   3187   3708   -427   -298    -79       C  
ATOM   2339  NH1 ARG B 101      -9.337  -4.204  32.729  1.00 16.47           N  
ANISOU 2339  NH1 ARG B 101     1551   2116   2592   -398   -274   -117       N  
ATOM   2340  NH2 ARG B 101      -7.924  -2.752  31.644  1.00 19.24           N  
ANISOU 2340  NH2 ARG B 101     1840   2428   3045   -444   -290    -30       N  
ATOM   2341  N   THR B 102      -1.984  -6.623  33.997  1.00 19.54           N  
ANISOU 2341  N   THR B 102     1626   2648   3151   -419   -589   -116       N  
ATOM   2342  CA  THR B 102      -0.718  -7.273  34.327  1.00 18.77           C  
ANISOU 2342  CA  THR B 102     1432   2609   3091   -371   -666   -119       C  
ATOM   2343  C   THR B 102      -0.610  -7.539  35.825  1.00 26.90           C  
ANISOU 2343  C   THR B 102     2555   3605   4060   -345   -799   -164       C  
ATOM   2344  O   THR B 102      -0.280  -8.651  36.246  1.00 22.83           O  
ANISOU 2344  O   THR B 102     2069   3108   3498   -248   -844   -162       O  
ATOM   2345  CB  THR B 102       0.448  -6.410  33.850  1.00 28.94           C  
ANISOU 2345  CB  THR B 102     2536   3950   4509   -444   -678    -93       C  
ATOM   2346  OG1 THR B 102       0.403  -6.303  32.422  1.00 34.61           O  
ANISOU 2346  OG1 THR B 102     3183   4712   5254   -449   -539    -36       O  
ATOM   2347  CG2 THR B 102       1.756  -7.033  34.242  1.00 23.12           C  
ANISOU 2347  CG2 THR B 102     1664   3294   3826   -387   -770   -101       C  
ATOM   2348  N   ARG B 103      -0.887  -6.524  36.650  1.00 22.33           N  
ANISOU 2348  N   ARG B 103     2044   2972   3470   -420   -862   -204       N  
ATOM   2349  CA  ARG B 103      -0.900  -6.734  38.091  1.00 20.14           C  
ANISOU 2349  CA  ARG B 103     1890   2668   3096   -389   -982   -251       C  
ATOM   2350  C   ARG B 103      -2.002  -7.704  38.501  1.00 23.42           C  
ANISOU 2350  C   ARG B 103     2477   3044   3377   -317   -915   -240       C  
ATOM   2351  O   ARG B 103      -1.816  -8.518  39.416  1.00 25.01           O  
ANISOU 2351  O   ARG B 103     2772   3246   3487   -245   -987   -238       O  
ATOM   2352  CB  ARG B 103      -1.064  -5.399  38.810  1.00 24.00           C  
ANISOU 2352  CB  ARG B 103     2439   3095   3587   -481  -1048   -314       C  
ATOM   2353  CG  ARG B 103       0.106  -4.463  38.609  1.00 36.47           C  
ANISOU 2353  CG  ARG B 103     3856   4692   5307   -581  -1138   -332       C  
ATOM   2354  CD  ARG B 103       1.360  -4.955  39.320  1.00 35.12           C  
ANISOU 2354  CD  ARG B 103     3593   4603   5150   -549  -1309   -355       C  
ATOM   2355  NE  ARG B 103       2.414  -3.945  39.269  1.00 45.71           N  
ANISOU 2355  NE  ARG B 103     4795   5964   6608   -661  -1367   -379       N  
ATOM   2356  CZ  ARG B 103       3.465  -3.925  40.083  1.00 51.74           C  
ANISOU 2356  CZ  ARG B 103     5504   6794   7362   -662  -1505   -419       C  
ATOM   2357  NH1 ARG B 103       3.603  -4.864  41.012  1.00 47.07           N  
ANISOU 2357  NH1 ARG B 103     4980   6247   6659   -546  -1636   -436       N  
ATOM   2358  NH2 ARG B 103       4.373  -2.963  39.976  1.00 55.33           N  
ANISOU 2358  NH2 ARG B 103     5840   7268   7914   -779  -1520   -438       N  
ATOM   2359  N   PHE B 104      -3.156  -7.637  37.837  1.00 21.30           N  
ANISOU 2359  N   PHE B 104     2251   2746   3098   -338   -780   -225       N  
ATOM   2360  CA  PHE B 104      -4.292  -8.454  38.246  1.00 20.25           C  
ANISOU 2360  CA  PHE B 104     2261   2575   2858   -302   -706   -217       C  
ATOM   2361  C   PHE B 104      -3.970  -9.942  38.114  1.00 29.43           C  
ANISOU 2361  C   PHE B 104     3445   3743   3994   -225   -703   -179       C  
ATOM   2362  O   PHE B 104      -4.013 -10.693  39.096  1.00 25.81           O  
ANISOU 2362  O   PHE B 104     3114   3253   3441   -175   -741   -166       O  
ATOM   2363  CB  PHE B 104      -5.530  -8.078  37.422  1.00 24.44           C  
ANISOU 2363  CB  PHE B 104     2784   3093   3408   -343   -578   -213       C  
ATOM   2364  CG  PHE B 104      -6.784  -8.801  37.843  1.00 27.07           C  
ANISOU 2364  CG  PHE B 104     3232   3399   3656   -334   -493   -209       C  
ATOM   2365  CD1 PHE B 104      -7.549  -8.340  38.910  1.00 32.38           C  
ANISOU 2365  CD1 PHE B 104     4011   4043   4248   -342   -469   -236       C  
ATOM   2366  CD2 PHE B 104      -7.197  -9.946  37.175  1.00 23.72           C  
ANISOU 2366  CD2 PHE B 104     2805   2973   3233   -323   -428   -183       C  
ATOM   2367  CE1 PHE B 104      -8.716  -9.004  39.304  1.00 28.89           C  
ANISOU 2367  CE1 PHE B 104     3653   3587   3738   -347   -367   -222       C  
ATOM   2368  CE2 PHE B 104      -8.355 -10.610  37.564  1.00 26.69           C  
ANISOU 2368  CE2 PHE B 104     3270   3319   3552   -344   -345   -176       C  
ATOM   2369  CZ  PHE B 104      -9.111 -10.141  38.634  1.00 22.13           C  
ANISOU 2369  CZ  PHE B 104     2778   2728   2903   -359   -307   -188       C  
ATOM   2370  N   PHE B 105      -3.615 -10.388  36.909  1.00 23.62           N  
ANISOU 2370  N   PHE B 105     2603   3039   3333   -204   -657   -160       N  
ATOM   2371  CA  PHE B 105      -3.308 -11.806  36.760  1.00 29.39           C  
ANISOU 2371  CA  PHE B 105     3372   3750   4044   -116   -651   -137       C  
ATOM   2372  C   PHE B 105      -1.959 -12.174  37.356  1.00 29.58           C  
ANISOU 2372  C   PHE B 105     3356   3805   4080    -26   -776   -125       C  
ATOM   2373  O   PHE B 105      -1.758 -13.340  37.718  1.00 26.75           O  
ANISOU 2373  O   PHE B 105     3086   3402   3677     69   -799    -98       O  
ATOM   2374  CB  PHE B 105      -3.403 -12.205  35.290  1.00 24.93           C  
ANISOU 2374  CB  PHE B 105     2730   3209   3534   -108   -559   -139       C  
ATOM   2375  CG  PHE B 105      -4.802 -12.131  34.765  1.00 22.23           C  
ANISOU 2375  CG  PHE B 105     2440   2840   3165   -179   -461   -152       C  
ATOM   2376  CD1 PHE B 105      -5.725 -13.106  35.103  1.00 27.90           C  
ANISOU 2376  CD1 PHE B 105     3288   3485   3828   -188   -417   -153       C  
ATOM   2377  CD2 PHE B 105      -5.213 -11.075  33.975  1.00 15.89           C  
ANISOU 2377  CD2 PHE B 105     1555   2085   2399   -239   -418   -157       C  
ATOM   2378  CE1 PHE B 105      -7.021 -13.043  34.641  1.00 27.87           C  
ANISOU 2378  CE1 PHE B 105     3299   3475   3817   -262   -339   -170       C  
ATOM   2379  CE2 PHE B 105      -6.511 -11.007  33.503  1.00 24.05           C  
ANISOU 2379  CE2 PHE B 105     2617   3111   3411   -288   -349   -169       C  
ATOM   2380  CZ  PHE B 105      -7.419 -11.993  33.841  1.00 28.21           C  
ANISOU 2380  CZ  PHE B 105     3242   3583   3893   -304   -313   -182       C  
ATOM   2381  N   GLY B 106      -1.048 -11.206  37.490  1.00 26.77           N  
ANISOU 2381  N   GLY B 106     2867   3517   3790    -55   -864   -141       N  
ATOM   2382  CA  GLY B 106       0.181 -11.458  38.223  1.00 24.94           C  
ANISOU 2382  CA  GLY B 106     2577   3330   3568     23  -1014   -138       C  
ATOM   2383  C   GLY B 106      -0.075 -11.837  39.670  1.00 30.06           C  
ANISOU 2383  C   GLY B 106     3414   3930   4079     68  -1110   -132       C  
ATOM   2384  O   GLY B 106       0.508 -12.797  40.183  1.00 26.86           O  
ANISOU 2384  O   GLY B 106     3054   3520   3630    191  -1192    -99       O  
ATOM   2385  N   ASP B 107      -0.939 -11.076  40.357  1.00 25.82           N  
ANISOU 2385  N   ASP B 107     2995   3354   3461    -17  -1098   -162       N  
ATOM   2386  CA  ASP B 107      -1.353 -11.468  41.708  1.00 25.02           C  
ANISOU 2386  CA  ASP B 107     3104   3209   3195     26  -1150   -150       C  
ATOM   2387  C   ASP B 107      -2.022 -12.834  41.690  1.00 31.43           C  
ANISOU 2387  C   ASP B 107     4062   3943   3938     91  -1049    -82       C  
ATOM   2388  O   ASP B 107      -1.797 -13.660  42.579  1.00 33.30           O  
ANISOU 2388  O   ASP B 107     4439   4146   4066    184  -1116    -34       O  
ATOM   2389  CB  ASP B 107      -2.328 -10.450  42.304  1.00 25.75           C  
ANISOU 2389  CB  ASP B 107     3301   3273   3210    -66  -1105   -199       C  
ATOM   2390  CG  ASP B 107      -1.646  -9.177  42.781  1.00 41.96           C  
ANISOU 2390  CG  ASP B 107     5290   5364   5287   -122  -1244   -277       C  
ATOM   2391  OD1 ASP B 107      -0.433  -9.214  43.082  1.00 44.89           O  
ANISOU 2391  OD1 ASP B 107     5572   5794   5690    -85  -1411   -288       O  
ATOM   2392  OD2 ASP B 107      -2.337  -8.137  42.871  1.00 43.11           O  
ANISOU 2392  OD2 ASP B 107     5475   5478   5428   -203  -1191   -331       O  
HETATM 2393  N   MSE B 108      -2.868 -13.077  40.698  1.00 23.65           N  
ANISOU 2393  N   MSE B 108     3055   2920   3010     38   -894    -78       N  
HETATM 2394  CA  MSE B 108      -3.647 -14.302  40.631  1.00 28.08           C  
ANISOU 2394  CA  MSE B 108     3755   3389   3524     58   -789    -28       C  
HETATM 2395  C   MSE B 108      -2.731 -15.502  40.461  1.00 30.82           C  
ANISOU 2395  C   MSE B 108     4115   3701   3894    190   -848     15       C  
HETATM 2396  O   MSE B 108      -2.787 -16.461  41.227  1.00 33.40           O  
ANISOU 2396  O   MSE B 108     4614   3945   4130    261   -865     77       O  
HETATM 2397  CB  MSE B 108      -4.642 -14.197  39.489  1.00 33.38           C  
ANISOU 2397  CB  MSE B 108     4364   4049   4268    -35   -645    -53       C  
HETATM 2398  CG  MSE B 108      -5.249 -15.488  39.083  1.00 43.78           C  
ANISOU 2398  CG  MSE B 108     5777   5273   5586    -31   -553    -24       C  
HETATM 2399 SE   MSE B 108      -7.169 -15.480  39.344  1.00 42.00          SE  
ANISOU 2399 SE   MSE B 108     5648   4998   5310   -176   -392    -19      SE  
HETATM 2400  CE  MSE B 108      -7.654 -13.619  39.066  1.00 30.46           C  
ANISOU 2400  CE  MSE B 108     4033   3653   3885   -250   -377    -83       C  
ATOM   2401  N   PHE B 109      -1.844 -15.421  39.474  1.00 35.75           N  
ANISOU 2401  N   PHE B 109     4558   4388   4638    234   -874    -13       N  
ATOM   2402  CA  PHE B 109      -0.866 -16.476  39.275  1.00 38.95           C  
ANISOU 2402  CA  PHE B 109     4948   4773   5077    388   -929     16       C  
ATOM   2403  C   PHE B 109       0.164 -16.521  40.399  1.00 55.51           C  
ANISOU 2403  C   PHE B 109     7055   6912   7123    502  -1108     48       C  
ATOM   2404  O   PHE B 109       0.986 -17.446  40.421  1.00 55.22           O  
ANISOU 2404  O   PHE B 109     7019   6857   7105    662  -1173     84       O  
ATOM   2405  CB  PHE B 109      -0.200 -16.303  37.911  1.00 24.75           C  
ANISOU 2405  CB  PHE B 109     2939   3052   3411    410   -887    -26       C  
ATOM   2406  CG  PHE B 109      -1.173 -16.280  36.772  1.00 28.01           C  
ANISOU 2406  CG  PHE B 109     3354   3436   3852    313   -736    -61       C  
ATOM   2407  CD1 PHE B 109      -2.431 -16.857  36.904  1.00 22.54           C  
ANISOU 2407  CD1 PHE B 109     2837   2631   3097    246   -651    -53       C  
ATOM   2408  CD2 PHE B 109      -0.848 -15.662  35.573  1.00 23.84           C  
ANISOU 2408  CD2 PHE B 109     2648   3002   3408    283   -680    -97       C  
ATOM   2409  CE1 PHE B 109      -3.336 -16.825  35.857  1.00 22.80           C  
ANISOU 2409  CE1 PHE B 109     2854   2654   3156    155   -539    -94       C  
ATOM   2410  CE2 PHE B 109      -1.752 -15.618  34.536  1.00 24.64           C  
ANISOU 2410  CE2 PHE B 109     2761   3089   3511    205   -563   -129       C  
ATOM   2411  CZ  PHE B 109      -2.997 -16.206  34.675  1.00 23.28           C  
ANISOU 2411  CZ  PHE B 109     2752   2813   3282    143   -504   -134       C  
ATOM   2412  N   GLY B 110       0.128 -15.544  41.316  1.00 75.84           N  
ANISOU 2412  N   GLY B 110     8579  12202   8035   -912  -1376   -302       N  
ATOM   2413  CA  GLY B 110       0.791 -15.574  42.612  1.00 81.04           C  
ANISOU 2413  CA  GLY B 110     9263  12985   8542  -1098  -1537   -168       C  
ATOM   2414  C   GLY B 110       2.303 -15.569  42.582  1.00 79.79           C  
ANISOU 2414  C   GLY B 110     8908  12864   8544  -1106  -1726     27       C  
ATOM   2415  O   GLY B 110       2.945 -16.463  43.148  1.00 81.79           O  
ANISOU 2415  O   GLY B 110     9072  13188   8816  -1108  -1892    309       O  
ATOM   2416  N   THR B 111       2.897 -14.548  41.975  1.00 72.05           N  
ANISOU 2416  N   THR B 111     7852  11833   7693  -1119  -1699   -111       N  
ATOM   2417  CA  THR B 111       4.244 -14.721  41.470  1.00 70.82           C  
ANISOU 2417  CA  THR B 111     7450  11665   7792  -1042  -1824     86       C  
ATOM   2418  C   THR B 111       5.157 -13.535  41.756  1.00 68.06           C  
ANISOU 2418  C   THR B 111     7063  11350   7448  -1214  -1897    -10       C  
ATOM   2419  O   THR B 111       4.752 -12.473  42.246  1.00 60.76           O  
ANISOU 2419  O   THR B 111     6305  10435   6344  -1388  -1835   -255       O  
ATOM   2420  CB  THR B 111       4.213 -14.983  39.956  1.00 59.83           C  
ANISOU 2420  CB  THR B 111     5913  10148   6672   -801  -1696     85       C  
ATOM   2421  OG1 THR B 111       3.094 -14.303  39.369  1.00 54.58           O  
ANISOU 2421  OG1 THR B 111     5413   9380   5944   -770  -1484   -205       O  
ATOM   2422  CG2 THR B 111       4.126 -16.479  39.669  1.00 54.35           C  
ANISOU 2422  CG2 THR B 111     5127   9413   6111   -598  -1710    340       C  
ATOM   2423  N   ARG B 112       6.430 -13.781  41.479  1.00 73.86           N  
ANISOU 2423  N   ARG B 112     7563  12089   8411  -1159  -2022    198       N  
ATOM   2424  CA  ARG B 112       7.353 -12.784  40.977  1.00 81.97           C  
ANISOU 2424  CA  ARG B 112     8458  13082   9604  -1213  -2030    124       C  
ATOM   2425  C   ARG B 112       7.712 -13.060  39.534  1.00 85.53           C  
ANISOU 2425  C   ARG B 112     8705  13411  10383   -981  -1913    192       C  
ATOM   2426  O   ARG B 112       8.071 -12.132  38.803  1.00 91.87           O  
ANISOU 2426  O   ARG B 112     9436  14154  11315  -1000  -1831     64       O  
ATOM   2427  CB  ARG B 112       8.633 -12.757  41.822  1.00 89.32           C  
ANISOU 2427  CB  ARG B 112     9260  14125  10553  -1348  -2250    305       C  
ATOM   2428  N   ALA B 113       7.592 -14.325  39.113  1.00 78.24           N  
ANISOU 2428  N   ALA B 113     7694  12439   9596   -763  -1883    388       N  
ATOM   2429  CA  ALA B 113       7.847 -14.715  37.733  1.00 68.03           C  
ANISOU 2429  CA  ALA B 113     6226  11014   8608   -520  -1724    446       C  
ATOM   2430  C   ALA B 113       6.873 -14.023  36.788  1.00 57.68           C  
ANISOU 2430  C   ALA B 113     5089   9568   7260   -459  -1481    165       C  
ATOM   2431  O   ALA B 113       5.663 -14.019  37.023  1.00 60.09           O  
ANISOU 2431  O   ALA B 113     5625   9847   7359   -476  -1408     11       O  
ATOM   2432  CB  ALA B 113       7.731 -16.235  37.585  1.00 64.92           C  
ANISOU 2432  CB  ALA B 113     5769  10550   8347   -304  -1708    677       C  
ATOM   2433  N   GLU B 114       7.404 -13.441  35.713  1.00 48.85           N  
ANISOU 2433  N   GLU B 114     3881   8326   6354   -380  -1336    106       N  
ATOM   2434  CA  GLU B 114       6.567 -12.758  34.736  1.00 43.54           C  
ANISOU 2434  CA  GLU B 114     3389   7483   5670   -312  -1102   -128       C  
ATOM   2435  C   GLU B 114       5.898 -13.763  33.804  1.00 40.96           C  
ANISOU 2435  C   GLU B 114     3144   6995   5423    -69   -919   -104       C  
ATOM   2436  O   GLU B 114       6.520 -14.734  33.358  1.00 35.78           O  
ANISOU 2436  O   GLU B 114     2344   6287   4965     89   -883     72       O  
ATOM   2437  CB  GLU B 114       7.391 -11.756  33.927  1.00 36.10           C  
ANISOU 2437  CB  GLU B 114     2331   6478   4908   -339  -1018   -179       C  
ATOM   2438  N   TYR B 115       4.613 -13.530  33.533  1.00 35.69           N  
ANISOU 2438  N   TYR B 115     2705   6245   4612    -49   -800   -286       N  
ATOM   2439  CA  TYR B 115       3.833 -14.309  32.588  1.00 39.07           C  
ANISOU 2439  CA  TYR B 115     3242   6523   5080    138   -630   -305       C  
ATOM   2440  C   TYR B 115       3.555 -13.477  31.342  1.00 33.38           C  
ANISOU 2440  C   TYR B 115     2597   5671   4416    186   -448   -447       C  
ATOM   2441  O   TYR B 115       3.331 -12.266  31.430  1.00 38.89           O  
ANISOU 2441  O   TYR B 115     3350   6372   5054     70   -447   -581       O  
ATOM   2442  CB  TYR B 115       2.517 -14.778  33.220  1.00 37.53           C  
ANISOU 2442  CB  TYR B 115     3229   6348   4684    117   -651   -369       C  
ATOM   2443  CG  TYR B 115       2.682 -15.943  34.166  1.00 32.91           C  
ANISOU 2443  CG  TYR B 115     2589   5853   4062    117   -790   -183       C  
ATOM   2444  CD1 TYR B 115       2.438 -17.238  33.744  1.00 38.57           C  
ANISOU 2444  CD1 TYR B 115     3318   6464   4875    278   -723    -74       C  
ATOM   2445  CD2 TYR B 115       3.091 -15.751  35.469  1.00 32.28           C  
ANISOU 2445  CD2 TYR B 115     2455   5961   3851    -56   -993   -108       C  
ATOM   2446  CE1 TYR B 115       2.590 -18.310  34.595  1.00 35.94           C  
ANISOU 2446  CE1 TYR B 115     2931   6188   4535    284   -849    125       C  
ATOM   2447  CE2 TYR B 115       3.253 -16.816  36.328  1.00 39.66           C  
ANISOU 2447  CE2 TYR B 115     3337   6985   4746    -63  -1138    103       C  
ATOM   2448  CZ  TYR B 115       3.002 -18.094  35.886  1.00 43.02           C  
ANISOU 2448  CZ  TYR B 115     3763   7282   5298    117  -1064    229       C  
ATOM   2449  OH  TYR B 115       3.157 -19.165  36.736  1.00 48.96           O  
ANISOU 2449  OH  TYR B 115     4462   8101   6039    115  -1207    466       O  
ATOM   2450  N   PHE B 116       3.578 -14.131  30.184  1.00 28.72           N  
ANISOU 2450  N   PHE B 116     2014   4958   3939    347   -292   -414       N  
ATOM   2451  CA  PHE B 116       3.404 -13.483  28.890  1.00 28.30           C  
ANISOU 2451  CA  PHE B 116     2031   4796   3925    391   -123   -506       C  
ATOM   2452  C   PHE B 116       2.175 -14.041  28.183  1.00 30.59           C  
ANISOU 2452  C   PHE B 116     2509   4993   4121    479    -19   -580       C  
ATOM   2453  O   PHE B 116       1.930 -15.254  28.207  1.00 25.75           O  
ANISOU 2453  O   PHE B 116     1922   4349   3512    567     -4   -528       O  
ATOM   2454  CB  PHE B 116       4.628 -13.702  28.003  1.00 29.12           C  
ANISOU 2454  CB  PHE B 116     1980   4855   4230    475     -5   -410       C  
ATOM   2455  CG  PHE B 116       5.943 -13.314  28.653  1.00 32.77           C  
ANISOU 2455  CG  PHE B 116     2209   5415   4828    395   -116   -301       C  
ATOM   2456  CD1 PHE B 116       6.415 -12.016  28.568  1.00 30.80           C  
ANISOU 2456  CD1 PHE B 116     1907   5189   4607    268   -127   -351       C  
ATOM   2457  CD2 PHE B 116       6.712 -14.257  29.327  1.00 35.39           C  
ANISOU 2457  CD2 PHE B 116     2362   5808   5276    440   -217   -132       C  
ATOM   2458  CE1 PHE B 116       7.635 -11.657  29.147  1.00 36.67           C  
ANISOU 2458  CE1 PHE B 116     2424   6031   5479    170   -241   -250       C  
ATOM   2459  CE2 PHE B 116       7.926 -13.909  29.917  1.00 41.38           C  
ANISOU 2459  CE2 PHE B 116     2880   6675   6168    354   -346     -7       C  
ATOM   2460  CZ  PHE B 116       8.391 -12.602  29.824  1.00 40.38           C  
ANISOU 2460  CZ  PHE B 116     2703   6586   6055    210   -361    -75       C  
ATOM   2461  N   ILE B 117       1.420 -13.168  27.530  1.00 24.77           N  
ANISOU 2461  N   ILE B 117     1892   4202   3316    451     45   -688       N  
ATOM   2462  CA  ILE B 117       0.351 -13.624  26.652  1.00 23.67           C  
ANISOU 2462  CA  ILE B 117     1909   3984   3099    519    134   -740       C  
ATOM   2463  C   ILE B 117       0.961 -14.063  25.332  1.00 30.08           C  
ANISOU 2463  C   ILE B 117     2719   4725   3983    603    292   -705       C  
ATOM   2464  O   ILE B 117       1.714 -13.314  24.702  1.00 24.79           O  
ANISOU 2464  O   ILE B 117     1990   4045   3384    584    366   -687       O  
ATOM   2465  CB  ILE B 117      -0.693 -12.521  26.437  1.00 25.67           C  
ANISOU 2465  CB  ILE B 117     2268   4210   3274    460    130   -835       C  
ATOM   2466  CG1 ILE B 117      -1.348 -12.143  27.764  1.00 22.62           C  
ANISOU 2466  CG1 ILE B 117     1894   3882   2817    378     20   -901       C  
ATOM   2467  CG2 ILE B 117      -1.735 -12.988  25.448  1.00 25.32           C  
ANISOU 2467  CG2 ILE B 117     2361   4105   3153    515    195   -859       C  
ATOM   2468  CD1 ILE B 117      -2.274 -10.965  27.655  1.00 22.22           C  
ANISOU 2468  CD1 ILE B 117     1913   3779   2751    331     36   -995       C  
ATOM   2469  N   ARG B 118       0.623 -15.276  24.897  1.00 26.66           N  
ANISOU 2469  N   ARG B 118     2360   4238   3530    685    360   -704       N  
ATOM   2470  CA  ARG B 118       1.252 -15.878  23.736  1.00 25.03           C  
ANISOU 2470  CA  ARG B 118     2164   3958   3387    760    539   -696       C  
ATOM   2471  C   ARG B 118       0.298 -16.123  22.582  1.00 25.38           C  
ANISOU 2471  C   ARG B 118     2407   3948   3288    755    630   -780       C  
ATOM   2472  O   ARG B 118       0.753 -16.291  21.449  1.00 25.48           O  
ANISOU 2472  O   ARG B 118     2465   3917   3299    777    797   -801       O  
ATOM   2473  CB  ARG B 118       1.910 -17.212  24.120  1.00 28.66           C  
ANISOU 2473  CB  ARG B 118     2531   4371   3987    860    577   -626       C  
ATOM   2474  CG  ARG B 118       3.137 -17.046  25.010  1.00 27.30           C  
ANISOU 2474  CG  ARG B 118     2125   4261   3988    868    499   -501       C  
ATOM   2475  CD  ARG B 118       3.905 -18.343  25.111  1.00 28.90           C  
ANISOU 2475  CD  ARG B 118     2210   4386   4385    994    572   -402       C  
ATOM   2476  NE  ARG B 118       4.315 -18.806  23.795  1.00 29.88           N  
ANISOU 2476  NE  ARG B 118     2373   4392   4587   1079    827   -460       N  
ATOM   2477  CZ  ARG B 118       5.559 -18.767  23.334  1.00 31.62           C  
ANISOU 2477  CZ  ARG B 118     2421   4586   5005   1140    974   -404       C  
ATOM   2478  NH1 ARG B 118       6.542 -18.299  24.091  1.00 32.56           N  
ANISOU 2478  NH1 ARG B 118     2298   4792   5281   1125    862   -268       N  
ATOM   2479  NH2 ARG B 118       5.816 -19.223  22.117  1.00 32.68           N  
ANISOU 2479  NH2 ARG B 118     2626   4613   5176   1205   1238   -487       N  
ATOM   2480  N   ARG B 119      -0.999 -16.139  22.845  1.00 23.43           N  
ANISOU 2480  N   ARG B 119     2273   3713   2915    714    527   -826       N  
ATOM   2481  CA  ARG B 119      -1.986 -16.506  21.853  1.00 25.16           C  
ANISOU 2481  CA  ARG B 119     2667   3897   2995    691    572   -891       C  
ATOM   2482  C   ARG B 119      -3.309 -15.943  22.325  1.00 22.07           C  
ANISOU 2482  C   ARG B 119     2323   3548   2514    632    426   -909       C  
ATOM   2483  O   ARG B 119      -3.551 -15.840  23.532  1.00 30.53           O  
ANISOU 2483  O   ARG B 119     3325   4654   3620    626    323   -898       O  
ATOM   2484  CB  ARG B 119      -2.055 -18.031  21.677  1.00 26.06           C  
ANISOU 2484  CB  ARG B 119     2851   3932   3120    743    652   -927       C  
ATOM   2485  CG  ARG B 119      -2.894 -18.465  20.512  1.00 28.23           C  
ANISOU 2485  CG  ARG B 119     3316   4173   3236    690    713  -1011       C  
ATOM   2486  CD  ARG B 119      -2.913 -19.983  20.371  1.00 30.82           C  
ANISOU 2486  CD  ARG B 119     3722   4391   3597    729    810  -1071       C  
ATOM   2487  NE  ARG B 119      -4.098 -20.378  19.624  1.00 35.83           N  
ANISOU 2487  NE  ARG B 119     4541   5018   4055    635    787  -1156       N  
ATOM   2488  CZ  ARG B 119      -4.305 -21.586  19.119  1.00 38.71           C  
ANISOU 2488  CZ  ARG B 119     5035   5279   4392    619    888  -1250       C  
ATOM   2489  NH1 ARG B 119      -3.401 -22.542  19.278  1.00 36.08           N  
ANISOU 2489  NH1 ARG B 119     4664   4818   4227    717   1041  -1267       N  
ATOM   2490  NH2 ARG B 119      -5.418 -21.831  18.441  1.00 35.66           N  
ANISOU 2490  NH2 ARG B 119     4811   4910   3826    501    836  -1325       N  
ATOM   2491  N   CYS B 120      -4.145 -15.548  21.366  1.00 31.32           N  
ANISOU 2491  N   CYS B 120     3606   4722   3573    582    421   -927       N  
ATOM   2492  CA  CYS B 120      -5.397 -14.873  21.679  1.00 25.33           C  
ANISOU 2492  CA  CYS B 120     2860   3992   2773    537    297   -925       C  
ATOM   2493  C   CYS B 120      -6.311 -14.934  20.463  1.00 23.84           C  
ANISOU 2493  C   CYS B 120     2798   3808   2453    483    283   -922       C  
ATOM   2494  O   CYS B 120      -5.857 -14.726  19.336  1.00 28.14           O  
ANISOU 2494  O   CYS B 120     3410   4354   2926    455    359   -901       O  
ATOM   2495  CB  CYS B 120      -5.135 -13.414  22.092  1.00 26.06           C  
ANISOU 2495  CB  CYS B 120     2857   4094   2949    523    260   -894       C  
ATOM   2496  SG  CYS B 120      -6.610 -12.472  22.418  1.00 27.33           S  
ANISOU 2496  SG  CYS B 120     3010   4252   3122    492    152   -892       S  
ATOM   2497  N   GLN B 121      -7.595 -15.213  20.694  1.00 25.21           N  
ANISOU 2497  N   GLN B 121     2998   3996   2585    452    184   -933       N  
ATOM   2498  CA  GLN B 121      -8.533 -15.335  19.582  1.00 22.07           C  
ANISOU 2498  CA  GLN B 121     2707   3623   2057    378    132   -914       C  
ATOM   2499  C   GLN B 121      -9.968 -15.301  20.093  1.00 25.42           C  
ANISOU 2499  C   GLN B 121     3087   4070   2503    352      3   -899       C  
ATOM   2500  O   GLN B 121     -10.246 -15.603  21.259  1.00 22.61           O  
ANISOU 2500  O   GLN B 121     2660   3705   2225    385    -13   -934       O  
ATOM   2501  CB  GLN B 121      -8.301 -16.621  18.786  1.00 27.82           C  
ANISOU 2501  CB  GLN B 121     3577   4332   2662    339    217   -986       C  
ATOM   2502  CG  GLN B 121      -8.707 -17.916  19.505  1.00 27.07           C  
ANISOU 2502  CG  GLN B 121     3499   4193   2593    348    212  -1055       C  
ATOM   2503  CD  GLN B 121      -8.249 -19.144  18.725  1.00 30.72           C  
ANISOU 2503  CD  GLN B 121     4105   4591   2978    320    340  -1146       C  
ATOM   2504  OE1 GLN B 121      -7.075 -19.246  18.383  1.00 29.43           O  
ANISOU 2504  OE1 GLN B 121     3951   4386   2845    370    488  -1170       O  
ATOM   2505  NE2 GLN B 121      -9.177 -20.059  18.411  1.00 26.96           N  
ANISOU 2505  NE2 GLN B 121     3735   4096   2413    233    297  -1205       N  
ATOM   2506  N   ILE B 122     -10.876 -14.944  19.184  1.00 23.76           N  
ANISOU 2506  N   ILE B 122     2911   3897   2218    285    -90   -833       N  
ATOM   2507  CA  ILE B 122     -12.309 -14.879  19.453  1.00 23.41           C  
ANISOU 2507  CA  ILE B 122     2801   3880   2213    254   -217   -794       C  
ATOM   2508  C   ILE B 122     -12.946 -16.118  18.838  1.00 23.28           C  
ANISOU 2508  C   ILE B 122     2898   3895   2054    154   -263   -835       C  
ATOM   2509  O   ILE B 122     -12.833 -16.334  17.624  1.00 29.19           O  
ANISOU 2509  O   ILE B 122     3773   4678   2639     66   -273   -824       O  
ATOM   2510  CB  ILE B 122     -12.941 -13.611  18.850  1.00 26.67           C  
ANISOU 2510  CB  ILE B 122     3145   4311   2677    243   -317   -656       C  
ATOM   2511  CG1 ILE B 122     -12.198 -12.346  19.262  1.00 28.70           C  
ANISOU 2511  CG1 ILE B 122     3320   4508   3076    323   -254   -624       C  
ATOM   2512  CG2 ILE B 122     -14.389 -13.508  19.220  1.00 25.77           C  
ANISOU 2512  CG2 ILE B 122     2916   4215   2660    232   -433   -606       C  
ATOM   2513  CD1 ILE B 122     -11.893 -12.267  20.688  1.00 24.85           C  
ANISOU 2513  CD1 ILE B 122     2747   3978   2717    392   -183   -721       C  
ATOM   2514  N   ASN B 123     -13.612 -16.931  19.657  1.00 22.88           N  
ANISOU 2514  N   ASN B 123     2811   3833   2049    146   -283   -887       N  
ATOM   2515  CA  ASN B 123     -14.370 -18.084  19.171  1.00 25.80           C  
ANISOU 2515  CA  ASN B 123     3274   4218   2312     32   -338   -929       C  
ATOM   2516  C   ASN B 123     -15.860 -17.764  19.182  1.00 27.39           C  
ANISOU 2516  C   ASN B 123     3362   4482   2564    -28   -495   -843       C  
ATOM   2517  O   ASN B 123     -16.416 -17.428  20.232  1.00 23.75           O  
ANISOU 2517  O   ASN B 123     2752   4015   2257     33   -500   -822       O  
ATOM   2518  CB  ASN B 123     -14.099 -19.328  20.014  1.00 23.26           C  
ANISOU 2518  CB  ASN B 123     2989   3825   2023     50   -251  -1026       C  
ATOM   2519  CG  ASN B 123     -12.650 -19.767  19.945  1.00 34.45           C  
ANISOU 2519  CG  ASN B 123     4493   5169   3426    116    -98  -1092       C  
ATOM   2520  OD1 ASN B 123     -11.951 -19.486  18.974  1.00 33.64           O  
ANISOU 2520  OD1 ASN B 123     4474   5071   3235    106    -42  -1102       O  
ATOM   2521  ND2 ASN B 123     -12.191 -20.452  20.980  1.00 37.29           N  
ANISOU 2521  ND2 ASN B 123     4822   5467   3882    183    -29  -1119       N  
ATOM   2522  N   ARG B 124     -16.504 -17.889  18.019  1.00 25.90           N  
ANISOU 2522  N   ARG B 124     3238   4360   2241   -159   -618   -792       N  
ATOM   2523  CA  ARG B 124     -17.945 -17.701  17.872  1.00 31.25           C  
ANISOU 2523  CA  ARG B 124     3793   5110   2971   -237   -794   -687       C  
ATOM   2524  C   ARG B 124     -18.589 -19.040  17.509  1.00 28.06           C  
ANISOU 2524  C   ARG B 124     3490   4728   2444   -401   -856   -763       C  
ATOM   2525  O   ARG B 124     -18.397 -19.545  16.397  1.00 33.28           O  
ANISOU 2525  O   ARG B 124     4329   5422   2893   -538   -889   -806       O  
ATOM   2526  CB  ARG B 124     -18.226 -16.643  16.810  1.00 28.32           C  
ANISOU 2526  CB  ARG B 124     3390   4816   2556   -275   -932   -522       C  
ATOM   2527  CG  ARG B 124     -19.658 -16.136  16.760  1.00 34.06           C  
ANISOU 2527  CG  ARG B 124     3917   5607   3416   -310  -1120   -359       C  
ATOM   2528  CD  ARG B 124     -19.744 -14.897  15.873  1.00 36.62           C  
ANISOU 2528  CD  ARG B 124     4185   5978   3752   -303  -1242   -156       C  
ATOM   2529  NE  ARG B 124     -19.535 -15.224  14.473  1.00 34.98           N  
ANISOU 2529  NE  ARG B 124     4170   5872   3247   -477  -1344   -118       N  
ATOM   2530  CZ  ARG B 124     -20.491 -15.682  13.673  1.00 44.59           C  
ANISOU 2530  CZ  ARG B 124     5400   7211   4331   -663  -1552    -37       C  
ATOM   2531  NH1 ARG B 124     -21.718 -15.869  14.150  1.00 49.16           N  
ANISOU 2531  NH1 ARG B 124     5782   7815   5081   -682  -1675     26       N  
ATOM   2532  NH2 ARG B 124     -20.226 -15.955  12.401  1.00 45.53           N  
ANISOU 2532  NH2 ARG B 124     5726   7435   4137   -844  -1631    -21       N  
HETATM 2533  N   MSE B 125     -19.366 -19.601  18.435  1.00 27.76           N  
ANISOU 2533  N   MSE B 125     3346   4670   2533   -405   -861   -786       N  
HETATM 2534  CA  MSE B 125     -19.981 -20.929  18.262  1.00 30.70           C  
ANISOU 2534  CA  MSE B 125     3804   5035   2827   -566   -904   -864       C  
HETATM 2535  C   MSE B 125     -21.497 -20.833  18.121  1.00 31.87           C  
ANISOU 2535  C   MSE B 125     3785   5278   3044   -680  -1096   -751       C  
HETATM 2536  O   MSE B 125     -22.142 -20.086  18.854  1.00 36.72           O  
ANISOU 2536  O   MSE B 125     4176   5916   3861   -586  -1117   -650       O  
HETATM 2537  CB  MSE B 125     -19.644 -21.841  19.453  1.00 29.77           C  
ANISOU 2537  CB  MSE B 125     3702   4809   2801   -503   -752   -966       C  
HETATM 2538  CG  MSE B 125     -18.165 -21.930  19.788  1.00 33.38           C  
ANISOU 2538  CG  MSE B 125     4266   5172   3245   -371   -575  -1045       C  
HETATM 2539 SE   MSE B 125     -17.803 -22.838  21.479  1.00 37.47          SE  
ANISOU 2539 SE   MSE B 125     4748   5582   3907   -278   -429  -1091      SE  
HETATM 2540  CE  MSE B 125     -18.518 -24.597  21.008  1.00 26.97           C  
ANISOU 2540  CE  MSE B 125     3565   4167   2514   -479   -455  -1179       C  
ATOM   2541  N   LEU B 126     -22.070 -21.600  17.197  1.00 35.48           N  
ANISOU 2541  N   LEU B 126     4345   5789   3346   -892  -1228   -774       N  
ATOM   2542  CA  LEU B 126     -23.497 -21.561  16.906  1.00 37.66           C  
ANISOU 2542  CA  LEU B 126     4454   6176   3677  -1034  -1445   -649       C  
ATOM   2543  C   LEU B 126     -24.156 -22.868  17.327  1.00 39.04           C  
ANISOU 2543  C   LEU B 126     4648   6309   3877  -1176  -1441   -745       C  
ATOM   2544  O   LEU B 126     -23.503 -23.794  17.817  1.00 38.23           O  
ANISOU 2544  O   LEU B 126     4697   6079   3750  -1158  -1273   -897       O  
ATOM   2545  CB  LEU B 126     -23.743 -21.298  15.422  1.00 45.83           C  
ANISOU 2545  CB  LEU B 126     5578   7342   4495  -1211  -1652   -565       C  
ATOM   2546  CG  LEU B 126     -23.026 -20.100  14.798  1.00 48.71           C  
ANISOU 2546  CG  LEU B 126     5969   7748   4792  -1110  -1661   -458       C  
ATOM   2547  CD1 LEU B 126     -23.284 -20.096  13.302  1.00 56.18           C  
ANISOU 2547  CD1 LEU B 126     7050   8795   5501  -1298  -1830   -381       C  
ATOM   2548  CD2 LEU B 126     -23.479 -18.794  15.431  1.00 41.66           C  
ANISOU 2548  CD2 LEU B 126     4785   6860   4184   -922  -1696   -266       C  
ATOM   2549  N   LYS B 127     -25.469 -22.933  17.113  1.00 41.27           N  
ANISOU 2549  N   LYS B 127     4761   6693   4226  -1323  -1637   -635       N  
ATOM   2550  CA  LYS B 127     -26.257 -24.091  17.510  1.00 39.92           C  
ANISOU 2550  CA  LYS B 127     4569   6492   4107  -1480  -1653   -698       C  
ATOM   2551  C   LYS B 127     -25.625 -25.375  16.986  1.00 44.72           C  
ANISOU 2551  C   LYS B 127     5495   6997   4501  -1636  -1581   -905       C  
ATOM   2552  O   LYS B 127     -25.226 -25.453  15.822  1.00 48.19           O  
ANISOU 2552  O   LYS B 127     6135   7429   4745  -1700  -1610   -945       O  
ATOM   2553  CB  LYS B 127     -27.690 -23.936  16.987  1.00 40.15           C  
ANISOU 2553  CB  LYS B 127     4392   6653   4210  -1638  -1902   -537       C  
ATOM   2554  CG  LYS B 127     -28.677 -24.987  17.498  1.00 42.33           C  
ANISOU 2554  CG  LYS B 127     4581   6901   4602  -1789  -1918   -566       C  
ATOM   2555  CD  LYS B 127     -30.105 -24.685  17.037  1.00 49.42           C  
ANISOU 2555  CD  LYS B 127     5239   7901   5638  -1869  -2121   -380       C  
ATOM   2556  CE  LYS B 127     -31.116 -25.632  17.692  1.00 52.91           C  
ANISOU 2556  CE  LYS B 127     5547   8321   6235  -2006  -2119   -393       C  
ATOM   2557  NZ  LYS B 127     -32.539 -25.309  17.370  1.00 51.09           N  
ANISOU 2557  NZ  LYS B 127     5041   8192   6178  -2065  -2295   -208       N  
ATOM   2558  N   ASP B 128     -25.499 -26.363  17.873  1.00 45.68           N  
ANISOU 2558  N   ASP B 128     5665   6976   4715  -1624  -1424  -1010       N  
ATOM   2559  CA  ASP B 128     -25.002 -27.721  17.660  1.00 42.76           C  
ANISOU 2559  CA  ASP B 128     5561   6449   4239  -1749  -1315  -1203       C  
ATOM   2560  C   ASP B 128     -23.478 -27.821  17.736  1.00 42.81           C  
ANISOU 2560  C   ASP B 128     5768   6313   4184  -1574  -1092  -1321       C  
ATOM   2561  O   ASP B 128     -22.956 -28.935  17.719  1.00 39.89           O  
ANISOU 2561  O   ASP B 128     5597   5772   3789  -1626   -956  -1473       O  
ATOM   2562  CB  ASP B 128     -25.464 -28.345  16.329  1.00 43.69           C  
ANISOU 2562  CB  ASP B 128     5837   6568   4194  -1965  -1433  -1254       C  
ATOM   2563  CG  ASP B 128     -26.968 -28.475  16.236  1.00 49.59           C  
ANISOU 2563  CG  ASP B 128     6388   7416   5037  -2126  -1634  -1132       C  
ATOM   2564  OD1 ASP B 128     -27.624 -28.589  17.294  1.00 51.29           O  
ANISOU 2564  OD1 ASP B 128     6400   7646   5444  -2133  -1639  -1072       O  
ATOM   2565  OD2 ASP B 128     -27.490 -28.468  15.100  1.00 52.26           O  
ANISOU 2565  OD2 ASP B 128     6770   7829   5259  -2251  -1777  -1094       O  
ATOM   2566  N   SER B 129     -22.744 -26.716  17.822  1.00 34.95           N  
ANISOU 2566  N   SER B 129     4718   5369   3191  -1372  -1043  -1253       N  
ATOM   2567  CA  SER B 129     -21.298 -26.841  17.913  1.00 33.70           C  
ANISOU 2567  CA  SER B 129     4721   5083   2999  -1216   -836  -1353       C  
ATOM   2568  C   SER B 129     -20.873 -27.185  19.341  1.00 33.54           C  
ANISOU 2568  C   SER B 129     4625   4945   3176  -1046   -679  -1336       C  
ATOM   2569  O   SER B 129     -21.618 -26.994  20.307  1.00 34.26           O  
ANISOU 2569  O   SER B 129     4525   5082   3410  -1014   -715  -1234       O  
ATOM   2570  CB  SER B 129     -20.613 -25.555  17.456  1.00 33.66           C  
ANISOU 2570  CB  SER B 129     4691   5175   2924  -1085   -841  -1285       C  
ATOM   2571  OG  SER B 129     -20.769 -24.532  18.424  1.00 35.56           O  
ANISOU 2571  OG  SER B 129     4700   5473   3339   -909   -849  -1146       O  
ATOM   2572  N   PHE B 130     -19.658 -27.719  19.461  1.00 31.55           N  
ANISOU 2572  N   PHE B 130     4519   4541   2927   -944   -498  -1428       N  
ATOM   2573  CA  PHE B 130     -19.060 -28.009  20.758  1.00 31.61           C  
ANISOU 2573  CA  PHE B 130     4465   4448   3099   -780   -366  -1384       C  
ATOM   2574  C   PHE B 130     -17.556 -28.105  20.572  1.00 32.37           C  
ANISOU 2574  C   PHE B 130     4680   4432   3188   -637   -202  -1450       C  
ATOM   2575  O   PHE B 130     -17.069 -28.261  19.454  1.00 35.15           O  
ANISOU 2575  O   PHE B 130     5192   4745   3417   -691   -153  -1563       O  
ATOM   2576  CB  PHE B 130     -19.619 -29.297  21.381  1.00 36.79           C  
ANISOU 2576  CB  PHE B 130     5147   4975   3857   -880   -336  -1398       C  
ATOM   2577  CG  PHE B 130     -19.257 -30.569  20.635  1.00 42.57           C  
ANISOU 2577  CG  PHE B 130     6110   5510   4555   -991   -245  -1554       C  
ATOM   2578  CD1 PHE B 130     -18.163 -31.331  21.018  1.00 36.16           C  
ANISOU 2578  CD1 PHE B 130     5392   4494   3852   -869    -64  -1590       C  
ATOM   2579  CD2 PHE B 130     -20.039 -31.022  19.576  1.00 45.34           C  
ANISOU 2579  CD2 PHE B 130     6576   5871   4780  -1229   -339  -1663       C  
ATOM   2580  CE1 PHE B 130     -17.848 -32.515  20.347  1.00 40.30           C  
ANISOU 2580  CE1 PHE B 130     6127   4800   4385   -962     53  -1748       C  
ATOM   2581  CE2 PHE B 130     -19.722 -32.202  18.902  1.00 49.62           C  
ANISOU 2581  CE2 PHE B 130     7351   6211   5290  -1350   -230  -1841       C  
ATOM   2582  CZ  PHE B 130     -18.624 -32.945  19.291  1.00 44.00           C  
ANISOU 2582  CZ  PHE B 130     6735   5269   4714  -1206    -18  -1892       C  
ATOM   2583  N   ILE B 131     -16.822 -28.008  21.675  1.00 34.44           N  
ANISOU 2583  N   ILE B 131     4857   4652   3578   -466   -115  -1373       N  
ATOM   2584  CA AILE B 131     -15.374 -28.183  21.665  0.57 34.53           C  
ANISOU 2584  CA AILE B 131     4934   4550   3637   -320     37  -1404       C  
ATOM   2585  CA BILE B 131     -15.371 -28.170  21.683  0.43 34.63           C  
ANISOU 2585  CA BILE B 131     4944   4565   3650   -318     37  -1402       C  
ATOM   2586  C   ILE B 131     -15.065 -29.460  22.432  1.00 36.31           C  
ANISOU 2586  C   ILE B 131     5196   4585   4014   -289    135  -1387       C  
ATOM   2587  O   ILE B 131     -15.248 -29.534  23.655  1.00 35.37           O  
ANISOU 2587  O   ILE B 131     4962   4486   3989   -241    108  -1262       O  
ATOM   2588  CB AILE B 131     -14.637 -26.977  22.257  0.57 34.68           C  
ANISOU 2588  CB AILE B 131     4814   4680   3683   -156     38  -1310       C  
ATOM   2589  CB BILE B 131     -14.658 -26.973  22.329  0.43 34.53           C  
ANISOU 2589  CB BILE B 131     4787   4662   3669   -153     35  -1304       C  
ATOM   2590  CG1AILE B 131     -14.844 -25.741  21.379  0.57 29.98           C  
ANISOU 2590  CG1AILE B 131     4198   4232   2962   -180    -42  -1317       C  
ATOM   2591  CG1BILE B 131     -15.038 -25.663  21.632  0.43 29.81           C  
ANISOU 2591  CG1BILE B 131     4140   4229   2958   -179    -64  -1294       C  
ATOM   2592  CG2AILE B 131     -13.150 -27.284  22.386  0.57 37.67           C  
ANISOU 2592  CG2AILE B 131     5223   4940   4150    -10    185  -1315       C  
ATOM   2593  CG2BILE B 131     -13.147 -27.174  22.290  0.43 37.43           C  
ANISOU 2593  CG2BILE B 131     5194   4922   4106    -12    182  -1320       C  
ATOM   2594  CD1AILE B 131     -14.289 -24.486  21.981  0.57 24.83           C  
ANISOU 2594  CD1AILE B 131     3406   3676   2352    -45    -50  -1232       C  
ATOM   2595  CD1BILE B 131     -14.555 -25.572  20.210  0.43 26.82           C  
ANISOU 2595  CD1BILE B 131     3907   3839   2444   -228    -21  -1389       C  
ATOM   2596  N   GLY B 132     -14.601 -30.474  21.708  1.00 35.36           N  
ANISOU 2596  N   GLY B 132     5243   4272   3919   -324    260  -1510       N  
ATOM   2597  CA  GLY B 132     -14.351 -31.755  22.323  1.00 38.21           C  
ANISOU 2597  CA  GLY B 132     5646   4412   4460   -299    358  -1486       C  
ATOM   2598  C   GLY B 132     -13.189 -31.714  23.290  1.00 38.24           C  
ANISOU 2598  C   GLY B 132     5541   4366   4625    -91    430  -1345       C  
ATOM   2599  O   GLY B 132     -12.378 -30.795  23.291  1.00 39.57           O  
ANISOU 2599  O   GLY B 132     5629   4639   4767     32    440  -1311       O  
HETATM 2600  N   MSE B 133     -13.127 -32.749  24.121  1.00 40.20           N  
ANISOU 2600  N   MSE B 133     5780   4450   5045    -66    470  -1248       N  
HETATM 2601  CA  MSE B 133     -12.086 -32.899  25.130  1.00 43.56           C  
ANISOU 2601  CA  MSE B 133     6093   4820   5637    110    509  -1071       C  
HETATM 2602  C   MSE B 133     -10.693 -32.747  24.555  1.00 41.11           C  
ANISOU 2602  C   MSE B 133     5780   4425   5413    268    644  -1116       C  
HETATM 2603  O   MSE B 133     -10.349 -33.409  23.580  1.00 46.32           O  
ANISOU 2603  O   MSE B 133     6575   4893   6133    263    800  -1271       O  
HETATM 2604  CB  MSE B 133     -12.189 -34.265  25.795  1.00 51.66           C  
ANISOU 2604  CB  MSE B 133     7151   5619   6858     98    556   -968       C  
HETATM 2605  CG  MSE B 133     -11.375 -34.365  27.052  1.00 62.34           C  
ANISOU 2605  CG  MSE B 133     8362   6972   8352    243    528   -720       C  
HETATM 2606 SE   MSE B 133     -12.440 -33.750  28.551  1.00 72.16          SE  
ANISOU 2606 SE   MSE B 133     9483   8500   9434    137    337   -534      SE  
HETATM 2607  CE  MSE B 133     -13.539 -35.361  28.784  1.00 65.49           C  
ANISOU 2607  CE  MSE B 133     8751   7418   8714    -28    369   -493       C  
ATOM   2608  N   HIS B 134      -9.884 -31.893  25.175  1.00 38.61           N  
ANISOU 2608  N   HIS B 134     5311   4250   5108    398    597   -988       N  
ATOM   2609  CA  HIS B 134      -8.543 -31.625  24.674  1.00 41.69           C  
ANISOU 2609  CA  HIS B 134     5660   4589   5590    545    719  -1011       C  
ATOM   2610  C   HIS B 134      -7.693 -31.052  25.800  1.00 41.02           C  
ANISOU 2610  C   HIS B 134     5378   4625   5582    670    632   -800       C  
ATOM   2611  O   HIS B 134      -8.204 -30.619  26.837  1.00 38.27           O  
ANISOU 2611  O   HIS B 134     4951   4442   5147    623    478   -678       O  
ATOM   2612  CB  HIS B 134      -8.580 -30.656  23.494  1.00 42.16           C  
ANISOU 2612  CB  HIS B 134     5786   4774   5459    496    747  -1184       C  
ATOM   2613  CG  HIS B 134      -8.962 -29.263  23.885  1.00 46.69           C  
ANISOU 2613  CG  HIS B 134     6257   5617   5866    467    585  -1126       C  
ATOM   2614  ND1 HIS B 134     -10.275 -28.848  23.973  1.00 43.36           N  
ANISOU 2614  ND1 HIS B 134     5856   5330   5288    331    450  -1148       N  
ATOM   2615  CD2 HIS B 134      -8.205 -28.194  24.231  1.00 45.86           C  
ANISOU 2615  CD2 HIS B 134     6018   5653   5753    556    546  -1049       C  
ATOM   2616  CE1 HIS B 134     -10.308 -27.581  24.345  1.00 43.15           C  
ANISOU 2616  CE1 HIS B 134     5720   5499   5177    351    352  -1095       C  
ATOM   2617  NE2 HIS B 134      -9.066 -27.161  24.508  1.00 47.96           N  
ANISOU 2617  NE2 HIS B 134     6245   6116   5863    476    404  -1041       N  
ATOM   2618  N   LEU B 135      -6.380 -31.052  25.572  1.00 39.14           N  
ANISOU 2618  N   LEU B 135     5058   4309   5504    818    740   -767       N  
ATOM   2619  CA  LEU B 135      -5.412 -30.373  26.425  1.00 39.58           C  
ANISOU 2619  CA  LEU B 135     4916   4498   5622    922    654   -586       C  
ATOM   2620  C   LEU B 135      -4.819 -29.193  25.667  1.00 38.08           C  
ANISOU 2620  C   LEU B 135     4690   4439   5341    948    695   -690       C  
ATOM   2621  O   LEU B 135      -4.297 -29.364  24.557  1.00 38.69           O  
ANISOU 2621  O   LEU B 135     4828   4398   5473    993    876   -823       O  
ATOM   2622  CB  LEU B 135      -4.297 -31.321  26.866  1.00 44.44           C  
ANISOU 2622  CB  LEU B 135     5415   4923   6546   1077    726   -412       C  
ATOM   2623  CG  LEU B 135      -4.572 -32.148  28.118  1.00 52.82           C  
ANISOU 2623  CG  LEU B 135     6427   5937   7705   1070    606   -182       C  
ATOM   2624  CD1 LEU B 135      -3.737 -33.434  28.145  1.00 59.08           C  
ANISOU 2624  CD1 LEU B 135     7163   6431   8853   1218    734    -51       C  
ATOM   2625  CD2 LEU B 135      -4.299 -31.304  29.346  1.00 54.93           C  
ANISOU 2625  CD2 LEU B 135     6537   6467   7866   1052    397     14       C  
ATOM   2626  N   ASP B 136      -4.912 -28.001  26.265  1.00 37.71           N  
ANISOU 2626  N   ASP B 136     4552   4625   5151    908    544   -635       N  
ATOM   2627  CA  ASP B 136      -4.261 -26.822  25.701  1.00 43.65           C  
ANISOU 2627  CA  ASP B 136     5246   5494   5845    932    570   -695       C  
ATOM   2628  C   ASP B 136      -2.761 -27.023  25.564  1.00 40.27           C  
ANISOU 2628  C   ASP B 136     4680   4979   5641   1075    682   -616       C  
ATOM   2629  O   ASP B 136      -2.151 -26.500  24.626  1.00 39.35           O  
ANISOU 2629  O   ASP B 136     4562   4864   5526   1105    806   -710       O  
ATOM   2630  CB  ASP B 136      -4.535 -25.596  26.572  1.00 46.75           C  
ANISOU 2630  CB  ASP B 136     5552   6115   6095    867    394   -636       C  
ATOM   2631  CG  ASP B 136      -5.964 -25.126  26.481  1.00 53.45           C  
ANISOU 2631  CG  ASP B 136     6508   7055   6745    742    320   -734       C  
ATOM   2632  OD1 ASP B 136      -6.656 -25.509  25.514  1.00 61.56           O  
ANISOU 2632  OD1 ASP B 136     7672   8004   7715    693    388   -856       O  
ATOM   2633  OD2 ASP B 136      -6.388 -24.360  27.371  1.00 55.78           O  
ANISOU 2633  OD2 ASP B 136     6746   7502   6946    686    199   -693       O  
ATOM   2634  N   ALA B 137      -2.154 -27.773  26.486  1.00 49.53           N  
ANISOU 2634  N   ALA B 137     5725   6081   7013   1160    639   -427       N  
ATOM   2635  CA  ALA B 137      -0.727 -28.063  26.415  1.00 59.12           C  
ANISOU 2635  CA  ALA B 137     6766   7200   8497   1311    739   -318       C  
ATOM   2636  C   ALA B 137      -0.322 -28.713  25.095  1.00 58.72           C  
ANISOU 2636  C   ALA B 137     6800   6927   8584   1391   1020   -477       C  
ATOM   2637  O   ALA B 137       0.851 -28.625  24.711  1.00 61.77           O  
ANISOU 2637  O   ALA B 137     7047   7261   9162   1506   1155   -449       O  
ATOM   2638  CB  ALA B 137      -0.322 -28.961  27.588  1.00 66.94           C  
ANISOU 2638  CB  ALA B 137     7618   8122   9695   1384    635    -60       C  
ATOM   2639  N   ALA B 138      -1.259 -29.360  24.393  1.00 52.57           N  
ANISOU 2639  N   ALA B 138     6243   6019   7710   1320   1120   -652       N  
ATOM   2640  CA  ALA B 138      -0.942 -29.945  23.093  1.00 46.02           C  
ANISOU 2640  CA  ALA B 138     5537   4990   6960   1359   1402   -848       C  
ATOM   2641  C   ALA B 138      -0.575 -28.870  22.078  1.00 46.74           C  
ANISOU 2641  C   ALA B 138     5655   5213   6891   1322   1498   -987       C  
ATOM   2642  O   ALA B 138       0.289 -29.090  21.223  1.00 57.93           O  
ANISOU 2642  O   ALA B 138     7064   6511   8435   1401   1747  -1077       O  
ATOM   2643  CB  ALA B 138      -2.117 -30.782  22.583  1.00 42.62           C  
ANISOU 2643  CB  ALA B 138     5357   4424   6413   1241   1453  -1019       C  
ATOM   2644  N   SER B 139      -1.220 -27.701  22.152  1.00 40.32           N  
ANISOU 2644  N   SER B 139     4873   4636   5811   1203   1320  -1000       N  
ATOM   2645  CA  SER B 139      -0.848 -26.592  21.277  1.00 46.67           C  
ANISOU 2645  CA  SER B 139     5687   5570   6475   1165   1387  -1085       C  
ATOM   2646  C   SER B 139       0.527 -26.040  21.639  1.00 51.05           C  
ANISOU 2646  C   SER B 139     5996   6175   7227   1283   1416   -946       C  
ATOM   2647  O   SER B 139       1.313 -25.677  20.754  1.00 48.32           O  
ANISOU 2647  O   SER B 139     5629   5821   6909   1312   1603  -1014       O  
ATOM   2648  CB  SER B 139      -1.894 -25.480  21.351  1.00 44.20           C  
ANISOU 2648  CB  SER B 139     5445   5467   5882   1022   1181  -1104       C  
ATOM   2649  OG  SER B 139      -3.198 -25.977  21.102  1.00 50.43           O  
ANISOU 2649  OG  SER B 139     6422   6228   6511    907   1126  -1203       O  
ATOM   2650  N   ASN B 140       0.829 -25.962  22.931  1.00 45.74           N  
ANISOU 2650  N   ASN B 140     5134   5566   6680   1332   1230   -747       N  
ATOM   2651  CA  ASN B 140       2.107 -25.440  23.391  1.00 42.04           C  
ANISOU 2651  CA  ASN B 140     4409   5165   6398   1419   1210   -593       C  
ATOM   2652  C   ASN B 140       2.355 -26.013  24.778  1.00 34.40           C  
ANISOU 2652  C   ASN B 140     3274   4194   5603   1478   1030   -367       C  
ATOM   2653  O   ASN B 140       1.614 -25.707  25.717  1.00 35.85           O  
ANISOU 2653  O   ASN B 140     3484   4510   5627   1384    804   -303       O  
ATOM   2654  CB  ASN B 140       2.093 -23.902  23.388  1.00 41.85           C  
ANISOU 2654  CB  ASN B 140     4352   5360   6187   1316   1090   -605       C  
ATOM   2655  CG  ASN B 140       3.455 -23.277  23.723  1.00 40.50           C  
ANISOU 2655  CG  ASN B 140     3920   5265   6204   1374   1080   -468       C  
ATOM   2656  OD1 ASN B 140       4.211 -23.796  24.541  1.00 46.96           O  
ANISOU 2656  OD1 ASN B 140     4536   6055   7251   1463   1017   -292       O  
ATOM   2657  ND2 ASN B 140       3.757 -22.137  23.090  1.00 33.10           N  
ANISOU 2657  ND2 ASN B 140     2975   4427   5172   1313   1127   -531       N  
ATOM   2658  N   PRO B 141       3.388 -26.841  24.951  1.00 42.67           N  
ANISOU 2658  N   PRO B 141     4141   5095   6976   1630   1128   -230       N  
ATOM   2659  CA  PRO B 141       3.624 -27.457  26.267  1.00 45.25           C  
ANISOU 2659  CA  PRO B 141     4307   5418   7468   1681    936     29       C  
ATOM   2660  C   PRO B 141       3.945 -26.448  27.352  1.00 46.21           C  
ANISOU 2660  C   PRO B 141     4264   5801   7493   1597    662    191       C  
ATOM   2661  O   PRO B 141       3.919 -26.806  28.534  1.00 40.21           O  
ANISOU 2661  O   PRO B 141     3415   5100   6762   1580    455    399       O  
ATOM   2662  CB  PRO B 141       4.812 -28.394  26.007  1.00 43.53           C  
ANISOU 2662  CB  PRO B 141     3895   4979   7664   1879   1130    144       C  
ATOM   2663  CG  PRO B 141       5.550 -27.746  24.884  1.00 43.80           C  
ANISOU 2663  CG  PRO B 141     3934   5042   7667   1865   1314    -12       C  
ATOM   2664  CD  PRO B 141       4.495 -27.093  24.011  1.00 43.32           C  
ANISOU 2664  CD  PRO B 141     4126   5038   7295   1754   1403   -276       C  
ATOM   2665  N   ASP B 142       4.235 -25.202  26.990  1.00 46.99           N  
ANISOU 2665  N   ASP B 142     4332   6056   7468   1525    655    102       N  
ATOM   2666  CA  ASP B 142       4.579 -24.168  27.949  1.00 40.05           C  
ANISOU 2666  CA  ASP B 142     3311   5410   6495   1422    415    217       C  
ATOM   2667  C   ASP B 142       3.394 -23.276  28.324  1.00 32.35           C  
ANISOU 2667  C   ASP B 142     2523   4594   5174   1250    271     89       C  
ATOM   2668  O   ASP B 142       3.570 -22.338  29.108  1.00 37.09           O  
ANISOU 2668  O   ASP B 142     3045   5380   5667   1140     91    137       O  
ATOM   2669  CB  ASP B 142       5.744 -23.334  27.397  1.00 39.73           C  
ANISOU 2669  CB  ASP B 142     3089   5422   6584   1446    503    217       C  
ATOM   2670  CG  ASP B 142       7.012 -24.169  27.197  1.00 46.34           C  
ANISOU 2670  CG  ASP B 142     3679   6118   7811   1623    638    376       C  
ATOM   2671  OD1 ASP B 142       7.291 -25.016  28.072  1.00 48.08           O  
ANISOU 2671  OD1 ASP B 142     3763   6298   8206   1691    513    595       O  
ATOM   2672  OD2 ASP B 142       7.715 -23.995  26.173  1.00 44.42           O  
ANISOU 2672  OD2 ASP B 142     3411   5801   7664   1669    856    280       O  
ATOM   2673  N   TYR B 143       2.194 -23.551  27.816  1.00 30.95           N  
ANISOU 2673  N   TYR B 143     2580   4344   4834   1218    345    -71       N  
ATOM   2674  CA  TYR B 143       1.006 -22.856  28.309  1.00 29.56           C  
ANISOU 2674  CA  TYR B 143     2548   4302   4380   1074    209   -160       C  
ATOM   2675  C   TYR B 143       0.710 -23.287  29.740  1.00 32.22           C  
ANISOU 2675  C   TYR B 143     2848   4725   4667   1018     13     -4       C  
ATOM   2676  O   TYR B 143       0.638 -24.484  30.034  1.00 31.65           O  
ANISOU 2676  O   TYR B 143     2777   4542   4707   1082     18    111       O  
ATOM   2677  CB  TYR B 143      -0.208 -23.150  27.431  1.00 27.77           C  
ANISOU 2677  CB  TYR B 143     2549   3981   4021   1050    321   -338       C  
ATOM   2678  CG  TYR B 143      -0.159 -22.519  26.064  1.00 31.53           C  
ANISOU 2678  CG  TYR B 143     3104   4426   4449   1050    478   -497       C  
ATOM   2679  CD1 TYR B 143       0.785 -21.556  25.757  1.00 30.71           C  
ANISOU 2679  CD1 TYR B 143     2882   4390   4395   1055    509   -488       C  
ATOM   2680  CD2 TYR B 143      -1.072 -22.877  25.084  1.00 30.52           C  
ANISOU 2680  CD2 TYR B 143     3171   4212   4211   1023    584   -645       C  
ATOM   2681  CE1 TYR B 143       0.822 -20.971  24.506  1.00 34.96           C  
ANISOU 2681  CE1 TYR B 143     3502   4908   4872   1041    654   -610       C  
ATOM   2682  CE2 TYR B 143      -1.044 -22.302  23.838  1.00 32.24           C  
ANISOU 2682  CE2 TYR B 143     3475   4424   4350   1000    710   -768       C  
ATOM   2683  CZ  TYR B 143      -0.096 -21.349  23.550  1.00 35.11           C  
ANISOU 2683  CZ  TYR B 143     3726   4854   4760   1013    751   -745       C  
ATOM   2684  OH  TYR B 143      -0.069 -20.779  22.302  1.00 33.15           O  
ANISOU 2684  OH  TYR B 143     3572   4606   4416    978    880   -845       O  
ATOM   2685  N   GLU B 144       0.550 -22.318  30.635  1.00 29.08           N  
ANISOU 2685  N   GLU B 144     2427   4521   4100    889   -151      1       N  
ATOM   2686  CA  GLU B 144       0.241 -22.616  32.030  1.00 32.91           C  
ANISOU 2686  CA  GLU B 144     2901   5126   4478    799   -334    137       C  
ATOM   2687  C   GLU B 144      -1.165 -22.210  32.441  1.00 30.03           C  
ANISOU 2687  C   GLU B 144     2711   4841   3859    674   -363      1       C  
ATOM   2688  O   GLU B 144      -1.823 -22.956  33.169  1.00 29.16           O  
ANISOU 2688  O   GLU B 144     2662   4742   3675    634   -420     80       O  
ATOM   2689  CB  GLU B 144       1.269 -21.955  32.962  1.00 30.73           C  
ANISOU 2689  CB  GLU B 144     2449   5028   4199    721   -510    270       C  
ATOM   2690  CG  GLU B 144       2.588 -22.761  33.030  1.00 46.69           C  
ANISOU 2690  CG  GLU B 144     4249   6988   6503    842   -543    512       C  
ATOM   2691  CD  GLU B 144       3.592 -22.221  34.040  1.00 54.21           C  
ANISOU 2691  CD  GLU B 144     5006   8140   7450    741   -763    683       C  
ATOM   2692  OE1 GLU B 144       3.246 -21.274  34.778  1.00 56.03           O  
ANISOU 2692  OE1 GLU B 144     5301   8557   7430    559   -889    599       O  
ATOM   2693  OE2 GLU B 144       4.729 -22.748  34.097  1.00 59.20           O  
ANISOU 2693  OE2 GLU B 144     5415   8740   8340    837   -809    900       O  
ATOM   2694  N   PHE B 145      -1.658 -21.060  31.986  1.00 24.08           N  
ANISOU 2694  N   PHE B 145     1765   3479   3905    496    376    238       N  
ATOM   2695  CA  PHE B 145      -3.017 -20.637  32.289  1.00 20.48           C  
ANISOU 2695  CA  PHE B 145     1517   2981   3285    372    283    159       C  
ATOM   2696  C   PHE B 145      -3.703 -20.155  31.026  1.00 23.02           C  
ANISOU 2696  C   PHE B 145     1946   3349   3450    361    407     66       C  
ATOM   2697  O   PHE B 145      -3.058 -19.701  30.073  1.00 24.72           O  
ANISOU 2697  O   PHE B 145     2082   3658   3653    390    544     98       O  
ATOM   2698  CB  PHE B 145      -3.065 -19.536  33.362  1.00 20.01           C  
ANISOU 2698  CB  PHE B 145     1439   2949   3214    201    118    237       C  
ATOM   2699  CG  PHE B 145      -2.519 -19.968  34.699  1.00 26.70           C  
ANISOU 2699  CG  PHE B 145     2220   3773   4151    178    -49    333       C  
ATOM   2700  CD1 PHE B 145      -3.271 -20.773  35.546  1.00 21.13           C  
ANISOU 2700  CD1 PHE B 145     1660   2975   3393    177   -136    307       C  
ATOM   2701  CD2 PHE B 145      -1.248 -19.579  35.101  1.00 31.32           C  
ANISOU 2701  CD2 PHE B 145     2591   4440   4869    146   -129    465       C  
ATOM   2702  CE1 PHE B 145      -2.763 -21.171  36.768  1.00 25.43           C  
ANISOU 2702  CE1 PHE B 145     2167   3512   3984    152   -303    424       C  
ATOM   2703  CE2 PHE B 145      -0.727 -19.971  36.328  1.00 27.38           C  
ANISOU 2703  CE2 PHE B 145     2030   3943   4432    119   -324    573       C  
ATOM   2704  CZ  PHE B 145      -1.482 -20.764  37.163  1.00 29.37           C  
ANISOU 2704  CZ  PHE B 145     2457   4105   4598    126   -413    559       C  
ATOM   2705  N   SER B 146      -5.025 -20.279  31.029  1.00 24.13           N  
ANISOU 2705  N   SER B 146     2262   3436   3470    315    354    -35       N  
ATOM   2706  CA  SER B 146      -5.871 -19.730  29.983  1.00 22.96           C  
ANISOU 2706  CA  SER B 146     2218   3342   3163    286    402    -99       C  
ATOM   2707  C   SER B 146      -6.912 -18.832  30.627  1.00 16.03           C  
ANISOU 2707  C   SER B 146     1402   2444   2245    170    279    -87       C  
ATOM   2708  O   SER B 146      -7.381 -19.110  31.728  1.00 23.91           O  
ANISOU 2708  O   SER B 146     2428   3371   3284    124    186   -103       O  
ATOM   2709  CB  SER B 146      -6.549 -20.830  29.181  1.00 31.22           C  
ANISOU 2709  CB  SER B 146     3397   4350   4114    352    457   -251       C  
ATOM   2710  OG  SER B 146      -7.311 -20.268  28.140  1.00 42.12           O  
ANISOU 2710  OG  SER B 146     4869   5815   5320    316    468   -293       O  
ATOM   2711  N   VAL B 147      -7.257 -17.749  29.943  1.00 18.60           N  
ANISOU 2711  N   VAL B 147     1749   2827   2493    132    292    -50       N  
ATOM   2712  CA  VAL B 147      -8.253 -16.791  30.404  1.00 15.51           C  
ANISOU 2712  CA  VAL B 147     1404   2400   2090     57    203    -39       C  
ATOM   2713  C   VAL B 147      -9.325 -16.707  29.331  1.00 19.75           C  
ANISOU 2713  C   VAL B 147     2019   2984   2502     84    197    -79       C  
ATOM   2714  O   VAL B 147      -8.999 -16.618  28.143  1.00 19.42           O  
ANISOU 2714  O   VAL B 147     1999   3027   2355    121    265    -49       O  
ATOM   2715  CB  VAL B 147      -7.614 -15.409  30.664  1.00 21.13           C  
ANISOU 2715  CB  VAL B 147     2059   3101   2867    -15    199     77       C  
ATOM   2716  CG1 VAL B 147      -8.656 -14.364  31.060  1.00 14.85           C  
ANISOU 2716  CG1 VAL B 147     1327   2233   2082    -62    136     74       C  
ATOM   2717  CG2 VAL B 147      -6.524 -15.513  31.722  1.00 17.45           C  
ANISOU 2717  CG2 VAL B 147     1501   2614   2515    -67    163    115       C  
ATOM   2718  N   VAL B 148     -10.598 -16.749  29.735  1.00 18.41           N  
ANISOU 2718  N   VAL B 148     1884   2776   2333     61    115   -139       N  
ATOM   2719  CA  VAL B 148     -11.705 -16.647  28.785  1.00 17.24           C  
ANISOU 2719  CA  VAL B 148     1775   2687   2086     77     63   -163       C  
ATOM   2720  C   VAL B 148     -12.693 -15.576  29.233  1.00 22.06           C  
ANISOU 2720  C   VAL B 148     2354   3257   2771     64     -3   -114       C  
ATOM   2721  O   VAL B 148     -13.310 -15.706  30.300  1.00 18.20           O  
ANISOU 2721  O   VAL B 148     1840   2703   2373     35    -19   -171       O  
ATOM   2722  CB  VAL B 148     -12.466 -17.966  28.608  1.00 19.21           C  
ANISOU 2722  CB  VAL B 148     2065   2942   2290     67     24   -301       C  
ATOM   2723  CG1 VAL B 148     -13.584 -17.743  27.587  1.00 17.63           C  
ANISOU 2723  CG1 VAL B 148     1884   2833   1983     63    -72   -311       C  
ATOM   2724  CG2 VAL B 148     -11.529 -19.098  28.183  1.00 25.23           C  
ANISOU 2724  CG2 VAL B 148     2879   3701   3006    104    109   -374       C  
ATOM   2725  N   ILE B 149     -12.917 -14.590  28.361  1.00 17.17           N  
ANISOU 2725  N   ILE B 149     1741   2677   2106     96    -30     -8       N  
ATOM   2726  CA  ILE B 149     -13.909 -13.532  28.531  1.00 19.13           C  
ANISOU 2726  CA  ILE B 149     1952   2873   2443    126    -91     56       C  
ATOM   2727  C   ILE B 149     -15.158 -13.921  27.738  1.00 17.26           C  
ANISOU 2727  C   ILE B 149     1686   2735   2139    156   -206     37       C  
ATOM   2728  O   ILE B 149     -15.087 -14.153  26.524  1.00 20.95           O  
ANISOU 2728  O   ILE B 149     2206   3318   2437    165   -254     74       O  
ATOM   2729  CB  ILE B 149     -13.357 -12.174  28.048  1.00 17.21           C  
ANISOU 2729  CB  ILE B 149     1737   2585   2219    145    -67    223       C  
ATOM   2730  CG1 ILE B 149     -12.041 -11.819  28.763  1.00 18.16           C  
ANISOU 2730  CG1 ILE B 149     1866   2623   2412     78     25    239       C  
ATOM   2731  CG2 ILE B 149     -14.402 -11.076  28.205  1.00 18.06           C  
ANISOU 2731  CG2 ILE B 149     1810   2599   2453    208   -124    295       C  
ATOM   2732  CD1 ILE B 149     -11.439 -10.477  28.306  1.00 19.29           C  
ANISOU 2732  CD1 ILE B 149     2036   2695   2598     59     59    409       C  
ATOM   2733  N   GLN B 150     -16.309 -13.980  28.400  1.00 18.97           N  
ANISOU 2733  N   GLN B 150     1813   2920   2475    163   -250    -19       N  
ATOM   2734  CA  GLN B 150     -17.555 -14.327  27.725  1.00 20.60           C  
ANISOU 2734  CA  GLN B 150     1942   3230   2656    174   -385    -30       C  
ATOM   2735  C   GLN B 150     -18.202 -13.051  27.224  1.00 24.29           C  
ANISOU 2735  C   GLN B 150     2344   3694   3191    272   -467    132       C  
ATOM   2736  O   GLN B 150     -18.528 -12.170  28.026  1.00 27.17           O  
ANISOU 2736  O   GLN B 150     2646   3935   3742    334   -409    165       O  
ATOM   2737  CB  GLN B 150     -18.514 -15.074  28.652  1.00 24.67           C  
ANISOU 2737  CB  GLN B 150     2353   3726   3296    124   -380   -153       C  
ATOM   2738  CG  GLN B 150     -19.798 -15.547  27.962  1.00 19.85           C  
ANISOU 2738  CG  GLN B 150     1624   3236   2682    100   -538   -172       C  
ATOM   2739  CD  GLN B 150     -19.494 -16.405  26.760  1.00 29.47           C  
ANISOU 2739  CD  GLN B 150     2952   4568   3678     36   -639   -222       C  
ATOM   2740  OE1 GLN B 150     -20.011 -16.166  25.664  1.00 28.50           O  
ANISOU 2740  OE1 GLN B 150     2811   4571   3448     50   -801   -154       O  
ATOM   2741  NE2 GLN B 150     -18.623 -17.405  26.948  1.00 27.43           N  
ANISOU 2741  NE2 GLN B 150     2820   4262   3339    -27   -545   -339       N  
ATOM   2742  N   LEU B 151     -18.353 -12.947  25.904  1.00 24.52           N  
ANISOU 2742  N   LEU B 151     2407   3850   3059    292   -598    235       N  
ATOM   2743  CA  LEU B 151     -19.020 -11.824  25.250  1.00 23.60           C  
ANISOU 2743  CA  LEU B 151     2233   3747   2989    396   -719    432       C  
ATOM   2744  C   LEU B 151     -20.343 -12.222  24.611  1.00 25.54           C  
ANISOU 2744  C   LEU B 151     2344   4146   3214    403   -934    443       C  
ATOM   2745  O   LEU B 151     -20.974 -11.393  23.948  1.00 35.57           O  
ANISOU 2745  O   LEU B 151     3548   5456   4511    498  -1082    631       O  
ATOM   2746  CB  LEU B 151     -18.112 -11.219  24.179  1.00 27.83           C  
ANISOU 2746  CB  LEU B 151     2923   4323   3331    407   -719    602       C  
ATOM   2747  CG  LEU B 151     -16.788 -10.651  24.684  1.00 29.96           C  
ANISOU 2747  CG  LEU B 151     3289   4449   3647    385   -527    632       C  
ATOM   2748  CD1 LEU B 151     -15.880 -10.302  23.514  1.00 31.37           C  
ANISOU 2748  CD1 LEU B 151     3606   4708   3603    363   -502    792       C  
ATOM   2749  CD2 LEU B 151     -17.037  -9.428  25.554  1.00 28.89           C  
ANISOU 2749  CD2 LEU B 151     3097   4099   3783    461   -478    707       C  
ATOM   2750  N   GLY B 152     -20.761 -13.472  24.774  1.00 25.16           N  
ANISOU 2750  N   GLY B 152     2251   4179   3127    296   -971    261       N  
ATOM   2751  CA  GLY B 152     -21.950 -13.949  24.094  1.00 42.62           C  
ANISOU 2751  CA  GLY B 152     4333   6555   5305    256  -1202    256       C  
ATOM   2752  C   GLY B 152     -23.183 -13.347  24.724  1.00 59.57           C  
ANISOU 2752  C   GLY B 152     6212   8667   7757    349  -1249    326       C  
ATOM   2753  O   GLY B 152     -23.350 -13.380  25.950  1.00 61.94           O  
ANISOU 2753  O   GLY B 152     6422   8843   8271    359  -1077    234       O  
ATOM   2754  N   ARG B 153     -24.044 -12.768  23.885  1.00 63.81           N  
ANISOU 2754  N   ARG B 153     6617   9318   8310    428  -1478    500       N  
ATOM   2755  CA  ARG B 153     -25.294 -12.175  24.336  1.00 71.78           C  
ANISOU 2755  CA  ARG B 153     7323  10311   9637    549  -1538    589       C  
ATOM   2756  C   ARG B 153     -26.008 -13.127  25.283  1.00 71.03           C  
ANISOU 2756  C   ARG B 153     7044  10226   9716    440  -1456    393       C  
ATOM   2757  O   ARG B 153     -26.104 -12.869  26.488  1.00 75.45           O  
ANISOU 2757  O   ARG B 153     7527  10641  10499    496  -1227    328       O  
ATOM   2758  CB  ARG B 153     -26.189 -11.837  23.141  1.00 74.04           C  
ANISOU 2758  CB  ARG B 153     7540  10736   9857    601  -1815    730       C  
ATOM   2759  N   ALA B 154     -26.484 -14.242  24.747  1.00 59.47           N  
ANISOU 2759  N   ALA B 154     5550   8916   8129    269  -1620    281       N  
ATOM   2760  CA  ALA B 154     -27.123 -15.255  25.567  1.00 51.69           C  
ANISOU 2760  CA  ALA B 154     4423   7931   7286    128  -1533     99       C  
ATOM   2761  C   ALA B 154     -27.275 -16.501  24.720  1.00 42.60           C  
ANISOU 2761  C   ALA B 154     3373   6866   5946    -87  -1729    -25       C  
ATOM   2762  O   ALA B 154     -27.563 -16.414  23.527  1.00 44.61           O  
ANISOU 2762  O   ALA B 154     3681   7235   6035    -85  -1961     20       O  
ATOM   2763  CB  ALA B 154     -28.486 -14.797  26.098  1.00 55.06           C  
