HEADER    SIGNALING PROTEIN                       29-APR-15   4ZJC              
TITLE     STRUCTURES OF THE HUMAN OX1 OREXIN RECEPTOR BOUND TO SELECTIVE AND    
TITLE    2 DUAL ANTAGONISTS                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HUMAN OX1R FUSION PROTEIN TO P.ABYSII GLYCOGEN SYNTHASE;   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP O43613 RESIDUES 1-245,UNP Q9V2J8 RESIDUES 218-413,UNP  
COMPND   5 O43613 RESIDUES 288-380;                                             
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, PYROCOCCUS ABYSSI (STRAIN GE5 /   
SOURCE   3 ORSAY);                                                              
SOURCE   4 ORGANISM_COMMON: HUMAN;                                              
SOURCE   5 ORGANISM_TAXID: 9606, 272844;                                        
SOURCE   6 STRAIN: GE5 / ORSAY;                                                 
SOURCE   7 GENE: HCRTR1, PAB2292, PYRAB00770;                                   
SOURCE   8 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   9 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1                                 
KEYWDS    OREXIN, SUVOREXANT, SB-674042, MEMBRANE PROTEIN-TRANSFERASE COMPLEX,  
KEYWDS   2 SIGNALING PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.YIN,C.A.BRAUTIGAM,Z.SHAO,L.CLARK,C.M.HARRELL,A.L.GOTTER,            
AUTHOR   2 P.J.COLEMAN,J.J.RENGER,D.M.ROSENBAUM                                 
REVDAT   3   13-APR-16 4ZJC    1       JRNL                                     
REVDAT   2   23-MAR-16 4ZJC    1       JRNL                                     
REVDAT   1   09-MAR-16 4ZJC    0                                                
JRNL        AUTH   J.YIN,K.BABAOGLU,C.A.BRAUTIGAM,L.CLARK,Z.SHAO,               
JRNL        AUTH 2 T.H.SCHEUERMANN,C.M.HARRELL,A.L.GOTTER,A.J.ROECKER,          
JRNL        AUTH 3 C.J.WINROW,J.J.RENGER,P.J.COLEMAN,D.M.ROSENBAUM              
JRNL        TITL   STRUCTURE AND LIGAND-BINDING MECHANISM OF THE HUMAN OX1 AND  
JRNL        TITL 2 OX2 OREXIN RECEPTORS.                                        
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  23   293 2016              
JRNL        REFN                   ESSN 1545-9985                               
JRNL        PMID   26950369                                                     
JRNL        DOI    10.1038/NSMB.3183                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.83 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.83                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.83                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 79.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 15148                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.320                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 806                             
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 44.8310 -  5.1436    0.99     3143   176  0.2011 0.2222        
REMARK   3     2  5.1436 -  4.0835    1.00     3035   169  0.1954 0.2577        
REMARK   3     3  4.0835 -  3.5675    0.99     2971   147  0.2118 0.2610        
REMARK   3     4  3.5675 -  3.2415    0.85     2545   139  0.2524 0.2919        
REMARK   3     5  3.2415 -  3.0092    0.58     1678   116  0.2734 0.3332        
REMARK   3     6  3.0092 -  2.8318    0.33      970    59  0.2802 0.3173        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.140           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           4175                                  
REMARK   3   ANGLE     :  0.667           5646                                  
REMARK   3   CHIRALITY :  0.023            628                                  
REMARK   3   PLANARITY :  0.003            728                                  
REMARK   3   DIHEDRAL  : 10.272           1533                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 20                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 26:40 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.7107   0.9939 -81.9567              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5233 T22:   0.1799                                     
REMARK   3      T33:   0.3324 T12:   0.0003                                     
REMARK   3      T13:  -0.0117 T23:  -0.1586                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6697 L22:   6.6499                                     
REMARK   3      L33:   5.2198 L12:   1.4737                                     
REMARK   3      L13:   0.7493 L23:   1.3014                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2743 S12:  -0.5054 S13:   0.4805                       
REMARK   3      S21:   0.4251 S22:  -0.0999 S23:   0.5732                       
REMARK   3      S31:  -0.5386 S32:  -0.1531 S33:  -0.0237                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 41:47 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):  13.0240   4.0551 -63.2366              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0905 T22:   1.2716                                     
REMARK   3      T33:   1.3756 T12:  -0.5315                                     
REMARK   3      T13:   0.4877 T23:  -0.5134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6448 L22:   9.6760                                     
REMARK   3      L33:   5.1806 L12:   2.3460                                     
REMARK   3      L13:  -4.2184 L23:  -5.9542                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9868 S12:   2.0812 S13:  -1.0880                       
REMARK   3      S21:  -0.3523 S22:  -0.1843 S23:   1.0080                       
REMARK   3      S31:   1.2426 S32:  -0.8675 S33:   0.9600                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 48:72 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):   5.4425  -5.1903 -41.0480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5346 T22:   0.1968                                     
REMARK   3      T33:   0.1910 T12:   0.0954                                     
REMARK   3      T13:  -0.0434 T23:  -0.2047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1318 L22:   2.3930                                     
REMARK   3      L33:   0.9706 L12:  -0.7378                                     
REMARK   3      L13:  -0.0835 L23:   1.4145                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1042 S12:  -0.2473 S13:  -0.0793                       
REMARK   3      S21:   0.5540 S22:   0.1883 S23:  -0.2285                       
REMARK   3      S31:   0.5252 S32:   0.2159 S33:  -0.5592                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 73:116 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.3953  -6.1770 -42.9393              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6041 T22:   0.1025                                     
REMARK   3      T33:   0.0667 T12:   0.1323                                     
REMARK   3      T13:   0.0215 T23:  -0.2198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7616 L22:   1.8341                                     
REMARK   3      L33:   5.0495 L12:  -0.1541                                     
REMARK   3      L13:  -0.9154 L23:   2.6112                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0582 S12:  -0.2547 S13:  -0.1178                       
REMARK   3      S21:   0.3153 S22:  -0.0868 S23:  -0.1299                       
REMARK   3      S31:   0.6893 S32:  -0.1665 S33:   0.0787                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 117:154 )                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.2376   1.5220 -36.4786              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4704 T22:   0.3443                                     
REMARK   3      T33:   0.0101 T12:  -0.0782                                     
REMARK   3      T13:   0.1593 T23:  -0.1861                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6343 L22:   0.9129                                     
REMARK   3      L33:   1.2710 L12:  -0.6370                                     
REMARK   3      L13:  -0.3969 L23:   0.1485                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0359 S12:  -0.0366 S13:  -0.0165                       
REMARK   3      S21:  -0.0006 S22:  -0.0058 S23:   0.1230                       
REMARK   3      S31:   0.2466 S32:  -0.3980 S33:   0.0810                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 155:162 )                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.8312  -5.1696 -23.8155              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3329 T22:   0.9300                                     
REMARK   3      T33:   0.9535 T12:  -0.3926                                     
REMARK   3      T13:   0.1103 T23:  -0.0595                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7003 L22:   5.8617                                     
REMARK   3      L33:   9.1268 L12:  -3.9462                                     
REMARK   3      L13:  -1.6650 L23:   2.4463                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5965 S12:  -0.1099 S13:  -0.9687                       
REMARK   3      S21:   1.1806 S22:  -0.4138 S23:   2.0820                       
REMARK   3      S31:   0.6205 S32:  -0.2841 S33:  -0.2399                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 163:187 )                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.9680  -5.7878 -49.5083              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3863 T22:   0.3996                                     
REMARK   3      T33:   0.1391 T12:  -0.0186                                     
REMARK   3      T13:   0.0178 T23:  -0.1678                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0507 L22:   1.5442                                     
REMARK   3      L33:   0.0118 L12:   0.3536                                     
REMARK   3      L13:   0.0708 L23:   0.1320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0754 S12:   0.2233 S13:  -0.1409                       
REMARK   3      S21:   0.1013 S22:  -0.5231 S23:   0.3917                       
REMARK   3      S31:   0.1762 S32:  -0.2256 S33:   0.3441                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 188:211 )                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.5550  -3.6645 -70.6387              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6825 T22:   0.8899                                     
REMARK   3      T33:   0.3397 T12:   0.1876                                     
REMARK   3      T13:  -0.0976 T23:  -0.3376                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0683 L22:   1.8295                                     
REMARK   3      L33:   5.0761 L12:  -0.2426                                     
REMARK   3      L13:  -0.5925 L23:   1.9267                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2798 S12:  -0.1092 S13:  -0.0361                       
REMARK   3      S21:  -0.2609 S22:  -0.4633 S23:   0.8665                       
REMARK   3      S31:  -0.9920 S32:  -1.6765 S33:   0.4660                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 212:228 )                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.6894   7.8157 -49.9662              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5630 T22:   0.5113                                     
REMARK   3      T33:   0.2991 T12:   0.2939                                     
REMARK   3      T13:  -0.0837 T23:  -0.1640                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0445 L22:   1.8340                                     
REMARK   3      L33:   0.7435 L12:   0.9216                                     
REMARK   3      L13:   0.2777 L23:  -0.8750                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2642 S12:   0.4177 S13:   0.6484                       
REMARK   3      S21:  -0.4281 S22:  -0.7637 S23:   0.2583                       
REMARK   3      S31:  -0.7558 S32:  -0.6606 S33:   0.0059                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 229:245 )                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.7770  17.3282 -27.1128              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4157 T22:   0.3155                                     
REMARK   3      T33:   0.1603 T12:   0.1098                                     
REMARK   3      T13:   0.0580 T23:   0.0391                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0489 L22:   7.1884                                     
REMARK   3      L33:   5.3427 L12:   6.8493                                     
REMARK   3      L13:   6.0423 L23:   6.1673                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4185 S12:  -0.3951 S13:   0.6388                       
REMARK   3      S21:  -0.2601 S22:  -0.4060 S23:   0.7764                       
REMARK   3      S31:  -0.5775 S32:  -0.4461 S33:   0.5329                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 246:246 ) OR ( CHAIN A AND RESID   
REMARK   3               1001:1011 )                                            
REMARK   3    ORIGIN FOR THE GROUP (A):   6.2089  17.9570  -4.7774              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3040 T22:   0.3354                                     
REMARK   3      T33:   0.2261 T12:   0.0083                                     
REMARK   3      T13:  -0.0411 T23:   0.0424                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5351 L22:   8.3383                                     
REMARK   3      L33:   4.2880 L12:  -5.2714                                     
REMARK   3      L13:   5.9041 L23:  -4.6666                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2184 S12:  -0.2949 S13:  -0.6759                       
REMARK   3      S21:  -0.1475 S22:   0.2974 S23:   0.9119                       
REMARK   3      S31:   1.0457 S32:  -0.5722 S33:  -0.5269                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 1012:1036 )                        
REMARK   3    ORIGIN FOR THE GROUP (A):   1.5941  25.4406  13.6670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3927 T22:   0.6148                                     
REMARK   3      T33:   0.1210 T12:  -0.0032                                     
REMARK   3      T13:  -0.1000 T23:  -0.0701                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6099 L22:   2.6652                                     
REMARK   3      L33:   3.0799 L12:   1.1275                                     
REMARK   3      L13:   1.5860 L23:  -2.0703                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2017 S12:  -1.0727 S13:   0.4949                       
REMARK   3      S21:   0.8165 S22:   0.0648 S23:   0.0835                       
REMARK   3      S31:  -0.5520 S32:   0.0059 S33:   0.1977                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 1037:1096 )                        
REMARK   3    ORIGIN FOR THE GROUP (A): -10.8090  36.4084   6.5879              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6897 T22:   0.4163                                     
REMARK   3      T33:   0.3849 T12:   0.0375                                     
REMARK   3      T13:  -0.0399 T23:  -0.3155                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5217 L22:   2.7745                                     
REMARK   3      L33:   3.1340 L12:  -0.3841                                     
REMARK   3      L13:  -1.0818 L23:   1.4696                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0294 S12:  -0.4362 S13:   0.7723                       
REMARK   3      S21:   0.1573 S22:  -0.0289 S23:   0.2476                       
REMARK   3      S31:  -1.1927 S32:  -0.1896 S33:   0.0458                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 1097:1121 )                        
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2580  28.1601   0.9776              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3785 T22:   0.1941                                     
REMARK   3      T33:   0.1411 T12:  -0.0138                                     
REMARK   3      T13:  -0.0232 T23:  -0.1090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1638 L22:   4.4054                                     
REMARK   3      L33:   1.7266 L12:  -1.1084                                     
REMARK   3      L13:  -0.8677 L23:  -0.8282                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0808 S12:  -0.3385 S13:   0.6143                       
REMARK   3      S21:  -0.0905 S22:  -0.0035 S23:  -0.3617                       
REMARK   3      S31:  -0.8180 S32:   0.1949 S33:   0.0060                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 1122:1162 )                        
REMARK   3    ORIGIN FOR THE GROUP (A): -11.0397  20.0151  -3.1824              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2935 T22:   0.1695                                     
REMARK   3      T33:   0.0510 T12:   0.0468                                     
REMARK   3      T13:  -0.0179 T23:  -0.0229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.8533 L22:   2.3487                                     
REMARK   3      L33:   8.7994 L12:  -0.4346                                     
REMARK   3      L13:  -0.7268 L23:  -0.4216                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1817 S12:   0.2933 S13:  -0.2074                       
REMARK   3      S21:  -0.0712 S22:  -0.1083 S23:   0.3454                       
REMARK   3      S31:   0.2502 S32:  -0.6133 S33:  -0.0975                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 1163:1196 )                        
REMARK   3    ORIGIN FOR THE GROUP (A): -10.0150  16.1772   5.9122              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5259 T22:   0.5263                                     
REMARK   3      T33:   0.0445 T12:   0.0437                                     
REMARK   3      T13:   0.0690 T23:   0.0513                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8730 L22:   2.0556                                     
REMARK   3      L33:   2.8391 L12:   0.1543                                     
REMARK   3      L13:  -0.5186 L23:   0.1893                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0398 S12:  -0.7265 S13:  -0.1935                       
REMARK   3      S21:   0.4704 S22:  -0.1218 S23:   0.1970                       
REMARK   3      S31:   0.4391 S32:  -0.4049 S33:   0.0925                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 288:324 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.3023  10.3311 -38.4863              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6638 T22:   0.3151                                     
REMARK   3      T33:   0.0343 T12:   0.1121                                     
REMARK   3      T13:  -0.0702 T23:  -0.0914                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5064 L22:   2.1981                                     
REMARK   3      L33:   2.4129 L12:   0.1396                                     
REMARK   3      L13:  -0.5842 L23:   0.4087                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1341 S12:  -0.0584 S13:   0.0053                       
REMARK   3      S21:  -0.4159 S22:  -0.2239 S23:   0.1454                       
REMARK   3      S31:  -0.3815 S32:  -0.2499 S33:   0.1030                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 325:339 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.0153  10.3613 -66.3142              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9537 T22:   0.8857                                     
REMARK   3      T33:   0.6909 T12:   0.1762                                     
REMARK   3      T13:   0.3251 T23:  -0.0948                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5424 L22:   0.2288                                     
REMARK   3      L33:   0.1757 L12:   1.2255                                     
REMARK   3      L13:  -1.0740 L23:  -0.2018                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1332 S12:   2.6165 S13:  -0.3383                       
REMARK   3      S21:  -2.0359 S22:  -0.0062 S23:  -0.5256                       
REMARK   3      S31:  -0.4842 S32:   0.0681 S33:  -0.3197                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 340:365 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.6109   3.3989 -40.6496              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2950 T22:   0.2873                                     
REMARK   3      T33:   0.1621 T12:   0.0588                                     
REMARK   3      T13:   0.0300 T23:  -0.1270                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4772 L22:   4.0069                                     
REMARK   3      L33:   6.1004 L12:  -0.3637                                     
REMARK   3      L13:   1.3328 L23:  -0.3945                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1437 S12:  -0.1248 S13:   0.0869                       
REMARK   3      S21:   0.0211 S22:  -0.0111 S23:  -0.1934                       
REMARK   3      S31:   0.4908 S32:  -0.0103 S33:  -0.1725                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 366:373 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.8992  -4.4996 -26.1390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1582 T22:   0.7028                                     
REMARK   3      T33:   0.5176 T12:   0.2181                                     
REMARK   3      T13:  -0.2531 T23:  -0.2188                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0196 L22:   7.8731                                     
REMARK   3      L33:   4.4392 L12:   1.9612                                     
REMARK   3      L13:  -2.2538 L23:  -5.8341                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3671 S12:  -1.0604 S13:   0.8442                       
REMARK   3      S21:  -0.1388 S22:  -0.3770 S23:  -0.0818                       
REMARK   3      S31:   1.1336 S32:   1.9822 S33:   0.1439                       
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 4ZJC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-APR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000209401.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18893                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.830                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 9.600                              
REMARK 200  R MERGE                    (I) : 0.17000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4S0V,2BFW                                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE PH 5.6, 32% PEG    
REMARK 280  400, 200 MM POTOSSIUM, LIPIDIC CUBIC PHASE, TEMPERATURE 293K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       31.71550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       91.06450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.23300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       91.06450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.71550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.23300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A    -7                                                      
REMARK 465     TYR A    -6                                                      
REMARK 465     LYS A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     PRO A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     MET A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     VAL A    13                                                      
REMARK 465     PRO A    14                                                      
REMARK 465     PRO A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     SER A    17                                                      
REMARK 465     ARG A    18                                                      
REMARK 465     GLU A    19                                                      
REMARK 465     PRO A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     PRO A    22                                                      
REMARK 465     VAL A    23                                                      
REMARK 465     PRO A    24                                                      
REMARK 465     PRO A    25                                                      
REMARK 465     SER A   374                                                      
REMARK 465     CYS A   375                                                      
REMARK 465     CYS A   376                                                      
REMARK 465     LEU A   377                                                      
REMARK 465     PRO A   378                                                      
REMARK 465     GLY A   379                                                      
REMARK 465     LEU A   380                                                      
REMARK 465     HIS A   381                                                      
REMARK 465     HIS A   382                                                      
REMARK 465     HIS A   383                                                      
REMARK 465     HIS A   384                                                      
REMARK 465     HIS A   385                                                      
REMARK 465     HIS A   386                                                      
REMARK 465     HIS A   387                                                      
REMARK 465     HIS A   388                                                      
REMARK 465     HIS A   389                                                      
REMARK 465     HIS A   390                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  61      -78.04    -69.91                                   
REMARK 500    ARG A 162       71.61    -69.49                                   
REMARK 500    SER A 187      -49.24   -150.77                                   
REMARK 500    TYR A 224      -57.85   -143.79                                   
REMARK 500    ARG A 245       79.05   -117.21                                   
REMARK 500    TRP A1007       76.83    -68.33                                   
REMARK 500    GLN A1045      -74.37   -137.82                                   
REMARK 500    SER A1060     -151.45    -83.44                                   
REMARK 500    LYS A1061      162.75     63.40                                   
REMARK 500    SER A1111      -51.04   -127.30                                   
REMARK 500    PRO A1118       42.37    -86.12                                   
REMARK 500    PHE A1121       11.60   -141.46                                   
REMARK 500    GLU A1122      105.81    -30.94                                   
REMARK 500    ALA A1142       67.19    -68.63                                   
REMARK 500    THR A1151     -161.53   -118.15                                   
REMARK 500    VAL A 323      -73.10   -126.04                                   
REMARK 500    ARG A 328      -16.74   -148.00                                   
REMARK 500    ALA A 330     -144.34     55.17                                   
REMARK 500    SER A 331       46.85    -84.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLA A 2002                                                       
REMARK 610     OLA A 2003                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 4OT A 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2003                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ZJ8   RELATED DB: PDB                                   
DBREF  4ZJC A    1   246  UNP    O43613   OX1R_HUMAN       1    246             
DBREF  4ZJC A 1001  1196  UNP    Q9V2J8   Q9V2J8_PYRAB   218    413             
DBREF  4ZJC A  288   380  UNP    O43613   OX1R_HUMAN     288    380             
SEQADV 4ZJC ASP A   -7  UNP  O43613              EXPRESSION TAG                 
SEQADV 4ZJC TYR A   -6  UNP  O43613              EXPRESSION TAG                 
SEQADV 4ZJC LYS A   -5  UNP  O43613              EXPRESSION TAG                 
SEQADV 4ZJC ASP A   -4  UNP  O43613              EXPRESSION TAG                 
SEQADV 4ZJC ASP A   -3  UNP  O43613              EXPRESSION TAG                 
SEQADV 4ZJC ASP A   -2  UNP  O43613              EXPRESSION TAG                 
SEQADV 4ZJC ASP A   -1  UNP  O43613              EXPRESSION TAG                 
SEQADV 4ZJC ALA A    0  UNP  O43613              EXPRESSION TAG                 
SEQADV 4ZJC ILE A  319  UNP  O43613    VAL   319 ENGINEERED MUTATION            
SEQADV 4ZJC HIS A  381  UNP  O43613              EXPRESSION TAG                 
SEQADV 4ZJC HIS A  382  UNP  O43613              EXPRESSION TAG                 
SEQADV 4ZJC HIS A  383  UNP  O43613              EXPRESSION TAG                 
SEQADV 4ZJC HIS A  384  UNP  O43613              EXPRESSION TAG                 
SEQADV 4ZJC HIS A  385  UNP  O43613              EXPRESSION TAG                 
SEQADV 4ZJC HIS A  386  UNP  O43613              EXPRESSION TAG                 
SEQADV 4ZJC HIS A  387  UNP  O43613              EXPRESSION TAG                 
SEQADV 4ZJC HIS A  388  UNP  O43613              EXPRESSION TAG                 
SEQADV 4ZJC HIS A  389  UNP  O43613              EXPRESSION TAG                 
SEQADV 4ZJC HIS A  390  UNP  O43613              EXPRESSION TAG                 
SEQRES   1 A  553  ASP TYR LYS ASP ASP ASP ASP ALA MET GLU PRO SER ALA          
SEQRES   2 A  553  THR PRO GLY ALA GLN MET GLY VAL PRO PRO GLY SER ARG          
SEQRES   3 A  553  GLU PRO SER PRO VAL PRO PRO ASP TYR GLU ASP GLU PHE          
SEQRES   4 A  553  LEU ARG TYR LEU TRP ARG ASP TYR LEU TYR PRO LYS GLN          
SEQRES   5 A  553  TYR GLU TRP VAL LEU ILE ALA ALA TYR VAL ALA VAL PHE          
SEQRES   6 A  553  VAL VAL ALA LEU VAL GLY ASN THR LEU VAL CYS LEU ALA          
SEQRES   7 A  553  VAL TRP ARG ASN HIS HIS MET ARG THR VAL THR ASN TYR          
SEQRES   8 A  553  PHE ILE VAL ASN LEU SER LEU ALA ASP VAL LEU VAL THR          
SEQRES   9 A  553  ALA ILE CYS LEU PRO ALA SER LEU LEU VAL ASP ILE THR          
SEQRES  10 A  553  GLU SER TRP LEU PHE GLY HIS ALA LEU CYS LYS VAL ILE          
SEQRES  11 A  553  PRO TYR LEU GLN ALA VAL SER VAL SER VAL ALA VAL LEU          
SEQRES  12 A  553  THR LEU SER PHE ILE ALA LEU ASP ARG TRP TYR ALA ILE          
SEQRES  13 A  553  CYS HIS PRO LEU LEU PHE LYS SER THR ALA ARG ARG ALA          
SEQRES  14 A  553  ARG GLY SER ILE LEU GLY ILE TRP ALA VAL SER LEU ALA          
SEQRES  15 A  553  ILE MET VAL PRO GLN ALA ALA VAL MET GLU CYS SER SER          
SEQRES  16 A  553  VAL LEU PRO GLU LEU ALA ASN ARG THR ARG LEU PHE SER          
SEQRES  17 A  553  VAL CYS ASP GLU ARG TRP ALA ASP ASP LEU TYR PRO LYS          
SEQRES  18 A  553  ILE TYR HIS SER CYS PHE PHE ILE VAL THR TYR LEU ALA          
SEQRES  19 A  553  PRO LEU GLY LEU MET ALA MET ALA TYR PHE GLN ILE PHE          
SEQRES  20 A  553  ARG LYS LEU TRP GLY ARG GLN GLY ILE ASP CYS SER PHE          
SEQRES  21 A  553  TRP ASN GLU SER TYR LEU THR GLY SER ARG ASP GLU ARG          
SEQRES  22 A  553  LYS LYS SER LEU LEU SER LYS PHE GLY MET ASP GLU GLY          
SEQRES  23 A  553  VAL THR PHE MET PHE ILE GLY ARG PHE ASP ARG GLY GLN          
SEQRES  24 A  553  LYS GLY VAL ASP VAL LEU LEU LYS ALA ILE GLU ILE LEU          
SEQRES  25 A  553  SER SER LYS LYS GLU PHE GLN GLU MET ARG PHE ILE ILE          
SEQRES  26 A  553  ILE GLY LYS GLY ASP PRO GLU LEU GLU GLY TRP ALA ARG          
SEQRES  27 A  553  SER LEU GLU GLU LYS HIS GLY ASN VAL LYS VAL ILE THR          
SEQRES  28 A  553  GLU MET LEU SER ARG GLU PHE VAL ARG GLU LEU TYR GLY          
SEQRES  29 A  553  SER VAL ASP PHE VAL ILE ILE PRO SER TYR PHE GLU PRO          
SEQRES  30 A  553  PHE GLY LEU VAL ALA LEU GLU ALA MET CYS LEU GLY ALA          
SEQRES  31 A  553  ILE PRO ILE ALA SER ALA VAL GLY GLY LEU ARG ASP ILE          
SEQRES  32 A  553  ILE THR ASN GLU THR GLY ILE LEU VAL LYS ALA GLY ASP          
SEQRES  33 A  553  PRO GLY GLU LEU ALA ASN ALA ILE LEU LYS ALA LEU GLU          
SEQRES  34 A  553  LEU SER ARG SER ASP LEU SER LYS PHE ARG GLU ASN CYS          
SEQRES  35 A  553  LYS LYS ARG ALA MET SER PHE SER LYS GLN MET ARG ALA          
SEQRES  36 A  553  ARG ARG LYS THR ALA LYS MET LEU MET VAL VAL LEU LEU          
SEQRES  37 A  553  VAL PHE ALA LEU CYS TYR LEU PRO ILE SER VAL LEU ASN          
SEQRES  38 A  553  ILE LEU LYS ARG VAL PHE GLY MET PHE ARG GLN ALA SER          
SEQRES  39 A  553  ASP ARG GLU ALA VAL TYR ALA CYS PHE THR PHE SER HIS          
SEQRES  40 A  553  TRP LEU VAL TYR ALA ASN SER ALA ALA ASN PRO ILE ILE          
SEQRES  41 A  553  TYR ASN PHE LEU SER GLY LYS PHE ARG GLU GLN PHE LYS          
SEQRES  42 A  553  ALA ALA PHE SER CYS CYS LEU PRO GLY LEU HIS HIS HIS          
SEQRES  43 A  553  HIS HIS HIS HIS HIS HIS HIS                                  
HET    4OT  A2001      32                                                       
HET    OLA  A2002       9                                                       
HET    OLA  A2003       8                                                       
HETNAM     4OT [5-(2-FLUOROPHENYL)-2-METHYL-1,3-THIAZOL-4-YL]{(2S)-2-           
HETNAM   2 4OT  [(5-PHENYL-1,3,4-OXADIAZOL-2-YL)METHYL]PYRROLIDIN-1-            
HETNAM   3 4OT  YL}METHANONE                                                    
HETNAM     OLA OLEIC ACID                                                       
FORMUL   2  4OT    C24 H21 F N4 O2 S                                            
FORMUL   3  OLA    2(C18 H34 O2)                                                
HELIX    1 AA1 TYR A   27  TRP A   36  1                                  10    
HELIX    2 AA2 GLU A   46  ASN A   74  1                                  29    
HELIX    3 AA3 THR A   79  GLU A  110  1                                  32    
HELIX    4 AA4 ALA A  117  HIS A  150  1                                  34    
HELIX    5 AA5 PRO A  151  PHE A  154  5                                   4    
HELIX    6 AA6 THR A  157  MET A  176  1                                  20    
HELIX    7 AA7 MET A  176  VAL A  182  1                                   7    
HELIX    8 AA8 ASP A  209  TYR A  224  1                                  16    
HELIX    9 AA9 TYR A  224  TRP A  243  1                                  20    
HELIX   10 AB1 ASN A 1008  LEU A 1012  5                                   5    
HELIX   11 AB2 SER A 1015  PHE A 1027  1                                  13    
HELIX   12 AB3 GLY A 1047  LEU A 1058  1                                  12    
HELIX   13 AB4 GLU A 1063  GLN A 1065  5                                   3    
HELIX   14 AB5 ASP A 1076  HIS A 1090  1                                  15    
HELIX   15 AB6 SER A 1101  GLY A 1110  1                                  10    
HELIX   16 AB7 GLY A 1125  LEU A 1134  1                                  10    
HELIX   17 AB8 GLY A 1144  ILE A 1150  1                                   7    
HELIX   18 AB9 ASP A 1162  SER A 1177  1                                  16    
HELIX   19 AC1 LEU A 1181  VAL A  323  1                                  52    
HELIX   20 AC2 ALA A  335  SER A  362  1                                  28    
HELIX   21 AC3 SER A  362  ALA A  372  1                                  11    
SHEET    1 AA1 2 MET A 183  SER A 186  0                                        
SHEET    2 AA1 2 VAL A 201  GLU A 204 -1  O  ASP A 203   N  GLU A 184           
SHEET    1 AA2 6 VAL A1093  ILE A1096  0                                        
SHEET    2 AA2 6 MET A1067  ILE A1072  1  N  PHE A1069   O  LYS A1094           
SHEET    3 AA2 6 VAL A1033  ILE A1038  1  N  PHE A1037   O  ILE A1070           
SHEET    4 AA2 6 PHE A1114  ILE A1117  1  O  ILE A1116   N  MET A1036           
SHEET    5 AA2 6 ILE A1137  SER A1141  1  O  ILE A1139   N  VAL A1115           
SHEET    6 AA2 6 ILE A1156  VAL A1158  1  O  ILE A1156   N  PRO A1138           
SSBOND   1 CYS A  119    CYS A  202                          1555   1555  2.03  
SITE     1 AC1 11 SER A 103  PRO A 123  GLN A 126  VAL A 130                    
SITE     2 AC1 11 GLN A 179  MET A 183  PHE A 219  ILE A 314                    
SITE     3 AC1 11 ASN A 318  HIS A 344  TYR A 348                               
SITE     1 AC2  4 THR A 109  PHE A 239  ARG A 240  TRP A 243                    
SITE     1 AC3  3 TYR A 146  LEU A 153  LYS A 155                               
CRYST1   63.431   66.466  182.129  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015765  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015045  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005491        0.00000                         
ATOM      1  N   ASP A  26     -11.354   6.612 -88.148  1.00 69.84           N  
ANISOU    1  N   ASP A  26     9410   5927  11199   2028  -1024   -996       N  
ATOM      2  CA  ASP A  26     -12.279   5.673 -87.525  1.00 69.05           C  
ANISOU    2  CA  ASP A  26     8873   6020  11344   2089   -946  -1172       C  
ATOM      3  C   ASP A  26     -11.530   4.590 -86.757  1.00 66.16           C  
ANISOU    3  C   ASP A  26     8561   5841  10734   1825   -723  -1284       C  
ATOM      4  O   ASP A  26     -11.903   4.236 -85.638  1.00 66.85           O  
ANISOU    4  O   ASP A  26     8425   6042  10932   1807   -417  -1514       O  
ATOM      5  CB  ASP A  26     -13.183   5.030 -88.579  1.00 65.00           C  
ANISOU    5  CB  ASP A  26     8087   5574  11036   2189  -1355  -1039       C  
ATOM      6  CG  ASP A  26     -13.911   6.053 -89.424  1.00 64.10           C  
ANISOU    6  CG  ASP A  26     7946   5283  11127   2439  -1642   -901       C  
ATOM      7  OD1 ASP A  26     -14.254   7.129 -88.892  1.00 65.32           O  
ANISOU    7  OD1 ASP A  26     8065   5281  11471   2629  -1465   -998       O  
ATOM      8  OD2 ASP A  26     -14.135   5.782 -90.622  1.00 62.11           O  
ANISOU    8  OD2 ASP A  26     7735   5038  10828   2441  -2055   -700       O  
ATOM      9  N   TYR A  27     -10.471   4.072 -87.368  1.00 61.82           N  
ANISOU    9  N   TYR A  27     8313   5334   9843   1611   -861  -1129       N  
ATOM     10  CA  TYR A  27      -9.711   2.966 -86.797  1.00 58.42           C  
ANISOU   10  CA  TYR A  27     7955   5074   9168   1366   -726  -1196       C  
ATOM     11  C   TYR A  27      -8.380   3.432 -86.212  1.00 59.12           C  
ANISOU   11  C   TYR A  27     8371   5175   8915   1167   -496  -1215       C  
ATOM     12  O   TYR A  27      -7.387   2.707 -86.263  1.00 55.96           O  
ANISOU   12  O   TYR A  27     8120   4909   8235    951   -504  -1161       O  
ATOM     13  CB  TYR A  27      -9.460   1.895 -87.860  1.00 54.05           C  
ANISOU   13  CB  TYR A  27     7457   4598   8481   1258  -1037  -1037       C  
ATOM     14  CG  TYR A  27     -10.714   1.376 -88.526  1.00 55.28           C  
ANISOU   14  CG  TYR A  27     7280   4808   8918   1378  -1300   -980       C  
ATOM     15  CD1 TYR A  27     -11.776   0.892 -87.774  1.00 57.05           C  
ANISOU   15  CD1 TYR A  27     7080   5184   9412   1391  -1140  -1103       C  
ATOM     16  CD2 TYR A  27     -10.839   1.379 -89.909  1.00 55.49           C  
ANISOU   16  CD2 TYR A  27     7413   4757   8916   1443  -1704   -803       C  
ATOM     17  CE1 TYR A  27     -12.925   0.415 -88.380  1.00 59.85           C  
ANISOU   17  CE1 TYR A  27     7072   5612  10054   1467  -1391  -1064       C  
ATOM     18  CE2 TYR A  27     -11.984   0.906 -90.525  1.00 58.38           C  
ANISOU   18  CE2 TYR A  27     7461   5192   9529   1532  -1995   -758       C  
ATOM     19  CZ  TYR A  27     -13.024   0.425 -89.756  1.00 61.56           C  
ANISOU   19  CZ  TYR A  27     7392   5746  10252   1545  -1845   -894       C  
ATOM     20  OH  TYR A  27     -14.166  -0.046 -90.365  1.00 64.01           O  
ANISOU   20  OH  TYR A  27     7334   6140  10847   1607  -2149   -867       O  
ATOM     21  N   GLU A  28      -8.364   4.639 -85.655  1.00 60.14           N  
ANISOU   21  N   GLU A  28     8586   5170   9095   1240   -300  -1301       N  
ATOM     22  CA  GLU A  28      -7.128   5.227 -85.145  1.00 61.21           C  
ANISOU   22  CA  GLU A  28     8993   5291   8972   1036   -109  -1330       C  
ATOM     23  C   GLU A  28      -6.690   4.618 -83.815  1.00 59.68           C  
ANISOU   23  C   GLU A  28     8826   5270   8579    866    129  -1506       C  
ATOM     24  O   GLU A  28      -5.504   4.358 -83.605  1.00 56.83           O  
ANISOU   24  O   GLU A  28     8559   5032   8002    625    157  -1493       O  
ATOM     25  CB  GLU A  28      -7.280   6.742 -84.991  1.00 65.84           C  
ANISOU   25  CB  GLU A  28     9693   5626   9697   1156      8  -1378       C  
ATOM     26  CG  GLU A  28      -6.051   7.426 -84.406  1.00 65.22           C  
ANISOU   26  CG  GLU A  28     9800   5517   9465    912    199  -1467       C  
ATOM     27  CD  GLU A  28      -6.177   8.936 -84.366  1.00 71.58           C  
ANISOU   27  CD  GLU A  28    10727   6017  10455   1009    289  -1518       C  
ATOM     28  OE1 GLU A  28      -7.042   9.484 -85.082  1.00 75.91           O  
ANISOU   28  OE1 GLU A  28    11276   6364  11202   1267    146  -1402       O  
ATOM     29  OE2 GLU A  28      -5.410   9.576 -83.616  1.00 72.48           O  
ANISOU   29  OE2 GLU A  28    10827   6157  10556    830    387  -1684       O  
ATOM     30  N   ASP A  29      -7.648   4.397 -82.921  1.00 63.93           N  
ANISOU   30  N   ASP A  29     9192   5860   9238    985    278  -1694       N  
ATOM     31  CA  ASP A  29      -7.356   3.866 -81.593  1.00 63.85           C  
ANISOU   31  CA  ASP A  29     9216   6038   9005    818    489  -1869       C  
ATOM     32  C   ASP A  29      -6.707   2.484 -81.684  1.00 58.44           C  
ANISOU   32  C   ASP A  29     8561   5514   8131    605    384  -1776       C  
ATOM     33  O   ASP A  29      -5.644   2.243 -81.102  1.00 58.32           O  
ANISOU   33  O   ASP A  29     8717   5628   7813    421    359  -1764       O  
ATOM     34  CB  ASP A  29      -8.636   3.801 -80.754  1.00 69.08           C  
ANISOU   34  CB  ASP A  29     9581   6771   9894    914    793  -2095       C  
ATOM     35  CG  ASP A  29      -8.370   3.942 -79.264  1.00 73.98           C  
ANISOU   35  CG  ASP A  29    10335   7550  10225    749   1101  -2285       C  
ATOM     36  OD1 ASP A  29      -7.305   3.489 -78.797  1.00 74.24           O  
ANISOU   36  OD1 ASP A  29    10602   7706   9898    517   1041  -2225       O  
ATOM     37  OD2 ASP A  29      -9.231   4.511 -78.559  1.00 78.05           O  
ANISOU   37  OD2 ASP A  29    10704   8083  10869    856   1380  -2489       O  
ATOM     38  N   GLU A  30      -7.341   1.588 -82.433  1.00 53.34           N  
ANISOU   38  N   GLU A  30     7701   4926   7642    641    230  -1642       N  
ATOM     39  CA  GLU A  30      -6.858   0.219 -82.565  1.00 49.02           C  
ANISOU   39  CA  GLU A  30     7177   4546   6900    454     96  -1488       C  
ATOM     40  C   GLU A  30      -5.538   0.132 -83.329  1.00 46.52           C  
ANISOU   40  C   GLU A  30     7091   4180   6405    392   -128  -1389       C  
ATOM     41  O   GLU A  30      -4.711  -0.734 -83.042  1.00 47.01           O  
ANISOU   41  O   GLU A  30     7233   4372   6257    234   -175  -1329       O  
ATOM     42  CB  GLU A  30      -7.913  -0.654 -83.249  1.00 52.84           C  
ANISOU   42  CB  GLU A  30     7381   5091   7604    493    -34  -1375       C  
ATOM     43  CG  GLU A  30      -8.418  -0.122 -84.581  1.00 57.62           C  
ANISOU   43  CG  GLU A  30     7888   5545   8458    701   -286  -1304       C  
ATOM     44  CD  GLU A  30      -9.433  -1.049 -85.225  1.00 63.05           C  
ANISOU   44  CD  GLU A  30     8290   6317   9348    704   -459  -1213       C  
ATOM     45  OE1 GLU A  30     -10.612  -0.656 -85.338  1.00 67.09           O  
ANISOU   45  OE1 GLU A  30     8497   6809  10185    863   -457  -1266       O  
ATOM     46  OE2 GLU A  30      -9.053  -2.174 -85.614  1.00 62.44           O  
ANISOU   46  OE2 GLU A  30     8277   6315   9131    550   -609  -1109       O  
ATOM     47  N   PHE A  31      -5.336   1.023 -84.294  1.00 47.23           N  
ANISOU   47  N   PHE A  31     7197   4185   6563    466   -202  -1290       N  
ATOM     48  CA  PHE A  31      -4.107   1.006 -85.081  1.00 44.33           C  
ANISOU   48  CA  PHE A  31     6907   3907   6029    347   -301  -1153       C  
ATOM     49  C   PHE A  31      -2.935   1.554 -84.272  1.00 43.13           C  
ANISOU   49  C   PHE A  31     6808   3840   5741    201   -169  -1229       C  
ATOM     50  O   PHE A  31      -1.823   1.023 -84.333  1.00 44.13           O  
ANISOU   50  O   PHE A  31     6927   4117   5725     85   -223  -1183       O  
ATOM     51  CB  PHE A  31      -4.278   1.803 -86.376  1.00 42.65           C  
ANISOU   51  CB  PHE A  31     6750   3556   5899    448   -436  -1040       C  
ATOM     52  CG  PHE A  31      -3.169   1.589 -87.366  1.00 39.19           C  
ANISOU   52  CG  PHE A  31     6406   3203   5281    334   -535   -932       C  
ATOM     53  CD1 PHE A  31      -3.032   0.373 -88.017  1.00 35.78           C  
ANISOU   53  CD1 PHE A  31     5940   2893   4762    304   -672   -872       C  
ATOM     54  CD2 PHE A  31      -2.266   2.600 -87.648  1.00 43.56           C  
ANISOU   54  CD2 PHE A  31     7087   3696   5768    254   -476   -919       C  
ATOM     55  CE1 PHE A  31      -2.013   0.167 -88.929  1.00 37.69           C  
ANISOU   55  CE1 PHE A  31     6269   3206   4844    215   -715   -822       C  
ATOM     56  CE2 PHE A  31      -1.245   2.402 -88.561  1.00 44.51           C  
ANISOU   56  CE2 PHE A  31     7303   3881   5727    143   -529   -858       C  
ATOM     57  CZ  PHE A  31      -1.119   1.183 -89.202  1.00 41.04           C  
ANISOU   57  CZ  PHE A  31     6823   3574   5195    133   -633   -821       C  
ATOM     58  N   LEU A  32      -3.188   2.616 -83.514  1.00 42.94           N  
ANISOU   58  N   LEU A  32     6806   3715   5794    230    -23  -1371       N  
ATOM     59  CA  LEU A  32      -2.168   3.173 -82.632  1.00 44.45           C  
ANISOU   59  CA  LEU A  32     7027   3994   5869    111     22  -1479       C  
ATOM     60  C   LEU A  32      -1.821   2.177 -81.533  1.00 42.85           C  
ANISOU   60  C   LEU A  32     6835   3984   5461     17     17  -1521       C  
ATOM     61  O   LEU A  32      -0.666   2.079 -81.118  1.00 40.64           O  
ANISOU   61  O   LEU A  32     6573   3831   5038    -98    -40  -1518       O  
ATOM     62  CB  LEU A  32      -2.629   4.500 -82.025  1.00 45.92           C  
ANISOU   62  CB  LEU A  32     7250   4021   6175    197    119  -1648       C  
ATOM     63  CG  LEU A  32      -2.534   5.725 -82.936  1.00 42.73           C  
ANISOU   63  CG  LEU A  32     6905   3389   5941    237    104  -1596       C  
ATOM     64  CD1 LEU A  32      -2.889   6.991 -82.170  1.00 45.66           C  
ANISOU   64  CD1 LEU A  32     7323   3590   6435    330    166  -1794       C  
ATOM     65  CD2 LEU A  32      -1.142   5.832 -83.546  1.00 37.08           C  
ANISOU   65  CD2 LEU A  32     6259   2742   5086     72     16  -1485       C  
ATOM     66  N   ARG A  33      -2.821   1.435 -81.065  1.00 43.72           N  
ANISOU   66  N   ARG A  33     6962   4093   5556     62     79  -1556       N  
ATOM     67  CA  ARG A  33      -2.569   0.366 -80.106  1.00 43.63           C  
ANISOU   67  CA  ARG A  33     7046   4226   5307    -64     80  -1544       C  
ATOM     68  C   ARG A  33      -1.775  -0.761 -80.763  1.00 42.61           C  
ANISOU   68  C   ARG A  33     6873   4177   5139   -116   -122  -1375       C  
ATOM     69  O   ARG A  33      -0.983  -1.436 -80.108  1.00 45.84           O  
ANISOU   69  O   ARG A  33     7352   4696   5370   -214   -209  -1336       O  
ATOM     70  CB  ARG A  33      -3.879  -0.176 -79.529  1.00 44.16           C  
ANISOU   70  CB  ARG A  33     7174   4249   5355    -69    280  -1624       C  
ATOM     71  CG  ARG A  33      -4.520   0.721 -78.484  1.00 47.59           C  
ANISOU   71  CG  ARG A  33     7637   4693   5753    -61    580  -1829       C  
ATOM     72  CD  ARG A  33      -5.708   0.033 -77.832  1.00 53.21           C  
ANISOU   72  CD  ARG A  33     8251   5508   6461   -128    846  -1867       C  
ATOM     73  NE  ARG A  33      -6.398   0.901 -76.882  1.00 63.84           N  
ANISOU   73  NE  ARG A  33     9596   6871   7789   -108   1212  -2129       N  
ATOM     74  CZ  ARG A  33      -6.095   0.990 -75.591  1.00 70.51           C  
ANISOU   74  CZ  ARG A  33    10658   7857   8275   -288   1393  -2240       C  
ATOM     75  NH1 ARG A  33      -5.107   0.263 -75.086  1.00 72.43           N  
ANISOU   75  NH1 ARG A  33    11138   8218   8163   -492   1203  -2097       N  
ATOM     76  NH2 ARG A  33      -6.779   1.808 -74.803  1.00 72.78           N  
ANISOU   76  NH2 ARG A  33    10890   8188   8575   -242   1703  -2452       N  
ATOM     77  N   TYR A  34      -1.985  -0.950 -82.062  1.00 42.09           N  
ANISOU   77  N   TYR A  34     6707   4050   5233    -37   -205  -1274       N  
ATOM     78  CA  TYR A  34      -1.311  -2.014 -82.801  1.00 38.60           C  
ANISOU   78  CA  TYR A  34     6215   3686   4766    -54   -368  -1139       C  
ATOM     79  C   TYR A  34       0.162  -1.694 -83.043  1.00 41.98           C  
ANISOU   79  C   TYR A  34     6600   4212   5139   -107   -399  -1133       C  
ATOM     80  O   TYR A  34       1.005  -2.591 -83.062  1.00 41.89           O  
ANISOU   80  O   TYR A  34     6561   4280   5074   -129   -507  -1092       O  
ATOM     81  CB  TYR A  34      -2.020  -2.267 -84.137  1.00 36.12           C  
ANISOU   81  CB  TYR A  34     5837   3298   4590     39   -450  -1055       C  
ATOM     82  CG  TYR A  34      -1.460  -3.430 -84.930  1.00 39.58           C  
ANISOU   82  CG  TYR A  34     6227   3810   5000     35   -595   -958       C  
ATOM     83  CD1 TYR A  34      -1.811  -4.740 -84.622  1.00 43.37           C  
ANISOU   83  CD1 TYR A  34     6714   4278   5485     16   -696   -920       C  
ATOM     84  CD2 TYR A  34      -0.591  -3.218 -85.994  1.00 33.90           C  
ANISOU   84  CD2 TYR A  34     5482   3141   4256     40   -618   -929       C  
ATOM     85  CE1 TYR A  34      -1.306  -5.805 -85.343  1.00 27.84           C  
ANISOU   85  CE1 TYR A  34     4706   2348   3522     35   -820   -858       C  
ATOM     86  CE2 TYR A  34      -0.082  -4.278 -86.721  1.00 30.31           C  
ANISOU   86  CE2 TYR A  34     4989   2741   3785     53   -713   -895       C  
ATOM     87  CZ  TYR A  34      -0.443  -5.568 -86.391  1.00 29.79           C  
ANISOU   87  CZ  TYR A  34     4910   2661   3748     67   -816   -860       C  
ATOM     88  OH  TYR A  34       0.062  -6.624 -87.111  1.00 32.74           O  
ANISOU   88  OH  TYR A  34     5253   3056   4131     99   -905   -851       O  
ATOM     89  N   LEU A  35       0.468  -0.415 -83.232  1.00 41.40           N  
ANISOU   89  N   LEU A  35     6525   4099   5105   -124   -312  -1195       N  
ATOM     90  CA  LEU A  35       1.840  -0.001 -83.505  1.00 40.38           C  
ANISOU   90  CA  LEU A  35     6357   4036   4951   -204   -326  -1232       C  
ATOM     91  C   LEU A  35       2.677   0.143 -82.236  1.00 43.73           C  
ANISOU   91  C   LEU A  35     6788   4552   5276   -293   -346  -1339       C  
ATOM     92  O   LEU A  35       3.905   0.105 -82.293  1.00 48.25           O  
ANISOU   92  O   LEU A  35     7299   5205   5829   -367   -402  -1392       O  
ATOM     93  CB  LEU A  35       1.860   1.322 -84.275  1.00 40.31           C  
ANISOU   93  CB  LEU A  35     6394   3904   5020   -208   -263  -1247       C  
ATOM     94  CG  LEU A  35       1.298   1.330 -85.697  1.00 38.93           C  
ANISOU   94  CG  LEU A  35     6273   3630   4889   -140   -296  -1133       C  
ATOM     95  CD1 LEU A  35       1.557   2.674 -86.363  1.00 30.00           C  
ANISOU   95  CD1 LEU A  35     5274   2341   3785   -180   -262  -1127       C  
ATOM     96  CD2 LEU A  35       1.890   0.196 -86.518  1.00 39.18           C  
ANISOU   96  CD2 LEU A  35     6249   3774   4863   -150   -372  -1087       C  
ATOM     97  N   TRP A  36       2.014   0.303 -81.094  1.00 41.55           N  
ANISOU   97  N   TRP A  36     6601   4265   4923   -294   -307  -1394       N  
ATOM     98  CA  TRP A  36       2.713   0.633 -79.855  1.00 40.26           C  
ANISOU   98  CA  TRP A  36     6498   4182   4617   -386   -340  -1504       C  
ATOM     99  C   TRP A  36       2.477  -0.362 -78.723  1.00 38.90           C  
ANISOU   99  C   TRP A  36     6456   4086   4237   -426   -409  -1472       C  
ATOM    100  O   TRP A  36       2.725  -0.048 -77.559  1.00 42.38           O  
ANISOU  100  O   TRP A  36     7013   4591   4499   -509   -417  -1557       O  
ATOM    101  CB  TRP A  36       2.301   2.030 -79.383  1.00 31.82           C  
ANISOU  101  CB  TRP A  36     5502   3019   3570   -383   -224  -1630       C  
ATOM    102  CG  TRP A  36       2.711   3.127 -80.314  1.00 42.67           C  
ANISOU  102  CG  TRP A  36     6832   4276   5104   -380   -203  -1647       C  
ATOM    103  CD1 TRP A  36       2.082   3.510 -81.463  1.00 43.68           C  
ANISOU  103  CD1 TRP A  36     6948   4263   5385   -303   -150  -1570       C  
ATOM    104  CD2 TRP A  36       3.842   3.992 -80.170  1.00 42.85           C  
ANISOU  104  CD2 TRP A  36     6868   4287   5125   -485   -251  -1738       C  
ATOM    105  NE1 TRP A  36       2.754   4.557 -82.045  1.00 45.99           N  
ANISOU  105  NE1 TRP A  36     7282   4447   5744   -364   -150  -1586       N  
ATOM    106  CE2 TRP A  36       3.839   4.872 -81.271  1.00 44.87           C  
ANISOU  106  CE2 TRP A  36     7150   4378   5521   -483   -203  -1694       C  
ATOM    107  CE3 TRP A  36       4.860   4.106 -79.218  1.00 34.94           C  
ANISOU  107  CE3 TRP A  36     5882   3386   4008   -599   -346  -1851       C  
ATOM    108  CZ2 TRP A  36       4.812   5.852 -81.444  1.00 44.62           C  
ANISOU  108  CZ2 TRP A  36     7175   4263   5515   -614   -220  -1754       C  
ATOM    109  CZ3 TRP A  36       5.823   5.078 -79.392  1.00 46.20           C  
ANISOU  109  CZ3 TRP A  36     7325   4742   5489   -710   -384  -1931       C  
ATOM    110  CH2 TRP A  36       5.794   5.938 -80.496  1.00 46.01           C  
ANISOU  110  CH2 TRP A  36     7341   4538   5602   -730   -306  -1877       C  
ATOM    111  N   ARG A  37       2.010  -1.559 -79.061  1.00 35.80           N  
ANISOU  111  N   ARG A  37     6084   3674   3846   -381   -476  -1344       N  
ATOM    112  CA  ARG A  37       1.648  -2.546 -78.049  1.00 36.24           C  
ANISOU  112  CA  ARG A  37     6336   3751   3683   -444   -551  -1281       C  
ATOM    113  C   ARG A  37       2.857  -3.133 -77.326  1.00 40.40           C  
ANISOU  113  C   ARG A  37     6923   4372   4055   -506   -790  -1241       C  
ATOM    114  O   ARG A  37       2.729  -3.650 -76.216  1.00 44.96           O  
ANISOU  114  O   ARG A  37     7723   4985   4374   -601   -868  -1187       O  
ATOM    115  CB  ARG A  37       0.830  -3.672 -78.681  1.00 28.70           C  
ANISOU  115  CB  ARG A  37     5401   2699   2806   -390   -598  -1158       C  
ATOM    116  CG  ARG A  37       1.511  -4.360 -79.850  1.00 27.02           C  
ANISOU  116  CG  ARG A  37     5018   2469   2777   -287   -758  -1072       C  
ATOM    117  CD  ARG A  37       0.602  -5.412 -80.463  1.00 26.36           C  
ANISOU  117  CD  ARG A  37     4950   2277   2790   -240   -811   -973       C  
ATOM    118  NE  ARG A  37       1.184  -6.015 -81.658  1.00 52.83           N  
ANISOU  118  NE  ARG A  37     8141   5626   6305   -133   -919   -922       N  
ATOM    119  CZ  ARG A  37       0.562  -6.908 -82.421  1.00 52.98           C  
ANISOU  119  CZ  ARG A  37     8128   5565   6437    -83   -980   -853       C  
ATOM    120  NH1 ARG A  37      -0.665  -7.301 -82.112  1.00 54.36           N  
ANISOU  120  NH1 ARG A  37     8399   5638   6617   -150   -962   -820       N  
ATOM    121  NH2 ARG A  37       1.164  -7.405 -83.493  1.00 52.84           N  
ANISOU  121  NH2 ARG A  37     7988   5565   6523      7  -1046   -843       N  
ATOM    122  N   ASP A  38       4.027  -3.050 -77.951  1.00 38.96           N  
ANISOU  122  N   ASP A  38     6557   4233   4013   -467   -905  -1268       N  
ATOM    123  CA  ASP A  38       5.238  -3.617 -77.370  1.00 43.45           C  
ANISOU  123  CA  ASP A  38     7131   4883   4497   -492  -1176  -1253       C  
ATOM    124  C   ASP A  38       6.160  -2.533 -76.823  1.00 45.22           C  
ANISOU  124  C   ASP A  38     7288   5225   4668   -603  -1173  -1417       C  
ATOM    125  O   ASP A  38       7.249  -2.825 -76.328  1.00 47.29           O  
ANISOU  125  O   ASP A  38     7511   5580   4876   -637  -1415  -1437       O  
ATOM    126  CB  ASP A  38       5.985  -4.459 -78.405  1.00 53.11           C  
ANISOU  126  CB  ASP A  38     8182   6069   5926   -367  -1337  -1211       C  
ATOM    127  CG  ASP A  38       6.545  -3.625 -79.538  1.00 62.13           C  
ANISOU  127  CG  ASP A  38     9113   7245   7251   -379  -1175  -1331       C  
ATOM    128  OD1 ASP A  38       5.803  -3.366 -80.509  1.00 63.30           O  
ANISOU  128  OD1 ASP A  38     9226   7325   7499   -340   -981  -1304       O  
ATOM    129  OD2 ASP A  38       7.728  -3.229 -79.456  1.00 66.96           O  
ANISOU  129  OD2 ASP A  38     9609   7947   7887   -449  -1257  -1448       O  
ATOM    130  N   TYR A  39       5.719  -1.283 -76.913  1.00 54.07           N  
ANISOU  130  N   TYR A  39     8389   6325   5832   -645   -934  -1541       N  
ATOM    131  CA  TYR A  39       6.519  -0.161 -76.438  1.00 41.96           C  
ANISOU  131  CA  TYR A  39     6806   4858   4280   -748   -934  -1722       C  
ATOM    132  C   TYR A  39       6.551  -0.111 -74.917  1.00 60.41           C  
ANISOU  132  C   TYR A  39     9342   7285   6327   -840  -1034  -1761       C  
ATOM    133  O   TYR A  39       5.565   0.250 -74.274  1.00 59.58           O  
ANISOU  133  O   TYR A  39     9422   7139   6076   -853   -873  -1778       O  
ATOM    134  CB  TYR A  39       5.985   1.160 -76.994  1.00 44.02           C  
ANISOU  134  CB  TYR A  39     7037   4992   4697   -720   -710  -1816       C  
ATOM    135  CG  TYR A  39       6.778   2.372 -76.554  1.00 50.84           C  
ANISOU  135  CG  TYR A  39     7897   5850   5569   -814   -744  -1995       C  
ATOM    136  CD1 TYR A  39       8.078   2.577 -77.001  1.00 44.31           C  
ANISOU  136  CD1 TYR A  39     6904   5068   4864   -887   -873  -2088       C  
ATOM    137  CD2 TYR A  39       6.225   3.315 -75.698  1.00 55.77           C  
ANISOU  137  CD2 TYR A  39     8699   6407   6086   -841   -646  -2091       C  
ATOM    138  CE1 TYR A  39       8.807   3.683 -76.603  1.00 46.82           C  
ANISOU  138  CE1 TYR A  39     7254   5335   5201   -992   -943  -2239       C  
ATOM    139  CE2 TYR A  39       6.947   4.425 -75.295  1.00 61.94           C  
ANISOU  139  CE2 TYR A  39     9516   7144   6873   -942   -693  -2252       C  
ATOM    140  CZ  TYR A  39       8.237   4.604 -75.751  1.00 63.25           C  
ANISOU  140  CZ  TYR A  39     9534   7333   7165  -1026   -852  -2312       C  
ATOM    141  OH  TYR A  39       8.961   5.705 -75.356  1.00 68.08           O  
ANISOU  141  OH  TYR A  39    10203   7875   7789  -1163   -914  -2466       O  
ATOM    142  N   LEU A  40       7.691  -0.483 -74.347  1.00 70.98           N  
ANISOU  142  N   LEU A  40    10646   8755   7570   -911  -1303  -1781       N  
ATOM    143  CA  LEU A  40       7.891  -0.382 -72.909  1.00 78.35           C  
ANISOU  143  CA  LEU A  40    11774   9797   8200  -1016  -1440  -1819       C  
ATOM    144  C   LEU A  40       8.878   0.735 -72.597  1.00 80.26           C  
ANISOU  144  C   LEU A  40    11903  10114   8478  -1124  -1503  -2056       C  
ATOM    145  O   LEU A  40       9.966   0.797 -73.171  1.00 84.21           O  
ANISOU  145  O   LEU A  40    12155  10677   9166  -1160  -1631  -2137       O  
ATOM    146  CB  LEU A  40       8.375  -1.717 -72.329  1.00 83.39           C  
ANISOU  146  CB  LEU A  40    12502  10511   8673  -1003  -1781  -1627       C  
ATOM    147  CG  LEU A  40       9.628  -2.387 -72.907  1.00 90.81           C  
ANISOU  147  CG  LEU A  40    13188  11498   9818   -937  -2083  -1591       C  
ATOM    148  CD1 LEU A  40      10.872  -2.039 -72.098  1.00 98.55           C  
ANISOU  148  CD1 LEU A  40    14079  12656  10708  -1048  -2361  -1711       C  
ATOM    149  CD2 LEU A  40       9.445  -3.897 -72.987  1.00 92.42           C  
ANISOU  149  CD2 LEU A  40    13485  11604  10027   -787  -2315  -1332       C  
ATOM    150  N   TYR A  41       8.483   1.632 -71.700  1.00147.01           N  
ANISOU  150  N   TYR A  41    16103  22836  16917  -9238   2928  -8330       N  
ATOM    151  CA  TYR A  41       9.363   2.708 -71.269  1.00138.04           C  
ANISOU  151  CA  TYR A  41    14800  21736  15911  -8649   2890  -7811       C  
ATOM    152  C   TYR A  41       9.568   2.625 -69.764  1.00131.04           C  
ANISOU  152  C   TYR A  41    13954  20005  15832  -8106   3393  -7557       C  
ATOM    153  O   TYR A  41       8.831   3.249 -68.997  1.00128.38           O  
ANISOU  153  O   TYR A  41    13120  19638  16018  -7941   3178  -7145       O  
ATOM    154  CB  TYR A  41       8.798   4.075 -71.661  1.00137.68           C  
ANISOU  154  CB  TYR A  41    14018  22532  15763  -8557   2078  -7144       C  
ATOM    155  CG  TYR A  41       9.773   5.212 -71.449  1.00130.56           C  
ANISOU  155  CG  TYR A  41    13078  21679  14849  -7779   2027  -6448       C  
ATOM    156  CD1 TYR A  41      10.774   5.476 -72.378  1.00130.95           C  
ANISOU  156  CD1 TYR A  41    13436  22083  14237  -7620   1980  -6383       C  
ATOM    157  CD2 TYR A  41       9.696   6.019 -70.321  1.00124.07           C  
ANISOU  157  CD2 TYR A  41    11960  20514  14667  -7235   2060  -5861       C  
ATOM    158  CE1 TYR A  41      11.669   6.512 -72.188  1.00124.89           C  
ANISOU  158  CE1 TYR A  41    12600  21348  13505  -6948   1917  -5721       C  
ATOM    159  CE2 TYR A  41      10.587   7.056 -70.124  1.00118.30           C  
ANISOU  159  CE2 TYR A  41    11241  19798  13908  -6616   1991  -5252       C  
ATOM    160  CZ  TYR A  41      11.570   7.297 -71.061  1.00118.63           C  
ANISOU  160  CZ  TYR A  41    11511  20218  13346  -6478   1894  -5170       C  
ATOM    161  OH  TYR A  41      12.459   8.329 -70.869  1.00113.30           O  
ANISOU  161  OH  TYR A  41    10812  19549  12689  -5896   1808  -4536       O  
ATOM    162  N   PRO A  42      10.574   1.845 -69.340  1.00138.73           N  
ANISOU  162  N   PRO A  42    15538  20271  16901  -7831   4105  -7761       N  
ATOM    163  CA  PRO A  42      10.858   1.596 -67.923  1.00130.03           C  
ANISOU  163  CA  PRO A  42    14572  18351  16481  -7386   4610  -7538       C  
ATOM    164  C   PRO A  42      11.277   2.855 -67.167  1.00120.07           C  
ANISOU  164  C   PRO A  42    13079  17111  15432  -6754   4342  -6733       C  
ATOM    165  O   PRO A  42      12.125   3.614 -67.637  1.00115.46           O  
ANISOU  165  O   PRO A  42    12513  16863  14493  -6434   4106  -6338       O  
ATOM    166  CB  PRO A  42      12.005   0.580 -67.969  1.00128.17           C  
ANISOU  166  CB  PRO A  42    14991  17537  16172  -7239   5357  -7811       C  
ATOM    167  CG  PRO A  42      12.650   0.794 -69.294  1.00130.92           C  
ANISOU  167  CG  PRO A  42    15529  18420  15795  -7314   5205  -7894       C  
ATOM    168  CD  PRO A  42      11.532   1.158 -70.224  1.00138.62           C  
ANISOU  168  CD  PRO A  42    16136  20196  16339  -7921   4513  -8155       C  
ATOM    169  N   LYS A  43      10.673   3.062 -66.002  1.00116.79           N  
ANISOU  169  N   LYS A  43    12492  16298  15583  -6607   4418  -6506       N  
ATOM    170  CA  LYS A  43      10.995   4.199 -65.149  1.00110.57           C  
ANISOU  170  CA  LYS A  43    11625  15396  14990  -6089   4250  -5814       C  
ATOM    171  C   LYS A  43      12.411   4.074 -64.592  1.00104.84           C  
ANISOU  171  C   LYS A  43    11382  14210  14241  -5662   4569  -5516       C  
ATOM    172  O   LYS A  43      12.849   2.979 -64.239  1.00104.95           O  
ANISOU  172  O   LYS A  43    11759  13696  14421  -5683   5109  -5776       O  
ATOM    173  CB  LYS A  43       9.979   4.309 -64.008  1.00111.11           C  
ANISOU  173  CB  LYS A  43    11530  15043  15645  -6077   4402  -5710       C  
ATOM    174  CG  LYS A  43      10.228   5.449 -63.033  1.00105.06           C  
ANISOU  174  CG  LYS A  43    10833  14040  15046  -5614   4330  -5067       C  
ATOM    175  CD  LYS A  43       9.162   5.476 -61.949  1.00103.64           C  
ANISOU  175  CD  LYS A  43    10573  13381  15423  -5615   4616  -5013       C  
ATOM    176  CE  LYS A  43       9.390   6.615 -60.970  1.00 99.61           C  
ANISOU  176  CE  LYS A  43    10286  12559  15002  -5213   4625  -4433       C  
ATOM    177  NZ  LYS A  43       8.329   6.666 -59.925  1.00 98.62           N  
ANISOU  177  NZ  LYS A  43    10173  11914  15383  -5155   4995  -4358       N  
ATOM    178  N   GLN A  44      13.123   5.196 -64.528  1.00105.18           N  
ANISOU  178  N   GLN A  44    11393  14456  14116  -5294   4234  -4918       N  
ATOM    179  CA  GLN A  44      14.471   5.220 -63.970  1.00104.97           C  
ANISOU  179  CA  GLN A  44    11728  14057  14097  -4927   4410  -4484       C  
ATOM    180  C   GLN A  44      14.470   4.785 -62.511  1.00103.15           C  
ANISOU  180  C   GLN A  44    11811  13088  14294  -4835   4779  -4366       C  
ATOM    181  O   GLN A  44      15.294   3.971 -62.092  1.00103.86           O  
ANISOU  181  O   GLN A  44    12207  12738  14515  -4727   5176  -4294       O  
ATOM    182  CB  GLN A  44      15.081   6.618 -64.088  1.00105.18           C  
ANISOU  182  CB  GLN A  44    11628  14429  13905  -4628   3913  -3844       C  
ATOM    183  CG  GLN A  44      15.354   7.075 -65.508  1.00110.94           C  
ANISOU  183  CG  GLN A  44    12097  15874  14181  -4634   3579  -3829       C  
ATOM    184  CD  GLN A  44      15.989   8.452 -65.556  1.00111.52           C  
ANISOU  184  CD  GLN A  44    12041  16221  14112  -4319   3137  -3158       C  
ATOM    185  OE1 GLN A  44      15.946   9.201 -64.579  1.00109.28           O  
ANISOU  185  OE1 GLN A  44    11834  15647  14041  -4180   3016  -2776       O  
ATOM    186  NE2 GLN A  44      16.588   8.790 -66.692  1.00114.11           N  
ANISOU  186  NE2 GLN A  44    12226  17073  14060  -4227   2933  -3020       N  
ATOM    187  N   TYR A  45      13.534   5.332 -61.744  1.00 98.37           N  
ANISOU  187  N   TYR A  45    11125  12336  13915  -4866   4690  -4297       N  
ATOM    188  CA  TYR A  45      13.474   5.072 -60.314  1.00 96.24           C  
ANISOU  188  CA  TYR A  45    11220  11379  13968  -4784   5023  -4147       C  
ATOM    189  C   TYR A  45      12.468   3.976 -59.978  1.00 93.41           C  
ANISOU  189  C   TYR A  45    10843  10657  13990  -5031   5497  -4679       C  
ATOM    190  O   TYR A  45      11.477   4.218 -59.289  1.00 93.72           O  
ANISOU  190  O   TYR A  45    10852  10477  14281  -5021   5569  -4681       O  
ATOM    191  CB  TYR A  45      13.131   6.358 -59.560  1.00 94.73           C  
ANISOU  191  CB  TYR A  45    11098  11109  13786  -4644   4776  -3720       C  
ATOM    192  CG  TYR A  45      14.101   7.488 -59.823  1.00 91.51           C  
ANISOU  192  CG  TYR A  45    10731  11003  13037  -4442   4310  -3186       C  
ATOM    193  CD1 TYR A  45      15.434   7.386 -59.445  1.00 83.55           C  
ANISOU  193  CD1 TYR A  45    10051   9805  11890  -4314   4255  -2784       C  
ATOM    194  CD2 TYR A  45      13.685   8.658 -60.446  1.00 86.92           C  
ANISOU  194  CD2 TYR A  45     9810  10891  12324  -4386   3929  -3015       C  
ATOM    195  CE1 TYR A  45      16.326   8.414 -59.684  1.00 81.63           C  
ANISOU  195  CE1 TYR A  45     9811   9825  11381  -4170   3811  -2265       C  
ATOM    196  CE2 TYR A  45      14.570   9.693 -60.689  1.00 83.09           C  
ANISOU  196  CE2 TYR A  45     9360  10647  11563  -4209   3534  -2524       C  
ATOM    197  CZ  TYR A  45      15.889   9.566 -60.305  1.00 83.30           C  
ANISOU  197  CZ  TYR A  45     9731  10470  11451  -4119   3465  -2170       C  
ATOM    198  OH  TYR A  45      16.774  10.592 -60.544  1.00 85.12           O  
ANISOU  198  OH  TYR A  45     9963  10928  11451  -3982   3052  -1652       O  
ATOM    199  N   GLU A  46      12.730   2.770 -60.473  1.00 96.13           N  
ANISOU  199  N   GLU A  46    11245  10909  14373  -5186   5842  -5093       N  
ATOM    200  CA  GLU A  46      11.921   1.608 -60.128  1.00 99.35           C  
ANISOU  200  CA  GLU A  46    11741  10943  15066  -5256   6250  -5532       C  
ATOM    201  C   GLU A  46      12.492   0.906 -58.904  1.00 98.02           C  
ANISOU  201  C   GLU A  46    12020  10121  15104  -4933   6673  -5278       C  
ATOM    202  O   GLU A  46      11.749   0.434 -58.044  1.00 98.94           O  
ANISOU  202  O   GLU A  46    12231   9906  15457  -4804   6925  -5336       O  
ATOM    203  CB  GLU A  46      11.839   0.626 -61.298  1.00104.13           C  
ANISOU  203  CB  GLU A  46    12253  11750  15560  -5607   6451  -6144       C  
ATOM    204  CG  GLU A  46      10.856   1.019 -62.387  1.00107.54           C  
ANISOU  204  CG  GLU A  46    12238  12837  15785  -6000   6005  -6474       C  
ATOM    205  CD  GLU A  46      10.627  -0.097 -63.391  1.00113.63           C  
ANISOU  205  CD  GLU A  46    13065  13735  16375  -6407   6224  -7118       C  
ATOM    206  OE1 GLU A  46      11.274  -1.158 -63.258  1.00114.99           O  
ANISOU  206  OE1 GLU A  46    13610  13449  16633  -6344   6824  -7300       O  
ATOM    207  OE2 GLU A  46       9.800   0.084 -64.309  1.00117.73           O  
ANISOU  207  OE2 GLU A  46    13259  14818  16656  -6795   5807  -7376       O  
ATOM    208  N   TRP A  47      13.818   0.845 -58.830  1.00 96.36           N  
ANISOU  208  N   TRP A  47    12027   9776  14810  -4792   6744  -4913       N  
ATOM    209  CA  TRP A  47      14.491   0.151 -57.739  1.00 95.92           C  
ANISOU  209  CA  TRP A  47    12337   9171  14936  -4496   7066  -4560       C  
ATOM    210  C   TRP A  47      14.254   0.847 -56.402  1.00 96.23           C  
ANISOU  210  C   TRP A  47    12616   9015  14934  -4306   6853  -4114       C  
ATOM    211  O   TRP A  47      14.330   0.217 -55.347  1.00 99.52           O  
ANISOU  211  O   TRP A  47    13304   9031  15478  -4106   7115  -3931       O  
ATOM    212  CB  TRP A  47      15.992   0.037 -58.016  1.00 95.48           C  
ANISOU  212  CB  TRP A  47    12357   9091  14830  -4365   7113  -4091       C  
ATOM    213  CG  TRP A  47      16.727   1.344 -57.955  1.00 92.02           C  
ANISOU  213  CG  TRP A  47    11867   8976  14120  -4326   6586  -3469       C  
ATOM    214  CD1 TRP A  47      16.934   2.218 -58.983  1.00 91.04           C  
ANISOU  214  CD1 TRP A  47    11482   9421  13689  -4366   6185  -3446       C  
ATOM    215  CD2 TRP A  47      17.361   1.920 -56.806  1.00 89.73           C  
ANISOU  215  CD2 TRP A  47    11847   8497  13750  -4173   6287  -2759       C  
ATOM    216  NE1 TRP A  47      17.654   3.303 -58.544  1.00 88.08           N  
ANISOU  216  NE1 TRP A  47    11184   9180  13104  -4218   5675  -2771       N  
ATOM    217  CE2 TRP A  47      17.930   3.144 -57.212  1.00 87.44           C  
ANISOU  217  CE2 TRP A  47    11443   8617  13163  -4199   5763  -2361       C  
ATOM    218  CE3 TRP A  47      17.502   1.520 -55.473  1.00 89.98           C  
ANISOU  218  CE3 TRP A  47    12223   8103  13860  -4013   6349  -2416       C  
ATOM    219  CZ2 TRP A  47      18.626   3.972 -56.333  1.00 85.63           C  
ANISOU  219  CZ2 TRP A  47    11476   8312  12748  -4173   5332  -1666       C  
ATOM    220  CZ3 TRP A  47      18.195   2.343 -54.603  1.00 88.36           C  
ANISOU  220  CZ3 TRP A  47    12277   7881  13415  -4006   5893  -1722       C  
ATOM    221  CH2 TRP A  47      18.748   3.555 -55.036  1.00 86.32           C  
ANISOU  221  CH2 TRP A  47    11943   7961  12894  -4135   5408  -1368       C  
ATOM    222  N   VAL A  48      13.968   2.145 -56.448  1.00 63.22           N  
ANISOU  222  N   VAL A  48     8702   7345   7974    426    474  -1559       N  
ATOM    223  CA  VAL A  48      13.649   2.884 -55.232  1.00 65.47           C  
ANISOU  223  CA  VAL A  48     8945   7638   8292    384    424  -1554       C  
ATOM    224  C   VAL A  48      12.231   2.554 -54.779  1.00 63.47           C  
ANISOU  224  C   VAL A  48     8811   7380   7925    382    354  -1460       C  
ATOM    225  O   VAL A  48      11.915   2.644 -53.592  1.00 64.89           O  
ANISOU  225  O   VAL A  48     8967   7573   8115    351    303  -1453       O  
ATOM    226  CB  VAL A  48      13.791   4.414 -55.421  1.00 66.36           C  
ANISOU  226  CB  VAL A  48     8992   7746   8474    338    485  -1578       C  
ATOM    227  CG1 VAL A  48      15.149   4.755 -56.011  1.00 72.61           C  
ANISOU  227  CG1 VAL A  48     9646   8530   9411    303    609  -1692       C  
ATOM    228  CG2 VAL A  48      12.674   4.966 -56.293  1.00 62.18           C  
ANISOU  228  CG2 VAL A  48     8566   7207   7852    345    495  -1507       C  
ATOM    229  N   LEU A  49      11.383   2.164 -55.726  1.00 51.31           N  
ANISOU  229  N   LEU A  49     7381   5828   6286    414    349  -1399       N  
ATOM    230  CA  LEU A  49      10.012   1.797 -55.407  1.00 45.40           C  
ANISOU  230  CA  LEU A  49     6694   5088   5466    382    299  -1297       C  
ATOM    231  C   LEU A  49      10.012   0.446 -54.713  1.00 49.24           C  
ANISOU  231  C   LEU A  49     7185   5567   5958    336    314  -1295       C  
ATOM    232  O   LEU A  49       9.569   0.329 -53.568  1.00 54.70           O  
ANISOU  232  O   LEU A  49     7848   6272   6664    290    289  -1299       O  