ANISOU 2763  CB  ALA B 154     4560   8389   7972    221  -1473    139       C  
ATOM   2764  N   PHE B 155     -27.059 -17.646  25.348  1.00 32.96           N  
ANISOU 2764  N   PHE B 155     2216   5591   4717   -270  -1604   -182       N  
ATOM   2765  CA  PHE B 155     -27.038 -18.931  24.674  1.00 37.26           C  
ANISOU 2765  CA  PHE B 155     2919   6159   5078   -481  -1729   -333       C  
ATOM   2766  C   PHE B 155     -27.454 -19.978  25.692  1.00 39.63           C  
ANISOU 2766  C   PHE B 155     3151   6357   5548   -644  -1579   -448       C  
ATOM   2767  O   PHE B 155     -27.332 -19.770  26.899  1.00 42.95           O  
ANISOU 2767  O   PHE B 155     3498   6691   6131   -589  -1342   -447       O  
ATOM   2768  CB  PHE B 155     -25.645 -19.247  24.116  1.00 33.52           C  
ANISOU 2768  CB  PHE B 155     2765   5692   4280   -489  -1685   -440       C  
ATOM   2769  CG  PHE B 155     -24.559 -19.189  25.159  1.00 37.89           C  
ANISOU 2769  CG  PHE B 155     3442   6077   4876   -416  -1390   -482       C  
ATOM   2770  CD1 PHE B 155     -23.855 -18.012  25.387  1.00 34.24           C  
ANISOU 2770  CD1 PHE B 155     3030   5557   4421   -231  -1266   -340       C  
ATOM   2771  CD2 PHE B 155     -24.263 -20.300  25.930  1.00 33.43           C  
ANISOU 2771  CD2 PHE B 155     2960   5378   4364   -538  -1240   -640       C  
ATOM   2772  CE1 PHE B 155     -22.863 -17.949  26.359  1.00 28.60           C  
ANISOU 2772  CE1 PHE B 155     2437   4680   3750   -183  -1017   -369       C  
ATOM   2773  CE2 PHE B 155     -23.286 -20.242  26.898  1.00 33.16           C  
ANISOU 2773  CE2 PHE B 155     3046   5185   4368   -468   -995   -643       C  
ATOM   2774  CZ  PHE B 155     -22.581 -19.061  27.113  1.00 29.25           C  
ANISOU 2774  CZ  PHE B 155     2589   4659   3865   -297   -893   -515       C  
ATOM   2775  N   ASP B 156     -27.964 -21.099  25.200  1.00 39.97           N  
ANISOU 2775  N   ASP B 156     3242   6394   5552   -847  -1718   -545       N  
ATOM   2776  CA  ASP B 156     -28.265 -22.241  26.048  1.00 42.65           C  
ANISOU 2776  CA  ASP B 156     3571   6616   6018  -1026  -1585   -646       C  
ATOM   2777  C   ASP B 156     -27.204 -23.317  25.856  1.00 44.21           C  
ANISOU 2777  C   ASP B 156     4092   6684   6020  -1120  -1524   -841       C  
ATOM   2778  O   ASP B 156     -26.691 -23.510  24.751  1.00 43.29           O  
ANISOU 2778  O   ASP B 156     4183   6603   5662  -1128  -1658   -922       O  
ATOM   2779  CB  ASP B 156     -29.653 -22.797  25.732  1.00 39.00           C  
ANISOU 2779  CB  ASP B 156     2913   6201   5704  -1200  -1777   -607       C  
ATOM   2780  CG  ASP B 156     -30.728 -21.757  25.897  1.00 45.58           C  
ANISOU 2780  CG  ASP B 156     3419   7177   6721  -1086  -1797   -400       C  
ATOM   2781  OD1 ASP B 156     -30.379 -20.631  26.295  1.00 49.06           O  
ANISOU 2781  OD1 ASP B 156     3794   7669   7177   -879  -1664   -301       O  
ATOM   2782  OD2 ASP B 156     -31.911 -22.052  25.633  1.00 53.46           O  
ANISOU 2782  OD2 ASP B 156     4228   8265   7819  -1203  -1924   -334       O  
ATOM   2783  N   GLY B 157     -26.878 -24.018  26.938  1.00 47.72           N  
ANISOU 2783  N   GLY B 157     4591   6972   6569  -1182  -1307   -906       N  
ATOM   2784  CA  GLY B 157     -25.793 -24.985  26.866  1.00 48.14           C  
ANISOU 2784  CA  GLY B 157     4940   6869   6482  -1232  -1222  -1066       C  
ATOM   2785  C   GLY B 157     -24.439 -24.296  26.850  1.00 42.88           C  
ANISOU 2785  C   GLY B 157     4411   6213   5667  -1051  -1113  -1080       C  
ATOM   2786  O   GLY B 157     -24.233 -23.258  27.487  1.00 36.22           O  
ANISOU 2786  O   GLY B 157     3455   5411   4895   -905  -1011   -963       O  
ATOM   2787  N   GLY B 158     -23.499 -24.878  26.111  1.00 39.30           N  
ANISOU 2787  N   GLY B 158     4219   5704   5009  -1052  -1116  -1214       N  
ATOM   2788  CA  GLY B 158     -22.174 -24.286  26.012  1.00 28.08           C  
ANISOU 2788  CA  GLY B 158     2954   4270   3447   -864   -985  -1174       C  
ATOM   2789  C   GLY B 158     -21.468 -24.124  27.340  1.00 27.49           C  
ANISOU 2789  C   GLY B 158     2881   4050   3515   -768   -760  -1085       C  
ATOM   2790  O   GLY B 158     -20.776 -23.119  27.558  1.00 25.33           O  
ANISOU 2790  O   GLY B 158     2607   3807   3211   -609   -675   -965       O  
ATOM   2791  N   GLU B 159     -21.621 -25.093  28.236  1.00 24.56           N  
ANISOU 2791  N   GLU B 159     2524   3519   3290   -876   -672  -1134       N  
ATOM   2792  CA  GLU B 159     -20.888 -25.055  29.490  1.00 27.34           C  
ANISOU 2792  CA  GLU B 159     2914   3743   3733   -800   -483  -1045       C  
ATOM   2793  C   GLU B 159     -19.421 -25.399  29.258  1.00 25.13           C  
ANISOU 2793  C   GLU B 159     2843   3358   3347   -684   -393  -1077       C  
ATOM   2794  O   GLU B 159     -19.092 -26.247  28.427  1.00 26.95           O  
ANISOU 2794  O   GLU B 159     3224   3522   3494   -712   -420  -1215       O  
ATOM   2795  CB  GLU B 159     -21.487 -26.030  30.504  1.00 32.09           C  
ANISOU 2795  CB  GLU B 159     3485   4205   4502   -958   -416  -1055       C  
ATOM   2796  CG  GLU B 159     -22.934 -25.769  30.844  1.00 38.50           C  
ANISOU 2796  CG  GLU B 159     4051   5123   5455  -1081   -461  -1018       C  
ATOM   2797  CD  GLU B 159     -23.872 -26.549  29.958  1.00 43.26           C  
ANISOU 2797  CD  GLU B 159     4611   5748   6078  -1259   -632  -1124       C  
ATOM   2798  OE1 GLU B 159     -23.424 -27.028  28.890  1.00 38.68           O  
ANISOU 2798  OE1 GLU B 159     4204   5140   5353  -1265   -735  -1244       O  
ATOM   2799  OE2 GLU B 159     -25.053 -26.692  30.338  1.00 50.39           O  
ANISOU 2799  OE2 GLU B 159     5339   6686   7122  -1369   -647  -1054       O  
ATOM   2800  N   PHE B 160     -18.550 -24.724  30.001  1.00 21.04           N  
ANISOU 2800  N   PHE B 160     2326   2826   2842   -556   -282   -957       N  
ATOM   2801  CA  PHE B 160     -17.130 -25.054  30.078  1.00 19.24           C  
ANISOU 2801  CA  PHE B 160     2234   2498   2579   -444   -183   -949       C  
ATOM   2802  C   PHE B 160     -16.931 -26.053  31.215  1.00 23.45           C  
ANISOU 2802  C   PHE B 160     2823   2844   3241   -492   -109   -921       C  
ATOM   2803  O   PHE B 160     -17.204 -25.742  32.381  1.00 20.83           O  
ANISOU 2803  O   PHE B 160     2426   2509   2980   -527    -70   -813       O  
ATOM   2804  CB  PHE B 160     -16.311 -23.784  30.313  1.00 23.98           C  
ANISOU 2804  CB  PHE B 160     2785   3189   3139   -313   -134   -820       C  
ATOM   2805  CG  PHE B 160     -14.824 -24.001  30.388  1.00 22.21           C  
ANISOU 2805  CG  PHE B 160     2639   2897   2904   -199    -43   -788       C  
ATOM   2806  CD1 PHE B 160     -14.093 -24.272  29.254  1.00 31.71           C  
ANISOU 2806  CD1 PHE B 160     3923   4119   4008   -123     -8   -864       C  
ATOM   2807  CD2 PHE B 160     -14.157 -23.895  31.596  1.00 22.00           C  
ANISOU 2807  CD2 PHE B 160     2592   2805   2960   -169      8   -678       C  
ATOM   2808  CE1 PHE B 160     -12.704 -24.459  29.314  1.00 36.84           C  
ANISOU 2808  CE1 PHE B 160     4596   4717   4684     -2     98   -825       C  
ATOM   2809  CE2 PHE B 160     -12.772 -24.061  31.667  1.00 29.67           C  
ANISOU 2809  CE2 PHE B 160     3587   3735   3952    -61     67   -628       C  
ATOM   2810  CZ  PHE B 160     -12.044 -24.357  30.518  1.00 28.31           C  
ANISOU 2810  CZ  PHE B 160     3458   3575   3722     31    122   -699       C  
ATOM   2811  N   VAL B 161     -16.477 -27.255  30.881  1.00 25.15           N  
ANISOU 2811  N   VAL B 161     3178   2896   3483   -494    -84  -1015       N  
ATOM   2812  CA  VAL B 161     -16.335 -28.322  31.859  1.00 21.27           C  
ANISOU 2812  CA  VAL B 161     2761   2193   3128   -541    -29   -969       C  
ATOM   2813  C   VAL B 161     -14.873 -28.713  31.891  1.00 23.01           C  
ANISOU 2813  C   VAL B 161     3072   2299   3373   -368     46   -934       C  
ATOM   2814  O   VAL B 161     -14.280 -28.992  30.844  1.00 23.83           O  
ANISOU 2814  O   VAL B 161     3250   2380   3423   -275     77  -1056       O  
ATOM   2815  CB  VAL B 161     -17.233 -29.531  31.532  1.00 29.19           C  
ANISOU 2815  CB  VAL B 161     3842   3042   4208   -713    -69  -1104       C  
ATOM   2816  CG1 VAL B 161     -17.147 -30.577  32.638  1.00 27.85           C  
ANISOU 2816  CG1 VAL B 161     3754   2634   4193   -774     -6  -1009       C  
ATOM   2817  CG2 VAL B 161     -18.677 -29.086  31.327  1.00 23.82           C  
ANISOU 2817  CG2 VAL B 161     3016   2516   3520   -882   -164  -1140       C  
ATOM   2818  N   VAL B 162     -14.288 -28.695  33.077  1.00 20.68           N  
ANISOU 2818  N   VAL B 162     2760   1952   3147   -321     77   -765       N  
ATOM   2819  CA  VAL B 162     -12.919 -29.153  33.288  1.00 29.24           C  
ANISOU 2819  CA  VAL B 162     3888   2922   4302   -155    125   -690       C  
ATOM   2820  C   VAL B 162     -12.972 -30.538  33.919  1.00 28.71           C  
ANISOU 2820  C   VAL B 162     3939   2584   4383   -191    140   -647       C  
ATOM   2821  O   VAL B 162     -13.797 -30.795  34.802  1.00 26.31           O  
ANISOU 2821  O   VAL B 162     3654   2234   4109   -343    118   -566       O  
ATOM   2822  CB  VAL B 162     -12.134 -28.165  34.173  1.00 23.83           C  
ANISOU 2822  CB  VAL B 162     3099   2370   3586    -85    107   -510       C  
ATOM   2823  CG1 VAL B 162     -10.692 -28.597  34.289  1.00 23.73           C  
ANISOU 2823  CG1 VAL B 162     3076   2271   3669     92    133   -423       C  
ATOM   2824  CG2 VAL B 162     -12.223 -26.780  33.607  1.00 23.28           C  
ANISOU 2824  CG2 VAL B 162     2929   2523   3395    -78     96   -542       C  
ATOM   2825  N   HIS B 163     -12.093 -31.436  33.473  1.00 27.95           N  
ANISOU 2825  N   HIS B 163     3927   2299   4394    -45    196   -694       N  
ATOM   2826  CA  HIS B 163     -12.061 -32.817  33.952  1.00 28.74           C  
ANISOU 2826  CA  HIS B 163     4162   2087   4670    -50    215   -651       C  
ATOM   2827  C   HIS B 163     -10.715 -33.136  34.591  1.00 29.42           C  
ANISOU 2827  C   HIS B 163     4221   2071   4885    161    227   -461       C  
ATOM   2828  O   HIS B 163      -9.913 -33.886  34.020  1.00 29.69           O  
ANISOU 2828  O   HIS B 163     4306   1922   5054    340    304   -529       O  
ATOM   2829  CB  HIS B 163     -12.331 -33.799  32.817  1.00 30.65           C  
ANISOU 2829  CB  HIS B 163     4554   2122   4969    -63    272   -902       C  
ATOM   2830  CG  HIS B 163     -13.676 -33.643  32.181  1.00 36.07           C  
ANISOU 2830  CG  HIS B 163     5260   2898   5546   -292    217  -1082       C  
ATOM   2831  ND1 HIS B 163     -14.686 -34.567  32.342  1.00 41.19           N  
ANISOU 2831  ND1 HIS B 163     6012   3347   6292   -502    188  -1143       N  
ATOM   2832  CD2 HIS B 163     -14.171 -32.685  31.362  1.00 35.11           C  
ANISOU 2832  CD2 HIS B 163     5057   3043   5242   -347    172  -1198       C  
ATOM   2833  CE1 HIS B 163     -15.747 -34.183  31.655  1.00 39.70           C  
ANISOU 2833  CE1 HIS B 163     5778   3317   5990   -681    115  -1297       C  
ATOM   2834  NE2 HIS B 163     -15.460 -33.044  31.050  1.00 37.78           N  
ANISOU 2834  NE2 HIS B 163     5427   3355   5571   -579     97  -1326       N  
ATOM   2835  N   PRO B 164     -10.450 -32.624  35.790  1.00 33.02           N  
ANISOU 2835  N   PRO B 164     4600   2637   5310    147    150   -224       N  
ATOM   2836  CA  PRO B 164      -9.167 -32.914  36.438  1.00 30.44           C  
ANISOU 2836  CA  PRO B 164     4221   2239   5106    337    114    -16       C  
ATOM   2837  C   PRO B 164      -9.035 -34.388  36.770  1.00 39.76           C  
ANISOU 2837  C   PRO B 164     5545   3064   6498    399    129     69       C  
ATOM   2838  O   PRO B 164     -10.023 -35.078  37.035  1.00 39.38           O  
ANISOU 2838  O   PRO B 164     5645   2846   6473    227    137     56       O  
ATOM   2839  CB  PRO B 164      -9.207 -32.061  37.705  1.00 39.97           C  
ANISOU 2839  CB  PRO B 164     5363   3648   6175    234      1    194       C  
ATOM   2840  CG  PRO B 164     -10.666 -31.839  37.957  1.00 41.36           C  
ANISOU 2840  CG  PRO B 164     5613   3877   6224     -9     18    124       C  
ATOM   2841  CD  PRO B 164     -11.290 -31.736  36.608  1.00 35.36           C  
ANISOU 2841  CD  PRO B 164     4850   3135   5450    -39     92   -143       C  
ATOM   2842  N   GLN B 165      -7.791 -34.866  36.739  1.00 41.34           N  
ANISOU 2842  N   GLN B 165     5687   3141   6878    650    139    168       N  
ATOM   2843  CA  GLN B 165      -7.531 -36.279  36.982  1.00 45.78           C  
ANISOU 2843  CA  GLN B 165     6383   3324   7689    762    160    260       C  
ATOM   2844  C   GLN B 165      -8.043 -36.673  38.358  1.00 41.87           C  
ANISOU 2844  C   GLN B 165     5993   2741   7175    607     43    536       C  
ATOM   2845  O   GLN B 165      -7.805 -35.975  39.344  1.00 35.76           O  
ANISOU 2845  O   GLN B 165     5133   2189   6263    561    -82    753       O  
ATOM   2846  CB  GLN B 165      -6.034 -36.575  36.863  1.00 43.33           C  
ANISOU 2846  CB  GLN B 165     5932   2936   7594   1089    178    369       C  
ATOM   2847  N   GLY B 166      -8.798 -37.766  38.407  1.00 45.05           N  
ANISOU 2847  N   GLY B 166     6599   2824   7695    499     90    514       N  
ATOM   2848  CA  GLY B 166      -9.214 -38.349  39.665  1.00 55.79           C  
ANISOU 2848  CA  GLY B 166     8087   4045   9067    364     11    804       C  
ATOM   2849  C   GLY B 166     -10.229 -37.568  40.466  1.00 47.97           C  
ANISOU 2849  C   GLY B 166     7096   3323   7806     77    -28    873       C  
ATOM   2850  O   GLY B 166     -10.385 -37.835  41.658  1.00 47.11           O  
ANISOU 2850  O   GLY B 166     7075   3185   7641    -21    -95   1156       O  
ATOM   2851  N   ARG B 167     -10.931 -36.625  39.854  1.00 41.78           N  
ANISOU 2851  N   ARG B 167     6225   2796   6855    -54     22    631       N  
ATOM   2852  CA  ARG B 167     -11.928 -35.813  40.534  1.00 42.17           C  
ANISOU 2852  CA  ARG B 167     6248   3100   6673   -298     19    663       C  
ATOM   2853  C   ARG B 167     -13.168 -35.717  39.660  1.00 39.46           C  
ANISOU 2853  C   ARG B 167     5897   2780   6316   -485    108    388       C  
ATOM   2854  O   ARG B 167     -13.113 -36.012  38.463  1.00 38.80           O  
ANISOU 2854  O   ARG B 167     5818   2591   6332   -417    145    152       O  
ATOM   2855  CB  ARG B 167     -11.394 -34.405  40.837  1.00 43.83           C  
ANISOU 2855  CB  ARG B 167     6301   3673   6679   -239    -49    690       C  
ATOM   2856  CG  ARG B 167     -11.104 -34.163  42.307  1.00 51.76           C  
ANISOU 2856  CG  ARG B 167     7346   4790   7531   -289   -146    981       C  
ATOM   2857  CD  ARG B 167     -10.369 -32.855  42.506  1.00 53.87           C  
ANISOU 2857  CD  ARG B 167     7469   5366   7635   -219   -234    981       C  
ATOM   2858  NE  ARG B 167     -11.128 -31.727  41.982  1.00 53.14           N  
ANISOU 2858  NE  ARG B 167     7289   5493   7411   -322   -155    749       N  
ATOM   2859  CZ  ARG B 167     -10.573 -30.604  41.535  1.00 47.55           C  
ANISOU 2859  CZ  ARG B 167     6440   4990   6639   -242   -188    647       C  
ATOM   2860  NH1 ARG B 167      -9.249 -30.467  41.538  1.00 41.77           N  
ANISOU 2860  NH1 ARG B 167     5616   4290   5966    -74   -293    745       N  
ATOM   2861  NH2 ARG B 167     -11.341 -29.625  41.075  1.00 34.81           N  
ANISOU 2861  NH2 ARG B 167     4762   3539   4924   -330   -117    462       N  
ATOM   2862  N   PRO B 168     -14.305 -35.312  40.230  1.00 38.67           N  
ANISOU 2862  N   PRO B 168     5779   2827   6088   -722    145    410       N  
ATOM   2863  CA  PRO B 168     -15.493 -35.106  39.402  1.00 38.50           C  
ANISOU 2863  CA  PRO B 168     5690   2873   6065   -895    199    167       C  
ATOM   2864  C   PRO B 168     -15.294 -33.939  38.457  1.00 32.73           C  
ANISOU 2864  C   PRO B 168     4808   2405   5224   -786    173    -34       C  
ATOM   2865  O   PRO B 168     -14.543 -32.998  38.759  1.00 28.39           O  
ANISOU 2865  O   PRO B 168     4179   2053   4555   -654    137     38       O  
ATOM   2866  CB  PRO B 168     -16.597 -34.812  40.434  1.00 42.58           C  
ANISOU 2866  CB  PRO B 168     6178   3523   6476  -1134    263    290       C  
ATOM   2867  CG  PRO B 168     -15.866 -34.406  41.682  1.00 43.55           C  
ANISOU 2867  CG  PRO B 168     6343   3756   6449  -1057    234    543       C  
ATOM   2868  CD  PRO B 168     -14.606 -35.202  41.666  1.00 39.88           C  
ANISOU 2868  CD  PRO B 168     5984   3060   6110   -853    150    669       C  
ATOM   2869  N   PRO B 169     -15.951 -33.946  37.300  1.00 34.52           N  
ANISOU 2869  N   PRO B 169     4996   2643   5476   -854    176   -277       N  
ATOM   2870  CA  PRO B 169     -15.862 -32.791  36.403  1.00 30.86           C  
ANISOU 2870  CA  PRO B 169     4399   2441   4887   -767    147   -434       C  
ATOM   2871  C   PRO B 169     -16.288 -31.508  37.109  1.00 24.74           C  
ANISOU 2871  C   PRO B 169     3483   1948   3968   -813    151   -347       C  
ATOM   2872  O   PRO B 169     -17.060 -31.531  38.066  1.00 25.24           O  
ANISOU 2872  O   PRO B 169     3535   2037   4019   -967    197   -238       O  
ATOM   2873  CB  PRO B 169     -16.822 -33.151  35.267  1.00 27.70           C  
ANISOU 2873  CB  PRO B 169     3998   2005   4520   -907    124   -670       C  
ATOM   2874  CG  PRO B 169     -16.890 -34.648  35.303  1.00 35.74           C  
ANISOU 2874  CG  PRO B 169     5193   2672   5716   -988    148   -688       C  
ATOM   2875  CD  PRO B 169     -16.814 -35.006  36.757  1.00 33.06           C  
ANISOU 2875  CD  PRO B 169     4898   2232   5430  -1033    189   -413       C  
ATOM   2876  N   ASN B 170     -15.745 -30.390  36.642  1.00 22.83           N  
ANISOU 2876  N   ASN B 170     3147   1905   3621   -678    124   -395       N  
ATOM   2877  CA  ASN B 170     -16.053 -29.053  37.161  1.00 25.09           C  
ANISOU 2877  CA  ASN B 170     3315   2432   3785   -693    132   -348       C  
ATOM   2878  C   ASN B 170     -16.799 -28.288  36.087  1.00 22.96           C  
ANISOU 2878  C   ASN B 170     2925   2317   3482   -712    107   -508       C  
ATOM   2879  O   ASN B 170     -16.232 -27.999  35.028  1.00 28.07           O  
ANISOU 2879  O   ASN B 170     3566   3007   4094   -597     68   -600       O  
ATOM   2880  CB  ASN B 170     -14.798 -28.262  37.517  1.00 23.84           C  
ANISOU 2880  CB  ASN B 170     3143   2366   3549   -537    102   -254       C  
ATOM   2881  CG  ASN B 170     -14.004 -28.887  38.616  1.00 28.18           C  
ANISOU 2881  CG  ASN B 170     3789   2805   4114   -508     82    -66       C  
ATOM   2882  OD1 ASN B 170     -12.775 -28.816  38.602  1.00 29.47           O  
ANISOU 2882  OD1 ASN B 170     3944   2963   4292   -361     30      2       O  
ATOM   2883  ND2 ASN B 170     -14.688 -29.493  39.589  1.00 27.93           N  
ANISOU 2883  ND2 ASN B 170     3837   2697   4079   -651    120     39       N  
ATOM   2884  N   VAL B 171     -18.042 -27.931  36.369  1.00 20.58           N  
ANISOU 2884  N   VAL B 171     2520   2111   3189   -847    134   -522       N  
ATOM   2885  CA  VAL B 171     -18.947 -27.371  35.377  1.00 21.03           C  
ANISOU 2885  CA  VAL B 171     2439   2302   3247   -881     80   -646       C  
ATOM   2886  C   VAL B 171     -19.125 -25.874  35.624  1.00 19.18           C  
ANISOU 2886  C   VAL B 171     2078   2259   2948   -804    102   -609       C  
ATOM   2887  O   VAL B 171     -19.507 -25.455  36.726  1.00 19.16           O  
ANISOU 2887  O   VAL B 171     2039   2300   2942   -846    195   -533       O  
ATOM   2888  CB  VAL B 171     -20.293 -28.108  35.406  1.00 22.44           C  
ANISOU 2888  CB  VAL B 171     2546   2442   3540  -1089     84   -690       C  
ATOM   2889  CG1 VAL B 171     -21.239 -27.528  34.373  1.00 22.83           C  
ANISOU 2889  CG1 VAL B 171     2424   2653   3599  -1124    -15   -799       C  
ATOM   2890  CG2 VAL B 171     -20.057 -29.610  35.147  1.00 24.14           C  
ANISOU 2890  CG2 VAL B 171     2923   2413   3837  -1174     63   -739       C  
ATOM   2891  N   PHE B 172     -18.883 -25.077  34.585  1.00 23.58           N  
ANISOU 2891  N   PHE B 172     2588   2921   3450   -697     29   -666       N  
ATOM   2892  CA  PHE B 172     -18.968 -23.621  34.645  1.00 21.58           C  
ANISOU 2892  CA  PHE B 172     2234   2807   3159   -606     39   -630       C  
ATOM   2893  C   PHE B 172     -19.929 -23.153  33.561  1.00 22.30           C  
ANISOU 2893  C   PHE B 172     2184   3015   3273   -610    -55   -689       C  
ATOM   2894  O   PHE B 172     -19.733 -23.455  32.385  1.00 27.43           O  
ANISOU 2894  O   PHE B 172     2876   3683   3863   -595   -156   -756       O  
ATOM   2895  CB  PHE B 172     -17.586 -22.994  34.451  1.00 17.17           C  
ANISOU 2895  CB  PHE B 172     1756   2254   2515   -468     31   -589       C  
ATOM   2896  CG  PHE B 172     -16.604 -23.313  35.561  1.00 24.69           C  
ANISOU 2896  CG  PHE B 172     2813   3122   3448   -458     82   -506       C  
ATOM   2897  CD1 PHE B 172     -16.436 -22.443  36.634  1.00 20.11           C  
ANISOU 2897  CD1 PHE B 172     2234   2581   2828   -456    131   -442       C  
ATOM   2898  CD2 PHE B 172     -15.854 -24.484  35.532  1.00 28.03           C  
ANISOU 2898  CD2 PHE B 172     3337   3420   3892   -448     70   -492       C  
ATOM   2899  CE1 PHE B 172     -15.537 -22.733  37.666  1.00 21.13           C  
ANISOU 2899  CE1 PHE B 172     2461   2658   2909   -465    137   -355       C  
ATOM   2900  CE2 PHE B 172     -14.956 -24.779  36.550  1.00 27.13           C  
ANISOU 2900  CE2 PHE B 172     3298   3240   3768   -428     83   -382       C  
ATOM   2901  CZ  PHE B 172     -14.807 -23.907  37.630  1.00 17.48           C  
ANISOU 2901  CZ  PHE B 172     2074   2089   2477   -448    101   -307       C  
ATOM   2902  N   ALA B 173     -20.971 -22.431  33.947  1.00 25.98           N  
ANISOU 2902  N   ALA B 173     2485   3566   3819   -625    -22   -664       N  
ATOM   2903  CA  ALA B 173     -21.849 -21.827  32.957  1.00 27.56           C  
ANISOU 2903  CA  ALA B 173     2521   3892   4058   -597   -138   -680       C  
ATOM   2904  C   ALA B 173     -21.544 -20.333  32.878  1.00 30.26           C  
ANISOU 2904  C   ALA B 173     2830   4288   4381   -434   -123   -610       C  
ATOM   2905  O   ALA B 173     -21.915 -19.589  33.800  1.00 34.45           O  
ANISOU 2905  O   ALA B 173     3286   4813   4990   -394     -4   -578       O  
ATOM   2906  CB  ALA B 173     -23.314 -22.060  33.313  1.00 27.19           C  
ANISOU 2906  CB  ALA B 173     2261   3902   4171   -712   -120   -688       C  
ATOM   2907  N   PRO B 174     -20.857 -19.848  31.822  1.00 28.37           N  
ANISOU 2907  N   PRO B 174     2661   4086   4034   -342   -221   -589       N  
ATOM   2908  CA  PRO B 174     -20.420 -18.439  31.799  1.00 23.50           C  
ANISOU 2908  CA  PRO B 174     2044   3476   3411   -204   -195   -504       C  
ATOM   2909  C   PRO B 174     -21.482 -17.470  31.287  1.00 27.94           C  
ANISOU 2909  C   PRO B 174     2426   4120   4071   -124   -273   -441       C  
ATOM   2910  O   PRO B 174     -22.084 -17.678  30.232  1.00 38.22           O  
ANISOU 2910  O   PRO B 174     3650   5526   5347   -140   -433   -431       O  
ATOM   2911  CB  PRO B 174     -19.205 -18.467  30.862  1.00 18.63           C  
ANISOU 2911  CB  PRO B 174     1576   2865   2638   -160   -245   -487       C  
ATOM   2912  CG  PRO B 174     -19.515 -19.589  29.904  1.00 30.69           C  
ANISOU 2912  CG  PRO B 174     3131   4445   4085   -241   -354   -572       C  
ATOM   2913  CD  PRO B 174     -20.297 -20.621  30.697  1.00 28.02           C  
ANISOU 2913  CD  PRO B 174     2736   4054   3856   -369   -323   -647       C  
ATOM   2914  N   ALA B 175     -21.723 -16.399  32.024  1.00 25.20           N  
ANISOU 2914  N   ALA B 175     2015   3722   3838    -33   -169   -398       N  
ATOM   2915  CA  ALA B 175     -22.598 -15.335  31.553  1.00 26.91           C  
ANISOU 2915  CA  ALA B 175     2063   3977   4183     91   -231   -313       C  
ATOM   2916  C   ALA B 175     -21.753 -14.219  30.950  1.00 26.53           C  
ANISOU 2916  C   ALA B 175     2129   3877   4073    206   -267   -209       C  
ATOM   2917  O   ALA B 175     -20.528 -14.192  31.093  1.00 18.81           O  
ANISOU 2917  O   ALA B 175     1332   2835   2980    181   -211   -217       O  
ATOM   2918  CB  ALA B 175     -23.477 -14.799  32.696  1.00 24.48           C  
ANISOU 2918  CB  ALA B 175     1610   3619   4073    143    -63   -340       C  
ATOM   2919  N   TYR B 176     -22.428 -13.296  30.260  1.00 21.99           N  
ANISOU 2919  N   TYR B 176     1433   3329   3595    331   -366    -91       N  
ATOM   2920  CA  TYR B 176     -21.749 -12.151  29.654  1.00 23.55           C  
ANISOU 2920  CA  TYR B 176     1734   3456   3758    436   -398     44       C  
ATOM   2921  C   TYR B 176     -20.852 -11.442  30.668  1.00 23.46           C  
ANISOU 2921  C   TYR B 176     1862   3264   3787    448   -215      5       C  
ATOM   2922  O   TYR B 176     -21.286 -11.107  31.773  1.00 21.26           O  
ANISOU 2922  O   TYR B 176     1538   2889   3650    478    -72    -76       O  
ATOM   2923  CB  TYR B 176     -22.775 -11.162  29.076  1.00 24.68           C  
ANISOU 2923  CB  TYR B 176     1704   3607   4066    596   -508    196       C  
ATOM   2924  CG  TYR B 176     -22.087  -9.948  28.459  1.00 31.69           C  
ANISOU 2924  CG  TYR B 176     2720   4389   4933    698   -535    367       C  
ATOM   2925  CD1 TYR B 176     -21.607  -9.991  27.153  1.00 28.36           C  
ANISOU 2925  CD1 TYR B 176     2398   4078   4300    675   -691    500       C  
ATOM   2926  CD2 TYR B 176     -21.869  -8.779  29.200  1.00 27.53           C  
ANISOU 2926  CD2 TYR B 176     2240   3640   4582    797   -386    386       C  
ATOM   2927  CE1 TYR B 176     -20.969  -8.903  26.584  1.00 30.75           C  
ANISOU 2927  CE1 TYR B 176     2822   4283   4579    746   -699    683       C  
ATOM   2928  CE2 TYR B 176     -21.223  -7.679  28.632  1.00 29.19           C  
ANISOU 2928  CE2 TYR B 176     2575   3722   4792    865   -407    553       C  
ATOM   2929  CZ  TYR B 176     -20.770  -7.753  27.322  1.00 31.25           C  
ANISOU 2929  CZ  TYR B 176     2917   4106   4850    836   -562    717       C  
ATOM   2930  OH  TYR B 176     -20.122  -6.684  26.728  1.00 30.25           O  
ANISOU 2930  OH  TYR B 176     2920   3859   4716    883   -570    913       O  
ATOM   2931  N   GLY B 177     -19.588 -11.229  30.293  1.00 21.40           N  
ANISOU 2931  N   GLY B 177     1773   2968   3391    411   -215     53       N  
ATOM   2932  CA  GLY B 177     -18.677 -10.451  31.100  1.00 22.05           C  
ANISOU 2932  CA  GLY B 177     1979   2886   3512    398    -89     33       C  
ATOM   2933  C   GLY B 177     -17.991 -11.220  32.197  1.00 25.34           C  
ANISOU 2933  C   GLY B 177     2478   3292   3859    276      9   -108       C  
ATOM   2934  O   GLY B 177     -17.143 -10.654  32.899  1.00 21.87           O  
ANISOU 2934  O   GLY B 177     2147   2739   3426    234     83   -134       O  
ATOM   2935  N   THR B 178     -18.327 -12.489  32.370  1.00 19.38           N  
ANISOU 2935  N   THR B 178     1681   2644   3041    208     -5   -190       N  
ATOM   2936  CA  THR B 178     -17.586 -13.327  33.284  1.00 20.98           C  
ANISOU 2936  CA  THR B 178     1972   2837   3161     99     59   -278       C  
ATOM   2937  C   THR B 178     -16.229 -13.679  32.687  1.00 18.15           C  
ANISOU 2937  C   THR B 178     1706   2509   2683     60     15   -231       C  
ATOM   2938  O   THR B 178     -16.022 -13.672  31.467  1.00 18.85           O  
ANISOU 2938  O   THR B 178     1791   2664   2707     95    -54   -158       O  
ATOM   2939  CB  THR B 178     -18.372 -14.601  33.608  1.00 25.09           C  
ANISOU 2939  CB  THR B 178     2429   3433   3674     35     65   -356       C  
ATOM   2940  OG1 THR B 178     -18.610 -15.363  32.407  1.00 19.87           O  
ANISOU 2940  OG1 THR B 178     1723   2872   2953     27    -55   -337       O  
ATOM   2941  CG2 THR B 178     -19.697 -14.232  34.264  1.00 23.04           C  
ANISOU 2941  CG2 THR B 178     2042   3160   3552     70    147   -398       C  
ATOM   2942  N   VAL B 179     -15.292 -13.997  33.565  1.00 19.89           N  
ANISOU 2942  N   VAL B 179     2003   2691   2865    -12     59   -267       N  
ATOM   2943  CA  VAL B 179     -13.947 -14.367  33.140  1.00 17.79           C  
ANISOU 2943  CA  VAL B 179     1779   2453   2526    -38     37   -220       C  
ATOM   2944  C   VAL B 179     -13.572 -15.684  33.812  1.00 17.33           C  
ANISOU 2944  C   VAL B 179     1748   2411   2426    -92     42   -273       C  
ATOM   2945  O   VAL B 179     -13.603 -15.794  35.046  1.00 19.06           O  
ANISOU 2945  O   VAL B 179     2005   2588   2650   -151     67   -310       O  
ATOM   2946  CB  VAL B 179     -12.926 -13.261  33.458  1.00 21.00           C  
ANISOU 2946  CB  VAL B 179     2224   2787   2966    -69     54   -163       C  
ATOM   2947  CG1 VAL B 179     -11.516 -13.731  33.120  1.00 17.23           C  
ANISOU 2947  CG1 VAL B 179     1739   2361   2446    -99     45   -107       C  
ATOM   2948  CG2 VAL B 179     -13.280 -11.977  32.680  1.00 14.99           C  
ANISOU 2948  CG2 VAL B 179     1455   1975   2265    -10     52    -80       C  
ATOM   2949  N   ILE B 180     -13.247 -16.687  33.003  1.00 18.51           N  
ANISOU 2949  N   ILE B 180     1896   2611   2526    -71     23   -277       N  
ATOM   2950  CA  ILE B 180     -12.812 -17.989  33.500  1.00 21.74           C  
ANISOU 2950  CA  ILE B 180     2337   2998   2927    -97     27   -309       C  
ATOM   2951  C   ILE B 180     -11.299 -18.069  33.377  1.00 15.41           C  
ANISOU 2951  C   ILE B 180     1527   2202   2128    -69     36   -245       C  
ATOM   2952  O   ILE B 180     -10.737 -17.842  32.295  1.00 19.19           O  
ANISOU 2952  O   ILE B 180     1981   2731   2579    -17     62   -216       O  
ATOM   2953  CB  ILE B 180     -13.491 -19.142  32.736  1.00 20.86           C  
ANISOU 2953  CB  ILE B 180     2237   2900   2790    -91     13   -382       C  
ATOM   2954  CG1 ILE B 180     -14.975 -19.239  33.099  1.00 15.48           C  
ANISOU 2954  CG1 ILE B 180     1518   2218   2145   -147     -1   -433       C  
ATOM   2955  CG2 ILE B 180     -12.788 -20.470  33.016  1.00 20.29           C  
ANISOU 2955  CG2 ILE B 180     2214   2761   2733    -88     30   -399       C  
ATOM   2956  CD1 ILE B 180     -15.731 -20.272  32.246  1.00 17.52           C  
ANISOU 2956  CD1 ILE B 180     1777   2494   2388   -179    -47   -515       C  
ATOM   2957  N   VAL B 181     -10.632 -18.360  34.485  1.00 18.05           N  
ANISOU 2957  N   VAL B 181     1869   2499   2489   -107     14   -211       N  
ATOM   2958  CA  VAL B 181      -9.197 -18.623  34.489  1.00 19.12           C  
ANISOU 2958  CA  VAL B 181     1950   2648   2666    -75      4   -137       C  
ATOM   2959  C   VAL B 181      -8.999 -20.090  34.818  1.00 16.73           C  
ANISOU 2959  C   VAL B 181     1671   2291   2395    -35     -4   -139       C  
ATOM   2960  O   VAL B 181      -9.455 -20.566  35.864  1.00 16.43           O  
ANISOU 2960  O   VAL B 181     1695   2203   2344    -91    -44   -132       O  
ATOM   2961  CB  VAL B 181      -8.441 -17.748  35.499  1.00 22.23           C  
ANISOU 2961  CB  VAL B 181     2319   3048   3080   -156    -60    -71       C  
ATOM   2962  CG1 VAL B 181      -6.948 -17.995  35.357  1.00 14.75           C  
ANISOU 2962  CG1 VAL B 181     1255   2139   2209   -121    -82     23       C  
ATOM   2963  CG2 VAL B 181      -8.825 -16.270  35.331  1.00 17.19           C  
ANISOU 2963  CG2 VAL B 181     1696   2402   2432   -207    -45    -87       C  
ATOM   2964  N   THR B 182      -8.277 -20.796  33.966  1.00 17.97           N  
ANISOU 2964  N   THR B 182     1787   2445   2596     65     48   -139       N  
ATOM   2965  CA  THR B 182      -8.112 -22.214  34.201  1.00 21.50           C  
ANISOU 2965  CA  THR B 182     2270   2793   3106    125     52   -145       C  
ATOM   2966  C   THR B 182      -6.657 -22.607  33.981  1.00 23.78           C  
ANISOU 2966  C   THR B 182     2447   3084   3505    244     82    -68       C  
ATOM   2967  O   THR B 182      -5.916 -21.941  33.258  1.00 23.49           O  
ANISOU 2967  O   THR B 182     2309   3139   3479    282    144    -47       O  
ATOM   2968  CB  THR B 182      -9.059 -23.020  33.303  1.00 19.48           C  
ANISOU 2968  CB  THR B 182     2108   2480   2812    141    108   -281       C  
ATOM   2969  OG1 THR B 182      -8.991 -24.403  33.667  1.00 28.47           O  
ANISOU 2969  OG1 THR B 182     3309   3471   4035    179    112   -288       O  
ATOM   2970  CG2 THR B 182      -8.658 -22.886  31.871  1.00 22.36           C  
ANISOU 2970  CG2 THR B 182     2456   2909   3131    223    199   -348       C  
ATOM   2971  N   SER B 183      -6.255 -23.685  34.639  1.00 23.43           N  
ANISOU 2971  N   SER B 183     2407   2935   3559    304     45     -8       N  
ATOM   2972  CA  SER B 183      -4.935 -24.264  34.434  1.00 23.66           C  
ANISOU 2972  CA  SER B 183     2306   2942   3742    457     82     69       C  
ATOM   2973  C   SER B 183      -4.926 -25.143  33.181  1.00 28.52           C  
ANISOU 2973  C   SER B 183     2968   3475   4392    593    248    -68       C  
ATOM   2974  O   SER B 183      -5.845 -25.940  32.948  1.00 29.50           O  
ANISOU 2974  O   SER B 183     3253   3476   4479    576    272   -186       O  
ATOM   2975  CB  SER B 183      -4.537 -25.083  35.666  1.00 20.81           C  
ANISOU 2975  CB  SER B 183     1939   2485   3483    484    -43    214       C  
ATOM   2976  OG  SER B 183      -3.387 -25.867  35.422  1.00 23.65           O  
ANISOU 2976  OG  SER B 183     2165   2784   4036    673     -1    289       O  
ATOM   2977  N   CYS B 184      -3.874 -25.006  32.377  1.00 28.64           N  
ANISOU 2977  N   CYS B 184     2846   3559   4477    716    371    -62       N  
ATOM   2978  CA  CYS B 184      -3.744 -25.796  31.160  1.00 31.46           C  
ANISOU 2978  CA  CYS B 184     3262   3849   4840    855    562   -214       C  
ATOM   2979  C   CYS B 184      -3.274 -27.217  31.423  1.00 32.60           C  
ANISOU 2979  C   CYS B 184     3419   3785   5184   1025    602   -214       C  
ATOM   2980  O   CYS B 184      -3.069 -27.969  30.468  1.00 37.32           O  
ANISOU 2980  O   CYS B 184     4078   4292   5810   1161    782   -363       O  
ATOM   2981  CB  CYS B 184      -2.783 -25.115  30.187  1.00 29.92           C  
ANISOU 2981  CB  CYS B 184     2917   3815   4637    927    725   -205       C  
ATOM   2982  SG  CYS B 184      -3.325 -23.469  29.696  1.00 32.01           S  
ANISOU 2982  SG  CYS B 184     3198   4281   4682    743    697   -188       S  
ATOM   2983  N   ALA B 185      -3.080 -27.602  32.678  1.00 29.01           N  
ANISOU 2983  N   ALA B 185     2920   3243   4858   1026    446    -49       N  
ATOM   2984  CA  ALA B 185      -2.712 -28.981  32.951  1.00 32.53           C  
ANISOU 2984  CA  ALA B 185     3397   3452   5511   1195    471    -19       C  
ATOM   2985  C   ALA B 185      -3.913 -29.920  32.968  1.00 28.06           C  
ANISOU 2985  C   ALA B 185     3097   2668   4896   1120    464   -149       C  
ATOM   2986  O   ALA B 185      -3.732 -31.127  33.149  1.00 32.89           O  
ANISOU 2986  O   ALA B 185     3780   3030   5686   1247    493   -137       O  
ATOM   2987  CB  ALA B 185      -1.962 -29.071  34.280  1.00 37.71           C  
ANISOU 2987  CB  ALA B 185     3903   4105   6322   1231    283    249       C  
ATOM   2988  N   HIS B 186      -5.123 -29.406  32.777  1.00 29.85           N  
ANISOU 2988  N   HIS B 186     3458   2970   4913    919    426   -263       N  
ATOM   2989  CA  HIS B 186      -6.341 -30.188  32.907  1.00 30.12           C  
ANISOU 2989  CA  HIS B 186     3704   2829   4912    797    394   -364       C  
ATOM   2990  C   HIS B 186      -7.056 -30.238  31.565  1.00 32.08           C  
ANISOU 2990  C   HIS B 186     4079   3091   5019    747    500   -627       C  
ATOM   2991  O   HIS B 186      -7.206 -29.206  30.901  1.00 26.71           O  
ANISOU 2991  O   HIS B 186     3349   2631   4170    692    517   -683       O  
ATOM   2992  CB  HIS B 186      -7.266 -29.589  33.973  1.00 24.46           C  
ANISOU 2992  CB  HIS B 186     3011   2200   4081    587    242   -256       C  
ATOM   2993  CG  HIS B 186      -6.634 -29.450  35.321  1.00 31.99           C  
ANISOU 2993  CG  HIS B 186     3878   3176   5099    598    115     -7       C  
ATOM   2994  ND1 HIS B 186      -6.099 -30.520  36.007  1.00 36.71           N  
ANISOU 2994  ND1 HIS B 186     4501   3576   5872    704     72    142       N  
ATOM   2995  CD2 HIS B 186      -6.470 -28.370  36.123  1.00 29.53           C  
ANISOU 2995  CD2 HIS B 186     3474   3058   4689    507      5    119       C  
ATOM   2996  CE1 HIS B 186      -5.618 -30.104  37.165  1.00 34.41           C  
ANISOU 2996  CE1 HIS B 186     4128   3383   5562    674    -77    362       C  
ATOM   2997  NE2 HIS B 186      -5.832 -28.804  37.261  1.00 33.34           N  
ANISOU 2997  NE2 HIS B 186     3929   3484   5255    545   -116    334       N  
ATOM   2998  N   ARG B 187      -7.491 -31.437  31.178  1.00 27.93           N  
ANISOU 2998  N   ARG B 187     3730   2321   4560    755    556   -782       N  
ATOM   2999  CA  ARG B 187      -8.362 -31.600  30.024  1.00 29.11           C  
ANISOU 2999  CA  ARG B 187     4034   2473   4552    652    603  -1043       C  
ATOM   3000  C   ARG B 187      -9.668 -30.859  30.262  1.00 27.38           C  
ANISOU 3000  C   ARG B 187     3816   2413   4176    413    459  -1034       C  
ATOM   3001  O   ARG B 187     -10.133 -30.734  31.395  1.00 27.87           O  
ANISOU 3001  O   ARG B 187     3837   2464   4289    309    356   -878       O  
ATOM   3002  CB  ARG B 187      -8.642 -33.084  29.772  1.00 42.23           C  
ANISOU 3002  CB  ARG B 187     5902   3801   6344    665    661  -1208       C  
ATOM   3003  CG  ARG B 187      -7.417 -33.895  29.397  1.00 48.15           C  
ANISOU 3003  CG  ARG B 187     6665   4356   7273    935    839  -1258       C  
ATOM   3004  CD  ARG B 187      -7.728 -35.374  29.165  1.00 52.64           C  
ANISOU 3004  CD  ARG B 187     7465   4562   7972    941    887  -1422       C  
ATOM   3005  NE  ARG B 187      -8.426 -35.627  27.903  1.00 64.25           N  
ANISOU 3005  NE  ARG B 187     9124   6077   9211    818    901  -1710       N  
ATOM   3006  CZ  ARG B 187      -7.846 -35.648  26.702  1.00 70.67           C  
ANISOU 3006  CZ  ARG B 187     9984   6994   9872    942   1028  -1878       C  
ATOM   3007  NH1 ARG B 187      -6.546 -35.411  26.572  1.00 71.86           N  
ANISOU 3007  NH1 ARG B 187     9982   7230  10092   1188   1173  -1792       N  
ATOM   3008  NH2 ARG B 187      -8.573 -35.900  25.619  1.00 71.90           N  
ANISOU 3008  NH2 ARG B 187    10328   7188   9801    809    999  -2122       N  
ATOM   3009  N   HIS B 188     -10.260 -30.352  29.187  1.00 30.06           N  
ANISOU 3009  N   HIS B 188     4196   2908   4316    332    457  -1196       N  
ATOM   3010  CA  HIS B 188     -11.470 -29.551  29.322  1.00 28.92           C  
ANISOU 3010  CA  HIS B 188     4009   2931   4049    140    322  -1174       C  
ATOM   3011  C   HIS B 188     -12.186 -29.524  27.982  1.00 26.71           C  
ANISOU 3011  C   HIS B 188     3829   2742   3577     53    298  -1388       C  
ATOM   3012  O   HIS B 188     -11.626 -29.894  26.950  1.00 29.39           O  
ANISOU 3012  O   HIS B 188     4278   3062   3828    145    403  -1545       O  
ATOM   3013  CB  HIS B 188     -11.162 -28.126  29.813  1.00 31.88           C  
ANISOU 3013  CB  HIS B 188     4213   3531   4370    162    286   -988       C  
ATOM   3014  CG  HIS B 188     -10.222 -27.377  28.923  1.00 48.09           C  
ANISOU 3014  CG  HIS B 188     6211   5740   6319    287    377   -989       C  
ATOM   3015  ND1 HIS B 188      -8.919 -27.105  29.276  1.00 53.76           N  
ANISOU 3015  ND1 HIS B 188     6816   6479   7133    429    455   -858       N  
ATOM   3016  CD2 HIS B 188     -10.391 -26.861  27.683  1.00 51.01           C  
ANISOU 3016  CD2 HIS B 188     6622   6264   6495    279    404  -1090       C  
ATOM   3017  CE1 HIS B 188      -8.326 -26.453  28.294  1.00 52.80           C  
ANISOU 3017  CE1 HIS B 188     6658   6509   6896    498    552   -881       C  
ATOM   3018  NE2 HIS B 188      -9.197 -26.291  27.316  1.00 53.97           N  
ANISOU 3018  NE2 HIS B 188     6916   6739   6850    411    526  -1017       N  
ATOM   3019  N   GLU B 189     -13.436 -29.063  28.015  1.00 24.64           N  
ANISOU 3019  N   GLU B 189     3524   2594   3244   -123    157  -1389       N  
ATOM   3020  CA  GLU B 189     -14.311 -29.099  26.855  1.00 26.06           C  
ANISOU 3020  CA  GLU B 189     3784   2869   3248   -244     68  -1570       C  
ATOM   3021  C   GLU B 189     -15.343 -27.993  26.996  1.00 27.67           C  
ANISOU 3021  C   GLU B 189     3831   3290   3391   -352    -78  -1462       C  
ATOM   3022  O   GLU B 189     -15.557 -27.453  28.084  1.00 25.84           O  
ANISOU 3022  O   GLU B 189     3462   3077   3278   -362    -90  -1294       O  
ATOM   3023  CB  GLU B 189     -15.021 -30.462  26.740  1.00 28.38           C  
ANISOU 3023  CB  GLU B 189     4225   2937   3621   -393     25  -1758       C  
ATOM   3024  CG  GLU B 189     -15.828 -30.787  27.997  1.00 27.68           C  
ANISOU 3024  CG  GLU B 189     4048   2734   3736   -533    -38  -1636       C  
ATOM   3025  CD  GLU B 189     -16.785 -31.958  27.838  1.00 35.82           C  
ANISOU 3025  CD  GLU B 189     5188   3572   4849   -747   -110  -1802       C  
ATOM   3026  OE1 GLU B 189     -17.081 -32.343  26.692  1.00 40.95           O  
ANISOU 3026  OE1 GLU B 189     5963   4239   5356   -806   -176  -1986       O  
ATOM   3027  OE2 GLU B 189     -17.255 -32.489  28.870  1.00 37.02           O  
ANISOU 3027  OE2 GLU B 189     5307   3570   5189   -857   -111  -1702       O  
ATOM   3028  N   VAL B 190     -15.996 -27.671  25.884  1.00 25.80           N  
ANISOU 3028  N   VAL B 190     3624   3215   2965   -427   -189  -1561       N  
ATOM   3029  CA  VAL B 190     -17.226 -26.892  25.901  1.00 28.59           C  
ANISOU 3029  CA  VAL B 190     3823   3739   3300   -543   -361  -1486       C  
ATOM   3030  C   VAL B 190     -18.334 -27.783  25.372  1.00 28.13           C  
ANISOU 3030  C   VAL B 190     3819   3646   3224   -747   -511  -1666       C  
ATOM   3031  O   VAL B 190     -18.217 -28.343  24.275  1.00 33.54           O  
ANISOU 3031  O   VAL B 190     4682   4331   3731   -786   -544  -1858       O  
ATOM   3032  CB  VAL B 190     -17.107 -25.600  25.078  1.00 31.62           C  
ANISOU 3032  CB  VAL B 190     4159   4364   3490   -461   -412  -1391       C  
ATOM   3033  CG1 VAL B 190     -18.464 -24.876  25.027  1.00 27.84           C  
ANISOU 3033  CG1 VAL B 190     3507   4043   3027   -560   -608  -1311       C  
ATOM   3034  CG2 VAL B 190     -16.015 -24.699  25.671  1.00 28.27           C  
ANISOU 3034  CG2 VAL B 190     3670   3952   3117   -296   -267  -1213       C  
ATOM   3035  N   ARG B 191     -19.394 -27.936  26.159  1.00 32.23           N  
ANISOU 3035  N   ARG B 191     4186   4135   3923   -892   -591  -1614       N  
ATOM   3036  CA  ARG B 191     -20.504 -28.790  25.770  1.00 34.74           C  
ANISOU 3036  CA  ARG B 191     4519   4408   4273  -1103   -739  -1730       C  
ATOM   3037  C   ARG B 191     -21.390 -28.080  24.753  1.00 33.48           C  
ANISOU 3037  C   ARG B 191     4268   4496   3958  -1154   -954  -1703       C  
ATOM   3038  O   ARG B 191     -21.285 -26.871  24.533  1.00 35.26           O  
ANISOU 3038  O   ARG B 191     4381   4929   4087  -1049   -992  -1601       O  
ATOM   3039  CB  ARG B 191     -21.301 -29.214  26.997  1.00 36.99           C  
ANISOU 3039  CB  ARG B 191     4660   4577   4818  -1230   -716  -1633       C  
ATOM   3040  CG  ARG B 191     -20.479 -30.085  27.910  1.00 40.11           C  
ANISOU 3040  CG  ARG B 191     5186   4702   5352  -1198   -537  -1639       C  
ATOM   3041  CD  ARG B 191     -21.241 -30.542  29.128  1.00 44.52           C  
ANISOU 3041  CD  ARG B 191     5636   5151   6130  -1336   -496  -1518       C  
ATOM   3042  NE  ARG B 191     -20.513 -31.621  29.783  1.00 42.42           N  
ANISOU 3042  NE  ARG B 191     5548   4591   5980  -1323   -366  -1520       N  
ATOM   3043  CZ  ARG B 191     -20.775 -32.078  31.001  1.00 40.02           C  
ANISOU 3043  CZ  ARG B 191     5212   4151   5844  -1409   -282  -1384       C  
ATOM   3044  NH1 ARG B 191     -21.759 -31.551  31.724  1.00 33.10           N  
ANISOU 3044  NH1 ARG B 191     4126   3418   5034  -1513   -283  -1255       N  
ATOM   3045  NH2 ARG B 191     -20.042 -33.063  31.495  1.00 43.17           N  
ANISOU 3045  NH2 ARG B 191     5791   4269   6343  -1375   -184  -1363       N  
ATOM   3046  N   THR B 192     -22.263 -28.867  24.131  1.00 34.75           N  
ANISOU 3046  N   THR B 192     4483   4615   4105  -1315  -1113  -1786       N  
ATOM   3047  CA  THR B 192     -23.072 -28.424  23.004  1.00 38.81           C  
ANISOU 3047  CA  THR B 192     4957   5331   4458  -1374  -1356  -1780       C  
ATOM   3048  C   THR B 192     -23.746 -27.080  23.264  1.00 42.42           C  
ANISOU 3048  C   THR B 192     5120   6018   4979  -1320  -1450  -1574       C  
ATOM   3049  O   THR B 192     -24.296 -26.838  24.341  1.00 39.87           O  
ANISOU 3049  O   THR B 192     4571   5680   4899  -1340  -1395  -1457       O  
ATOM   3050  CB  THR B 192     -24.134 -29.484  22.705  1.00 43.69           C  
ANISOU 3050  CB  THR B 192     5590   5845   5167  -1583  -1531  -1876       C  
ATOM   3051  OG1 THR B 192     -23.526 -30.783  22.709  1.00 45.42           O  
ANISOU 3051  OG1 THR B 192     6065   5794   5398  -1619  -1416  -2055       O  
ATOM   3052  CG2 THR B 192     -24.783 -29.225  21.358  1.00 43.50           C  
ANISOU 3052  CG2 THR B 192     5588   5999   4942  -1631  -1804  -1923       C  
ATOM   3053  N   VAL B 193     -23.685 -26.201  22.268  1.00 36.17           N  
ANISOU 3053  N   VAL B 193     4830   5476   3436  -1770   -574   -588       N  
ATOM   3054  CA  VAL B 193     -24.494 -24.987  22.257  1.00 34.75           C  
ANISOU 3054  CA  VAL B 193     4314   5529   3361  -1692   -656   -544       C  
ATOM   3055  C   VAL B 193     -25.881 -25.360  21.745  1.00 34.86           C  
ANISOU 3055  C   VAL B 193     4199   5733   3314  -1946   -794   -539       C  
ATOM   3056  O   VAL B 193     -26.020 -25.890  20.638  1.00 33.43           O  
ANISOU 3056  O   VAL B 193     4176   5507   3018  -2061   -881   -550       O  
ATOM   3057  CB  VAL B 193     -23.854 -23.901  21.383  1.00 34.66           C  
ANISOU 3057  CB  VAL B 193     4289   5500   3382  -1471   -698   -509       C  
ATOM   3058  CG1 VAL B 193     -24.810 -22.734  21.209  1.00 36.28           C  
ANISOU 3058  CG1 VAL B 193     4176   5928   3682  -1399   -803   -455       C  
ATOM   3059  CG2 VAL B 193     -22.535 -23.426  21.991  1.00 26.29           C  
ANISOU 3059  CG2 VAL B 193     3299   4285   2406  -1239   -569   -506       C  
ATOM   3060  N   ARG B 194     -26.911 -25.082  22.546  1.00 35.90           N  
ANISOU 3060  N   ARG B 194     4036   6073   3529  -2005   -796   -512       N  
ATOM   3061  CA  ARG B 194     -28.263 -25.563  22.270  1.00 39.47           C  
ANISOU 3061  CA  ARG B 194     4359   6669   3968  -2191   -867   -472       C  
ATOM   3062  C   ARG B 194     -29.164 -24.532  21.597  1.00 38.69           C  
ANISOU 3062  C   ARG B 194     3978   6790   3932  -2087   -991   -411       C  
ATOM   3063  O   ARG B 194     -30.191 -24.913  21.021  1.00 38.99           O  
ANISOU 3063  O   ARG B 194     3944   6935   3936  -2229  -1081   -379       O  
ATOM   3064  CB  ARG B 194     -28.923 -26.031  23.575  1.00 44.43           C  
ANISOU 3064  CB  ARG B 194     4850   7387   4643  -2310   -763   -459       C  
ATOM   3065  CG  ARG B 194     -29.068 -27.539  23.689  1.00 49.01           C  
ANISOU 3065  CG  ARG B 194     5671   7825   5125  -2577   -723   -470       C  
ATOM   3066  CD  ARG B 194     -29.863 -27.925  24.928  1.00 50.07           C  
ANISOU 3066  CD  ARG B 194     5639   8088   5296  -2707   -628   -431       C  
ATOM   3067  NE  ARG B 194     -29.224 -27.441  26.149  1.00 54.68           N  
ANISOU 3067  NE  ARG B 194     6157   8680   5937  -2568   -500   -448       N  
ATOM   3068  CZ  ARG B 194     -28.108 -27.953  26.658  1.00 58.25           C  
ANISOU 3068  CZ  ARG B 194     6870   8918   6343  -2569   -411   -489       C  
ATOM   3069  NH1 ARG B 194     -27.497 -28.961  26.045  1.00 67.25           N  
ANISOU 3069  NH1 ARG B 194     8366   9800   7385  -2673   -425   -515       N  
ATOM   3070  NH2 ARG B 194     -27.602 -27.464  27.782  1.00 52.01           N  
ANISOU 3070  NH2 ARG B 194     6023   8125   5615  -2363   -281   -483       N  
ATOM   3071  N   ALA B 195     -28.806 -23.254  21.659  1.00 34.91           N  
ANISOU 3071  N   ALA B 195     3347   6374   3544  -1841  -1002   -392       N  
ATOM   3072  CA  ALA B 195     -29.557 -22.186  21.034  1.00 36.03           C  
ANISOU 3072  CA  ALA B 195     3244   6693   3754  -1698  -1116   -321       C  
ATOM   3073  C   ALA B 195     -28.674 -20.943  20.973  1.00 43.52           C  
ANISOU 3073  C   ALA B 195     4158   7602   4774  -1432  -1117   -309       C  
ATOM   3074  O   ALA B 195     -27.849 -20.716  21.863  1.00 43.36           O  
ANISOU 3074  O   ALA B 195     4203   7448   4824  -1302   -981   -348       O  
ATOM   3075  CB  ALA B 195     -30.837 -21.906  21.812  1.00 37.75           C  
ANISOU 3075  CB  ALA B 195     3140   7126   4075  -1687  -1088   -281       C  
ATOM   3076  N   ASN B 196     -28.848 -20.156  19.913  1.00 34.87           N  
ANISOU 3076  N   ASN B 196     3008   6565   3676  -1316  -1244   -238       N  
ATOM   3077  CA  ASN B 196     -28.169 -18.861  19.687  1.00 40.34           C  
ANISOU 3077  CA  ASN B 196     3679   7189   4460  -1035  -1245   -189       C  
ATOM   3078  C   ASN B 196     -26.644 -19.062  19.624  1.00 37.55           C  
ANISOU 3078  C   ASN B 196     3645   6549   4073   -974  -1132   -226       C  
ATOM   3079  O   ASN B 196     -26.158 -20.133  19.242  1.00 44.92           O  
ANISOU 3079  O   ASN B 196     4825   7376   4866  -1140  -1116   -273       O  
ATOM   3080  CB  ASN B 196     -28.637 -17.848  20.724  1.00 37.05           C  
ANISOU 3080  CB  ASN B 196     2989   6861   4227   -826  -1179   -179       C  
ATOM   3081  CG  ASN B 196     -30.047 -17.346  20.446  1.00 57.13           C  
ANISOU 3081  CG  ASN B 196     5247   9636   6825   -781  -1283   -104       C  
ATOM   3082  OD1 ASN B 196     -30.231 -16.262  19.890  1.00 72.50           O  
ANISOU 3082  OD1 ASN B 196     7092  11614   8842   -577  -1364    -21       O  
ATOM   3083  ND2 ASN B 196     -31.048 -18.140  20.818  1.00 53.56           N  
ANISOU 3083  ND2 ASN B 196     4697   9302   6351   -957  -1262   -120       N  
ATOM   3084  N   GLU B 197     -25.862 -18.042  19.976  1.00 33.05           N  
ANISOU 3084  N   GLU B 197     3077   5850   3631   -736  -1055   -207       N  
ATOM   3085  CA  GLU B 197     -24.430 -18.058  19.711  1.00 42.02           C  
ANISOU 3085  CA  GLU B 197     4470   6755   4742   -666   -971   -212       C  
ATOM   3086  C   GLU B 197     -23.607 -17.708  20.946  1.00 36.04           C  
ANISOU 3086  C   GLU B 197     3721   5860   4113   -537   -825   -265       C  
ATOM   3087  O   GLU B 197     -23.914 -16.764  21.682  1.00 31.86           O  
ANISOU 3087  O   GLU B 197     3012   5365   3727   -391   -806   -268       O  
ATOM   3088  CB  GLU B 197     -24.071 -17.097  18.585  1.00 48.84           C  
ANISOU 3088  CB  GLU B 197     5367   7582   5608   -526  -1046   -109       C  
ATOM   3089  CG  GLU B 197     -24.481 -15.675  18.827  1.00 52.10           C  
ANISOU 3089  CG  GLU B 197     5567   8036   6192   -316  -1082    -42       C  
ATOM   3090  CD  GLU B 197     -23.582 -14.721  18.085  1.00 60.30           C  
ANISOU 3090  CD  GLU B 197     6714   8929   7269   -163  -1083     53       C  
ATOM   3091  OE1 GLU B 197     -23.082 -13.775  18.722  1.00 59.18           O  
ANISOU 3091  OE1 GLU B 197     6533   8662   7288     -2  -1016     56       O  
ATOM   3092  OE2 GLU B 197     -23.355 -14.937  16.872  1.00 62.24           O  
ANISOU 3092  OE2 GLU B 197     7094   9180   7373   -216  -1148    123       O  
ATOM   3093  N   ARG B 198     -22.539 -18.469  21.142  1.00 30.15           N  
ANISOU 3093  N   ARG B 198     3193   4956   3305   -583   -727   -309       N  
ATOM   3094  CA  ARG B 198     -21.604 -18.274  22.237  1.00 27.67           C  
ANISOU 3094  CA  ARG B 198     2915   4516   3084   -480   -603   -355       C  
ATOM   3095  C   ARG B 198     -20.336 -17.653  21.658  1.00 29.05           C  
ANISOU 3095  C   ARG B 198     3209   4538   3291   -353   -573   -304       C  
ATOM   3096  O   ARG B 198     -19.733 -18.200  20.726  1.00 29.52           O  
ANISOU 3096  O   ARG B 198     3446   4534   3235   -398   -568   -275       O  
ATOM   3097  CB  ARG B 198     -21.333 -19.612  22.918  1.00 28.82           C  
ANISOU 3097  CB  ARG B 198     3199   4611   3138   -616   -517   -422       C  
ATOM   3098  CG  ARG B 198     -20.577 -19.598  24.223  1.00 22.14           C  
ANISOU 3098  CG  ARG B 198     2369   3683   2361   -536   -403   -470       C  
ATOM   3099  CD  ARG B 198     -20.105 -21.026  24.401  1.00 27.25           C  
ANISOU 3099  CD  ARG B 198     3228   4242   2885   -659   -335   -498       C  
ATOM   3100  NE  ARG B 198     -19.531 -21.352  25.699  1.00 26.37           N  
ANISOU 3100  NE  ARG B 198     3148   4076   2795   -621   -236   -535       N  
ATOM   3101  CZ  ARG B 198     -18.230 -21.370  25.950  1.00 22.91           C  
ANISOU 3101  CZ  ARG B 198     2821   3511   2371   -513   -171   -530       C  
ATOM   3102  NH1 ARG B 198     -17.352 -21.048  24.996  1.00 26.47           N  
ANISOU 3102  NH1 ARG B 198     3354   3879   2826   -432   -178   -489       N  
ATOM   3103  NH2 ARG B 198     -17.807 -21.711  27.157  1.00 25.17           N  
ANISOU 3103  NH2 ARG B 198     3128   3775   2660   -487    -99   -557       N  
ATOM   3104  N   THR B 199     -19.958 -16.490  22.169  1.00 31.37           N  
ANISOU 3104  N   THR B 199     3406   4776   3737   -198   -553   -293       N  
ATOM   3105  CA  THR B 199     -18.772 -15.796  21.691  1.00 26.41           C  
ANISOU 3105  CA  THR B 199     2863   4010   3161    -98   -525   -232       C  
ATOM   3106  C   THR B 199     -17.860 -15.565  22.880  1.00 27.01           C  
ANISOU 3106  C   THR B 199     2938   3988   3335    -34   -436   -293       C  
ATOM   3107  O   THR B 199     -18.304 -15.048  23.910  1.00 29.01           O  
ANISOU 3107  O   THR B 199     3069   4268   3686     20   -433   -357       O  
ATOM   3108  CB  THR B 199     -19.135 -14.482  21.004  1.00 23.29           C  
ANISOU 3108  CB  THR B 199     2372   3617   2860     12   -609   -141       C  
ATOM   3109  OG1 THR B 199     -20.188 -14.726  20.066  1.00 24.79           O  
ANISOU 3109  OG1 THR B 199     2526   3944   2951    -49   -714    -90       O  
ATOM   3110  CG2 THR B 199     -17.930 -13.942  20.263  1.00 28.48           C  
ANISOU 3110  CG2 THR B 199     3140   4143   3537     67   -578    -51       C  
ATOM   3111  N   SER B 200     -16.601 -15.983  22.754  1.00 24.10           N  
ANISOU 3111  N   SER B 200     2703   3525   2931    -36   -365   -277       N  
ATOM   3112  CA  SER B 200     -15.674 -15.899  23.866  1.00 21.42           C  
ANISOU 3112  CA  SER B 200     2359   3115   2663      9   -296   -330       C  
ATOM   3113  C   SER B 200     -14.303 -15.509  23.355  1.00 24.45           C  
ANISOU 3113  C   SER B 200     2803   3401   3084     59   -255   -257       C  
ATOM   3114  O   SER B 200     -13.864 -15.989  22.307  1.00 23.44           O  
ANISOU 3114  O   SER B 200     2783   3263   2860     39   -229   -189       O  
ATOM   3115  CB  SER B 200     -15.589 -17.227  24.631  1.00 26.36           C  
ANISOU 3115  CB  SER B 200     3066   3766   3185    -61   -232   -396       C  
ATOM   3116  OG  SER B 200     -14.945 -18.208  23.842  1.00 33.87           O  
ANISOU 3116  OG  SER B 200     4181   4674   4014    -99   -186   -356       O  
ATOM   3117  N   LEU B 201     -13.642 -14.616  24.097  1.00 25.95           N  
ANISOU 3117  N   LEU B 201     2922   3526   3410    117   -250   -275       N  
ATOM   3118  CA  LEU B 201     -12.266 -14.226  23.831  1.00 22.04           C  
ANISOU 3118  CA  LEU B 201     2447   2955   2970    141   -210   -207       C  
ATOM   3119  C   LEU B 201     -11.350 -15.098  24.678  1.00 17.99           C  
ANISOU 3119  C   LEU B 201     1967   2454   2414    138   -143   -253       C  
ATOM   3120  O   LEU B 201     -11.398 -15.031  25.907  1.00 21.93           O  
ANISOU 3120  O   LEU B 201     2414   2964   2952    145   -155   -342       O  
ATOM   3121  CB  LEU B 201     -12.059 -12.742  24.160  1.00 23.36           C  
ANISOU 3121  CB  LEU B 201     2524   3035   3316    181   -259   -202       C  
ATOM   3122  CG  LEU B 201     -10.730 -12.045  23.800  1.00 26.99           C  
ANISOU 3122  CG  LEU B 201     2977   3411   3868    175   -234   -111       C  
ATOM   3123  CD1 LEU B 201     -10.896 -10.534  23.903  1.00 27.43           C  
ANISOU 3123  CD1 LEU B 201     2978   3349   4095    196   -302    -99       C  
ATOM   3124  CD2 LEU B 201      -9.544 -12.490  24.622  1.00 23.85           C  
ANISOU 3124  CD2 LEU B 201     2559   3029   3475    159   -187   -146       C  
ATOM   3125  N   VAL B 202     -10.500 -15.887  24.025  1.00 18.56           N  
ANISOU 3125  N   VAL B 202     2127   2528   2395    144    -71   -189       N  
ATOM   3126  CA  VAL B 202      -9.597 -16.827  24.688  1.00 17.66           C  
ANISOU 3126  CA  VAL B 202     2053   2429   2228    170     -3   -208       C  
ATOM   3127  C   VAL B 202      -8.159 -16.347  24.534  1.00 20.73           C  
ANISOU 3127  C   VAL B 202     2378   2805   2695    211     37   -129       C  
ATOM   3128  O   VAL B 202      -7.731 -16.017  23.421  1.00 24.07           O  
ANISOU 3128  O   VAL B 202     2812   3217   3117    218     72    -31       O  
ATOM   3129  CB  VAL B 202      -9.730 -18.242  24.095  1.00 19.96           C  
ANISOU 3129  CB  VAL B 202     2507   2728   2349    165     62   -202       C  
ATOM   3130  CG1 VAL B 202      -8.820 -19.186  24.823  1.00 20.23           C  
ANISOU 3130  CG1 VAL B 202     2587   2761   2337    221    131   -211       C  
ATOM   3131  CG2 VAL B 202     -11.172 -18.708  24.119  1.00 29.50           C  
ANISOU 3131  CG2 VAL B 202     3765   3959   3483     86     14   -267       C  
ATOM   3132  N   TYR B 203      -7.395 -16.353  25.628  1.00 23.17           N  
ANISOU 3132  N   TYR B 203     2615   3134   3056    231     33   -162       N  
ATOM   3133  CA  TYR B 203      -5.956 -16.150  25.499  1.00 22.22           C  
ANISOU 3133  CA  TYR B 203     2416   3036   2990    263     76    -78       C  
ATOM   3134  C   TYR B 203      -5.201 -17.003  26.511  1.00 22.38           C  
ANISOU 3134  C   TYR B 203     2421   3116   2967    319     99   -103       C  
ATOM   3135  O   TYR B 203      -5.775 -17.490  27.490  1.00 20.93           O  
ANISOU 3135  O   TYR B 203     2278   2943   2733    318     66   -191       O  
ATOM   3136  CB  TYR B 203      -5.549 -14.656  25.595  1.00 21.70           C  
ANISOU 3136  CB  TYR B 203     2219   2931   3097    205     10    -53       C  
ATOM   3137  CG  TYR B 203      -6.006 -13.833  26.793  1.00 24.64           C  
ANISOU 3137  CG  TYR B 203     2530   3266   3566    162    -94   -170       C  
ATOM   3138  CD1 TYR B 203      -5.087 -13.354  27.732  1.00 21.72           C  
ANISOU 3138  CD1 TYR B 203     2056   2914   3282    131   -144   -200       C  
ATOM   3139  CD2 TYR B 203      -7.326 -13.459  26.940  1.00 18.74           C  
ANISOU 3139  CD2 TYR B 203     1822   2473   2825    154   -145   -251       C  
ATOM   3140  CE1 TYR B 203      -5.497 -12.565  28.802  1.00 20.93           C  
ANISOU 3140  CE1 TYR B 203     1927   2771   3254     94   -238   -325       C  
ATOM   3141  CE2 TYR B 203      -7.743 -12.677  28.009  1.00 18.96           C  
ANISOU 3141  CE2 TYR B 203     1806   2466   2933    138   -222   -367       C  
ATOM   3142  CZ  TYR B 203      -6.837 -12.232  28.928  1.00 22.16           C  
ANISOU 3142  CZ  TYR B 203     2141   2872   3407    108   -267   -412       C  
ATOM   3143  OH  TYR B 203      -7.280 -11.450  29.983  1.00 28.97           O  
ANISOU 3143  OH  TYR B 203     2989   3692   4328     96   -342   -548       O  
ATOM   3144  N   PHE B 204      -3.888 -17.185  26.243  1.00 22.46           N  
ANISOU 3144  N   PHE B 204     2365   3179   2991    376    161    -10       N  
ATOM   3145  CA  PHE B 204      -3.024 -18.115  26.969  1.00 24.08           C  
ANISOU 3145  CA  PHE B 204     2552   3455   3141    468    196      5       C  
ATOM   3146  C   PHE B 204      -1.769 -17.428  27.480  1.00 23.52           C  
ANISOU 3146  C   PHE B 204     2281   3469   3187    458    156     56       C  
ATOM   3147  O   PHE B 204      -1.117 -16.669  26.750  1.00 24.36           O  
ANISOU 3147  O   PHE B 204     2281   3592   3383    419    179    143       O  
ATOM   3148  CB  PHE B 204      -2.603 -19.301  26.087  1.00 25.31           C  
ANISOU 3148  CB  PHE B 204     2828   3616   3174    586    330     76       C  
ATOM   3149  CG  PHE B 204      -3.754 -20.058  25.541  1.00 26.52           C  
ANISOU 3149  CG  PHE B 204     3191   3684   3202    572    360     22       C  
ATOM   3150  CD1 PHE B 204      -4.214 -21.191  26.187  1.00 28.33           C  
ANISOU 3150  CD1 PHE B 204     3560   3876   3327    605    369    -35       C  
ATOM   3151  CD2 PHE B 204      -4.415 -19.608  24.408  1.00 32.80           C  
ANISOU 3151  CD2 PHE B 204     4042   4437   3982    510    366     33       C  
ATOM   3152  CE1 PHE B 204      -5.297 -21.880  25.706  1.00 30.08           C  
ANISOU 3152  CE1 PHE B 204     3970   4019   3440    556    385    -87       C  
ATOM   3153  CE2 PHE B 204      -5.501 -20.295  23.913  1.00 32.49           C  
ANISOU 3153  CE2 PHE B 204     4183   4338   3823    474    371    -22       C  
ATOM   3154  CZ  PHE B 204      -5.941 -21.432  24.561  1.00 30.93           C  
ANISOU 3154  CZ  PHE B 204     4118   4102   3532    486    380    -86       C  
ATOM   3155  N   TYR B 205      -1.411 -17.754  28.714  1.00 20.86           N  
ANISOU 3155  N   TYR B 205     1894   3197   2837    487     97     14       N  
ATOM   3156  CA  TYR B 205      -0.270 -17.187  29.415  1.00 25.21           C  
ANISOU 3156  CA  TYR B 205     2247   3851   3481    462     26     45       C  
ATOM   3157  C   TYR B 205       0.800 -18.243  29.605  1.00 27.17           C  
ANISOU 3157  C   TYR B 205     2445   4217   3661    612     88    137       C  
ATOM   3158  O   TYR B 205       0.493 -19.402  29.906  1.00 31.71           O  
ANISOU 3158  O   TYR B 205     3161   4777   4111    724    133    124       O  
ATOM   3159  CB  TYR B 205      -0.657 -16.684  30.804  1.00 28.58           C  
ANISOU 3159  CB  TYR B 205     2650   4284   3927    386   -113    -81       C  
ATOM   3160  CG  TYR B 205      -1.205 -15.291  30.905  1.00 23.94           C  
ANISOU 3160  CG  TYR B 205     2031   3607   3457    244   -203   -168       C  
ATOM   3161  CD1 TYR B 205      -0.362 -14.190  30.939  1.00 22.98           C  
ANISOU 3161  CD1 TYR B 205     1756   3499   3478    137   -276   -144       C  
ATOM   3162  CD2 TYR B 205      -2.570 -15.078  31.034  1.00 26.19           C  
ANISOU 3162  CD2 TYR B 205     2442   3794   3715    217   -220   -275       C  
ATOM   3163  CE1 TYR B 205      -0.870 -12.914  31.067  1.00 25.42           C  
ANISOU 3163  CE1 TYR B 205     2071   3689   3898     16   -359   -230       C  
ATOM   3164  CE2 TYR B 205      -3.087 -13.797  31.160  1.00 26.99           C  
ANISOU 3164  CE2 TYR B 205     2527   3801   3928    121   -297   -358       C  
ATOM   3165  CZ  TYR B 205      -2.239 -12.727  31.173  1.00 24.56           C  
ANISOU 3165  CZ  TYR B 205     2101   3473   3759     25   -366   -338       C  
ATOM   3166  OH  TYR B 205      -2.769 -11.469  31.304  1.00 34.47           O  
ANISOU 3166  OH  TYR B 205     3374   4597   5126    -60   -440   -425       O  
ATOM   3167  N   SER B 206       2.060 -17.827  29.490  1.00 25.82           N  
ANISOU 3167  N   SER B 206     2065   4166   3579    612     85    235       N  
ATOM   3168  CA  SER B 206       3.180 -18.708  29.768  1.00 27.62           C  
ANISOU 3168  CA  SER B 206     2192   4539   3762    771    129    333       C  
ATOM   3169  C   SER B 206       4.264 -17.912  30.470  1.00 27.20           C  
ANISOU 3169  C   SER B 206     1869   4641   3823    686     10    370       C  
ATOM   3170  O   SER B 206       4.304 -16.683  30.388  1.00 27.44           O  
ANISOU 3170  O   SER B 206     1798   4649   3980    502    -66    345       O  
ATOM   3171  CB  SER B 206       3.739 -19.340  28.491  1.00 30.19           C  
ANISOU 3171  CB  SER B 206     2532   4889   4051    913    310    455       C  
ATOM   3172  OG  SER B 206       4.938 -20.049  28.764  1.00 34.53           O  
ANISOU 3172  OG  SER B 206     2941   5598   4581   1084    354    562       O  
ATOM   3173  N   ARG B 207       5.124 -18.623  31.194  1.00 28.44           N  
ANISOU 3173  N   ARG B 207     1920   4952   3934    815    -16    430       N  
ATOM   3174  CA  ARG B 207       6.364 -18.018  31.664  1.00 30.43           C  
ANISOU 3174  CA  ARG B 207     1875   5399   4288    751   -116    501       C  
ATOM   3175  C   ARG B 207       7.411 -17.947  30.565  1.00 31.92           C  
ANISOU 3175  C   ARG B 207     1871   5704   4555    802     16    664       C  
ATOM   3176  O   ARG B 207       8.477 -17.360  30.780  1.00 33.84           O  
ANISOU 3176  O   ARG B 207     1832   6122   4903    719    -54    743       O  
ATOM   3177  CB  ARG B 207       6.933 -18.790  32.860  1.00 31.55           C  
ANISOU 3177  CB  ARG B 207     1947   5695   4344    882   -208    523       C  
ATOM   3178  CG  ARG B 207       6.132 -18.630  34.152  1.00 38.43           C  
ANISOU 3178  CG  ARG B 207     2946   6514   5142    794   -366    371       C  
ATOM   3179  CD  ARG B 207       6.721 -19.429  35.315  1.00 47.32           C  
ANISOU 3179  CD  ARG B 207     4013   7805   6160    933   -458    415       C  
ATOM   3180  NE  ARG B 207       6.563 -20.874  35.152  1.00 48.26           N  
ANISOU 3180  NE  ARG B 207     4305   7881   6151   1184   -326    493       N  
ATOM   3181  CZ  ARG B 207       7.527 -21.768  35.363  1.00 51.57           C  
ANISOU 3181  CZ  ARG B 207     4621   8450   6523   1403   -303    634       C  
ATOM   3182  NH1 ARG B 207       8.736 -21.378  35.761  1.00 46.28           N  
ANISOU 3182  NH1 ARG B 207     3663   8000   5920   1384   -408    713       N  
ATOM   3183  NH2 ARG B 207       7.278 -23.058  35.186  1.00 51.33           N  
ANISOU 3183  NH2 ARG B 207     4798   8326   6380   1627   -176    691       N  
ATOM   3184  N   HIS B 208       7.132 -18.529  29.404  1.00 31.33           N  
ANISOU 3184  N   HIS B 208     1937   5545   4420    927    203    714       N  
ATOM   3185  CA  HIS B 208       8.078 -18.611  28.303  1.00 43.81           C  
ANISOU 3185  CA  HIS B 208     3364   7244   6038   1014    366    870       C  
ATOM   3186  C   HIS B 208       7.633 -17.692  27.176  1.00 42.98           C  
ANISOU 3186  C   HIS B 208     3308   7027   5997    852    433    879       C  
ATOM   3187  O   HIS B 208       6.462 -17.706  26.783  1.00 38.00           O  
ANISOU 3187  O   HIS B 208     2932   6201   5304    818    452    785       O  
ATOM   3188  CB  HIS B 208       8.185 -20.046  27.797  1.00 46.95           C  
ANISOU 3188  CB  HIS B 208     3909   7638   6292   1310    544    922       C  
ATOM   3189  CG  HIS B 208       8.967 -20.182  26.530  1.00 54.86           C  
ANISOU 3189  CG  HIS B 208     4859   8699   7286   1392    732   1039       C  
ATOM   3190  ND1 HIS B 208      10.316 -19.901  26.452  1.00 54.66           N  
ANISOU 3190  ND1 HIS B 208     4595   8842   7330   1369    736   1146       N  
ATOM   3191  CD2 HIS B 208       8.592 -20.581  25.293  1.00 51.92           C  
ANISOU 3191  CD2 HIS B 208     4668   8236   6825   1487    915   1054       C  
ATOM   3192  CE1 HIS B 208      10.737 -20.119  25.221  1.00 54.60           C  
ANISOU 3192  CE1 HIS B 208     4616   8853   7278   1455    922   1229       C  
ATOM   3193  NE2 HIS B 208       9.712 -20.534  24.498  1.00 56.14           N  
ANISOU 3193  NE2 HIS B 208     5072   8889   7370   1527   1029   1171       N  
ATOM   3194  N   ASN B 209       8.569 -16.896  26.663  1.00 45.29           N  
ANISOU 3194  N   ASN B 209     3348   7450   6410    747    466   1004       N  
ATOM   3195  CA  ASN B 209       8.269 -15.904  25.640  1.00 42.98           C  
ANISOU 3195  CA  ASN B 209     3080   7060   6189    575    519   1043       C  
ATOM   3196  C   ASN B 209       9.088 -16.101  24.368  1.00 49.07           C  
ANISOU 3196  C   ASN B 209     3740   7963   6940    674    736   1218       C  
ATOM   3197  O   ASN B 209       9.033 -15.253  23.468  1.00 46.85           O  
ANISOU 3197  O   ASN B 209     3447   7639   6717    530    794   1291       O  
ATOM   3198  CB  ASN B 209       8.490 -14.496  26.194  1.00 42.89           C  
ANISOU 3198  CB  ASN B 209     2902   7039   6357    288    345   1028       C  
ATOM   3199  CG  ASN B 209       7.862 -13.437  25.330  1.00 57.14           C  
ANISOU 3199  CG  ASN B 209     4811   8667   8231    108    363   1039       C  
ATOM   3200  OD1 ASN B 209       6.922 -13.714  24.585  1.00 65.50           O  
ANISOU 3200  OD1 ASN B 209     6109   9585   9193    182    448   1006       O  
ATOM   3201  ND2 ASN B 209       8.380 -12.219  25.408  1.00 61.18           N  
ANISOU 3201  ND2 ASN B 209     5149   9185   8912   -133    277   1094       N  
ATOM   3202  N   GLY B 210       9.844 -17.193  24.263  1.00 48.86           N  
ANISOU 3202  N   GLY B 210     3712   8045   6807    902    843   1260       N  
ATOM   3203  CA  GLY B 210      10.590 -17.495  23.058  1.00 48.94           C  
ANISOU 3203  CA  GLY B 210     3711   8132   6751   1008   1041   1378       C  
ATOM   3204  C   GLY B 210       9.736 -18.251  22.064  1.00 48.81           C  
ANISOU 3204  C   GLY B 210     3980   7994   6570   1173   1207   1346       C  
ATOM   3205  O   GLY B 210       8.504 -18.207  22.099  1.00 45.60           O  
ANISOU 3205  O   GLY B 210     3753   7440   6132   1141   1176   1254       O  
ATOM   3206  N   ALA B 211      10.404 -18.967  21.164  1.00 46.67           N  
ANISOU 3206  N   ALA B 211     3762   7783   6186   1349   1380   1412       N  
ATOM   3207  CA  ALA B 211       9.684 -19.760  20.178  1.00 38.42           C  
ANISOU 3207  CA  ALA B 211     3019   6617   4960   1504   1532   1363       C  
ATOM   3208  C   ALA B 211       9.002 -20.954  20.841  1.00 46.60           C  
ANISOU 3208  C   ALA B 211     4295   7521   5890   1673   1497   1230       C  
ATOM   3209  O   ALA B 211       9.557 -21.589  21.746  1.00 46.82           O  
ANISOU 3209  O   ALA B 211     4264   7594   5933   1780   1433   1222       O  
ATOM   3210  CB  ALA B 211      10.635 -20.229  19.080  1.00 41.00           C  
ANISOU 3210  CB  ALA B 211     3347   7042   5190   1651   1715   1456       C  
ATOM   3211  N   ASN B 212       7.785 -21.255  20.387  1.00 40.72           N  
ANISOU 3211  N   ASN B 212     3831   6610   5033   1686   1535   1132       N  
ATOM   3212  CA  ASN B 212       7.006 -22.347  20.961  1.00 41.72           C  
ANISOU 3212  CA  ASN B 212     4216   6581   5055   1808   1500   1002       C  
ATOM   3213  C   ASN B 212       7.723 -23.675  20.743  1.00 45.05           C  
ANISOU 3213  C   ASN B 212     4773   6984   5360   2043   1598   1010       C  
ATOM   3214  O   ASN B 212       8.112 -24.013  19.621  1.00 46.36           O  
ANISOU 3214  O   ASN B 212     5029   7157   5428   2135   1740   1045       O  
ATOM   3215  CB  ASN B 212       5.607 -22.356  20.344  1.00 44.19           C  
ANISOU 3215  CB  ASN B 212     4825   6705   5258   1715   1496    889       C  
ATOM   3216  CG  ASN B 212       4.825 -23.638  20.616  1.00 46.55           C  
ANISOU 3216  CG  ASN B 212     5449   6823   5416   1829   1494    757       C  
ATOM   3217  OD1 ASN B 212       5.197 -24.476  21.441  1.00 40.54           O  
ANISOU 3217  OD1 ASN B 212     4698   6056   4649   1981   1487    749       O  
ATOM   3218  ND2 ASN B 212       3.704 -23.779  19.914  1.00 49.73           N  
ANISOU 3218  ND2 ASN B 212     6122   7071   5702   1738   1486    660       N  
ATOM   3219  N   ARG B 213       7.878 -24.435  21.824  1.00 41.54           N  
ANISOU 3219  N   ARG B 213     4350   6513   4921   2147   1520    981       N  
ATOM   3220  CA  ARG B 213       8.745 -25.605  21.814  1.00 47.13           C  
ANISOU 3220  CA  ARG B 213     5126   7228   5552   2375   1598   1022       C  
ATOM   3221  C   ARG B 213       8.082 -26.858  21.250  1.00 54.75           C  
ANISOU 3221  C   ARG B 213     6486   7972   6346   2510   1687    928       C  
ATOM   3222  O   ARG B 213       8.734 -27.905  21.220  1.00 62.95           O  
ANISOU 3222  O   ARG B 213     7615   8985   7316   2711   1757    958       O  
ATOM   3223  CB  ARG B 213       9.261 -25.875  23.229  1.00 50.74           C  
ANISOU 3223  CB  ARG B 213     5434   7762   6082   2428   1473   1054       C  
ATOM   3224  CG  ARG B 213      10.545 -25.129  23.586  1.00 57.11           C  
ANISOU 3224  CG  ARG B 213     5859   8819   7022   2384   1425   1177       C  
ATOM   3225  CD  ARG B 213      10.507 -24.631  25.029  1.00 60.16           C  
ANISOU 3225  CD  ARG B 213     6065   9278   7516   2267   1224   1164       C  
ATOM   3226  NE  ARG B 213      11.832 -24.552  25.643  1.00 64.74           N  
ANISOU 3226  NE  ARG B 213     6361  10067   8169   2307   1167   1269       N  
ATOM   3227  CZ  ARG B 213      12.095 -23.910  26.782  1.00 62.36           C  
ANISOU 3227  CZ  ARG B 213     5841   9881   7970   2174    983   1274       C  
ATOM   3228  NH1 ARG B 213      11.121 -23.277  27.434  1.00 52.98           N  
ANISOU 3228  NH1 ARG B 213     4685   8619   6825   2000    844   1178       N  
ATOM   3229  NH2 ARG B 213      13.335 -23.898  27.268  1.00 63.20           N  
ANISOU 3229  NH2 ARG B 213     5699  10184   8131   2214    935   1368       N  
ATOM   3230  N   ARG B 214       6.831 -26.793  20.790  1.00 57.50           N  
ANISOU 3230  N   ARG B 214     7071   8157   6619   2399   1682    815       N  
ATOM   3231  CA  ARG B 214       6.203 -27.964  20.165  1.00 57.47           C  
ANISOU 3231  CA  ARG B 214     7452   7934   6451   2484   1749    717       C  
ATOM   3232  C   ARG B 214       6.938 -28.353  18.885  1.00 57.64           C  
ANISOU 3232  C   ARG B 214     7535   7985   6380   2614   1904    758       C  
ATOM   3233  O   ARG B 214       7.076 -27.540  17.974  1.00 60.86           O  
ANISOU 3233  O   ARG B 214     7841   8495   6788   2538   1963    796       O  
ATOM   3234  CB  ARG B 214       4.723 -27.715  19.849  1.00 54.99           C  
ANISOU 3234  CB  ARG B 214     7357   7466   6070   2301   1698    588       C  
ATOM   3235  CG  ARG B 214       3.909 -29.013  19.746  1.00 59.49           C  
ANISOU 3235  CG  ARG B 214     8318   7784   6502   2333   1697    469       C  
ATOM   3236  CD  ARG B 214       2.934 -29.049  18.573  1.00 62.20           C  
ANISOU 3236  CD  ARG B 214     8912   8006   6716   2207   1715    365       C  
ATOM   3237  NE  ARG B 214       2.503 -27.716  18.166  1.00 70.51           N  
ANISOU 3237  NE  ARG B 214     9809   9178   7805   2040   1686    376       N  
ATOM   3238  CZ  ARG B 214       1.265 -27.409  17.787  1.00 72.61           C  
ANISOU 3238  CZ  ARG B 214    10228   9362   7998   1857   1619    282       C  
ATOM   3239  NH1 ARG B 214       0.318 -28.342  17.785  1.00 73.73           N  
ANISOU 3239  NH1 ARG B 214    10668   9307   8040   1791   1561    160       N  
ATOM   3240  NH2 ARG B 214       0.969 -26.161  17.428  1.00 65.56           N  
ANISOU 3240  NH2 ARG B 214     9185   8590   7136   1729   1602    322       N  
TER    3241      ARG B 214                                                      
ATOM   3242  N   THR C   3      26.955 -25.799  83.740  1.00 60.69           N  
ANISOU 3242  N   THR C   3     7776   6097   9185   1211    565  -1306       N  
ATOM   3243  CA  THR C   3      27.371 -26.221  85.075  1.00 63.39           C  
ANISOU 3243  CA  THR C   3     8118   6315   9652   1244    434  -1210       C  
ATOM   3244  C   THR C   3      27.235 -25.055  86.049  1.00 56.35           C  
ANISOU 3244  C   THR C   3     7164   5503   8743   1158    423  -1054       C  
ATOM   3245  O   THR C   3      27.063 -25.251  87.262  1.00 51.44           O  
ANISOU 3245  O   THR C   3     6599   4781   8165   1140    306   -942       O  
ATOM   3246  CB  THR C   3      28.829 -26.747  85.078  1.00 72.59           C  
ANISOU 3246  CB  THR C   3     9194   7492  10895   1393    420  -1267       C  
ATOM   3247  OG1 THR C   3      29.173 -27.240  86.380  1.00 75.23           O  
ANISOU 3247  OG1 THR C   3     9559   7704  11320   1429    270  -1170       O  
ATOM   3248  CG2 THR C   3      29.806 -25.644  84.673  1.00 72.01           C  
ANISOU 3248  CG2 THR C   3     8927   7608  10825   1425    554  -1287       C  
ATOM   3249  N   ALA C   4      27.292 -23.839  85.497  1.00 47.31           N  
ANISOU 3249  N   ALA C   4     5923   4543   7511   1102    547  -1039       N  
ATOM   3250  CA  ALA C   4      27.221 -22.610  86.271  1.00 41.96           C  
ANISOU 3250  CA  ALA C   4     5179   3959   6806   1021    543   -907       C  
ATOM   3251  C   ALA C   4      26.215 -21.657  85.641  1.00 36.67           C  
ANISOU 3251  C   ALA C   4     4538   3416   5977    891    630   -860       C  
ATOM   3252  O   ALA C   4      26.126 -21.547  84.414  1.00 28.98           O  
ANISOU 3252  O   ALA C   4     3566   2524   4920    895    739   -940       O  
ATOM   3253  CB  ALA C   4      28.596 -21.943  86.368  1.00 38.26           C  
ANISOU 3253  CB  ALA C   4     4522   3569   6446   1100    592   -932       C  
ATOM   3254  N   GLU C   5      25.442 -20.982  86.483  1.00 27.17           N  
ANISOU 3254  N   GLU C   5     3369   2231   4725    789    578   -733       N  
ATOM   3255  CA  GLU C   5      24.532 -19.939  86.034  1.00 32.39           C  
ANISOU 3255  CA  GLU C   5     4041   3012   5255    678    642   -679       C  
ATOM   3256  C   GLU C   5      24.716 -18.714  86.922  1.00 24.90           C  
ANISOU 3256  C   GLU C   5     3017   2128   4314    636    628   -572       C  
ATOM   3257  O   GLU C   5      24.985 -18.834  88.119  1.00 29.48           O  
ANISOU 3257  O   GLU C   5     3599   2641   4960    661    530   -517       O  
ATOM   3258  CB  GLU C   5      23.070 -20.445  86.037  1.00 28.24           C  
ANISOU 3258  CB  GLU C   5     3643   2429   4657    587    588   -655       C  
ATOM   3259  CG  GLU C   5      22.868 -21.626  85.048  1.00 28.34           C  
ANISOU 3259  CG  GLU C   5     3731   2368   4670    626    585   -786       C  
ATOM   3260  CD  GLU C   5      21.453 -22.187  85.014  1.00 34.48           C  
ANISOU 3260  CD  GLU C   5     4611   3073   5417    527    520   -779       C  
ATOM   3261  OE1 GLU C   5      20.671 -21.977  85.970  1.00 34.14           O  
ANISOU 3261  OE1 GLU C   5     4588   3001   5382    437    475   -664       O  
ATOM   3262  OE2 GLU C   5      21.131 -22.871  84.025  1.00 37.62           O  
ANISOU 3262  OE2 GLU C   5     5065   3438   5791    541    512   -899       O  
ATOM   3263  N   LEU C   6      24.597 -17.538  86.328  1.00 24.28           N  
ANISOU 3263  N   LEU C   6     2887   2173   4165    583    717   -547       N  
ATOM   3264  CA  LEU C   6      24.810 -16.285  87.042  1.00 23.46           C  
ANISOU 3264  CA  LEU C   6     2709   2125   4081    543    705   -462       C  
ATOM   3265  C   LEU C   6      23.461 -15.775  87.539  1.00 22.21           C  
ANISOU 3265  C   LEU C   6     2636   1984   3821    450    659   -377       C  
ATOM   3266  O   LEU C   6      22.585 -15.444  86.732  1.00 26.08           O  
ANISOU 3266  O   LEU C   6     3170   2534   4207    393    709   -375       O  
ATOM   3267  CB  LEU C   6      25.497 -15.274  86.122  1.00 23.80           C  
ANISOU 3267  CB  LEU C   6     2645   2271   4126    536    838   -474       C  
ATOM   3268  CG  LEU C   6      26.160 -14.046  86.745  1.00 30.78           C  
ANISOU 3268  CG  LEU C   6     3410   3187   5097    510    832   -417       C  
ATOM   3269  CD1 LEU C   6      27.060 -14.436  87.889  1.00 24.08           C  
ANISOU 3269  CD1 LEU C   6     2488   2262   4398    580    714   -438       C  
ATOM   3270  CD2 LEU C   6      26.959 -13.273  85.686  1.00 36.36           C  
ANISOU 3270  CD2 LEU C   6     4007   3975   5834    501    995   -428       C  
ATOM   3271  N   HIS C   7      23.278 -15.728  88.863  1.00 21.79           N  
ANISOU 3271  N   HIS C   7     2609   1881   3790    445    561   -312       N  
ATOM   3272  CA  HIS C   7      22.041 -15.219  89.451  1.00 20.82           C  
ANISOU 3272  CA  HIS C   7     2552   1781   3578    368    533   -234       C  
ATOM   3273  C   HIS C   7      22.210 -13.749  89.831  1.00 22.36           C  
ANISOU 3273  C   HIS C   7     2682   2048   3764    346    533   -189       C  
ATOM   3274  O   HIS C   7      23.236 -13.356  90.394  1.00 28.74           O  
ANISOU 3274  O   HIS C   7     3419   2845   4656    393    491   -195       O  
ATOM   3275  CB  HIS C   7      21.613 -16.033  90.676  1.00 21.63           C  
ANISOU 3275  CB  HIS C   7     2748   1790   3682    376    449   -181       C  
ATOM   3276  CG  HIS C   7      21.260 -17.460  90.367  1.00 22.40           C  
ANISOU 3276  CG  HIS C   7     2922   1788   3801    377    442   -211       C  
ATOM   3277  ND1 HIS C   7      20.201 -18.111  90.959  1.00 24.24           N  
ANISOU 3277  ND1 HIS C   7     3251   1953   4006    319    422   -151       N  
ATOM   3278  CD2 HIS C   7      21.831 -18.357  89.530  1.00 22.65           C  
ANISOU 3278  CD2 HIS C   7     2948   1767   3890    428    456   -300       C  
ATOM   3279  CE1 HIS C   7      20.136 -19.350  90.501  1.00 31.67           C  
ANISOU 3279  CE1 HIS C   7     4243   2790   5001    326    412   -199       C  
ATOM   3280  NE2 HIS C   7      21.111 -19.523  89.626  1.00 24.22           N  
ANISOU 3280  NE2 HIS C   7     3245   1856   4103    399    426   -298       N  
ATOM   3281  N   PHE C   8      21.204 -12.940  89.496  1.00 20.97           N  
ANISOU 3281  N   PHE C   8     2526   1939   3502    278    567   -155       N  
ATOM   3282  CA  PHE C   8      21.212 -11.497  89.714  1.00 25.91           C  
ANISOU 3282  CA  PHE C   8     3103   2621   4118    254    569   -116       C  
ATOM   3283  C   PHE C   8      20.087 -11.108  90.660  1.00 28.71           C  
ANISOU 3283  C   PHE C   8     3518   2986   4404    223    519    -63       C  
ATOM   3284  O   PHE C   8      18.949 -11.560  90.497  1.00 36.18           O  
ANISOU 3284  O   PHE C   8     4519   3939   5288    183    534    -51       O  
ATOM   3285  CB  PHE C   8      20.993 -10.717  88.419  1.00 23.30           C  
ANISOU 3285  CB  PHE C   8     2752   2361   3741    216    656   -117       C  
ATOM   3286  CG  PHE C   8      22.159 -10.719  87.478  1.00 31.70           C  
ANISOU 3286  CG  PHE C   8     3746   3439   4861    243    742   -154       C  
ATOM   3287  CD1 PHE C   8      23.049  -9.652  87.453  1.00 30.62           C  
ANISOU 3287  CD1 PHE C   8     3515   3316   4805    235    779   -131       C  
ATOM   3288  CD2 PHE C   8      22.342 -11.756  86.578  1.00 28.58           C  
ANISOU 3288  CD2 PHE C   8     3375   3040   4444    274    798   -215       C  
ATOM   3289  CE1 PHE C   8      24.123  -9.642  86.560  1.00 28.18           C  
ANISOU 3289  CE1 PHE C   8     3126   3025   4558    252    891   -158       C  
ATOM   3290  CE2 PHE C   8      23.416 -11.747  85.686  1.00 26.76           C  
ANISOU 3290  CE2 PHE C   8     3077   2835   4255    309    905   -253       C  
ATOM   3291  CZ  PHE C   8      24.300 -10.682  85.678  1.00 23.49           C  
ANISOU 3291  CZ  PHE C   8     2558   2443   3924    293    963   -218       C  
ATOM   3292  N   ARG C   9      20.387 -10.241  91.620  1.00 23.60           N  
ANISOU 3292  N   ARG C   9     2851   2340   3775    243    463    -41       N  
ATOM   3293  CA  ARG C   9      19.342  -9.643  92.432  1.00 22.77           C  
ANISOU 3293  CA  ARG C   9     2796   2262   3593    226    436     -1       C  
ATOM   3294  C   ARG C   9      18.946  -8.316  91.781  1.00 30.28           C  
ANISOU 3294  C   ARG C   9     3707   3269   4529    191    467      6       C  
ATOM   3295  O   ARG C   9      19.468  -7.956  90.724  1.00 20.30           O  
ANISOU 3295  O   ARG C   9     2394   2019   3301    174    515     -5       O  
ATOM   3296  CB  ARG C   9      19.830  -9.479  93.869  1.00 31.03           C  
ANISOU 3296  CB  ARG C   9     3872   3276   4643    285    345      7       C  
ATOM   3297  N   CYS C  10      18.005  -7.580  92.380  1.00 16.94           N  
ANISOU 3297  N   CYS C  10     2045   1611   2783    185    446     27       N  
ATOM   3298  CA  CYS C  10      17.644  -6.286  91.810  1.00 20.06           C  
ANISOU 3298  CA  CYS C  10     2411   2040   3172    165    457     35       C  
ATOM   3299  C   CYS C  10      18.820  -5.333  91.932  1.00 19.33           C  
ANISOU 3299  C   CYS C  10     2264   1911   3171    180    423     25       C  
ATOM   3300  O   CYS C  10      19.548  -5.348  92.928  1.00 24.43           O  
ANISOU 3300  O   CYS C  10     2902   2519   3863    218    353      2       O  
ATOM   3301  CB  CYS C  10      16.418  -5.701  92.521  1.00 29.39           C  
ANISOU 3301  CB  CYS C  10     3622   3255   4288    174    438     45       C  
ATOM   3302  SG  CYS C  10      14.932  -6.725  92.405  1.00 28.41           S  
ANISOU 3302  SG  CYS C  10     3524   3172   4099    138    487     56       S  
ATOM   3303  N   ASN C  11      19.017  -4.511  90.905  1.00 22.70           N  
ANISOU 3303  N   ASN C  11     2657   2342   3628    148    468     44       N  
ATOM   3304  CA  ASN C  11      20.050  -3.486  90.948  1.00 18.80           C  
ANISOU 3304  CA  ASN C  11     2097   1799   3246    139    449     44       C  
ATOM   3305  C   ASN C  11      19.694  -2.442  92.004  1.00 26.21           C  
ANISOU 3305  C   ASN C  11     3054   2711   4194    164    354     28       C  
ATOM   3306  O   ASN C  11      18.621  -1.837  91.942  1.00 21.06           O  
ANISOU 3306  O   ASN C  11     2447   2083   3472    168    350     45       O  
ATOM   3307  CB  ASN C  11      20.204  -2.827  89.588  1.00 21.33           C  
ANISOU 3307  CB  ASN C  11     2400   2124   3579     94    540     92       C  
ATOM   3308  CG  ASN C  11      21.468  -1.987  89.495  1.00 28.10           C  
ANISOU 3308  CG  ASN C  11     3168   2918   4591     63    556    101       C  
ATOM   3309  OD1 ASN C  11      21.694  -1.082  90.300  1.00 25.68           O  
ANISOU 3309  OD1 ASN C  11     2834   2554   4369     64    470     85       O  
ATOM   3310  ND2 ASN C  11      22.316  -2.309  88.528  1.00 23.85           N  
ANISOU 3310  ND2 ASN C  11     2576   2386   4099     36    668    120       N  
ATOM   3311  N   GLU C  12      20.583  -2.235  92.976  1.00 21.48           N  
ANISOU 3311  N   GLU C  12     2419   2062   3682    193    265    -16       N  
ATOM   3312  CA  GLU C  12      20.288  -1.334  94.080  1.00 28.64           C  
ANISOU 3312  CA  GLU C  12     3359   2941   4581    235    159    -55       C  
ATOM   3313  C   GLU C  12      20.816   0.078  93.848  1.00 24.50           C  
ANISOU 3313  C   GLU C  12     2778   2342   4189    203    122    -61       C  
ATOM   3314  O   GLU C  12      20.772   0.899  94.769  1.00 30.69           O  
ANISOU 3314  O   GLU C  12     3583   3083   4996    242     14   -115       O  
ATOM   3315  CB  GLU C  12      20.850  -1.895  95.389  1.00 36.29           C  
ANISOU 3315  CB  GLU C  12     4349   3893   5545    303     50   -111       C  
ATOM   3316  CG  GLU C  12      20.367  -3.298  95.727  1.00 41.42           C  
ANISOU 3316  CG  GLU C  12     5072   4593   6074    334     85    -89       C  
ATOM   3317  CD  GLU C  12      20.868  -3.808  97.083  1.00 49.42           C  
ANISOU 3317  CD  GLU C  12     6142   5583   7051    417    -31   -128       C  
ATOM   3318  OE1 GLU C  12      20.122  -4.561  97.743  1.00 55.08           O  
ANISOU 3318  OE1 GLU C  12     6962   6335   7631    454    -12   -100       O  
ATOM   3319  OE2 GLU C  12      21.998  -3.467  97.490  1.00 53.97           O  
ANISOU 3319  OE2 GLU C  12     6662   6105   7740    447   -142   -185       O  
ATOM   3320  N   GLY C  13      21.289   0.383  92.647  1.00 21.98           N  
ANISOU 3320  N   GLY C  13     2400   2001   3952    133    215     -7       N  
ATOM   3321  CA  GLY C  13      21.912   1.664  92.387  1.00 21.71           C  
ANISOU 3321  CA  GLY C  13     2306   1874   4070     84    198      5       C  
ATOM   3322  C   GLY C  13      20.949   2.671  91.810  1.00 23.94           C  
ANISOU 3322  C   GLY C  13     2657   2139   4299     71    224     61       C  
ATOM   3323  O   GLY C  13      19.782   2.713  92.202  1.00 24.43           O  
ANISOU 3323  O   GLY C  13     2801   2248   4236    126    187     46       O  
ATOM   3324  N   GLY C  14      21.430   3.490  90.877  1.00 32.68           N  
ANISOU 3324  N   GLY C  14     3731   3178   5509      1    294    132       N  
ATOM   3325  CA  GLY C  14      20.587   4.459  90.213  1.00 30.41           C  
ANISOU 3325  CA  GLY C  14     3522   2859   5174     -5    314    202       C  
ATOM   3326  C   GLY C  14      20.572   4.290  88.708  1.00 31.99           C  
ANISOU 3326  C   GLY C  14     3753   3093   5309    -51    464    313       C  
ATOM   3327  O   GLY C  14      20.914   3.221  88.184  1.00 27.20           O  
ANISOU 3327  O   GLY C  14     3124   2564   4648    -61    557    320       O  
HETATM 3328  N   MSE C  15      20.177   5.346  88.003  1.00 26.43           N  
ANISOU 3328  N   MSE C  15     3115   2324   4603    -68    483    399       N  
HETATM 3329  CA  MSE C  15      20.046   5.294  86.554  1.00 31.26           C  
ANISOU 3329  CA  MSE C  15     3795   2968   5112    -92    615    513       C  
HETATM 3330  C   MSE C  15      21.362   4.959  85.859  1.00 28.34           C  
ANISOU 3330  C   MSE C  15     3349   2592   4828   -170    771    566       C  
HETATM 3331  O   MSE C  15      21.383   4.163  84.920  1.00 30.66           O  
ANISOU 3331  O   MSE C  15     3678   2976   4995   -164    887    601       O  
HETATM 3332  CB  MSE C  15      19.502   6.618  86.018  1.00 30.19           C  
ANISOU 3332  CB  MSE C  15     3757   2737   4977    -91    593    607       C  
HETATM 3333  CG  MSE C  15      19.320   6.624  84.512  1.00 36.80           C  
ANISOU 3333  CG  MSE C  15     4701   3607   5676    -99    717    737       C  
HETATM 3334 SE   MSE C  15      18.322   5.094  83.774  1.00 42.56          SE  
ANISOU 3334 SE   MSE C  15     5504   4534   6134    -21    738    694      SE  
HETATM 3335  CE  MSE C  15      16.586   5.387  84.627  1.00 27.15           C  
ANISOU 3335  CE  MSE C  15     3589   2605   4123     82    536    606       C  
ATOM   3336  N   ALA C  16      22.461   5.557  86.322  1.00 26.60           N  
ANISOU 3336  N   ALA C  16     3015   2264   4829   -239    771    559       N  
ATOM   3337  CA  ALA C  16      23.761   5.231  85.741  1.00 29.18           C  
ANISOU 3337  CA  ALA C  16     3229   2588   5271   -313    930    597       C  
ATOM   3338  C   ALA C  16      24.095   3.758  85.945  1.00 32.15           C  
ANISOU 3338  C   ALA C  16     3539   3081   5594   -271    951    506       C  
ATOM   3339  O   ALA C  16      24.699   3.121  85.074  1.00 25.61           O  
ANISOU 3339  O   ALA C  16     2678   2312   4740   -289   1112    540       O  
ATOM   3340  CB  ALA C  16      24.846   6.114  86.350  1.00 28.14           C  
ANISOU 3340  CB  ALA C  16     2954   2311   5426   -397    895    582       C  
ATOM   3341  N   ASP C  17      23.708   3.201  87.094  1.00 26.61           N  
ANISOU 3341  N   ASP C  17     2828   2410   4873   -207    796    392       N  
ATOM   3342  CA  ASP C  17      23.914   1.777  87.344  1.00 23.22           C  
ANISOU 3342  CA  ASP C  17     2362   2075   4387   -158    799    313       C  
ATOM   3343  C   ASP C  17      22.985   0.913  86.489  1.00 29.45           C  
ANISOU 3343  C   ASP C  17     3269   2971   4947   -114    867    337       C  
ATOM   3344  O   ASP C  17      23.421  -0.105  85.931  1.00 25.10           O  
ANISOU 3344  O   ASP C  17     2696   2484   4358   -102    963    320       O  
ATOM   3345  CB  ASP C  17      23.733   1.483  88.838  1.00 22.01           C  
ANISOU 3345  CB  ASP C  17     2191   1911   4260   -101    618    205       C  
ATOM   3346  CG  ASP C  17      24.630   2.352  89.713  1.00 31.09           C  
ANISOU 3346  CG  ASP C  17     3232   2951   5631   -132    514    156       C  
ATOM   3347  OD1 ASP C  17      25.869   2.275  89.560  1.00 27.19           O  
ANISOU 3347  OD1 ASP C  17     2594   2419   5317   -178    564    143       O  
ATOM   3348  OD2 ASP C  17      24.099   3.131  90.538  1.00 33.79           O  
ANISOU 3348  OD2 ASP C  17     3623   3239   5977   -107    380    121       O  
ATOM   3349  N   TYR C  18      21.705   1.294  86.368  1.00 21.44           N  
ANISOU 3349  N   TYR C  18     2377   1977   3793    -84    810    365       N  
ATOM   3350  CA  TYR C  18      20.788   0.518  85.533  1.00 26.96           C  
ANISOU 3350  CA  TYR C  18     3178   2771   4294    -45    849    374       C  
ATOM   3351  C   TYR C  18      21.251   0.497  84.076  1.00 27.24           C  
ANISOU 3351  C   TYR C  18     3253   2833   4263    -68   1012    453       C  
ATOM   3352  O   TYR C  18      21.266  -0.557  83.431  1.00 28.00           O  
ANISOU 3352  O   TYR C  18     3377   3007   4255    -40   1079    422       O  
ATOM   3353  CB  TYR C  18      19.367   1.077  85.600  1.00 20.40           C  
ANISOU 3353  CB  TYR C  18     2446   1950   3356     -7    752    388       C  
ATOM   3354  CG  TYR C  18      18.767   1.354  86.970  1.00 27.23           C  
ANISOU 3354  CG  TYR C  18     3290   2791   4264     25    613    323       C  
ATOM   3355  CD1 TYR C  18      19.121   0.627  88.095  1.00 29.94           C  
ANISOU 3355  CD1 TYR C  18     3573   3143   4661     40    561    243       C  
ATOM   3356  CD2 TYR C  18      17.825   2.360  87.119  1.00 25.67           C  
ANISOU 3356  CD2 TYR C  18     3147   2563   4042     54    536    341       C  
ATOM   3357  CE1 TYR C  18      18.539   0.900  89.338  1.00 29.77           C  
ANISOU 3357  CE1 TYR C  18     3557   3110   4645     81    450    187       C  
ATOM   3358  CE2 TYR C  18      17.260   2.640  88.335  1.00 22.17           C  
ANISOU 3358  CE2 TYR C  18     2691   2108   3624     96    428    274       C  
ATOM   3359  CZ  TYR C  18      17.605   1.915  89.437  1.00 25.87           C  
ANISOU 3359  CZ  TYR C  18     3111   2596   4124    109    392    199       C  
ATOM   3360  OH  TYR C  18      16.992   2.230  90.623  1.00 27.76           O  
ANISOU 3360  OH  TYR C  18     3361   2833   4356    163    300    137       O  
ATOM   3361  N   ALA C  19      21.589   1.671  83.529  1.00 23.33           N  
ANISOU 3361  N   ALA C  19     2777   2270   3816   -114   1080    557       N  
ATOM   3362  CA  ALA C  19      22.045   1.766  82.146  1.00 24.80           C  
ANISOU 3362  CA  ALA C  19     3023   2482   3920   -135   1259    654       C  
ATOM   3363  C   ALA C  19      23.313   0.960  81.929  1.00 26.00           C  
ANISOU 3363  C   ALA C  19     3056   2666   4157   -158   1403    618       C  
ATOM   3364  O   ALA C  19      23.468   0.307  80.896  1.00 26.26           O  
ANISOU 3364  O   ALA C  19     3146   2777   4053   -130   1535    630       O  
ATOM   3365  CB  ALA C  19      22.300   3.230  81.766  1.00 26.22           C  
ANISOU 3365  CB  ALA C  19     3235   2554   4175   -195   1314    788       C  
ATOM   3366  N   ALA C  20      24.253   1.036  82.875  1.00 30.37           N  
ANISOU 3366  N   ALA C  20     3443   3158   4938   -199   1374    567       N  
ATOM   3367  CA  ALA C  20      25.504   0.302  82.737  1.00 29.32           C  
ANISOU 3367  CA  ALA C  20     3168   3051   4922   -212   1498    522       C  
ATOM   3368  C   ALA C  20      25.264  -1.204  82.744  1.00 28.84           C  
ANISOU 3368  C   ALA C  20     3131   3084   4743   -130   1471    415       C  
ATOM   3369  O   ALA C  20      25.919  -1.945  82.003  1.00 26.43           O  
ANISOU 3369  O   ALA C  20     2793   2836   4413   -108   1617    394       O  
ATOM   3370  CB  ALA C  20      26.474   0.688  83.853  1.00 26.73           C  
ANISOU 3370  CB  ALA C  20     2652   2632   4873   -260   1421    469       C  
ATOM   3371  N   GLN C  21      24.329  -1.680  83.570  1.00 27.97           N  
ANISOU 3371  N   GLN C  21     3076   2985   4566    -83   1295    346       N  
ATOM   3372  CA  GLN C  21      24.111  -3.127  83.613  1.00 23.15           C  
ANISOU 3372  CA  GLN C  21     2488   2437   3870    -18   1268    252       C  
ATOM   3373  C   GLN C  21      23.452  -3.615  82.337  1.00 31.44           C  
ANISOU 3373  C   GLN C  21     3677   3565   4702     18   1351    267       C  
ATOM   3374  O   GLN C  21      23.830  -4.671  81.797  1.00 23.97           O  
ANISOU 3374  O   GLN C  21     2730   2668   3709     62   1426    205       O  
ATOM   3375  CB  GLN C  21      23.273  -3.539  84.816  1.00 21.61           C  
ANISOU 3375  CB  GLN C  21     2320   2228   3661     13   1082    190       C  
ATOM   3376  CG  GLN C  21      23.244  -5.072  84.959  1.00 21.20           C  
ANISOU 3376  CG  GLN C  21     2278   2210   3569     68   1059    102       C  
ATOM   3377  CD  GLN C  21      22.418  -5.559  86.122  1.00 33.90           C  
ANISOU 3377  CD  GLN C  21     3923   3801   5155     92    906     61       C  
ATOM   3378  OE1 GLN C  21      22.401  -4.948  87.181  1.00 23.55           O  
ANISOU 3378  OE1 GLN C  21     2581   2448   3917     84    811     66       O  
ATOM   3379  NE2 GLN C  21      21.732  -6.689  85.930  1.00 37.68           N  
ANISOU 3379  NE2 GLN C  21     4474   4308   5536    121    887     18       N  
ATOM   3380  N   LEU C  22      22.452  -2.866  81.856  1.00 23.35           N  
ANISOU 3380  N   LEU C  22     2777   2551   3544     13   1320    337       N  
ATOM   3381  CA  LEU C  22      21.838  -3.161  80.569  1.00 30.89           C  
ANISOU 3381  CA  LEU C  22     3878   3578   4281     54   1380    354       C  
ATOM   3382  C   LEU C  22      22.895  -3.185  79.474  1.00 31.45           C  
ANISOU 3382  C   LEU C  22     3948   3683   4321     55   1594    396       C  
ATOM   3383  O   LEU C  22      22.892  -4.075  78.613  1.00 33.38           O  
ANISOU 3383  O   LEU C  22     4264   3998   4421    113   1664    342       O  
ATOM   3384  CB  LEU C  22      20.750  -2.125  80.273  1.00 25.18           C  
ANISOU 3384  CB  LEU C  22     3273   2843   3449     53   1303    436       C  
ATOM   3385  CG  LEU C  22      19.894  -2.300  79.013  1.00 29.74           C  
ANISOU 3385  CG  LEU C  22     4023   3492   3787    112   1306    450       C  
ATOM   3386  CD1 LEU C  22      19.148  -3.626  79.056  1.00 26.88           C  
ANISOU 3386  CD1 LEU C  22     3683   3183   3345    160   1204    319       C  
ATOM   3387  CD2 LEU C  22      18.905  -1.139  78.828  1.00 26.13           C  
ANISOU 3387  CD2 LEU C  22     3666   3006   3257    120   1211    538       C  
ATOM   3388  N   ARG C  23      23.835  -2.229  79.537  1.00 31.69           N  
ANISOU 3388  N   ARG C  23     3886   3658   4498    -11   1705    485       N  
ATOM   3389  CA  ARG C  23      24.941  -2.118  78.585  1.00 34.77           C  
ANISOU 3389  CA  ARG C  23     4243   4074   4896    -28   1946    544       C  
ATOM   3390  C   ARG C  23      25.867  -3.330  78.646  1.00 36.89           C  
ANISOU 3390  C   ARG C  23     4387   4385   5243     12   2024    425       C  
ATOM   3391  O   ARG C  23      26.193  -3.931  77.614  1.00 38.07           O  
ANISOU 3391  O   ARG C  23     4592   4612   5259     66   2182    405       O  
ATOM   3392  CB  ARG C  23      25.734  -0.838  78.892  1.00 36.81           C  
ANISOU 3392  CB  ARG C  23     4388   4236   5364   -130   2022    655       C  
ATOM   3393  CG  ARG C  23      26.397  -0.123  77.737  1.00 42.98           C  
ANISOU 3393  CG  ARG C  23     5207   5020   6105   -174   2274    797       C  
ATOM   3394  CD  ARG C  23      27.214   1.058  78.291  1.00 48.43           C  
ANISOU 3394  CD  ARG C  23     5741   5584   7076   -294   2317    884       C  
ATOM   3395  NE  ARG C  23      26.389   1.900  79.157  1.00 49.81           N  
ANISOU 3395  NE  ARG C  23     5957   5662   7305   -319   2095    901       N  
ATOM   3396  CZ  ARG C  23      26.835   2.620  80.184  1.00 41.07           C  
ANISOU 3396  CZ  ARG C  23     4702   4439   6463   -393   1999    889       C  
ATOM   3397  NH1 ARG C  23      28.119   2.615  80.512  1.00 37.36           N  
ANISOU 3397  NH1 ARG C  23     4018   3930   6246   -456   2081    856       N  
ATOM   3398  NH2 ARG C  23      25.980   3.340  80.896  1.00 39.18           N  
ANISOU 3398  NH2 ARG C  23     4528   4123   6233   -392   1801    892       N  
ATOM   3399  N   GLU C  24      26.344  -3.675  79.842  1.00 29.37           N  
ANISOU 3399  N   GLU C  24     3272   3382   4506      0   1916    343       N  
ATOM   3400  CA  GLU C  24      27.367  -4.711  79.937  1.00 29.42           C  
ANISOU 3400  CA  GLU C  24     3140   3411   4626     44   1987    238       C  
ATOM   3401  C   GLU C  24      26.755  -6.105  79.950  1.00 30.69           C  
ANISOU 3401  C   GLU C  24     3389   3613   4657    136   1887    116       C  
ATOM   3402  O   GLU C  24      27.246  -7.009  79.267  1.00 36.72           O  
ANISOU 3402  O   GLU C  24     4150   4430   5372    203   2000     43       O  
ATOM   3403  CB  GLU C  24      28.224  -4.491  81.185  1.00 32.74           C  
ANISOU 3403  CB  GLU C  24     3352   3751   5337      4   1897    200       C  
ATOM   3404  N   VAL C  25      25.681  -6.290  80.719  1.00 29.89           N  
ANISOU 3404  N   VAL C  25     3364   3483   4509    140   1682     91       N  
ATOM   3405  CA  VAL C  25      25.091  -7.608  80.933  1.00 30.62           C  
ANISOU 3405  CA  VAL C  25     3521   3585   4528    205   1571    -17       C  
ATOM   3406  C   VAL C  25      24.074  -7.934  79.844  1.00 33.04           C  
ANISOU 3406  C   VAL C  25     4010   3954   4591    241   1580    -29       C  
ATOM   3407  O   VAL C  25      23.960  -9.087  79.402  1.00 33.75           O  
ANISOU 3407  O   VAL C  25     4154   4066   4604    305   1577   -130       O  
ATOM   3408  CB  VAL C  25      24.457  -7.671  82.341  1.00 31.87           C  
ANISOU 3408  CB  VAL C  25     3663   3681   4766    185   1367    -32       C  
ATOM   3409  CG1 VAL C  25      23.608  -8.909  82.500  1.00 25.73           C  
ANISOU 3409  CG1 VAL C  25     2975   2900   3902    229   1260   -113       C  
ATOM   3410  CG2 VAL C  25      25.529  -7.605  83.411  1.00 35.96           C  
ANISOU 3410  CG2 VAL C  25     4017   4139   5508    180   1328    -53       C  
ATOM   3411  N   GLY C  26      23.333  -6.929  79.393  1.00 27.99           N  
ANISOU 3411  N   GLY C  26     3469   3335   3833    208   1575     66       N  
ATOM   3412  CA  GLY C  26      22.247  -7.118  78.465  1.00 25.75           C  
ANISOU 3412  CA  GLY C  26     3358   3104   3322    247   1534     53       C  
ATOM   3413  C   GLY C  26      20.893  -7.160  79.129  1.00 31.85           C  
ANISOU 3413  C   GLY C  26     4175   3853   4075    231   1332     34       C  
ATOM   3414  O   GLY C  26      19.878  -7.108  78.425  1.00 29.26           O  
ANISOU 3414  O   GLY C  26     3973   3563   3583    257   1267     29       O  
ATOM   3415  N   THR C  27      20.853  -7.216  80.464  1.00 23.66           N  
ANISOU 3415  N   THR C  27     3036   2755   3199    195   1232     23       N  
ATOM   3416  CA  THR C  27      19.615  -7.341  81.219  1.00 21.67           C  
ANISOU 3416  CA  THR C  27     2805   2483   2945    178   1068      3       C  
ATOM   3417  C   THR C  27      19.802  -6.688  82.578  1.00 20.67           C  
ANISOU 3417  C   THR C  27     2582   2302   2971    137   1010     46       C  
ATOM   3418  O   THR C  27      20.877  -6.779  83.171  1.00 23.99           O  
ANISOU 3418  O   THR C  27     2906   2685   3523    132   1048     40       O  
ATOM   3419  CB  THR C  27      19.217  -8.821  81.390  1.00 24.48           C  
ANISOU 3419  CB  THR C  27     3176   2826   3300    202    999   -107       C  
ATOM   3420  OG1 THR C  27      19.175  -9.449  80.102  1.00 26.04           O  
ANISOU 3420  OG1 THR C  27     3467   3069   3360    252   1047   -171       O  
ATOM   3421  CG2 THR C  27      17.840  -8.950  82.035  1.00 22.73           C  
ANISOU 3421  CG2 THR C  27     2971   2589   3075    174    858   -119       C  
ATOM   3422  N   VAL C  28      18.751  -6.048  83.073  1.00 19.92           N  
ANISOU 3422  N   VAL C  28     2511   2202   2856    119    910     77       N  
ATOM   3423  CA  VAL C  28      18.759  -5.441  84.398  1.00 23.52           C  
ANISOU 3423  CA  VAL C  28     2899   2611   3426     96    841    101       C  
ATOM   3424  C   VAL C  28      17.380  -5.612  85.020  1.00 20.67           C  
ANISOU 3424  C   VAL C  28     2565   2261   3028     96    733     79       C  
ATOM   3425  O   VAL C  28      16.363  -5.538  84.320  1.00 23.63           O  
ANISOU 3425  O   VAL C  28     2998   2675   3305    105    700     75       O  
ATOM   3426  CB  VAL C  28      19.176  -3.948  84.332  1.00 27.77           C  
ANISOU 3426  CB  VAL C  28     3419   3121   4012     72    872    184       C  
ATOM   3427  CG1 VAL C  28      18.139  -3.105  83.583  1.00 23.38           C  
ANISOU 3427  CG1 VAL C  28     2956   2589   3340     80    845    237       C  
ATOM   3428  CG2 VAL C  28      19.402  -3.404  85.720  1.00 27.51           C  
ANISOU 3428  CG2 VAL C  28     3315   3031   4106     59    794    180       C  
HETATM 3429  N   MSE C  29      17.353  -5.870  86.332  1.00 21.69           N  
ANISOU 3429  N   MSE C  29     2650   2359   3233     93    678     61       N  
HETATM 3430  CA  MSE C  29      16.111  -5.956  87.111  1.00 21.39           C  
ANISOU 3430  CA  MSE C  29     2621   2332   3174     90    605     50       C  
HETATM 3431  C   MSE C  29      16.005  -4.790  88.087  1.00 21.30           C  
ANISOU 3431  C   MSE C  29     2587   2303   3204     99    561     80       C  
HETATM 3432  O   MSE C  29      16.880  -4.594  88.929  1.00 22.21           O  
ANISOU 3432  O   MSE C  29     2671   2378   3391    108    548     79       O  
HETATM 3433  CB  MSE C  29      16.016  -7.274  87.899  1.00 17.52           C  
ANISOU 3433  CB  MSE C  29     2128   1818   2712     85    589     14       C  
HETATM 3434  CG  MSE C  29      14.655  -7.474  88.549  1.00 17.08           C  
ANISOU 3434  CG  MSE C  29     2073   1780   2635     68    551     10       C  
HETATM 3435 SE   MSE C  29      14.307  -9.355  89.063  1.00 33.24          SE  
ANISOU 3435 SE   MSE C  29     4139   3780   4711     37    557    -18      SE  
HETATM 3436  CE  MSE C  29      15.864  -9.672  90.193  1.00 19.97           C  
ANISOU 3436  CE  MSE C  29     2471   2032   3084     81    553      3       C  
ATOM   3437  N   LEU C  30      14.927  -4.030  87.976  1.00 18.59           N  
ANISOU 3437  N   LEU C  30     2257   1987   2820    108    523     92       N  
ATOM   3438  CA  LEU C  30      14.748  -2.859  88.827  1.00 21.61           C  
ANISOU 3438  CA  LEU C  30     2627   2348   3237    131    477    105       C  
ATOM   3439  C   LEU C  30      13.849  -3.220  89.997  1.00 22.73           C  
ANISOU 3439  C   LEU C  30     2756   2514   3366    148    449     74       C  
ATOM   3440  O   LEU C  30      12.893  -3.982  89.826  1.00 23.93           O  
ANISOU 3440  O   LEU C  30     2902   2707   3485    133    459     57       O  
ATOM   3441  CB  LEU C  30      14.116  -1.714  88.044  1.00 17.11           C  
ANISOU 3441  CB  LEU C  30     2082   1782   2636    148    452    137       C  
ATOM   3442  CG  LEU C  30      14.742  -1.428  86.682  1.00 18.34           C  
ANISOU 3442  CG  LEU C  30     2278   1926   2762    133    502    188       C  
ATOM   3443  CD1 LEU C  30      13.827  -0.511  85.865  1.00 18.35           C  
ANISOU 3443  CD1 LEU C  30     2334   1938   2701    165    457    224       C  
ATOM   3444  CD2 LEU C  30      16.113  -0.814  86.852  1.00 25.54           C  
ANISOU 3444  CD2 LEU C  30     3166   2772   3767    108    545    224       C  
ATOM   3445  N   PRO C  31      14.120  -2.742  91.201  1.00 19.90           N  
ANISOU 3445  N   PRO C  31     2395   2131   3034    178    418     63       N  
ATOM   3446  CA  PRO C  31      13.293  -3.136  92.346  1.00 18.96           C  
ANISOU 3446  CA  PRO C  31     2281   2044   2877    201    419     43       C  
ATOM   3447  C   PRO C  31      11.971  -2.376  92.360  1.00 26.65           C  
ANISOU 3447  C   PRO C  31     3233   3063   3830    229    408     28       C  
ATOM   3448  O   PRO C  31      11.804  -1.329  91.726  1.00 24.33           O  
ANISOU 3448  O   PRO C  31     2935   2757   3552    249    371     32       O  
ATOM   3449  CB  PRO C  31      14.161  -2.777  93.557  1.00 17.60           C  
ANISOU 3449  CB  PRO C  31     2134   1831   2720    243    376     26       C  
ATOM   3450  CG  PRO C  31      15.081  -1.678  93.059  1.00 20.28           C  
ANISOU 3450  CG  PRO C  31     2456   2115   3136    242    333     27       C  
ATOM   3451  CD  PRO C  31      15.285  -1.925  91.581  1.00 20.87           C  
ANISOU 3451  CD  PRO C  31     2512   2192   3225    191    384     64       C  
ATOM   3452  N   ALA C  32      11.005  -2.936  93.076  1.00 20.79           N  
ANISOU 3452  N   ALA C  32     2474   2369   3057    233    448     16       N  
ATOM   3453  CA  ALA C  32       9.808  -2.161  93.375  1.00 24.27           C  
ANISOU 3453  CA  ALA C  32     2874   2856   3491    278    445    -12       C  
ATOM   3454  C   ALA C  32      10.203  -1.031  94.322  1.00 22.10           C  
ANISOU 3454  C   ALA C  32     2637   2555   3205    353    403    -39       C  
ATOM   3455  O   ALA C  32      10.962  -1.262  95.267  1.00 22.33           O  
ANISOU 3455  O   ALA C  32     2718   2560   3205    371    401    -42       O  
ATOM   3456  CB  ALA C  32       8.744  -3.061  94.001  1.00 26.33           C  
ANISOU 3456  CB  ALA C  32     3093   3175   3737    257    525    -15       C  
ATOM   3457  N   TYR C  33       9.736   0.200  94.074  1.00 21.59           N  
ANISOU 3457  N   TYR C  33     2555   2482   3165    406    351    -66       N  
ATOM   3458  CA  TYR C  33       8.857   0.608  92.982  1.00 20.35           C  
ANISOU 3458  CA  TYR C  33     2350   2345   3036    409    325    -64       C  
ATOM   3459  C   TYR C  33       9.480   1.797  92.214  1.00 18.21           C  
ANISOU 3459  C   TYR C  33     2122   1994   2804    429    247    -41       C  
ATOM   3460  O   TYR C  33       8.882   2.875  92.117  1.00 18.78           O  
ANISOU 3460  O   TYR C  33     2190   2047   2901    494    191    -62       O  
ATOM   3461  CB  TYR C  33       7.471   0.998  93.537  1.00 24.30           C  
ANISOU 3461  CB  TYR C  33     2785   2910   3539    475    341   -116       C  
ATOM   3462  CG  TYR C  33       6.757  -0.155  94.217  1.00 26.18           C  
ANISOU 3462  CG  TYR C  33     2969   3223   3754    441    445   -122       C  
ATOM   3463  CD1 TYR C  33       6.915  -0.403  95.583  1.00 25.98           C  
ANISOU 3463  CD1 TYR C  33     2984   3218   3670    467    515   -130       C  
ATOM   3464  CD2 TYR C  33       5.930  -1.007  93.486  1.00 25.86           C  
ANISOU 3464  CD2 TYR C  33     2847   3227   3753    380    471   -117       C  
ATOM   3465  CE1 TYR C  33       6.262  -1.483  96.198  1.00 27.63           C  
ANISOU 3465  CE1 TYR C  33     3157   3485   3855    426    633   -110       C  
ATOM   3466  CE2 TYR C  33       5.282  -2.071  94.084  1.00 21.02           C  
ANISOU 3466  CE2 TYR C  33     2176   2662   3147    329    575   -112       C  
ATOM   3467  CZ  TYR C  33       5.452  -2.307  95.436  1.00 21.83           C  
ANISOU 3467  CZ  TYR C  33     2325   2780   3188    349    668    -97       C  
ATOM   3468  OH  TYR C  33       4.804  -3.378  96.004  1.00 24.87           O  
ANISOU 3468  OH  TYR C  33     2666   3204   3581    289    791    -70       O  
ATOM   3469  N   VAL C  34      10.682   1.576  91.683  1.00 17.81           N  
ANISOU 3469  N   VAL C  34     2109   1889   2767    372    251      5       N  
ATOM   3470  CA  VAL C  34      11.439   2.623  90.999  1.00 18.07           C  
ANISOU 3470  CA  VAL C  34     2183   1835   2849    368    209     47       C  
ATOM   3471  C   VAL C  34      10.707   3.094  89.749  1.00 23.50           C  
ANISOU 3471  C   VAL C  34     2887   2526   3514    385    179     86       C  
ATOM   3472  O   VAL C  34      10.432   4.287  89.585  1.00 19.67           O  
ANISOU 3472  O   VAL C  34     2429   1982   3061    437    117     97       O  
ATOM   3473  CB  VAL C  34      12.850   2.112  90.655  1.00 23.84           C  
ANISOU 3473  CB  VAL C  34     2925   2525   3607    298    251     88       C  
ATOM   3474  CG1 VAL C  34      13.528   2.990  89.632  1.00 18.29           C  
ANISOU 3474  CG1 VAL C  34     2256   1745   2950    271    250    156       C  
ATOM   3475  CG2 VAL C  34      13.697   1.972  91.919  1.00 26.25           C  
ANISOU 3475  CG2 VAL C  34     3222   2800   3953    303    235     44       C  
ATOM   3476  N   ALA C  35      10.411   2.169  88.828  1.00 21.48           N  
ANISOU 3476  N   ALA C  35     2629   2331   3203    351    208    104       N  
ATOM   3477  CA  ALA C  35       9.907   2.576  87.513  1.00 19.05           C  
ANISOU 3477  CA  ALA C  35     2364   2023   2850    374    164    146       C  
ATOM   3478  C   ALA C  35       8.407   2.868  87.515  1.00 24.23           C  
ANISOU 3478  C   ALA C  35     2973   2728   3504    447     88     96       C  
ATOM   3479  O   ALA C  35       7.943   3.747  86.776  1.00 23.25           O  
ANISOU 3479  O   ALA C  35     2892   2574   3367    506     11    125       O  
ATOM   3480  CB  ALA C  35      10.227   1.498  86.470  1.00 18.95           C  
ANISOU 3480  CB  ALA C  35     2381   2054   2767    323    210    167       C  
ATOM   3481  N   PHE C  36       7.627   2.120  88.292  1.00 19.39           N  
ANISOU 3481  N   PHE C  36     2269   2189   2911    445    111     26       N  
ATOM   3482  CA  PHE C  36       6.188   2.324  88.391  1.00 20.13           C  
ANISOU 3482  CA  PHE C  36     2277   2338   3033    509     56    -34       C  
ATOM   3483  C   PHE C  36       5.816   2.261  89.865  1.00 20.05           C  
ANISOU 3483  C   PHE C  36     2192   2362   3064    527    117    -91       C  
ATOM   3484  O   PHE C  36       6.144   1.286  90.545  1.00 20.21           O  
ANISOU 3484  O   PHE C  36     2196   2410   3073    466    204    -95       O  
ATOM   3485  CB  PHE C  36       5.392   1.262  87.618  1.00 20.46           C  
ANISOU 3485  CB  PHE C  36     2260   2452   3061    475     35    -66       C  
ATOM   3486  CG  PHE C  36       5.622   1.268  86.129  1.00 22.64           C  
ANISOU 3486  CG  PHE C  36     2627   2712   3264    478    -34    -25       C  
ATOM   3487  CD1 PHE C  36       4.795   1.990  85.284  1.00 21.95           C  
ANISOU 3487  CD1 PHE C  36     2553   2627   3160    562   -159    -31       C  
ATOM   3488  CD2 PHE C  36       6.652   0.528  85.565  1.00 20.34           C  
ANISOU 3488  CD2 PHE C  36     2414   2406   2908    410     23     15       C  
ATOM   3489  CE1 PHE C  36       4.998   1.989  83.895  1.00 22.58           C  
ANISOU 3489  CE1 PHE C  36     2747   2698   3137    579   -225     12       C  
ATOM   3490  CE2 PHE C  36       6.864   0.546  84.183  1.00 21.66           C  
ANISOU 3490  CE2 PHE C  36     2683   2569   2979    426    -24     51       C  
ATOM   3491  CZ  PHE C  36       6.028   1.265  83.349  1.00 22.11           C  
ANISOU 3491  CZ  PHE C  36     2773   2631   2996    510   -148     53       C  
ATOM   3492  N   ASP C  37       5.151   3.298  90.358  1.00 20.76           N  
ANISOU 3492  N   ASP C  37     2250   2445   3192    621     75   -134       N  
ATOM   3493  CA  ASP C  37       4.773   3.342  91.761  1.00 25.01           C  
ANISOU 3493  CA  ASP C  37     2734   3024   3745    660    144   -194       C  
ATOM   3494  C   ASP C  37       3.786   2.211  92.078  1.00 28.75           C  
ANISOU 3494  C   ASP C  37     3085   3601   4236    619    229   -229       C  
ATOM   3495  O   ASP C  37       3.170   1.626  91.187  1.00 23.65           O  
ANISOU 3495  O   ASP C  37     2374   2990   3621    582    197   -232       O  
ATOM   3496  CB  ASP C  37       4.194   4.715  92.098  1.00 21.93           C  
ANISOU 3496  CB  ASP C  37     2333   2603   3397    786     76   -248       C  
ATOM   3497  CG  ASP C  37       5.212   5.853  91.878  1.00 21.82           C  
ANISOU 3497  CG  ASP C  37     2442   2458   3390    811     -5   -209       C  
ATOM   3498  OD1 ASP C  37       4.789   7.015  91.714  1.00 24.54           O  
ANISOU 3498  OD1 ASP C  37     2801   2744   3781    908    -94   -233       O  
ATOM   3499  OD2 ASP C  37       6.436   5.587  91.863  1.00 21.02           O  
ANISOU 3499  OD2 ASP C  37     2416   2304   3266    734     19   -156       O  
ATOM   3500  N   ALA C  38       3.673   1.869  93.367  1.00 23.27           N  
ANISOU 3500  N   ALA C  38     2249   2742   3851   -329    823   -890       N  
ATOM   3501  CA  ALA C  38       2.804   0.761  93.741  1.00 24.54           C  
ANISOU 3501  CA  ALA C  38     2141   3187   3995   -413    796   -839       C  
ATOM   3502  C   ALA C  38       1.353   1.084  93.406  1.00 28.75           C  
ANISOU 3502  C   ALA C  38     2556   3809   4559   -243    631   -936       C  
ATOM   3503  O   ALA C  38       0.610   0.219  92.930  1.00 22.01           O  
ANISOU 3503  O   ALA C  38     1619   3015   3727   -285    535   -858       O  
ATOM   3504  CB  ALA C  38       2.959   0.433  95.228  1.00 21.57           C  
ANISOU 3504  CB  ALA C  38     1722   3055   3418   -417    747   -713       C  
ATOM   3505  N   HIS C  39       0.943   2.340  93.600  1.00 23.74           N  
ANISOU 3505  N   HIS C  39     1916   3154   3951    -42    574  -1117       N  
ATOM   3506  CA  HIS C  39      -0.445   2.677  93.307  1.00 22.89           C  
ANISOU 3506  CA  HIS C  39     1692   3135   3868    129    413  -1215       C  
ATOM   3507  C   HIS C  39      -0.718   2.640  91.814  1.00 23.78           C  
ANISOU 3507  C   HIS C  39     2057   2979   4000    184    278  -1123       C  
ATOM   3508  O   HIS C  39      -1.845   2.350  91.405  1.00 28.37           O  
ANISOU 3508  O   HIS C  39     2538   3655   4586    251    151  -1134       O  
ATOM   3509  CB  HIS C  39      -0.808   4.038  93.909  1.00 30.03           C  
ANISOU 3509  CB  HIS C  39     2505   4077   4828    347    364  -1462       C  
ATOM   3510  CG  HIS C  39      -0.350   5.219  93.109  1.00 32.37           C  
ANISOU 3510  CG  HIS C  39     3088   3968   5244    479    282  -1496       C  
ATOM   3511  ND1 HIS C  39       0.862   5.840  93.325  1.00 33.23           N  
ANISOU 3511  ND1 HIS C  39     3343   3862   5422    450    361  -1508       N  
ATOM   3512  CD2 HIS C  39      -0.970   5.931  92.136  1.00 32.19           C  
ANISOU 3512  CD2 HIS C  39     3196   3726   5307    641    117  -1499       C  
ATOM   3513  CE1 HIS C  39       0.981   6.868  92.500  1.00 34.55           C  
ANISOU 3513  CE1 HIS C  39     3712   3682   5735    579    240  -1489       C  
ATOM   3514  NE2 HIS C  39      -0.117   6.946  91.769  1.00 31.69           N  
ANISOU 3514  NE2 HIS C  39     3343   3319   5379    698     94  -1477       N  
ATOM   3515  N   GLU C  40       0.297   2.920  90.994  1.00 22.20           N  
ANISOU 3515  N   GLU C  40     2159   2482   3795    161    303  -1024       N  
ATOM   3516  CA  GLU C  40       0.154   2.798  89.547  1.00 27.54           C  
ANISOU 3516  CA  GLU C  40     3048   2980   4436    214    188   -916       C  
ATOM   3517  C   GLU C  40       0.040   1.333  89.122  1.00 24.96           C  
ANISOU 3517  C   GLU C  40     2676   2749   4057     74    169   -835       C  
ATOM   3518  O   GLU C  40      -0.749   0.996  88.233  1.00 26.72           O  
ANISOU 3518  O   GLU C  40     2908   2981   4265    146     24   -835       O  
ATOM   3519  CB  GLU C  40       1.344   3.470  88.848  1.00 23.34           C  
ANISOU 3519  CB  GLU C  40     2804   2173   3892    225    229   -796       C  
ATOM   3520  CG  GLU C  40       1.439   4.996  89.016  1.00 28.83           C  
ANISOU 3520  CG  GLU C  40     3551   2682   4722    378    186   -849       C  
ATOM   3521  CD  GLU C  40       2.692   5.620  88.367  1.00 33.27           C  
ANISOU 3521  CD  GLU C  40     4363   2972   5305    360    225   -665       C  
ATOM   3522  OE1 GLU C  40       3.788   5.029  88.472  1.00 28.65           O  
ANISOU 3522  OE1 GLU C  40     3869   2378   4637    200    363   -570       O  
ATOM   3523  OE2 GLU C  40       2.585   6.706  87.748  1.00 31.45           O  
ANISOU 3523  OE2 GLU C  40     4219   2541   5189    503    109   -589       O  
ATOM   3524  N   LEU C  41       0.833   0.448  89.726  1.00 22.65           N  
ANISOU 3524  N   LEU C  41     2326   2517   3763   -122    296   -773       N  
ATOM   3525  CA  LEU C  41       0.709  -0.962  89.383  1.00 23.85           C  
ANISOU 3525  CA  LEU C  41     2395   2723   3942   -255    244   -711       C  
ATOM   3526  C   LEU C  41      -0.646  -1.496  89.813  1.00 29.32           C  
ANISOU 3526  C   LEU C  41     2783   3632   4726   -251    137   -746       C  
ATOM   3527  O   LEU C  41      -1.257  -2.286  89.089  1.00 27.90           O  
ANISOU 3527  O   LEU C  41     2557   3442   4603   -254    -11   -743       O  
ATOM   3528  CB  LEU C  41       1.845  -1.778  90.004  1.00 21.94           C  
ANISOU 3528  CB  LEU C  41     2129   2486   3721   -470    393   -620       C  
ATOM   3529  CG  LEU C  41       3.219  -1.427  89.393  1.00 30.41           C  
ANISOU 3529  CG  LEU C  41     3511   3348   4696   -483    484   -567       C  
ATOM   3530  CD1 LEU C  41       4.342  -2.276  89.952  1.00 25.18           C  
ANISOU 3530  CD1 LEU C  41     2837   2693   4037   -676    615   -475       C  
ATOM   3531  CD2 LEU C  41       3.212  -1.521  87.872  1.00 26.29           C  
ANISOU 3531  CD2 LEU C  41     3194   2705   4090   -375    352   -563       C  
ATOM   3532  N   ALA C  42      -1.141  -1.056  90.978  1.00 30.12           N  
ANISOU 3532  N   ALA C  42     2652   3953   4841   -231    198   -788       N  
ATOM   3533  CA  ALA C  42      -2.491  -1.430  91.388  1.00 31.16           C  
ANISOU 3533  CA  ALA C  42     2470   4335   5035   -206     95   -800       C  
ATOM   3534  C   ALA C  42      -3.508  -1.011  90.336  1.00 28.98           C  
ANISOU 3534  C   ALA C  42     2287   3969   4755    -20    -88   -886       C  
ATOM   3535  O   ALA C  42      -4.404  -1.786  89.988  1.00 31.88           O  
ANISOU 3535  O   ALA C  42     2505   4406   5203    -39   -227   -859       O  
ATOM   3536  CB  ALA C  42      -2.829  -0.816  92.747  1.00 27.48           C  
ANISOU 3536  CB  ALA C  42     1740   4176   4526   -158    190   -865       C  
ATOM   3537  N   ARG C  43      -3.361   0.194  89.787  1.00 24.51           N  
ANISOU 3537  N   ARG C  43     1958   3234   4122    156   -105   -972       N  
ATOM   3538  CA  ARG C  43      -4.288   0.637  88.753  1.00 34.59           C  
ANISOU 3538  CA  ARG C  43     3322   4433   5389    337   -277  -1028       C  
ATOM   3539  C   ARG C  43      -4.192  -0.261  87.523  1.00 34.47           C  
ANISOU 3539  C   ARG C  43     3437   4303   5358    297   -384   -970       C  
ATOM   3540  O   ARG C  43      -5.213  -0.702  86.974  1.00 29.30           O  
ANISOU 3540  O   ARG C  43     2685   3711   4739    354   -543  -1005       O  
ATOM   3541  CB  ARG C  43      -4.008   2.094  88.394  1.00 26.54           C  
ANISOU 3541  CB  ARG C  43     2515   3228   4342    515   -281  -1078       C  
ATOM   3542  CG  ARG C  43      -5.159   2.762  87.693  1.00 36.80           C  
ANISOU 3542  CG  ARG C  43     3817   4510   5655    721   -451  -1141       C  
ATOM   3543  CD  ARG C  43      -4.737   4.080  87.087  1.00 46.31           C  
ANISOU 3543  CD  ARG C  43     5245   5470   6880    873   -483  -1116       C  
ATOM   3544  NE  ARG C  43      -5.833   4.693  86.345  1.00 49.59           N  
ANISOU 3544  NE  ARG C  43     5659   5864   7318   1068   -655  -1146       N  
ATOM   3545  CZ  ARG C  43      -5.681   5.675  85.461  1.00 52.58           C  
ANISOU 3545  CZ  ARG C  43     6214   6038   7724   1207   -736  -1055       C  
ATOM   3546  NH1 ARG C  43      -4.471   6.160  85.203  1.00 53.14           N  
ANISOU 3546  NH1 ARG C  43     6474   5909   7807   1169   -661   -917       N  
ATOM   3547  NH2 ARG C  43      -6.738   6.167  84.830  1.00 50.20           N  
ANISOU 3547  NH2 ARG C  43     5883   5741   7448   1379   -895  -1072       N  
ATOM   3548  N   ILE C  44      -2.959  -0.556  87.093  1.00 26.80           N  
ANISOU 3548  N   ILE C  44     2666   3184   4332    208   -305   -902       N  
ATOM   3549  CA  ILE C  44      -2.722  -1.444  85.957  1.00 28.40           C  
ANISOU 3549  CA  ILE C  44     2973   3316   4503    187   -408   -894       C  
ATOM   3550  C   ILE C  44      -3.376  -2.797  86.189  1.00 29.75           C  
ANISOU 3550  C   ILE C  44     2885   3586   4834     63   -514   -917       C  
ATOM   3551  O   ILE C  44      -3.982  -3.379  85.281  1.00 32.66           O  
ANISOU 3551  O   ILE C  44     3228   3948   5233    125   -696   -989       O  
ATOM   3552  CB  ILE C  44      -1.209  -1.608  85.718  1.00 27.22           C  
ANISOU 3552  CB  ILE C  44     3030   3043   4271     94   -282   -822       C  
ATOM   3553  CG1 ILE C  44      -0.550  -0.270  85.376  1.00 33.22           C  
ANISOU 3553  CG1 ILE C  44     4028   3684   4909    211   -204   -753       C  
ATOM   3554  CG2 ILE C  44      -0.951  -2.659  84.636  1.00 23.44           C  
ANISOU 3554  CG2 ILE C  44     2605   2542   3760     82   -401   -866       C  
ATOM   3555  CD1 ILE C  44      -0.915   0.242  84.034  1.00 41.38           C  
ANISOU 3555  CD1 ILE C  44     5202   4696   5823    402   -340   -732       C  
ATOM   3556  N   ASP C  45      -3.230  -3.333  87.399  1.00 33.86           N  
ANISOU 3556  N   ASP C  45     3188   4203   5476   -114   -415   -845       N  
ATOM   3557  CA  ASP C  45      -3.778  -4.648  87.703  1.00 35.40           C  
ANISOU 3557  CA  ASP C  45     3093   4474   5885   -261   -523   -801       C  
ATOM   3558  C   ASP C  45      -5.288  -4.648  87.540  1.00 46.01           C  
ANISOU 3558  C   ASP C  45     4243   5939   7302   -158   -696   -847       C  
ATOM   3559  O   ASP C  45      -5.862  -5.584  86.968  1.00 53.06           O  
ANISOU 3559  O   ASP C  45     5014   6793   8355   -184   -888   -878       O  
ATOM   3560  CB  ASP C  45      -3.389  -5.051  89.125  1.00 44.32           C  
ANISOU 3560  CB  ASP C  45     3986   5746   7109   -460   -369   -654       C  
ATOM   3561  CG  ASP C  45      -2.996  -6.500  89.231  1.00 51.80           C  
ANISOU 3561  CG  ASP C  45     4993   6638   8052   -597   -376   -473       C  
ATOM   3562  OD1 ASP C  45      -3.354  -7.270  88.316  1.00 53.62           O  
ANISOU 3562  OD1 ASP C  45     5230   6746   8397   -572   -548   -539       O  
ATOM   3563  OD2 ASP C  45      -2.332  -6.869  90.226  1.00 50.92           O  
ANISOU 3563  OD2 ASP C  45     4920   6627   7798   -701   -231   -293       O  
ATOM   3564  N   ALA C  46      -5.945  -3.591  88.020  1.00 47.91           N  
ANISOU 3564  N   ALA C  46     4444   6318   7442    -30   -648   -873       N  
ATOM   3565  CA  ALA C  46      -7.394  -3.493  87.897  1.00 42.00           C  
ANISOU 3565  CA  ALA C  46     3512   5704   6742     81   -802   -918       C  
ATOM   3566  C   ALA C  46      -7.814  -3.364  86.438  1.00 41.61           C  
ANISOU 3566  C   ALA C  46     3661   5511   6640    246   -979  -1035       C  
ATOM   3567  O   ALA C  46      -8.762  -4.024  85.997  1.00 42.56           O  
ANISOU 3567  O   ALA C  46     3626   5666   6880    262  -1167  -1069       O  
ATOM   3568  CB  ALA C  46      -7.901  -2.306  88.720  1.00 29.23           C  
ANISOU 3568  CB  ALA C  46     1818   4271   5019    210   -712   -960       C  
ATOM   3569  N   LEU C  47      -7.122  -2.520  85.671  1.00 41.36           N  
ANISOU 3569  N   LEU C  47     3947   5336   6431    372   -931  -1080       N  
ATOM   3570  CA  LEU C  47      -7.501  -2.323  84.275  1.00 38.39           C  
ANISOU 3570  CA  LEU C  47     3734   4892   5959    547  -1090  -1163       C  
ATOM   3571  C   LEU C  47      -7.319  -3.600  83.461  1.00 39.57           C  
ANISOU 3571  C   LEU C  47     3860   4990   6184    484  -1235  -1230       C  
ATOM   3572  O   LEU C  47      -8.194  -3.967  82.666  1.00 39.48           O  
ANISOU 3572  O   LEU C  47     3780   5014   6205    584  -1435  -1331       O  
ATOM   3573  CB  LEU C  47      -6.690  -1.183  83.663  1.00 34.73           C  
ANISOU 3573  CB  LEU C  47     3574   4318   5302    676  -1004  -1129       C  
ATOM   3574  CG  LEU C  47      -6.956   0.239  84.157  1.00 37.26           C  
ANISOU 3574  CG  LEU C  47     3936   4628   5595    798   -934  -1107       C  
ATOM   3575  CD1 LEU C  47      -5.848   1.158  83.666  1.00 36.80           C  
ANISOU 3575  CD1 LEU C  47     4149   4411   5423    858   -842  -1013       C  
ATOM   3576  CD2 LEU C  47      -8.310   0.742  83.684  1.00 33.74           C  
ANISOU 3576  CD2 LEU C  47     3417   4252   5150    983  -1095  -1170       C  
ATOM   3577  N   GLN C  48      -6.192  -4.298  83.643  1.00 41.90           N  
ANISOU 3577  N   GLN C  48     4198   5202   6522    331  -1153  -1199       N  
ATOM   3578  CA  GLN C  48      -5.916  -5.442  82.777  1.00 44.58           C  
ANISOU 3578  CA  GLN C  48     4525   5477   6939    306  -1313  -1315       C  
ATOM   3579  C   GLN C  48      -6.937  -6.560  82.977  1.00 49.52           C  
ANISOU 3579  C   GLN C  48     4831   6117   7868    221  -1518  -1366       C  
ATOM   3580  O   GLN C  48      -7.236  -7.299  82.030  1.00 47.69           O  
ANISOU 3580  O   GLN C  48     4555   5848   7717    290  -1739  -1534       O  
ATOM   3581  CB  GLN C  48      -4.485  -5.943  83.005  1.00 28.57           C  
ANISOU 3581  CB  GLN C  48     2592   3349   4915    159  -1184  -1275       C  
ATOM   3582  CG  GLN C  48      -4.215  -6.459  84.386  1.00 28.85           C  
ANISOU 3582  CG  GLN C  48     2428   3373   5160    -77  -1063  -1133       C  
ATOM   3583  CD  GLN C  48      -4.540  -7.926  84.514  1.00 38.43           C  
ANISOU 3583  CD  GLN C  48     3414   4529   6657   -209  -1200  -1123       C  
ATOM   3584  OE1 GLN C  48      -4.555  -8.656  83.519  1.00 39.57           O  
ANISOU 3584  OE1 GLN C  48     3607   4593   6835   -131  -1354  -1263       O  
ATOM   3585  NE2 GLN C  48      -4.809  -8.371  85.735  1.00 41.66           N  
ANISOU 3585  NE2 GLN C  48     3698   5005   7125   -352  -1054   -878       N  
ATOM   3586  N   ALA C  49      -7.510  -6.676  84.179  1.00 49.15           N  
ANISOU 3586  N   ALA C  49     4543   6147   7987     87  -1455  -1216       N  
ATOM   3587  CA  ALA C  49      -8.530  -7.697  84.417  1.00 54.16           C  
ANISOU 3587  CA  ALA C  49     5035   6783   8761      7  -1500  -1102       C  
ATOM   3588  C   ALA C  49      -9.749  -7.513  83.518  1.00 50.03           C  
ANISOU 3588  C   ALA C  49     4489   6296   8225    180  -1695  -1240       C  
ATOM   3589  O   ALA C  49     -10.403  -8.494  83.150  1.00 58.61           O  
ANISOU 3589  O   ALA C  49     5509   7314   9446    155  -1803  -1247       O  
ATOM   3590  CB  ALA C  49      -8.956  -7.683  85.886  1.00 55.47           C  
ANISOU 3590  CB  ALA C  49     5036   7114   8926   -135  -1325   -843       C  
ATOM   3591  N   ARG C  50     -10.075  -6.271  83.161  1.00 46.67           N  
ANISOU 3591  N   ARG C  50     4119   5975   7641    371  -1743  -1345       N  
ATOM   3592  CA  ARG C  50     -11.226  -5.992  82.313  1.00 45.19           C  
ANISOU 3592  CA  ARG C  50     3932   5843   7396    553  -1910  -1457       C  
ATOM   3593  C   ARG C  50     -11.011  -6.413  80.873  1.00 42.74           C  
ANISOU 3593  C   ARG C  50     3754   5467   7020    687  -2084  -1661       C  
ATOM   3594  O   ARG C  50     -11.957  -6.365  80.083  1.00 45.28           O  
ANISOU 3594  O   ARG C  50     4073   5836   7295    828  -2221  -1760       O  
ATOM   3595  CB  ARG C  50     -11.550  -4.499  82.354  1.00 43.06           C  
ANISOU 3595  CB  ARG C  50     3739   5689   6933    742  -1871  -1466       C  
ATOM   3596  CG  ARG C  50     -11.390  -3.889  83.730  1.00 46.25           C  
ANISOU 3596  CG  ARG C  50     4066   6173   7335    651  -1659  -1323       C  
ATOM   3597  CD  ARG C  50     -11.912  -2.475  83.780  1.00 51.29           C  
ANISOU 3597  CD  ARG C  50     4803   6881   7804    842  -1603  -1336       C  
ATOM   3598  NE  ARG C  50     -12.659  -2.241  85.013  1.00 63.08           N  
ANISOU 3598  NE  ARG C  50     6031   8564   9373    805  -1545  -1281       N  
ATOM   3599  CZ  ARG C  50     -13.887  -2.703  85.246  1.00 69.19           C  
ANISOU 3599  CZ  ARG C  50     6611   9464  10215    770  -1613  -1227       C  
ATOM   3600  NH1 ARG C  50     -14.519  -3.432  84.328  1.00 69.76           N  
ANISOU 3600  NH1 ARG C  50     6697   9464  10344    775  -1770  -1257       N  
ATOM   3601  NH2 ARG C  50     -14.487  -2.441  86.402  1.00 68.92           N  
ANISOU 3601  NH2 ARG C  50     6407   9632  10150    723  -1492  -1120       N  
ATOM   3602  N   LEU C  51      -9.810  -6.810  80.515  1.00 41.74           N  
ANISOU 3602  N   LEU C  51     3387   5300   7170    194   -923  -1792       N  
ATOM   3603  CA  LEU C  51      -9.503  -7.050  79.122  1.00 41.13           C  
ANISOU 3603  CA  LEU C  51     3562   5066   7002    216  -1282  -1763       C  
ATOM   3604  C   LEU C  51      -9.937  -8.453  78.731  1.00 50.58           C  
ANISOU 3604  C   LEU C  51     4663   6190   8366     73  -1354  -1748       C  
ATOM   3605  O   LEU C  51     -10.033  -9.334  79.588  1.00 56.28           O  
ANISOU 3605  O   LEU C  51     5204   7002   9176    -83  -1064  -1686       O  
ATOM   3606  CB  LEU C  51      -8.010  -6.894  78.865  1.00 38.27           C  
ANISOU 3606  CB  LEU C  51     3612   4709   6219    220  -1229  -1591       C  
ATOM   3607  CG  LEU C  51      -7.282  -5.614  79.252  1.00 43.85           C  
ANISOU 3607  CG  LEU C  51     4468   5450   6742    311  -1182  -1548       C  
ATOM   3608  CD1 LEU C  51      -6.040  -5.460  78.366  1.00 47.37           C  
ANISOU 3608  CD1 LEU C  51     5286   5816   6897    338  -1269  -1361       C  
ATOM   3609  CD2 LEU C  51      -8.190  -4.390  79.176  1.00 45.05           C  
ANISOU 3609  CD2 LEU C  51     4482   5541   7094    474  -1375  -1726       C  
ATOM   3610  N   PRO C  52     -10.216  -8.680  77.445  1.00 51.91           N  
ANISOU 3610  N   PRO C  52     4987   6165   8570    124  -1763  -1804       N  
ATOM   3611  CA  PRO C  52     -10.496 -10.050  76.981  1.00 54.18           C  
ANISOU 3611  CA  PRO C  52     5285   6329   8974    -10  -1901  -1797       C  
ATOM   3612  C   PRO C  52      -9.234 -10.899  77.013  1.00 47.64           C  
ANISOU 3612  C   PRO C  52     4804   5531   7767    -79  -1676  -1633       C  