ATOM    233  CB  LEU A  49       9.147   1.758 -56.669  1.00 29.03           C  
ANISOU  233  CB  LEU A  49     4652   3045   3334    442    249  -1252       C  
ATOM    234  CG  LEU A  49       7.637   1.638 -56.445  1.00 36.41           C  
ANISOU  234  CG  LEU A  49     5626   3991   4216    429    180  -1171       C  
ATOM    235  CD1 LEU A  49       7.114   2.846 -55.687  1.00 36.86           C  
ANISOU  235  CD1 LEU A  49     5653   4056   4295    394    158  -1168       C  
ATOM    236  CD2 LEU A  49       6.902   1.475 -57.766  1.00 39.53           C  
ANISOU  236  CD2 LEU A  49     5665   4576   4777    438    108  -1362       C  
ATOM    237  N   ILE A  50      10.529  -0.560 -55.419  1.00 45.83           N  
ANISOU  237  N   ILE A  50     6764   5123   5525    362    344  -1313       N  
ATOM    238  CA  ILE A  50      10.670  -1.915 -54.894  1.00 45.02           C  
ANISOU  238  CA  ILE A  50     6632   5023   5452    342    339  -1350       C  
ATOM    239  C   ILE A  50      11.200  -1.909 -53.470  1.00 50.29           C  
ANISOU  239  C   ILE A  50     7236   5706   6167    357    274  -1411       C  
ATOM    240  O   ILE A  50      10.544  -2.412 -52.555  1.00 53.56           O  
ANISOU  240  O   ILE A  50     7638   6139   6573    336    227  -1399       O  
ATOM    241  CB  ILE A  50      11.622  -2.764 -55.755  1.00 35.53           C  
ANISOU  241  CB  ILE A  50     5433   3805   4264    395    367  -1395       C  
ATOM    242  CG1 ILE A  50      11.185  -2.758 -57.219  1.00 34.96           C  
ANISOU  242  CG1 ILE A  50     5426   3725   4134    402    417  -1334       C  
ATOM    243  CG2 ILE A  50      11.693  -4.186 -55.221  1.00 29.96           C  
ANISOU  243  CG2 ILE A  50     4698   3101   3586    399    330  -1438       C  
ATOM    244  CD1 ILE A  50      12.140  -3.494 -58.131  1.00 33.75           C  
ANISOU  244  CD1 ILE A  50     5277   3561   3985    465    446  -1382       C  
ATOM    245  N   ALA A  51      12.383  -1.322 -53.302  1.00 45.66           N  
ANISOU  245  N   ALA A  51     6574   5131   5645    400    256  -1474       N  
ATOM    246  CA  ALA A  51      13.017  -1.173 -51.998  1.00 41.40           C  
ANISOU  246  CA  ALA A  51     5937   4624   5168    424    172  -1534       C  
ATOM    247  C   ALA A  51      12.014  -0.682 -50.968  1.00 44.08           C  
ANISOU  247  C   ALA A  51     6300   4980   5469    387    133  -1489       C  
ATOM    248  O   ALA A  51      11.787  -1.343 -49.950  1.00 44.46           O  
ANISOU  248  O   ALA A  51     6348   5044   5500    407     63  -1492       O  
ATOM    249  CB  ALA A  51      14.195  -0.218 -52.086  1.00 34.34           C  
ANISOU  249  CB  ALA A  51     4929   3744   4374    443    183  -1617       C  
ATOM    250  N   ALA A  52      11.395   0.459 -51.259  1.00 43.93           N  
ANISOU  250  N   ALA A  52     6308   4953   5429    344    175  -1449       N  
ATOM    251  CA  ALA A  52      10.393   1.034 -50.373  1.00 44.74           C  
ANISOU  251  CA  ALA A  52     6427   5072   5498    304    147  -1409       C  
ATOM    252  C   ALA A  52       9.321  -0.005 -50.073  1.00 43.08           C  
ANISOU  252  C   ALA A  52     6271   4863   5232    275    145  -1366       C  
ATOM    253  O   ALA A  52       9.049  -0.315 -48.909  1.00 42.94           O  
ANISOU  253  O   ALA A  52     6241   4869   5204    285     86  -1373       O  
ATOM    254  CB  ALA A  52       9.783   2.280 -50.992  1.00 39.48           C  
ANISOU  254  CB  ALA A  52     5798   4391   4813    272    189  -1367       C  
ATOM    255  N   TYR A  53       8.755  -0.575 -51.135  1.00 38.13           N  
ANISOU  255  N   TYR A  53     5695   4215   4578    245    206  -1333       N  
ATOM    256  CA  TYR A  53       7.719  -1.592 -51.004  1.00 36.36           C  
ANISOU  256  CA  TYR A  53     5471   4007   4339    215    203  -1313       C  
ATOM    257  C   TYR A  53       8.181  -2.770 -50.156  1.00 36.35           C  
ANISOU  257  C   TYR A  53     5461   4008   4340    273    133  -1344       C  
ATOM    258  O   TYR A  53       7.390  -3.343 -49.409  1.00 35.95           O  
ANISOU  258  O   TYR A  53     5423   3966   4268    270    100  -1331       O  
ATOM    259  CB  TYR A  53       7.273  -2.086 -52.381  1.00 32.06           C  
ANISOU  259  CB  TYR A  53     4923   3462   3797    194    252  -1287       C  
ATOM    260  CG  TYR A  53       5.976  -1.475 -52.867  1.00 33.92           C  
ANISOU  260  CG  TYR A  53     5130   3725   4032    138    275  -1250       C  
ATOM    261  CD1 TYR A  53       4.748  -2.018 -52.501  1.00 33.66           C  
ANISOU  261  CD1 TYR A  53     5066   3719   4006    123    242  -1253       C  
ATOM    262  CD2 TYR A  53       5.978  -0.361 -53.695  1.00 33.85           C  
ANISOU  262  CD2 TYR A  53     5136   3708   4016    115    322  -1219       C  
ATOM    263  CE1 TYR A  53       3.560  -1.465 -52.946  1.00 30.92           C  
ANISOU  263  CE1 TYR A  53     4683   3399   3668     93    243  -1241       C  
ATOM    264  CE2 TYR A  53       4.797   0.198 -54.145  1.00 31.57           C  
ANISOU  264  CE2 TYR A  53     4783   3461   3751     74    326  -1222       C  
ATOM    265  CZ  TYR A  53       3.591  -0.357 -53.768  1.00 31.31           C  
ANISOU  265  CZ  TYR A  53     4712   3459   3726     74    274  -1233       C  
ATOM    266  OH  TYR A  53       2.414   0.197 -54.214  1.00 33.56           O  
ANISOU  266  OH  TYR A  53     4962   3770   4020     65    254  -1236       O  
ATOM    267  N   VAL A  54       9.458  -3.124 -50.263  1.00 27.60           N  
ANISOU  267  N   VAL A  54     4337   2891   3260    335    104  -1386       N  
ATOM    268  CA  VAL A  54       9.986  -4.211 -49.451  1.00 34.38           C  
ANISOU  268  CA  VAL A  54     5198   3748   4117    409     19  -1414       C  
ATOM    269  C   VAL A  54      10.117  -3.741 -48.010  1.00 38.74           C  
ANISOU  269  C   VAL A  54     5744   4320   4656    444    -60  -1429       C  
ATOM    270  O   VAL A  54       9.712  -4.445 -47.085  1.00 40.56           O  
ANISOU  270  O   VAL A  54     6025   4544   4841    478   -116  -1415       O  
ATOM    271  CB  VAL A  54      11.346  -4.718 -49.965  1.00 37.86           C  
ANISOU  271  CB  VAL A  54     5603   4178   4603    475     -3  -1471       C  
ATOM    272  CG1 VAL A  54      11.903  -5.775 -49.026  1.00 35.50           C  
ANISOU  272  CG1 VAL A  54     5317   3874   4299    567   -114  -1503       C  
ATOM    273  CG2 VAL A  54      11.207  -5.282 -51.371  1.00 40.86           C  
ANISOU  273  CG2 VAL A  54     6003   4537   4985    449     73  -1457       C  
ATOM    274  N   ALA A  55      10.663  -2.540 -47.827  1.00 40.25           N  
ANISOU  274  N   ALA A  55     5880   4532   4883    441    -63  -1459       N  
ATOM    275  CA  ALA A  55      10.834  -1.975 -46.492  1.00 26.19           C  
ANISOU  275  CA  ALA A  55     4079   2777   3096    479   -144  -1484       C  
ATOM    276  C   ALA A  55       9.496  -1.994 -45.768  1.00 37.27           C  
ANISOU  276  C   ALA A  55     5549   4182   4430    436   -133  -1427       C  
ATOM    277  O   ALA A  55       9.295  -2.768 -44.824  1.00 26.09           O  
ANISOU  277  O   ALA A  55     4193   2759   2962    486   -194  -1421       O  
ATOM    278  CB  ALA A  55      11.387  -0.563 -46.573  1.00 26.23           C  
ANISOU  278  CB  ALA A  55     4000   2803   3164    463   -134  -1523       C  
ATOM    279  N   VAL A  56       8.576  -1.169 -46.261  1.00 33.70           N  
ANISOU  279  N   VAL A  56     5094   3735   3976    348    -55  -1388       N  
ATOM    280  CA  VAL A  56       7.196  -1.136 -45.794  1.00 32.44           C  
ANISOU  280  CA  VAL A  56     4973   3582   3772    293    -26  -1347       C  
ATOM    281  C   VAL A  56       6.632  -2.534 -45.558  1.00 34.23           C  
ANISOU  281  C   VAL A  56     5255   3789   3961    313    -37  -1331       C  
ATOM    282  O   VAL A  56       5.910  -2.752 -44.589  1.00 32.67           O  
ANISOU  282  O   VAL A  56     5102   3592   3718    315    -55  -1318       O  
ATOM    283  CB  VAL A  56       6.295  -0.381 -46.798  1.00 32.90           C  
ANISOU  283  CB  VAL A  56     5017   3638   3843    205     59  -1313       C  
ATOM    284  CG1 VAL A  56       4.823  -0.648 -46.526  1.00 34.13           C  
ANISOU  284  CG1 VAL A  56     5183   3806   3979    152     88  -1293       C  
ATOM    285  CG2 VAL A  56       6.589   1.108 -46.746  1.00 33.33           C  
ANISOU  285  CG2 VAL A  56     5047   3701   3917    192     59  -1314       C  
ATOM    286  N   PHE A  57       6.989  -3.484 -46.420  1.00 32.85           N  
ANISOU  286  N   PHE A  57     5087   3591   3804    333    -28  -1332       N  
ATOM    287  CA  PHE A  57       6.524  -4.855 -46.254  1.00 22.49           C  
ANISOU  287  CA  PHE A  57     3838   2247   2462    362    -45  -1315       C  
ATOM    288  C   PHE A  57       7.009  -5.403 -44.917  1.00 31.28           C  
ANISOU  288  C   PHE A  57     5028   3339   3516    450   -131  -1320       C  
ATOM    289  O   PHE A  57       6.205  -5.614 -44.002  1.00 39.14           O  
ANISOU  289  O   PHE A  57     6094   4321   4457    449   -135  -1296       O  
ATOM    290  CB  PHE A  57       7.001  -5.733 -47.414  1.00 22.60           C  
ANISOU  290  CB  PHE A  57     3842   2237   2507    380    -30  -1323       C  
ATOM    291  CG  PHE A  57       6.451  -7.130 -47.396  1.00 31.08           C  
ANISOU  291  CG  PHE A  57     4983   3268   3559    403    -40  -1304       C  
ATOM    292  CD1 PHE A  57       5.146  -7.381 -47.781  1.00 31.41           C  
ANISOU  292  CD1 PHE A  57     5023   3302   3608    346      9  -1284       C  
ATOM    293  CD2 PHE A  57       7.249  -8.198 -47.022  1.00 32.13           C  
ANISOU  293  CD2 PHE A  57     5178   3361   3669    489   -105  -1311       C  
ATOM    294  CE1 PHE A  57       4.642  -8.669 -47.777  1.00 31.53           C  
ANISOU  294  CE1 PHE A  57     5102   3264   3613    365      5  -1272       C  
ATOM    295  CE2 PHE A  57       6.751  -9.488 -47.017  1.00 24.09           C  
ANISOU  295  CE2 PHE A  57     4237   2286   2630    510   -109  -1290       C  
ATOM    296  CZ  PHE A  57       5.446  -9.723 -47.394  1.00 23.68           C  
ANISOU  296  CZ  PHE A  57     4186   2221   2590    443    -47  -1269       C  
ATOM    297  N   VAL A  58       8.323  -5.579 -44.782  1.00 28.46           N  
ANISOU  297  N   VAL A  58     4663   2980   3172    533   -204  -1358       N  
ATOM    298  CA  VAL A  58       8.861  -6.270 -43.613  1.00 32.29           C  
ANISOU  298  CA  VAL A  58     5235   3438   3595    642   -307  -1366       C  
ATOM    299  C   VAL A  58       8.506  -5.513 -42.335  1.00 36.66           C  
ANISOU  299  C   VAL A  58     5826   4013   4093    653   -338  -1361       C  
ATOM    300  O   VAL A  58       8.015  -6.108 -41.372  1.00 44.93           O  
ANISOU  300  O   VAL A  58     6996   5024   5052    693   -364  -1329       O  
ATOM    301  CB  VAL A  58      10.398  -6.477 -43.711  1.00 41.91           C  
ANISOU  301  CB  VAL A  58     6407   4662   4855    741   -399  -1430       C  
ATOM    302  CG1 VAL A  58      10.721  -7.563 -44.726  1.00 39.34           C  
ANISOU  302  CG1 VAL A  58     6082   4303   4560    754   -382  -1432       C  
ATOM    303  CG2 VAL A  58      11.118  -5.187 -44.071  1.00 43.19           C  
ANISOU  303  CG2 VAL A  58     6438   4875   5097    716   -390  -1484       C  
ATOM    304  N   VAL A  59       8.704  -4.198 -42.356  1.00 32.28           N  
ANISOU  304  N   VAL A  59     5175   3508   3584    614   -327  -1390       N  
ATOM    305  CA  VAL A  59       8.384  -3.347 -41.218  1.00 35.69           C  
ANISOU  305  CA  VAL A  59     5622   3965   3972    620   -355  -1394       C  
ATOM    306  C   VAL A  59       6.925  -3.508 -40.793  1.00 36.38           C  
ANISOU  306  C   VAL A  59     5787   4039   3997    552   -285  -1342       C  
ATOM    307  O   VAL A  59       6.617  -3.497 -39.599  1.00 41.33           O  
ANISOU  307  O   VAL A  59     6499   4661   4544    591   -318  -1333       O  
ATOM    308  CB  VAL A  59       8.669  -1.860 -41.534  1.00 32.84           C  
ANISOU  308  CB  VAL A  59     5139   3653   3687    569   -335  -1428       C  
ATOM    309  CG1 VAL A  59       8.292  -0.975 -40.353  1.00 28.59           C  
ANISOU  309  CG1 VAL A  59     4612   3143   3107    575   -366  -1436       C  
ATOM    310  CG2 VAL A  59      10.134  -1.665 -41.898  1.00 30.37           C  
ANISOU  310  CG2 VAL A  59     4735   3353   3451    637   -401  -1497       C  
ATOM    311  N   ALA A  60       6.030  -3.682 -41.762  1.00 31.61           N  
ANISOU  311  N   ALA A  60     5152   3429   3432    460   -190  -1315       N  
ATOM    312  CA  ALA A  60       4.617  -3.816 -41.429  1.00 31.69           C  
ANISOU  312  CA  ALA A  60     5204   3429   3408    398   -126  -1286       C  
ATOM    313  C   ALA A  60       4.351  -5.166 -40.790  1.00 37.32           C  
ANISOU  313  C   ALA A  60     6064   4075   4040    455   -142  -1252       C  
ATOM    314  O   ALA A  60       3.507  -5.283 -39.904  1.00 45.19           O  
ANISOU  314  O   ALA A  60     7147   5051   4971    445   -116  -1232       O  
ATOM    315  CB  ALA A  60       3.750  -3.637 -42.655  1.00 33.87           C  
ANISOU  315  CB  ALA A  60     5393   3719   3757    304    -45  -1282       C  
ATOM    316  N   LEU A  61       5.076  -6.186 -41.238  1.00 35.04           N  
ANISOU  316  N   LEU A  61     5816   3745   3754    515   -179  -1247       N  
ATOM    317  CA  LEU A  61       4.876  -7.526 -40.704  1.00 38.69           C  
ANISOU  317  CA  LEU A  61     6441   4123   4135    574   -191  -1207       C  
ATOM    318  C   LEU A  61       5.375  -7.597 -39.268  1.00 42.02           C  
ANISOU  318  C   LEU A  61     7039   4504   4422    702   -291  -1193       C  
ATOM    319  O   LEU A  61       4.579  -7.531 -38.323  1.00 45.85           O  
ANISOU  319  O   LEU A  61     7646   4958   4816    697   -259  -1161       O  
ATOM    320  CB  LEU A  61       5.578  -8.569 -41.574  1.00 38.14           C  
ANISOU  320  CB  LEU A  61     6382   4012   4098    622   -223  -1209       C  
ATOM    321  CG  LEU A  61       4.939  -8.801 -42.945  1.00 37.93           C  
ANISOU  321  CG  LEU A  61     6252   3995   4165    528   -139  -1213       C  
ATOM    322  CD1 LEU A  61       5.654  -9.912 -43.695  1.00 39.53           C  
ANISOU  322  CD1 LEU A  61     6471   4155   4394    579   -168  -1218       C  
ATOM    323  CD2 LEU A  61       3.456  -9.114 -42.798  1.00 33.10           C  
ANISOU  323  CD2 LEU A  61     5687   3346   3543    458    -58  -1185       C  
ATOM    324  N   VAL A  62       6.696  -7.697 -39.116  1.00 39.77           N  
ANISOU  324  N   VAL A  62     6762   4222   4125    823   -415  -1226       N  
ATOM    325  CA  VAL A  62       7.326  -7.814 -37.803  1.00 39.89           C  
ANISOU  325  CA  VAL A  62     6939   4202   4014    983   -546  -1226       C  
ATOM    326  C   VAL A  62       6.814  -6.752 -36.838  1.00 37.03           C  
ANISOU  326  C   VAL A  62     6577   3885   3607    955   -528  -1230       C  
ATOM    327  O   VAL A  62       6.706  -6.999 -35.644  1.00 38.70           O  
ANISOU  327  O   VAL A  62     6985   4044   3676   1055   -582  -1200       O  
ATOM    328  CB  VAL A  62       8.869  -7.718 -37.893  1.00 41.05           C  
ANISOU  328  CB  VAL A  62     7006   4383   4207   1110   -697  -1299       C  
ATOM    329  CG1 VAL A  62       9.428  -8.880 -38.698  1.00 39.67           C  
ANISOU  329  CG1 VAL A  62     6853   4158   4060   1160   -730  -1301       C  
ATOM    330  CG2 VAL A  62       9.307  -6.388 -38.491  1.00 41.83           C  
ANISOU  330  CG2 VAL A  62     6861   4587   4447   1023   -668  -1365       C  
ATOM    331  N   GLY A  63       6.475  -5.580 -37.365  1.00 33.12           N  
ANISOU  331  N   GLY A  63     5877   3480   3226    820   -448  -1263       N  
ATOM    332  CA  GLY A  63       5.877  -4.538 -36.558  1.00 32.96           C  
ANISOU  332  CA  GLY A  63     5835   3508   3181    773   -417  -1272       C  
ATOM    333  C   GLY A  63       4.548  -4.983 -35.983  1.00 34.36           C  
ANISOU  333  C   GLY A  63     6159   3633   3264    726   -325  -1216       C  
ATOM    334  O   GLY A  63       4.424  -5.180 -34.772  1.00 36.10           O  
ANISOU  334  O   GLY A  63     6568   3805   3342    814   -362  -1189       O  
ATOM    335  N   ASN A  64       3.562  -5.175 -36.855  1.00 31.01           N  
ANISOU  335  N   ASN A  64     5657   3208   2916    598   -205  -1202       N  
ATOM    336  CA  ASN A  64       2.192  -5.416 -36.409  1.00 38.61           C  
ANISOU  336  CA  ASN A  64     6715   4130   3826    532   -103  -1167       C  
ATOM    337  C   ASN A  64       2.056  -6.700 -35.601  1.00 48.08           C  
ANISOU  337  C   ASN A  64     8220   5188   4859    624    -99  -1094       C  
ATOM    338  O   ASN A  64       1.337  -6.735 -34.602  1.00 60.41           O  
ANISOU  338  O   ASN A  64     9947   6698   6307    623    -41  -1059       O  
ATOM    339  CB  ASN A  64       1.240  -5.443 -37.606  1.00 32.41           C  
ANISOU  339  CB  ASN A  64     5769   3372   3175    405     -6  -1182       C  
ATOM    340  CG  ASN A  64       1.034  -4.071 -38.217  1.00 39.65           C  
ANISOU  340  CG  ASN A  64     6486   4383   4196    332      1  -1233       C  
ATOM    341  OD1 ASN A  64       0.245  -3.269 -37.718  1.00 45.51           O  
ANISOU  341  OD1 ASN A  64     7192   5162   4935    285     34  -1254       O  
ATOM    342  ND2 ASN A  64       1.741  -3.797 -39.306  1.00 41.67           N  
ANISOU  342  ND2 ASN A  64     6623   4671   4539    323    -26  -1252       N  
ATOM    343  N   THR A  65       2.757  -7.746 -36.029  1.00 41.48           N  
ANISOU  343  N   THR A  65     7474   4281   4004    701   -152  -1068       N  
ATOM    344  CA  THR A  65       2.796  -8.990 -35.270  1.00 43.19           C  
ANISOU  344  CA  THR A  65     8011   4347   4053    807   -159   -992       C  
ATOM    345  C   THR A  65       3.263  -8.705 -33.846  1.00 47.57           C  
ANISOU  345  C   THR A  65     8749   4879   4444    942   -246   -975       C  
ATOM    346  O   THR A  65       2.632  -9.147 -32.879  1.00 48.65           O  
ANISOU  346  O   THR A  65     9150   4911   4426    966   -175   -909       O  
ATOM    347  CB  THR A  65       3.723 -10.036 -35.921  1.00 42.01           C  
ANISOU  347  CB  THR A  65     7905   4142   3914    898   -244   -984       C  
ATOM    348  OG1 THR A  65       5.060  -9.524 -35.984  1.00 45.87           O  
ANISOU  348  OG1 THR A  65     8271   4713   4444   1001   -399  -1045       O  
ATOM    349  CG2 THR A  65       3.246 -10.376 -37.327  1.00 38.50           C  
ANISOU  349  CG2 THR A  65     7288   3718   3624    773   -158  -1002       C  
ATOM    350  N   LEU A  66       4.340  -7.929 -33.725  1.00 50.72           N  
ANISOU  350  N   LEU A  66     9010   5375   4885   1026   -389  -1040       N  
ATOM    351  CA  LEU A  66       4.887  -7.581 -32.416  1.00 48.24           C  
ANISOU  351  CA  LEU A  66     8836   5058   4437   1175   -502  -1044       C  
ATOM    352  C   LEU A  66       3.856  -6.864 -31.562  1.00 46.83           C  
ANISOU  352  C   LEU A  66     8702   4898   4194   1097   -398  -1031       C  
ATOM    353  O   LEU A  66       3.892  -6.960 -30.339  1.00 52.71           O  
ANISOU  353  O   LEU A  66     9669   5586   4771   1212   -435   -998       O  
ATOM    354  CB  LEU A  66       6.140  -6.712 -32.545  1.00 36.47           C  
ANISOU  354  CB  LEU A  66     7132   3679   3045   1252   -658  -1139       C  
ATOM    355  CG  LEU A  66       7.470  -7.446 -32.724  1.00 40.27           C  
ANISOU  355  CG  LEU A  66     7653   4127   3521   1424   -828  -1165       C  
ATOM    356  CD1 LEU A  66       8.636  -6.478 -32.594  1.00 43.40           C  
ANISOU  356  CD1 LEU A  66     7852   4628   4009   1508   -977  -1271       C  
ATOM    357  CD2 LEU A  66       7.597  -8.594 -31.739  1.00 42.45           C  
ANISOU  357  CD2 LEU A  66     8284   4260   3587   1606   -903  -1094       C  
ATOM    358  N   VAL A  67       2.937  -6.147 -32.203  1.00 44.87           N  
ANISOU  358  N   VAL A  67     8243   4729   4077    913   -272  -1060       N  
ATOM    359  CA  VAL A  67       1.849  -5.523 -31.468  1.00 45.41           C  
ANISOU  359  CA  VAL A  67     8338   4817   4099    829   -164  -1057       C  
ATOM    360  C   VAL A  67       0.944  -6.614 -30.912  1.00 48.84           C  
ANISOU  360  C   VAL A  67     9079   5095   4384    821    -33   -965       C  
ATOM    361  O   VAL A  67       0.725  -6.690 -29.699  1.00 52.61           O  
ANISOU  361  O   VAL A  67     9787   5509   4693    888     -9   -923       O  
ATOM    362  CB  VAL A  67       1.034  -4.554 -32.348  1.00 44.28           C  
ANISOU  362  CB  VAL A  67     7897   4789   4140    649    -74  -1118       C  
ATOM    363  CG1 VAL A  67      -0.218  -4.096 -31.619  1.00 43.18           C  
ANISOU  363  CG1 VAL A  67     7798   4655   3954    565     44  -1119       C  
ATOM    364  CG2 VAL A  67       1.888  -3.365 -32.761  1.00 44.93           C  
ANISOU  364  CG2 VAL A  67     7719   5001   4350    643   -169  -1198       C  
ATOM    365  N   CYS A  68       0.458  -7.477 -31.804  1.00 49.40           N  
ANISOU  365  N   CYS A  68     9162   5093   4515    741     60   -932       N  
ATOM    366  CA  CYS A  68      -0.487  -8.529 -31.435  1.00 52.85           C  
ANISOU  366  CA  CYS A  68     9877   5363   4841    696    225   -848       C  
ATOM    367  C   CYS A  68       0.021  -9.344 -30.254  1.00 58.02           C  
ANISOU  367  C   CYS A  68    10915   5870   5261    862    192   -762       C  
ATOM    368  O   CYS A  68      -0.629  -9.401 -29.206  1.00 63.32           O  
ANISOU  368  O   CYS A  68    11813   6457   5789    857    304   -712       O  
ATOM    369  CB  CYS A  68      -0.763  -9.448 -32.629  1.00 50.74           C  
ANISOU  369  CB  CYS A  68     9563   5036   4681    619    290   -836       C  
ATOM    370  SG  CYS A  68      -1.787  -8.708 -33.923  1.00 57.71           S  
ANISOU  370  SG  CYS A  68    10070   6046   5812    426    369   -921       S  
ATOM    371  N   LEU A  69       1.192  -9.951 -30.429  1.00 56.62           N  
ANISOU  371  N   LEU A  69    10808   5659   5046   1016     35   -749       N  
ATOM    372  CA  LEU A  69       1.854 -10.698 -29.365  1.00 56.49           C  
ANISOU  372  CA  LEU A  69    11147   5507   4810   1218    -49   -677       C  
ATOM    373  C   LEU A  69       1.859  -9.910 -28.060  1.00 56.73           C  
ANISOU  373  C   LEU A  69    11268   5572   4716   1298    -85   -683       C  
ATOM    374  O   LEU A  69       1.441 -10.420 -27.015  1.00 52.53           O  
ANISOU  374  O   LEU A  69    11074   4895   3989   1356      5   -600       O  
ATOM    375  CB  LEU A  69       3.290 -11.049 -29.766  1.00 53.06           C  
ANISOU  375  CB  LEU A  69    10663   5097   4400   1390   -275   -711       C  
ATOM    376  CG  LEU A  69       3.483 -11.961 -30.979  1.00 52.95           C  
ANISOU  376  CG  LEU A  69    10587   5044   4488   1349   -268   -706       C  
ATOM    377  CD1 LEU A  69       4.964 -12.168 -31.268  1.00 46.02           C  
ANISOU  377  CD1 LEU A  69     9637   4210   3640   1526   -501   -759       C  
ATOM    378  CD2 LEU A  69       2.784 -13.293 -30.761  1.00 55.45           C  
ANISOU  378  CD2 LEU A  69    11254   5148   4668   1334   -114   -596       C  
ATOM    379  N   ALA A  70       2.292  -8.652 -28.143  1.00 55.95           N  
ANISOU  379  N   ALA A  70    10867   5658   4733   1292   -198   -783       N  
ATOM    380  CA  ALA A  70       2.462  -7.807 -26.965  1.00 44.99           C  
ANISOU  380  CA  ALA A  70     9516   4329   3248   1381   -266   -811       C  
ATOM    381  C   ALA A  70       1.176  -7.686 -26.162  1.00 55.81           C  
ANISOU  381  C   ALA A  70    11048   5644   4514   1276    -63   -761       C  
ATOM    382  O   ALA A  70       1.212  -7.528 -24.942  1.00 62.50           O  
ANISOU  382  O   ALA A  70    12094   6459   5197   1385    -83   -738       O  
ATOM    383  CB  ALA A  70       2.954  -6.429 -27.371  1.00 43.15           C  
ANISOU  383  CB  ALA A  70     8903   4299   3193   1339   -375   -931       C  
ATOM    384  N   VAL A  71       0.042  -7.767 -26.849  1.00 50.99           N  
ANISOU  384  N   VAL A  71    10347   5022   4005   1069    131   -753       N  
ATOM    385  CA  VAL A  71      -1.245  -7.656 -26.181  1.00 44.49           C  
ANISOU  385  CA  VAL A  71     9648   4145   3112    947    344   -721       C  
ATOM    386  C   VAL A  71      -1.739  -9.032 -25.748  1.00 72.38           C  
ANISOU  386  C   VAL A  71    13584   7436   6480    957    515   -598       C  
ATOM    387  O   VAL A  71      -2.356  -9.181 -24.692  1.00 75.47           O  
ANISOU  387  O   VAL A  71    14231   7727   6719    956    655   -543       O  
ATOM    388  CB  VAL A  71      -2.293  -6.988 -27.092  1.00 42.34           C  
ANISOU  388  CB  VAL A  71     9062   3977   3047    724    467   -792       C  
ATOM    389  CG1 VAL A  71      -3.622  -6.842 -26.369  1.00 43.38           C  
ANISOU  389  CG1 VAL A  71     9305   4056   3122    599    685   -776       C  
ATOM    390  CG2 VAL A  71      -1.790  -5.633 -27.567  1.00 43.89           C  
ANISOU  390  CG2 VAL A  71     8879   4390   3406    713    311   -907       C  
ATOM    391  N   TRP A  72      -1.439 -10.041 -26.558  1.00 68.72           N  
ANISOU  391  N   TRP A  72    13187   6874   6051    967    511   -558       N  
ATOM    392  CA  TRP A  72      -1.975 -11.379 -26.332  1.00 70.34           C  
ANISOU  392  CA  TRP A  72    13759   6836   6132    946    702   -446       C  
ATOM    393  C   TRP A  72      -1.291 -12.097 -25.172  1.00 75.49           C  
ANISOU  393  C   TRP A  72    14828   7323   6533   1170    637   -353       C  
ATOM    394  O   TRP A  72      -1.945 -12.785 -24.388  1.00 77.88           O  
ANISOU  394  O   TRP A  72    15480   7425   6684   1155    837   -263       O  
ATOM    395  CB  TRP A  72      -1.860 -12.214 -27.609  1.00 68.69           C  
ANISOU  395  CB  TRP A  72    13470   6583   6047    888    709   -443       C  
ATOM    396  CG  TRP A  72      -2.867 -11.843 -28.659  1.00 64.08           C  
ANISOU  396  CG  TRP A  72    12573   6088   5688    656    844   -514       C  
ATOM    397  CD1 TRP A  72      -4.023 -11.138 -28.476  1.00 59.99           C  
ANISOU  397  CD1 TRP A  72    11933   5618   5241    490   1006   -558       C  
ATOM    398  CD2 TRP A  72      -2.804 -12.153 -30.058  1.00 60.88           C  
ANISOU  398  CD2 TRP A  72    11929   5735   5470    582    812   -560       C  
ATOM    399  NE1 TRP A  72      -4.684 -10.995 -29.673  1.00 54.73           N  
ANISOU  399  NE1 TRP A  72    10971   5028   4797    328   1064   -629       N  
ATOM    400  CE2 TRP A  72      -3.956 -11.608 -30.659  1.00 56.72           C  
ANISOU  400  CE2 TRP A  72    11147   5284   5121    382    948   -630       C  
ATOM    401  CE3 TRP A  72      -1.885 -12.839 -30.859  1.00 62.73           C  
ANISOU  401  CE3 TRP A  72    12132   5961   5742    673    673   -557       C  
ATOM    402  CZ2 TRP A  72      -4.214 -11.727 -32.025  1.00 56.06           C  
ANISOU  402  CZ2 TRP A  72    10788   5267   5245    284    942   -692       C  
ATOM    403  CZ3 TRP A  72      -2.143 -12.957 -32.216  1.00 57.45           C  
ANISOU  403  CZ3 TRP A  72    11185   5362   5282    559    684   -617       C  
ATOM    404  CH2 TRP A  72      -3.298 -12.404 -32.784  1.00 54.75           C  
ANISOU  404  CH2 TRP A  72    10601   5093   5108    374    813   -682       C  
ATOM    405  N   ARG A  73       0.022 -11.928 -25.061  1.00 73.33           N  
ANISOU  405  N   ARG A  73    14359   7485   6018   1853   -296   -397       N  
ATOM    406  CA  ARG A  73       0.798 -12.616 -24.034  1.00 80.24           C  
ANISOU  406  CA  ARG A  73    15650   8205   6633   2199   -405   -338       C  
ATOM    407  C   ARG A  73       0.520 -12.086 -22.628  1.00 81.82           C  
ANISOU  407  C   ARG A  73    15798   8608   6682   2116   -405   -380       C  
ATOM    408  O   ARG A  73       0.374 -12.861 -21.683  1.00 87.23           O  
ANISOU  408  O   ARG A  73    16939   9101   7105   2173   -364   -297       O  
ATOM    409  CB  ARG A  73       2.295 -12.504 -24.336  1.00 84.06           C  
ANISOU  409  CB  ARG A  73    16008   8770   7163   2656   -639   -384       C  
ATOM    410  CG  ARG A  73       2.734 -13.239 -25.591  1.00 87.87           C  
ANISOU  410  CG  ARG A  73    16632   9028   7728   2818   -664   -327       C  
ATOM    411  CD  ARG A  73       4.228 -13.079 -25.831  1.00 94.20           C  
ANISOU  411  CD  ARG A  73    17254   9972   8566   3276   -904   -408       C  
ATOM    412  NE  ARG A  73       4.679 -13.846 -26.991  1.00100.44           N  
ANISOU  412  NE  ARG A  73    18152  10607   9405   3411   -932   -355       N  
ATOM    413  CZ  ARG A  73       5.928 -13.847 -27.448  1.00101.54           C  
ANISOU  413  CZ  ARG A  73    18026  10966   9588   3673  -1098   -451       C  
ATOM    414  NH1 ARG A  73       6.858 -13.119 -26.847  1.00103.55           N  
ANISOU  414  NH1 ARG A  73    18014  11484   9847   3957  -1278   -592       N  
ATOM    415  NH2 ARG A  73       6.247 -14.575 -28.509  1.00 98.87           N  
ANISOU  415  NH2 ARG A  73    17684  10604   9280   3644  -1082   -418       N  
ATOM    416  N   ASN A  74       0.445 -10.766 -22.495  1.00 82.37           N  
ANISOU  416  N   ASN A  74    15329   9055   6911   1974   -440   -511       N  
ATOM    417  CA  ASN A  74       0.349 -10.134 -21.182  1.00 83.63           C  
ANISOU  417  CA  ASN A  74    15378   9457   6939   1927   -467   -570       C  
ATOM    418  C   ASN A  74      -1.085  -9.853 -20.738  1.00 87.49           C  
ANISOU  418  C   ASN A  74    15806  10032   7404   1497   -269   -600       C  
ATOM    419  O   ASN A  74      -1.993  -9.744 -21.562  1.00 89.63           O  
ANISOU  419  O   ASN A  74    15927  10289   7838   1219   -131   -633       O  
ATOM    420  CB  ASN A  74       1.156  -8.835 -21.174  1.00 77.33           C  
ANISOU  420  CB  ASN A  74    14056   9015   6313   2024   -610   -723       C  
ATOM    421  CG  ASN A  74       2.620  -9.057 -21.498  1.00 78.45           C  
ANISOU  421  CG  ASN A  74    14201   9143   6465   2461   -813   -737       C  
ATOM    422  OD1 ASN A  74       3.457  -9.170 -20.602  1.00 88.33           O  
ANISOU  422  OD1 ASN A  74    15539  10479   7542   2762   -959   -759       O  
ATOM    423  ND2 ASN A  74       2.937  -9.127 -22.786  1.00 71.41           N  
ANISOU  423  ND2 ASN A  74    13192   8170   5769   2506   -828   -741       N  
ATOM    424  N   HIS A  75      -1.277  -9.733 -19.427  1.00 88.04           N  
ANISOU  424  N   HIS A  75    15970  10218   7262   1461   -264   -604       N  
ATOM    425  CA  HIS A  75      -2.597  -9.487 -18.856  1.00 88.57           C  
ANISOU  425  CA  HIS A  75    15979  10401   7272   1082    -84   -654       C  
ATOM    426  C   HIS A  75      -2.860  -7.996 -18.670  1.00 80.59           C  
ANISOU  426  C   HIS A  75    14377   9808   6437    925   -102   -845       C  
ATOM    427  O   HIS A  75      -4.002  -7.543 -18.743  1.00 78.24           O  
ANISOU  427  O   HIS A  75    13849   9653   6224    629     35   -948       O  
ATOM    428  CB  HIS A  75      -2.743 -10.207 -17.513  1.00100.22           C  
ANISOU  428  CB  HIS A  75    17910  11767   8402   1101    -44   -552       C  
ATOM    429  CG  HIS A  75      -2.391 -11.661 -17.563  1.00110.09           C  
ANISOU  429  CG  HIS A  75    19805  12570   9455   1292    -27   -371       C  
ATOM    430  ND1 HIS A  75      -2.843 -12.503 -18.556  1.00112.62           N  
ANISOU  430  ND1 HIS A  75    20383  12561   9848   1171    106   -308       N  
ATOM    431  CD2 HIS A  75      -1.636 -12.425 -16.738  1.00115.71           C  
ANISOU  431  CD2 HIS A  75    20967  13103   9895   1605   -124   -255       C  
ATOM    432  CE1 HIS A  75      -2.378 -13.721 -18.343  1.00116.80           C  
ANISOU  432  CE1 HIS A  75    21514  12702  10163   1393    103   -167       C  
ATOM    433  NE2 HIS A  75      -1.643 -13.701 -17.246  1.00119.30           N  
ANISOU  433  NE2 HIS A  75    21958  13102  10267   1677    -41   -132       N  
ATOM    434  N   HIS A  76      -1.795  -7.239 -18.426  1.00 80.34           N  
ANISOU  434  N   HIS A  76    14105   9963   6459   1137   -269   -911       N  
ATOM    435  CA  HIS A  76      -1.908  -5.804 -18.183  1.00 75.90           C  
ANISOU  435  CA  HIS A  76    13040   9747   6053    987   -277  -1095       C  
ATOM    436  C   HIS A  76      -2.100  -5.028 -19.482  1.00 70.09           C  
ANISOU  436  C   HIS A  76    11920   9058   5651    866   -239  -1192       C  
ATOM    437  O   HIS A  76      -2.389  -3.831 -19.463  1.00 68.10           O  
ANISOU  437  O   HIS A  76    11329   9004   5541    726   -212  -1340       O  
ATOM    438  CB  HIS A  76      -0.668  -5.289 -17.452  1.00 79.96           C  
ANISOU  438  CB  HIS A  76    13468  10415   6498   1230   -452  -1139       C  
ATOM    439  CG  HIS A  76       0.578  -5.325 -18.282  1.00 79.03           C  
ANISOU  439  CG  HIS A  76    13294  10215   6516   1528   -600  -1127       C  
ATOM    440  ND1 HIS A  76       1.360  -6.453 -18.402  1.00 81.01           N  
ANISOU  440  ND1 HIS A  76    13905  10247   6627   1870   -712   -999       N  
ATOM    441  CD2 HIS A  76       1.173  -4.372 -19.037  1.00 76.11           C  
ANISOU  441  CD2 HIS A  76    12558   9954   6405   1538   -647  -1240       C  
ATOM    442  CE1 HIS A  76       2.385  -6.194 -19.194  1.00 78.75           C  
ANISOU  442  CE1 HIS A  76    13429   9983   6508   2088   -832  -1054       C  
ATOM    443  NE2 HIS A  76       2.295  -4.938 -19.593  1.00 76.22           N  
ANISOU  443  NE2 HIS A  76    12672   9857   6429   1877   -789  -1194       N  
ATOM    444  N   MET A  77      -1.930  -5.714 -20.608  1.00 72.20           N  
ANISOU  444  N   MET A  77    12322   9095   6017    954   -240  -1100       N  
ATOM    445  CA  MET A  77      -2.043  -5.086 -21.919  1.00 59.10           C  
ANISOU  445  CA  MET A  77    10360   7447   4648    877   -214  -1163       C  
ATOM    446  C   MET A  77      -3.413  -5.312 -22.544  1.00 57.66           C  
ANISOU  446  C   MET A  77    10167   7212   4531    644    -64  -1180       C  
ATOM    447  O   MET A  77      -3.673  -4.867 -23.660  1.00 59.69           O  
ANISOU  447  O   MET A  77    10224   7460   4996    591    -39  -1223       O  
ATOM    448  CB  MET A  77      -0.956  -5.614 -22.857  1.00 53.59           C  
ANISOU  448  CB  MET A  77     9759   6573   4030   1124   -318  -1074       C  
ATOM    449  CG  MET A  77       0.454  -5.215 -22.464  1.00 54.48           C  
ANISOU  449  CG  MET A  77     9801   6779   4121   1399   -489  -1110       C  
ATOM    450  SD  MET A  77       0.790  -3.475 -22.791  1.00 60.31           S  
ANISOU  450  SD  MET A  77    10051   7748   5116   1288   -496  -1282       S  
ATOM    451  CE  MET A  77       0.659  -3.433 -24.578  1.00 43.47           C  
ANISOU  451  CE  MET A  77     7809   5473   3234   1246   -450  -1251       C  
ATOM    452  N   ARG A  78      -4.289  -6.002 -21.822  1.00 57.06           N  
ANISOU  452  N   ARG A  78    10308   7109   4265    508     38  -1151       N  
ATOM    453  CA  ARG A  78      -5.600  -6.348 -22.358  1.00 57.38           C  
ANISOU  453  CA  ARG A  78    10358   7101   4342    291    184  -1180       C  
ATOM    454  C   ARG A  78      -6.640  -5.273 -22.062  1.00 57.78           C  
ANISOU  454  C   ARG A  78    10075   7420   4460    134    236  -1366       C  
ATOM    455  O   ARG A  78      -7.621  -5.513 -21.359  1.00 57.21           O  
ANISOU  455  O   ARG A  78    10082   7405   4249    -15    335  -1408       O  
ATOM    456  CB  ARG A  78      -6.053  -7.700 -21.809  1.00 61.93           C  
ANISOU  456  CB  ARG A  78    11394   7458   4678    201    295  -1055       C  
ATOM    457  CG  ARG A  78      -5.219  -8.855 -22.336  1.00 69.16           C  
ANISOU  457  CG  ARG A  78    12750   8006   5520    375    262   -871       C  
ATOM    458  CD  ARG A  78      -5.523 -10.159 -21.624  1.00 80.24           C  
ANISOU  458  CD  ARG A  78    14754   9099   6634    305    380   -732       C  
ATOM    459  NE  ARG A  78      -4.605 -11.217 -22.040  1.00 86.70           N  
ANISOU  459  NE  ARG A  78    16019   9552   7370    549    322   -569       N  
ATOM    460  CZ  ARG A  78      -4.506 -12.400 -21.444  1.00 94.43           C  
ANISOU  460  CZ  ARG A  78    17605  10186   8087    598    386   -430       C  
ATOM    461  NH1 ARG A  78      -5.268 -12.684 -20.397  1.00 97.91           N  
ANISOU  461  NH1 ARG A  78    18283  10602   8318    379    524   -423       N  
ATOM    462  NH2 ARG A  78      -3.641 -13.299 -21.893  1.00 97.59           N  
ANISOU  462  NH2 ARG A  78    18388  10259   8433    877    316   -309       N  
ATOM    463  N   THR A  79      -6.409  -4.086 -22.614  1.00 54.91           N  
ANISOU  463  N   THR A  79     9360   7198   4304    178    171  -1478       N  
ATOM    464  CA  THR A  79      -7.362  -2.987 -22.533  1.00 57.42           C  
ANISOU  464  CA  THR A  79     9350   7751   4715     91    197  -1668       C  
ATOM    465  C   THR A  79      -8.226  -2.986 -23.789  1.00 50.25           C  
ANISOU  465  C   THR A  79     8326   6804   3965     51    237  -1709       C  
ATOM    466  O   THR A  79      -7.787  -3.454 -24.840  1.00 50.31           O  
ANISOU  466  O   THR A  79     8407   6642   4069     82    232  -1610       O  
ATOM    467  CB  THR A  79      -6.647  -1.626 -22.387  1.00 64.56           C  
ANISOU  467  CB  THR A  79     9987   8795   5748    120    135  -1767       C  
ATOM    468  OG1 THR A  79      -5.571  -1.747 -21.449  1.00 69.37           O  
ANISOU  468  OG1 THR A  79    10745   9391   6222    193     74  -1696       O  
ATOM    469  CG2 THR A  79      -7.613  -0.545 -21.913  1.00 67.57           C  
ANISOU  469  CG2 THR A  79    10077   9397   6199     56    154  -1933       C  
ATOM    470  N   VAL A  80      -9.453  -2.480 -23.674  1.00 43.15           N  
ANISOU  470  N   VAL A  80     7277   6045   3073     26    255  -1844       N  
ATOM    471  CA  VAL A  80     -10.346  -2.322 -24.821  1.00 38.56           C  
ANISOU  471  CA  VAL A  80     6589   5440   2620     37    259  -1893       C  
ATOM    472  C   VAL A  80      -9.642  -1.578 -25.954  1.00 50.78           C  
ANISOU  472  C   VAL A  80     7902   6992   4400    121    190  -1900       C  
ATOM    473  O   VAL A  80      -9.697  -1.992 -27.119  1.00 54.63           O  
ANISOU  473  O   VAL A  80     8405   7387   4966    110    210  -1867       O  
ATOM    474  CB  VAL A  80     -11.633  -1.561 -24.430  1.00 39.45           C  
ANISOU  474  CB  VAL A  80     6669   5617   2702     60    252  -1990       C  
ATOM    475  CG1 VAL A  80     -12.447  -1.205 -25.665  1.00 45.45           C  
ANISOU  475  CG1 VAL A  80     7374   6312   3584     83    246  -2008       C  
ATOM    476  CG2 VAL A  80     -12.461  -2.383 -23.454  1.00 42.05           C  
ANISOU  476  CG2 VAL A  80     7182   5948   2847   -195    413  -1989       C  
ATOM    477  N   THR A  81      -8.972  -0.487 -25.591  1.00 39.39           N  
ANISOU  477  N   THR A  81     6265   5624   3079    109    166  -1916       N  
ATOM    478  CA  THR A  81      -8.174   0.295 -26.528  1.00 37.52           C  
ANISOU  478  CA  THR A  81     5979   5257   3021     19    215  -1858       C  
ATOM    479  C   THR A  81      -7.166  -0.589 -27.259  1.00 39.83           C  
ANISOU  479  C   THR A  81     6467   5376   3289    132    170  -1745       C  
ATOM    480  O   THR A  81      -7.039  -0.525 -28.482  1.00 42.09           O  
ANISOU  480  O   THR A  81     6731   5558   3703    169    165  -1688       O  
ATOM    481  CB  THR A  81      -7.421   1.435 -25.809  1.00 43.67           C  
ANISOU  481  CB  THR A  81     6827   5961   3804    -34    235  -1826       C  
ATOM    482  OG1 THR A  81      -8.347   2.232 -25.059  1.00 45.66           O  
ANISOU  482  OG1 THR A  81     7200   6144   4005   -182    319  -1808       O  
ATOM    483  CG2 THR A  81      -6.692   2.314 -26.814  1.00 35.74           C  
ANISOU  483  CG2 THR A  81     5845   4803   2931     81    193  -1772       C  
ATOM    484  N   ASN A  82      -6.465  -1.426 -26.501  1.00 36.83           N  
ANISOU  484  N   ASN A  82     6294   4930   2768    199    131  -1648       N  
ATOM    485  CA  ASN A  82      -5.451  -2.306 -27.067  1.00 43.78           C  
ANISOU  485  CA  ASN A  82     7379   5608   3649    330     76  -1482       C  
ATOM    486  C   ASN A  82      -6.043  -3.454 -27.880  1.00 42.50           C  
ANISOU  486  C   ASN A  82     7362   5319   3466    293    129  -1414       C  
ATOM    487  O   ASN A  82      -5.403  -3.952 -28.803  1.00 43.69           O  
ANISOU  487  O   ASN A  82     7603   5315   3681    381     98  -1307       O  
ATOM    488  CB  ASN A  82      -4.557  -2.860 -25.958  1.00 46.33           C  
ANISOU  488  CB  ASN A  82     7908   5894   3801    430     18  -1408       C  
ATOM    489  CG  ASN A  82      -3.594  -1.823 -25.414  1.00 47.61           C  
ANISOU  489  CG  ASN A  82     7942   6145   4002    512    -59  -1454       C  
ATOM    490  OD1 ASN A  82      -3.666  -0.646 -25.768  1.00 47.96           O  
ANISOU  490  OD1 ASN A  82     7779   6248   4194    463    -45  -1532       O  
ATOM    491  ND2 ASN A  82      -2.686  -2.255 -24.545  1.00 48.42           N  
ANISOU  491  ND2 ASN A  82     8194   6242   3962    643   -138  -1405       N  
ATOM    492  N   TYR A  83      -7.254  -3.882 -27.534  1.00 39.46           N  
ANISOU  492  N   TYR A  83     7006   5002   2985    162    212  -1482       N  
ATOM    493  CA  TYR A  83      -7.955  -4.877 -28.342  1.00 43.24           C  
ANISOU  493  CA  TYR A  83     7613   5365   3451     80    288  -1442       C  
ATOM    494  C   TYR A  83      -8.276  -4.285 -29.709  1.00 43.82           C  
ANISOU  494  C   TYR A  83     7446   5492   3713    100    269  -1505       C  
ATOM    495  O   TYR A  83      -8.096  -4.935 -30.747  1.00 48.91           O  
ANISOU  495  O   TYR A  83     8175   5998   4409    110    283  -1425       O  
ATOM    496  CB  TYR A  83      -9.236  -5.352 -27.650  1.00 51.20           C  
ANISOU  496  CB  TYR A  83     8705   6434   4313    -87    395  -1513       C  
ATOM    497  CG  TYR A  83      -9.022  -6.456 -26.637  1.00 62.78           C  
ANISOU  497  CG  TYR A  83    10545   7742   5565   -163    469  -1396       C  
ATOM    498  CD1 TYR A  83      -8.806  -7.766 -27.044  1.00 67.57           C  
ANISOU  498  CD1 TYR A  83    11483   8088   6101   -213    542  -1257       C  
ATOM    499  CD2 TYR A  83      -9.048  -6.191 -25.273  1.00 68.23           C  
ANISOU  499  CD2 TYR A  83    11280   8535   6110   -178    467  -1426       C  
ATOM    500  CE1 TYR A  83      -8.612  -8.779 -26.123  1.00 70.99           C  
ANISOU  500  CE1 TYR A  83    12312   8341   6322   -265    611  -1143       C  
ATOM    501  CE2 TYR A  83      -8.854  -7.198 -24.344  1.00 72.21           C  
ANISOU  501  CE2 TYR A  83    12159   8883   6393   -237    533  -1311       C  
ATOM    502  CZ  TYR A  83      -8.637  -8.490 -24.774  1.00 72.92           C  
ANISOU  502  CZ  TYR A  83    12605   8688   6413   -275    604  -1166       C  
ATOM    503  OH  TYR A  83      -8.446  -9.495 -23.854  1.00 75.51           O  
ANISOU  503  OH  TYR A  83    13376   8813   6503   -317    674  -1043       O  
ATOM    504  N   PHE A  84      -8.749  -3.042 -29.700  1.00 42.32           N  
ANISOU  504  N   PHE A  84     6968   5499   3613    114    236  -1654       N  
ATOM    505  CA  PHE A  84      -8.991  -2.315 -30.940  1.00 38.94           C  
ANISOU  505  CA  PHE A  84     6327   5117   3349    136    220  -1715       C  
ATOM    506  C   PHE A  84      -7.702  -2.174 -31.745  1.00 37.88           C  
ANISOU  506  C   PHE A  84     6264   4803   3325    214    185  -1559       C  
ATOM    507  O   PHE A  84      -7.684  -2.423 -32.952  1.00 43.68           O  
ANISOU  507  O   PHE A  84     6997   5463   4137    238    184  -1512       O  
ATOM    508  CB  PHE A  84      -9.586  -0.940 -30.644  1.00 39.36           C  
ANISOU  508  CB  PHE A  84     6118   5335   3500    104    216  -1819       C  
ATOM    509  CG  PHE A  84     -11.044  -0.973 -30.288  1.00 41.36           C  
ANISOU  509  CG  PHE A  84     6367   5688   3661    287    105  -1882       C  
ATOM    510  CD1 PHE A  84     -11.887  -1.914 -30.856  1.00 42.38           C  
ANISOU  510  CD1 PHE A  84     6690   5732   3680    251    152  -1881       C  
ATOM    511  CD2 PHE A  84     -11.572  -0.065 -29.386  1.00 41.83           C  
ANISOU  511  CD2 PHE A  84     6701   5591   3600    433     32  -1788       C  
ATOM    512  CE1 PHE A  84     -13.229  -1.947 -30.534  1.00 44.03           C  
ANISOU  512  CE1 PHE A  84     7056   5931   3742    163    224  -1949       C  
ATOM    513  CE2 PHE A  84     -12.913  -0.093 -29.058  1.00 46.08           C  
ANISOU  513  CE2 PHE A  84     7370   6135   4002    249    161  -1880       C  
ATOM    514  CZ  PHE A  84     -13.743  -1.037 -29.633  1.00 47.45           C  
ANISOU  514  CZ  PHE A  84     7524   6388   4119    137    239  -1986       C  
ATOM    515  N   ILE A  85      -6.626  -1.785 -31.067  1.00 29.81           N  
ANISOU  515  N   ILE A  85     5300   3732   2295    288    135  -1491       N  
ATOM    516  CA  ILE A  85      -5.313  -1.673 -31.698  1.00 28.76           C  
ANISOU  516  CA  ILE A  85     5219   3468   2241    427     60  -1366       C  
ATOM    517  C   ILE A  85      -4.917  -2.995 -32.355  1.00 32.06           C  
ANISOU  517  C   ILE A  85     5822   3737   2624    482     50  -1248       C  
ATOM    518  O   ILE A  85      -4.357  -3.013 -33.454  1.00 34.17           O  
ANISOU  518  O   ILE A  85     6075   3928   2980    554     17  -1180       O  
ATOM    519  CB  ILE A  85      -4.233  -1.250 -30.674  1.00 29.12           C  
ANISOU  519  CB  ILE A  85     5291   3527   2245    513     -5  -1353       C  
ATOM    520  CG1 ILE A  85      -4.463   0.195 -30.228  1.00 28.91           C  
ANISOU  520  CG1 ILE A  85     5099   3606   2278    461     11  -1453       C  
ATOM    521  CG2 ILE A  85      -2.838  -1.396 -31.259  1.00 28.55           C  
ANISOU  521  CG2 ILE A  85     5261   3361   2225    670    -91  -1261       C  
ATOM    522  CD1 ILE A  85      -3.427   0.713 -29.254  1.00 29.40           C  
ANISOU  522  CD1 ILE A  85     5160   3706   2304    532    -47  -1468       C  
ATOM    523  N   VAL A  86      -5.229  -4.100 -31.685  1.00 30.24           N  
ANISOU  523  N   VAL A  86     5787   3454   2248    438     89  -1220       N  
ATOM    524  CA  VAL A  86      -4.968  -5.429 -32.227  1.00 44.09           C  
ANISOU  524  CA  VAL A  86     7775   5030   3948    467    106  -1104       C  
ATOM    525  C   VAL A  86      -5.772  -5.672 -33.499  1.00 46.25           C  
ANISOU  525  C   VAL A  86     7973   5299   4303    377    167  -1131       C  
ATOM    526  O   VAL A  86      -5.236  -6.179 -34.484  1.00 46.67           O  
ANISOU  526  O   VAL A  86     8090   5240   4403    441    149  -1046       O  
ATOM    527  CB  VAL A  86      -5.285  -6.535 -31.198  1.00 42.58           C  
ANISOU  527  CB  VAL A  86     7869   4747   3561    406    167  -1063       C  
ATOM    528  CG1 VAL A  86      -5.433  -7.889 -31.883  1.00 33.53           C  
ANISOU  528  CG1 VAL A  86     6975   3402   2362    365    236   -968       C  
ATOM    529  CG2 VAL A  86      -4.203  -6.592 -30.140  1.00 33.59           C  
ANISOU  529  CG2 VAL A  86     6871   3573   2320    560     79  -1003       C  
ATOM    530  N   ASN A  87      -7.053  -5.310 -33.481  1.00 32.03           N  
ANISOU  530  N   ASN A  87     6018   3643   2508    246    230  -1268       N  
ATOM    531  CA  ASN A  87      -7.881  -5.429 -34.682  1.00 31.70           C  
ANISOU  531  CA  ASN A  87     5862   3647   2537    185    269  -1334       C  
ATOM    532  C   ASN A  87      -7.276  -4.650 -35.850  1.00 37.34           C  
ANISOU  532  C   ASN A  87     6432   4356   3401    285    207  -1301       C  
ATOM    533  O   ASN A  87      -7.198  -5.146 -36.983  1.00 29.60           O  
ANISOU  533  O   ASN A  87     5476   3307   2463    296    215  -1257       O  
ATOM    534  CB  ASN A  87      -9.303  -4.941 -34.406  1.00 32.53           C  
ANISOU  534  CB  ASN A  87     5777   3964   2617    100    300  -1525       C  
ATOM    535  CG  ASN A  87     -10.244  -5.198 -35.568  1.00 41.66           C  
ANISOU  535  CG  ASN A  87     6834   5187   3808     73    319  -1616       C  
ATOM    536  OD1 ASN A  87     -10.119  -6.203 -36.269  1.00 38.98           O  
ANISOU  536  OD1 ASN A  87     6640   4714   3458     22    371  -1540       O  
ATOM    537  ND2 ASN A  87     -11.189  -4.289 -35.781  1.00 41.34           N  
ANISOU  537  ND2 ASN A  87     6564   5350   3793    144    258  -1781       N  
ATOM    538  N   LEU A  88      -6.841  -3.429 -35.551  1.00 37.63           N  
ANISOU  538  N   LEU A  88     6344   4452   3503    346    155  -1315       N  
ATOM    539  CA  LEU A  88      -6.181  -2.567 -36.525  1.00 28.07           C  
ANISOU  539  CA  LEU A  88     5049   3208   2408    437    102  -1258       C  
ATOM    540  C   LEU A  88      -4.944  -3.241 -37.113  1.00 38.53           C  
ANISOU  540  C   LEU A  88     6501   4395   3744    541     52  -1119       C  
ATOM    541  O   LEU A  88      -4.739  -3.244 -38.332  1.00 40.49           O  
ANISOU  541  O   LEU A  88     6723   4608   4055    573     41  -1078       O  
ATOM    542  CB  LEU A  88      -5.799  -1.237 -35.869  1.00 27.75           C  
ANISOU  542  CB  LEU A  88     4919   3219   2407    478     66  -1283       C  
ATOM    543  CG  LEU A  88      -5.182  -0.153 -36.753  1.00 33.69           C  
ANISOU  543  CG  LEU A  88     5601   3939   3259    565     17  -1237       C  
ATOM    544  CD1 LEU A  88      -6.142   0.235 -37.860  1.00 37.26           C  
ANISOU  544  CD1 LEU A  88     5987   4418   3753    547     42  -1271       C  
ATOM    545  CD2 LEU A  88      -4.802   1.063 -35.920  1.00 31.01           C  
ANISOU  545  CD2 LEU A  88     5202   3639   2939    587     -4  -1277       C  
ATOM    546  N   SER A  89      -4.128  -3.820 -36.238  1.00 38.52           N  
ANISOU  546  N   SER A  89     6640   4330   3667    600     19  -1060       N  
ATOM    547  CA  SER A  89      -2.905  -4.496 -36.657  1.00 38.87           C  
ANISOU  547  CA  SER A  89     6800   4267   3701    719    -38   -957       C  
ATOM    548  C   SER A  89      -3.197  -5.733 -37.499  1.00 36.12           C  
ANISOU  548  C   SER A  89     6587   3814   3321    686      9   -901       C  
ATOM    549  O   SER A  89      -2.436  -6.061 -38.404  1.00 36.31           O  
ANISOU  549  O   SER A  89     6633   3785   3380    761    -25   -842       O  
ATOM    550  CB  SER A  89      -2.062  -4.883 -35.440  1.00 43.80           C  
ANISOU  550  CB  SER A  89     7558   4859   4225    818    -94   -928       C  
ATOM    551  OG  SER A  89      -1.469  -3.742 -34.846  1.00 45.10           O  
ANISOU  551  OG  SER A  89     7580   5125   4432    866   -148   -987       O  
ATOM    552  N   LEU A  90      -4.293  -6.420 -37.197  1.00 40.21           N  
ANISOU  552  N   LEU A  90     7192   4317   3770    560     97   -938       N  
ATOM    553  CA  LEU A  90      -4.697  -7.584 -37.976  1.00 42.28           C  
ANISOU  553  CA  LEU A  90     7584   4480   3999    493    167   -908       C  
ATOM    554  C   LEU A  90      -5.111  -7.161 -39.381  1.00 40.83           C  
ANISOU  554  C   LEU A  90     7216   4370   3928    463    176   -958       C  
ATOM    555  O   LEU A  90      -4.740  -7.802 -40.371  1.00 38.59           O  
ANISOU  555  O   LEU A  90     6988   4010   3662    488    181   -905       O  
ATOM    556  CB  LEU A  90      -5.839  -8.332 -37.286  1.00 43.52           C  
ANISOU  556  CB  LEU A  90     7869   4620   4047    329    278   -964       C  
ATOM    557  CG  LEU A  90      -5.489  -9.065 -35.988  1.00 49.75           C  
ANISOU  557  CG  LEU A  90     8939   5281   4682    343    294   -889       C  
ATOM    558  CD1 LEU A  90      -6.723  -9.721 -35.387  1.00 53.69           C  
ANISOU  558  CD1 LEU A  90     9567   5767   5066    132    432   -952       C  
ATOM    559  CD2 LEU A  90      -4.391 -10.093 -36.227  1.00 47.80           C  
ANISOU  559  CD2 LEU A  90     8954   4835   4372    480    258   -746       C  
ATOM    560  N   ALA A  91      -5.880  -6.078 -39.460  1.00 36.89           N  
ANISOU  560  N   ALA A  91     6504   4021   3493    420    176  -1067       N  
ATOM    561  CA  ALA A  91      -6.274  -5.523 -40.752  1.00 40.23           C  
ANISOU  561  CA  ALA A  91     6767   4515   4005    421    171  -1116       C  
ATOM    562  C   ALA A  91      -5.046  -5.148 -41.580  1.00 41.93           C  
ANISOU  562  C   ALA A  91     6985   4665   4283    540    103  -1005       C  
ATOM    563  O   ALA A  91      -4.910  -5.559 -42.739  1.00 38.94           O  
ANISOU  563  O   ALA A  91     6612   4253   3931    549    110   -979       O  
ATOM    564  CB  ALA A  91      -7.174  -4.313 -40.558  1.00 39.91           C  
ANISOU  564  CB  ALA A  91     6535   4629   3999    390    172  -1242       C  
ATOM    565  N   ASP A  92      -4.147  -4.378 -40.972  1.00 40.70           N  
ANISOU  565  N   ASP A  92     6812   4508   4143    622     40   -962       N  
ATOM    566  CA  ASP A  92      -2.929  -3.945 -41.650  1.00 44.82           C  
ANISOU  566  CA  ASP A  92     7312   5003   4715    715    -17   -899       C  
ATOM    567  C   ASP A  92      -2.047  -5.125 -42.062  1.00 44.43           C  
ANISOU  567  C   ASP A  92     7386   4866   4632    766    -30   -830       C  
ATOM    568  O   ASP A  92      -1.357  -5.066 -43.081  1.00 45.19           O  
ANISOU  568  O   ASP A  92     7449   4952   4768    803    -47   -807       O  
ATOM    569  CB  ASP A  92      -2.141  -2.981 -40.760  1.00 48.44           C  
ANISOU  569  CB  ASP A  92     7719   5499   5189    769    -67   -912       C  
ATOM    570  CG  ASP A  92      -2.826  -1.634 -40.614  1.00 55.68           C  
ANISOU  570  CG  ASP A  92     8519   6487   6148    737    -57   -974       C  
ATOM    571  OD1 ASP A  92      -3.653  -1.291 -41.486  1.00 54.58           O  
ANISOU  571  OD1 ASP A  92     8334   6369   6034    712    -34   -993       O  
ATOM    572  OD2 ASP A  92      -2.534  -0.919 -39.631  1.00 60.72           O  
ANISOU  572  OD2 ASP A  92     9121   7163   6787    747    -74  -1011       O  
ATOM    573  N   VAL A  93      -2.073  -6.192 -41.268  1.00 40.38           N  
ANISOU  573  N   VAL A  93     7029   4282   4033    768    -16   -803       N  
ATOM    574  CA  VAL A  93      -1.362  -7.419 -41.610  1.00 35.99           C  
ANISOU  574  CA  VAL A  93     6630   3623   3422    829    -24   -739       C  
ATOM    575  C   VAL A  93      -1.969  -8.037 -42.863  1.00 39.13           C  
ANISOU  575  C   VAL A  93     7033   3991   3844    750     43   -743       C  
ATOM    576  O   VAL A  93      -1.249  -8.451 -43.771  1.00 41.63           O  
ANISOU  576  O   VAL A  93     7362   4276   4178    801     26   -715       O  
ATOM    577  CB  VAL A  93      -1.397  -8.449 -40.455  1.00 35.64           C  
ANISOU  577  CB  VAL A  93     6817   3475   3248    851    -12   -697       C  
ATOM    578  CG1 VAL A  93      -1.236  -9.867 -40.984  1.00 34.22           C  
ANISOU  578  CG1 VAL A  93     6845   3161   2997    863     27   -638       C  
ATOM    579  CG2 VAL A  93      -0.315  -8.143 -39.436  1.00 39.91           C  
ANISOU  579  CG2 VAL A  93     7381   4036   3747    998   -111   -686       C  
ATOM    580  N   LEU A  94      -3.298  -8.093 -42.902  1.00 38.84           N  
ANISOU  580  N   LEU A  94     6966   3983   3807    622    119   -807       N  
ATOM    581  CA  LEU A  94      -4.017  -8.586 -44.074  1.00 37.58           C  
ANISOU  581  CA  LEU A  94     6773   3830   3675    540    182   -854       C  
ATOM    582  C   LEU A  94      -3.590  -7.824 -45.329  1.00 39.73           C  
ANISOU  582  C   LEU A  94     6901   4162   4034    595    138   -851       C  
ATOM    583  O   LEU A  94      -3.226  -8.430 -46.351  1.00 38.58           O  
ANISOU  583  O   LEU A  94     6784   3976   3900    605    151   -832       O  
ATOM    584  CB  LEU A  94      -5.528  -8.463 -43.859  1.00 37.84           C  
ANISOU  584  CB  LEU A  94     6721   3956   3701    406    251   -982       C  
ATOM    585  CG  LEU A  94      -6.451  -8.831 -45.021  1.00 42.53           C  
ANISOU  585  CG  LEU A  94     7226   4614   4319    323    305  -1089       C  
ATOM    586  CD1 LEU A  94      -6.311 -10.301 -45.377  1.00 45.88           C  
ANISOU  586  CD1 LEU A  94     7839   4903   4690    264    379  -1051       C  
ATOM    587  CD2 LEU A  94      -7.894  -8.498 -44.679  1.00 43.30           C  
ANISOU  587  CD2 LEU A  94     7181   4873   4397    228    340  -1266       C  
ATOM    588  N   VAL A  95      -3.621  -6.495 -45.234  1.00 40.83           N  
ANISOU  588  N   VAL A  95     6907   4385   4220    626     94   -870       N  
ATOM    589  CA  VAL A  95      -3.194  -5.632 -46.334  1.00 35.30           C  
ANISOU  589  CA  VAL A  95     6115   3719   3576    675     61   -856       C  
ATOM    590  C   VAL A  95      -1.770  -5.941 -46.771  1.00 34.81           C  
ANISOU  590  C   VAL A  95     6097   3605   3523    743     31   -795       C  
ATOM    591  O   VAL A  95      -1.503  -6.150 -47.953  1.00 35.15           O  
ANISOU  591  O   VAL A  95     6128   3638   3588    745     44   -791       O  
ATOM    592  CB  VAL A  95      -3.253  -4.140 -45.957  1.00 35.19           C  
ANISOU  592  CB  VAL A  95     6011   3767   3592    707     23   -869       C  
ATOM    593  CG1 VAL A  95      -3.044  -3.282 -47.184  1.00 37.08           C  
ANISOU  593  CG1 VAL A  95     6206   4020   3863    743      9   -856       C  
ATOM    594  CG2 VAL A  95      -4.567  -3.802 -45.314  1.00 41.37           C  
ANISOU  594  CG2 VAL A  95     6738   4620   4362    654     47   -953       C  
ATOM    595  N   THR A  96      -0.861  -5.964 -45.801  1.00 34.74           N  
ANISOU  595  N   THR A  96     6127   3577   3494    800    -11   -773       N  
ATOM    596  CA  THR A  96       0.560  -6.161 -46.068  1.00 39.10           C  
ANISOU  596  CA  THR A  96     6683   4115   4059    876    -47   -766       C  
ATOM    597  C   THR A  96       0.847  -7.501 -46.741  1.00 38.95           C  
ANISOU  597  C   THR A  96     6761   4027   4011    894    -29   -746       C  
ATOM    598  O   THR A  96       1.676  -7.590 -47.647  1.00 31.60           O  
ANISOU  598  O   THR A  96     5790   3101   3117    922    -31   -766       O  
ATOM    599  CB  THR A  96       1.381  -6.071 -44.769  1.00 38.77           C  
ANISOU  599  CB  THR A  96     6662   4082   3987    954   -105   -778       C  
ATOM    600  OG1 THR A  96       1.113  -4.821 -44.121  1.00 43.04           O  
ANISOU  600  OG1 THR A  96     7110   4684   4559    925   -111   -810       O  
ATOM    601  CG2 THR A  96       2.868  -6.180 -45.066  1.00 37.33           C  
ANISOU  601  CG2 THR A  96     6439   3915   3830   1037   -144   -822       C  
ATOM    602  N   ALA A  97       0.146  -8.538 -46.300  1.00 43.16           N  
ANISOU  602  N   ALA A  97     7431   4491   4477    866      4   -719       N  
ATOM    603  CA  ALA A  97       0.373  -9.883 -46.810  1.00 25.76           C  
ANISOU  603  CA  ALA A  97     5358   2197   2231    882     33   -700       C  
ATOM    604  C   ALA A  97      -0.216 -10.077 -48.202  1.00 29.57           C  
ANISOU  604  C   ALA A  97     5782   2691   2764    798     96   -732       C  
ATOM    605  O   ALA A  97       0.460 -10.582 -49.098  1.00 29.89           O  
ANISOU  605  O   ALA A  97     5826   2708   2823    832     98   -740       O  
ATOM    606  CB  ALA A  97      -0.201 -10.911 -45.850  1.00 26.89           C  
ANISOU  606  CB  ALA A  97     5710   2236   2271    859     73   -665       C  
ATOM    607  N   ILE A  98      -1.469  -9.675 -48.389  1.00 35.52           N  
ANISOU  607  N   ILE A  98     6468   3490   3537    699    141   -771       N  
ATOM    608  CA  ILE A  98      -2.160  -9.992 -49.636  1.00 34.84           C  
ANISOU  608  CA  ILE A  98     6331   3424   3482    627    196   -826       C  
ATOM    609  C   ILE A  98      -2.111  -8.876 -50.682  1.00 37.23           C  
ANISOU  609  C   ILE A  98     6487   3814   3844    647    168   -846       C  
ATOM    610  O   ILE A  98      -1.798  -9.125 -51.848  1.00 40.36           O  
ANISOU  610  O   ILE A  98     6863   4208   4262    651    183   -860       O  
ATOM    611  CB  ILE A  98      -3.632 -10.357 -49.363  1.00 37.30           C  
ANISOU  611  CB  ILE A  98     6645   3759   3770    509    266   -908       C  
ATOM    612  CG1 ILE A  98      -3.707 -11.634 -48.522  1.00 39.48           C  
ANISOU  612  CG1 ILE A  98     7127   3908   3963    461    327   -881       C  
ATOM    613  CG2 ILE A  98      -4.392 -10.538 -50.667  1.00 39.29           C  
ANISOU  613  CG2 ILE A  98     6800   4075   4053    447    306  -1008       C  
ATOM    614  CD1 ILE A  98      -5.113 -12.147 -48.302  1.00 43.28           C  
ANISOU  614  CD1 ILE A  98     7625   4410   4409    306    422   -987       C  
ATOM    615  N   CYS A  99      -2.407  -7.649 -50.267  1.00 35.95           N  
ANISOU  615  N   CYS A  99     6246   3717   3696    663    133   -846       N  
ATOM    616  CA  CYS A  99      -2.591  -6.552 -51.216  1.00 32.88           C  
ANISOU  616  CA  CYS A  99     5771   3388   3333    684    115   -858       C  
ATOM    617  C   CYS A  99      -1.297  -5.860 -51.651  1.00 34.26           C  
ANISOU  617  C   CYS A  99     5940   3547   3531    738     90   -812       C  
ATOM    618  O   CYS A  99      -1.199  -5.389 -52.784  1.00 39.64           O  
ANISOU  618  O   CYS A  99     6605   4239   4218    748     99   -815       O  
ATOM    619  CB  CYS A  99      -3.547  -5.514 -50.626  1.00 23.09           C  
ANISOU  619  CB  CYS A  99     4472   2214   2087    685     95   -890       C  
ATOM    620  SG  CYS A  99      -5.235  -6.114 -50.383  1.00 50.14           S  
ANISOU  620  SG  CYS A  99     7843   5717   5492    594    146  -1025       S  
ATOM    621  N   LEU A 100      -0.312  -5.794 -50.759  1.00 32.51           N  
ANISOU  621  N   LEU A 100     5730   3305   3316    769     66   -793       N  
ATOM    622  CA  LEU A 100       0.934  -5.081 -51.050  1.00 29.97           C  
ANISOU  622  CA  LEU A 100     5369   2988   3031    794     63   -806       C  
ATOM    623  C   LEU A 100       1.732  -5.669 -52.227  1.00 32.00           C  
ANISOU  623  C   LEU A 100     5623   3224   3312    793     95   -832       C  
ATOM    624  O   LEU A 100       2.132  -4.919 -53.118  1.00 35.72           O  
ANISOU  624  O   LEU A 100     6067   3701   3806    776    127   -854       O  
ATOM    625  CB  LEU A 100       1.817  -5.015 -49.795  1.00 25.90           C  
ANISOU  625  CB  LEU A 100     4840   2475   2524    830     29   -825       C  
ATOM    626  CG  LEU A 100       3.066  -4.124 -49.838  1.00 29.55           C  
ANISOU  626  CG  LEU A 100     5227   2959   3042    832     45   -894       C  
ATOM    627  CD1 LEU A 100       3.329  -3.517 -48.470  1.00 34.82           C  
ANISOU  627  CD1 LEU A 100     5862   3655   3713    850     14   -923       C  
ATOM    628  CD2 LEU A 100       4.296  -4.891 -50.308  1.00 30.65           C  
ANISOU  628  CD2 LEU A 100     5340   3091   3214    861     57   -959       C  
ATOM    629  N   PRO A 101       1.981  -6.997 -52.241  1.00 24.18           N  
ANISOU  629  N   PRO A 101     4678   2199   2312    811     95   -837       N  
ATOM    630  CA  PRO A 101       2.778  -7.517 -53.362  1.00 24.64           C  
ANISOU  630  CA  PRO A 101     4718   2242   2402    814    127   -882       C  
ATOM    631  C   PRO A 101       2.084  -7.358 -54.715  1.00 31.17           C  
ANISOU  631  C   PRO A 101     5540   3080   3226    767    168   -881       C  
ATOM    632  O   PRO A 101       2.738  -7.049 -55.716  1.00 33.39           O  
ANISOU  632  O   PRO A 101     5787   3366   3534    756    202   -921       O  
ATOM    633  CB  PRO A 101       2.948  -9.001 -53.016  1.00 27.08           C  
ANISOU  633  CB  PRO A 101     5110   2495   2684    855    116   -880       C  
ATOM    634  CG  PRO A 101       2.719  -9.081 -51.547  1.00 25.44           C  
ANISOU  634  CG  PRO A 101     4964   2273   2429    891     71   -840       C  
ATOM    635  CD  PRO A 101       1.666  -8.063 -51.271  1.00 24.59           C  
ANISOU  635  CD  PRO A 101     4818   2208   2317    833     75   -811       C  
ATOM    636  N   ALA A 102       0.772  -7.572 -54.733  1.00 25.07           N  
ANISOU  636  N   ALA A 102     4795   2314   2418    740    168   -859       N  
ATOM    637  CA  ALA A 102      -0.020  -7.403 -55.945  1.00 37.75           C  
ANISOU  637  CA  ALA A 102     6388   3948   4009    716    192   -880       C  
ATOM    638  C   ALA A 102       0.078  -5.970 -56.453  1.00 36.09           C  
ANISOU  638  C   ALA A 102     6170   3758   3784    739    185   -858       C  
ATOM    639  O   ALA A 102       0.265  -5.731 -57.648  1.00 25.21           O  
ANISOU  639  O   ALA A 102     4806   2379   2394    740    212   -870       O  
ATOM    640  CB  ALA A 102      -1.472  -7.780 -55.686  1.00 35.63           C  
ANISOU  640  CB  ALA A 102     6114   3709   3715    681    196   -911       C  
ATOM    641  N   SER A 103      -0.040  -5.020 -55.532  1.00 32.82           N  
ANISOU  641  N   SER A 103     5755   3351   3363    757    156   -826       N  
ATOM    642  CA  SER A 103       0.045  -3.605 -55.872  1.00 35.06           C  
ANISOU  642  CA  SER A 103     6071   3628   3621    782    158   -802       C  
ATOM    643  C   SER A 103       1.430  -3.232 -56.381  1.00 24.13           C  
ANISOU  643  C   SER A 103     4690   2209   2269    755    213   -829       C  
ATOM    644  O   SER A 103       1.561  -2.409 -57.285  1.00 24.60           O  
ANISOU  644  O   SER A 103     4814   2238   2293    757    250   -820       O  
ATOM    645  CB  SER A 103      -0.312  -2.744 -54.664  1.00 23.53           C  
ANISOU  645  CB  SER A 103     4605   2178   2156    801    122   -782       C  
ATOM    646  OG  SER A 103      -0.126  -1.369 -54.951  1.00 23.88           O  
ANISOU  646  OG  SER A 103     4709   2192   2172    823    137   -763       O  
ATOM    647  N   LEU A 104       2.461  -3.830 -55.792  1.00 23.72           N  
ANISOU  647  N   LEU A 104     4575   2160   2278    735    222   -879       N  
ATOM    648  CA  LEU A 104       3.828  -3.602 -56.245  1.00 24.32           C  
ANISOU  648  CA  LEU A 104     4608   2226   2408    702    281   -964       C  
ATOM    649  C   LEU A 104       3.991  -4.079 -57.680  1.00 39.17           C  
ANISOU  649  C   LEU A 104     6508   4096   4278    686    325   -987       C  
ATOM    650  O   LEU A 104       4.483  -3.342 -58.538  1.00 40.18           O  
ANISOU  650  O   LEU A 104     6668   4203   4396    654    387  -1019       O  
ATOM    651  CB  LEU A 104       4.831  -4.311 -55.331  1.00 24.55           C  
ANISOU  651  CB  LEU A 104     4551   2277   2502    714    266  -1043       C  
ATOM    652  CG  LEU A 104       6.285  -4.327 -55.812  1.00 25.48           C  
ANISOU  652  CG  LEU A 104     4577   2411   2694    683    330  -1192       C  
ATOM    653  CD1 LEU A 104       6.829  -2.915 -55.971  1.00 26.00           C  
ANISOU  653  CD1 LEU A 104     4618   2480   2780    622    393  -1270       C  
ATOM    654  CD2 LEU A 104       7.163  -5.140 -54.871  1.00 40.05           C  
ANISOU  654  CD2 LEU A 104     6354   4280   4584    730    304  -1271       C  
ATOM    655  N   LEU A 105       3.561  -5.313 -57.934  1.00 39.54           N  
ANISOU  655  N   LEU A 105     6551   4152   4321    703    301   -977       N  
ATOM    656  CA  LEU A 105       3.656  -5.897 -59.267  1.00 34.28           C  
ANISOU  656  CA  LEU A 105     5892   3484   3649    688    340  -1012       C  
ATOM    657  C   LEU A 105       2.893  -5.077 -60.303  1.00 36.96           C  
ANISOU  657  C   LEU A 105     6316   3816   3913    691    357   -964       C  
ATOM    658  O   LEU A 105       3.400  -4.823 -61.396  1.00 41.75           O  
ANISOU  658  O   LEU A 105     6953   4409   4503    669    414   -998       O  
ATOM    659  CB  LEU A 105       3.142  -7.338 -59.261  1.00 35.52           C  
ANISOU  659  CB  LEU A 105     6046   3641   3811    700    317  -1016       C  
ATOM    660  CG  LEU A 105       4.088  -8.381 -58.664  1.00 36.12           C  
ANISOU  660  CG  LEU A 105     6085   3698   3941    724    311  -1073       C  
ATOM    661  CD1 LEU A 105       3.482  -9.773 -58.750  1.00 39.84           C  
ANISOU  661  CD1 LEU A 105     6602   4138   4398    729    306  -1070       C  
ATOM    662  CD2 LEU A 105       5.434  -8.333 -59.369  1.00 34.70           C  
ANISOU  662  CD2 LEU A 105     5832   3531   3821    714    360  -1187       C  
ATOM    663  N   VAL A 106       1.681  -4.657 -59.954  1.00 35.26           N  
ANISOU  663  N   VAL A 106     6146   3610   3642    728    308   -897       N  
ATOM    664  CA  VAL A 106       0.863  -3.865 -60.867  1.00 36.78           C  
ANISOU  664  CA  VAL A 106     6431   3797   3746    772    303   -858       C  
ATOM    665  C   VAL A 106       1.493  -2.501 -61.138  1.00 38.52           C  
ANISOU  665  C   VAL A 106     6759   3952   3924    771    353   -825       C  
ATOM    666  O   VAL A 106       1.539  -2.044 -62.277  1.00 36.96           O  
ANISOU  666  O   VAL A 106     6670   3716   3656    785    395   -811       O  
ATOM    667  CB  VAL A 106      -0.565  -3.668 -60.320  1.00 40.59           C  
ANISOU  667  CB  VAL A 106     6913   4321   4187    831    230   -833       C  
ATOM    668  CG1 VAL A 106      -1.332  -2.658 -61.163  1.00 25.81           C  
ANISOU  668  CG1 VAL A 106     5152   2444   2211    924    204   -800       C  
ATOM    669  CG2 VAL A 106      -1.297  -4.994 -60.287  1.00 40.62           C  
ANISOU  669  CG2 VAL A 106     6830   4382   4220    803    217   -897       C  
ATOM    670  N   ASP A 107       1.993  -1.859 -60.089  1.00 40.38           N  
ANISOU  670  N   ASP A 107     6978   4167   4198    748    359   -820       N  
ATOM    671  CA  ASP A 107       2.582  -0.533 -60.231  1.00 46.23           C  
ANISOU  671  CA  ASP A 107     7830   4833   4902    724    428   -807       C  
ATOM    672  C   ASP A 107       3.921  -0.561 -60.964  1.00 44.82           C  
ANISOU  672  C   ASP A 107     7643   4627   4760    636    534   -890       C  
ATOM    673  O   ASP A 107       4.344   0.449 -61.523  1.00 46.48           O  
ANISOU  673  O   ASP A 107     7994   4755   4911    596    625   -880       O  
ATOM    674  CB  ASP A 107       2.761   0.124 -58.860  1.00 52.55           C  
ANISOU  674  CB  ASP A 107     8589   5631   5745    710    413   -814       C  
ATOM    675  CG  ASP A 107       1.452   0.608 -58.269  1.00 53.46           C  
ANISOU  675  CG  ASP A 107     8755   5757   5801    798    329   -738       C  
ATOM    676  OD1 ASP A 107       0.451   0.673 -59.015  1.00 53.29           O  
ANISOU  676  OD1 ASP A 107     8818   5736   5693    882    286   -689       O  
ATOM    677  OD2 ASP A 107       1.430   0.933 -57.061  1.00 49.77           O  
ANISOU  677  OD2 ASP A 107     8231   5306   5372    792    302   -749       O  
ATOM    678  N   ILE A 108       4.588  -1.711 -60.965  1.00 45.56           N  
ANISOU  678  N   ILE A 108     7586   4783   4940    607    529   -982       N  
ATOM    679  CA  ILE A 108       5.909  -1.791 -61.578  1.00 46.82           C  
ANISOU  679  CA  ILE A 108     7697   4948   5145    535    615  -1105       C  
ATOM    680  C   ILE A 108       5.883  -2.403 -62.985  1.00 48.39           C  
ANISOU  680  C   ILE A 108     7935   5149   5301    530    649  -1116       C  
ATOM    681  O   ILE A 108       6.799  -2.180 -63.776  1.00 52.40           O  
ANISOU  681  O   ILE A 108     8463   5646   5802    467    740  -1196       O  
ATOM    682  CB  ILE A 108       6.892  -2.594 -60.689  1.00 44.99           C  
ANISOU  682  CB  ILE A 108     7262   4796   5036    532    581  -1247       C  
ATOM    683  CG1 ILE A 108       8.340  -2.280 -61.073  1.00 46.95           C  
ANISOU  683  CG1 ILE A 108     7443   5074   5322    476    654  -1418       C  
ATOM    684  CG2 ILE A 108       6.612  -4.088 -60.764  1.00 45.49           C  
ANISOU  684  CG2 ILE A 108     7248   4900   5135    577    523  -1253       C  
ATOM    685  CD1 ILE A 108       9.355  -3.127 -60.355  1.00 50.15           C  
ANISOU  685  CD1 ILE A 108     7636   5585   5834    522    595  -1604       C  
ATOM    686  N   THR A 109       4.836  -3.160 -63.305  1.00 46.83           N  
ANISOU  686  N   THR A 109     7746   4975   5072    589    584  -1053       N  
ATOM    687  CA  THR A 109       4.751  -3.797 -64.619  1.00 43.44           C  
ANISOU  687  CA  THR A 109     7337   4561   4605    587    611  -1082       C  
ATOM    688  C   THR A 109       3.546  -3.323 -65.424  1.00 40.32           C  
ANISOU  688  C   THR A 109     7097   4139   4086    650    590   -985       C  
ATOM    689  O   THR A 109       3.430  -3.634 -66.610  1.00 41.16           O  
ANISOU  689  O   THR A 109     7246   4256   4137    653    618  -1009       O  
ATOM    690  CB  THR A 109       4.682  -5.333 -64.505  1.00 41.99           C  
ANISOU  690  CB  THR A 109     7013   4442   4498    600    563  -1147       C  
ATOM    691  OG1 THR A 109       3.503  -5.711 -63.785  1.00 42.31           O  
ANISOU  691  OG1 THR A 109     7050   4497   4530    646    483  -1076       O  
ATOM    692  CG2 THR A 109       5.909  -5.872 -63.789  1.00 27.88           C  
ANISOU  692  CG2 THR A 109     5087   2684   2823    580    567  -1261       C  
ATOM    693  N   GLU A 110       2.660  -2.575 -64.771  1.00 42.33           N  
ANISOU  693  N   GLU A 110     7424   4368   4290    715    532   -894       N  