ATOM   3613  O   PRO C  52      -8.142 -10.439  76.676  1.00 45.56           O  
ANISOU 3613  O   PRO C  52     4888   5292   7133     27  -1611  -1532       O  
ATOM   3614  CB  PRO C  52     -11.009  -9.852  75.549  1.00 52.49           C  
ANISOU 3614  CB  PRO C  52     5271   5872   8802    116  -2455  -1917       C  
ATOM   3615  CG  PRO C  52     -11.376  -8.392  75.462  1.00 60.10           C  
ANISOU 3615  CG  PRO C  52     6148   6853   9834    293  -2588  -1999       C  
ATOM   3616  CD  PRO C  52     -10.479  -7.666  76.410  1.00 51.74           C  
ANISOU 3616  CD  PRO C  52     5128   6002   8528    314  -2161  -1896       C  
ATOM   3617  N   GLU C  53      -9.388 -12.150  77.440  1.00 45.23           N  
ANISOU 3617  N   GLU C  53     4376   5213   7598   -257  -1548  -1585       N  
ATOM   3618  CA  GLU C  53      -8.260 -13.039  77.680  1.00 48.11           C  
ANISOU 3618  CA  GLU C  53     4999   5610   7670   -326  -1298  -1423       C  
ATOM   3619  C   GLU C  53      -8.380 -14.286  76.807  1.00 54.28           C  
ANISOU 3619  C   GLU C  53     5991   6160   8471   -372  -1550  -1452       C  
ATOM   3620  O   GLU C  53      -9.407 -14.971  76.827  1.00 59.18           O  
ANISOU 3620  O   GLU C  53     6359   6661   9466   -511  -1727  -1532       O  
ATOM   3621  CB  GLU C  53      -8.194 -13.391  79.164  1.00 50.80           C  
ANISOU 3621  CB  GLU C  53     5069   6136   8097   -487   -876  -1317       C  
ATOM   3622  CG  GLU C  53      -7.558 -14.717  79.501  1.00 56.18           C  
ANISOU 3622  CG  GLU C  53     5877   6790   8679   -624   -694  -1172       C  
ATOM   3623  CD  GLU C  53      -7.542 -14.962  81.000  1.00 59.27           C  
ANISOU 3623  CD  GLU C  53     6045   7357   9119   -769   -292  -1055       C  
ATOM   3624  OE1 GLU C  53      -6.656 -14.403  81.680  1.00 58.36           O  
ANISOU 3624  OE1 GLU C  53     6048   7389   8737   -720    -78   -959       O  
ATOM   3625  OE2 GLU C  53      -8.421 -15.704  81.504  1.00 60.59           O  
ANISOU 3625  OE2 GLU C  53     5930   7496   9594   -934   -203  -1047       O  
ATOM   3626  N   GLU C  54      -7.326 -14.568  76.036  1.00 47.71           N  
ANISOU 3626  N   GLU C  54     5627   5247   7254   -246  -1564  -1381       N  
ATOM   3627  CA  GLU C  54      -7.264 -15.661  75.083  1.00 45.64           C  
ANISOU 3627  CA  GLU C  54     5709   4735   6896   -217  -1805  -1427       C  
ATOM   3628  C   GLU C  54      -6.189 -16.665  75.488  1.00 45.77           C  
ANISOU 3628  C   GLU C  54     5904   4776   6712   -255  -1480  -1261       C  
ATOM   3629  O   GLU C  54      -5.174 -16.292  76.078  1.00 47.48           O  
ANISOU 3629  O   GLU C  54     6127   5179   6735   -220  -1132  -1095       O  
ATOM   3630  CB  GLU C  54      -6.962 -15.145  73.671  1.00 44.67           C  
ANISOU 3630  CB  GLU C  54     6074   4456   6442     37  -2088  -1492       C  
ATOM   3631  N   PRO C  55      -6.383 -17.945  75.185  1.00 43.92           N  
ANISOU 3631  N   PRO C  55     5814   4328   6547   -326  -1624  -1301       N  
ATOM   3632  CA  PRO C  55      -5.329 -18.929  75.450  1.00 45.37           C  
ANISOU 3632  CA  PRO C  55     6212   4494   6534   -320  -1346  -1150       C  
ATOM   3633  C   PRO C  55      -4.321 -18.978  74.312  1.00 56.85           C  
ANISOU 3633  C   PRO C  55     8218   5828   7554    -32  -1346  -1127       C  
ATOM   3634  O   PRO C  55      -4.675 -18.941  73.132  1.00 69.79           O  
ANISOU 3634  O   PRO C  55    10209   7255   9052    123  -1684  -1278       O  
ATOM   3635  CB  PRO C  55      -6.112 -20.244  75.552  1.00 44.91           C  
ANISOU 3635  CB  PRO C  55     6079   4208   6776   -517  -1549  -1220       C  
ATOM   3636  CG  PRO C  55      -7.276 -20.040  74.624  1.00 47.91           C  
ANISOU 3636  CG  PRO C  55     6479   4374   7350   -507  -2069  -1441       C  
ATOM   3637  CD  PRO C  55      -7.606 -18.567  74.650  1.00 46.78           C  
ANISOU 3637  CD  PRO C  55     6117   4428   7228   -430  -2078  -1480       C  
ATOM   3638  N   VAL C  56      -3.044 -19.037  74.672  1.00 62.34           N  
ANISOU 3638  N   VAL C  56     8997   6652   8037     55   -959   -921       N  
ATOM   3639  CA  VAL C  56      -1.986 -19.180  73.674  1.00 70.43           C  
ANISOU 3639  CA  VAL C  56    10505   7572   8681    347   -843   -849       C  
ATOM   3640  C   VAL C  56      -0.957 -20.177  74.177  1.00 72.84           C  
ANISOU 3640  C   VAL C  56    10856   7876   8943    363   -522   -671       C  
ATOM   3641  O   VAL C  56      -0.092 -19.828  74.975  1.00 71.52           O  
ANISOU 3641  O   VAL C  56    10464   7914   8795    332   -205   -460       O  
ATOM   3642  CB  VAL C  56      -1.314 -17.824  73.335  1.00 74.02           C  
ANISOU 3642  CB  VAL C  56    11005   8189   8930    515   -680   -729       C  
ATOM   3643  CG1 VAL C  56      -0.138 -18.034  72.383  1.00 79.53           C  
ANISOU 3643  CG1 VAL C  56    12161   8793   9263    822   -445   -593       C  
ATOM   3644  CG2 VAL C  56      -2.314 -16.861  72.713  1.00 73.38           C  
ANISOU 3644  CG2 VAL C  56    10947   8067   8868    538  -1034   -906       C  
ATOM   3645  N   HIS C  65      -3.954 -25.751  77.699  1.00 50.23           N  
ANISOU 3645  N   HIS C  65     7154   4390   7543   -905   -879   -672       N  
ATOM   3646  CA  HIS C  65      -4.067 -24.342  78.069  1.00 55.61           C  
ANISOU 3646  CA  HIS C  65     7544   5398   8188   -894   -732   -658       C  
ATOM   3647  C   HIS C  65      -3.454 -24.030  79.423  1.00 53.05           C  
ANISOU 3647  C   HIS C  65     6968   5361   7826   -985   -328   -431       C  
ATOM   3648  O   HIS C  65      -4.101 -24.211  80.452  1.00 57.64           O  
ANISOU 3648  O   HIS C  65     7233   6021   8647  -1229   -211   -353       O  
ATOM   3649  CB  HIS C  65      -5.531 -23.912  78.094  1.00 61.76           C  
ANISOU 3649  CB  HIS C  65     7970   6169   9327  -1085   -973   -797       C  
ATOM   3650  CG  HIS C  65      -6.159 -23.824  76.743  1.00 67.94           C  
ANISOU 3650  CG  HIS C  65     8985   6703  10125   -971  -1446  -1035       C  
ATOM   3651  ND1 HIS C  65      -7.481 -23.482  76.562  1.00 71.39           N  
ANISOU 3651  ND1 HIS C  65     9116   7073  10937  -1114  -1764  -1174       N  
ATOM   3652  CD2 HIS C  65      -5.648 -24.026  75.506  1.00 69.13           C  
ANISOU 3652  CD2 HIS C  65     9669   6643   9955   -709  -1664  -1155       C  
ATOM   3653  CE1 HIS C  65      -7.760 -23.481  75.271  1.00 75.06           C  
ANISOU 3653  CE1 HIS C  65     9931   7282  11308   -961  -2221  -1375       C  
ATOM   3654  NE2 HIS C  65      -6.665 -23.807  74.609  1.00 73.83           N  
ANISOU 3654  NE2 HIS C  65    10321   7036  10696   -706  -2153  -1372       N  
ATOM   3655  N   ASP C  66      -2.216 -23.541  79.441  1.00 46.24           N  
ANISOU 3655  N   ASP C  66     6250   4645   6674   -787   -118   -313       N  
ATOM   3656  CA  ASP C  66      -1.604 -23.163  80.706  1.00 46.28           C  
ANISOU 3656  CA  ASP C  66     6056   4894   6634   -866    178   -111       C  
ATOM   3657  C   ASP C  66      -1.031 -21.751  80.683  1.00 40.03           C  
ANISOU 3657  C   ASP C  66     5211   4330   5670   -725    264    -88       C  
ATOM   3658  O   ASP C  66      -0.409 -21.332  81.668  1.00 39.69           O  
ANISOU 3658  O   ASP C  66     5052   4463   5564   -766    449     69       O  
ATOM   3659  CB  ASP C  66      -0.531 -24.184  81.119  1.00 52.72           C  
ANISOU 3659  CB  ASP C  66     7036   5625   7369   -829    332     90       C  
ATOM   3660  CG  ASP C  66       0.541 -24.378  80.062  1.00 56.85           C  
ANISOU 3660  CG  ASP C  66     7881   6028   7692   -529    337    106       C  
ATOM   3661  OD1 ASP C  66       0.575 -23.588  79.093  1.00 53.32           O  
ANISOU 3661  OD1 ASP C  66     7547   5601   7113   -350    265     -6       O  
ATOM   3662  OD2 ASP C  66       1.348 -25.329  80.200  1.00 61.08           O  
ANISOU 3662  OD2 ASP C  66     8567   6439   8201   -456    434    243       O  
ATOM   3663  N   ILE C  67      -1.241 -21.000  79.602  1.00 41.27           N  
ANISOU 3663  N   ILE C  67     5472   4461   5749   -569    103   -236       N  
ATOM   3664  CA  ILE C  67      -0.850 -19.595  79.521  1.00 41.60           C  
ANISOU 3664  CA  ILE C  67     5454   4683   5668   -459    150   -218       C  
ATOM   3665  C   ILE C  67      -1.972 -18.830  78.831  1.00 41.13           C  
ANISOU 3665  C   ILE C  67     5340   4600   5686   -442    -96   -439       C  
ATOM   3666  O   ILE C  67      -2.364 -19.174  77.712  1.00 38.07           O  
ANISOU 3666  O   ILE C  67     5176   4018   5270   -343   -325   -576       O  
ATOM   3667  CB  ILE C  67       0.474 -19.398  78.762  1.00 37.14           C  
ANISOU 3667  CB  ILE C  67     5137   4093   4882   -213    256    -84       C  
ATOM   3668  CG1 ILE C  67       1.618 -20.076  79.507  1.00 33.54           C  
ANISOU 3668  CG1 ILE C  67     4667   3661   4416   -219    476    155       C  
ATOM   3669  CG2 ILE C  67       0.786 -17.939  78.618  1.00 32.17           C  
ANISOU 3669  CG2 ILE C  67     4437   3610   4176   -131    271    -52       C  
ATOM   3670  CD1 ILE C  67       2.974 -19.701  78.984  1.00 32.69           C  
ANISOU 3670  CD1 ILE C  67     4666   3568   4187      4    637    343       C  
ATOM   3671  N   TYR C  68      -2.486 -17.796  79.489  1.00 41.52           N  
ANISOU 3671  N   TYR C  68     5125   4823   5827   -520    -74   -480       N  
ATOM   3672  CA  TYR C  68      -3.560 -16.975  78.947  1.00 39.91           C  
ANISOU 3672  CA  TYR C  68     4815   4604   5744   -493   -307   -678       C  
ATOM   3673  C   TYR C  68      -3.084 -15.537  78.773  1.00 38.40           C  
ANISOU 3673  C   TYR C  68     4653   4534   5403   -353   -297   -659       C  
ATOM   3674  O   TYR C  68      -2.459 -14.968  79.674  1.00 37.99           O  
ANISOU 3674  O   TYR C  68     4504   4639   5292   -385   -106   -538       O  
ATOM   3675  CB  TYR C  68      -4.779 -17.013  79.856  1.00 36.20           C  
ANISOU 3675  CB  TYR C  68     3971   4202   5583   -688   -283   -758       C  
ATOM   3676  CG  TYR C  68      -5.484 -18.353  79.885  1.00 39.89           C  
ANISOU 3676  CG  TYR C  68     4363   4503   6291   -856   -355   -778       C  
ATOM   3677  CD1 TYR C  68      -6.697 -18.537  79.232  1.00 41.01           C  
ANISOU 3677  CD1 TYR C  68     4373   4480   6731   -909   -667   -948       C  
ATOM   3678  CD2 TYR C  68      -4.949 -19.424  80.586  1.00 39.58           C  
ANISOU 3678  CD2 TYR C  68     4374   4446   6221   -972   -148   -616       C  
ATOM   3679  CE1 TYR C  68      -7.351 -19.758  79.264  1.00 46.77           C  
ANISOU 3679  CE1 TYR C  68     5009   5019   7741  -1093   -773   -950       C  
ATOM   3680  CE2 TYR C  68      -5.590 -20.648  80.622  1.00 47.74           C  
ANISOU 3680  CE2 TYR C  68     5345   5295   7500  -1143   -227   -616       C  
ATOM   3681  CZ  TYR C  68      -6.789 -20.813  79.961  1.00 48.97           C  
ANISOU 3681  CZ  TYR C  68     5356   5278   7972  -1214   -539   -781       C  
ATOM   3682  OH  TYR C  68      -7.419 -22.039  80.007  1.00 52.06           O  
ANISOU 3682  OH  TYR C  68     5667   5450   8663  -1413   -653   -763       O  
ATOM   3683  N   VAL C  69      -3.414 -14.947  77.624  1.00 37.88           N  
ANISOU 3683  N   VAL C  69     4744   4367   5281   -205   -540   -777       N  
ATOM   3684  CA  VAL C  69      -2.860 -13.674  77.178  1.00 33.30           C  
ANISOU 3684  CA  VAL C  69     4277   3840   4536    -53   -554   -728       C  
ATOM   3685  C   VAL C  69      -3.969 -12.635  77.071  1.00 34.13           C  
ANISOU 3685  C   VAL C  69     4210   3957   4802    -39   -784   -911       C  
ATOM   3686  O   VAL C  69      -5.051 -12.916  76.543  1.00 36.07           O  
ANISOU 3686  O   VAL C  69     4413   4080   5214    -46  -1052  -1085       O  
ATOM   3687  CB  VAL C  69      -2.133 -13.851  75.828  1.00 33.99           C  
ANISOU 3687  CB  VAL C  69     4782   3778   4355    157   -599   -663       C  
ATOM   3688  CG1 VAL C  69      -1.753 -12.521  75.229  1.00 33.74           C  
ANISOU 3688  CG1 VAL C  69     4872   3764   4182    305   -638   -604       C  
ATOM   3689  CG2 VAL C  69      -0.893 -14.718  76.014  1.00 33.33           C  
ANISOU 3689  CG2 VAL C  69     4821   3699   4143    185   -311   -453       C  
ATOM   3690  N   ARG C  70      -3.695 -11.432  77.578  1.00 34.72           N  
ANISOU 3690  N   ARG C  70     4182   4153   4857    -14   -712   -869       N  
ATOM   3691  CA  ARG C  70      -4.544 -10.256  77.396  1.00 37.75           C  
ANISOU 3691  CA  ARG C  70     4452   4530   5361     55   -922  -1021       C  
ATOM   3692  C   ARG C  70      -3.774  -9.237  76.570  1.00 37.54           C  
ANISOU 3692  C   ARG C  70     4693   4449   5121    214   -996   -920       C  
ATOM   3693  O   ARG C  70      -2.804  -8.645  77.054  1.00 38.26           O  
ANISOU 3693  O   ARG C  70     4798   4618   5120    203   -826   -756       O  
ATOM   3694  CB  ARG C  70      -4.948  -9.657  78.738  1.00 38.00           C  
ANISOU 3694  CB  ARG C  70     4173   4716   5551    -32   -772  -1073       C  
ATOM   3695  CG  ARG C  70      -5.989 -10.453  79.451  1.00 35.30           C  
ANISOU 3695  CG  ARG C  70     3532   4415   5467   -164   -691  -1175       C  
ATOM   3696  CD  ARG C  70      -5.907 -10.237  80.935  1.00 41.02           C  
ANISOU 3696  CD  ARG C  70     4087   5306   6195   -247   -392  -1137       C  
ATOM   3697  NE  ARG C  70      -7.222 -10.323  81.548  1.00 50.84           N  
ANISOU 3697  NE  ARG C  70     4988   6594   7737   -296   -312  -1271       N  
ATOM   3698  CZ  ARG C  70      -7.436 -10.821  82.756  1.00 57.79           C  
ANISOU 3698  CZ  ARG C  70     5714   7585   8657   -409      3  -1221       C  
ATOM   3699  NH1 ARG C  70      -6.415 -11.289  83.456  1.00 61.92           N  
ANISOU 3699  NH1 ARG C  70     6426   8174   8927   -489    197  -1057       N  
ATOM   3700  NH2 ARG C  70      -8.664 -10.864  83.252  1.00 60.48           N  
ANISOU 3700  NH2 ARG C  70     5715   7963   9303   -435    129  -1316       N  
ATOM   3701  N   ARG C  71      -4.201  -9.023  75.334  1.00 37.11           N  
ANISOU 3701  N   ARG C  71     4863   4240   4998    353  -1270  -1001       N  
ATOM   3702  CA  ARG C  71      -3.440  -8.194  74.413  1.00 38.20           C  
ANISOU 3702  CA  ARG C  71     5319   4301   4894    513  -1304   -862       C  
ATOM   3703  C   ARG C  71      -3.858  -6.736  74.543  1.00 35.35           C  
ANISOU 3703  C   ARG C  71     4853   3941   4638    560  -1469   -924       C  
ATOM   3704  O   ARG C  71      -5.047  -6.424  74.611  1.00 36.59           O  
ANISOU 3704  O   ARG C  71     4828   4066   5009    572  -1713  -1137       O  
ATOM   3705  CB  ARG C  71      -3.624  -8.691  72.985  1.00 43.96           C  
ANISOU 3705  CB  ARG C  71     6452   4837   5414    671  -1513   -904       C  
ATOM   3706  CG  ARG C  71      -3.336 -10.172  72.863  1.00 44.41           C  
ANISOU 3706  CG  ARG C  71     6638   4851   5383    643  -1391   -888       C  
ATOM   3707  CD  ARG C  71      -3.225 -10.637  71.429  1.00 47.33           C  
ANISOU 3707  CD  ARG C  71     7535   5009   5439    847  -1544   -903       C  
ATOM   3708  NE  ARG C  71      -2.979 -12.076  71.382  1.00 51.15           N  
ANISOU 3708  NE  ARG C  71     8154   5425   5858    830  -1441   -914       N  
ATOM   3709  CZ  ARG C  71      -1.771 -12.625  71.394  1.00 51.70           C  
ANISOU 3709  CZ  ARG C  71     8376   5530   5739    898  -1065   -708       C  
ATOM   3710  NH1 ARG C  71      -0.695 -11.851  71.443  1.00 54.15           N  
ANISOU 3710  NH1 ARG C  71     8687   5948   5942    967   -760   -457       N  
ATOM   3711  NH2 ARG C  71      -1.636 -13.944  71.353  1.00 54.64           N  
ANISOU 3711  NH2 ARG C  71     8881   5811   6071    897  -1008   -742       N  
ATOM   3712  N   ILE C  72      -2.870  -5.855  74.609  1.00 27.20           N  
ANISOU 3712  N   ILE C  72     4296   2929   3108    776  -1065   -560       N  
ATOM   3713  CA  ILE C  72      -3.091  -4.418  74.619  1.00 29.87           C  
ANISOU 3713  CA  ILE C  72     4674   3250   3424    866  -1121   -537       C  
ATOM   3714  C   ILE C  72      -2.759  -3.800  73.268  1.00 31.09           C  
ANISOU 3714  C   ILE C  72     5134   3305   3375    938  -1211   -505       C  
ATOM   3715  O   ILE C  72      -3.456  -2.902  72.790  1.00 36.47           O  
ANISOU 3715  O   ILE C  72     5879   3940   4037   1032  -1389   -514       O  
ATOM   3716  CB  ILE C  72      -2.256  -3.782  75.749  1.00 26.20           C  
ANISOU 3716  CB  ILE C  72     4137   2829   2991    831   -917   -472       C  
ATOM   3717  CG1 ILE C  72      -2.902  -4.077  77.108  1.00 29.69           C  
ANISOU 3717  CG1 ILE C  72     4299   3366   3617    778   -867   -511       C  
ATOM   3718  CG2 ILE C  72      -2.101  -2.284  75.532  1.00 26.40           C  
ANISOU 3718  CG2 ILE C  72     4283   2800   2948    917   -944   -432       C  
ATOM   3719  CD1 ILE C  72      -1.910  -4.275  78.268  1.00 32.85           C  
ANISOU 3719  CD1 ILE C  72     4633   3816   4033    683   -658   -449       C  
HETATM 3720  N   MSE C  73      -1.706  -4.297  72.645  1.00 31.22           N  
ANISOU 3720  N   MSE C  73     5344   3277   3242    894  -1086   -468       N  
HETATM 3721  CA  MSE C  73      -1.249  -3.801  71.369  1.00 36.18           C  
ANISOU 3721  CA  MSE C  73     6295   3807   3645    939  -1117   -432       C  
HETATM 3722  C   MSE C  73      -0.598  -4.930  70.590  1.00 33.58           C  
ANISOU 3722  C   MSE C  73     6125   3439   3195    882  -1028   -455       C  
HETATM 3723  O   MSE C  73       0.222  -5.668  71.144  1.00 32.36           O  
ANISOU 3723  O   MSE C  73     5872   3314   3110    809   -829   -443       O  
HETATM 3724  CB  MSE C  73      -0.273  -2.658  71.588  1.00 38.06           C  
ANISOU 3724  CB  MSE C  73     6624   4014   3821    948   -955   -337       C  
HETATM 3725  CG  MSE C  73       0.549  -2.290  70.398  1.00 45.67           C  
ANISOU 3725  CG  MSE C  73     7924   4878   4551    956   -885   -281       C  
HETATM 3726 SE   MSE C  73       0.964  -0.410  70.570  1.00 59.68          SE  
ANISOU 3726 SE   MSE C  73     9800   6590   6285   1009   -844   -175      SE  
HETATM 3727  CE  MSE C  73      -0.720   0.298  69.935  1.00 49.35           C  
ANISOU 3727  CE  MSE C  73     8562   5232   4958   1141  -1234   -214       C  
ATOM   3728  N   VAL C  74      -0.958  -5.062  69.313  1.00 34.21           N  
ANISOU 3728  N   VAL C  74     6460   3444   3095    917  -1182   -491       N  
ATOM   3729  CA  VAL C  74      -0.483  -6.152  68.479  1.00 32.50           C  
ANISOU 3729  CA  VAL C  74     6422   3178   2749    869  -1113   -539       C  
ATOM   3730  C   VAL C  74       0.433  -5.592  67.394  1.00 40.24           C  
ANISOU 3730  C   VAL C  74     7763   4064   3461    881   -991   -486       C  
ATOM   3731  O   VAL C  74       0.342  -4.425  67.009  1.00 38.67           O  
ANISOU 3731  O   VAL C  74     7725   3822   3146    936  -1063   -421       O  
ATOM   3732  CB  VAL C  74      -1.662  -6.932  67.869  1.00 46.63           C  
ANISOU 3732  CB  VAL C  74     8232   4951   4534    879  -1389   -643       C  
ATOM   3733  CG1 VAL C  74      -2.629  -7.368  68.966  1.00 39.10           C  
ANISOU 3733  CG1 VAL C  74     6906   4087   3863    860  -1494   -690       C  
ATOM   3734  CG2 VAL C  74      -2.373  -6.082  66.841  1.00 49.29           C  
ANISOU 3734  CG2 VAL C  74     8815   5217   4694    960  -1652   -639       C  
ATOM   3735  N   ASP C  75       1.326  -6.456  66.881  1.00 33.96           N  
ANISOU 3735  N   ASP C  75     7104   3226   2571    828   -793   -515       N  
ATOM   3736  CA  ASP C  75       2.389  -6.044  65.965  1.00 42.27           C  
ANISOU 3736  CA  ASP C  75     8473   4192   3393    817   -587   -468       C  
ATOM   3737  C   ASP C  75       2.623  -7.171  64.950  1.00 42.49           C  
ANISOU 3737  C   ASP C  75     8730   4154   3261    785   -530   -564       C  
ATOM   3738  O   ASP C  75       3.689  -7.779  64.886  1.00 44.91           O  
ANISOU 3738  O   ASP C  75     9052   4431   3579    739   -250   -580       O  
ATOM   3739  CB  ASP C  75       3.664  -5.695  66.740  1.00 34.48           C  
ANISOU 3739  CB  ASP C  75     7342   3225   2532    777   -277   -387       C  
ATOM   3740  CG  ASP C  75       4.766  -5.137  65.854  1.00 38.20           C  
ANISOU 3740  CG  ASP C  75     8109   3605   2799    759    -38   -331       C  
ATOM   3741  OD1 ASP C  75       4.473  -4.667  64.733  1.00 40.30           O  
ANISOU 3741  OD1 ASP C  75     8715   3797   2800    785   -129   -324       O  
ATOM   3742  OD2 ASP C  75       5.938  -5.178  66.280  1.00 36.95           O  
ANISOU 3742  OD2 ASP C  75     7844   3443   2751    712    241   -291       O  
ATOM   3743  N   ARG C  76       1.610  -7.437  64.126  1.00 43.71           N  
ANISOU 3743  N   ARG C  76     9067   4273   3269    811   -807   -637       N  
ATOM   3744  CA  ARG C  76       1.625  -8.594  63.237  1.00 44.31           C  
ANISOU 3744  CA  ARG C  76     9336   4287   3212    776   -803   -749       C  
ATOM   3745  C   ARG C  76       2.662  -8.456  62.125  1.00 55.39           C  
ANISOU 3745  C   ARG C  76    11021   5608   4415    741   -540   -699       C  
ATOM   3746  O   ARG C  76       2.993  -7.351  61.683  1.00 57.30           O  
ANISOU 3746  O   ARG C  76    11430   5813   4530    753   -482   -593       O  
ATOM   3747  CB  ARG C  76       0.250  -8.802  62.609  1.00 52.40           C  
ANISOU 3747  CB  ARG C  76    10406   5299   4205    797  -1177   -797       C  
ATOM   3748  CG  ARG C  76      -0.867  -8.973  63.610  1.00 57.44           C  
ANISOU 3748  CG  ARG C  76    10734   6014   5076    822  -1441   -851       C  
ATOM   3749  CD  ARG C  76      -2.135  -9.453  62.930  1.00 61.58           C  
ANISOU 3749  CD  ARG C  76    11280   6512   5606    826  -1781   -920       C  
ATOM   3750  NE  ARG C  76      -3.292  -9.265  63.798  1.00 65.50           N  
ANISOU 3750  NE  ARG C  76    11476   7076   6335    860  -2052   -951       N  
ATOM   3751  CZ  ARG C  76      -4.142  -8.249  63.696  1.00 67.47           C  
ANISOU 3751  CZ  ARG C  76    11691   7325   6619    932  -2291   -896       C  
ATOM   3752  NH1 ARG C  76      -5.164  -8.154  64.533  1.00 72.82           N  
ANISOU 3752  NH1 ARG C  76    12048   8067   7552    960  -2497   -932       N  
ATOM   3753  NH2 ARG C  76      -3.976  -7.331  62.754  1.00 64.86           N  
ANISOU 3753  NH2 ARG C  76    11633   6917   6093    973  -2310   -805       N  
ATOM   3754  N   ALA C  77       3.145  -9.611  61.650  1.00 55.24           N  
ANISOU 3754  N   ALA C  77    11055   5551   4382    693   -384   -783       N  
ATOM   3755  CA  ALA C  77       4.142  -9.656  60.581  1.00 54.63           C  
ANISOU 3755  CA  ALA C  77    11227   5395   4136    651   -113   -761       C  
ATOM   3756  C   ALA C  77       3.690  -8.835  59.384  1.00 52.44           C  
ANISOU 3756  C   ALA C  77    11261   5051   3613    660   -265   -696       C  
ATOM   3757  O   ALA C  77       2.577  -9.005  58.882  1.00 56.21           O  
ANISOU 3757  O   ALA C  77    11820   5516   4023    679   -582   -733       O  
ATOM   3758  CB  ALA C  77       4.398 -11.105  60.148  1.00 47.86           C  
ANISOU 3758  CB  ALA C  77    10387   4501   3296    610     -9   -886       C  
ATOM   3759  N   GLY C  78       4.556  -7.936  58.933  1.00 55.36           N  
ANISOU 3759  N   GLY C  78    11798   5367   3869    641    -43   -598       N  
ATOM   3760  CA  GLY C  78       4.207  -7.112  57.794  1.00 61.67           C  
ANISOU 3760  CA  GLY C  78    12913   6079   4439    643   -169   -531       C  
ATOM   3761  C   GLY C  78       3.231  -5.995  58.080  1.00 62.86           C  
ANISOU 3761  C   GLY C  78    13041   6240   4604    707   -484   -454       C  
ATOM   3762  O   GLY C  78       2.787  -5.328  57.139  1.00 67.96           O  
ANISOU 3762  O   GLY C  78    13943   6800   5079    717   -642   -404       O  
ATOM   3763  N   GLU C  79       2.886  -5.753  59.341  1.00 52.25           N  
ANISOU 3763  N   GLU C  79    11401   4988   3463    753   -578   -445       N  
ATOM   3764  CA  GLU C  79       1.908  -4.731  59.682  1.00 51.34           C  
ANISOU 3764  CA  GLU C  79    11227   4883   3398    824   -881   -387       C  
ATOM   3765  C   GLU C  79       2.503  -3.704  60.640  1.00 52.86           C  
ANISOU 3765  C   GLU C  79    11280   5110   3692    842   -731   -295       C  
ATOM   3766  O   GLU C  79       3.612  -3.855  61.157  1.00 49.59           O  
ANISOU 3766  O   GLU C  79    10781   4724   3337    799   -412   -281       O  
ATOM   3767  CB  GLU C  79       0.654  -5.357  60.298  1.00 49.36           C  
ANISOU 3767  CB  GLU C  79    10734   4707   3312    869  -1204   -476       C  
ATOM   3768  CG  GLU C  79      -0.071  -6.316  59.382  1.00 56.15           C  
ANISOU 3768  CG  GLU C  79    11714   5527   4094    850  -1399   -567       C  
ATOM   3769  CD  GLU C  79      -1.292  -6.920  60.041  1.00 59.68           C  
ANISOU 3769  CD  GLU C  79    11887   6044   4747    882  -1705   -656       C  
ATOM   3770  OE1 GLU C  79      -1.570  -6.546  61.200  1.00 58.66           O  
ANISOU 3770  OE1 GLU C  79    11483   5994   4809    921  -1758   -647       O  
ATOM   3771  OE2 GLU C  79      -1.981  -7.755  59.409  1.00 62.15           O  
ANISOU 3771  OE2 GLU C  79    12253   6327   5036    863  -1890   -738       O  
ATOM   3772  N   ARG C  80       1.748  -2.655  60.867  1.00 52.14           N  
ANISOU 3772  N   ARG C  80    11160   5011   3641    907   -968   -236       N  
ATOM   3773  CA  ARG C  80       2.115  -1.643  61.836  1.00 49.89           C  
ANISOU 3773  CA  ARG C  80    10730   4760   3465    933   -882   -155       C  
ATOM   3774  C   ARG C  80       1.444  -1.933  63.171  1.00 44.80           C  
ANISOU 3774  C   ARG C  80     9747   4237   3037    985  -1034   -209       C  
ATOM   3775  O   ARG C  80       0.455  -2.667  63.230  1.00 46.17           O  
ANISOU 3775  O   ARG C  80     9806   4451   3284   1011  -1275   -300       O  
ATOM   3776  CB  ARG C  80       1.714  -0.254  61.323  1.00 52.01           C  
ANISOU 3776  CB  ARG C  80    11162   4934   3666    976  -1039    -63       C  
ATOM   3777  N   PRO C  81       1.971  -1.392  64.269  1.00 45.89           N  
ANISOU 3777  N   PRO C  81     9692   4431   3311    987   -887   -156       N  
ATOM   3778  CA  PRO C  81       1.366  -1.648  65.586  1.00 42.48           C  
ANISOU 3778  CA  PRO C  81     8829   4113   3199   1006   -974   -201       C  
ATOM   3779  C   PRO C  81      -0.067  -1.139  65.669  1.00 43.09           C  
ANISOU 3779  C   PRO C  81     8827   4194   3352   1099  -1341   -222       C  
ATOM   3780  O   PRO C  81      -0.399  -0.084  65.133  1.00 50.37           O  
ANISOU 3780  O   PRO C  81     9949   5033   4155   1163  -1498   -157       O  
ATOM   3781  CB  PRO C  81       2.282  -0.884  66.548  1.00 43.43           C  
ANISOU 3781  CB  PRO C  81     8779   4258   3463    977   -735   -117       C  
ATOM   3782  CG  PRO C  81       3.587  -0.778  65.831  1.00 45.57           C  
ANISOU 3782  CG  PRO C  81     9307   4453   3555    914   -445    -59       C  
ATOM   3783  CD  PRO C  81       3.231  -0.634  64.378  1.00 50.92           C  
ANISOU 3783  CD  PRO C  81    10404   5028   3916    940   -577    -55       C  
ATOM   3784  N   GLN C  82      -0.912  -1.887  66.381  1.00 42.56           N  
ANISOU 3784  N   GLN C  82     8450   4215   3506   1105  -1472   -312       N  
ATOM   3785  CA  GLN C  82      -2.341  -1.598  66.448  1.00 40.73           C  
ANISOU 3785  CA  GLN C  82     8094   3988   3393   1189  -1816   -357       C  
ATOM   3786  C   GLN C  82      -2.867  -1.746  67.864  1.00 38.48           C  
ANISOU 3786  C   GLN C  82     7373   3815   3433   1188  -1799   -402       C  
ATOM   3787  O   GLN C  82      -2.701  -2.805  68.476  1.00 41.26           O  
ANISOU 3787  O   GLN C  82     7525   4246   3905   1113  -1672   -456       O  
ATOM   3788  CB  GLN C  82      -3.131  -2.546  65.550  1.00 43.57           C  
ANISOU 3788  CB  GLN C  82     8571   4321   3665   1189  -2060   -449       C  
ATOM   3789  CG  GLN C  82      -2.911  -2.369  64.070  1.00 41.83           C  
ANISOU 3789  CG  GLN C  82     8770   3978   3147   1187  -2118   -414       C  
ATOM   3790  CD  GLN C  82      -3.662  -3.407  63.312  1.00 45.37           C  
ANISOU 3790  CD  GLN C  82     9252   4401   3585   1160  -2306   -508       C  
ATOM   3791  OE1 GLN C  82      -3.934  -4.491  63.839  1.00 53.62           O  
ANISOU 3791  OE1 GLN C  82    10095   5521   4755   1123  -2327   -607       O  
ATOM   3792  NE2 GLN C  82      -4.015  -3.101  62.082  1.00 46.24           N  
ANISOU 3792  NE2 GLN C  82     9618   4398   3553   1171  -2450   -482       N  
ATOM   3793  N   LEU C  83      -3.545  -0.714  68.360  1.00 38.74           N  
ANISOU 3793  N   LEU C  83     7270   3845   3604   1270  -1931   -384       N  
ATOM   3794  CA  LEU C  83      -4.246  -0.838  69.633  1.00 41.59           C  
ANISOU 3794  CA  LEU C  83     7233   4305   4262   1274  -1933   -446       C  
ATOM   3795  C   LEU C  83      -5.443  -1.769  69.485  1.00 44.99           C  
ANISOU 3795  C   LEU C  83     7501   4767   4825   1278  -2162   -553       C  
ATOM   3796  O   LEU C  83      -6.186  -1.705  68.500  1.00 42.35           O  
ANISOU 3796  O   LEU C  83     7314   4358   4419   1340  -2448   -578       O  
ATOM   3797  CB  LEU C  83      -4.725   0.525  70.127  1.00 41.98           C  
ANISOU 3797  CB  LEU C  83     7191   4326   4434   1372  -2015   -418       C  
ATOM   3798  CG  LEU C  83      -3.901   1.285  71.155  1.00 33.45           C  
ANISOU 3798  CG  LEU C  83     6022   3275   3412   1347  -1762   -363       C  
ATOM   3799  CD1 LEU C  83      -4.503   2.675  71.357  1.00 36.29           C  
ANISOU 3799  CD1 LEU C  83     6352   3569   3867   1463  -1896   -348       C  
ATOM   3800  CD2 LEU C  83      -3.865   0.503  72.456  1.00 43.98           C  
ANISOU 3800  CD2 LEU C  83     7037   4739   4934   1264  -1584   -419       C  
ATOM   3801  N   VAL C  84      -5.622  -2.643  70.477  1.00 43.66           N  
ANISOU 3801  N   VAL C  84     7033   4701   4854   1205  -2044   -612       N  
ATOM   3802  CA  VAL C  84      -6.751  -3.560  70.530  1.00 41.89           C  
ANISOU 3802  CA  VAL C  84     6600   4513   4805   1187  -2224   -715       C  
ATOM   3803  C   VAL C  84      -7.313  -3.537  71.940  1.00 39.47           C  
ANISOU 3803  C   VAL C  84     5910   4305   4783   1167  -2125   -755       C  
ATOM   3804  O   VAL C  84      -6.665  -3.078  72.881  1.00 37.71           O  
ANISOU 3804  O   VAL C  84     5612   4130   4585   1144  -1895   -707       O  
ATOM   3805  CB  VAL C  84      -6.363  -5.005  70.149  1.00 39.35           C  
ANISOU 3805  CB  VAL C  84     6349   4200   4403   1083  -2161   -753       C  
ATOM   3806  CG1 VAL C  84      -5.782  -5.043  68.751  1.00 47.88           C  
ANISOU 3806  CG1 VAL C  84     7832   5180   5180   1096  -2225   -728       C  
ATOM   3807  CG2 VAL C  84      -5.373  -5.574  71.162  1.00 36.08           C  
ANISOU 3807  CG2 VAL C  84     5813   3861   4034    983  -1834   -718       C  
ATOM   3808  N   ASN C  85      -8.527  -4.063  72.076  1.00 37.21           N  
ANISOU 3808  N   ASN C  85     5386   4042   4708   1167  -2297   -848       N  
ATOM   3809  CA  ASN C  85      -9.198  -4.193  73.370  1.00 41.19           C  
ANISOU 3809  CA  ASN C  85     5521   4639   5491   1132  -2192   -903       C  
ATOM   3810  C   ASN C  85      -9.393  -2.834  74.039  1.00 42.58           C  
ANISOU 3810  C   ASN C  85     5597   4818   5762   1226  -2145   -888       C  
ATOM   3811  O   ASN C  85      -9.194  -2.674  75.242  1.00 41.52           O  
ANISOU 3811  O   ASN C  85     5293   4761   5722   1181  -1916   -887       O  
ATOM   3812  CB  ASN C  85      -8.453  -5.165  74.277  1.00 41.04           C  
ANISOU 3812  CB  ASN C  85     5417   4703   5473    993  -1910   -881       C  
ATOM   3813  CG  ASN C  85      -8.636  -6.603  73.835  1.00 44.64           C  
ANISOU 3813  CG  ASN C  85     5869   5153   5939    901  -1974   -927       C  
ATOM   3814  OD1 ASN C  85      -9.461  -6.884  72.971  1.00 47.33           O  
ANISOU 3814  OD1 ASN C  85     6226   5440   6316    933  -2233   -992       O  
ATOM   3815  ND2 ASN C  85      -7.885  -7.520  74.432  1.00 43.77           N  
ANISOU 3815  ND2 ASN C  85     5737   5086   5807    786  -1756   -896       N  
ATOM   3816  N   LEU C  86      -9.793  -1.848  73.239  1.00 40.73           N  
ANISOU 3816  N   LEU C  86     5490   4491   5497   1356  -2374   -879       N  
ATOM   3817  CA  LEU C  86     -10.198  -0.554  73.753  1.00 43.22           C  
ANISOU 3817  CA  LEU C  86     5695   4781   5944   1467  -2385   -885       C  
ATOM   3818  C   LEU C  86     -11.420  -0.714  74.659  1.00 45.36           C  
ANISOU 3818  C   LEU C  86     5565   5116   6556   1474  -2388   -999       C  
ATOM   3819  O   LEU C  86     -12.172  -1.684  74.539  1.00 44.51           O  
ANISOU 3819  O   LEU C  86     5287   5037   6589   1422  -2490  -1070       O  
ATOM   3820  CB  LEU C  86     -10.510   0.386  72.588  1.00 45.97           C  
ANISOU 3820  CB  LEU C  86     6263   4994   6208   1607  -2683   -851       C  
ATOM   3821  CG  LEU C  86      -9.345   0.595  71.615  1.00 49.94           C  
ANISOU 3821  CG  LEU C  86     7190   5425   6362   1593  -2665   -737       C  
ATOM   3822  CD1 LEU C  86      -9.836   1.005  70.233  1.00 54.92           C  
ANISOU 3822  CD1 LEU C  86     8068   5922   6875   1695  -3020   -712       C  
ATOM   3823  CD2 LEU C  86      -8.378   1.632  72.165  1.00 46.57           C  
ANISOU 3823  CD2 LEU C  86     6865   4985   5847   1604  -2437   -655       C  
ATOM   3824  N   PRO C  87     -11.649   0.235  75.578  1.00 48.16           N  
ANISOU 3824  N   PRO C  87     5758   5483   7056   1533  -2266  -1027       N  
ATOM   3825  CA  PRO C  87     -10.881   1.460  75.823  1.00 48.50           C  
ANISOU 3825  CA  PRO C  87     5968   5481   6978   1596  -2154   -959       C  
ATOM   3826  C   PRO C  87      -9.751   1.310  76.849  1.00 47.34           C  
ANISOU 3826  C   PRO C  87     5859   5421   6708   1475  -1815   -911       C  
ATOM   3827  O   PRO C  87      -8.817   2.111  76.842  1.00 52.25           O  
ANISOU 3827  O   PRO C  87     6685   5998   7169   1492  -1728   -833       O  
ATOM   3828  CB  PRO C  87     -11.953   2.420  76.337  1.00 51.44           C  
ANISOU 3828  CB  PRO C  87     6094   5818   7632   1723  -2220  -1051       C  
ATOM   3829  CG  PRO C  87     -12.871   1.526  77.115  1.00 50.34           C  
ANISOU 3829  CG  PRO C  87     5599   5780   7748   1650  -2137  -1162       C  
ATOM   3830  CD  PRO C  87     -12.884   0.197  76.384  1.00 46.48           C  
ANISOU 3830  CD  PRO C  87     5161   5317   7183   1554  -2255  -1148       C  
ATOM   3831  N   HIS C  88      -9.820   0.284  77.704  1.00 47.75           N  
ANISOU 3831  N   HIS C  88     5724   5584   6834   1348  -1640   -949       N  
ATOM   3832  CA  HIS C  88      -8.890   0.188  78.825  1.00 43.21           C  
ANISOU 3832  CA  HIS C  88     5157   5088   6174   1239  -1346   -909       C  
ATOM   3833  C   HIS C  88      -7.458  -0.102  78.391  1.00 41.16           C  
ANISOU 3833  C   HIS C  88     5172   4812   5656   1170  -1269   -793       C  
ATOM   3834  O   HIS C  88      -6.524   0.243  79.120  1.00 37.83           O  
ANISOU 3834  O   HIS C  88     4814   4414   5146   1117  -1079   -741       O  
ATOM   3835  CB  HIS C  88      -9.374  -0.873  79.803  1.00 41.76           C  
ANISOU 3835  CB  HIS C  88     4727   5014   6129   1117  -1197   -968       C  
ATOM   3836  CG  HIS C  88     -10.770  -0.638  80.292  1.00 47.03           C  
ANISOU 3836  CG  HIS C  88     5094   5699   7074   1169  -1225  -1091       C  
ATOM   3837  ND1 HIS C  88     -11.131   0.491  80.996  1.00 48.46           N  
ANISOU 3837  ND1 HIS C  88     5178   5868   7365   1251  -1142  -1151       N  
ATOM   3838  CD2 HIS C  88     -11.896  -1.380  80.167  1.00 51.81           C  
ANISOU 3838  CD2 HIS C  88     5466   6326   7894   1152  -1321  -1174       C  
ATOM   3839  CE1 HIS C  88     -12.418   0.431  81.290  1.00 51.02           C  
ANISOU 3839  CE1 HIS C  88     5212   6209   7965   1287  -1169  -1268       C  
ATOM   3840  NE2 HIS C  88     -12.905  -0.695  80.800  1.00 50.75           N  
ANISOU 3840  NE2 HIS C  88     5082   6196   8006   1223  -1280  -1280       N  
ATOM   3841  N   SER C  89      -7.261  -0.731  77.230  1.00 38.90           N  
ANISOU 3841  N   SER C  89     5046   4480   5253   1168  -1408   -759       N  
ATOM   3842  CA  SER C  89      -5.908  -0.902  76.706  1.00 36.83           C  
ANISOU 3842  CA  SER C  89     5048   4186   4760   1118  -1321   -658       C  
ATOM   3843  C   SER C  89      -5.188   0.438  76.565  1.00 35.90           C  
ANISOU 3843  C   SER C  89     5115   3995   4531   1184  -1285   -590       C  
ATOM   3844  O   SER C  89      -4.017   0.564  76.943  1.00 35.21           O  
ANISOU 3844  O   SER C  89     5123   3916   4340   1118  -1102   -519       O  
ATOM   3845  CB  SER C  89      -5.964  -1.617  75.358  1.00 31.61           C  
ANISOU 3845  CB  SER C  89     4559   3468   3985   1126  -1491   -653       C  
ATOM   3846  OG  SER C  89      -6.590  -0.808  74.364  1.00 35.14           O  
ANISOU 3846  OG  SER C  89     5130   3820   4402   1251  -1736   -661       O  
ATOM   3847  N   GLU C  90      -5.868   1.446  76.014  1.00 33.49           N  
ANISOU 3847  N   GLU C  90     4858   3606   4259   1312  -1469   -607       N  
ATOM   3848  CA  GLU C  90      -5.250   2.759  75.851  1.00 39.17           C  
ANISOU 3848  CA  GLU C  90     5763   4236   4885   1374  -1447   -538       C  
ATOM   3849  C   GLU C  90      -4.936   3.410  77.190  1.00 35.76           C  
ANISOU 3849  C   GLU C  90     5200   3847   4540   1346  -1253   -553       C  
ATOM   3850  O   GLU C  90      -3.941   4.134  77.312  1.00 35.42           O  
ANISOU 3850  O   GLU C  90     5308   3759   4393   1327  -1142   -482       O  
ATOM   3851  CB  GLU C  90      -6.157   3.669  75.022  1.00 45.85           C  
ANISOU 3851  CB  GLU C  90     6679   4969   5774   1525  -1713   -553       C  
ATOM   3852  CG  GLU C  90      -5.718   5.127  74.978  1.00 53.30           C  
ANISOU 3852  CG  GLU C  90     7783   5804   6666   1600  -1705   -490       C  
ATOM   3853  CD  GLU C  90      -6.193   5.855  73.736  1.00 64.95           C  
ANISOU 3853  CD  GLU C  90     9470   7134   8074   1725  -1981   -447       C  
ATOM   3854  OE1 GLU C  90      -7.208   5.438  73.136  1.00 66.71           O  
ANISOU 3854  OE1 GLU C  90     9633   7343   8372   1788  -2222   -498       O  
ATOM   3855  OE2 GLU C  90      -5.537   6.848  73.354  1.00 70.76           O  
ANISOU 3855  OE2 GLU C  90    10442   7760   8683   1755  -1967   -356       O  
ATOM   3856  N   THR C  91      -5.771   3.176  78.201  1.00 35.62           N  
ANISOU 3856  N   THR C  91     4912   3912   4711   1337  -1205   -650       N  
ATOM   3857  CA  THR C  91      -5.479   3.704  79.527  1.00 35.82           C  
ANISOU 3857  CA  THR C  91     4837   3983   4790   1296  -1009   -676       C  
ATOM   3858  C   THR C  91      -4.174   3.127  80.062  1.00 33.84           C  
ANISOU 3858  C   THR C  91     4662   3791   4405   1152   -814   -600       C  
ATOM   3859  O   THR C  91      -3.358   3.852  80.639  1.00 37.81           O  
ANISOU 3859  O   THR C  91     5241   4273   4853   1123   -698   -564       O  
ATOM   3860  CB  THR C  91      -6.640   3.393  80.477  1.00 33.89           C  
ANISOU 3860  CB  THR C  91     4299   3822   4756   1294   -965   -799       C  
ATOM   3861  OG1 THR C  91      -7.873   3.813  79.881  1.00 36.72           O  
ANISOU 3861  OG1 THR C  91     4553   4118   5279   1432  -1171   -872       O  
ATOM   3862  CG2 THR C  91      -6.466   4.100  81.818  1.00 30.42           C  
ANISOU 3862  CG2 THR C  91     3787   3414   4356   1266   -772   -844       C  
ATOM   3863  N   ILE C  92      -3.963   1.820  79.884  1.00 26.62           N  
ANISOU 3863  N   ILE C  92     3723   2938   3453   1063   -789   -578       N  
ATOM   3864  CA  ILE C  92      -2.717   1.198  80.337  1.00 26.26           C  
ANISOU 3864  CA  ILE C  92     3737   2933   3308    937   -626   -502       C  
ATOM   3865  C   ILE C  92      -1.536   1.775  79.566  1.00 30.45           C  
ANISOU 3865  C   ILE C  92     4504   3373   3692    947   -610   -406       C  
ATOM   3866  O   ILE C  92      -0.531   2.205  80.148  1.00 30.96           O  
ANISOU 3866  O   ILE C  92     4617   3430   3716    889   -485   -353       O  
ATOM   3867  CB  ILE C  92      -2.782  -0.335  80.183  1.00 28.32           C  
ANISOU 3867  CB  ILE C  92     3931   3254   3577    854   -620   -501       C  
ATOM   3868  CG1 ILE C  92      -3.833  -0.942  81.106  1.00 27.83           C  
ANISOU 3868  CG1 ILE C  92     3630   3281   3663    811   -592   -583       C  
ATOM   3869  CG2 ILE C  92      -1.413  -0.965  80.466  1.00 23.29           C  
ANISOU 3869  CG2 ILE C  92     3369   2629   2851    744   -479   -413       C  
ATOM   3870  CD1 ILE C  92      -3.991  -2.452  80.922  1.00 27.32           C  
ANISOU 3870  CD1 ILE C  92     3499   3257   3625    726   -602   -583       C  
ATOM   3871  N   LEU C  93      -1.650   1.792  78.236  1.00 28.05           N  
ANISOU 3871  N   LEU C  93     4356   2996   3308   1013   -737   -382       N  
ATOM   3872  CA  LEU C  93      -0.571   2.292  77.394  1.00 34.72           C  
ANISOU 3872  CA  LEU C  93     5442   3747   4003   1014   -700   -290       C  
ATOM   3873  C   LEU C  93      -0.186   3.725  77.767  1.00 40.30           C  
ANISOU 3873  C   LEU C  93     6215   4386   4709   1048   -661   -258       C  
ATOM   3874  O   LEU C  93       1.004   4.063  77.806  1.00 42.29           O  
ANISOU 3874  O   LEU C  93     6575   4599   4895    987   -535   -183       O  
ATOM   3875  CB  LEU C  93      -1.000   2.195  75.932  1.00 33.28           C  
ANISOU 3875  CB  LEU C  93     5439   3490   3716   1087   -865   -282       C  
ATOM   3876  CG  LEU C  93       0.100   2.069  74.881  1.00 37.36           C  
ANISOU 3876  CG  LEU C  93     6214   3933   4048   1052   -789   -197       C  
ATOM   3877  CD1 LEU C  93       1.279   1.296  75.419  1.00 32.42           C  
ANISOU 3877  CD1 LEU C  93     5531   3357   3430    935   -574   -161       C  
ATOM   3878  CD2 LEU C  93      -0.464   1.391  73.651  1.00 44.44           C  
ANISOU 3878  CD2 LEU C  93     7247   4797   4841   1090   -943   -222       C  
ATOM   3879  N   ASN C  94      -1.177   4.571  78.073  1.00 35.67           N  
ANISOU 3879  N   ASN C  94     5554   3778   4220   1142   -765   -322       N  
ATOM   3880  CA  ASN C  94      -0.902   5.968  78.416  1.00 38.40           C  
ANISOU 3880  CA  ASN C  94     5969   4041   4580   1184   -742   -305       C  
ATOM   3881  C   ASN C  94       0.006   6.092  79.630  1.00 34.54           C  
ANISOU 3881  C   ASN C  94     5414   3600   4110   1077   -559   -295       C  
ATOM   3882  O   ASN C  94       0.795   7.041  79.717  1.00 35.85           O  
ANISOU 3882  O   ASN C  94     5696   3685   4241   1062   -504   -244       O  
ATOM   3883  CB  ASN C  94      -2.208   6.722  78.663  1.00 37.96           C  
ANISOU 3883  CB  ASN C  94     5801   3956   4665   1310   -875   -398       C  
ATOM   3884  CG  ASN C  94      -2.965   6.998  77.384  1.00 38.84           C  
ANISOU 3884  CG  ASN C  94     6029   3972   4757   1433  -1103   -386       C  
ATOM   3885  OD1 ASN C  94      -2.398   6.939  76.298  1.00 44.61           O  
ANISOU 3885  OD1 ASN C  94     6987   4635   5327   1425  -1147   -295       O  
ATOM   3886  ND2 ASN C  94      -4.250   7.302  77.504  1.00 39.22           N  
ANISOU 3886  ND2 ASN C  94     5925   4008   4970   1546  -1249   -478       N  
ATOM   3887  N   LEU C  95      -0.080   5.142  80.567  1.00 27.82           N  
ANISOU 3887  N   LEU C  95     4388   2870   3312    994   -475   -338       N  
ATOM   3888  CA  LEU C  95       0.850   5.117  81.692  1.00 31.04           C  
ANISOU 3888  CA  LEU C  95     4755   3322   3717    879   -329   -317       C  
ATOM   3889  C   LEU C  95       2.245   4.732  81.240  1.00 31.10           C  
ANISOU 3889  C   LEU C  95     4874   3299   3642    794   -251   -209       C  
ATOM   3890  O   LEU C  95       3.218   5.432  81.537  1.00 29.49           O  
ANISOU 3890  O   LEU C  95     4740   3040   3424    745   -183   -160       O  
ATOM   3891  CB  LEU C  95       0.363   4.148  82.771  1.00 23.31           C  
ANISOU 3891  CB  LEU C  95     3588   2471   2798    808   -270   -377       C  
ATOM   3892  CG  LEU C  95      -0.472   4.800  83.871  1.00 44.03           C  
ANISOU 3892  CG  LEU C  95     6101   5127   5501    833   -240   -482       C  
ATOM   3893  CD1 LEU C  95      -1.346   3.789  84.589  1.00 41.78           C  
ANISOU 3893  CD1 LEU C  95     5635   4959   5282    787   -196   -551       C  
ATOM   3894  CD2 LEU C  95       0.422   5.533  84.863  1.00 44.46           C  
ANISOU 3894  CD2 LEU C  95     6215   5162   5515    760   -146   -468       C  
ATOM   3895  N   LEU C  96       2.361   3.604  80.533  1.00 31.22           N  
ANISOU 3895  N   LEU C  96     4897   3343   3623    772   -255   -180       N  
ATOM   3896  CA  LEU C  96       3.664   3.122  80.088  1.00 25.28           C  
ANISOU 3896  CA  LEU C  96     4226   2560   2820    697   -158    -92       C  
ATOM   3897  C   LEU C  96       4.363   4.144  79.205  1.00 24.38           C  
ANISOU 3897  C   LEU C  96     4307   2323   2634    725   -135    -25       C  
ATOM   3898  O   LEU C  96       5.593   4.147  79.113  1.00 30.53           O  
ANISOU 3898  O   LEU C  96     5132   3060   3407    651    -19     45       O  
ATOM   3899  CB  LEU C  96       3.497   1.805  79.320  1.00 27.69           C  
ANISOU 3899  CB  LEU C  96     4530   2896   3096    692   -174    -94       C  
ATOM   3900  CG  LEU C  96       2.711   0.653  79.962  1.00 21.68           C  
ANISOU 3900  CG  LEU C  96     3593   2238   2405    661   -205   -154       C  
ATOM   3901  CD1 LEU C  96       2.566  -0.502  78.970  1.00 23.74           C  
ANISOU 3901  CD1 LEU C  96     3895   2495   2629    666   -238   -160       C  
ATOM   3902  CD2 LEU C  96       3.428   0.199  81.213  1.00 20.83           C  
ANISOU 3902  CD2 LEU C  96     3369   2189   2358    553   -107   -125       C  
ATOM   3903  N   GLY C  97       3.597   4.993  78.532  1.00 27.28           N  
ANISOU 3903  N   GLY C  97     4785   2622   2958    828   -245    -42       N  
ATOM   3904  CA  GLY C  97       4.156   5.919  77.576  1.00 29.02           C  
ANISOU 3904  CA  GLY C  97     5224   2713   3089    853   -232     33       C  
ATOM   3905  C   GLY C  97       4.058   7.363  78.002  1.00 25.74           C  
ANISOU 3905  C   GLY C  97     4851   2217   2714    892   -265     33       C  
ATOM   3906  O   GLY C  97       4.160   8.255  77.155  1.00 31.82           O  
ANISOU 3906  O   GLY C  97     5816   2864   3412    939   -301     89       O  
ATOM   3907  N   ASP C  98       3.861   7.626  79.293  1.00 25.44           N  
ANISOU 3907  N   ASP C  98     4654   2233   2778    871   -252    -31       N  
ATOM   3908  CA  ASP C  98       3.741   9.015  79.710  1.00 31.53           C  
ANISOU 3908  CA  ASP C  98     5473   2914   3592    912   -282    -48       C  
ATOM   3909  C   ASP C  98       5.132   9.639  79.825  1.00 29.78           C  
ANISOU 3909  C   ASP C  98     5343   2610   3364    812   -165     34       C  
ATOM   3910  O   ASP C  98       6.156   8.971  79.661  1.00 30.76           O  
ANISOU 3910  O   ASP C  98     5462   2757   3470    715    -57     97       O  
ATOM   3911  CB  ASP C  98       2.930   9.128  81.004  1.00 31.21           C  
ANISOU 3911  CB  ASP C  98     5255   2952   3653    932   -301   -165       C  
ATOM   3912  CG  ASP C  98       3.606   8.464  82.201  1.00 36.85           C  
ANISOU 3912  CG  ASP C  98     5840   3770   4392    801   -190   -177       C  
ATOM   3913  OD1 ASP C  98       4.807   8.126  82.134  1.00 33.69           O  
ANISOU 3913  OD1 ASP C  98     5473   3362   3967    700   -109    -95       O  
ATOM   3914  OD2 ASP C  98       2.922   8.283  83.228  1.00 35.42           O  
ANISOU 3914  OD2 ASP C  98     5525   3672   4260    799   -185   -269       O  
ATOM   3915  N   ALA C  99       5.169  10.942  80.111  1.00 30.31           N  
ANISOU 3915  N   ALA C  99     5482   2570   3466    837   -188     27       N  
ATOM   3916  CA  ALA C  99       6.433  11.676  80.076  1.00 30.20           C  
ANISOU 3916  CA  ALA C  99     5567   2449   3458    743    -93    109       C  
ATOM   3917  C   ALA C  99       7.458  11.089  81.044  1.00 28.02           C  
ANISOU 3917  C   ALA C  99     5152   2251   3244    602     10    113       C  
ATOM   3918  O   ALA C  99       8.632  10.925  80.694  1.00 25.64           O  
ANISOU 3918  O   ALA C  99     4878   1910   2953    507    112    198       O  
ATOM   3919  CB  ALA C  99       6.185  13.151  80.392  1.00 31.26           C  
ANISOU 3919  CB  ALA C  99     5786   2452   3641    792   -151     81       C  
ATOM   3920  N   ARG C 100       7.039  10.780  82.269  1.00 25.00           N  
ANISOU 3920  N   ARG C 100     4620   1972   2908    585    -17     23       N  
ATOM   3921  CA  ARG C 100       7.977  10.220  83.236  1.00 24.26           C  
ANISOU 3921  CA  ARG C 100     4411   1944   2862    453     43     34       C  
ATOM   3922  C   ARG C 100       8.618   8.931  82.716  1.00 26.15           C  
ANISOU 3922  C   ARG C 100     4591   2246   3098    399    109    104       C  
ATOM   3923  O   ARG C 100       9.841   8.765  82.795  1.00 23.93           O  
ANISOU 3923  O   ARG C 100     4279   1934   2877    297    179    171       O  
ATOM   3924  CB  ARG C 100       7.259   9.980  84.562  1.00 27.77           C  
ANISOU 3924  CB  ARG C 100     4741   2495   3315    447      4    -73       C  
ATOM   3925  CG  ARG C 100       8.004   9.104  85.541  1.00 26.66           C  
ANISOU 3925  CG  ARG C 100     4489   2444   3196    320     31    -56       C  
ATOM   3926  CD  ARG C 100       7.090   8.755  86.705  1.00 27.22           C  
ANISOU 3926  CD  ARG C 100     4480   2626   3236    321      9   -158       C  
ATOM   3927  NE  ARG C 100       7.756   7.926  87.698  1.00 25.41           N  
ANISOU 3927  NE  ARG C 100     4176   2474   3006    196     12   -133       N  
ATOM   3928  CZ  ARG C 100       7.207   7.542  88.845  1.00 25.02           C  
ANISOU 3928  CZ  ARG C 100     4082   2518   2907    156      8   -201       C  
ATOM   3929  NH1 ARG C 100       5.970   7.912  89.154  1.00 29.97           N  
ANISOU 3929  NH1 ARG C 100     4707   3178   3502    233     26   -312       N  
ATOM   3930  NH2 ARG C 100       7.897   6.786  89.684  1.00 27.51           N  
ANISOU 3930  NH2 ARG C 100     4357   2886   3211     38    -12   -156       N  
ATOM   3931  N   ARG C 101       7.816   8.023  82.147  1.00 25.90           N  
ANISOU 3931  N   ARG C 101     4538   2289   3015    468     84     85       N  
ATOM   3932  CA  ARG C 101       8.373   6.764  81.648  1.00 25.80           C  
ANISOU 3932  CA  ARG C 101     4476   2324   3002    424    149    137       C  
ATOM   3933  C   ARG C 101       9.233   6.984  80.403  1.00 30.88           C  
ANISOU 3933  C   ARG C 101     5253   2861   3619    412    243    223       C  
ATOM   3934  O   ARG C 101      10.284   6.346  80.241  1.00 23.14           O  
ANISOU 3934  O   ARG C 101     4222   1875   2694    336    347    277       O  
ATOM   3935  CB  ARG C 101       7.249   5.770  81.363  1.00 25.94           C  
ANISOU 3935  CB  ARG C 101     4446   2435   2974    494     90     84       C  
ATOM   3936  CG  ARG C 101       7.197   4.599  82.360  1.00 28.87           C  
ANISOU 3936  CG  ARG C 101     4649   2926   3394    429     91     57       C  
ATOM   3937  CD  ARG C 101       6.981   5.071  83.787  1.00 21.21           C  
ANISOU 3937  CD  ARG C 101     3605   1999   2454    386     62      5       C  
ATOM   3938  NE  ARG C 101       5.678   5.707  83.950  1.00 21.68           N  
ANISOU 3938  NE  ARG C 101     3673   2074   2491    479      1    -87       N  
ATOM   3939  CZ  ARG C 101       5.028   5.805  85.106  1.00 27.91           C  
ANISOU 3939  CZ  ARG C 101     4384   2930   3290    464     -8   -166       C  
ATOM   3940  NH1 ARG C 101       5.557   5.293  86.209  1.00 21.40           N  
ANISOU 3940  NH1 ARG C 101     3497   2166   2468    353     22   -155       N  
ATOM   3941  NH2 ARG C 101       3.854   6.423  85.161  1.00 28.68           N  
ANISOU 3941  NH2 ARG C 101     4473   3026   3399    560    -46   -258       N  
ATOM   3942  N   THR C 102       8.815   7.891  79.521  1.00 27.06           N  
ANISOU 3942  N   THR C 102     4943   2283   3055    487    215    239       N  
ATOM   3943  CA  THR C 102       9.593   8.152  78.312  1.00 34.10           C  
ANISOU 3943  CA  THR C 102     5999   3066   3890    466    324    326       C  
ATOM   3944  C   THR C 102      10.990   8.661  78.651  1.00 35.02           C  
ANISOU 3944  C   THR C 102     6082   3108   4116    347    449    389       C  
ATOM   3945  O   THR C 102      11.986   8.198  78.084  1.00 39.01           O  
ANISOU 3945  O   THR C 102     6589   3582   4653    281    596    447       O  
ATOM   3946  CB  THR C 102       8.847   9.144  77.424  1.00 41.38           C  
ANISOU 3946  CB  THR C 102     7137   3888   4700    562    243    343       C  
ATOM   3947  OG1 THR C 102       7.589   8.566  77.056  1.00 43.45           O  
ANISOU 3947  OG1 THR C 102     7407   4217   4886    669    110    284       O  
ATOM   3948  CG2 THR C 102       9.658   9.466  76.162  1.00 37.43           C  
ANISOU 3948  CG2 THR C 102     6848   3264   4108    526    373    444       C  
ATOM   3949  N   ARG C 103      11.088   9.612  79.581  1.00 34.26           N  
ANISOU 3949  N   ARG C 103     5947   2976   4095    317    395    370       N  
ATOM   3950  CA  ARG C 103      12.402  10.048  80.047  1.00 28.76           C  
ANISOU 3950  CA  ARG C 103     5187   2211   3531    192    482    418       C  
ATOM   3951  C   ARG C 103      13.165   8.899  80.701  1.00 28.24           C  
ANISOU 3951  C   ARG C 103     4917   2235   3579    110    521    419       C  
ATOM   3952  O   ARG C 103      14.353   8.689  80.428  1.00 28.14           O  
ANISOU 3952  O   ARG C 103     4846   2170   3675     24    644    481       O  
ATOM   3953  CB  ARG C 103      12.249  11.200  81.030  1.00 26.27           C  
ANISOU 3953  CB  ARG C 103     4873   1846   3264    175    387    375       C  
ATOM   3954  CG  ARG C 103      11.782  12.503  80.404  1.00 34.80           C  
ANISOU 3954  CG  ARG C 103     6154   2791   4280    240    357    392       C  
ATOM   3955  CD  ARG C 103      12.889  13.159  79.591  1.00 35.82           C  
ANISOU 3955  CD  ARG C 103     6395   2770   4445    156    493    499       C  
ATOM   3956  NE  ARG C 103      12.600  14.572  79.359  1.00 45.37           N  
ANISOU 3956  NE  ARG C 103     7781   3827   5629    188    445    516       N  
ATOM   3957  CZ  ARG C 103      13.348  15.381  78.616  1.00 46.80           C  
ANISOU 3957  CZ  ARG C 103     8108   3850   5825    123    550    613       C  
ATOM   3958  NH1 ARG C 103      14.436  14.913  78.019  1.00 45.76           N  
ANISOU 3958  NH1 ARG C 103     7953   3699   5735     21    731    693       N  
ATOM   3959  NH2 ARG C 103      13.006  16.653  78.465  1.00 44.58           N  
ANISOU 3959  NH2 ARG C 103     7993   3421   5525    159    486    629       N  
ATOM   3960  N   PHE C 104      12.489   8.159  81.585  1.00 25.76           N  
ANISOU 3960  N   PHE C 104     4488   2047   3255    134    417    353       N  
ATOM   3961  CA  PHE C 104      13.114   7.054  82.306  1.00 27.96           C  
ANISOU 3961  CA  PHE C 104     4586   2403   3635     61    419    361       C  
ATOM   3962  C   PHE C 104      13.763   6.056  81.352  1.00 28.17           C  
ANISOU 3962  C   PHE C 104     4581   2420   3702     53    549    412       C  
ATOM   3963  O   PHE C 104      14.940   5.717  81.504  1.00 24.05           O  
ANISOU 3963  O   PHE C 104     3942   1863   3333    -29    620    459       O  
ATOM   3964  CB  PHE C 104      12.066   6.365  83.177  1.00 24.01           C  
ANISOU 3964  CB  PHE C 104     4016   2033   3075     99    306    289       C  
ATOM   3965  CG  PHE C 104      12.610   5.294  84.072  1.00 25.14           C  
ANISOU 3965  CG  PHE C 104     3999   2247   3306     22    276    304       C  
ATOM   3966  CD1 PHE C 104      13.131   5.611  85.313  1.00 22.28           C  
ANISOU 3966  CD1 PHE C 104     3571   1885   3008    -68    198    302       C  
ATOM   3967  CD2 PHE C 104      12.561   3.957  83.688  1.00 23.26           C  
ANISOU 3967  CD2 PHE C 104     3692   2065   3080     39    309    318       C  
ATOM   3968  CE1 PHE C 104      13.613   4.629  86.152  1.00 35.16           C  
ANISOU 3968  CE1 PHE C 104     5077   3572   4712   -139    140    328       C  
ATOM   3969  CE2 PHE C 104      13.040   2.958  84.533  1.00 21.29           C  
ANISOU 3969  CE2 PHE C 104     3305   1866   2920    -27    263    342       C  
ATOM   3970  CZ  PHE C 104      13.566   3.294  85.766  1.00 26.45           C  
ANISOU 3970  CZ  PHE C 104     3899   2518   3633   -116    173    353       C  
ATOM   3971  N   PHE C 105      13.020   5.574  80.357  1.00 27.21           N  
ANISOU 3971  N   PHE C 105     4562   2322   3455    140    577    396       N  
ATOM   3972  CA  PHE C 105      13.629   4.591  79.468  1.00 31.22           C  
ANISOU 3972  CA  PHE C 105     5057   2816   3990    132    713    426       C  
ATOM   3973  C   PHE C 105      14.501   5.242  78.401  1.00 34.61           C  
ANISOU 3973  C   PHE C 105     5607   3119   4423    101    888    488       C  
ATOM   3974  O   PHE C 105      15.430   4.595  77.901  1.00 34.51           O  
ANISOU 3974  O   PHE C 105     5539   3072   4502     59   1045    516       O  
ATOM   3975  CB  PHE C 105      12.556   3.692  78.851  1.00 26.35           C  
ANISOU 3975  CB  PHE C 105     4504   2269   3238    222    670    377       C  
ATOM   3976  CG  PHE C 105      11.953   2.735  79.849  1.00 23.93           C  
ANISOU 3976  CG  PHE C 105     4044   2080   2968    225    552    329       C  
ATOM   3977  CD1 PHE C 105      12.664   1.623  80.279  1.00 30.80           C  
ANISOU 3977  CD1 PHE C 105     4758   2976   3968    171    587    347       C  
ATOM   3978  CD2 PHE C 105      10.700   2.973  80.389  1.00 22.81           C  
ANISOU 3978  CD2 PHE C 105     3910   2009   2747    277    413    270       C  
ATOM   3979  CE1 PHE C 105      12.121   0.745  81.215  1.00 26.49           C  
ANISOU 3979  CE1 PHE C 105     4093   2525   3445    161    480    318       C  
ATOM   3980  CE2 PHE C 105      10.154   2.108  81.313  1.00 20.88           C  
ANISOU 3980  CE2 PHE C 105     3536   1867   2532    264    332    231       C  
ATOM   3981  CZ  PHE C 105      10.867   0.992  81.728  1.00 31.78           C  
ANISOU 3981  CZ  PHE C 105     4786   3271   4016    201    363    262       C  
ATOM   3982  N   GLY C 106      14.254   6.513  78.083  1.00 33.08           N  
ANISOU 3982  N   GLY C 106     5576   2847   4147    114    874    510       N  
ATOM   3983  CA  GLY C 106      15.201   7.261  77.275  1.00 29.28           C  
ANISOU 3983  CA  GLY C 106     5202   2234   3691     54   1048    582       C  
ATOM   3984  C   GLY C 106      16.580   7.302  77.904  1.00 34.07           C  
ANISOU 3984  C   GLY C 106     5610   2795   4539    -67   1139    618       C  
ATOM   3985  O   GLY C 106      17.588   7.043  77.242  1.00 39.42           O  
ANISOU 3985  O   GLY C 106     6260   3406   5310   -125   1341    661       O  
ATOM   3986  N   ASP C 107      16.645   7.629  79.196  1.00 32.50           N  
ANISOU 3986  N   ASP C 107     5271   2628   4451   -108    992    596       N  
ATOM   3987  CA  ASP C 107      17.923   7.567  79.898  1.00 34.91           C  
ANISOU 3987  CA  ASP C 107     5367   2895   5002   -223   1025    627       C  
ATOM   3988  C   ASP C 107      18.431   6.134  80.021  1.00 38.33           C  
ANISOU 3988  C   ASP C 107     5612   3391   5561   -230   1065    622       C  
ATOM   3989  O   ASP C 107      19.644   5.898  80.042  1.00 45.58           O  
ANISOU 3989  O   ASP C 107     6367   4247   6702   -308   1169    659       O  
ATOM   3990  CB  ASP C 107      17.783   8.186  81.282  1.00 36.27           C  
ANISOU 3990  CB  ASP C 107     5467   3089   5225   -265    828    595       C  
ATOM   3991  CG  ASP C 107      17.519   9.676  81.224  1.00 42.51           C  
ANISOU 3991  CG  ASP C 107     6419   3782   5949   -273    800    598       C  
ATOM   3992  OD1 ASP C 107      17.496  10.241  80.111  1.00 38.42           O  
ANISOU 3992  OD1 ASP C 107     6069   3175   5352   -251    928    641       O  
ATOM   3993  OD2 ASP C 107      17.333  10.274  82.299  1.00 42.10           O  
ANISOU 3993  OD2 ASP C 107     6342   3736   5917   -301    649    556       O  
HETATM 3994  N   MSE C 108      17.527   5.179  80.112  1.00 26.22           N  
ANISOU 3994  N   MSE C 108     4085   1966   3911   -149    983    576       N  
HETATM 3995  CA  MSE C 108      17.878   3.777  80.321  1.00 33.87           C  
ANISOU 3995  CA  MSE C 108     4886   2989   4996   -148    991    569       C  
HETATM 3996  C   MSE C 108      18.543   3.207  79.077  1.00 32.74           C  
ANISOU 3996  C   MSE C 108     4758   2780   4901   -138   1227    585       C  
HETATM 3997  O   MSE C 108      19.505   2.441  79.164  1.00 32.47           O  
ANISOU 3997  O   MSE C 108     4540   2716   5080   -175   1308    600       O  
HETATM 3998  CB  MSE C 108      16.620   2.998  80.696  1.00 30.58           C  
ANISOU 3998  CB  MSE C 108     4498   2694   4427    -71    847    514       C  
HETATM 3999  CG  MSE C 108      16.707   1.505  80.587  1.00 42.85           C  
ANISOU 3999  CG  MSE C 108     5946   4292   6043    -47    871    502       C  
HETATM 4000 SE   MSE C 108      17.314   0.697  82.255  1.00 45.35          SE  
ANISOU 4000 SE   MSE C 108     6008   4652   6573   -122    694    530      SE  
HETATM 4001  CE  MSE C 108      16.139   1.511  83.594  1.00 23.54           C  
ANISOU 4001  CE  MSE C 108     3324   1987   3634   -134    469    493       C  
ATOM   4002  N   PHE C 109      18.036   3.606  77.915  1.00 27.38           N  
ANISOU 4002  N   PHE C 109     4309   2070   4024    -89   1338    580       N  
ATOM   4003  CA  PHE C 109      18.570   3.130  76.647  1.00 31.49           C  
ANISOU 4003  CA  PHE C 109     4905   2526   4534    -82   1583    586       C  
ATOM   4004  C   PHE C 109      19.780   3.915  76.173  1.00 40.34           C  
ANISOU 4004  C   PHE C 109     6015   3520   5794   -172   1801    643       C  
ATOM   4005  O   PHE C 109      20.544   3.405  75.348  1.00 45.47           O  
ANISOU 4005  O   PHE C 109     6648   4108   6520   -191   2043    644       O  
ATOM   4006  CB  PHE C 109      17.482   3.170  75.569  1.00 32.10           C  
ANISOU 4006  CB  PHE C 109     5268   2618   4310      4   1591    558       C  
ATOM   4007  CG  PHE C 109      16.285   2.334  75.902  1.00 27.15           C  
ANISOU 4007  CG  PHE C 109     4640   2107   3568     88   1398    495       C  
ATOM   4008  CD1 PHE C 109      16.399   1.277  76.787  1.00 30.98           C  
ANISOU 4008  CD1 PHE C 109     4903   2662   4205     82   1314    469       C  
ATOM   4009  CD2 PHE C 109      15.050   2.614  75.352  1.00 32.51           C  
ANISOU 4009  CD2 PHE C 109     5533   2815   4003    167   1291    467       C  
ATOM   4010  CE1 PHE C 109      15.298   0.505  77.120  1.00 30.23           C  
ANISOU 4010  CE1 PHE C 109     4804   2667   4016    143   1151    416       C  
ATOM   4011  CE2 PHE C 109      13.935   1.839  75.676  1.00 29.19           C  
ANISOU 4011  CE2 PHE C 109     5085   2497   3509    234   1116    405       C  
ATOM   4012  CZ  PHE C 109      14.068   0.788  76.564  1.00 28.55           C  
ANISOU 4012  CZ  PHE C 109     4784   2487   3577    216   1060    380       C  
ATOM   4013  N   GLY C 110      19.967   5.137  76.660  1.00 35.46           N  
ANISOU 4013  N   GLY C 110     5404   2851   5216   -233   1737    685       N  
ATOM   4014  CA  GLY C 110      21.122   5.916  76.275  1.00 41.96           C  
ANISOU 4014  CA  GLY C 110     6200   3545   6198   -336   1940    743       C  
ATOM   4015  C   GLY C 110      21.075   6.510  74.886  1.00 52.51           C  
ANISOU 4015  C   GLY C 110     7818   4790   7342   -339   2163    780       C  
ATOM   4016  O   GLY C 110      22.130   6.692  74.269  1.00 50.81           O  
ANISOU 4016  O   GLY C 110     7553   4510   7244   -406   2387    794       O  
ATOM   4017  N   THR C 111      19.885   6.803  74.357  1.00 56.89           N  
ANISOU 4017  N   THR C 111     8650   5374   7591   -253   2066    771       N  
ATOM   4018  CA  THR C 111      19.779   7.572  73.124  1.00 64.83           C  
ANISOU 4018  CA  THR C 111     9951   6298   8383   -255   2206    811       C  
ATOM   4019  C   THR C 111      18.738   8.665  73.287  1.00 55.87           C  
ANISOU 4019  C   THR C 111     9016   5147   7066   -206   1992    835       C  
ATOM   4020  O   THR C 111      17.793   8.542  74.073  1.00 51.49           O  
ANISOU 4020  O   THR C 111     8421   4672   6473   -132   1751    794       O  
ATOM   4021  CB  THR C 111      19.394   6.735  71.881  1.00 74.28           C  
ANISOU 4021  CB  THR C 111    11359   7513   9352   -189   2338    779       C  
ATOM   4022  OG1 THR C 111      17.974   6.545  71.847  1.00 75.43           O  
ANISOU 4022  OG1 THR C 111    11679   7720   9260    -78   2112    754       O  
ATOM   4023  CG2 THR C 111      20.101   5.386  71.867  1.00 77.27           C  
ANISOU 4023  CG2 THR C 111    11539   7914   9903   -201   2509    733       C  
ATOM   4024  N   ARG C 112      18.929   9.737  72.528  1.00 52.15           N  
ANISOU 4024  N   ARG C 112     8719   4604   6492   -238   2056    874       N  
ATOM   4025  CA  ARG C 112      17.923  10.778  72.405  1.00 51.88           C  
ANISOU 4025  CA  ARG C 112     8906   4536   6269   -176   1867    896       C  
ATOM   4026  C   ARG C 112      16.862  10.423  71.376  1.00 50.25           C  
ANISOU 4026  C   ARG C 112     8975   4354   5764    -68   1807    882       C  
ATOM   4027  O   ARG C 112      15.864  11.142  71.259  1.00 54.96           O  
ANISOU 4027  O   ARG C 112     9744   4930   6210      8   1612    891       O  
ATOM   4028  CB  ARG C 112      18.592  12.107  72.040  1.00 47.74           C  
ANISOU 4028  CB  ARG C 112     8452   3910   5776   -262   1946    953       C  
ATOM   4029  N   ALA C 113      17.048   9.324  70.649  1.00 47.90           N  
ANISOU 4029  N   ALA C 113     8716   4092   5392    -56   1956    851       N  
ATOM   4030  CA  ALA C 113      16.126   8.946  69.590  1.00 46.28           C  
ANISOU 4030  CA  ALA C 113     8788   3900   4897     33   1895    829       C  
ATOM   4031  C   ALA C 113      14.748   8.607  70.148  1.00 41.70           C  
ANISOU 4031  C   ALA C 113     8224   3385   4235    152   1611    798       C  
ATOM   4032  O   ALA C 113      14.597   8.163  71.288  1.00 34.74           O  
ANISOU 4032  O   ALA C 113     7099   2579   3523    167   1510    760       O  
ATOM   4033  CB  ALA C 113      16.676   7.758  68.803  1.00 38.22           C  
ANISOU 4033  CB  ALA C 113     7788   2897   3836     14   2123    784       C  
ATOM   4034  N   GLU C 114      13.733   8.829  69.323  1.00 38.52           N  
ANISOU 4034  N   GLU C 114     8077   2972   3589    238   1455    792       N  
ATOM   4035  CA  GLU C 114      12.373   8.489  69.704  1.00 39.72           C  
ANISOU 4035  CA  GLU C 114     8242   3181   3667    361   1178    753       C  
ATOM   4036  C   GLU C 114      12.180   6.973  69.684  1.00 33.96           C  
ANISOU 4036  C   GLU C 114     7399   2567   2937    388   1189    666       C  
ATOM   4037  O   GLU C 114      12.567   6.296  68.724  1.00 35.11           O  
ANISOU 4037  O   GLU C 114     7697   2690   2954    362   1356    661       O  