ATOM    694  CA  GLU A 110       1.426  -2.088 -65.390  1.00 44.46           C  
ANISOU  694  CA  GLU A 110     7824   4631   4438    823    479   -825       C  
ATOM    695  C   GLU A 110       0.586  -3.232 -65.953  1.00 45.59           C  
ANISOU  695  C   GLU A 110     7868   4871   4582    856    424   -885       C  
ATOM    696  O   GLU A 110      -0.036  -3.098 -67.006  1.00 52.83           O  
ANISOU  696  O   GLU A 110     8866   5806   5399    926    411   -889       O  
ATOM    697  CB  GLU A 110       1.739  -1.068 -66.490  1.00 49.18           C  
ANISOU  697  CB  GLU A 110     8647   5128   4912    838    559   -779       C  
ATOM    698  CG  GLU A 110       2.423   0.193 -65.986  1.00 56.26           C  
ANISOU  698  CG  GLU A 110     9683   5908   5786    790    638   -727       C  
ATOM    699  CD  GLU A 110       2.700   1.190 -67.094  1.00 64.40           C  
ANISOU  699  CD  GLU A 110    10992   6803   6673    789    744   -670       C  
ATOM    700  OE1 GLU A 110       2.235   0.964 -68.231  1.00 69.69           O  
ANISOU  700  OE1 GLU A 110    11753   7478   7249    861    729   -659       O  
ATOM    701  OE2 GLU A 110       3.385   2.200 -66.825  1.00 66.31           O  
ANISOU  701  OE2 GLU A 110    11375   6929   6890    710    851   -644       O  
ATOM    702  N   SER A 111       0.572  -4.355 -65.241  1.00 39.80           N  
ANISOU  702  N   SER A 111     6971   4198   3955    805    400   -942       N  
ATOM    703  CA  SER A 111      -0.184  -5.526 -65.670  1.00 37.14           C  
ANISOU  703  CA  SER A 111     6537   3944   3630    800    377  -1024       C  
ATOM    704  C   SER A 111      -0.651  -6.356 -64.478  1.00 35.62           C  
ANISOU  704  C   SER A 111     6232   3785   3516    767    340  -1049       C  
ATOM    705  O   SER A 111      -0.018  -6.355 -63.422  1.00 35.13           O  
ANISOU  705  O   SER A 111     6148   3682   3519    741    340  -1014       O  
ATOM    706  CB  SER A 111       0.659  -6.389 -66.612  1.00 28.70           C  
ANISOU  706  CB  SER A 111     5426   2883   2595    735    443  -1104       C  
ATOM    707  OG  SER A 111       1.811  -6.885 -65.951  1.00 28.25           O  
ANISOU  707  OG  SER A 111     5299   2794   2642    676    474  -1127       O  
ATOM    708  N   TRP A 112      -1.764  -7.062 -64.654  1.00 35.70           N  
ANISOU  708  N   TRP A 112     6177   3875   3513    762    321  -1129       N  
ATOM    709  CA  TRP A 112      -2.279  -7.948 -63.615  1.00 33.89           C  
ANISOU  709  CA  TRP A 112     5864   3668   3346    707    316  -1176       C  
ATOM    710  C   TRP A 112      -1.801  -9.376 -63.856  1.00 35.93           C  
ANISOU  710  C   TRP A 112     6075   3911   3666    632    368  -1253       C  
ATOM    711  O   TRP A 112      -2.236 -10.037 -64.800  1.00 36.79           O  
ANISOU  711  O   TRP A 112     6141   4081   3756    599    398  -1361       O  
ATOM    712  CB  TRP A 112      -3.807  -7.895 -63.567  1.00 30.40           C  
ANISOU  712  CB  TRP A 112     5365   3334   2852    716    291  -1262       C  
ATOM    713  CG  TRP A 112      -4.386  -8.661 -62.420  1.00 42.44           C  
ANISOU  713  CG  TRP A 112     6819   4879   4428    637    307  -1323       C  
ATOM    714  CD1 TRP A 112      -4.970  -9.893 -62.466  1.00 42.49           C  
ANISOU  714  CD1 TRP A 112     6746   4944   4456    535    362  -1470       C  
ATOM    715  CD2 TRP A 112      -4.425  -8.249 -61.049  1.00 43.02           C  
ANISOU  715  CD2 TRP A 112     6903   4914   4527    646    276  -1254       C  
ATOM    716  NE1 TRP A 112      -5.376 -10.271 -61.207  1.00 43.80           N  
ANISOU  716  NE1 TRP A 112     6890   5102   4652    486    367  -1491       N  
ATOM    717  CE2 TRP A 112      -5.052  -9.279 -60.320  1.00 45.03           C  
ANISOU  717  CE2 TRP A 112     7098   5200   4812    551    316  -1356       C  
ATOM    718  CE3 TRP A 112      -3.994  -7.107 -60.368  1.00 28.80           C  
ANISOU  718  CE3 TRP A 112     5160   3061   2720    720    224  -1131       C  
ATOM    719  CZ2 TRP A 112      -5.256  -9.201 -58.944  1.00 42.71           C  
ANISOU  719  CZ2 TRP A 112     6810   4883   4537    533    305  -1326       C  
ATOM    720  CZ3 TRP A 112      -4.197  -7.032 -59.002  1.00 40.97           C  
ANISOU  720  CZ3 TRP A 112     6686   4591   4289    701    209  -1108       C  
ATOM    721  CH2 TRP A 112      -4.823  -8.071 -58.305  1.00 39.95           C  
ANISOU  721  CH2 TRP A 112     6505   4489   4184    610    249  -1200       C  
ATOM    722  N   LEU A 113      -0.904  -9.847 -62.995  1.00 35.17           N  
ANISOU  722  N   LEU A 113     5991   3738   3635    616    374  -1208       N  
ATOM    723  CA  LEU A 113      -0.253 -11.140 -63.190  1.00 39.82           C  
ANISOU  723  CA  LEU A 113     6571   4283   4274    583    412  -1265       C  
ATOM    724  C   LEU A 113      -0.960 -12.272 -62.455  1.00 43.21           C  
ANISOU  724  C   LEU A 113     7009   4691   4718    539    425  -1312       C  
ATOM    725  O   LEU A 113      -0.492 -13.410 -62.457  1.00 45.94           O  
ANISOU  725  O   LEU A 113     7391   4971   5094    525    454  -1346       O  
ATOM    726  CB  LEU A 113       1.205 -11.066 -62.736  1.00 26.97           C  
ANISOU  726  CB  LEU A 113     4961   2590   2695    614    412  -1218       C  
ATOM    727  CG  LEU A 113       2.029  -9.934 -63.352  1.00 26.85           C  
ANISOU  727  CG  LEU A 113     4942   2588   2671    632    423  -1198       C  
ATOM    728  CD1 LEU A 113       3.432  -9.910 -62.768  1.00 30.61           C  
ANISOU  728  CD1 LEU A 113     5389   3031   3210    649    429  -1215       C  
ATOM    729  CD2 LEU A 113       2.072 -10.071 -64.865  1.00 27.55           C  
ANISOU  729  CD2 LEU A 113     5023   2712   2732    616    464  -1268       C  
ATOM    730  N   PHE A 114      -2.087 -11.958 -61.828  1.00 46.66           N  
ANISOU  730  N   PHE A 114     7424   5179   5127    517    408  -1325       N  
ATOM    731  CA  PHE A 114      -2.829 -12.955 -61.068  1.00 51.53           C  
ANISOU  731  CA  PHE A 114     8060   5775   5742    456    433  -1385       C  
ATOM    732  C   PHE A 114      -4.093 -13.375 -61.812  1.00 62.58           C  
ANISOU  732  C   PHE A 114     9369   7303   7107    400    453  -1560       C  
ATOM    733  O   PHE A 114      -4.405 -12.836 -62.873  1.00 68.87           O  
ANISOU  733  O   PHE A 114    10081   8211   7875    416    445  -1630       O  
ATOM    734  CB  PHE A 114      -3.169 -12.416 -59.678  1.00 46.17           C  
ANISOU  734  CB  PHE A 114     7405   5082   5054    460    406  -1315       C  
ATOM    735  CG  PHE A 114      -1.976 -11.886 -58.932  1.00 40.01           C  
ANISOU  735  CG  PHE A 114     6686   4222   4292    529    369  -1175       C  
ATOM    736  CD1 PHE A 114      -1.169 -12.737 -58.196  1.00 42.54           C  
ANISOU  736  CD1 PHE A 114     7104   4436   4621    546    379  -1127       C  
ATOM    737  CD2 PHE A 114      -1.657 -10.539 -58.974  1.00 35.95           C  
ANISOU  737  CD2 PHE A 114     6140   3744   3774    584    324  -1109       C  
ATOM    738  CE1 PHE A 114      -0.069 -12.252 -57.513  1.00 43.00           C  
ANISOU  738  CE1 PHE A 114     7186   4462   4691    619    335  -1046       C  
ATOM    739  CE2 PHE A 114      -0.558 -10.051 -58.294  1.00 35.25           C  
ANISOU  739  CE2 PHE A 114     6081   3611   3703    634    294  -1025       C  
ATOM    740  CZ  PHE A 114       0.236 -10.908 -57.562  1.00 37.85           C  
ANISOU  740  CZ  PHE A 114     6466   3868   4047    652    296  -1007       C  
ATOM    741  N   GLY A 115      -4.814 -14.340 -61.252  1.00 58.73           N  
ANISOU  741  N   GLY A 115     8915   6800   6600    338    481  -1635       N  
ATOM    742  CA  GLY A 115      -5.989 -14.886 -61.905  1.00 59.26           C  
ANISOU  742  CA  GLY A 115     8910   7001   6606    309    479  -1820       C  
ATOM    743  C   GLY A 115      -7.136 -13.903 -62.042  1.00 57.23           C  
ANISOU  743  C   GLY A 115     8481   6972   6293    358    409  -1940       C  
ATOM    744  O   GLY A 115      -7.044 -12.756 -61.605  1.00 54.41           O  
ANISOU  744  O   GLY A 115     8068   6640   5966    350    413  -1875       O  
ATOM    745  N   HIS A 116      -8.222 -14.357 -62.661  1.00 58.16           N  
ANISOU  745  N   HIS A 116     8596   7202   6299    414    351  -2034       N  
ATOM    746  CA  HIS A 116      -9.416 -13.537 -62.809  1.00 56.62           C  
ANISOU  746  CA  HIS A 116     8430   7123   5959    571    235  -2004       C  
ATOM    747  C   HIS A 116     -10.145 -13.429 -61.475  1.00 53.02           C  
ANISOU  747  C   HIS A 116     8061   6627   5458    516    265  -1997       C  
ATOM    748  O   HIS A 116     -10.815 -12.434 -61.199  1.00 53.16           O  
ANISOU  748  O   HIS A 116     8291   6556   5350    537    289  -1853       O  
ATOM    749  CB  HIS A 116     -10.349 -14.118 -63.877  1.00 63.65           C  
ANISOU  749  CB  HIS A 116     9599   7939   6647    489    355  -2035       C  
ATOM    750  CG  HIS A 116      -9.757 -14.142 -65.252  1.00 72.54           C  
ANISOU  750  CG  HIS A 116    10784   9030   7749    539    359  -1980       C  
ATOM    751  ND1 HIS A 116      -8.685 -14.940 -65.588  1.00 75.10           N  
ANISOU  751  ND1 HIS A 116    10909   9403   8222    561    311  -2069       N  
ATOM    752  CD2 HIS A 116     -10.093 -13.471 -66.379  1.00 73.53           C  
ANISOU  752  CD2 HIS A 116    11007   9145   7784    381    523  -1968       C  
ATOM    753  CE1 HIS A 116      -8.384 -14.758 -66.862  1.00 74.99           C  
ANISOU  753  CE1 HIS A 116    10958   9390   8146    643    291  -2020       C  
ATOM    754  NE2 HIS A 116      -9.223 -13.871 -67.365  1.00 73.53           N  
ANISOU  754  NE2 HIS A 116    11066   9074   7799    423    523  -1910       N  
ATOM    755  N   ALA A 117     -10.001 -14.461 -60.650  1.00 39.48           N  
ANISOU  755  N   ALA A 117     7317   4717   2966   -422    358  -1268       N  
ATOM    756  CA  ALA A 117     -10.653 -14.502 -59.346  1.00 44.03           C  
ANISOU  756  CA  ALA A 117     7838   5315   3578   -519    373  -1274       C  
ATOM    757  C   ALA A 117      -9.984 -13.554 -58.357  1.00 43.91           C  
ANISOU  757  C   ALA A 117     7765   5285   3634   -490    429  -1191       C  
ATOM    758  O   ALA A 117     -10.661 -12.815 -57.643  1.00 37.40           O  
ANISOU  758  O   ALA A 117     6840   4538   2831   -509    429  -1208       O  
ATOM    759  CB  ALA A 117     -10.653 -15.921 -58.802  1.00 47.84           C  
ANISOU  759  CB  ALA A 117     8423   5698   4055   -633    388  -1270       C  
ATOM    760  N   LEU A 118      -8.654 -13.579 -58.318  1.00 48.01           N  
ANISOU  760  N   LEU A 118     8349   5705   4186   -442    474  -1106       N  
ATOM    761  CA  LEU A 118      -7.903 -12.700 -57.427  1.00 43.22           C  
ANISOU  761  CA  LEU A 118     7692   5081   3648   -410    522  -1034       C  
ATOM    762  C   LEU A 118      -8.053 -11.242 -57.846  1.00 46.36           C  
ANISOU  762  C   LEU A 118     7987   5570   4058   -323    515  -1043       C  
ATOM    763  O   LEU A 118      -7.856 -10.331 -57.037  1.00 50.95           O  
ANISOU  763  O   LEU A 118     8496   6171   4692   -310    543  -1010       O  
ATOM    764  CB  LEU A 118      -6.425 -13.094 -57.394  1.00 36.67           C  
ANISOU  764  CB  LEU A 118     6959   4129   2846   -370    563   -948       C  
ATOM    765  CG  LEU A 118      -6.102 -14.370 -56.613  1.00 33.50           C  
ANISOU  765  CG  LEU A 118     6652   3631   2444   -449    586   -919       C  
ATOM    766  CD1 LEU A 118      -4.601 -14.592 -56.540  1.00 33.05           C  
ANISOU  766  CD1 LEU A 118     6675   3468   2413   -389    624   -835       C  
ATOM    767  CD2 LEU A 118      -6.704 -14.307 -55.219  1.00 33.16           C  
ANISOU  767  CD2 LEU A 118     6548   3618   2433   -536    604   -925       C  
ATOM    768  N   CYS A 119      -8.407 -11.032 -59.111  1.00 46.17           N  
ANISOU  768  N   CYS A 119     7962   5600   3981   -262    479  -1089       N  
ATOM    769  CA  CYS A 119      -8.716  -9.701 -59.624  1.00 43.03           C  
ANISOU  769  CA  CYS A 119     7472   5299   3578   -180    472  -1107       C  
ATOM    770  C   CYS A 119      -9.911  -9.111 -58.883  1.00 40.14           C  
ANISOU  770  C   CYS A 119     6992   5047   3212   -216    451  -1160       C  
ATOM    771  O   CYS A 119     -10.024  -7.895 -58.727  1.00 31.06           O  
ANISOU  771  O   CYS A 119     5758   3960   2082   -163    465  -1150       O  
ATOM    772  CB  CYS A 119      -8.992  -9.755 -61.129  1.00 44.64           C  
ANISOU  772  CB  CYS A 119     7704   5546   3710   -116    434  -1155       C  
ATOM    773  SG  CYS A 119      -9.531  -8.188 -61.855  1.00 58.44           S  
ANISOU  773  SG  CYS A 119     9347   7426   5433    -18    428  -1185       S  
ATOM    774  N   LYS A 120     -10.805  -9.982 -58.430  1.00 33.60           N  
ANISOU  774  N   LYS A 120     6170   4238   2360   -308    420  -1212       N  
ATOM    775  CA  LYS A 120     -11.943  -9.561 -57.625  1.00 33.59           C  
ANISOU  775  CA  LYS A 120     6076   4327   2358   -350    403  -1255       C  
ATOM    776  C   LYS A 120     -11.605  -9.597 -56.139  1.00 40.53           C  
ANISOU  776  C   LYS A 120     6949   5144   3304   -422    454  -1194       C  
ATOM    777  O   LYS A 120     -11.954  -8.685 -55.391  1.00 41.23           O  
ANISOU  777  O   LYS A 120     6956   5288   3422   -413    468  -1185       O  
ATOM    778  CB  LYS A 120     -13.158 -10.448 -57.905  1.00 34.79           C  
ANISOU  778  CB  LYS A 120     6239   4530   2450   -419    343  -1346       C  
ATOM    779  CG  LYS A 120     -13.869 -10.145 -59.213  1.00 35.69           C  
ANISOU  779  CG  LYS A 120     6320   4754   2488   -338    275  -1430       C  
ATOM    780  CD  LYS A 120     -15.072 -11.055 -59.405  1.00 36.99           C  
ANISOU  780  CD  LYS A 120     6497   4960   2597   -414    207  -1527       C  
ATOM    781  CE  LYS A 120     -16.130 -10.401 -60.279  1.00 46.96           C  
ANISOU  781  CE  LYS A 120     7688   6368   3785   -325    129  -1617       C  
ATOM    782  NZ  LYS A 120     -15.586  -9.956 -61.590  1.00 50.27           N  
ANISOU  782  NZ  LYS A 120     8104   6835   4161   -206    119  -1630       N  
ATOM    783  N   VAL A 121     -10.915 -10.654 -55.722  1.00 30.98           N  
ANISOU  783  N   VAL A 121     5831   3823   2116   -487    482  -1154       N  
ATOM    784  CA  VAL A 121     -10.619 -10.881 -54.310  1.00 36.46           C  
ANISOU  784  CA  VAL A 121     6531   4461   2862   -560    529  -1104       C  
ATOM    785  C   VAL A 121      -9.728  -9.802 -53.694  1.00 41.20           C  
ANISOU  785  C   VAL A 121     7083   5046   3525   -498    569  -1039       C  
ATOM    786  O   VAL A 121     -10.082  -9.217 -52.670  1.00 39.71           O  
ANISOU  786  O   VAL A 121     6825   4894   3367   -523    586  -1033       O  
ATOM    787  CB  VAL A 121      -9.950 -12.258 -54.102  1.00 30.72           C  
ANISOU  787  CB  VAL A 121     5925   3614   2133   -624    553  -1070       C  
ATOM    788  CG1 VAL A 121      -9.398 -12.381 -52.689  1.00 30.05           C  
ANISOU  788  CG1 VAL A 121     5849   3469   2099   -670    605  -1010       C  
ATOM    789  CG2 VAL A 121     -10.937 -13.377 -54.387  1.00 31.89           C  
ANISOU  789  CG2 VAL A 121     6120   3770   2228   -716    522  -1137       C  
ATOM    790  N   ILE A 122      -8.581  -9.535 -54.315  1.00 30.35           N  
ANISOU  790  N   ILE A 122     5747   3617   2168   -419    583   -994       N  
ATOM    791  CA  ILE A 122      -7.586  -8.641 -53.716  1.00 29.39           C  
ANISOU  791  CA  ILE A 122     5592   3464   2109   -370    622   -934       C  
ATOM    792  C   ILE A 122      -8.066  -7.183 -53.536  1.00 33.71           C  
ANISOU  792  C   ILE A 122     6028   4104   2677   -322    621   -949       C  
ATOM    793  O   ILE A 122      -7.919  -6.625 -52.443  1.00 32.34           O  
ANISOU  793  O   ILE A 122     5805   3932   2549   -337    645   -926       O  
ATOM    794  CB  ILE A 122      -6.266  -8.664 -54.530  1.00 29.22           C  
ANISOU  794  CB  ILE A 122     5640   3364   2099   -295    639   -883       C  
ATOM    795  CG1 ILE A 122      -5.642 -10.061 -54.477  1.00 29.59           C  
ANISOU  795  CG1 ILE A 122     5802   3310   2131   -335    647   -855       C  
ATOM    796  CG2 ILE A 122      -5.290  -7.619 -54.008  1.00 28.33           C  
ANISOU  796  CG2 ILE A 122     5484   3230   2051   -243    675   -832       C  
ATOM    797  CD1 ILE A 122      -4.334 -10.183 -55.223  1.00 29.49           C  
ANISOU  797  CD1 ILE A 122     5866   3215   2125   -259    665   -802       C  
ATOM    798  N   PRO A 123      -8.649  -6.561 -54.583  1.00 35.85           N  
ANISOU  798  N   PRO A 123     6262   4453   2909   -260    594   -989       N  
ATOM    799  CA  PRO A 123      -9.147  -5.197 -54.353  1.00 36.75           C  
ANISOU  799  CA  PRO A 123     6275   4652   3035   -213    597  -1001       C  
ATOM    800  C   PRO A 123     -10.288  -5.146 -53.336  1.00 34.15           C  
ANISOU  800  C   PRO A 123     5884   4390   2700   -274    584  -1035       C  
ATOM    801  O   PRO A 123     -10.418  -4.170 -52.585  1.00 38.94           O  
ANISOU  801  O   PRO A 123     6424   5032   3340   -257    602  -1023       O  
ATOM    802  CB  PRO A 123      -9.638  -4.766 -55.739  1.00 43.96           C  
ANISOU  802  CB  PRO A 123     7173   5640   3889   -138    567  -1044       C  
ATOM    803  CG  PRO A 123      -8.884  -5.624 -56.692  1.00 30.81           C  
ANISOU  803  CG  PRO A 123     5605   3897   2205   -125    565  -1028       C  
ATOM    804  CD  PRO A 123      -8.780  -6.944 -56.000  1.00 30.96           C  
ANISOU  804  CD  PRO A 123     5688   3846   2231   -218    563  -1021       C  
ATOM    805  N   TYR A 124     -11.106  -6.195 -53.323  1.00 29.44           N  
ANISOU  805  N   TYR A 124     5316   3807   2061   -347    556  -1077       N  
ATOM    806  CA  TYR A 124     -12.171  -6.330 -52.338  1.00 39.11           C  
ANISOU  806  CA  TYR A 124     6498   5080   3280   -424    553  -1105       C  
ATOM    807  C   TYR A 124     -11.595  -6.292 -50.929  1.00 41.71           C  
ANISOU  807  C   TYR A 124     6824   5350   3674   -474    599  -1052       C  
ATOM    808  O   TYR A 124     -12.034  -5.503 -50.090  1.00 44.50           O  
ANISOU  808  O   TYR A 124     7109   5752   4048   -474    612  -1050       O  
ATOM    809  CB  TYR A 124     -12.949  -7.629 -52.562  1.00 37.82           C  
ANISOU  809  CB  TYR A 124     6385   4915   3069   -514    524  -1154       C  
ATOM    810  CG  TYR A 124     -13.911  -7.978 -51.448  1.00 37.99           C  
ANISOU  810  CG  TYR A 124     6377   4963   3093   -621    536  -1173       C  
ATOM    811  CD1 TYR A 124     -15.086  -7.259 -51.266  1.00 35.85           C  
ANISOU  811  CD1 TYR A 124     6026   4798   2799   -615    516  -1213       C  
ATOM    812  CD2 TYR A 124     -13.651  -9.035 -50.584  1.00 37.35           C  
ANISOU  812  CD2 TYR A 124     6355   4801   3034   -727    570  -1148       C  
ATOM    813  CE1 TYR A 124     -15.971  -7.576 -50.252  1.00 31.89           C  
ANISOU  813  CE1 TYR A 124     5494   4322   2300   -721    534  -1229       C  
ATOM    814  CE2 TYR A 124     -14.530  -9.360 -49.568  1.00 36.56           C  
ANISOU  814  CE2 TYR A 124     6230   4727   2935   -830    590  -1165       C  
ATOM    815  CZ  TYR A 124     -15.688  -8.627 -49.408  1.00 33.98           C  
ANISOU  815  CZ  TYR A 124     5814   4508   2589   -831    573  -1206       C  
ATOM    816  OH  TYR A 124     -16.566  -8.947 -48.398  1.00 31.60           O  
ANISOU  816  OH  TYR A 124     5483   4234   2288   -938    599  -1222       O  
ATOM    817  N   LEU A 125     -10.599  -7.139 -50.685  1.00 40.43           N  
ANISOU  817  N   LEU A 125     6740   5086   3537   -507    623  -1011       N  
ATOM    818  CA  LEU A 125      -9.939  -7.199 -49.387  1.00 39.12           C  
ANISOU  818  CA  LEU A 125     6580   4862   3422   -543    662   -964       C  
ATOM    819  C   LEU A 125      -9.266  -5.875 -49.046  1.00 37.94           C  
ANISOU  819  C   LEU A 125     6370   4724   3323   -467    679   -933       C  
ATOM    820  O   LEU A 125      -9.166  -5.512 -47.875  1.00 28.07           O  
ANISOU  820  O   LEU A 125     5085   3473   2108   -487    700   -916       O  
ATOM    821  CB  LEU A 125      -8.915  -8.337 -49.354  1.00 38.46           C  
ANISOU  821  CB  LEU A 125     6599   4669   3344   -569    680   -925       C  
ATOM    822  CG  LEU A 125      -9.487  -9.745 -49.529  1.00 41.31           C  
ANISOU  822  CG  LEU A 125     7037   4999   3659   -657    672   -950       C  
ATOM    823  CD1 LEU A 125      -8.416 -10.799 -49.281  1.00 42.58           C  
ANISOU  823  CD1 LEU A 125     7306   5047   3826   -675    697   -902       C  
ATOM    824  CD2 LEU A 125     -10.690  -9.959 -48.618  1.00 30.57           C  
ANISOU  824  CD2 LEU A 125     5638   3690   2287   -750    679   -983       C  
ATOM    825  N   GLN A 126      -8.809  -5.157 -50.070  1.00 38.16           N  
ANISOU  825  N   GLN A 126     6387   4760   3350   -382    671   -928       N  
ATOM    826  CA  GLN A 126      -8.252  -3.821 -49.878  1.00 28.70           C  
ANISOU  826  CA  GLN A 126     5133   3575   2197   -313    690   -905       C  
ATOM    827  C   GLN A 126      -9.305  -2.887 -49.282  1.00 39.85           C  
ANISOU  827  C   GLN A 126     6457   5077   3605   -310    685   -933       C  
ATOM    828  O   GLN A 126      -9.095  -2.282 -48.219  1.00 41.77           O  
ANISOU  828  O   GLN A 126     6661   5318   3890   -315    706   -916       O  
ATOM    829  CB  GLN A 126      -7.730  -3.262 -51.205  1.00 29.47           C  
ANISOU  829  CB  GLN A 126     5242   3669   2287   -229    689   -898       C  
ATOM    830  CG  GLN A 126      -7.096  -1.887 -51.101  1.00 33.72           C  
ANISOU  830  CG  GLN A 126     5732   4207   2872   -165    716   -873       C  
ATOM    831  CD  GLN A 126      -5.691  -1.930 -50.532  1.00 36.43           C  
ANISOU  831  CD  GLN A 126     6107   4462   3272   -166    747   -825       C  
ATOM    832  OE1 GLN A 126      -4.787  -2.519 -51.125  1.00 32.01           O  
ANISOU  832  OE1 GLN A 126     5615   3834   2714   -151    756   -797       O  
ATOM    833  NE2 GLN A 126      -5.499  -1.302 -49.378  1.00 40.86           N  
ANISOU  833  NE2 GLN A 126     6620   5029   3877   -179    763   -817       N  
ATOM    834  N   ALA A 127     -10.444  -2.791 -49.966  1.00 27.32           N  
ANISOU  834  N   ALA A 127     4844   3574   1964   -295    655   -979       N  
ATOM    835  CA  ALA A 127     -11.546  -1.943 -49.514  1.00 27.39           C  
ANISOU  835  CA  ALA A 127     4776   3674   1955   -281    648  -1006       C  
ATOM    836  C   ALA A 127     -12.002  -2.311 -48.102  1.00 38.70           C  
ANISOU  836  C   ALA A 127     6194   5104   3407   -367    664  -1003       C  
ATOM    837  O   ALA A 127     -12.109  -1.445 -47.222  1.00 43.25           O  
ANISOU  837  O   ALA A 127     6717   5703   4011   -353    682   -992       O  
ATOM    838  CB  ALA A 127     -12.710  -2.039 -50.483  1.00 28.14           C  
ANISOU  838  CB  ALA A 127     4858   3859   1977   -254    608  -1060       C  
ATOM    839  N   VAL A 128     -12.257  -3.601 -47.896  1.00 35.13           N  
ANISOU  839  N   VAL A 128     5790   4620   2936   -457    660  -1013       N  
ATOM    840  CA  VAL A 128     -12.686  -4.111 -46.596  1.00 34.93           C  
ANISOU  840  CA  VAL A 128     5761   4588   2924   -548    683  -1011       C  
ATOM    841  C   VAL A 128     -11.694  -3.737 -45.500  1.00 36.29           C  
ANISOU  841  C   VAL A 128     5930   4706   3154   -539    714   -966       C  
ATOM    842  O   VAL A 128     -12.086  -3.292 -44.421  1.00 36.00           O  
ANISOU  842  O   VAL A 128     5848   4698   3131   -557    730   -965       O  
ATOM    843  CB  VAL A 128     -12.854  -5.645 -46.613  1.00 34.20           C  
ANISOU  843  CB  VAL A 128     5741   4448   2806   -647    683  -1022       C  
ATOM    844  CG1 VAL A 128     -13.200  -6.160 -45.224  1.00 29.23           C  
ANISOU  844  CG1 VAL A 128     5113   3804   2189   -738    716  -1013       C  
ATOM    845  CG2 VAL A 128     -13.922  -6.053 -47.608  1.00 37.74           C  
ANISOU  845  CG2 VAL A 128     6188   4957   3194   -668    647  -1078       C  
ATOM    846  N   SER A 129     -10.410  -3.913 -45.792  1.00 35.15           N  
ANISOU  846  N   SER A 129     5833   4483   3038   -506    720   -932       N  
ATOM    847  CA  SER A 129      -9.356  -3.596 -44.839  1.00 32.01           C  
ANISOU  847  CA  SER A 129     5436   4036   2691   -490    744   -896       C  
ATOM    848  C   SER A 129      -9.367  -2.122 -44.453  1.00 32.37           C  
ANISOU  848  C   SER A 129     5405   4129   2767   -429    749   -897       C  
ATOM    849  O   SER A 129      -9.288  -1.787 -43.265  1.00 36.08           O  
ANISOU  849  O   SER A 129     5847   4602   3260   -441    763   -890       O  
ATOM    850  CB  SER A 129      -7.992  -3.971 -45.408  1.00 31.02           C  
ANISOU  850  CB  SER A 129     5372   3830   2585   -455    748   -863       C  
ATOM    851  OG  SER A 129      -7.881  -5.373 -45.581  1.00 37.18           O  
ANISOU  851  OG  SER A 129     6234   4554   3338   -510    748   -857       O  
ATOM    852  N   VAL A 130      -9.462  -1.248 -45.455  1.00 32.69           N  
ANISOU  852  N   VAL A 130     5416   4203   2800   -361    738   -906       N  
ATOM    853  CA  VAL A 130      -9.563   0.186 -45.187  1.00 34.71           C  
ANISOU  853  CA  VAL A 130     5606   4503   3079   -302    747   -908       C  
ATOM    854  C   VAL A 130     -10.737   0.464 -44.251  1.00 36.81           C  
ANISOU  854  C   VAL A 130     5823   4837   3327   -331    747   -929       C  
ATOM    855  O   VAL A 130     -10.586   1.141 -43.223  1.00 35.93           O  
ANISOU  855  O   VAL A 130     5678   4729   3245   -323    762   -921       O  
ATOM    856  CB  VAL A 130      -9.734   1.004 -46.483  1.00 36.18           C  
ANISOU  856  CB  VAL A 130     5774   4727   3245   -225    738   -918       C  
ATOM    857  CG1 VAL A 130      -9.918   2.480 -46.157  1.00 31.64           C  
ANISOU  857  CG1 VAL A 130     5139   4195   2689   -166    753   -920       C  
ATOM    858  CG2 VAL A 130      -8.537   0.802 -47.399  1.00 41.86           C  
ANISOU  858  CG2 VAL A 130     6544   5377   3984   -195    746   -894       C  
ATOM    859  N   SER A 131     -11.896  -0.091 -44.601  1.00 37.01           N  
ANISOU  859  N   SER A 131     5846   4915   3301   -366    731   -957       N  
ATOM    860  CA  SER A 131     -13.104   0.058 -43.787  1.00 36.96           C  
ANISOU  860  CA  SER A 131     5795   4977   3271   -401    736   -978       C  
ATOM    861  C   SER A 131     -12.879  -0.340 -42.328  1.00 33.47           C  
ANISOU  861  C   SER A 131     5359   4502   2858   -463    759   -962       C  
ATOM    862  O   SER A 131     -13.157   0.439 -41.410  1.00 30.21           O  
ANISOU  862  O   SER A 131     4901   4120   2456   -446    772   -961       O  
ATOM    863  CB  SER A 131     -14.246  -0.772 -44.378  1.00 39.97           C  
ANISOU  863  CB  SER A 131     6185   5408   3595   -453    717  -1013       C  
ATOM    864  OG  SER A 131     -15.412  -0.672 -43.580  1.00 39.77           O  
ANISOU  864  OG  SER A 131     6114   5449   3547   -497    727  -1032       O  
ATOM    865  N   VAL A 132     -12.373  -1.554 -42.125  1.00 27.41           N  
ANISOU  865  N   VAL A 132     4652   3669   2094   -527    765   -951       N  
ATOM    866  CA  VAL A 132     -12.110  -2.083 -40.789  1.00 27.36           C  
ANISOU  866  CA  VAL A 132     4664   3627   2103   -579    787   -936       C  
ATOM    867  C   VAL A 132     -11.182  -1.167 -39.998  1.00 34.33           C  
ANISOU  867  C   VAL A 132     5524   4489   3029   -520    795   -916       C  
ATOM    868  O   VAL A 132     -11.436  -0.874 -38.826  1.00 35.35           O  
ANISOU  868  O   VAL A 132     5628   4641   3164   -528    808   -917       O  
ATOM    869  CB  VAL A 132     -11.488  -3.496 -40.856  1.00 30.98           C  
ANISOU  869  CB  VAL A 132     5207   4006   2556   -636    793   -920       C  
ATOM    870  CG1 VAL A 132     -11.042  -3.958 -39.476  1.00 31.88           C  
ANISOU  870  CG1 VAL A 132     5350   4081   2683   -665    817   -901       C  
ATOM    871  CG2 VAL A 132     -12.473  -4.483 -41.455  1.00 28.22           C  
ANISOU  871  CG2 VAL A 132     4886   3675   2162   -712    789   -946       C  
ATOM    872  N   ALA A 133     -10.113  -0.711 -40.648  1.00 32.32           N  
ANISOU  872  N   ALA A 133     5279   4196   2805   -461    787   -900       N  
ATOM    873  CA  ALA A 133      -9.163   0.196 -40.008  1.00 30.86           C  
ANISOU  873  CA  ALA A 133     5071   3993   2663   -409    794   -888       C  
ATOM    874  C   ALA A 133      -9.845   1.471 -39.517  1.00 26.92           C  
ANISOU  874  C   ALA A 133     4505   3557   2167   -372    798   -904       C  
ATOM    875  O   ALA A 133      -9.749   1.827 -38.331  1.00 33.48           O  
ANISOU  875  O   ALA A 133     5315   4395   3009   -369    806   -905       O  
ATOM    876  CB  ALA A 133      -8.032   0.542 -40.968  1.00 28.67           C  
ANISOU  876  CB  ALA A 133     4809   3670   2414   -359    791   -873       C  
ATOM    877  N   VAL A 134     -10.537   2.151 -40.430  1.00 24.61           N  
ANISOU  877  N   VAL A 134     4181   3311   1857   -336    791   -916       N  
ATOM    878  CA  VAL A 134     -11.189   3.416 -40.097  1.00 24.62           C  
ANISOU  878  CA  VAL A 134     4126   3372   1856   -288    797   -928       C  
ATOM    879  C   VAL A 134     -12.213   3.248 -38.977  1.00 37.39           C  
ANISOU  879  C   VAL A 134     5720   5038   3447   -327    805   -939       C  
ATOM    880  O   VAL A 134     -12.222   4.015 -38.010  1.00 36.61           O  
ANISOU  880  O   VAL A 134     5592   4955   3361   -301    816   -941       O  
ATOM    881  CB  VAL A 134     -11.889   4.034 -41.320  1.00 24.82           C  
ANISOU  881  CB  VAL A 134     4132   3449   1851   -235    789   -939       C  
ATOM    882  CG1 VAL A 134     -12.427   5.399 -40.972  1.00 28.67           C  
ANISOU  882  CG1 VAL A 134     4569   3989   2334   -172    800   -946       C  
ATOM    883  CG2 VAL A 134     -10.928   4.147 -42.482  1.00 56.58           C  
ANISOU  883  CG2 VAL A 134     8181   7425   5893   -197    785   -928       C  
ATOM    884  N   LEU A 135     -13.068   2.238 -39.110  1.00 39.74           N  
ANISOU  884  N   LEU A 135     6031   5360   3708   -390    803   -949       N  
ATOM    885  CA  LEU A 135     -14.095   1.971 -38.106  1.00 27.04           C  
ANISOU  885  CA  LEU A 135     4401   3800   2072   -438    819   -960       C  
ATOM    886  C   LEU A 135     -13.486   1.663 -36.742  1.00 33.95           C  
ANISOU  886  C   LEU A 135     5296   4636   2967   -460    833   -948       C  
ATOM    887  O   LEU A 135     -14.012   2.086 -35.711  1.00 35.08           O  
ANISOU  887  O   LEU A 135     5410   4818   3100   -454    848   -952       O  
ATOM    888  CB  LEU A 135     -14.992   0.817 -38.552  1.00 29.82           C  
ANISOU  888  CB  LEU A 135     4770   4175   2383   -518    818   -977       C  
ATOM    889  CG  LEU A 135     -15.985   1.136 -39.670  1.00 30.68           C  
ANISOU  889  CG  LEU A 135     4849   4355   2453   -497    802  -1000       C  
ATOM    890  CD1 LEU A 135     -16.692  -0.127 -40.137  1.00 31.54           C  
ANISOU  890  CD1 LEU A 135     4982   4478   2525   -588    798  -1024       C  
ATOM    891  CD2 LEU A 135     -16.990   2.177 -39.202  1.00 30.56           C  
ANISOU  891  CD2 LEU A 135     4772   4424   2416   -455    815  -1009       C  
ATOM    892  N   THR A 136     -12.378   0.928 -36.741  1.00 26.28           N  
ANISOU  892  N   THR A 136     4376   3591   2018   -477    829   -932       N  
ATOM    893  CA  THR A 136     -11.678   0.610 -35.501  1.00 26.21           C  
ANISOU  893  CA  THR A 136     4392   3546   2021   -483    838   -921       C  
ATOM    894  C   THR A 136     -11.165   1.880 -34.828  1.00 38.88           C  
ANISOU  894  C   THR A 136     5958   5163   3651   -411    835   -925       C  
ATOM    895  O   THR A 136     -11.338   2.068 -33.615  1.00 41.44           O  
ANISOU  895  O   THR A 136     6272   5509   3965   -403    844   -929       O  
ATOM    896  CB  THR A 136     -10.503  -0.350 -35.746  1.00 26.07           C  
ANISOU  896  CB  THR A 136     4439   3450   2017   -497    833   -903       C  
ATOM    897  OG1 THR A 136     -11.002  -1.596 -36.247  1.00 26.45           O  
ANISOU  897  OG1 THR A 136     4534   3479   2037   -569    839   -901       O  
ATOM    898  CG2 THR A 136      -9.748  -0.601 -34.456  1.00 26.07           C  
ANISOU  898  CG2 THR A 136     4462   3422   2020   -484    839   -895       C  
ATOM    899  N   LEU A 137     -10.542   2.753 -35.618  1.00 36.59           N  
ANISOU  899  N   LEU A 137     5650   4860   3393   -359    824   -924       N  
ATOM    900  CA  LEU A 137     -10.095   4.043 -35.099  1.00 24.84           C  
ANISOU  900  CA  LEU A 137     4126   3381   1931   -297    825   -932       C  
ATOM    901  C   LEU A 137     -11.271   4.834 -34.528  1.00 25.10           C  
ANISOU  901  C   LEU A 137     4117   3483   1938   -278    835   -945       C  
ATOM    902  O   LEU A 137     -11.140   5.514 -33.506  1.00 25.13           O  
ANISOU  902  O   LEU A 137     4103   3500   1946   -245    839   -954       O  
ATOM    903  CB  LEU A 137      -9.392   4.855 -36.188  1.00 24.53           C  
ANISOU  903  CB  LEU A 137     4078   3317   1926   -253    821   -930       C  
ATOM    904  CG  LEU A 137      -8.058   4.301 -36.695  1.00 31.48           C  
ANISOU  904  CG  LEU A 137     4996   4131   2835   -258    815   -916       C  
ATOM    905  CD1 LEU A 137      -7.383   5.289 -37.636  1.00 36.35           C  
ANISOU  905  CD1 LEU A 137     5600   4726   3487   -211    821   -915       C  
ATOM    906  CD2 LEU A 137      -7.143   3.953 -35.532  1.00 24.25           C  
ANISOU  906  CD2 LEU A 137     4095   3189   1929   -259    811   -919       C  
ATOM    907  N   SER A 138     -12.422   4.729 -35.188  1.00 25.85           N  
ANISOU  907  N   SER A 138     4196   3625   2002   -293    839   -948       N  
ATOM    908  CA  SER A 138     -13.629   5.417 -34.737  1.00 34.62           C  
ANISOU  908  CA  SER A 138     5266   4809   3081   -270    852   -958       C  
ATOM    909  C   SER A 138     -14.119   4.888 -33.393  1.00 31.80           C  
ANISOU  909  C   SER A 138     4912   4473   2698   -307    867   -960       C  
ATOM    910  O   SER A 138     -14.565   5.659 -32.542  1.00 29.79           O  
ANISOU  910  O   SER A 138     4631   4258   2430   -268    879   -965       O  
ATOM    911  CB  SER A 138     -14.739   5.293 -35.782  1.00 35.71           C  
ANISOU  911  CB  SER A 138     5386   4998   3182   -279    851   -963       C  
ATOM    912  OG  SER A 138     -14.427   6.041 -36.943  1.00 41.14           O  
ANISOU  912  OG  SER A 138     6069   5680   3881   -220    840   -962       O  
ATOM    913  N   PHE A 139     -14.038   3.575 -33.201  1.00 29.64           N  
ANISOU  913  N   PHE A 139     4676   4173   2415   -376    870   -954       N  
ATOM    914  CA  PHE A 139     -14.452   2.981 -31.934  1.00 36.44           C  
ANISOU  914  CA  PHE A 139     5549   5050   3248   -410    891   -954       C  
ATOM    915  C   PHE A 139     -13.476   3.338 -30.818  1.00 39.35           C  
ANISOU  915  C   PHE A 139     5931   5389   3630   -362    886   -952       C  
ATOM    916  O   PHE A 139     -13.879   3.516 -29.664  1.00 42.82           O  
ANISOU  916  O   PHE A 139     6364   5863   4044   -344    901   -956       O  
ATOM    917  CB  PHE A 139     -14.588   1.464 -32.067  1.00 38.28           C  
ANISOU  917  CB  PHE A 139     5828   5252   3463   -497    901   -948       C  
ATOM    918  CG  PHE A 139     -15.966   1.016 -32.468  1.00 43.11           C  
ANISOU  918  CG  PHE A 139     6420   5922   4039   -560    919   -959       C  
ATOM    919  CD1 PHE A 139     -16.361   1.052 -33.797  1.00 39.41           C  
ANISOU  919  CD1 PHE A 139     5933   5473   3569   -573    904   -970       C  
ATOM    920  CD2 PHE A 139     -16.868   0.565 -31.517  1.00 43.07           C  
ANISOU  920  CD2 PHE A 139     6411   5958   3997   -605    953   -962       C  
ATOM    921  CE1 PHE A 139     -17.628   0.646 -34.172  1.00 33.65           C  
ANISOU  921  CE1 PHE A 139     5178   4807   2802   -632    917   -989       C  
ATOM    922  CE2 PHE A 139     -18.136   0.157 -31.886  1.00 40.53           C  
ANISOU  922  CE2 PHE A 139     6061   5696   3642   -671    973   -977       C  
ATOM    923  CZ  PHE A 139     -18.516   0.198 -33.217  1.00 38.48           C  
ANISOU  923  CZ  PHE A 139     5779   5460   3381   -687    953   -993       C  
ATOM    924  N   ILE A 140     -12.195   3.446 -31.160  1.00 28.48           N  
ANISOU  924  N   ILE A 140     4573   3957   2292   -337    865   -950       N  
ATOM    925  CA  ILE A 140     -11.204   3.939 -30.206  1.00 29.16           C  
ANISOU  925  CA  ILE A 140     4663   4025   2392   -284    854   -958       C  
ATOM    926  C   ILE A 140     -11.555   5.353 -29.756  1.00 27.75           C  
ANISOU  926  C   ILE A 140     4440   3889   2214   -222    856   -974       C  
ATOM    927  O   ILE A 140     -11.618   5.644 -28.555  1.00 31.77           O  
ANISOU  927  O   ILE A 140     4947   4423   2700   -189    859   -985       O  
ATOM    928  CB  ILE A 140      -9.787   3.943 -30.804  1.00 31.19           C  
ANISOU  928  CB  ILE A 140     4937   4223   2691   -267    833   -957       C  
ATOM    929  CG1 ILE A 140      -9.303   2.515 -31.043  1.00 31.13           C  
ANISOU  929  CG1 ILE A 140     4984   4168   2675   -315    832   -939       C  
ATOM    930  CG2 ILE A 140      -8.820   4.671 -29.884  1.00 35.54           C  
ANISOU  930  CG2 ILE A 140     5478   4770   3256   -208    820   -977       C  
ATOM    931  CD1 ILE A 140      -7.877   2.424 -31.550  1.00 32.02           C  
ANISOU  931  CD1 ILE A 140     5115   4228   2823   -293    815   -936       C  
ATOM    932  N   ALA A 141     -11.786   6.223 -30.735  1.00 25.33           N  
ANISOU  932  N   ALA A 141     4104   3591   1928   -201    855   -976       N  
ATOM    933  CA  ALA A 141     -12.104   7.623 -30.471  1.00 33.50           C  
ANISOU  933  CA  ALA A 141     5105   4659   2964   -139    860   -989       C  
ATOM    934  C   ALA A 141     -13.383   7.770 -29.653  1.00 36.91           C  
ANISOU  934  C   ALA A 141     5519   5157   3347   -128    881   -989       C  
ATOM    935  O   ALA A 141     -13.464   8.620 -28.769  1.00 39.71           O  
ANISOU  935  O   ALA A 141     5863   5534   3690    -76    886  -1002       O  
ATOM    936  CB  ALA A 141     -12.227   8.389 -31.777  1.00 25.20           C  
ANISOU  936  CB  ALA A 141     4035   3607   1934   -116    861   -986       C  
ATOM    937  N   LEU A 142     -14.382   6.945 -29.954  1.00 30.88           N  
ANISOU  937  N   LEU A 142     4754   4426   2553   -179    895   -978       N  
ATOM    938  CA  LEU A 142     -15.639   6.966 -29.212  1.00 33.89           C  
ANISOU  938  CA  LEU A 142     5117   4875   2885   -178    922   -976       C  
ATOM    939  C   LEU A 142     -15.419   6.515 -27.771  1.00 37.12           C  
ANISOU  939  C   LEU A 142     5551   5283   3271   -176    931   -977       C  
ATOM    940  O   LEU A 142     -15.953   7.109 -26.828  1.00 35.42           O  
ANISOU  940  O   LEU A 142     5322   5111   3023   -129    948   -980       O  
ATOM    941  CB  LEU A 142     -16.681   6.075 -29.894  1.00 25.61           C  
ANISOU  941  CB  LEU A 142     4060   3861   1811   -247    937   -969       C  
ATOM    942  CG  LEU A 142     -18.077   6.079 -29.265  1.00 26.25           C  
ANISOU  942  CG  LEU A 142     4113   4020   1841   -254    972   -966       C  
ATOM    943  CD1 LEU A 142     -18.702   7.460 -29.374  1.00 26.39           C  
ANISOU  943  CD1 LEU A 142     4095   4088   1846   -172    982   -966       C  
ATOM    944  CD2 LEU A 142     -18.970   5.031 -29.910  1.00 26.59           C  
ANISOU  944  CD2 LEU A 142     4147   4094   1862   -342    986   -968       C  
ATOM    945  N   ASP A 143     -14.623   5.461 -27.615  1.00 35.97           N  
ANISOU  945  N   ASP A 143     5444   5087   3134   -219    920   -973       N  
ATOM    946  CA  ASP A 143     -14.300   4.927 -26.298  1.00 32.22           C  
ANISOU  946  CA  ASP A 143     5001   4609   2631   -209    927   -974       C  
ATOM    947  C   ASP A 143     -13.630   5.987 -25.430  1.00 33.05           C  
ANISOU  947  C   ASP A 143     5099   4720   2739   -124    910   -994       C  
ATOM    948  O   ASP A 143     -14.036   6.216 -24.289  1.00 33.47           O  
ANISOU  948  O   ASP A 143     5153   4813   2750    -83    924   -999       O  
ATOM    949  CB  ASP A 143     -13.390   3.703 -26.427  1.00 43.36           C  
ANISOU  949  CB  ASP A 143     6462   5960   4053   -255    916   -966       C  
ATOM    950  CG  ASP A 143     -13.264   2.933 -25.129  1.00 53.99           C  
ANISOU  950  CG  ASP A 143     7849   7309   5355   -248    930   -963       C  
ATOM    951  OD1 ASP A 143     -14.314   2.576 -24.556  1.00 57.66           O  
ANISOU  951  OD1 ASP A 143     8315   7815   5776   -270    967   -953       O  
ATOM    952  OD2 ASP A 143     -12.124   2.689 -24.679  1.00 57.74           O  
ANISOU  952  OD2 ASP A 143     8354   7750   5835   -216    908   -970       O  
ATOM    953  N   ARG A 144     -12.608   6.637 -25.980  1.00 34.93           N  
ANISOU  953  N   ARG A 144     5329   4917   3024    -98    881  -1008       N  
ATOM    954  CA  ARG A 144     -11.896   7.679 -25.249  1.00 36.31           C  
ANISOU  954  CA  ARG A 144     5498   5093   3207    -26    863  -1036       C  
ATOM    955  C   ARG A 144     -12.771   8.905 -25.016  1.00 36.36           C  
ANISOU  955  C   ARG A 144     5475   5145   3197     25    880  -1043       C  
ATOM    956  O   ARG A 144     -12.623   9.597 -24.010  1.00 36.46           O  
ANISOU  956  O   ARG A 144     5489   5176   3188     86    875  -1066       O  
ATOM    957  CB  ARG A 144     -10.623   8.080 -25.992  1.00 26.81           C  
ANISOU  957  CB  ARG A 144     4292   3833   2061    -21    837  -1050       C  
ATOM    958  CG  ARG A 144      -9.563   6.994 -26.026  1.00 33.87           C  
ANISOU  958  CG  ARG A 144     5218   4686   2966    -48    819  -1047       C  
ATOM    959  CD  ARG A 144      -9.081   6.630 -24.629  1.00 33.50           C  
ANISOU  959  CD  ARG A 144     5193   4656   2878     -7    806  -1067       C  
ATOM    960  NE  ARG A 144      -9.851   5.535 -24.046  1.00 36.33           N  
ANISOU  960  NE  ARG A 144     5580   5038   3185    -36    827  -1045       N  
ATOM    961  CZ  ARG A 144      -9.905   5.268 -22.746  1.00 44.45           C  
ANISOU  961  CZ  ARG A 144     6627   6101   4160      4    829  -1057       C  
ATOM    962  NH1 ARG A 144      -9.237   6.023 -21.886  1.00 47.07           N  
ANISOU  962  NH1 ARG A 144     6949   6453   4482     79    802  -1097       N  
ATOM    963  NH2 ARG A 144     -10.633   4.251 -22.306  1.00 46.97           N  
ANISOU  963  NH2 ARG A 144     6975   6437   4434    -29    859  -1033       N  
ATOM    964  N   TRP A 145     -13.683   9.170 -25.945  1.00 39.34           N  
ANISOU  964  N   TRP A 145     5828   5543   3578      7    898  -1026       N  
ATOM    965  CA  TRP A 145     -14.584  10.308 -25.816  1.00 40.01           C  
ANISOU  965  CA  TRP A 145     5888   5674   3640     63    918  -1028       C  
ATOM    966  C   TRP A 145     -15.536  10.102 -24.645  1.00 40.71           C  
ANISOU  966  C   TRP A 145     5980   5822   3667     85    944  -1020       C  
ATOM    967  O   TRP A 145     -15.789  11.026 -23.875  1.00 45.96           O  
ANISOU  967  O   TRP A 145     6642   6514   4305    154    953  -1032       O  
ATOM    968  CB  TRP A 145     -15.369  10.531 -27.108  1.00 39.39           C  
ANISOU  968  CB  TRP A 145     5784   5614   3568     48    930  -1011       C  
ATOM    969  CG  TRP A 145     -16.279  11.713 -27.055  1.00 26.72           C  
ANISOU  969  CG  TRP A 145     4159   4057   1935    117    954  -1009       C  
ATOM    970  CD1 TRP A 145     -15.920  13.025 -27.137  1.00 26.70           C  
ANISOU  970  CD1 TRP A 145     4152   4042   1950    183    951  -1025       C  
ATOM    971  CD2 TRP A 145     -17.704  11.694 -26.915  1.00 27.23           C  
ANISOU  971  CD2 TRP A 145     4207   4190   1948    129    989   -989       C  
ATOM    972  NE1 TRP A 145     -17.033  13.826 -27.052  1.00 27.16           N  
ANISOU  972  NE1 TRP A 145     4199   4155   1966    244    982  -1013       N  
ATOM    973  CE2 TRP A 145     -18.141  13.033 -26.916  1.00 36.13           C  
ANISOU  973  CE2 TRP A 145     5327   5341   3059    213   1007   -989       C  
ATOM    974  CE3 TRP A 145     -18.653  10.675 -26.787  1.00 27.56           C  
ANISOU  974  CE3 TRP A 145     4241   4275   1955     73   1012   -972       C  
ATOM    975  CZ2 TRP A 145     -19.484  13.380 -26.794  1.00 38.83           C  
ANISOU  975  CZ2 TRP A 145     5660   5744   3351    250   1049   -966       C  
ATOM    976  CZ3 TRP A 145     -19.985  11.021 -26.666  1.00 28.13           C  
ANISOU  976  CZ3 TRP A 145     4292   4415   1982     99   1053   -955       C  
ATOM    977  CH2 TRP A 145     -20.389  12.362 -26.671  1.00 28.37           C  
ANISOU  977  CH2 TRP A 145     4320   4463   1996    190   1072   -950       C  
ATOM    978  N   TYR A 146     -16.059   8.887 -24.510  1.00 38.30           N  
ANISOU  978  N   TYR A 146     5683   5533   3335     25    961  -1002       N  
ATOM    979  CA  TYR A 146     -16.908   8.566 -23.370  1.00 35.22           C  
ANISOU  979  CA  TYR A 146     5300   5197   2884     41    995   -991       C  
ATOM    980  C   TYR A 146     -16.097   8.526 -22.079  1.00 34.14           C  
ANISOU  980  C   TYR A 146     5194   5052   2727     90    979  -1009       C  
ATOM    981  O   TYR A 146     -16.566   8.968 -21.036  1.00 34.75           O  
ANISOU  981  O   TYR A 146     5274   5175   2755    152    998  -1012       O  
ATOM    982  CB  TYR A 146     -17.630   7.233 -23.579  1.00 40.14           C  
ANISOU  982  CB  TYR A 146     5927   5836   3488    -46   1022   -969       C  
ATOM    983  CG  TYR A 146     -18.979   7.375 -24.246  1.00 44.28           C  
ANISOU  983  CG  TYR A 146     6412   6416   3996    -71   1056   -954       C  
ATOM    984  CD1 TYR A 146     -20.080   7.826 -23.533  1.00 49.01           C  
ANISOU  984  CD1 TYR A 146     6992   7084   4546    -29   1099   -941       C  
ATOM    985  CD2 TYR A 146     -19.153   7.057 -25.587  1.00 46.75           C  
ANISOU  985  CD2 TYR A 146     6707   6718   4338   -131   1045   -954       C  
ATOM    986  CE1 TYR A 146     -21.316   7.960 -24.134  1.00 50.94           C  
ANISOU  986  CE1 TYR A 146     7196   7386   4773    -50   1132   -928       C  
ATOM    987  CE2 TYR A 146     -20.390   7.188 -26.197  1.00 49.18           C  
ANISOU  987  CE2 TYR A 146     6974   7087   4625   -150   1072   -946       C  
ATOM    988  CZ  TYR A 146     -21.467   7.640 -25.465  1.00 49.40           C  
ANISOU  988  CZ  TYR A 146     6978   7185   4607   -111   1116   -934       C  
ATOM    989  OH  TYR A 146     -22.699   7.774 -26.064  1.00 50.57           O  
ANISOU  989  OH  TYR A 146     7080   7400   4732   -130   1146   -928       O  
ATOM    990  N   ALA A 147     -14.878   8.001 -22.154  1.00 39.21           N  
ANISOU  990  N   ALA A 147     5860   5640   3399     69    945  -1024       N  
ATOM    991  CA  ALA A 147     -14.025   7.879 -20.974  1.00 32.91           C  
ANISOU  991  CA  ALA A 147     5089   4840   2576    120    924  -1048       C  
ATOM    992  C   ALA A 147     -13.640   9.238 -20.387  1.00 36.39           C  
ANISOU  992  C   ALA A 147     5520   5292   3014    207    903  -1084       C  
ATOM    993  O   ALA A 147     -13.641   9.421 -19.169  1.00 39.38           O  
ANISOU  993  O   ALA A 147     5911   5711   3342    271    902  -1103       O  
ATOM    994  CB  ALA A 147     -12.775   7.084 -21.315  1.00 33.78           C  
ANISOU  994  CB  ALA A 147     5223   4892   2720     85    892  -1055       C  
ATOM    995  N   ILE A 148     -13.315  10.187 -21.258  1.00 32.45           N  
ANISOU  995  N   ILE A 148     5001   4760   2568    211    890  -1095       N  
ATOM    996  CA  ILE A 148     -12.835  11.494 -20.819  1.00 27.83           C  
ANISOU  996  CA  ILE A 148     4414   4171   1990    282    871  -1134       C  
ATOM    997  C   ILE A 148     -13.977  12.493 -20.626  1.00 34.44           C  
ANISOU  997  C   ILE A 148     5238   5054   2795    333    903  -1126       C  
ATOM    998  O   ILE A 148     -14.070  13.144 -19.583  1.00 40.90           O  
ANISOU  998  O   ILE A 148     6063   5895   3581    399    900  -1145       O  
ATOM    999  CB  ILE A 148     -11.806  12.084 -21.818  1.00 39.16           C  
ANISOU  999  CB  ILE A 148     5838   5542   3498    263    848  -1152       C  
ATOM   1000  CG1 ILE A 148     -10.409  11.505 -21.571  1.00 39.02           C  
ANISOU 1000  CG1 ILE A 148     5839   5484   3501    255    810  -1177       C  
ATOM   1001  CG2 ILE A 148     -11.734  13.599 -21.695  1.00 43.79           C  
ANISOU 1001  CG2 ILE A 148     6418   6122   4097    321    848  -1183       C  
ATOM   1002  CD1 ILE A 148     -10.214  10.082 -22.049  1.00 37.13           C  
ANISOU 1002  CD1 ILE A 148     5610   5230   3268    190    809  -1147       C  
ATOM   1003  N   CYS A 149     -14.852  12.602 -21.622  1.00 31.96           N  
ANISOU 1003  N   CYS A 149     4899   4750   2493    302    930  -1094       N  
ATOM   1004  CA  CYS A 149     -15.860  13.660 -21.640  1.00 32.56           C  
ANISOU 1004  CA  CYS A 149     4963   4866   2542    359    961  -1085       C  
ATOM   1005  C   CYS A 149     -17.168  13.282 -20.942  1.00 33.95           C  
ANISOU 1005  C   CYS A 149     5140   5107   2651    378   1004  -1051       C  
ATOM   1006  O   CYS A 149     -17.980  14.154 -20.630  1.00 36.39           O  
ANISOU 1006  O   CYS A 149     5442   5443   2942    431   1028  -1035       O  
ATOM   1007  CB  CYS A 149     -16.150  14.079 -23.083  1.00 28.69           C  
ANISOU 1007  CB  CYS A 149     4448   4362   2092    335    969  -1068       C  
ATOM   1008  SG  CYS A 149     -14.700  14.668 -23.988  1.00 50.00           S  
ANISOU 1008  SG  CYS A 149     7142   6983   4871    316    934  -1100       S  
ATOM   1009  N   HIS A 150     -17.376  11.992 -20.700  1.00 29.58           N  
ANISOU 1009  N   HIS A 150     4593   4570   2077    323   1014  -1033       N  
ATOM   1010  CA  HIS A 150     -18.573  11.538 -19.992  1.00 37.69           C  
ANISOU 1010  CA  HIS A 150     5620   5660   3039    333   1064  -1001       C  
ATOM   1011  C   HIS A 150     -18.285  10.342 -19.085  1.00 42.11           C  
ANISOU 1011  C   HIS A 150     6202   6231   3567    307   1064  -1000       C  
ATOM   1012  O   HIS A 150     -18.742   9.232 -19.358  1.00 47.88           O  
ANISOU 1012  O   HIS A 150     6929   6969   4293    232   1089   -975       O  
ATOM   1013  CB  HIS A 150     -19.679  11.176 -20.986  1.00 38.18           C  
ANISOU 1013  CB  HIS A 150     5654   5747   3106    273   1101   -967       C  
ATOM   1014  CG  HIS A 150     -20.178  12.338 -21.788  1.00 41.29           C  
ANISOU 1014  CG  HIS A 150     6030   6144   3513    315   1113   -961       C  
ATOM   1015  ND1 HIS A 150     -19.653  12.673 -23.018  1.00 43.14           N  
ANISOU 1015  ND1 HIS A 150     6251   6339   3802    292   1082   -972       N  
ATOM   1016  CD2 HIS A 150     -21.149  13.246 -21.533  1.00 43.43           C  
ANISOU 1016  CD2 HIS A 150     6301   6448   3751    380   1157   -940       C  
ATOM   1017  CE1 HIS A 150     -20.283  13.736 -23.487  1.00 44.10           C  
ANISOU 1017  CE1 HIS A 150     6366   6475   3914    350   1107   -962       C  
ATOM   1018  NE2 HIS A 150     -21.195  14.103 -22.605  1.00 44.32           N  
ANISOU 1018  NE2 HIS A 150     6402   6540   3898    396   1151   -940       N  
ATOM   1019  N   PRO A 151     -17.532  10.571 -17.997  1.00 29.58           N  
ANISOU 1019  N   PRO A 151     4634   4645   1959    368   1036  -1030       N  
ATOM   1020  CA  PRO A 151     -17.079   9.499 -17.101  1.00 29.87           C  
ANISOU 1020  CA  PRO A 151     4693   4697   1959    359   1031  -1037       C  
ATOM   1021  C   PRO A 151     -18.224   8.658 -16.542  1.00 36.71           C  
ANISOU 1021  C   PRO A 151     5562   5625   2760    343   1094   -997       C  
ATOM   1022  O   PRO A 151     -18.090   7.441 -16.416  1.00 30.63           O  
ANISOU 1022  O   PRO A 151     4811   4847   1981    283   1106   -983       O  
ATOM   1023  CB  PRO A 151     -16.371  10.260 -15.974  1.00 44.58           C  
ANISOU 1023  CB  PRO A 151     6553   6565   3820    434    987  -1074       C  
ATOM   1024  CG  PRO A 151     -15.989  11.563 -16.577  1.00 29.84           C  
ANISOU 1024  CG  PRO A 151     4676   4653   2008    460    959  -1095       C  
ATOM   1025  CD  PRO A 151     -17.093  11.896 -17.527  1.00 29.70           C  
ANISOU 1025  CD  PRO A 151     4644   4644   1996    439   1004  -1057       C  
ATOM   1026  N   LEU A 152     -19.338   9.306 -16.219  1.00 34.34           N  
ANISOU 1026  N   LEU A 152     5242   5370   2434    383   1134   -969       N  
ATOM   1027  CA  LEU A 152     -20.472   8.624 -15.603  1.00 36.85           C  
ANISOU 1027  CA  LEU A 152     5557   5753   2690    374   1203   -928       C  
ATOM   1028  C   LEU A 152     -21.131   7.616 -16.545  1.00 41.61           C  
ANISOU 1028  C   LEU A 152     6153   6349   3308    266   1245   -898       C  
ATOM   1029  O   LEU A 152     -21.760   6.659 -16.096  1.00 43.65           O  
ANISOU 1029  O   LEU A 152     6416   6642   3528    225   1297   -868       O  
ATOM   1030  CB  LEU A 152     -21.510   9.644 -15.126  1.00 36.89           C  
ANISOU 1030  CB  LEU A 152     5543   5798   2675    444   1238   -900       C  
ATOM   1031  CG  LEU A 152     -21.039  10.634 -14.060  1.00 32.79           C  
ANISOU 1031  CG  LEU A 152     5019   5290   2148    540   1194   -927       C  
ATOM   1032  CD1 LEU A 152     -22.174  11.554 -13.647  1.00 33.47           C  
ANISOU 1032  CD1 LEU A 152     5105   5403   2209    610   1241   -888       C  
ATOM   1033  CD2 LEU A 152     -20.475   9.901 -12.852  1.00 33.26           C  
ANISOU 1033  CD2 LEU A 152     5067   5405   2165    546   1173   -956       C  
ATOM   1034  N   LEU A 153     -20.980   7.829 -17.847  1.00 47.40           N  
ANISOU 1034  N   LEU A 153     6867   7035   4106    210   1217   -906       N  
ATOM   1035  CA  LEU A 153     -21.614   6.965 -18.837  1.00 46.25           C  
ANISOU 1035  CA  LEU A 153     6700   6886   3987     98   1242   -887       C  
ATOM   1036  C   LEU A 153     -20.629   5.958 -19.422  1.00 50.64           C  
ANISOU 1036  C   LEU A 153     7282   7372   4587     16   1202   -902       C  
ATOM   1037  O   LEU A 153     -20.980   5.171 -20.301  1.00 55.75           O  
ANISOU 1037  O   LEU A 153     7918   8006   5258    -82   1213   -895       O  
ATOM   1038  CB  LEU A 153     -22.227   7.805 -19.960  1.00 41.01           C  
ANISOU 1038  CB  LEU A 153     5993   6232   3356     93   1242   -887       C  
ATOM   1039  CG  LEU A 153     -23.188   8.913 -19.529  1.00 40.98           C  
ANISOU 1039  CG  LEU A 153     5973   6283   3314    179   1286   -869       C  
ATOM   1040  CD1 LEU A 153     -23.600   9.758 -20.725  1.00 37.70           C  
ANISOU 1040  CD1 LEU A 153     5524   5866   2932    179   1280   -872       C  
ATOM   1041  CD2 LEU A 153     -24.408   8.326 -18.835  1.00 46.35           C  
ANISOU 1041  CD2 LEU A 153     6638   7034   3940    161   1365   -832       C  
ATOM   1042  N   PHE A 154     -19.397   5.989 -18.926  1.00 48.73           N  
ANISOU 1042  N   PHE A 154     7074   7088   4352     58   1157   -925       N  
ATOM   1043  CA  PHE A 154     -18.336   5.138 -19.453  1.00 48.49           C  
ANISOU 1043  CA  PHE A 154     7075   6986   4363     -3   1119   -937       C  
ATOM   1044  C   PHE A 154     -18.562   3.664 -19.134  1.00 49.23           C  
ANISOU 1044  C   PHE A 154     7207   7070   4428    -76   1158   -914       C  
ATOM   1045  O   PHE A 154     -18.606   3.263 -17.970  1.00 52.93           O  
ANISOU 1045  O   PHE A 154     7705   7567   4841    -41   1185   -905       O  
ATOM   1046  CB  PHE A 154     -16.976   5.589 -18.911  1.00 54.98           C  
ANISOU 1046  CB  PHE A 154     7918   7776   5195     68   1066   -969       C  
ATOM   1047  CG  PHE A 154     -15.822   4.759 -19.399  1.00 50.92           C  
ANISOU 1047  CG  PHE A 154     7436   7191   4720     20   1031   -978       C  
ATOM   1048  CD1 PHE A 154     -15.520   4.698 -20.747  1.00 36.85           C  
ANISOU 1048  CD1 PHE A 154     5644   5358   3001    -40   1009   -976       C  
ATOM   1049  CD2 PHE A 154     -15.032   4.052 -18.507  1.00 51.23           C  
ANISOU 1049  CD2 PHE A 154     7518   7221   4728     43   1021   -986       C  
ATOM   1050  CE1 PHE A 154     -14.459   3.942 -21.200  1.00 36.47           C  
ANISOU 1050  CE1 PHE A 154     5627   5246   2985    -77    981   -980       C  
ATOM   1051  CE2 PHE A 154     -13.968   3.294 -18.955  1.00 37.44           C  
ANISOU 1051  CE2 PHE A 154     5803   5409   3012      8    992   -991       C  
ATOM   1052  CZ  PHE A 154     -13.682   3.242 -20.303  1.00 36.76           C  
ANISOU 1052  CZ  PHE A 154     5707   5269   2990    -52    973   -986       C  
ATOM   1053  N   LYS A 155     -18.708   2.865 -20.186  1.00 90.21           N  
ANISOU 1053  N   LYS A 155    14680  10003   9593  -3992   3888   -852       N  
ATOM   1054  CA  LYS A 155     -18.848   1.420 -20.058  1.00 90.20           C  
ANISOU 1054  CA  LYS A 155    14541  10055   9676  -4123   3739   -695       C  
ATOM   1055  C   LYS A 155     -18.097   0.718 -21.181  1.00 86.72           C  
ANISOU 1055  C   LYS A 155    13996   9721   9232  -4049   3115   -658       C  
ATOM   1056  O   LYS A 155     -18.533   0.736 -22.332  1.00 86.03           O  
ANISOU 1056  O   LYS A 155    13540   9639   9509  -3837   2838   -698       O  
ATOM   1057  CB  LYS A 155     -20.319   1.007 -20.079  1.00 93.58           C  
ANISOU 1057  CB  LYS A 155    14497  10365  10692  -4104   4008   -659       C  
ATOM   1058  CG  LYS A 155     -21.073   1.261 -18.787  1.00 97.91           C  
ANISOU 1058  CG  LYS A 155    15128  10867  11204  -4214   4678   -635       C  
ATOM   1059  CD  LYS A 155     -22.437   0.596 -18.833  1.00101.84           C  
ANISOU 1059  CD  LYS A 155    15073  11296  12325  -4283   4934   -585       C  
ATOM   1060  CE  LYS A 155     -23.127   0.639 -17.483  1.00106.81           C  
ANISOU 1060  CE  LYS A 155    15787  11928  12869  -4422   5660   -495       C  
ATOM   1061  NZ  LYS A 155     -24.372  -0.174 -17.493  1.00111.42           N  
ANISOU 1061  NZ  LYS A 155    15790  12447  14097  -4598   5951   -423       N  
ATOM   1062  N   SER A 156     -16.970   0.100 -20.847  1.00 85.11           N  
ANISOU 1062  N   SER A 156    14108   9658   8573  -4159   2882   -606       N  
ATOM   1063  CA  SER A 156     -16.166  -0.588 -21.848  1.00 82.23           C  
ANISOU 1063  CA  SER A 156    13666   9438   8139  -4048   2302   -597       C  
ATOM   1064  C   SER A 156     -15.674  -1.938 -21.342  1.00 82.72           C  
ANISOU 1064  C   SER A 156    13929   9509   7991  -4126   2137   -467       C  
ATOM   1065  O   SER A 156     -14.530  -2.069 -20.906  1.00 81.85           O  
ANISOU 1065  O   SER A 156    14141   9623   7335  -4129   1982   -465       O  
ATOM   1066  CB  SER A 156     -14.973   0.274 -22.263  1.00 79.83           C  
ANISOU 1066  CB  SER A 156    13531   9365   7434  -4002   2098   -697       C  
ATOM   1067  OG  SER A 156     -14.008   0.332 -21.228  1.00 82.94           O  
ANISOU 1067  OG  SER A 156    14296   9935   7283  -4173   2178   -752       O  
ATOM   1068  N   THR A 157     -16.544  -2.939 -21.398  1.00 84.89           N  
ANISOU 1068  N   THR A 157    14005   9529   8721  -4180   2179   -372       N  
ATOM   1069  CA  THR A 157     -16.152  -4.301 -21.069  1.00 86.20           C  
ANISOU 1069  CA  THR A 157    14393   9570   8790  -4218   2026   -212       C  
ATOM   1070  C   THR A 157     -15.446  -4.928 -22.264  1.00 83.71           C  
ANISOU 1070  C   THR A 157    13955   9361   8490  -4004   1374   -333       C  
ATOM   1071  O   THR A 157     -15.559  -4.434 -23.386  1.00 81.68           O  
ANISOU 1071  O   THR A 157    13361   9246   8427  -3849   1093   -517       O  
ATOM   1072  CB  THR A 157     -17.364  -5.166 -20.672  1.00 90.68           C  
ANISOU 1072  CB  THR A 157    14801   9726   9926  -4432   2386    -67       C  
ATOM   1073  OG1 THR A 157     -16.949  -6.528 -20.506  1.00 92.54           O  
ANISOU 1073  OG1 THR A 157    15301   9725  10133  -4443   2217    109       O  
ATOM   1074  CG2 THR A 157     -18.443  -5.097 -21.742  1.00 91.22           C  
ANISOU 1074  CG2 THR A 157    14243   9692  10725  -4433   2256   -293       C  
ATOM   1075  N   ALA A 158     -14.714  -6.010 -22.022  1.00 84.47           N  
ANISOU 1075  N   ALA A 158    14350   9407   8336  -3931   1145   -220       N  
ATOM   1076  CA  ALA A 158     -14.029  -6.717 -23.098  1.00 82.84           C  
ANISOU 1076  CA  ALA A 158    14053   9302   8121  -3679    534   -362       C  
ATOM   1077  C   ALA A 158     -15.045  -7.373 -24.027  1.00 85.37           C  
ANISOU 1077  C   ALA A 158    13953   9306   9177  -3700    355   -528       C  
ATOM   1078  O   ALA A 158     -14.778  -7.582 -25.213  1.00 87.01           O  
ANISOU 1078  O   ALA A 158    13917   9678   9464  -3454   -152   -763       O  
ATOM   1079  CB  ALA A 158     -13.071  -7.755 -22.532  1.00 84.27           C  
ANISOU 1079  CB  ALA A 158    14683   9462   7872  -3531    358   -203       C  
ATOM   1080  N   ARG A 159     -16.213  -7.688 -23.477  1.00 88.29           N  
ANISOU 1080  N   ARG A 159    14206   9268  10075  -3993    784   -439       N  
ATOM   1081  CA  ARG A 159     -17.286  -8.305 -24.245  1.00 91.20           C  
ANISOU 1081  CA  ARG A 159    14088   9341  11224  -4098    655   -672       C  
ATOM   1082  C   ARG A 159     -17.861  -7.338 -25.276  1.00 89.84           C  
ANISOU 1082  C   ARG A 159    13371   9500  11266  -3929    465   -963       C  
ATOM   1083  O   ARG A 159     -18.299  -7.756 -26.348  1.00 93.31           O  
ANISOU 1083  O   ARG A 159    13384   9951  12118  -3801     51  -1286       O  
ATOM   1084  CB  ARG A 159     -18.393  -8.804 -23.314  1.00 96.57           C  
ANISOU 1084  CB  ARG A 159    14723   9541  12429  -4515   1258   -492       C  
ATOM   1085  CG  ARG A 159     -17.947  -9.898 -22.353  1.00 99.87           C  
ANISOU 1085  CG  ARG A 159    15719   9542  12686  -4637   1487   -135       C  
ATOM   1086  CD  ARG A 159     -19.123 -10.467 -21.572  1.00106.35           C  
ANISOU 1086  CD  ARG A 159    16448   9841  14121  -5088   2138     70       C  
ATOM   1087  NE  ARG A 159     -18.708 -11.521 -20.651  1.00110.50           N  
ANISOU 1087  NE  ARG A 159    17610   9911  14465  -5156   2417    504       N  
ATOM   1088  CZ  ARG A 159     -19.542 -12.214 -19.882  1.00117.29           C  
ANISOU 1088  CZ  ARG A 159    18545  10226  15792  -5546   3051    807       C  
ATOM   1089  NH1 ARG A 159     -20.844 -11.967 -19.923  1.00120.57           N  
ANISOU 1089  NH1 ARG A 159    18356  10538  16917  -5943   3455    662       N  
ATOM   1090  NH2 ARG A 159     -19.076 -13.155 -19.072  1.00121.50           N  
ANISOU 1090  NH2 ARG A 159    19753  10333  16077  -5517   3306   1273       N  
ATOM   1091  N   ARG A 160     -17.861  -6.048 -24.951  1.00 87.40           N  
ANISOU 1091  N   ARG A 160    13099   9452  10658  -3887    761   -864       N  
ATOM   1092  CA  ARG A 160     -18.325  -5.036 -25.895  1.00 90.64           C  
ANISOU 1092  CA  ARG A 160    13101  10151  11185  -3633    620  -1055       C  
ATOM   1093  C   ARG A 160     -17.353  -4.937 -27.063  1.00 87.63           C  
ANISOU 1093  C   ARG A 160    12736  10126  10433  -3252     41  -1171       C  
ATOM   1094  O   ARG A 160     -17.764  -4.833 -28.218  1.00 90.26           O  
ANISOU 1094  O   ARG A 160    12669  10659  10965  -2954   -316  -1398       O  
ATOM   1095  CB  ARG A 160     -18.476  -3.672 -25.218  1.00 94.84           C  
ANISOU 1095  CB  ARG A 160    13772  10776  11488  -3663   1113   -907       C  
ATOM   1096  CG  ARG A 160     -19.197  -2.640 -26.081  1.00 99.45           C  
ANISOU 1096  CG  ARG A 160    13958  11549  12279  -3360   1073  -1046       C  
ATOM   1097  CD  ARG A 160     -19.253  -1.271 -25.415  1.00101.14           C  
ANISOU 1097  CD  ARG A 160    14398  11760  12269  -3359   1564   -915       C  
ATOM   1098  NE  ARG A 160     -18.012  -0.520 -25.586  1.00 99.08           N  
ANISOU 1098  NE  ARG A 160    14538  11658  11452  -3264   1466   -820       N  
ATOM   1099  CZ  ARG A 160     -17.792   0.346 -26.571  1.00 96.70           C  
ANISOU 1099  CZ  ARG A 160    14183  11520  11039  -2935   1300   -814       C  
ATOM   1100  NH1 ARG A 160     -18.731   0.572 -27.480  1.00 96.83           N  
ANISOU 1100  NH1 ARG A 160    13785  11615  11389  -2578   1159   -899       N  
ATOM   1101  NH2 ARG A 160     -16.633   0.986 -26.649  1.00 94.69           N  
ANISOU 1101  NH2 ARG A 160    14275  11370  10333  -2953   1291   -721       N  
ATOM   1102  N   ALA A 161     -16.060  -4.973 -26.750  1.00 83.19           N  
ANISOU 1102  N   ALA A 161    12612   9704   9294  -3230    -47  -1026       N  
ATOM   1103  CA  ALA A 161     -15.018  -4.930 -27.768  1.00 77.78           C  
ANISOU 1103  CA  ALA A 161    11943   9402   8206  -2894   -531  -1110       C  
ATOM   1104  C   ALA A 161     -15.106  -6.153 -28.676  1.00 79.31           C  
ANISOU 1104  C   ALA A 161    11917   9566   8651  -2686  -1068  -1367       C  
ATOM   1105  O   ALA A 161     -15.444  -6.038 -29.858  1.00 79.84           O  
ANISOU 1105  O   ALA A 161    11622   9867   8846  -2370  -1415  -1590       O  
ATOM   1106  CB  ALA A 161     -13.645  -4.841 -27.119  1.00 75.67           C  
ANISOU 1106  CB  ALA A 161    12111   9322   7317  -2953   -500   -957       C  
ATOM   1107  N   ARG A 162     -14.807  -7.324 -28.118  1.00 80.74           N  
ANISOU 1107  N   ARG A 162    12344   9451   8883  -2823  -1135  -1349       N  
ATOM   1108  CA  ARG A 162     -14.970  -8.574 -28.852  1.00 83.32           C  
ANISOU 1108  CA  ARG A 162    12511   9596   9550  -2681  -1600  -1641       C  
ATOM   1109  C   ARG A 162     -16.454  -8.860 -29.052  1.00 87.28           C  
ANISOU 1109  C   ARG A 162    12551   9772  10838  -2889  -1517  -1876       C  
ATOM   1110  O   ARG A 162     -17.018  -9.763 -28.433  1.00 91.04           O  
ANISOU 1110  O   ARG A 162    13073   9716  11804  -3229  -1318  -1872       O  
ATOM   1111  CB  ARG A 162     -14.294  -9.734 -28.121  1.00 84.82           C  
ANISOU 1111  CB  ARG A 162    13161   9443   9623  -2755  -1626  -1511       C  
ATOM   1112  CG  ARG A 162     -12.780  -9.622 -28.030  1.00 81.90           C  
ANISOU 1112  CG  ARG A 162    13146   9491   8481  -2472  -1823  -1381       C  
ATOM   1113  CD  ARG A 162     -12.164 -10.928 -27.548  1.00 85.50           C  
ANISOU 1113  CD  ARG A 162    14020   9624   8843  -2372  -1977  -1313       C  
ATOM   1114  NE  ARG A 162     -12.758 -11.385 -26.294  1.00 88.18           N  
ANISOU 1114  NE  ARG A 162    14670   9385   9449  -2732  -1480  -1013       N  
ATOM   1115  CZ  ARG A 162     -12.276 -11.096 -25.090  1.00 87.43           C  
ANISOU 1115  CZ  ARG A 162    14980   9361   8880  -2813  -1115   -661       C  
ATOM   1116  NH1 ARG A 162     -11.186 -10.351 -24.974  1.00 84.14           N  
ANISOU 1116  NH1 ARG A 162    14655   9551   7761  -2617  -1223   -633       N  
ATOM   1117  NH2 ARG A 162     -12.881 -11.552 -24.002  1.00 91.20           N  
ANISOU 1117  NH2 ARG A 162    15750   9329   9574  -3092   -629   -356       N  
ATOM   1118  N   GLY A 163     -17.074  -8.075 -29.924  1.00 53.15           N  
ANISOU 1118  N   GLY A 163     8341   7023   4829  -1890   1391   -943       N  
ATOM   1119  CA  GLY A 163     -18.502  -8.140 -30.160  1.00 65.06           C  
ANISOU 1119  CA  GLY A 163     9733   8537   6451  -1927   1509  -1161       C  
ATOM   1120  C   GLY A 163     -18.915  -6.957 -31.013  1.00 72.12           C  
ANISOU 1120  C   GLY A 163    10481   9479   7443  -1789   1405  -1280       C  
ATOM   1121  O   GLY A 163     -19.899  -7.017 -31.748  1.00 76.23           O  
ANISOU 1121  O   GLY A 163    10870   9996   8098  -1745   1441  -1430       O  
ATOM   1122  N   SER A 164     -18.154  -5.872 -30.904  1.00 65.94           N  
ANISOU 1122  N   SER A 164     9716   8737   6600  -1712   1265  -1207       N  
ATOM   1123  CA  SER A 164     -18.324  -4.725 -31.787  1.00 65.11           C  
ANISOU 1123  CA  SER A 164     9489   8667   6581  -1559   1138  -1287       C  
ATOM   1124  C   SER A 164     -17.299  -4.801 -32.911  1.00 65.49           C  
ANISOU 1124  C   SER A 164     9557   8700   6625  -1425   1011  -1157       C  
ATOM   1125  O   SER A 164     -17.526  -4.288 -34.006  1.00 66.81           O  
ANISOU 1125  O   SER A 164     9623   8881   6881  -1292    921  -1223       O  
ATOM   1126  CB  SER A 164     -18.181  -3.410 -31.019  1.00 56.60           C  
ANISOU 1126  CB  SER A 164     8408   7640   5459  -1554   1066  -1310       C  
ATOM   1127  OG  SER A 164     -16.862  -3.252 -30.525  1.00 51.66           O  
ANISOU 1127  OG  SER A 164     7907   7017   4706  -1559    982  -1125       O  
ATOM   1128  N   ILE A 165     -16.169  -5.444 -32.628  1.00 61.63           N  
ANISOU 1128  N   ILE A 165     9200   8180   6038  -1460    998   -966       N  
ATOM   1129  CA  ILE A 165     -15.147  -5.691 -33.641  1.00 53.98           C  
ANISOU 1129  CA  ILE A 165     8255   7188   5066  -1349    900   -827       C  
ATOM   1130  C   ILE A 165     -15.711  -6.600 -34.730  1.00 58.88           C  
ANISOU 1130  C   ILE A 165     8812   7782   5777  -1313    966   -910       C  
ATOM   1131  O   ILE A 165     -15.499  -6.376 -35.927  1.00 58.44           O  
ANISOU 1131  O   ILE A 165     8696   7741   5769  -1183    877   -916       O  
ATOM   1132  CB  ILE A 165     -13.884  -6.327 -33.023  1.00 43.31           C  
ANISOU 1132  CB  ILE A 165     7040   5793   3622  -1395    879   -599       C  
ATOM   1133  CG1 ILE A 165     -13.158  -5.312 -32.136  1.00 34.01           C  
ANISOU 1133  CG1 ILE A 165     5904   4645   2371  -1393    773   -508       C  
ATOM   1134  CG2 ILE A 165     -12.954  -6.842 -34.108  1.00 38.13           C  
ANISOU 1134  CG2 ILE A 165     6395   5101   2992  -1290    813   -465       C  
ATOM   1135  CD1 ILE A 165     -11.904  -5.851 -31.484  1.00 37.53           C  
ANISOU 1135  CD1 ILE A 165     6451   5050   2759  -1412    723   -283       C  
ATOM   1136  N   LEU A 166     -16.448  -7.619 -34.299  1.00 56.63           N  
ANISOU 1136  N   LEU A 166     8540   7460   5517  -1433   1122   -980       N  
ATOM   1137  CA  LEU A 166     -17.122  -8.526 -35.217  1.00 51.93           C  
ANISOU 1137  CA  LEU A 166     7872   6835   5025  -1415   1202  -1085       C  
ATOM   1138  C   LEU A 166     -18.152  -7.773 -36.050  1.00 46.75           C  
ANISOU 1138  C   LEU A 166     7048   6224   4492  -1309   1143  -1268       C  
ATOM   1139  O   LEU A 166     -18.370  -8.090 -37.218  1.00 50.21           O  
ANISOU 1139  O   LEU A 166     7408   6659   5011  -1215   1112  -1324       O  
ATOM   1140  CB  LEU A 166     -17.786  -9.668 -34.447  1.00 55.73           C  
ANISOU 1140  CB  LEU A 166     8393   7262   5520  -1577   1388  -1135       C  
ATOM   1141  CG  LEU A 166     -16.831 -10.546 -33.637  1.00 60.96           C  
ANISOU 1141  CG  LEU A 166     9220   7867   6074  -1674   1440   -944       C  
ATOM   1142  CD1 LEU A 166     -17.590 -11.619 -32.868  1.00 65.05           C  
ANISOU 1142  CD1 LEU A 166     9773   8332   6611  -1830   1624  -1004       C  
ATOM   1143  CD2 LEU A 166     -15.785 -11.170 -34.548  1.00 60.83           C  
ANISOU 1143  CD2 LEU A 166     9246   7809   6058  -1588   1388   -804       C  
ATOM   1144  N   GLY A 167     -18.779  -6.771 -35.442  1.00 42.16           N  
ANISOU 1144  N   GLY A 167     6412   5681   3927  -1323   1122  -1356       N  
ATOM   1145  CA  GLY A 167     -19.707  -5.913 -36.154  1.00 44.58           C  
ANISOU 1145  CA  GLY A 167     6566   6018   4353  -1217   1045  -1506       C  
ATOM   1146  C   GLY A 167     -18.988  -5.111 -37.221  1.00 46.36           C  
ANISOU 1146  C   GLY A 167     6772   6270   4572  -1051    866  -1447       C  
ATOM   1147  O   GLY A 167     -19.487  -4.947 -38.337  1.00 47.82           O  
ANISOU 1147  O   GLY A 167     6858   6461   4849   -944    795  -1527       O  
ATOM   1148  N   ILE A 168     -17.806  -4.614 -36.870  1.00 45.38           N  
ANISOU 1148  N   ILE A 168     6747   6161   4336  -1036    790  -1298       N  
ATOM   1149  CA  ILE A 168     -16.970  -3.867 -37.803  1.00 46.29           C  
ANISOU 1149  CA  ILE A 168     6857   6300   4430   -893    627  -1219       C  
ATOM   1150  C   ILE A 168     -16.609  -4.722 -39.012  1.00 47.25           C  
ANISOU 1150  C   ILE A 168     6976   6411   4564   -821    614  -1177       C  
ATOM   1151  O   ILE A 168     -16.792  -4.300 -40.156  1.00 50.18           O  
ANISOU 1151  O   ILE A 168     7274   6806   4988   -699    514  -1229       O  
ATOM   1152  CB  ILE A 168     -15.677  -3.368 -37.128  1.00 47.61           C  
ANISOU 1152  CB  ILE A 168     7135   6475   4479   -908    561  -1042       C  
ATOM   1153  CG1 ILE A 168     -16.000  -2.308 -36.073  1.00 47.97           C  
ANISOU 1153  CG1 ILE A 168     7170   6542   4516   -955    546  -1103       C  
ATOM   1154  CG2 ILE A 168     -14.708  -2.812 -38.162  1.00 47.37           C  
ANISOU 1154  CG2 ILE A 168     7104   6467   4429   -770    409   -935       C  