ATOM   4038  CB  GLU C 114      11.399   9.174  68.749  1.00 46.97           C  
ANISOU 4038  CB  GLU C 114     9431   4056   4361    440    987    759       C  
ATOM   4039  CG  GLU C 114       9.944   8.956  69.075  1.00 53.33           C  
ANISOU 4039  CG  GLU C 114    10230   4912   5121    574    678    712       C  
ATOM   4040  CD  GLU C 114       9.029   9.839  68.248  1.00 59.86           C  
ANISOU 4040  CD  GLU C 114    11278   5676   5789    649    464    722       C  
ATOM   4041  OE1 GLU C 114       9.504  10.467  67.271  1.00 55.12           O  
ANISOU 4041  OE1 GLU C 114    10884   4993   5066    593    562    769       O  
ATOM   4042  OE2 GLU C 114       7.830   9.906  68.588  1.00 65.08           O  
ANISOU 4042  OE2 GLU C 114    11895   6365   6466    763    196    682       O  
ATOM   4043  N   TYR C 115      11.584   6.435  70.740  1.00 32.01           N  
ANISOU 4043  N   TYR C 115     6887   2443   2833    434   1018    588       N  
ATOM   4044  CA  TYR C 115      11.284   5.010  70.826  1.00 36.91           C  
ANISOU 4044  CA  TYR C 115     7377   3174   3474    460    992    501       C  
ATOM   4045  C   TYR C 115       9.777   4.803  70.893  1.00 38.93           C  
ANISOU 4045  C   TYR C 115     7648   3497   3644    569    705    437       C  
ATOM   4046  O   TYR C 115       9.060   5.605  71.498  1.00 40.52           O  
ANISOU 4046  O   TYR C 115     7799   3706   3890    621    527    436       O  
ATOM   4047  CB  TYR C 115      11.952   4.370  72.047  1.00 34.38           C  
ANISOU 4047  CB  TYR C 115     6713   2936   3414    403   1055    469       C  
ATOM   4048  CG  TYR C 115      13.375   3.899  71.814  1.00 35.96           C  
ANISOU 4048  CG  TYR C 115     6845   3091   3728    310   1337    495       C  
ATOM   4049  CD1 TYR C 115      13.657   2.560  71.617  1.00 38.74           C  
ANISOU 4049  CD1 TYR C 115     7109   3485   4124    307   1431    438       C  
ATOM   4050  CD2 TYR C 115      14.434   4.798  71.797  1.00 35.95           C  
ANISOU 4050  CD2 TYR C 115     6852   2993   3815    225   1511    571       C  
ATOM   4051  CE1 TYR C 115      14.961   2.120  71.413  1.00 38.82           C  
ANISOU 4051  CE1 TYR C 115     7031   3444   4275    234   1697    451       C  
ATOM   4052  CE2 TYR C 115      15.734   4.373  71.594  1.00 35.99           C  
ANISOU 4052  CE2 TYR C 115     6759   2951   3965    142   1777    588       C  
ATOM   4053  CZ  TYR C 115      15.997   3.035  71.405  1.00 34.27           C  
ANISOU 4053  CZ  TYR C 115     6442   2776   3801    152   1872    525       C  
ATOM   4054  OH  TYR C 115      17.298   2.611  71.195  1.00 35.07           O  
ANISOU 4054  OH  TYR C 115     6425   2820   4080     80   2146    533       O  
ATOM   4055  N   PHE C 116       9.298   3.725  70.274  1.00 32.80           N  
ANISOU 4055  N   PHE C 116     6934   2764   2764    604    664    375       N  
ATOM   4056  CA  PHE C 116       7.875   3.422  70.218  1.00 33.06           C  
ANISOU 4056  CA  PHE C 116     6974   2854   2732    699    391    309       C  
ATOM   4057  C   PHE C 116       7.589   2.075  70.870  1.00 34.37           C  
ANISOU 4057  C   PHE C 116     6893   3139   3027    693    357    220       C  
ATOM   4058  O   PHE C 116       8.315   1.099  70.649  1.00 34.92           O  
ANISOU 4058  O   PHE C 116     6932   3216   3118    642    524    199       O  
ATOM   4059  CB  PHE C 116       7.367   3.391  68.774  1.00 32.46           C  
ANISOU 4059  CB  PHE C 116     7242   2703   2388    745    313    314       C  
ATOM   4060  CG  PHE C 116       7.707   4.622  67.975  1.00 34.25           C  
ANISOU 4060  CG  PHE C 116     7770   2794   2449    738    362    418       C  
ATOM   4061  CD1 PHE C 116       6.807   5.669  67.876  1.00 34.97           C  
ANISOU 4061  CD1 PHE C 116     7975   2828   2485    820    125    455       C  
ATOM   4062  CD2 PHE C 116       8.917   4.724  67.316  1.00 37.41           C  
ANISOU 4062  CD2 PHE C 116     8339   3113   2763    649    652    480       C  
ATOM   4063  CE1 PHE C 116       7.106   6.803  67.135  1.00 38.23           C  
ANISOU 4063  CE1 PHE C 116     8662   3108   2757    807    159    552       C  
ATOM   4064  CE2 PHE C 116       9.223   5.861  66.572  1.00 42.28           C  
ANISOU 4064  CE2 PHE C 116     9215   3605   3242    625    705    569       C  
ATOM   4065  CZ  PHE C 116       8.313   6.900  66.487  1.00 37.94           C  
ANISOU 4065  CZ  PHE C 116     8745   3014   2656    698    448    590       C  
ATOM   4066  N   ILE C 117       6.524   2.023  71.666  1.00 28.10           N  
ANISOU 4066  N   ILE C 117     5922   2426   2328    746    151    167       N  
ATOM   4067  CA  ILE C 117       6.020   0.752  72.186  1.00 33.24           C  
ANISOU 4067  CA  ILE C 117     6371   3179   3078    742     89     85       C  
ATOM   4068  C   ILE C 117       5.242   0.097  71.048  1.00 32.60           C  
ANISOU 4068  C   ILE C 117     6473   3079   2836    790    -37     31       C  
ATOM   4069  O   ILE C 117       4.178   0.579  70.659  1.00 37.93           O  
ANISOU 4069  O   ILE C 117     7239   3736   3436    867   -254     14       O  
ATOM   4070  CB  ILE C 117       5.140   0.943  73.432  1.00 25.91           C  
ANISOU 4070  CB  ILE C 117     5199   2341   2306    768    -58     45       C  
ATOM   4071  CG1 ILE C 117       5.916   1.612  74.569  1.00 33.43           C  
ANISOU 4071  CG1 ILE C 117     6004   3305   3391    712     51     90       C  
ATOM   4072  CG2 ILE C 117       4.582  -0.394  73.913  1.00 25.12           C  
ANISOU 4072  CG2 ILE C 117     4911   2337   2299    750   -113    -30       C  
ATOM   4073  CD1 ILE C 117       5.071   1.911  75.817  1.00 31.57           C  
ANISOU 4073  CD1 ILE C 117     5564   3151   3281    733    -67     43       C  
ATOM   4074  N   ARG C 118       5.784  -0.985  70.494  1.00 33.37           N  
ANISOU 4074  N   ARG C 118     6626   3166   2886    749     89      1       N  
ATOM   4075  CA  ARG C 118       5.170  -1.620  69.333  1.00 34.23           C  
ANISOU 4075  CA  ARG C 118     6950   3240   2815    782    -19    -57       C  
ATOM   4076  C   ARG C 118       4.222  -2.746  69.700  1.00 36.27           C  
ANISOU 4076  C   ARG C 118     7031   3577   3173    793   -182   -152       C  
ATOM   4077  O   ARG C 118       3.325  -3.068  68.914  1.00 39.29           O  
ANISOU 4077  O   ARG C 118     7551   3940   3438    835   -371   -209       O  
ATOM   4078  CB  ARG C 118       6.239  -2.178  68.391  1.00 31.76           C  
ANISOU 4078  CB  ARG C 118     6839   2856   2374    732    220    -57       C  
ATOM   4079  CG  ARG C 118       7.040  -1.134  67.644  1.00 32.52           C  
ANISOU 4079  CG  ARG C 118     7195   2852   2311    715    381     31       C  
ATOM   4080  CD  ARG C 118       7.844  -1.779  66.540  1.00 39.17           C  
ANISOU 4080  CD  ARG C 118     8274   3619   2989    672    607      5       C  
ATOM   4081  NE  ARG C 118       7.009  -2.461  65.562  1.00 35.57           N  
ANISOU 4081  NE  ARG C 118     8045   3142   2326    708    446    -75       N  
ATOM   4082  CZ  ARG C 118       6.697  -1.965  64.366  1.00 44.04           C  
ANISOU 4082  CZ  ARG C 118     9499   4130   3104    729    373    -55       C  
ATOM   4083  NH1 ARG C 118       7.151  -0.770  63.991  1.00 40.83           N  
ANISOU 4083  NH1 ARG C 118     9287   3647   2581    716    463     52       N  
ATOM   4084  NH2 ARG C 118       5.934  -2.668  63.538  1.00 42.55           N  
ANISOU 4084  NH2 ARG C 118     9491   3923   2753    753    198   -137       N  
ATOM   4085  N   ARG C 119       4.412  -3.369  70.856  1.00 35.82           N  
ANISOU 4085  N   ARG C 119     6684   3599   3327    749   -119   -166       N  
ATOM   4086  CA  ARG C 119       3.628  -4.535  71.230  1.00 34.09           C  
ANISOU 4086  CA  ARG C 119     6297   3443   3212    738   -235   -247       C  
ATOM   4087  C   ARG C 119       3.563  -4.575  72.744  1.00 31.32           C  
ANISOU 4087  C   ARG C 119     5639   3184   3078    702   -219   -230       C  
ATOM   4088  O   ARG C 119       4.519  -4.200  73.417  1.00 39.38           O  
ANISOU 4088  O   ARG C 119     6581   4208   4173    663    -64   -166       O  
ATOM   4089  CB  ARG C 119       4.239  -5.825  70.655  1.00 33.31           C  
ANISOU 4089  CB  ARG C 119     6266   3306   3085    695   -109   -294       C  
ATOM   4090  CG  ARG C 119       3.585  -7.126  71.134  1.00 34.16           C  
ANISOU 4090  CG  ARG C 119     6188   3464   3328    666   -202   -369       C  
ATOM   4091  CD  ARG C 119       4.101  -8.336  70.352  1.00 38.85           C  
ANISOU 4091  CD  ARG C 119     6900   3990   3870    638    -99   -431       C  
ATOM   4092  NE  ARG C 119       3.673  -9.607  70.931  1.00 35.02           N  
ANISOU 4092  NE  ARG C 119     6224   3537   3546    597   -157   -487       N  
ATOM   4093  CZ  ARG C 119       3.780 -10.785  70.316  1.00 35.65           C  
ANISOU 4093  CZ  ARG C 119     6384   3555   3606    577   -130   -565       C  
ATOM   4094  NH1 ARG C 119       4.295 -10.862  69.095  1.00 31.14           N  
ANISOU 4094  NH1 ARG C 119     6089   2895   2848    597    -35   -607       N  
ATOM   4095  NH2 ARG C 119       3.366 -11.894  70.924  1.00 32.90           N  
ANISOU 4095  NH2 ARG C 119     5853   3227   3422    533   -190   -605       N  
ATOM   4096  N   CYS C 120       2.421  -5.006  73.273  1.00 28.80           N  
ANISOU 4096  N   CYS C 120     5154   2931   2857    710   -380   -288       N  
ATOM   4097  CA  CYS C 120       2.170  -4.970  74.707  1.00 24.27           C  
ANISOU 4097  CA  CYS C 120     4319   2444   2457    673   -372   -277       C  
ATOM   4098  C   CYS C 120       1.067  -5.962  75.054  1.00 28.82           C  
ANISOU 4098  C   CYS C 120     4734   3078   3140    652   -495   -351       C  
ATOM   4099  O   CYS C 120       0.013  -5.963  74.407  1.00 28.94           O  
ANISOU 4099  O   CYS C 120     4789   3083   3125    702   -674   -414       O  
ATOM   4100  CB  CYS C 120       1.770  -3.560  75.142  1.00 24.21           C  
ANISOU 4100  CB  CYS C 120     4291   2452   2457    726   -430   -254       C  
ATOM   4101  SG  CYS C 120       1.357  -3.457  76.910  1.00 29.07           S  
ANISOU 4101  SG  CYS C 120     4619   3173   3253    679   -408   -262       S  
ATOM   4102  N   GLN C 121       1.303  -6.791  76.074  1.00 29.55           N  
ANISOU 4102  N   GLN C 121     4644   3221   3362    573   -412   -339       N  
ATOM   4103  CA  GLN C 121       0.318  -7.780  76.497  1.00 27.38           C  
ANISOU 4103  CA  GLN C 121     4209   2994   3201    531   -500   -398       C  
ATOM   4104  C   GLN C 121       0.614  -8.264  77.913  1.00 27.21           C  
ANISOU 4104  C   GLN C 121     3999   3033   3306    441   -395   -353       C  
ATOM   4105  O   GLN C 121       1.755  -8.220  78.380  1.00 29.42           O  
ANISOU 4105  O   GLN C 121     4288   3301   3589    405   -267   -280       O  
ATOM   4106  CB  GLN C 121       0.300  -8.971  75.540  1.00 29.05           C  
ANISOU 4106  CB  GLN C 121     4514   3145   3379    516   -540   -450       C  
ATOM   4107  CG  GLN C 121       1.564  -9.790  75.654  1.00 29.66           C  
ANISOU 4107  CG  GLN C 121     4616   3179   3476    462   -372   -404       C  
ATOM   4108  CD  GLN C 121       1.737 -10.739  74.511  1.00 34.77           C  
ANISOU 4108  CD  GLN C 121     5415   3741   4055    467   -381   -465       C  
ATOM   4109  OE1 GLN C 121       1.915 -10.322  73.368  1.00 44.00           O  
ANISOU 4109  OE1 GLN C 121     6801   4851   5064    523   -392   -490       O  
ATOM   4110  NE2 GLN C 121       1.685 -12.033  74.806  1.00 29.58           N  
ANISOU 4110  NE2 GLN C 121     4663   3067   3510    405   -372   -490       N  
ATOM   4111  N   ILE C 122      -0.440  -8.751  78.580  1.00 28.38           N  
ANISOU 4111  N   ILE C 122     3979   3241   3563    398   -457   -395       N  
ATOM   4112  CA  ILE C 122      -0.340  -9.436  79.873  1.00 27.34           C  
ANISOU 4112  CA  ILE C 122     3694   3161   3535    295   -372   -354       C  
ATOM   4113  C   ILE C 122      -0.247 -10.943  79.634  1.00 29.49           C  
ANISOU 4113  C   ILE C 122     3952   3387   3865    231   -377   -361       C  
ATOM   4114  O   ILE C 122      -1.118 -11.526  78.976  1.00 30.39           O  
ANISOU 4114  O   ILE C 122     4055   3482   4011    236   -484   -437       O  
ATOM   4115  CB  ILE C 122      -1.553  -9.118  80.764  1.00 34.56           C  
ANISOU 4115  CB  ILE C 122     4439   4157   4535    272   -401   -398       C  
ATOM   4116  CG1 ILE C 122      -1.792  -7.613  80.882  1.00 33.67           C  
ANISOU 4116  CG1 ILE C 122     4341   4071   4380    354   -413   -415       C  
ATOM   4117  CG2 ILE C 122      -1.370  -9.716  82.144  1.00 37.41           C  
ANISOU 4117  CG2 ILE C 122     4688   4568   4958    155   -295   -342       C  
ATOM   4118  CD1 ILE C 122      -0.808  -6.941  81.727  1.00 35.30           C  
ANISOU 4118  CD1 ILE C 122     4582   4293   4537    329   -296   -342       C  
ATOM   4119  N   ASN C 123       0.801 -11.579  80.176  1.00 25.50           N  
ANISOU 4119  N   ASN C 123     3444   2854   3392    170   -276   -284       N  
ATOM   4120  CA  ASN C 123       0.958 -13.032  80.143  1.00 24.74           C  
ANISOU 4120  CA  ASN C 123     3323   2701   3377    105   -271   -279       C  
ATOM   4121  C   ASN C 123       0.626 -13.602  81.516  1.00 26.32           C  
ANISOU 4121  C   ASN C 123     3378   2949   3673     -5   -243   -224       C  
ATOM   4122  O   ASN C 123       1.262 -13.239  82.514  1.00 27.42           O  
ANISOU 4122  O   ASN C 123     3494   3120   3806    -43   -175   -140       O  
ATOM   4123  CB  ASN C 123       2.377 -13.449  79.751  1.00 26.77           C  
ANISOU 4123  CB  ASN C 123     3672   2867   3630    120   -184   -230       C  
ATOM   4124  CG  ASN C 123       2.692 -13.160  78.306  1.00 32.18           C  
ANISOU 4124  CG  ASN C 123     4527   3489   4211    209   -182   -291       C  
ATOM   4125  OD1 ASN C 123       1.792 -13.025  77.476  1.00 37.46           O  
ANISOU 4125  OD1 ASN C 123     5261   4159   4813    249   -285   -374       O  
ATOM   4126  ND2 ASN C 123       3.978 -13.075  77.989  1.00 31.12           N  
ANISOU 4126  ND2 ASN C 123     4469   3290   4065    235    -66   -250       N  
ATOM   4127  N   ARG C 124      -0.343 -14.516  81.563  1.00 27.12           N  
ANISOU 4127  N   ARG C 124     3397   3048   3858    -67   -298   -269       N  
ATOM   4128  CA  ARG C 124      -0.781 -15.139  82.805  1.00 23.22           C  
ANISOU 4128  CA  ARG C 124     2784   2592   3448   -188   -259   -217       C  
ATOM   4129  C   ARG C 124      -0.378 -16.609  82.753  1.00 29.79           C  
ANISOU 4129  C   ARG C 124     3627   3325   4367   -255   -263   -180       C  
ATOM   4130  O   ARG C 124      -1.026 -17.421  82.082  1.00 25.18           O  
ANISOU 4130  O   ARG C 124     3029   2690   3849   -271   -331   -252       O  
ATOM   4131  CB  ARG C 124      -2.285 -14.974  82.985  1.00 37.98           C  
ANISOU 4131  CB  ARG C 124     4524   4531   5375   -217   -299   -297       C  
ATOM   4132  CG  ARG C 124      -2.748 -14.942  84.419  1.00 37.94           C  
ANISOU 4132  CG  ARG C 124     4411   4603   5402   -325   -204   -248       C  
ATOM   4133  CD  ARG C 124      -4.206 -14.536  84.474  1.00 40.46           C  
ANISOU 4133  CD  ARG C 124     4584   4990   5798   -328   -221   -347       C  
ATOM   4134  NE  ARG C 124      -5.089 -15.682  84.266  1.00 44.21           N  
ANISOU 4134  NE  ARG C 124     4957   5429   6412   -412   -267   -391       N  
ATOM   4135  CZ  ARG C 124      -5.442 -16.507  85.243  1.00 42.75           C  
ANISOU 4135  CZ  ARG C 124     4693   5251   6300   -557   -179   -339       C  
ATOM   4136  NH1 ARG C 124      -6.255 -17.534  85.016  1.00 40.89           N  
ANISOU 4136  NH1 ARG C 124     4360   4971   6207   -641   -221   -380       N  
ATOM   4137  NH2 ARG C 124      -4.969 -16.296  86.459  1.00 45.92           N  
ANISOU 4137  NH2 ARG C 124     5128   5698   6622   -626    -51   -243       N  
HETATM 4138  N   MSE C 125       0.675 -16.947  83.485  1.00 23.24           N  
ANISOU 4138  N   MSE C 125     2821   2458   3550   -296   -205    -69       N  
HETATM 4139  CA  MSE C 125       1.263 -18.264  83.402  1.00 24.58           C  
ANISOU 4139  CA  MSE C 125     3012   2510   3816   -337   -213    -25       C  
HETATM 4140  C   MSE C 125       0.851 -19.116  84.590  1.00 24.35           C  
ANISOU 4140  C   MSE C 125     2913   2479   3859   -477   -204     60       C  
HETATM 4141  O   MSE C 125       1.098 -18.747  85.742  1.00 28.29           O  
ANISOU 4141  O   MSE C 125     3401   3033   4314   -536   -164    155       O  
HETATM 4142  CB  MSE C 125       2.787 -18.155  83.326  1.00 23.16           C  
ANISOU 4142  CB  MSE C 125     2898   2263   3639   -280   -171     46       C  
HETATM 4143  CG  MSE C 125       3.278 -17.291  82.165  1.00 27.89           C  
ANISOU 4143  CG  MSE C 125     3583   2856   4157   -156   -146    -27       C  
HETATM 4144 SE   MSE C 125       5.230 -17.288  82.078  1.00 32.14          SE  
ANISOU 4144 SE   MSE C 125     4161   3292   4760    -99    -63     56      SE  
HETATM 4145  CE  MSE C 125       5.492 -19.190  81.772  1.00 25.41           C  
ANISOU 4145  CE  MSE C 125     3300   2273   4080   -129    -79     50       C  
ATOM   4146  N   LEU C 126       0.232 -20.254  84.296  1.00 25.32           N  
ANISOU 4146  N   LEU C 126     3007   2531   4083   -537   -244     25       N  
ATOM   4147  CA  LEU C 126      -0.233 -21.179  85.312  1.00 26.23           C  
ANISOU 4147  CA  LEU C 126     3069   2624   4275   -683   -231    106       C  
ATOM   4148  C   LEU C 126       0.884 -22.140  85.711  1.00 30.47           C  
ANISOU 4148  C   LEU C 126     3664   3030   4883   -712   -242    226       C  
ATOM   4149  O   LEU C 126       1.923 -22.224  85.057  1.00 26.11           O  
ANISOU 4149  O   LEU C 126     3168   2396   4358   -615   -256    220       O  
ATOM   4150  CB  LEU C 126      -1.454 -21.936  84.794  1.00 27.37           C  
ANISOU 4150  CB  LEU C 126     3143   2739   4518   -742   -276      9       C  
ATOM   4151  CG  LEU C 126      -2.543 -20.945  84.393  1.00 27.35           C  
ANISOU 4151  CG  LEU C 126     3061   2855   4475   -699   -290   -109       C  
ATOM   4152  CD1 LEU C 126      -3.773 -21.641  83.850  1.00 28.69           C  
ANISOU 4152  CD1 LEU C 126     3140   2994   4768   -757   -361   -212       C  
ATOM   4153  CD2 LEU C 126      -2.898 -20.065  85.567  1.00 27.60           C  
ANISOU 4153  CD2 LEU C 126     3032   3016   4440   -749   -196    -57       C  
ATOM   4154  N   LYS C 127       0.659 -22.871  86.809  1.00 27.36           N  
ANISOU 4154  N   LYS C 127     3257   2610   4530   -850   -232    339       N  
ATOM   4155  CA  LYS C 127       1.645 -23.832  87.296  1.00 37.06           C  
ANISOU 4155  CA  LYS C 127     4541   3699   5841   -884   -271    470       C  
ATOM   4156  C   LYS C 127       2.015 -24.831  86.205  1.00 37.88           C  
ANISOU 4156  C   LYS C 127     4663   3644   6088   -820   -319    404       C  
ATOM   4157  O   LYS C 127       1.150 -25.313  85.474  1.00 28.97           O  
ANISOU 4157  O   LYS C 127     3508   2488   5011   -836   -335    293       O  
ATOM   4158  CB  LYS C 127       1.099 -24.572  88.519  1.00 32.47           C  
ANISOU 4158  CB  LYS C 127     3964   3100   5272  -1058   -259    594       C  
ATOM   4159  CG  LYS C 127       2.010 -25.657  89.076  1.00 37.21           C  
ANISOU 4159  CG  LYS C 127     4633   3536   5970  -1104   -328    746       C  
ATOM   4160  CD  LYS C 127       1.391 -26.275  90.338  1.00 39.62           C  
ANISOU 4160  CD  LYS C 127     4976   3832   6244  -1293   -307    881       C  
ATOM   4161  CE  LYS C 127       2.211 -27.437  90.870  1.00 44.47           C  
ANISOU 4161  CE  LYS C 127     5672   4259   6965  -1343   -403   1044       C  
ATOM   4162  NZ  LYS C 127       2.542 -28.381  89.779  1.00 46.32           N  
ANISOU 4162  NZ  LYS C 127     5877   4326   7396  -1259   -460    971       N  
ATOM   4163  N   ASP C 128       3.319 -25.117  86.092  1.00 33.63           N  
ANISOU 4163  N   ASP C 128     4164   2994   5622   -744   -342    463       N  
ATOM   4164  CA  ASP C 128       3.919 -26.026  85.115  1.00 28.96           C  
ANISOU 4164  CA  ASP C 128     3597   2232   5173   -665   -362    400       C  
ATOM   4165  C   ASP C 128       3.963 -25.440  83.711  1.00 32.98           C  
ANISOU 4165  C   ASP C 128     4134   2768   5627   -536   -320    231       C  
ATOM   4166  O   ASP C 128       4.360 -26.130  82.774  1.00 40.68           O  
ANISOU 4166  O   ASP C 128     5152   3612   6694   -469   -314    147       O  
ATOM   4167  CB  ASP C 128       3.205 -27.384  85.070  1.00 31.50           C  
ANISOU 4167  CB  ASP C 128     3921   2429   5619   -763   -406    390       C  
ATOM   4168  CG  ASP C 128       3.068 -28.009  86.437  1.00 47.91           C  
ANISOU 4168  CG  ASP C 128     6000   4469   7735   -909   -441    567       C  
ATOM   4169  OD1 ASP C 128       4.080 -28.057  87.167  1.00 54.87           O  
ANISOU 4169  OD1 ASP C 128     6905   5296   8646   -897   -476    706       O  
ATOM   4170  OD2 ASP C 128       1.951 -28.440  86.789  1.00 56.62           O  
ANISOU 4170  OD2 ASP C 128     7081   5593   8838  -1040   -436    570       O  
ATOM   4171  N   SER C 129       3.566 -24.191  83.530  1.00 27.29           N  
ANISOU 4171  N   SER C 129     3409   2206   4754   -499   -290    177       N  
ATOM   4172  CA  SER C 129       3.836 -23.557  82.255  1.00 27.24           C  
ANISOU 4172  CA  SER C 129     3461   2212   4677   -373   -251     48       C  
ATOM   4173  C   SER C 129       5.285 -23.064  82.222  1.00 26.35           C  
ANISOU 4173  C   SER C 129     3363   2065   4583   -281   -187    101       C  
ATOM   4174  O   SER C 129       5.952 -22.942  83.253  1.00 26.14           O  
ANISOU 4174  O   SER C 129     3289   2042   4601   -313   -197    235       O  
ATOM   4175  CB  SER C 129       2.878 -22.394  82.016  1.00 31.72           C  
ANISOU 4175  CB  SER C 129     4023   2940   5089   -360   -258    -25       C  
ATOM   4176  OG  SER C 129       3.145 -21.326  82.923  1.00 28.75           O  
ANISOU 4176  OG  SER C 129     3612   2681   4633   -367   -226     64       O  
ATOM   4177  N   PHE C 130       5.760 -22.779  81.013  1.00 28.70           N  
ANISOU 4177  N   PHE C 130     3733   2325   4846   -173   -121     -6       N  
ATOM   4178  CA  PHE C 130       7.092 -22.227  80.798  1.00 27.68           C  
ANISOU 4178  CA  PHE C 130     3608   2163   4745    -85    -31     21       C  
ATOM   4179  C   PHE C 130       7.099 -21.515  79.455  1.00 29.18           C  
ANISOU 4179  C   PHE C 130     3909   2376   4800      7     50   -110       C  
ATOM   4180  O   PHE C 130       6.184 -21.677  78.646  1.00 27.97           O  
ANISOU 4180  O   PHE C 130     3841   2233   4554     10     13   -224       O  
ATOM   4181  CB  PHE C 130       8.167 -23.314  80.833  1.00 27.20           C  
ANISOU 4181  CB  PHE C 130     3510   1924   4899    -57     -3     59       C  
ATOM   4182  CG  PHE C 130       7.977 -24.375  79.790  1.00 39.37           C  
ANISOU 4182  CG  PHE C 130     5127   3331   6501    -25     23    -70       C  
ATOM   4183  CD1 PHE C 130       8.532 -24.235  78.525  1.00 39.45           C  
ANISOU 4183  CD1 PHE C 130     5230   3279   6479     75    148   -197       C  
ATOM   4184  CD2 PHE C 130       7.232 -25.507  80.071  1.00 39.35           C  
ANISOU 4184  CD2 PHE C 130     5119   3256   6578   -104    -69    -69       C  
ATOM   4185  CE1 PHE C 130       8.352 -25.217  77.561  1.00 42.00           C  
ANISOU 4185  CE1 PHE C 130     5649   3471   6839    102    175   -330       C  
ATOM   4186  CE2 PHE C 130       7.043 -26.491  79.112  1.00 42.50           C  
ANISOU 4186  CE2 PHE C 130     5597   3519   7034    -80    -55   -198       C  
ATOM   4187  CZ  PHE C 130       7.604 -26.344  77.855  1.00 42.13           C  
ANISOU 4187  CZ  PHE C 130     5653   3412   6943     26     63   -335       C  
ATOM   4188  N   ILE C 131       8.148 -20.720  79.222  1.00 27.98           N  
ANISOU 4188  N   ILE C 131     3765   2227   4640     76    153    -91       N  
ATOM   4189  CA  ILE C 131       8.421 -20.145  77.910  1.00 30.02           C  
ANISOU 4189  CA  ILE C 131     4153   2472   4779    161    265   -200       C  
ATOM   4190  C   ILE C 131       9.733 -20.728  77.408  1.00 34.96           C  
ANISOU 4190  C   ILE C 131     4773   2948   5561    224    408   -222       C  
ATOM   4191  O   ILE C 131      10.787 -20.509  78.015  1.00 29.71           O  
ANISOU 4191  O   ILE C 131     3993   2256   5038    235    458   -129       O  
ATOM   4192  CB  ILE C 131       8.498 -18.615  77.938  1.00 28.29           C  
ANISOU 4192  CB  ILE C 131     3959   2375   4415    184    295   -169       C  
ATOM   4193  CG1 ILE C 131       7.342 -18.021  78.740  1.00 39.31           C  
ANISOU 4193  CG1 ILE C 131     5311   3911   5713    124    164   -130       C  
ATOM   4194  CG2 ILE C 131       8.458 -18.086  76.522  1.00 27.74           C  
ANISOU 4194  CG2 ILE C 131     4069   2293   4179    254    382   -282       C  
ATOM   4195  CD1 ILE C 131       6.012 -18.223  78.111  1.00 39.94           C  
ANISOU 4195  CD1 ILE C 131     5466   4025   5685    115     72   -233       C  
ATOM   4196  N   GLY C 132       9.671 -21.461  76.299  1.00 37.48           N  
ANISOU 4196  N   GLY C 132     5213   3163   5863    265    474   -353       N  
ATOM   4197  CA  GLY C 132      10.868 -22.052  75.746  1.00 32.97           C  
ANISOU 4197  CA  GLY C 132     4640   2439   5450    332    640   -399       C  
ATOM   4198  C   GLY C 132      11.787 -21.017  75.132  1.00 32.93           C  
ANISOU 4198  C   GLY C 132     4679   2450   5383    392    826   -412       C  
ATOM   4199  O   GLY C 132      11.399 -19.884  74.831  1.00 31.22           O  
ANISOU 4199  O   GLY C 132     4557   2349   4958    390    826   -413       O  
HETATM 4200  N   MSE C 133      13.040 -21.431  74.970  1.00 36.29           N  
ANISOU 4200  N   MSE C 133     5024   2746   6019    445    987   -420       N  
HETATM 4201  CA  MSE C 133      14.087 -20.637  74.337  1.00 37.24           C  
ANISOU 4201  CA  MSE C 133     5163   2845   6141    497   1211   -441       C  
HETATM 4202  C   MSE C 133      13.620 -19.981  73.041  1.00 35.31           C  
ANISOU 4202  C   MSE C 133     5181   2644   5592    516   1318   -556       C  
HETATM 4203  O   MSE C 133      13.053 -20.657  72.188  1.00 35.64           O  
ANISOU 4203  O   MSE C 133     5396   2629   5515    530   1324   -682       O  
HETATM 4204  CB  MSE C 133      15.286 -21.531  74.040  1.00 54.08           C  
ANISOU 4204  CB  MSE C 133     7199   4796   8554    560   1391   -492       C  
HETATM 4205  CG  MSE C 133      16.526 -20.767  73.724  1.00 68.93           C  
ANISOU 4205  CG  MSE C 133     9010   6647  10535    599   1620   -481       C  
HETATM 4206 SE   MSE C 133      17.228 -20.087  75.386  1.00 74.31          SE  
ANISOU 4206 SE   MSE C 133     9386   7393  11455    554   1458   -267      SE  
HETATM 4207  CE  MSE C 133      18.381 -21.617  75.802  1.00 72.63           C  
ANISOU 4207  CE  MSE C 133     8926   6950  11720    619   1484   -261       C  
ATOM   4208  N   HIS C 134      13.852 -18.675  72.886  1.00 36.95           N  
ANISOU 4208  N   HIS C 134     5434   2939   5667    513   1389   -510       N  
ATOM   4209  CA  HIS C 134      13.455 -17.984  71.664  1.00 36.77           C  
ANISOU 4209  CA  HIS C 134     5683   2946   5342    529   1481   -598       C  
ATOM   4210  C   HIS C 134      14.127 -16.619  71.609  1.00 36.44           C  
ANISOU 4210  C   HIS C 134     5642   2955   5247    526   1610   -524       C  
ATOM   4211  O   HIS C 134      14.708 -16.142  72.590  1.00 34.38           O  
ANISOU 4211  O   HIS C 134     5170   2729   5164    505   1584   -408       O  
ATOM   4212  CB  HIS C 134      11.937 -17.824  71.574  1.00 38.57           C  
ANISOU 4212  CB  HIS C 134     6050   3276   5331    500   1244   -622       C  
ATOM   4213  CG  HIS C 134      11.380 -16.872  72.582  1.00 43.08           C  
ANISOU 4213  CG  HIS C 134     6507   3990   5873    461   1068   -500       C  
ATOM   4214  ND1 HIS C 134      11.178 -17.222  73.901  1.00 40.79           N  
ANISOU 4214  ND1 HIS C 134     5998   3744   5758    418    917   -408       N  
ATOM   4215  CD2 HIS C 134      10.999 -15.577  72.472  1.00 41.16           C  
ANISOU 4215  CD2 HIS C 134     6351   3845   5443    458   1027   -460       C  
ATOM   4216  CE1 HIS C 134      10.690 -16.185  74.558  1.00 38.43           C  
ANISOU 4216  CE1 HIS C 134     5657   3570   5376    390    806   -327       C  
ATOM   4217  NE2 HIS C 134      10.566 -15.176  73.713  1.00 39.78           N  
ANISOU 4217  NE2 HIS C 134     6001   3772   5340    418    864   -359       N  
ATOM   4218  N   LEU C 135      14.029 -15.994  70.436  1.00 41.01           N  
ANISOU 4218  N   LEU C 135     6482   3531   5570    541   1740   -591       N  
ATOM   4219  CA  LEU C 135      14.508 -14.638  70.193  1.00 45.19           C  
ANISOU 4219  CA  LEU C 135     7076   4100   5995    530   1863   -527       C  
ATOM   4220  C   LEU C 135      13.321 -13.738  69.901  1.00 43.31           C  
ANISOU 4220  C   LEU C 135     7041   3966   5449    519   1680   -514       C  
ATOM   4221  O   LEU C 135      12.533 -14.022  68.993  1.00 42.27           O  
ANISOU 4221  O   LEU C 135     7153   3822   5087    535   1622   -608       O  
ATOM   4222  CB  LEU C 135      15.480 -14.587  69.013  1.00 45.64           C  
ANISOU 4222  CB  LEU C 135     7290   4045   6005    551   2200   -606       C  
ATOM   4223  CG  LEU C 135      16.961 -14.777  69.311  1.00 49.16           C  
ANISOU 4223  CG  LEU C 135     7497   4397   6783    559   2445   -581       C  
ATOM   4224  CD1 LEU C 135      17.705 -15.126  68.030  1.00 55.65           C  
ANISOU 4224  CD1 LEU C 135     8473   5124   7548    567   2750   -684       C  
ATOM   4225  CD2 LEU C 135      17.545 -13.521  69.952  1.00 44.18           C  
ANISOU 4225  CD2 LEU C 135     6723   3825   6240    519   2463   -448       C  
ATOM   4226  N   ASP C 136      13.201 -12.653  70.667  1.00 49.47           N  
ANISOU 4226  N   ASP C 136     7723   4838   6235    495   1577   -401       N  
ATOM   4227  CA  ASP C 136      12.135 -11.695  70.405  1.00 52.73           C  
ANISOU 4227  CA  ASP C 136     8311   5335   6388    497   1409   -385       C  
ATOM   4228  C   ASP C 136      12.265 -11.113  69.008  1.00 48.01           C  
ANISOU 4228  C   ASP C 136     8037   4682   5524    513   1561   -431       C  
ATOM   4229  O   ASP C 136      11.261 -10.898  68.321  1.00 51.85           O  
ANISOU 4229  O   ASP C 136     8753   5189   5758    531   1414   -474       O  
ATOM   4230  CB  ASP C 136      12.147 -10.591  71.460  1.00 59.86           C  
ANISOU 4230  CB  ASP C 136     9056   6326   7364    471   1313   -265       C  
ATOM   4231  CG  ASP C 136      11.543 -11.042  72.771  1.00 66.81           C  
ANISOU 4231  CG  ASP C 136     9705   7285   8395    448   1100   -227       C  
ATOM   4232  OD1 ASP C 136      10.834 -12.075  72.772  1.00 70.38           O  
ANISOU 4232  OD1 ASP C 136    10148   7738   8855    452    989   -289       O  
ATOM   4233  OD2 ASP C 136      11.772 -10.362  73.796  1.00 66.52           O  
ANISOU 4233  OD2 ASP C 136     9509   7304   8462    419   1048   -137       O  
ATOM   4234  N   ALA C 137      13.497 -10.892  68.555  1.00 46.91           N  
ANISOU 4234  N   ALA C 137     7923   4461   5441    503   1855   -423       N  
ATOM   4235  CA  ALA C 137      13.719 -10.355  67.219  1.00 50.77           C  
ANISOU 4235  CA  ALA C 137     8742   4885   5663    504   2042   -460       C  
ATOM   4236  C   ALA C 137      13.078 -11.204  66.124  1.00 49.82           C  
ANISOU 4236  C   ALA C 137     8903   4715   5312    529   2018   -594       C  
ATOM   4237  O   ALA C 137      12.927 -10.725  64.997  1.00 49.62           O  
ANISOU 4237  O   ALA C 137     9209   4654   4993    525   2083   -618       O  
ATOM   4238  CB  ALA C 137      15.218 -10.214  66.967  1.00 53.51           C  
ANISOU 4238  CB  ALA C 137     9026   5141   6165    480   2405   -447       C  
ATOM   4239  N   ALA C 138      12.685 -12.444  66.425  1.00 55.46           N  
ANISOU 4239  N   ALA C 138     9503   5422   6149    546   1905   -673       N  
ATOM   4240  CA  ALA C 138      12.030 -13.271  65.416  1.00 60.66           C  
ANISOU 4240  CA  ALA C 138    10428   6025   6594    563   1854   -811       C  
ATOM   4241  C   ALA C 138      10.620 -12.773  65.120  1.00 57.30           C  
ANISOU 4241  C   ALA C 138    10192   5671   5907    569   1535   -809       C  
ATOM   4242  O   ALA C 138      10.152 -12.859  63.979  1.00 64.66           O  
ANISOU 4242  O   ALA C 138    11413   6579   6578    564   1477   -868       O  
ATOM   4243  CB  ALA C 138      12.001 -14.733  65.863  1.00 61.37           C  
ANISOU 4243  CB  ALA C 138    10330   6073   6914    573   1814   -893       C  
ATOM   4244  N   SER C 139       9.928 -12.254  66.136  1.00 45.38           N  
ANISOU 4244  N   SER C 139     8472   4269   4501    567   1293   -717       N  
ATOM   4245  CA  SER C 139       8.590 -11.715  65.920  1.00 47.84           C  
ANISOU 4245  CA  SER C 139     8917   4643   4616    582    987   -713       C  
ATOM   4246  C   SER C 139       8.632 -10.381  65.187  1.00 49.47           C  
ANISOU 4246  C   SER C 139     9390   4839   4566    593   1017   -650       C  
ATOM   4247  O   SER C 139       7.709 -10.063  64.425  1.00 48.27           O  
ANISOU 4247  O   SER C 139     9492   4682   4166    614    815   -679       O  
ATOM   4248  CB  SER C 139       7.871 -11.560  67.255  1.00 47.62           C  
ANISOU 4248  CB  SER C 139     8574   4727   4793    577    760   -644       C  
ATOM   4249  OG  SER C 139       7.781 -12.810  67.911  1.00 54.93           O  
ANISOU 4249  OG  SER C 139     9283   5651   5935    557    724   -691       O  
ATOM   4250  N   ASN C 140       9.684  -9.589  65.415  1.00 49.81           N  
ANISOU 4250  N   ASN C 140     9379   4871   4678    576   1250   -559       N  
ATOM   4251  CA  ASN C 140       9.929  -8.330  64.722  1.00 43.61           C  
ANISOU 4251  CA  ASN C 140     8849   4052   3669    572   1333   -486       C  
ATOM   4252  C   ASN C 140      11.419  -8.015  64.801  1.00 38.46           C  
ANISOU 4252  C   ASN C 140     8121   3346   3146    532   1698   -433       C  
ATOM   4253  O   ASN C 140      11.943  -7.762  65.892  1.00 38.18           O  
ANISOU 4253  O   ASN C 140     7771   3354   3381    516   1734   -359       O  
ATOM   4254  CB  ASN C 140       9.097  -7.195  65.327  1.00 40.28           C  
ANISOU 4254  CB  ASN C 140     8358   3708   3239    594   1073   -389       C  
ATOM   4255  CG  ASN C 140       9.216  -5.897  64.538  1.00 43.02           C  
ANISOU 4255  CG  ASN C 140     9007   4001   3338    594   1117   -309       C  
ATOM   4256  OD1 ASN C 140      10.256  -5.616  63.951  1.00 45.90           O  
ANISOU 4256  OD1 ASN C 140     9521   4290   3628    555   1413   -283       O  
ATOM   4257  ND2 ASN C 140       8.145  -5.110  64.510  1.00 37.13           N  
ANISOU 4257  ND2 ASN C 140     8349   3285   2476    636    826   -269       N  
ATOM   4258  N   PRO C 141      12.129  -8.007  63.673  1.00 41.34           N  
ANISOU 4258  N   PRO C 141     8702   3629   3377    495   1930   -441       N  
ATOM   4259  CA  PRO C 141      13.585  -7.802  63.729  1.00 45.20           C  
ANISOU 4259  CA  PRO C 141     9065   4061   4048    447   2281   -396       C  
ATOM   4260  C   PRO C 141      13.989  -6.447  64.275  1.00 51.79           C  
ANISOU 4260  C   PRO C 141     9844   4905   4928    427   2341   -274       C  
ATOM   4261  O   PRO C 141      15.155  -6.282  64.656  1.00 63.49           O  
ANISOU 4261  O   PRO C 141    11133   6352   6637    388   2596   -236       O  
ATOM   4262  CB  PRO C 141      14.016  -7.966  62.265  1.00 47.31           C  
ANISOU 4262  CB  PRO C 141     9599   4241   4135    401   2450   -420       C  
ATOM   4263  CG  PRO C 141      12.807  -7.569  61.490  1.00 49.87           C  
ANISOU 4263  CG  PRO C 141    10236   4576   4138    419   2170   -414       C  
ATOM   4264  CD  PRO C 141      11.630  -8.054  62.289  1.00 42.39           C  
ANISOU 4264  CD  PRO C 141     9167   3716   3221    481   1849   -466       C  
ATOM   4265  N   ASP C 142      13.068  -5.481  64.338  1.00 45.76           N  
ANISOU 4265  N   ASP C 142     9226   4182   3977    451   2105   -212       N  
ATOM   4266  CA  ASP C 142      13.356  -4.131  64.809  1.00 42.24           C  
ANISOU 4266  CA  ASP C 142     8736   3742   3572    425   2119    -86       C  
ATOM   4267  C   ASP C 142      13.105  -3.944  66.304  1.00 38.54           C  
ANISOU 4267  C   ASP C 142     7887   3371   3387    437   1914    -37       C  
ATOM   4268  O   ASP C 142      13.258  -2.829  66.805  1.00 40.99           O  
ANISOU 4268  O   ASP C 142     8136   3688   3752    417   1884     59       O  
ATOM   4269  CB  ASP C 142      12.529  -3.104  64.018  1.00 41.81           C  
ANISOU 4269  CB  ASP C 142     9010   3660   3214    439   1931    -26       C  
ATOM   4270  CG  ASP C 142      12.836  -3.119  62.529  1.00 55.76           C  
ANISOU 4270  CG  ASP C 142    11067   5323   4796    395   2050    -36       C  
ATOM   4271  OD1 ASP C 142      14.028  -3.099  62.153  1.00 58.75           O  
ANISOU 4271  OD1 ASP C 142    11427   5629   5267    330   2365    -26       O  
ATOM   4272  OD2 ASP C 142      11.881  -3.161  61.727  1.00 62.09           O  
ANISOU 4272  OD2 ASP C 142    12111   6111   5370    425   1824    -59       O  
ATOM   4273  N   TYR C 143      12.732  -4.989  67.033  1.00 36.09           N  
ANISOU 4273  N   TYR C 143     7338   3126   3247    463   1779   -101       N  
ATOM   4274  CA  TYR C 143      12.619  -4.867  68.483  1.00 40.82           C  
ANISOU 4274  CA  TYR C 143     7595   3812   4105    459   1624    -52       C  
ATOM   4275  C   TYR C 143      14.004  -4.710  69.095  1.00 39.06           C  
ANISOU 4275  C   TYR C 143     7139   3554   4148    404   1852      3       C  
ATOM   4276  O   TYR C 143      14.888  -5.537  68.865  1.00 43.60           O  
ANISOU 4276  O   TYR C 143     7638   4072   4856    388   2067    -41       O  
ATOM   4277  CB  TYR C 143      11.939  -6.096  69.080  1.00 35.75           C  
ANISOU 4277  CB  TYR C 143     6775   3235   3575    486   1448   -125       C  
ATOM   4278  CG  TYR C 143      10.454  -6.201  68.849  1.00 31.78           C  
ANISOU 4278  CG  TYR C 143     6394   2785   2897    533   1163   -173       C  
ATOM   4279  CD1 TYR C 143       9.705  -5.097  68.489  1.00 31.64           C  
ANISOU 4279  CD1 TYR C 143     6558   2775   2687    562   1012   -133       C  
ATOM   4280  CD2 TYR C 143       9.799  -7.416  69.021  1.00 32.97           C  
ANISOU 4280  CD2 TYR C 143     6458   2967   3101    547   1033   -256       C  
ATOM   4281  CE1 TYR C 143       8.342  -5.197  68.286  1.00 36.96           C  
ANISOU 4281  CE1 TYR C 143     7312   3489   3241    611    734   -180       C  
ATOM   4282  CE2 TYR C 143       8.443  -7.529  68.827  1.00 33.25           C  
ANISOU 4282  CE2 TYR C 143     6574   3047   3013    583    768   -305       C  
ATOM   4283  CZ  TYR C 143       7.717  -6.421  68.456  1.00 37.76           C  
ANISOU 4283  CZ  TYR C 143     7310   3628   3410    617    615   -269       C  
ATOM   4284  OH  TYR C 143       6.362  -6.536  68.256  1.00 35.69           O  
ANISOU 4284  OH  TYR C 143     7100   3401   3060    658    336   -321       O  
ATOM   4285  N   GLU C 144      14.203  -3.657  69.880  1.00 38.23           N  
ANISOU 4285  N   GLU C 144     6913   3473   4140    375   1797     93       N  
ATOM   4286  CA  GLU C 144      15.498  -3.476  70.527  1.00 31.27           C  
ANISOU 4286  CA  GLU C 144     5792   2555   3533    315   1972    146       C  
ATOM   4287  C   GLU C 144      15.485  -3.846  72.000  1.00 29.43           C  
ANISOU 4287  C   GLU C 144     5234   2398   3551    305   1798    166       C  
ATOM   4288  O   GLU C 144      16.463  -4.392  72.509  1.00 32.06           O  
ANISOU 4288  O   GLU C 144     5338   2701   4143    275   1902    175       O  
ATOM   4289  CB  GLU C 144      15.968  -2.031  70.392  1.00 31.94           C  
ANISOU 4289  CB  GLU C 144     5966   2590   3580    267   2062    235       C  
ATOM   4290  CG  GLU C 144      16.332  -1.592  69.004  1.00 39.80           C  
ANISOU 4290  CG  GLU C 144     7272   3487   4363    247   2301    242       C  
ATOM   4291  CD  GLU C 144      16.784  -0.156  69.007  1.00 47.97           C  
ANISOU 4291  CD  GLU C 144     8374   4464   5390    189   2373    343       C  
ATOM   4292  OE1 GLU C 144      17.362   0.269  70.032  1.00 50.18           O  
ANISOU 4292  OE1 GLU C 144     8391   4754   5920    143   2349    392       O  
ATOM   4293  OE2 GLU C 144      16.540   0.551  68.012  1.00 52.10           O  
ANISOU 4293  OE2 GLU C 144     9220   4924   5650    184   2435    375       O  
ATOM   4294  N   PHE C 145      14.416  -3.527  72.710  1.00 28.21           N  
ANISOU 4294  N   PHE C 145     4666   2955   3098    -63   1656   -102       N  
ATOM   4295  CA  PHE C 145      14.373  -3.742  74.143  1.00 27.69           C  
ANISOU 4295  CA  PHE C 145     4278   2956   3287    -70   1475   -138       C  
ATOM   4296  C   PHE C 145      13.011  -4.279  74.512  1.00 30.61           C  
ANISOU 4296  C   PHE C 145     4710   3397   3524    -68   1222   -303       C  
ATOM   4297  O   PHE C 145      11.999  -3.919  73.906  1.00 38.28           O  
ANISOU 4297  O   PHE C 145     5885   4365   4295    -79   1053   -375       O  
ATOM   4298  CB  PHE C 145      14.631  -2.465  74.945  1.00 23.12           C  
ANISOU 4298  CB  PHE C 145     3491   2385   2910   -112   1289    -43       C  
ATOM   4299  CG  PHE C 145      15.979  -1.876  74.724  1.00 34.02           C  
ANISOU 4299  CG  PHE C 145     4734   3667   4523   -132   1498    143       C  
ATOM   4300  CD1 PHE C 145      17.101  -2.461  75.292  1.00 33.13           C  
ANISOU 4300  CD1 PHE C 145     4363   3493   4732   -110   1649    207       C  
ATOM   4301  CD2 PHE C 145      16.129  -0.723  73.954  1.00 26.23           C  
ANISOU 4301  CD2 PHE C 145     3865   2624   3478   -178   1528    265       C  
ATOM   4302  CE1 PHE C 145      18.350  -1.916  75.089  1.00 31.74           C  
ANISOU 4302  CE1 PHE C 145     4004   3198   4860   -133   1842    387       C  
ATOM   4303  CE2 PHE C 145      17.370  -0.173  73.747  1.00 34.08           C  
ANISOU 4303  CE2 PHE C 145     4700   3510   4740   -212   1745    462       C  
ATOM   4304  CZ  PHE C 145      18.487  -0.767  74.313  1.00 36.00           C  
ANISOU 4304  CZ  PHE C 145     4640   3687   5350   -189   1910    522       C  
ATOM   4305  N   SER C 146      13.005  -5.128  75.523  1.00 31.66           N  
ANISOU 4305  N   SER C 146     4658   3571   3802    -59   1188   -350       N  
ATOM   4306  CA  SER C 146      11.798  -5.657  76.130  1.00 28.69           C  
ANISOU 4306  CA  SER C 146     4262   3259   3379    -71    989   -473       C  
ATOM   4307  C   SER C 146      11.717  -5.161  77.570  1.00 23.70           C  
ANISOU 4307  C   SER C 146     3409   2697   2900    -85    839   -455       C  
ATOM   4308  O   SER C 146      12.744  -5.051  78.247  1.00 24.73           O  
ANISOU 4308  O   SER C 146     3394   2801   3202    -77    885   -365       O  
ATOM   4309  CB  SER C 146      11.822  -7.193  76.085  1.00 26.92           C  
ANISOU 4309  CB  SER C 146     4065   3002   3159    -52   1096   -532       C  
ATOM   4310  OG  SER C 146      10.755  -7.723  76.833  1.00 40.86           O  
ANISOU 4310  OG  SER C 146     5759   4819   4945    -83    931   -613       O  
ATOM   4311  N   VAL C 147      10.503  -4.852  78.037  1.00 18.98           N  
ANISOU 4311  N   VAL C 147     2793   2166   2253    -97    654   -545       N  
ATOM   4312  CA  VAL C 147      10.264  -4.416  79.411  1.00 23.47           C  
ANISOU 4312  CA  VAL C 147     3214   2800   2904    -90    538   -555       C  
ATOM   4313  C   VAL C 147       9.183  -5.311  80.002  1.00 22.12           C  
ANISOU 4313  C   VAL C 147     3006   2683   2714   -107    527   -640       C  
ATOM   4314  O   VAL C 147       8.127  -5.496  79.390  1.00 26.99           O  
ANISOU 4314  O   VAL C 147     3667   3296   3291   -124    471   -725       O  
ATOM   4315  CB  VAL C 147       9.841  -2.933  79.500  1.00 23.00           C  
ANISOU 4315  CB  VAL C 147     3143   2760   2835    -73    361   -578       C  
ATOM   4316  CG1 VAL C 147       9.522  -2.559  80.945  1.00 16.55           C  
ANISOU 4316  CG1 VAL C 147     2224   2004   2061    -38    263   -619       C  
ATOM   4317  CG2 VAL C 147      10.928  -2.039  78.943  1.00 21.96           C  
ANISOU 4317  CG2 VAL C 147     3033   2555   2756    -75    373   -462       C  
ATOM   4318  N   VAL C 148       9.445  -5.871  81.184  1.00 25.64           N  
ANISOU 4318  N   VAL C 148     3380   3153   3209   -108    566   -607       N  
ATOM   4319  CA  VAL C 148       8.545  -6.830  81.819  1.00 25.01           C  
ANISOU 4319  CA  VAL C 148     3267   3110   3124   -141    607   -647       C  
ATOM   4320  C   VAL C 148       8.231  -6.356  83.220  1.00 18.50           C  
ANISOU 4320  C   VAL C 148     2404   2351   2273   -117    581   -650       C  
ATOM   4321  O   VAL C 148       9.134  -6.287  84.060  1.00 23.45           O  
ANISOU 4321  O   VAL C 148     3062   2953   2895    -92    557   -580       O  
ATOM   4322  CB  VAL C 148       9.154  -8.236  81.893  1.00 25.48           C  
ANISOU 4322  CB  VAL C 148     3345   3109   3227   -170    706   -589       C  
ATOM   4323  CG1 VAL C 148       8.104  -9.202  82.418  1.00 28.39           C  
ANISOU 4323  CG1 VAL C 148     3680   3499   3609   -225    744   -611       C  
ATOM   4324  CG2 VAL C 148       9.683  -8.655  80.544  1.00 32.45           C  
ANISOU 4324  CG2 VAL C 148     4304   3914   4113   -161    764   -595       C  
ATOM   4325  N   ILE C 149       6.954  -6.097  83.494  1.00 17.37           N  
ANISOU 4325  N   ILE C 149     2204   2271   2125   -117    587   -733       N  
ATOM   4326  CA  ILE C 149       6.490  -5.715  84.827  1.00 18.73           C  
ANISOU 4326  CA  ILE C 149     2370   2508   2238    -78    630   -754       C  
ATOM   4327  C   ILE C 149       5.841  -6.930  85.480  1.00 26.17           C  
ANISOU 4327  C   ILE C 149     3291   3467   3186   -140    798   -718       C  
ATOM   4328  O   ILE C 149       4.876  -7.481  84.938  1.00 27.35           O  
ANISOU 4328  O   ILE C 149     3332   3609   3450   -196    848   -755       O  
ATOM   4329  CB  ILE C 149       5.492  -4.554  84.756  1.00 20.42           C  
ANISOU 4329  CB  ILE C 149     2506   2768   2483    -23    570   -875       C  
ATOM   4330  CG1 ILE C 149       6.084  -3.393  83.957  1.00 20.81           C  
ANISOU 4330  CG1 ILE C 149     2587   2778   2543     17    382   -890       C  
ATOM   4331  CG2 ILE C 149       5.114  -4.074  86.158  1.00 19.75           C  
ANISOU 4331  CG2 ILE C 149     2456   2744   2305     49    649   -914       C  
ATOM   4332  CD1 ILE C 149       5.092  -2.276  83.798  1.00 19.42           C  
ANISOU 4332  CD1 ILE C 149     2335   2618   2425     72    277  -1015       C  
ATOM   4333  N   GLN C 150       6.336  -7.328  86.657  1.00 28.64           N  
ANISOU 4333  N   GLN C 150     3718   3777   3386   -135    860   -639       N  
ATOM   4334  CA  GLN C 150       5.778  -8.467  87.390  1.00 25.88           C  
ANISOU 4334  CA  GLN C 150     3386   3430   3016   -205   1034   -571       C  
ATOM   4335  C   GLN C 150       4.593  -7.999  88.221  1.00 26.87           C  
ANISOU 4335  C   GLN C 150     3476   3639   3095   -174   1208   -626       C  
ATOM   4336  O   GLN C 150       4.746  -7.208  89.158  1.00 25.84           O  
ANISOU 4336  O   GLN C 150     3482   3542   2793    -85   1218   -653       O  
ATOM   4337  CB  GLN C 150       6.827  -9.125  88.286  1.00 21.90           C  
ANISOU 4337  CB  GLN C 150     3068   2858   2395   -214   1004   -450       C  
ATOM   4338  CG  GLN C 150       6.369 -10.480  88.908  1.00 31.28           C  
ANISOU 4338  CG  GLN C 150     4301   4016   3568   -311   1165   -344       C  
ATOM   4339  CD  GLN C 150       6.036 -11.538  87.862  1.00 31.91           C  
ANISOU 4339  CD  GLN C 150     4228   4045   3851   -405   1179   -333       C  
ATOM   4340  OE1 GLN C 150       5.036 -12.245  87.978  1.00 39.56           O  
ANISOU 4340  OE1 GLN C 150     5110   5014   4906   -488   1323   -302       O  
ATOM   4341  NE2 GLN C 150       6.867 -11.640  86.833  1.00 23.67           N  
ANISOU 4341  NE2 GLN C 150     3157   2940   2896   -387   1037   -361       N  
ATOM   4342  N   LEU C 151       3.412  -8.493  87.882  1.00 28.50           N  
ANISOU 4342  N   LEU C 151     3498   3857   3475   -241   1343   -649       N  
ATOM   4343  CA  LEU C 151       2.207  -8.271  88.657  1.00 27.75           C  
ANISOU 4343  CA  LEU C 151     3310   3822   3412   -227   1585   -684       C  
ATOM   4344  C   LEU C 151       1.804  -9.507  89.432  1.00 27.91           C  
ANISOU 4344  C   LEU C 151     3354   3822   3427   -330   1833   -544       C  
ATOM   4345  O   LEU C 151       0.787  -9.485  90.141  1.00 37.18           O  
ANISOU 4345  O   LEU C 151     4446   5038   4643   -334   2115   -540       O  
ATOM   4346  CB  LEU C 151       1.060  -7.849  87.737  1.00 32.49           C  
ANISOU 4346  CB  LEU C 151     3625   4413   4307   -230   1550   -805       C  
ATOM   4347  CG  LEU C 151       1.403  -6.669  86.838  1.00 33.39           C  
ANISOU 4347  CG  LEU C 151     3733   4521   4431   -146   1279   -925       C  
ATOM   4348  CD1 LEU C 151       0.314  -6.489  85.786  1.00 33.08           C  
ANISOU 4348  CD1 LEU C 151     3451   4420   4699   -171   1168  -1027       C  
ATOM   4349  CD2 LEU C 151       1.584  -5.404  87.676  1.00 29.53           C  
ANISOU 4349  CD2 LEU C 151     3349   4100   3770    -11   1293  -1003       C  
ATOM   4350  N   GLY C 152       2.572 -10.582  89.311  1.00 33.68           N  
ANISOU 4350  N   GLY C 152     4193   4478   4127   -414   1751   -424       N  
ATOM   4351  CA  GLY C 152       2.189 -11.832  89.938  1.00 45.94           C  
ANISOU 4351  CA  GLY C 152     5767   5983   5703   -533   1948   -272       C  
ATOM   4352  C   GLY C 152       2.347 -11.724  91.432  1.00 53.72           C  
ANISOU 4352  C   GLY C 152     7027   7005   6378   -497   2147   -185       C  
ATOM   4353  O   GLY C 152       3.416 -11.347  91.930  1.00 39.27           O  
ANISOU 4353  O   GLY C 152     5467   5160   4295   -419   1990   -176       O  
ATOM   4354  N   ARG C 153       1.263 -12.027  92.152  1.00 76.51           N  
ANISOU 4354  N   ARG C 153     9849   9918   9303   -534   2430   -115       N  
ATOM   4355  CA  ARG C 153       1.190 -11.980  93.607  1.00 87.73           C  
ANISOU 4355  CA  ARG C 153    11545  11368  10422   -482   2595    -22       C  
ATOM   4356  C   ARG C 153       2.375 -12.693  94.239  1.00 87.50           C  
ANISOU 4356  C   ARG C 153    11892  11245  10110   -527   2500    117       C  
ATOM   4357  O   ARG C 153       3.254 -12.058  94.831  1.00100.83           O  
ANISOU 4357  O   ARG C 153    13896  12921  11495   -423   2371     84       O  
ATOM   4358  CB  ARG C 153      -0.123 -12.609  94.091  1.00 92.28           C  
ANISOU 4358  CB  ARG C 153    11947  11952  11162   -555   2872     81       C  
ATOM   4359  N   ALA C 154       2.409 -14.012  94.110  1.00 66.30           N  
ANISOU 4359  N   ALA C 154     9184   8463   7543   -680   2522    273       N  
ATOM   4360  CA  ALA C 154       3.496 -14.793  94.670  1.00 56.24           C  
ANISOU 4360  CA  ALA C 154     8264   7062   6043   -738   2400    423       C  
ATOM   4361  C   ALA C 154       3.495 -16.139  93.974  1.00 55.93           C  
ANISOU 4361  C   ALA C 154     8047   6909   6293   -896   2320    531       C  
ATOM   4362  O   ALA C 154       2.427 -16.697  93.704  1.00 59.96           O  
ANISOU 4362  O   ALA C 154     8296   7426   7060   -993   2496    576       O  
ATOM   4363  CB  ALA C 154       3.347 -14.963  96.185  1.00 61.99           C  
ANISOU 4363  CB  ALA C 154     9331   7776   6446   -710   2527    548       C  
ATOM   4364  N   PHE C 155       4.691 -16.646  93.677  1.00 50.91           N  
ANISOU 4364  N   PHE C 155     7520   6153   5668   -893   1986    553       N  
ATOM   4365  CA  PHE C 155       4.838 -17.883  92.920  1.00 48.92           C  
ANISOU 4365  CA  PHE C 155     7114   5776   5698  -1007   1851    615       C  
ATOM   4366  C   PHE C 155       6.247 -18.420  93.112  1.00 48.34           C  
ANISOU 4366  C   PHE C 155     7265   5548   5555   -983   1536    672       C  
ATOM   4367  O   PHE C 155       7.173 -17.682  93.462  1.00 44.13           O  
ANISOU 4367  O   PHE C 155     6909   5008   4851   -867   1360    620       O  
ATOM   4368  CB  PHE C 155       4.537 -17.675  91.425  1.00 45.98           C  
ANISOU 4368  CB  PHE C 155     6389   5441   5640   -986   1754    447       C  
ATOM   4369  CG  PHE C 155       5.362 -16.581  90.778  1.00 42.20           C  
ANISOU 4369  CG  PHE C 155     5893   5025   5116   -836   1557    275       C  
ATOM   4370  CD1 PHE C 155       6.492 -16.891  90.029  1.00 37.70           C  
ANISOU 4370  CD1 PHE C 155     5323   4360   4642   -794   1302    231       C  
ATOM   4371  CD2 PHE C 155       5.008 -15.245  90.933  1.00 32.77           C  
ANISOU 4371  CD2 PHE C 155     4676   3970   3804   -737   1644    165       C  
ATOM   4372  CE1 PHE C 155       7.253 -15.890  89.449  1.00 35.01           C  
ANISOU 4372  CE1 PHE C 155     4952   4063   4285   -673   1165    105       C  
ATOM   4373  CE2 PHE C 155       5.768 -14.243  90.355  1.00 34.16           C  
ANISOU 4373  CE2 PHE C 155     4837   4183   3959   -617   1456     34       C  
ATOM   4374  CZ  PHE C 155       6.891 -14.569  89.609  1.00 35.54           C  
ANISOU 4374  CZ  PHE C 155     5004   4264   4236   -594   1229     16       C  
ATOM   4375  N   ASP C 156       6.392 -19.720  92.887  1.00 56.71           N  
ANISOU 4375  N   ASP C 156     8299   6457   6793  -1093   1442    777       N  
ATOM   4376  CA  ASP C 156       7.687 -20.382  92.915  1.00 52.21           C  
ANISOU 4376  CA  ASP C 156     7870   5704   6261  -1071   1127    817       C  
ATOM   4377  C   ASP C 156       8.200 -20.565  91.491  1.00 44.11           C  
ANISOU 4377  C   ASP C 156     6580   4644   5536  -1015    954    661       C  
ATOM   4378  O   ASP C 156       7.420 -20.603  90.533  1.00 33.54           O  
ANISOU 4378  O   ASP C 156     5001   3371   4373  -1040   1050    570       O  
ATOM   4379  CB  ASP C 156       7.599 -21.734  93.631  1.00 59.46           C  
ANISOU 4379  CB  ASP C 156     8970   6447   7176  -1217   1111   1035       C  
ATOM   4380  N   GLY C 157       9.525 -20.644  91.356  1.00 40.47           N  
ANISOU 4380  N   GLY C 157     6177   4060   5138   -929    697    626       N  
ATOM   4381  CA  GLY C 157      10.112 -20.845  90.038  1.00 35.28           C  
ANISOU 4381  CA  GLY C 157     5306   3357   4742   -858    586    481       C  
ATOM   4382  C   GLY C 157       9.806 -19.699  89.093  1.00 29.77           C  
ANISOU 4382  C   GLY C 157     4431   2834   4044   -774    693    313       C  
ATOM   4383  O   GLY C 157       9.798 -18.523  89.480  1.00 27.81           O  
ANISOU 4383  O   GLY C 157     4224   2708   3633   -715    738    283       O  
ATOM   4384  N   GLY C 158       9.569 -20.035  87.826  1.00 26.23           N  
ANISOU 4384  N   GLY C 158     3818   2378   3769   -762    706    199       N  
ATOM   4385  CA  GLY C 158       9.255 -19.004  86.843  1.00 25.20           C  
ANISOU 4385  CA  GLY C 158     3564   2386   3626   -688    779     49       C  
ATOM   4386  C   GLY C 158      10.340 -17.969  86.623  1.00 28.05           C  
ANISOU 4386  C   GLY C 158     3922   2782   3955   -565    726    -16       C  
ATOM   4387  O   GLY C 158      10.030 -16.794  86.367  1.00 27.17           O  
ANISOU 4387  O   GLY C 158     3765   2805   3752   -520    785    -86       O  
ATOM   4388  N   GLU C 159      11.610 -18.365  86.702  1.00 24.46           N  
ANISOU 4388  N   GLU C 159     3490   2186   3618   -511    605      8       N  
ATOM   4389  CA  GLU C 159      12.680 -17.393  86.522  1.00 22.95           C  
ANISOU 4389  CA  GLU C 159     3252   1996   3474   -406    557    -31       C  
ATOM   4390  C   GLU C 159      12.793 -16.956  85.061  1.00 28.23           C  
ANISOU 4390  C   GLU C 159     3805   2714   4205   -335    667   -161       C  
ATOM   4391  O   GLU C 159      12.546 -17.725  84.126  1.00 23.59           O  
ANISOU 4391  O   GLU C 159     3203   2082   3680   -332    722   -232       O  
ATOM   4392  CB  GLU C 159      14.016 -17.962  86.994  1.00 26.17           C  
ANISOU 4392  CB  GLU C 159     3669   2201   4074   -365    387     33       C  
ATOM   4393  CG  GLU C 159      14.057 -18.378  88.466  1.00 30.51           C  
ANISOU 4393  CG  GLU C 159     4408   2655   4530   -428    222    174       C  
ATOM   4394  CD  GLU C 159      13.586 -19.815  88.700  1.00 41.77           C  
ANISOU 4394  CD  GLU C 159     5912   3978   5980   -524    205    247       C  
ATOM   4395  OE1 GLU C 159      12.821 -20.333  87.858  1.00 40.17           O  
ANISOU 4395  OE1 GLU C 159     5626   3828   5810   -562    337    185       O  
ATOM   4396  OE2 GLU C 159      13.984 -20.422  89.725  1.00 45.80           O  
ANISOU 4396  OE2 GLU C 159     6585   4332   6485   -564     27    371       O  
ATOM   4397  N   PHE C 160      13.177 -15.703  84.871  1.00 19.12           N  
ANISOU 4397  N   PHE C 160     2814   2061   2391   -283    700    232       N  
ATOM   4398  CA  PHE C 160      13.514 -15.210  83.550  1.00 18.95           C  
ANISOU 4398  CA  PHE C 160     2788   2103   2309   -317    698    250       C  
ATOM   4399  C   PHE C 160      15.004 -15.469  83.331  1.00 20.24           C  
ANISOU 4399  C   PHE C 160     2939   2353   2398   -217    784    184       C  
ATOM   4400  O   PHE C 160      15.834 -15.006  84.114  1.00 23.71           O  
ANISOU 4400  O   PHE C 160     3267   2826   2917   -160    817    162       O  
ATOM   4401  CB  PHE C 160      13.147 -13.727  83.446  1.00 14.56           C  
ANISOU 4401  CB  PHE C 160     2115   1569   1847   -397    662    325       C  
ATOM   4402  CG  PHE C 160      13.417 -13.139  82.124  1.00 18.82           C  
ANISOU 4402  CG  PHE C 160     2694   2154   2303   -460    655    379       C  
ATOM   4403  CD1 PHE C 160      12.566 -13.379  81.068  1.00 27.98           C  
ANISOU 4403  CD1 PHE C 160     3983   3259   3388   -519    564    400       C  
ATOM   4404  CD2 PHE C 160      14.518 -12.337  81.925  1.00 18.80           C  
ANISOU 4404  CD2 PHE C 160     2612   2236   2297   -469    731    416       C  
ATOM   4405  CE1 PHE C 160      12.820 -12.831  79.838  1.00 28.44           C  
ANISOU 4405  CE1 PHE C 160     4138   3350   3319   -574    556    461       C  
ATOM   4406  CE2 PHE C 160      14.759 -11.778  80.694  1.00 19.78           C  
ANISOU 4406  CE2 PHE C 160     2800   2404   2313   -553    755    495       C  
ATOM   4407  CZ  PHE C 160      13.913 -12.035  79.651  1.00 22.05           C  
ANISOU 4407  CZ  PHE C 160     3264   2639   2475   -599    671    519       C  
ATOM   4408  N   VAL C 161      15.344 -16.247  82.303  1.00 23.42           N  
ANISOU 4408  N   VAL C 161     3451   2787   2662   -177    808    131       N  
ATOM   4409  CA  VAL C 161      16.726 -16.665  82.064  1.00 17.52           C  
ANISOU 4409  CA  VAL C 161     2668   2136   1853    -56    907     31       C  
ATOM   4410  C   VAL C 161      17.151 -16.188  80.687  1.00 28.36           C  
ANISOU 4410  C   VAL C 161     4046   3634   3095    -96   1019     61       C  
ATOM   4411  O   VAL C 161      16.538 -16.567  79.682  1.00 31.97           O  
ANISOU 4411  O   VAL C 161     4677   4070   3401   -117    980     67       O  
ATOM   4412  CB  VAL C 161      16.890 -18.180  82.168  1.00 18.15           C  
ANISOU 4412  CB  VAL C 161     2890   2145   1859     75    846    -97       C  
ATOM   4413  CG1 VAL C 161      18.361 -18.553  82.113  1.00 19.39           C  
ANISOU 4413  CG1 VAL C 161     2963   2400   2006    233    932   -237       C  
ATOM   4414  CG2 VAL C 161      16.268 -18.670  83.451  1.00 23.17           C  
ANISOU 4414  CG2 VAL C 161     3583   2636   2586     70    740    -81       C  
ATOM   4415  N   VAL C 162      18.216 -15.386  80.641  1.00 19.61           N  
ANISOU 4415  N   VAL C 162     2762   2648   2042   -109   1154     80       N  
ATOM   4416  CA  VAL C 162      18.821 -14.915  79.403  1.00 21.53           C  
ANISOU 4416  CA  VAL C 162     2996   3035   2149   -162   1322    126       C  
ATOM   4417  C   VAL C 162      20.062 -15.743  79.128  1.00 25.94           C  
ANISOU 4417  C   VAL C 162     3481   3725   2652     -5   1479    -34       C  
ATOM   4418  O   VAL C 162      20.825 -16.059  80.053  1.00 23.15           O  
ANISOU 4418  O   VAL C 162     2968   3365   2464    104   1464   -143       O  
ATOM   4419  CB  VAL C 162      19.184 -13.417  79.492  1.00 23.87           C  
ANISOU 4419  CB  VAL C 162     3121   3374   2575   -315   1379    274       C  
ATOM   4420  CG1 VAL C 162      19.614 -12.896  78.127  1.00 27.25           C  
ANISOU 4420  CG1 VAL C 162     3591   3935   2827   -412   1536    370       C  
ATOM   4421  CG2 VAL C 162      18.032 -12.620  80.045  1.00 25.58           C  
ANISOU 4421  CG2 VAL C 162     3371   3447   2900   -417   1188    381       C  
ATOM   4422  N   HIS C 163      20.296 -16.046  77.845  1.00 25.48           N  
ANISOU 4422  N   HIS C 163     3541   3784   2356     21   1622    -60       N  
ATOM   4423  CA  HIS C 163      21.348 -16.957  77.398  1.00 33.45           C  
ANISOU 4423  CA  HIS C 163     4501   4933   3274    206   1766   -249       C  
ATOM   4424  C   HIS C 163      22.250 -16.252  76.383  1.00 34.60           C  
ANISOU 4424  C   HIS C 163     4499   5307   3342    130   1951   -182       C  
ATOM   4425  O   HIS C 163      22.193 -16.541  75.178  1.00 34.41           O  
ANISOU 4425  O   HIS C 163     4633   5382   3058    155   2016   -198       O  
ATOM   4426  CB  HIS C 163      20.748 -18.228  76.788  1.00 32.44           C  
ANISOU 4426  CB  HIS C 163     4670   4735   2920    353   1659   -380       C  
ATOM   4427  CG  HIS C 163      20.043 -19.117  77.775  1.00 30.25           C  
ANISOU 4427  CG  HIS C 163     4487   4242   2764    422   1386   -447       C  
ATOM   4428  ND1 HIS C 163      20.586 -20.300  78.233  1.00 31.10           N  
ANISOU 4428  ND1 HIS C 163     4603   4303   2911    627   1304   -648       N  
ATOM   4429  CD2 HIS C 163      18.829 -19.013  78.366  1.00 30.33           C  
ANISOU 4429  CD2 HIS C 163     4594   4068   2862    306   1184   -335       C  
ATOM   4430  CE1 HIS C 163      19.748 -20.875  79.079  1.00 25.10           C  
ANISOU 4430  CE1 HIS C 163     3966   3330   2241    611   1068   -629       C  
ATOM   4431  NE2 HIS C 163      18.671 -20.119  79.172  1.00 29.32           N  
ANISOU 4431  NE2 HIS C 163     4539   3794   2809    416   1015   -443       N  
ATOM   4432  N   PRO C 164      23.099 -15.327  76.833  1.00 31.05           N  
ANISOU 4432  N   PRO C 164     3757   4936   3106     38   2030   -103       N  
ATOM   4433  CA  PRO C 164      24.024 -14.671  75.902  1.00 35.95           C  
ANISOU 4433  CA  PRO C 164     4225   5775   3657    -43   2221    -17       C  
ATOM   4434  C   PRO C 164      25.046 -15.655  75.364  1.00 42.19           C  
ANISOU 4434  C   PRO C 164     4915   6767   4348    162   2377   -223       C  
ATOM   4435  O   PRO C 164      25.429 -16.624  76.027  1.00 36.87           O  
ANISOU 4435  O   PRO C 164     4170   6057   3783    370   2319   -437       O  
ATOM   4436  CB  PRO C 164      24.688 -13.589  76.756  1.00 38.11           C  
ANISOU 4436  CB  PRO C 164     4204   6034   4243   -170   2214     88       C  
ATOM   4437  CG  PRO C 164      24.583 -14.097  78.138  1.00 40.70           C  
ANISOU 4437  CG  PRO C 164     4469   6197   4800    -49   2066    -52       C  
ATOM   4438  CD  PRO C 164      23.318 -14.893  78.219  1.00 32.03           C  
ANISOU 4438  CD  PRO C 164     3681   4947   3543     18   1941   -100       C  
ATOM   4439  N   GLN C 165      25.472 -15.400  74.129  1.00 43.78           N  
ANISOU 4439  N   GLN C 165     5126   7178   4330    117   2564   -159       N  
ATOM   4440  CA  GLN C 165      26.391 -16.302  73.456  1.00 47.11           C  
ANISOU 4440  CA  GLN C 165     5466   7814   4619    318   2723   -362       C  
ATOM   4441  C   GLN C 165      27.701 -16.418  74.225  1.00 50.49           C  
ANISOU 4441  C   GLN C 165     5538   8289   5356    469   2801   -435       C  
ATOM   4442  O   GLN C 165      28.312 -15.410  74.594  1.00 49.52           O  
ANISOU 4442  O   GLN C 165     5156   8204   5456    318   2881   -280       O  
ATOM   4443  CB  GLN C 165      26.642 -15.821  72.029  1.00 53.18           C  
ANISOU 4443  CB  GLN C 165     6303   8797   5105    211   2934   -245       C  
ATOM   4444  CG  GLN C 165      25.685 -16.432  71.035  1.00 63.18           C  
ANISOU 4444  CG  GLN C 165     7959  10035   6010    229   2876   -324       C  
ATOM   4445  CD  GLN C 165      25.616 -17.943  71.178  1.00 73.59           C  
ANISOU 4445  CD  GLN C 165     9384  11270   7306    445   2777   -671       C  
ATOM   4446  OE1 GLN C 165      24.577 -18.497  71.550  1.00 74.36           O  
ANISOU 4446  OE1 GLN C 165     9736  11122   7396    497   2549   -706       O  
ATOM   4447  NE2 GLN C 165      26.729 -18.618  70.889  1.00 73.01           N  
ANISOU 4447  NE2 GLN C 165     9136  11335   7270    558   2937   -921       N  
ATOM   4448  N   GLY C 166      28.112 -17.658  74.478  1.00 49.82           N  
ANISOU 4448  N   GLY C 166     5478   8137   5314    773   2762   -655       N  
ATOM   4449  CA  GLY C 166      29.409 -17.930  75.080  1.00 54.90           C  
ANISOU 4449  CA  GLY C 166     5844   8737   6280    935   2882   -748       C  
ATOM   4450  C   GLY C 166      29.573 -17.347  76.463  1.00 53.03           C  
ANISOU 4450  C   GLY C 166     5361   8397   6392    838   2714   -732       C  
ATOM   4451  O   GLY C 166      30.664 -16.884  76.818  1.00 56.94           O  
ANISOU 4451  O   GLY C 166     5515   8963   7157    808   2781   -734       O  
ATOM   4452  N   ARG C 167      28.506 -17.343  77.247  1.00 46.25           N  
ANISOU 4452  N   ARG C 167     4681   7346   5546    770   2470   -725       N  
ATOM   4453  CA  ARG C 167      28.529 -16.831  78.607  1.00 46.41           C  
ANISOU 4453  CA  ARG C 167     4548   7203   5882    688   2274   -723       C  
ATOM   4454  C   ARG C 167      27.566 -17.673  79.422  1.00 42.85           C  
ANISOU 4454  C   ARG C 167     4355   6524   5403    795   2033   -843       C  
ATOM   4455  O   ARG C 167      26.660 -18.299  78.860  1.00 41.80           O  
ANISOU 4455  O   ARG C 167     4515   6363   5002    832   2014   -859       O  
ATOM   4456  CB  ARG C 167      28.137 -15.344  78.655  1.00 49.84           C  
ANISOU 4456  CB  ARG C 167     4917   7645   6375    380   2284   -473       C  
ATOM   4457  CG  ARG C 167      29.318 -14.379  78.789  1.00 58.06           C  
ANISOU 4457  CG  ARG C 167     5599   8784   7677    263   2371   -393       C  
ATOM   4458  CD  ARG C 167      29.177 -13.177  77.855  1.00 65.25           C  
ANISOU 4458  CD  ARG C 167     6511   9824   8455    -16   2517   -130       C  
ATOM   4459  NE  ARG C 167      28.045 -12.313  78.199  1.00 64.26           N  
ANISOU 4459  NE  ARG C 167     6575   9525   8317   -214   2353     37       N  
ATOM   4460  CZ  ARG C 167      27.594 -11.318  77.433  1.00 61.59           C  
ANISOU 4460  CZ  ARG C 167     6347   9223   7832   -449   2396    267       C  
ATOM   4461  NH1 ARG C 167      28.173 -11.058  76.267  1.00 61.36           N  
ANISOU 4461  NH1 ARG C 167     6265   9413   7635   -531   2620    372       N  
ATOM   4462  NH2 ARG C 167      26.558 -10.586  77.829  1.00 55.37           N  