ATOM   1155  CD1 ILE A 168     -14.783  -1.780 -35.347  1.00 49.68           C  
ANISOU 1155  CD1 ILE A 168     7485   6764   4627   -971    473   -938       C  
ATOM   1156  N   TRP A 169     -16.106  -5.925 -38.755  1.00 48.61           N  
ANISOU 1156  N   TRP A 169     7236   6546   4688   -903    718  -1085       N  
ATOM   1157  CA  TRP A 169     -15.730  -6.835 -39.833  1.00 42.82           C  
ANISOU 1157  CA  TRP A 169     6503   5797   3967   -846    727  -1052       C  
ATOM   1158  C   TRP A 169     -16.931  -7.235 -40.685  1.00 43.61           C  
ANISOU 1158  C   TRP A 169     6479   5900   4191   -806    757  -1236       C  
ATOM   1159  O   TRP A 169     -16.828  -7.325 -41.908  1.00 43.52           O  
ANISOU 1159  O   TRP A 169     6420   5908   4206   -696    687  -1256       O  
ATOM   1160  CB  TRP A 169     -15.049  -8.084 -39.272  1.00 38.30           C  
ANISOU 1160  CB  TRP A 169     6053   5162   3338   -958    848   -926       C  
ATOM   1161  CG  TRP A 169     -13.606  -7.874 -38.946  1.00 35.53           C  
ANISOU 1161  CG  TRP A 169     5817   4798   2887   -946    776   -698       C  
ATOM   1162  CD1 TRP A 169     -13.070  -7.617 -37.719  1.00 35.42           C  
ANISOU 1162  CD1 TRP A 169     5891   4763   2804  -1025    769   -573       C  
ATOM   1163  CD2 TRP A 169     -12.509  -7.896 -39.868  1.00 37.89           C  
ANISOU 1163  CD2 TRP A 169     6136   5099   3162   -839    687   -559       C  
ATOM   1164  NE1 TRP A 169     -11.706  -7.481 -37.818  1.00 36.49           N  
ANISOU 1164  NE1 TRP A 169     6084   4880   2900   -963    670   -362       N  
ATOM   1165  CE2 TRP A 169     -11.337  -7.647 -39.127  1.00 39.08           C  
ANISOU 1165  CE2 TRP A 169     6372   5220   3257   -852    624   -344       C  
ATOM   1166  CE3 TRP A 169     -12.405  -8.103 -41.247  1.00 33.57           C  
ANISOU 1166  CE3 TRP A 169     5531   4579   2645   -729    651   -596       C  
ATOM   1167  CZ2 TRP A 169     -10.075  -7.600 -39.720  1.00 34.13           C  
ANISOU 1167  CZ2 TRP A 169     5758   4580   2629   -754    530   -161       C  
ATOM   1168  CZ3 TRP A 169     -11.153  -8.056 -41.833  1.00 30.90           C  
ANISOU 1168  CZ3 TRP A 169     5231   4240   2271   -647    571   -415       C  
ATOM   1169  CH2 TRP A 169     -10.005  -7.806 -41.070  1.00 32.05           C  
ANISOU 1169  CH2 TRP A 169     5446   4345   2386   -658    513   -195       C  
ATOM   1170  N   ALA A 170     -18.068  -7.468 -40.036  1.00 42.13           N  
ANISOU 1170  N   ALA A 170     6238   5692   4078   -897    857  -1363       N  
ATOM   1171  CA  ALA A 170     -19.285  -7.861 -40.740  1.00 41.18           C  
ANISOU 1171  CA  ALA A 170     5992   5565   4090   -870    885  -1527       C  
ATOM   1172  C   ALA A 170     -19.754  -6.764 -41.690  1.00 42.24           C  
ANISOU 1172  C   ALA A 170     6030   5739   4280   -734    730  -1599       C  
ATOM   1173  O   ALA A 170     -19.957  -7.008 -42.883  1.00 42.68           O  
ANISOU 1173  O   ALA A 170     6030   5803   4382   -647    673  -1643       O  
ATOM   1174  CB  ALA A 170     -20.385  -8.208 -39.747  1.00 36.16           C  
ANISOU 1174  CB  ALA A 170     5317   4902   3522  -1004   1025  -1635       C  
ATOM   1175  N   VAL A 171     -19.920  -5.557 -41.155  1.00 39.33           N  
ANISOU 1175  N   VAL A 171     5648   5389   3905   -727    665  -1611       N  
ATOM   1176  CA  VAL A 171     -20.358  -4.415 -41.949  1.00 40.84           C  
ANISOU 1176  CA  VAL A 171     5761   5602   4153   -621    524  -1671       C  
ATOM   1177  C   VAL A 171     -19.376  -4.124 -43.082  1.00 43.64           C  
ANISOU 1177  C   VAL A 171     6158   5983   4439   -501    392  -1574       C  
ATOM   1178  O   VAL A 171     -19.785  -3.885 -44.220  1.00 45.97           O  
ANISOU 1178  O   VAL A 171     6392   6292   4785   -425    310  -1626       O  
ATOM   1179  CB  VAL A 171     -20.530  -3.155 -41.075  1.00 40.16           C  
ANISOU 1179  CB  VAL A 171     5665   5523   4069   -643    484  -1691       C  
ATOM   1180  CG1 VAL A 171     -20.779  -1.927 -41.940  1.00 40.00           C  
ANISOU 1180  CG1 VAL A 171     5578   5516   4104   -543    331  -1730       C  
ATOM   1181  CG2 VAL A 171     -21.665  -3.353 -40.080  1.00 38.13           C  
ANISOU 1181  CG2 VAL A 171     5347   5250   3890   -758    616  -1810       C  
ATOM   1182  N   SER A 172     -18.084  -4.164 -42.769  1.00 42.95           N  
ANISOU 1182  N   SER A 172     6176   5909   4236   -496    378  -1425       N  
ATOM   1183  CA  SER A 172     -17.045  -3.934 -43.770  1.00 43.42           C  
ANISOU 1183  CA  SER A 172     6277   6001   4219   -390    267  -1316       C  
ATOM   1184  C   SER A 172     -17.136  -4.942 -44.912  1.00 41.67           C  
ANISOU 1184  C   SER A 172     6034   5782   4017   -346    292  -1345       C  
ATOM   1185  O   SER A 172     -17.163  -4.563 -46.083  1.00 38.68           O  
ANISOU 1185  O   SER A 172     5628   5430   3640   -259    193  -1357       O  
ATOM   1186  CB  SER A 172     -15.657  -3.995 -43.132  1.00 44.83           C  
ANISOU 1186  CB  SER A 172     6560   6193   4282   -414    273  -1136       C  
ATOM   1187  OG  SER A 172     -15.502  -2.993 -42.143  1.00 44.60           O  
ANISOU 1187  OG  SER A 172     6551   6165   4230   -449    233  -1106       O  
ATOM   1188  N   LEU A 173     -17.186  -6.224 -44.564  1.00 41.70           N  
ANISOU 1188  N   LEU A 173     6053   5757   4035   -422    429  -1356       N  
ATOM   1189  CA  LEU A 173     -17.296  -7.289 -45.555  1.00 27.14           C  
ANISOU 1189  CA  LEU A 173     4181   3907   2222   -391    469  -1401       C  
ATOM   1190  C   LEU A 173     -18.562  -7.153 -46.394  1.00 40.15           C  
ANISOU 1190  C   LEU A 173     5720   5559   3976   -354    428  -1552       C  
ATOM   1191  O   LEU A 173     -18.561  -7.455 -47.588  1.00 37.41           O  
ANISOU 1191  O   LEU A 173     5347   5234   3634   -287    384  -1578       O  
ATOM   1192  CB  LEU A 173     -17.273  -8.659 -44.871  1.00 27.72           C  
ANISOU 1192  CB  LEU A 173     4286   3928   2319   -508    638  -1402       C  
ATOM   1193  CG  LEU A 173     -15.927  -9.171 -44.356  1.00 29.76           C  
ANISOU 1193  CG  LEU A 173     4667   4166   2476   -560    699  -1232       C  
ATOM   1194  CD1 LEU A 173     -16.107 -10.470 -43.589  1.00 28.08           C  
ANISOU 1194  CD1 LEU A 173     4496   3874   2299   -702    878  -1245       C  
ATOM   1195  CD2 LEU A 173     -14.954  -9.363 -45.506  1.00 32.81           C  
ANISOU 1195  CD2 LEU A 173     5076   4586   2806   -458    639  -1153       C  
ATOM   1196  N   ALA A 174     -19.638  -6.690 -45.765  1.00 44.08           N  
ANISOU 1196  N   ALA A 174     6150   6039   4558   -408    446  -1650       N  
ATOM   1197  CA  ALA A 174     -20.933  -6.604 -46.429  1.00 44.78           C  
ANISOU 1197  CA  ALA A 174     6119   6132   4763   -395    422  -1792       C  
ATOM   1198  C   ALA A 174     -21.016  -5.444 -47.420  1.00 45.77           C  
ANISOU 1198  C   ALA A 174     6202   6304   4884   -309    268  -1797       C  
ATOM   1199  O   ALA A 174     -21.470  -5.622 -48.550  1.00 47.16           O  
ANISOU 1199  O   ALA A 174     6308   6512   5098   -266    221  -1861       O  
ATOM   1200  CB  ALA A 174     -22.044  -6.485 -45.392  1.00 45.21           C  
ANISOU 1200  CB  ALA A 174     6104   6158   4915   -488    505  -1892       C  
ATOM   1201  N   ILE A 175     -20.578  -4.259 -47.003  1.00 44.62           N  
ANISOU 1201  N   ILE A 175     6090   6171   4695   -294    189  -1734       N  
ATOM   1202  CA  ILE A 175     -20.753  -3.065 -47.827  1.00 42.65           C  
ANISOU 1202  CA  ILE A 175     5773   5970   4464   -234     47  -1748       C  
ATOM   1203  C   ILE A 175     -19.725  -2.950 -48.951  1.00 43.28           C  
ANISOU 1203  C   ILE A 175     5898   6107   4440   -157    -48  -1642       C  
ATOM   1204  O   ILE A 175     -19.839  -2.075 -49.810  1.00 39.74           O  
ANISOU 1204  O   ILE A 175     5372   5723   4003   -103   -173  -1649       O  
ATOM   1205  CB  ILE A 175     -20.688  -1.777 -46.979  1.00 41.16           C  
ANISOU 1205  CB  ILE A 175     5582   5772   4284   -251     -7  -1729       C  
ATOM   1206  CG1 ILE A 175     -19.269  -1.551 -46.455  1.00 37.90           C  
ANISOU 1206  CG1 ILE A 175     5306   5354   3740   -241    -30  -1569       C  
ATOM   1207  CG2 ILE A 175     -21.698  -1.832 -45.843  1.00 41.31           C  
ANISOU 1207  CG2 ILE A 175     5549   5746   4400   -332     95  -1835       C  
ATOM   1208  CD1 ILE A 175     -19.104  -0.271 -45.670  1.00 34.81           C  
ANISOU 1208  CD1 ILE A 175     4915   4956   3354   -255    -95  -1548       C  
ATOM   1209  N   MET A 176     -18.726  -3.827 -48.951  1.00 45.99           N  
ANISOU 1209  N   MET A 176     6350   6437   4688   -150     10  -1543       N  
ATOM   1210  CA  MET A 176     -17.672  -3.759 -49.959  1.00 43.38           C  
ANISOU 1210  CA  MET A 176     6063   6164   4254    -84    -63  -1428       C  
ATOM   1211  C   MET A 176     -17.854  -4.783 -51.074  1.00 51.54           C  
ANISOU 1211  C   MET A 176     7064   7227   5293    -56    -30  -1484       C  
ATOM   1212  O   MET A 176     -16.976  -4.946 -51.919  1.00 50.43           O  
ANISOU 1212  O   MET A 176     6959   7138   5066     -8    -63  -1396       O  
ATOM   1213  CB  MET A 176     -16.298  -3.942 -49.311  1.00 33.10           C  
ANISOU 1213  CB  MET A 176     4899   4838   2840    -83    -32  -1265       C  
ATOM   1214  CG  MET A 176     -15.899  -2.806 -48.387  1.00 35.49           C  
ANISOU 1214  CG  MET A 176     5238   5129   3116    -98    -96  -1187       C  
ATOM   1215  SD  MET A 176     -16.051  -1.186 -49.162  1.00 45.98           S  
ANISOU 1215  SD  MET A 176     6457   6539   4475    -57   -275  -1171       S  
ATOM   1216  CE  MET A 176     -15.665  -0.116 -47.778  1.00 25.68           C  
ANISOU 1216  CE  MET A 176     3937   3925   1895    -99   -312  -1108       C  
ATOM   1217  N   VAL A 177     -18.996  -5.464 -51.083  1.00 51.43           N  
ANISOU 1217  N   VAL A 177     6973   7185   5383    -89     36  -1629       N  
ATOM   1218  CA  VAL A 177     -19.287  -6.423 -52.146  1.00 54.41           C  
ANISOU 1218  CA  VAL A 177     7305   7591   5779    -67     60  -1703       C  
ATOM   1219  C   VAL A 177     -19.502  -5.800 -53.543  1.00 53.29           C  
ANISOU 1219  C   VAL A 177     7075   7555   5618      1    -72  -1732       C  
ATOM   1220  O   VAL A 177     -19.318  -6.500 -54.544  1.00 56.39           O  
ANISOU 1220  O   VAL A 177     7458   7991   5976     34    -68  -1752       O  
ATOM   1221  CB  VAL A 177     -20.519  -7.305 -51.794  1.00 46.55           C  
ANISOU 1221  CB  VAL A 177     6231   6541   4912   -125    156  -1851       C  
ATOM   1222  CG1 VAL A 177     -20.269  -8.075 -50.503  1.00 44.56           C  
ANISOU 1222  CG1 VAL A 177     6048   6209   4675   -194    290  -1820       C  
ATOM   1223  CG2 VAL A 177     -21.791  -6.480 -51.690  1.00 49.86           C  
ANISOU 1223  CG2 VAL A 177     6530   6975   5439   -142    101  -1962       C  
ATOM   1224  N   PRO A 178     -19.881  -4.502 -53.640  1.00 50.09           N  
ANISOU 1224  N   PRO A 178     6597   7199   5236     28   -193  -1737       N  
ATOM   1225  CA  PRO A 178     -19.888  -4.005 -55.022  1.00 47.18           C  
ANISOU 1225  CA  PRO A 178     6153   6948   4827    108   -326  -1738       C  
ATOM   1226  C   PRO A 178     -18.484  -3.921 -55.614  1.00 50.77           C  
ANISOU 1226  C   PRO A 178     6690   7461   5141    162   -365  -1570       C  
ATOM   1227  O   PRO A 178     -18.314  -4.120 -56.819  1.00 49.72           O  
ANISOU 1227  O   PRO A 178     6528   7414   4949    218   -415  -1565       O  
ATOM   1228  CB  PRO A 178     -20.506  -2.607 -54.895  1.00 43.14           C  
ANISOU 1228  CB  PRO A 178     5546   6466   4380    134   -451  -1764       C  
ATOM   1229  CG  PRO A 178     -21.271  -2.641 -53.628  1.00 44.64           C  
ANISOU 1229  CG  PRO A 178     5723   6556   4681     55   -360  -1849       C  
ATOM   1230  CD  PRO A 178     -20.477  -3.514 -52.719  1.00 44.80           C  
ANISOU 1230  CD  PRO A 178     5884   6495   4644     -3   -223  -1770       C  
ATOM   1231  N   GLN A 179     -17.500  -3.629 -54.767  1.00 49.56           N  
ANISOU 1231  N   GLN A 179     6633   7263   4933    144   -340  -1432       N  
ATOM   1232  CA  GLN A 179     -16.105  -3.574 -55.190  1.00 50.42           C  
ANISOU 1232  CA  GLN A 179     6817   7414   4926    188   -363  -1253       C  
ATOM   1233  C   GLN A 179     -15.694  -4.896 -55.823  1.00 51.61           C  
ANISOU 1233  C   GLN A 179     7012   7567   5031    189   -264  -1273       C  
ATOM   1234  O   GLN A 179     -15.110  -4.925 -56.904  1.00 56.61           O  
ANISOU 1234  O   GLN A 179     7637   8282   5591    248   -309  -1207       O  
ATOM   1235  CB  GLN A 179     -15.190  -3.252 -54.007  1.00 50.31           C  
ANISOU 1235  CB  GLN A 179     6902   7334   4880    151   -331  -1116       C  
ATOM   1236  CG  GLN A 179     -13.780  -2.856 -54.407  1.00 49.76           C  
ANISOU 1236  CG  GLN A 179     6876   7306   4723    202   -386   -899       C  
ATOM   1237  CD  GLN A 179     -13.719  -1.454 -54.976  1.00 51.65           C  
ANISOU 1237  CD  GLN A 179     7038   7610   4977    273   -547   -803       C  
ATOM   1238  OE1 GLN A 179     -13.245  -1.242 -56.092  1.00 50.19           O  
ANISOU 1238  OE1 GLN A 179     6826   7490   4755    337   -608   -709       O  
ATOM   1239  NE2 GLN A 179     -14.201  -0.485 -54.208  1.00 54.95           N  
ANISOU 1239  NE2 GLN A 179     7419   8000   5458    257   -610   -826       N  
ATOM   1240  N   ALA A 180     -16.015  -5.990 -55.140  1.00 50.97           N  
ANISOU 1240  N   ALA A 180     6975   7390   5000    127   -126  -1361       N  
ATOM   1241  CA  ALA A 180     -15.732  -7.325 -55.647  1.00 44.56           C  
ANISOU 1241  CA  ALA A 180     6193   6562   4174    126    -23  -1403       C  
ATOM   1242  C   ALA A 180     -16.542  -7.608 -56.905  1.00 45.50           C  
ANISOU 1242  C   ALA A 180     6211   6759   4318    159    -68  -1534       C  
ATOM   1243  O   ALA A 180     -16.067  -8.280 -57.818  1.00 45.57           O  
ANISOU 1243  O   ALA A 180     6228   6813   4274    190    -43  -1537       O  
ATOM   1244  CB  ALA A 180     -16.024  -8.370 -54.584  1.00 37.67           C  
ANISOU 1244  CB  ALA A 180     5367   5570   3375     65    119  -1466       C  
ATOM   1245  N   ALA A 181     -17.763  -7.083 -56.949  1.00 45.38           N  
ANISOU 1245  N   ALA A 181     6097   6763   4383    152   -136  -1647       N  
ATOM   1246  CA  ALA A 181     -18.670  -7.346 -58.062  1.00 46.97           C  
ANISOU 1246  CA  ALA A 181     6193   7037   4615    178   -185  -1784       C  
ATOM   1247  C   ALA A 181     -18.191  -6.735 -59.378  1.00 49.16           C  
ANISOU 1247  C   ALA A 181     6445   7454   4781    259   -308  -1719       C  
ATOM   1248  O   ALA A 181     -18.204  -7.399 -60.414  1.00 51.29           O  
ANISOU 1248  O   ALA A 181     6693   7786   5010    284   -303  -1779       O  
ATOM   1249  CB  ALA A 181     -20.066  -6.839 -57.729  1.00 33.41           C  
ANISOU 1249  CB  ALA A 181     4370   5307   3019    154   -232  -1911       C  
ATOM   1250  N   VAL A 182     -17.769  -5.475 -59.336  1.00 53.70           N  
ANISOU 1250  N   VAL A 182     7020   8076   5308    301   -419  -1592       N  
ATOM   1251  CA  VAL A 182     -17.453  -4.745 -60.563  1.00 51.92           C  
ANISOU 1251  CA  VAL A 182     6760   7979   4989    381   -549  -1513       C  
ATOM   1252  C   VAL A 182     -16.030  -4.967 -61.068  1.00 53.44           C  
ANISOU 1252  C   VAL A 182     7035   8207   5061    414   -519  -1352       C  
ATOM   1253  O   VAL A 182     -15.688  -4.534 -62.168  1.00 53.93           O  
ANISOU 1253  O   VAL A 182     7080   8372   5040    473   -602  -1277       O  
ATOM   1254  CB  VAL A 182     -17.665  -3.231 -60.381  1.00 36.80           C  
ANISOU 1254  CB  VAL A 182     4795   6088   3098    418   -690  -1432       C  
ATOM   1255  CG1 VAL A 182     -19.118  -2.941 -60.060  1.00 58.81           C  
ANISOU 1255  CG1 VAL A 182     7480   8852   6011    396   -730  -1603       C  
ATOM   1256  CG2 VAL A 182     -16.747  -2.691 -59.295  1.00 35.38           C  
ANISOU 1256  CG2 VAL A 182     4691   5835   2916    400   -668  -1276       C  
ATOM   1257  N   MET A 183     -15.203  -5.638 -60.273  1.00 50.69           N  
ANISOU 1257  N   MET A 183     6779   7773   4710    374   -398  -1293       N  
ATOM   1258  CA  MET A 183     -13.830  -5.908 -60.685  1.00 47.21           C  
ANISOU 1258  CA  MET A 183     6409   7355   4174    403   -358  -1144       C  
ATOM   1259  C   MET A 183     -13.785  -6.894 -61.846  1.00 46.63           C  
ANISOU 1259  C   MET A 183     6325   7347   4047    421   -308  -1236       C  
ATOM   1260  O   MET A 183     -14.328  -7.994 -61.761  1.00 50.07           O  
ANISOU 1260  O   MET A 183     6754   7734   4536    380   -213  -1394       O  
ATOM   1261  CB  MET A 183     -12.999  -6.436 -59.515  1.00 41.66           C  
ANISOU 1261  CB  MET A 183     5802   6539   3488    354   -240  -1068       C  
ATOM   1262  CG  MET A 183     -12.506  -5.346 -58.582  1.00 41.19           C  
ANISOU 1262  CG  MET A 183     5770   6439   3440    351   -301   -907       C  
ATOM   1263  SD  MET A 183     -11.971  -3.886 -59.495  1.00 46.80           S  
ANISOU 1263  SD  MET A 183     6433   7238   4111    431   -463   -722       S  
ATOM   1264  CE  MET A 183     -11.413  -2.830 -58.164  1.00 51.12           C  
ANISOU 1264  CE  MET A 183     7013   7692   4717    405   -505   -555       C  
ATOM   1265  N   GLU A 184     -13.140  -6.483 -62.933  1.00 43.55           N  
ANISOU 1265  N   GLU A 184     5929   7059   3557    480   -371  -1134       N  
ATOM   1266  CA  GLU A 184     -13.014  -7.318 -64.120  1.00 47.23           C  
ANISOU 1266  CA  GLU A 184     6388   7607   3953    499   -330  -1216       C  
ATOM   1267  C   GLU A 184     -11.596  -7.276 -64.679  1.00 45.33           C  
ANISOU 1267  C   GLU A 184     6201   7406   3615    537   -301  -1049       C  
ATOM   1268  O   GLU A 184     -10.850  -6.314 -64.456  1.00 35.53           O  
ANISOU 1268  O   GLU A 184     4981   6157   2362    562   -358   -854       O  
ATOM   1269  CB  GLU A 184     -14.019  -6.887 -65.192  1.00 55.88           C  
ANISOU 1269  CB  GLU A 184     7399   8819   5015    530   -448  -1312       C  
ATOM   1270  CG  GLU A 184     -15.472  -7.182 -64.834  1.00 65.21           C  
ANISOU 1270  CG  GLU A 184     8509   9964   6303    493   -460  -1511       C  
ATOM   1271  CD  GLU A 184     -15.751  -8.667 -64.677  1.00 71.01           C  
ANISOU 1271  CD  GLU A 184     9252  10629   7101    442   -321  -1676       C  
ATOM   1272  OE1 GLU A 184     -15.105  -9.472 -65.383  1.00 71.37           O  
ANISOU 1272  OE1 GLU A 184     9329  10709   7081    452   -250  -1692       O  
ATOM   1273  OE2 GLU A 184     -16.615  -9.027 -63.848  1.00 72.41           O  
ANISOU 1273  OE2 GLU A 184     9399  10710   7402    392   -279  -1787       O  
ATOM   1274  N   CYS A 185     -11.240  -8.330 -65.408  1.00 52.32           N  
ANISOU 1274  N   CYS A 185     7103   8326   4450    538   -208  -1132       N  
ATOM   1275  CA  CYS A 185      -9.897  -8.494 -65.950  1.00 56.61           C  
ANISOU 1275  CA  CYS A 185     7694   8905   4912    569   -151  -1003       C  
ATOM   1276  C   CYS A 185      -9.852  -8.122 -67.432  1.00 52.52           C  
ANISOU 1276  C   CYS A 185     7144   8536   4274    615   -224   -991       C  
ATOM   1277  O   CYS A 185     -10.027  -8.975 -68.303  1.00 35.93           O  
ANISOU 1277  O   CYS A 185     5032   6500   2118    614   -172  -1133       O  
ATOM   1278  CB  CYS A 185      -9.420  -9.935 -65.746  1.00 33.23           C  
ANISOU 1278  CB  CYS A 185     4774   5873   1978    539     19  -1102       C  
ATOM   1279  SG  CYS A 185      -7.628 -10.135 -65.642  1.00 68.28           S  
ANISOU 1279  SG  CYS A 185     9280  10285   6379    563    120   -913       S  
ATOM   1280  N   SER A 186      -9.619  -6.842 -67.709  1.00 45.70           N  
ANISOU 1280  N   SER A 186     6268   7717   3378    650   -342   -821       N  
ATOM   1281  CA  SER A 186      -9.571  -6.346 -69.082  1.00 53.77           C  
ANISOU 1281  CA  SER A 186     7269   8876   4285    687   -418   -782       C  
ATOM   1282  C   SER A 186      -8.291  -6.782 -69.788  1.00 60.14           C  
ANISOU 1282  C   SER A 186     8121   9728   5001    707   -326   -702       C  
ATOM   1283  O   SER A 186      -7.373  -7.311 -69.160  1.00 67.03           O  
ANISOU 1283  O   SER A 186     9036  10518   5914    699   -217   -648       O  
ATOM   1284  CB  SER A 186      -9.690  -4.821 -69.103  1.00 56.82           C  
ANISOU 1284  CB  SER A 186     7631   9264   4692    705   -561   -612       C  
ATOM   1285  OG  SER A 186      -9.647  -4.324 -70.429  1.00 62.98           O  
ANISOU 1285  OG  SER A 186     8399  10168   5360    732   -634   -563       O  
ATOM   1286  N   SER A 187      -8.234  -6.548 -71.095  1.00 58.65           N  
ANISOU 1286  N   SER A 187     7922   9673   4688    732   -370   -694       N  
ATOM   1287  CA  SER A 187      -7.111  -6.994 -71.910  1.00 59.06           C  
ANISOU 1287  CA  SER A 187     8011   9789   4639    750   -277   -645       C  
ATOM   1288  C   SER A 187      -6.882  -6.075 -73.107  1.00 57.04           C  
ANISOU 1288  C   SER A 187     7752   9656   4265    777   -368   -525       C  
ATOM   1289  O   SER A 187      -5.761  -5.637 -73.367  1.00 54.92           O  
ANISOU 1289  O   SER A 187     7510   9386   3971    795   -341   -352       O  
ATOM   1290  CB  SER A 187      -7.348  -8.426 -72.389  1.00 62.79           C  
ANISOU 1290  CB  SER A 187     8487  10307   5064    732   -162   -874       C  
ATOM   1291  OG  SER A 187      -8.563  -8.528 -73.109  1.00 69.69           O  
ANISOU 1291  OG  SER A 187     9318  11278   5885    725   -242  -1040       O  
ATOM   1292  N   VAL A 188      -7.958  -5.790 -73.831  1.00 64.55           N  
ANISOU 1292  N   VAL A 188     9418   9196   5910    323   -600  -1908       N  
ATOM   1293  CA  VAL A 188      -7.896  -4.945 -75.015  1.00 63.88           C  
ANISOU 1293  CA  VAL A 188     9485   8984   5801    435   -780  -1881       C  
ATOM   1294  C   VAL A 188      -9.260  -4.279 -75.194  1.00 69.51           C  
ANISOU 1294  C   VAL A 188    10074   9872   6465    843   -985  -2086       C  
ATOM   1295  O   VAL A 188     -10.199  -4.593 -74.460  1.00 69.95           O  
ANISOU 1295  O   VAL A 188     9843  10212   6525    978   -960  -2271       O  
ATOM   1296  CB  VAL A 188      -7.504  -5.763 -76.272  1.00 56.62           C  
ANISOU 1296  CB  VAL A 188     8585   8005   4923    206   -767  -1812       C  
ATOM   1297  CG1 VAL A 188      -8.697  -6.544 -76.801  1.00 50.51           C  
ANISOU 1297  CG1 VAL A 188     7577   7452   4163    306   -846  -1990       C  
ATOM   1298  CG2 VAL A 188      -6.912  -4.865 -77.355  1.00 60.36           C  
ANISOU 1298  CG2 VAL A 188     9249   8288   5396    259   -879  -1716       C  
ATOM   1299  N   LEU A 189      -9.363  -3.353 -76.145  1.00 69.12           N  
ANISOU 1299  N   LEU A 189    10212   9680   6369   1053  -1176  -2070       N  
ATOM   1300  CA  LEU A 189     -10.614  -2.645 -76.408  1.00 75.44           C  
ANISOU 1300  CA  LEU A 189    10926  10634   7105   1496  -1400  -2267       C  
ATOM   1301  C   LEU A 189     -11.771  -3.601 -76.667  1.00 75.89           C  
ANISOU 1301  C   LEU A 189    10564  11072   7199   1558  -1431  -2508       C  
ATOM   1302  O   LEU A 189     -11.623  -4.576 -77.405  1.00 76.26           O  
ANISOU 1302  O   LEU A 189    10527  11146   7302   1311  -1376  -2487       O  
ATOM   1303  CB  LEU A 189     -10.457  -1.700 -77.601  1.00 77.12           C  
ANISOU 1303  CB  LEU A 189    11456  10588   7259   1685  -1590  -2190       C  
ATOM   1304  CG  LEU A 189      -9.438  -0.570 -77.460  1.00 79.93           C  
ANISOU 1304  CG  LEU A 189    12208  10586   7574   1668  -1576  -1992       C  
ATOM   1305  CD1 LEU A 189      -9.480   0.336 -78.681  1.00 79.87           C  
ANISOU 1305  CD1 LEU A 189    12520  10333   7495   1901  -1769  -1948       C  
ATOM   1306  CD2 LEU A 189      -9.690   0.221 -76.184  1.00 82.80           C  
ANISOU 1306  CD2 LEU A 189    12595  10980   7883   1875  -1578  -2036       C  
ATOM   1307  N   PRO A 190     -12.930  -3.325 -76.049  1.00 77.92           N  
ANISOU 1307  N   PRO A 190    10526  11654   7426   1877  -1507  -2753       N  
ATOM   1308  CA  PRO A 190     -14.140  -4.125 -76.256  1.00 78.58           C  
ANISOU 1308  CA  PRO A 190    10117  12190   7548   1946  -1527  -3043       C  
ATOM   1309  C   PRO A 190     -14.609  -4.063 -77.705  1.00 83.36           C  
ANISOU 1309  C   PRO A 190    10727  12809   8136   2111  -1738  -3116       C  
ATOM   1310  O   PRO A 190     -14.228  -3.138 -78.424  1.00 85.24           O  
ANISOU 1310  O   PRO A 190    11351  12728   8307   2298  -1902  -2979       O  
ATOM   1311  CB  PRO A 190     -15.166  -3.470 -75.324  1.00 80.24           C  
ANISOU 1311  CB  PRO A 190    10068  12713   7707   2317  -1595  -3281       C  
ATOM   1312  CG  PRO A 190     -14.353  -2.721 -74.318  1.00 78.31           C  
ANISOU 1312  CG  PRO A 190    10150  12180   7424   2306  -1518  -3082       C  
ATOM   1313  CD  PRO A 190     -13.140  -2.255 -75.060  1.00 76.40           C  
ANISOU 1313  CD  PRO A 190    10415  11448   7163   2167  -1556  -2783       C  
ATOM   1314  N   GLU A 191     -15.418  -5.037 -78.114  1.00 85.93           N  
ANISOU 1314  N   GLU A 191    10630  13499   8522   2024  -1713  -3333       N  
ATOM   1315  CA  GLU A 191     -15.975  -5.084 -79.464  1.00 94.18           C  
ANISOU 1315  CA  GLU A 191    11619  14612   9554   2179  -1906  -3435       C  
ATOM   1316  C   GLU A 191     -14.878  -5.093 -80.527  1.00 87.73           C  
ANISOU 1316  C   GLU A 191    11264  13334   8735   1972  -1929  -3136       C  
ATOM   1317  O   GLU A 191     -15.006  -4.457 -81.574  1.00 87.33           O  
ANISOU 1317  O   GLU A 191    11426  13130   8624   2217  -2136  -3118       O  
ATOM   1318  CB  GLU A 191     -16.926  -3.906 -79.689  1.00103.83           C  
ANISOU 1318  CB  GLU A 191    12815  15962  10675   2769  -2183  -3630       C  
ATOM   1319  CG  GLU A 191     -18.027  -3.806 -78.645  1.00110.38           C  
ANISOU 1319  CG  GLU A 191    13166  17279  11493   3008  -2167  -3946       C  
ATOM   1320  CD  GLU A 191     -18.820  -2.520 -78.749  1.00117.83           C  
ANISOU 1320  CD  GLU A 191    14158  18296  12317   3639  -2444  -4109       C  
ATOM   1321  OE1 GLU A 191     -18.468  -1.669 -79.592  1.00119.95           O  
ANISOU 1321  OE1 GLU A 191    14881  18188  12505   3884  -2637  -3955       O  
ATOM   1322  OE2 GLU A 191     -19.795  -2.360 -77.985  1.00121.99           O  
ANISOU 1322  OE2 GLU A 191    14273  19256  12821   3893  -2460  -4397       O  
ATOM   1323  N   LEU A 192     -13.801  -5.819 -80.245  1.00 78.90           N  
ANISOU 1323  N   LEU A 192    10293  12007   7677   1527  -1708  -2915       N  
ATOM   1324  CA  LEU A 192     -12.689  -5.955 -81.178  1.00 68.12           C  
ANISOU 1324  CA  LEU A 192     9307  10257   6317   1271  -1683  -2646       C  
ATOM   1325  C   LEU A 192     -12.462  -7.428 -81.506  1.00 65.45           C  
ANISOU 1325  C   LEU A 192     8804   9996   6068    864  -1516  -2619       C  
ATOM   1326  O   LEU A 192     -12.195  -8.234 -80.615  1.00 67.14           O  
ANISOU 1326  O   LEU A 192     8877  10293   6339    609  -1303  -2603       O  
ATOM   1327  CB  LEU A 192     -11.418  -5.330 -80.596  1.00 59.26           C  
ANISOU 1327  CB  LEU A 192     8561   8780   5173   1132  -1572  -2387       C  
ATOM   1328  CG  LEU A 192     -10.153  -5.354 -81.457  1.00 51.10           C  
ANISOU 1328  CG  LEU A 192     7859   7404   4153    853  -1505  -2132       C  
ATOM   1329  CD1 LEU A 192     -10.357  -4.576 -82.748  1.00 51.54           C  
ANISOU 1329  CD1 LEU A 192     8123   7305   4153   1098  -1714  -2126       C  
ATOM   1330  CD2 LEU A 192      -8.967  -4.802 -80.680  1.00 43.93           C  
ANISOU 1330  CD2 LEU A 192     7169   6273   3250    706  -1361  -1943       C  
ATOM   1331  N   ALA A 193     -12.572  -7.772 -82.786  1.00 49.85           N  
ANISOU 1331  N   ALA A 193     6865   7979   4097    818  -1611  -2612       N  
ATOM   1332  CA  ALA A 193     -12.466  -9.160 -83.226  1.00 51.87           C  
ANISOU 1332  CA  ALA A 193     6973   8302   4432    464  -1476  -2598       C  
ATOM   1333  C   ALA A 193     -11.098  -9.761 -82.913  1.00 50.99           C  
ANISOU 1333  C   ALA A 193     7130   7890   4353     93  -1266  -2326       C  
ATOM   1334  O   ALA A 193     -10.976 -10.967 -82.693  1.00 52.13           O  
ANISOU 1334  O   ALA A 193     7120   8107   4578   -165  -1095  -2319       O  
ATOM   1335  CB  ALA A 193     -12.755  -9.261 -84.717  1.00 49.75           C  
ANISOU 1335  CB  ALA A 193     6759   7997   4146    509  -1636  -2615       C  
ATOM   1336  N   ASN A 194     -10.074  -8.916 -82.893  1.00 52.69           N  
ANISOU 1336  N   ASN A 194     7706   7800   4513     75  -1260  -2119       N  
ATOM   1337  CA  ASN A 194      -8.717  -9.365 -82.607  1.00 39.73           C  
ANISOU 1337  CA  ASN A 194     6287   5918   2890   -262  -1060  -1885       C  
ATOM   1338  C   ASN A 194      -8.439  -9.386 -81.105  1.00 38.75           C  
ANISOU 1338  C   ASN A 194     6140   5802   2780   -265   -931  -1863       C  
ATOM   1339  O   ASN A 194      -8.214  -8.344 -80.491  1.00 46.12           O  
ANISOU 1339  O   ASN A 194     7140   6711   3674   -149   -934  -1849       O  
ATOM   1340  CB  ASN A 194      -7.702  -8.474 -83.324  1.00 38.68           C  
ANISOU 1340  CB  ASN A 194     6297   5643   2755   -279  -1043  -1763       C  
ATOM   1341  CG  ASN A 194      -6.295  -9.032 -83.270  1.00 35.55           C  
ANISOU 1341  CG  ASN A 194     5759   5244   2506   -426   -848  -1663       C  
ATOM   1342  OD1 ASN A 194      -6.091 -10.204 -82.955  1.00 34.17           O  
ANISOU 1342  OD1 ASN A 194     5360   5127   2497   -350   -797  -1676       O  
ATOM   1343  ND2 ASN A 194      -5.313  -8.193 -83.583  1.00 34.70           N  
ANISOU 1343  ND2 ASN A 194     5849   4893   2444   -317   -883  -1518       N  
ATOM   1344  N   ARG A 195      -8.454 -10.581 -80.521  1.00 37.83           N  
ANISOU 1344  N   ARG A 195     5843   5773   2757   -354   -800  -1883       N  
ATOM   1345  CA  ARG A 195      -8.287 -10.742 -79.079  1.00 46.69           C  
ANISOU 1345  CA  ARG A 195     6839   6992   3908   -366   -629  -1890       C  
ATOM   1346  C   ARG A 195      -6.818 -10.822 -78.656  1.00 41.59           C  
ANISOU 1346  C   ARG A 195     6426   6071   3306   -390   -558  -1661       C  
ATOM   1347  O   ARG A 195      -6.515 -11.099 -77.494  1.00 40.24           O  
ANISOU 1347  O   ARG A 195     6153   5970   3167   -449   -385  -1628       O  
ATOM   1348  CB  ARG A 195      -9.024 -11.995 -78.601  1.00 52.81           C  
ANISOU 1348  CB  ARG A 195     7195   8102   4767   -551   -416  -2041       C  
ATOM   1349  CG  ARG A 195     -10.541 -11.944 -78.738  1.00 41.24           C  
ANISOU 1349  CG  ARG A 195     5353   7024   3291   -452   -477  -2344       C  
ATOM   1350  CD  ARG A 195     -11.176 -11.096 -77.644  1.00 42.94           C  
ANISOU 1350  CD  ARG A 195     5423   7436   3457   -227   -498  -2500       C  
ATOM   1351  NE  ARG A 195     -11.283  -9.689 -78.018  1.00 44.01           N  
ANISOU 1351  NE  ARG A 195     5760   7453   3510    113   -762  -2501       N  
ATOM   1352  CZ  ARG A 195     -11.684  -8.727 -77.192  1.00 50.35           C  
ANISOU 1352  CZ  ARG A 195     6526   8345   4260    374   -825  -2592       C  
ATOM   1353  NH1 ARG A 195     -12.008  -9.018 -75.939  1.00 54.04           N  
ANISOU 1353  NH1 ARG A 195     6760   9026   4746    328   -646  -2694       N  
ATOM   1354  NH2 ARG A 195     -11.756  -7.473 -77.617  1.00 46.57           N  
ANISOU 1354  NH2 ARG A 195     6259   7729   3708    678  -1049  -2575       N  
ATOM   1355  N   THR A 196      -5.915 -10.580 -79.600  1.00 44.50           N  
ANISOU 1355  N   THR A 196     6905   6264   3737   -276   -673  -1562       N  
ATOM   1356  CA  THR A 196      -4.480 -10.658 -79.341  1.00 39.21           C  
ANISOU 1356  CA  THR A 196     6172   5550   3175   -368   -528  -1409       C  
ATOM   1357  C   THR A 196      -4.045  -9.635 -78.293  1.00 38.51           C  
ANISOU 1357  C   THR A 196     6088   5494   3052   -262   -513  -1414       C  
ATOM   1358  O   THR A 196      -4.561  -8.517 -78.255  1.00 41.39           O  
ANISOU 1358  O   THR A 196     6375   5992   3360   -213   -553  -1525       O  
ATOM   1359  CB  THR A 196      -3.671 -10.438 -80.635  1.00 35.95           C  
ANISOU 1359  CB  THR A 196     5798   5025   2836   -436   -547  -1308       C  
ATOM   1360  OG1 THR A 196      -4.176 -11.295 -81.666  1.00 31.38           O  
ANISOU 1360  OG1 THR A 196     5192   4450   2280   -504   -582  -1337       O  
ATOM   1361  CG2 THR A 196      -2.198 -10.736 -80.413  1.00 33.65           C  
ANISOU 1361  CG2 THR A 196     5584   4556   2646   -600   -395  -1066       C  
ATOM   1362  N   ARG A 197      -3.099 -10.027 -77.444  1.00 36.18           N  
ANISOU 1362  N   ARG A 197     5817   5108   2820   -385   -359  -1245       N  
ATOM   1363  CA  ARG A 197      -2.603  -9.152 -76.389  1.00 35.49           C  
ANISOU 1363  CA  ARG A 197     5748   5028   2708   -312   -338  -1228       C  
ATOM   1364  C   ARG A 197      -1.240  -9.596 -75.867  1.00 32.10           C  
ANISOU 1364  C   ARG A 197     5349   4475   2372   -459   -199  -1028       C  
ATOM   1365  O   ARG A 197      -0.794 -10.714 -76.129  1.00 29.45           O  
ANISOU 1365  O   ARG A 197     4996   4088   2106   -622    -91   -919       O  
ATOM   1366  CB  ARG A 197      -3.596  -9.104 -75.228  1.00 38.61           C  
ANISOU 1366  CB  ARG A 197     6121   5549   3001   -177   -339  -1359       C  
ATOM   1367  CG  ARG A 197      -3.770 -10.442 -74.529  1.00 43.86           C  
ANISOU 1367  CG  ARG A 197     6732   6236   3698   -379   -132  -1290       C  
ATOM   1368  CD  ARG A 197      -4.527 -10.295 -73.225  1.00 52.09           C  
ANISOU 1368  CD  ARG A 197     7739   7390   4662   -334    -47  -1380       C  
ATOM   1369  NE  ARG A 197      -4.759 -11.581 -72.576  1.00 54.29           N  
ANISOU 1369  NE  ARG A 197     7839   7794   4995   -553    196  -1369       N  
ATOM   1370  CZ  ARG A 197      -5.785 -12.380 -72.848  1.00 57.67           C  
ANISOU 1370  CZ  ARG A 197     8074   8405   5434   -701    296  -1501       C  
ATOM   1371  NH1 ARG A 197      -6.679 -12.029 -73.764  1.00 59.21           N  
ANISOU 1371  NH1 ARG A 197     8199   8703   5595   -643    159  -1658       N  
ATOM   1372  NH2 ARG A 197      -5.916 -13.533 -72.206  1.00 58.69           N  
ANISOU 1372  NH2 ARG A 197     8077   8615   5609   -903    526  -1485       N  
ATOM   1373  N   LEU A 198      -0.585  -8.711 -75.123  1.00 32.18           N  
ANISOU 1373  N   LEU A 198     5424   4444   2360   -437   -193   -993       N  
ATOM   1374  CA  LEU A 198       0.649  -9.057 -74.430  1.00 25.50           C  
ANISOU 1374  CA  LEU A 198     4617   3510   1561   -572    -76   -849       C  
ATOM   1375  C   LEU A 198       0.362  -9.288 -72.952  1.00 35.40           C  
ANISOU 1375  C   LEU A 198     5786   4881   2783   -490     -9   -886       C  
ATOM   1376  O   LEU A 198       0.832 -10.258 -72.359  1.00 42.46           O  
ANISOU 1376  O   LEU A 198     6639   5778   3716   -582    111   -809       O  
ATOM   1377  CB  LEU A 198       1.705  -7.960 -74.598  1.00 25.73           C  
ANISOU 1377  CB  LEU A 198     4804   3388   1583   -631   -107   -778       C  
ATOM   1378  CG  LEU A 198       2.283  -7.733 -75.996  1.00 25.75           C  
ANISOU 1378  CG  LEU A 198     4949   3223   1612   -749   -138   -697       C  
ATOM   1379  CD1 LEU A 198       1.449  -6.732 -76.778  1.00 27.21           C  
ANISOU 1379  CD1 LEU A 198     5240   3366   1731   -631   -269   -778       C  
ATOM   1380  CD2 LEU A 198       3.731  -7.280 -75.910  1.00 25.56           C  
ANISOU 1380  CD2 LEU A 198     5046   3066   1601   -896    -84   -592       C  
ATOM   1381  N   PHE A 199      -0.424  -8.391 -72.365  1.00 27.81           N  
ANISOU 1381  N   PHE A 199     4802   4022   1743   -315    -83  -1013       N  
ATOM   1382  CA  PHE A 199      -0.757  -8.482 -70.951  1.00 43.51           C  
ANISOU 1382  CA  PHE A 199     6742   6109   3683   -224    -19  -1049       C  
ATOM   1383  C   PHE A 199      -2.210  -8.095 -70.694  1.00 41.28           C  
ANISOU 1383  C   PHE A 199     6453   5949   3283    -62    -77  -1226       C  
ATOM   1384  O   PHE A 199      -2.894  -7.574 -71.576  1.00 37.23           O  
ANISOU 1384  O   PHE A 199     5913   5475   2757     -6   -189  -1328       O  
ATOM   1385  CB  PHE A 199       0.181  -7.599 -70.121  1.00 28.06           C  
ANISOU 1385  CB  PHE A 199     4840   4109   1713   -233    -15  -1003       C  
ATOM   1386  CG  PHE A 199       0.197  -6.156 -70.549  1.00 37.68           C  
ANISOU 1386  CG  PHE A 199     6151   5277   2887   -209   -118  -1055       C  
ATOM   1387  CD1 PHE A 199       1.030  -5.733 -71.573  1.00 37.99           C  
ANISOU 1387  CD1 PHE A 199     6346   5127   2961   -327   -154   -964       C  
ATOM   1388  CD2 PHE A 199      -0.612  -5.222 -69.922  1.00 39.48           C  
ANISOU 1388  CD2 PHE A 199     6346   5619   3035   -107   -153  -1182       C  
ATOM   1389  CE1 PHE A 199       1.051  -4.409 -71.972  1.00 37.10           C  
ANISOU 1389  CE1 PHE A 199     6410   4892   2794   -308   -234   -977       C  
ATOM   1390  CE2 PHE A 199      -0.595  -3.894 -70.315  1.00 41.60           C  
ANISOU 1390  CE2 PHE A 199     6798   5754   3255   -108   -229  -1186       C  
ATOM   1391  CZ  PHE A 199       0.239  -3.488 -71.342  1.00 39.97           C  
ANISOU 1391  CZ  PHE A 199     6791   5320   3075   -183   -279  -1078       C  
ATOM   1392  N   SER A 200      -2.673  -8.362 -69.478  1.00 45.09           N  
ANISOU 1392  N   SER A 200     6952   6470   3711    -15     22  -1240       N  
ATOM   1393  CA  SER A 200      -4.028  -8.016 -69.074  1.00 45.06           C  
ANISOU 1393  CA  SER A 200     7051   6464   3605     64     30  -1350       C  
ATOM   1394  C   SER A 200      -3.987  -7.093 -67.865  1.00 46.78           C  
ANISOU 1394  C   SER A 200     7372   6612   3790    169     40  -1321       C  
ATOM   1395  O   SER A 200      -2.970  -7.009 -67.177  1.00 48.83           O  
ANISOU 1395  O   SER A 200     7424   7011   4116    212     45  -1284       O  
ATOM   1396  CB  SER A 200      -4.831  -9.277 -68.753  1.00 44.94           C  
ANISOU 1396  CB  SER A 200     6836   6622   3617   -124    242  -1417       C  
ATOM   1397  OG  SER A 200      -4.699 -10.239 -69.785  1.00 45.82           O  
ANISOU 1397  OG  SER A 200     6855   6747   3808   -287    267  -1384       O  
ATOM   1398  N   VAL A 201      -5.090  -6.398 -67.608  1.00 45.56           N  
ANISOU 1398  N   VAL A 201     7265   6517   3527     16    116  -1477       N  
ATOM   1399  CA  VAL A 201      -5.177  -5.519 -66.446  1.00 44.67           C  
ANISOU 1399  CA  VAL A 201     7139   6467   3368     40    166  -1535       C  
ATOM   1400  C   VAL A 201      -6.417  -5.828 -65.620  1.00 49.47           C  
ANISOU 1400  C   VAL A 201     7537   7301   3958    238    236  -1690       C  
ATOM   1401  O   VAL A 201      -7.272  -6.614 -66.030  1.00 52.24           O  
ANISOU 1401  O   VAL A 201     7647   7856   4348    257    267  -1807       O  
ATOM   1402  CB  VAL A 201      -5.204  -4.032 -66.853  1.00 41.03           C  
ANISOU 1402  CB  VAL A 201     6679   6034   2876    146     -4  -1605       C  
ATOM   1403  CG1 VAL A 201      -3.917  -3.649 -67.573  1.00 37.06           C  
ANISOU 1403  CG1 VAL A 201     6157   5489   2435     18    -67  -1513       C  
ATOM   1404  CG2 VAL A 201      -6.418  -3.740 -67.717  1.00 46.01           C  
ANISOU 1404  CG2 VAL A 201     7261   6742   3478    398   -165  -1738       C  
ATOM   1405  N   CYS A 202      -6.506  -5.207 -64.450  1.00 44.89           N  
ANISOU 1405  N   CYS A 202     6967   6742   3348    317    285  -1711       N  
ATOM   1406  CA  CYS A 202      -7.653  -5.382 -63.571  1.00 44.40           C  
ANISOU 1406  CA  CYS A 202     6663   6921   3286    464    376  -1865       C  
ATOM   1407  C   CYS A 202      -8.262  -4.028 -63.237  1.00 47.79           C  
ANISOU 1407  C   CYS A 202     7085   7411   3660    717    238  -1978       C  
ATOM   1408  O   CYS A 202      -7.602  -3.179 -62.636  1.00 48.61           O  
ANISOU 1408  O   CYS A 202     7377   7360   3732    726    210  -1889       O  
ATOM   1409  CB  CYS A 202      -7.246  -6.114 -62.289  1.00 45.43           C  
ANISOU 1409  CB  CYS A 202     6824   7008   3431    365    588  -1763       C  
ATOM   1410  SG  CYS A 202      -8.618  -6.503 -61.177  1.00 53.49           S  
ANISOU 1410  SG  CYS A 202     7532   8323   4467    439    764  -1942       S  
ATOM   1411  N   ASP A 203      -9.516  -3.821 -63.624  1.00 51.55           N  
ANISOU 1411  N   ASP A 203     7325   8134   4129    937    144  -2182       N  
ATOM   1412  CA  ASP A 203     -10.155  -2.531 -63.375  1.00 54.99           C  
ANISOU 1412  CA  ASP A 203     7774   8619   4500   1259    -19  -2287       C  
ATOM   1413  C   ASP A 203     -11.657  -2.674 -63.139  1.00 54.40           C  
ANISOU 1413  C   ASP A 203     7320   8921   4427   1469    -14  -2549       C  
ATOM   1414  O   ASP A 203     -12.207  -3.769 -63.215  1.00 49.79           O  
ANISOU 1414  O   ASP A 203     6443   8569   3905   1316    129  -2658       O  
ATOM   1415  CB  ASP A 203      -9.891  -1.571 -64.539  1.00 58.43           C  
ANISOU 1415  CB  ASP A 203     8429   8879   4894   1402   -266  -2241       C  
ATOM   1416  CG  ASP A 203      -9.963  -0.111 -64.123  1.00 62.97           C  
ANISOU 1416  CG  ASP A 203     9200   9336   5389   1674   -410  -2232       C  
ATOM   1417  OD1 ASP A 203     -10.622   0.188 -63.105  1.00 63.67           O  
ANISOU 1417  OD1 ASP A 203     9172   9572   5448   1846   -369  -2333       O  
ATOM   1418  OD2 ASP A 203      -9.363   0.737 -64.817  1.00 64.24           O  
ANISOU 1418  OD2 ASP A 203     9639   9253   5516   1708   -552  -2122       O  
ATOM   1419  N   GLU A 204     -12.313  -1.555 -62.851  1.00 54.29           N  
ANISOU 1419  N   GLU A 204     7304   8978   4346   1805   -165  -2655       N  
ATOM   1420  CA  GLU A 204     -13.731  -1.555 -62.514  1.00 58.75           C  
ANISOU 1420  CA  GLU A 204     7485   9932   4907   2025   -170  -2924       C  
ATOM   1421  C   GLU A 204     -14.617  -1.474 -63.752  1.00 62.52           C  
ANISOU 1421  C   GLU A 204     7745  10638   5371   2246   -382  -3123       C  
ATOM   1422  O   GLU A 204     -14.472  -0.570 -64.574  1.00 59.34           O  
ANISOU 1422  O   GLU A 204     7576  10068   4902   2491   -629  -3080       O  
ATOM   1423  CB  GLU A 204     -14.042  -0.395 -61.569  1.00 62.45           C  
ANISOU 1423  CB  GLU A 204     8049  10382   5297   2315   -241  -2951       C  
ATOM   1424  CG  GLU A 204     -13.180  -0.381 -60.317  1.00 65.97           C  
ANISOU 1424  CG  GLU A 204     8712  10606   5748   2118    -51  -2766       C  
ATOM   1425  CD  GLU A 204     -13.468   0.801 -59.415  1.00 71.20           C  
ANISOU 1425  CD  GLU A 204     9486  11237   6329   2396   -127  -2789       C  
ATOM   1426  OE1 GLU A 204     -14.460   1.517 -59.668  1.00 74.24           O  
ANISOU 1426  OE1 GLU A 204     9744  11811   6653   2756   -308  -2964       O  
ATOM   1427  OE2 GLU A 204     -12.700   1.013 -58.453  1.00 70.80           O  
ANISOU 1427  OE2 GLU A 204     9651  10981   6270   2264    -13  -2636       O  
ATOM   1428  N   ARG A 205     -15.536  -2.425 -63.873  1.00 67.99           N  
ANISOU 1428  N   ARG A 205     7995  11709   6127   2142   -275  -3342       N  
ATOM   1429  CA  ARG A 205     -16.468  -2.463 -64.993  1.00 60.69           C  
ANISOU 1429  CA  ARG A 205     6786  11076   5195   2334   -465  -3575       C  
ATOM   1430  C   ARG A 205     -17.901  -2.299 -64.500  1.00 64.79           C  
ANISOU 1430  C   ARG A 205     6848  12070   5700   2561   -488  -3897       C  
ATOM   1431  O   ARG A 205     -18.455  -3.193 -63.860  1.00 65.72           O  
ANISOU 1431  O   ARG A 205     6617  12462   5892   2298   -245  -4030       O  
ATOM   1432  CB  ARG A 205     -16.314  -3.771 -65.768  1.00 62.04           C  
ANISOU 1432  CB  ARG A 205     6796  11322   5456   1971   -335  -3585       C  
ATOM   1433  CG  ARG A 205     -17.154  -3.865 -67.028  1.00 69.49           C  
ANISOU 1433  CG  ARG A 205     7465  12542   6394   2134   -537  -3814       C  
ATOM   1434  CD  ARG A 205     -16.820  -5.132 -67.805  1.00 74.52           C  
ANISOU 1434  CD  ARG A 205     8021  13177   7115   1738   -400  -3776       C  
ATOM   1435  NE  ARG A 205     -17.480  -5.176 -69.108  1.00 81.82           N  
ANISOU 1435  NE  ARG A 205     8743  14314   8032   1891   -611  -3965       N  
ATOM   1436  CZ  ARG A 205     -17.255  -6.111 -70.027  1.00 82.65           C  
ANISOU 1436  CZ  ARG A 205     8801  14407   8195   1611   -559  -3942       C  
ATOM   1437  NH1 ARG A 205     -16.384  -7.079 -69.785  1.00 80.97           N  
ANISOU 1437  NH1 ARG A 205     8737  13981   8047   1179   -306  -3736       N  
ATOM   1438  NH2 ARG A 205     -17.897  -6.078 -71.187  1.00 84.35           N  
ANISOU 1438  NH2 ARG A 205     8834  14816   8399   1779   -765  -4120       N  
ATOM   1439  N   TRP A 206     -18.495  -1.148 -64.799  1.00 67.49           N  
ANISOU 1439  N   TRP A 206     7212  12492   5939   3041   -779  -4014       N  
ATOM   1440  CA  TRP A 206     -19.845  -0.842 -64.343  1.00 71.76           C  
ANISOU 1440  CA  TRP A 206     7330  13495   6442   3313   -849  -4326       C  
ATOM   1441  C   TRP A 206     -20.854  -0.862 -65.486  1.00 75.05           C  
ANISOU 1441  C   TRP A 206     7394  14296   6827   3571  -1094  -4619       C  
ATOM   1442  O   TRP A 206     -20.488  -0.731 -66.654  1.00 74.21           O  
ANISOU 1442  O   TRP A 206     7482  14014   6699   3676  -1277  -4546       O  
ATOM   1443  CB  TRP A 206     -19.876   0.522 -63.651  1.00 84.69           C  
ANISOU 1443  CB  TRP A 206     9237  14982   7960   3715  -1006  -4264       C  
ATOM   1444  CG  TRP A 206     -19.101   0.571 -62.369  1.00 81.62           C  
ANISOU 1444  CG  TRP A 206     9105  14310   7596   3487   -765  -4041       C  
ATOM   1445  CD1 TRP A 206     -17.764   0.803 -62.227  1.00 74.71           C  
ANISOU 1445  CD1 TRP A 206     8722  12944   6719   3322   -708  -3720       C  
ATOM   1446  CD2 TRP A 206     -19.620   0.395 -61.046  1.00 71.94           C  
ANISOU 1446  CD2 TRP A 206     7657  13281   6397   3394   -553  -4131       C  
ATOM   1447  NE1 TRP A 206     -17.417   0.777 -60.898  1.00 65.92           N  
ANISOU 1447  NE1 TRP A 206     7696  11726   5625   3156   -488  -3613       N  
ATOM   1448  CE2 TRP A 206     -18.539   0.528 -60.152  1.00 68.85           C  
ANISOU 1448  CE2 TRP A 206     7653  12492   6015   3200   -384  -3850       C  
ATOM   1449  CE3 TRP A 206     -20.893   0.132 -60.530  1.00 75.62           C  
ANISOU 1449  CE3 TRP A 206     7634  14220   6877   3433   -488  -4426       C  
ATOM   1450  CZ2 TRP A 206     -18.692   0.410 -58.773  1.00 69.21           C  
ANISOU 1450  CZ2 TRP A 206     7636  12578   6084   3076   -156  -3843       C  
ATOM   1451  CZ3 TRP A 206     -21.042   0.016 -59.161  1.00 75.98           C  
ANISOU 1451  CZ3 TRP A 206     7628  14290   6952   3282   -245  -4411       C  
ATOM   1452  CH2 TRP A 206     -19.949   0.154 -58.299  1.00 72.74           C  
ANISOU 1452  CH2 TRP A 206     7633  13457   6550   3119    -83  -4116       C  
ATOM   1453  N   ALA A 207     -22.127  -1.023 -65.138  1.00 80.89           N  
ANISOU 1453  N   ALA A 207     7616  15561   7557   3660  -1098  -4953       N  
ATOM   1454  CA  ALA A 207     -23.199  -0.995 -66.124  1.00 86.83           C  
ANISOU 1454  CA  ALA A 207     7974  16760   8257   3933  -1358  -5283       C  
ATOM   1455  C   ALA A 207     -23.447   0.431 -66.599  1.00 94.72           C  
ANISOU 1455  C   ALA A 207     9218  17683   9086   4593  -1766  -5299       C  
ATOM   1456  O   ALA A 207     -23.266   0.744 -67.776  1.00 92.90           O  
ANISOU 1456  O   ALA A 207     9172  17313   8814   4840  -2006  -5260       O  
ATOM   1457  CB  ALA A 207     -24.471  -1.594 -65.547  1.00 90.06           C  
ANISOU 1457  CB  ALA A 207     7769  17760   8688   3772  -1236  -5647       C  
ATOM   1458  N   ASP A 208     -23.862   1.294 -65.677  1.00 99.93           N  
ANISOU 1458  N   ASP A 208     9917  18408   9645   4876  -1834  -5341       N  
ATOM   1459  CA  ASP A 208     -24.075   2.702 -65.988  1.00107.49           C  
ANISOU 1459  CA  ASP A 208    11176  19251  10413   5506  -2208  -5326       C  
ATOM   1460  C   ASP A 208     -22.828   3.522 -65.681  1.00102.95           C  
ANISOU 1460  C   ASP A 208    11297  18010   9812   5541  -2182  -4920       C  
ATOM   1461  O   ASP A 208     -21.779   2.971 -65.344  1.00103.30           O  
ANISOU 1461  O   ASP A 208    11563  17709   9975   5090  -1907  -4667       O  
ATOM   1462  CB  ASP A 208     -25.271   3.253 -65.208  1.00115.03           C  
ANISOU 1462  CB  ASP A 208    11813  20660  11232   5813  -2326  -5613       C  
ATOM   1463  CG  ASP A 208     -26.585   2.630 -65.637  1.00124.80           C  
ANISOU 1463  CG  ASP A 208    12399  22582  12435   5815  -2422  -6060       C  
ATOM   1464  OD1 ASP A 208     -26.688   2.196 -66.803  1.00128.25           O  
ANISOU 1464  OD1 ASP A 208    12702  23141  12887   5826  -2561  -6162       O  
ATOM   1465  OD2 ASP A 208     -27.517   2.578 -64.807  1.00129.18           O  
ANISOU 1465  OD2 ASP A 208    12589  23550  12944   5787  -2350  -6316       O  
ATOM   1466  N   ASP A 209     -22.948   4.840 -65.800  1.00103.11           N  
ANISOU 1466  N   ASP A 209    11668  17855   9655   6065  -2474  -4866       N  
ATOM   1467  CA  ASP A 209     -21.831   5.738 -65.532  1.00 99.13           C  
ANISOU 1467  CA  ASP A 209    11839  16725   9102   6092  -2463  -4503       C  
ATOM   1468  C   ASP A 209     -22.069   6.564 -64.273  1.00 97.59           C  
ANISOU 1468  C   ASP A 209    11744  16533   8803   6278  -2448  -4492       C  
ATOM   1469  O   ASP A 209     -21.141   7.168 -63.735  1.00 94.18           O  
ANISOU 1469  O   ASP A 209    11797  15635   8352   6189  -2361  -4211       O  
ATOM   1470  CB  ASP A 209     -21.583   6.656 -66.729  1.00101.60           C  
ANISOU 1470  CB  ASP A 209    12619  16693   9293   6488  -2774  -4381       C  
ATOM   1471  CG  ASP A 209     -21.031   5.910 -67.927  1.00101.60           C  
ANISOU 1471  CG  ASP A 209    12668  16527   9410   6225  -2737  -4301       C  
ATOM   1472  OD1 ASP A 209     -20.264   4.945 -67.725  1.00 99.49           O  
ANISOU 1472  OD1 ASP A 209    12354  16148   9298   5671  -2448  -4172       O  
ATOM   1473  OD2 ASP A 209     -21.364   6.285 -69.071  1.00105.07           O  
ANISOU 1473  OD2 ASP A 209    13206  16940   9777   6581  -2999  -4363       O  
ATOM   1474  N   LEU A 210     -23.313   6.586 -63.806  1.00 93.89           N  
ANISOU 1474  N   LEU A 210    10810  16603   8262   6511  -2530  -4808       N  
ATOM   1475  CA  LEU A 210     -23.632   7.242 -62.545  1.00 93.70           C  
ANISOU 1475  CA  LEU A 210    10818  16632   8151   6647  -2480  -4825       C  
ATOM   1476  C   LEU A 210     -23.304   6.325 -61.373  1.00 90.51           C  
ANISOU 1476  C   LEU A 210    10199  16258   7933   6099  -2058  -4777       C  
ATOM   1477  O   LEU A 210     -22.988   6.794 -60.282  1.00 94.21           O  
ANISOU 1477  O   LEU A 210    10880  16533   8383   6065  -1927  -4644       O  
ATOM   1478  CB  LEU A 210     -25.104   7.656 -62.498  1.00 99.62           C  
ANISOU 1478  CB  LEU A 210    11173  17952   8726   7098  -2734  -5193       C  
ATOM   1479  CG  LEU A 210     -25.502   8.849 -63.369  1.00104.75           C  
ANISOU 1479  CG  LEU A 210    12134  18557   9109   7756  -3191  -5228       C  
ATOM   1480  CD1 LEU A 210     -26.953   9.233 -63.123  1.00113.27           C  
ANISOU 1480  CD1 LEU A 210    12821  20243   9972   8165  -3423  -5614       C  
ATOM   1481  CD2 LEU A 210     -24.578  10.031 -63.113  1.00101.31           C  
ANISOU 1481  CD2 LEU A 210    12433  17489   8570   7943  -3248  -4870       C  
ATOM   1482  N   TYR A 211     -23.382   5.018 -61.610  1.00 89.11           N  
ANISOU 1482  N   TYR A 211     9623  16309   7924   5675  -1846  -4882       N  
ATOM   1483  CA  TYR A 211     -23.048   4.019 -60.595  1.00 89.77           C  
ANISOU 1483  CA  TYR A 211     9537  16392   8179   5131  -1433  -4820       C  
ATOM   1484  C   TYR A 211     -21.629   4.180 -60.016  1.00 85.72           C  
ANISOU 1484  C   TYR A 211     9555  15302   7712   4877  -1250  -4441       C  
ATOM   1485  O   TYR A 211     -21.467   4.147 -58.792  1.00 84.74           O  
ANISOU 1485  O   TYR A 211     9463  15114   7622   4706  -1026  -4369       O  
ATOM   1486  CB  TYR A 211     -23.222   2.604 -61.164  1.00 94.02           C  
ANISOU 1486  CB  TYR A 211     9668  17185   8870   4711  -1257  -4949       C  
ATOM   1487  CG  TYR A 211     -24.657   2.140 -61.281  1.00 97.37           C  
ANISOU 1487  CG  TYR A 211     9462  18246   9289   4751  -1297  -5357       C  
ATOM   1488  CD1 TYR A 211     -25.622   2.563 -60.377  1.00100.46           C  
ANISOU 1488  CD1 TYR A 211     9604  18958   9609   4926  -1298  -5565       C  
ATOM   1489  CD2 TYR A 211     -25.044   1.270 -62.295  1.00 94.52           C  
ANISOU 1489  CD2 TYR A 211     8757  18170   8987   4585  -1327  -5544       C  
ATOM   1490  CE1 TYR A 211     -26.933   2.137 -60.480  1.00104.56           C  
ANISOU 1490  CE1 TYR A 211     9549  20071  10109   4921  -1329  -5959       C  
ATOM   1491  CE2 TYR A 211     -26.353   0.839 -62.407  1.00 96.91           C  
ANISOU 1491  CE2 TYR A 211     8484  19069   9269   4573  -1362  -5941       C  
ATOM   1492  CZ  TYR A 211     -27.293   1.275 -61.496  1.00105.55           C  
ANISOU 1492  CZ  TYR A 211     9342  20477  10284   4733  -1363  -6151       C  
ATOM   1493  OH  TYR A 211     -28.597   0.849 -61.602  1.00115.47           O  
ANISOU 1493  OH  TYR A 211    10038  22333  11503   4687  -1391  -6567       O  
ATOM   1494  N   PRO A 212     -20.599   4.347 -60.876  1.00 69.26           N  
ANISOU 1494  N   PRO A 212     9630  10547   6137   4154  -1301  -1399       N  
ATOM   1495  CA  PRO A 212     -19.268   4.571 -60.296  1.00 65.34           C  
ANISOU 1495  CA  PRO A 212     9257   9894   5676   4041  -1174  -1231       C  
ATOM   1496  C   PRO A 212     -19.207   5.828 -59.436  1.00 69.27           C  
ANISOU 1496  C   PRO A 212     9864  10253   6205   4150  -1212  -1243       C  
ATOM   1497  O   PRO A 212     -18.607   5.812 -58.360  1.00 71.69           O  
ANISOU 1497  O   PRO A 212    10146  10457   6635   4016  -1166  -1212       O  
ATOM   1498  CB  PRO A 212     -18.367   4.720 -61.527  1.00 63.38           C  
ANISOU 1498  CB  PRO A 212     9223   9619   5240   4073  -1081  -1010       C  
ATOM   1499  CG  PRO A 212     -19.077   4.011 -62.604  1.00 66.54           C  
ANISOU 1499  CG  PRO A 212     9554  10186   5543   4097  -1138  -1081       C  
ATOM   1500  CD  PRO A 212     -20.529   4.242 -62.347  1.00 68.15           C  
ANISOU 1500  CD  PRO A 212     9616  10483   5796   4219  -1300  -1295       C  
ATOM   1501  N   LYS A 213     -19.832   6.900 -59.912  1.00 64.35           N  
ANISOU 1501  N   LYS A 213     9353   9623   5472   4324  -1320  -1252       N  
ATOM   1502  CA  LYS A 213     -19.842   8.169 -59.195  1.00 65.68           C  
ANISOU 1502  CA  LYS A 213     9614   9639   5703   4349  -1392  -1208       C  
ATOM   1503  C   LYS A 213     -20.495   8.025 -57.824  1.00 65.83           C  
ANISOU 1503  C   LYS A 213     9491   9700   5820   4283  -1452  -1478       C  
ATOM   1504  O   LYS A 213     -19.974   8.521 -56.824  1.00 62.01           O  
ANISOU 1504  O   LYS A 213     9036   9066   5459   4166  -1438  -1412       O  
ATOM   1505  CB  LYS A 213     -20.563   9.240 -60.017  1.00 66.85           C  
ANISOU 1505  CB  LYS A 213     9803   9759   5836   4508  -1535  -1113       C  
ATOM   1506  CG  LYS A 213     -19.942   9.489 -61.384  1.00 67.24           C  
ANISOU 1506  CG  LYS A 213     9994   9790   5766   4544  -1501   -833       C  
ATOM   1507  CD  LYS A 213     -20.654  10.607 -62.128  1.00 65.60           C  
ANISOU 1507  CD  LYS A 213     9805   9543   5576   4688  -1660   -718       C  
ATOM   1508  CE  LYS A 213     -19.990  10.884 -63.467  1.00 67.34           C  
ANISOU 1508  CE  LYS A 213    10159   9756   5669   4698  -1632   -429       C  
ATOM   1509  NZ  LYS A 213     -20.650  12.001 -64.198  1.00 70.60           N  
ANISOU 1509  NZ  LYS A 213    10579  10127   6119   4825  -1800   -289       N  
ATOM   1510  N   ILE A 214     -21.631   7.335 -57.784  1.00 64.65           N  
ANISOU 1510  N   ILE A 214     9107   9708   5750   4230  -1520  -1660       N  
ATOM   1511  CA  ILE A 214     -22.351   7.114 -56.536  1.00 64.57           C  
ANISOU 1511  CA  ILE A 214     8860   9759   5915   4044  -1625  -1784       C  
ATOM   1512  C   ILE A 214     -21.545   6.248 -55.574  1.00 65.96           C  
ANISOU 1512  C   ILE A 214     8898   9897   6268   3791  -1522  -1719       C  
ATOM   1513  O   ILE A 214     -21.338   6.626 -54.419  1.00 68.32           O  
ANISOU 1513  O   ILE A 214     9178  10103   6679   3656  -1500  -1758       O  
ATOM   1514  CB  ILE A 214     -23.723   6.450 -56.781  1.00 49.82           C  
ANISOU 1514  CB  ILE A 214     6747   8064   4120   4045  -1709  -1941       C  
ATOM   1515  CG1 ILE A 214     -24.624   7.371 -57.605  1.00 52.98           C  
ANISOU 1515  CG1 ILE A 214     7293   8497   4338   4341  -1798  -2091       C  
ATOM   1516  CG2 ILE A 214     -24.395   6.110 -55.459  1.00 48.62           C  
ANISOU 1516  CG2 ILE A 214     6349   7964   4162   3852  -1740  -2093       C  
ATOM   1517  CD1 ILE A 214     -25.982   6.775 -57.922  1.00 65.82           C  
ANISOU 1517  CD1 ILE A 214     8727  10283   6000   4367  -1860  -2270       C  
ATOM   1518  N   TYR A 215     -21.085   5.094 -56.053  1.00 63.46           N  
ANISOU 1518  N   TYR A 215     8505   9635   5973   3695  -1421  -1648       N  
ATOM   1519  CA  TYR A 215     -20.356   4.165 -55.195  1.00 59.33           C  
ANISOU 1519  CA  TYR A 215     7882   9066   5594   3344  -1271  -1611       C  
ATOM   1520  C   TYR A 215     -19.067   4.767 -54.652  1.00 54.81           C  
ANISOU 1520  C   TYR A 215     7511   8298   5015   3255  -1155  -1469       C  
ATOM   1521  O   TYR A 215     -18.693   4.503 -53.512  1.00 55.78           O  
ANISOU 1521  O   TYR A 215     7560   8343   5289   2972  -1054  -1491       O  
ATOM   1522  CB  TYR A 215     -20.034   2.867 -55.938  1.00 62.01           C  
ANISOU 1522  CB  TYR A 215     8162   9476   5924   3217  -1172  -1558       C  
ATOM   1523  CG  TYR A 215     -19.175   1.921 -55.125  1.00 60.16           C  
ANISOU 1523  CG  TYR A 215     7863   9172   5824   2849  -1009  -1505       C  
ATOM   1524  CD1 TYR A 215     -19.735   1.114 -54.141  1.00 59.08           C  
ANISOU 1524  CD1 TYR A 215     7500   9082   5867   2593   -988  -1615       C  
ATOM   1525  CD2 TYR A 215     -17.803   1.844 -55.333  1.00 57.10           C  
ANISOU 1525  CD2 TYR A 215     7644   8671   5380   2774   -874  -1336       C  
ATOM   1526  CE1 TYR A 215     -18.954   0.254 -53.391  1.00 56.34           C  
ANISOU 1526  CE1 TYR A 215     7105   8666   5637   2277   -846  -1564       C  
ATOM   1527  CE2 TYR A 215     -17.015   0.989 -54.588  1.00 55.24           C  
ANISOU 1527  CE2 TYR A 215     7349   8373   5267   2459   -734  -1296       C  
ATOM   1528  CZ  TYR A 215     -17.595   0.195 -53.619  1.00 54.22           C  
ANISOU 1528  CZ  TYR A 215     7001   8287   5312   2211   -726  -1414       C  
ATOM   1529  OH  TYR A 215     -16.813  -0.660 -52.876  1.00 48.60           O  
ANISOU 1529  OH  TYR A 215     6240   7511   4714   1916   -595  -1371       O  
ATOM   1530  N   HIS A 216     -18.386   5.569 -55.464  1.00 54.82           N  
ANISOU 1530  N   HIS A 216     7773   8214   4842   3508  -1159  -1316       N  
ATOM   1531  CA  HIS A 216     -17.098   6.122 -55.057  1.00 53.72           C  
ANISOU 1531  CA  HIS A 216     7852   7875   4683   3454  -1038  -1152       C  
ATOM   1532  C   HIS A 216     -17.240   7.392 -54.221  1.00 51.54           C  
ANISOU 1532  C   HIS A 216     7675   7434   4476   3509  -1084  -1201       C  
ATOM   1533  O   HIS A 216     -16.408   7.658 -53.354  1.00 49.74           O  
ANISOU 1533  O   HIS A 216     7518   7015   4365   3350   -970  -1137       O  
ATOM   1534  CB  HIS A 216     -16.221   6.383 -56.281  1.00 56.53           C  
ANISOU 1534  CB  HIS A 216     8454   8176   4851   3673   -963   -935       C  
ATOM   1535  CG  HIS A 216     -15.581   5.147 -56.831  1.00 58.82           C  
ANISOU 1535  CG  HIS A 216     8674   8534   5143   3475   -820   -845       C  
ATOM   1536  ND1 HIS A 216     -14.460   4.577 -56.266  1.00 58.65           N  
ANISOU 1536  ND1 HIS A 216     8668   8424   5192   3217   -661   -731       N  
ATOM   1537  CD2 HIS A 216     -15.909   4.364 -57.886  1.00 62.66           C  
ANISOU 1537  CD2 HIS A 216     9083   9158   5567   3498   -816   -866       C  
ATOM   1538  CE1 HIS A 216     -14.122   3.500 -56.953  1.00 59.42           C  
ANISOU 1538  CE1 HIS A 216     8697   8603   5278   3104   -569   -688       C  
ATOM   1539  NE2 HIS A 216     -14.985   3.349 -57.941  1.00 61.50           N  
ANISOU 1539  NE2 HIS A 216     8910   9002   5457   3264   -663   -771       N  
ATOM   1540  N   SER A 217     -18.287   8.173 -54.472  1.00 47.22           N  
ANISOU 1540  N   SER A 217     7115   6922   3905   3705  -1231  -1311       N  
ATOM   1541  CA  SER A 217     -18.585   9.308 -53.604  1.00 44.47           C  
ANISOU 1541  CA  SER A 217     6774   6380   3744   3698  -1250  -1368       C  
ATOM   1542  C   SER A 217     -18.970   8.792 -52.223  1.00 51.80           C  
ANISOU 1542  C   SER A 217     7484   7343   4855   3409  -1201  -1558       C  
ATOM   1543  O   SER A 217     -18.491   9.291 -51.200  1.00 52.89           O  
ANISOU 1543  O   SER A 217     7665   7291   5140   3266  -1116  -1561       O  
ATOM   1544  CB  SER A 217     -19.703  10.176 -54.185  1.00 47.29           C  
ANISOU 1544  CB  SER A 217     7115   6761   4092   3927  -1396  -1437       C  
ATOM   1545  OG  SER A 217     -19.267  10.861 -55.346  1.00 55.55           O  
ANISOU 1545  OG  SER A 217     8341   7713   5053   4094  -1409  -1194       O  
ATOM   1546  N   CYS A 218     -19.827   7.776 -52.206  1.00 50.28           N  
ANISOU 1546  N   CYS A 218     7052   7381   4671   3306  -1246  -1693       N  
ATOM   1547  CA  CYS A 218     -20.239   7.146 -50.959  1.00 53.42           C  
ANISOU 1547  CA  CYS A 218     7218   7822   5256   2998  -1174  -1829       C  
ATOM   1548  C   CYS A 218     -19.064   6.459 -50.275  1.00 50.61           C  
ANISOU 1548  C   CYS A 218     6879   7378   4971   2694  -1002  -1728       C  
ATOM   1549  O   CYS A 218     -19.001   6.409 -49.052  1.00 52.44           O  
ANISOU 1549  O   CYS A 218     7035   7548   5344   2447   -913  -1797       O  
ATOM   1550  CB  CYS A 218     -21.366   6.140 -51.207  1.00 56.12           C  
ANISOU 1550  CB  CYS A 218     7308   8404   5612   2967  -1252  -1944       C  
ATOM   1551  SG  CYS A 218     -22.943   6.896 -51.668  1.00 79.57           S  
ANISOU 1551  SG  CYS A 218    10209  11497   8527   3267  -1462  -2119       S  
ATOM   1552  N   PHE A 219     -18.136   5.931 -51.067  1.00 49.37           N  
ANISOU 1552  N   PHE A 219     6830   7221   4707   2711   -949  -1565       N  
ATOM   1553  CA  PHE A 219     -16.942   5.297 -50.517  1.00 46.35           C  
ANISOU 1553  CA  PHE A 219     6483   6752   4377   2441   -790  -1458       C  
ATOM   1554  C   PHE A 219     -16.070   6.334 -49.827  1.00 48.69           C  
ANISOU 1554  C   PHE A 219     6991   6811   4696   2436   -733  -1395       C  
ATOM   1555  O   PHE A 219     -15.618   6.127 -48.700  1.00 45.41           O  
ANISOU 1555  O   PHE A 219     6540   6321   4391   2160   -641  -1424       O  
ATOM   1556  CB  PHE A 219     -16.145   4.582 -51.613  1.00 43.45           C  
ANISOU 1556  CB  PHE A 219     6198   6426   3886   2491   -735  -1292       C  
ATOM   1557  CG  PHE A 219     -14.956   3.814 -51.099  1.00 40.51           C  
ANISOU 1557  CG  PHE A 219     5840   5983   3570   2215   -575  -1187       C  
ATOM   1558  CD1 PHE A 219     -13.712   4.419 -50.994  1.00 37.86           C  
ANISOU 1558  CD1 PHE A 219     5751   5466   3167   2249   -487  -1017       C  
ATOM   1559  CD2 PHE A 219     -15.081   2.484 -50.729  1.00 40.64           C  
ANISOU 1559  CD2 PHE A 219     5643   6100   3700   1939   -514  -1243       C  
ATOM   1560  CE1 PHE A 219     -12.620   3.714 -50.523  1.00 34.83           C  
ANISOU 1560  CE1 PHE A 219     5387   5027   2820   2009   -346   -911       C  
ATOM   1561  CE2 PHE A 219     -13.992   1.775 -50.260  1.00 30.91           C  
ANISOU 1561  CE2 PHE A 219     4422   4807   2515   1699   -379  -1152       C  
ATOM   1562  CZ  PHE A 219     -12.761   2.391 -50.156  1.00 33.18           C  
ANISOU 1562  CZ  PHE A 219     4940   4940   2728   1734   -297   -991       C  
ATOM   1563  N   PHE A 220     -15.839   7.450 -50.512  1.00 51.79           N  
ANISOU 1563  N   PHE A 220     7618   7070   4991   2744   -791  -1297       N  
ATOM   1564  CA  PHE A 220     -15.024   8.531 -49.971  1.00 49.47           C  
ANISOU 1564  CA  PHE A 220     7554   6480   4763   2783   -747  -1199       C  
ATOM   1565  C   PHE A 220     -15.635   9.103 -48.697  1.00 49.98           C  
ANISOU 1565  C   PHE A 220     7526   6471   4993   2633   -764  -1395       C  
ATOM   1566  O   PHE A 220     -14.927   9.349 -47.721  1.00 50.08           O  
ANISOU 1566  O   PHE A 220     7634   6303   5091   2441   -689  -1384       O  
ATOM   1567  CB  PHE A 220     -14.843   9.641 -51.010  1.00 47.49           C  
ANISOU 1567  CB  PHE A 220     7490   6077   4478   3086   -827   -963       C  
ATOM   1568  CG  PHE A 220     -14.191  10.880 -50.464  1.00 47.17           C  
ANISOU 1568  CG  PHE A 220     7614   5714   4596   3036   -824   -780       C  
ATOM   1569  CD1 PHE A 220     -12.822  10.922 -50.252  1.00 45.39           C  
ANISOU 1569  CD1 PHE A 220     7516   5305   4427   2813   -725   -476       C  
ATOM   1570  CD2 PHE A 220     -14.946  12.003 -50.166  1.00 51.86           C  
ANISOU 1570  CD2 PHE A 220     8230   6177   5296   3211   -922   -909       C  
ATOM   1571  CE1 PHE A 220     -12.217  12.061 -49.750  1.00 46.33           C  
ANISOU 1571  CE1 PHE A 220     7790   5120   4692   2755   -736   -303       C  
ATOM   1572  CE2 PHE A 220     -14.349  13.146 -49.663  1.00 52.25           C  
ANISOU 1572  CE2 PHE A 220     8439   5916   5498   3161   -924   -753       C  
ATOM   1573  CZ  PHE A 220     -12.982  13.175 -49.455  1.00 51.04           C  
ANISOU 1573  CZ  PHE A 220     8421   5585   5386   2927   -837   -448       C  
ATOM   1574  N   ILE A 221     -16.949   9.309 -48.709  1.00 43.94           N  
ANISOU 1574  N   ILE A 221     6588   5841   4265   2718   -859  -1570       N  
ATOM   1575  CA  ILE A 221     -17.639   9.850 -47.543  1.00 38.09           C  
ANISOU 1575  CA  ILE A 221     5747   5047   3678   2594   -850  -1759       C  
ATOM   1576  C   ILE A 221     -17.608   8.870 -46.370  1.00 47.64           C  
ANISOU 1576  C   ILE A 221     6777   6359   4965   2205   -736  -1852       C  
ATOM   1577  O   ILE A 221     -17.280   9.246 -45.244  1.00 52.21           O  
ANISOU 1577  O   ILE A 221     7400   6803   5633   2005   -659  -1908       O  
ATOM   1578  CB  ILE A 221     -19.104  10.209 -47.869  1.00 40.20           C  
ANISOU 1578  CB  ILE A 221     5864   5445   3966   2785   -965  -1913       C  
ATOM   1579  CG1 ILE A 221     -19.157  11.377 -48.857  1.00 42.60           C  
ANISOU 1579  CG1 ILE A 221     6348   5607   4233   3140  -1075  -1810       C  
ATOM   1580  CG2 ILE A 221     -19.860  10.564 -46.601  1.00 40.79           C  
ANISOU 1580  CG2 ILE A 221     5806   5496   4195   2627   -915  -2111       C  
ATOM   1581  CD1 ILE A 221     -20.559  11.798 -49.235  1.00 44.94           C  
ANISOU 1581  CD1 ILE A 221     6512   6013   4551   3338  -1196  -1952       C  
ATOM   1582  N   VAL A 222     -17.933   7.610 -46.644  1.00 49.63           N  
ANISOU 1582  N   VAL A 222     6837   6831   5189   2090   -726  -1851       N  
ATOM   1583  CA  VAL A 222     -18.039   6.598 -45.597  1.00 49.49           C  
ANISOU 1583  CA  VAL A 222     6635   6908   5262   1737   -625  -1905       C  
ATOM   1584  C   VAL A 222     -16.692   6.236 -44.970  1.00 48.82           C  
ANISOU 1584  C   VAL A 222     6658   6709   5184   1470   -510  -1795       C  
ATOM   1585  O   VAL A 222     -16.585   6.134 -43.750  1.00 44.79           O  
ANISOU 1585  O   VAL A 222     6111   6160   4746   1196   -432  -1846       O  
ATOM   1586  CB  VAL A 222     -18.707   5.307 -46.135  1.00 40.25           C  
ANISOU 1586  CB  VAL A 222     5249   5960   4084   1706   -655  -1904       C  
ATOM   1587  CG1 VAL A 222     -18.378   4.105 -45.257  1.00 32.51           C  
ANISOU 1587  CG1 VAL A 222     4143   5025   3185   1356   -543  -1868       C  
ATOM   1588  CG2 VAL A 222     -20.213   5.495 -46.244  1.00 41.38           C  
ANISOU 1588  CG2 VAL A 222     5230   6239   4255   1861   -762  -2057       C  
ATOM   1589  N   THR A 223     -15.666   6.049 -45.793  1.00 50.34           N  
ANISOU 1589  N   THR A 223     6996   6849   5283   1554   -504  -1635       N  
ATOM   1590  CA  THR A 223     -14.389   5.557 -45.280  1.00 40.53           C  
ANISOU 1590  CA  THR A 223     5843   5521   4036   1306   -410  -1524       C  
ATOM   1591  C   THR A 223     -13.373   6.654 -44.968  1.00 37.66           C  
ANISOU 1591  C   THR A 223     5791   4881   3637   1353   -414  -1441       C  
ATOM   1592  O   THR A 223     -12.254   6.356 -44.554  1.00 37.07           O  
ANISOU 1592  O   THR A 223     5768   4693   3626   1076   -342  -1217       O  
ATOM   1593  CB  THR A 223     -13.731   4.571 -46.267  1.00 39.73           C  
ANISOU 1593  CB  THR A 223     5740   5503   3851   1339   -375  -1372       C  
ATOM   1594  OG1 THR A 223     -13.488   5.229 -47.516  1.00 42.86           O  
ANISOU 1594  OG1 THR A 223     6335   5837   4112   1693   -423  -1250       O  
ATOM   1595  CG2 THR A 223     -14.624   3.362 -46.497  1.00 43.81           C  
ANISOU 1595  CG2 THR A 223     5986   6232   4429   1250   -377  -1439       C  
ATOM   1596  N   TYR A 224     -13.747   7.916 -45.158  1.00 38.58           N  
ANISOU 1596  N   TYR A 224     6043   4846   3768   1597   -483  -1468       N  
ATOM   1597  CA  TYR A 224     -12.797   8.999 -44.916  1.00 38.25           C  
ANISOU 1597  CA  TYR A 224     6216   4490   3826   1526   -473  -1205       C  
ATOM   1598  C   TYR A 224     -13.435  10.253 -44.321  1.00 42.10           C  
ANISOU 1598  C   TYR A 224     6784   4821   4390   1633   -530  -1383       C  
ATOM   1599  O   TYR A 224     -13.034  10.702 -43.251  1.00 48.20           O  
ANISOU 1599  O   TYR A 224     7631   5430   5251   1385   -497  -1391       O  
ATOM   1600  CB  TYR A 224     -12.068   9.360 -46.213  1.00 33.37           C  
ANISOU 1600  CB  TYR A 224     5746   3761   3172   1737   -487   -858       C  
ATOM   1601  CG  TYR A 224     -10.806  10.164 -45.994  1.00 38.93           C  
ANISOU 1601  CG  TYR A 224     6650   4158   3985   1591   -461   -510       C  
ATOM   1602  CD1 TYR A 224      -9.593   9.533 -45.755  1.00 31.76           C  
ANISOU 1602  CD1 TYR A 224     5752   3191   3125   1294   -369   -243       C  
ATOM   1603  CD2 TYR A 224     -10.827  11.554 -46.023  1.00 43.25           C  
ANISOU 1603  CD2 TYR A 224     7364   4462   4605   1747   -533   -438       C  
ATOM   1604  CE1 TYR A 224      -8.437  10.260 -45.552  1.00 37.04           C  
ANISOU 1604  CE1 TYR A 224     6594   3579   3903   1152   -354     92       C  
ATOM   1605  CE2 TYR A 224      -9.675  12.291 -45.821  1.00 35.66           C  
ANISOU 1605  CE2 TYR A 224     6585   3214   3749   1605   -521   -112       C  
ATOM   1606  CZ  TYR A 224      -8.483  11.638 -45.586  1.00 40.82           C  
ANISOU 1606  CZ  TYR A 224     7245   3825   4439   1305   -433    155       C  
ATOM   1607  OH  TYR A 224      -7.333  12.365 -45.383  1.00 43.07           O  
ANISOU 1607  OH  TYR A 224     7702   3825   4837   1155   -430    496       O  
ATOM   1608  N   LEU A 225     -14.417  10.817 -45.017  1.00 40.03           N  
ANISOU 1608  N   LEU A 225     6508   4602   4101   1996   -614  -1522       N  
ATOM   1609  CA  LEU A 225     -15.025  12.082 -44.605  1.00 41.12           C  
ANISOU 1609  CA  LEU A 225     6720   4564   4341   2144   -665  -1669       C  
ATOM   1610  C   LEU A 225     -15.680  12.010 -43.228  1.00 38.29           C  
ANISOU 1610  C   LEU A 225     6185   4295   4068   1853   -593  -1913       C  
ATOM   1611  O   LEU A 225     -15.221  12.644 -42.273  1.00 48.82           O  
ANISOU 1611  O   LEU A 225     7657   5417   5474   1678   -558  -1946       O  
ATOM   1612  CB  LEU A 225     -16.062  12.531 -45.636  1.00 46.70           C  
ANISOU 1612  CB  LEU A 225     7333   5374   5037   2491   -765  -1693       C  
ATOM   1613  CG  LEU A 225     -15.765  13.818 -46.407  1.00 50.20           C  
ANISOU 1613  CG  LEU A 225     7993   5544   5536   2790   -854  -1491       C  
ATOM   1614  CD1 LEU A 225     -16.926  14.171 -47.327  1.00 56.09           C  
ANISOU 1614  CD1 LEU A 225     8611   6438   6263   3072   -962  -1544       C  
ATOM   1615  CD2 LEU A 225     -15.463  14.961 -45.451  1.00 47.62           C  
ANISOU 1615  CD2 LEU A 225     7820   4903   5371   2700   -838  -1516       C  