ANISOU 4462  NH2 ARG C 167     5729   8248   7061   -587   2210    394       N  
ATOM   4463  N   PRO C 168      27.736 -17.724  80.741  1.00 45.54           N  
ANISOU 4463  N   PRO C 168     4609   6692   6003    849   1824   -930       N  
ATOM   4464  CA  PRO C 168      26.767 -18.440  81.563  1.00 38.52           C  
ANISOU 4464  CA  PRO C 168     3981   5586   5069    927   1594  -1010       C  
ATOM   4465  C   PRO C 168      25.406 -17.791  81.452  1.00 35.16           C  
ANISOU 4465  C   PRO C 168     3749   5102   4508    716   1613   -815       C  
ATOM   4466  O   PRO C 168      25.300 -16.571  81.226  1.00 32.68           O  
ANISOU 4466  O   PRO C 168     3326   4850   4242    508   1721   -622       O  
ATOM   4467  CB  PRO C 168      27.343 -18.309  82.980  1.00 32.01           C  
ANISOU 4467  CB  PRO C 168     3011   4605   4547   1003   1369  -1090       C  
ATOM   4468  CG  PRO C 168      28.801 -17.961  82.750  1.00 36.34           C  
ANISOU 4468  CG  PRO C 168     3222   5289   5297   1030   1468  -1134       C  
ATOM   4469  CD  PRO C 168      28.793 -17.106  81.556  1.00 37.82           C  
ANISOU 4469  CD  PRO C 168     3311   5696   5362    839   1759   -953       C  
ATOM   4470  N   PRO C 169      24.325 -18.570  81.575  1.00 34.27           N  
ANISOU 4470  N   PRO C 169     3959   4841   4221    748   1441   -805       N  
ATOM   4471  CA  PRO C 169      22.983 -17.979  81.657  1.00 30.15           C  
ANISOU 4471  CA  PRO C 169     3622   4221   3614    554   1367   -588       C  
ATOM   4472  C   PRO C 169      22.889 -16.974  82.795  1.00 30.04           C  
ANISOU 4472  C   PRO C 169     3489   4115   3811    455   1267   -476       C  
ATOM   4473  O   PRO C 169      23.516 -17.141  83.843  1.00 26.16           O  
ANISOU 4473  O   PRO C 169     2906   3540   3492    570   1142   -577       O  
ATOM   4474  CB  PRO C 169      22.076 -19.188  81.914  1.00 25.14           C  
ANISOU 4474  CB  PRO C 169     3284   3414   2853    636   1170   -643       C  
ATOM   4475  CG  PRO C 169      22.838 -20.344  81.413  1.00 31.92           C  
ANISOU 4475  CG  PRO C 169     4173   4319   3636    853   1180   -866       C  
ATOM   4476  CD  PRO C 169      24.285 -20.040  81.626  1.00 37.30           C  
ANISOU 4476  CD  PRO C 169     4539   5129   4505    959   1292   -997       C  
ATOM   4477  N   ASN C 170      22.097 -15.917  82.561  1.00 28.91           N  
ANISOU 4477  N   ASN C 170     3366   3972   3645    259   1293   -281       N  
ATOM   4478  CA  ASN C 170      21.775 -14.898  83.554  1.00 23.47           C  
ANISOU 4478  CA  ASN C 170     2609   3186   3121    171   1177   -175       C  
ATOM   4479  C   ASN C 170      20.363 -15.167  84.065  1.00 18.54           C  
ANISOU 4479  C   ASN C 170     2211   2424   2410    138   1038   -112       C  
ATOM   4480  O   ASN C 170      19.392 -15.039  83.312  1.00 19.22           O  
ANISOU 4480  O   ASN C 170     2415   2514   2373     28   1057    -16       O  
ATOM   4481  CB  ASN C 170      21.869 -13.491  82.950  1.00 21.02           C  
ANISOU 4481  CB  ASN C 170     2159   2957   2871    -17   1276    -12       C  
ATOM   4482  CG  ASN C 170      23.238 -13.193  82.345  1.00 28.18           C  
ANISOU 4482  CG  ASN C 170     2815   4021   3873    -32   1467    -43       C  
ATOM   4483  OD1 ASN C 170      24.276 -13.575  82.890  1.00 33.84           O  
ANISOU 4483  OD1 ASN C 170     3351   4751   4757    102   1457   -192       O  
ATOM   4484  ND2 ASN C 170      23.243 -12.506  81.216  1.00 28.12           N  
ANISOU 4484  ND2 ASN C 170     2796   4127   3763   -198   1636     98       N  
ATOM   4485  N   VAL C 171      20.245 -15.512  85.341  1.00 18.04           N  
ANISOU 4485  N   VAL C 171     2206   2235   2414    229    900   -164       N  
ATOM   4486  CA  VAL C 171      18.988 -15.947  85.943  1.00 16.43           C  
ANISOU 4486  CA  VAL C 171     2199   1911   2131    201    810   -114       C  
ATOM   4487  C   VAL C 171      18.416 -14.799  86.760  1.00 22.65           C  
ANISOU 4487  C   VAL C 171     2934   2658   3015    133    758    -22       C  
ATOM   4488  O   VAL C 171      19.102 -14.246  87.628  1.00 27.63           O  
ANISOU 4488  O   VAL C 171     3476   3258   3765    204    691    -60       O  
ATOM   4489  CB  VAL C 171      19.198 -17.183  86.840  1.00 19.04           C  
ANISOU 4489  CB  VAL C 171     2687   2122   2426    345    706   -220       C  
ATOM   4490  CG1 VAL C 171      17.872 -17.611  87.474  1.00 21.36           C  
ANISOU 4490  CG1 VAL C 171     3172   2300   2642    276    658   -136       C  
ATOM   4491  CG2 VAL C 171      19.815 -18.347  86.058  1.00 22.56           C  
ANISOU 4491  CG2 VAL C 171     3189   2591   2793    451    715   -347       C  
ATOM   4492  N   PHE C 172      17.150 -14.464  86.513  1.00 19.09           N  
ANISOU 4492  N   PHE C 172     2538   2192   2523     16    763     76       N  
ATOM   4493  CA  PHE C 172      16.471 -13.389  87.226  1.00 21.67           C  
ANISOU 4493  CA  PHE C 172     2812   2487   2935    -28    710    137       C  
ATOM   4494  C   PHE C 172      15.186 -13.949  87.800  1.00 20.01           C  
ANISOU 4494  C   PHE C 172     2725   2212   2668    -51    710    159       C  
ATOM   4495  O   PHE C 172      14.329 -14.433  87.051  1.00 22.79           O  
ANISOU 4495  O   PHE C 172     3129   2558   2974   -140    730    198       O  
ATOM   4496  CB  PHE C 172      16.167 -12.196  86.309  1.00 29.33           C  
ANISOU 4496  CB  PHE C 172     3679   3505   3959   -155    707    228       C  
ATOM   4497  CG  PHE C 172      17.390 -11.527  85.740  1.00 27.42           C  
ANISOU 4497  CG  PHE C 172     3302   3330   3787   -180    739    245       C  
ATOM   4498  CD1 PHE C 172      17.910 -10.388  86.333  1.00 21.80           C  
ANISOU 4498  CD1 PHE C 172     2458   2588   3235   -178    655    262       C  
ATOM   4499  CD2 PHE C 172      17.995 -12.015  84.592  1.00 22.36           C  
ANISOU 4499  CD2 PHE C 172     2663   2781   3054   -210    857    245       C  
ATOM   4500  CE1 PHE C 172      19.026  -9.761  85.806  1.00 23.21           C  
ANISOU 4500  CE1 PHE C 172     2483   2820   3516   -237    693    298       C  
ATOM   4501  CE2 PHE C 172      19.112 -11.398  84.059  1.00 27.26           C  
ANISOU 4501  CE2 PHE C 172     3131   3485   3743   -257    938    274       C  
ATOM   4502  CZ  PHE C 172      19.635 -10.267  84.672  1.00 21.88           C  
ANISOU 4502  CZ  PHE C 172     2291   2765   3257   -287    858    311       C  
ATOM   4503  N   ALA C 173      15.060 -13.887  89.125  1.00 25.13           N  
ANISOU 4503  N   ALA C 173     3422   2807   3319     27    687    135       N  
ATOM   4504  CA  ALA C 173      13.880 -14.346  89.845  1.00 24.65           C  
ANISOU 4504  CA  ALA C 173     3460   2704   3204     -4    736    168       C  
ATOM   4505  C   ALA C 173      13.074 -13.127  90.278  1.00 27.50           C  
ANISOU 4505  C   ALA C 173     3708   3095   3644    -20    736    186       C  
ATOM   4506  O   ALA C 173      13.421 -12.485  91.278  1.00 33.14           O  
ANISOU 4506  O   ALA C 173     4430   3796   4365     91    695    142       O  
ATOM   4507  CB  ALA C 173      14.292 -15.185  91.056  1.00 21.64           C  
ANISOU 4507  CB  ALA C 173     3263   2242   2718    104    730    131       C  
ATOM   4508  N   PRO C 174      12.022 -12.748  89.568  1.00 33.80           N  
ANISOU 4508  N   PRO C 174     4410   3920   4514   -130    745    227       N  
ATOM   4509  CA  PRO C 174      11.362 -11.475  89.851  1.00 35.31           C  
ANISOU 4509  CA  PRO C 174     4473   4133   4810   -117    701    213       C  
ATOM   4510  C   PRO C 174      10.286 -11.631  90.914  1.00 33.51           C  
ANISOU 4510  C   PRO C 174     4248   3919   4565    -92    810    192       C  
ATOM   4511  O   PRO C 174       9.744 -12.711  91.141  1.00 36.67           O  
ANISOU 4511  O   PRO C 174     4721   4307   4903   -154    927    228       O  
ATOM   4512  CB  PRO C 174      10.747 -11.096  88.495  1.00 34.80           C  
ANISOU 4512  CB  PRO C 174     4319   4070   4832   -240    631    255       C  
ATOM   4513  CG  PRO C 174      10.433 -12.428  87.862  1.00 42.30           C  
ANISOU 4513  CG  PRO C 174     5357   4998   5716   -323    688    286       C  
ATOM   4514  CD  PRO C 174      11.363 -13.473  88.469  1.00 39.94           C  
ANISOU 4514  CD  PRO C 174     5199   4685   5291   -252    756    269       C  
ATOM   4515  N   ALA C 175      10.002 -10.516  91.574  1.00 22.47           N  
ANISOU 4515  N   ALA C 175     2769   2544   3224      1    772    133       N  
ATOM   4516  CA  ALA C 175       8.952 -10.420  92.571  1.00 24.58           C  
ANISOU 4516  CA  ALA C 175     3005   2860   3476     50    902     90       C  
ATOM   4517  C   ALA C 175       7.967  -9.336  92.154  1.00 24.79           C  
ANISOU 4517  C   ALA C 175     2822   2914   3684     43    823     34       C  
ATOM   4518  O   ALA C 175       8.190  -8.589  91.191  1.00 27.27           O  
ANISOU 4518  O   ALA C 175     3065   3187   4112      7    639     42       O  
ATOM   4519  CB  ALA C 175       9.532 -10.106  93.956  1.00 25.08           C  
ANISOU 4519  CB  ALA C 175     3205   2922   3404    233    915     25       C  
ATOM   4520  N   TYR C 176       6.878  -9.235  92.905  1.00 23.51           N  
ANISOU 4520  N   TYR C 176     2567   2820   3545     84    964    -25       N  
ATOM   4521  CA  TYR C 176       5.862  -8.248  92.581  1.00 22.28           C  
ANISOU 4521  CA  TYR C 176     2189   2688   3590    106    877   -115       C  
ATOM   4522  C   TYR C 176       6.483  -6.862  92.499  1.00 18.43           C  
ANISOU 4522  C   TYR C 176     1697   2145   3162    234    623   -185       C  
ATOM   4523  O   TYR C 176       7.262  -6.468  93.366  1.00 27.61           O  
ANISOU 4523  O   TYR C 176     2977   3298   4216    378    591   -228       O  
ATOM   4524  CB  TYR C 176       4.753  -8.245  93.627  1.00 23.47           C  
ANISOU 4524  CB  TYR C 176     2223   2949   3744    179   1101   -202       C  
ATOM   4525  CG  TYR C 176       3.684  -7.222  93.294  1.00 27.32           C  
ANISOU 4525  CG  TYR C 176     2446   3458   4476    232    988   -334       C  
ATOM   4526  CD1 TYR C 176       2.672  -7.521  92.394  1.00 24.47           C  
ANISOU 4526  CD1 TYR C 176     1883   3080   4334     87    963   -325       C  
ATOM   4527  CD2 TYR C 176       3.701  -5.961  93.857  1.00 26.54           C  
ANISOU 4527  CD2 TYR C 176     2309   3372   4405    442    860   -483       C  
ATOM   4528  CE1 TYR C 176       1.705  -6.606  92.083  1.00 29.08           C  
ANISOU 4528  CE1 TYR C 176     2223   3663   5165    152    820   -466       C  
ATOM   4529  CE2 TYR C 176       2.726  -5.034  93.554  1.00 24.90           C  
ANISOU 4529  CE2 TYR C 176     1862   3165   4432    514    720   -626       C  
ATOM   4530  CZ  TYR C 176       1.734  -5.363  92.660  1.00 25.19           C  
ANISOU 4530  CZ  TYR C 176     1691   3188   4693    369    700   -619       C  
ATOM   4531  OH  TYR C 176       0.758  -4.449  92.340  1.00 26.83           O  
ANISOU 4531  OH  TYR C 176     1655   3376   5163    455    520   -782       O  
ATOM   4532  N   GLY C 177       6.124  -6.114  91.460  1.00 18.71           N  
ANISOU 4532  N   GLY C 177     1614   2117   3376    178    411   -193       N  
ATOM   4533  CA  GLY C 177       6.593  -4.747  91.342  1.00 18.24           C  
ANISOU 4533  CA  GLY C 177     1553   1977   3401    273    142   -244       C  
ATOM   4534  C   GLY C 177       7.974  -4.585  90.742  1.00 21.71           C  
ANISOU 4534  C   GLY C 177     2123   2336   3791    200      9   -129       C  
ATOM   4535  O   GLY C 177       8.351  -3.458  90.406  1.00 21.35           O  
ANISOU 4535  O   GLY C 177     2072   2196   3846    217   -234   -129       O  
ATOM   4536  N   THR C 178       8.749  -5.657  90.596  1.00 20.98           N  
ANISOU 4536  N   THR C 178     2139   2271   3562    118    156    -33       N  
ATOM   4537  CA  THR C 178      10.020  -5.495  89.912  1.00 17.65           C  
ANISOU 4537  CA  THR C 178     1787   1795   3123     43     58     63       C  
ATOM   4538  C   THR C 178       9.783  -5.372  88.414  1.00 20.48           C  
ANISOU 4538  C   THR C 178     2134   2116   3532   -123    -31    159       C  
ATOM   4539  O   THR C 178       8.729  -5.736  87.888  1.00 20.47           O  
ANISOU 4539  O   THR C 178     2095   2119   3563   -182    -14    151       O  
ATOM   4540  CB  THR C 178      10.973  -6.660  90.198  1.00 24.50           C  
ANISOU 4540  CB  THR C 178     2763   2702   3845     39    220    102       C  
ATOM   4541  OG1 THR C 178      10.407  -7.880  89.691  1.00 23.99           O  
ANISOU 4541  OG1 THR C 178     2729   2680   3704    -61    375    146       O  
ATOM   4542  CG2 THR C 178      11.239  -6.787  91.701  1.00 20.81           C  
ANISOU 4542  CG2 THR C 178     2369   2243   3293    212    274     13       C  
ATOM   4543  N   VAL C 179      10.795  -4.857  87.725  1.00 20.18           N  
ANISOU 4543  N   VAL C 179     2468   2039   3160    104    -63   -834       N  
ATOM   4544  CA  VAL C 179      10.721  -4.569  86.300  1.00 22.80           C  
ANISOU 4544  CA  VAL C 179     2865   2196   3602    147    -56   -661       C  
ATOM   4545  C   VAL C 179      12.024  -5.048  85.674  1.00 20.92           C  
ANISOU 4545  C   VAL C 179     2647   1921   3382     48     15   -448       C  
ATOM   4546  O   VAL C 179      13.108  -4.625  86.097  1.00 24.47           O  
ANISOU 4546  O   VAL C 179     3039   2296   3962    -42    -10   -449       O  
ATOM   4547  CB  VAL C 179      10.517  -3.061  86.029  1.00 24.46           C  
ANISOU 4547  CB  VAL C 179     3113   2144   4039    208   -158   -725       C  
ATOM   4548  CG1 VAL C 179      10.677  -2.762  84.557  1.00 21.46           C  
ANISOU 4548  CG1 VAL C 179     2857   1580   3718    218   -156   -469       C  
ATOM   4549  CG2 VAL C 179       9.142  -2.594  86.520  1.00 21.00           C  
ANISOU 4549  CG2 VAL C 179     2614   1728   3636    354   -216   -968       C  
ATOM   4550  N   ILE C 180      11.927  -5.924  84.678  1.00 18.00           N  
ANISOU 4550  N   ILE C 180     2337   1600   2904     67    101   -297       N  
ATOM   4551  CA  ILE C 180      13.092  -6.408  83.945  1.00 18.44           C  
ANISOU 4551  CA  ILE C 180     2399   1631   2975      3    222   -127       C  
ATOM   4552  C   ILE C 180      13.170  -5.669  82.615  1.00 20.70           C  
ANISOU 4552  C   ILE C 180     2822   1762   3282     10    284     33       C  
ATOM   4553  O   ILE C 180      12.159  -5.494  81.918  1.00 18.01           O  
ANISOU 4553  O   ILE C 180     2612   1394   2838     99    219     56       O  
ATOM   4554  CB  ILE C 180      13.052  -7.938  83.748  1.00 18.39           C  
ANISOU 4554  CB  ILE C 180     2392   1773   2822     26    291    -97       C  
ATOM   4555  CG1 ILE C 180      13.173  -8.645  85.104  1.00 17.97           C  
ANISOU 4555  CG1 ILE C 180     2235   1845   2750     -8    225   -180       C  
ATOM   4556  CG2 ILE C 180      14.216  -8.396  82.842  1.00 18.60           C  
ANISOU 4556  CG2 ILE C 180     2415   1769   2883     -1    454     33       C  
ATOM   4557  CD1 ILE C 180      12.868 -10.180  85.108  1.00 19.06           C  
ANISOU 4557  CD1 ILE C 180     2384   2080   2776      9    250   -147       C  
ATOM   4558  N   VAL C 181      14.361  -5.186  82.291  1.00 20.66           N  
ANISOU 4558  N   VAL C 181     2781   1650   3419    -94    395    156       N  
ATOM   4559  CA  VAL C 181      14.649  -4.597  80.994  1.00 24.33           C  
ANISOU 4559  CA  VAL C 181     3396   1989   3861   -130    522    371       C  
ATOM   4560  C   VAL C 181      15.730  -5.444  80.356  1.00 22.18           C  
ANISOU 4560  C   VAL C 181     3072   1820   3537   -186    776    468       C  
ATOM   4561  O   VAL C 181      16.701  -5.826  81.021  1.00 25.15           O  
ANISOU 4561  O   VAL C 181     3226   2240   4090   -248    828    410       O  
ATOM   4562  CB  VAL C 181      15.108  -3.132  81.107  1.00 24.10           C  
ANISOU 4562  CB  VAL C 181     3356   1703   4098   -237    482    452       C  
ATOM   4563  CG1 VAL C 181      15.226  -2.532  79.726  1.00 25.75           C  
ANISOU 4563  CG1 VAL C 181     3781   1776   4226   -282    612    734       C  
ATOM   4564  CG2 VAL C 181      14.145  -2.320  81.968  1.00 23.11           C  
ANISOU 4564  CG2 VAL C 181     3232   1463   4087   -156    229    268       C  
ATOM   4565  N   THR C 182      15.565  -5.745  79.081  1.00 22.58           N  
ANISOU 4565  N   THR C 182     3322   1914   3344   -148    919    595       N  
ATOM   4566  CA  THR C 182      16.509  -6.642  78.452  1.00 23.48           C  
ANISOU 4566  CA  THR C 182     3386   2148   3387   -166   1194    625       C  
ATOM   4567  C   THR C 182      16.615  -6.284  76.980  1.00 26.31           C  
ANISOU 4567  C   THR C 182     4003   2499   3496   -193   1409    828       C  
ATOM   4568  O   THR C 182      15.641  -5.841  76.368  1.00 31.03           O  
ANISOU 4568  O   THR C 182     4871   3051   3870   -135   1264    913       O  
ATOM   4569  CB  THR C 182      16.075  -8.103  78.703  1.00 25.79           C  
ANISOU 4569  CB  THR C 182     3651   2594   3555    -42   1130    443       C  
ATOM   4570  OG1 THR C 182      17.001  -9.002  78.091  1.00 27.34           O  
ANISOU 4570  OG1 THR C 182     3788   2878   3723    -24   1392    426       O  
ATOM   4571  CG2 THR C 182      14.668  -8.354  78.182  1.00 24.64           C  
ANISOU 4571  CG2 THR C 182     3742   2483   3135     64    959    400       C  
ATOM   4572  N   SER C 183      17.831  -6.390  76.449  1.00 30.63           N  
ANISOU 4572  N   SER C 183     4455   3089   4095   -287   1751    918       N  
ATOM   4573  CA  SER C 183      18.078  -6.258  75.021  1.00 38.09           C  
ANISOU 4573  CA  SER C 183     5655   4093   4724   -321   2044   1101       C  
ATOM   4574  C   SER C 183      17.592  -7.491  74.260  1.00 43.46           C  
ANISOU 4574  C   SER C 183     6534   4964   5016   -159   2090    949       C  
ATOM   4575  O   SER C 183      17.819  -8.630  74.676  1.00 44.32           O  
ANISOU 4575  O   SER C 183     6460   5164   5216    -68   2104    722       O  
ATOM   4576  CB  SER C 183      19.568  -6.060  74.769  1.00 37.98           C  
ANISOU 4576  CB  SER C 183     5378   4134   4920   -451   2315   1135       C  
ATOM   4577  OG  SER C 183      19.857  -6.279  73.404  1.00 45.92           O  
ANISOU 4577  OG  SER C 183     6574   5297   5577   -446   2552   1198       O  
ATOM   4578  N   CYS C 184      16.949  -7.261  73.116  1.00 47.60           N  
ANISOU 4578  N   CYS C 184     7425   5534   5127   -121   2051   1057       N  
ATOM   4579  CA  CYS C 184      16.341  -8.337  72.338  1.00 49.92           C  
ANISOU 4579  CA  CYS C 184     7950   5986   5032     28   2012    883       C  
ATOM   4580  C   CYS C 184      17.344  -9.098  71.481  1.00 51.35           C  
ANISOU 4580  C   CYS C 184     8067   6346   5097     35   2324    762       C  
ATOM   4581  O   CYS C 184      16.932  -9.930  70.664  1.00 51.26           O  
ANISOU 4581  O   CYS C 184     8260   6460   4756    144   2293    603       O  
ATOM   4582  CB  CYS C 184      15.215  -7.779  71.462  1.00 51.12           C  
ANISOU 4582  CB  CYS C 184     8497   6122   4805     77   1747   1019       C  
ATOM   4583  SG  CYS C 184      13.774  -7.232  72.417  1.00 48.03           S  
ANISOU 4583  SG  CYS C 184     8091   5547   4609    153   1238   1010       S  
ATOM   4584  N   ALA C 185      18.641  -8.839  71.659  1.00 39.09           N  
ANISOU 4584  N   ALA C 185     6218   4802   3832    -76   2595    812       N  
ATOM   4585  CA  ALA C 185      19.685  -9.552  70.939  1.00 42.50           C  
ANISOU 4585  CA  ALA C 185     6532   5400   4215    -58   2906    683       C  
ATOM   4586  C   ALA C 185      20.017 -10.910  71.542  1.00 40.64           C  
ANISOU 4586  C   ALA C 185     6047   5185   4210     81   2913    382       C  
ATOM   4587  O   ALA C 185      20.712 -11.693  70.893  1.00 43.61           O  
ANISOU 4587  O   ALA C 185     6354   5691   4524    147   3126    219       O  
ATOM   4588  CB  ALA C 185      20.962  -8.716  70.891  1.00 45.63           C  
ANISOU 4588  CB  ALA C 185     6679   5795   4863   -235   3174    854       C  
ATOM   4589  N   HIS C 186      19.573 -11.204  72.760  1.00 36.88           N  
ANISOU 4589  N   HIS C 186     5426   4582   4005    129   2686    310       N  
ATOM   4590  CA  HIS C 186      19.892 -12.464  73.417  1.00 36.23           C  
ANISOU 4590  CA  HIS C 186     5103   4483   4180    255   2644     67       C  
ATOM   4591  C   HIS C 186      18.652 -13.338  73.490  1.00 35.26           C  
ANISOU 4591  C   HIS C 186     5202   4334   3862    383   2395    -98       C  
ATOM   4592  O   HIS C 186      17.554 -12.851  73.779  1.00 31.45           O  
ANISOU 4592  O   HIS C 186     4910   3800   3240    365   2187    -16       O  
ATOM   4593  CB  HIS C 186      20.433 -12.245  74.831  1.00 38.78           C  
ANISOU 4593  CB  HIS C 186     5057   4689   4989    203   2549    107       C  
ATOM   4594  CG  HIS C 186      21.628 -11.346  74.894  1.00 44.65           C  
ANISOU 4594  CG  HIS C 186     5546   5425   5994     58   2720    247       C  
ATOM   4595  ND1 HIS C 186      22.841 -11.676  74.329  1.00 48.79           N  
ANISOU 4595  ND1 HIS C 186     5873   6036   6628     64   2974    180       N  
ATOM   4596  CD2 HIS C 186      21.794 -10.127  75.460  1.00 44.51           C  
ANISOU 4596  CD2 HIS C 186     5427   5312   6173   -103   2657    430       C  
ATOM   4597  CE1 HIS C 186      23.702 -10.697  74.542  1.00 51.27           C  
ANISOU 4597  CE1 HIS C 186     5971   6316   7194    -95   3066    326       C  
ATOM   4598  NE2 HIS C 186      23.093  -9.745  75.227  1.00 46.67           N  
ANISOU 4598  NE2 HIS C 186     5450   5611   6674   -201   2859    475       N  
ATOM   4599  N   ARG C 187      18.834 -14.627  73.225  1.00 37.34           N  
ANISOU 4599  N   ARG C 187     5427   4617   4142    512   2400   -343       N  
ATOM   4600  CA  ARG C 187      17.765 -15.582  73.460  1.00 31.83           C  
ANISOU 4600  CA  ARG C 187     4868   3845   3382    612   2129   -520       C  
ATOM   4601  C   ARG C 187      17.441 -15.630  74.948  1.00 31.57           C  
ANISOU 4601  C   ARG C 187     4642   3671   3683    596   1920   -472       C  
ATOM   4602  O   ARG C 187      18.319 -15.463  75.797  1.00 31.25           O  
ANISOU 4602  O   ARG C 187     4295   3589   3990    565   1968   -397       O  
ATOM   4603  CB  ARG C 187      18.179 -16.967  72.979  1.00 35.62           C  
ANISOU 4603  CB  ARG C 187     5299   4327   3910    746   2168   -793       C  
ATOM   4604  CG  ARG C 187      18.672 -17.049  71.545  1.00 44.76           C  
ANISOU 4604  CG  ARG C 187     6596   5659   4751    779   2411   -893       C  
ATOM   4605  CD  ARG C 187      19.255 -18.435  71.293  1.00 53.39           C  
ANISOU 4605  CD  ARG C 187     7560   6729   5997    942   2461  -1196       C  
ATOM   4606  NE  ARG C 187      20.518 -18.621  72.009  1.00 64.83           N  
ANISOU 4606  NE  ARG C 187     8624   8122   7886    980   2600  -1173       N  
ATOM   4607  CZ  ARG C 187      20.893 -19.751  72.610  1.00 71.38           C  
ANISOU 4607  CZ  ARG C 187     9255   8798   9066   1120   2483  -1332       C  
ATOM   4608  NH1 ARG C 187      20.092 -20.811  72.607  1.00 70.56           N  
ANISOU 4608  NH1 ARG C 187     9303   8559   8946   1221   2241  -1524       N  
ATOM   4609  NH2 ARG C 187      22.068 -19.815  73.228  1.00 71.48           N  
ANISOU 4609  NH2 ARG C 187     8918   8769   9472   1152   2575  -1285       N  
ATOM   4610  N   HIS C 188      16.173 -15.867  75.270  1.00 34.34           N  
ANISOU 4610  N   HIS C 188     5126   3972   3951    584   1585   -497       N  
ATOM   4611  CA  HIS C 188      15.759 -15.902  76.671  1.00 28.00           C  
ANISOU 4611  CA  HIS C 188     4135   3084   3419    523   1317   -421       C  
ATOM   4612  C   HIS C 188      14.574 -16.849  76.833  1.00 31.66           C  
ANISOU 4612  C   HIS C 188     4700   3476   3853    540   1050   -543       C  
ATOM   4613  O   HIS C 188      13.937 -17.250  75.853  1.00 27.41           O  
ANISOU 4613  O   HIS C 188     4385   2950   3081    587   1008   -684       O  
ATOM   4614  CB  HIS C 188      15.415 -14.501  77.175  1.00 27.49           C  
ANISOU 4614  CB  HIS C 188     4051   3056   3338    409   1226   -227       C  
ATOM   4615  CG  HIS C 188      14.377 -13.818  76.353  1.00 41.45           C  
ANISOU 4615  CG  HIS C 188     6083   4868   4797    399   1129   -189       C  
ATOM   4616  ND1 HIS C 188      14.679 -12.813  75.460  1.00 46.27           N  
ANISOU 4616  ND1 HIS C 188     6852   5525   5204    370   1290    -54       N  
ATOM   4617  CD2 HIS C 188      13.041 -14.013  76.266  1.00 44.00           C  
ANISOU 4617  CD2 HIS C 188     6532   5186   5001    413    868   -254       C  
ATOM   4618  CE1 HIS C 188      13.570 -12.405  74.872  1.00 47.49           C  
ANISOU 4618  CE1 HIS C 188     7244   5692   5109    389   1092    -28       C  
ATOM   4619  NE2 HIS C 188      12.561 -13.119  75.341  1.00 54.14           N  
ANISOU 4619  NE2 HIS C 188     8045   6509   6017    420    830   -168       N  
ATOM   4620  N   GLU C 189      14.282 -17.199  78.095  1.00 33.27           N  
ANISOU 4620  N   GLU C 189     4743   3607   4290    485    864   -483       N  
ATOM   4621  CA  GLU C 189      13.240 -18.163  78.434  1.00 19.91           C  
ANISOU 4621  CA  GLU C 189     3091   1823   2652    455    644   -558       C  
ATOM   4622  C   GLU C 189      12.647 -17.827  79.797  1.00 30.54           C  
ANISOU 4622  C   GLU C 189     4308   3189   4108    338    489   -411       C  
ATOM   4623  O   GLU C 189      13.229 -17.087  80.597  1.00 22.97           O  
ANISOU 4623  O   GLU C 189     3225   2286   3217    305    523   -286       O  
ATOM   4624  CB  GLU C 189      13.794 -19.598  78.473  1.00 21.52           C  
ANISOU 4624  CB  GLU C 189     3252   1855   3068    536    653   -675       C  
ATOM   4625  CG  GLU C 189      14.826 -19.795  79.574  1.00 25.11           C  
ANISOU 4625  CG  GLU C 189     3488   2246   3805    551    665   -544       C  
ATOM   4626  CD  GLU C 189      15.236 -21.249  79.759  1.00 28.35           C  
ANISOU 4626  CD  GLU C 189     3855   2429   4488    643    598   -624       C  
ATOM   4627  OE1 GLU C 189      14.414 -22.133  79.479  1.00 35.38           O  
ANISOU 4627  OE1 GLU C 189     4871   3183   5388    623    477   -732       O  
ATOM   4628  OE2 GLU C 189      16.375 -21.508  80.189  1.00 28.07           O  
ANISOU 4628  OE2 GLU C 189     3645   2324   4696    735    640   -584       O  
ATOM   4629  N   VAL C 190      11.497 -18.426  80.082  1.00 30.15           N  
ANISOU 4629  N   VAL C 190     4279   3095   4083    264    324   -443       N  
ATOM   4630  CA  VAL C 190      10.941 -18.415  81.428  1.00 22.98           C  
ANISOU 4630  CA  VAL C 190     3251   2210   3269    144    231   -316       C  
ATOM   4631  C   VAL C 190      10.887 -19.863  81.895  1.00 20.45           C  
ANISOU 4631  C   VAL C 190     2917   1717   3135     99    154   -295       C  
ATOM   4632  O   VAL C 190      10.264 -20.707  81.240  1.00 24.74           O  
ANISOU 4632  O   VAL C 190     3533   2140   3727     87     80   -420       O  
ATOM   4633  CB  VAL C 190       9.560 -17.746  81.470  1.00 25.93           C  
ANISOU 4633  CB  VAL C 190     3611   2689   3553     68    143   -343       C  
ATOM   4634  CG1 VAL C 190       9.055 -17.674  82.897  1.00 28.22           C  
ANISOU 4634  CG1 VAL C 190     3772   3048   3904    -56    126   -231       C  
ATOM   4635  CG2 VAL C 190       9.638 -16.339  80.850  1.00 30.40           C  
ANISOU 4635  CG2 VAL C 190     4227   3357   3966    138    181   -351       C  
ATOM   4636  N   ARG C 191      11.582 -20.161  82.989  1.00 25.49           N  
ANISOU 4636  N   ARG C 191     3480   2317   3888     77    141   -137       N  
ATOM   4637  CA  ARG C 191      11.609 -21.521  83.488  1.00 27.00           C  
ANISOU 4637  CA  ARG C 191     3684   2300   4275     37     44    -58       C  
ATOM   4638  C   ARG C 191      10.304 -21.856  84.191  1.00 25.34           C  
ANISOU 4638  C   ARG C 191     3470   2100   4056   -162    -20     40       C  
ATOM   4639  O   ARG C 191       9.516 -20.978  84.551  1.00 22.32           O  
ANISOU 4639  O   ARG C 191     3036   1919   3526   -249     22     52       O  
ATOM   4640  CB  ARG C 191      12.792 -21.744  84.426  1.00 30.16           C  
ANISOU 4640  CB  ARG C 191     4021   2647   4793     90     -1    111       C  
ATOM   4641  CG  ARG C 191      14.109 -21.633  83.698  1.00 37.19           C  
ANISOU 4641  CG  ARG C 191     4844   3493   5793    282     83     -4       C  
ATOM   4642  CD  ARG C 191      15.271 -22.118  84.522  1.00 37.95           C  
ANISOU 4642  CD  ARG C 191     4834   3475   6108    364    -25    135       C  
ATOM   4643  NE  ARG C 191      16.436 -22.322  83.670  1.00 36.72           N  
ANISOU 4643  NE  ARG C 191     4568   3232   6153    562     84    -25       N  
ATOM   4644  CZ  ARG C 191      17.694 -22.274  84.094  1.00 35.51           C  
ANISOU 4644  CZ  ARG C 191     4228   3050   6214    673     42     28       C  
ATOM   4645  NH1 ARG C 191      17.965 -22.018  85.374  1.00 31.57           N  
ANISOU 4645  NH1 ARG C 191     3674   2602   5719    608   -158    243       N  
ATOM   4646  NH2 ARG C 191      18.677 -22.478  83.234  1.00 36.37           N  
ANISOU 4646  NH2 ARG C 191     4196   3094   6528    852    200   -151       N  
ATOM   4647  N   THR C 192      10.106 -23.158  84.391  1.00 22.08           N  
ANISOU 4647  N   THR C 192     3098   1448   3844   -232   -109    107       N  
ATOM   4648  CA  THR C 192       8.823 -23.723  84.778  1.00 31.57           C  
ANISOU 4648  CA  THR C 192     4283   2600   5114   -450   -145    178       C  
ATOM   4649  C   THR C 192       8.222 -22.998  85.969  1.00 22.81           C  
ANISOU 4649  C   THR C 192     3101   1742   3825   -604    -56    354       C  
ATOM   4650  O   THR C 192       8.894 -22.773  86.975  1.00 30.55           O  
ANISOU 4650  O   THR C 192     4109   2804   4694   -600    -44    541       O  
ATOM   4651  CB  THR C 192       9.008 -25.211  85.109  1.00 26.18           C  
ANISOU 4651  CB  THR C 192     3669   1574   4702   -516   -257    316       C  
ATOM   4652  OG1 THR C 192       9.534 -25.882  83.962  1.00 31.76           O  
ANISOU 4652  OG1 THR C 192     4439   2039   5587   -347   -326     80       O  
ATOM   4653  CG2 THR C 192       7.692 -25.864  85.527  1.00 28.19           C  
ANISOU 4653  CG2 THR C 192     3888   1745   5077   -791   -269    424       C  
ATOM   4654  N   VAL C 193       6.942 -22.654  85.849  1.00 29.10           N  
ANISOU 4654  N   VAL C 193     3794   2663   4599   -731     -3    269       N  
ATOM   4655  CA  VAL C 193       6.214 -22.082  86.974  1.00 28.19           C  
ANISOU 4655  CA  VAL C 193     3585   2787   4339   -884    130    391       C  
ATOM   4656  C   VAL C 193       5.894 -23.209  87.940  1.00 28.45           C  
ANISOU 4656  C   VAL C 193     3653   2698   4459  -1112    160    663       C  
ATOM   4657  O   VAL C 193       5.280 -24.212  87.559  1.00 38.51           O  
ANISOU 4657  O   VAL C 193     4900   3747   5985  -1246    106    669       O  
ATOM   4658  CB  VAL C 193       4.948 -21.356  86.500  1.00 24.79           C  
ANISOU 4658  CB  VAL C 193     2977   2517   3924   -922    179    191       C  
ATOM   4659  CG1 VAL C 193       4.171 -20.810  87.680  1.00 24.01           C  
ANISOU 4659  CG1 VAL C 193     2747   2672   3702  -1066    368    273       C  
ATOM   4660  CG2 VAL C 193       5.327 -20.218  85.549  1.00 24.77           C  
ANISOU 4660  CG2 VAL C 193     2994   2601   3815   -696    122    -15       C  
ATOM   4661  N   ARG C 194       6.320 -23.057  89.195  1.00 28.66           N  
ANISOU 4661  N   ARG C 194     3762   2858   4272  -1167    228    897       N  
ATOM   4662  CA  ARG C 194       6.274 -24.156  90.149  1.00 36.95           C  
ANISOU 4662  CA  ARG C 194     4924   3766   5348  -1367    230   1235       C  
ATOM   4663  C   ARG C 194       5.101 -24.081  91.113  1.00 45.18           C  
ANISOU 4663  C   ARG C 194     5888   5030   6247  -1640    472   1375       C  
ATOM   4664  O   ARG C 194       4.844 -25.062  91.820  1.00 54.38           O  
ANISOU 4664  O   ARG C 194     7145   6079   7440  -1801    520   1626       O  
ATOM   4665  CB  ARG C 194       7.586 -24.236  90.946  1.00 43.16           C  
ANISOU 4665  CB  ARG C 194     5898   4530   5970  -1257    100   1454       C  
ATOM   4666  CG  ARG C 194       8.739 -24.868  90.158  1.00 49.47           C  
ANISOU 4666  CG  ARG C 194     6755   5006   7034  -1041   -126   1406       C  
ATOM   4667  CD  ARG C 194       9.833 -25.446  91.049  1.00 59.19           C  
ANISOU 4667  CD  ARG C 194     8146   6101   8241   -986   -315   1707       C  
ATOM   4668  NE  ARG C 194      11.057 -24.651  90.981  1.00 67.26           N  
ANISOU 4668  NE  ARG C 194     9132   7234   9191   -744   -419   1587       N  
ATOM   4669  CZ  ARG C 194      11.678 -24.125  92.035  1.00 78.82           C  
ANISOU 4669  CZ  ARG C 194    10666   8890  10393   -725   -507   1736       C  
ATOM   4670  NH1 ARG C 194      11.201 -24.322  93.261  1.00 81.97           N  
ANISOU 4670  NH1 ARG C 194    11224   9416  10505   -922   -486   2022       N  
ATOM   4671  NH2 ARG C 194      12.787 -23.408  91.865  1.00 82.58           N  
ANISOU 4671  NH2 ARG C 194    11057   9434  10886   -522   -615   1595       N  
ATOM   4672  N   ALA C 195       4.387 -22.960  91.165  1.00 43.63           N  
ANISOU 4672  N   ALA C 195     5521   5150   5907  -1626    646   1162       N  
ATOM   4673  CA  ALA C 195       3.191 -22.903  91.991  1.00 51.48           C  
ANISOU 4673  CA  ALA C 195     6378   6369   6812  -1876    931   1240       C  
ATOM   4674  C   ALA C 195       2.362 -21.698  91.575  1.00 42.78           C  
ANISOU 4674  C   ALA C 195     5012   5518   5725  -1780   1053    890       C  
ATOM   4675  O   ALA C 195       2.853 -20.785  90.914  1.00 36.54           O  
ANISOU 4675  O   ALA C 195     4219   4757   4906  -1529    921    658       O  
ATOM   4676  CB  ALA C 195       3.533 -22.850  93.487  1.00 49.27           C  
ANISOU 4676  CB  ALA C 195     6295   6288   6139  -1909   1060   1476       C  
ATOM   4677  N   ASN C 196       1.095 -21.724  91.990  1.00 41.34           N  
ANISOU 4677  N   ASN C 196     4596   5491   5618  -1963   1300    871       N  
ATOM   4678  CA  ASN C 196       0.061 -20.745  91.673  1.00 43.97           C  
ANISOU 4678  CA  ASN C 196     4611   6036   6061  -1890   1415    556       C  
ATOM   4679  C   ASN C 196       0.192 -20.199  90.257  1.00 45.70           C  
ANISOU 4679  C   ASN C 196     4752   6121   6491  -1670   1147    268       C  
ATOM   4680  O   ASN C 196       0.138 -20.964  89.289  1.00 55.04           O  
ANISOU 4680  O   ASN C 196     5930   7039   7942  -1691    936    252       O  
ATOM   4681  CB  ASN C 196       0.069 -19.603  92.694  1.00 47.49           C  
ANISOU 4681  CB  ASN C 196     5074   6818   6150  -1772   1621    459       C  
ATOM   4682  CG  ASN C 196      -1.302 -18.944  92.849  1.00 56.05           C  
ANISOU 4682  CG  ASN C 196     5820   8103   7374  -1735   1811    235       C  
ATOM   4683  OD1 ASN C 196      -2.330 -19.505  92.457  1.00 51.52           O  
ANISOU 4683  OD1 ASN C 196     4993   7457   7125  -1848   1823    236       O  
ATOM   4684  ND2 ASN C 196      -1.319 -17.746  93.425  1.00 65.77           N  
ANISOU 4684  ND2 ASN C 196     7040   9567   8381  -1568   1932     30       N  
ATOM   4685  N   GLU C 197       0.371 -18.885  90.126  1.00 32.57           N  
ANISOU 4685  N   GLU C 197     3060   4617   4697  -1433   1127     45       N  
ATOM   4686  CA  GLU C 197       0.380 -18.241  88.827  1.00 29.54           C  
ANISOU 4686  CA  GLU C 197     2625   4126   4475  -1204    875   -189       C  
ATOM   4687  C   GLU C 197       1.409 -17.123  88.815  1.00 31.69           C  
ANISOU 4687  C   GLU C 197     3081   4448   4512   -964    803   -260       C  
ATOM   4688  O   GLU C 197       1.689 -16.504  89.842  1.00 28.01           O  
ANISOU 4688  O   GLU C 197     2665   4166   3814   -952    961   -252       O  
ATOM   4689  CB  GLU C 197      -1.002 -17.683  88.468  1.00 38.77           C  
ANISOU 4689  CB  GLU C 197     3427   5400   5903  -1186    904   -431       C  
ATOM   4690  CG  GLU C 197      -1.513 -16.638  89.431  1.00 49.90           C  
ANISOU 4690  CG  GLU C 197     4661   7093   7205  -1139   1167   -566       C  
ATOM   4691  CD  GLU C 197      -2.717 -15.876  88.891  1.00 62.31           C  
ANISOU 4691  CD  GLU C 197     5880   8717   9077  -1008   1105   -840       C  
ATOM   4692  OE1 GLU C 197      -3.228 -16.257  87.815  1.00 60.39           O  
ANISOU 4692  OE1 GLU C 197     5510   8315   9119  -1002    854   -904       O  
ATOM   4693  OE2 GLU C 197      -3.145 -14.894  89.541  1.00 67.44           O  
ANISOU 4693  OE2 GLU C 197     6436   9532   9656   -876   1250   -982       O  
ATOM   4694  N   ARG C 198       1.968 -16.880  87.632  1.00 26.57           N  
ANISOU 4694  N   ARG C 198     2541   3632   3921   -790    566   -334       N  
ATOM   4695  CA  ARG C 198       2.938 -15.821  87.388  1.00 25.16           C  
ANISOU 4695  CA  ARG C 198     2514   3452   3593   -585    486   -389       C  
ATOM   4696  C   ARG C 198       2.338 -14.919  86.323  1.00 22.82           C  
ANISOU 4696  C   ARG C 198     2118   3121   3431   -419    336   -582       C  
ATOM   4697  O   ARG C 198       2.037 -15.382  85.217  1.00 27.23           O  
ANISOU 4697  O   ARG C 198     2684   3552   4111   -397    163   -619       O  
ATOM   4698  CB  ARG C 198       4.274 -16.420  86.928  1.00 25.95           C  
ANISOU 4698  CB  ARG C 198     2853   3379   3627   -544    374   -252       C  
ATOM   4699  CG  ARG C 198       5.374 -15.447  86.498  1.00 27.32           C  
ANISOU 4699  CG  ARG C 198     3158   3519   3703   -367    304   -286       C  
ATOM   4700  CD  ARG C 198       6.363 -16.231  85.623  1.00 24.16           C  
ANISOU 4700  CD  ARG C 198     2911   2936   3332   -319    213   -211       C  
ATOM   4701  NE  ARG C 198       7.703 -15.657  85.502  1.00 27.05           N  
ANISOU 4701  NE  ARG C 198     3379   3271   3628   -213    208   -174       N  
ATOM   4702  CZ  ARG C 198       8.054 -14.771  84.568  1.00 28.86           C  
ANISOU 4702  CZ  ARG C 198     3658   3466   3840    -93    180   -240       C  
ATOM   4703  NH1 ARG C 198       7.155 -14.335  83.698  1.00 28.11           N  
ANISOU 4703  NH1 ARG C 198     3555   3367   3759    -40    111   -340       N  
ATOM   4704  NH2 ARG C 198       9.296 -14.321  84.500  1.00 28.07           N  
ANISOU 4704  NH2 ARG C 198     3611   3332   3723    -36    209   -190       N  
ATOM   4705  N   THR C 199       2.146 -13.646  86.659  1.00 21.65           N  
ANISOU 4705  N   THR C 199     1894   3071   3261   -296    375   -712       N  
ATOM   4706  CA  THR C 199       1.443 -12.698  85.800  1.00 27.61           C  
ANISOU 4706  CA  THR C 199     2537   3779   4176   -125    213   -875       C  
ATOM   4707  C   THR C 199       2.343 -11.511  85.514  1.00 26.56           C  
ANISOU 4707  C   THR C 199     2584   3562   3948     42    132   -878       C  
ATOM   4708  O   THR C 199       2.860 -10.892  86.445  1.00 23.86           O  
ANISOU 4708  O   THR C 199     2273   3285   3506     50    254   -904       O  
ATOM   4709  CB  THR C 199       0.148 -12.217  86.451  1.00 31.19           C  
ANISOU 4709  CB  THR C 199     2663   4381   4806   -118    330  -1061       C  
ATOM   4710  OG1 THR C 199      -0.800 -13.289  86.467  1.00 32.61           O  
ANISOU 4710  OG1 THR C 199     2628   4607   5154   -292    380  -1054       O  
ATOM   4711  CG2 THR C 199      -0.425 -11.026  85.696  1.00 31.50           C  
ANISOU 4711  CG2 THR C 199     2598   4337   5032    113    122  -1226       C  
ATOM   4712  N   SER C 200       2.520 -11.193  84.234  1.00 20.30           N  
ANISOU 4712  N   SER C 200     1289   2420   4005   -594     27   -404       N  
ATOM   4713  CA  SER C 200       3.490 -10.193  83.824  1.00 23.09           C  
ANISOU 4713  CA  SER C 200     1701   2751   4323   -507    -11   -384       C  
ATOM   4714  C   SER C 200       2.947  -9.365  82.669  1.00 22.34           C  
ANISOU 4714  C   SER C 200     1624   2588   4278   -304    -82   -652       C  
ATOM   4715  O   SER C 200       2.241  -9.883  81.797  1.00 27.55           O  
ANISOU 4715  O   SER C 200     2248   3172   5046   -200   -140   -802       O  
ATOM   4716  CB  SER C 200       4.817 -10.848  83.415  1.00 32.17           C  
ANISOU 4716  CB  SER C 200     2876   3775   5572   -468    -22   -151       C  
ATOM   4717  OG  SER C 200       4.625 -11.698  82.305  1.00 37.71           O  
ANISOU 4717  OG  SER C 200     3555   4288   6486   -347    -29   -247       O  
ATOM   4718  N   LEU C 201       3.282  -8.072  82.694  1.00 24.36           N  
ANISOU 4718  N   LEU C 201     1993   2872   4390   -245    -88   -684       N  
ATOM   4719  CA  LEU C 201       3.004  -7.128  81.618  1.00 23.69           C  
ANISOU 4719  CA  LEU C 201     2033   2702   4267    -19   -169   -836       C  
ATOM   4720  C   LEU C 201       4.268  -6.993  80.775  1.00 23.41           C  
ANISOU 4720  C   LEU C 201     2168   2559   4167     53   -178   -688       C  
ATOM   4721  O   LEU C 201       5.300  -6.542  81.278  1.00 23.83           O  
ANISOU 4721  O   LEU C 201     2278   2638   4136    -51   -120   -536       O  
ATOM   4722  CB  LEU C 201       2.594  -5.771  82.195  1.00 22.27           C  
ANISOU 4722  CB  LEU C 201     1893   2565   4003     -6   -134   -958       C  
ATOM   4723  CG  LEU C 201       1.902  -4.750  81.285  1.00 37.36           C  
ANISOU 4723  CG  LEU C 201     3891   4376   5928    251   -231  -1122       C  
ATOM   4724  CD1 LEU C 201       1.369  -3.607  82.118  1.00 41.23           C  
ANISOU 4724  CD1 LEU C 201     4372   4881   6414    249   -144  -1267       C  
ATOM   4725  CD2 LEU C 201       2.798  -4.205  80.184  1.00 41.88           C  
ANISOU 4725  CD2 LEU C 201     4706   4807   6399    379   -296  -1010       C  
ATOM   4726  N   VAL C 202       4.186  -7.362  79.498  1.00 22.75           N  
ANISOU 4726  N   VAL C 202     2160   2377   4106    206   -243   -748       N  
ATOM   4727  CA  VAL C 202       5.349  -7.403  78.615  1.00 21.73           C  
ANISOU 4727  CA  VAL C 202     2181   2156   3920    260   -203   -635       C  
ATOM   4728  C   VAL C 202       5.111  -6.432  77.462  1.00 20.09           C  
ANISOU 4728  C   VAL C 202     2182   1885   3565    430   -290   -727       C  
ATOM   4729  O   VAL C 202       4.030  -6.422  76.864  1.00 27.74           O  
ANISOU 4729  O   VAL C 202     3151   2860   4530    548   -423   -884       O  
ATOM   4730  CB  VAL C 202       5.618  -8.826  78.086  1.00 22.92           C  
ANISOU 4730  CB  VAL C 202     2275   2229   4203    259   -157   -620       C  
ATOM   4731  CG1 VAL C 202       6.771  -8.825  77.100  1.00 28.86           C  
ANISOU 4731  CG1 VAL C 202     3174   2892   4901    327    -69   -551       C  
ATOM   4732  CG2 VAL C 202       5.911  -9.789  79.230  1.00 23.85           C  
ANISOU 4732  CG2 VAL C 202     2206   2368   4485    105    -85   -463       C  
ATOM   4733  N   TYR C 203       6.113  -5.616  77.154  1.00 20.76           N  
ANISOU 4733  N   TYR C 203     2439   1920   3530    431   -227   -612       N  
ATOM   4734  CA  TYR C 203       6.007  -4.750  75.992  1.00 20.80           C  
ANISOU 4734  CA  TYR C 203     2686   1844   3372    574   -299   -644       C  
ATOM   4735  C   TYR C 203       7.383  -4.552  75.373  1.00 25.16           C  
ANISOU 4735  C   TYR C 203     3399   2342   3817    523   -160   -505       C  
ATOM   4736  O   TYR C 203       8.416  -4.792  76.002  1.00 23.23           O  
ANISOU 4736  O   TYR C 203     3051   2130   3645    387    -26   -381       O  
ATOM   4737  CB  TYR C 203       5.312  -3.418  76.324  1.00 20.38           C  
ANISOU 4737  CB  TYR C 203     2710   1750   3282    654   -385   -688       C  
ATOM   4738  CG  TYR C 203       5.864  -2.558  77.444  1.00 25.99           C  
ANISOU 4738  CG  TYR C 203     3423   2450   4001    515   -273   -625       C  
ATOM   4739  CD1 TYR C 203       6.431  -1.322  77.164  1.00 29.33           C  
ANISOU 4739  CD1 TYR C 203     4083   2745   4316    517   -233   -552       C  
ATOM   4740  CD2 TYR C 203       5.750  -2.937  78.779  1.00 18.51           C  
ANISOU 4740  CD2 TYR C 203     2266   1619   3147    357   -211   -649       C  
ATOM   4741  CE1 TYR C 203       6.916  -0.494  78.173  1.00 27.19           C  
ANISOU 4741  CE1 TYR C 203     3834   2455   4043    353   -130   -535       C  
ATOM   4742  CE2 TYR C 203       6.231  -2.109  79.804  1.00 22.45           C  
ANISOU 4742  CE2 TYR C 203     2792   2133   3603    192   -118   -624       C  
ATOM   4743  CZ  TYR C 203       6.814  -0.894  79.492  1.00 28.89           C  
ANISOU 4743  CZ  TYR C 203     3838   2814   4325    187    -78   -584       C  
ATOM   4744  OH  TYR C 203       7.298  -0.066  80.491  1.00 34.61           O  
ANISOU 4744  OH  TYR C 203     4604   3545   5000    -16     19   -596       O  
ATOM   4745  N   PHE C 204       7.375  -4.142  74.108  1.00 21.29           N  
ANISOU 4745  N   PHE C 204     3151   1789   3148    625   -199   -519       N  
ATOM   4746  CA  PHE C 204       8.560  -4.149  73.267  1.00 23.54           C  
ANISOU 4746  CA  PHE C 204     3593   2039   3311    574    -36   -429       C  
ATOM   4747  C   PHE C 204       8.763  -2.761  72.670  1.00 23.04           C  
ANISOU 4747  C   PHE C 204     3827   1887   3039    597    -51   -336       C  
ATOM   4748  O   PHE C 204       7.807  -2.130  72.214  1.00 25.39           O  
ANISOU 4748  O   PHE C 204     4276   2136   3233    735   -238   -368       O  
ATOM   4749  CB  PHE C 204       8.421  -5.209  72.173  1.00 29.10           C  
ANISOU 4749  CB  PHE C 204     4346   2755   3954    627    -19   -549       C  
ATOM   4750  CG  PHE C 204       8.163  -6.607  72.710  1.00 33.29           C  
ANISOU 4750  CG  PHE C 204     4615   3310   4723    601      6   -643       C  
ATOM   4751  CD1 PHE C 204       9.205  -7.504  72.872  1.00 34.34           C  
ANISOU 4751  CD1 PHE C 204     4616   3413   5020    537    217   -589       C  
ATOM   4752  CD2 PHE C 204       6.884  -7.006  73.062  1.00 33.35           C  
ANISOU 4752  CD2 PHE C 204     4497   3357   4818    642   -174   -771       C  
ATOM   4753  CE1 PHE C 204       8.976  -8.774  73.366  1.00 35.08           C  
ANISOU 4753  CE1 PHE C 204     4497   3475   5355    522    242   -642       C  
ATOM   4754  CE2 PHE C 204       6.646  -8.278  73.559  1.00 36.32           C  
ANISOU 4754  CE2 PHE C 204     4659   3726   5415    588   -135   -840       C  
ATOM   4755  CZ  PHE C 204       7.692  -9.165  73.708  1.00 34.21           C  
ANISOU 4755  CZ  PHE C 204     4303   3389   5305    531     70   -765       C  
ATOM   4756  N   TYR C 205      10.011  -2.291  72.687  1.00 27.09           N  
ANISOU 4756  N   TYR C 205     4408   2372   3511    460    140   -205       N  
ATOM   4757  CA  TYR C 205      10.388  -0.959  72.224  1.00 27.33           C  
ANISOU 4757  CA  TYR C 205     4731   2288   3366    424    175    -89       C  
ATOM   4758  C   TYR C 205      11.150  -1.049  70.907  1.00 29.06           C  
ANISOU 4758  C   TYR C 205     5172   2502   3366    385    328    -33       C  
ATOM   4759  O   TYR C 205      11.950  -1.965  70.708  1.00 34.96           O  
ANISOU 4759  O   TYR C 205     5780   3333   4171    316    515    -61       O  
ATOM   4760  CB  TYR C 205      11.275  -0.246  73.252  1.00 30.83           C  
ANISOU 4760  CB  TYR C 205     5095   2712   3908    229    301      6       C  
ATOM   4761  CG  TYR C 205      10.563   0.572  74.309  1.00 34.08           C  
ANISOU 4761  CG  TYR C 205     5485   3056   4409    234    185    -40       C  
ATOM   4762  CD1 TYR C 205      10.552   0.161  75.639  1.00 35.68           C  
ANISOU 4762  CD1 TYR C 205     5406   3375   4775    128    184    -91       C  
ATOM   4763  CD2 TYR C 205       9.928   1.766  73.988  1.00 32.87           C  
ANISOU 4763  CD2 TYR C 205     5603   2710   4177    339     94    -29       C  
ATOM   4764  CE1 TYR C 205       9.918   0.911  76.619  1.00 39.27           C  
ANISOU 4764  CE1 TYR C 205     5855   3780   5286    105    127   -175       C  
ATOM   4765  CE2 TYR C 205       9.290   2.528  74.969  1.00 37.99           C  
ANISOU 4765  CE2 TYR C 205     6227   3266   4942    354     38   -111       C  
ATOM   4766  CZ  TYR C 205       9.291   2.088  76.281  1.00 39.32           C  
ANISOU 4766  CZ  TYR C 205     6117   3577   5247    224     71   -207       C  
ATOM   4767  OH  TYR C 205       8.662   2.818  77.258  1.00 43.91           O  
ANISOU 4767  OH  TYR C 205     6685   4082   5918    214     59   -330       O  
ATOM   4768  N   SER C 206      10.915  -0.081  70.024  1.00 29.69           N  
ANISOU 4768  N   SER C 206     5603   2476   3203    429    264     53       N  
ATOM   4769  CA  SER C 206      11.601   0.013  68.741  1.00 29.69           C  
ANISOU 4769  CA  SER C 206     5880   2477   2923    357    423    124       C  
ATOM   4770  C   SER C 206      11.628   1.479  68.310  1.00 38.34           C  
ANISOU 4770  C   SER C 206     7345   3398   3825    330    388    313       C  
ATOM   4771  O   SER C 206      10.692   2.227  68.597  1.00 32.16           O  
ANISOU 4771  O   SER C 206     6651   2487   3083    475    155    352       O  
ATOM   4772  CB  SER C 206      10.903  -0.854  67.683  1.00 30.88           C  
ANISOU 4772  CB  SER C 206     6128   2724   2881    473    311     -4       C  
ATOM   4773  OG  SER C 206      11.452  -0.719  66.369  1.00 35.00           O  
ANISOU 4773  OG  SER C 206     6974   3268   3056    387    460     50       O  
ATOM   4774  N   ARG C 207      12.704   1.894  67.636  1.00 39.24           N  
ANISOU 4774  N   ARG C 207     7667   3486   3755    146    641    434       N  
ATOM   4775  CA  ARG C 207      12.704   3.214  67.017  1.00 39.50           C  
ANISOU 4775  CA  ARG C 207     8120   3328   3561    109    615    643       C  
ATOM   4776  C   ARG C 207      11.956   3.226  65.695  1.00 40.18           C  
ANISOU 4776  C   ARG C 207     8551   3428   3286    243    431    709       C  
ATOM   4777  O   ARG C 207      11.779   4.295  65.106  1.00 42.33           O  
ANISOU 4777  O   ARG C 207     9204   3528   3350    256    347    926       O  
ATOM   4778  CB  ARG C 207      14.126   3.706  66.781  1.00 38.30           C  
ANISOU 4778  CB  ARG C 207     8073   3147   3331   -182    969    762       C  
ATOM   4779  CG  ARG C 207      15.002   3.671  68.001  1.00 36.28           C  
ANISOU 4779  CG  ARG C 207     7459   2930   3395   -359   1138    712       C  
ATOM   4780  CD  ARG C 207      16.442   3.886  67.579  1.00 38.32           C  
ANISOU 4780  CD  ARG C 207     7746   3237   3578   -651   1503    799       C  
ATOM   4781  NE  ARG C 207      16.866   2.905  66.582  1.00 41.91           N  
ANISOU 4781  NE  ARG C 207     8181   3871   3872   -650   1703    723       N  
ATOM   4782  CZ  ARG C 207      17.043   3.154  65.284  1.00 48.54           C  
ANISOU 4782  CZ  ARG C 207     9397   4702   4344   -721   1844    804       C  
ATOM   4783  NH1 ARG C 207      16.852   4.372  64.781  1.00 45.25           N  
ANISOU 4783  NH1 ARG C 207     9315   4129   3748   -763   1734    964       N  
ATOM   4784  NH2 ARG C 207      17.428   2.175  64.481  1.00 55.83           N  
ANISOU 4784  NH2 ARG C 207    10273   5800   5139   -731   2059    673       N  
ATOM   4785  N   HIS C 208      11.526   2.070  65.214  1.00 39.08           N  
ANISOU 4785  N   HIS C 208     8303   3486   3060    328    359    535       N  
ATOM   4786  CA  HIS C 208      10.766   1.969  63.980  1.00 47.32           C  
ANISOU 4786  CA  HIS C 208     9649   4603   3727    425    144    565       C  
ATOM   4787  C   HIS C 208       9.284   1.933  64.310  1.00 47.15           C  
ANISOU 4787  C   HIS C 208     9501   4578   3835    692   -283    513       C  
ATOM   4788  O   HIS C 208       8.842   1.090  65.099  1.00 45.68           O  
ANISOU 4788  O   HIS C 208     8940   4479   3939    766   -343    303       O  
ATOM   4789  CB  HIS C 208      11.166   0.717  63.200  1.00 42.67           C  
ANISOU 4789  CB  HIS C 208     9031   4232   2948    322    335    358       C  
ATOM   4790  CG  HIS C 208      10.405   0.524  61.928  1.00 52.71           C  
ANISOU 4790  CG  HIS C 208    10619   5629   3779    369    108    349       C  
ATOM   4791  ND1 HIS C 208      10.392   1.461  60.916  1.00 58.33           N  
ANISOU 4791  ND1 HIS C 208    11803   6302   4060    319     29    605       N  
ATOM   4792  CD2 HIS C 208       9.648  -0.512  61.491  1.00 53.31           C  
ANISOU 4792  CD2 HIS C 208    10618   5881   3755    430    -65    118       C  
ATOM   4793  CE1 HIS C 208       9.656   1.013  59.914  1.00 60.17           C  
ANISOU 4793  CE1 HIS C 208    12231   6712   3919    351   -207    541       C  
ATOM   4794  NE2 HIS C 208       9.190  -0.180  60.240  1.00 56.77           N  
ANISOU 4794  NE2 HIS C 208    11468   6416   3686    410   -266    227       N  
ATOM   4795  N   ASN C 209       8.522   2.838  63.703  1.00 44.40           N  
ANISOU 4795  N   ASN C 209     9452   4130   3286    836   -576    719       N  
ATOM   4796  CA  ASN C 209       7.077   2.862  63.867  1.00 48.31           C  
ANISOU 4796  CA  ASN C 209     9811   4642   3902   1110  -1001    687       C  
ATOM   4797  C   ASN C 209       6.334   2.456  62.598  1.00 54.34           C  
ANISOU 4797  C   ASN C 209    10772   5605   4269   1171  -1298    699       C  
ATOM   4798  O   ASN C 209       5.098   2.486  62.584  1.00 55.26           O  
ANISOU 4798  O   ASN C 209    10765   5774   4459   1397  -1693    691       O  
ATOM   4799  CB  ASN C 209       6.621   4.254  64.326  1.00 53.70           C  
ANISOU 4799  CB  ASN C 209    10604   5032   4767   1291  -1162    913       C  
ATOM   4800  CG  ASN C 209       5.331   4.216  65.137  1.00 55.76           C  
ANISOU 4800  CG  ASN C 209    10517   5282   5388   1564  -1454    788       C  
ATOM   4801  OD1 ASN C 209       5.038   3.232  65.822  1.00 58.65           O  
ANISOU 4801  OD1 ASN C 209    10497   5817   5971   1554  -1431    523       O  
ATOM   4802  ND2 ASN C 209       4.557   5.298  65.067  1.00 54.49           N  
ANISOU 4802  ND2 ASN C 209    10348   4988   5366   1733  -1641    919       N  
ATOM   4803  N   GLY C 210       7.048   2.074  61.535  1.00 55.17           N  
ANISOU 4803  N   GLY C 210    11166   5845   3949    962  -1117    703       N  
ATOM   4804  CA  GLY C 210       6.424   1.587  60.320  1.00 54.34           C  
ANISOU 4804  CA  GLY C 210    11261   5976   3410    952  -1373    667       C  
ATOM   4805  C   GLY C 210       5.955   0.157  60.473  1.00 56.49           C  
ANISOU 4805  C   GLY C 210    11203   6470   3792    932  -1412    289       C  
ATOM   4806  O   GLY C 210       5.681  -0.317  61.583  1.00 54.42           O  
ANISOU 4806  O   GLY C 210    10519   6168   3990   1015  -1389    112       O  
ATOM   4807  N   ALA C 211       5.867  -0.553  59.353  1.00 55.05           N  
ANISOU 4807  N   ALA C 211    11224   6516   3175    790  -1454    153       N  
ATOM   4808  CA  ALA C 211       5.365  -1.919  59.388  1.00 54.13           C  
ANISOU 4808  CA  ALA C 211    10836   6584   3145    743  -1498   -226       C  
ATOM   4809  C   ALA C 211       6.452  -2.900  59.817  1.00 60.51           C  
ANISOU 4809  C   ALA C 211    11471   7347   4173    575   -983   -487       C  
ATOM   4810  O   ALA C 211       7.645  -2.694  59.569  1.00 58.70           O  
ANISOU 4810  O   ALA C 211    11428   7052   3823    430   -588   -421       O  
ATOM   4811  CB  ALA C 211       4.808  -2.331  58.030  1.00 61.29           C  
ANISOU 4811  CB  ALA C 211    11891   7756   3639    608  -1694   -303       C  
ATOM   4812  N   ASN C 212       6.019  -3.976  60.479  1.00 58.45           N  
ANISOU 4812  N   ASN C 212    10831   7113   4262    599   -990   -773       N  
ATOM   4813  CA  ASN C 212       6.903  -5.045  60.930  1.00 52.58           C  
ANISOU 4813  CA  ASN C 212     9879   6306   3793    483   -557  -1016       C  
ATOM   4814  C   ASN C 212       7.629  -5.646  59.735  1.00 53.62           C  
ANISOU 4814  C   ASN C 212    10319   6534   3520    274   -256  -1199       C  
ATOM   4815  O   ASN C 212       7.009  -6.282  58.875  1.00 53.40           O  
ANISOU 4815  O   ASN C 212    10435   6668   3187    182   -410  -1421       O  
ATOM   4816  CB  ASN C 212       6.097  -6.114  61.681  1.00 49.09           C  
ANISOU 4816  CB  ASN C 212     9043   5873   3735    533   -683  -1270       C  
ATOM   4817  CG  ASN C 212       6.975  -7.117  62.422  1.00 46.82           C  
ANISOU 4817  CG  ASN C 212     8490   5453   3845    472   -272  -1434       C  
ATOM   4818  OD1 ASN C 212       8.116  -7.372  62.036  1.00 51.96           O  
ANISOU 4818  OD1 ASN C 212     9258   6058   4426    368    117  -1476       O  
ATOM   4819  ND2 ASN C 212       6.433  -7.701  63.490  1.00 39.17           N  
ANISOU 4819  ND2 ASN C 212     7150   4426   3307    539   -357  -1514       N  
ATOM   4820  N   ARG C 213       8.948  -5.453  59.672  1.00 51.41           N  
ANISOU 4820  N   ARG C 213    10129   6170   3236    177    189  -1131       N  
ATOM   4821  CA  ARG C 213       9.706  -5.898  58.510  1.00 61.57           C  
ANISOU 4821  CA  ARG C 213    11676   7554   4164    -28    532  -1291       C  
ATOM   4822  C   ARG C 213       9.682  -7.413  58.316  1.00 57.33           C  
ANISOU 4822  C   ARG C 213    10917   7048   3818    -99    712  -1690       C  
ATOM   4823  O   ARG C 213      10.153  -7.888  57.277  1.00 58.75           O  
ANISOU 4823  O   ARG C 213    11208   7334   3781   -254    948  -1848       O  
ATOM   4824  CB  ARG C 213      11.151  -5.398  58.602  1.00 67.07           C  
ANISOU 4824  CB  ARG C 213    12411   8155   4920   -113    999  -1140       C  
ATOM   4825  CG  ARG C 213      11.311  -3.899  58.331  1.00 67.54           C  
ANISOU 4825  CG  ARG C 213    12770   8198   4696   -136    887   -747       C  
ATOM   4826  CD  ARG C 213      12.759  -3.541  58.027  1.00 61.33           C  
ANISOU 4826  CD  ARG C 213    12023   7379   3900   -311   1374   -653       C  
ATOM   4827  NE  ARG C 213      13.583  -3.561  59.229  1.00 58.46           N  
ANISOU 4827  NE  ARG C 213    11365   6868   3980   -266   1655   -629       N  
ATOM   4828  CZ  ARG C 213      14.904  -3.684  59.223  1.00 62.38           C  
ANISOU 4828  CZ  ARG C 213    11700   7350   4651   -395   2119   -649       C  
ATOM   4829  NH1 ARG C 213      15.552  -3.806  58.071  1.00 70.28           N  
ANISOU 4829  NH1 ARG C 213    12828   8458   5418   -567   2370   -716       N  
ATOM   4830  NH2 ARG C 213      15.577  -3.692  60.367  1.00 58.51           N  
ANISOU 4830  NH2 ARG C 213    10841   6759   4630   -349   2283   -593       N  
ATOM   4831  N   ARG C 214       9.144  -8.180  59.261  1.00 51.34           N  
ANISOU 4831  N   ARG C 214     9851   6185   3471      8    608  -1853       N  
ATOM   4832  CA  ARG C 214       8.994  -9.617  59.057  1.00 60.79           C  
ANISOU 4832  CA  ARG C 214    10844   7379   4875    -61    736  -2210       C  
ATOM   4833  C   ARG C 214       7.772  -9.905  58.189  1.00 67.66           C  
ANISOU 4833  C   ARG C 214    11834   8464   5412   -150    358  -2374       C  
ATOM   4834  O   ARG C 214       6.665  -9.454  58.500  1.00 72.55           O  
ANISOU 4834  O   ARG C 214    12428   9155   5983    -74    -91  -2274       O  
ATOM   4835  CB  ARG C 214       8.868 -10.339  60.398  1.00 57.58           C  
ANISOU 4835  CB  ARG C 214    10050   6770   5059     62    767  -2280       C  
ATOM   4836  N   ALA C 215       7.971 -10.664  57.111  1.00 65.82           N  
ANISOU 4836  N   ALA C 215    11699   8337   4971   -300    528  -2627       N  
ATOM   4837  CA  ALA C 215       6.886 -11.017  56.188  1.00 64.63           C  
ANISOU 4837  CA  ALA C 215    11653   8425   4480   -417    193  -2815       C  
ATOM   4838  C   ALA C 215       5.956 -12.067  56.776  1.00 62.73           C  
ANISOU 4838  C   ALA C 215    11116   8124   4594   -400     12  -3081       C  
ATOM   4839  O   ALA C 215       6.413 -13.027  57.390  1.00 67.19           O  
ANISOU 4839  O   ALA C 215    11470   8447   5610   -349    288  -3236       O  
ATOM   4840  CB  ALA C 215       7.453 -11.513  54.870  1.00 72.45           C  
ANISOU 4840  CB  ALA C 215    12870   9526   5132   -579    458  -3015       C  
TER    4841      ALA C 215                                                      
ATOM   4842  N   THR D   3     -21.744  -8.592  94.239  1.00 59.38           N  
ANISOU 4842  N   THR D   3     7958   4620   9982    894   1545    -73       N  
ATOM   4843  CA  THR D   3     -22.611  -8.304  93.098  1.00 61.42           C  
ANISOU 4843  CA  THR D   3     8434   4943   9959   1086   1734    261       C  
ATOM   4844  C   THR D   3     -22.702  -9.463  92.111  1.00 57.31           C  
ANISOU 4844  C   THR D   3     7918   4635   9221   1147   1716    457       C  
ATOM   4845  O   THR D   3     -23.746  -9.698  91.495  1.00 54.73           O  
ANISOU 4845  O   THR D   3     7717   4519   8559   1373   1686    650       O  
ATOM   4846  CB  THR D   3     -22.127  -7.077  92.314  1.00 68.03           C  
ANISOU 4846  CB  THR D   3     9385   5503  10960   1044   2117    359       C  
ATOM   4847  OG1 THR D   3     -22.880  -6.977  91.095  1.00 67.97           O  
ANISOU 4847  OG1 THR D   3     9608   5605  10613   1287   2281    674       O  
ATOM   4848  CG2 THR D   3     -20.617  -7.188  92.000  1.00 47.56           C  
ANISOU 4848  CG2 THR D   3     6603   2724   8743    774   2309    240       C  
ATOM   4849  N   ALA D   4     -21.593 -10.176  91.959  1.00 53.96           N  
ANISOU 4849  N   ALA D   4     7337   4171   8995    955   1721    373       N  
ATOM   4850  CA  ALA D   4     -21.472 -11.187  90.923  1.00 38.29           C  
ANISOU 4850  CA  ALA D   4     5363   2342   6845    994   1745    550       C  
ATOM   4851  C   ALA D   4     -20.592 -12.297  91.474  1.00 36.57           C  
ANISOU 4851  C   ALA D   4     4930   2167   6800    816   1557    361       C  
ATOM   4852  O   ALA D   4     -19.453 -12.047  91.871  1.00 38.04           O  
ANISOU 4852  O   ALA D   4     4947   2180   7328    617   1600    144       O  
ATOM   4853  CB  ALA D   4     -20.886 -10.567  89.646  1.00 46.24           C  
ANISOU 4853  CB  ALA D   4     6481   3192   7898    998   2117    724       C  
ATOM   4854  N   GLU D   5     -21.125 -13.511  91.552  1.00 33.89           N  
ANISOU 4854  N   GLU D   5     4575   2066   6237    897   1344    410       N  
ATOM   4855  CA  GLU D   5     -20.364 -14.637  92.068  1.00 32.43           C  
ANISOU 4855  CA  GLU D   5     4225   1939   6159    774   1158    248       C  
ATOM   4856  C   GLU D   5     -20.499 -15.804  91.103  1.00 30.77           C  
ANISOU 4856  C   GLU D   5     4038   1945   5707    812   1130    430       C  
ATOM   4857  O   GLU D   5     -21.547 -15.994  90.478  1.00 33.35           O  
ANISOU 4857  O   GLU D   5     4476   2446   5749    977   1131    610       O  
ATOM   4858  CB  GLU D   5     -20.824 -15.033  93.488  1.00 31.28           C  
ANISOU 4858  CB  GLU D   5     4031   1988   5866    782    849     55       C  
ATOM   4859  CG  GLU D   5     -20.585 -13.932  94.507  1.00 34.13           C  
ANISOU 4859  CG  GLU D   5     4356   2150   6461    766    828   -185       C  
ATOM   4860  CD  GLU D   5     -21.124 -14.251  95.896  1.00 40.62           C  
ANISOU 4860  CD  GLU D   5     5196   3164   7073    853    551   -348       C  
ATOM   4861  OE1 GLU D   5     -21.862 -15.247  96.044  1.00 33.54           O  
ANISOU 4861  OE1 GLU D   5     4363   2524   5855    918    443   -232       O  
ATOM   4862  OE2 GLU D   5     -20.805 -13.488  96.844  1.00 41.32           O  
ANISOU 4862  OE2 GLU D   5     5245   3124   7332    866    468   -607       O  
ATOM   4863  N   LEU D   6     -19.416 -16.565  90.975  1.00 30.45           N  
ANISOU 4863  N   LEU D   6     3875   1900   5796    677   1092    343       N  
ATOM   4864  CA  LEU D   6     -19.316 -17.675  90.037  1.00 32.24           C  
ANISOU 4864  CA  LEU D   6     4117   2290   5842    697   1079    486       C  
ATOM   4865  C   LEU D   6     -19.603 -18.966  90.800  1.00 34.84           C  
ANISOU 4865  C   LEU D   6     4397   2886   5955    663    783    386       C  
ATOM   4866  O   LEU D   6     -18.822 -19.367  91.667  1.00 33.99           O  
ANISOU 4866  O   LEU D   6     4192   2773   5948    579    634    186       O  
ATOM   4867  CB  LEU D   6     -17.923 -17.683  89.403  1.00 41.43           C  
ANISOU 4867  CB  LEU D   6     5188   3257   7296    583   1268    458       C  
ATOM   4868  CG  LEU D   6     -17.606 -18.424  88.104  1.00 40.05           C  
ANISOU 4868  CG  LEU D   6     5072   3142   7006    637   1391    648       C  
ATOM   4869  CD1 LEU D   6     -18.706 -18.255  87.085  1.00 31.88           C  
ANISOU 4869  CD1 LEU D   6     4248   2233   5633    865   1475    897       C  
ATOM   4870  CD2 LEU D   6     -16.300 -17.885  87.541  1.00 44.89           C  
ANISOU 4870  CD2 LEU D   6     5591   3526   7939    512   1683    612       C  
ATOM   4871  N   HIS D   7     -20.731 -19.605  90.492  1.00 25.88           N  
ANISOU 4871  N   HIS D   7     3333   1971   4531    751    713    501       N  
ATOM   4872  CA  HIS D   7     -21.121 -20.849  91.140  1.00 24.44           C  
ANISOU 4872  CA  HIS D   7     3138   1984   4165    709    529    432       C  
ATOM   4873  C   HIS D   7     -20.660 -22.033  90.311  1.00 28.30           C  
ANISOU 4873  C   HIS D   7     3614   2558   4581    670    512    484       C  
ATOM   4874  O   HIS D   7     -20.899 -22.066  89.101  1.00 29.74           O  
ANISOU 4874  O   HIS D   7     3819   2787   4693    746    598    611       O  
ATOM   4875  CB  HIS D   7     -22.633 -20.912  91.315  1.00 27.66           C  
ANISOU 4875  CB  HIS D   7     3575   2557   4377    785    502    466       C  
ATOM   4876  CG  HIS D   7     -23.164 -19.938  92.309  1.00 27.60           C  
ANISOU 4876  CG  HIS D   7     3594   2495   4400    833    498    402       C  
ATOM   4877  ND1 HIS D   7     -23.985 -20.314  93.345  1.00 29.32           N  
ANISOU 4877  ND1 HIS D   7     3831   2815   4495    837    436    332       N  
ATOM   4878  CD2 HIS D   7     -22.991 -18.598  92.428  1.00 25.98           C  
ANISOU 4878  CD2 HIS D   7     3413   2119   4340    887    578    397       C  
ATOM   4879  CE1 HIS D   7     -24.303 -19.247  94.059  1.00 35.28           C  
ANISOU 4879  CE1 HIS D   7     4617   3495   5292    908    446    285       C  
ATOM   4880  NE2 HIS D   7     -23.713 -18.193  93.522  1.00 28.53           N  
ANISOU 4880  NE2 HIS D   7     3762   2471   4606    933    521    314       N  
ATOM   4881  N   PHE D   8     -20.028 -23.008  90.971  1.00 25.54           N  
ANISOU 4881  N   PHE D   8     3256   2235   4211    601    395    382       N  
ATOM   4882  CA  PHE D   8     -19.495 -24.209  90.335  1.00 27.12           C  
ANISOU 4882  CA  PHE D   8     3460   2500   4345    567    369    411       C  
ATOM   4883  C   PHE D   8     -20.257 -25.454  90.771  1.00 30.08           C  
ANISOU 4883  C   PHE D   8     3911   2998   4520    546    304    394       C  
ATOM   4884  O   PHE D   8     -20.677 -25.581  91.925  1.00 27.40           O  
ANISOU 4884  O   PHE D   8     3642   2657   4112    556    269    329       O  
ATOM   4885  CB  PHE D   8     -18.014 -24.427  90.667  1.00 22.91           C  
ANISOU 4885  CB  PHE D   8     2867   1878   3961    535    309    289       C  
ATOM   4886  CG  PHE D   8     -17.099 -23.396  90.091  1.00 34.58           C  
ANISOU 4886  CG  PHE D   8     4228   3192   5719    504    446    274       C  
ATOM   4887  CD1 PHE D   8     -16.375 -23.666  88.941  1.00 30.09           C  
ANISOU 4887  CD1 PHE D   8     3623   2587   5224    489    574    362       C  
ATOM   4888  CD2 PHE D   8     -16.958 -22.151  90.701  1.00 31.63           C  
ANISOU 4888  CD2 PHE D   8     3787   2671   5559    486    487    164       C  
ATOM   4889  CE1 PHE D   8     -15.531 -22.715  88.401  1.00 33.32           C  
ANISOU 4889  CE1 PHE D   8     3936   2794   5930    448    793    358       C  
ATOM   4890  CE2 PHE D   8     -16.106 -21.195  90.173  1.00 35.69           C  
ANISOU 4890  CE2 PHE D   8     4189   2971   6400    423    690    132       C  
ATOM   4891  CZ  PHE D   8     -15.391 -21.478  89.011  1.00 35.05           C  
ANISOU 4891  CZ  PHE D   8     4078   2833   6406    399    871    239       C  
ATOM   4892  N   ARG D   9     -20.411 -26.381  89.839  1.00 30.89           N  
ANISOU 4892  N   ARG D   9     4015   3183   4541    526    321    445       N  
ATOM   4893  CA  ARG D   9     -20.903 -27.712  90.140  1.00 28.02           C  
ANISOU 4893  CA  ARG D   9     3719   2872   4054    469    313    407       C  
ATOM   4894  C   ARG D   9     -19.700 -28.652  90.243  1.00 25.16           C  
ANISOU 4894  C   ARG D   9     3435   2455   3669    470    263    388       C  
ATOM   4895  O   ARG D   9     -18.554 -28.241  90.043  1.00 21.01           O  
ANISOU 4895  O   ARG D   9     2858   1881   3243    505    221    377       O  
ATOM   4896  CB  ARG D   9     -21.897 -28.156  89.065  1.00 27.12           C  
ANISOU 4896  CB  ARG D   9     3528   2887   3891    453    342    405       C  
ATOM   4897  N   CYS D  10     -19.953 -29.924  90.562  1.00 22.49           N  
ANISOU 4897  N   CYS D  10     3219   2106   3220    436    295    368       N  
ATOM   4898  CA  CYS D  10     -18.884 -30.915  90.479  1.00 23.51           C  
ANISOU 4898  CA  CYS D  10     3445   2195   3294    475    250    359       C  
ATOM   4899  C   CYS D  10     -18.377 -31.023  89.045  1.00 24.10           C  
ANISOU 4899  C   CYS D  10     3408   2327   3422    461    234    399       C  
ATOM   4900  O   CYS D  10     -19.138 -30.899  88.079  1.00 25.49           O  
ANISOU 4900  O   CYS D  10     3500   2582   3601    431    270    425       O  
ATOM   4901  CB  CYS D  10     -19.360 -32.286  90.958  1.00 21.72           C  
ANISOU 4901  CB  CYS D  10     3413   1899   2939    447    354    352       C  
ATOM   4902  SG  CYS D  10     -19.843 -32.335  92.659  1.00 27.40           S  
ANISOU 4902  SG  CYS D  10     4363   2513   3537    534    449    345       S  
ATOM   4903  N   ASN D  11     -17.080 -31.261  88.908  1.00 24.08           N  
ANISOU 4903  N   ASN D  11     3407   2298   3446    522    174    384       N  
ATOM   4904  CA  ASN D  11     -16.492 -31.482  87.595  1.00 23.79           C  
ANISOU 4904  CA  ASN D  11     3300   2299   3440    534    195    434       C  
ATOM   4905  C   ASN D  11     -16.847 -32.888  87.110  1.00 29.05           C  
ANISOU 4905  C   ASN D  11     4075   2990   3971    510    205    431       C  
ATOM   4906  O   ASN D  11     -16.558 -33.873  87.795  1.00 27.13           O  
ANISOU 4906  O   ASN D  11     3984   2684   3641    529    191    393       O  
ATOM   4907  CB  ASN D  11     -14.980 -31.314  87.681  1.00 26.06           C  
ANISOU 4907  CB  ASN D  11     3514   2546   3841    596    151    380       C  
ATOM   4908  CG  ASN D  11     -14.319 -31.229  86.323  1.00 29.92           C  
ANISOU 4908  CG  ASN D  11     3917   3049   4404    615    240    453       C  
ATOM   4909  OD1 ASN D  11     -14.383 -32.172  85.535  1.00 25.33           O  
ANISOU 4909  OD1 ASN D  11     3411   2518   3697    640    246    498       O  
ATOM   4910  ND2 ASN D  11     -13.649 -30.108  86.055  1.00 22.26           N  
ANISOU 4910  ND2 ASN D  11     2799   2007   3650    609    343    456       N  
ATOM   4911  N   GLU D  12     -17.459 -32.989  85.928  1.00 24.40           N  
ANISOU 4911  N   GLU D  12     3430   2485   3355    503    231    452       N  
ATOM   4912  CA  GLU D  12     -17.909 -34.272  85.402  1.00 25.51           C  
ANISOU 4912  CA  GLU D  12     3634   2646   3411    465    233    386       C  
ATOM   4913  C   GLU D  12     -16.908 -34.932  84.461  1.00 30.57           C  
ANISOU 4913  C   GLU D  12     4312   3304   3999    549    207    413       C  
ATOM   4914  O   GLU D  12     -17.247 -35.935  83.817  1.00 33.11           O  
ANISOU 4914  O   GLU D  12     4674   3648   4256    535    198    340       O  
ATOM   4915  CB  GLU D  12     -19.243 -34.105  84.687  1.00 31.15           C  
ANISOU 4915  CB  GLU D  12     4236   3478   4122    446    226    304       C  
ATOM   4916  CG  GLU D  12     -20.291 -33.454  85.538  1.00 44.71           C  
ANISOU 4916  CG  GLU D  12     5889   5196   5902    372    263    264       C  
ATOM   4917  CD  GLU D  12     -21.438 -32.930  84.710  1.00 57.53           C  
ANISOU 4917  CD  GLU D  12     7350   6987   7520    434    213    169       C  
ATOM   4918  OE1 GLU D  12     -21.203 -32.575  83.531  1.00 53.16           O  
ANISOU 4918  OE1 GLU D  12     6774   6545   6880    609    148    205       O  
ATOM   4919  OE2 GLU D  12     -22.568 -32.881  85.239  1.00 63.71           O  
ANISOU 4919  OE2 GLU D  12     8039   7795   8372    344    247     49       O  
ATOM   4920  N   GLY D  13     -15.694 -34.413  84.368  1.00 25.75           N  
ANISOU 4920  N   GLY D  13     3668   2675   3442    628    210    484       N  
ATOM   4921  CA  GLY D  13     -14.689 -34.951  83.467  1.00 25.44           C  
ANISOU 4921  CA  GLY D  13     3644   2653   3368    719    217    514       C  
ATOM   4922  C   GLY D  13     -13.807 -35.997  84.113  1.00 21.79           C  
ANISOU 4922  C   GLY D  13     3288   2126   2865    743    166    460       C  
ATOM   4923  O   GLY D  13     -14.216 -36.713  85.033  1.00 24.07           O  
ANISOU 4923  O   GLY D  13     3717   2344   3084    704    147    409       O  
ATOM   4924  N   GLY D  14     -12.574 -36.086  83.617  1.00 22.50           N  
ANISOU 4924  N   GLY D  14     3327   2229   2991    838    173    474       N  
ATOM   4925  CA  GLY D  14     -11.562 -36.961  84.175  1.00 26.42           C  
ANISOU 4925  CA  GLY D  14     3900   2695   3443    927    100    403       C  
ATOM   4926  C   GLY D  14     -10.383 -36.181  84.725  1.00 24.73           C  
ANISOU 4926  C   GLY D  14     3502   2489   3406    988     63    320       C  
ATOM   4927  O   GLY D  14     -10.470 -34.965  84.896  1.00 23.77           O  
ANISOU 4927  O   GLY D  14     3219   2352   3460    918    112    316       O  
HETATM 4928  N   MSE D  15      -9.279 -36.871  84.994  1.00 25.90           N  
ANISOU 4928  N   MSE D  15     3656   2657   3526   1127    -23    219       N  
HETATM 4929  CA  MSE D  15      -8.142 -36.237  85.670  1.00 27.93           C  
ANISOU 4929  CA  MSE D  15     3688   2946   3978   1208   -109     36       C  
HETATM 4930  C   MSE D  15      -7.629 -34.979  84.953  1.00 28.25           C  
ANISOU 4930  C   MSE D  15     3419   2966   4348   1094     58     29       C  
HETATM 4931  O   MSE D  15      -7.326 -33.989  85.596  1.00 26.96           O  
ANISOU 4931  O   MSE D  15     3052   2776   4418   1048     40   -115       O  
HETATM 4932  CB  MSE D  15      -7.000 -37.240  85.837  1.00 26.74           C  
ANISOU 4932  CB  MSE D  15     3565   2856   3740   1421   -233    -97       C  
HETATM 4933  CG  MSE D  15      -5.730 -36.651  86.447  1.00 41.24           C  
ANISOU 4933  CG  MSE D  15     5090   4766   5812   1534   -358   -378       C  
HETATM 4934 SE   MSE D  15      -6.022 -35.860  88.215  1.00 45.76          SE  
ANISOU 4934 SE   MSE D  15     5644   5351   6390   1620   -578   -594      SE  
HETATM 4935  CE  MSE D  15      -6.332 -37.497  89.239  1.00 46.15           C  
ANISOU 4935  CE  MSE D  15     6223   5404   5907   1964   -750   -551       C  
ATOM   4936  N   ALA D  16      -7.534 -35.023  83.622  1.00 27.12           N  
ANISOU 4936  N   ALA D  16     3268   2813   4224   1067    249    178       N  
ATOM   4937  CA  ALA D  16      -7.061 -33.851  82.886  1.00 29.92           C  
ANISOU 4937  CA  ALA D  16     3402   3090   4877    987    506    218       C  
ATOM   4938  C   ALA D  16      -7.963 -32.645  83.120  1.00 26.81           C  
ANISOU 4938  C   ALA D  16     2999   2612   4576    868    595    292       C  
ATOM   4939  O   ALA D  16      -7.478 -31.509  83.193  1.00 28.28           O  
ANISOU 4939  O   ALA D  16     2972   2687   5088    783    763    225       O  
ATOM   4940  CB  ALA D  16      -6.964 -34.160  81.391  1.00 28.14           C  
ANISOU 4940  CB  ALA D  16     3269   2865   4560   1052    718    410       C  
ATOM   4941  N   ASP D  17      -9.284 -32.871  83.235  1.00 28.01           N  
ANISOU 4941  N   ASP D  17     3750   3224   3668   -538    803    -35       N  
ATOM   4942  CA  ASP D  17     -10.198 -31.779  83.557  1.00 22.73           C  
ANISOU 4942  CA  ASP D  17     2996   2584   3055   -526    638     58       C  
ATOM   4943  C   ASP D  17     -10.056 -31.350  85.018  1.00 23.47           C  
ANISOU 4943  C   ASP D  17     2952   2665   3301   -359    604     38       C  
ATOM   4944  O   ASP D  17     -10.037 -30.146  85.317  1.00 20.16           O  
ANISOU 4944  O   ASP D  17     2463   2235   2960   -321    533     82       O  
ATOM   4945  CB  ASP D  17     -11.647 -32.174  83.243  1.00 23.33           C  
ANISOU 4945  CB  ASP D  17     3117   2700   3047   -617    535    124       C  
ATOM   4946  CG  ASP D  17     -11.835 -32.666  81.796  1.00 30.65           C  
ANISOU 4946  CG  ASP D  17     4208   3648   3792   -823    559    144       C  
ATOM   4947  OD1 ASP D  17     -11.506 -31.920  80.853  1.00 28.84           O  
ANISOU 4947  OD1 ASP D  17     4021   3427   3512   -920    546    193       O  
ATOM   4948  OD2 ASP D  17     -12.307 -33.812  81.598  1.00 31.10           O  
ANISOU 4948  OD2 ASP D  17     4368   3708   3743   -904    593    109       O  
ATOM   4949  N   TYR D  18      -9.940 -32.310  85.946  1.00 19.73           N  
ANISOU 4949  N   TYR D  18     2454   2182   2860   -266    656    -27       N  
ATOM   4950  CA  TYR D  18      -9.743 -31.937  87.349  1.00 23.92           C  
ANISOU 4950  CA  TYR D  18     2869   2707   3511   -131    625    -47       C  
ATOM   4951  C   TYR D  18      -8.515 -31.046  87.494  1.00 21.67           C  
ANISOU 4951  C   TYR D  18     2524   2414   3295   -104    652    -58       C  
ATOM   4952  O   TYR D  18      -8.574 -29.971  88.096  1.00 28.18           O  
ANISOU 4952  O   TYR D  18     3290   3228   4191    -69    582    -37       O  
ATOM   4953  CB  TYR D  18      -9.575 -33.172  88.244  1.00 24.91           C  
ANISOU 4953  CB  TYR D  18     2988   2826   3651    -49    685   -107       C  
ATOM   4954  CG  TYR D  18     -10.672 -34.211  88.227  1.00 25.41           C  
ANISOU 4954  CG  TYR D  18     3120   2893   3641    -87    671   -106       C  
ATOM   4955  CD1 TYR D  18     -11.995 -33.879  87.945  1.00 20.98           C  
ANISOU 4955  CD1 TYR D  18     2562   2370   3041   -155    569    -42       C  
ATOM   4956  CD2 TYR D  18     -10.381 -35.534  88.539  1.00 25.79           C  
ANISOU 4956  CD2 TYR D  18     3225   2910   3665    -54    759   -159       C  
ATOM   4957  CE1 TYR D  18     -12.992 -34.849  87.942  1.00 23.80           C  
ANISOU 4957  CE1 TYR D  18     2973   2749   3322   -214    550    -33       C  
ATOM   4958  CE2 TYR D  18     -11.363 -36.506  88.539  1.00 29.68           C  
ANISOU 4958  CE2 TYR D  18     3799   3399   4079   -110    747   -160       C  
ATOM   4959  CZ  TYR D  18     -12.661 -36.170  88.241  1.00 26.61           C  
ANISOU 4959  CZ  TYR D  18     3408   3064   3639   -201    640    -99       C  
ATOM   4960  OH  TYR D  18     -13.609 -37.167  88.261  1.00 24.27           O  
ANISOU 4960  OH  TYR D  18     3185   2779   3257   -278    625    -95       O  
ATOM   4961  N   ALA D  19      -7.389 -31.484  86.927  1.00 21.42           N  
ANISOU 4961  N   ALA D  19     2512   2386   3241   -127    764    -90       N  
ATOM   4962  CA  ALA D  19      -6.136 -30.757  87.092  1.00 20.11           C  
ANISOU 4962  CA  ALA D  19     2268   2235   3139   -113    796    -92       C  
ATOM   4963  C   ALA D  19      -6.162 -29.409  86.376  1.00 20.25           C  
ANISOU 4963  C   ALA D  19     2308   2245   3143   -208    736    -40       C  
ATOM   4964  O   ALA D  19      -5.572 -28.442  86.868  1.00 22.18           O  
ANISOU 4964  O   ALA D  19     2490   2489   3451   -202    701    -29       O  
ATOM   4965  CB  ALA D  19      -4.974 -31.615  86.583  1.00 23.46           C  
ANISOU 4965  CB  ALA D  19     2692   2674   3549   -105    950   -127       C  
ATOM   4966  N   ALA D  20      -6.847 -29.317  85.232  1.00 23.83           N  
ANISOU 4966  N   ALA D  20     2858   2689   3505   -310    716      1       N  
ATOM   4967  CA  ALA D  20      -6.942 -28.031  84.536  1.00 26.84           C  
ANISOU 4967  CA  ALA D  20     3269   3054   3874   -399    647     71       C  
ATOM   4968  C   ALA D  20      -7.794 -27.030  85.314  1.00 22.80           C  
ANISOU 4968  C   ALA D  20     2719   2501   3444   -337    522    119       C  
ATOM   4969  O   ALA D  20      -7.436 -25.850  85.417  1.00 21.81           O  
ANISOU 4969  O   ALA D  20     2583   2336   3367   -352    484    148       O  
ATOM   4970  CB  ALA D  20      -7.512 -28.228  83.132  1.00 24.23           C  
ANISOU 4970  CB  ALA D  20     3055   2735   3415   -535    642    121       C  
ATOM   4971  N   GLN D  21      -8.921 -27.476  85.875  1.00 25.64           N  
ANISOU 4971  N   GLN D  21     3061   2861   3819   -269    468    126       N  
ATOM   4972  CA  GLN D  21      -9.748 -26.549  86.645  1.00 27.29           C  
ANISOU 4972  CA  GLN D  21     3230   3025   4116   -191    380    166       C  
ATOM   4973  C   GLN D  21      -9.000 -26.047  87.875  1.00 23.70           C  
ANISOU 4973  C   GLN D  21     2724   2536   3744   -116    400    101       C  
ATOM   4974  O   GLN D  21      -8.976 -24.841  88.154  1.00 20.36           O  
ANISOU 4974  O   GLN D  21     2311   2045   3378   -107    362    123       O  
ATOM   4975  CB  GLN D  21     -11.070 -27.195  87.055  1.00 23.89           C  
ANISOU 4975  CB  GLN D  21     2771   2621   3686   -133    336    187       C  
ATOM   4976  CG  GLN D  21     -12.063 -26.140  87.526  1.00 29.57           C  
ANISOU 4976  CG  GLN D  21     3450   3292   4495    -55    260    255       C  
ATOM   4977  CD  GLN D  21     -13.337 -26.693  88.115  1.00 30.55           C  
ANISOU 4977  CD  GLN D  21     3514   3454   4638     15    228    277       C  
ATOM   4978  OE1 GLN D  21     -13.843 -27.735  87.695  1.00 31.22           O  
ANISOU 4978  OE1 GLN D  21     3606   3612   4645    -43    220    291       O  
ATOM   4979  NE2 GLN D  21     -13.871 -25.985  89.104  1.00 34.58           N  
ANISOU 4979  NE2 GLN D  21     3974   3917   5249    130    220    276       N  
ATOM   4980  N   LEU D  22      -8.386 -26.966  88.626  1.00 23.32           N  
ANISOU 4980  N   LEU D  22     2631   2528   3699    -72    457     25       N  
ATOM   4981  CA  LEU D  22      -7.555 -26.584  89.762  1.00 20.58           C  
ANISOU 4981  CA  LEU D  22     2235   2175   3411    -34    466    -26       C  
ATOM   4982  C   LEU D  22      -6.498 -25.569  89.345  1.00 25.64           C  
ANISOU 4982  C   LEU D  22     2885   2799   4059   -119    471    -10       C  
ATOM   4983  O   LEU D  22      -6.254 -24.582  90.051  1.00 20.17           O  
ANISOU 4983  O   LEU D  22     2197   2058   3407   -127    437    -21       O  
ATOM   4984  CB  LEU D  22      -6.901 -27.836  90.361  1.00 18.77           C  
ANISOU 4984  CB  LEU D  22     1949   2008   3176     12    524    -77       C  
ATOM   4985  CG  LEU D  22      -5.998 -27.593  91.569  1.00 18.82           C  
ANISOU 4985  CG  LEU D  22     1888   2035   3228     33    515   -112       C  
ATOM   4986  CD1 LEU D  22      -6.768 -26.932  92.718  1.00 18.62           C  
ANISOU 4986  CD1 LEU D  22     1883   1961   3232     74    455   -135       C  
ATOM   4987  CD2 LEU D  22      -5.345 -28.876  92.056  1.00 25.94           C  
ANISOU 4987  CD2 LEU D  22     2722   3000   4132     88    567   -131       C  
ATOM   4988  N   ARG D  23      -5.890 -25.789  88.176  1.00 28.31           N  
ANISOU 4988  N   ARG D  23     3239   3171   4345   -199    522     14       N  
ATOM   4989  CA  ARG D  23      -4.812 -24.938  87.675  1.00 32.73           C  
ANISOU 4989  CA  ARG D  23     3800   3735   4901   -299    540     33       C  
ATOM   4990  C   ARG D  23      -5.320 -23.543  87.327  1.00 32.79           C  
ANISOU 4990  C   ARG D  23     3888   3651   4919   -352    466     91       C  
ATOM   4991  O   ARG D  23      -4.658 -22.538  87.618  1.00 35.31           O  
ANISOU 4991  O   ARG D  23     4218   3934   5263   -410    448     92       O  
ATOM   4992  CB  ARG D  23      -4.184 -25.615  86.446  1.00 27.83           C  
ANISOU 4992  CB  ARG D  23     3189   3173   4211   -368    634     42       C  
ATOM   4993  CG  ARG D  23      -2.863 -25.075  85.970  1.00 30.48           C  
ANISOU 4993  CG  ARG D  23     3490   3550   4540   -467    689     55       C  
ATOM   4994  CD  ARG D  23      -2.430 -25.686  84.633  1.00 28.85           C  
ANISOU 4994  CD  ARG D  23     3320   3388   4253   -539    802     61       C  
ATOM   4995  NE  ARG D  23      -2.543 -27.140  84.651  1.00 47.42           N  
ANISOU 4995  NE  ARG D  23     5662   5768   6589   -454    892     12       N  
ATOM   4996  CZ  ARG D  23      -3.272 -27.846  83.791  1.00 49.40           C  
ANISOU 4996  CZ  ARG D  23     6020   6000   6751   -484    927      6       C  
ATOM   4997  NH1 ARG D  23      -3.937 -27.230  82.820  1.00 59.10           N  
ANISOU 4997  NH1 ARG D  23     7355   7201   7898   -597    869     59       N  
ATOM   4998  NH2 ARG D  23      -3.329 -29.168  83.895  1.00 32.10           N  
ANISOU 4998  NH2 ARG D  23     3838   3814   4546   -412   1017    -45       N  
ATOM   4999  N   GLU D  24      -6.496 -23.464  86.710  1.00 28.25           N  
ANISOU 4999  N   GLU D  24     3372   3037   4326   -338    419    148       N  
ATOM   5000  CA  GLU D  24      -7.013 -22.226  86.139  1.00 23.09           C  
ANISOU 5000  CA  GLU D  24     2794   2294   3684   -380    352    233       C  
ATOM   5001  C   GLU D  24      -7.885 -21.472  87.129  1.00 25.94           C  
ANISOU 5001  C   GLU D  24     3165   2555   4135   -273    300    238       C  
ATOM   5002  O   GLU D  24      -7.740 -20.257  87.286  1.00 29.71           O  
ANISOU 5002  O   GLU D  24     3704   2929   4656   -292    277    261       O  
ATOM   5003  CB  GLU D  24      -7.806 -22.535  84.864  1.00 29.90           C  
ANISOU 5003  CB  GLU D  24     3703   3183   4476   -433    320    320       C  
ATOM   5004  CG  GLU D  24      -6.950 -23.124  83.746  1.00 44.49           C  
ANISOU 5004  CG  GLU D  24     5579   5107   6216   -561    393    312       C  
ATOM   5005  CD  GLU D  24      -7.743 -23.853  82.676  1.00 55.40           C  
ANISOU 5005  CD  GLU D  24     7017   6537   7497   -626    377    365       C  
ATOM   5006  OE1 GLU D  24      -8.982 -23.987  82.816  1.00 57.49           O  
ANISOU 5006  OE1 GLU D  24     7272   6795   7777   -571    297    419       O  
ATOM   5007  OE2 GLU D  24      -7.109 -24.300  81.692  1.00 56.59           O  
ANISOU 5007  OE2 GLU D  24     7221   6738   7544   -743    450    353       O  
ATOM   5008  N   VAL D  25      -8.781 -22.187  87.802  1.00 22.20           N  
ANISOU 5008  N   VAL D  25     2642   2105   3687   -163    295    214       N  
ATOM   5009  CA  VAL D  25      -9.702 -21.579  88.753  1.00 23.15           C  
ANISOU 5009  CA  VAL D  25     2765   2138   3893    -47    272    213       C  
ATOM   5010  C   VAL D  25      -9.108 -21.489  90.152  1.00 26.39           C  
ANISOU 5010  C   VAL D  25     3168   2527   4330    -15    311    104       C  
ATOM   5011  O   VAL D  25      -9.410 -20.547  90.892  1.00 22.27           O  
ANISOU 5011  O   VAL D  25     2701   1895   3867     33    314     86       O  
ATOM   5012  CB  VAL D  25     -11.016 -22.376  88.770  1.00 22.83           C  
ANISOU 5012  CB  VAL D  25     2666   2150   3859     38    249    252       C  
ATOM   5013  CG1 VAL D  25     -12.017 -21.769  89.750  1.00 24.19           C  
ANISOU 5013  CG1 VAL D  25     2824   2240   4128    173    249    255       C  
ATOM   5014  CG2 VAL D  25     -11.588 -22.468  87.368  1.00 23.01           C  
ANISOU 5014  CG2 VAL D  25     2699   2210   3833    -28    193    373       C  
ATOM   5015  N   GLY D  26      -8.287 -22.463  90.537  1.00 24.19           N  
ANISOU 5015  N   GLY D  26     2832   2349   4009    -42    343     36       N  
ATOM   5016  CA  GLY D  26      -7.704 -22.503  91.857  1.00 28.21           C  
ANISOU 5016  CA  GLY D  26     3324   2866   4528    -31    360    -49       C  
ATOM   5017  C   GLY D  26      -8.465 -23.363  92.839  1.00 24.55           C  
ANISOU 5017  C   GLY D  26     2818   2438   4074     70    371    -94       C  
ATOM   5018  O   GLY D  26      -8.106 -23.395  94.023  1.00 23.13           O  
ANISOU 5018  O   GLY D  26     2634   2265   3891     75    378   -160       O  
ATOM   5019  N   THR D  27      -9.502 -24.054  92.373  1.00 22.53           N  
ANISOU 5019  N   THR D  27     2533   2211   3815    131    366    -53       N  
ATOM   5020  CA  THR D  27     -10.411 -24.853  93.184  1.00 19.35           C  
ANISOU 5020  CA  THR D  27     2091   1843   3418    218    375    -81       C  
ATOM   5021  C   THR D  27     -11.144 -25.795  92.240  1.00 20.91           C  
ANISOU 5021  C   THR D  27     2259   2107   3581    217    362    -22       C  
ATOM   5022  O   THR D  27     -11.630 -25.361  91.191  1.00 22.39           O  
ANISOU 5022  O   THR D  27     2462   2275   3768    190    329     59       O  
ATOM   5023  CB  THR D  27     -11.443 -23.992  93.927  1.00 22.12           C  
ANISOU 5023  CB  THR D  27     2467   2107   3831    303    381    -84       C  
ATOM   5024  OG1 THR D  27     -10.787 -22.959  94.656  1.00 24.55           O  
ANISOU 5024  OG1 THR D  27     2845   2326   4155    276    399   -140       O  
ATOM   5025  CG2 THR D  27     -12.243 -24.842  94.913  1.00 22.18           C  
ANISOU 5025  CG2 THR D  27     2428   2166   3833    377    404   -123       C  
ATOM   5026  N   VAL D  28     -11.226 -27.069  92.605  1.00 20.96           N  
ANISOU 5026  N   VAL D  28     2231   2184   3547    233    381    -56       N  
ATOM   5027  CA  VAL D  28     -12.064 -28.006  91.866  1.00 24.25           C  
ANISOU 5027  CA  VAL D  28     2641   2656   3916    215    370     -9       C  
ATOM   5028  C   VAL D  28     -12.873 -28.819  92.870  1.00 25.60           C  
ANISOU 5028  C   VAL D  28     2777   2864   4085    275    377    -38       C  
ATOM   5029  O   VAL D  28     -12.428 -29.064  93.997  1.00 20.60           O  
ANISOU 5029  O   VAL D  28     2134   2232   3462    314    402   -105       O  
ATOM   5030  CB  VAL D  28     -11.236 -28.920  90.925  1.00 26.43           C  
ANISOU 5030  CB  VAL D  28     2951   2971   4118    136    407    -18       C  
ATOM   5031  CG1 VAL D  28     -10.207 -29.722  91.695  1.00 19.57           C  
ANISOU 5031  CG1 VAL D  28     2064   2123   3249    165    462    -89       C  
ATOM   5032  CG2 VAL D  28     -12.145 -29.840  90.123  1.00 20.03           C  
ANISOU 5032  CG2 VAL D  28     2170   2205   3235     84    394     25       C  
HETATM 5033  N   MSE D  29     -14.092 -29.185  92.473  1.00 21.70           N  
ANISOU 5033  N   MSE D  29     2260   2411   3573    270    347     23       N  
HETATM 5034  CA  MSE D  29     -14.928 -30.045  93.306  1.00 24.82           C  
ANISOU 5034  CA  MSE D  29     2620   2856   3954    304    355      6       C  
HETATM 5035  C   MSE D  29     -15.183 -31.378  92.593  1.00 21.01           C  
ANISOU 5035  C   MSE D  29     2172   2432   3378    218    351     24       C  
HETATM 5036  O   MSE D  29     -15.716 -31.410  91.481  1.00 22.23           O  
ANISOU 5036  O   MSE D  29     2340   2617   3489    140    310     99       O  
HETATM 5037  CB  MSE D  29     -16.249 -29.353  93.661  1.00 21.57           C  
ANISOU 5037  CB  MSE D  29     2137   2452   3607    372    334     64       C  
HETATM 5038  CG  MSE D  29     -17.168 -30.237  94.491  1.00 24.45           C  
ANISOU 5038  CG  MSE D  29     2454   2885   3951    393    349     53       C  
HETATM 5039 SE   MSE D  29     -18.592 -29.302  95.423  1.00 31.39          SE  
ANISOU 5039 SE   MSE D  29     3225   3765   4935    520    378     93      SE  
HETATM 5040  CE  MSE D  29     -19.574 -28.630  93.886  1.00 28.07           C  
ANISOU 5040  CE  MSE D  29     2725   3379   4561    503    294    274       C  
ATOM   5041  N   LEU D  30     -14.752 -32.462  93.229  1.00 16.99           N  
ANISOU 5041  N   LEU D  30     1693   1932   2831    222    393    -40       N  
ATOM   5042  CA  LEU D  30     -14.827 -33.803  92.655  1.00 22.87           C  
ANISOU 5042  CA  LEU D  30     2508   2698   3484    142    414    -42       C  
ATOM   5043  C   LEU D  30     -16.112 -34.471  93.101  1.00 20.98           C  
ANISOU 5043  C   LEU D  30     2245   2518   3211    119    387    -14       C  
ATOM   5044  O   LEU D  30     -16.459 -34.398  94.287  1.00 20.16           O  
ANISOU 5044  O   LEU D  30     2085   2427   3147    190    392    -36       O  
ATOM   5045  CB  LEU D  30     -13.641 -34.660  93.085  1.00 16.69           C  
ANISOU 5045  CB  LEU D  30     1774   1877   2691    173    483   -112       C  
ATOM   5046  CG  LEU D  30     -12.240 -34.090  92.872  1.00 29.76           C  
ANISOU 5046  CG  LEU D  30     3422   3495   4390    203    518   -137       C  
ATOM   5047  CD1 LEU D  30     -11.185 -35.028  93.451  1.00 29.18           C  
ANISOU 5047  CD1 LEU D  30     3361   3402   4325    254    581   -178       C  
ATOM   5048  CD2 LEU D  30     -11.959 -33.815  91.397  1.00 26.76           C  
ANISOU 5048  CD2 LEU D  30     3094   3103   3969    121    534   -110       C  
ATOM   5049  N   PRO D  31     -16.833 -35.128  92.201  1.00 18.94           N  
ANISOU 5049  N   PRO D  31     2030   2301   2866      3    359     37       N  
ATOM   5050  CA  PRO D  31     -18.088 -35.764  92.598  1.00 24.83           C  
ANISOU 5050  CA  PRO D  31     2741   3121   3573    -43    326     77       C  
ATOM   5051  C   PRO D  31     -17.843 -37.033  93.404  1.00 21.79           C  
ANISOU 5051  C   PRO D  31     2429   2711   3140    -45    380      9       C  
ATOM   5052  O   PRO D  31     -16.758 -37.621  93.401  1.00 22.05           O  
ANISOU 5052  O   PRO D  31     2553   2668   3157    -25    442    -55       O  
ATOM   5053  CB  PRO D  31     -18.770 -36.076  91.265  1.00 21.78           C  
ANISOU 5053  CB  PRO D  31     2400   2789   3088   -203    270    156       C  
ATOM   5054  CG  PRO D  31     -17.625 -36.293  90.330  1.00 27.97           C  
ANISOU 5054  CG  PRO D  31     3315   3496   3817   -253    321    107       C  
ATOM   5055  CD  PRO D  31     -16.552 -35.314  90.766  1.00 19.40           C  
ANISOU 5055  CD  PRO D  31     2181   2348   2842   -114    357     61       C  
ATOM   5056  N   ALA D  32     -18.873 -37.423  94.138  1.00 19.03           N  
ANISOU 5056  N   ALA D  32     2027   2427   2777    -60    360     33       N  
ATOM   5057  CA  ALA D  32     -18.879 -38.736  94.760  1.00 26.06           C  
ANISOU 5057  CA  ALA D  32     3002   3299   3599    -99    397     -8       C  
ATOM   5058  C   ALA D  32     -19.069 -39.776  93.660  1.00 25.61           C  
ANISOU 5058  C   ALA D  32     3084   3228   3418   -260    398      7       C  
ATOM   5059  O   ALA D  32     -19.915 -39.600  92.779  1.00 26.06           O  
ANISOU 5059  O   ALA D  32     3121   3359   3423   -379    335     80       O  
ATOM   5060  CB  ALA D  32     -19.993 -38.813  95.802  1.00 19.68           C  
ANISOU 5060  CB  ALA D  32     2099   2577   2800    -92    378     20       C  
ATOM   5061  N   TYR D  33     -18.259 -40.833  93.660  1.00 26.11           N  
ANISOU 5061  N   TYR D  33     3297   3191   3433   -270    471    -56       N  
ATOM   5062  CA  TYR D  33     -17.262 -41.143  94.674  1.00 24.59           C  
ANISOU 5062  CA  TYR D  33     3119   2922   3302   -137    531   -114       C  
ATOM   5063  C   TYR D  33     -15.907 -41.358  93.988  1.00 23.44           C  
ANISOU 5063  C   TYR D  33     3066   2670   3169    -92    611   -159       C  
ATOM   5064  O   TYR D  33     -15.301 -42.428  94.091  1.00 18.42           O  
ANISOU 5064  O   TYR D  33     2550   1941   2510    -75    688   -191       O  
ATOM   5065  CB  TYR D  33     -17.692 -42.393  95.473  1.00 23.61           C  
ANISOU 5065  CB  TYR D  33     3076   2779   3116   -179    549   -121       C  
ATOM   5066  CG  TYR D  33     -18.926 -42.165  96.332  1.00 25.92           C  
ANISOU 5066  CG  TYR D  33     3256   3188   3406   -208    489    -80       C  
ATOM   5067  CD1 TYR D  33     -20.213 -42.274  95.799  1.00 19.04           C  
ANISOU 5067  CD1 TYR D  33     2358   2414   2464   -353    436    -20       C  
ATOM   5068  CD2 TYR D  33     -18.798 -41.807  97.672  1.00 20.33           C  
ANISOU 5068  CD2 TYR D  33     2460   2502   2763    -98    490    -97       C  
ATOM   5069  CE1 TYR D  33     -21.337 -42.022  96.597  1.00 19.27           C  
ANISOU 5069  CE1 TYR D  33     2256   2562   2506   -364    397     26       C  
ATOM   5070  CE2 TYR D  33     -19.899 -41.581  98.461  1.00 20.58           C  
ANISOU 5070  CE2 TYR D  33     2392   2636   2791   -119    463    -68       C  
ATOM   5071  CZ  TYR D  33     -21.159 -41.691  97.930  1.00 24.09           C  
ANISOU 5071  CZ  TYR D  33     2792   3178   3183   -241    423     -6       C  
ATOM   5072  OH  TYR D  33     -22.227 -41.455  98.765  1.00 28.30           O  
ANISOU 5072  OH  TYR D  33     3204   3823   3727   -245    414     28       O  
ATOM   5073  N   VAL D  34     -15.432 -40.321  93.294  1.00 17.86           N  
ANISOU 5073  N   VAL D  34     2303   1976   2507    -67    602   -154       N  
ATOM   5074  CA  VAL D  34     -14.243 -40.466  92.463  1.00 18.14           C  
ANISOU 5074  CA  VAL D  34     2417   1929   2545    -47    688   -189       C  
ATOM   5075  C   VAL D  34     -13.001 -40.694  93.316  1.00 19.47           C  
ANISOU 5075  C   VAL D  34     2553   2042   2803    101    748   -218       C  
ATOM   5076  O   VAL D  34     -12.273 -41.672  93.115  1.00 21.20           O  
ANISOU 5076  O   VAL D  34     2873   2171   3012    132    847   -244       O  
ATOM   5077  CB  VAL D  34     -14.082 -39.246  91.547  1.00 24.22           C  
ANISOU 5077  CB  VAL D  34     3130   2737   3335    -73    655   -166       C  
ATOM   5078  CG1 VAL D  34     -12.666 -39.145  91.055  1.00 24.14           C  
ANISOU 5078  CG1 VAL D  34     3146   2663   3362    -14    748   -203       C  
ATOM   5079  CG2 VAL D  34     -15.035 -39.363  90.384  1.00 24.41           C  
ANISOU 5079  CG2 VAL D  34     3233   2799   3244   -244    615   -126       C  
ATOM   5080  N   ALA D  35     -12.723 -39.792  94.261  1.00 17.28           N  
ANISOU 5080  N   ALA D  35     2137   1815   2615    192    693   -208       N  
ATOM   5081  CA  ALA D  35     -11.436 -39.845  94.945  1.00 19.60           C  
ANISOU 5081  CA  ALA D  35     2378   2080   2989    310    730   -215       C  
ATOM   5082  C   ALA D  35     -11.431 -40.853  96.084  1.00 25.06           C  
ANISOU 5082  C   ALA D  35     3092   2748   3681    361    733   -206       C  
ATOM   5083  O   ALA D  35     -10.385 -41.451  96.380  1.00 22.93           O  
ANISOU 5083  O   ALA D  35     2823   2430   3460    448    787   -193       O  
ATOM   5084  CB  ALA D  35     -11.063 -38.465  95.472  1.00 16.79           C  
ANISOU 5084  CB  ALA D  35     1890   1784   2706    353    666   -209       C  
ATOM   5085  N   PHE D  36     -12.577 -41.046  96.729  1.00 17.65           N  
ANISOU 5085  N   PHE D  36     2164   1849   2694    310    678   -201       N  
ATOM   5086  CA  PHE D  36     -12.747 -42.030  97.787  1.00 17.43           C  
ANISOU 5086  CA  PHE D  36     2177   1802   2645    331    675   -187       C  
ATOM   5087  C   PHE D  36     -14.066 -42.745  97.553  1.00 18.48           C  
ANISOU 5087  C   PHE D  36     2404   1938   2680    213    668   -186       C  
ATOM   5088  O   PHE D  36     -15.081 -42.100  97.260  1.00 18.91           O  
ANISOU 5088  O   PHE D  36     2409   2069   2705    138    619   -181       O  
ATOM   5089  CB  PHE D  36     -12.751 -41.363  99.170  1.00 17.05           C  
ANISOU 5089  CB  PHE D  36     2020   1825   2631    375    605   -178       C  
ATOM   5090  CG  PHE D  36     -11.464 -40.691  99.526  1.00 17.32           C  
ANISOU 5090  CG  PHE D  36     1965   1871   2745    458    593   -169       C  
ATOM   5091  CD1 PHE D  36     -10.434 -41.411 100.109  1.00 19.79           C  
ANISOU 5091  CD1 PHE D  36     2272   2153   3095    533    606   -127       C  
ATOM   5092  CD2 PHE D  36     -11.294 -39.323  99.315  1.00 19.31           C  
ANISOU 5092  CD2 PHE D  36     2134   2168   3036    455    562   -188       C  
ATOM   5093  CE1 PHE D  36      -9.249 -40.788 100.462  1.00 26.12           C  
ANISOU 5093  CE1 PHE D  36     2968   2990   3965    590    580   -100       C  
ATOM   5094  CE2 PHE D  36     -10.113 -38.702  99.643  1.00 18.00           C  
ANISOU 5094  CE2 PHE D  36     1889   2022   2929    501    544   -176       C  
ATOM   5095  CZ  PHE D  36      -9.090 -39.423 100.221  1.00 24.07           C  
ANISOU 5095  CZ  PHE D  36     2634   2783   3729    562    548   -129       C  
ATOM   5096  N   ASP D  37     -14.054 -44.069  97.666  1.00 22.47           N  
ANISOU 5096  N   ASP D  37     3040   2361   3138    194    717   -181       N  
ATOM   5097  CA  ASP D  37     -15.274 -44.836  97.460  1.00 18.74           C  
ANISOU 5097  CA  ASP D  37     2671   1892   2556     54    709   -177       C  
ATOM   5098  C   ASP D  37     -16.213 -44.686  98.657  1.00 18.46           C  
ANISOU 5098  C   ASP D  37     2557   1956   2503     26    638   -154       C  
ATOM   5099  O   ASP D  37     -15.788 -44.415  99.777  1.00 19.49           O  
ANISOU 5099  O   ASP D  37     2612   2109   2684    115    614   -147       O  
ATOM   5100  CB  ASP D  37     -14.938 -46.311  97.235  1.00 22.92           C  
ANISOU 5100  CB  ASP D  37     3396   2276   3035     36    796   -184       C  
ATOM   5101  CG  ASP D  37     -14.046 -46.512  96.037  1.00 28.78           C  
ANISOU 5101  CG  ASP D  37     4234   2913   3791     64    899   -217       C  
ATOM   5102  OD1 ASP D  37     -14.157 -45.699  95.097  1.00 28.60           O  
ANISOU 5102  OD1 ASP D  37     4170   2942   3755     11    887   -234       O  
ATOM   5103  OD2 ASP D  37     -13.235 -47.462  96.036  1.00 28.00           O  
ANISOU 5103  OD2 ASP D  37     4248   2675   3715    143   1000   -220       O  
ATOM   5104  N   ALA D  38     -17.510 -44.889  98.406  1.00 18.75           N  
ANISOU 5104  N   ALA D  38     2611   2058   2456   -114    606   -138       N  
ATOM   5105  CA  ALA D  38     -18.500 -44.770  99.476  1.00 25.57           C  
ANISOU 5105  CA  ALA D  38     3391   3027   3297   -149    559   -115       C  
ATOM   5106  C   ALA D  38     -18.136 -45.611 100.699  1.00 22.09           C  
ANISOU 5106  C   ALA D  38     3013   2536   2844   -109    573   -109       C  
ATOM   5107  O   ALA D  38     -18.244 -45.142 101.838  1.00 24.84           O  
ANISOU 5107  O   ALA D  38     3269   2953   3215    -62    547   -107       O  
ATOM   5108  CB  ALA D  38     -19.885 -45.166  98.964  1.00 19.37           C  
ANISOU 5108  CB  ALA D  38     2626   2319   2415   -324    530    -80       C  
ATOM   5109  N   HIS D  39     -17.715 -46.863 100.496  1.00 22.27           N  
ANISOU 5109  N   HIS D  39     3206   2432   2823   -132    620   -104       N  
ATOM   5110  CA  HIS D  39     -17.402 -47.691 101.663  1.00 20.05           C  
ANISOU 5110  CA  HIS D  39     2989   2098   2531    -95    623    -77       C  
ATOM   5111  C   HIS D  39     -16.147 -47.187 102.375  1.00 22.35           C  
ANISOU 5111  C   HIS D  39     3194   2375   2923     70    612    -66       C  
ATOM   5112  O   HIS D  39     -16.008 -47.347 103.595  1.00 21.29           O  
ANISOU 5112  O   HIS D  39     3039   2266   2783     98    577    -35       O  
ATOM   5113  CB  HIS D  39     -17.255 -49.154 101.250  1.00 21.11           C  
ANISOU 5113  CB  HIS D  39     3342   2075   2605   -148    686    -66       C  
ATOM   5114  CG  HIS D  39     -15.961 -49.454 100.559  1.00 30.40           C  
ANISOU 5114  CG  HIS D  39     4593   3103   3853    -25    764    -77       C  
ATOM   5115  ND1 HIS D  39     -15.790 -49.300  99.201  1.00 27.56           N  
ANISOU 5115  ND1 HIS D  39     4288   2696   3487    -54    822   -121       N  
ATOM   5116  CD2 HIS D  39     -14.770 -49.882 101.041  1.00 29.26           C  
ANISOU 5116  CD2 HIS D  39     4467   2858   3793    131    800    -41       C  
ATOM   5117  CE1 HIS D  39     -14.554 -49.631  98.873  1.00 27.36           C  
ANISOU 5117  CE1 HIS D  39     4315   2542   3539     83    908   -123       C  
ATOM   5118  NE2 HIS D  39     -13.914 -49.988  99.971  1.00 31.12           N  
ANISOU 5118  NE2 HIS D  39     4758   2985   4081    205    895    -68       N  
ATOM   5119  N   GLU D  40     -15.243 -46.542 101.643  1.00 19.67           N  
ANISOU 5119  N   GLU D  40     2799   2010   2665    161    634    -86       N  
ATOM   5120  CA  GLU D  40     -14.098 -45.920 102.294  1.00 25.80           C  
ANISOU 5120  CA  GLU D  40     3468   2805   3531    290    608    -68       C  
ATOM   5121  C   GLU D  40     -14.526 -44.734 103.153  1.00 20.82           C  
ANISOU 5121  C   GLU D  40     2703   2306   2901    275    541    -86       C  
ATOM   5122  O   GLU D  40     -14.042 -44.569 104.277  1.00 19.97           O  
ANISOU 5122  O   GLU D  40     2551   2233   2803    314    498    -61       O  
ATOM   5123  CB  GLU D  40     -13.072 -45.497 101.243  1.00 28.15           C  
ANISOU 5123  CB  GLU D  40     3734   3054   3910    371    656    -83       C  
ATOM   5124  CG  GLU D  40     -12.423 -46.682 100.517  1.00 30.44           C  
ANISOU 5124  CG  GLU D  40     4163   3191   4212    417    754    -68       C  
ATOM   5125  CD  GLU D  40     -11.388 -46.242  99.496  1.00 27.05           C  
ANISOU 5125  CD  GLU D  40     3692   2724   3860    497    821    -85       C  
ATOM   5126  OE1 GLU D  40     -11.652 -45.261  98.776  1.00 24.74           O  
ANISOU 5126  OE1 GLU D  40     3341   2498   3562    447    805   -127       O  
ATOM   5127  OE2 GLU D  40     -10.312 -46.873  99.420  1.00 27.22           O  
ANISOU 5127  OE2 GLU D  40     3737   2653   3953    614    894    -48       O  
ATOM   5128  N   LEU D  41     -15.435 -43.896 102.643  1.00 26.76           N  
ANISOU 5128  N   LEU D  41     3397   3130   3641    218    535   -124       N  
ATOM   5129  CA  LEU D  41     -15.909 -42.763 103.430  1.00 17.60           C  
ANISOU 5129  CA  LEU D  41     2128   2072   2489    218    502   -149       C  
ATOM   5130  C   LEU D  41     -16.676 -43.231 104.655  1.00 21.02           C  
ANISOU 5130  C   LEU D  41     2582   2558   2847    159    490   -138       C  
ATOM   5131  O   LEU D  41     -16.574 -42.622 105.730  1.00 18.66           O  
ANISOU 5131  O   LEU D  41     2237   2312   2542    175    472   -155       O  
ATOM   5132  CB  LEU D  41     -16.780 -41.851 102.571  1.00 18.19           C  
ANISOU 5132  CB  LEU D  41     2131   2199   2580    186    507   -170       C  
ATOM   5133  CG  LEU D  41     -15.952 -41.213 101.462  1.00 24.98           C  
ANISOU 5133  CG  LEU D  41     2970   3015   3508    236    513   -180       C  
ATOM   5134  CD1 LEU D  41     -16.745 -40.171 100.709  1.00 24.91           C  
ANISOU 5134  CD1 LEU D  41     2883   3057   3523    214    503   -183       C  
ATOM   5135  CD2 LEU D  41     -14.684 -40.614 102.061  1.00 18.71           C  
ANISOU 5135  CD2 LEU D  41     2132   2205   2773    321    498   -191       C  
ATOM   5136  N   ALA D  42     -17.457 -44.309 104.509  1.00 22.03           N  
ANISOU 5136  N   ALA D  42     2794   2672   2904     73    505   -114       N  
ATOM   5137  CA  ALA D  42     -18.203 -44.829 105.650  1.00 29.22           C  
ANISOU 5137  CA  ALA D  42     3732   3636   3733      1    500    -97       C  
ATOM   5138  C   ALA D  42     -17.252 -45.276 106.751  1.00 25.80           C  
ANISOU 5138  C   ALA D  42     3349   3165   3289     45    471    -66       C  
ATOM   5139  O   ALA D  42     -17.464 -44.972 107.933  1.00 22.71           O  
ANISOU 5139  O   ALA D  42     2932   2845   2852     20    454    -72       O  
ATOM   5140  CB  ALA D  42     -19.113 -45.976 105.202  1.00 23.62           C  
ANISOU 5140  CB  ALA D  42     3120   2910   2943   -120    516    -68       C  
ATOM   5141  N   ARG D  43     -16.171 -45.959 106.372  1.00 22.63           N  
ANISOU 5141  N   ARG D  43     3014   2655   2930    113    467    -27       N  
ATOM   5142  CA  ARG D  43     -15.170 -46.369 107.345  1.00 25.12           C  
ANISOU 5142  CA  ARG D  43     3351   2940   3252    169    425     34       C  
ATOM   5143  C   ARG D  43     -14.436 -45.166 107.933  1.00 33.12           C  
ANISOU 5143  C   ARG D  43     4249   4028   4306    218    379     17       C  
ATOM   5144  O   ARG D  43     -14.230 -45.098 109.150  1.00 32.71           O  
ANISOU 5144  O   ARG D  43     4195   4030   4204    190    328     45       O  
ATOM   5145  CB  ARG D  43     -14.192 -47.342 106.700  1.00 28.70           C  
ANISOU 5145  CB  ARG D  43     3883   3256   3768    256    451     91       C  
ATOM   5146  CG  ARG D  43     -13.197 -47.924 107.668  1.00 38.76           C  
ANISOU 5146  CG  ARG D  43     5168   4496   5061    323    401    189       C  
ATOM   5147  CD  ARG D  43     -12.128 -48.693 106.912  1.00 43.96           C  
ANISOU 5147  CD  ARG D  43     5868   5015   5817    451    452    247       C  
ATOM   5148  NE  ARG D  43     -11.114 -49.235 107.808  1.00 51.80           N  
ANISOU 5148  NE  ARG D  43     6844   5985   6853    537    396    371       N  
ATOM   5149  CZ  ARG D  43      -9.890 -49.573 107.421  1.00 58.17           C  
ANISOU 5149  CZ  ARG D  43     7609   6714   7778    685    424    448       C  
ATOM   5150  NH1 ARG D  43      -9.531 -49.412 106.156  1.00 58.92           N  
ANISOU 5150  NH1 ARG D  43     7693   6744   7949    754    520    395       N  
ATOM   5151  NH2 ARG D  43      -9.025 -50.066 108.296  1.00 62.40           N  
ANISOU 5151  NH2 ARG D  43     8108   7245   8357    762    359    587       N  
ATOM   5152  N   ILE D  44     -14.052 -44.195 107.097  1.00 24.23           N  
ANISOU 5152  N   ILE D  44     3041   2908   3257    271    393    -27       N  
ATOM   5153  CA  ILE D  44     -13.480 -42.967 107.646  1.00 19.01           C  
ANISOU 5153  CA  ILE D  44     2290   2315   2618    287    353    -54       C  
ATOM   5154  C   ILE D  44     -14.455 -42.317 108.611  1.00 28.32           C  
ANISOU 5154  C   ILE D  44     3465   3579   3718    207    358   -109       C  
ATOM   5155  O   ILE D  44     -14.075 -41.896 109.709  1.00 30.09           O  
ANISOU 5155  O   ILE D  44     3687   3853   3895    174    317   -110       O  
ATOM   5156  CB  ILE D  44     -13.068 -41.995 106.527  1.00 20.75           C  
ANISOU 5156  CB  ILE D  44     2438   2522   2926    339    375    -95       C  
ATOM   5157  CG1 ILE D  44     -11.798 -42.511 105.834  1.00 23.32           C  
ANISOU 5157  CG1 ILE D  44     2751   2779   3330    425    378    -37       C  
ATOM   5158  CG2 ILE D  44     -12.885 -40.574 107.092  1.00 19.84           C  
ANISOU 5158  CG2 ILE D  44     2258   2470   2812    321    350   -146       C  
ATOM   5159  CD1 ILE D  44     -11.347 -41.672 104.644  1.00 24.14           C  
ANISOU 5159  CD1 ILE D  44     2795   2867   3509    463    409    -72       C  
ATOM   5160  N   ASP D  45     -15.732 -42.240 108.226  1.00 22.58           N  
ANISOU 5160  N   ASP D  45     2737   2875   2969    168    413   -152       N  
ATOM   5161  CA  ASP D  45     -16.692 -41.544 109.064  1.00 21.99           C  
ANISOU 5161  CA  ASP D  45     2640   2878   2837    114    449   -207       C  
ATOM   5162  C   ASP D  45     -16.885 -42.270 110.389  1.00 27.53           C  
ANISOU 5162  C   ASP D  45     3413   3619   3429     37    432   -180       C  
ATOM   5163  O   ASP D  45     -17.014 -41.630 111.438  1.00 25.79           O  
ANISOU 5163  O   ASP D  45     3198   3454   3147     -6    445   -222       O  
ATOM   5164  CB  ASP D  45     -18.019 -41.376 108.326  1.00 26.49           C  
ANISOU 5164  CB  ASP D  45     3162   3481   3423     97    508   -229       C  
ATOM   5165  CG  ASP D  45     -18.869 -40.230 108.896  1.00 43.16           C  
ANISOU 5165  CG  ASP D  45     5208   5658   5531     97    573   -292       C  
ATOM   5166  OD1 ASP D  45     -18.467 -39.635 109.918  1.00 43.81           O  
ANISOU 5166  OD1 ASP D  45     5317   5752   5577     90    580   -335       O  
ATOM   5167  OD2 ASP D  45     -19.934 -39.913 108.321  1.00 46.64           O  
ANISOU 5167  OD2 ASP D  45     5575   6140   6007    102    621   -294       O  
ATOM   5168  N   ALA D  46     -16.868 -43.603 110.372  1.00 29.60           N  
ANISOU 5168  N   ALA D  46     3748   3842   3656     10    408   -110       N  
ATOM   5169  CA  ALA D  46     -16.951 -44.343 111.624  1.00 26.51           C  
ANISOU 5169  CA  ALA D  46     3436   3479   3157    -68    380    -66       C  
ATOM   5170  C   ALA D  46     -15.703 -44.135 112.471  1.00 32.81           C  
ANISOU 5170  C   ALA D  46     4242   4282   3941    -53    299    -23       C  
ATOM   5171  O   ALA D  46     -15.791 -43.969 113.695  1.00 37.69           O  
ANISOU 5171  O   ALA D  46     4898   4966   4456   -136    279    -27       O  
ATOM   5172  CB  ALA D  46     -17.165 -45.827 111.338  1.00 24.23           C  
ANISOU 5172  CB  ALA D  46     3242   3122   2841    -97    373      9       C  
ATOM   5173  N   LEU D  47     -14.534 -44.138 111.837  1.00 24.69           N  
ANISOU 5173  N   LEU D  47     3176   3196   3010     40    253     23       N  
ATOM   5174  CA  LEU D  47     -13.283 -44.003 112.570  1.00 22.57           C  
ANISOU 5174  CA  LEU D  47     2888   2949   2737     49    160     92       C  
ATOM   5175  C   LEU D  47     -13.179 -42.646 113.256  1.00 26.17           C  
ANISOU 5175  C   LEU D  47     3312   3488   3144    -15    148     15       C  
ATOM   5176  O   LEU D  47     -12.849 -42.568 114.445  1.00 32.11           O  
ANISOU 5176  O   LEU D  47     4103   4302   3796   -104     85     46       O  
ATOM   5177  CB  LEU D  47     -12.111 -44.215 111.618  1.00 21.83           C  
ANISOU 5177  CB  LEU D  47     2733   2788   2775    171    136    156       C  
ATOM   5178  CG  LEU D  47     -11.807 -45.671 111.268  1.00 28.61           C  
ANISOU 5178  CG  LEU D  47     3650   3545   3675    240    139    260       C  
ATOM   5179  CD1 LEU D  47     -10.975 -45.724 109.997  1.00 29.07           C  
ANISOU 5179  CD1 LEU D  47     3651   3523   3870    368    179    276       C  
ATOM   5180  CD2 LEU D  47     -11.073 -46.338 112.421  1.00 28.26           C  
ANISOU 5180  CD2 LEU D  47     3626   3522   3590    227     40    395       C  
ATOM   5181  N   GLN D  48     -13.449 -41.562 112.521  1.00 25.28           N  
ANISOU 5181  N   GLN D  48     3144   3368   3093     20    210    -82       N  
ATOM   5182  CA  GLN D  48     -13.294 -40.229 113.097  1.00 24.65           C  
ANISOU 5182  CA  GLN D  48     3059   3334   2972    -36    214   -162       C  
ATOM   5183  C   GLN D  48     -14.241 -40.010 114.270  1.00 28.56           C  
ANISOU 5183  C   GLN D  48     3635   3885   3332   -144    267   -227       C  
ATOM   5184  O   GLN D  48     -13.887 -39.317 115.230  1.00 27.41           O  
ANISOU 5184  O   GLN D  48     3538   3781   3094   -235    244   -263       O  
ATOM   5185  CB  GLN D  48     -13.512 -39.162 112.027  1.00 21.25           C  
ANISOU 5185  CB  GLN D  48     2568   2864   2641     31    280   -244       C  
ATOM   5186  CG  GLN D  48     -14.922 -39.095 111.473  1.00 24.29           C  
ANISOU 5186  CG  GLN D  48     2942   3236   3048     60    384   -303       C  
ATOM   5187  CD  GLN D  48     -15.828 -38.100 112.192  1.00 29.89           C  
ANISOU 5187  CD  GLN D  48     3678   3977   3703     17    475   -404       C  
ATOM   5188  OE1 GLN D  48     -15.396 -37.345 113.073  1.00 28.22           O  
ANISOU 5188  OE1 GLN D  48     3520   3778   3425    -45    470   -452       O  
ATOM   5189  NE2 GLN D  48     -17.106 -38.099 111.816  1.00 30.02           N  
ANISOU 5189  NE2 GLN D  48     3658   4004   3743     45    565   -432       N  
ATOM   5190  N   ALA D  49     -15.430 -40.620 114.229  1.00 31.62           N  
ANISOU 5190  N   ALA D  49     4042   4278   3694   -150    340   -242       N  
ATOM   5191  CA  ALA D  49     -16.410 -40.440 115.293  1.00 34.37           C  
ANISOU 5191  CA  ALA D  49     4454   4686   3919   -246    417   -305       C  
ATOM   5192  C   ALA D  49     -15.892 -40.922 116.638  1.00 39.49           C  
ANISOU 5192  C   ALA D  49     5197   5386   4420   -368    338   -251       C  
ATOM   5193  O   ALA D  49     -16.418 -40.513 117.680  1.00 43.64           O  
ANISOU 5193  O   ALA D  49     5797   5964   4818   -472    399   -319       O  
ATOM   5194  CB  ALA D  49     -17.707 -41.167 114.935  1.00 33.88           C  
ANISOU 5194  CB  ALA D  49     4374   4639   3861   -241    495   -301       C  
ATOM   5195  N   ARG D  50     -14.868 -41.772 116.636  1.00 32.55           N  
ANISOU 5195  N   ARG D  50     4319   4492   3557   -357    210   -125       N  
ATOM   5196  CA  ARG D  50     -14.244 -42.267 117.850  1.00 28.87           C  
ANISOU 5196  CA  ARG D  50     3928   4079   2961   -469    104    -36       C  
ATOM   5197  C   ARG D  50     -13.143 -41.355 118.367  1.00 33.92           C  
ANISOU 5197  C   ARG D  50     4563   4762   3562   -532     17    -35       C  
ATOM   5198  O   ARG D  50     -12.531 -41.661 119.397  1.00 33.51           O  
ANISOU 5198  O   ARG D  50     4567   4774   3392   -646    -93     53       O  
ATOM   5199  CB  ARG D  50     -13.691 -43.663 117.590  1.00 29.43           C  
ANISOU 5199  CB  ARG D  50     3992   4105   3083   -410     11    123       C  
ATOM   5200  CG  ARG D  50     -14.765 -44.602 117.131  1.00 32.30           C  
ANISOU 5200  CG  ARG D  50     4390   4421   3460   -386     91    122       C  
ATOM   5201  CD  ARG D  50     -14.296 -46.027 117.128  1.00 42.16           C  
ANISOU 5201  CD  ARG D  50     5685   5607   4727   -354     13    275       C  
ATOM   5202  NE  ARG D  50     -15.420 -46.956 117.222  1.00 51.58           N  
ANISOU 5202  NE  ARG D  50     6965   6779   5854   -414     74    277       N  
ATOM   5203  CZ  ARG D  50     -15.311 -48.210 117.649  1.00 56.00           C  
ANISOU 5203  CZ  ARG D  50     7619   7292   6367   -444     19    402       C  
ATOM   5204  NH1 ARG D  50     -14.129 -48.679 118.027  1.00 60.50           N  
ANISOU 5204  NH1 ARG D  50     8194   7833   6962   -400   -100    545       N  
ATOM   5205  NH2 ARG D  50     -16.381 -48.991 117.704  1.00 53.77           N  
ANISOU 5205  NH2 ARG D  50     7421   6993   6015   -522     80    396       N  
ATOM   5206  N   LEU D  51     -12.880 -40.249 117.686  1.00 35.58           N  
ANISOU 5206  N   LEU D  51     4530   5211   3778    615    190     74       N  
ATOM   5207  CA  LEU D  51     -11.831 -39.347 118.121  1.00 38.65           C  
ANISOU 5207  CA  LEU D  51     4885   5719   4084    613     15     20       C  
ATOM   5208  C   LEU D  51     -12.349 -38.393 119.197  1.00 36.48           C  
ANISOU 5208  C   LEU D  51     4686   5527   3648    574      6   -110       C  
ATOM   5209  O   LEU D  51     -13.524 -38.010 119.187  1.00 37.55           O  
ANISOU 5209  O   LEU D  51     4852   5605   3810    545    122   -206       O  
ATOM   5210  CB  LEU D  51     -11.288 -38.545 116.933  1.00 34.35           C  
ANISOU 5210  CB  LEU D  51     4226   5117   3707    563    -75    -64       C  
ATOM   5211  CG  LEU D  51     -10.635 -39.353 115.802  1.00 30.50           C  
ANISOU 5211  CG  LEU D  51     3661   4555   3373    600    -71     45       C  
ATOM   5212  CD1 LEU D  51     -10.223 -38.476 114.634  1.00 26.38           C  
ANISOU 5212  CD1 LEU D  51     3043   3978   3002    535   -138    -46       C  
ATOM   5213  CD2 LEU D  51      -9.445 -40.139 116.318  1.00 33.32           C  
ANISOU 5213  CD2 LEU D  51     3997   5017   3644    694   -146    198       C  
ATOM   5214  N   PRO D  52     -11.490 -38.012 120.140  1.00 29.02           N  
ANISOU 5214  N   PRO D  52     3770   4728   2528    576   -129   -116       N  
ATOM   5215  CA  PRO D  52     -11.848 -36.959 121.101  1.00 32.77           C  
ANISOU 5215  CA  PRO D  52     4335   5274   2843    524   -149   -271       C  
ATOM   5216  C   PRO D  52     -12.121 -35.630 120.403  1.00 34.32           C  
ANISOU 5216  C   PRO D  52     4499   5375   3166    449   -169   -457       C  
ATOM   5217  O   PRO D  52     -11.344 -35.178 119.559  1.00 32.55           O  
ANISOU 5217  O   PRO D  52     4185   5117   3067    404   -275   -482       O  
ATOM   5218  CB  PRO D  52     -10.609 -36.870 122.000  1.00 36.29           C  
ANISOU 5218  CB  PRO D  52     4791   5903   3096    521   -331   -232       C  
ATOM   5219  CG  PRO D  52      -9.882 -38.167 121.791  1.00 36.95           C  
ANISOU 5219  CG  PRO D  52     4813   6023   3206    620   -357    -14       C  
ATOM   5220  CD  PRO D  52     -10.143 -38.550 120.377  1.00 29.99           C  
ANISOU 5220  CD  PRO D  52     3842   4969   2585    630   -269     17       C  
ATOM   5221  N   GLU D  53     -13.225 -34.996 120.771  1.00 34.68           N  
ANISOU 5221  N   GLU D  53     4626   5376   3176    442    -56   -583       N  
ATOM   5222  CA  GLU D  53     -13.643 -33.758 120.131  1.00 30.59           C  
ANISOU 5222  CA  GLU D  53     4102   4744   2778    404    -48   -748       C  
ATOM   5223  C   GLU D  53     -13.349 -32.580 121.050  1.00 30.53           C  
ANISOU 5223  C   GLU D  53     4214   4784   2603    346   -120   -911       C  
ATOM   5224  O   GLU D  53     -13.450 -32.698 122.271  1.00 32.21           O  
ANISOU 5224  O   GLU D  53     4532   5107   2598    354   -101   -927       O  
ATOM   5225  CB  GLU D  53     -15.131 -33.814 119.778  1.00 32.78           C  
ANISOU 5225  CB  GLU D  53     4369   4932   3156    456    135   -780       C  
ATOM   5226  CG  GLU D  53     -15.661 -32.625 118.994  1.00 31.70           C  
ANISOU 5226  CG  GLU D  53     4217   4668   3161    457    152   -919       C  
ATOM   5227  CD  GLU D  53     -17.003 -32.927 118.365  1.00 34.89           C  
ANISOU 5227  CD  GLU D  53     4543   5013   3701    517    303   -904       C  
ATOM   5228  OE1 GLU D  53     -17.095 -32.955 117.111  1.00 35.00           O  
ANISOU 5228  OE1 GLU D  53     4460   4941   3899    515    283   -873       O  
ATOM   5229  OE2 GLU D  53     -17.958 -33.171 119.130  1.00 38.84           O  
ANISOU 5229  OE2 GLU D  53     5074   5570   4115    558    442   -918       O  
ATOM   5230  N   GLU D  54     -12.962 -31.452 120.465  1.00 30.56           N  
ANISOU 5230  N   GLU D  54     4218   4697   2697    279   -198  -1034       N  
ATOM   5231  CA  GLU D  54     -12.760 -30.273 121.287  1.00 34.01           C  
ANISOU 5231  CA  GLU D  54     4798   5143   2982    207   -247  -1212       C  
ATOM   5232  C   GLU D  54     -13.406 -29.059 120.642  1.00 32.90           C  
ANISOU 5232  C   GLU D  54     4714   4812   2973    210   -179  -1363       C  
ATOM   5233  O   GLU D  54     -13.451 -28.953 119.415  1.00 32.81           O  
ANISOU 5233  O   GLU D  54     4612   4685   3171    221   -180  -1326       O  
ATOM   5234  CB  GLU D  54     -11.268 -30.001 121.522  1.00 40.82           C  
ANISOU 5234  CB  GLU D  54     5639   6114   3756     80   -454  -1222       C  
ATOM   5235  CG  GLU D  54     -10.437 -29.868 120.267  1.00 51.93           C  
ANISOU 5235  CG  GLU D  54     6909   7457   5366     19   -548  -1176       C  
ATOM   5236  CD  GLU D  54      -8.947 -29.875 120.565  1.00 67.90           C  
ANISOU 5236  CD  GLU D  54     8857   9645   7299    -96   -746  -1148       C  
ATOM   5237  OE1 GLU D  54      -8.510 -30.752 121.342  1.00 73.38           O  
ANISOU 5237  OE1 GLU D  54     9514  10524   7843    -56   -808  -1036       O  
ATOM   5238  OE2 GLU D  54      -8.218 -28.999 120.039  1.00 70.27           O  
ANISOU 5238  OE2 GLU D  54     9132   9896   7672   -228   -837  -1234       O  
ATOM   5239  N   PRO D  55     -13.923 -28.133 121.441  1.00 38.07           N  
ANISOU 5239  N   PRO D  55     5536   5426   3503    213   -113  -1530       N  
ATOM   5240  CA  PRO D  55     -14.482 -26.907 120.863  1.00 41.47           C  
ANISOU 5240  CA  PRO D  55     6046   5656   4055    237    -47  -1671       C  
ATOM   5241  C   PRO D  55     -13.373 -25.987 120.382  1.00 38.25           C  
ANISOU 5241  C   PRO D  55     5680   5161   3691     89   -194  -1749       C  
ATOM   5242  O   PRO D  55     -12.306 -25.908 120.992  1.00 43.56           O  
ANISOU 5242  O   PRO D  55     6384   5945   4221    -50   -333  -1780       O  
ATOM   5243  CB  PRO D  55     -15.266 -26.290 122.026  1.00 41.76           C  
ANISOU 5243  CB  PRO D  55     6267   5687   3913    289     78  -1826       C  
ATOM   5244  CG  PRO D  55     -14.602 -26.828 123.250  1.00 43.79           C  
ANISOU 5244  CG  PRO D  55     6581   6143   3916    209     -1  -1811       C  
ATOM   5245  CD  PRO D  55     -14.127 -28.208 122.898  1.00 38.55           C  
ANISOU 5245  CD  PRO D  55     5732   5613   3302    216    -72  -1591       C  
ATOM   5246  N   VAL D  56     -13.628 -25.306 119.265  1.00 36.79           N  
ANISOU 5246  N   VAL D  56     5489   4789   3703    113   -165  -1771       N  
ATOM   5247  CA  VAL D  56     -12.696 -24.334 118.694  1.00 41.89           C  
ANISOU 5247  CA  VAL D  56     6193   5314   4411    -33   -272  -1846       C  
ATOM   5248  C   VAL D  56     -13.485 -23.108 118.269  1.00 43.84           C  
ANISOU 5248  C   VAL D  56     6595   5313   4748     39   -163  -1969       C  
ATOM   5249  O   VAL D  56     -14.472 -23.224 117.534  1.00 42.08           O  
ANISOU 5249  O   VAL D  56     6310   5008   4670    200    -60  -1906       O  
ATOM   5250  CB  VAL D  56     -11.914 -24.899 117.489  1.00 40.60           C  
ANISOU 5250  CB  VAL D  56     5843   5170   4415    -88   -367  -1694       C  
ATOM   5251  CG1 VAL D  56     -11.127 -23.790 116.805  1.00 39.43           C  
ANISOU 5251  CG1 VAL D  56     5765   4869   4346   -237   -439  -1773       C  
ATOM   5252  CG2 VAL D  56     -10.982 -26.019 117.923  1.00 41.15           C  
ANISOU 5252  CG2 VAL D  56     5769   5472   4395   -148   -480  -1575       C  
ATOM   5253  N   THR D  57     -13.053 -21.936 118.726  1.00 48.83           N  
ANISOU 5253  N   THR D  57     7434   5827   5292    -79   -188  -2142       N  
ATOM   5254  CA  THR D  57     -13.706 -20.695 118.334  1.00 54.41           C  
ANISOU 5254  CA  THR D  57     8326   6265   6083     -5    -81  -2259       C  
ATOM   5255  C   THR D  57     -13.482 -20.435 116.849  1.00 53.59           C  
ANISOU 5255  C   THR D  57     8151   6013   6197    -12   -114  -2162       C  
ATOM   5256  O   THR D  57     -12.362 -20.570 116.344  1.00 53.11           O  
ANISOU 5256  O   THR D  57     8010   5994   6176   -187   -241  -2107       O  
ATOM   5257  CB  THR D  57     -13.174 -19.524 119.159  1.00 61.12           C  
ANISOU 5257  CB  THR D  57     9443   7002   6779   -163   -101  -2474       C  
ATOM   5258  OG1 THR D  57     -11.831 -19.236 118.759  1.00 65.64           O  
ANISOU 5258  OG1 THR D  57     9993   7575   7374   -408   -261  -2472       O  
ATOM   5259  CG2 THR D  57     -13.192 -19.863 120.645  1.00 59.90           C  
ANISOU 5259  CG2 THR D  57     9355   7031   6371   -193   -100  -2563       C  
ATOM   5260  N   ALA D  58     -14.554 -20.087 116.146  1.00 49.73           N  
ANISOU 5260  N   ALA D  58     7681   5371   5844    185      3  -2134       N  
ATOM   5261  CA  ALA D  58     -14.479 -19.755 114.730  1.00 44.82           C  
ANISOU 5261  CA  ALA D  58     7024   4597   5410    203    -17  -2041       C  
ATOM   5262  C   ALA D  58     -15.360 -18.535 114.504  1.00 45.27           C  
ANISOU 5262  C   ALA D  58     7280   4393   5526    358    107  -2125       C  
ATOM   5263  O   ALA D  58     -15.717 -17.813 115.440  1.00 44.94           O  
ANISOU 5263  O   ALA D  58     7364   4306   5404    376    200  -2242       O  
ATOM   5264  CB  ALA D  58     -14.878 -20.953 113.861  1.00 43.58           C  
ANISOU 5264  CB  ALA D  58     6605   4581   5373    305    -29  -1850       C  
ATOM   5265  N   GLY D  59     -15.736 -18.301 113.255  1.00 48.63           N  
ANISOU 5265  N   GLY D  59     7658   4701   6118    457    125  -2011       N  
ATOM   5266  CA  GLY D  59     -16.482 -17.101 112.946  1.00 55.26           C  
ANISOU 5266  CA  GLY D  59     8602   5345   7050    581    241  -2016       C  
ATOM   5267  C   GLY D  59     -15.553 -15.947 112.646  1.00 58.06           C  
ANISOU 5267  C   GLY D  59     9110   5513   7437    404    194  -2066       C  
ATOM   5268  O   GLY D  59     -14.484 -16.144 112.060  1.00 61.51           O  
ANISOU 5268  O   GLY D  59     9522   5955   7895    214     88  -2023       O  
ATOM   5269  N   ASP D  60     -15.944 -14.739 113.043  1.00 59.13           N  
ANISOU 5269  N   ASP D  60     9400   5490   7579    465    271  -2150       N  
ATOM   5270  CA  ASP D  60     -15.129 -13.550 112.863  1.00 57.67           C  
ANISOU 5270  CA  ASP D  60     9386   5115   7411    306    235  -2201       C  
ATOM   5271  C   ASP D  60     -14.967 -12.865 114.214  1.00 63.95           C  
ANISOU 5271  C   ASP D  60    10339   5886   8072    232    261  -2380       C  
ATOM   5272  O   ASP D  60     -15.593 -13.249 115.206  1.00 66.23           O  
ANISOU 5272  O   ASP D  60    10608   6293   8264    332    319  -2456       O  
ATOM   5273  CB  ASP D  60     -15.750 -12.599 111.828  1.00 56.82           C  
ANISOU 5273  CB  ASP D  60     9356   4789   7445    462    302  -2108       C  
ATOM   5274  N   ALA D  61     -14.107 -11.844 114.251  1.00 64.30           N  
ANISOU 5274  N   ALA D  61    10547   5780   8104     47    222  -2446       N  
ATOM   5275  CA  ALA D  61     -13.817 -11.165 115.513  1.00 65.00           C  
ANISOU 5275  CA  ALA D  61    10800   5843   8053    -59    233  -2621       C  
ATOM   5276  C   ALA D  61     -15.065 -10.506 116.097  1.00 69.58           C  
ANISOU 5276  C   ALA D  61    11501   6313   8625    182    386  -2694       C  
ATOM   5277  O   ALA D  61     -15.273 -10.520 117.318  1.00 71.43           O  
ANISOU 5277  O   ALA D  61    11794   6627   8718    187    421  -2827       O  
ATOM   5278  CB  ALA D  61     -12.705 -10.139 115.306  1.00 57.70           C  
ANISOU 5278  CB  ALA D  61    10027   4761   7135   -306    176  -2665       C  
ATOM   5279  N   GLY D  62     -15.912  -9.928 115.243  1.00 69.62           N  
ANISOU 5279  N   GLY D  62    11537   6144   8771    390    477  -2603       N  
ATOM   5280  CA  GLY D  62     -17.150  -9.341 115.727  1.00 68.68           C  
ANISOU 5280  CA  GLY D  62    11500   5936   8659    643    625  -2655       C  
ATOM   5281  C   GLY D  62     -18.197 -10.368 116.110  1.00 67.82           C  
ANISOU 5281  C   GLY D  62    11194   6039   8534    847    687  -2626       C  
ATOM   5282  O   GLY D  62     -18.976 -10.145 117.041  1.00 67.51           O  
ANISOU 5282  O   GLY D  62    11204   6020   8428    982    797  -2723       O  
ATOM   5283  N   ASP D  63     -18.234 -11.502 115.410  1.00 65.94           N  
ANISOU 5283  N   ASP D  63    10737   5964   8354    867    629  -2492       N  
ATOM   5284  CA  ASP D  63     -19.236 -12.544 115.635  1.00 67.10           C  
ANISOU 5284  CA  ASP D  63    10680   6315   8499   1048    694  -2440       C  
ATOM   5285  C   ASP D  63     -18.505 -13.878 115.740  1.00 62.27           C  
ANISOU 5285  C   ASP D  63     9928   5922   7809    886    592  -2409       C  
ATOM   5286  O   ASP D  63     -18.112 -14.452 114.720  1.00 58.69           O  
ANISOU 5286  O   ASP D  63     9365   5495   7437    837    511  -2282       O  
ATOM   5287  CB  ASP D  63     -20.267 -12.563 114.506  1.00 70.88           C  
ANISOU 5287  CB  ASP D  63    11025   6759   9146   1286    744  -2278       C  
ATOM   5288  CG  ASP D  63     -21.404 -13.542 114.762  1.00 74.67           C  
ANISOU 5288  CG  ASP D  63    11284   7454   9633   1472    824  -2224       C  
ATOM   5289  OD1 ASP D  63     -21.494 -14.084 115.886  1.00 77.75           O  
ANISOU 5289  OD1 ASP D  63    11653   7994   9896   1438    870  -2320       O  
ATOM   5290  OD2 ASP D  63     -22.212 -13.771 113.837  1.00 73.34           O  
ANISOU 5290  OD2 ASP D  63    10960   7316   9591   1643    839  -2079       O  
ATOM   5291  N   THR D  64     -18.326 -14.374 116.963  1.00 61.07           N  
ANISOU 5291  N   THR D  64     9788   5927   7489    810    596  -2518       N  
ATOM   5292  CA  THR D  64     -17.618 -15.627 117.201  1.00 59.84           C  
ANISOU 5292  CA  THR D  64     9522   5984   7232    663    499  -2492       C  
ATOM   5293  C   THR D  64     -18.598 -16.769 117.461  1.00 56.84           C  
ANISOU 5293  C   THR D  64     8970   5798   6828    828    588  -2422       C  
ATOM   5294  O   THR D  64     -19.602 -16.601 118.160  1.00 60.89           O  
ANISOU 5294  O   THR D  64     9481   6346   7311    984    724  -2473       O  
ATOM   5295  CB  THR D  64     -16.651 -15.503 118.384  1.00 60.67           C  
ANISOU 5295  CB  THR D  64     9751   6163   7138    450    417  -2638       C  
ATOM   5296  OG1 THR D  64     -17.347 -15.002 119.533  1.00 62.42           O  
ANISOU 5296  OG1 THR D  64    10080   6385   7251    546    533  -2765       O  
ATOM   5297  CG2 THR D  64     -15.488 -14.578 118.044  1.00 60.07           C  
ANISOU 5297  CG2 THR D  64     9804   5935   7086    235    303  -2680       C  
ATOM   5298  N   HIS D  65     -18.292 -17.936 116.900  1.00 51.49           N  
ANISOU 5298  N   HIS D  65     8148   5251   6163    793    511  -2303       N  
ATOM   5299  CA  HIS D  65     -19.071 -19.142 117.132  1.00 52.45           C  
ANISOU 5299  CA  HIS D  65     8097   5579   6253    928    564  -2224       C  
ATOM   5300  C   HIS D  65     -18.114 -20.306 117.334  1.00 49.99           C  
ANISOU 5300  C   HIS D  65     7700   5457   5838    781    416  -2195       C  
ATOM   5301  O   HIS D  65     -16.981 -20.297 116.849  1.00 48.46           O  
ANISOU 5301  O   HIS D  65     7505   5239   5669    595    273  -2160       O  
ATOM   5302  CB  HIS D  65     -20.027 -19.451 115.966  1.00 55.47           C  
ANISOU 5302  CB  HIS D  65     8289   5964   6824   1119    600  -2071       C  
ATOM   5303  CG  HIS D  65     -21.030 -18.372 115.701  1.00 62.20           C  
ANISOU 5303  CG  HIS D  65     9172   6667   7792   1286    724  -2073       C  
ATOM   5304  ND1 HIS D  65     -22.287 -18.369 116.266  1.00 64.59           N  
ANISOU 5304  ND1 HIS D  65     9390   7050   8102   1462    874  -2084       N  
ATOM   5305  CD2 HIS D  65     -20.962 -17.261 114.931  1.00 63.83           C  
ANISOU 5305  CD2 HIS D  65     9472   6663   8117   1311    709  -2063       C  
ATOM   5306  CE1 HIS D  65     -22.948 -17.300 115.860  1.00 66.68           C  
ANISOU 5306  CE1 HIS D  65     9689   7163   8484   1600    935  -2086       C  
ATOM   5307  NE2 HIS D  65     -22.166 -16.610 115.049  1.00 67.31           N  
ANISOU 5307  NE2 HIS D  65     9886   7059   8628   1518    836  -2069       N  
ATOM   5308  N   ASP D  66     -18.581 -21.317 118.056  1.00 49.28           N  
ANISOU 5308  N   ASP D  66     7483   5584   5659    823    468  -2150       N  
ATOM   5309  CA  ASP D  66     -17.791 -22.520 118.264  1.00 46.09           C  
ANISOU 5309  CA  ASP D  66     6936   5388   5189    674    354  -2042       C  
ATOM   5310  C   ASP D  66     -18.088 -23.532 117.169  1.00 45.43           C  
ANISOU 5310  C   ASP D  66     6606   5383   5274    723    329  -1853       C  
ATOM   5311  O   ASP D  66     -19.250 -23.759 116.818  1.00 45.65           O  
ANISOU 5311  O   ASP D  66     6524   5427   5392    886    438  -1806       O  
ATOM   5312  CB  ASP D  66     -18.071 -23.137 119.634  1.00 47.50           C  