ATOM   1616  N   ALA A 226     -16.755  11.234 -43.136  1.00 37.35           N  
ANISOU 1616  N   ALA A 226     5779   4469   3942   1794   -569  -2053       N  
ATOM   1617  CA  ALA A 226     -17.542  11.135 -41.909  1.00 47.91           C  
ANISOU 1617  CA  ALA A 226     6955   5896   5352   1556   -480  -2241       C  
ATOM   1618  C   ALA A 226     -16.743  10.682 -40.676  1.00 45.20           C  
ANISOU 1618  C   ALA A 226     6653   5513   5009   1144   -368  -2228       C  
ATOM   1619  O   ALA A 226     -16.807  11.339 -39.634  1.00 45.43           O  
ANISOU 1619  O   ALA A 226     6752   5423   5087    992   -306  -2330       O  
ATOM   1620  CB  ALA A 226     -18.739  10.205 -42.131  1.00 48.13           C  
ANISOU 1620  CB  ALA A 226     6707   6214   5368   1571   -491  -2315       C  
ATOM   1621  N   PRO A 227     -15.989   9.568 -40.775  1.00 45.72           N  
ANISOU 1621  N   PRO A 227     6684   5674   5014    953   -344  -2097       N  
ATOM   1622  CA  PRO A 227     -15.352   9.113 -39.535  1.00 41.69           C  
ANISOU 1622  CA  PRO A 227     6199   5140   4503    541   -258  -2072       C  
ATOM   1623  C   PRO A 227     -14.226  10.026 -39.071  1.00 39.88           C  
ANISOU 1623  C   PRO A 227     6232   4625   4297    428   -281  -2030       C  
ATOM   1624  O   PRO A 227     -14.085  10.232 -37.872  1.00 43.07           O  
ANISOU 1624  O   PRO A 227     6683   4967   4714    129   -218  -2078       O  
ATOM   1625  CB  PRO A 227     -14.798   7.732 -39.902  1.00 36.65           C  
ANISOU 1625  CB  PRO A 227     5459   4649   3819    403   -249  -1925       C  
ATOM   1626  CG  PRO A 227     -15.438   7.371 -41.195  1.00 36.37           C  
ANISOU 1626  CG  PRO A 227     5300   4758   3760    714   -304  -1916       C  
ATOM   1627  CD  PRO A 227     -15.682   8.660 -41.893  1.00 40.30           C  
ANISOU 1627  CD  PRO A 227     5940   5115   4258   1066   -386  -1962       C  
ATOM   1628  N   LEU A 228     -13.437  10.556 -39.999  1.00 34.54           N  
ANISOU 1628  N   LEU A 228     5793   3727   3604    667   -386  -1880       N  
ATOM   1629  CA  LEU A 228     -12.333  11.435 -39.629  1.00 39.15           C  
ANISOU 1629  CA  LEU A 228     6619   3986   4269    503   -394  -1628       C  
ATOM   1630  C   LEU A 228     -12.866  12.774 -39.137  1.00 46.10           C  
ANISOU 1630  C   LEU A 228     7636   4665   5216    626   -419  -1824       C  
ATOM   1631  O   LEU A 228     -12.248  13.421 -38.292  1.00 51.79           O  
ANISOU 1631  O   LEU A 228     8517   5164   5996    383   -408  -1762       O  
ATOM   1632  CB  LEU A 228     -11.373  11.640 -40.803  1.00 38.75           C  
ANISOU 1632  CB  LEU A 228     6691   3788   4244    653   -424  -1215       C  
ATOM   1633  CG  LEU A 228     -10.235  10.623 -40.959  1.00 37.73           C  
ANISOU 1633  CG  LEU A 228     6519   3702   4113    393   -373   -900       C  
ATOM   1634  CD1 LEU A 228     -10.750   9.191 -41.019  1.00 35.43           C  
ANISOU 1634  CD1 LEU A 228     5984   3739   3741    334   -332  -1069       C  
ATOM   1635  CD2 LEU A 228      -9.407  10.935 -42.193  1.00 42.38           C  
ANISOU 1635  CD2 LEU A 228     7231   4152   4720    592   -387   -518       C  
ATOM   1636  N   GLY A 229     -14.016  13.183 -39.666  1.00 42.40           N  
ANISOU 1636  N   GLY A 229     7311   5433   3366   -587   -195   1005       N  
ATOM   1637  CA  GLY A 229     -14.683  14.376 -39.177  1.00 44.95           C  
ANISOU 1637  CA  GLY A 229     7909   5335   3834   -395   -729   1103       C  
ATOM   1638  C   GLY A 229     -15.148  14.194 -37.743  1.00 39.80           C  
ANISOU 1638  C   GLY A 229     7108   4631   3381    177   -624   1001       C  
ATOM   1639  O   GLY A 229     -14.802  14.982 -36.853  1.00 38.21           O  
ANISOU 1639  O   GLY A 229     6910   4328   3282    324   -719    971       O  
ATOM   1640  N   LEU A 230     -15.927  13.139 -37.519  1.00 33.03           N  
ANISOU 1640  N   LEU A 230     5892   3921   2738    467   -336    815       N  
ATOM   1641  CA  LEU A 230     -16.447  12.827 -36.191  1.00 36.01           C  
ANISOU 1641  CA  LEU A 230     5878   4389   3415    884    -99    559       C  
ATOM   1642  C   LEU A 230     -15.328  12.636 -35.173  1.00 34.63           C  
ANISOU 1642  C   LEU A 230     5602   4432   3124    856    281    593       C  
ATOM   1643  O   LEU A 230     -15.427  13.096 -34.036  1.00 32.11           O  
ANISOU 1643  O   LEU A 230     5156   4103   2939   1046    296    455       O  
ATOM   1644  CB  LEU A 230     -17.322  11.572 -36.241  1.00 40.64           C  
ANISOU 1644  CB  LEU A 230     6166   5153   4121   1028    181    407       C  
ATOM   1645  CG  LEU A 230     -18.673  11.694 -36.949  1.00 47.65           C  
ANISOU 1645  CG  LEU A 230     7035   5828   5244   1170   -182    259       C  
ATOM   1646  CD1 LEU A 230     -19.444  10.386 -36.862  1.00 43.56           C  
ANISOU 1646  CD1 LEU A 230     6199   5546   4806   1281    177    102       C  
ATOM   1647  CD2 LEU A 230     -19.485  12.839 -36.364  1.00 52.92           C  
ANISOU 1647  CD2 LEU A 230     7604   6211   6293   1462   -629    -54       C  
ATOM   1648  N   MET A 231     -14.265  11.957 -35.589  1.00 31.17           N  
ANISOU 1648  N   MET A 231     5183   4191   2471    600    560    711       N  
ATOM   1649  CA  MET A 231     -13.120  11.715 -34.722  1.00 31.84           C  
ANISOU 1649  CA  MET A 231     5031   4381   2685    503    729    633       C  
ATOM   1650  C   MET A 231     -12.363  13.005 -34.435  1.00 33.80           C  
ANISOU 1650  C   MET A 231     5474   4540   2826    404    564    717       C  
ATOM   1651  O   MET A 231     -11.834  13.186 -33.340  1.00 36.03           O  
ANISOU 1651  O   MET A 231     5656   4831   3201    492    636    675       O  
ATOM   1652  CB  MET A 231     -12.182  10.677 -35.343  1.00 35.62           C  
ANISOU 1652  CB  MET A 231     5299   5030   3204    235    866    528       C  
ATOM   1653  CG  MET A 231     -12.669   9.243 -35.204  1.00 35.05           C  
ANISOU 1653  CG  MET A 231     5002   4984   3332    360    978    432       C  
ATOM   1654  SD  MET A 231     -11.451   8.034 -35.758  1.00 53.17           S  
ANISOU 1654  SD  MET A 231     7068   7444   5692    182   1131    229       S  
ATOM   1655  CE  MET A 231     -11.699   8.085 -37.529  1.00 33.24           C  
ANISOU 1655  CE  MET A 231     4537   5162   2932   -106   1147    169       C  
ATOM   1656  N   ALA A 232     -12.313  13.898 -35.421  1.00 28.01           N  
ANISOU 1656  N   ALA A 232     5025   3704   1914    167    284    849       N  
ATOM   1657  CA  ALA A 232     -11.706  15.208 -35.221  1.00 26.52           C  
ANISOU 1657  CA  ALA A 232     5027   3379   1671     51     39    937       C  
ATOM   1658  C   ALA A 232     -12.476  15.975 -34.156  1.00 41.49           C  
ANISOU 1658  C   ALA A 232     7072   4998   3694    457   -204    906       C  
ATOM   1659  O   ALA A 232     -11.884  16.593 -33.270  1.00 45.82           O  
ANISOU 1659  O   ALA A 232     7601   5534   4275    519   -186    887       O  
ATOM   1660  CB  ALA A 232     -11.673  15.989 -36.517  1.00 29.96           C  
ANISOU 1660  CB  ALA A 232     5753   3670   1963   -317   -298   1043       C  
ATOM   1661  N   MET A 233     -13.802  15.921 -34.248  1.00 37.62           N  
ANISOU 1661  N   MET A 233     6538   4336   3421    737   -438    775       N  
ATOM   1662  CA  MET A 233     -14.667  16.567 -33.266  1.00 35.34           C  
ANISOU 1662  CA  MET A 233     6027   3892   3510   1116   -647    463       C  
ATOM   1663  C   MET A 233     -14.458  15.977 -31.867  1.00 32.03           C  
ANISOU 1663  C   MET A 233     5270   3804   3097   1248   -127    288       C  
ATOM   1664  O   MET A 233     -14.298  16.706 -30.877  1.00 31.59           O  
ANISOU 1664  O   MET A 233     5133   3732   3137   1357   -162    132       O  
ATOM   1665  CB  MET A 233     -16.131  16.432 -33.691  1.00 38.52           C  
ANISOU 1665  CB  MET A 233     6260   4128   4246   1343   -932    195       C  
ATOM   1666  CG  MET A 233     -17.103  17.276 -32.886  1.00 47.64           C  
ANISOU 1666  CG  MET A 233     7115   5092   5894   1710  -1265   -310       C  
ATOM   1667  SD  MET A 233     -18.766  17.252 -33.582  1.00114.79           S  
ANISOU 1667  SD  MET A 233    15402  13316  14898   1980  -1753   -718       S  
ATOM   1668  CE  MET A 233     -19.616  18.379 -32.480  1.00 75.24           C  
ANISOU 1668  CE  MET A 233     9904   8172  10512   2329  -2092  -1483       C  
ATOM   1669  N   ALA A 234     -14.446  14.649 -31.803  1.00 30.00           N  
ANISOU 1669  N   ALA A 234     4854   3821   2722   1185    297    328       N  
ATOM   1670  CA  ALA A 234     -14.290  13.926 -30.547  1.00 33.20           C  
ANISOU 1670  CA  ALA A 234     5047   4494   3073   1181    685    243       C  
ATOM   1671  C   ALA A 234     -12.971  14.265 -29.863  1.00 33.78           C  
ANISOU 1671  C   ALA A 234     5247   4592   2997   1076    770    416       C  
ATOM   1672  O   ALA A 234     -12.945  14.572 -28.671  1.00 33.59           O  
ANISOU 1672  O   ALA A 234     5136   4658   2969   1094    857    290       O  
ATOM   1673  CB  ALA A 234     -14.393  12.427 -30.787  1.00 23.21           C  
ANISOU 1673  CB  ALA A 234     3679   3392   1747   1073    943    331       C  
ATOM   1674  N   TYR A 235     -11.879  14.214 -30.620  1.00 32.63           N  
ANISOU 1674  N   TYR A 235     5192   4368   2837    865    702    594       N  
ATOM   1675  CA  TYR A 235     -10.569  14.524 -30.063  1.00 22.82           C  
ANISOU 1675  CA  TYR A 235     3911   3116   1644    699    689    622       C  
ATOM   1676  C   TYR A 235     -10.440  16.012 -29.761  1.00 28.84           C  
ANISOU 1676  C   TYR A 235     4907   3758   2293    793    522    667       C  
ATOM   1677  O   TYR A 235      -9.630  16.410 -28.923  1.00 32.98           O  
ANISOU 1677  O   TYR A 235     5391   4292   2846    743    545    661       O  
ATOM   1678  CB  TYR A 235      -9.455  14.066 -31.007  1.00 22.54           C  
ANISOU 1678  CB  TYR A 235     3815   3137   1611    428    690    638       C  
ATOM   1679  CG  TYR A 235      -9.201  12.577 -30.950  1.00 21.69           C  
ANISOU 1679  CG  TYR A 235     3518   3102   1622    418    815    572       C  
ATOM   1680  CD1 TYR A 235      -8.715  11.983 -29.792  1.00 38.10           C  
ANISOU 1680  CD1 TYR A 235     5534   5156   3784    481    848    583       C  
ATOM   1681  CD2 TYR A 235      -9.443  11.764 -32.051  1.00 28.62           C  
ANISOU 1681  CD2 TYR A 235     4333   4051   2490    343    874    524       C  
ATOM   1682  CE1 TYR A 235      -8.480  10.620 -29.730  1.00 39.09           C  
ANISOU 1682  CE1 TYR A 235     5592   5289   3973    527    921    596       C  
ATOM   1683  CE2 TYR A 235      -9.211  10.399 -31.998  1.00 32.33           C  
ANISOU 1683  CE2 TYR A 235     4659   4555   3069    395    979    466       C  
ATOM   1684  CZ  TYR A 235      -8.729   9.832 -30.835  1.00 37.60           C  
ANISOU 1684  CZ  TYR A 235     5314   5161   3811    519    999    527       C  
ATOM   1685  OH  TYR A 235      -8.496   8.476 -30.776  1.00 38.73           O  
ANISOU 1685  OH  TYR A 235     5384   5303   4030    639   1104    541       O  
ATOM   1686  N   PHE A 236     -11.240  16.833 -30.434  1.00 23.99           N  
ANISOU 1686  N   PHE A 236     4543   2952   1618    925    217    693       N  
ATOM   1687  CA  PHE A 236     -11.293  18.252 -30.102  1.00 34.85           C  
ANISOU 1687  CA  PHE A 236     6047   4081   3112   1015   -165    628       C  
ATOM   1688  C   PHE A 236     -11.875  18.434 -28.706  1.00 37.49           C  
ANISOU 1688  C   PHE A 236     6071   4520   3655   1259    -46    286       C  
ATOM   1689  O   PHE A 236     -11.307  19.150 -27.875  1.00 43.27           O  
ANISOU 1689  O   PHE A 236     6821   5243   4378   1278    -59    252       O  
ATOM   1690  CB  PHE A 236     -12.117  19.034 -31.126  1.00 29.09           C  
ANISOU 1690  CB  PHE A 236     5523   2987   2543   1034   -752    617       C  
ATOM   1691  CG  PHE A 236     -12.333  20.474 -30.754  1.00 35.04           C  
ANISOU 1691  CG  PHE A 236     6371   3378   3563   1191  -1303    475       C  
ATOM   1692  CD1 PHE A 236     -11.327  21.409 -30.929  1.00 33.10           C  
ANISOU 1692  CD1 PHE A 236     6401   3006   3168    901  -1494    697       C  
ATOM   1693  CD2 PHE A 236     -13.544  20.893 -30.229  1.00 38.86           C  
ANISOU 1693  CD2 PHE A 236     6528   3704   4532   1564  -1580     -8       C  
ATOM   1694  CE1 PHE A 236     -11.524  22.733 -30.587  1.00 36.29           C  
ANISOU 1694  CE1 PHE A 236     6855   3068   3866   1011  -2012    533       C  
ATOM   1695  CE2 PHE A 236     -13.746  22.214 -29.885  1.00 39.89           C  
ANISOU 1695  CE2 PHE A 236     6676   3457   5025   1753  -2165   -244       C  
ATOM   1696  CZ  PHE A 236     -12.735  23.135 -30.064  1.00 38.90           C  
ANISOU 1696  CZ  PHE A 236     6918   3154   4707   1470  -2405     76       C  
ATOM   1697  N   GLN A 237     -13.003  17.777 -28.448  1.00 29.45           N  
ANISOU 1697  N   GLN A 237     4757   3650   2784   1379    101     -5       N  
ATOM   1698  CA  GLN A 237     -13.624  17.847 -27.129  1.00 30.79           C  
ANISOU 1698  CA  GLN A 237     4591   4050   3059   1451    302   -433       C  
ATOM   1699  C   GLN A 237     -12.716  17.252 -26.052  1.00 28.94           C  
ANISOU 1699  C   GLN A 237     4397   4087   2511   1224    699   -247       C  
ATOM   1700  O   GLN A 237     -12.584  17.814 -24.959  1.00 31.20           O  
ANISOU 1700  O   GLN A 237     4588   4492   2776   1187    771   -452       O  
ATOM   1701  CB  GLN A 237     -14.979  17.136 -27.136  1.00 32.20           C  
ANISOU 1701  CB  GLN A 237     4445   4413   3376   1496    441   -810       C  
ATOM   1702  CG  GLN A 237     -15.988  17.755 -28.095  1.00 51.81           C  
ANISOU 1702  CG  GLN A 237     6841   6573   6270   1759    -48  -1083       C  
ATOM   1703  CD  GLN A 237     -17.405  17.262 -27.864  1.00 55.67           C  
ANISOU 1703  CD  GLN A 237     6881   7286   6986   1835     92  -1658       C  
ATOM   1704  OE1 GLN A 237     -17.654  16.439 -26.982  1.00 53.98           O  
ANISOU 1704  OE1 GLN A 237     6459   7512   6539   1591    593  -1816       O  
ATOM   1705  NE2 GLN A 237     -18.344  17.769 -28.656  1.00 60.47           N  
ANISOU 1705  NE2 GLN A 237     7362   7569   8044   2103   -404  -1971       N  
ATOM   1706  N   ILE A 238     -12.083  16.125 -26.370  1.00 34.82           N  
ANISOU 1706  N   ILE A 238     5279   4898   3053   1066    888    107       N  
ATOM   1707  CA  ILE A 238     -11.162  15.464 -25.448  1.00 32.58           C  
ANISOU 1707  CA  ILE A 238     4968   4673   2738    757    964    278       C  
ATOM   1708  C   ILE A 238      -9.994  16.371 -25.072  1.00 33.08           C  
ANISOU 1708  C   ILE A 238     5157   4622   2791    766    866    392       C  
ATOM   1709  O   ILE A 238      -9.698  16.557 -23.892  1.00 41.57           O  
ANISOU 1709  O   ILE A 238     6200   5792   3800    628    914    341       O  
ATOM   1710  CB  ILE A 238     -10.607  14.157 -26.045  1.00 27.08           C  
ANISOU 1710  CB  ILE A 238     4234   3892   2162    591    899    463       C  
ATOM   1711  CG1 ILE A 238     -11.709  13.099 -26.120  1.00 24.78           C  
ANISOU 1711  CG1 ILE A 238     3838   3725   1852    504    990    380       C  
ATOM   1712  CG2 ILE A 238      -9.442  13.639 -25.215  1.00 23.45           C  
ANISOU 1712  CG2 ILE A 238     3792   3403   1716    400    830    578       C  
ATOM   1713  CD1 ILE A 238     -11.260  11.794 -26.744  1.00 24.40           C  
ANISOU 1713  CD1 ILE A 238     3780   3590   1900    432    924    519       C  
ATOM   1714  N   PHE A 239      -9.338  16.936 -26.080  1.00 22.98           N  
ANISOU 1714  N   PHE A 239     4017   3164   1550    840    717    527       N  
ATOM   1715  CA  PHE A 239      -8.195  17.812 -25.841  1.00 44.66           C  
ANISOU 1715  CA  PHE A 239     6845   5814   4310    775    611    598       C  
ATOM   1716  C   PHE A 239      -8.598  19.090 -25.116  1.00 41.29           C  
ANISOU 1716  C   PHE A 239     6605   5371   3712   1014    556    507       C  
ATOM   1717  O   PHE A 239      -7.834  19.620 -24.306  1.00 40.75           O  
ANISOU 1717  O   PHE A 239     6537   5297   3648    949    554    518       O  
ATOM   1718  CB  PHE A 239      -7.496  18.149 -27.158  1.00 22.70           C  
ANISOU 1718  CB  PHE A 239     4138   2935   1551    624    462    692       C  
ATOM   1719  CG  PHE A 239      -6.627  17.042 -27.672  1.00 25.75           C  
ANISOU 1719  CG  PHE A 239     4350   3422   2010    424    548    690       C  
ATOM   1720  CD1 PHE A 239      -5.908  16.250 -26.793  1.00 28.65           C  
ANISOU 1720  CD1 PHE A 239     4606   3825   2456    411    621    670       C  
ATOM   1721  CD2 PHE A 239      -6.540  16.781 -29.027  1.00 30.14           C  
ANISOU 1721  CD2 PHE A 239     4917   4034   2501    268    533    711       C  
ATOM   1722  CE1 PHE A 239      -5.112  15.226 -27.257  1.00 31.87           C  
ANISOU 1722  CE1 PHE A 239     4951   4272   2886    360    694    657       C  
ATOM   1723  CE2 PHE A 239      -5.748  15.758 -29.496  1.00 31.21           C  
ANISOU 1723  CE2 PHE A 239     4922   4295   2640    151    661    647       C  
ATOM   1724  CZ  PHE A 239      -5.032  14.980 -28.610  1.00 34.38           C  
ANISOU 1724  CZ  PHE A 239     5247   4680   3137    247    752    608       C  
ATOM   1725  N   ARG A 240      -9.799  19.582 -25.403  1.00 38.61           N  
ANISOU 1725  N   ARG A 240     6151   4948   3571   1185    359    230       N  
ATOM   1726  CA  ARG A 240     -10.304  20.755 -24.704  1.00 36.21           C  
ANISOU 1726  CA  ARG A 240     5702   4564   3493   1349    146   -140       C  
ATOM   1727  C   ARG A 240     -10.566  20.421 -23.238  1.00 33.14           C  
ANISOU 1727  C   ARG A 240     5052   4538   3003   1239    512   -438       C  
ATOM   1728  O   ARG A 240     -10.445  21.282 -22.367  1.00 33.10           O  
ANISOU 1728  O   ARG A 240     4949   4568   3061   1267    475   -687       O  
ATOM   1729  CB  ARG A 240     -11.575  21.284 -25.370  1.00 38.16           C  
ANISOU 1729  CB  ARG A 240     5796   4584   4120   1579   -251   -494       C  
ATOM   1730  CG  ARG A 240     -12.099  22.566 -24.746  1.00 41.19           C  
ANISOU 1730  CG  ARG A 240     5952   4801   4896   1810   -603  -1010       C  
ATOM   1731  CD  ARG A 240     -13.022  23.317 -25.688  1.00 54.17           C  
ANISOU 1731  CD  ARG A 240     7579   5980   7024   2068  -1292  -1255       C  
ATOM   1732  NE  ARG A 240     -13.489  24.572 -25.104  1.00 70.51           N  
ANISOU 1732  NE  ARG A 240     9377   7807   9606   2341  -1754  -1840       N  
ATOM   1733  CZ  ARG A 240     -12.783  25.700 -25.087  1.00 80.20           C  
ANISOU 1733  CZ  ARG A 240    10874   8670  10927   2380  -2215  -1676       C  
ATOM   1734  NH1 ARG A 240     -11.569  25.736 -25.619  1.00 80.44           N  
ANISOU 1734  NH1 ARG A 240    11454   8596  10512   2107  -2216   -954       N  
ATOM   1735  NH2 ARG A 240     -13.289  26.794 -24.534  1.00 85.00           N  
ANISOU 1735  NH2 ARG A 240    11130   9182  11982   2484  -2593  -2190       N  
ATOM   1736  N   LYS A 241     -10.913  19.166 -22.964  1.00 31.60           N  
ANISOU 1736  N   LYS A 241     4776   4618   2612   1039    842   -408       N  
ATOM   1737  CA  LYS A 241     -11.156  18.741 -21.589  1.00 36.11           C  
ANISOU 1737  CA  LYS A 241     5206   5568   2947    735   1167   -627       C  
ATOM   1738  C   LYS A 241      -9.849  18.468 -20.841  1.00 38.06           C  
ANISOU 1738  C   LYS A 241     5653   5776   3034    435   1160   -221       C  
ATOM   1739  O   LYS A 241      -9.782  18.620 -19.620  1.00 38.28           O  
ANISOU 1739  O   LYS A 241     5602   6047   2897    153   1265   -371       O  
ATOM   1740  CB  LYS A 241     -12.044  17.495 -21.558  1.00 31.33           C  
ANISOU 1740  CB  LYS A 241     4487   5132   2286    434   1361   -688       C  
ATOM   1741  CG  LYS A 241     -12.617  17.176 -20.185  1.00 34.62           C  
ANISOU 1741  CG  LYS A 241     4783   5796   2576    113   1512   -857       C  
ATOM   1742  CD  LYS A 241     -13.620  18.236 -19.755  1.00 48.02           C  
ANISOU 1742  CD  LYS A 241     6057   7682   4505    147   1533  -1551       C  
ATOM   1743  CE  LYS A 241     -14.131  17.990 -18.343  1.00 55.99           C  
ANISOU 1743  CE  LYS A 241     6891   9035   5347   -363   1694  -1787       C  
ATOM   1744  NZ  LYS A 241     -13.069  18.205 -17.319  1.00 57.48           N  
ANISOU 1744  NZ  LYS A 241     7308   9237   5293   -579   1705  -1531       N  
ATOM   1745  N   LEU A 242      -8.813  18.068 -21.574  1.00 39.63           N  
ANISOU 1745  N   LEU A 242     6001   5705   3351    470    973    194       N  
ATOM   1746  CA  LEU A 242      -7.543  17.692 -20.954  1.00 26.39           C  
ANISOU 1746  CA  LEU A 242     4361   3958   1707    251    850    434       C  
ATOM   1747  C   LEU A 242      -6.524  18.829 -20.940  1.00 25.63           C  
ANISOU 1747  C   LEU A 242     4362   3698   1679    396    753    496       C  
ATOM   1748  O   LEU A 242      -5.440  18.686 -20.376  1.00 25.14           O  
ANISOU 1748  O   LEU A 242     4296   3592   1662    262    660    618       O  
ATOM   1749  CB  LEU A 242      -6.940  16.478 -21.667  1.00 24.88           C  
ANISOU 1749  CB  LEU A 242     4151   3627   1675    197    723    626       C  
ATOM   1750  CG  LEU A 242      -7.758  15.186 -21.633  1.00 25.70           C  
ANISOU 1750  CG  LEU A 242     4204   3858   1702     31    757    647       C  
ATOM   1751  CD1 LEU A 242      -6.979  14.040 -22.257  1.00 24.78           C  
ANISOU 1751  CD1 LEU A 242     4120   3560   1734     48    622    815       C  
ATOM   1752  CD2 LEU A 242      -8.171  14.845 -20.210  1.00 28.29           C  
ANISOU 1752  CD2 LEU A 242     4473   4497   1779   -189    810    687       C  
ATOM   1753  N   TRP A 243      -6.871  19.954 -21.558  1.00 36.66           N  
ANISOU 1753  N   TRP A 243     5879   5004   3047    690    731    412       N  
ATOM   1754  CA  TRP A 243      -5.952  21.086 -21.645  1.00 31.10           C  
ANISOU 1754  CA  TRP A 243     5318   4131   2368    784    583    497       C  
ATOM   1755  C   TRP A 243      -5.654  21.679 -20.273  1.00 28.52           C  
ANISOU 1755  C   TRP A 243     4994   3916   1926    730    651    396       C  
ATOM   1756  O   TRP A 243      -6.555  21.858 -19.456  1.00 29.02           O  
ANISOU 1756  O   TRP A 243     4982   4215   1829    745    815     77       O  
ATOM   1757  CB  TRP A 243      -6.520  22.172 -22.562  1.00 27.28           C  
ANISOU 1757  CB  TRP A 243     5035   3453   1877   1059    331    434       C  
ATOM   1758  CG  TRP A 243      -5.573  23.314 -22.791  1.00 31.68           C  
ANISOU 1758  CG  TRP A 243     5809   3788   2440   1043     77    585       C  
ATOM   1759  CD1 TRP A 243      -4.705  23.462 -23.833  1.00 32.99           C  
ANISOU 1759  CD1 TRP A 243     5929   3869   2737    753    -27    723       C  
ATOM   1760  CD2 TRP A 243      -5.402  24.470 -21.959  1.00 31.56           C  
ANISOU 1760  CD2 TRP A 243     5798   3690   2505   1143    -83    430       C  
ATOM   1761  NE1 TRP A 243      -4.004  24.637 -23.702  1.00 27.98           N  
ANISOU 1761  NE1 TRP A 243     5404   3107   2118    688   -219    763       N  
ATOM   1762  CE2 TRP A 243      -4.412  25.273 -22.559  1.00 31.19           C  
ANISOU 1762  CE2 TRP A 243     5937   3441   2471    984   -304    641       C  
ATOM   1763  CE3 TRP A 243      -5.988  24.902 -20.765  1.00 33.50           C  
ANISOU 1763  CE3 TRP A 243     5781   4068   2878   1244    -22     28       C  
ATOM   1764  CZ2 TRP A 243      -3.996  26.483 -22.006  1.00 35.47           C  
ANISOU 1764  CZ2 TRP A 243     6603   3823   3050   1055   -539    605       C  
ATOM   1765  CZ3 TRP A 243      -5.573  26.102 -20.217  1.00 35.70           C  
ANISOU 1765  CZ3 TRP A 243     6093   4209   3262   1325   -235    -84       C  
ATOM   1766  CH2 TRP A 243      -4.587  26.879 -20.837  1.00 36.83           C  
ANISOU 1766  CH2 TRP A 243     6576   4064   3354   1281   -529    254       C  
ATOM   1767  N   GLY A 244      -4.383  21.987 -20.032  1.00 29.08           N  
ANISOU 1767  N   GLY A 244     5065   3878   2107    621    551    544       N  
ATOM   1768  CA  GLY A 244      -3.968  22.633 -18.800  1.00 32.90           C  
ANISOU 1768  CA  GLY A 244     5578   4438   2486    564    584    489       C  
ATOM   1769  C   GLY A 244      -3.932  21.706 -17.601  1.00 34.62           C  
ANISOU 1769  C   GLY A 244     5669   4879   2606    240    668    499       C  
ATOM   1770  O   GLY A 244      -3.771  22.155 -16.466  1.00 44.12           O  
ANISOU 1770  O   GLY A 244     6874   6233   3655    115    720    427       O  
ATOM   1771  N   ARG A 245      -4.080  20.410 -17.850  1.00 30.93           N  
ANISOU 1771  N   ARG A 245     5114   4451   2187     98    640    608       N  
ATOM   1772  CA  ARG A 245      -4.097  19.426 -16.775  1.00 26.33           C  
ANISOU 1772  CA  ARG A 245     4472   4068   1464   -135    634    725       C  
ATOM   1773  C   ARG A 245      -2.928  18.457 -16.904  1.00 40.12           C  
ANISOU 1773  C   ARG A 245     6245   5601   3398   -143    435    974       C  
ATOM   1774  O   ARG A 245      -3.089  17.331 -17.375  1.00 42.49           O  
ANISOU 1774  O   ARG A 245     6548   5834   3761   -153    380   1066       O  
ATOM   1775  CB  ARG A 245      -5.424  18.665 -16.772  1.00 27.97           C  
ANISOU 1775  CB  ARG A 245     4629   4477   1522   -191    784    625       C  
ATOM   1776  CG  ARG A 245      -6.642  19.570 -16.697  1.00 29.72           C  
ANISOU 1776  CG  ARG A 245     4784   4918   1589   -118   1021    217       C  
ATOM   1777  CD  ARG A 245      -7.936  18.784 -16.812  1.00 31.54           C  
ANISOU 1777  CD  ARG A 245     4977   5241   1764   -203   1182     41       C  
ATOM   1778  NE  ARG A 245      -9.086  19.664 -16.994  1.00 33.52           N  
ANISOU 1778  NE  ARG A 245     5050   5629   2057   -117   1368   -507       N  
ATOM   1779  CZ  ARG A 245      -9.797  20.179 -15.997  1.00 50.34           C  
ANISOU 1779  CZ  ARG A 245     6944   8017   4167   -372   1506   -973       C  
ATOM   1780  NH1 ARG A 245      -9.478  19.900 -14.740  1.00 54.79           N  
ANISOU 1780  NH1 ARG A 245     7577   8711   4529   -792   1533   -878       N  
ATOM   1781  NH2 ARG A 245     -10.827  20.972 -16.256  1.00 53.88           N  
ANISOU 1781  NH2 ARG A 245     7016   8589   4868   -216   1551  -1588       N  
ATOM   1782  N   GLN A 246      -1.750  18.902 -16.481  1.00 54.55           N  
ANISOU 1782  N   GLN A 246     7582   5985   7161   -512  -3623   -217       N  
ATOM   1783  CA  GLN A 246      -0.544  18.089 -16.580  1.00 51.22           C  
ANISOU 1783  CA  GLN A 246     7609   5540   6312   -139  -3642   -484       C  
ATOM   1784  C   GLN A 246      -0.173  17.481 -15.230  1.00 49.25           C  
ANISOU 1784  C   GLN A 246     7234   5212   6266   -331  -3536   -350       C  
ATOM   1785  O   GLN A 246       0.721  16.638 -15.141  1.00 47.10           O  
ANISOU 1785  O   GLN A 246     7322   4823   5750    -69  -3587   -539       O  
ATOM   1786  CB  GLN A 246       0.617  18.925 -17.122  1.00 45.82           C  
ANISOU 1786  CB  GLN A 246     6985   5416   5011    276  -3202   -606       C  
ATOM   1787  CG  GLN A 246       0.303  19.641 -18.426  1.00 45.15           C  
ANISOU 1787  CG  GLN A 246     6959   5502   4695    454  -3258   -650       C  
ATOM   1788  CD  GLN A 246       1.515  20.321 -19.029  1.00 44.00           C  
ANISOU 1788  CD  GLN A 246     6846   5887   3984    883  -2831   -630       C  
ATOM   1789  OE1 GLN A 246       2.653  20.031 -18.659  1.00 47.06           O  
ANISOU 1789  OE1 GLN A 246     7319   6425   4136   1137  -2536   -650       O  
ATOM   1790  NE2 GLN A 246       1.277  21.233 -19.964  1.00 46.33           N  
ANISOU 1790  NE2 GLN A 246     7039   6446   4119    956  -2788   -525       N  
ATOM   1791  N   GLY A1001      -0.869  17.911 -14.182  1.00 50.30           N  
ANISOU 1791  N   GLY A1001     6842   5431   6840   -749  -3354      1       N  
ATOM   1792  CA  GLY A1001      -0.598  17.440 -12.837  1.00 44.81           C  
ANISOU 1792  CA  GLY A1001     5948   4736   6341   -950  -3214    213       C  
ATOM   1793  C   GLY A1001       0.297  18.399 -12.077  1.00 40.19           C  
ANISOU 1793  C   GLY A1001     5130   4683   5458   -835  -2680    220       C  
ATOM   1794  O   GLY A1001       0.396  19.574 -12.430  1.00 43.22           O  
ANISOU 1794  O   GLY A1001     5335   5412   5676   -714  -2416    182       O  
ATOM   1795  N   ILE A1002       0.944  17.903 -11.027  1.00 35.11           N  
ANISOU 1795  N   ILE A1002     4495   4068   4775   -808  -2394    299       N  
ATOM   1796  CA  ILE A1002       1.876  18.718 -10.255  1.00 30.81           C  
ANISOU 1796  CA  ILE A1002     3808   3939   3959   -595  -1797    288       C  
ATOM   1797  C   ILE A1002       3.215  18.012 -10.091  1.00 34.78           C  
ANISOU 1797  C   ILE A1002     4705   4386   4126   -307  -1724     96       C  
ATOM   1798  O   ILE A1002       3.327  16.805 -10.312  1.00 38.06           O  
ANISOU 1798  O   ILE A1002     5471   4439   4551   -298  -2093     -5       O  
ATOM   1799  CB  ILE A1002       1.326  19.062  -8.854  1.00 39.42           C  
ANISOU 1799  CB  ILE A1002     4445   5225   5307   -781  -1423    619       C  
ATOM   1800  CG1 ILE A1002       1.254  17.809  -7.979  1.00 41.23           C  
ANISOU 1800  CG1 ILE A1002     4727   5224   5715   -943  -1489    852       C  
ATOM   1801  CG2 ILE A1002      -0.033  19.736  -8.958  1.00 42.28           C  
ANISOU 1801  CG2 ILE A1002     4362   5677   6026  -1015  -1452    854       C  
ATOM   1802  CD1 ILE A1002       0.880  18.096  -6.544  1.00 32.80           C  
ANISOU 1802  CD1 ILE A1002     3265   4462   4735   -979  -1037   1210       C  
ATOM   1803  N   ASP A1003       4.228  18.777  -9.702  1.00 34.83           N  
ANISOU 1803  N   ASP A1003     4635   4704   3893    -65  -1313     57       N  
ATOM   1804  CA  ASP A1003       5.551  18.226  -9.448  1.00 33.63           C  
ANISOU 1804  CA  ASP A1003     4766   4531   3479    212  -1194    -61       C  
ATOM   1805  C   ASP A1003       5.591  17.584  -8.067  1.00 30.04           C  
ANISOU 1805  C   ASP A1003     4270   3965   3179     51  -1076     88       C  
ATOM   1806  O   ASP A1003       5.804  18.265  -7.063  1.00 26.52           O  
ANISOU 1806  O   ASP A1003     3590   3735   2751     68   -758    199       O  
ATOM   1807  CB  ASP A1003       6.619  19.316  -9.567  1.00 35.67           C  
ANISOU 1807  CB  ASP A1003     4883   5118   3550    499   -876    -56       C  
ATOM   1808  CG  ASP A1003       8.028  18.767  -9.464  1.00 44.90           C  
ANISOU 1808  CG  ASP A1003     6294   6278   4488    818   -762   -120       C  
ATOM   1809  OD1 ASP A1003       8.211  17.549  -9.669  1.00 51.77           O  
ANISOU 1809  OD1 ASP A1003     7537   6906   5229    910   -965   -269       O  
ATOM   1810  OD2 ASP A1003       8.956  19.557  -9.186  1.00 47.02           O  
ANISOU 1810  OD2 ASP A1003     6362   6742   4760    983   -525     -4       O  
ATOM   1811  N   CYS A1004       5.388  16.270  -8.021  1.00 30.73           N  
ANISOU 1811  N   CYS A1004     4605   3693   3378    -69  -1391     94       N  
ATOM   1812  CA  CYS A1004       5.364  15.536  -6.758  1.00 33.81           C  
ANISOU 1812  CA  CYS A1004     4938   3969   3937   -242  -1313    330       C  
ATOM   1813  C   CYS A1004       6.760  15.382  -6.160  1.00 37.08           C  
ANISOU 1813  C   CYS A1004     5551   4445   4091     31  -1084    214       C  
ATOM   1814  O   CYS A1004       6.926  14.793  -5.090  1.00 42.48           O  
ANISOU 1814  O   CYS A1004     6236   5059   4843    -54  -1006    392       O  
ATOM   1815  CB  CYS A1004       4.724  14.159  -6.954  1.00 35.82           C  
ANISOU 1815  CB  CYS A1004     5357   3736   4516   -492  -1837    439       C  
ATOM   1816  SG  CYS A1004       2.996  14.206  -7.483  1.00 59.73           S  
ANISOU 1816  SG  CYS A1004     8066   6588   8043   -896  -2214    714       S  
ATOM   1817  N   SER A1005       7.759  15.911  -6.859  1.00 35.49           N  
ANISOU 1817  N   SER A1005     5479   4389   3618    366   -982    -18       N  
ATOM   1818  CA  SER A1005       9.127  15.917  -6.363  1.00 38.00           C  
ANISOU 1818  CA  SER A1005     5898   4772   3768    632   -775    -68       C  
ATOM   1819  C   SER A1005       9.367  17.134  -5.481  1.00 41.19           C  
ANISOU 1819  C   SER A1005     5990   5449   4212    651   -476     51       C  
ATOM   1820  O   SER A1005      10.193  17.096  -4.572  1.00 49.19           O  
ANISOU 1820  O   SER A1005     7041   6449   5199    758   -369     82       O  
ATOM   1821  CB  SER A1005      10.121  15.897  -7.522  1.00 36.64           C  
ANISOU 1821  CB  SER A1005     5929   4660   3330   1034   -791   -251       C  
ATOM   1822  OG  SER A1005      10.135  14.630  -8.153  1.00 45.90           O  
ANISOU 1822  OG  SER A1005     7517   5532   4391   1165  -1131   -455       O  
ATOM   1823  N   PHE A1006       8.640  18.211  -5.757  1.00 38.99           N  
ANISOU 1823  N   PHE A1006     5431   5370   4014    575   -418     90       N  
ATOM   1824  CA  PHE A1006       8.720  19.417  -4.942  1.00 32.13           C  
ANISOU 1824  CA  PHE A1006     4299   4695   3212    639   -262    141       C  
ATOM   1825  C   PHE A1006       7.711  19.363  -3.802  1.00 37.25           C  
ANISOU 1825  C   PHE A1006     4834   5424   3896    502   -162    264       C  
ATOM   1826  O   PHE A1006       8.081  19.409  -2.628  1.00 34.31           O  
ANISOU 1826  O   PHE A1006     4509   5098   3429    637    -64    290       O  
ATOM   1827  CB  PHE A1006       8.483  20.667  -5.793  1.00 26.00           C  
ANISOU 1827  CB  PHE A1006     3260   4086   2531    674   -284    135       C  
ATOM   1828  CG  PHE A1006       8.376  21.934  -4.991  1.00 26.93           C  
ANISOU 1828  CG  PHE A1006     3127   4322   2784    752   -262    138       C  
ATOM   1829  CD1 PHE A1006       9.516  22.608  -4.584  1.00 25.79           C  
ANISOU 1829  CD1 PHE A1006     2935   4127   2738    960   -338    136       C  
ATOM   1830  CD2 PHE A1006       7.137  22.451  -4.642  1.00 29.43           C  
ANISOU 1830  CD2 PHE A1006     3252   4767   3164    658   -226    146       C  
ATOM   1831  CE1 PHE A1006       9.422  23.771  -3.843  1.00 29.07           C  
ANISOU 1831  CE1 PHE A1006     3248   4464   3333    968   -410     56       C  
ATOM   1832  CE2 PHE A1006       7.037  23.613  -3.902  1.00 26.92           C  
ANISOU 1832  CE2 PHE A1006     2767   4540   2921    841   -266     72       C  
ATOM   1833  CZ  PHE A1006       8.180  24.274  -3.502  1.00 28.12           C  
ANISOU 1833  CZ  PHE A1006     3000   4504   3180    981   -393     -8       C  
ATOM   1834  N   TRP A1007       6.434  19.269  -4.156  1.00 34.40           N  
ANISOU 1834  N   TRP A1007     4309   5103   3660    278   -190    380       N  
ATOM   1835  CA  TRP A1007       5.369  19.192  -3.165  1.00 33.97           C  
ANISOU 1835  CA  TRP A1007     4044   5208   3656    185    -28    631       C  
ATOM   1836  C   TRP A1007       5.445  17.865  -2.423  1.00 39.52           C  
ANISOU 1836  C   TRP A1007     4894   5772   4350     76    -20    859       C  
ATOM   1837  O   TRP A1007       4.670  16.943  -2.676  1.00 43.24           O  
ANISOU 1837  O   TRP A1007     5299   6071   5059   -212   -171   1112       O  
ATOM   1838  CB  TRP A1007       4.006  19.376  -3.831  1.00 29.02           C  
ANISOU 1838  CB  TRP A1007     3131   4623   3273    -56    -96    786       C  
ATOM   1839  CG  TRP A1007       3.901  20.683  -4.551  1.00 27.56           C  
ANISOU 1839  CG  TRP A1007     2789   4567   3118     38   -126    593       C  
ATOM   1840  CD1 TRP A1007       4.045  20.895  -5.891  1.00 26.12           C  
ANISOU 1840  CD1 TRP A1007     2668   4270   2988    -24   -341    447       C  
ATOM   1841  CD2 TRP A1007       3.656  21.966  -3.964  1.00 34.02           C  
ANISOU 1841  CD2 TRP A1007     3376   5645   3904    261     23    533       C  
ATOM   1842  NE1 TRP A1007       3.893  22.230  -6.176  1.00 25.94           N  
ANISOU 1842  NE1 TRP A1007     2412   4418   3025     75   -320    369       N  
ATOM   1843  CE2 TRP A1007       3.654  22.909  -5.010  1.00 31.88           C  
ANISOU 1843  CE2 TRP A1007     2991   5363   3760    245   -137    390       C  
ATOM   1844  CE3 TRP A1007       3.433  22.408  -2.657  1.00 38.91           C  
ANISOU 1844  CE3 TRP A1007     3906   6514   4367    537    242    575       C  
ATOM   1845  CZ2 TRP A1007       3.437  24.269  -4.789  1.00 35.80           C  
ANISOU 1845  CZ2 TRP A1007     3261   6012   4329    434   -143    287       C  
ATOM   1846  CZ3 TRP A1007       3.218  23.757  -2.439  1.00 38.74           C  
ANISOU 1846  CZ3 TRP A1007     3721   6657   4344    806    228    401       C  
ATOM   1847  CH2 TRP A1007       3.221  24.671  -3.499  1.00 36.28           C  
ANISOU 1847  CH2 TRP A1007     3273   6253   4257    723      9    257       C  
ATOM   1848  N   ASN A1008       6.398  17.789  -1.501  1.00 37.67           N  
ANISOU 1848  N   ASN A1008     4847   5567   3898    300     86    796       N  
ATOM   1849  CA  ASN A1008       6.712  16.560  -0.793  1.00 38.21           C  
ANISOU 1849  CA  ASN A1008     5093   5484   3942    226     70    998       C  
ATOM   1850  C   ASN A1008       6.929  16.852   0.687  1.00 41.46           C  
ANISOU 1850  C   ASN A1008     5519   6167   4066    505    321   1110       C  
ATOM   1851  O   ASN A1008       7.608  17.815   1.040  1.00 39.84           O  
ANISOU 1851  O   ASN A1008     5405   6062   3669    820    341    834       O  
ATOM   1852  CB  ASN A1008       7.954  15.908  -1.405  1.00 38.03           C  
ANISOU 1852  CB  ASN A1008     5412   5126   3911    265   -156    743       C  
ATOM   1853  CG  ASN A1008       8.093  14.445  -1.041  1.00 46.41           C  
ANISOU 1853  CG  ASN A1008     6657   5903   5073    102   -314    938       C  
ATOM   1854  OD1 ASN A1008       7.723  14.024   0.053  1.00 52.35           O  
ANISOU 1854  OD1 ASN A1008     7318   6759   5813     40   -182   1283       O  
ATOM   1855  ND2 ASN A1008       8.631  13.658  -1.965  1.00 47.27           N  
ANISOU 1855  ND2 ASN A1008     7030   5664   5267     83   -616    734       N  
ATOM   1856  N   GLU A1009       6.349  16.027   1.552  1.00 42.46           N  
ANISOU 1856  N   GLU A1009     5553   6403   4176    417    463   1549       N  
ATOM   1857  CA  GLU A1009       6.491  16.218   2.991  1.00 44.33           C  
ANISOU 1857  CA  GLU A1009     5845   6970   4028    769    723   1698       C  
ATOM   1858  C   GLU A1009       7.915  15.900   3.436  1.00 41.74           C  
ANISOU 1858  C   GLU A1009     5918   6408   3536    928    565   1449       C  
ATOM   1859  O   GLU A1009       8.339  16.280   4.528  1.00 43.10           O  
ANISOU 1859  O   GLU A1009     6203   6697   3478   1237    619   1308       O  
ATOM   1860  CB  GLU A1009       5.489  15.346   3.753  1.00 56.37           C  
ANISOU 1860  CB  GLU A1009     7092   8707   5621    631    942   2347       C  
ATOM   1861  CG  GLU A1009       5.331  15.715   5.222  1.00 68.14           C  
ANISOU 1861  CG  GLU A1009     8549  10549   6792   1053   1195   2348       C  
ATOM   1862  CD  GLU A1009       4.581  14.662   6.012  1.00 79.74           C  
ANISOU 1862  CD  GLU A1009     9742  12170   8387    924   1361   2972       C  
ATOM   1863  OE1 GLU A1009       4.502  13.509   5.539  1.00 82.10           O  
ANISOU 1863  OE1 GLU A1009     9967  12162   9067    471   1176   3332       O  
ATOM   1864  OE2 GLU A1009       4.070  14.986   7.105  1.00 87.10           O  
ANISOU 1864  OE2 GLU A1009    10522  13500   9071   1306   1623   3118       O  
ATOM   1865  N   SER A1010       8.652  15.212   2.570  1.00 45.97           N  
ANISOU 1865  N   SER A1010     6621   6519   4324    692    297   1286       N  
ATOM   1866  CA  SER A1010      10.007  14.771   2.875  1.00 36.78           C  
ANISOU 1866  CA  SER A1010     5784   5096   3094    810    139   1106       C  
ATOM   1867  C   SER A1010      10.978  15.931   3.086  1.00 30.95           C  
ANISOU 1867  C   SER A1010     5152   4379   2227   1150     70    734       C  
ATOM   1868  O   SER A1010      12.035  15.756   3.686  1.00 36.43           O  
ANISOU 1868  O   SER A1010     6005   4897   2938   1260    -46    608       O  
ATOM   1869  CB  SER A1010      10.526  13.862   1.758  1.00 37.83           C  
ANISOU 1869  CB  SER A1010     6053   4815   3506    586   -122    982       C  
ATOM   1870  OG  SER A1010       9.676  12.743   1.579  1.00 44.87           O  
ANISOU 1870  OG  SER A1010     6870   5545   4634    258   -238   1303       O  
ATOM   1871  N   TYR A1011      10.619  17.114   2.597  1.00 34.00           N  
ANISOU 1871  N   TYR A1011     5359   4910   2648   1245     82    555       N  
ATOM   1872  CA  TYR A1011      11.497  18.275   2.710  1.00 35.77           C  
ANISOU 1872  CA  TYR A1011     5575   5033   2981   1482    -97    245       C  
ATOM   1873  C   TYR A1011      11.158  19.125   3.930  1.00 37.05           C  
ANISOU 1873  C   TYR A1011     5733   5366   2979   1800    -82    144       C  
ATOM   1874  O   TYR A1011      11.775  20.163   4.171  1.00 37.73           O  
ANISOU 1874  O   TYR A1011     5855   5316   3166   2040   -315   -113       O  
ATOM   1875  CB  TYR A1011      11.430  19.112   1.432  1.00 32.70           C  
ANISOU 1875  CB  TYR A1011     5001   4647   2778   1434   -184    140       C  
ATOM   1876  CG  TYR A1011      12.029  18.401   0.241  1.00 32.61           C  
ANISOU 1876  CG  TYR A1011     5011   4440   2938   1254   -224    168       C  
ATOM   1877  CD1 TYR A1011      13.400  18.425   0.014  1.00 31.88           C  
ANISOU 1877  CD1 TYR A1011     4951   4140   3023   1349   -347    112       C  
ATOM   1878  CD2 TYR A1011      11.229  17.690  -0.644  1.00 32.16           C  
ANISOU 1878  CD2 TYR A1011     4916   4391   2913   1007   -150    242       C  
ATOM   1879  CE1 TYR A1011      13.958  17.770  -1.068  1.00 31.83           C  
ANISOU 1879  CE1 TYR A1011     4970   4038   3085   1317   -328    140       C  
ATOM   1880  CE2 TYR A1011      11.777  17.031  -1.729  1.00 34.18           C  
ANISOU 1880  CE2 TYR A1011     5274   4477   3237    973   -229    190       C  
ATOM   1881  CZ  TYR A1011      13.142  17.074  -1.936  1.00 35.17           C  
ANISOU 1881  CZ  TYR A1011     5461   4492   3408   1184   -281    142       C  
ATOM   1882  OH  TYR A1011      13.694  16.420  -3.014  1.00 40.39           O  
ANISOU 1882  OH  TYR A1011     6232   5067   4045   1284   -306     97       O  
ATOM   1883  N   LEU A1012      10.174  18.670   4.697  1.00 34.92           N  
ANISOU 1883  N   LEU A1012     3635   6337   3297   -184   -691    405       N  
ATOM   1884  CA  LEU A1012       9.804  19.318   5.948  1.00 38.07           C  
ANISOU 1884  CA  LEU A1012     4145   6616   3705   -214   -759    380       C  
ATOM   1885  C   LEU A1012      10.433  18.567   7.117  1.00 41.85           C  
ANISOU 1885  C   LEU A1012     4578   7172   4152   -138   -819    466       C  
ATOM   1886  O   LEU A1012      10.580  17.347   7.066  1.00 45.37           O  
ANISOU 1886  O   LEU A1012     4957   7688   4594    -34   -801    544       O  
ATOM   1887  CB  LEU A1012       8.283  19.368   6.101  1.00 34.68           C  
ANISOU 1887  CB  LEU A1012     3861   6040   3275   -217   -721    315       C  
ATOM   1888  CG  LEU A1012       7.496  20.520   5.466  1.00 28.99           C  
ANISOU 1888  CG  LEU A1012     3208   5202   2605   -303   -708    242       C  
ATOM   1889  CD1 LEU A1012       7.910  20.792   4.029  1.00 24.65           C  
ANISOU 1889  CD1 LEU A1012     2580   4692   2093   -379   -669    254       C  
ATOM   1890  CD2 LEU A1012       6.015  20.208   5.529  1.00 23.87           C  
ANISOU 1890  CD2 LEU A1012     2653   4462   1954   -283   -657    225       C  
ATOM   1891  N   THR A1013      10.805  19.293   8.167  1.00 37.94           N  
ANISOU 1891  N   THR A1013     4120   6662   3635   -186   -908    460       N  
ATOM   1892  CA  THR A1013      11.459  18.678   9.319  1.00 38.27           C  
ANISOU 1892  CA  THR A1013     4115   6786   3639   -148   -980    561       C  
ATOM   1893  C   THR A1013      10.529  18.583  10.524  1.00 36.22           C  
ANISOU 1893  C   THR A1013     3989   6478   3296   -142   -998    530       C  
ATOM   1894  O   THR A1013       9.487  19.236  10.572  1.00 33.82           O  
ANISOU 1894  O   THR A1013     3808   6082   2961   -165   -966    419       O  
ATOM   1895  CB  THR A1013      12.721  19.455   9.733  1.00 40.54           C  
ANISOU 1895  CB  THR A1013     4332   7141   3931   -223  -1090    604       C  
ATOM   1896  OG1 THR A1013      12.350  20.749  10.223  1.00 44.19           O  
ANISOU 1896  OG1 THR A1013     4935   7505   4352   -306  -1163    481       O  
ATOM   1897  CG2 THR A1013      13.665  19.610   8.550  1.00 38.85           C  
ANISOU 1897  CG2 THR A1013     3958   7014   3789   -239  -1061    662       C  
ATOM   1898  N   GLY A1014      10.919  17.760  11.494  1.00 39.48           N  
ANISOU 1898  N   GLY A1014     4356   6974   3671   -109  -1048    648       N  
ATOM   1899  CA  GLY A1014      10.164  17.597  12.724  1.00 40.05           C  
ANISOU 1899  CA  GLY A1014     4526   7058   3635   -116  -1063    649       C  
ATOM   1900  C   GLY A1014       8.824  16.917  12.530  1.00 37.52           C  
ANISOU 1900  C   GLY A1014     4264   6676   3314    -66   -966    648       C  
ATOM   1901  O   GLY A1014       8.565  16.321  11.484  1.00 39.67           O  
ANISOU 1901  O   GLY A1014     4507   6892   3675    -17   -908    667       O  
ATOM   1902  N   SER A1015       7.971  17.000  13.548  1.00 29.67           N  
ANISOU 1902  N   SER A1015     3351   5715   2207    -81   -955    634       N  
ATOM   1903  CA  SER A1015       6.621  16.455  13.464  1.00 27.40           C  
ANISOU 1903  CA  SER A1015     3106   5388   1915    -50   -866    654       C  
ATOM   1904  C   SER A1015       5.664  17.533  12.974  1.00 41.06           C  
ANISOU 1904  C   SER A1015     4924   7044   3633    -65   -798    500       C  
ATOM   1905  O   SER A1015       6.015  18.712  12.954  1.00 40.02           O  
ANISOU 1905  O   SER A1015     4837   6893   3474    -99   -837    377       O  
ATOM   1906  CB  SER A1015       6.162  15.909  14.819  1.00 29.14           C  
ANISOU 1906  CB  SER A1015     3328   5729   2014    -60   -877    756       C  
ATOM   1907  OG  SER A1015       5.928  16.959  15.742  1.00 47.37           O  
ANISOU 1907  OG  SER A1015     5714   8125   4158    -98   -886    642       O  
ATOM   1908  N   ARG A1016       4.459  17.131  12.583  1.00 37.43           N  
ANISOU 1908  N   ARG A1016     4482   6537   3202    -44   -715    525       N  
ATOM   1909  CA  ARG A1016       3.504  18.071  12.007  1.00 31.18           C  
ANISOU 1909  CA  ARG A1016     3743   5680   2422    -54   -654    414       C  
ATOM   1910  C   ARG A1016       2.946  19.042  13.043  1.00 41.97           C  
ANISOU 1910  C   ARG A1016     5167   7145   3636    -51   -646    321       C  
ATOM   1911  O   ARG A1016       2.850  20.241  12.786  1.00 36.74           O  
ANISOU 1911  O   ARG A1016     4556   6443   2960    -64   -664    185       O  
ATOM   1912  CB  ARG A1016       2.350  17.330  11.331  1.00 27.64           C  
ANISOU 1912  CB  ARG A1016     3287   5170   2045    -44   -582    495       C  
ATOM   1913  CG  ARG A1016       1.447  18.255  10.532  1.00 22.17           C  
ANISOU 1913  CG  ARG A1016     2621   4411   1391    -65   -533    413       C  
ATOM   1914  CD  ARG A1016       0.282  17.514   9.908  1.00 21.43           C  
ANISOU 1914  CD  ARG A1016     2517   4262   1365    -76   -479    519       C  
ATOM   1915  NE  ARG A1016      -0.475  18.383   9.012  1.00 23.61           N  
ANISOU 1915  NE  ARG A1016     2798   4480   1693   -114   -450    469       N  
ATOM   1916  CZ  ARG A1016      -0.213  18.528   7.717  1.00 19.21           C  
ANISOU 1916  CZ  ARG A1016     2250   3811   1239   -171   -466    441       C  
ATOM   1917  NH1 ARG A1016       0.785  17.855   7.160  1.00 18.94           N  
ANISOU 1917  NH1 ARG A1016     2221   3731   1245   -176   -496    441       N  
ATOM   1918  NH2 ARG A1016      -0.950  19.344   6.976  1.00 18.58           N  
ANISOU 1918  NH2 ARG A1016     2159   3695   1206   -226   -455    425       N  
ATOM   1919  N   ASP A1017       2.574  18.523  14.208  1.00 45.97           N  
ANISOU 1919  N   ASP A1017     5661   7793   4014    -34   -627    393       N  
ATOM   1920  CA  ASP A1017       2.006  19.356  15.263  1.00 54.02           C  
ANISOU 1920  CA  ASP A1017     6735   8952   4837    -17   -601    292       C  
ATOM   1921  C   ASP A1017       3.039  20.332  15.819  1.00 50.11           C  
ANISOU 1921  C   ASP A1017     6327   8468   4243    -53   -709    154       C  
ATOM   1922  O   ASP A1017       2.686  21.396  16.330  1.00 51.50           O  
ANISOU 1922  O   ASP A1017     6595   8696   4276    -40   -710     -9       O  
ATOM   1923  CB  ASP A1017       1.433  18.490  16.388  1.00 59.42           C  
ANISOU 1923  CB  ASP A1017     7367   9820   5392     -5   -554    426       C  
ATOM   1924  CG  ASP A1017       2.336  17.328  16.751  1.00 67.19           C  
ANISOU 1924  CG  ASP A1017     8291  10821   6418    -44   -632    592       C  
ATOM   1925  OD1 ASP A1017       2.976  16.766  15.837  1.00 67.79           O  
ANISOU 1925  OD1 ASP A1017     8335  10754   6667    -48   -673    649       O  
ATOM   1926  OD2 ASP A1017       2.399  16.977  17.949  1.00 71.79           O  
ANISOU 1926  OD2 ASP A1017     8850  11578   6848    -67   -652    668       O  
ATOM   1927  N   GLU A1018       4.313  19.970  15.717  1.00 45.03           N  
ANISOU 1927  N   GLU A1018     5655   7780   3673    -95   -808    216       N  
ATOM   1928  CA  GLU A1018       5.386  20.863  16.131  1.00 39.44           C  
ANISOU 1928  CA  GLU A1018     5019   7065   2902   -146   -942    117       C  
ATOM   1929  C   GLU A1018       5.549  21.986  15.113  1.00 35.52           C  
ANISOU 1929  C   GLU A1018     4567   6410   2519   -165   -987    -13       C  
ATOM   1930  O   GLU A1018       5.852  23.123  15.473  1.00 41.10           O  
ANISOU 1930  O   GLU A1018     5382   7089   3146   -200  -1093   -156       O  
ATOM   1931  CB  GLU A1018       6.700  20.098  16.300  1.00 39.68           C  
ANISOU 1931  CB  GLU A1018     4962   7128   2987   -181  -1032    258       C  
ATOM   1932  CG  GLU A1018       7.856  20.961  16.783  1.00 47.37           C  
ANISOU 1932  CG  GLU A1018     5989   8111   3898   -246  -1191    189       C  
ATOM   1933  CD  GLU A1018       8.484  20.441  18.061  1.00 57.54           C  
ANISOU 1933  CD  GLU A1018     7257   9564   5040   -290  -1272    292       C  
ATOM   1934  OE1 GLU A1018       9.497  21.020  18.507  1.00 59.21           O  
ANISOU 1934  OE1 GLU A1018     7497   9799   5199   -355  -1418    265       O  
ATOM   1935  OE2 GLU A1018       7.964  19.454  18.622  1.00 61.19           O  
ANISOU 1935  OE2 GLU A1018     7666  10139   5444   -272  -1202    415       O  
ATOM   1936  N   ARG A1019       5.338  21.664  13.841  1.00 36.93           N  
ANISOU 1936  N   ARG A1019     4671   6484   2879   -151   -923     39       N  
ATOM   1937  CA  ARG A1019       5.383  22.670  12.789  1.00 34.76           C  
ANISOU 1937  CA  ARG A1019     4413   6073   2720   -182   -962    -53       C  
ATOM   1938  C   ARG A1019       4.182  23.602  12.896  1.00 36.66           C  
ANISOU 1938  C   ARG A1019     4735   6307   2889   -162   -932   -188       C  
ATOM   1939  O   ARG A1019       4.269  24.782  12.561  1.00 39.55           O  
ANISOU 1939  O   ARG A1019     5158   6581   3287   -201  -1029   -309       O  
ATOM   1940  CB  ARG A1019       5.427  22.014  11.407  1.00 32.90           C  
ANISOU 1940  CB  ARG A1019     4077   5760   2664   -182   -891     40       C  
ATOM   1941  CG  ARG A1019       6.710  21.245  11.126  1.00 35.15           C  
ANISOU 1941  CG  ARG A1019     4266   6075   3015   -193   -919    143       C  
ATOM   1942  CD  ARG A1019       6.825  20.861   9.656  1.00 31.09           C  
ANISOU 1942  CD  ARG A1019     3672   5502   2637   -201   -855    186       C  
ATOM   1943  NE  ARG A1019       5.756  19.965   9.227  1.00 28.63           N  
ANISOU 1943  NE  ARG A1019     3366   5167   2345   -162   -752    232       N  
ATOM   1944  CZ  ARG A1019       5.833  18.639   9.259  1.00 30.72           C  
ANISOU 1944  CZ  ARG A1019     3588   5472   2611   -114   -721    335       C  
ATOM   1945  NH1 ARG A1019       6.933  18.046   9.703  1.00 26.58           N  
ANISOU 1945  NH1 ARG A1019     2994   5034   2073    -89   -775    410       N  
ATOM   1946  NH2 ARG A1019       4.809  17.904   8.847  1.00 32.97           N  
ANISOU 1946  NH2 ARG A1019     3898   5711   2919    -94   -658    379       N  
ATOM   1947  N   LYS A1020       3.060  23.064  13.365  1.00 28.71           N  
ANISOU 1947  N   LYS A1020     3715   5408   1786    -98   -806   -160       N  
ATOM   1948  CA  LYS A1020       1.864  23.868  13.577  1.00 29.56           C  
ANISOU 1948  CA  LYS A1020     3864   5575   1791    -45   -745   -293       C  
ATOM   1949  C   LYS A1020       2.062  24.811  14.757  1.00 49.70           C  
ANISOU 1949  C   LYS A1020     6547   8200   4138    -38   -810   -487       C  
ATOM   1950  O   LYS A1020       1.770  26.004  14.667  1.00 48.17           O  
ANISOU 1950  O   LYS A1020     6429   7957   3917    -27   -859   -688       O  
ATOM   1951  CB  LYS A1020       0.640  22.980  13.815  1.00 29.40           C  
ANISOU 1951  CB  LYS A1020     3766   5687   1717     32   -586   -181       C  
ATOM   1952  CG  LYS A1020      -0.654  23.762  14.007  1.00 30.56           C  
ANISOU 1952  CG  LYS A1020     3915   5946   1749    130   -491   -308       C  
ATOM   1953  CD  LYS A1020      -1.852  22.843  14.192  1.00 42.75           C  
ANISOU 1953  CD  LYS A1020     5352   7632   3259    198   -339   -137       C  
ATOM   1954  CE  LYS A1020      -1.753  22.052  15.486  1.00 46.62           C  
ANISOU 1954  CE  LYS A1020     5835   8281   3598    207   -299    -57       C  
ATOM   1955  NZ  LYS A1020      -2.945  21.186  15.701  1.00 49.24           N  
ANISOU 1955  NZ  LYS A1020     6044   8754   3912    255   -174    134       N  
ATOM   1956  N   LYS A1021       2.560  24.264  15.862  1.00 46.93           N  
ANISOU 1956  N   LYS A1021     6228   7960   3642    -49   -822   -439       N  
ATOM   1957  CA  LYS A1021       2.830  25.051  17.059  1.00 47.24           C  
ANISOU 1957  CA  LYS A1021     6420   8075   3456    -63   -891   -618       C  
ATOM   1958  C   LYS A1021       3.838  26.155  16.757  1.00 47.49           C  
ANISOU 1958  C   LYS A1021     6563   7927   3553   -158  -1099   -742       C  
ATOM   1959  O   LYS A1021       3.670  27.297  17.185  1.00 51.59           O  
ANISOU 1959  O   LYS A1021     7232   8413   3958   -170  -1162   -977       O  
ATOM   1960  CB  LYS A1021       3.345  24.152  18.186  1.00 47.33           C  
ANISOU 1960  CB  LYS A1021     6425   8239   3319    -89   -902   -493       C  
ATOM   1961  CG  LYS A1021       3.405  24.823  19.549  1.00 48.69           C  
ANISOU 1961  CG  LYS A1021     6765   8535   3199   -101   -944   -671       C  
ATOM   1962  CD  LYS A1021       3.873  23.847  20.618  1.00 50.36           C  
ANISOU 1962  CD  LYS A1021     6942   8927   3267   -141   -963   -510       C  
ATOM   1963  CE  LYS A1021       3.728  24.432  22.014  1.00 58.87           C  
ANISOU 1963  CE  LYS A1021     8190  10169   4007   -150   -972   -686       C  
ATOM   1964  NZ  LYS A1021       4.511  25.687  22.182  1.00 64.37           N  
ANISOU 1964  NZ  LYS A1021     9103  10720   4634   -219  -1163   -909       N  
ATOM   1965  N   SER A1022       4.876  25.803  16.005  1.00 48.09           N  
ANISOU 1965  N   SER A1022     6559   7888   3823   -221  -1203   -589       N  
ATOM   1966  CA  SER A1022       5.905  26.756  15.610  1.00 46.50           C  
ANISOU 1966  CA  SER A1022     6418   7524   3727   -305  -1419   -649       C  
ATOM   1967  C   SER A1022       5.339  27.843  14.705  1.00 46.43           C  
ANISOU 1967  C   SER A1022     6439   7362   3842   -335  -1461   -774       C  
ATOM   1968  O   SER A1022       5.620  29.026  14.894  1.00 50.23           O  
ANISOU 1968  O   SER A1022     7055   7725   4304   -420  -1637   -930       O  
ATOM   1969  CB  SER A1022       7.057  26.038  14.905  1.00 44.26           C  
ANISOU 1969  CB  SER A1022     5973   7211   3633   -320  -1459   -458       C  
ATOM   1970  OG  SER A1022       8.025  26.961  14.439  1.00 45.26           O  
ANISOU 1970  OG  SER A1022     6090   7221   3885   -369  -1648   -508       O  
ATOM   1971  N   LEU A1023       4.542  27.431  13.723  1.00 45.51           N  
ANISOU 1971  N   LEU A1023     6195   7240   3856   -287  -1320   -697       N  
ATOM   1972  CA  LEU A1023       3.930  28.362  12.780  1.00 39.93           C  
ANISOU 1972  CA  LEU A1023     5472   6412   3288   -318  -1362   -787       C  
ATOM   1973  C   LEU A1023       3.039  29.369  13.494  1.00 45.51           C  
ANISOU 1973  C   LEU A1023     6288   7154   3849   -269  -1347  -1076       C  
ATOM   1974  O   LEU A1023       3.159  30.576  13.286  1.00 49.17           O  
ANISOU 1974  O   LEU A1023     6809   7473   4398   -347  -1494  -1243       O  
ATOM   1975  CB  LEU A1023       3.118  27.603  11.730  1.00 32.90           C  
ANISOU 1975  CB  LEU A1023     4430   5547   2524   -264  -1205   -649       C  
ATOM   1976  CG  LEU A1023       2.429  28.446  10.656  1.00 35.04           C  
ANISOU 1976  CG  LEU A1023     4645   5709   2959   -302  -1259   -702       C  
ATOM   1977  CD1 LEU A1023       3.461  29.176   9.812  1.00 37.82           C  
ANISOU 1977  CD1 LEU A1023     4980   5860   3531   -414  -1462   -654       C  
ATOM   1978  CD2 LEU A1023       1.527  27.579   9.787  1.00 30.31           C  
ANISOU 1978  CD2 LEU A1023     3916   5168   2431   -260  -1102   -550       C  
ATOM   1979  N   LEU A1024       2.147  28.857  14.337  1.00 41.13           N  
ANISOU 1979  N   LEU A1024     5742   6787   3098   -114  -1156  -1149       N  
ATOM   1980  CA  LEU A1024       1.228  29.695  15.098  1.00 49.51           C  
ANISOU 1980  CA  LEU A1024     6902   7894   4013     37  -1084  -1469       C  
ATOM   1981  C   LEU A1024       1.981  30.623  16.044  1.00 54.44           C  
ANISOU 1981  C   LEU A1024     7732   8438   4516    -47  -1232  -1684       C  
ATOM   1982  O   LEU A1024       1.632  31.796  16.179  1.00 56.69           O  
ANISOU 1982  O   LEU A1024     8125   8577   4839     20  -1290  -1992       O  
ATOM   1983  CB  LEU A1024       0.242  28.828  15.884  1.00 49.28           C  
ANISOU 1983  CB  LEU A1024     6825   8122   3779    203   -832  -1428       C  
ATOM   1984  CG  LEU A1024      -0.719  27.976  15.052  1.00 45.65           C  
ANISOU 1984  CG  LEU A1024     6176   7755   3413    284   -680  -1224       C  
ATOM   1985  CD1 LEU A1024      -1.489  27.015  15.940  1.00 44.24           C  
ANISOU 1985  CD1 LEU A1024     5936   7825   3047    385   -466  -1099       C  
ATOM   1986  CD2 LEU A1024      -1.672  28.857  14.262  1.00 42.03           C  
ANISOU 1986  CD2 LEU A1024     5678   7219   3072    417   -673  -1414       C  
ATOM   1987  N   SER A1025       3.014  30.094  16.694  1.00 54.29           N  
ANISOU 1987  N   SER A1025     7776   8480   4373   -183  -1310  -1526       N  
ATOM   1988  CA  SER A1025       3.832  30.889  17.603  1.00 57.26           C  
ANISOU 1988  CA  SER A1025     8357   8798   4600   -317  -1481  -1683       C  
ATOM   1989  C   SER A1025       4.544  32.016  16.862  1.00 58.07           C  
ANISOU 1989  C   SER A1025     8471   8682   4910   -510  -1706  -1740       C  
ATOM   1990  O   SER A1025       4.745  33.100  17.408  1.00 59.65           O  
ANISOU 1990  O   SER A1025     8807   8804   5054   -581  -1809  -2003       O  
ATOM   1991  CB  SER A1025       4.856  30.006  18.318  1.00 59.63           C  
ANISOU 1991  CB  SER A1025     8698   9189   4769   -400  -1569  -1459       C  
ATOM   1992  OG  SER A1025       5.699  30.777  19.156  1.00 66.24           O  
ANISOU 1992  OG  SER A1025     9755   9959   5453   -550  -1781  -1584       O  
ATOM   1993  N   LYS A1026       4.920  31.747  15.616  1.00 58.75           N  
ANISOU 1993  N   LYS A1026     8386   8694   5244   -599  -1764  -1492       N  
ATOM   1994  CA  LYS A1026       5.616  32.725  14.787  1.00 62.98           C  
ANISOU 1994  CA  LYS A1026     8776   9152   6003   -795  -1903  -1490       C  
ATOM   1995  C   LYS A1026       4.695  33.885  14.415  1.00 67.78           C  
ANISOU 1995  C   LYS A1026     9444   9508   6801   -653  -1960  -1787       C  
ATOM   1996  O   LYS A1026       5.144  35.020  14.248  1.00 71.80           O  
ANISOU 1996  O   LYS A1026     9974   9825   7481   -738  -2142  -1904       O  
ATOM   1997  CB  LYS A1026       6.169  32.047  13.529  1.00 61.00           C  
ANISOU 1997  CB  LYS A1026     8234   8963   5980   -853  -1824  -1147       C  
ATOM   1998  CG  LYS A1026       6.935  32.963  12.590  1.00 63.31           C  
ANISOU 1998  CG  LYS A1026     8255   9254   6547   -809  -1954  -1248       C  
ATOM   1999  CD  LYS A1026       7.676  32.154  11.535  1.00 65.34           C  
ANISOU 1999  CD  LYS A1026     8316   9495   7016   -638  -1940  -1039       C  
ATOM   2000  CE  LYS A1026       8.121  33.027  10.373  1.00 69.04           C  
ANISOU 2000  CE  LYS A1026     8685   9834   7713   -801  -2036   -934       C  
ATOM   2001  NZ  LYS A1026       6.959  33.489   9.561  1.00 67.42           N  
ANISOU 2001  NZ  LYS A1026     8493   9478   7644   -850  -1995   -930       N  
ATOM   2002  N   PHE A1027       3.404  33.596  14.300  1.00 63.26           N  
ANISOU 2002  N   PHE A1027     8892   8906   6236   -408  -1814  -1892       N  
ATOM   2003  CA  PHE A1027       2.417  34.620  13.980  1.00 63.80           C  
ANISOU 2003  CA  PHE A1027     9016   8703   6521   -231  -1865  -2173       C  
ATOM   2004  C   PHE A1027       1.865  35.265  15.248  1.00 65.70           C  
ANISOU 2004  C   PHE A1027     9483   8900   6580    -40  -1795  -2569       C  
ATOM   2005  O   PHE A1027       1.047  36.183  15.182  1.00 68.83           O  
ANISOU 2005  O   PHE A1027     9956   9037   7158    146  -1814  -2855       O  
ATOM   2006  CB  PHE A1027       1.274  34.028  13.153  1.00 64.56           C  
ANISOU 2006  CB  PHE A1027     8960   8841   6729    -60  -1730  -2104       C  
ATOM   2007  CG  PHE A1027       1.696  33.539  11.796  1.00 65.80           C  
ANISOU 2007  CG  PHE A1027     8911   8998   7092   -252  -1792  -1738       C  
ATOM   2008  CD1 PHE A1027       2.833  34.042  11.186  1.00 69.13           C  
ANISOU 2008  CD1 PHE A1027     9266   9319   7680   -508  -1953  -1552       C  
ATOM   2009  CD2 PHE A1027       0.954  32.576  11.131  1.00 66.61           C  
ANISOU 2009  CD2 PHE A1027     8860   9251   7199   -176  -1648  -1573       C  
ATOM   2010  CE1 PHE A1027       3.224  33.593   9.936  1.00 69.17           C  
ANISOU 2010  CE1 PHE A1027     9052   9394   7836   -655  -1920  -1231       C  
ATOM   2011  CE2 PHE A1027       1.339  32.123   9.881  1.00 65.65           C  
ANISOU 2011  CE2 PHE A1027     8569   9127   7248   -361  -1671  -1240       C  
ATOM   2012  CZ  PHE A1027       2.475  32.632   9.283  1.00 65.68           C  
ANISOU 2012  CZ  PHE A1027     8504   9057   7393   -594  -1780  -1079       C  
ATOM   2013  N   GLY A1028       2.315  34.778  16.399  1.00 67.32           N  
ANISOU 2013  N   GLY A1028     9791   9345   6442    -91  -1707  -2573       N  
ATOM   2014  CA  GLY A1028       1.870  35.303  17.676  1.00 69.04           C  
ANISOU 2014  CA  GLY A1028    10225   9579   6428     54  -1608  -2920       C  
ATOM   2015  C   GLY A1028       0.531  34.736  18.106  1.00 66.96           C  
ANISOU 2015  C   GLY A1028     9917   9521   6006    359  -1285  -3018       C  
ATOM   2016  O   GLY A1028      -0.332  35.462  18.599  1.00 70.23           O  
ANISOU 2016  O   GLY A1028    10436   9838   6409    593  -1162  -3351       O  
ATOM   2017  N   MET A1029       0.356  33.432  17.917  1.00 64.40           N  
ANISOU 2017  N   MET A1029     9415   9477   5575    358  -1135  -2706       N  
ATOM   2018  CA  MET A1029      -0.886  32.765  18.287  1.00 61.29           C  
ANISOU 2018  CA  MET A1029     8920   9334   5032    604   -821  -2703       C  
ATOM   2019  C   MET A1029      -0.624  31.496  19.091  1.00 59.06           C  
ANISOU 2019  C   MET A1029     8592   9379   4470    513   -704  -2425       C  
ATOM   2020  O   MET A1029       0.421  30.861  18.947  1.00 54.42           O  
ANISOU 2020  O   MET A1029     7982   8804   3891    295   -850  -2162       O  
ATOM   2021  CB  MET A1029      -1.708  32.429  17.040  1.00 48.78           C  
ANISOU 2021  CB  MET A1029     7121   7728   3685    724   -752  -2570       C  
ATOM   2022  CG  MET A1029      -2.308  33.638  16.342  1.00 49.94           C  
ANISOU 2022  CG  MET A1029     7297   7537   4142    886   -834  -2863       C  
ATOM   2023  SD  MET A1029      -3.303  33.183  14.908  1.00 64.01           S  
ANISOU 2023  SD  MET A1029     8788   9228   6307    925   -710  -2507       S  
ATOM   2024  CE  MET A1029      -2.053  32.488  13.831  1.00 81.69           C  
ANISOU 2024  CE  MET A1029    10937  11458   8641    570   -963  -2139       C  
ATOM   2025  N   ASP A1030      -1.578  31.136  19.945  1.00 63.46           N  
ANISOU 2025  N   ASP A1030     9123  10177   4811    688   -445  -2471       N  
ATOM   2026  CA  ASP A1030      -1.504  29.883  20.686  1.00 64.55           C  
ANISOU 2026  CA  ASP A1030     9186  10608   4732    615   -345  -2185       C  
ATOM   2027  C   ASP A1030      -2.000  28.734  19.817  1.00 57.28           C  
ANISOU 2027  C   ASP A1030     8010   9787   3967    630   -255  -1831       C  
ATOM   2028  O   ASP A1030      -2.599  28.957  18.764  1.00 51.71           O  
ANISOU 2028  O   ASP A1030     7196   8983   3469    727   -222  -1834       O  
ATOM   2029  CB  ASP A1030      -2.315  29.968  21.979  1.00 75.66           C  
ANISOU 2029  CB  ASP A1030    10656  12250   5840    763   -119  -2350       C  
ATOM   2030  CG  ASP A1030      -1.672  30.873  23.011  1.00 89.15           C  
ANISOU 2030  CG  ASP A1030    12654  13892   7327    693   -219  -2661       C  
ATOM   2031  OD1 ASP A1030      -0.425  30.921  23.066  1.00 91.42           O  
ANISOU 2031  OD1 ASP A1030    13067  14065   7605    463   -472  -2599       O  
ATOM   2032  OD2 ASP A1030      -2.412  31.538  23.767  1.00 95.98           O  
ANISOU 2032  OD2 ASP A1030    13623  14816   8028    867    -44  -2961       O  
ATOM   2033  N   GLU A1031      -1.751  27.507  20.260  1.00 55.97           N  
ANISOU 2033  N   GLU A1031     7757   9798   3711    530   -233  -1529       N  
ATOM   2034  CA  GLU A1031      -2.081  26.334  19.460  1.00 52.07           C  
ANISOU 2034  CA  GLU A1031     7049   9346   3389    507   -187  -1184       C  
ATOM   2035  C   GLU A1031      -3.588  26.129  19.340  1.00 51.79           C  
ANISOU 2035  C   GLU A1031     6858   9475   3344    690     47  -1132       C  
ATOM   2036  O   GLU A1031      -4.325  26.243  20.318  1.00 57.78           O  
ANISOU 2036  O   GLU A1031     7617  10439   3897    809    214  -1221       O  
ATOM   2037  CB  GLU A1031      -1.427  25.082  20.047  1.00 57.94           C  
ANISOU 2037  CB  GLU A1031     7744  10196   4076    372   -241   -904       C  
ATOM   2038  CG  GLU A1031      -1.498  23.868  19.131  1.00 64.46           C  
ANISOU 2038  CG  GLU A1031     8388  10969   5134    321   -246   -579       C  
ATOM   2039  CD  GLU A1031      -0.638  22.717  19.611  1.00 72.35           C  
ANISOU 2039  CD  GLU A1031     9350  12003   6137    201   -337   -353       C  
ATOM   2040  OE1 GLU A1031      -0.093  21.988  18.755  1.00 73.75           O  
ANISOU 2040  OE1 GLU A1031     9454  12028   6541    136   -412   -179       O  
ATOM   2041  OE2 GLU A1031      -0.510  22.542  20.843  1.00 73.76           O  
ANISOU 2041  OE2 GLU A1031     9569  12368   6088    182   -329   -359       O  
ATOM   2042  N   GLY A1032      -4.031  25.827  18.124  1.00 51.15           N  
ANISOU 2042  N   GLY A1032     6642   9311   3483    704     56   -970       N  
ATOM   2043  CA  GLY A1032      -5.433  25.586  17.843  1.00 43.93           C  
ANISOU 2043  CA  GLY A1032     5559   8537   2594    855    256   -850       C  
ATOM   2044  C   GLY A1032      -5.603  25.037  16.441  1.00 44.90           C  
ANISOU 2044  C   GLY A1032     5563   8543   2955    781    201   -600       C  
ATOM   2045  O   GLY A1032      -4.658  25.037  15.651  1.00 45.65           O  
ANISOU 2045  O   GLY A1032     5712   8439   3193    640     21   -586       O  
ATOM   2046  N   VAL A1033      -6.806  24.564  16.130  1.00 40.45           N  
ANISOU 2046  N   VAL A1033     4830   8100   2438    859    354   -380       N  
ATOM   2047  CA  VAL A1033      -7.087  23.993  14.818  1.00 37.32           C  
ANISOU 2047  CA  VAL A1033     4329   7596   2254    761    304   -107       C  
ATOM   2048  C   VAL A1033      -6.935  25.050  13.730  1.00 40.02           C  
ANISOU 2048  C   VAL A1033     4715   7686   2805    765    222   -267       C  
ATOM   2049  O   VAL A1033      -7.710  26.005  13.662  1.00 37.74           O  
ANISOU 2049  O   VAL A1033     4384   7286   2669    913    324   -402       O  
ATOM   2050  CB  VAL A1033      -8.495  23.387  14.763  1.00 41.73           C  
ANISOU 2050  CB  VAL A1033     4693   8305   2859    822    471    191       C  
ATOM   2051  CG1 VAL A1033      -8.718  22.690  13.431  1.00 34.94           C  
ANISOU 2051  CG1 VAL A1033     3757   7281   2237    661    378    497       C  
ATOM   2052  CG2 VAL A1033      -8.685  22.416  15.914  1.00 43.99           C  
ANISOU 2052  CG2 VAL A1033     4923   8759   3034    792    502    336       C  
ATOM   2053  N   THR A1034      -5.931  24.867  12.880  1.00 31.03           N  
ANISOU 2053  N   THR A1034     3638   6353   1798    579     19   -228       N  
ATOM   2054  CA  THR A1034      -5.539  25.893  11.922  1.00 30.12           C  
ANISOU 2054  CA  THR A1034     3566   5913   1967    511   -120   -365       C  
ATOM   2055  C   THR A1034      -6.154  25.692  10.541  1.00 40.88           C  
ANISOU 2055  C   THR A1034     4810   7084   3637    397   -143   -112       C  
ATOM   2056  O   THR A1034      -6.087  24.607   9.962  1.00 37.34           O  
ANISOU 2056  O   THR A1034     4323   6672   3190    265   -174    136       O  
ATOM   2057  CB  THR A1034      -4.007  25.951  11.777  1.00 28.99           C  
ANISOU 2057  CB  THR A1034     3539   5704   1772    362   -332   -470       C  
ATOM   2058  OG1 THR A1034      -3.408  26.026  13.077  1.00 37.00           O  
ANISOU 2058  OG1 THR A1034     4663   6901   2494    425   -336   -658       O  
ATOM   2059  CG2 THR A1034      -3.592  27.165  10.960  1.00 28.79           C  
ANISOU 2059  CG2 THR A1034     3549   5376   2013    288   -490   -615       C  
ATOM   2060  N   PHE A1035      -6.754  26.759  10.026  1.00 30.63           N  
ANISOU 2060  N   PHE A1035     3464   5571   2604    445   -143   -180       N  
ATOM   2061  CA  PHE A1035      -7.321  26.779   8.686  1.00 33.46           C  
ANISOU 2061  CA  PHE A1035     3709   5739   3263    308   -198     57       C  
ATOM   2062  C   PHE A1035      -6.574  27.803   7.844  1.00 30.91           C  
ANISOU 2062  C   PHE A1035     3431   5149   3164    180   -399    -59       C  
ATOM   2063  O   PHE A1035      -6.285  28.901   8.314  1.00 33.35           O  
ANISOU 2063  O   PHE A1035     3810   5335   3527    277   -452   -321       O  
ATOM   2064  CB  PHE A1035      -8.813  27.113   8.730  1.00 30.83           C  
ANISOU 2064  CB  PHE A1035     3219   5398   3098    455    -37    173       C  
ATOM   2065  CG  PHE A1035      -9.626  26.150   9.545  1.00 36.50           C  
ANISOU 2065  CG  PHE A1035     3853   6413   3602    567    159    337       C  
ATOM   2066  CD1 PHE A1035      -9.750  26.310  10.916  1.00 42.61           C  
ANISOU 2066  CD1 PHE A1035     4655   7414   4121    790    322    136       C  
ATOM   2067  CD2 PHE A1035     -10.272  25.086   8.938  1.00 32.50           C  
ANISOU 2067  CD2 PHE A1035     3241   5972   3137    430    166    702       C  
ATOM   2068  CE1 PHE A1035     -10.497  25.424  11.668  1.00 44.23           C  
ANISOU 2068  CE1 PHE A1035     4755   7938   4113    872    498    328       C  
ATOM   2069  CE2 PHE A1035     -11.020  24.195   9.682  1.00 37.63           C  
ANISOU 2069  CE2 PHE A1035     3795   6898   3606    504    316    900       C  
ATOM   2070  CZ  PHE A1035     -11.134  24.364  11.050  1.00 41.94           C  
ANISOU 2070  CZ  PHE A1035     4339   7700   3896    725    487    729       C  
ATOM   2071  N   MET A1036      -6.259  27.450   6.604  1.00 29.35           N  
ANISOU 2071  N   MET A1036     3200   4866   3087    -48   -521    137       N  
ATOM   2072  CA  MET A1036      -5.507  28.355   5.747  1.00 31.82           C  
ANISOU 2072  CA  MET A1036     3526   4976   3588   -207   -722     84       C  
ATOM   2073  C   MET A1036      -6.222  28.622   4.430  1.00 35.40           C  
ANISOU 2073  C   MET A1036     3851   5274   4324   -369   -788    329       C  
ATOM   2074  O   MET A1036      -6.864  27.738   3.861  1.00 35.08           O  
ANISOU 2074  O   MET A1036     3750   5308   4271   -455   -727    568       O  
ATOM   2075  CB  MET A1036      -4.111  27.793   5.471  1.00 25.77           C  
ANISOU 2075  CB  MET A1036     2836   4302   2655   -359   -833     67       C  
ATOM   2076  CG  MET A1036      -3.142  28.810   4.893  1.00 31.39           C  
ANISOU 2076  CG  MET A1036     3556   4865   3504   -507  -1045    -11       C  
ATOM   2077  SD  MET A1036      -2.138  28.135   3.558  1.00 70.13           S  
ANISOU 2077  SD  MET A1036     8453   9784   8410   -708  -1065    152       S  
ATOM   2078  CE  MET A1036      -1.607  26.597   4.296  1.00 35.82           C  
ANISOU 2078  CE  MET A1036     4192   5614   3804   -589   -906    132       C  
ATOM   2079  N   PHE A1037      -6.112  29.858   3.959  1.00 34.88           N  
ANISOU 2079  N   PHE A1037     5368   4427   3459   -371   -446  -1575       N  
ATOM   2080  CA  PHE A1037      -6.579  30.223   2.632  1.00 34.34           C  
ANISOU 2080  CA  PHE A1037     5358   4259   3431   -362   -471  -1565       C  
ATOM   2081  C   PHE A1037      -5.442  30.886   1.873  1.00 37.17           C  
ANISOU 2081  C   PHE A1037     5703   4537   3882   -430   -561  -1590       C  
ATOM   2082  O   PHE A1037      -4.649  31.624   2.455  1.00 39.29           O  
ANISOU 2082  O   PHE A1037     6003   4755   4170   -482   -599  -1678       O  
ATOM   2083  CB  PHE A1037      -7.787  31.157   2.713  1.00 37.87           C  
ANISOU 2083  CB  PHE A1037     5949   4604   3836   -314   -395  -1658       C  
ATOM   2084  CG  PHE A1037      -8.129  31.823   1.409  1.00 43.61           C  
ANISOU 2084  CG  PHE A1037     6732   5241   4596   -375   -356  -1685       C  
ATOM   2085  CD1 PHE A1037      -8.875  31.159   0.450  1.00 43.87           C  
ANISOU 2085  CD1 PHE A1037     6662   5363   4644   -302   -366  -1676       C  
ATOM   2086  CD2 PHE A1037      -7.706  33.116   1.143  1.00 48.45           C  
ANISOU 2086  CD2 PHE A1037     7255   5812   5343   -410   -337  -1902       C  
ATOM   2087  CE1 PHE A1037      -9.190  31.772  -0.750  1.00 48.71           C  
ANISOU 2087  CE1 PHE A1037     7300   5913   5296   -245   -413  -1737       C  
ATOM   2088  CE2 PHE A1037      -8.016  33.732  -0.056  1.00 49.93           C  
ANISOU 2088  CE2 PHE A1037     7642   5797   5531   -328   -425  -1899       C  
ATOM   2089  CZ  PHE A1037      -8.760  33.061  -1.002  1.00 50.67           C  
ANISOU 2089  CZ  PHE A1037     7726   5946   5579   -234   -465  -1805       C  
ATOM   2090  N   ILE A1038      -5.355  30.617   0.576  1.00 39.97           N  
ANISOU 2090  N   ILE A1038     5996   4900   4291   -469   -561  -1544       N  
ATOM   2091  CA  ILE A1038      -4.343  31.256  -0.251  1.00 37.16           C  
ANISOU 2091  CA  ILE A1038     5639   4474   4007   -625   -544  -1557       C  
ATOM   2092  C   ILE A1038      -4.826  31.393  -1.693  1.00 30.72           C  
ANISOU 2092  C   ILE A1038     4879   3606   3185   -651   -514  -1527       C  
ATOM   2093  O   ILE A1038      -5.184  30.413  -2.348  1.00 29.18           O  
ANISOU 2093  O   ILE A1038     4594   3518   2977   -615   -512  -1437       O  
ATOM   2094  CB  ILE A1038      -3.002  30.487  -0.200  1.00 36.59           C  
ANISOU 2094  CB  ILE A1038     5436   4499   3968   -762   -510  -1450       C  
ATOM   2095  CG1 ILE A1038      -1.999  31.090  -1.187  1.00 30.66           C  
ANISOU 2095  CG1 ILE A1038     4730   3655   3263   -951   -462  -1431       C  
ATOM   2096  CG2 ILE A1038      -3.213  28.999  -0.451  1.00 36.79           C  
ANISOU 2096  CG2 ILE A1038     5312   4677   3990   -726   -467  -1319       C  
ATOM   2097  CD1 ILE A1038      -0.602  30.533  -1.050  1.00 34.03           C  
ANISOU 2097  CD1 ILE A1038     5024   4178   3728  -1075   -429  -1375       C  
ATOM   2098  N   GLY A1039      -4.849  32.632  -2.171  1.00 36.52           N  
ANISOU 2098  N   GLY A1039     5831   4136   3907   -724   -487  -1577       N  
ATOM   2099  CA  GLY A1039      -5.334  32.936  -3.503  1.00 40.91           C  
ANISOU 2099  CA  GLY A1039     6592   4561   4391   -738   -483  -1503       C  
ATOM   2100  C   GLY A1039      -5.586  34.421  -3.667  1.00 42.57           C  
ANISOU 2100  C   GLY A1039     7165   4443   4566   -723   -486  -1533       C  
ATOM   2101  O   GLY A1039      -5.688  35.152  -2.681  1.00 45.92           O  
ANISOU 2101  O   GLY A1039     7628   4783   5036   -678   -477  -1646       O  
ATOM   2102  N   ARG A1040      -5.678  34.867  -4.915  1.00 42.74           N  
ANISOU 2102  N   ARG A1040     7480   4258   4499   -742   -503  -1425       N  
ATOM   2103  CA  ARG A1040      -5.950  36.269  -5.210  1.00 46.81           C  
ANISOU 2103  CA  ARG A1040     8414   4396   4977   -674   -514  -1414       C  
ATOM   2104  C   ARG A1040      -7.315  36.679  -4.663  1.00 51.17           C  
ANISOU 2104  C   ARG A1040     9042   4880   5520   -350   -604  -1507       C  
ATOM   2105  O   ARG A1040      -8.254  35.884  -4.656  1.00 52.82           O  
ANISOU 2105  O   ARG A1040     9075   5298   5697   -158   -683  -1537       O  
ATOM   2106  CB  ARG A1040      -5.873  36.522  -6.718  1.00 47.30           C  
ANISOU 2106  CB  ARG A1040     8810   4250   4910   -707   -529  -1259       C  
ATOM   2107  CG  ARG A1040      -6.733  35.588  -7.550  1.00 44.93           C  
ANISOU 2107  CG  ARG A1040     8449   4132   4491   -533   -648  -1209       C  
ATOM   2108  CD  ARG A1040      -6.561  35.857  -9.036  1.00 47.71           C  
ANISOU 2108  CD  ARG A1040     9044   4357   4728   -547   -641  -1003       C  
ATOM   2109  NE  ARG A1040      -7.552  35.147  -9.841  1.00 51.14           N  
ANISOU 2109  NE  ARG A1040     9335   5021   5074   -299   -764   -925       N  
ATOM   2110  CZ  ARG A1040      -7.355  33.954 -10.394  1.00 51.49           C  
ANISOU 2110  CZ  ARG A1040     9129   5355   5080   -409   -761   -903       C  
ATOM   2111  NH1 ARG A1040      -6.198  33.327 -10.234  1.00 49.19           N  
ANISOU 2111  NH1 ARG A1040     8703   5155   4833   -740   -643   -938       N  
ATOM   2112  NH2 ARG A1040      -8.316  33.388 -11.111  1.00 53.46           N  
ANISOU 2112  NH2 ARG A1040     9253   5807   5254   -181   -879   -863       N  
ATOM   2113  N   PHE A1041      -7.417  37.918  -4.195  1.00 52.00           N  
ANISOU 2113  N   PHE A1041     9381   4706   5672   -286   -578  -1561       N  
ATOM   2114  CA  PHE A1041      -8.646  38.395  -3.571  1.00 60.63           C  
ANISOU 2114  CA  PHE A1041    10517   5734   6785     33   -642  -1662       C  
ATOM   2115  C   PHE A1041      -9.663  38.851  -4.613  1.00 69.51           C  
ANISOU 2115  C   PHE A1041    11949   6641   7821    364   -768  -1578       C  
ATOM   2116  O   PHE A1041      -9.534  39.929  -5.194  1.00 72.24           O  
ANISOU 2116  O   PHE A1041    12677   6623   8147    410   -754  -1485       O  
ATOM   2117  CB  PHE A1041      -8.340  39.529  -2.590  1.00 57.18           C  
ANISOU 2117  CB  PHE A1041    10174   5104   6449    -22   -556  -1770       C  
ATOM   2118  CG  PHE A1041      -7.574  39.088  -1.371  1.00 51.41           C  
ANISOU 2118  CG  PHE A1041     9113   4628   5793   -239   -481  -1901       C  
ATOM   2119  CD1 PHE A1041      -7.456  37.743  -1.057  1.00 47.98           C  
ANISOU 2119  CD1 PHE A1041     8326   4563   5340   -301   -487  -1910       C  
ATOM   2120  CD2 PHE A1041      -6.979  40.018  -0.535  1.00 52.21           C  
ANISOU 2120  CD2 PHE A1041     9260   4599   5980   -356   -412  -2019       C  
ATOM   2121  CE1 PHE A1041      -6.754  37.336   0.064  1.00 47.18           C  
ANISOU 2121  CE1 PHE A1041     7948   4687   5292   -438   -444  -2017       C  
ATOM   2122  CE2 PHE A1041      -6.277  39.615   0.589  1.00 51.21           C  
ANISOU 2122  CE2 PHE A1041     8838   4718   5902   -500   -388  -2152       C  
ATOM   2123  CZ  PHE A1041      -6.166  38.273   0.887  1.00 41.62           C  
ANISOU 2123  CZ  PHE A1041     7298   3862   4654   -521   -414  -2142       C  
ATOM   2124  N   ASP A1042     -10.678  38.022  -4.840  1.00 66.86           N  
ANISOU 2124  N   ASP A1042    11392   6564   7450    605   -877  -1593       N  
ATOM   2125  CA  ASP A1042     -11.675  38.289  -5.870  1.00 71.71           C  
ANISOU 2125  CA  ASP A1042    12099   7141   8008    939  -1002  -1462       C  
ATOM   2126  C   ASP A1042     -13.084  38.399  -5.299  1.00 73.02           C  
ANISOU 2126  C   ASP A1042    12106   7405   8235   1321  -1089  -1597       C  
ATOM   2127  O   ASP A1042     -13.408  37.775  -4.287  1.00 73.83           O  
ANISOU 2127  O   ASP A1042    11916   7734   8401   1308  -1050  -1770       O  
ATOM   2128  CB  ASP A1042     -11.640  37.195  -6.939  1.00 77.78           C  
ANISOU 2128  CB  ASP A1042    12675   8190   8688    878  -1056  -1336       C  
ATOM   2129  CG  ASP A1042     -10.282  37.062  -7.594  1.00 84.36           C  
ANISOU 2129  CG  ASP A1042    13652   8941   9461    514   -959  -1207       C  
ATOM   2130  OD1 ASP A1042      -9.577  38.086  -7.713  1.00 90.26           O  
ANISOU 2130  OD1 ASP A1042    14750   9342  10204    392   -881  -1145       O  
ATOM   2131  OD2 ASP A1042      -9.919  35.934  -7.988  1.00 82.89           O  
ANISOU 2131  OD2 ASP A1042    13225   9028   9242    344   -946  -1180       O  
ATOM   2132  N   ARG A1043     -13.919  39.194  -5.962  1.00 76.56           N  
ANISOU 2132  N   ARG A1043    12752   7682   8655   1670  -1201  -1514       N  
ATOM   2133  CA  ARG A1043     -15.320  39.326  -5.584  1.00 76.69           C  
ANISOU 2133  CA  ARG A1043    12598   7805   8735   2071  -1299  -1644       C  
ATOM   2134  C   ARG A1043     -16.182  38.274  -6.275  1.00 78.01           C  
ANISOU 2134  C   ARG A1043    12415   8362   8864   2232  -1425  -1638       C  
ATOM   2135  O   ARG A1043     -17.368  38.142  -5.972  1.00 85.30           O  
ANISOU 2135  O   ARG A1043    13097   9460   9854   2530  -1500  -1778       O  
ATOM   2136  CB  ARG A1043     -15.841  40.728  -5.920  1.00 77.35           C  
ANISOU 2136  CB  ARG A1043    13058   7514   8820   2414  -1372  -1575       C  
ATOM   2137  CG  ARG A1043     -15.649  41.758  -4.817  1.00 77.37           C  
ANISOU 2137  CG  ARG A1043    13277   7193   8927   2406  -1258  -1714       C  
ATOM   2138  CD  ARG A1043     -16.586  41.493  -3.649  1.00 75.84           C  
ANISOU 2138  CD  ARG A1043    12703   7264   8849   2536  -1230  -1928       C  
ATOM   2139  NE  ARG A1043     -16.548  42.568  -2.661  1.00 78.87           N  
ANISOU 2139  NE  ARG A1043    13203   7429   9334   2504  -1107  -2000       N  
ATOM   2140  CZ  ARG A1043     -17.288  42.594  -1.556  1.00 82.59           C  
ANISOU 2140  CZ  ARG A1043    13418   8058   9904   2591  -1045  -2173       C  
ATOM   2141  NH1 ARG A1043     -18.127  41.602  -1.295  1.00 83.43           N  
ANISOU 2141  NH1 ARG A1043    13132   8540  10029   2696  -1079  -2278       N  
ATOM   2142  NH2 ARG A1043     -17.189  43.612  -0.712  1.00 84.33           N  
ANISOU 2142  NH2 ARG A1043    13775   8059  10208   2554   -930  -2248       N  
ATOM   2143  N   GLY A1044     -15.587  37.524  -7.198  1.00 65.84           N  
ANISOU 2143  N   GLY A1044    10831   6962   7223   2024  -1439  -1498       N  
ATOM   2144  CA  GLY A1044     -16.340  36.534  -7.946  1.00 58.35           C  
ANISOU 2144  CA  GLY A1044     9566   6373   6231   2149  -1557  -1504       C  
ATOM   2145  C   GLY A1044     -15.549  35.386  -8.547  1.00 55.20           C  
ANISOU 2145  C   GLY A1044     9019   6190   5764   1818  -1506  -1428       C  
ATOM   2146  O   GLY A1044     -15.962  34.814  -9.555  1.00 57.03           O  
ANISOU 2146  O   GLY A1044     9126   6631   5910   1907  -1619  -1377       O  
ATOM   2147  N   GLN A1045     -14.420  35.035  -7.935  1.00 57.72           N  
ANISOU 2147  N   GLN A1045     9341   6471   6118   1448  -1345  -1437       N  
ATOM   2148  CA  GLN A1045     -13.627  33.904  -8.414  1.00 58.45           C  
ANISOU 2148  CA  GLN A1045     9275   6766   6167   1139  -1281  -1382       C  
ATOM   2149  C   GLN A1045     -13.100  33.027  -7.280  1.00 55.76           C  
ANISOU 2149  C   GLN A1045     8682   6579   5925    877  -1135  -1509       C  
ATOM   2150  O   GLN A1045     -13.600  31.924  -7.063  1.00 52.97           O  
ANISOU 2150  O   GLN A1045     7990   6516   5621    873  -1115  -1607       O  
ATOM   2151  CB  GLN A1045     -12.460  34.392  -9.276  1.00 64.27           C  
ANISOU 2151  CB  GLN A1045    10351   7273   6795    925  -1239  -1187       C  
ATOM   2152  CG  GLN A1045     -12.862  34.781 -10.695  1.00 71.83           C  
ANISOU 2152  CG  GLN A1045    11514   8181   7597   1130  -1374  -1020       C  
ATOM   2153  CD  GLN A1045     -11.670  34.960 -11.618  1.00 75.01           C  
ANISOU 2153  CD  GLN A1045    12200   8423   7878    863  -1291   -832       C  
ATOM   2154  OE1 GLN A1045     -10.548  35.185 -11.164  1.00 76.59           O  
ANISOU 2154  OE1 GLN A1045    12517   8454   8129    558  -1137   -825       O  
ATOM   2155  NE2 GLN A1045     -11.907  34.855 -12.922  1.00 75.83           N  
ANISOU 2155  NE2 GLN A1045    12403   8596   7813    975  -1389   -692       N  
ATOM   2156  N   LYS A1046     -12.090  33.511  -6.565  1.00 59.30           N  
ANISOU 2156  N   LYS A1046     9302   6832   6398    661  -1030  -1513       N  
ATOM   2157  CA  LYS A1046     -11.459  32.717  -5.513  1.00 54.49           C  
ANISOU 2157  CA  LYS A1046     8488   6368   5848    423   -911  -1614       C  
ATOM   2158  C   LYS A1046     -12.307  32.651  -4.246  1.00 51.44           C  
ANISOU 2158  C   LYS A1046     7907   6082   5554    570   -864  -1761       C  
ATOM   2159  O   LYS A1046     -12.071  31.811  -3.377  1.00 52.57           O  
ANISOU 2159  O   LYS A1046     7803   6409   5761    407   -730  -1768       O  
ATOM   2160  CB  LYS A1046     -10.071  33.271  -5.189  1.00 56.50           C  
ANISOU 2160  CB  LYS A1046     8932   6425   6109    135   -814  -1566       C  
ATOM   2161  CG  LYS A1046      -9.033  32.980  -6.262  1.00 51.88           C  
ANISOU 2161  CG  LYS A1046     8434   5819   5459   -106   -790  -1430       C  
ATOM   2162  CD  LYS A1046      -8.971  31.489  -6.569  1.00 41.84           C  
ANISOU 2162  CD  LYS A1046     6807   4882   4210   -204   -747  -1401       C  
ATOM   2163  CE  LYS A1046      -7.970  31.182  -7.671  1.00 38.43           C  
ANISOU 2163  CE  LYS A1046     6432   4446   3725   -424   -708  -1272       C  
ATOM   2164  NZ  LYS A1046      -7.979  29.739  -8.039  1.00 37.33           N  
ANISOU 2164  NZ  LYS A1046     5947   4609   3626   -478   -664  -1256       N  
ATOM   2165  N   GLY A1047     -13.289  33.541  -4.146  1.00 51.29           N  
ANISOU 2165  N   GLY A1047     8012   5933   5544    880   -953  -1846       N  
ATOM   2166  CA  GLY A1047     -14.239  33.521  -3.048  1.00 51.73           C  
ANISOU 2166  CA  GLY A1047     7870   6094   5691   1040   -898  -1981       C  
ATOM   2167  C   GLY A1047     -13.651  33.787  -1.675  1.00 47.84           C  
ANISOU 2167  C   GLY A1047     7383   5549   5247    856   -748  -2008       C  
ATOM   2168  O   GLY A1047     -14.050  33.162  -0.694  1.00 44.57           O  
ANISOU 2168  O   GLY A1047     6738   5318   4879    832   -641  -2061       O  
ATOM   2169  N   VAL A1048     -12.704  34.717  -1.601  1.00 50.29           N  
ANISOU 2169  N   VAL A1048     7965   5607   5536    721   -734  -1974       N  
ATOM   2170  CA  VAL A1048     -12.148  35.126  -0.316  1.00 50.20           C  
ANISOU 2170  CA  VAL A1048     7963   5554   5559    563   -612  -2035       C  
ATOM   2171  C   VAL A1048     -13.210  35.895   0.471  1.00 52.36           C  
ANISOU 2171  C   VAL A1048     8264   5748   5880    816   -605  -2160       C  
ATOM   2172  O   VAL A1048     -13.200  35.917   1.704  1.00 51.15           O  
ANISOU 2172  O   VAL A1048     8031   5661   5742    746   -496  -2237       O  
ATOM   2173  CB  VAL A1048     -10.873  35.988  -0.492  1.00 39.51           C  
ANISOU 2173  CB  VAL A1048     6850   3962   4200    344   -592  -1997       C  
ATOM   2174  CG1 VAL A1048     -11.186  37.261  -1.258  1.00 42.30           C  
ANISOU 2174  CG1 VAL A1048     7562   3962   4549    529   -680  -1972       C  
ATOM   2175  CG2 VAL A1048     -10.241  36.311   0.858  1.00 39.84           C  
ANISOU 2175  CG2 VAL A1048     6834   4028   4275    172   -478  -2100       C  
ATOM   2176  N   ASP A1049     -14.141  36.507  -0.256  1.00 52.47           N  
ANISOU 2176  N   ASP A1049     8397   5630   5909   1124   -723  -2177       N  
ATOM   2177  CA  ASP A1049     -15.243  37.240   0.356  1.00 59.58           C  
ANISOU 2177  CA  ASP A1049     9298   6466   6874   1401   -721  -2293       C  
ATOM   2178  C   ASP A1049     -16.170  36.291   1.114  1.00 60.21           C  
ANISOU 2178  C   ASP A1049     9021   6862   6993   1462   -646  -2376       C  
ATOM   2179  O   ASP A1049     -16.658  36.617   2.201  1.00 64.48           O  
ANISOU 2179  O   ASP A1049     9508   7416   7574   1512   -551  -2476       O  
ATOM   2180  CB  ASP A1049     -16.020  38.019  -0.710  1.00 61.41           C  
ANISOU 2180  CB  ASP A1049     9721   6505   7109   1751   -880  -2267       C  
ATOM   2181  CG  ASP A1049     -16.507  37.135  -1.845  1.00 59.66           C  
ANISOU 2181  CG  ASP A1049     9350   6478   6839   1886  -1009  -2225       C  
ATOM   2182  OD1 ASP A1049     -15.662  36.652  -2.629  1.00 56.26           O  
ANISOU 2182  OD1 ASP A1049     9000   6051   6326   1696  -1040  -2119       O  
ATOM   2183  OD2 ASP A1049     -17.735  36.931  -1.957  1.00 60.71           O  
ANISOU 2183  OD2 ASP A1049     9269   6778   7020   2172  -1075  -2309       O  
ATOM   2184  N   VAL A1050     -16.400  35.115   0.535  1.00 54.85           N  
ANISOU 2184  N   VAL A1050     8111   6427   6304   1439   -672  -2335       N  
ATOM   2185  CA  VAL A1050     -17.201  34.081   1.177  1.00 51.07           C  
ANISOU 2185  CA  VAL A1050     7297   6235   5872   1444   -574  -2392       C  
ATOM   2186  C   VAL A1050     -16.540  33.644   2.477  1.00 48.06           C  
ANISOU 2186  C   VAL A1050     6887   5915   5460   1188   -404  -2371       C  
ATOM   2187  O   VAL A1050     -17.211  33.433   3.489  1.00 50.09           O  
ANISOU 2187  O   VAL A1050     7015   6274   5742   1228   -294  -2442       O  
ATOM   2188  CB  VAL A1050     -17.390  32.854   0.263  1.00 38.86           C  
ANISOU 2188  CB  VAL A1050     5519   4917   4327   1408   -614  -2345       C  
ATOM   2189  CG1 VAL A1050     -18.310  31.835   0.921  1.00 38.40           C  
ANISOU 2189  CG1 VAL A1050     5127   5120   4343   1406   -492  -2409       C  
ATOM   2190  CG2 VAL A1050     -17.945  33.278  -1.082  1.00 44.13           C  
ANISOU 2190  CG2 VAL A1050     6244   5540   4984   1672   -809  -2366       C  
ATOM   2191  N   LEU A1051     -15.216  33.522   2.443  1.00 46.34           N  
ANISOU 2191  N   LEU A1051     6798   5635   5176    934   -389  -2273       N  
ATOM   2192  CA  LEU A1051     -14.450  33.139   3.623  1.00 44.44           C  
ANISOU 2192  CA  LEU A1051     6559   5449   4879    715   -265  -2243       C  
ATOM   2193  C   LEU A1051     -14.538  34.194   4.718  1.00 48.98           C  
ANISOU 2193  C   LEU A1051     7279   5891   5441    755   -209  -2355       C  
ATOM   2194  O   LEU A1051     -14.789  33.872   5.877  1.00 50.48           O  
ANISOU 2194  O   LEU A1051     7405   6181   5596    738   -105  -2391       O  
ATOM   2195  CB  LEU A1051     -12.984  32.898   3.265  1.00 39.89           C  
ANISOU 2195  CB  LEU A1051     6077   4836   4243    450   -280  -2126       C  
ATOM   2196  CG  LEU A1051     -12.103  32.633   4.488  1.00 40.85           C  
ANISOU 2196  CG  LEU A1051     6234   5000   4286    264   -197  -2098       C  
ATOM   2197  CD1 LEU A1051     -12.442  31.288   5.113  1.00 36.30           C  
ANISOU 2197  CD1 LEU A1051     5465   4635   3694    276   -125  -2034       C  
ATOM   2198  CD2 LEU A1051     -10.631  32.715   4.136  1.00 46.65           C  
ANISOU 2198  CD2 LEU A1051     7085   5667   4974     23   -229  -2014       C  
ATOM   2199  N   LEU A1052     -14.318  35.451   4.346  1.00 50.83           N  
ANISOU 2199  N   LEU A1052     7728   5886   5701    807   -274  -2407       N  
ATOM   2200  CA  LEU A1052     -14.376  36.554   5.299  1.00 45.28           C  
ANISOU 2200  CA  LEU A1052     7173   5027   5003    838   -216  -2531       C  
ATOM   2201  C   LEU A1052     -15.754  36.640   5.944  1.00 50.04           C  
ANISOU 2201  C   LEU A1052     7664   5700   5651   1077   -162  -2634       C  
ATOM   2202  O   LEU A1052     -15.875  36.799   7.164  1.00 47.75           O  
ANISOU 2202  O   LEU A1052     7382   5440   5322   1044    -52  -2715       O  
ATOM   2203  CB  LEU A1052     -14.027  37.875   4.610  1.00 54.59           C  
ANISOU 2203  CB  LEU A1052     8608   5899   6234    884   -292  -2558       C  
ATOM   2204  CG  LEU A1052     -12.578  38.012   4.139  1.00 54.51           C  
ANISOU 2204  CG  LEU A1052     8718   5795   6201    609   -310  -2491       C  
ATOM   2205  CD1 LEU A1052     -12.374  39.297   3.351  1.00 55.91           C  
ANISOU 2205  CD1 LEU A1052     9177   5627   6439    680   -378  -2490       C  
ATOM   2206  CD2 LEU A1052     -11.628  37.953   5.324  1.00 52.07           C  
ANISOU 2206  CD2 LEU A1052     8375   5573   5837    345   -204  -2558       C  
ATOM   2207  N   LYS A1053     -16.791  36.519   5.121  1.00 45.45           N  
ANISOU 2207  N   LYS A1053     6968   5158   5143   1317   -240  -2637       N  
ATOM   2208  CA  LYS A1053     -18.159  36.527   5.624  1.00 52.25           C  
ANISOU 2208  CA  LYS A1053     7666   6119   6067   1540   -188  -2742       C  
ATOM   2209  C   LYS A1053     -18.394  35.342   6.557  1.00 53.98           C  
ANISOU 2209  C   LYS A1053     7673   6591   6245   1416    -44  -2732       C  
ATOM   2210  O   LYS A1053     -19.113  35.456   7.551  1.00 58.48           O  
ANISOU 2210  O   LYS A1053     8187   7210   6823   1483     70  -2825       O  
ATOM   2211  CB  LYS A1053     -19.162  36.502   4.468  1.00 51.55           C  
ANISOU 2211  CB  LYS A1053     7454   6070   6061   1809   -321  -2748       C  
ATOM   2212  CG  LYS A1053     -20.600  36.760   4.893  1.00 56.09           C  
ANISOU 2212  CG  LYS A1053     7862   6723   6726   2059   -284  -2876       C  
ATOM   2213  CD  LYS A1053     -20.726  38.091   5.617  1.00 53.13           C  
ANISOU 2213  CD  LYS A1053     7695   6116   6376   2163   -238  -2973       C  
ATOM   2214  CE  LYS A1053     -22.160  38.356   6.040  1.00 67.31           C  
ANISOU 2214  CE  LYS A1053     9314   7993   8267   2409   -192  -3104       C  
ATOM   2215  NZ  LYS A1053     -23.084  38.389   4.874  1.00 67.92           N  
ANISOU 2215  NZ  LYS A1053     9252   8129   8425   2691   -361  -3105       N  
ATOM   2216  N   ALA A1054     -17.774  34.210   6.236  1.00 45.41           N  
ANISOU 2216  N   ALA A1054     6492   5646   5115   1238    -43  -2611       N  
ATOM   2217  CA  ALA A1054     -17.889  33.008   7.056  1.00 50.94           C  
ANISOU 2217  CA  ALA A1054     7033   6550   5773   1121     91  -2568       C  
ATOM   2218  C   ALA A1054     -17.237  33.203   8.421  1.00 53.51           C  
ANISOU 2218  C   ALA A1054     7511   6838   5982    993    191  -2579       C  
ATOM   2219  O   ALA A1054     -17.748  32.729   9.436  1.00 58.12           O  
ANISOU 2219  O   ALA A1054     8027   7528   6528   1001    321  -2608       O  
ATOM   2220  CB  ALA A1054     -17.271  31.818   6.340  1.00 41.42           C  
ANISOU 2220  CB  ALA A1054     5721   5464   4554    970     62  -2429       C  
ATOM   2221  N   ILE A1055     -16.103  33.897   8.440  1.00 47.84           N  
ANISOU 2221  N   ILE A1055     7002   5972   5202    868    131  -2563       N  
ATOM   2222  CA  ILE A1055     -15.419  34.205   9.690  1.00 50.79           C  
ANISOU 2222  CA  ILE A1055     7528   6314   5456    749    195  -2597       C  
ATOM   2223  C   ILE A1055     -16.266  35.166  10.515  1.00 56.03           C  
ANISOU 2223  C   ILE A1055     8259   6896   6135    894    273  -2760       C  
ATOM   2224  O   ILE A1055     -16.360  35.033  11.739  1.00 56.01           O  
ANISOU 2224  O   ILE A1055     8290   6956   6034    872    376  -2807       O  
ATOM   2225  CB  ILE A1055     -14.021  34.813   9.447  1.00 53.07           C  
ANISOU 2225  CB  ILE A1055     8003   6466   5695    563    112  -2569       C  
ATOM   2226  CG1 ILE A1055     -13.132  33.822   8.693  1.00 49.80           C  
ANISOU 2226  CG1 ILE A1055     7519   6139   5262    416     46  -2404       C  
ATOM   2227  CG2 ILE A1055     -13.365  35.206  10.765  1.00 55.67           C  
ANISOU 2227  CG2 ILE A1055     8480   6776   5895    456    158  -2635       C  
ATOM   2228  CD1 ILE A1055     -11.710  34.299   8.499  1.00 38.95           C  
ANISOU 2228  CD1 ILE A1055     6304   4658   3839    209    -22  -2372       C  
ATOM   2229  N   GLU A1056     -16.890  36.128   9.839  1.00 58.57           N  
ANISOU 2229  N   GLU A1056     8611   7069   6574   1059    220  -2845       N  
ATOM   2230  CA  GLU A1056     -17.820  37.035  10.506  1.00 60.66           C  
ANISOU 2230  CA  GLU A1056     8918   7248   6883   1233    294  -3002       C  
ATOM   2231  C   GLU A1056     -18.972  36.260  11.138  1.00 57.49           C  
ANISOU 2231  C   GLU A1056     8315   7041   6488   1338    416  -3030       C  
ATOM   2232  O   GLU A1056     -19.416  36.582  12.240  1.00 59.75           O  
ANISOU 2232  O   GLU A1056     8645   7329   6729   1377    538  -3134       O  
ATOM   2233  CB  GLU A1056     -18.363  38.078   9.529  1.00 68.14           C  
ANISOU 2233  CB  GLU A1056     9919   8002   7970   1443    194  -3060       C  
ATOM   2234  CG  GLU A1056     -17.434  39.256   9.294  1.00 72.25           C  
ANISOU 2234  CG  GLU A1056    10702   8251   8498   1364    138  -3094       C  
ATOM   2235  CD  GLU A1056     -18.113  40.387   8.548  1.00 77.35           C  
ANISOU 2235  CD  GLU A1056    11449   8664   9277   1623     60  -3152       C  
ATOM   2236  OE1 GLU A1056     -19.236  40.178   8.043  1.00 78.48           O  
ANISOU 2236  OE1 GLU A1056    11436   8886   9497   1870     12  -3150       O  
ATOM   2237  OE2 GLU A1056     -17.524  41.486   8.471  1.00 81.18           O  
ANISOU 2237  OE2 GLU A1056    12168   8884   9794   1584     46  -3199       O  
ATOM   2238  N   ILE A1057     -19.452  35.239  10.434  1.00 56.07           N  
ANISOU 2238  N   ILE A1057     7916   7021   6367   1368    395  -2946       N  
ATOM   2239  CA  ILE A1057     -20.492  34.366  10.968  1.00 54.22           C  
ANISOU 2239  CA  ILE A1057     7474   6975   6153   1420    530  -2965       C  
ATOM   2240  C   ILE A1057     -19.973  33.615  12.193  1.00 46.24           C  
ANISOU 2240  C   ILE A1057     6528   6055   4985   1258    664  -2911       C  
ATOM   2241  O   ILE A1057     -20.694  33.432  13.174  1.00 64.02           O  
ANISOU 2241  O   ILE A1057     8747   8375   7201   1304    819  -2974       O  
ATOM   2242  CB  ILE A1057     -20.983  33.357   9.906  1.00 52.32           C  
ANISOU 2242  CB  ILE A1057     6984   6886   6010   1441    480  -2891       C  
ATOM   2243  CG1 ILE A1057     -21.698  34.086   8.767  1.00 46.54           C  
ANISOU 2243  CG1 ILE A1057     6175   6092   5414   1657    336  -2963       C  
ATOM   2244  CG2 ILE A1057     -21.913  32.326  10.526  1.00 45.63           C  
ANISOU 2244  CG2 ILE A1057     5934   6223   5181   1429    649  -2901       C  
ATOM   2245  CD1 ILE A1057     -22.127  33.180   7.640  1.00 45.22           C  
ANISOU 2245  CD1 ILE A1057     5769   6082   5330   1678    257  -2913       C  
ATOM   2246  N   LEU A1058     -18.711  33.203  12.138  1.00 57.91           N  
ANISOU 2246  N   LEU A1058     8109   7531   6363   1083    601  -2793       N  
ATOM   2247  CA  LEU A1058     -18.108  32.434  13.223  1.00 57.61           C  
ANISOU 2247  CA  LEU A1058     8141   7583   6163    957    690  -2724       C  
ATOM   2248  C   LEU A1058     -17.612  33.306  14.375  1.00 59.61           C  
ANISOU 2248  C   LEU A1058     8619   7751   6279    926    717  -2820       C  
ATOM   2249  O   LEU A1058     -17.096  32.788  15.364  1.00 56.69           O  
ANISOU 2249  O   LEU A1058     8333   7457   5750    847    773  -2781       O  
ATOM   2250  CB  LEU A1058     -16.951  31.585  12.690  1.00 43.35           C  
ANISOU 2250  CB  LEU A1058     6332   5826   4313    801    597  -2562       C  
ATOM   2251  CG  LEU A1058     -17.328  30.392  11.812  1.00 41.43           C  
ANISOU 2251  CG  LEU A1058     5872   5701   4167    792    608  -2456       C  
ATOM   2252  CD1 LEU A1058     -16.080  29.673  11.333  1.00 39.03           C  
ANISOU 2252  CD1 LEU A1058     5588   5423   3818    642    517  -2308       C  
ATOM   2253  CD2 LEU A1058     -18.240  29.439  12.570  1.00 42.15           C  
ANISOU 2253  CD2 LEU A1058     5851   5919   4244    828    792  -2449       C  
ATOM   2254  N   SER A1059     -17.765  34.622  14.250  1.00 60.13           N  
ANISOU 2254  N   SER A1059     8787   7656   6403    996    675  -2951       N  
ATOM   2255  CA  SER A1059     -17.326  35.545  15.298  1.00 61.67           C  
ANISOU 2255  CA  SER A1059     9195   7755   6481    958    704  -3070       C  
ATOM   2256  C   SER A1059     -18.031  35.266  16.621  1.00 66.83           C  
ANISOU 2256  C   SER A1059     9860   8507   7024   1021    875  -3140       C  
ATOM   2257  O   SER A1059     -17.466  35.484  17.693  1.00 69.05           O  
ANISOU 2257  O   SER A1059    10306   8793   7137    951    904  -3191       O  
ATOM   2258  CB  SER A1059     -17.562  36.996  14.876  1.00 65.10           C  
ANISOU 2258  CB  SER A1059     9729   7974   7031   1045    662  -3211       C  
ATOM   2259  OG  SER A1059     -16.637  37.390  13.879  1.00 66.11           O  
ANISOU 2259  OG  SER A1059     9926   7979   7213    945    522  -3156       O  
ATOM   2260  N   SER A1060     -19.266  34.785  16.541  1.00 68.47           N  
ANISOU 2260  N   SER A1060     9894   8799   7322   1152    988  -3148       N  
ATOM   2261  CA  SER A1060     -19.985  34.338  17.725  1.00 69.23           C  
ANISOU 2261  CA  SER A1060     9990   9000   7316   1203   1179  -3191       C  
ATOM   2262  C   SER A1060     -19.583  32.904  18.054  1.00 71.09           C  
ANISOU 2262  C   SER A1060    10190   9389   7432   1104   1233  -3028       C  
ATOM   2263  O   SER A1060     -18.464  32.486  17.753  1.00 69.85           O  
ANISOU 2263  O   SER A1060    10079   9246   7215    978   1112  -2914       O  
ATOM   2264  CB  SER A1060     -21.497  34.439  17.516  1.00 69.53           C  
ANISOU 2264  CB  SER A1060     9844   9062   7512   1376   1292  -3279       C  
ATOM   2265  OG  SER A1060     -21.906  33.701  16.379  1.00 71.78           O  
ANISOU 2265  OG  SER A1060     9899   9423   7951   1392   1239  -3186       O  
ATOM   2266  N   LYS A1061     -20.499  32.164  18.676  1.00 73.34           N  
ANISOU 2266  N   LYS A1061    10399   9778   7687   1167   1422  -3020       N  
ATOM   2267  CA  LYS A1061     -20.297  30.753  19.019  1.00 70.40           C  
ANISOU 2267  CA  LYS A1061    10004   9531   7213   1102   1514  -2864       C  
ATOM   2268  C   LYS A1061     -19.158  30.526  20.017  1.00 75.50           C  
ANISOU 2268  C   LYS A1061    10878  10200   7608   1013   1498  -2812       C  
ATOM   2269  O   LYS A1061     -18.306  31.390  20.229  1.00 80.78           O  
ANISOU 2269  O   LYS A1061    11692  10799   8201    957   1369  -2881       O  
ATOM   2270  CB  LYS A1061     -20.046  29.925  17.753  1.00 59.04           C  
ANISOU 2270  CB  LYS A1061     8388   8130   5915   1036   1413  -2725       C  
ATOM   2271  CG  LYS A1061     -21.128  30.066  16.697  1.00 58.90           C  
ANISOU 2271  CG  LYS A1061     8129   8116   6134   1116   1403  -2779       C  
ATOM   2272  CD  LYS A1061     -20.721  29.410  15.389  1.00 59.69           C  
ANISOU 2272  CD  LYS A1061     8084   8244   6353   1039   1272  -2661       C  
ATOM   2273  CE  LYS A1061     -21.751  29.679  14.306  1.00 64.10           C  
ANISOU 2273  CE  LYS A1061     8413   8813   7130   1131   1226  -2739       C  
ATOM   2274  NZ  LYS A1061     -22.013  31.137  14.151  1.00 66.99           N  
ANISOU 2274  NZ  LYS A1061     8839   9063   7553   1257   1138  -2887       N  
ATOM   2275  N   LYS A1062     -19.156  29.347  20.630  1.00 73.45           N  
ANISOU 2275  N   LYS A1062    10648  10038   7220   1005   1633  -2693       N  
ATOM   2276  CA  LYS A1062     -18.151  28.991  21.624  1.00 67.28           C  
ANISOU 2276  CA  LYS A1062    10081   9298   6184    939   1631  -2639       C  
ATOM   2277  C   LYS A1062     -16.986  28.225  21.003  1.00 69.03           C  
ANISOU 2277  C   LYS A1062    10277   9550   6400    824   1482  -2483       C  
ATOM   2278  O   LYS A1062     -16.057  27.817  21.702  1.00 71.80           O  
ANISOU 2278  O   LYS A1062    10772   9953   6556    757   1455  -2426       O  
ATOM   2279  CB  LYS A1062     -18.788  28.159  22.738  1.00 64.93           C  
ANISOU 2279  CB  LYS A1062     9858   9083   5731   1015   1868  -2584       C  
ATOM   2280  CG  LYS A1062     -19.756  27.104  22.227  1.00 63.37           C  
ANISOU 2280  CG  LYS A1062     9468   8945   5666   1090   2016  -2479       C  
ATOM   2281  CD  LYS A1062     -20.257  26.215  23.349  1.00 65.27           C  
ANISOU 2281  CD  LYS A1062     9766   9289   5744   1177   2221  -2390       C  
ATOM   2282  CE  LYS A1062     -21.413  25.344  22.885  1.00 67.10           C  
ANISOU 2282  CE  LYS A1062     9757   9616   6122   1251   2378  -2343       C  
ATOM   2283  NZ  LYS A1062     -21.043  24.506  21.712  1.00 55.81           N  
ANISOU 2283  NZ  LYS A1062     8175   8186   4844   1169   2295  -2217       N  
ATOM   2284  N   GLU A1063     -17.036  28.041  19.688  1.00 64.80           N  
ANISOU 2284  N   GLU A1063     9551   8992   6078    801   1383  -2423       N  
ATOM   2285  CA  GLU A1063     -16.047  27.228  18.988  1.00 60.39           C  
ANISOU 2285  CA  GLU A1063     8940   8465   5540    707   1262  -2273       C  
ATOM   2286  C   GLU A1063     -15.002  28.055  18.243  1.00 55.02           C  
ANISOU 2286  C   GLU A1063     8261   7724   4918    619   1019  -2302       C  
ATOM   2287  O   GLU A1063     -14.055  27.505  17.683  1.00 58.81           O  
ANISOU 2287  O   GLU A1063     8705   8232   5410    539    902  -2191       O  
ATOM   2288  CB  GLU A1063     -16.742  26.286  18.002  1.00 63.14           C  
ANISOU 2288  CB  GLU A1063     9076   8841   6073    726   1330  -2174       C  
ATOM   2289  CG  GLU A1063     -17.461  25.108  18.643  1.00 66.28           C  
ANISOU 2289  CG  GLU A1063     9469   9309   6407    791   1564  -2085       C  
ATOM   2290  CD  GLU A1063     -18.909  25.408  18.979  1.00 70.93           C  
ANISOU 2290  CD  GLU A1063     9977   9910   7062    895   1734  -2190       C  
ATOM   2291  OE1 GLU A1063     -19.302  26.593  18.935  1.00 75.01           O  
ANISOU 2291  OE1 GLU A1063    10489  10372   7639    929   1681  -2344       O  
ATOM   2292  OE2 GLU A1063     -19.657  24.453  19.280  1.00 71.55           O  
ANISOU 2292  OE2 GLU A1063     9986  10061   7138    949   1920  -2123       O  
ATOM   2293  N   PHE A1064     -15.174  29.373  18.236  1.00 51.27           N  
ANISOU 2293  N   PHE A1064     7838   7159   4484    638    956  -2450       N  
ATOM   2294  CA  PHE A1064     -14.299  30.248  17.461  1.00 53.18           C  
ANISOU 2294  CA  PHE A1064     8098   7309   4798    560    754  -2479       C  
ATOM   2295  C   PHE A1064     -12.893  30.356  18.046  1.00 54.44           C  
ANISOU 2295  C   PHE A1064     8390   7497   4796    453    625  -2466       C  
ATOM   2296  O   PHE A1064     -11.922  30.545  17.313  1.00 52.76           O  
ANISOU 2296  O   PHE A1064     8161   7246   4640    362    465  -2421       O  
ATOM   2297  CB  PHE A1064     -14.915  31.643  17.344  1.00 57.17           C  
ANISOU 2297  CB  PHE A1064     8650   7684   5390    621    750  -2645       C  
ATOM   2298  CG  PHE A1064     -14.155  32.567  16.433  1.00 57.47           C  
ANISOU 2298  CG  PHE A1064     8727   7590   5520    545    579  -2670       C  
ATOM   2299  CD1 PHE A1064     -14.066  32.303  15.076  1.00 47.12           C  
ANISOU 2299  CD1 PHE A1064     7292   6250   4362    523    498  -2577       C  
ATOM   2300  CD2 PHE A1064     -13.537  33.703  16.932  1.00 60.60           C  
ANISOU 2300  CD2 PHE A1064     9297   7882   5845    489    514  -2793       C  
ATOM   2301  CE1 PHE A1064     -13.372  33.151  14.234  1.00 56.81           C  
ANISOU 2301  CE1 PHE A1064     8585   7340   5660    447    367  -2594       C  
ATOM   2302  CE2 PHE A1064     -12.840  34.557  16.095  1.00 59.77           C  
ANISOU 2302  CE2 PHE A1064     9253   7632   5826    404    386  -2815       C  
ATOM   2303  CZ  PHE A1064     -12.758  34.280  14.744  1.00 57.40           C  
ANISOU 2303  CZ  PHE A1064     8844   7297   5670    383    319  -2710       C  
ATOM   2304  N   GLN A1065     -12.784  30.236  19.365  1.00 53.93           N  
ANISOU 2304  N   GLN A1065     8455   7506   4529    464    696  -2511       N  
ATOM   2305  CA  GLN A1065     -11.494  30.386  20.029  1.00 55.19           C  
ANISOU 2305  CA  GLN A1065     8727   7721   4522    372    563  -2527       C  
ATOM   2306  C   GLN A1065     -10.653  29.118  19.932  1.00 53.51           C  
ANISOU 2306  C   GLN A1065     8455   7630   4246    327    512  -2362       C  
ATOM   2307  O   GLN A1065      -9.481  29.111  20.307  1.00 49.11           O  
ANISOU 2307  O   GLN A1065     7943   7140   3575    256    373  -2359       O  
ATOM   2308  CB  GLN A1065     -11.690  30.779  21.495  1.00 67.10           C  
ANISOU 2308  CB  GLN A1065    10402   9278   5815    402    649  -2655       C  
ATOM   2309  CG  GLN A1065     -12.454  32.082  21.696  1.00 77.61           C  
ANISOU 2309  CG  GLN A1065    11807  10482   7197    453    703  -2839       C  
ATOM   2310  CD  GLN A1065     -11.719  33.299  21.154  1.00 83.49           C  
ANISOU 2310  CD  GLN A1065    12597  11094   8032    372    530  -2937       C  
ATOM   2311  OE1 GLN A1065     -10.527  33.240  20.847  1.00 84.23           O  
ANISOU 2311  OE1 GLN A1065    12684  11207   8114    267    363  -2886       O  
ATOM   2312  NE2 GLN A1065     -12.432  34.413  21.038  1.00 84.53           N  
ANISOU 2312  NE2 GLN A1065    12781  11079   8257    424    581  -3081       N  
ATOM   2313  N   GLU A1066     -11.255  28.046  19.430  1.00 46.05           N  
ANISOU 2313  N   GLU A1066     7402   6714   3381    374    628  -2234       N  
ATOM   2314  CA  GLU A1066     -10.529  26.805  19.195  1.00 55.12           C  
ANISOU 2314  CA  GLU A1066     8491   7953   4498    340    599  -2075       C  
ATOM   2315  C   GLU A1066      -9.987  26.783  17.771  1.00 55.10           C  
ANISOU 2315  C   GLU A1066     8341   7899   4694    283    456  -2005       C  
ATOM   2316  O   GLU A1066      -9.410  25.788  17.330  1.00 55.78           O  
ANISOU 2316  O   GLU A1066     8350   8044   4801    258    427  -1878       O  
ATOM   2317  CB  GLU A1066     -11.429  25.591  19.435  1.00 53.21           C  
ANISOU 2317  CB  GLU A1066     8234   7752   4232    408    826  -1973       C  
ATOM   2318  CG  GLU A1066     -12.106  25.570  20.797  1.00 59.69           C  
ANISOU 2318  CG  GLU A1066     9212   8607   4860    457   1016  -2035       C  
ATOM   2319  CD  GLU A1066     -13.000  24.356  20.985  1.00 63.58           C  
ANISOU 2319  CD  GLU A1066     9684   9109   5365    512   1261  -1914       C  
ATOM   2320  OE1 GLU A1066     -14.130  24.519  21.491  1.00 68.34           O  
ANISOU 2320  OE1 GLU A1066    10311   9680   5974    593   1438  -1961       O  
ATOM   2321  OE2 GLU A1066     -12.569  23.237  20.632  1.00 61.24           O  
ANISOU 2321  OE2 GLU A1066     9339   8844   5085    481   1277  -1767       O  
ATOM   2322  N   MET A1067     -10.179  27.889  17.059  1.00 55.91           N  
ANISOU 2322  N   MET A1067     8422   7884   4937    263    380  -2092       N  
ATOM   2323  CA  MET A1067      -9.796  27.983  15.656  1.00 53.12           C  
ANISOU 2323  CA  MET A1067     7953   7463   4767    204    268  -2034       C  
ATOM   2324  C   MET A1067      -8.740  29.054  15.411  1.00 56.11           C  
ANISOU 2324  C   MET A1067     8402   7758   5159    107     93  -2099       C  
ATOM   2325  O   MET A1067      -8.711  30.083  16.086  1.00 61.13           O  
ANISOU 2325  O   MET A1067     9167   8337   5723     98     72  -2231       O  
ATOM   2326  CB  MET A1067     -11.023  28.277  14.790  1.00 49.63           C  
ANISOU 2326  CB  MET A1067     7423   6942   4493    264    346  -2062       C  
ATOM   2327  CG  MET A1067     -12.129  27.245  14.892  1.00 50.23           C  
ANISOU 2327  CG  MET A1067     7399   7092   4596    348    524  -2009       C  
ATOM   2328  SD  MET A1067     -13.602  27.764  13.992  1.00 46.13           S  
ANISOU 2328  SD  MET A1067     6750   6505   4273    431    590  -2087       S  
ATOM   2329  CE  MET A1067     -14.692  26.374  14.280  1.00 44.58           C  
ANISOU 2329  CE  MET A1067     6427   6414   4096    494    805  -2017       C  
ATOM   2330  N   ARG A1068      -7.873  28.793  14.440  1.00 49.17           N  
ANISOU 2330  N   ARG A1068     7441   6866   4376     28    -18  -2011       N  
ATOM   2331  CA  ARG A1068      -6.923  29.786  13.954  1.00 45.55           C  
ANISOU 2331  CA  ARG A1068     7038   6300   3969    -74   -165  -2060       C  
ATOM   2332  C   ARG A1068      -7.120  29.954  12.451  1.00 39.20           C  
ANISOU 2332  C   ARG A1068     6168   5385   3342   -104   -187  -2000       C  
ATOM   2333  O   ARG A1068      -7.368  28.980  11.746  1.00 35.20           O  
ANISOU 2333  O   ARG A1068     5526   4938   2911    -84   -146  -1889       O  
ATOM   2334  CB  ARG A1068      -5.481  29.377  14.268  1.00 49.01           C  
ANISOU 2334  CB  ARG A1068     7445   6834   4342   -150   -288  -2025       C  
ATOM   2335  CG  ARG A1068      -4.944  29.889  15.600  1.00 51.27           C  
ANISOU 2335  CG  ARG A1068     7844   7179   4455   -165   -341  -2145       C  
ATOM   2336  CD  ARG A1068      -5.654  29.254  16.784  1.00 51.77           C  
ANISOU 2336  CD  ARG A1068     7955   7366   4348    -65   -221  -2150       C  
ATOM   2337  NE  ARG A1068      -5.178  29.782  18.060  1.00 55.79           N  
ANISOU 2337  NE  ARG A1068     8582   7942   4673    -79   -274  -2276       N  
ATOM   2338  CZ  ARG A1068      -5.782  29.570  19.224  1.00 58.82           C  
ANISOU 2338  CZ  ARG A1068     9058   8412   4879     -4   -171  -2319       C  
ATOM   2339  NH1 ARG A1068      -6.891  28.846  19.274  1.00 58.57           N  
ANISOU 2339  NH1 ARG A1068     9013   8398   4844     86      4  -2247       N  
ATOM   2340  NH2 ARG A1068      -5.281  30.086  20.338  1.00 60.91           N  
ANISOU 2340  NH2 ARG A1068     9429   8746   4967    -24   -235  -2444       N  
ATOM   2341  N   PHE A1069      -7.020  31.185  11.962  1.00 36.27           N  
ANISOU 2341  N   PHE A1069     5907   4847   3027   -153   -244  -2079       N  
ATOM   2342  CA  PHE A1069      -7.228  31.444  10.541  1.00 35.00           C  
ANISOU 2342  CA  PHE A1069     5726   4569   3003   -178   -264  -2029       C  
ATOM   2343  C   PHE A1069      -6.054  32.188   9.918  1.00 35.37           C  
ANISOU 2343  C   PHE A1069     5852   4492   3097   -290   -402  -2037       C  
ATOM   2344  O   PHE A1069      -5.641  33.235  10.409  1.00 37.40           O  
ANISOU 2344  O   PHE A1069     6235   4649   3326   -328   -454  -2147       O  
ATOM   2345  CB  PHE A1069      -8.520  32.237  10.326  1.00 35.93           C  
ANISOU 2345  CB  PHE A1069     5910   4577   3164   -100   -170  -2123       C  
ATOM   2346  CG  PHE A1069      -9.764  31.477  10.685  1.00 39.98           C  
ANISOU 2346  CG  PHE A1069     6295   5212   3684     35    -45  -2120       C  
ATOM   2347  CD1 PHE A1069     -10.353  30.617   9.772  1.00 36.13           C  
ANISOU 2347  CD1 PHE A1069     5644   4791   3292     81    -12  -2032       C  
ATOM   2348  CD2 PHE A1069     -10.346  31.624  11.935  1.00 37.24           C  
ANISOU 2348  CD2 PHE A1069     5991   4912   3246    113     42  -2215       C  
ATOM   2349  CE1 PHE A1069     -11.498  29.916  10.098  1.00 33.70           C  
ANISOU 2349  CE1 PHE A1069     5211   4591   3004    197    106  -2041       C  
ATOM   2350  CE2 PHE A1069     -11.491  30.926  12.267  1.00 37.17           C  
ANISOU 2350  CE2 PHE A1069     5871   5005   3247    233    169  -2213       C  
ATOM   2351  CZ  PHE A1069     -12.068  30.070  11.347  1.00 55.42           C  
ANISOU 2351  CZ  PHE A1069     8012   7378   5669    272    201  -2127       C  
ATOM   2352  N   ILE A1070      -5.521  31.640   8.831  1.00 32.73           N  
ANISOU 2352  N   ILE A1070     5409   4169   2856   -335   -454  -1925       N  
ATOM   2353  CA  ILE A1070      -4.420  32.268   8.113  1.00 33.12           C  
ANISOU 2353  CA  ILE A1070     5473   4119   2993   -423   -575  -1938       C  
ATOM   2354  C   ILE A1070      -4.841  32.613   6.688  1.00 47.22           C  
ANISOU 2354  C   ILE A1070     7265   5782   4897   -408   -578  -1892       C  
ATOM   2355  O   ILE A1070      -4.909  31.741   5.819  1.00 51.03           O  
ANISOU 2355  O   ILE A1070     7633   6330   5425   -414   -560  -1785       O  
ATOM   2356  CB  ILE A1070      -3.175  31.361   8.080  1.00 39.32           C  
ANISOU 2356  CB  ILE A1070     6086   5051   3805   -504   -620  -1863       C  
ATOM   2357  CG1 ILE A1070      -2.796  30.926   9.496  1.00 41.78           C  
ANISOU 2357  CG1 ILE A1070     6379   5510   3988   -496   -619  -1900       C  
ATOM   2358  CG2 ILE A1070      -2.011  32.077   7.409  1.00 32.98           C  
ANISOU 2358  CG2 ILE A1070     5259   4162   3108   -622   -706  -1911       C  
ATOM   2359  CD1 ILE A1070      -1.578  30.028   9.559  1.00 44.63           C  
ANISOU 2359  CD1 ILE A1070     6580   6021   4358   -561   -660  -1840       C  
ATOM   2360  N   ILE A1071      -5.127  33.891   6.459  1.00 45.27           N  
ANISOU 2360  N   ILE A1071     7149   5354   4697   -374   -605  -1990       N  
ATOM   2361  CA  ILE A1071      -5.595  34.362   5.161  1.00 36.30           C  
ANISOU 2361  CA  ILE A1071     5991   4115   3688   -307   -628  -2007       C  
ATOM   2362  C   ILE A1071      -4.459  34.985   4.359  1.00 37.07           C  
ANISOU 2362  C   ILE A1071     5981   4166   3938   -457   -653  -2113       C  
ATOM   2363  O   ILE A1071      -3.930  36.029   4.730  1.00 39.25           O  
ANISOU 2363  O   ILE A1071     6334   4321   4258   -537   -663  -2255       O  
ATOM   2364  CB  ILE A1071      -6.725  35.396   5.316  1.00 38.17           C  
ANISOU 2364  CB  ILE A1071     6404   4185   3914   -175   -600  -2096       C  
ATOM   2365  CG1 ILE A1071      -7.803  34.863   6.261  1.00 38.26           C  
ANISOU 2365  CG1 ILE A1071     6438   4330   3771   -366   -246  -2105       C  
ATOM   2366  CG2 ILE A1071      -7.313  35.754   3.959  1.00 48.21           C  
ANISOU 2366  CG2 ILE A1071     7414   5539   5364   -395   -294  -2285       C  
ATOM   2367  CD1 ILE A1071      -8.896  35.860   6.564  1.00 40.27           C  
ANISOU 2367  CD1 ILE A1071     6702   4507   4094   -261   -140  -2329       C  
ATOM   2368  N   ILE A1072      -4.090  34.340   3.257  1.00 36.50           N  
ANISOU 2368  N   ILE A1072     5834   4132   3903   -545   -636  -2007       N  
ATOM   2369  CA  ILE A1072      -2.977  34.798   2.434  1.00 44.63           C  
ANISOU 2369  CA  ILE A1072     6886   5064   5009   -756   -603  -1990       C  
ATOM   2370  C   ILE A1072      -3.438  35.120   1.014  1.00 42.59           C  
ANISOU 2370  C   ILE A1072     6732   4672   4778   -806   -524  -1930       C  
ATOM   2371  O   ILE A1072      -4.251  34.398   0.439  1.00 44.18           O  
ANISOU 2371  O   ILE A1072     6881   4960   4944   -710   -518  -1860       O  
ATOM   2372  CB  ILE A1072      -1.851  33.744   2.381  1.00 35.69           C  
ANISOU 2372  CB  ILE A1072     5603   4088   3869   -860   -613  -1856       C  
ATOM   2373  CG1 ILE A1072      -1.492  33.281   3.794  1.00 35.72           C  
ANISOU 2373  CG1 ILE A1072     5560   4218   3794   -814   -672  -1878       C  
ATOM   2374  CG2 ILE A1072      -0.626  34.299   1.672  1.00 40.55           C  
ANISOU 2374  CG2 ILE A1072     6235   4613   4558  -1083   -561  -1849       C  
ATOM   2375  CD1 ILE A1072      -0.420  32.224   3.835  1.00 40.14           C  
ANISOU 2375  CD1 ILE A1072     5957   4941   4353   -902   -660  -1772       C  
ATOM   2376  N   GLY A1073      -2.922  36.211   0.457  1.00 41.12           N  
ANISOU 2376  N   GLY A1073     6741   4251   4633   -959   -468  -1941       N  
ATOM   2377  CA  GLY A1073      -3.255  36.602  -0.899  1.00 44.34           C  
ANISOU 2377  CA  GLY A1073     7373   4460   5013  -1007   -408  -1831       C  
ATOM   2378  C   GLY A1073      -3.168  38.100  -1.111  1.00 50.80           C  
ANISOU 2378  C   GLY A1073     8513   4929   5860  -1076   -351  -1870       C  
ATOM   2379  O   GLY A1073      -2.739  38.839  -0.224  1.00 53.79           O  
ANISOU 2379  O   GLY A1073     8894   5239   6302  -1124   -346  -2005       O  
ATOM   2380  N   LYS A1074      -3.577  38.546  -2.294  1.00 51.97           N  
ANISOU 2380  N   LYS A1074     8957   4839   5952  -1065   -318  -1746       N  
ATOM   2381  CA  LYS A1074      -3.561  39.963  -2.633  1.00 56.56           C  
ANISOU 2381  CA  LYS A1074     9906   5032   6552  -1096   -253  -1738       C  
ATOM   2382  C   LYS A1074      -4.477  40.230  -3.823  1.00 57.30           C  
ANISOU 2382  C   LYS A1074    10350   4885   6537   -929   -278  -1582       C  
ATOM   2383  O   LYS A1074      -4.545  39.426  -4.753  1.00 59.05           O  
ANISOU 2383  O   LYS A1074    10561   5210   6667   -935   -310  -1457       O  
ATOM   2384  CB  LYS A1074      -2.134  40.423  -2.942  1.00 59.89           C  
ANISOU 2384  CB  LYS A1074    10351   5370   7034  -1393   -148  -1718       C  
ATOM   2385  CG  LYS A1074      -1.887  41.903  -2.704  1.00 67.03           C  
ANISOU 2385  CG  LYS A1074    11518   5936   8015  -1461    -64  -1790       C  
ATOM   2386  CD  LYS A1074      -0.419  42.252  -2.891  1.00 68.56           C  
ANISOU 2386  CD  LYS A1074    11665   6105   8280  -1767     45  -1805       C  
ATOM   2387  CE  LYS A1074      -0.100  43.630  -2.333  1.00 73.21           C  
ANISOU 2387  CE  LYS A1074    12426   6416   8973  -1849    117  -1937       C  
ATOM   2388  NZ  LYS A1074      -0.911  44.698  -2.979  1.00 76.95           N  
ANISOU 2388  NZ  LYS A1074    13338   6478   9423  -1728    188  -1838       N  
ATOM   2389  N   GLY A1075      -5.182  41.357  -3.792  1.00 56.87           N  
ANISOU 2389  N   GLY A1075    10609   4509   6491   -751   -278  -1591       N  
ATOM   2390  CA  GLY A1075      -6.094  41.706  -4.867  1.00 58.21           C  
ANISOU 2390  CA  GLY A1075    11140   4425   6551   -506   -337  -1436       C  
ATOM   2391  C   GLY A1075      -6.803  43.031  -4.661  1.00 62.01           C  
ANISOU 2391  C   GLY A1075    11933   4552   7075   -273   -330  -1451       C  
ATOM   2392  O   GLY A1075      -6.171  44.087  -4.649  1.00 61.97           O  
ANISOU 2392  O   GLY A1075    12129   4279   7138   -422   -207  -1442       O  
ATOM   2393  N   ASP A1076      -8.122  42.973  -4.504  1.00 66.15           N  
ANISOU 2393  N   ASP A1076    12471   5091   7571    106   -457  -1479       N  
ATOM   2394  CA  ASP A1076      -8.931  44.172  -4.317  1.00 72.96           C  
ANISOU 2394  CA  ASP A1076    13592   5648   8482    392   -465  -1489       C  
ATOM   2395  C   ASP A1076      -8.610  44.866  -2.998  1.00 76.04           C  
ANISOU 2395  C   ASP A1076    13866   6005   9021    263   -361  -1692       C  
ATOM   2396  O   ASP A1076      -8.451  44.208  -1.970  1.00 78.71           O  
ANISOU 2396  O   ASP A1076    13855   6649   9403    155   -361  -1862       O  
ATOM   2397  CB  ASP A1076     -10.422  43.828  -4.375  1.00 73.90           C  
ANISOU 2397  CB  ASP A1076    13647   5876   8557    846   -635  -1505       C  
ATOM   2398  CG  ASP A1076     -10.876  43.425  -5.765  1.00 79.63           C  
ANISOU 2398  CG  ASP A1076    14553   6569   9135   1063   -767  -1312       C  
ATOM   2399  OD1 ASP A1076     -10.313  43.944  -6.751  1.00 82.01           O  
ANISOU 2399  OD1 ASP A1076    15195   6603   9362    969   -713  -1117       O  
ATOM   2400  OD2 ASP A1076     -11.798  42.590  -5.870  1.00 81.41           O  
ANISOU 2400  OD2 ASP A1076    14566   7051   9316   1329   -918  -1363       O  
ATOM   2401  N   PRO A1077      -8.510  46.203  -3.028  1.00 77.55           N  
ANISOU 2401  N   PRO A1077    14357   5824   9283    281   -271  -1673       N  
ATOM   2402  CA  PRO A1077      -8.233  47.011  -1.834  1.00 73.85           C  
ANISOU 2402  CA  PRO A1077    13821   5276   8961    173   -177  -1885       C  
ATOM   2403  C   PRO A1077      -9.319  46.862  -0.775  1.00 62.58           C  
ANISOU 2403  C   PRO A1077    12188   4015   7574    440   -245  -2063       C  
ATOM   2404  O   PRO A1077      -9.024  46.883   0.420  1.00 62.26           O  
ANISOU 2404  O   PRO A1077    11925   4118   7612    303   -197  -2279       O  
ATOM   2405  CB  PRO A1077      -8.198  48.444  -2.377  1.00 77.48           C  
ANISOU 2405  CB  PRO A1077    14701   5266   9471    228    -82  -1781       C  
ATOM   2406  CG  PRO A1077      -7.919  48.295  -3.839  1.00 78.30           C  
ANISOU 2406  CG  PRO A1077    15061   5245   9445    202    -78  -1508       C  
ATOM   2407  CD  PRO A1077      -8.605  47.031  -4.242  1.00 64.39           C  
ANISOU 2407  CD  PRO A1077    13125   3788   7554    397   -244  -1443       C  
ATOM   2408  N   GLU A1078     -10.562  46.713  -1.220  1.00 67.72           N  
ANISOU 2408  N   GLU A1078    12899   4664   8166    826   -357  -1979       N  
ATOM   2409  CA  GLU A1078     -11.695  46.554  -0.316  1.00 75.75           C  
ANISOU 2409  CA  GLU A1078    13703   5856   9223   1100   -408  -2138       C  
ATOM   2410  C   GLU A1078     -11.591  45.254   0.476  1.00 76.29           C  
ANISOU 2410  C   GLU A1078    13359   6373   9256    960   -422  -2264       C  
ATOM   2411  O   GLU A1078     -11.814  45.232   1.688  1.00 78.59           O  
ANISOU 2411  O   GLU A1078    13446   6815   9599    942   -366  -2456       O  
ATOM   2412  CB  GLU A1078     -13.010  46.589  -1.099  1.00 80.42           C  
ANISOU 2412  CB  GLU A1078    14393   6399   9762   1556   -547  -2016       C  
ATOM   2413  CG  GLU A1078     -14.257  46.481  -0.233  1.00 85.74           C  
ANISOU 2413  CG  GLU A1078    14823   7261  10494   1853   -586  -2181       C  
ATOM   2414  CD  GLU A1078     -15.532  46.425  -1.053  1.00 93.65           C  
ANISOU 2414  CD  GLU A1078    15840   8287  11454   2310   -749  -2077       C  
ATOM   2415  OE1 GLU A1078     -16.610  46.738  -0.503  1.00 97.58           O  
ANISOU 2415  OE1 GLU A1078    16212   8838  12026   2596   -767  -2191       O  
ATOM   2416  OE2 GLU A1078     -15.456  46.064  -2.247  1.00 95.67           O  
ANISOU 2416  OE2 GLU A1078    16219   8529  11604   2385   -859  -1891       O  
ATOM   2417  N   LEU A1079     -11.250  44.174  -0.219  1.00 78.38           N  
ANISOU 2417  N   LEU A1079    13511   6844   9425    858   -485  -2147       N  
ATOM   2418  CA  LEU A1079     -11.123  42.864   0.410  1.00 71.83           C  
ANISOU 2418  CA  LEU A1079    12299   6435   8557    727   -490  -2227       C  
ATOM   2419  C   LEU A1079      -9.927  42.816   1.356  1.00 70.65           C  
ANISOU 2419  C   LEU A1079    11993   6399   8452    368   -386  -2351       C  
ATOM   2420  O   LEU A1079      -9.977  42.167   2.402  1.00 72.98           O  
ANISOU 2420  O   LEU A1079    12005   6984   8739    312   -353  -2478       O  
ATOM   2421  CB  LEU A1079     -11.004  41.773  -0.655  1.00 67.43           C  
ANISOU 2421  CB  LEU A1079    11674   6045   7900    702   -577  -2073       C  
ATOM   2422  CG  LEU A1079     -12.250  41.574  -1.520  1.00 67.98           C  
ANISOU 2422  CG  LEU A1079    11800   6113   7916   1089   -719  -1994       C  
ATOM   2423  CD1 LEU A1079     -11.994  40.545  -2.608  1.00 65.10           C  
ANISOU 2423  CD1 LEU A1079    11387   5901   7447   1027   -801  -1865       C  
ATOM   2424  CD2 LEU A1079     -13.436  41.166  -0.658  1.00 65.42           C  
ANISOU 2424  CD2 LEU A1079    11183   6038   7635   1330   -738  -2138       C  
ATOM   2425  N   GLU A1080      -8.853  43.505   0.984  1.00 67.17           N  
ANISOU 2425  N   GLU A1080    11732   5737   8053    138   -334  -2313       N  
ATOM   2426  CA  GLU A1080      -7.676  43.591   1.839  1.00 55.82           C  
ANISOU 2426  CA  GLU A1080    10129   4403   6677   -161   -273  -2455       C  
ATOM   2427  C   GLU A1080      -7.996  44.385   3.097  1.00 59.33           C  
ANISOU 2427  C   GLU A1080    10553   4794   7198    -99   -226  -2679       C  
ATOM   2428  O   GLU A1080      -7.547  44.040   4.187  1.00 59.11           O  
ANISOU 2428  O   GLU A1080    10273   5011   7175   -216   -222  -2847       O  
ATOM   2429  CB  GLU A1080      -6.503  44.227   1.093  1.00 65.69           C  
ANISOU 2429  CB  GLU A1080    11572   5418   7970   -410   -221  -2368       C  
ATOM   2430  CG  GLU A1080      -5.970  43.389  -0.057  1.00 65.40           C  
ANISOU 2430  CG  GLU A1080    11521   5475   7854   -537   -240  -2169       C  
ATOM   2431  CD  GLU A1080      -4.678  43.937  -0.628  1.00 70.13           C  
ANISOU 2431  CD  GLU A1080    12244   5902   8498   -832   -151  -2107       C  
ATOM   2432  OE1 GLU A1080      -4.416  43.713  -1.829  1.00 71.60           O  
ANISOU 2432  OE1 GLU A1080    12576   6011   8616   -903   -126  -1916       O  
ATOM   2433  OE2 GLU A1080      -3.921  44.585   0.126  1.00 72.59           O  
ANISOU 2433  OE2 GLU A1080    12505   6166   8908   -994   -105  -2260       O  
ATOM   2434  N   GLY A1081      -8.773  45.451   2.938  1.00 63.31           N  
ANISOU 2434  N   GLY A1081    11326   4975   7755    108   -199  -2682       N  
ATOM   2435  CA  GLY A1081      -9.214  46.242   4.072  1.00 67.92           C  
ANISOU 2435  CA  GLY A1081    11905   5485   8416    194   -143  -2899       C  
ATOM   2436  C   GLY A1081     -10.083  45.423   5.006  1.00 68.47           C  
ANISOU 2436  C   GLY A1081    11708   5885   8421    332   -141  -3003       C  
ATOM   2437  O   GLY A1081      -9.939  45.492   6.227  1.00 73.88           O  
ANISOU 2437  O   GLY A1081    12240   6716   9116    248    -85  -3209       O  
ATOM   2438  N   TRP A1082     -10.985  44.643   4.418  1.00 60.57           N  
ANISOU 2438  N   TRP A1082    10658   5009   7346    544   -201  -2861       N  
ATOM   2439  CA  TRP A1082     -11.860  43.749   5.169  1.00 65.85           C  
ANISOU 2439  CA  TRP A1082    11077   5994   7948    669   -186  -2917       C  
ATOM   2440  C   TRP A1082     -11.047  42.743   5.986  1.00 64.83           C  
ANISOU 2440  C   TRP A1082    10684   6210   7738    395   -139  -2975       C  
ATOM   2441  O   TRP A1082     -11.228  42.612   7.204  1.00 65.06           O  
ANISOU 2441  O   TRP A1082    10601   6398   7722    355    -51  -3111       O  
ATOM   2442  CB  TRP A1082     -12.805  43.021   4.207  1.00 57.34           C  
ANISOU 2442  CB  TRP A1082     9958   5005   6825    923   -290  -2755       C  
ATOM   2443  CG  TRP A1082     -13.981  42.354   4.859  1.00 63.05           C  
ANISOU 2443  CG  TRP A1082    10452   5981   7521   1123   -272  -2815       C  
ATOM   2444  CD1 TRP A1082     -14.288  42.343   6.188  1.00 63.67           C  
ANISOU 2444  CD1 TRP A1082    10414   6192   7587   1095   -157  -2965       C  
ATOM   2445  CD2 TRP A1082     -15.013  41.604   4.203  1.00 62.06           C  
ANISOU 2445  CD2 TRP A1082    10184   6016   7381   1374   -363  -2731       C  
ATOM   2446  NE1 TRP A1082     -15.444  41.630   6.401  1.00 64.12           N  
ANISOU 2446  NE1 TRP A1082    10270   6464   7627   1301   -157  -2964       N  
ATOM   2447  CE2 TRP A1082     -15.908  41.167   5.198  1.00 61.36           C  
ANISOU 2447  CE2 TRP A1082     9873   6148   7291   1472   -285  -2837       C  
ATOM   2448  CE3 TRP A1082     -15.265  41.259   2.871  1.00 63.05           C  
ANISOU 2448  CE3 TRP A1082    10341   6125   7488   1521   -502  -2589       C  
ATOM   2449  CZ2 TRP A1082     -17.036  40.403   4.905  1.00 54.78           C  
ANISOU 2449  CZ2 TRP A1082     8814   5530   6471   1694   -333  -2817       C  
ATOM   2450  CZ3 TRP A1082     -16.385  40.500   2.582  1.00 54.11           C  
ANISOU 2450  CZ3 TRP A1082     8978   5223   6358   1759   -568  -2586       C  
ATOM   2451  CH2 TRP A1082     -17.256  40.081   3.594  1.00 54.12           C  
ANISOU 2451  CH2 TRP A1082     8724   5450   6388   1833   -479  -2704       C  
ATOM   2452  N   ALA A1083     -10.144  42.045   5.303  1.00 67.46           N  
ANISOU 2452  N   ALA A1083    10940   6650   8042    213   -193  -2857       N  
ATOM   2453  CA  ALA A1083      -9.307  41.027   5.930  1.00 66.52           C  
ANISOU 2453  CA  ALA A1083    10560   6862   7854    -16   -169  -2884       C  
ATOM   2454  C   ALA A1083      -8.426  41.609   7.033  1.00 68.66           C  
ANISOU 2454  C   ALA A1083    10759   7168   8161   -181   -144  -3092       C  
ATOM   2455  O   ALA A1083      -8.292  41.015   8.101  1.00 71.50           O  
ANISOU 2455  O   ALA A1083    10949   7799   8418   -260    -89  -3101       O  
ATOM   2456  CB  ALA A1083      -8.449  40.334   4.882  1.00 62.04           C  
ANISOU 2456  CB  ALA A1083     9922   6364   7286   -146   -249  -2730       C  
ATOM   2457  N   ARG A1084      -7.826  42.766   6.769  1.00 66.67           N  
ANISOU 2457  N   ARG A1084    10675   6631   8027   -221   -195  -3171       N  
ATOM   2458  CA  ARG A1084      -6.965  43.423   7.748  1.00 67.21           C  
ANISOU 2458  CA  ARG A1084    10694   6705   8139   -312   -258  -3356       C  
ATOM   2459  C   ARG A1084      -7.760  43.875   8.968  1.00 72.73           C  
ANISOU 2459  C   ARG A1084    11372   7449   8811   -223   -153  -3521       C  
ATOM   2460  O   ARG A1084      -7.287  43.768  10.102  1.00 73.52           O  
ANISOU 2460  O   ARG A1084    11310   7764   8860   -236   -234  -3629       O  
ATOM   2461  CB  ARG A1084      -6.244  44.618   7.120  1.00 64.92           C  
ANISOU 2461  CB  ARG A1084    10665   6032   7968   -416   -284  -3377       C  
ATOM   2462  CG  ARG A1084      -5.121  44.238   6.167  1.00 58.80           C  
ANISOU 2462  CG  ARG A1084     9898   5249   7193   -607   -338  -3199       C  
ATOM   2463  CD  ARG A1084      -3.964  43.586   6.906  1.00 65.01           C  
ANISOU 2463  CD  ARG A1084    10485   6304   7914   -719   -482  -3245       C  
ATOM   2464  NE  ARG A1084      -2.927  43.112   5.994  1.00 64.80           N  
ANISOU 2464  NE  ARG A1084    10428   6302   7891   -914   -489  -3071       N  
ATOM   2465  CZ  ARG A1084      -1.769  42.592   6.386  1.00 64.05           C  
ANISOU 2465  CZ  ARG A1084    10203   6387   7745  -1045   -583  -3057       C  
ATOM   2466  NH1 ARG A1084      -1.493  42.483   7.678  1.00 62.59           N  
ANISOU 2466  NH1 ARG A1084     9972   6348   7463   -998   -699  -3176       N  
ATOM   2467  NH2 ARG A1084      -0.883  42.184   5.487  1.00 62.02           N  
ANISOU 2467  NH2 ARG A1084     9894   6155   7514  -1225   -550  -2911       N  
ATOM   2468  N   SER A1085      -8.968  44.380   8.732  1.00 74.00           N  
ANISOU 2468  N   SER A1085    11733   7387   8998    -68    -29  -3535       N  
ATOM   2469  CA  SER A1085      -9.835  44.812   9.821  1.00 75.30           C  
ANISOU 2469  CA  SER A1085    11938   7550   9122     26     98  -3670       C  
ATOM   2470  C   SER A1085     -10.235  43.620  10.683  1.00 74.06           C  
ANISOU 2470  C   SER A1085    11674   7724   8740    -12    187  -3566       C  
ATOM   2471  O   SER A1085     -10.343  43.736  11.905  1.00 77.26           O  
ANISOU 2471  O   SER A1085    12142   8201   9013    -62    278  -3634       O  
ATOM   2472  CB  SER A1085     -11.079  45.520   9.282  1.00 75.18           C  
ANISOU 2472  CB  SER A1085    12145   7232   9190    310    134  -3648       C  
ATOM   2473  OG  SER A1085     -11.843  44.655   8.461  1.00 73.46           O  
ANISOU 2473  OG  SER A1085    11894   7106   8913    489     77  -3427       O  
ATOM   2474  N   LEU A1086     -10.448  42.473  10.044  1.00 72.70           N  
ANISOU 2474  N   LEU A1086    11426   7703   8493     24    144  -3374       N  
ATOM   2475  CA  LEU A1086     -10.733  41.249  10.789  1.00 71.51           C  
ANISOU 2475  CA  LEU A1086    11224   7812   8133     23    171  -3241       C  
ATOM   2476  C   LEU A1086      -9.505  40.781  11.569  1.00 70.86           C  
ANISOU 2476  C   LEU A1086    11185   7870   7867   -208    133  -3140       C  
ATOM   2477  O   LEU A1086      -9.627  40.245  12.670  1.00 66.01           O  
ANISOU 2477  O   LEU A1086    10631   7381   7071   -148    105  -3109       O  
ATOM   2478  CB  LEU A1086     -11.219  40.143   9.853  1.00 69.30           C  
ANISOU 2478  CB  LEU A1086    10826   7648   7855    129    114  -3079       C  
ATOM   2479  CG  LEU A1086     -12.705  40.181   9.490  1.00 71.28           C  
ANISOU 2479  CG  LEU A1086    11031   7861   8192    451    103  -3067       C  
ATOM   2480  CD1 LEU A1086     -13.074  38.990   8.622  1.00 69.50           C  
ANISOU 2480  CD1 LEU A1086    10638   7804   7966    530     32  -2892       C  
ATOM   2481  CD2 LEU A1086     -13.562  40.216  10.747  1.00 74.16           C  
ANISOU 2481  CD2 LEU A1086    11387   8302   8490    573    200  -3167       C  
ATOM   2482  N   GLU A1087      -8.325  40.988  10.991  1.00 68.97           N  
ANISOU 2482  N   GLU A1087    10911   7607   7687   -423    101  -3105       N  
ATOM   2483  CA  GLU A1087      -7.072  40.640  11.653  1.00 71.55           C  
ANISOU 2483  CA  GLU A1087    11564   7875   7747   -338   -268  -2896       C  
ATOM   2484  C   GLU A1087      -6.888  41.471  12.915  1.00 74.88           C  
ANISOU 2484  C   GLU A1087    12117   8240   8095   -268   -351  -3085       C  
ATOM   2485  O   GLU A1087      -6.428  40.972  13.942  1.00 76.90           O  
ANISOU 2485  O   GLU A1087    12299   8688   8231   -290   -405  -3134       O  
ATOM   2486  CB  GLU A1087      -5.884  40.850  10.711  1.00 73.58           C  
ANISOU 2486  CB  GLU A1087    11486   8164   8306   -125   -705  -3015       C  
ATOM   2487  CG  GLU A1087      -4.534  40.539  11.341  1.00 75.25           C  
ANISOU 2487  CG  GLU A1087    11704   8475   8411   -337   -755  -3015       C  
ATOM   2488  CD  GLU A1087      -3.369  41.021  10.499  1.00 74.92           C  
ANISOU 2488  CD  GLU A1087    11534   8361   8571   -503   -817  -3112       C  
ATOM   2489  OE1 GLU A1087      -3.534  42.025   9.776  1.00 76.90           O  
ANISOU 2489  OE1 GLU A1087    11786   8407   9024   -529   -765  -3246       O  
ATOM   2490  OE2 GLU A1087      -2.289  40.396  10.561  1.00 71.05           O  
ANISOU 2490  OE2 GLU A1087    10972   7995   8027   -657   -867  -3049       O  
ATOM   2491  N   GLU A1088      -7.251  42.746  12.825  1.00 77.74           N  
ANISOU 2491  N   GLU A1088    12678   8335   8525   -214   -320  -3199       N  
ATOM   2492  CA  GLU A1088      -7.160  43.657  13.958  1.00 76.32           C  
ANISOU 2492  CA  GLU A1088    12610   8086   8304   -131   -400  -3418       C  
ATOM   2493  C   GLU A1088      -8.231  43.339  14.997  1.00 74.30           C  
ANISOU 2493  C   GLU A1088    12338   7971   7923   -224    -42  -3485       C  
ATOM   2494  O   GLU A1088      -8.009  43.486  16.199  1.00 75.27           O  
ANISOU 2494  O   GLU A1088    12519   8167   7912   -178   -119  -3610       O  
ATOM   2495  CB  GLU A1088      -7.292  45.106  13.484  1.00 78.91           C  
ANISOU 2495  CB  GLU A1088    12541   8324   9116    173   -659  -3838       C  
ATOM   2496  CG  GLU A1088      -7.181  46.145  14.586  1.00 84.89           C  
ANISOU 2496  CG  GLU A1088    13656   8879   9720    145   -646  -3972       C  
ATOM   2497  CD  GLU A1088      -7.436  47.550  14.081  1.00 90.11           C  
ANISOU 2497  CD  GLU A1088    13984   9387  10866    131   -542  -4371       C  
ATOM   2498  OE1 GLU A1088      -7.796  47.696  12.894  1.00 90.19           O  
ANISOU 2498  OE1 GLU A1088    13849   9283  11135    -12   -279  -4375       O  
ATOM   2499  OE2 GLU A1088      -7.277  48.505  14.871  1.00 93.12           O  
ANISOU 2499  OE2 GLU A1088    14636   9574  11170    153   -596  -4513       O  
ATOM   2500  N   LYS A1089      -9.391  42.893  14.523  1.00 73.54           N  
ANISOU 2500  N   LYS A1089    12019   7968   7955   -197    190  -3493       N  
ATOM   2501  CA  LYS A1089     -10.513  42.582  15.403  1.00 73.51           C  
ANISOU 2501  CA  LYS A1089    11959   8082   7889    -16    278  -3577       C  
ATOM   2502  C   LYS A1089     -10.267  41.319  16.226  1.00 71.10           C  
ANISOU 2502  C   LYS A1089    11575   8055   7384      9    194  -3475       C  
ATOM   2503  O   LYS A1089     -10.440  41.321  17.446  1.00 70.89           O  
ANISOU 2503  O   LYS A1089    11607   8116   7213     62    217  -3573       O  
ATOM   2504  CB  LYS A1089     -11.799  42.426  14.588  1.00 73.47           C  
ANISOU 2504  CB  LYS A1089    11796   8056   8063    168    375  -3591       C  
ATOM   2505  CG  LYS A1089     -13.028  42.103  15.422  1.00 74.99           C  
ANISOU 2505  CG  LYS A1089    11954   8347   8190    378    468  -3658       C  
ATOM   2506  CD  LYS A1089     -14.040  43.235  15.374  1.00 78.94           C  
ANISOU 2506  CD  LYS A1089    12521   8628   8847    556    576  -3840       C  
ATOM   2507  CE  LYS A1089     -14.525  43.481  13.954  1.00 77.13           C  
ANISOU 2507  CE  LYS A1089    12206   8256   8843    697    527  -3790       C  
ATOM   2508  NZ  LYS A1089     -15.527  44.581  13.890  1.00 79.16           N  
ANISOU 2508  NZ  LYS A1089    12528   8286   9264    932    588  -3931       N  
ATOM   2509  N   HIS A1090      -9.864  40.245  15.556  1.00 70.52           N  
ANISOU 2509  N   HIS A1090    11358   8121   7315    -32    116  -3292       N  
ATOM   2510  CA  HIS A1090      -9.681  38.957  16.217  1.00 68.19           C  
ANISOU 2510  CA  HIS A1090    10951   8085   6873     -7     74  -3195       C  
ATOM   2511  C   HIS A1090      -8.207  38.598  16.378  1.00 69.56           C  
ANISOU 2511  C   HIS A1090    11127   8343   6962   -133   -106  -3127       C  
ATOM   2512  O   HIS A1090      -7.410  38.767  15.456  1.00 72.27           O  
ANISOU 2512  O   HIS A1090    11465   8596   7398   -220   -217  -3051       O  
ATOM   2513  CB  HIS A1090     -10.403  37.855  15.439  1.00 65.96           C  
ANISOU 2513  CB  HIS A1090    10485   7915   6662     74    128  -3054       C  
ATOM   2514  CG  HIS A1090     -11.874  38.092  15.283  1.00 68.81           C  
ANISOU 2514  CG  HIS A1090    10797   8226   7121    245    270  -3133       C  
ATOM   2515  ND1 HIS A1090     -12.770  37.906  16.313  1.00 67.47           N  
ANISOU 2515  ND1 HIS A1090    10605   8151   6879    376    381  -3205       N  
ATOM   2516  CD2 HIS A1090     -12.604  38.497  14.217  1.00 68.86           C  
ANISOU 2516  CD2 HIS A1090    10743   8111   7311    336    299  -3144       C  
ATOM   2517  CE1 HIS A1090     -13.989  38.189  15.889  1.00 68.86           C  
ANISOU 2517  CE1 HIS A1090    10703   8266   7196    540    467  -3255       C  
ATOM   2518  NE2 HIS A1090     -13.916  38.550  14.621  1.00 69.84           N  
ANISOU 2518  NE2 HIS A1090    10798   8262   7477    535    404  -3219       N  
ATOM   2519  N   GLY A1091      -7.855  38.091  17.555  1.00 67.26           N  
ANISOU 2519  N   GLY A1091    10830   8230   6494   -129   -134  -3165       N  
ATOM   2520  CA  GLY A1091      -6.484  37.720  17.848  1.00 62.62           C  
ANISOU 2520  CA  GLY A1091    10212   7757   5824   -232   -300  -3141       C  
ATOM   2521  C   GLY A1091      -6.101  36.359  17.302  1.00 54.59           C  
ANISOU 2521  C   GLY A1091     9020   6902   4818   -244   -339  -2948       C  
ATOM   2522  O   GLY A1091      -4.962  35.918  17.459  1.00 58.03           O  
ANISOU 2522  O   GLY A1091     9396   7449   5202   -321   -467  -2920       O  
ATOM   2523  N   ASN A1092      -7.051  35.689  16.658  1.00 51.81           N  
ANISOU 2523  N   ASN A1092     8577   6566   4542   -164   -228  -2830       N  
ATOM   2524  CA  ASN A1092      -6.799  34.370  16.089  1.00 48.61           C  
ANISOU 2524  CA  ASN A1092     8001   6300   4168   -162   -249  -2645       C  
ATOM   2525  C   ASN A1092      -6.896  34.368  14.565  1.00 52.05           C  
ANISOU 2525  C   ASN A1092     8377   6619   4782   -187   -268  -2542       C  
ATOM   2526  O   ASN A1092      -7.101  33.321  13.951  1.00 50.52           O  
ANISOU 2526  O   ASN A1092     8034   6516   4643   -157   -241  -2398       O  
ATOM   2527  CB  ASN A1092      -7.769  33.343  16.680  1.00 48.01           C  
ANISOU 2527  CB  ASN A1092     7843   6378   4020    -43   -108  -2585       C  
ATOM   2528  CG  ASN A1092      -9.223  33.682  16.401  1.00 50.28           C  
ANISOU 2528  CG  ASN A1092     8130   6580   4396     64     39  -2630       C  
ATOM   2529  OD1 ASN A1092      -9.557  34.821  16.077  1.00 51.38           O  
ANISOU 2529  OD1 ASN A1092     8363   6547   4611     63     51  -2741       O  
ATOM   2530  ND2 ASN A1092     -10.096  32.690  16.535  1.00 47.12           N  
ANISOU 2530  ND2 ASN A1092     7619   6294   3992    164    159  -2553       N  
ATOM   2531  N   VAL A1093      -6.752  35.544  13.962  1.00 47.59           N  
ANISOU 2531  N   VAL A1093     7911   5854   4317   -237   -306  -2607       N  
ATOM   2532  CA  VAL A1093      -6.764  35.672  12.508  1.00 42.91           C  
ANISOU 2532  CA  VAL A1093     7285   5138   3879   -267   -328  -2511       C  
ATOM   2533  C   VAL A1093      -5.559  36.477  12.025  1.00 55.49           C  
ANISOU 2533  C   VAL A1093     8940   6596   5546   -357   -487  -2539       C  
ATOM   2534  O   VAL A1093      -5.351  37.614  12.447  1.00 60.70           O  
ANISOU 2534  O   VAL A1093     9740   7118   6207   -371   -524  -2682       O  
ATOM   2535  CB  VAL A1093      -8.059  36.341  12.003  1.00 43.44           C  
ANISOU 2535  CB  VAL A1093     7403   5070   4033   -202   -184  -2573       C  
ATOM   2536  CG1 VAL A1093      -7.982  36.583  10.503  1.00 42.37           C  
ANISOU 2536  CG1 VAL A1093     7255   4808   4035   -260   -194  -2494       C  
ATOM   2537  CG2 VAL A1093      -9.269  35.487  12.344  1.00 42.53           C  
ANISOU 2537  CG2 VAL A1093     7172   5097   3889    -63    -65  -2570       C  
ATOM   2538  N   LYS A1094      -4.770  35.875  11.141  1.00 56.82           N  