ANISOU 5312  CB  ASP D  66     7136   5748   5165    680    425  -2078       C  
ATOM   5313  CG  ASP D  66     -17.289 -22.465 120.752  1.00 54.85           C  
ANISOU 5313  CG  ASP D  66     8294   6668   5879    542    376  -2241       C  
ATOM   5314  OD1 ASP D  66     -16.597 -21.453 120.490  1.00 56.98           O  
ANISOU 5314  OD1 ASP D  66     8711   6773   6165    436    302  -2344       O  
ATOM   5315  OD2 ASP D  66     -17.367 -22.958 121.899  1.00 52.13           O  
ANISOU 5315  OD2 ASP D  66     7987   6482   5338    527    413  -2268       O  
ATOM   5316  N   ILE D  67     -17.032 -24.115 116.614  1.00 40.28           N  
ANISOU 5316  N   ILE D  67     5863   4782   4659    579    188  -1753       N  
ATOM   5317  CA  ILE D  67     -17.133 -25.340 115.844  1.00 32.62           C  
ANISOU 5317  CA  ILE D  67     4680   3922   3794    591    164  -1582       C  
ATOM   5318  C   ILE D  67     -16.395 -26.412 116.635  1.00 32.20           C  
ANISOU 5318  C   ILE D  67     4576   4052   3607    490    105  -1517       C  
ATOM   5319  O   ILE D  67     -15.618 -26.115 117.546  1.00 31.82           O  
ANISOU 5319  O   ILE D  67     4638   4048   3404    392     41  -1594       O  
ATOM   5320  CB  ILE D  67     -16.569 -25.191 114.414  1.00 33.11           C  
ANISOU 5320  CB  ILE D  67     4679   3881   4020    539     71  -1503       C  
ATOM   5321  CG1 ILE D  67     -15.044 -25.110 114.437  1.00 35.65           C  
ANISOU 5321  CG1 ILE D  67     5035   4216   4297    352    -69  -1504       C  
ATOM   5322  CG2 ILE D  67     -17.160 -23.960 113.743  1.00 35.53           C  
ANISOU 5322  CG2 ILE D  67     5085   3987   4427    638    116  -1568       C  
ATOM   5323  CD1 ILE D  67     -14.421 -25.089 113.060  1.00 35.99           C  
ANISOU 5323  CD1 ILE D  67     5006   4182   4489    290   -143  -1416       C  
ATOM   5324  N   TYR D  68     -16.654 -27.672 116.297  1.00 27.44           N  
ANISOU 5324  N   TYR D  68     3815   3556   3055    516    126  -1373       N  
ATOM   5325  CA  TYR D  68     -16.169 -28.803 117.082  1.00 34.11           C  
ANISOU 5325  CA  TYR D  68     4622   4565   3774    466    101  -1288       C  
ATOM   5326  C   TYR D  68     -15.230 -29.635 116.223  1.00 33.98           C  
ANISOU 5326  C   TYR D  68     4486   4576   3849    398     -2  -1150       C  
ATOM   5327  O   TYR D  68     -15.606 -30.072 115.132  1.00 35.47           O  
ANISOU 5327  O   TYR D  68     4571   4717   4191    430     24  -1070       O  
ATOM   5328  CB  TYR D  68     -17.351 -29.608 117.620  1.00 27.66           C  
ANISOU 5328  CB  TYR D  68     3758   3837   2915    558    253  -1244       C  
ATOM   5329  CG  TYR D  68     -18.247 -28.651 118.348  1.00 29.35           C  
ANISOU 5329  CG  TYR D  68     4081   4015   3056    641    367  -1391       C  
ATOM   5330  CD1 TYR D  68     -17.913 -28.200 119.616  1.00 34.92           C  
ANISOU 5330  CD1 TYR D  68     4946   4766   3555    607    368  -1497       C  
ATOM   5331  CD2 TYR D  68     -19.362 -28.110 117.731  1.00 29.56           C  
ANISOU 5331  CD2 TYR D  68     4059   3958   3214    758    467  -1432       C  
ATOM   5332  CE1 TYR D  68     -18.695 -27.277 120.272  1.00 37.82           C  
ANISOU 5332  CE1 TYR D  68     5438   5083   3851    690    487  -1646       C  
ATOM   5333  CE2 TYR D  68     -20.153 -27.190 118.375  1.00 31.19           C  
ANISOU 5333  CE2 TYR D  68     4367   4121   3362    861    584  -1567       C  
ATOM   5334  CZ  TYR D  68     -19.816 -26.776 119.646  1.00 36.03           C  
ANISOU 5334  CZ  TYR D  68     5156   4764   3772    827    604  -1679       C  
ATOM   5335  OH  TYR D  68     -20.603 -25.850 120.278  1.00 40.00           O  
ANISOU 5335  OH  TYR D  68     5778   5208   4211    938    739  -1825       O  
ATOM   5336  N   VAL D  69     -14.005 -29.832 116.712  1.00 32.77           N  
ANISOU 5336  N   VAL D  69     4346   4511   3595    307   -120  -1126       N  
ATOM   5337  CA  VAL D  69     -12.889 -30.327 115.913  1.00 30.86           C  
ANISOU 5337  CA  VAL D  69     3998   4289   3438    242   -228  -1021       C  
ATOM   5338  C   VAL D  69     -12.404 -31.661 116.473  1.00 31.14           C  
ANISOU 5338  C   VAL D  69     3972   4475   3385    261   -248   -882       C  
ATOM   5339  O   VAL D  69     -12.287 -31.833 117.692  1.00 34.17           O  
ANISOU 5339  O   VAL D  69     4422   4974   3587    262   -262   -892       O  
ATOM   5340  CB  VAL D  69     -11.735 -29.297 115.888  1.00 28.50           C  
ANISOU 5340  CB  VAL D  69     3742   3969   3117    115   -361  -1109       C  
ATOM   5341  CG1 VAL D  69     -10.529 -29.857 115.158  1.00 30.17           C  
ANISOU 5341  CG1 VAL D  69     3819   4238   3407     53   -460   -996       C  
ATOM   5342  CG2 VAL D  69     -12.186 -27.996 115.239  1.00 27.74           C  
ANISOU 5342  CG2 VAL D  69     3735   3685   3118    102   -328  -1229       C  
ATOM   5343  N   ARG D  70     -12.107 -32.599 115.578  1.00 28.64           N  
ANISOU 5343  N   ARG D  70     3545   4149   3187    282   -247   -749       N  
ATOM   5344  CA  ARG D  70     -11.437 -33.846 115.933  1.00 31.33           C  
ANISOU 5344  CA  ARG D  70     3833   4603   3467    313   -273   -600       C  
ATOM   5345  C   ARG D  70     -10.117 -33.886 115.174  1.00 28.00           C  
ANISOU 5345  C   ARG D  70     3307   4202   3129    268   -385   -543       C  
ATOM   5346  O   ARG D  70     -10.109 -34.046 113.950  1.00 32.95           O  
ANISOU 5346  O   ARG D  70     3871   4732   3917    267   -355   -508       O  
ATOM   5347  CB  ARG D  70     -12.309 -35.066 115.612  1.00 30.26           C  
ANISOU 5347  CB  ARG D  70     3679   4428   3392    387   -137   -490       C  
ATOM   5348  CG  ARG D  70     -13.478 -35.261 116.588  1.00 34.45           C  
ANISOU 5348  CG  ARG D  70     4292   4988   3809    426    -16   -517       C  
ATOM   5349  CD  ARG D  70     -14.313 -36.503 116.270  1.00 30.43           C  
ANISOU 5349  CD  ARG D  70     3761   4441   3359    462    123   -409       C  
ATOM   5350  NE  ARG D  70     -15.134 -36.903 117.415  1.00 31.17           N  
ANISOU 5350  NE  ARG D  70     3933   4600   3309    487    236   -398       N  
ATOM   5351  CZ  ARG D  70     -16.448 -36.712 117.497  1.00 32.24           C  
ANISOU 5351  CZ  ARG D  70     4069   4717   3466    490    368   -464       C  
ATOM   5352  NH1 ARG D  70     -17.099 -36.139 116.489  1.00 30.39           N  
ANISOU 5352  NH1 ARG D  70     3756   4402   3389    483    388   -539       N  
ATOM   5353  NH2 ARG D  70     -17.112 -37.093 118.585  1.00 30.26           N  
ANISOU 5353  NH2 ARG D  70     3888   4537   3072    505    482   -449       N  
ATOM   5354  N   ARG D  71      -9.007 -33.744 115.900  1.00 30.20           N  
ANISOU 5354  N   ARG D  71     3561   4623   3291    226   -514   -535       N  
ATOM   5355  CA  ARG D  71      -7.691 -33.625 115.285  1.00 25.40           C  
ANISOU 5355  CA  ARG D  71     2829   4068   2754    168   -626   -497       C  
ATOM   5356  C   ARG D  71      -7.110 -34.995 114.949  1.00 27.20           C  
ANISOU 5356  C   ARG D  71     2953   4354   3028    272   -610   -314       C  
ATOM   5357  O   ARG D  71      -7.146 -35.921 115.766  1.00 32.06           O  
ANISOU 5357  O   ARG D  71     3593   5057   3532    366   -596   -210       O  
ATOM   5358  CB  ARG D  71      -6.756 -32.857 116.209  1.00 27.32           C  
ANISOU 5358  CB  ARG D  71     3068   4463   2851     64   -779   -575       C  
ATOM   5359  CG  ARG D  71      -7.272 -31.480 116.543  1.00 28.90           C  
ANISOU 5359  CG  ARG D  71     3404   4576   3001    -42   -781   -769       C  
ATOM   5360  CD  ARG D  71      -6.186 -30.570 117.112  1.00 34.41           C  
ANISOU 5360  CD  ARG D  71     4091   5391   3591   -203   -940   -869       C  
ATOM   5361  NE  ARG D  71      -6.763 -29.345 117.658  1.00 38.15           N  
ANISOU 5361  NE  ARG D  71     4747   5769   3981   -292   -924  -1062       N  
ATOM   5362  CZ  ARG D  71      -7.082 -28.278 116.930  1.00 42.44           C  
ANISOU 5362  CZ  ARG D  71     5370   6117   4639   -364   -876  -1179       C  
ATOM   5363  NH1 ARG D  71      -6.867 -28.270 115.616  1.00 43.59           N  
ANISOU 5363  NH1 ARG D  71     5425   6157   4979   -372   -850  -1120       N  
ATOM   5364  NH2 ARG D  71      -7.621 -27.219 117.518  1.00 45.63           N  
ANISOU 5364  NH2 ARG D  71     5961   6422   4955   -418   -847  -1351       N  
ATOM   5365  N   ILE D  72      -6.585 -35.120 113.733  1.00 25.55           N  
ANISOU 5365  N   ILE D  72     2644   4084   2979    262   -600   -272       N  
ATOM   5366  CA  ILE D  72      -5.884 -36.313 113.293  1.00 25.25           C  
ANISOU 5366  CA  ILE D  72     2507   4086   2999    364   -578   -112       C  
ATOM   5367  C   ILE D  72      -4.378 -36.083 113.218  1.00 35.54           C  
ANISOU 5367  C   ILE D  72     3649   5546   4309    328   -707    -78       C  
ATOM   5368  O   ILE D  72      -3.595 -36.936 113.646  1.00 32.61           O  
ANISOU 5368  O   ILE D  72     3190   5313   3886    433   -750     55       O  
ATOM   5369  CB  ILE D  72      -6.437 -36.796 111.934  1.00 24.86           C  
ANISOU 5369  CB  ILE D  72     2467   3860   3118    393   -447    -84       C  
ATOM   5370  CG1 ILE D  72      -7.884 -37.283 112.099  1.00 33.60           C  
ANISOU 5370  CG1 ILE D  72     3699   4856   4210    433   -323    -91       C  
ATOM   5371  CG2 ILE D  72      -5.545 -37.885 111.344  1.00 23.31           C  
ANISOU 5371  CG2 ILE D  72     2176   3688   2993    491   -417     61       C  
ATOM   5372  CD1 ILE D  72      -8.622 -37.584 110.807  1.00 27.44           C  
ANISOU 5372  CD1 ILE D  72     2939   3915   3574    425   -211    -96       C  
HETATM 5373  N   MSE D  73      -3.959 -34.935 112.679  1.00 34.66           N  
ANISOU 5373  N   MSE D  73     3491   5417   4260    181   -765   -190       N  
HETATM 5374  CA  MSE D  73      -2.549 -34.561 112.573  1.00 38.53           C  
ANISOU 5374  CA  MSE D  73     3809   6067   4763    102   -884   -179       C  
HETATM 5375  C   MSE D  73      -2.371 -33.052 112.780  1.00 37.22           C  
ANISOU 5375  C   MSE D  73     3678   5904   4562   -105   -976   -349       C  
HETATM 5376  O   MSE D  73      -3.078 -32.242 112.181  1.00 41.53           O  
ANISOU 5376  O   MSE D  73     4339   6263   5178   -184   -912   -455       O  
HETATM 5377  CB  MSE D  73      -1.978 -34.988 111.218  1.00 30.76           C  
ANISOU 5377  CB  MSE D  73     2708   5029   3951    135   -809   -101       C  
HETATM 5378  CG  MSE D  73      -0.604 -34.426 110.902  1.00 43.12           C  
ANISOU 5378  CG  MSE D  73     4081   6743   5559     21   -904   -109       C  
HETATM 5379 SE   MSE D  73       0.202 -35.338 109.365  1.00 49.11          SE  
ANISOU 5379 SE   MSE D  73     4679   7476   6506    128   -779     27      SE  
HETATM 5380  CE  MSE D  73       0.814 -36.931 110.301  1.00 55.31           C  
ANISOU 5380  CE  MSE D  73     5352   8457   7207    390   -808    229       C  
ATOM   5381  N   VAL D  74      -1.432 -32.692 113.647  1.00 34.04           N  
ANISOU 5381  N   VAL D  74     3182   5712   4041   -193  -1128   -374       N  
ATOM   5382  CA  VAL D  74      -1.155 -31.303 113.969  1.00 35.20           C  
ANISOU 5382  CA  VAL D  74     3373   5869   4131   -415  -1222   -544       C  
ATOM   5383  C   VAL D  74       0.143 -30.899 113.296  1.00 38.57           C  
ANISOU 5383  C   VAL D  74     3602   6403   4651   -555  -1290   -538       C  
ATOM   5384  O   VAL D  74       1.009 -31.725 112.997  1.00 41.36           O  
ANISOU 5384  O   VAL D  74     3750   6910   5056   -467  -1309   -399       O  
ATOM   5385  CB  VAL D  74      -1.074 -31.036 115.494  1.00 33.62           C  
ANISOU 5385  CB  VAL D  74     3232   5837   3704   -465  -1352   -612       C  
ATOM   5386  CG1 VAL D  74      -2.410 -31.322 116.157  1.00 34.69           C  
ANISOU 5386  CG1 VAL D  74     3574   5861   3745   -344  -1260   -633       C  
ATOM   5387  CG2 VAL D  74       0.050 -31.844 116.122  1.00 34.59           C  
ANISOU 5387  CG2 VAL D  74     3149   6261   3734   -401  -1489   -478       C  
ATOM   5388  N   ASP D  75       0.285 -29.595 113.076  1.00 41.61           N  
ANISOU 5388  N   ASP D  75     4053   6702   5054   -778  -1317   -690       N  
ATOM   5389  CA  ASP D  75       1.430 -29.028 112.397  1.00 38.65           C  
ANISOU 5389  CA  ASP D  75     3514   6401   4769   -960  -1362   -707       C  
ATOM   5390  C   ASP D  75       1.824 -27.744 113.126  1.00 40.03           C  
ANISOU 5390  C   ASP D  75     3756   6622   4833  -1229  -1483   -885       C  
ATOM   5391  O   ASP D  75       1.735 -26.643 112.598  1.00 35.87           O  
ANISOU 5391  O   ASP D  75     3358   5898   4372  -1401  -1434   -997       O  
ATOM   5392  CB  ASP D  75       1.107 -28.775 110.929  1.00 40.88           C  
ANISOU 5392  CB  ASP D  75     3849   6446   5237   -969  -1212   -696       C  
ATOM   5393  CG  ASP D  75       2.333 -28.408 110.130  1.00 42.84           C  
ANISOU 5393  CG  ASP D  75     3905   6785   5587  -1132  -1226   -678       C  
ATOM   5394  OD1 ASP D  75       3.446 -28.643 110.639  1.00 42.34           O  
ANISOU 5394  OD1 ASP D  75     3638   6967   5481  -1169  -1332   -629       O  
ATOM   5395  OD2 ASP D  75       2.178 -27.888 109.005  1.00 41.13           O  
ANISOU 5395  OD2 ASP D  75     3759   6377   5492  -1204  -1120   -698       O  
ATOM   5396  N   ARG D  76       2.244 -27.898 114.378  1.00 47.41           N  
ANISOU 5396  N   ARG D  76     4663   7744   5606  -1225  -1610   -882       N  
ATOM   5397  CA  ARG D  76       2.487 -26.756 115.247  1.00 50.83           C  
ANISOU 5397  CA  ARG D  76     5239   8149   5924  -1424  -1692  -1035       C  
ATOM   5398  C   ARG D  76       3.674 -25.943 114.742  1.00 51.50           C  
ANISOU 5398  C   ARG D  76     5223   8231   6114  -1624  -1715  -1058       C  
ATOM   5399  O   ARG D  76       4.573 -26.460 114.074  1.00 54.19           O  
ANISOU 5399  O   ARG D  76     5332   8688   6570  -1590  -1707   -934       O  
ATOM   5400  CB  ARG D  76       2.719 -27.229 116.687  1.00 55.55           C  
ANISOU 5400  CB  ARG D  76     5817   8972   6317  -1360  -1826  -1011       C  
ATOM   5401  CG  ARG D  76       1.538 -28.024 117.279  1.00 52.50           C  
ANISOU 5401  CG  ARG D  76     5545   8601   5801  -1164  -1794   -986       C  
ATOM   5402  CD  ARG D  76       1.793 -28.515 118.717  1.00 61.00           C  
ANISOU 5402  CD  ARG D  76     6622   9900   6657  -1096  -1920   -942       C  
ATOM   5403  NE  ARG D  76       0.544 -28.840 119.417  1.00 66.89           N  
ANISOU 5403  NE  ARG D  76     7561  10613   7243   -976  -1872   -983       N  
ATOM   5404  CZ  ARG D  76       0.159 -30.066 119.773  1.00 64.67           C  
ANISOU 5404  CZ  ARG D  76     7244  10439   6888   -745  -1852   -828       C  
ATOM   5405  NH1 ARG D  76      -0.999 -30.242 120.399  1.00 57.25           N  
ANISOU 5405  NH1 ARG D  76     6525   9384   5843   -637  -1752   -856       N  
ATOM   5406  NH2 ARG D  76       0.929 -31.116 119.517  1.00 66.17           N  
ANISOU 5406  NH2 ARG D  76     7208  10795   7137   -601  -1895   -625       N  
ATOM   5407  N   ALA D  77       3.660 -24.650 115.057  1.00 49.80           N  
ANISOU 5407  N   ALA D  77     5193   7872   5858  -1827  -1728  -1222       N  
ATOM   5408  CA  ALA D  77       4.687 -23.748 114.553  1.00 49.88           C  
ANISOU 5408  CA  ALA D  77     5139   7850   5963  -2039  -1731  -1261       C  
ATOM   5409  C   ALA D  77       6.066 -24.178 115.037  1.00 52.86           C  
ANISOU 5409  C   ALA D  77     5243   8534   6309  -2072  -1860  -1181       C  
ATOM   5410  O   ALA D  77       6.265 -24.447 116.226  1.00 54.15           O  
ANISOU 5410  O   ALA D  77     5383   8879   6310  -2045  -1988  -1192       O  
ATOM   5411  CB  ALA D  77       4.390 -22.314 114.990  1.00 54.18           C  
ANISOU 5411  CB  ALA D  77     5954   8187   6446  -2233  -1725  -1452       C  
ATOM   5412  N   GLY D  78       7.016 -24.249 114.104  1.00 50.49           N  
ANISOU 5412  N   GLY D  78     4735   8292   6158  -2122  -1822  -1099       N  
ATOM   5413  CA  GLY D  78       8.369 -24.672 114.401  1.00 51.75           C  
ANISOU 5413  CA  GLY D  78     4608   8740   6314  -2139  -1924  -1017       C  
ATOM   5414  C   GLY D  78       8.562 -26.158 114.595  1.00 53.98           C  
ANISOU 5414  C   GLY D  78     4685   9243   6583  -1869  -1960   -839       C  
ATOM   5415  O   GLY D  78       9.660 -26.575 114.978  1.00 59.21           O  
ANISOU 5415  O   GLY D  78     5113  10158   7227  -1849  -2056   -763       O  
ATOM   5416  N   GLU D  79       7.544 -26.974 114.337  1.00 53.34           N  
ANISOU 5416  N   GLU D  79     4683   9071   6512  -1657  -1881   -767       N  
ATOM   5417  CA  GLU D  79       7.588 -28.403 114.607  1.00 51.92           C  
ANISOU 5417  CA  GLU D  79     4359   9063   6304  -1382  -1900   -596       C  
ATOM   5418  C   GLU D  79       7.315 -29.211 113.346  1.00 47.98           C  
ANISOU 5418  C   GLU D  79     3788   8470   5971  -1210  -1745   -475       C  
ATOM   5419  O   GLU D  79       6.788 -28.701 112.355  1.00 52.27           O  
ANISOU 5419  O   GLU D  79     4435   8803   6623  -1290  -1627   -531       O  
ATOM   5420  CB  GLU D  79       6.566 -28.790 115.676  1.00 49.87           C  
ANISOU 5420  CB  GLU D  79     4277   8807   5866  -1263  -1954   -612       C  
ATOM   5421  CG  GLU D  79       6.739 -28.063 116.988  1.00 51.41           C  
ANISOU 5421  CG  GLU D  79     4572   9090   5872  -1415  -2100   -735       C  
ATOM   5422  CD  GLU D  79       5.735 -28.531 118.016  1.00 58.29           C  
ANISOU 5422  CD  GLU D  79     5618   9973   6556  -1281  -2134   -738       C  
ATOM   5423  OE1 GLU D  79       4.886 -29.380 117.660  1.00 55.48           O  
ANISOU 5423  OE1 GLU D  79     5300   9550   6228  -1083  -2039   -648       O  
ATOM   5424  OE2 GLU D  79       5.793 -28.059 119.173  1.00 63.77           O  
ANISOU 5424  OE2 GLU D  79     6415  10745   7070  -1377  -2248   -832       O  
ATOM   5425  N   ARG D  80       7.699 -30.486 113.396  1.00 45.82           N  
ANISOU 5425  N   ARG D  80     3350   8348   5712   -967  -1741   -306       N  
ATOM   5426  CA  ARG D  80       7.334 -31.432 112.363  1.00 47.03           C  
ANISOU 5426  CA  ARG D  80     3466   8408   5996   -764  -1589   -186       C  
ATOM   5427  C   ARG D  80       5.864 -31.817 112.526  1.00 42.15           C  
ANISOU 5427  C   ARG D  80     3053   7648   5316   -644  -1539   -193       C  
ATOM   5428  O   ARG D  80       5.300 -31.667 113.613  1.00 41.14           O  
ANISOU 5428  O   ARG D  80     3054   7552   5025   -655  -1631   -249       O  
ATOM   5429  CB  ARG D  80       8.213 -32.680 112.445  1.00 48.07           C  
ANISOU 5429  CB  ARG D  80     3390   8720   6154   -526  -1590     -7       C  
ATOM   5430  CG  ARG D  80       9.576 -32.572 111.798  1.00 53.19           C  
ANISOU 5430  CG  ARG D  80     3803   9483   6924   -582  -1569     27       C  
ATOM   5431  CD  ARG D  80      10.060 -33.950 111.351  1.00 56.96           C  
ANISOU 5431  CD  ARG D  80     4137  10022   7482   -293  -1476    204       C  
ATOM   5432  NE  ARG D  80      11.240 -33.849 110.494  1.00 63.51           N  
ANISOU 5432  NE  ARG D  80     4751  10931   8448   -339  -1413    227       N  
ATOM   5433  CZ  ARG D  80      11.652 -34.798 109.657  1.00 60.88           C  
ANISOU 5433  CZ  ARG D  80     4313  10588   8230   -138  -1275    342       C  
ATOM   5434  NH1 ARG D  80      12.731 -34.601 108.917  1.00 54.46           N  
ANISOU 5434  NH1 ARG D  80     3301   9860   7530   -200  -1217    347       N  
ATOM   5435  NH2 ARG D  80      10.980 -35.937 109.547  1.00 65.87           N  
ANISOU 5435  NH2 ARG D  80     5052  11115   8861    121  -1183    444       N  
ATOM   5436  N   PRO D  81       5.216 -32.306 111.461  1.00 41.94           N  
ANISOU 5436  N   PRO D  81     3060   7468   5409   -535  -1390   -143       N  
ATOM   5437  CA  PRO D  81       3.836 -32.786 111.608  1.00 40.58           C  
ANISOU 5437  CA  PRO D  81     3051   7185   5181   -404  -1339   -140       C  
ATOM   5438  C   PRO D  81       3.802 -33.987 112.539  1.00 45.70           C  
ANISOU 5438  C   PRO D  81     3680   7963   5721   -162  -1380      2       C  
ATOM   5439  O   PRO D  81       4.767 -34.749 112.634  1.00 49.48           O  
ANISOU 5439  O   PRO D  81     4009   8566   6224    -29  -1390    134       O  
ATOM   5440  CB  PRO D  81       3.432 -33.170 110.181  1.00 32.51           C  
ANISOU 5440  CB  PRO D  81     2067   5951   4333   -323  -1151    -93       C  
ATOM   5441  CG  PRO D  81       4.445 -32.499 109.296  1.00 33.60           C  
ANISOU 5441  CG  PRO D  81     2048   6133   4586   -494  -1136   -122       C  
ATOM   5442  CD  PRO D  81       5.699 -32.444 110.076  1.00 36.36           C  
ANISOU 5442  CD  PRO D  81     2245   6689   4883   -528  -1255    -93       C  
ATOM   5443  N   GLN D  82       2.681 -34.152 113.241  1.00 43.27           N  
ANISOU 5443  N   GLN D  82     3576   7564   5299    -96  -1370    -27       N  
ATOM   5444  CA  GLN D  82       2.619 -35.169 114.283  1.00 41.37           C  
ANISOU 5444  CA  GLN D  82     3344   7459   4918    104  -1422    102       C  
ATOM   5445  C   GLN D  82       1.201 -35.717 114.395  1.00 43.90           C  
ANISOU 5445  C   GLN D  82     3921   7541   5217    228  -1282    113       C  
ATOM   5446  O   GLN D  82       0.246 -34.947 114.539  1.00 39.86           O  
ANISOU 5446  O   GLN D  82     3598   6876   4673    112  -1249    -30       O  
ATOM   5447  CB  GLN D  82       3.100 -34.590 115.624  1.00 37.70           C  
ANISOU 5447  CB  GLN D  82     2864   7206   4255    -13  -1614     38       C  
ATOM   5448  N   LEU D  83       1.072 -37.044 114.315  1.00 42.14           N  
ANISOU 5448  N   LEU D  83     3706   7288   5018    462  -1190    284       N  
ATOM   5449  CA  LEU D  83      -0.215 -37.696 114.515  1.00 39.47           C  
ANISOU 5449  CA  LEU D  83     3595   6753   4649    569  -1057    310       C  
ATOM   5450  C   LEU D  83      -0.662 -37.534 115.958  1.00 39.43           C  
ANISOU 5450  C   LEU D  83     3711   6847   4423    556  -1146    281       C  
ATOM   5451  O   LEU D  83       0.143 -37.642 116.887  1.00 34.83           O  
ANISOU 5451  O   LEU D  83     3030   6510   3695    589  -1298    344       O  
ATOM   5452  CB  LEU D  83      -0.132 -39.186 114.182  1.00 36.34           C  
ANISOU 5452  CB  LEU D  83     3193   6302   4313    807   -939    503       C  
ATOM   5453  CG  LEU D  83      -0.501 -39.707 112.794  1.00 36.49           C  
ANISOU 5453  CG  LEU D  83     3251   6089   4523    855   -754    522       C  
ATOM   5454  CD1 LEU D  83      -0.597 -41.214 112.830  1.00 39.81           C  
ANISOU 5454  CD1 LEU D  83     3739   6437   4949   1086   -637    701       C  
ATOM   5455  CD2 LEU D  83      -1.795 -39.120 112.271  1.00 38.51           C  
ANISOU 5455  CD2 LEU D  83     3680   6120   4831    723   -658    378       C  
ATOM   5456  N   VAL D  84      -1.957 -37.277 116.145  1.00 33.10           N  
ANISOU 5456  N   VAL D  84     3117   5869   3589    513  -1049    186       N  
ATOM   5457  CA  VAL D  84      -2.564 -37.200 117.465  1.00 34.52           C  
ANISOU 5457  CA  VAL D  84     3445   6112   3559    513  -1086    156       C  
ATOM   5458  C   VAL D  84      -3.754 -38.149 117.491  1.00 32.91           C  
ANISOU 5458  C   VAL D  84     3408   5734   3363    637   -907    232       C  
ATOM   5459  O   VAL D  84      -4.176 -38.669 116.463  1.00 39.55           O  
ANISOU 5459  O   VAL D  84     4260   6397   4371    685   -768    269       O  
ATOM   5460  CB  VAL D  84      -2.999 -35.768 117.824  1.00 34.75           C  
ANISOU 5460  CB  VAL D  84     3567   6116   3520    313  -1139    -64       C  
ATOM   5461  CG1 VAL D  84      -1.807 -34.825 117.783  1.00 33.60           C  
ANISOU 5461  CG1 VAL D  84     3268   6132   3368    152  -1310   -148       C  
ATOM   5462  CG2 VAL D  84      -4.068 -35.304 116.863  1.00 36.01           C  
ANISOU 5462  CG2 VAL D  84     3827   6015   3839    262   -987   -170       C  
ATOM   5463  N   ASN D  85      -4.283 -38.383 118.691  1.00 35.08           N  
ANISOU 5463  N   ASN D  85     3816   6069   3442    676   -908    252       N  
ATOM   5464  CA  ASN D  85      -5.490 -39.195 118.877  1.00 35.91           C  
ANISOU 5464  CA  ASN D  85     4090   6024   3530    757   -730    310       C  
ATOM   5465  C   ASN D  85      -5.354 -40.586 118.258  1.00 34.92           C  
ANISOU 5465  C   ASN D  85     3950   5802   3515    916   -619    499       C  
ATOM   5466  O   ASN D  85      -6.286 -41.109 117.646  1.00 37.70           O  
ANISOU 5466  O   ASN D  85     4391   5959   3975    926   -450    506       O  
ATOM   5467  CB  ASN D  85      -6.716 -38.481 118.318  1.00 32.92           C  
ANISOU 5467  CB  ASN D  85     3796   5458   3253    648   -609    145       C  
ATOM   5468  CG  ASN D  85      -7.041 -37.228 119.081  1.00 34.03           C  
ANISOU 5468  CG  ASN D  85     4008   5657   3265    525   -675    -35       C  
ATOM   5469  OD1 ASN D  85      -6.884 -37.183 120.300  1.00 34.89           O  
ANISOU 5469  OD1 ASN D  85     4183   5914   3158    531   -748    -29       O  
ATOM   5470  ND2 ASN D  85      -7.487 -36.193 118.372  1.00 28.84           N  
ANISOU 5470  ND2 ASN D  85     3354   4876   2727    418   -649   -195       N  
ATOM   5471  N   LEU D  86      -4.182 -41.190 118.424  1.00 34.49           N  
ANISOU 5471  N   LEU D  86     3785   5890   3429   1040   -715    651       N  
ATOM   5472  CA  LEU D  86      -3.974 -42.573 118.030  1.00 39.55           C  
ANISOU 5472  CA  LEU D  86     4444   6440   4144   1224   -606    845       C  
ATOM   5473  C   LEU D  86      -4.948 -43.499 118.767  1.00 42.93           C  
ANISOU 5473  C   LEU D  86     5089   6766   4458   1299   -467    943       C  
ATOM   5474  O   LEU D  86      -5.451 -43.166 119.845  1.00 41.51           O  
ANISOU 5474  O   LEU D  86     5011   6668   4093   1250   -498    904       O  
ATOM   5475  CB  LEU D  86      -2.531 -42.980 118.323  1.00 35.82           C  
ANISOU 5475  CB  LEU D  86     3808   6179   3622   1374   -749   1000       C  
ATOM   5476  CG  LEU D  86      -1.498 -42.121 117.606  1.00 42.45           C  
ANISOU 5476  CG  LEU D  86     4412   7142   4577   1287   -876    914       C  
ATOM   5477  CD1 LEU D  86      -0.133 -42.315 118.226  1.00 45.76           C  
ANISOU 5477  CD1 LEU D  86     4642   7850   4896   1405  -1058   1045       C  
ATOM   5478  CD2 LEU D  86      -1.470 -42.475 116.128  1.00 46.13           C  
ANISOU 5478  CD2 LEU D  86     4831   7415   5282   1311   -732    916       C  
ATOM   5479  N   PRO D  87      -5.218 -44.691 118.213  1.00 38.80           N  
ANISOU 5479  N   PRO D  87     4652   6057   4034   1409   -301   1070       N  
ATOM   5480  CA  PRO D  87      -4.672 -45.266 116.983  1.00 37.31           C  
ANISOU 5480  CA  PRO D  87     4384   5748   4043   1489   -232   1127       C  
ATOM   5481  C   PRO D  87      -5.499 -44.971 115.727  1.00 29.90           C  
ANISOU 5481  C   PRO D  87     3465   4606   3292   1346   -107    980       C  
ATOM   5482  O   PRO D  87      -4.944 -44.996 114.634  1.00 33.31           O  
ANISOU 5482  O   PRO D  87     3795   4982   3877   1361    -92    968       O  
ATOM   5483  CB  PRO D  87      -4.670 -46.759 117.293  1.00 37.90           C  
ANISOU 5483  CB  PRO D  87     4609   5714   4077   1682   -106   1342       C  
ATOM   5484  CG  PRO D  87      -5.877 -46.935 118.148  1.00 38.76           C  
ANISOU 5484  CG  PRO D  87     4919   5757   4051   1607    -12   1331       C  
ATOM   5485  CD  PRO D  87      -6.059 -45.659 118.936  1.00 39.36           C  
ANISOU 5485  CD  PRO D  87     4937   6025   3992   1471   -159   1184       C  
ATOM   5486  N   HIS D  88      -6.794 -44.674 115.882  1.00 31.56           N  
ANISOU 5486  N   HIS D  88     3791   4722   3479   1214    -23    871       N  
ATOM   5487  CA  HIS D  88      -7.680 -44.541 114.728  1.00 26.85           C  
ANISOU 5487  CA  HIS D  88     3217   3941   3043   1095     96    754       C  
ATOM   5488  C   HIS D  88      -7.305 -43.374 113.833  1.00 30.24           C  
ANISOU 5488  C   HIS D  88     3497   4407   3587    994      0    610       C  
ATOM   5489  O   HIS D  88      -7.679 -43.364 112.652  1.00 28.44           O  
ANISOU 5489  O   HIS D  88     3262   4040   3503    931     77    547       O  
ATOM   5490  CB  HIS D  88      -9.126 -44.389 115.193  1.00 34.78           C  
ANISOU 5490  CB  HIS D  88     4340   4886   3990    984    191    672       C  
ATOM   5491  CG  HIS D  88      -9.583 -45.497 116.084  1.00 36.83           C  
ANISOU 5491  CG  HIS D  88     4763   5101   4131   1052    307    810       C  
ATOM   5492  ND1 HIS D  88      -9.539 -46.821 115.701  1.00 36.57           N  
ANISOU 5492  ND1 HIS D  88     4835   4909   4152   1134    443    947       N  
ATOM   5493  CD2 HIS D  88     -10.087 -45.484 117.341  1.00 37.56           C  
ANISOU 5493  CD2 HIS D  88     4950   5275   4044   1048    320    834       C  
ATOM   5494  CE1 HIS D  88      -9.998 -47.575 116.684  1.00 38.27           C  
ANISOU 5494  CE1 HIS D  88     5207   5102   4232   1172    534   1058       C  
ATOM   5495  NE2 HIS D  88     -10.339 -46.788 117.690  1.00 37.72           N  
ANISOU 5495  NE2 HIS D  88     5129   5187   4016   1122    461    995       N  
ATOM   5496  N   SER D  89      -6.578 -42.390 114.356  1.00 28.71           N  
ANISOU 5496  N   SER D  89     3195   4392   3322    964   -166    557       N  
ATOM   5497  CA  SER D  89      -6.079 -41.341 113.481  1.00 29.35           C  
ANISOU 5497  CA  SER D  89     3146   4494   3513    865   -247    440       C  
ATOM   5498  C   SER D  89      -5.138 -41.918 112.430  1.00 31.35           C  
ANISOU 5498  C   SER D  89     3299   4712   3900    944   -218    524       C  
ATOM   5499  O   SER D  89      -5.222 -41.559 111.250  1.00 23.78           O  
ANISOU 5499  O   SER D  89     2306   3652   3077    869   -175    448       O  
ATOM   5500  CB  SER D  89      -5.384 -40.263 114.300  1.00 26.15           C  
ANISOU 5500  CB  SER D  89     2654   4286   2997    801   -427    371       C  
ATOM   5501  OG  SER D  89      -4.294 -40.802 115.032  1.00 28.11           O  
ANISOU 5501  OG  SER D  89     2822   4712   3146    919   -524    508       O  
ATOM   5502  N   GLU D  90      -4.261 -42.847 112.830  1.00 28.64           N  
ANISOU 5502  N   GLU D  90     2918   4447   3515   1109   -229    687       N  
ATOM   5503  CA  GLU D  90      -3.330 -43.419 111.863  1.00 31.09           C  
ANISOU 5503  CA  GLU D  90     3130   4731   3954   1210   -183    768       C  
ATOM   5504  C   GLU D  90      -4.064 -44.219 110.801  1.00 29.22           C  
ANISOU 5504  C   GLU D  90     3024   4245   3834   1216      8    768       C  
ATOM   5505  O   GLU D  90      -3.702 -44.171 109.619  1.00 33.66           O  
ANISOU 5505  O   GLU D  90     3527   4738   4523   1198     60    735       O  
ATOM   5506  CB  GLU D  90      -2.294 -44.294 112.552  1.00 30.40           C  
ANISOU 5506  CB  GLU D  90     2977   4777   3796   1421   -225    957       C  
ATOM   5507  CG  GLU D  90      -1.097 -44.581 111.657  1.00 36.11           C  
ANISOU 5507  CG  GLU D  90     3533   5544   4645   1528   -210   1024       C  
ATOM   5508  CD  GLU D  90      -0.138 -45.569 112.268  1.00 51.41           C  
ANISOU 5508  CD  GLU D  90     5407   7599   6527   1782   -232   1230       C  
ATOM   5509  OE1 GLU D  90      -0.273 -45.858 113.475  1.00 58.30           O  
ANISOU 5509  OE1 GLU D  90     6348   8562   7243   1856   -301   1319       O  
ATOM   5510  OE2 GLU D  90       0.747 -46.068 111.542  1.00 56.33           O  
ANISOU 5510  OE2 GLU D  90     5938   8210   7256   1887   -169   1288       O  
ATOM   5511  N   THR D  91      -5.093 -44.967 111.202  1.00 25.97           N  
ANISOU 5511  N   THR D  91     2794   3702   3371   1228    118    801       N  
ATOM   5512  CA  THR D  91      -5.909 -45.690 110.233  1.00 32.73           C  
ANISOU 5512  CA  THR D  91     3784   4328   4324   1189    292    778       C  
ATOM   5513  C   THR D  91      -6.461 -44.738 109.177  1.00 32.01           C  
ANISOU 5513  C   THR D  91     3650   4185   4329   1015    283    610       C  
ATOM   5514  O   THR D  91      -6.334 -44.979 107.971  1.00 25.86           O  
ANISOU 5514  O   THR D  91     2873   3295   3657    999    360    586       O  
ATOM   5515  CB  THR D  91      -7.047 -46.421 110.949  1.00 31.90           C  
ANISOU 5515  CB  THR D  91     3864   4119   4137   1172    397    814       C  
ATOM   5516  OG1 THR D  91      -6.520 -47.166 112.048  1.00 34.09           O  
ANISOU 5516  OG1 THR D  91     4192   4460   4299   1336    387    980       O  
ATOM   5517  CG2 THR D  91      -7.748 -47.391 110.001  1.00 27.85           C  
ANISOU 5517  CG2 THR D  91     3497   3371   3716   1133    581    810       C  
ATOM   5518  N   ILE D  92      -7.043 -43.623 109.620  1.00 27.81           N  
ANISOU 5518  N   ILE D  92     3086   3732   3749    895    189    497       N  
ATOM   5519  CA  ILE D  92      -7.531 -42.623 108.677  1.00 23.56           C  
ANISOU 5519  CA  ILE D  92     2511   3150   3293    753    168    353       C  
ATOM   5520  C   ILE D  92      -6.381 -42.082 107.833  1.00 21.45           C  
ANISOU 5520  C   ILE D  92     2112   2931   3106    751    108    341       C  
ATOM   5521  O   ILE D  92      -6.487 -41.974 106.603  1.00 25.79           O  
ANISOU 5521  O   ILE D  92     2666   3384   3751    695    162    291       O  
ATOM   5522  CB  ILE D  92      -8.262 -41.492 109.416  1.00 26.56           C  
ANISOU 5522  CB  ILE D  92     2888   3602   3601    658     84    243       C  
ATOM   5523  CG1 ILE D  92      -9.568 -41.997 110.014  1.00 25.64           C  
ANISOU 5523  CG1 ILE D  92     2889   3428   3426    639    177    239       C  
ATOM   5524  CG2 ILE D  92      -8.504 -40.322 108.459  1.00 18.99           C  
ANISOU 5524  CG2 ILE D  92     1883   2608   2726    544     40    114       C  
ATOM   5525  CD1 ILE D  92     -10.203 -41.001 110.985  1.00 25.06           C  
ANISOU 5525  CD1 ILE D  92     2820   3443   3257    586    113    146       C  
ATOM   5526  N   LEU D  93      -5.254 -41.759 108.471  1.00 23.57           N  
ANISOU 5526  N   LEU D  93     2260   3365   3330    805     -3    388       N  
ATOM   5527  CA  LEU D  93      -4.135 -41.208 107.712  1.00 32.29           C  
ANISOU 5527  CA  LEU D  93     3217   4538   4512    783    -53    376       C  
ATOM   5528  C   LEU D  93      -3.631 -42.195 106.662  1.00 34.27           C  
ANISOU 5528  C   LEU D  93     3466   4695   4859    881     76    454       C  
ATOM   5529  O   LEU D  93      -3.294 -41.796 105.538  1.00 30.46           O  
ANISOU 5529  O   LEU D  93     2933   4174   4465    818    106    405       O  
ATOM   5530  CB  LEU D  93      -3.000 -40.803 108.646  1.00 35.40           C  
ANISOU 5530  CB  LEU D  93     3460   5156   4834    816   -199    419       C  
ATOM   5531  CG  LEU D  93      -1.973 -39.944 107.908  1.00 33.82           C  
ANISOU 5531  CG  LEU D  93     3095   5043   4713    729   -259    373       C  
ATOM   5532  CD1 LEU D  93      -2.603 -38.616 107.476  1.00 35.67           C  
ANISOU 5532  CD1 LEU D  93     3380   5203   4971    535   -295    216       C  
ATOM   5533  CD2 LEU D  93      -0.749 -39.720 108.767  1.00 36.95           C  
ANISOU 5533  CD2 LEU D  93     3309   5688   5045    761   -401    429       C  
ATOM   5534  N   ASN D  94      -3.581 -43.487 107.008  1.00 31.19           N  
ANISOU 5534  N   ASN D  94     3149   4254   4446   1037    166    576       N  
ATOM   5535  CA  ASN D  94      -3.089 -44.504 106.081  1.00 31.16           C  
ANISOU 5535  CA  ASN D  94     3173   4140   4527   1152    309    649       C  
ATOM   5536  C   ASN D  94      -3.934 -44.596 104.808  1.00 31.47           C  
ANISOU 5536  C   ASN D  94     3337   3984   4637   1039    427    553       C  
ATOM   5537  O   ASN D  94      -3.402 -44.912 103.735  1.00 25.68           O  
ANISOU 5537  O   ASN D  94     2593   3185   3980   1071    520    557       O  
ATOM   5538  CB  ASN D  94      -3.021 -45.853 106.794  1.00 28.73           C  
ANISOU 5538  CB  ASN D  94     2967   3779   4170   1340    391    798       C  
ATOM   5539  CG  ASN D  94      -1.870 -45.919 107.797  1.00 40.12           C  
ANISOU 5539  CG  ASN D  94     4256   5437   5551   1501    278    926       C  
ATOM   5540  OD1 ASN D  94      -0.993 -45.053 107.805  1.00 43.53           O  
ANISOU 5540  OD1 ASN D  94     4485   6060   5996   1467    153    901       O  
ATOM   5541  ND2 ASN D  94      -1.860 -46.950 108.631  1.00 42.95           N  
ANISOU 5541  ND2 ASN D  94     4713   5770   5838   1671    321   1070       N  
ATOM   5542  N   LEU D  95      -5.237 -44.307 104.905  1.00 20.87           N  
ANISOU 5542  N   LEU D  95     2104   2564   3264    908    423    464       N  
ATOM   5543  CA  LEU D  95      -6.106 -44.280 103.729  1.00 21.48           C  
ANISOU 5543  CA  LEU D  95     2277   2493   3392    785    501    367       C  
ATOM   5544  C   LEU D  95      -5.862 -43.040 102.873  1.00 31.74           C  
ANISOU 5544  C   LEU D  95     3481   3843   4737    674    426    274       C  
ATOM   5545  O   LEU D  95      -5.801 -43.126 101.639  1.00 30.28           O  
ANISOU 5545  O   LEU D  95     3329   3572   4603    633    498    239       O  
ATOM   5546  CB  LEU D  95      -7.566 -44.323 104.168  1.00 22.58           C  
ANISOU 5546  CB  LEU D  95     2524   2572   3483    689    510    311       C  
ATOM   5547  CG  LEU D  95      -8.179 -45.693 104.390  1.00 30.33           C  
ANISOU 5547  CG  LEU D  95     3665   3417   4443    724    648    370       C  
ATOM   5548  CD1 LEU D  95      -9.492 -45.543 105.153  1.00 34.97           C  
ANISOU 5548  CD1 LEU D  95     4303   4012   4971    627    636    324       C  
ATOM   5549  CD2 LEU D  95      -8.416 -46.331 103.042  1.00 35.02           C  
ANISOU 5549  CD2 LEU D  95     4359   3851   5095    668    770    327       C  
ATOM   5550  N   LEU D  96      -5.756 -41.867 103.510  1.00 29.70           N  
ANISOU 5550  N   LEU D  96     3126   3709   4449    616    288    230       N  
ATOM   5551  CA  LEU D  96      -5.488 -40.646 102.757  1.00 28.17           C  
ANISOU 5551  CA  LEU D  96     2865   3543   4295    505    224    151       C  
ATOM   5552  C   LEU D  96      -4.139 -40.699 102.061  1.00 27.06           C  
ANISOU 5552  C   LEU D  96     2617   3453   4213    545    256    198       C  
ATOM   5553  O   LEU D  96      -3.952 -40.047 101.031  1.00 34.06           O  
ANISOU 5553  O   LEU D  96     3490   4310   5142    456    267    148       O  
ATOM   5554  CB  LEU D  96      -5.551 -39.412 103.677  1.00 22.36           C  
ANISOU 5554  CB  LEU D  96     2071   2914   3512    435     82     92       C  
ATOM   5555  CG  LEU D  96      -6.807 -39.268 104.552  1.00 24.91           C  
ANISOU 5555  CG  LEU D  96     2480   3216   3769    414     55     45       C  
ATOM   5556  CD1 LEU D  96      -6.745 -38.022 105.437  1.00 30.19           C  
ANISOU 5556  CD1 LEU D  96     3109   3978   4382    352    -70    -25       C  
ATOM   5557  CD2 LEU D  96      -8.097 -39.291 103.709  1.00 22.24           C  
ANISOU 5557  CD2 LEU D  96     2241   2750   3461    352    117    -17       C  
ATOM   5558  N   GLY D  97      -3.189 -41.461 102.592  1.00 20.87           N  
ANISOU 5558  N   GLY D  97     1751   2753   3427    684    276    302       N  
ATOM   5559  CA  GLY D  97      -1.863 -41.447 102.013  1.00 22.05           C  
ANISOU 5559  CA  GLY D  97     1756   2986   3635    731    306    349       C  
ATOM   5560  C   GLY D  97      -1.447 -42.728 101.327  1.00 21.90           C  
ANISOU 5560  C   GLY D  97     1782   2879   3661    879    472    426       C  
ATOM   5561  O   GLY D  97      -0.247 -42.954 101.109  1.00 28.19           O  
ANISOU 5561  O   GLY D  97     2435   3772   4502    979    511    495       O  
ATOM   5562  N   ASP D  98      -2.410 -43.570 100.960  1.00 29.94           N  
ANISOU 5562  N   ASP D  98     2995   3713   4669    890    580    411       N  
ATOM   5563  CA  ASP D  98      -2.082 -44.851 100.360  1.00 25.24           C  
ANISOU 5563  CA  ASP D  98     2487   2997   4107   1028    754    473       C  
ATOM   5564  C   ASP D  98      -1.716 -44.664  98.884  1.00 25.28           C  
ANISOU 5564  C   ASP D  98     2500   2944   4162    970    854    416       C  
ATOM   5565  O   ASP D  98      -1.796 -43.569  98.314  1.00 24.65           O  
ANISOU 5565  O   ASP D  98     2371   2907   4088    818    788    338       O  
ATOM   5566  CB  ASP D  98      -3.223 -45.857 100.585  1.00 23.22           C  
ANISOU 5566  CB  ASP D  98     2450   2561   3812   1036    836    472       C  
ATOM   5567  CG  ASP D  98      -4.544 -45.484  99.877  1.00 24.57           C  
ANISOU 5567  CG  ASP D  98     2752   2620   3965    839    835    345       C  
ATOM   5568  OD1 ASP D  98      -4.573 -44.563  99.029  1.00 20.45           O  
ANISOU 5568  OD1 ASP D  98     2186   2125   3459    720    792    265       O  
ATOM   5569  OD2 ASP D  98      -5.580 -46.145 100.178  1.00 24.82           O  
ANISOU 5569  OD2 ASP D  98     2931   2540   3961    803    879    332       O  
ATOM   5570  N   ALA D  99      -1.293 -45.760  98.264  1.00 23.37           N  
ANISOU 5570  N   ALA D  99     2338   2594   3949   1100   1027    460       N  
ATOM   5571  CA  ALA D  99      -0.797 -45.713  96.895  1.00 28.68           C  
ANISOU 5571  CA  ALA D  99     3022   3220   4656   1073   1149    416       C  
ATOM   5572  C   ALA D  99      -1.797 -45.058  95.954  1.00 27.03           C  
ANISOU 5572  C   ALA D  99     2937   2922   4410    858   1125    292       C  
ATOM   5573  O   ALA D  99      -1.439 -44.183  95.157  1.00 27.24           O  
ANISOU 5573  O   ALA D  99     2899   3006   4446    759   1111    248       O  
ATOM   5574  CB  ALA D  99      -0.477 -47.128  96.422  1.00 28.58           C  
ANISOU 5574  CB  ALA D  99     3165   3069   4625   1198   1317    454       C  
ATOM   5575  N   ARG D 100      -3.059 -45.474  96.034  1.00 26.55           N  
ANISOU 5575  N   ARG D 100     3054   2731   4303    782   1121    240       N  
ATOM   5576  CA  ARG D 100      -4.078 -44.941  95.135  1.00 26.24           C  
ANISOU 5576  CA  ARG D 100     3125   2624   4221    594   1089    130       C  
ATOM   5577  C   ARG D 100      -4.215 -43.423  95.285  1.00 24.71           C  
ANISOU 5577  C   ARG D 100     2807   2558   4025    476    920     96       C  
ATOM   5578  O   ARG D 100      -4.192 -42.682  94.290  1.00 18.82           O  
ANISOU 5578  O   ARG D 100     2071   1814   3267    374    912     47       O  
ATOM   5579  CB  ARG D 100      -5.406 -45.660  95.408  1.00 25.32           C  
ANISOU 5579  CB  ARG D 100     3175   2386   4061    531   1098     89       C  
ATOM   5580  CG  ARG D 100      -6.587 -45.087  94.681  1.00 24.18           C  
ANISOU 5580  CG  ARG D 100     3106   2215   3867    345   1029    -14       C  
ATOM   5581  CD  ARG D 100      -7.874 -45.796  95.090  1.00 24.76           C  
ANISOU 5581  CD  ARG D 100     3299   2205   3905    273   1033    -50       C  
ATOM   5582  NE  ARG D 100      -9.015 -45.058  94.564  1.00 28.21           N  
ANISOU 5582  NE  ARG D 100     3744   2674   4299    111    928   -137       N  
ATOM   5583  CZ  ARG D 100     -10.277 -45.439  94.692  1.00 26.69           C  
ANISOU 5583  CZ  ARG D 100     3621   2449   4073      4    911   -189       C  
ATOM   5584  NH1 ARG D 100     -10.555 -46.564  95.340  1.00 23.13           N  
ANISOU 5584  NH1 ARG D 100     3257   1908   3622     24   1005   -165       N  
ATOM   5585  NH2 ARG D 100     -11.256 -44.699  94.163  1.00 21.71           N  
ANISOU 5585  NH2 ARG D 100     2967   1878   3406   -121    803   -257       N  
ATOM   5586  N   ARG D 101      -4.332 -42.939  96.529  1.00 18.70           N  
ANISOU 5586  N   ARG D 101     1945   1895   3267    492    792    124       N  
ATOM   5587  CA  ARG D 101      -4.484 -41.505  96.761  1.00 22.59           C  
ANISOU 5587  CA  ARG D 101     2348   2481   3755    384    643     83       C  
ATOM   5588  C   ARG D 101      -3.198 -40.736  96.474  1.00 24.56           C  
ANISOU 5588  C   ARG D 101     2449   2838   4044    375    631    108       C  
ATOM   5589  O   ARG D 101      -3.249 -39.554  96.119  1.00 21.32           O  
ANISOU 5589  O   ARG D 101     2017   2453   3631    255    557     63       O  
ATOM   5590  CB  ARG D 101      -4.936 -41.244  98.203  1.00 21.87           C  
ANISOU 5590  CB  ARG D 101     2207   2460   3641    402    526     93       C  
ATOM   5591  CG  ARG D 101      -6.409 -40.852  98.358  1.00 21.95           C  
ANISOU 5591  CG  ARG D 101     2307   2419   3612    309    459     21       C  
ATOM   5592  CD  ARG D 101      -7.363 -41.892  97.795  1.00 19.47           C  
ANISOU 5592  CD  ARG D 101     2138   1981   3278    289    555     -2       C  
ATOM   5593  NE  ARG D 101      -7.248 -43.176  98.476  1.00 25.80           N  
ANISOU 5593  NE  ARG D 101     2987   2740   4075    391    645     62       N  
ATOM   5594  CZ  ARG D 101      -8.233 -44.073  98.533  1.00 25.45           C  
ANISOU 5594  CZ  ARG D 101     3067   2597   4005    359    711     45       C  
ATOM   5595  NH1 ARG D 101      -9.395 -43.803  97.954  1.00 17.40           N  
ANISOU 5595  NH1 ARG D 101     2102   1546   2963    228    683    -39       N  
ATOM   5596  NH2 ARG D 101      -8.058 -45.235  99.158  1.00 23.83           N  
ANISOU 5596  NH2 ARG D 101     2930   2330   3794    455    806    115       N  
ATOM   5597  N   THR D 102      -2.044 -41.369  96.650  1.00 21.79           N  
ANISOU 5597  N   THR D 102     1991   2556   3731    500    706    184       N  
ATOM   5598  CA  THR D 102      -0.789 -40.693  96.351  1.00 20.77           C  
ANISOU 5598  CA  THR D 102     1692   2554   3645    479    707    209       C  
ATOM   5599  C   THR D 102      -0.675 -40.382  94.865  1.00 25.47           C  
ANISOU 5599  C   THR D 102     2358   3077   4242    388    808    167       C  
ATOM   5600  O   THR D 102      -0.387 -39.242  94.476  1.00 20.75           O  
ANISOU 5600  O   THR D 102     1708   2526   3649    256    758    139       O  
ATOM   5601  CB  THR D 102       0.365 -41.558  96.832  1.00 24.68           C  
ANISOU 5601  CB  THR D 102     2042   3154   4182    661    773    309       C  
ATOM   5602  OG1 THR D 102       0.279 -41.653  98.261  1.00 35.49           O  
ANISOU 5602  OG1 THR D 102     3343   4615   5526    728    650    353       O  
ATOM   5603  CG2 THR D 102       1.688 -40.938  96.449  1.00 25.54           C  
ANISOU 5603  CG2 THR D 102     1943   3418   4342    633    791    335       C  
ATOM   5604  N   ARG D 103      -0.914 -41.384  94.017  1.00 24.08           N  
ANISOU 5604  N   ARG D 103     2323   2776   4050    448    956    160       N  
ATOM   5605  CA  ARG D 103      -0.888 -41.163  92.580  1.00 21.16           C  
ANISOU 5605  CA  ARG D 103     2052   2335   3653    361   1056    116       C  
ATOM   5606  C   ARG D 103      -2.005 -40.224  92.150  1.00 20.77           C  
ANISOU 5606  C   ARG D 103     2123   2224   3545    196    947     46       C  
ATOM   5607  O   ARG D 103      -1.822 -39.387  91.254  1.00 22.55           O  
ANISOU 5607  O   ARG D 103     2371   2449   3748     88    956     27       O  
ATOM   5608  CB  ARG D 103      -1.004 -42.497  91.857  1.00 21.85           C  
ANISOU 5608  CB  ARG D 103     2295   2291   3717    454   1234    108       C  
ATOM   5609  CG  ARG D 103       0.145 -43.424  92.130  1.00 36.85           C  
ANISOU 5609  CG  ARG D 103     4090   4236   5678    649   1369    186       C  
ATOM   5610  CD  ARG D 103       1.449 -42.911  91.526  1.00 38.36           C  
ANISOU 5610  CD  ARG D 103     4111   4552   5912    655   1452    219       C  
ATOM   5611  NE  ARG D 103       2.508 -43.909  91.670  1.00 48.97           N  
ANISOU 5611  NE  ARG D 103     5355   5938   7314    873   1601    296       N  
ATOM   5612  CZ  ARG D 103       3.573 -43.999  90.880  1.00 54.62           C  
ANISOU 5612  CZ  ARG D 103     6006   6716   8030    905   1715    313       C  
ATOM   5613  NH1 ARG D 103       3.734 -43.147  89.874  1.00 52.35           N  
ANISOU 5613  NH1 ARG D 103     5707   6448   7734    762   1784    269       N  
ATOM   5614  NH2 ARG D 103       4.475 -44.951  91.091  1.00 59.22           N  
ANISOU 5614  NH2 ARG D 103     6541   7340   8619   1080   1767    376       N  
ATOM   5615  N   PHE D 104      -3.162 -40.332  92.792  1.00 18.80           N  
ANISOU 5615  N   PHE D 104     1948   1927   3270    183    848     15       N  
ATOM   5616  CA  PHE D 104      -4.301 -39.519  92.392  1.00 24.69           C  
ANISOU 5616  CA  PHE D 104     2795   2623   3962     60    746    -44       C  
ATOM   5617  C   PHE D 104      -3.985 -38.032  92.547  1.00 28.29           C  
ANISOU 5617  C   PHE D 104     3169   3145   4436    -27    639    -42       C  
ATOM   5618  O   PHE D 104      -4.004 -37.266  91.577  1.00 25.33           O  
ANISOU 5618  O   PHE D 104     2858   2737   4028   -118    642    -55       O  
ATOM   5619  CB  PHE D 104      -5.529 -39.924  93.212  1.00 23.85           C  
ANISOU 5619  CB  PHE D 104     2740   2484   3837     74    669    -71       C  
ATOM   5620  CG  PHE D 104      -6.759 -39.148  92.868  1.00 24.58           C  
ANISOU 5620  CG  PHE D 104     2908   2549   3882    -24    563   -125       C  
ATOM   5621  CD1 PHE D 104      -7.595 -39.576  91.856  1.00 20.31           C  
ANISOU 5621  CD1 PHE D 104     2500   1940   3277    -83    593   -168       C  
ATOM   5622  CD2 PHE D 104      -7.063 -37.967  93.532  1.00 20.69           C  
ANISOU 5622  CD2 PHE D 104     2355   2103   3403    -53    432   -134       C  
ATOM   5623  CE1 PHE D 104      -8.736 -38.860  91.517  1.00 26.95           C  
ANISOU 5623  CE1 PHE D 104     3386   2782   4072   -154    483   -206       C  
ATOM   5624  CE2 PHE D 104      -8.207 -37.250  93.202  1.00 27.78           C  
ANISOU 5624  CE2 PHE D 104     3317   2976   4262   -109    340   -172       C  
ATOM   5625  CZ  PHE D 104      -9.045 -37.703  92.189  1.00 20.80           C  
ANISOU 5625  CZ  PHE D 104     2538   2046   3317   -152    360   -201       C  
ATOM   5626  N   PHE D 105      -3.647 -37.612  93.761  1.00 30.00           N  
ANISOU 5626  N   PHE D 105     3259   3447   4693     -4    550    -25       N  
ATOM   5627  CA  PHE D 105      -3.355 -36.199  93.963  1.00 31.30           C  
ANISOU 5627  CA  PHE D 105     3371   3652   4871   -106    454    -39       C  
ATOM   5628  C   PHE D 105      -2.007 -35.817  93.370  1.00 27.93           C  
ANISOU 5628  C   PHE D 105     2847   3288   4478   -160    530     -5       C  
ATOM   5629  O   PHE D 105      -1.825 -34.671  92.938  1.00 27.71           O  
ANISOU 5629  O   PHE D 105     2841   3241   4446   -282    501    -17       O  
ATOM   5630  CB  PHE D 105      -3.447 -35.869  95.449  1.00 26.17           C  
ANISOU 5630  CB  PHE D 105     2634   3076   4235    -84    335    -48       C  
ATOM   5631  CG  PHE D 105      -4.851 -35.934  95.978  1.00 21.17           C  
ANISOU 5631  CG  PHE D 105     2096   2384   3565    -59    264    -89       C  
ATOM   5632  CD1 PHE D 105      -5.776 -34.978  95.605  1.00 28.02           C  
ANISOU 5632  CD1 PHE D 105     3063   3177   4407   -124    198   -135       C  
ATOM   5633  CD2 PHE D 105      -5.247 -36.943  96.834  1.00 16.73           C  
ANISOU 5633  CD2 PHE D 105     1522   1842   2993     37    271    -75       C  
ATOM   5634  CE1 PHE D 105      -7.061 -35.021  96.080  1.00 27.66           C  
ANISOU 5634  CE1 PHE D 105     3075   3102   4335    -92    141   -171       C  
ATOM   5635  CE2 PHE D 105      -6.528 -36.994  97.313  1.00 23.63           C  
ANISOU 5635  CE2 PHE D 105     2467   2676   3834     46    221   -112       C  
ATOM   5636  CZ  PHE D 105      -7.442 -36.031  96.930  1.00 30.14           C  
ANISOU 5636  CZ  PHE D 105     3361   3449   4641    -17    156   -164       C  
ATOM   5637  N   GLY D 106      -1.072 -36.767  93.303  1.00 29.87           N  
ANISOU 5637  N   GLY D 106     2991   3601   4757    -67    642     42       N  
ATOM   5638  CA  GLY D 106       0.165 -36.525  92.581  1.00 30.71           C  
ANISOU 5638  CA  GLY D 106     2995   3778   4897   -111    746     75       C  
ATOM   5639  C   GLY D 106      -0.077 -36.125  91.137  1.00 38.56           C  
ANISOU 5639  C   GLY D 106     4143   4669   5840   -206    830     57       C  
ATOM   5640  O   GLY D 106       0.497 -35.148  90.648  1.00 40.86           O  
ANISOU 5640  O   GLY D 106     4407   4982   6136   -333    845     64       O  
ATOM   5641  N   ASP D 107      -0.945 -36.869  90.437  1.00 34.35           N  
ANISOU 5641  N   ASP D 107     3782   4023   5245   -161    884     33       N  
ATOM   5642  CA  ASP D 107      -1.296 -36.498  89.068  1.00 27.92           C  
ANISOU 5642  CA  ASP D 107     3134   3121   4354   -251    941     15       C  
ATOM   5643  C   ASP D 107      -1.924 -35.116  89.017  1.00 30.46           C  
ANISOU 5643  C   ASP D 107     3530   3399   4646   -372    808      3       C  
ATOM   5644  O   ASP D 107      -1.627 -34.333  88.113  1.00 32.11           O  
ANISOU 5644  O   ASP D 107     3806   3578   4817   -474    849     20       O  
ATOM   5645  CB  ASP D 107      -2.256 -37.510  88.449  1.00 25.74           C  
ANISOU 5645  CB  ASP D 107     3031   2746   4002   -202    987    -24       C  
ATOM   5646  CG  ASP D 107      -1.571 -38.796  88.032  1.00 35.60           C  
ANISOU 5646  CG  ASP D 107     4282   3988   5257   -100   1172    -17       C  
ATOM   5647  OD1 ASP D 107      -0.334 -38.796  87.849  1.00 41.29           O  
ANISOU 5647  OD1 ASP D 107     4880   4783   6025    -70   1288     24       O  
ATOM   5648  OD2 ASP D 107      -2.278 -39.810  87.883  1.00 38.38           O  
ANISOU 5648  OD2 ASP D 107     4760   4256   5566    -50   1209    -55       O  
HETATM 5649  N   MSE D 108      -2.804 -34.799  89.961  1.00 27.08           N  
ANISOU 5649  N   MSE D 108     3106   2954   4229   -355    660    -24       N  
HETATM 5650  CA  MSE D 108      -3.542 -33.555  89.846  1.00 31.09           C  
ANISOU 5650  CA  MSE D 108     3714   3395   4704   -436    547    -36       C  
HETATM 5651  C   MSE D 108      -2.702 -32.356  90.230  1.00 36.03           C  
ANISOU 5651  C   MSE D 108     4266   4045   5377   -538    518    -22       C  
HETATM 5652  O   MSE D 108      -2.882 -31.266  89.697  1.00 38.83           O  
ANISOU 5652  O   MSE D 108     4731   4319   5701   -629    491    -12       O  
HETATM 5653  CB  MSE D 108      -4.793 -33.574  90.696  1.00 32.00           C  
ANISOU 5653  CB  MSE D 108     3857   3486   4815   -376    418    -74       C  
HETATM 5654  CG  MSE D 108      -5.768 -32.515  90.252  1.00 30.52           C  
ANISOU 5654  CG  MSE D 108     3804   3216   4577   -415    325    -80       C  
HETATM 5655 SE   MSE D 108      -7.220 -32.424  91.473  1.00 39.42          SE  
ANISOU 5655 SE   MSE D 108     4919   4342   5716   -329    181   -128      SE  
HETATM 5656  CE  MSE D 108      -7.832 -34.265  91.392  1.00 27.53           C  
ANISOU 5656  CE  MSE D 108     3399   2878   4185   -258    240   -149       C  
ATOM   5657  N   PHE D 109      -1.796 -32.553  91.183  1.00 36.49           N  
ANISOU 5657  N   PHE D 109     4145   4214   5507   -528    517    -20       N  
ATOM   5658  CA  PHE D 109      -0.820 -31.514  91.455  1.00 36.62           C  
ANISOU 5658  CA  PHE D 109     4071   4277   5565   -661    505    -15       C  
ATOM   5659  C   PHE D 109       0.232 -31.454  90.355  1.00 43.48           C  
ANISOU 5659  C   PHE D 109     4907   5176   6436   -743    655     30       C  
ATOM   5660  O   PHE D 109       0.879 -30.413  90.196  1.00 45.34           O  
ANISOU 5660  O   PHE D 109     5128   5410   6689   -898    666     37       O  
ATOM   5661  CB  PHE D 109      -0.182 -31.732  92.827  1.00 28.04           C  
ANISOU 5661  CB  PHE D 109     2786   3332   4537   -635    439    -27       C  
ATOM   5662  CG  PHE D 109      -1.171 -31.753  93.954  1.00 29.63           C  
ANISOU 5662  CG  PHE D 109     3026   3510   4722   -562    307    -71       C  
ATOM   5663  CD1 PHE D 109      -2.437 -31.214  93.796  1.00 23.03           C  
ANISOU 5663  CD1 PHE D 109     2369   2538   3844   -556    243   -104       C  
ATOM   5664  CD2 PHE D 109      -0.843 -32.330  95.172  1.00 24.79           C  
ANISOU 5664  CD2 PHE D 109     2266   3023   4130   -488    251    -72       C  
ATOM   5665  CE1 PHE D 109      -3.330 -31.247  94.825  1.00 24.78           C  
ANISOU 5665  CE1 PHE D 109     2612   2751   4053   -486    144   -146       C  
ATOM   5666  CE2 PHE D 109      -1.745 -32.361  96.204  1.00 20.18           C  
ANISOU 5666  CE2 PHE D 109     1726   2422   3519   -426    148   -111       C  
ATOM   5667  CZ  PHE D 109      -2.981 -31.827  96.033  1.00 20.16           C  
ANISOU 5667  CZ  PHE D 109     1893   2286   3483   -428    103   -152       C  
ATOM   5668  N   GLY D 110       0.395 -32.549  89.600  1.00 50.99           N  
ANISOU 5668  N   GLY D 110     4453   8401   6520    106   1116    286       N  
ATOM   5669  CA  GLY D 110       1.098 -32.609  88.326  1.00 52.27           C  
ANISOU 5669  CA  GLY D 110     4564   8660   6636    131   1246    311       C  
ATOM   5670  C   GLY D 110       2.608 -32.545  88.384  1.00 61.53           C  
ANISOU 5670  C   GLY D 110     5573   9845   7960    106   1316    296       C  
ATOM   5671  O   GLY D 110       3.209 -31.621  87.818  1.00 67.45           O  
ANISOU 5671  O   GLY D 110     6254  10620   8754     38   1424    371       O  
ATOM   5672  N   THR D 111       3.245 -33.544  88.996  1.00 62.92           N  
ANISOU 5672  N   THR D 111     5679  10012   8215    163   1260    206       N  
ATOM   5673  CA  THR D 111       4.591 -33.339  89.507  1.00 66.69           C  
ANISOU 5673  CA  THR D 111     5981  10471   8886    120   1276    199       C  
ATOM   5674  C   THR D 111       5.510 -34.533  89.289  1.00 67.69           C  
ANISOU 5674  C   THR D 111     6014  10649   9057    222   1306    125       C  
ATOM   5675  O   THR D 111       5.115 -35.615  88.838  1.00 61.20           O  
ANISOU 5675  O   THR D 111     5271   9869   8115    330   1307     63       O  
ATOM   5676  CB  THR D 111       4.547 -33.039  91.009  1.00 58.53           C  
ANISOU 5676  CB  THR D 111     4922   9338   7979     53   1132    185       C  
ATOM   5677  OG1 THR D 111       3.373 -33.639  91.572  1.00 49.70           O  
ANISOU 5677  OG1 THR D 111     3948   8179   6757    101   1018    141       O  
ATOM   5678  CG2 THR D 111       4.548 -31.540  91.263  1.00 59.62           C  
ANISOU 5678  CG2 THR D 111     5037   9431   8186    -86   1156    267       C  
ATOM   5679  N   ARG D 112       6.778 -34.266  89.581  1.00 74.92           N  
ANISOU 5679  N   ARG D 112     6749  11564  10154    181   1336    133       N  
ATOM   5680  CA  ARG D 112       7.693 -35.216  90.182  1.00 82.79           C  
ANISOU 5680  CA  ARG D 112     7619  12551  11286    248   1281     69       C  
ATOM   5681  C   ARG D 112       8.060 -34.775  91.587  1.00 87.34           C  
ANISOU 5681  C   ARG D 112     8108  13044  12032    159   1135     76       C  
ATOM   5682  O   ARG D 112       8.665 -35.556  92.336  1.00 97.35           O  
ANISOU 5682  O   ARG D 112     9286  14287  13415    208   1040     33       O  
ATOM   5683  CB  ARG D 112       8.958 -35.366  89.324  1.00 83.53           C  
ANISOU 5683  CB  ARG D 112     7548  12725  11463    281   1437     69       C  
ATOM   5684  N   ALA D 113       7.700 -33.546  91.959  1.00 74.79           N  
ANISOU 5684  N   ALA D 113     6547  11412  10455     28   1110    131       N  
ATOM   5685  CA  ALA D 113       7.871 -33.056  93.318  1.00 60.25           C  
ANISOU 5685  CA  ALA D 113     4656   9494   8743    -71    963    131       C  
ATOM   5686  C   ALA D 113       6.870 -33.763  94.219  1.00 51.34           C  
ANISOU 5686  C   ALA D 113     3668   8302   7538    -19    813     86       C  
ATOM   5687  O   ALA D 113       5.658 -33.625  94.032  1.00 51.42           O  
ANISOU 5687  O   ALA D 113     3844   8298   7397     -9    818     94       O  
ATOM   5688  CB  ALA D 113       7.676 -31.542  93.372  1.00 54.95           C  
ANISOU 5688  CB  ALA D 113     3997   8798   8085   -225    998    199       C  
ATOM   5689  N   GLU D 114       7.365 -34.539  95.181  1.00 45.54           N  
ANISOU 5689  N   GLU D 114     2866   7536   6901     13    677     44       N  
ATOM   5690  CA  GLU D 114       6.470 -35.226  96.100  1.00 42.57           C  
ANISOU 5690  CA  GLU D 114     2624   7108   6445     51    529      2       C  
ATOM   5691  C   GLU D 114       5.804 -34.228  97.045  1.00 44.38           C  
ANISOU 5691  C   GLU D 114     2924   7270   6670    -76    441     22       C  
ATOM   5692  O   GLU D 114       6.404 -33.226  97.449  1.00 38.93           O  
ANISOU 5692  O   GLU D 114     2136   6556   6099   -203    427     55       O  
ATOM   5693  CB  GLU D 114       7.231 -36.287  96.890  1.00 37.29           C  
ANISOU 5693  CB  GLU D 114     1865   6424   5879    113    401    -33       C  
ATOM   5694  N   TYR D 115       4.541 -34.492  97.372  1.00 41.29           N  
ANISOU 5694  N   TYR D 115     2703   6850   6135    -49    389     -6       N  
ATOM   5695  CA  TYR D 115       3.778 -33.670  98.297  1.00 38.36           C  
ANISOU 5695  CA  TYR D 115     2413   6418   5745   -154    314      3       C  
ATOM   5696  C   TYR D 115       3.514 -34.463  99.567  1.00 35.39           C  
ANISOU 5696  C   TYR D 115     2095   6000   5353   -141    135    -60       C  
ATOM   5697  O   TYR D 115       3.322 -35.681  99.516  1.00 43.49           O  
ANISOU 5697  O   TYR D 115     3172   7041   6312    -29     96   -111       O  
ATOM   5698  CB  TYR D 115       2.455 -33.213  97.673  1.00 39.09           C  
ANISOU 5698  CB  TYR D 115     2653   6511   5689   -140    408     27       C  
ATOM   5699  CG  TYR D 115       2.608 -32.078  96.690  1.00 38.81           C  
ANISOU 5699  CG  TYR D 115     2582   6495   5669   -197    560    106       C  
ATOM   5700  CD1 TYR D 115       2.361 -30.767  97.072  1.00 42.01           C  
ANISOU 5700  CD1 TYR D 115     2994   6849   6117   -323    581    161       C  
ATOM   5701  CD2 TYR D 115       3.008 -32.313  95.385  1.00 34.64           C  
ANISOU 5701  CD2 TYR D 115     2019   6036   5107   -131    685    127       C  
ATOM   5702  CE1 TYR D 115       2.507 -29.724  96.181  1.00 38.43           C  
ANISOU 5702  CE1 TYR D 115     2518   6408   5675   -380    718    241       C  
ATOM   5703  CE2 TYR D 115       3.158 -31.276  94.492  1.00 37.56           C  
ANISOU 5703  CE2 TYR D 115     2365   6427   5477   -189    819    204       C  
ATOM   5704  CZ  TYR D 115       2.909 -29.985  94.895  1.00 40.32           C  
ANISOU 5704  CZ  TYR D 115     2725   6721   5872   -312    832    263       C  
ATOM   5705  OH  TYR D 115       3.055 -28.947  93.999  1.00 48.13           O  
ANISOU 5705  OH  TYR D 115     3700   7730   6857   -374    963    350       O  
ATOM   5706  N   PHE D 116       3.528 -33.780 100.706  1.00 34.63           N  
ANISOU 5706  N   PHE D 116     1998   5849   5311   -267     25    -62       N  
ATOM   5707  CA  PHE D 116       3.315 -34.418 101.999  1.00 31.43           C  
ANISOU 5707  CA  PHE D 116     1663   5398   4881   -279   -157   -123       C  
ATOM   5708  C   PHE D 116       2.084 -33.836 102.675  1.00 31.49           C  
ANISOU 5708  C   PHE D 116     1815   5362   4787   -351   -183   -155       C  
ATOM   5709  O   PHE D 116       1.871 -32.618 102.656  1.00 30.71           O  
ANISOU 5709  O   PHE D 116     1711   5246   4712   -463   -119   -119       O  
ATOM   5710  CB  PHE D 116       4.510 -34.241 102.918  1.00 30.10           C  
ANISOU 5710  CB  PHE D 116     1377   5199   4861   -377   -301   -111       C  
ATOM   5711  CG  PHE D 116       5.823 -34.647 102.291  1.00 41.05           C  
ANISOU 5711  CG  PHE D 116     2583   6628   6385   -320   -265    -70       C  
ATOM   5712  CD1 PHE D 116       6.318 -35.920 102.464  1.00 32.22           C  
ANISOU 5712  CD1 PHE D 116     1430   5526   5285   -211   -343    -80       C  
ATOM   5713  CD2 PHE D 116       6.535 -33.761 101.505  1.00 33.28           C  
ANISOU 5713  CD2 PHE D 116     1464   5671   5511   -374   -140    -26       C  
ATOM   5714  CE1 PHE D 116       7.516 -36.296 101.888  1.00 43.20           C  
ANISOU 5714  CE1 PHE D 116     2641   6958   6814   -153   -297    -42       C  
ATOM   5715  CE2 PHE D 116       7.734 -34.134 100.915  1.00 47.43           C  
ANISOU 5715  CE2 PHE D 116     3081   7507   7434   -320    -91     -9       C  
ATOM   5716  CZ  PHE D 116       8.225 -35.403 101.110  1.00 42.55           C  
ANISOU 5716  CZ  PHE D 116     2417   6901   6848   -205   -170    -14       C  
ATOM   5717  N   ILE D 117       1.292 -34.714 103.285  1.00 30.34           N  
ANISOU 5717  N   ILE D 117     1797   5194   4538   -291   -270   -222       N  
ATOM   5718  CA  ILE D 117       0.195 -34.296 104.148  1.00 28.12           C  
ANISOU 5718  CA  ILE D 117     1649   4866   4171   -361   -315   -270       C  
ATOM   5719  C   ILE D 117       0.786 -33.837 105.473  1.00 34.35           C  
ANISOU 5719  C   ILE D 117     2440   5585   5024   -510   -474   -305       C  
ATOM   5720  O   ILE D 117       1.529 -34.575 106.129  1.00 30.66           O  
ANISOU 5720  O   ILE D 117     1962   5093   4596   -498   -618   -320       O  
ATOM   5721  CB  ILE D 117      -0.819 -35.429 104.352  1.00 23.30           C  
ANISOU 5721  CB  ILE D 117     1175   4246   3432   -251   -355   -327       C  
ATOM   5722  CG1 ILE D 117      -1.457 -35.809 103.010  1.00 23.97           C  
ANISOU 5722  CG1 ILE D 117     1277   4390   3440   -130   -210   -295       C  
ATOM   5723  CG2 ILE D 117      -1.875 -34.994 105.361  1.00 28.75           C  
ANISOU 5723  CG2 ILE D 117     1992   4885   4046   -331   -407   -381       C  
ATOM   5724  CD1 ILE D 117      -2.312 -37.089 103.034  1.00 21.44           C  
ANISOU 5724  CD1 ILE D 117     1076   4064   3007    -24   -251   -348       C  
ATOM   5725  N   ARG D 118       0.465 -32.611 105.864  1.00 30.24           N  
ANISOU 5725  N   ARG D 118     1958   5019   4513   -657   -447   -311       N  
ATOM   5726  CA  ARG D 118       1.081 -32.025 107.033  1.00 27.02           C  
ANISOU 5726  CA  ARG D 118     1597   4509   4159   -820   -589   -341       C  
ATOM   5727  C   ARG D 118       0.129 -31.838 108.198  1.00 26.32           C  
ANISOU 5727  C   ARG D 118     1772   4271   3956   -870   -649   -404       C  
ATOM   5728  O   ARG D 118       0.596 -31.754 109.337  1.00 30.13           O  
ANISOU 5728  O   ARG D 118     2322   4682   4442   -984   -810   -454       O  
ATOM   5729  CB  ARG D 118       1.710 -30.674 106.673  1.00 30.45           C  
ANISOU 5729  CB  ARG D 118     1952   4911   4707   -961   -510   -274       C  
ATOM   5730  CG  ARG D 118       2.978 -30.803 105.857  1.00 29.74           C  
ANISOU 5730  CG  ARG D 118     1623   4924   4754   -937   -486   -202       C  
ATOM   5731  CD  ARG D 118       3.646 -29.457 105.766  1.00 31.37           C  
ANISOU 5731  CD  ARG D 118     1756   5085   5079  -1117   -446   -147       C  
ATOM   5732  NE  ARG D 118       4.103 -29.013 107.073  1.00 33.59           N  
ANISOU 5732  NE  ARG D 118     2113   5257   5394  -1294   -627   -203       N  
ATOM   5733  CZ  ARG D 118       5.365 -29.085 107.488  1.00 40.28           C  
ANISOU 5733  CZ  ARG D 118     2854   6100   6351  -1343   -745   -225       C  
ATOM   5734  NH1 ARG D 118       6.305 -29.579 106.690  1.00 40.12           N  
ANISOU 5734  NH1 ARG D 118     2632   6187   6426  -1236   -690   -199       N  
ATOM   5735  NH2 ARG D 118       5.684 -28.657 108.700  1.00 35.30           N  
ANISOU 5735  NH2 ARG D 118     2334   5373   5707  -1498   -900   -290       N  
ATOM   5736  N   ARG D 119      -1.179 -31.805 107.945  1.00 27.59           N  
ANISOU 5736  N   ARG D 119     2079   4393   4012   -787   -528   -401       N  
ATOM   5