ANISOU 2538  N   LYS A1094     8979   6812   5797   -404   -582  -2428       N  
ATOM   2539  CA  LYS A1094      -3.571  36.505  10.602  1.00 55.02           C  
ANISOU 2539  CA  LYS A1094     8720   6499   5686   -489   -722  -2492       C  
ATOM   2540  C   LYS A1094      -3.665  36.661   9.085  1.00 52.95           C  
ANISOU 2540  C   LYS A1094     8386   6130   5603   -470   -744  -2435       C  
ATOM   2541  O   LYS A1094      -3.903  35.691   8.367  1.00 49.11           O  
ANISOU 2541  O   LYS A1094     7797   5731   5131   -453   -711  -2285       O  
ATOM   2542  CB  LYS A1094      -2.332  35.687  10.974  1.00 53.96           C  
ANISOU 2542  CB  LYS A1094     8449   6549   5505   -598   -794  -2467       C  
ATOM   2543  CG  LYS A1094      -1.065  36.101  10.247  1.00 55.92           C  
ANISOU 2543  CG  LYS A1094     8618   6741   5888   -742   -885  -2520       C  
ATOM   2544  CD  LYS A1094      -0.653  37.519  10.599  1.00 61.24           C  
ANISOU 2544  CD  LYS A1094     9408   7251   6609   -819   -932  -2728       C  
ATOM   2545  CE  LYS A1094       0.632  37.907   9.887  1.00 60.10           C  
ANISOU 2545  CE  LYS A1094     9156   7064   6614  -1017   -957  -2769       C  
ATOM   2546  NZ  LYS A1094       1.011  39.320  10.160  1.00 63.34           N  
ANISOU 2546  NZ  LYS A1094     9682   7289   7095  -1124   -972  -2979       N  
ATOM   2547  N   VAL A1095      -3.475  37.886   8.604  1.00 54.40           N  
ANISOU 2547  N   VAL A1095     8594   6137   5938   -488   -779  -2592       N  
ATOM   2548  CA  VAL A1095      -3.559  38.170   7.174  1.00 46.82           C  
ANISOU 2548  CA  VAL A1095     7539   5084   5165   -525   -736  -2604       C  
ATOM   2549  C   VAL A1095      -2.191  38.521   6.591  1.00 56.08           C  
ANISOU 2549  C   VAL A1095     8713   6170   6425   -763   -754  -2636       C  
ATOM   2550  O   VAL A1095      -1.486  39.384   7.113  1.00 62.76           O  
ANISOU 2550  O   VAL A1095     9639   6912   7294   -876   -779  -2770       O  
ATOM   2551  CB  VAL A1095      -4.545  39.319   6.891  1.00 48.73           C  
ANISOU 2551  CB  VAL A1095     7826   5153   5536   -461   -629  -2777       C  
ATOM   2552  CG1 VAL A1095      -4.503  39.713   5.423  1.00 58.89           C  
ANISOU 2552  CG1 VAL A1095     9208   6234   6933   -590   -535  -2747       C  
ATOM   2553  CG2 VAL A1095      -5.952  38.916   7.301  1.00 48.48           C  
ANISOU 2553  CG2 VAL A1095     7651   5286   5485   -292   -519  -2806       C  
ATOM   2554  N   ILE A1096      -1.827  37.844   5.506  1.00 50.77           N  
ANISOU 2554  N   ILE A1096     7945   5548   5797   -851   -715  -2486       N  
ATOM   2555  CA  ILE A1096      -0.534  38.037   4.863  1.00 51.89           C  
ANISOU 2555  CA  ILE A1096     8060   5642   6014  -1087   -679  -2443       C  
ATOM   2556  C   ILE A1096      -0.680  38.494   3.413  1.00 54.96           C  
ANISOU 2556  C   ILE A1096     8552   5841   6491  -1188   -562  -2364       C  
ATOM   2557  O   ILE A1096      -1.069  37.713   2.543  1.00 54.89           O  
ANISOU 2557  O   ILE A1096     8492   5903   6461  -1149   -531  -2219       O  
ATOM   2558  CB  ILE A1096       0.301  36.742   4.888  1.00 40.63           C  
ANISOU 2558  CB  ILE A1096     6446   4454   4539  -1134   -714  -2306       C  
ATOM   2559  CG1 ILE A1096       0.385  36.182   6.309  1.00 48.30           C  
ANISOU 2559  CG1 ILE A1096     7378   5595   5378  -1043   -802  -2337       C  
ATOM   2560  CG2 ILE A1096       1.688  36.990   4.320  1.00 41.75           C  
ANISOU 2560  CG2 ILE A1096     6532   4568   4762  -1372   -669  -2299       C  
ATOM   2561  CD1 ILE A1096       1.097  34.848   6.398  1.00 49.66           C  
ANISOU 2561  CD1 ILE A1096     7374   5990   5504  -1069   -811  -2203       C  
ATOM   2562  N   THR A1097      -0.370  39.762   3.158  1.00 57.10           N  
ANISOU 2562  N   THR A1097     9069   4513   8113   -535   -114  -2093       N  
ATOM   2563  CA  THR A1097      -0.362  40.291   1.799  1.00 61.46           C  
ANISOU 2563  CA  THR A1097     9691   4749   8913   -565    101  -1793       C  
ATOM   2564  C   THR A1097       1.056  40.242   1.240  1.00 66.05           C  
ANISOU 2564  C   THR A1097    10208   5229   9658   -817    151  -1676       C  
ATOM   2565  O   THR A1097       1.313  40.662   0.113  1.00 68.19           O  
ANISOU 2565  O   THR A1097    10520   5253  10135   -859    346  -1388       O  
ATOM   2566  CB  THR A1097      -0.889  41.738   1.744  1.00 68.65           C  
ANISOU 2566  CB  THR A1097    10719   5258  10106   -502    168  -1804       C  
ATOM   2567  OG1 THR A1097       0.024  42.611   2.422  1.00 74.88           O  
ANISOU 2567  OG1 THR A1097    11530   5845  11078   -702     91  -2024       O  
ATOM   2568  CG2 THR A1097      -2.260  41.832   2.400  1.00 70.20           C  
ANISOU 2568  CG2 THR A1097    10954   5547  10172   -256    125  -1945       C  
ATOM   2569  N   GLU A1098       1.971  39.718   2.049  1.00 66.37           N  
ANISOU 2569  N   GLU A1098    10136   5482   9601   -970    -18  -1868       N  
ATOM   2570  CA  GLU A1098       3.380  39.614   1.689  1.00 69.55           C  
ANISOU 2570  CA  GLU A1098    10414   5828  10185  -1227     13  -1788       C  
ATOM   2571  C   GLU A1098       3.614  38.559   0.609  1.00 61.94           C  
ANISOU 2571  C   GLU A1098     9413   5005   9116  -1226    176  -1502       C  
ATOM   2572  O   GLU A1098       2.961  37.517   0.599  1.00 58.56           O  
ANISOU 2572  O   GLU A1098     9020   4868   8363  -1081    157  -1472       O  
ATOM   2573  CB  GLU A1098       4.207  39.288   2.937  1.00 76.55           C  
ANISOU 2573  CB  GLU A1098    11190   6943  10954  -1375   -230  -2060       C  
ATOM   2574  CG  GLU A1098       5.665  38.951   2.681  1.00 81.46           C  
ANISOU 2574  CG  GLU A1098    11611   7592  11750  -1631   -228  -1986       C  
ATOM   2575  CD  GLU A1098       6.393  38.550   3.948  1.00 86.62           C  
ANISOU 2575  CD  GLU A1098    12147   8519  12246  -1756   -485  -2227       C  
ATOM   2576  OE1 GLU A1098       6.085  39.122   5.015  1.00 91.00           O  
ANISOU 2576  OE1 GLU A1098    12804   9086  12687  -1738   -626  -2483       O  
ATOM   2577  OE2 GLU A1098       7.264  37.657   3.880  1.00 85.36           O  
ANISOU 2577  OE2 GLU A1098    11796   8570  12067  -1867   -529  -2147       O  
ATOM   2578  N   MET A1099       4.542  38.840  -0.302  1.00 62.91           N  
ANISOU 2578  N   MET A1099     9479   4926   9500  -1383    353  -1274       N  
ATOM   2579  CA  MET A1099       4.921  37.880  -1.332  1.00 67.40           C  
ANISOU 2579  CA  MET A1099    10042   5617   9952  -1395    535   -995       C  
ATOM   2580  C   MET A1099       5.713  36.731  -0.716  1.00 41.23           C  
ANISOU 2580  C   MET A1099     6543   2628   6493  -1520    390  -1137       C  
ATOM   2581  O   MET A1099       6.724  36.955  -0.051  1.00 43.33           O  
ANISOU 2581  O   MET A1099     6611   2897   6956  -1709    257  -1281       O  
ATOM   2582  CB  MET A1099       5.741  38.560  -2.430  1.00 46.00           C  
ANISOU 2582  CB  MET A1099     7285   2627   7564  -1499    786   -676       C  
ATOM   2583  CG  MET A1099       5.105  39.817  -3.014  1.00 51.49           C  
ANISOU 2583  CG  MET A1099     8116   2992   8455  -1385    923   -493       C  
ATOM   2584  SD  MET A1099       3.681  39.495  -4.077  1.00 71.38           S  
ANISOU 2584  SD  MET A1099    10916   5571  10633  -1067   1074   -184       S  
ATOM   2585  CE  MET A1099       2.318  39.737  -2.940  1.00 48.74           C  
ANISOU 2585  CE  MET A1099     8138   2740   7643   -907    839   -523       C  
ATOM   2586  N   LEU A1100       5.256  35.504  -0.941  1.00 39.87           N  
ANISOU 2586  N   LEU A1100     6439   2734   5977  -1411    402  -1079       N  
ATOM   2587  CA  LEU A1100       5.871  34.338  -0.315  1.00 38.10           C  
ANISOU 2587  CA  LEU A1100     6028   2843   5605  -1494    257  -1189       C  
ATOM   2588  C   LEU A1100       6.653  33.482  -1.307  1.00 42.03           C  
ANISOU 2588  C   LEU A1100     6431   3437   6103  -1541    437   -925       C  
ATOM   2589  O   LEU A1100       6.546  33.662  -2.520  1.00 43.72           O  
ANISOU 2589  O   LEU A1100     6760   3532   6319  -1453    667   -647       O  
ATOM   2590  CB  LEU A1100       4.804  33.482   0.370  1.00 35.09           C  
ANISOU 2590  CB  LEU A1100     5707   2784   4842  -1287     89  -1304       C  
ATOM   2591  CG  LEU A1100       3.881  34.214   1.348  1.00 35.93           C  
ANISOU 2591  CG  LEU A1100     5862   2890   4901  -1137    -66  -1504       C  
ATOM   2592  CD1 LEU A1100       2.915  33.244   2.011  1.00 33.17           C  
ANISOU 2592  CD1 LEU A1100     5489   2893   4220   -917   -186  -1541       C  
ATOM   2593  CD2 LEU A1100       4.687  34.971   2.392  1.00 39.15           C  
ANISOU 2593  CD2 LEU A1100     6139   3234   5501  -1284   -245  -1732       C  
ATOM   2594  N   SER A1101       7.439  32.550  -0.775  1.00 38.17           N  
ANISOU 2594  N   SER A1101     5704   3207   5592  -1635    323   -987       N  
ATOM   2595  CA  SER A1101       8.191  31.611  -1.599  1.00 39.80           C  
ANISOU 2595  CA  SER A1101     5769   3555   5796  -1631    482   -751       C  
ATOM   2596  C   SER A1101       7.449  30.285  -1.703  1.00 40.17           C  
ANISOU 2596  C   SER A1101     5860   3919   5485  -1413    431   -712       C  
ATOM   2597  O   SER A1101       6.625  29.961  -0.849  1.00 48.48           O  
ANISOU 2597  O   SER A1101     6955   5128   6337  -1316    235   -872       O  
ATOM   2598  CB  SER A1101       9.593  31.385  -1.028  1.00 43.82           C  
ANISOU 2598  CB  SER A1101     5945   4122   6584  -1866    408   -806       C  
ATOM   2599  OG  SER A1101       9.535  30.782   0.255  1.00 46.12           O  
ANISOU 2599  OG  SER A1101     6105   4686   6734  -1880    115  -1025       O  
ATOM   2600  N   ARG A1102       7.748  29.521  -2.749  1.00 36.98           N  
ANISOU 2600  N   ARG A1102     5435   3596   5019  -1335    625   -506       N  
ATOM   2601  CA  ARG A1102       7.123  28.218  -2.956  1.00 38.48           C  
ANISOU 2601  CA  ARG A1102     5642   4042   4938  -1145    593   -488       C  
ATOM   2602  C   ARG A1102       7.439  27.258  -1.814  1.00 42.29           C  
ANISOU 2602  C   ARG A1102     5877   4758   5433  -1186    396   -603       C  
ATOM   2603  O   ARG A1102       6.589  26.472  -1.395  1.00 34.07           O  
ANISOU 2603  O   ARG A1102     4855   3892   4197  -1041    273   -659       O  
ATOM   2604  CB  ARG A1102       7.578  27.614  -4.286  1.00 41.57           C  
ANISOU 2604  CB  ARG A1102     6042   4464   5289  -1075    852   -294       C  
ATOM   2605  CG  ARG A1102       7.079  28.361  -5.505  1.00 44.43           C  
ANISOU 2605  CG  ARG A1102     6676   4683   5523   -967   1040   -136       C  
ATOM   2606  CD  ARG A1102       5.595  28.121  -5.733  1.00 36.60           C  
ANISOU 2606  CD  ARG A1102     5910   3782   4215   -748    916   -187       C  
ATOM   2607  NE  ARG A1102       5.039  29.062  -6.701  1.00 37.50           N  
ANISOU 2607  NE  ARG A1102     6277   3753   4217   -645   1038    -22       N  
ATOM   2608  CZ  ARG A1102       5.174  28.950  -8.019  1.00 44.95           C  
ANISOU 2608  CZ  ARG A1102     7345   4743   4990   -539   1249    165       C  
ATOM   2609  NH1 ARG A1102       5.852  27.934  -8.536  1.00 50.45           N  
ANISOU 2609  NH1 ARG A1102     7942   5603   5624   -526   1380    172       N  
ATOM   2610  NH2 ARG A1102       4.634  29.856  -8.822  1.00 48.87           N  
ANISOU 2610  NH2 ARG A1102     8065   5131   5372   -431   1340    353       N  
ATOM   2611  N   GLU A1103       8.668  27.332  -1.315  1.00 44.70           N  
ANISOU 2611  N   GLU A1103     5929   5066   5990  -1380    369   -611       N  
ATOM   2612  CA  GLU A1103       9.113  26.462  -0.235  1.00 44.87           C  
ANISOU 2612  CA  GLU A1103     5684   5330   6035  -1419    176   -671       C  
ATOM   2613  C   GLU A1103       8.348  26.760   1.052  1.00 40.25           C  
ANISOU 2613  C   GLU A1103     5159   4859   5274  -1394    -93   -871       C  
ATOM   2614  O   GLU A1103       7.972  25.845   1.792  1.00 39.68           O  
ANISOU 2614  O   GLU A1103     4994   5034   5048  -1288   -228   -878       O  
ATOM   2615  CB  GLU A1103      10.621  26.617  -0.007  1.00 50.76           C  
ANISOU 2615  CB  GLU A1103     6126   6048   7111  -1642    180   -631       C  
ATOM   2616  CG  GLU A1103      11.494  26.143  -1.169  1.00 51.85           C  
ANISOU 2616  CG  GLU A1103     6147   6116   7438  -1650    478   -415       C  
ATOM   2617  CD  GLU A1103      11.495  27.101  -2.349  1.00 53.32           C  
ANISOU 2617  CD  GLU A1103     6540   6034   7686  -1668    745   -312       C  
ATOM   2618  OE1 GLU A1103      10.985  28.233  -2.201  1.00 54.04           O  
ANISOU 2618  OE1 GLU A1103     6817   5947   7767  -1713    685   -399       O  
ATOM   2619  OE2 GLU A1103      12.004  26.720  -3.425  1.00 54.04           O  
ANISOU 2619  OE2 GLU A1103     6604   6092   7835  -1621   1032   -131       O  
ATOM   2620  N   PHE A1104       8.109  28.041   1.310  1.00 38.66           N  
ANISOU 2620  N   PHE A1104     5112   4468   5109  -1478   -147  -1024       N  
ATOM   2621  CA  PHE A1104       7.380  28.446   2.506  1.00 43.47           C  
ANISOU 2621  CA  PHE A1104     5807   5171   5538  -1443   -368  -1253       C  
ATOM   2622  C   PHE A1104       5.907  28.061   2.411  1.00 40.76           C  
ANISOU 2622  C   PHE A1104     5674   4897   4915  -1194   -347  -1230       C  
ATOM   2623  O   PHE A1104       5.296  27.676   3.407  1.00 41.85           O  
ANISOU 2623  O   PHE A1104     5786   5245   4871  -1048   -492  -1279       O  
ATOM   2624  CB  PHE A1104       7.513  29.951   2.744  1.00 45.90           C  
ANISOU 2624  CB  PHE A1104     6218   5209   6014  -1559   -407  -1425       C  
ATOM   2625  CG  PHE A1104       6.887  30.413   4.029  1.00 44.71           C  
ANISOU 2625  CG  PHE A1104     6134   5161   5695  -1417   -626  -1600       C  
ATOM   2626  CD1 PHE A1104       7.565  30.284   5.229  1.00 46.96           C  
ANISOU 2626  CD1 PHE A1104     6255   5643   5944  -1471   -857  -1693       C  
ATOM   2627  CD2 PHE A1104       5.619  30.970   4.039  1.00 41.34           C  
ANISOU 2627  CD2 PHE A1104     5937   4632   5138  -1221   -591  -1647       C  
ATOM   2628  CE1 PHE A1104       6.992  30.704   6.414  1.00 51.09           C  
ANISOU 2628  CE1 PHE A1104     6901   6250   6262  -1352  -1021  -1833       C  
ATOM   2629  CE2 PHE A1104       5.041  31.392   5.221  1.00 43.37           C  
ANISOU 2629  CE2 PHE A1104     6273   4964   5242  -1091   -754  -1790       C  
ATOM   2630  CZ  PHE A1104       5.728  31.259   6.409  1.00 49.06           C  
ANISOU 2630  CZ  PHE A1104     6892   5870   5879  -1171   -953  -1879       C  
ATOM   2631  N   VAL A1105       5.342  28.177   1.213  1.00 39.31           N  
ANISOU 2631  N   VAL A1105     5671   4544   4721  -1089   -163  -1097       N  
ATOM   2632  CA  VAL A1105       3.969  27.749   0.969  1.00 36.59           C  
ANISOU 2632  CA  VAL A1105     5488   4258   4157   -859   -154  -1057       C  
ATOM   2633  C   VAL A1105       3.865  26.246   1.206  1.00 35.13           C  
ANISOU 2633  C   VAL A1105     5127   4340   3880   -758   -198   -971       C  
ATOM   2634  O   VAL A1105       2.903  25.760   1.812  1.00 32.32           O  
ANISOU 2634  O   VAL A1105     4771   4124   3388   -597   -284   -981       O  
ATOM   2635  CB  VAL A1105       3.510  28.094  -0.462  1.00 23.52           C  
ANISOU 2635  CB  VAL A1105     4033   2410   2495   -769     25   -913       C  
ATOM   2636  CG1 VAL A1105       2.168  27.452  -0.765  1.00 33.05           C  
ANISOU 2636  CG1 VAL A1105     5345   3713   3500   -542     -4   -872       C  
ATOM   2637  CG2 VAL A1105       3.434  29.602  -0.645  1.00 25.65           C  
ANISOU 2637  CG2 VAL A1105     4475   2386   2885   -834     83   -954       C  
ATOM   2638  N   ARG A1106       4.877  25.521   0.737  1.00 35.99           N  
ANISOU 2638  N   ARG A1106     5055   4497   4122   -833   -115   -856       N  
ATOM   2639  CA  ARG A1106       4.983  24.087   0.971  1.00 29.59           C  
ANISOU 2639  CA  ARG A1106     4034   3894   3313   -757   -137   -764       C  
ATOM   2640  C   ARG A1106       4.987  23.781   2.463  1.00 27.76           C  
ANISOU 2640  C   ARG A1106     3640   3892   3014   -757   -331   -809       C  
ATOM   2641  O   ARG A1106       4.306  22.860   2.916  1.00 30.45           O  
ANISOU 2641  O   ARG A1106     3908   4391   3272   -613   -374   -744       O  
ATOM   2642  CB  ARG A1106       6.246  23.524   0.313  1.00 22.68           C  
ANISOU 2642  CB  ARG A1106     2970   3005   2642   -853      2   -648       C  
ATOM   2643  CG  ARG A1106       6.591  22.106   0.746  1.00 22.07           C  
ANISOU 2643  CG  ARG A1106     2618   3117   2652   -798    -24   -548       C  
ATOM   2644  CD  ARG A1106       7.729  21.530  -0.075  1.00 25.53           C  
ANISOU 2644  CD  ARG A1106     2886   3503   3310   -857    164   -439       C  
ATOM   2645  NE  ARG A1106       8.963  22.291   0.092  1.00 33.60           N  
ANISOU 2645  NE  ARG A1106     3780   4473   4512  -1057    170   -425       N  
ATOM   2646  CZ  ARG A1106      10.115  21.982  -0.493  1.00 39.10           C  
ANISOU 2646  CZ  ARG A1106     4290   5121   5447  -1135    342   -316       C  
ATOM   2647  NH1 ARG A1106      10.194  20.924  -1.288  1.00 41.41           N  
ANISOU 2647  NH1 ARG A1106     4526   5410   5797  -1018    533   -237       N  
ATOM   2648  NH2 ARG A1106      11.188  22.731  -0.284  1.00 42.55           N  
ANISOU 2648  NH2 ARG A1106     4581   5496   6089  -1329    331   -300       N  
ATOM   2649  N   GLU A1107       5.751  24.562   3.223  1.00 26.53           N  
ANISOU 2649  N   GLU A1107     3422   3760   2897   -918   -448   -919       N  
ATOM   2650  CA  GLU A1107       5.787  24.408   4.675  1.00 32.07           C  
ANISOU 2650  CA  GLU A1107     3998   4726   3461   -914   -656   -988       C  
ATOM   2651  C   GLU A1107       4.417  24.658   5.295  1.00 35.31           C  
ANISOU 2651  C   GLU A1107     4610   5123   3683   -682   -676  -1002       C  
ATOM   2652  O   GLU A1107       3.994  23.936   6.197  1.00 42.03           O  
ANISOU 2652  O   GLU A1107     5379   6170   4421   -549   -729   -905       O  
ATOM   2653  CB  GLU A1107       6.814  25.355   5.297  1.00 37.69           C  
ANISOU 2653  CB  GLU A1107     4645   5399   4278  -1086   -786  -1114       C  
ATOM   2654  CG  GLU A1107       8.259  24.984   5.020  1.00 49.08           C  
ANISOU 2654  CG  GLU A1107     5794   6888   5968  -1296   -794  -1038       C  
ATOM   2655  CD  GLU A1107       9.224  25.715   5.930  1.00 57.30           C  
ANISOU 2655  CD  GLU A1107     6724   7942   7107  -1413   -989  -1141       C  
ATOM   2656  OE1 GLU A1107       8.767  26.268   6.954  1.00 59.14           O  
ANISOU 2656  OE1 GLU A1107     7094   8224   7154  -1322  -1139  -1271       O  
ATOM   2657  OE2 GLU A1107      10.436  25.737   5.625  1.00 60.76           O  
ANISOU 2657  OE2 GLU A1107     6937   8327   7822  -1591   -986  -1085       O  
ATOM   2658  N   LEU A1108       3.733  25.687   4.803  1.00 32.83           N  
ANISOU 2658  N   LEU A1108     4538   4565   3371   -636   -613  -1090       N  
ATOM   2659  CA  LEU A1108       2.403  26.037   5.286  1.00 30.30           C  
ANISOU 2659  CA  LEU A1108     4403   4185   2924   -436   -616  -1083       C  
ATOM   2660  C   LEU A1108       1.421  24.891   5.079  1.00 26.91           C  
ANISOU 2660  C   LEU A1108     3947   3836   2442   -292   -539   -909       C  
ATOM   2661  O   LEU A1108       0.654  24.548   5.979  1.00 30.16           O  
ANISOU 2661  O   LEU A1108     4340   4363   2758   -208   -535   -845       O  
ATOM   2662  CB  LEU A1108       1.893  27.296   4.581  1.00 31.45           C  
ANISOU 2662  CB  LEU A1108     4720   4083   3148   -390   -561  -1201       C  
ATOM   2663  CG  LEU A1108       2.538  28.624   4.972  1.00 32.77           C  
ANISOU 2663  CG  LEU A1108     4942   4104   3403   -532   -624  -1394       C  
ATOM   2664  CD1 LEU A1108       2.172  29.702   3.967  1.00 32.02           C  
ANISOU 2664  CD1 LEU A1108     4962   3748   3457   -558   -486  -1452       C  
ATOM   2665  CD2 LEU A1108       2.108  29.029   6.372  1.00 33.09           C  
ANISOU 2665  CD2 LEU A1108     5097   4198   3277   -480   -719  -1446       C  
ATOM   2666  N   TYR A1109       1.454  24.299   3.889  1.00 27.79           N  
ANISOU 2666  N   TYR A1109     4024   3901   2634   -284   -458   -853       N  
ATOM   2667  CA  TYR A1109       0.588  23.165   3.579  1.00 29.61           C  
ANISOU 2667  CA  TYR A1109     4191   4191   2869   -167   -401   -726       C  
ATOM   2668  C   TYR A1109       0.891  21.960   4.466  1.00 28.94           C  
ANISOU 2668  C   TYR A1109     3835   4381   2779   -130   -453   -640       C  
ATOM   2669  O   TYR A1109       0.015  21.137   4.731  1.00 31.02           O  
ANISOU 2669  O   TYR A1109     4012   4729   3047     10   -436   -542       O  
ATOM   2670  CB  TYR A1109       0.728  22.774   2.108  1.00 25.73           C  
ANISOU 2670  CB  TYR A1109     3728   3602   2447   -172   -318   -726       C  
ATOM   2671  CG  TYR A1109       0.086  23.741   1.141  1.00 23.58           C  
ANISOU 2671  CG  TYR A1109     3579   3193   2189   -130   -240   -773       C  
ATOM   2672  CD1 TYR A1109      -0.968  24.552   1.538  1.00 25.59           C  
ANISOU 2672  CD1 TYR A1109     3884   3410   2430    -91   -225   -772       C  
ATOM   2673  CD2 TYR A1109       0.531  23.837  -0.173  1.00 24.68           C  
ANISOU 2673  CD2 TYR A1109     3846   3191   2340   -162   -162   -747       C  
ATOM   2674  CE1 TYR A1109      -1.560  25.436   0.656  1.00 30.16           C  
ANISOU 2674  CE1 TYR A1109     4608   3826   3027    -31   -195   -756       C  
ATOM   2675  CE2 TYR A1109      -0.055  24.717  -1.063  1.00 24.38           C  
ANISOU 2675  CE2 TYR A1109     3966   3017   2281   -115   -113   -716       C  
ATOM   2676  CZ  TYR A1109      -1.099  25.514  -0.643  1.00 29.72           C  
ANISOU 2676  CZ  TYR A1109     4676   3658   2960    -43   -149   -717       C  
ATOM   2677  OH  TYR A1109      -1.682  26.391  -1.527  1.00 31.26           O  
ANISOU 2677  OH  TYR A1109     5069   3695   3113     15   -121   -668       O  
ATOM   2678  N   GLY A1110       2.134  21.856   4.922  1.00 24.89           N  
ANISOU 2678  N   GLY A1110     3159   4022   2275   -259   -523   -651       N  
ATOM   2679  CA  GLY A1110       2.538  20.744   5.763  1.00 27.03           C  
ANISOU 2679  CA  GLY A1110     3147   4569   2554   -223   -582   -494       C  
ATOM   2680  C   GLY A1110       2.616  21.101   7.235  1.00 30.34           C  
ANISOU 2680  C   GLY A1110     3565   5124   2839   -191   -668   -481       C  
ATOM   2681  O   GLY A1110       3.310  20.440   8.007  1.00 33.27           O  
ANISOU 2681  O   GLY A1110     3721   5710   3212   -193   -733   -348       O  
ATOM   2682  N   SER A1111       1.900  22.151   7.622  1.00 26.19           N  
ANISOU 2682  N   SER A1111     3279   4466   2206   -157   -665   -607       N  
ATOM   2683  CA  SER A1111       1.846  22.572   9.017  1.00 31.04           C  
ANISOU 2683  CA  SER A1111     3926   5213   2653   -125   -739   -645       C  
ATOM   2684  C   SER A1111       0.398  22.701   9.479  1.00 29.70           C  
ANISOU 2684  C   SER A1111     3876   5020   2387     26   -647   -627       C  
ATOM   2685  O   SER A1111       0.008  22.148  10.509  1.00 31.74           O  
ANISOU 2685  O   SER A1111     4034   5496   2529    144   -637   -525       O  
ATOM   2686  CB  SER A1111       2.581  23.900   9.209  1.00 24.43           C  
ANISOU 2686  CB  SER A1111     3233   4262   1789   -273   -843   -858       C  
ATOM   2687  OG  SER A1111       3.936  23.797   8.807  1.00 37.66           O  
ANISOU 2687  OG  SER A1111     4745   5971   3591   -430   -927   -878       O  
ATOM   2688  N   VAL A1112      -0.392  23.433   8.700  1.00 32.02           N  
ANISOU 2688  N   VAL A1112     4361   5068   2739     22   -570   -706       N  
ATOM   2689  CA  VAL A1112      -1.798  23.657   9.009  1.00 28.90           C  
ANISOU 2689  CA  VAL A1112     4044   4644   2294    150   -476   -701       C  
ATOM   2690  C   VAL A1112      -2.589  22.355   8.982  1.00 30.98           C  
ANISOU 2690  C   VAL A1112     4122   5041   2609    325   -416   -518       C  
ATOM   2691  O   VAL A1112      -2.110  21.336   8.486  1.00 31.23           O  
ANISOU 2691  O   VAL A1112     3989   5138   2738    328   -428   -403       O  
ATOM   2692  CB  VAL A1112      -2.441  24.647   8.022  1.00 19.85           C  
ANISOU 2692  CB  VAL A1112     3076   3231   1234    100   -400   -791       C  
ATOM   2693  CG1 VAL A1112      -1.643  25.939   7.973  1.00 21.50           C  
ANISOU 2693  CG1 VAL A1112     3450   3302   1416    -72   -435   -963       C  
ATOM   2694  CG2 VAL A1112      -2.538  24.024   6.640  1.00 17.54           C  
ANISOU 2694  CG2 VAL A1112     2735   2829   1099    106   -366   -704       C  
ATOM   2695  N   ASP A1113      -3.804  22.398   9.515  1.00 31.15           N  
ANISOU 2695  N   ASP A1113     4153   5112   2572    483   -345   -490       N  
ATOM   2696  CA  ASP A1113      -4.659  21.220   9.557  1.00 30.46           C  
ANISOU 2696  CA  ASP A1113     3880   5158   2536    678   -278   -301       C  
ATOM   2697  C   ASP A1113      -5.581  21.171   8.344  1.00 31.90           C  
ANISOU 2697  C   ASP A1113     4107   5143   2868    745   -250   -313       C  
ATOM   2698  O   ASP A1113      -5.736  20.125   7.713  1.00 34.70           O  
ANISOU 2698  O   ASP A1113     4321   5525   3340    812   -250   -195       O  
ATOM   2699  CB  ASP A1113      -5.477  21.203  10.850  1.00 38.37           C  
ANISOU 2699  CB  ASP A1113     4839   6360   3380    852   -204   -230       C  
ATOM   2700  CG  ASP A1113      -4.604  21.156  12.091  1.00 50.47           C  
ANISOU 2700  CG  ASP A1113     6321   8126   4729    810   -250   -211       C  
ATOM   2701  OD1 ASP A1113      -3.578  20.443  12.071  1.00 54.25           O  
ANISOU 2701  OD1 ASP A1113     6660   8706   5247    734   -307   -111       O  
ATOM   2702  OD2 ASP A1113      -4.944  21.834  13.085  1.00 53.45           O  
ANISOU 2702  OD2 ASP A1113     6800   8592   4915    861   -231   -301       O  
ATOM   2703  N   PHE A1114      -6.187  22.308   8.017  1.00 32.34           N  
ANISOU 2703  N   PHE A1114     4352   5007   2929    729   -237   -447       N  
ATOM   2704  CA  PHE A1114      -7.115  22.379   6.895  1.00 27.77           C  
ANISOU 2704  CA  PHE A1114     3826   4247   2477    809   -235   -456       C  
ATOM   2705  C   PHE A1114      -6.818  23.550   5.964  1.00 29.97           C  
ANISOU 2705  C   PHE A1114     4284   4287   2818    649   -252   -568       C  
ATOM   2706  O   PHE A1114      -6.357  24.604   6.402  1.00 35.97           O  
ANISOU 2706  O   PHE A1114     5148   5011   3508    534   -233   -671       O  
ATOM   2707  CB  PHE A1114      -8.555  22.486   7.401  1.00 30.15           C  
ANISOU 2707  CB  PHE A1114     4122   4598   2735   1047   -169   -416       C  
ATOM   2708  CG  PHE A1114      -8.990  21.328   8.251  1.00 31.74           C  
ANISOU 2708  CG  PHE A1114     4113   5072   2875   1241    -90   -222       C  
ATOM   2709  CD1 PHE A1114      -9.506  20.182   7.673  1.00 32.39           C  
ANISOU 2709  CD1 PHE A1114     3981   5097   3230   1298    -81    -43       C  
ATOM   2710  CD2 PHE A1114      -8.894  21.392   9.631  1.00 28.42           C  
ANISOU 2710  CD2 PHE A1114     3643   4853   2303   1284    -20   -163       C  
ATOM   2711  CE1 PHE A1114      -9.911  19.118   8.454  1.00 30.38           C  
ANISOU 2711  CE1 PHE A1114     3493   4948   3100   1343     35    211       C  
ATOM   2712  CE2 PHE A1114      -9.298  20.331  10.417  1.00 25.09           C  
ANISOU 2712  CE2 PHE A1114     2996   4683   1854   1461     92    104       C  
ATOM   2713  CZ  PHE A1114      -9.807  19.193   9.828  1.00 26.73           C  
ANISOU 2713  CZ  PHE A1114     2985   4799   2371   1495    133    323       C  
ATOM   2714  N   VAL A1115      -7.088  23.354   4.677  1.00 32.81           N  
ANISOU 2714  N   VAL A1115     4665   4507   3293    656   -283   -546       N  
ATOM   2715  CA  VAL A1115      -6.971  24.418   3.686  1.00 30.10           C  
ANISOU 2715  CA  VAL A1115     4464   3983   2990    562   -280   -593       C  
ATOM   2716  C   VAL A1115      -8.338  24.712   3.080  1.00 27.68           C  
ANISOU 2716  C   VAL A1115     4225   3568   2723    737   -314   -568       C  
ATOM   2717  O   VAL A1115      -9.015  23.810   2.581  1.00 19.37           O  
ANISOU 2717  O   VAL A1115     3102   2530   1727    856   -376   -523       O  
ATOM   2718  CB  VAL A1115      -5.981  24.053   2.564  1.00 18.30           C  
ANISOU 2718  CB  VAL A1115     2960   2445   1548    425   -287   -576       C  
ATOM   2719  CG1 VAL A1115      -6.004  25.111   1.474  1.00 18.82           C  
ANISOU 2719  CG1 VAL A1115     3170   2361   1621    398   -278   -594       C  
ATOM   2720  CG2 VAL A1115      -4.580  23.899   3.124  1.00 31.24           C  
ANISOU 2720  CG2 VAL A1115     4551   4179   3140    266   -268   -610       C  
ATOM   2721  N   ILE A1116      -8.744  25.975   3.133  1.00 27.75           N  
ANISOU 2721  N   ILE A1116     4371   3468   2706    764   -286   -618       N  
ATOM   2722  CA  ILE A1116     -10.052  26.373   2.631  1.00 30.56           C  
ANISOU 2722  CA  ILE A1116     4808   3719   3085    951   -324   -588       C  
ATOM   2723  C   ILE A1116      -9.973  26.926   1.211  1.00 36.64           C  
ANISOU 2723  C   ILE A1116     5714   4344   3863    933   -380   -556       C  
ATOM   2724  O   ILE A1116      -9.286  27.913   0.952  1.00 42.21           O  
ANISOU 2724  O   ILE A1116     6545   4946   4548    836   -332   -591       O  
ATOM   2725  CB  ILE A1116     -10.705  27.422   3.547  1.00 26.71           C  
ANISOU 2725  CB  ILE A1116     4397   3182   2570   1039   -240   -656       C  
ATOM   2726  CG1 ILE A1116     -10.836  26.871   4.968  1.00 22.30           C  
ANISOU 2726  CG1 ILE A1116     3726   2804   1942   1092   -173   -678       C  
ATOM   2727  CG2 ILE A1116     -12.066  27.831   3.002  1.00 28.25           C  
ANISOU 2727  CG2 ILE A1116     4646   3258   2828   1233   -259   -604       C  
ATOM   2728  CD1 ILE A1116     -11.452  27.842   5.947  1.00 24.32           C  
ANISOU 2728  CD1 ILE A1116     4050   3035   2155   1176    -64   -769       C  
ATOM   2729  N   ILE A1117     -10.686  26.277   0.296  1.00 31.46           N  
ANISOU 2729  N   ILE A1117     5041   3687   3224   1048   -490   -503       N  
ATOM   2730  CA  ILE A1117     -10.723  26.697  -1.099  1.00 18.73           C  
ANISOU 2730  CA  ILE A1117     3584   1974   1560   1081   -567   -467       C  
ATOM   2731  C   ILE A1117     -12.151  27.065  -1.500  1.00 33.77           C  
ANISOU 2731  C   ILE A1117     5549   3811   3470   1297   -666   -443       C  
ATOM   2732  O   ILE A1117     -12.858  26.261  -2.105  1.00 34.97           O  
ANISOU 2732  O   ILE A1117     5588   4029   3669   1352   -789   -440       O  
ATOM   2733  CB  ILE A1117     -10.192  25.592  -2.037  1.00 17.87           C  
ANISOU 2733  CB  ILE A1117     3381   1941   1468    997   -620   -455       C  
ATOM   2734  CG1 ILE A1117      -8.920  24.963  -1.463  1.00 16.66           C  
ANISOU 2734  CG1 ILE A1117     3087   1882   1363    794   -507   -472       C  
ATOM   2735  CG2 ILE A1117      -9.946  26.142  -3.435  1.00 18.99           C  
ANISOU 2735  CG2 ILE A1117     3705   2010   1499   1006   -651   -418       C  
ATOM   2736  CD1 ILE A1117      -8.390  23.806  -2.277  1.00 23.04           C  
ANISOU 2736  CD1 ILE A1117     3791   2759   2206    716   -520   -480       C  
ATOM   2737  N   PRO A1118     -12.579  28.290  -1.166  1.00 35.22           N  
ANISOU 2737  N   PRO A1118     5824   3867   3691   1352   -577   -418       N  
ATOM   2738  CA  PRO A1118     -13.949  28.748  -1.400  1.00 35.11           C  
ANISOU 2738  CA  PRO A1118     5740   3800   3800   1485   -601   -330       C  
ATOM   2739  C   PRO A1118     -14.141  29.323  -2.799  1.00 29.30           C  
ANISOU 2739  C   PRO A1118     5129   2983   3019   1543   -695   -222       C  
ATOM   2740  O   PRO A1118     -14.805  30.347  -2.958  1.00 32.80           O  
ANISOU 2740  O   PRO A1118     5597   3304   3561   1626   -652   -120       O  
ATOM   2741  CB  PRO A1118     -14.134  29.832  -0.335  1.00 34.98           C  
ANISOU 2741  CB  PRO A1118     5760   3667   3863   1511   -431   -362       C  
ATOM   2742  CG  PRO A1118     -12.723  30.310  -0.010  1.00 36.42           C  
ANISOU 2742  CG  PRO A1118     6095   3795   3948   1360   -350   -466       C  
ATOM   2743  CD  PRO A1118     -11.731  29.377  -0.656  1.00 34.11           C  
ANISOU 2743  CD  PRO A1118     5813   3611   3537   1246   -438   -466       C  
ATOM   2744  N   SER A1119     -13.569  28.660  -3.797  1.00 35.20           N  
ANISOU 2744  N   SER A1119     5940   3809   3624   1504   -810   -232       N  
ATOM   2745  CA  SER A1119     -13.611  29.141  -5.173  1.00 36.86           C  
ANISOU 2745  CA  SER A1119     6270   4003   3731   1545   -882   -112       C  
ATOM   2746  C   SER A1119     -15.027  29.157  -5.747  1.00 39.65           C  
ANISOU 2746  C   SER A1119     6451   4417   4198   1632  -1002    -12       C  
ATOM   2747  O   SER A1119     -15.928  28.498  -5.229  1.00 38.44           O  
ANISOU 2747  O   SER A1119     6069   4326   4211   1634  -1046    -52       O  
ATOM   2748  CB  SER A1119     -12.705  28.282  -6.056  1.00 27.18           C  
ANISOU 2748  CB  SER A1119     5093   2897   2338   1451   -933   -172       C  
ATOM   2749  OG  SER A1119     -11.364  28.311  -5.599  1.00 25.86           O  
ANISOU 2749  OG  SER A1119     5057   2677   2091   1344   -813   -226       O  
ATOM   2750  N   TYR A1120     -15.212  29.919  -6.821  1.00 41.73           N  
ANISOU 2750  N   TYR A1120     6811   4660   4382   1698  -1047    150       N  
ATOM   2751  CA  TYR A1120     -16.508  30.021  -7.480  1.00 41.87           C  
ANISOU 2751  CA  TYR A1120     6673   4744   4491   1789  -1189    279       C  
ATOM   2752  C   TYR A1120     -16.602  29.120  -8.712  1.00 51.25           C  
ANISOU 2752  C   TYR A1120     7821   6136   5514   1761  -1379    242       C  
ATOM   2753  O   TYR A1120     -17.641  28.508  -8.955  1.00 47.95           O  
ANISOU 2753  O   TYR A1120     7204   5812   5202   1782  -1540    227       O  
ATOM   2754  CB  TYR A1120     -16.796  31.473  -7.878  1.00 48.62           C  
ANISOU 2754  CB  TYR A1120     7621   5459   5393   1899  -1128    520       C  
ATOM   2755  CG  TYR A1120     -17.352  32.340  -6.765  1.00 48.80           C  
ANISOU 2755  CG  TYR A1120     7575   5274   5690   1959   -977    557       C  
ATOM   2756  CD1 TYR A1120     -18.692  32.269  -6.407  1.00 46.17           C  
ANISOU 2756  CD1 TYR A1120     6997   4946   5598   2030  -1024    613       C  
ATOM   2757  CD2 TYR A1120     -16.542  33.244  -6.088  1.00 50.00           C  
ANISOU 2757  CD2 TYR A1120     7898   5214   5887   1938   -773    528       C  
ATOM   2758  CE1 TYR A1120     -19.208  33.064  -5.399  1.00 46.95           C  
ANISOU 2758  CE1 TYR A1120     7027   4855   5956   2091   -857    633       C  
ATOM   2759  CE2 TYR A1120     -17.050  34.046  -5.077  1.00 48.10           C  
ANISOU 2759  CE2 TYR A1120     7593   4782   5903   1988   -622    512       C  
ATOM   2760  CZ  TYR A1120     -18.383  33.950  -4.738  1.00 48.44           C  
ANISOU 2760  CZ  TYR A1120     7398   4846   6161   2073   -659    563       C  
ATOM   2761  OH  TYR A1120     -18.892  34.744  -3.736  1.00 50.99           O  
ANISOU 2761  OH  TYR A1120     7659   4979   6738   2132   -491    530       O  
ATOM   2762  N   PHE A1121     -15.524  29.034  -9.489  1.00 57.81           N  
ANISOU 2762  N   PHE A1121     8829   7032   6103   1707  -1347    224       N  
ATOM   2763  CA  PHE A1121     -15.567  28.280 -10.742  1.00 64.71           C  
ANISOU 2763  CA  PHE A1121     9680   8112   6796   1684  -1497    181       C  
ATOM   2764  C   PHE A1121     -14.284  27.494 -11.030  1.00 62.06           C  
ANISOU 2764  C   PHE A1121     9426   7844   6310   1560  -1405     29       C  
ATOM   2765  O   PHE A1121     -14.109  26.980 -12.135  1.00 74.64           O  
ANISOU 2765  O   PHE A1121    11034   9607   7721   1536  -1478     -8       O  
ATOM   2766  CB  PHE A1121     -15.874  29.227 -11.912  1.00 72.48           C  
ANISOU 2766  CB  PHE A1121    10758   9174   7606   1784  -1559    429       C  
ATOM   2767  CG  PHE A1121     -14.656  29.881 -12.511  1.00 78.12           C  
ANISOU 2767  CG  PHE A1121    11703   9884   8097   1763  -1393    550       C  
ATOM   2768  CD1 PHE A1121     -13.977  30.878 -11.828  1.00 78.70           C  
ANISOU 2768  CD1 PHE A1121    11916   9734   8254   1764  -1184    660       C  
ATOM   2769  CD2 PHE A1121     -14.202  29.507 -13.768  1.00 81.99           C  
ANISOU 2769  CD2 PHE A1121    12263  10587   8304   1738  -1434    559       C  
ATOM   2770  CE1 PHE A1121     -12.859  31.480 -12.383  1.00 82.08           C  
ANISOU 2770  CE1 PHE A1121    12536  10134   8519   1734  -1014    798       C  
ATOM   2771  CE2 PHE A1121     -13.086  30.102 -14.328  1.00 84.46           C  
ANISOU 2771  CE2 PHE A1121    12764  10902   8425   1718  -1251    701       C  
ATOM   2772  CZ  PHE A1121     -12.414  31.091 -13.635  1.00 84.75           C  
ANISOU 2772  CZ  PHE A1121    12924  10698   8578   1714  -1039    834       C  
ATOM   2773  N   GLU A1122     -13.413  27.398 -10.024  1.00 48.98           N  
ANISOU 2773  N   GLU A1122     6734   6981   4894   1694    -83    938       N  
ATOM   2774  CA  GLU A1122     -12.120  26.699 -10.101  1.00 43.70           C  
ANISOU 2774  CA  GLU A1122     6159   6221   4223   1440    -97    802       C  
ATOM   2775  C   GLU A1122     -12.076  25.499 -11.052  1.00 41.46           C  
ANISOU 2775  C   GLU A1122     5730   6254   3771   1312   -213    648       C  
ATOM   2776  O   GLU A1122     -12.624  24.442 -10.747  1.00 44.77           O  
ANISOU 2776  O   GLU A1122     6085   6776   4149   1218   -298    437       O  
ATOM   2777  CB  GLU A1122     -11.715  26.228  -8.701  1.00 43.23           C  
ANISOU 2777  CB  GLU A1122     6247   5905   4274   1319    -62    603       C  
ATOM   2778  CG  GLU A1122     -10.385  25.496  -8.643  1.00 43.82           C  
ANISOU 2778  CG  GLU A1122     6382   5899   4368   1095    -66    470       C  
ATOM   2779  CD  GLU A1122      -9.198  26.430  -8.741  1.00 51.53           C  
ANISOU 2779  CD  GLU A1122     7469   6706   5404   1044     22    617       C  
ATOM   2780  OE1 GLU A1122      -8.989  27.213  -7.789  1.00 52.88           O  
ANISOU 2780  OE1 GLU A1122     7807   6596   5689   1050    109    643       O  
ATOM   2781  OE2 GLU A1122      -8.481  26.385  -9.764  1.00 55.01           O  
ANISOU 2781  OE2 GLU A1122     7839   7303   5760    983      6    702       O  
ATOM   2782  N   PRO A1123     -11.423  25.663 -12.213  1.00 46.11           N  
ANISOU 2782  N   PRO A1123     6281   6986   4254   1297   -214    751       N  
ATOM   2783  CA  PRO A1123     -11.397  24.605 -13.228  1.00 44.09           C  
ANISOU 2783  CA  PRO A1123     5902   7036   3815   1220   -306    581       C  
ATOM   2784  C   PRO A1123     -10.277  23.576 -13.046  1.00 37.31           C  
ANISOU 2784  C   PRO A1123     5137   6050   2990   1042   -303    357       C  
ATOM   2785  O   PRO A1123     -10.393  22.473 -13.579  1.00 34.83           O  
ANISOU 2785  O   PRO A1123     4774   5893   2568    975   -379    138       O  
ATOM   2786  CB  PRO A1123     -11.198  25.386 -14.528  1.00 46.00           C  
ANISOU 2786  CB  PRO A1123     6053   7522   3903   1342   -280    826       C  
ATOM   2787  CG  PRO A1123     -10.402  26.574 -14.116  1.00 48.63           C  
ANISOU 2787  CG  PRO A1123     6542   7550   4385   1353   -164   1081       C  
ATOM   2788  CD  PRO A1123     -10.834  26.919 -12.710  1.00 48.44           C  
ANISOU 2788  CD  PRO A1123     6639   7193   4574   1372   -127   1052       C  
ATOM   2789  N   PHE A1124      -9.221  23.917 -12.313  1.00 34.58           N  
ANISOU 2789  N   PHE A1124     4916   5438   2785    977   -215    403       N  
ATOM   2790  CA  PHE A1124      -8.077  23.012 -12.189  1.00 33.62           C  
ANISOU 2790  CA  PHE A1124     4836   5250   2688    866   -198    235       C  
ATOM   2791  C   PHE A1124      -7.840  22.529 -10.756  1.00 31.63           C  
ANISOU 2791  C   PHE A1124     4677   4719   2622    780   -177    116       C  
ATOM   2792  O   PHE A1124      -7.590  21.343 -10.526  1.00 26.55           O  
ANISOU 2792  O   PHE A1124     4053   4027   2006    726   -205    -66       O  
ATOM   2793  CB  PHE A1124      -6.815  23.689 -12.727  1.00 33.09           C  
ANISOU 2793  CB  PHE A1124     4767   5240   2565    860   -120    394       C  
ATOM   2794  CG  PHE A1124      -6.903  24.063 -14.179  1.00 36.35           C  
ANISOU 2794  CG  PHE A1124     5073   5968   2770    955   -126    529       C  
ATOM   2795  CD1 PHE A1124      -6.714  23.111 -15.167  1.00 35.48           C  
ANISOU 2795  CD1 PHE A1124     4867   6128   2487    996   -165    355       C  
ATOM   2796  CD2 PHE A1124      -7.177  25.368 -14.555  1.00 39.87           C  
ANISOU 2796  CD2 PHE A1124     5515   6444   3190   1023    -86    841       C  
ATOM   2797  CE1 PHE A1124      -6.797  23.454 -16.502  1.00 37.72           C  
ANISOU 2797  CE1 PHE A1124     5013   6774   2544   1099   -165    476       C  
ATOM   2798  CE2 PHE A1124      -7.261  25.718 -15.888  1.00 41.39           C  
ANISOU 2798  CE2 PHE A1124     5584   6966   3177   1126    -83   1008       C  
ATOM   2799  CZ  PHE A1124      -7.071  24.761 -16.863  1.00 40.34           C  
ANISOU 2799  CZ  PHE A1124     5316   7169   2841   1162   -123    821       C  
ATOM   2800  N   GLY A1125      -7.911  23.448  -9.799  1.00 30.55           N  
ANISOU 2800  N   GLY A1125     4611   4395   2601    789   -122    227       N  
ATOM   2801  CA  GLY A1125      -7.779  23.106  -8.391  1.00 30.50           C  
ANISOU 2801  CA  GLY A1125     4682   4164   2741    728   -100    127       C  
ATOM   2802  C   GLY A1125      -6.442  22.505  -8.000  1.00 35.82           C  
ANISOU 2802  C   GLY A1125     5356   4786   3467    649    -76     60       C  
ATOM   2803  O   GLY A1125      -6.393  21.433  -7.398  1.00 40.62           O  
ANISOU 2803  O   GLY A1125     5979   5316   4140    623   -104    -51       O  
ATOM   2804  N   LEU A1126      -5.357  23.197  -8.328  1.00 36.59           N  
ANISOU 2804  N   LEU A1126     5440   4949   3513    618    -26    163       N  
ATOM   2805  CA  LEU A1126      -4.017  22.701  -8.032  1.00 29.09           C  
ANISOU 2805  CA  LEU A1126     4452   4043   2560    565     -6    118       C  
ATOM   2806  C   LEU A1126      -3.659  22.859  -6.555  1.00 29.39           C  
ANISOU 2806  C   LEU A1126     4534   3940   2693    494     13     94       C  
ATOM   2807  O   LEU A1126      -2.886  22.068  -6.008  1.00 33.90           O  
ANISOU 2807  O   LEU A1126     5064   4539   3279    490      3     35       O  
ATOM   2808  CB  LEU A1126      -2.985  23.418  -8.904  1.00 30.51           C  
ANISOU 2808  CB  LEU A1126     4588   4409   2597    519     41    254       C  
ATOM   2809  CG  LEU A1126      -3.026  23.085 -10.398  1.00 30.66           C  
ANISOU 2809  CG  LEU A1126     4539   4638   2473    609     29    261       C  
ATOM   2810  CD1 LEU A1126      -2.032  23.938 -11.172  1.00 24.49           C  
ANISOU 2810  CD1 LEU A1126     3720   4043   1542    560     98    448       C  
ATOM   2811  CD2 LEU A1126      -2.754  21.605 -10.623  1.00 26.49           C  
ANISOU 2811  CD2 LEU A1126     3969   4167   1928    727     -4     56       C  
ATOM   2812  N   VAL A1127      -4.222  23.882  -5.917  1.00 27.31           N  
ANISOU 2812  N   VAL A1127     4381   3531   2465    469     43    142       N  
ATOM   2813  CA  VAL A1127      -4.012  24.111  -4.490  1.00 27.33           C  
ANISOU 2813  CA  VAL A1127     4455   3418   2513    394     61     86       C  
ATOM   2814  C   VAL A1127      -4.467  22.897  -3.685  1.00 26.45           C  
ANISOU 2814  C   VAL A1127     4278   3276   2494    413     13     -1       C  
ATOM   2815  O   VAL A1127      -3.805  22.486  -2.730  1.00 29.54           O  
ANISOU 2815  O   VAL A1127     4622   3721   2883    359      8    -27       O  
ATOM   2816  CB  VAL A1127      -4.756  25.378  -4.004  1.00 28.09           C  
ANISOU 2816  CB  VAL A1127     4789   3283   2600    404    125    112       C  
ATOM   2817  CG1 VAL A1127      -4.846  25.412  -2.483  1.00 16.46           C  
ANISOU 2817  CG1 VAL A1127     3373   1728   1154    324    135    -10       C  
ATOM   2818  CG2 VAL A1127      -4.066  26.629  -4.525  1.00 29.44           C  
ANISOU 2818  CG2 VAL A1127     5127   3373   2686    321    217    270       C  
ATOM   2819  N   ALA A1128      -5.590  22.316  -4.093  1.00 24.30           N  
ANISOU 2819  N   ALA A1128     4014   2957   2261    481    -20    -20       N  
ATOM   2820  CA  ALA A1128      -6.101  21.100  -3.473  1.00 24.76           C  
ANISOU 2820  CA  ALA A1128     4079   2968   2360    480    -55    -61       C  
ATOM   2821  C   ALA A1128      -5.075  19.973  -3.560  1.00 28.91           C  
ANISOU 2821  C   ALA A1128     4607   3516   2863    533    -77    -78       C  
ATOM   2822  O   ALA A1128      -4.734  19.364  -2.550  1.00 32.59           O  
ANISOU 2822  O   ALA A1128     5114   3945   3325    543    -77    -67       O  
ATOM   2823  CB  ALA A1128      -7.410  20.683  -4.122  1.00 15.47           C  
ANISOU 2823  CB  ALA A1128     2924   1797   1157    505    -96    -92       C  
ATOM   2824  N   LEU A1129      -4.577  19.714  -4.765  1.00 21.92           N  
ANISOU 2824  N   LEU A1129     3693   2714   1921    605    -90   -104       N  
ATOM   2825  CA  LEU A1129      -3.595  18.653  -4.991  1.00 26.97           C  
ANISOU 2825  CA  LEU A1129     4368   3379   2502    743   -108   -142       C  
ATOM   2826  C   LEU A1129      -2.330  18.840  -4.158  1.00 32.65           C  
ANISOU 2826  C   LEU A1129     5021   4195   3189    757    -75    -93       C  
ATOM   2827  O   LEU A1129      -1.862  17.907  -3.500  1.00 38.38           O  
ANISOU 2827  O   LEU A1129     5826   4879   3877    905    -91    -89       O  
ATOM   2828  CB  LEU A1129      -3.226  18.581  -6.475  1.00 22.34           C  
ANISOU 2828  CB  LEU A1129     3721   2946   1821    818   -111   -197       C  
ATOM   2829  CG  LEU A1129      -4.296  18.081  -7.449  1.00 16.35           C  
ANISOU 2829  CG  LEU A1129     3003   2186   1023    815   -161   -302       C  
ATOM   2830  CD1 LEU A1129      -3.796  18.133  -8.884  1.00 39.51           C  
ANISOU 2830  CD1 LEU A1129     5851   5345   3817    885   -150   -360       C  
ATOM   2831  CD2 LEU A1129      -4.731  16.671  -7.093  1.00 17.51           C  
ANISOU 2831  CD2 LEU A1129     3323   2144   1187    863   -221   -422       C  
ATOM   2832  N   GLU A1130      -1.779  20.049  -4.197  1.00 30.28           N  
ANISOU 2832  N   GLU A1130     4606   4041   2860    610    -35    -48       N  
ATOM   2833  CA  GLU A1130      -0.547  20.355  -3.472  1.00 33.54           C  
ANISOU 2833  CA  GLU A1130     4933   4625   3184    548    -20    -11       C  
ATOM   2834  C   GLU A1130      -0.720  20.230  -1.964  1.00 26.06           C  
ANISOU 2834  C   GLU A1130     4001   3646   2254    487    -37     -1       C  
ATOM   2835  O   GLU A1130       0.082  19.564  -1.294  1.00 24.28           O  
ANISOU 2835  O   GLU A1130     3741   3531   1952    585    -55     30       O  
ATOM   2836  CB  GLU A1130      -0.055  21.759  -3.844  1.00 36.48           C  
ANISOU 2836  CB  GLU A1130     5266   5131   3465    351     18     36       C  
ATOM   2837  CG  GLU A1130       0.269  21.892  -5.336  1.00 35.59           C  
ANISOU 2837  CG  GLU A1130     5123   5122   3278    409     46     74       C  
ATOM   2838  CD  GLU A1130       0.194  23.324  -5.858  1.00 40.24           C  
ANISOU 2838  CD  GLU A1130     5762   5745   3781    240     94    186       C  
ATOM   2839  OE1 GLU A1130      -0.549  24.130  -5.268  1.00 40.95           O  
ANISOU 2839  OE1 GLU A1130     5933   5703   3921    177    105    207       O  
ATOM   2840  OE2 GLU A1130       0.868  23.650  -6.861  1.00 42.84           O  
ANISOU 2840  OE2 GLU A1130     6060   6229   3989    239    141    275       O  
ATOM   2841  N   ALA A1131      -1.767  20.860  -1.437  1.00 25.40           N  
ANISOU 2841  N   ALA A1131     3963   3449   2242    379    -28    -20       N  
ATOM   2842  CA  ALA A1131      -2.086  20.778  -0.014  1.00 21.37           C  
ANISOU 2842  CA  ALA A1131     3453   2956   1713    319    -33    -21       C  
ATOM   2843  C   ALA A1131      -2.257  19.327   0.435  1.00 25.06           C  
ANISOU 2843  C   ALA A1131     3989   3352   2179    470    -59     34       C  
ATOM   2844  O   ALA A1131      -1.676  18.901   1.437  1.00 31.35           O  
ANISOU 2844  O   ALA A1131     4752   4284   2876    487    -76     99       O  
ATOM   2845  CB  ALA A1131      -3.340  21.575   0.286  1.00 20.43           C  
ANISOU 2845  CB  ALA A1131     3386   2714   1661    258     -7    -66       C  
ATOM   2846  N   MET A1132      -3.047  18.570  -0.323  1.00 18.01           N  
ANISOU 2846  N   MET A1132     3237   2250   1355    589    -66     15       N  
ATOM   2847  CA  MET A1132      -3.283  17.161  -0.023  1.00 19.31           C  
ANISOU 2847  CA  MET A1132     3601   2262   1473    749    -83     55       C  
ATOM   2848  C   MET A1132      -1.991  16.354  -0.055  1.00 21.14           C  
ANISOU 2848  C   MET A1132     3854   2570   1607    991    -89     99       C  
ATOM   2849  O   MET A1132      -1.798  15.450   0.755  1.00 32.03           O  
ANISOU 2849  O   MET A1132     5318   3923   2931   1105    -89    221       O  
ATOM   2850  CB  MET A1132      -4.296  16.567  -1.005  1.00 24.81           C  
ANISOU 2850  CB  MET A1132     4518   2712   2197    790   -114    -17       C  
ATOM   2851  CG  MET A1132      -5.724  17.033  -0.777  1.00 25.92           C  
ANISOU 2851  CG  MET A1132     4648   2815   2385    598   -109    -20       C  
ATOM   2852  SD  MET A1132      -6.790  16.723  -2.197  1.00 22.44           S  
ANISOU 2852  SD  MET A1132     4290   2287   1949    560   -174   -114       S  
ATOM   2853  CE  MET A1132      -6.775  14.935  -2.244  1.00 21.79           C  
ANISOU 2853  CE  MET A1132     4566   1900   1812    618   -231   -176       C  
ATOM   2854  N   CYS A1133      -1.110  16.686  -0.994  1.00 30.33           N  
ANISOU 2854  N   CYS A1133     4909   3865   2751   1077    -87     42       N  
ATOM   2855  CA  CYS A1133       0.199  16.050  -1.064  1.00 28.68           C  
ANISOU 2855  CA  CYS A1133     4652   3827   2419   1362    -79     77       C  
ATOM   2856  C   CYS A1133       1.006  16.345   0.193  1.00 31.27           C  
ANISOU 2856  C   CYS A1133     4775   4431   2674   1283    -86    203       C  
ATOM   2857  O   CYS A1133       1.789  15.509   0.640  1.00 33.65           O  
ANISOU 2857  O   CYS A1133     5054   4854   2879   1546    -81    305       O  
ATOM   2858  CB  CYS A1133       0.966  16.506  -2.312  1.00 18.64           C  
ANISOU 2858  CB  CYS A1133     3229   2740   1113   1421    -70      6       C  
ATOM   2859  SG  CYS A1133       0.450  15.689  -3.849  1.00 36.68           S  
ANISOU 2859  SG  CYS A1133     5721   4828   3388   1648   -115   -119       S  
ATOM   2860  N   LEU A1134       0.812  17.529   0.768  1.00 28.76           N  
ANISOU 2860  N   LEU A1134     4332   4218   2379    938   -101    191       N  
ATOM   2861  CA  LEU A1134       1.548  17.880   1.980  1.00 28.31           C  
ANISOU 2861  CA  LEU A1134     4125   4432   2198    836   -133    259       C  
ATOM   2862  C   LEU A1134       0.756  17.609   3.257  1.00 30.66           C  
ANISOU 2862  C   LEU A1134     4489   4682   2478    749   -149    337       C  
ATOM   2863  O   LEU A1134       1.092  18.125   4.318  1.00 32.78           O  
ANISOU 2863  O   LEU A1134     4671   5157   2627    611   -178    343       O  
ATOM   2864  CB  LEU A1134       1.984  19.342   1.927  1.00 25.08           C  
ANISOU 2864  CB  LEU A1134     3632   4158   1740    543   -135    161       C  
ATOM   2865  CG  LEU A1134       3.195  19.504   1.011  1.00 33.64           C  
ANISOU 2865  CG  LEU A1134     4554   5473   2756    642   -122    157       C  
ATOM   2866  CD1 LEU A1134       3.263  20.907   0.472  1.00 37.87           C  
ANISOU 2866  CD1 LEU A1134     5117   5998   3272    369    -95     78       C  
ATOM   2867  CD2 LEU A1134       4.472  19.144   1.757  1.00 42.92           C  
ANISOU 2867  CD2 LEU A1134     5467   7069   3771    789   -151    232       C  
ATOM   2868  N   GLY A1135      -0.291  16.796   3.158  1.00 27.66           N  
ANISOU 2868  N   GLY A1135     4279   4044   2188    833   -128    390       N  
ATOM   2869  CA  GLY A1135      -1.016  16.357   4.340  1.00 26.27           C  
ANISOU 2869  CA  GLY A1135     4149   3861   1971    765   -135    527       C  
ATOM   2870  C   GLY A1135      -2.170  17.248   4.769  1.00 24.38           C  
ANISOU 2870  C   GLY A1135     3900   3616   1746    496   -111    434       C  
ATOM   2871  O   GLY A1135      -2.952  16.889   5.652  1.00 27.38           O  
ANISOU 2871  O   GLY A1135     4316   4015   2074    431   -101    545       O  
ATOM   2872  N   ALA A1136      -2.282  18.415   4.147  1.00 23.34           N  
ANISOU 2872  N   ALA A1136     3716   3476   1674    359    -91    253       N  
ATOM   2873  CA  ALA A1136      -3.361  19.340   4.475  1.00 26.28           C  
ANISOU 2873  CA  ALA A1136     4067   3854   2065    195    -47    147       C  
ATOM   2874  C   ALA A1136      -4.701  18.821   3.961  1.00 25.96           C  
ANISOU 2874  C   ALA A1136     4137   3587   2139    271    -19    170       C  
ATOM   2875  O   ALA A1136      -4.802  18.366   2.822  1.00 23.86           O  
ANISOU 2875  O   ALA A1136     3982   3105   1979    373    -31    152       O  
ATOM   2876  CB  ALA A1136      -3.073  20.723   3.904  1.00 23.50           C  
ANISOU 2876  CB  ALA A1136     3660   3523   1747     97    -22    -18       C  
ATOM   2877  N   ILE A1137      -5.726  18.894   4.804  1.00 26.61           N  
ANISOU 2877  N   ILE A1137     4208   3751   2152    193     18    194       N  
ATOM   2878  CA  ILE A1137      -7.059  18.432   4.430  1.00 27.28           C  
ANISOU 2878  CA  ILE A1137     4403   3676   2286    201     47    229       C  
ATOM   2879  C   ILE A1137      -7.883  19.575   3.847  1.00 26.97           C  
ANISOU 2879  C   ILE A1137     4334   3596   2317    181     77     66       C  
ATOM   2880  O   ILE A1137      -8.130  20.573   4.519  1.00 22.04           O  
ANISOU 2880  O   ILE A1137     3618   3123   1632    140    122    -34       O  
ATOM   2881  CB  ILE A1137      -7.810  17.828   5.628  1.00 29.92           C  
ANISOU 2881  CB  ILE A1137     4717   4180   2473    119     90    405       C  
ATOM   2882  CG1 ILE A1137      -6.961  16.751   6.306  1.00 30.59           C  
ANISOU 2882  CG1 ILE A1137     4828   4301   2495    146     50    643       C  
ATOM   2883  CG2 ILE A1137      -9.148  17.260   5.182  1.00 22.86           C  
ANISOU 2883  CG2 ILE A1137     3946   3135   1606     63    131    479       C  
ATOM   2884  CD1 ILE A1137      -7.640  16.102   7.493  1.00 27.06           C  
ANISOU 2884  CD1 ILE A1137     4377   4002   1903     13     82    892       C  
ATOM   2885  N   PRO A1138      -8.316  19.427   2.588  1.00 29.25           N  
ANISOU 2885  N   PRO A1138     4715   3692   2709    224     52     36       N  
ATOM   2886  CA  PRO A1138      -9.019  20.501   1.881  1.00 29.34           C  
ANISOU 2886  CA  PRO A1138     4691   3680   2776    251     68    -57       C  
ATOM   2887  C   PRO A1138     -10.486  20.659   2.281  1.00 29.94           C  
ANISOU 2887  C   PRO A1138     4746   3876   2753    232    125    -74       C  
ATOM   2888  O   PRO A1138     -11.201  19.675   2.469  1.00 30.79           O  
ANISOU 2888  O   PRO A1138     4905   4031   2763    155    132      9       O  
ATOM   2889  CB  PRO A1138      -8.908  20.075   0.418  1.00 27.48           C  
ANISOU 2889  CB  PRO A1138     4517   3308   2615    301      7    -58       C  
ATOM   2890  CG  PRO A1138      -8.874  18.589   0.478  1.00 31.33           C  
ANISOU 2890  CG  PRO A1138     5156   3698   3049    275    -28     -9       C  
ATOM   2891  CD  PRO A1138      -8.113  18.245   1.732  1.00 31.06           C  
ANISOU 2891  CD  PRO A1138     5108   3726   2966    269      0     79       C  
ATOM   2892  N   ILE A1139     -10.912  21.911   2.415  1.00 28.88           N  
ANISOU 2892  N   ILE A1139     4568   3787   2620    305    181   -171       N  
ATOM   2893  CA  ILE A1139     -12.321  22.253   2.549  1.00 29.62           C  
ANISOU 2893  CA  ILE A1139     4612   4027   2614    378    258   -212       C  
ATOM   2894  C   ILE A1139     -12.676  23.179   1.394  1.00 31.24           C  
ANISOU 2894  C   ILE A1139     4854   4132   2885    570    245   -241       C  
ATOM   2895  O   ILE A1139     -12.422  24.383   1.450  1.00 35.00           O  
ANISOU 2895  O   ILE A1139     5389   4483   3425    692    294   -306       O  
ATOM   2896  CB  ILE A1139     -12.631  22.936   3.890  1.00 28.37           C  
ANISOU 2896  CB  ILE A1139     4378   4033   2367    390    372   -319       C  
ATOM   2897  CG1 ILE A1139     -12.217  22.035   5.054  1.00 28.41           C  
ANISOU 2897  CG1 ILE A1139     4343   4206   2244    210    380   -239       C  
ATOM   2898  CG2 ILE A1139     -14.110  23.286   3.983  1.00 24.62           C  
ANISOU 2898  CG2 ILE A1139     3786   3766   1803    540    477   -358       C  
ATOM   2899  CD1 ILE A1139     -12.383  22.683   6.404  1.00 31.33           C  
ANISOU 2899  CD1 ILE A1139     4678   4738   2490    183    493   -364       C  
ATOM   2900  N   ALA A1140     -13.252  22.611   0.341  1.00 30.26           N  
ANISOU 2900  N   ALA A1140     4709   4073   2715    595    176   -186       N  
ATOM   2901  CA  ALA A1140     -13.400  23.337  -0.914  1.00 29.82           C  
ANISOU 2901  CA  ALA A1140     4677   3985   2670    794    134   -155       C  
ATOM   2902  C   ALA A1140     -14.825  23.338  -1.447  1.00 37.02           C  
ANISOU 2902  C   ALA A1140     5359   5189   3518    907    107   -119       C  
ATOM   2903  O   ALA A1140     -15.603  22.418  -1.192  1.00 41.54           O  
ANISOU 2903  O   ALA A1140     5757   5979   4048    725     77   -127       O  
ATOM   2904  CB  ALA A1140     -12.461  22.754  -1.953  1.00 21.95           C  
ANISOU 2904  CB  ALA A1140     3728   2869   1744    685     24   -113       C  
ATOM   2905  N   SER A1141     -15.155  24.386  -2.195  1.00 28.52           N  
ANISOU 2905  N   SER A1141     4247   4125   2466   1185    113    -44       N  
ATOM   2906  CA  SER A1141     -16.440  24.474  -2.874  1.00 35.13           C  
ANISOU 2906  CA  SER A1141     4794   5315   3238   1338     57     34       C  
ATOM   2907  C   SER A1141     -16.534  23.401  -3.949  1.00 36.53           C  
ANISOU 2907  C   SER A1141     4870   5699   3309   1129   -120     28       C  
ATOM   2908  O   SER A1141     -15.662  23.301  -4.812  1.00 39.74           O  
ANISOU 2908  O   SER A1141     5434   5980   3684   1113   -191     48       O  
ATOM   2909  CB  SER A1141     -16.632  25.860  -3.490  1.00 41.64           C  
ANISOU 2909  CB  SER A1141     5639   6067   4114   1743    101    184       C  
ATOM   2910  OG  SER A1141     -16.663  26.866  -2.494  1.00 48.06           O  
ANISOU 2910  OG  SER A1141     6565   6643   5053   1949    273    117       O  
ATOM   2911  N   ALA A1142     -17.593  22.601  -3.896  1.00 45.38           N  
ANISOU 2911  N   ALA A1142     5714   7165   4364    948   -182    -26       N  
ATOM   2912  CA  ALA A1142     -17.770  21.501  -4.835  1.00 24.03           C  
ANISOU 2912  CA  ALA A1142     2919   4642   1571    679   -354   -122       C  
ATOM   2913  C   ALA A1142     -18.042  22.005  -6.248  1.00 32.78           C  
ANISOU 2913  C   ALA A1142     3881   6057   2517    902   -481    -50       C  
ATOM   2914  O   ALA A1142     -19.139  21.825  -6.778  1.00 37.90           O  
ANISOU 2914  O   ALA A1142     4184   7187   3029    877   -589    -62       O  
ATOM   2915  CB  ALA A1142     -18.895  20.596  -4.376  1.00 26.37           C  
ANISOU 2915  CB  ALA A1142     2932   5233   1853    361   -382   -194       C  
ATOM   2916  N   VAL A1143     -17.040  22.639  -6.851  1.00 36.83           N  
ANISOU 2916  N   VAL A1143     4621   6320   3052   1088   -454     45       N  
ATOM   2917  CA  VAL A1143     -17.151  23.134  -8.219  1.00 37.46           C  
ANISOU 2917  CA  VAL A1143     4581   6575   3076   1234   -498    157       C  
ATOM   2918  C   VAL A1143     -15.927  22.752  -9.046  1.00 38.04           C  
ANISOU 2918  C   VAL A1143     4856   6422   3175   1095   -511     95       C  
ATOM   2919  O   VAL A1143     -14.846  22.529  -8.502  1.00 37.47           O  
ANISOU 2919  O   VAL A1143     5027   5992   3219    991   -446     42       O  
ATOM   2920  CB  VAL A1143     -17.318  24.668  -8.266  1.00 37.58           C  
ANISOU 2920  CB  VAL A1143     4598   6532   3150   1636   -377    426       C  
ATOM   2921  CG1 VAL A1143     -18.587  25.092  -7.547  1.00 40.03           C  
ANISOU 2921  CG1 VAL A1143     4662   7112   3436   1862   -344    487       C  
ATOM   2922  CG2 VAL A1143     -16.099  25.359  -7.672  1.00 28.39           C  
ANISOU 2922  CG2 VAL A1143     3784   4848   2153   1688   -241    485       C  
ATOM   2923  N   GLY A1144     -16.113  22.669 -10.361  1.00 44.22           N  
ANISOU 2923  N   GLY A1144     5497   7476   3830   1105   -584    103       N  
ATOM   2924  CA  GLY A1144     -15.026  22.423 -11.292  1.00 31.44           C  
ANISOU 2924  CA  GLY A1144     4005   5757   2184   1036   -581     66       C  
ATOM   2925  C   GLY A1144     -14.203  21.179 -11.017  1.00 31.67           C  
ANISOU 2925  C   GLY A1144     4223   5542   2270    779   -603   -182       C  
ATOM   2926  O   GLY A1144     -14.742  20.082 -10.873  1.00 35.51           O  
ANISOU 2926  O   GLY A1144     4689   6083   2720    572   -699   -410       O  
ATOM   2927  N   GLY A1145     -12.888  21.359 -10.942  1.00 26.78           N  
ANISOU 2927  N   GLY A1145     3774   4655   1748    789   -507   -132       N  
ATOM   2928  CA  GLY A1145     -11.972  20.252 -10.739  1.00 31.80           C  
ANISOU 2928  CA  GLY A1145     4558   5081   2446    624   -495   -322       C  
ATOM   2929  C   GLY A1145     -11.922  19.766  -9.304  1.00 33.06           C  
ANISOU 2929  C   GLY A1145     4836   4967   2758    517   -457   -381       C  
ATOM   2930  O   GLY A1145     -11.469  18.652  -9.036  1.00 41.28           O  
ANISOU 2930  O   GLY A1145     5982   5850   3852    394   -457   -547       O  
ATOM   2931  N   LEU A1146     -12.390  20.601  -8.381  1.00 21.98           N  
ANISOU 2931  N   LEU A1146     3422   3513   1417    598   -412   -245       N  
ATOM   2932  CA  LEU A1146     -12.386  20.260  -6.962  1.00 31.26           C  
ANISOU 2932  CA  LEU A1146     4700   4476   2702    515   -364   -276       C  
ATOM   2933  C   LEU A1146     -13.275  19.053  -6.674  1.00 34.51           C  
ANISOU 2933  C   LEU A1146     5119   4953   3040    315   -462   -462       C  
ATOM   2934  O   LEU A1146     -12.956  18.233  -5.813  1.00 37.79           O  
ANISOU 2934  O   LEU A1146     5687   5134   3538    196   -442   -527       O  
ATOM   2935  CB  LEU A1146     -12.833  21.461  -6.123  1.00 19.93           C  
ANISOU 2935  CB  LEU A1146     3253   3023   1298    670   -288   -133       C  
ATOM   2936  CG  LEU A1146     -11.896  22.671  -6.170  1.00 19.07           C  
ANISOU 2936  CG  LEU A1146     3222   2746   1277    815   -192      1       C  
ATOM   2937  CD1 LEU A1146     -12.467  23.844  -5.389  1.00 19.62           C  
ANISOU 2937  CD1 LEU A1146     3348   2760   1348   1012   -108     93       C  
ATOM   2938  CD2 LEU A1146     -10.520  22.298  -5.643  1.00 17.27           C  
ANISOU 2938  CD2 LEU A1146     3086   2299   1177    692   -144    -40       C  
ATOM   2939  N   ARG A1147     -14.386  18.949  -7.399  1.00 29.38           N  
ANISOU 2939  N   ARG A1147     4291   4624   2246    268   -582   -538       N  
ATOM   2940  CA  ARG A1147     -15.284  17.804  -7.271  1.00 34.60           C  
ANISOU 2940  CA  ARG A1147     4885   5401   2862    -22   -708   -771       C  
ATOM   2941  C   ARG A1147     -14.574  16.525  -7.689  1.00 36.83           C  
ANISOU 2941  C   ARG A1147     5401   5374   3219   -204   -749  -1008       C  
ATOM   2942  O   ARG A1147     -14.713  15.484  -7.047  1.00 42.42           O  
ANISOU 2942  O   ARG A1147     6232   5807   4078   -465   -760  -1133       O  
ATOM   2943  CB  ARG A1147     -16.543  17.993  -8.121  1.00 42.05           C  
ANISOU 2943  CB  ARG A1147     5484   6816   3679    -64   -817   -795       C  
ATOM   2944  CG  ARG A1147     -17.109  19.397  -8.118  1.00 43.42           C  
ANISOU 2944  CG  ARG A1147     5430   7284   3784    256   -760   -527       C  
ATOM   2945  CD  ARG A1147     -18.339  19.490  -9.008  1.00 47.05           C  
ANISOU 2945  CD  ARG A1147     5513   8257   4106    247   -865   -538       C  
ATOM   2946  NE  ARG A1147     -19.490  18.799  -8.433  1.00 48.82           N  
ANISOU 2946  NE  ARG A1147     5469   8766   4315    -70   -929   -658       N  
ATOM   2947  CZ  ARG A1147     -20.590  18.493  -9.113  1.00 48.27           C  
ANISOU 2947  CZ  ARG A1147     5057   9140   4144   -223  -1027   -742       C  
ATOM   2948  NH1 ARG A1147     -20.686  18.807 -10.398  1.00 42.23           N  
ANISOU 2948  NH1 ARG A1147     4195   8606   3246    -52  -1079   -730       N  
ATOM   2949  NH2 ARG A1147     -21.593  17.866  -8.511  1.00 55.58           N  
ANISOU 2949  NH2 ARG A1147     5720  10306   5091   -578  -1056   -825       N  
ATOM   2950  N   ASP A1148     -13.816  16.615  -8.777  1.00 32.53           N  
ANISOU 2950  N   ASP A1148     4883   4844   2632    -86   -714  -1006       N  
ATOM   2951  CA  ASP A1148     -13.085  15.473  -9.310  1.00 38.28           C  
ANISOU 2951  CA  ASP A1148     5762   5369   3414   -185   -693  -1239       C  
ATOM   2952  C   ASP A1148     -11.988  15.031  -8.352  1.00 35.32           C  
ANISOU 2952  C   ASP A1148     5539   4616   3265    -71   -580  -1198       C  
ATOM   2953  O   ASP A1148     -11.831  13.842  -8.078  1.00 33.23           O  
ANISOU 2953  O   ASP A1148     5439   4025   3163   -175   -591  -1371       O  
ATOM   2954  CB  ASP A1148     -12.480  15.813 -10.675  1.00 48.03           C  
ANISOU 2954  CB  ASP A1148     6949   6793   4509    -19   -686  -1217       C  
ATOM   2955  CG  ASP A1148     -13.511  16.335 -11.657  1.00 60.50           C  
ANISOU 2955  CG  ASP A1148     8316   8770   5900     11   -820  -1201       C  
ATOM   2956  OD1 ASP A1148     -14.693  15.944 -11.546  1.00 63.29           O  
ANISOU 2956  OD1 ASP A1148     8557   9256   6233   -165   -949  -1333       O  
ATOM   2957  OD2 ASP A1148     -13.136  17.138 -12.539  1.00 64.50           O  
ANISOU 2957  OD2 ASP A1148     8704   9506   6296    211   -788  -1056       O  
ATOM   2958  N   ILE A1149     -11.233  16.000  -7.845  1.00 36.21           N  
ANISOU 2958  N   ILE A1149     5636   4715   3409    136   -489   -924       N  
ATOM   2959  CA  ILE A1149     -10.113  15.713  -6.959  1.00 30.41           C  
ANISOU 2959  CA  ILE A1149     5050   3684   2819    248   -415   -806       C  
ATOM   2960  C   ILE A1149     -10.568  15.221  -5.588  1.00 33.71           C  
ANISOU 2960  C   ILE A1149     5650   3831   3326    122   -419   -748       C  
ATOM   2961  O   ILE A1149     -10.147  14.160  -5.131  1.00 37.87           O  
ANISOU 2961  O   ILE A1149     6385   4035   3969     91   -414   -775       O  
ATOM   2962  CB  ILE A1149      -9.224  16.953  -6.768  1.00 26.37           C  
ANISOU 2962  CB  ILE A1149     4439   3266   2315    411   -332   -565       C  
ATOM   2963  CG1 ILE A1149      -8.644  17.396  -8.112  1.00 20.20           C  
ANISOU 2963  CG1 ILE A1149     3541   2696   1438    497   -323   -577       C  
ATOM   2964  CG2 ILE A1149      -8.118  16.665  -5.764  1.00 24.71           C  
ANISOU 2964  CG2 ILE A1149     4346   2849   2192    494   -286   -453       C  
ATOM   2965  CD1 ILE A1149      -7.862  18.677  -8.044  1.00 31.84           C  
ANISOU 2965  CD1 ILE A1149     4933   4223   2940    584   -253   -375       C  
ATOM   2966  N   ILE A1150     -11.429  15.999  -4.940  1.00 34.71           N  
ANISOU 2966  N   ILE A1150     5712   4090   3384     51   -415   -644       N  
ATOM   2967  CA  ILE A1150     -11.856  15.702  -3.579  1.00 32.55           C  
ANISOU 2967  CA  ILE A1150     5549   3657   3160   -108   -373   -522       C  
ATOM   2968  C   ILE A1150     -13.041  14.743  -3.548  1.00 24.10           C  
ANISOU 2968  C   ILE A1150     4417   2537   2201   -453   -420   -595       C  
ATOM   2969  O   ILE A1150     -14.059  14.972  -4.200  1.00 43.86           O  
ANISOU 2969  O   ILE A1150     6704   5332   4631   -574   -494   -706       O  
ATOM   2970  CB  ILE A1150     -12.230  16.987  -2.818  1.00 19.24           C  
ANISOU 2970  CB  ILE A1150     3696   2214   1402    -20   -286   -353       C  
ATOM   2971  CG1 ILE A1150     -11.080  17.993  -2.884  1.00 16.96           C  
ANISOU 2971  CG1 ILE A1150     3358   1943   1144    216   -220   -271       C  
ATOM   2972  CG2 ILE A1150     -12.587  16.670  -1.375  1.00 20.65           C  
ANISOU 2972  CG2 ILE A1150     3858   2349   1639   -167   -192   -185       C  
ATOM   2973  CD1 ILE A1150     -11.383  19.309  -2.218  1.00 30.39           C  
ANISOU 2973  CD1 ILE A1150     4923   3772   2850    290   -134   -183       C  
ATOM   2974  N   THR A1151     -12.892  13.665  -2.787  1.00 34.04           N  
ANISOU 2974  N   THR A1151     5855   3444   3636   -621   -378   -503       N  
ATOM   2975  CA  THR A1151     -13.952  12.684  -2.617  1.00 42.46           C  
ANISOU 2975  CA  THR A1151     6891   4386   4856  -1034   -398   -523       C  
ATOM   2976  C   THR A1151     -14.366  12.615  -1.154  1.00 47.60           C  
ANISOU 2976  C   THR A1151     7473   5061   5552  -1185   -269   -181       C  
ATOM   2977  O   THR A1151     -14.088  13.529  -0.376  1.00 41.27           O  
ANISOU 2977  O   THR A1151     6578   4492   4609   -970   -183     -7       O  
ATOM   2978  CB  THR A1151     -13.508  11.283  -3.077  1.00 46.70           C  
ANISOU 2978  CB  THR A1151     7748   4386   5608  -1155   -447   -701       C  
ATOM   2979  OG1 THR A1151     -12.595  10.733  -2.118  1.00 32.49           O  
ANISOU 2979  OG1 THR A1151     6204   2200   3941  -1009   -350   -435       O  
ATOM   2980  CG2 THR A1151     -12.826  11.356  -4.435  1.00 31.93           C  
ANISOU 2980  CG2 THR A1151     5917   2570   3644   -892   -533  -1033       C  
ATOM   2981  N   ASN A1152     -15.032  11.529  -0.780  1.00 50.33           N  
ANISOU 2981  N   ASN A1152     7866   5174   6082  -1579   -250    -92       N  
ATOM   2982  CA  ASN A1152     -15.259  11.246   0.627  1.00 60.11           C  
ANISOU 2982  CA  ASN A1152     9084   6403   7351  -1726   -110    298       C  
ATOM   2983  C   ASN A1152     -13.984  10.657   1.224  1.00 66.46           C  
ANISOU 2983  C   ASN A1152    10228   6777   8244  -1491    -60    513       C  
ATOM   2984  O   ASN A1152     -13.171  10.077   0.502  1.00 69.92           O  
ANISOU 2984  O   ASN A1152    10942   6807   8819  -1334   -129    340       O  
ATOM   2985  CB  ASN A1152     -16.444  10.298   0.815  1.00 67.42           C  
ANISOU 2985  CB  ASN A1152     9919   7250   8449  -2284    -90    383       C  
ATOM   2986  CG  ASN A1152     -16.296   9.016   0.020  1.00 71.66           C  
ANISOU 2986  CG  ASN A1152    10775   7168   9286  -2538   -180    172       C  
ATOM   2987  OD1 ASN A1152     -15.645   8.070   0.462  1.00 73.43           O  
ANISOU 2987  OD1 ASN A1152    11242   6926   9731  -2413   -115    349       O  
ATOM   2988  ND2 ASN A1152     -16.901   8.979  -1.162  1.00 72.14           N  
ANISOU 2988  ND2 ASN A1152    10714   7351   9346  -2735   -320   -238       N  
ATOM   2989  N   GLU A1153     -13.808  10.832   2.532  1.00 67.37           N  
ANISOU 2989  N   GLU A1153    10295   7058   8245  -1427     59    881       N  
ATOM   2990  CA  GLU A1153     -12.602  10.404   3.250  1.00 67.48           C  
ANISOU 2990  CA  GLU A1153    10532   6841   8267  -1144    101   1146       C  
ATOM   2991  C   GLU A1153     -11.327  11.119   2.795  1.00 56.66           C  
ANISOU 2991  C   GLU A1153     9232   5535   6761   -700     37    961       C  
ATOM   2992  O   GLU A1153     -10.236  10.791   3.260  1.00 60.57           O  
ANISOU 2992  O   GLU A1153     9734   6007   7271   -404     47   1086       O  
ATOM   2993  CB  GLU A1153     -12.393   8.888   3.124  1.00 73.22           C  
ANISOU 2993  CB  GLU A1153    11426   7045   9350  -1184    101   1214       C  
ATOM   2994  CG  GLU A1153     -13.285   8.041   4.014  1.00 80.51           C  
ANISOU 2994  CG  GLU A1153    12263   7898  10428  -1522    216   1557       C  
ATOM   2995  CD  GLU A1153     -12.806   6.604   4.107  1.00 86.85           C  
ANISOU 2995  CD  GLU A1153    13256   8140  11601  -1451    253   1722       C  
ATOM   2996  OE1 GLU A1153     -11.826   6.260   3.410  1.00 84.64           O  
ANISOU 2996  OE1 GLU A1153    13148   7562  11447  -1145    173   1521       O  
ATOM   2997  OE2 GLU A1153     -13.402   5.821   4.876  1.00 92.86           O  
ANISOU 2997  OE2 GLU A1153    13984   8772  12528  -1688    382   2063       O  
ATOM   2998  N   THR A1154     -11.455  12.088   1.892  1.00 45.86           N  
ANISOU 2998  N   THR A1154     7721   4409   5293   -618    -28    628       N  
ATOM   2999  CA  THR A1154     -10.294  12.840   1.423  1.00 41.24           C  
ANISOU 2999  CA  THR A1154     7159   3930   4582   -260    -71    475       C  
ATOM   3000  C   THR A1154     -10.540  14.346   1.435  1.00 39.93           C  
ANISOU 3000  C   THR A1154     6756   4200   4215   -192    -54    361       C  
ATOM   3001  O   THR A1154      -9.819  15.102   0.784  1.00 37.30           O  
ANISOU 3001  O   THR A1154     6415   3953   3804     13    -91    205       O  
ATOM   3002  CB  THR A1154      -9.877  12.429  -0.008  1.00 42.29           C  
ANISOU 3002  CB  THR A1154     7436   3810   4822   -156   -166    171       C  
ATOM   3003  OG1 THR A1154     -10.931  12.735  -0.928  1.00 46.36           O  
ANISOU 3003  OG1 THR A1154     7815   4464   5336   -357   -227    -75       O  
ATOM   3004  CG2 THR A1154      -9.558  10.943  -0.079  1.00 45.99           C  
ANISOU 3004  CG2 THR A1154     8119   3822   5534   -160   -168    205       C  
ATOM   3005  N   GLY A1155     -11.559  14.780   2.170  1.00 41.80           N  
ANISOU 3005  N   GLY A1155     6803   4702   4376   -356     19    448       N  
ATOM   3006  CA  GLY A1155     -11.844  16.199   2.287  1.00 37.95           C  
ANISOU 3006  CA  GLY A1155     6129   4557   3734   -243     59    332       C  
ATOM   3007  C   GLY A1155     -13.304  16.536   2.522  1.00 38.06           C  
ANISOU 3007  C   GLY A1155     5898   4848   3713   -400    118    328       C  
ATOM   3008  O   GLY A1155     -14.161  15.653   2.566  1.00 43.06           O  
ANISOU 3008  O   GLY A1155     6468   5460   4433   -669    121    420       O  
ATOM   3009  N   ILE A1156     -13.582  17.828   2.677  1.00 36.14           N  
ANISOU 3009  N   ILE A1156     5513   4863   3356   -230    173    218       N  
ATOM   3010  CA  ILE A1156     -14.938  18.310   2.909  1.00 35.21           C  
ANISOU 3010  CA  ILE A1156     5120   5079   3179   -269    246    197       C  
ATOM   3011  C   ILE A1156     -15.396  19.200   1.754  1.00 35.96           C  
ANISOU 3011  C   ILE A1156     5115   5242   3307    -86    185     35       C  
ATOM   3012  O   ILE A1156     -14.688  20.127   1.359  1.00 35.53           O  
ANISOU 3012  O   ILE A1156     5179   5067   3253    149    173    -54       O  
ATOM   3013  CB  ILE A1156     -15.042  19.096   4.232  1.00 32.85           C  
ANISOU 3013  CB  ILE A1156     4720   5064   2697   -153    396    204       C  
ATOM   3014  CG1 ILE A1156     -14.418  18.300   5.382  1.00 22.68           C  
ANISOU 3014  CG1 ILE A1156     3527   3785   1306   -285    445    409       C  
ATOM   3015  CG2 ILE A1156     -16.492  19.441   4.536  1.00 35.09           C  
ANISOU 3015  CG2 ILE A1156     4679   5751   2901   -164    497    195       C  
ATOM   3016  CD1 ILE A1156     -14.429  19.027   6.707  1.00 23.83           C  
ANISOU 3016  CD1 ILE A1156     3568   4183   1303   -160    558    350       C  
ATOM   3017  N   LEU A1157     -16.579  18.915   1.216  1.00 38.24           N  
ANISOU 3017  N   LEU A1157     5166   5753   3611   -210    144     29       N  
ATOM   3018  CA  LEU A1157     -17.095  19.659   0.068  1.00 39.03           C  
ANISOU 3018  CA  LEU A1157     5125   6003   3701    -15     66    -66       C  
ATOM   3019  C   LEU A1157     -18.295  20.531   0.436  1.00 37.40           C  
ANISOU 3019  C   LEU A1157     4592   6211   3407    170    163    -55       C  
ATOM   3020  O   LEU A1157     -19.169  20.121   1.201  1.00 40.91           O  
ANISOU 3020  O   LEU A1157     4795   6957   3792     -5    245      7       O  
ATOM   3021  CB  LEU A1157     -17.463  18.697  -1.064  1.00 37.94           C  
ANISOU 3021  CB  LEU A1157     4930   5881   3605   -258    -95   -131       C  
ATOM   3022  CG  LEU A1157     -16.256  18.052  -1.750  1.00 34.26           C  
ANISOU 3022  CG  LEU A1157     4785   5020   3210   -299   -192   -211       C  
ATOM   3023  CD1 LEU A1157     -16.682  16.910  -2.655  1.00 37.52           C  
ANISOU 3023  CD1 LEU A1157     5170   5416   3669   -600   -333   -353       C  
ATOM   3024  CD2 LEU A1157     -15.477  19.097  -2.534  1.00 22.72           C  
ANISOU 3024  CD2 LEU A1157     3430   3512   1693     39   -218   -243       C  
ATOM   3025  N   VAL A1158     -18.321  21.740  -0.120  1.00 36.72           N  
ANISOU 3025  N   VAL A1158     4495   6142   3316    545    168    -91       N  
ATOM   3026  CA  VAL A1158     -19.299  22.759   0.256  1.00 39.18           C  
ANISOU 3026  CA  VAL A1158     4553   6765   3570    865    285    -93       C  
ATOM   3027  C   VAL A1158     -19.990  23.369  -0.965  1.00 41.65           C  
ANISOU 3027  C   VAL A1158     4664   7297   3864   1144    189    -36       C  
ATOM   3028  O   VAL A1158     -19.391  23.478  -2.035  1.00 44.61           O  
ANISOU 3028  O   VAL A1158     5200   7483   4267   1196     68     -1       O  
ATOM   3029  CB  VAL A1158     -18.626  23.897   1.066  1.00 36.70           C  
ANISOU 3029  CB  VAL A1158     4475   6179   3292   1155    436   -185       C  
ATOM   3030  CG1 VAL A1158     -19.664  24.828   1.674  1.00 41.35           C  
ANISOU 3030  CG1 VAL A1158     4821   7065   3825   1506    595   -246       C  
ATOM   3031  CG2 VAL A1158     -17.733  23.328   2.151  1.00 35.65           C  
ANISOU 3031  CG2 VAL A1158     4544   5879   3122    899    492   -229       C  
ATOM   3032  N   LYS A1159     -21.254  23.756  -0.803  1.00 44.67           N  
ANISOU 3032  N   LYS A1159     4659   8150   4164   1345    247     -2       N  
ATOM   3033  CA  LYS A1159     -21.955  24.541  -1.814  1.00 50.24           C  
ANISOU 3033  CA  LYS A1159     5138   9123   4826   1739    177    101       C  
ATOM   3034  C   LYS A1159     -21.256  25.886  -2.002  1.00 51.42           C  
ANISOU 3034  C   LYS A1159     5617   8815   5106   2200    258    148       C  
ATOM   3035  O   LYS A1159     -21.014  26.609  -1.036  1.00 53.72           O  
ANISOU 3035  O   LYS A1159     6081   8846   5485   2395    436     46       O  
ATOM   3036  CB  LYS A1159     -23.419  24.752  -1.417  1.00 52.86           C  
ANISOU 3036  CB  LYS A1159     4955  10091   5037   1930    255    132       C  
ATOM   3037  CG  LYS A1159     -24.171  25.735  -2.302  1.00 55.24           C  
ANISOU 3037  CG  LYS A1159     5071  10630   5289   2420    202    281       C  
ATOM   3038  CD  LYS A1159     -25.509  26.112  -1.687  1.00 61.14           C  
ANISOU 3038  CD  LYS A1159     5508  11792   5929   2573    293    293       C  
ATOM   3039  CE  LYS A1159     -26.196  27.213  -2.479  1.00 62.18           C  
ANISOU 3039  CE  LYS A1159     5617  11986   6024   3029    272    456       C  
ATOM   3040  NZ  LYS A1159     -27.444  27.683  -1.811  1.00 62.18           N  
ANISOU 3040  NZ  LYS A1159     5330  12369   5927   3264    373    455       N  
ATOM   3041  N   ALA A1160     -20.929  26.215  -3.247  1.00 48.97           N  
ANISOU 3041  N   ALA A1160     5396   8414   4798   2346    131    297       N  
ATOM   3042  CA  ALA A1160     -20.192  27.438  -3.545  1.00 47.15           C  
ANISOU 3042  CA  ALA A1160     5509   7688   4719   2693    206    407       C  
ATOM   3043  C   ALA A1160     -21.058  28.680  -3.366  1.00 53.22           C  
ANISOU 3043  C   ALA A1160     6247   8418   5556   3024    322    480       C  
ATOM   3044  O   ALA A1160     -22.264  28.647  -3.604  1.00 57.31           O  
ANISOU 3044  O   ALA A1160     6407   9427   5940   3161    289    553       O  
ATOM   3045  CB  ALA A1160     -19.637  27.386  -4.956  1.00 33.89           C  
ANISOU 3045  CB  ALA A1160     3938   5959   2981   2617     59    581       C  
ATOM   3046  N   GLY A1161     -20.430  29.772  -2.941  1.00 56.37           N  
ANISOU 3046  N   GLY A1161     7008   8240   6170   3125    447    445       N  
ATOM   3047  CA  GLY A1161     -21.119  31.039  -2.776  1.00 66.98           C  
ANISOU 3047  CA  GLY A1161     8369   9437   7642   3463    553    492       C  
ATOM   3048  C   GLY A1161     -22.074  31.050  -1.600  1.00 74.24           C  
ANISOU 3048  C   GLY A1161     9067  10621   8518   3586    654    295       C  
ATOM   3049  O   GLY A1161     -23.027  31.829  -1.570  1.00 84.29           O  
ANISOU 3049  O   GLY A1161    10206  12004   9817   3926    715    346       O  
ATOM   3050  N   ASP A1162     -21.818  30.183  -0.626  1.00 63.03           N  
ANISOU 3050  N   ASP A1162     7599   9331   7019   3311    681     81       N  
ATOM   3051  CA  ASP A1162     -22.668  30.085   0.556  1.00 64.23           C  
ANISOU 3051  CA  ASP A1162     7514   9806   7083   3352    789    -99       C  
ATOM   3052  C   ASP A1162     -21.819  30.058   1.824  1.00 61.49           C  
ANISOU 3052  C   ASP A1162     7407   9158   6797   3111    895   -375       C  
ATOM   3053  O   ASP A1162     -21.315  29.004   2.212  1.00 61.68           O  
ANISOU 3053  O   ASP A1162     7413   9315   6706   2765    867   -425       O  
ATOM   3054  CB  ASP A1162     -23.555  28.838   0.476  1.00 68.22           C  
ANISOU 3054  CB  ASP A1162     7550  11036   7337   3172    710    -29       C  
ATOM   3055  CG  ASP A1162     -24.715  28.877   1.458  1.00 76.40           C  
ANISOU 3055  CG  ASP A1162     8259  12522   8248   3260    815   -121       C  
ATOM   3056  OD1 ASP A1162     -24.487  29.180   2.649  1.00 77.76           O  
ANISOU 3056  OD1 ASP A1162     8566  12523   8458   3238    953   -331       O  
ATOM   3057  OD2 ASP A1162     -25.859  28.605   1.034  1.00 80.33           O  
ANISOU 3057  OD2 ASP A1162     8349  13588   8585   3331    754     11       O  
ATOM   3058  N   PRO A1163     -21.660  31.224   2.471  1.00 56.02           N  
ANISOU 3058  N   PRO A1163     7041   8930   5314   1519    918  -1029       N  
ATOM   3059  CA  PRO A1163     -20.868  31.365   3.700  1.00 52.79           C  
ANISOU 3059  CA  PRO A1163     6766   8437   4857   1390    993  -1021       C  
ATOM   3060  C   PRO A1163     -21.369  30.490   4.851  1.00 57.32           C  
ANISOU 3060  C   PRO A1163     7273   9183   5325   1292   1119  -1005       C  
ATOM   3061  O   PRO A1163     -20.570  30.066   5.687  1.00 62.88           O  
ANISOU 3061  O   PRO A1163     8094   9826   5970   1153   1146   -964       O  
ATOM   3062  CB  PRO A1163     -21.023  32.851   4.045  1.00 44.08           C  
ANISOU 3062  CB  PRO A1163     5718   7262   3768   1486   1041  -1100       C  
ATOM   3063  CG  PRO A1163     -21.326  33.509   2.748  1.00 47.97           C  
ANISOU 3063  CG  PRO A1163     6182   7700   4344   1639    941  -1116       C  
ATOM   3064  CD  PRO A1163     -22.162  32.523   1.990  1.00 52.29           C  
ANISOU 3064  CD  PRO A1163     6558   8421   4890   1693    897  -1093       C  
ATOM   3065  N   GLY A1164     -22.672  30.225   4.887  1.00 55.70           N  
ANISOU 3065  N   GLY A1164     6873   9199   5091   1358   1195  -1035       N  
ATOM   3066  CA  GLY A1164     -23.258  29.424   5.948  1.00 41.06           C  
ANISOU 3066  CA  GLY A1164     4938   7523   3139   1254   1335  -1017       C  
ATOM   3067  C   GLY A1164     -22.787  27.982   5.939  1.00 51.40           C  
ANISOU 3067  C   GLY A1164     6276   8852   4402   1088   1311   -919       C  
ATOM   3068  O   GLY A1164     -22.305  27.468   6.952  1.00 53.96           O  
ANISOU 3068  O   GLY A1164     6712   9150   4642    957   1375   -869       O  
ATOM   3069  N   GLU A1165     -22.925  27.327   4.790  1.00 53.47           N  
ANISOU 3069  N   GLU A1165     6450   9157   4709   1095   1220   -891       N  
ATOM   3070  CA  GLU A1165     -22.516  25.934   4.650  1.00 58.65           C  
ANISOU 3070  CA  GLU A1165     7142   9823   5321    937   1200   -797       C  
ATOM   3071  C   GLU A1165     -21.000  25.804   4.799  1.00 51.57           C  
ANISOU 3071  C   GLU A1165     6487   8676   4431    863   1120   -733       C  
ATOM   3072  O   GLU A1165     -20.495  24.777   5.261  1.00 45.68           O  
ANISOU 3072  O   GLU A1165     5832   7906   3619    723   1138   -646       O  
ATOM   3073  CB  GLU A1165     -22.979  25.373   3.303  1.00 59.30           C  
ANISOU 3073  CB  GLU A1165     7088   9997   5446    963   1118   -797       C  
ATOM   3074  CG  GLU A1165     -22.812  23.866   3.164  1.00 65.53           C  
ANISOU 3074  CG  GLU A1165     7890  10834   6173    778   1127   -702       C  
ATOM   3075  CD  GLU A1165     -23.454  23.320   1.905  1.00 70.86           C  
ANISOU 3075  CD  GLU A1165     8407  11651   6868    779   1069   -720       C  
ATOM   3076  OE1 GLU A1165     -24.612  23.695   1.618  1.00 75.14           O  
ANISOU 3076  OE1 GLU A1165     8708  12414   7429    860   1098   -802       O  
ATOM   3077  OE2 GLU A1165     -22.799  22.519   1.202  1.00 68.77           O  
ANISOU 3077  OE2 GLU A1165     8256  11277   6597    699    993   -656       O  
ATOM   3078  N   LEU A1166     -20.282  26.855   4.415  1.00 43.99           N  
ANISOU 3078  N   LEU A1166     5626   7536   3553    952   1034   -773       N  
ATOM   3079  CA  LEU A1166     -18.837  26.905   4.604  1.00 49.47           C  
ANISOU 3079  CA  LEU A1166     6508   8020   4267    876    964   -730       C  
ATOM   3080  C   LEU A1166     -18.502  26.919   6.091  1.00 50.19           C  
ANISOU 3080  C   LEU A1166     6693   8121   4258    783   1053   -720       C  
ATOM   3081  O   LEU A1166     -17.637  26.169   6.550  1.00 54.82           O  
ANISOU 3081  O   LEU A1166     7391   8645   4794    669   1030   -647       O  
ATOM   3082  CB  LEU A1166     -18.239  28.132   3.911  1.00 51.80           C  
ANISOU 3082  CB  LEU A1166     6861   8149   4672    968    876   -781       C  
ATOM   3083  CG  LEU A1166     -16.734  28.348   4.096  1.00 30.14           C  
ANISOU 3083  CG  LEU A1166     4267   5221   1962    881    811   -752       C  
ATOM   3084  CD1 LEU A1166     -15.959  27.095   3.717  1.00 28.78           C  
ANISOU 3084  CD1 LEU A1166     4143   4999   1793    786    746   -661       C  
ATOM   3085  CD2 LEU A1166     -16.257  29.540   3.281  1.00 39.83           C  
ANISOU 3085  CD2 LEU A1166     5522   6324   3288    982    732   -796       C  
ATOM   3086  N   ALA A1167     -19.197  27.774   6.836  1.00 49.28           N  
ANISOU 3086  N   ALA A1167     6537   8082   4104    840   1152   -794       N  
ATOM   3087  CA  ALA A1167     -19.024  27.857   8.281  1.00 47.22           C  
ANISOU 3087  CA  ALA A1167     6372   7841   3729    760   1252   -796       C  
ATOM   3088  C   ALA A1167     -19.325  26.514   8.939  1.00 38.73           C  
ANISOU 3088  C   ALA A1167     5291   6880   2543    646   1325   -709       C  
ATOM   3089  O   ALA A1167     -18.596  26.071   9.830  1.00 43.13           O  
ANISOU 3089  O   ALA A1167     5991   7388   3010    544   1334   -655       O  
ATOM   3090  CB  ALA A1167     -19.912  28.945   8.861  1.00 39.70           C  
ANISOU 3090  CB  ALA A1167     5365   6964   2756    851   1367   -894       C  
ATOM   3091  N   ASN A1168     -20.397  25.868   8.490  1.00 39.00           N  
ANISOU 3091  N   ASN A1168     5160   7076   2581    657   1376   -694       N  
ATOM   3092  CA  ASN A1168     -20.761  24.553   9.004  1.00 49.16           C  
ANISOU 3092  CA  ASN A1168     6432   8477   3770    528   1456   -603       C  
ATOM   3093  C   ASN A1168     -19.683  23.509   8.718  1.00 46.84           C  
ANISOU 3093  C   ASN A1168     6283   8051   3464    428   1356   -493       C  
ATOM   3094  O   ASN A1168     -19.377  22.667   9.568  1.00 44.06           O  
ANISOU 3094  O   ASN A1168     6044   7690   3005    320   1402   -405       O  
ATOM   3095  CB  ASN A1168     -22.099  24.104   8.414  1.00 53.76           C  
ANISOU 3095  CB  ASN A1168     6775   9275   4375    533   1521   -617       C  
ATOM   3096  CG  ASN A1168     -23.274  24.879   8.983  1.00 58.52           C  
ANISOU 3096  CG  ASN A1168     7223  10047   4967    608   1658   -708       C  
ATOM   3097  OD1 ASN A1168     -23.095  25.816   9.762  1.00 58.40           O  
ANISOU 3097  OD1 ASN A1168     7297   9966   4926    667   1705   -765       O  
ATOM   3098  ND2 ASN A1168     -24.484  24.493   8.593  1.00 61.19           N  
ANISOU 3098  ND2 ASN A1168     7318  10606   5323    596   1725   -727       N  
ATOM   3099  N   ALA A1169     -19.105  23.574   7.523  1.00 49.12           N  
ANISOU 3099  N   ALA A1169     6577   8228   3858    475   1222   -495       N  
ATOM   3100  CA  ALA A1169     -18.021  22.671   7.152  1.00 43.75           C  
ANISOU 3100  CA  ALA A1169     6033   7406   3184    397   1125   -400       C  
ATOM   3101  C   ALA A1169     -16.801  22.899   8.037  1.00 46.06           C  
ANISOU 3101  C   ALA A1169     6498   7570   3434    354   1083   -378       C  
ATOM   3102  O   ALA A1169     -16.113  21.950   8.419  1.00 46.93           O  
ANISOU 3102  O   ALA A1169     6729   7624   3479    263   1058   -282       O  
ATOM   3103  CB  ALA A1169     -17.657  22.851   5.694  1.00 37.23           C  
ANISOU 3103  CB  ALA A1169     5178   6483   2486    465   1001   -420       C  
ATOM   3104  N   ILE A1170     -16.538  24.162   8.358  1.00 45.40           N  
ANISOU 3104  N   ILE A1170     6423   7447   3382    416   1074   -468       N  
ATOM   3105  CA  ILE A1170     -15.434  24.513   9.246  1.00 44.13           C  
ANISOU 3105  CA  ILE A1170     6398   7201   3168    365   1038   -466       C  
ATOM   3106  C   ILE A1170     -15.673  23.947  10.645  1.00 47.72           C  
ANISOU 3106  C   ILE A1170     6942   7733   3455    287   1139   -416       C  
ATOM   3107  O   ILE A1170     -14.759  23.403  11.273  1.00 49.74           O  
ANISOU 3107  O   ILE A1170     7328   7938   3633    211   1092   -347       O  
ATOM   3108  CB  ILE A1170     -15.238  26.041   9.323  1.00 39.05           C  
ANISOU 3108  CB  ILE A1170     5748   6509   2579    433   1031   -578       C  
ATOM   3109  CG1 ILE A1170     -14.765  26.583   7.973  1.00 34.23           C  
ANISOU 3109  CG1 ILE A1170     5084   5795   2127    504    920   -609       C  
ATOM   3110  CG2 ILE A1170     -14.237  26.403  10.408  1.00 37.26           C  
ANISOU 3110  CG2 ILE A1170     5644   6256   2256    377   1011   -584       C  
ATOM   3111  CD1 ILE A1170     -14.540  28.080   7.958  1.00 34.46           C  
ANISOU 3111  CD1 ILE A1170     5106   5793   2193    598    907   -707       C  
ATOM   3112  N   LEU A1171     -16.909  24.067  11.121  1.00 43.35           N  
ANISOU 3112  N   LEU A1171     6312   7312   2846    311   1279   -448       N  
ATOM   3113  CA  LEU A1171     -17.289  23.495  12.409  1.00 47.59           C  
ANISOU 3113  CA  LEU A1171     6928   7930   3223    242   1400   -395       C  
ATOM   3114  C   LEU A1171     -17.083  21.982  12.424  1.00 46.67           C  
ANISOU 3114  C   LEU A1171     6883   7806   3045    153   1388   -254       C  
ATOM   3115  O   LEU A1171     -16.579  21.425  13.406  1.00 47.81           O  
ANISOU 3115  O   LEU A1171     7185   7919   3061     92   1401   -178       O  
ATOM   3116  CB  LEU A1171     -18.744  23.832  12.743  1.00 55.14           C  
ANISOU 3116  CB  LEU A1171     7745   9053   4154    281   1564   -453       C  
ATOM   3117  CG  LEU A1171     -19.005  25.232  13.303  1.00 60.20           C  
ANISOU 3117  CG  LEU A1171     8383   9702   4788    355   1629   -576       C  
ATOM   3118  CD1 LEU A1171     -20.496  25.477  13.471  1.00 65.26           C  
ANISOU 3118  CD1 LEU A1171     8851  10520   5423    406   1791   -633       C  
ATOM   3119  CD2 LEU A1171     -18.280  25.417  14.627  1.00 61.00           C  
ANISOU 3119  CD2 LEU A1171     8689   9744   4745    297   1654   -566       C  
ATOM   3120  N   LYS A1172     -17.467  21.320  11.335  1.00 46.05           N  
ANISOU 3120  N   LYS A1172     6703   7747   3049    149   1362   -216       N  
ATOM   3121  CA  LYS A1172     -17.257  19.880  11.233  1.00 45.94           C  
ANISOU 3121  CA  LYS A1172     6771   7699   2984     64   1353    -78       C  
ATOM   3122  C   LYS A1172     -15.772  19.547  11.258  1.00 47.12           C  
ANISOU 3122  C   LYS A1172     7098   7678   3127     39   1213    -18       C  
ATOM   3123  O   LYS A1172     -15.359  18.572  11.886  1.00 51.34           O  
ANISOU 3123  O   LYS A1172     7782   8167   3558    -20   1219     96       O  
ATOM   3124  CB  LYS A1172     -17.888  19.309   9.964  1.00 42.24           C  
ANISOU 3124  CB  LYS A1172     6167   7278   2605     52   1342    -59       C  
ATOM   3125  CG  LYS A1172     -17.728  17.799   9.870  1.00 43.54           C  
ANISOU 3125  CG  LYS A1172     6432   7397   2714    -43   1349     92       C  
ATOM   3126  CD  LYS A1172     -18.282  17.236   8.582  1.00 57.14           C  
ANISOU 3126  CD  LYS A1172     8034   9161   4515    -80   1331    108       C  
ATOM   3127  CE  LYS A1172     -18.335  15.718   8.644  1.00 66.77           C  
ANISOU 3127  CE  LYS A1172     9344  10357   5670   -197   1371    266       C  
ATOM   3128  NZ  LYS A1172     -19.092  15.246   9.840  1.00 66.73           N  
ANISOU 3128  NZ  LYS A1172     9324  10481   5549   -295   1523    324       N  
ATOM   3129  N   ALA A1173     -14.974  20.359  10.572  1.00 43.39           N  
ANISOU 3129  N   ALA A1173     6593   7123   2769     84   1089    -92       N  
ATOM   3130  CA  ALA A1173     -13.527  20.180  10.569  1.00 37.08           C  
ANISOU 3130  CA  ALA A1173     5894   6213   1981     47    950    -51       C  
ATOM   3131  C   ALA A1173     -12.977  20.291  11.986  1.00 44.39           C  
ANISOU 3131  C   ALA A1173     6949   7152   2767      5    958    -31       C  
ATOM   3132  O   ALA A1173     -12.062  19.558  12.366  1.00 38.62           O  
ANISOU 3132  O   ALA A1173     6301   6375   1997    -49    870     60       O  
ATOM   3133  CB  ALA A1173     -12.868  21.197   9.661  1.00 35.10           C  
ANISOU 3133  CB  ALA A1173     5551   5903   1882    115    844   -140       C  
ATOM   3134  N   LEU A1174     -13.545  21.205  12.765  1.00 44.78           N  
ANISOU 3134  N   LEU A1174     6989   7268   2759     37   1051   -114       N  
ATOM   3135  CA  LEU A1174     -13.169  21.341  14.167  1.00 45.54           C  
ANISOU 3135  CA  LEU A1174     7210   7382   2713      4   1068    -99       C  
ATOM   3136  C   LEU A1174     -13.549  20.093  14.958  1.00 51.51           C  
ANISOU 3136  C   LEU A1174     8071   8160   3342    -38   1140     28       C  
ATOM   3137  O   LEU A1174     -12.799  19.648  15.828  1.00 57.03           O  
ANISOU 3137  O   LEU A1174     8897   8827   3944    -75   1082     98       O  
ATOM   3138  CB  LEU A1174     -13.827  22.574  14.789  1.00 47.13           C  
ANISOU 3138  CB  LEU A1174     7391   7645   2871     48   1177   -219       C  
ATOM   3139  CG  LEU A1174     -13.632  22.706  16.301  1.00 50.08           C  
ANISOU 3139  CG  LEU A1174     7903   8044   3082     20   1217   -206       C  
ATOM   3140  CD1 LEU A1174     -12.171  22.940  16.643  1.00 49.52           C  
ANISOU 3140  CD1 LEU A1174     7910   7910   2993    -17   1058   -197       C  
ATOM   3141  CD2 LEU A1174     -14.499  23.809  16.871  1.00 50.96           C  
ANISOU 3141  CD2 LEU A1174     7994   8221   3149     63   1356   -319       C  
ATOM   3142  N   GLU A1175     -14.713  19.528  14.653  1.00 47.47           N  
ANISOU 3142  N   GLU A1175     7500   7712   2825    -27   1270     62       N  
ATOM   3143  CA  GLU A1175     -15.181  18.343  15.368  1.00 52.34           C  
ANISOU 3143  CA  GLU A1175     8200   8362   3323    -51   1366    194       C  
ATOM   3144  C   GLU A1175     -14.430  17.078  14.950  1.00 44.56           C  
ANISOU 3144  C   GLU A1175     7303   7260   2368    -75   1262    328       C  
ATOM   3145  O   GLU A1175     -14.476  16.063  15.645  1.00 46.23           O  
ANISOU 3145  O   GLU A1175     7615   7471   2479    -61   1309    460       O  
ATOM   3146  CB  GLU A1175     -16.684  18.154  15.157  1.00 61.14           C  
ANISOU 3146  CB  GLU A1175     9182   9629   4421    -56   1551    191       C  
ATOM   3147  CG  GLU A1175     -17.526  19.301  15.699  1.00 71.24           C  
ANISOU 3147  CG  GLU A1175    10355  11030   5682    -30   1666     64       C  
ATOM   3148  CD  GLU A1175     -17.308  19.537  17.183  1.00 78.60           C  
ANISOU 3148  CD  GLU A1175    11448  11974   6444    -23   1729     76       C  
ATOM   3149  OE1 GLU A1175     -17.189  18.547  17.936  1.00 81.49           O  
ANISOU 3149  OE1 GLU A1175    11923  12344   6697    -46   1755    206       O  
ATOM   3150  OE2 GLU A1175     -17.251  20.716  17.596  1.00 78.53           O  
ANISOU 3150  OE2 GLU A1175    11443  11970   6426     14   1739    -42       O  
ATOM   3151  N   LEU A1176     -13.740  17.143  13.816  1.00 47.12           N  
ANISOU 3151  N   LEU A1176     7580   7495   2830    -96   1126    300       N  
ATOM   3152  CA  LEU A1176     -12.941  16.018  13.342  1.00 40.20           C  
ANISOU 3152  CA  LEU A1176     6779   6499   1995   -145   1018    409       C  
ATOM   3153  C   LEU A1176     -11.531  16.061  13.917  1.00 51.82           C  
ANISOU 3153  C   LEU A1176     8306   7952   3431   -227    855    428       C  
ATOM   3154  O   LEU A1176     -10.867  15.032  14.038  1.00 52.37           O  
ANISOU 3154  O   LEU A1176     8420   8006   3474   -326    766    542       O  
ATOM   3155  CB  LEU A1176     -12.879  16.006  11.813  1.00 38.04           C  
ANISOU 3155  CB  LEU A1176     6390   6185   1876   -158    948    377       C  
ATOM   3156  CG  LEU A1176     -14.121  15.516  11.069  1.00 41.08           C  
ANISOU 3156  CG  LEU A1176     6713   6607   2289   -107   1075    407       C  
ATOM   3157  CD1 LEU A1176     -13.970  15.743   9.574  1.00 36.14           C  
ANISOU 3157  CD1 LEU A1176     5990   5937   1807   -115    989    349       C  
ATOM   3158  CD2 LEU A1176     -14.372  14.045  11.362  1.00 43.08           C  
ANISOU 3158  CD2 LEU A1176     7040   6851   2479    -58   1145    589       C  
ATOM   3159  N   SER A1177     -11.082  17.260  14.275  1.00 52.94           N  
ANISOU 3159  N   SER A1177     8399   8148   3567   -193    813    328       N  
ATOM   3160  CA  SER A1177      -9.736  17.458  14.801  1.00 51.80           C  
ANISOU 3160  CA  SER A1177     8271   8026   3383   -217    667    349       C  
ATOM   3161  C   SER A1177      -9.598  16.952  16.235  1.00 59.26           C  
ANISOU 3161  C   SER A1177     9377   8990   4149   -266    682    425       C  
ATOM   3162  O   SER A1177      -8.530  17.055  16.839  1.00 62.22           O  
ANISOU 3162  O   SER A1177     9778   9405   4459   -282    563    455       O  
ATOM   3163  CB  SER A1177      -9.353  18.936  14.732  1.00 43.03           C  
ANISOU 3163  CB  SER A1177     7090   6940   2320   -152    637    214       C  
ATOM   3164  OG  SER A1177     -10.288  19.725  15.445  1.00 43.61           O  
ANISOU 3164  OG  SER A1177     7201   7047   2322   -128    769    127       O  
ATOM   3165  N   ARG A1178     -10.684  16.412  16.777  1.00 57.71           N  
ANISOU 3165  N   ARG A1178     9299   8760   3868   -247    840    464       N  
ATOM   3166  CA  ARG A1178     -10.658  15.815  18.105  1.00 54.05           C  
ANISOU 3166  CA  ARG A1178     9027   8282   3229   -240    882    552       C  
ATOM   3167  C   ARG A1178     -10.301  14.336  18.000  1.00 54.66           C  
ANISOU 3167  C   ARG A1178     9179   8301   3289   -360    818    698       C  
ATOM   3168  O   ARG A1178     -10.391  13.590  18.975  1.00 57.67           O  
ANISOU 3168  O   ARG A1178     9777   8600   3536   -223    894    804       O  
ATOM   3169  CB  ARG A1178     -12.004  15.999  18.806  1.00 54.57           C  
ANISOU 3169  CB  ARG A1178     9115   8417   3201    -67   1106    554       C  
ATOM   3170  CG  ARG A1178     -12.555  17.413  18.706  1.00 54.79           C  
ANISOU 3170  CG  ARG A1178     9021   8531   3265    -77   1165    393       C  
ATOM   3171  CD  ARG A1178     -13.780  17.609  19.586  1.00 59.83           C  
ANISOU 3171  CD  ARG A1178     9647   9304   3781    -13   1367    391       C  
ATOM   3172  NE  ARG A1178     -14.448  18.878  19.308  1.00 61.39           N  
ANISOU 3172  NE  ARG A1178     9721   9568   4038    -22   1441    235       N  
ATOM   3173  CZ  ARG A1178     -14.063  20.051  19.800  1.00 61.94           C  
ANISOU 3173  CZ  ARG A1178     9819   9634   4080    -20   1407    122       C  
ATOM   3174  NH1 ARG A1178     -13.007  20.125  20.599  1.00 59.20           N  
ANISOU 3174  NH1 ARG A1178     9613   9240   3641    -33   1294    143       N  
ATOM   3175  NH2 ARG A1178     -14.732  21.153  19.490  1.00 63.10           N  
ANISOU 3175  NH2 ARG A1178     9853   9833   4290     -1   1486    -11       N  
ATOM   3176  N   SER A1179      -9.900  13.923  16.801  1.00 53.79           N  
ANISOU 3176  N   SER A1179     8831   8292   3316   -502    690    731       N  
ATOM   3177  CA  SER A1179      -9.445  12.561  16.555  1.00 58.25           C  
ANISOU 3177  CA  SER A1179     9050   9200   3884   -578    563    959       C  
ATOM   3178  C   SER A1179      -8.037  12.576  15.961  1.00 63.15           C  
ANISOU 3178  C   SER A1179     9694   9711   4587   -449    413    997       C  
ATOM   3179  O   SER A1179      -7.429  13.637  15.821  1.00 65.32           O  
ANISOU 3179  O   SER A1179    10025   9887   4905   -386    362    871       O  
ATOM   3180  CB  SER A1179     -10.415  11.826  15.629  1.00 62.10           C  
ANISOU 3180  CB  SER A1179     9200   9926   4467   -385    657   1082       C  
ATOM   3181  OG  SER A1179     -11.680  11.660  16.249  1.00 62.92           O  
ANISOU 3181  OG  SER A1179     9475   9931   4503    217    969   1163       O  
ATOM   3182  N   ASP A1180      -7.528  11.400  15.606  1.00 65.53           N  
ANISOU 3182  N   ASP A1180     9952  10034   4914   -366    359   1180       N  
ATOM   3183  CA  ASP A1180      -6.136  11.256  15.181  1.00 67.44           C  
ANISOU 3183  CA  ASP A1180    10255  10156   5214   -258    220   1231       C  
ATOM   3184  C   ASP A1180      -5.825  11.977  13.870  1.00 65.35           C  
ANISOU 3184  C   ASP A1180     9931   9777   5120   -184    190   1111       C  
ATOM   3185  O   ASP A1180      -4.774  12.605  13.740  1.00 69.29           O  
ANISOU 3185  O   ASP A1180    10437  10236   5652   -102     92   1065       O  
ATOM   3186  CB  ASP A1180      -5.777   9.776  15.049  1.00 71.90           C  
ANISOU 3186  CB  ASP A1180    10871  10677   5769   -193    198   1445       C  
ATOM   3187  CG  ASP A1180      -4.284   9.550  14.917  1.00 73.54           C  
ANISOU 3187  CG  ASP A1180    11153  10787   6003    -82     48   1518       C  
ATOM   3188  OD1 ASP A1180      -3.511  10.339  15.499  1.00 74.29           O  
ANISOU 3188  OD1 ASP A1180    11265  10920   6043    -62    -43   1454       O  
ATOM   3189  OD2 ASP A1180      -3.885   8.584  14.235  1.00 75.14           O  
ANISOU 3189  OD2 ASP A1180    11401  10872   6278     -5     25   1639       O  
ATOM   3190  N   LEU A1181      -6.731  11.858  12.901  1.00 59.79           N  
ANISOU 3190  N   LEU A1181     9155   9047   4516   -203    273   1074       N  
ATOM   3191  CA  LEU A1181      -6.623  12.536  11.603  1.00 58.32           C  
ANISOU 3191  CA  LEU A1181     8904   8769   4485   -138    260    961       C  
ATOM   3192  C   LEU A1181      -5.419  12.127  10.750  1.00 57.55           C  
ANISOU 3192  C   LEU A1181     8818   8554   4496     -8    162   1030       C  
ATOM   3193  O   LEU A1181      -5.186  12.715   9.697  1.00 57.38           O  
ANISOU 3193  O   LEU A1181     8732   8450   4622     70    147    932       O  
ATOM   3194  CB  LEU A1181      -6.588  14.058  11.795  1.00 36.30           C  
ANISOU 3194  CB  LEU A1181     6095   5991   1706   -131    262    780       C  
ATOM   3195  CG  LEU A1181      -7.902  14.800  12.035  1.00 36.48           C  
ANISOU 3195  CG  LEU A1181     6116   6039   1706   -208    387    648       C  
ATOM   3196  CD1 LEU A1181      -7.664  16.301  11.993  1.00 35.38           C  
ANISOU 3196  CD1 LEU A1181     5951   5885   1606   -142    381    490       C  
ATOM   3197  CD2 LEU A1181      -8.945  14.392  11.008  1.00 35.74           C  
ANISOU 3197  CD2 LEU A1181     5963   5921   1696   -239    465    639       C  
ATOM   3198  N   SER A1182      -4.661  11.126  11.185  1.00 58.66           N  
ANISOU 3198  N   SER A1182     9035   8658   4595     38    102   1183       N  
ATOM   3199  CA  SER A1182      -3.460  10.719  10.457  1.00 58.07           C  
ANISOU 3199  CA  SER A1182     8973   8439   4650    186     18   1230       C  
ATOM   3200  C   SER A1182      -3.797   9.979   9.160  1.00 56.48           C  
ANISOU 3200  C   SER A1182     8778   8088   4593    222     68   1257       C  
ATOM   3201  O   SER A1182      -3.308  10.332   8.075  1.00 57.24           O  
ANISOU 3201  O   SER A1182     8830   8079   4838    315     47   1182       O  
ATOM   3202  CB  SER A1182      -2.569   9.847  11.346  1.00 63.74           C  
ANISOU 3202  CB  SER A1182     9788   9154   5276    233    -61   1386       C  
ATOM   3203  OG  SER A1182      -3.304   8.785  11.927  1.00 70.35           O  
ANISOU 3203  OG  SER A1182    10707  10014   6007    151      2   1523       O  
ATOM   3204  N   LYS A1183      -4.637   8.955   9.275  1.00 57.27           N  
ANISOU 3204  N   LYS A1183     8941   8176   4644    148    143   1363       N  
ATOM   3205  CA  LYS A1183      -5.040   8.159   8.120  1.00 59.13           C  
ANISOU 3205  CA  LYS A1183     9214   8254   4999    162    198   1391       C  
ATOM   3206  C   LYS A1183      -5.828   8.993   7.112  1.00 51.18           C  
ANISOU 3206  C   LYS A1183     8112   7256   4078    133    246   1246       C  
ATOM   3207  O   LYS A1183      -5.829   8.697   5.916  1.00 50.46           O  
ANISOU 3207  O   LYS A1183     8041   7014   4117    175    257   1222       O  
ATOM   3208  CB  LYS A1183      -5.858   6.944   8.569  1.00 64.18           C  
ANISOU 3208  CB  LYS A1183     9951   8883   5552     77    283   1531       C  
ATOM   3209  CG  LYS A1183      -6.862   7.235   9.671  1.00 70.03           C  
ANISOU 3209  CG  LYS A1183    10648   9837   6123    -37    358   1541       C  
ATOM   3210  CD  LYS A1183      -7.408   5.945  10.264  1.00 74.60           C  
ANISOU 3210  CD  LYS A1183    11349  10383   6611    -90    443   1702       C  
ATOM   3211  CE  LYS A1183      -8.276   6.214  11.485  1.00 76.46           C  
ANISOU 3211  CE  LYS A1183    11545  10840   6668   -168    530   1723       C  
ATOM   3212  NZ  LYS A1183      -8.730   4.950  12.131  1.00 77.02           N  
ANISOU 3212  NZ  LYS A1183    11764  10852   6647   -213    623   1883       N  
ATOM   3213  N   PHE A1184      -6.487  10.038   7.601  1.00 43.99           N  
ANISOU 3213  N   PHE A1184     7109   6514   3090     63    273   1143       N  
ATOM   3214  CA  PHE A1184      -7.206  10.964   6.734  1.00 38.70           C  
ANISOU 3214  CA  PHE A1184     6347   5865   2493     48    310    997       C  
ATOM   3215  C   PHE A1184      -6.222  11.693   5.821  1.00 37.69           C  
ANISOU 3215  C   PHE A1184     6187   5620   2515    173    238    900       C  
ATOM   3216  O   PHE A1184      -6.399  11.731   4.599  1.00 43.93           O  
ANISOU 3216  O   PHE A1184     6966   6301   3423    214    249    850       O  
ATOM   3217  CB  PHE A1184      -8.006  11.969   7.566  1.00 44.08           C  
ANISOU 3217  CB  PHE A1184     6957   6734   3057    -48    357    896       C  
ATOM   3218  CG  PHE A1184      -9.237  12.491   6.877  1.00 49.15           C  
ANISOU 3218  CG  PHE A1184     7523   7426   3728    -99    435    789       C  
ATOM   3219  CD1 PHE A1184      -9.132  13.264   5.732  1.00 51.71           C  
ANISOU 3219  CD1 PHE A1184     7802   7660   4184    -25    408    672       C  
ATOM   3220  CD2 PHE A1184     -10.498  12.220   7.382  1.00 51.01           C  
ANISOU 3220  CD2 PHE A1184     7710   7786   3886   -190    537    799       C  
ATOM   3221  CE1 PHE A1184     -10.262  13.749   5.095  1.00 49.17           C  
ANISOU 3221  CE1 PHE A1184     7424   7383   3875    -67    471    575       C  
ATOM   3222  CE2 PHE A1184     -11.633  12.704   6.751  1.00 52.69           C  
ANISOU 3222  CE2 PHE A1184     7844   8044   4131   -226    606    695       C  
ATOM   3223  CZ  PHE A1184     -11.513  13.469   5.606  1.00 50.52           C  
ANISOU 3223  CZ  PHE A1184     7566   7667   3964   -174    569    579       C  
ATOM   3224  N   ARG A1185      -5.183  12.264   6.426  1.00 34.60           N  
ANISOU 3224  N   ARG A1185     5783   5254   2108    234    168    878       N  
ATOM   3225  CA  ARG A1185      -4.151  12.981   5.685  1.00 37.15           C  
ANISOU 3225  CA  ARG A1185     6063   5494   2558    359    110    795       C  
ATOM   3226  C   ARG A1185      -3.431  12.051   4.714  1.00 37.12           C  
ANISOU 3226  C   ARG A1185     6119   5313   2670    455     90    866       C  
ATOM   3227  O   ARG A1185      -3.118  12.438   3.583  1.00 46.66           O  
ANISOU 3227  O   ARG A1185     7302   6419   4007    532     89    789       O  
ATOM   3228  CB  ARG A1185      -3.140  13.624   6.641  1.00 29.50           C  
ANISOU 3228  CB  ARG A1185     5076   4607   1526    397     40    779       C  
ATOM   3229  CG  ARG A1185      -3.753  14.573   7.663  1.00 30.07           C  
ANISOU 3229  CG  ARG A1185     5119   4827   1479    301     64    697       C  
ATOM   3230  CD  ARG A1185      -2.682  15.282   8.476  1.00 30.62           C  
ANISOU 3230  CD  ARG A1185     5180   4959   1493    341    -12    668       C  
ATOM   3231  NE  ARG A1185      -3.228  15.964   9.646  1.00 31.69           N  
ANISOU 3231  NE  ARG A1185     5337   5216   1489    240     15    612       N  
ATOM   3232  CZ  ARG A1185      -3.771  17.177   9.623  1.00 30.96           C  
ANISOU 3232  CZ  ARG A1185     5197   5153   1413    209     64    467       C  
ATOM   3233  NH1 ARG A1185      -3.853  17.848   8.483  1.00 29.13           N  
ANISOU 3233  NH1 ARG A1185     4886   4852   1331    268     83    371       N  
ATOM   3234  NH2 ARG A1185      -4.238  17.717  10.740  1.00 59.56           N  
ANISOU 3234  NH2 ARG A1185     8867   8860   4901    127    100    421       N  
ATOM   3235  N   GLU A1186      -3.172  10.823   5.159  1.00 36.97           N  
ANISOU 3235  N   GLU A1186     6193   5250   2605    453     81   1010       N  
ATOM   3236  CA  GLU A1186      -2.539   9.831   4.296  1.00 47.19           C  
ANISOU 3236  CA  GLU A1186     7564   6360   4006    538     76   1077       C  
ATOM   3237  C   GLU A1186      -3.420   9.538   3.079  1.00 45.33           C  
ANISOU 3237  C   GLU A1186     7356   6008   3859    497    142   1034       C  
ATOM   3238  O   GLU A1186      -2.929   9.433   1.945  1.00 43.93           O  
ANISOU 3238  O   GLU A1186     7201   5682   3807    576    143    992       O  
ATOM   3239  CB  GLU A1186      -2.249   8.549   5.077  1.00 60.68           C  
ANISOU 3239  CB  GLU A1186     9379   8038   5639    535     62   1241       C  
ATOM   3240  CG  GLU A1186      -1.359   7.549   4.346  1.00 74.27           C  
ANISOU 3240  CG  GLU A1186    11183   9570   7465    645     51   1307       C  
ATOM   3241  CD  GLU A1186       0.107   7.962   4.304  1.00 81.02           C  
ANISOU 3241  CD  GLU A1186    11989  10425   8369    796    -25   1288       C  
ATOM   3242  OE1 GLU A1186       0.939   7.148   3.848  1.00 83.64           O  
ANISOU 3242  OE1 GLU A1186    12380  10628   8773    900    -35   1347       O  
ATOM   3243  OE2 GLU A1186       0.434   9.093   4.726  1.00 81.98           O  
ANISOU 3243  OE2 GLU A1186    12013  10680   8455    811    -71   1212       O  
ATOM   3244  N   ASN A1187      -4.724   9.422   3.322  1.00 41.94           N  
ANISOU 3244  N   ASN A1187     6927   5655   3354    370    202   1043       N  
ATOM   3245  CA  ASN A1187      -5.691   9.239   2.244  1.00 38.76           C  
ANISOU 3245  CA  ASN A1187     6544   5172   3010    315    258    999       C  
ATOM   3246  C   ASN A1187      -5.674  10.415   1.276  1.00 38.92           C  
ANISOU 3246  C   ASN A1187     6483   5179   3126    372    242    850       C  
ATOM   3247  O   ASN A1187      -5.807  10.233   0.063  1.00 33.61           O  
ANISOU 3247  O   ASN A1187     5854   4366   2549    392    255    808       O  
ATOM   3248  CB  ASN A1187      -7.102   9.044   2.804  1.00 29.96           C  
ANISOU 3248  CB  ASN A1187     5420   4189   1776    172    332   1032       C  
ATOM   3249  CG  ASN A1187      -7.327   7.647   3.344  1.00 40.90           C  
ANISOU 3249  CG  ASN A1187     6925   5518   3095    105    376   1183       C  
ATOM   3250  OD1 ASN A1187      -6.617   6.708   2.986  1.00 50.08           O  
ANISOU 3250  OD1 ASN A1187     8198   6505   4326    156    357   1252       O  
ATOM   3251  ND2 ASN A1187      -8.325   7.501   4.207  1.00 38.72           N  
ANISOU 3251  ND2 ASN A1187     6634   5391   2689     -4    447   1230       N  
ATOM   3252  N   CYS A1188      -5.502  11.619   1.815  1.00 26.27           N  
ANISOU 3252  N   CYS A1188     4776   3713   1493    394    215    766       N  
ATOM   3253  CA  CYS A1188      -5.395  12.813   0.981  1.00 24.49           C  
ANISOU 3253  CA  CYS A1188     4478   3468   1361    459    201    626       C  
ATOM   3254  C   CYS A1188      -4.177  12.719   0.065  1.00 28.92           C  
ANISOU 3254  C   CYS A1188     5079   3862   2049    583    169    609       C  
ATOM   3255  O   CYS A1188      -4.279  12.961  -1.145  1.00 34.47           O  
ANISOU 3255  O   CYS A1188     5797   4449   2849    620    181    538       O  
ATOM   3256  CB  CYS A1188      -5.312  14.075   1.843  1.00 24.35           C  
ANISOU 3256  CB  CYS A1188     4358   3604   1288    456    183    542       C  
ATOM   3257  SG  CYS A1188      -6.779  14.408   2.836  1.00 49.57           S  
ANISOU 3257  SG  CYS A1188     7501   6999   4336    314    243    518       S  
ATOM   3258  N   LYS A1189      -3.032  12.359   0.646  1.00 28.04           N  
ANISOU 3258  N   LYS A1189     4987   3744   1925    648    132    675       N  
ATOM   3259  CA  LYS A1189      -1.800  12.175  -0.125  1.00 34.83           C  
ANISOU 3259  CA  LYS A1189     5879   4468   2885    771    114    667       C  
ATOM   3260  C   LYS A1189      -1.991  11.182  -1.270  1.00 38.77           C  
ANISOU 3260  C   LYS A1189     6482   4783   3467    772    155    687       C  
ATOM   3261  O   LYS A1189      -1.742  11.508  -2.442  1.00 43.85           O  
ANISOU 3261  O   LYS A1189     7140   5315   4206    826    173    600       O  
ATOM   3262  CB  LYS A1189      -0.659  11.704   0.783  1.00 37.53           C  
ANISOU 3262  CB  LYS A1189     6230   4852   3177    835     66    763       C  
ATOM   3263  CG  LYS A1189      -0.138  12.758   1.743  1.00 40.65           C  
ANISOU 3263  CG  LYS A1189     6533   5410   3501    851     13    724       C  
ATOM   3264  CD  LYS A1189       1.013  12.214   2.571  1.00 45.55           C  
ANISOU 3264  CD  LYS A1189     7168   6072   4066    923    -50    828       C  
ATOM   3265  CE  LYS A1189       1.571  13.264   3.516  1.00 49.26           C  
ANISOU 3265  CE  LYS A1189     7555   6709   4453    929   -113    783       C  
ATOM   3266  NZ  LYS A1189       2.684  12.715   4.337  1.00 52.44           N  
ANISOU 3266  NZ  LYS A1189     7969   7165   4790   1004   -193    892       N  
ATOM   3267  N   LYS A1190      -2.443   9.978  -0.924  1.00 32.53           N  
ANISOU 3267  N   LYS A1190     5773   3958   2630    705    174    796       N  
ATOM   3268  CA  LYS A1190      -2.669   8.929  -1.918  1.00 26.76           C  
ANISOU 3268  CA  LYS A1190     5155   3049   1963    685    215    816       C  
ATOM   3269  C   LYS A1190      -3.613   9.395  -3.026  1.00 29.77           C  
ANISOU 3269  C   LYS A1190     5543   3378   2390    631    242    713       C  
ATOM   3270  O   LYS A1190      -3.354   9.171  -4.215  1.00 24.82           O  
ANISOU 3270  O   LYS A1190     4978   2604   1848    665    261    653       O  
ATOM   3271  CB  LYS A1190      -3.224   7.672  -1.245  1.00 28.65           C  
ANISOU 3271  CB  LYS A1190     5485   3275   2127    595    238    947       C  
ATOM   3272  CG  LYS A1190      -2.262   7.020  -0.264  1.00 46.88           C  
ANISOU 3272  CG  LYS A1190     7820   5602   4392    660    206   1064       C  
ATOM   3273  CD  LYS A1190      -2.922   5.874   0.490  1.00 52.91           C  
ANISOU 3273  CD  LYS A1190     8682   6357   5066    562    235   1195       C  
ATOM   3274  CE  LYS A1190      -1.978   5.278   1.525  1.00 54.71           C  
ANISOU 3274  CE  LYS A1190     8944   6608   5237    636    193   1317       C  
ATOM   3275  NZ  LYS A1190      -2.649   4.252   2.371  1.00 54.46           N  
ANISOU 3275  NZ  LYS A1190     9015   6577   5101    539    226   1448       N  
ATOM   3276  N   ARG A1191      -4.695  10.059  -2.628  1.00 23.57           N  
ANISOU 3276  N   ARG A1191     4692   2726   1537    548    245    688       N  
ATOM   3277  CA  ARG A1191      -5.687  10.557  -3.576  1.00 27.17           C  
ANISOU 3277  CA  ARG A1191     5146   3161   2016    499    260    601       C  
ATOM   3278  C   ARG A1191      -5.085  11.547  -4.571  1.00 26.34           C  
ANISOU 3278  C   ARG A1191     5012   2982   2014    605    240    479       C  
ATOM   3279  O   ARG A1191      -5.245  11.390  -5.784  1.00 26.53           O  
ANISOU 3279  O   ARG A1191     5111   2868   2100    608    251    424       O  
ATOM   3280  CB  ARG A1191      -6.853  11.212  -2.830  1.00 22.98           C  
ANISOU 3280  CB  ARG A1191     4521   2832   1380    412    271    590       C  
ATOM   3281  CG  ARG A1191      -7.911  11.821  -3.737  1.00 22.27           C  
ANISOU 3281  CG  ARG A1191     4409   2757   1297    374    278    501       C  
ATOM   3282  CD  ARG A1191      -8.451  10.802  -4.725  1.00 22.75           C  
ANISOU 3282  CD  ARG A1191     4606   2663   1373    298    300    530       C  
ATOM   3283  NE  ARG A1191      -9.372  11.408  -5.682  1.00 39.58           N  
ANISOU 3283  NE  ARG A1191     6728   4806   3504    271    289    443       N  
ATOM   3284  CZ  ARG A1191      -9.787  10.814  -6.797  1.00 33.46           C  
ANISOU 3284  CZ  ARG A1191     6077   3885   2751    211    288    432       C  
ATOM   3285  NH1 ARG A1191      -9.360   9.596  -7.100  1.00 31.86           N  
ANISOU 3285  NH1 ARG A1191     6015   3506   2585    171    306    492       N  
ATOM   3286  NH2 ARG A1191     -10.626  11.439  -7.612  1.00 21.93           N  
ANISOU 3286  NH2 ARG A1191     4602   2459   1270    192    262    353       N  
ATOM   3287  N   ALA A1192      -4.395  12.561  -4.055  1.00 26.26           N  
ANISOU 3287  N   ALA A1192     4904   3061   2011    681    214    435       N  
ATOM   3288  CA  ALA A1192      -3.786  13.577  -4.910  1.00 26.33           C  
ANISOU 3288  CA  ALA A1192     4890   3003   2113    777    205    325       C  
ATOM   3289  C   ALA A1192      -2.778  12.964  -5.879  1.00 32.76           C  
ANISOU 3289  C   ALA A1192     5801   3645   3003    850    228    306       C  
ATOM   3290  O   ALA A1192      -2.803  13.248  -7.087  1.00 35.99           O  
ANISOU 3290  O   ALA A1192     6262   3939   3474    875    246    217       O  
ATOM   3291  CB  ALA A1192      -3.122  14.649  -4.064  1.00 25.02           C  
ANISOU 3291  CB  ALA A1192     4615   2961   1930    830    176    295       C  
ATOM   3292  N   MET A1193      -1.900  12.115  -5.348  1.00 29.01           N  
ANISOU 3292  N   MET A1193     5346   3166   2509    880    232    387       N  
ATOM   3293  CA  MET A1193      -0.879  11.469  -6.170  1.00 29.59           C  
ANISOU 3293  CA  MET A1193     5486   3121   2634    944    265    372       C  
ATOM   3294  C   MET A1193      -1.497  10.645  -7.301  1.00 36.93           C  
ANISOU 3294  C   MET A1193     6523   3923   3587    878    301    345       C  
ATOM   3295  O   MET A1193      -1.146  10.822  -8.479  1.00 36.60           O  
ANISOU 3295  O   MET A1193     6516   3816   3573    898    332    251       O  
ATOM   3296  CB  MET A1193       0.021  10.586  -5.302  1.00 37.49           C  
ANISOU 3296  CB  MET A1193     6486   4151   3608    987    252    492       C  
ATOM   3297  CG  MET A1193       0.855  11.356  -4.288  1.00 44.45           C  
ANISOU 3297  CG  MET A1193     7270   5166   4452   1061    207    514       C  
ATOM   3298  SD  MET A1193       1.878  10.289  -3.253  1.00 78.71           S  
ANISOU 3298  SD  MET A1193    11615   9541   8749   1124    173    668       S  
ATOM   3299  CE  MET A1193       2.597  11.488  -2.132  1.00 73.57           C  
ANISOU 3299  CE  MET A1193    10843   9079   8030   1183    102    663       C  
ATOM   3300  N   SER A1194      -2.422   9.757  -6.942  1.00 38.21           N  
ANISOU 3300  N   SER A1194     6738   4069   3712    782    298    427       N  
ATOM   3301  CA  SER A1194      -3.063   8.886  -7.925  1.00 22.07           C  
ANISOU 3301  CA  SER A1194     4806   1904   1675    702    325    411       C  
ATOM   3302  C   SER A1194      -3.822   9.693  -8.977  1.00 26.83           C  
ANISOU 3302  C   SER A1194     5426   2479   2291    672    319    295       C  
ATOM   3303  O   SER A1194      -3.795   9.360 -10.164  1.00 28.62           O  
ANISOU 3303  O   SER A1194     5728   2619   2526    653    339    228       O  
ATOM   3304  CB  SER A1194      -4.013   7.901  -7.240  1.00 23.57           C  
ANISOU 3304  CB  SER A1194     5057   2094   1807    587    328    525       C  
ATOM   3305  OG  SER A1194      -5.183   8.555  -6.781  1.00 46.70           O  
ANISOU 3305  OG  SER A1194     7935   5131   4678    506    310    530       O  
ATOM   3306  N   PHE A1195      -4.491  10.755  -8.536  1.00 29.62           N  
ANISOU 3306  N   PHE A1195     5701   2922   2630    667    287    276       N  
ATOM   3307  CA  PHE A1195      -5.220  11.634  -9.446  1.00 21.77           C  
ANISOU 3307  CA  PHE A1195     4716   1901   1655    660    268    180       C  
ATOM   3308  C   PHE A1195      -4.281  12.249 -10.482  1.00 36.06           C  
ANISOU 3308  C   PHE A1195     6521   3667   3515    739    283     65       C  
ATOM   3309  O   PHE A1195      -4.524  12.155 -11.696  1.00 38.78           O  
ANISOU 3309  O   PHE A1195     6841   4008   3885    665    265     40       O  
ATOM   3310  CB  PHE A1195      -5.940  12.734  -8.662  1.00 21.49           C  
ANISOU 3310  CB  PHE A1195     4553   2016   1595    659    233    194       C  
ATOM   3311  CG  PHE A1195      -6.850  13.584  -9.500  1.00 25.34           C  
ANISOU 3311  CG  PHE A1195     5031   2499   2100    652    201    129       C  
ATOM   3312  CD1 PHE A1195      -8.144  13.174  -9.777  1.00 26.18           C  
ANISOU 3312  CD1 PHE A1195     5174   2643   2131    540    189    151       C  
ATOM   3313  CD2 PHE A1195      -6.416  14.798 -10.004  1.00 26.53           C  
ANISOU 3313  CD2 PHE A1195     5131   2611   2337    752    178     64       C  
ATOM   3314  CE1 PHE A1195      -8.987  13.957 -10.545  1.00 24.74           C  
ANISOU 3314  CE1 PHE A1195     4964   2489   1949    543    147     92       C  
ATOM   3315  CE2 PHE A1195      -7.253  15.584 -10.774  1.00 28.24           C  
ANISOU 3315  CE2 PHE A1195     5320   2835   2575    751    133     39       C  
ATOM   3316  CZ  PHE A1195      -8.541  15.163 -11.044  1.00 27.98           C  
ANISOU 3316  CZ  PHE A1195     5309   2865   2455    655    117     37       C  
ATOM   3317  N   SER A1196      -3.203  12.863  -9.994  1.00 33.37           N  
ANISOU 3317  N   SER A1196     6065   3404   3211    807    282     69       N  
ATOM   3318  CA  SER A1196      -2.208  13.483 -10.867  1.00 30.23           C  
ANISOU 3318  CA  SER A1196     5520   3088   2878    779    269     44       C  
ATOM   3319  C   SER A1196      -1.661  12.487 -11.891  1.00 35.09           C  
ANISOU 3319  C   SER A1196     6200   3667   3467    746    305     56       C  
ATOM   3320  O   SER A1196      -1.624  12.770 -13.101  1.00 44.52           O  
ANISOU 3320  O   SER A1196     7360   4885   4673    692    293     47       O  
ATOM   3321  CB  SER A1196      -1.063  14.068 -10.037  1.00 34.50           C  
ANISOU 3321  CB  SER A1196     5993   3688   3428    857    271     56       C  
ATOM   3322  OG  SER A1196      -0.121  14.730 -10.861  1.00 42.17           O  
ANISOU 3322  OG  SER A1196     6860   4734   4429    814    263     48       O  
ATOM   3323  N   LYS A 288      -1.255  11.315 -11.404  1.00 44.01           N  
ANISOU 3323  N   LYS A 288     7011   7382   2329   -259   -293   -436       N  
ATOM   3324  CA  LYS A 288      -0.719  10.279 -12.283  1.00 43.64           C  
ANISOU 3324  CA  LYS A 288     6961   7263   2356   -231   -299   -290       C  
ATOM   3325  C   LYS A 288      -1.728   9.852 -13.350  1.00 46.02           C  
ANISOU 3325  C   LYS A 288     7269   7448   2767   -157   -214   -336       C  
ATOM   3326  O   LYS A 288      -1.369   9.680 -14.522  1.00 44.73           O  
ANISOU 3326  O   LYS A 288     7080   7211   2703   -112   -233   -297       O  
ATOM   3327  CB  LYS A 288      -0.270   9.063 -11.470  1.00 39.69           C  
ANISOU 3327  CB  LYS A 288     6527   6792   1763   -271   -297   -128       C  
ATOM   3328  CG  LYS A 288       1.049   9.265 -10.742  1.00 41.12           C  
ANISOU 3328  CG  LYS A 288     6753   7015   1855   -358   -420    -35       C  
ATOM   3329  CD  LYS A 288       1.535   7.972 -10.109  1.00 48.04           C  
ANISOU 3329  CD  LYS A 288     7794   7813   2647   -351   -440    139       C  
ATOM   3330  CE  LYS A 288       2.875   8.163  -9.416  1.00 52.10           C  
ANISOU 3330  CE  LYS A 288     8527   8204   3066   -339   -607    215       C  
ATOM   3331  NZ  LYS A 288       3.338   6.913  -8.750  1.00 55.63           N  
ANISOU 3331  NZ  LYS A 288     9063   8664   3409   -238   -625    376       N  
ATOM   3332  N   GLN A 289      -2.987   9.695 -12.948  1.00 50.59           N  
ANISOU 3332  N   GLN A 289     7882   8019   3323   -148   -118   -425       N  
ATOM   3333  CA  GLN A 289      -4.033   9.315 -13.891  1.00 48.24           C  
ANISOU 3333  CA  GLN A 289     7583   7627   3118    -84    -38   -486       C  
ATOM   3334  C   GLN A 289      -4.193  10.357 -14.988  1.00 41.15           C  
ANISOU 3334  C   GLN A 289     6670   6638   2326    -47    -84   -591       C  
ATOM   3335  O   GLN A 289      -4.294  10.012 -16.169  1.00 40.43           O  
ANISOU 3335  O   GLN A 289     6562   6460   2338      9    -79   -573       O  
ATOM   3336  CB  GLN A 289      -5.373   9.110 -13.183  1.00 53.53           C  
ANISOU 3336  CB  GLN A 289     8285   8316   3738    -89     77   -585       C  
ATOM   3337  CG  GLN A 289      -6.497   8.734 -14.141  1.00 61.91           C  
ANISOU 3337  CG  GLN A 289     9336   9292   4896    -28    158   -664       C  
ATOM   3338  CD  GLN A 289      -7.855   8.666 -13.472  1.00 69.19           C  
ANISOU 3338  CD  GLN A 289    10281  10230   5777    -36    280   -784       C  
ATOM   3339  OE1 GLN A 289      -7.995   8.976 -12.290  1.00 73.50           O  
ANISOU 3339  OE1 GLN A 289    10861  10845   6220    -86    309   -816       O  
ATOM   3340  NE2 GLN A 289      -8.867   8.259 -14.230  1.00 67.48           N  
ANISOU 3340  NE2 GLN A 289    10049   9951   5641     11    358   -857       N  
ATOM   3341  N   MET A 290      -4.210  11.631 -14.604  1.00 40.38           N  
ANISOU 3341  N   MET A 290     6586   6552   2205    -71   -127   -697       N  
ATOM   3342  CA  MET A 290      -4.384  12.690 -15.594  1.00 40.13           C  
ANISOU 3342  CA  MET A 290     6565   6425   2259    -31   -169   -795       C  
ATOM   3343  C   MET A 290      -3.191  12.739 -16.555  1.00 34.26           C  
ANISOU 3343  C   MET A 290     5792   5641   1585    -14   -248   -698       C  
ATOM   3344  O   MET A 290      -3.361  12.995 -17.756  1.00 37.90           O  
ANISOU 3344  O   MET A 290     6258   5974   2166     49   -261   -715       O  
ATOM   3345  CB  MET A 290      -4.603  14.046 -14.908  1.00 46.23           C  
ANISOU 3345  CB  MET A 290     7375   7211   2979    -55   -191   -930       C  
ATOM   3346  CG  MET A 290      -3.391  14.960 -14.839  1.00 50.30           C  
ANISOU 3346  CG  MET A 290     7881   7763   3467    -85   -289   -921       C  
ATOM   3347  SD  MET A 290      -3.801  16.588 -14.179  1.00107.56           S  
ANISOU 3347  SD  MET A 290    15199  15005  10664    -98   -302  -1110       S  
ATOM   3348  CE  MET A 290      -4.206  16.181 -12.485  1.00 40.26           C  
ANISOU 3348  CE  MET A 290     6668   6623   2007   -157   -240  -1129       C  
ATOM   3349  N   ARG A 291      -1.994  12.458 -16.040  1.00 36.38           N  
ANISOU 3349  N   ARG A 291     6029   6010   1785    -62   -298   -591       N  
ATOM   3350  CA  ARG A 291      -0.802  12.440 -16.887  1.00 34.98           C  
ANISOU 3350  CA  ARG A 291     5823   5817   1652    -52   -363   -501       C  
ATOM   3351  C   ARG A 291      -0.874  11.306 -17.912  1.00 33.65           C  
ANISOU 3351  C   ARG A 291     5645   5561   1577      1   -319   -407       C  
ATOM   3352  O   ARG A 291      -0.663  11.520 -19.118  1.00 34.75           O  
ANISOU 3352  O   ARG A 291     5791   5593   1821     47   -334   -405       O  
ATOM   3353  CB  ARG A 291       0.462  12.305 -16.036  1.00 36.08           C  
ANISOU 3353  CB  ARG A 291     5918   6083   1707   -101   -426   -403       C  
ATOM   3354  CG  ARG A 291       1.728  12.791 -16.726  1.00 51.57           C  
ANISOU 3354  CG  ARG A 291     7852   8051   3692    -91   -503   -365       C  
ATOM   3355  CD  ARG A 291       2.955  12.596 -15.843  1.00 55.74           C  
ANISOU 3355  CD  ARG A 291     8318   8731   4130   -116   -573   -273       C  
ATOM   3356  NE  ARG A 291       2.749  13.112 -14.492  1.00 52.92           N  
ANISOU 3356  NE  ARG A 291     7949   8491   3666   -133   -593   -349       N  
ATOM   3357  CZ  ARG A 291       2.902  14.386 -14.147  1.00 53.61           C  
ANISOU 3357  CZ  ARG A 291     8056   8605   3706   -101   -649   -488       C  
ATOM   3358  NH1 ARG A 291       3.260  15.282 -15.056  1.00 54.91           N  
ANISOU 3358  NH1 ARG A 291     8271   8671   3920    -91   -690   -557       N  
ATOM   3359  NH2 ARG A 291       2.693  14.765 -12.894  1.00 52.37           N  
ANISOU 3359  NH2 ARG A 291     7902   8554   3444    -86   -666   -562       N  
ATOM   3360  N   ALA A 292      -1.177  10.103 -17.429  1.00 33.28           N  
ANISOU 3360  N   ALA A 292     5598   5554   1492     -2   -260   -331       N  
ATOM   3361  CA  ALA A 292      -1.322   8.941 -18.303  1.00 32.25           C  
ANISOU 3361  CA  ALA A 292     5465   5341   1447     59   -205   -253       C  
ATOM   3362  C   ALA A 292      -2.376   9.194 -19.380  1.00 37.70           C  
ANISOU 3362  C   ALA A 292     6164   5905   2256    124   -169   -359       C  
ATOM   3363  O   ALA A 292      -2.192   8.843 -20.554  1.00 38.05           O  
ANISOU 3363  O   ALA A 292     6207   5858   2394    173   -165   -325       O  
ATOM   3364  CB  ALA A 292      -1.681   7.710 -17.487  1.00 32.87           C  
ANISOU 3364  CB  ALA A 292     5561   5475   1454     54   -131   -179       C  
ATOM   3365  N   ARG A 293      -3.476   9.814 -18.963  1.00 35.17           N  
ANISOU 3365  N   ARG A 293     5859   5582   1922    122   -146   -488       N  
ATOM   3366  CA  ARG A 293      -4.558  10.185 -19.866  1.00 31.49           C  
ANISOU 3366  CA  ARG A 293     5402   5010   1554    184   -128   -594       C  
ATOM   3367  C   ARG A 293      -4.041  11.082 -20.987  1.00 30.82           C  
ANISOU 3367  C   ARG A 293     5332   4823   1554    217   -201   -602       C  
ATOM   3368  O   ARG A 293      -4.292  10.828 -22.177  1.00 29.96           O  
ANISOU 3368  O   ARG A 293     5228   4619   1537    272   -199   -598       O  
ATOM   3369  CB  ARG A 293      -5.670  10.890 -19.088  1.00 32.48           C  
ANISOU 3369  CB  ARG A 293     5547   5158   1636    176    -98   -731       C  
ATOM   3370  CG  ARG A 293      -6.990  11.010 -19.829  1.00 50.46           C  
ANISOU 3370  CG  ARG A 293     7826   7351   3995    248    -67   -838       C  
ATOM   3371  CD  ARG A 293      -8.129  10.432 -19.003  1.00 47.58           C  
ANISOU 3371  CD  ARG A 293     7457   7048   3571    235     36   -911       C  
ATOM   3372  NE  ARG A 293      -8.106  10.921 -17.629  1.00 45.55           N  
ANISOU 3372  NE  ARG A 293     7232   6877   3199    172     58   -951       N  
ATOM   3373  CZ  ARG A 293      -9.013  10.610 -16.710  1.00 46.55           C  
ANISOU 3373  CZ  ARG A 293     7376   7061   3250    147    158  -1023       C  
ATOM   3374  NH1 ARG A 293     -10.024   9.810 -17.019  1.00 51.38           N  
ANISOU 3374  NH1 ARG A 293     7969   7657   3895    179    249  -1067       N  
ATOM   3375  NH2 ARG A 293      -8.909  11.102 -15.483  1.00 43.92           N  
ANISOU 3375  NH2 ARG A 293     7084   6805   2801     84    175  -1058       N  
ATOM   3376  N   ARG A 294      -3.309  12.124 -20.596  1.00 30.57           N  
ANISOU 3376  N   ARG A 294     5320   4816   1481    178   -262   -617       N  
ATOM   3377  CA  ARG A 294      -2.691  13.035 -21.555  1.00 30.21           C  
ANISOU 3377  CA  ARG A 294     5310   4675   1495    199   -325   -620       C  
ATOM   3378  C   ARG A 294      -1.849  12.263 -22.573  1.00 32.57           C  
ANISOU 3378  C   ARG A 294     5596   4931   1847    215   -325   -509       C  
ATOM   3379  O   ARG A 294      -1.971  12.474 -23.789  1.00 31.36           O  
ANISOU 3379  O   ARG A 294     5478   4659   1777    264   -335   -516       O  
ATOM   3380  CB  ARG A 294      -1.833  14.069 -20.820  1.00 36.59           C  
ANISOU 3380  CB  ARG A 294     6138   5542   2223    139   -382   -644       C  
ATOM   3381  CG  ARG A 294      -1.490  15.312 -21.630  1.00 39.18           C  
ANISOU 3381  CG  ARG A 294     6541   5749   2597    160   -438   -689       C  
ATOM   3382  CD  ARG A 294      -0.710  16.312 -20.785  1.00 38.61           C  
ANISOU 3382  CD  ARG A 294     6496   5742   2433     94   -490   -735       C  
ATOM   3383  NE  ARG A 294      -0.419  17.551 -21.504  1.00 41.07           N  
ANISOU 3383  NE  ARG A 294     6913   5914   2779    107   -538   -785       N  
ATOM   3384  CZ  ARG A 294      -1.175  18.644 -21.447  1.00 45.70           C  
ANISOU 3384  CZ  ARG A 294     7586   6404   3376    140   -548   -894       C  
ATOM   3385  NH1 ARG A 294      -2.272  18.655 -20.703  1.00 45.19           N  
ANISOU 3385  NH1 ARG A 294     7502   6379   3291    165   -511   -974       N  
ATOM   3386  NH2 ARG A 294      -0.835  19.729 -22.132  1.00 42.55           N  
ANISOU 3386  NH2 ARG A 294     7308   5859   2998    150   -591   -922       N  
ATOM   3387  N   LYS A 295      -1.017  11.351 -22.072  1.00 29.34           N  
ANISOU 3387  N   LYS A 295     5145   4618   1383    177   -311   -403       N  
ATOM   3388  CA  LYS A 295      -0.147  10.560 -22.945  1.00 28.65           C  
ANISOU 3388  CA  LYS A 295     5053   4499   1336    195   -302   -294       C  
ATOM   3389  C   LYS A 295      -0.917   9.711 -23.964  1.00 34.00           C  
ANISOU 3389  C   LYS A 295     5740   5076   2101    260   -244   -295       C  
ATOM   3390  O   LYS A 295      -0.656   9.792 -25.173  1.00 35.38           O  
ANISOU 3390  O   LYS A 295     5947   5152   2344    291   -249   -284       O  
ATOM   3391  CB  LYS A 295       0.763   9.652 -22.114  1.00 29.19           C  
ANISOU 3391  CB  LYS A 295     5081   4690   1322    158   -297   -171       C  
ATOM   3392  CG  LYS A 295       1.841  10.385 -21.333  1.00 42.58           C  
ANISOU 3392  CG  LYS A 295     6755   6501   2921     92   -372   -147       C  
ATOM   3393  CD  LYS A 295       2.908   9.417 -20.848  1.00 46.06           C  
ANISOU 3393  CD  LYS A 295     7163   7046   3294     67   -384      6       C  
ATOM   3394  CE  LYS A 295       3.849  10.077 -19.853  1.00 53.15           C  
ANISOU 3394  CE  LYS A 295     8026   8097   4073     -3   -472     24       C  
ATOM   3395  NZ  LYS A 295       3.154  10.395 -18.573  1.00 54.87           N  
ANISOU 3395  NZ  LYS A 295     8240   8382   4225    -41   -474    -46       N  
ATOM   3396  N   THR A 296      -1.857   8.898 -23.482  1.00 33.21           N  
ANISOU 3396  N   THR A 296     5622   5007   1990    273   -185   -314       N  
ATOM   3397  CA  THR A 296      -2.601   8.009 -24.376  1.00 34.48           C  
ANISOU 3397  CA  THR A 296     5789   5094   2216    326   -128   -325       C  
ATOM   3398  C   THR A 296      -3.390   8.801 -25.417  1.00 26.79           C  
ANISOU 3398  C   THR A 296     4840   4020   1319    368   -162   -423       C  
ATOM   3399  O   THR A 296      -3.424   8.430 -26.600  1.00 26.21           O  
ANISOU 3399  O   THR A 296     4788   3863   1308    404   -153   -411       O  
ATOM   3400  CB  THR A 296      -3.567   7.090 -23.603  1.00 27.59           C  
ANISOU 3400  CB  THR A 296     4900   4280   1302    325    -52   -347       C  
ATOM   3401  OG1 THR A 296      -4.604   7.872 -22.999  1.00 51.06           O  
ANISOU 3401  OG1 THR A 296     7865   7284   4252    314    -60   -467       O  
ATOM   3402  CG2 THR A 296      -2.822   6.314 -22.527  1.00 28.21           C  
ANISOU 3402  CG2 THR A 296     4972   4452   1294    293    -22   -232       C  
ATOM   3403  N   ALA A 297      -4.009   9.897 -24.979  1.00 27.55           N  
ANISOU 3403  N   ALA A 297     4943   4122   1404    367   -200   -516       N  
ATOM   3404  CA  ALA A 297      -4.734  10.771 -25.899  1.00 27.24           C  
ANISOU 3404  CA  ALA A 297     4938   3984   1427    423   -245   -597       C  
ATOM   3405  C   ALA A 297      -3.803  11.295 -26.991  1.00 40.49           C  
ANISOU 3405  C   ALA A 297     6673   5567   3147    434   -291   -544       C  
ATOM   3406  O   ALA A 297      -4.155  11.292 -28.180  1.00 26.48           O  
ANISOU 3406  O   ALA A 297     4932   3702   1428    484   -305   -554       O  
ATOM   3407  CB  ALA A 297      -5.375  11.923 -25.145  1.00 28.10           C  
ANISOU 3407  CB  ALA A 297     5063   4107   1506    430   -276   -694       C  
ATOM   3408  N   LYS A 298      -2.613  11.732 -26.581  1.00 27.57           N  
ANISOU 3408  N   LYS A 298     5050   3957   1470    383   -313   -491       N  
ATOM   3409  CA  LYS A 298      -1.593  12.185 -27.523  1.00 27.37           C  
ANISOU 3409  CA  LYS A 298     5086   3850   1465    378   -342   -439       C  
ATOM   3410  C   LYS A 298      -1.284  11.118 -28.573  1.00 36.32           C  
ANISOU 3410  C   LYS A 298     6221   4938   2640    399   -299   -372       C  
ATOM   3411  O   LYS A 298      -1.304  11.393 -29.782  1.00 39.10           O  
ANISOU 3411  O   LYS A 298     6639   5182   3036    432   -312   -373       O  
ATOM   3412  CB  LYS A 298      -0.313  12.569 -26.778  1.00 35.76           C  
ANISOU 3412  CB  LYS A 298     6143   4986   2457    308   -365   -392       C  
ATOM   3413  CG  LYS A 298       0.865  12.890 -27.681  1.00 37.78           C  
ANISOU 3413  CG  LYS A 298     6463   5176   2717    287   -380   -335       C  
ATOM   3414  CD  LYS A 298       2.152  13.002 -26.879  1.00 43.93           C  
ANISOU 3414  CD  LYS A 298     7214   6067   3412    215   -403   -281       C  
ATOM   3415  CE  LYS A 298       3.360  13.200 -27.783  1.00 50.66           C  
ANISOU 3415  CE  LYS A 298     8131   6864   4254    187   -406   -221       C  
ATOM   3416  NZ  LYS A 298       4.640  13.124 -27.023  1.00 52.80           N  
ANISOU 3416  NZ  LYS A 298     8358   7271   4432    123   -434   -157       N  
ATOM   3417  N   MET A 299      -1.010   9.901 -28.107  1.00 34.55           N  
ANISOU 3417  N   MET A 299     5941   4791   2395    384   -244   -310       N  
ATOM   3418  CA  MET A 299      -0.680   8.802 -29.012  1.00 25.89           C  
ANISOU 3418  CA  MET A 299     4858   3649   1330    406   -190   -247       C  
ATOM   3419  C   MET A 299      -1.787   8.537 -30.029  1.00 33.49           C  
ANISOU 3419  C   MET A 299     5845   4530   2351    456   -180   -310       C  
ATOM   3420  O   MET A 299      -1.532   8.458 -31.237  1.00 32.05           O  
ANISOU 3420  O   MET A 299     5717   4258   2201    475   -175   -293       O  
ATOM   3421  CB  MET A 299      -0.399   7.520 -28.227  1.00 25.98           C  
ANISOU 3421  CB  MET A 299     4823   3744   1303    398   -127   -172       C  
ATOM   3422  CG  MET A 299       0.026   6.359 -29.113  1.00 25.66           C  
ANISOU 3422  CG  MET A 299     4812   3646   1292    430    -56   -103       C  
ATOM   3423  SD  MET A 299      -0.017   4.759 -28.284  1.00 70.66           S  
ANISOU 3423  SD  MET A 299    10487   9405   6956    447     37    -22       S  
ATOM   3424  CE  MET A 299      -1.778   4.553 -28.033  1.00 35.83           C  
ANISOU 3424  CE  MET A 299     6061   5000   2554    454     56   -142       C  
ATOM   3425  N   LEU A 300      -3.015   8.399 -29.535  1.00 26.07           N  
ANISOU 3425  N   LEU A 300     4864   3630   1410    471   -177   -385       N  
ATOM   3426  CA  LEU A 300      -4.147   8.111 -30.411  1.00 26.01           C  
ANISOU 3426  CA  LEU A 300     4863   3577   1443    512   -177   -454       C  
ATOM   3427  C   LEU A 300      -4.354   9.216 -31.443  1.00 35.19           C  
ANISOU 3427  C   LEU A 300     6086   4646   2638    552   -250   -490       C  
ATOM   3428  O   LEU A 300      -4.646   8.940 -32.614  1.00 35.47           O  
ANISOU 3428  O   LEU A 300     6157   4619   2700    581   -257   -499       O  
ATOM   3429  CB  LEU A 300      -5.417   7.904 -29.589  1.00 26.44           C  
ANISOU 3429  CB  LEU A 300     4860   3708   1479    515   -160   -542       C  
ATOM   3430  CG  LEU A 300      -5.340   6.701 -28.648  1.00 26.53           C  
ANISOU 3430  CG  LEU A 300     4835   3800   1445    481    -74   -504       C  
ATOM   3431  CD1 LEU A 300      -6.570   6.615 -27.773  1.00 27.16           C  
ANISOU 3431  CD1 LEU A 300     4870   3958   1494    473    -45   -600       C  
ATOM   3432  CD2 LEU A 300      -5.149   5.414 -29.435  1.00 26.24           C  
ANISOU 3432  CD2 LEU A 300     4823   3722   1426    488     -7   -460       C  
ATOM   3433  N   MET A 301      -4.191  10.464 -31.011  1.00 32.38           N  
ANISOU 3433  N   MET A 301     5756   4277   2269    555   -305   -507       N  
ATOM   3434  CA  MET A 301      -4.295  11.590 -31.933  1.00 34.05           C  
ANISOU 3434  CA  MET A 301     6057   4383   2499    602   -373   -526       C  
ATOM   3435  C   MET A 301      -3.241  11.504 -33.033  1.00 38.02           C  
ANISOU 3435  C   MET A 301     6638   4799   3009    586   -361   -451       C  
ATOM   3436  O   MET A 301      -3.535  11.747 -34.208  1.00 27.88           O  
ANISOU 3436  O   MET A 301     5427   3427   1740    631   -392   -457       O  
ATOM   3437  CB  MET A 301      -4.160  12.917 -31.193  1.00 32.52           C  
ANISOU 3437  CB  MET A 301     5901   4177   2277    603   -421   -555       C  
ATOM   3438  CG  MET A 301      -4.240  14.124 -32.110  1.00 33.39           C  
ANISOU 3438  CG  MET A 301     6137   4156   2393    663   -491   -567       C  
ATOM   3439  SD  MET A 301      -5.770  14.159 -33.064  1.00127.59           S  
ANISOU 3439  SD  MET A 301    18087  16043  14350    781   -548   -634       S  
ATOM   3440  CE  MET A 301      -5.560  15.683 -33.981  1.00 56.53           C  
ANISOU 3440  CE  MET A 301     9276   6873   5329    856   -634   -619       C  
ATOM   3441  N   VAL A 302      -2.014  11.157 -32.650  1.00 40.40           N  
ANISOU 3441  N   VAL A 302     6928   5132   3289    526   -317   -382       N  
ATOM   3442  CA  VAL A 302      -0.941  11.010 -33.631  1.00 39.00           C  
ANISOU 3442  CA  VAL A 302     6826   4883   3110    505   -289   -314       C  
ATOM   3443  C   VAL A 302      -1.268   9.911 -34.645  1.00 34.12           C  
ANISOU 3443  C   VAL A 302     6214   4232   2519    531   -244   -305       C  
ATOM   3444  O   VAL A 302      -1.104  10.104 -35.855  1.00 25.17           O  
ANISOU 3444  O   VAL A 302     5170   3003   1389    545   -249   -293       O  
ATOM   3445  CB  VAL A 302       0.408  10.706 -32.954  1.00 25.31           C  
ANISOU 3445  CB  VAL A 302     5062   3216   1337    443   -249   -242       C  
ATOM   3446  CG1 VAL A 302       1.446  10.302 -33.989  1.00 25.30           C  
ANISOU 3446  CG1 VAL A 302     5128   3154   1331    426   -197   -175       C  
ATOM   3447  CG2 VAL A 302       0.886  11.916 -32.167  1.00 25.87           C  
ANISOU 3447  CG2 VAL A 302     5152   3309   1366    402   -302   -256       C  
ATOM   3448  N   VAL A 303      -1.743   8.770 -34.150  1.00 33.24           N  
ANISOU 3448  N   VAL A 303     6022   4194   2415    532   -198   -313       N  
ATOM   3449  CA  VAL A 303      -2.134   7.662 -35.023  1.00 24.56           C  
ANISOU 3449  CA  VAL A 303     4935   3066   1332    549   -151   -319       C  
ATOM   3450  C   VAL A 303      -3.199   8.096 -36.029  1.00 32.43           C  
ANISOU 3450  C   VAL A 303     5968   4011   2342    590   -213   -388       C  
ATOM   3451  O   VAL A 303      -3.063   7.854 -37.236  1.00 32.56           O  
ANISOU 3451  O   VAL A 303     6056   3957   2358    598   -203   -377       O  
ATOM   3452  CB  VAL A 303      -2.661   6.461 -34.211  1.00 24.44           C  
ANISOU 3452  CB  VAL A 303     4843   3132   1311    542    -92   -331       C  
ATOM   3453  CG1 VAL A 303      -3.378   5.471 -35.120  1.00 24.54           C  
ANISOU 3453  CG1 VAL A 303     4874   3114   1336    554    -55   -372       C  
ATOM   3454  CG2 VAL A 303      -1.522   5.782 -33.472  1.00 24.32           C  
ANISOU 3454  CG2 VAL A 303     4815   3154   1272    519    -22   -238       C  
ATOM   3455  N   LEU A 304      -4.246   8.749 -35.531  1.00 34.66           N  
ANISOU 3455  N   LEU A 304     6208   4333   2628    621   -276   -459       N  
ATOM   3456  CA  LEU A 304      -5.314   9.245 -36.395  1.00 25.79           C  
ANISOU 3456  CA  LEU A 304     5117   3174   1507    679   -351   -525       C  
ATOM   3457  C   LEU A 304      -4.781  10.203 -37.461  1.00 28.95           C  
ANISOU 3457  C   LEU A 304     5647   3458   1896    708   -399   -485       C  
ATOM   3458  O   LEU A 304      -5.121  10.090 -38.642  1.00 26.58           O  
ANISOU 3458  O   LEU A 304     5408   3107   1583    738   -426   -496       O  
ATOM   3459  CB  LEU A 304      -6.395   9.942 -35.568  1.00 26.25           C  
ANISOU 3459  CB  LEU A 304     5121   3288   1565    722   -409   -604       C  
ATOM   3460  CG  LEU A 304      -7.528  10.560 -36.390  1.00 33.42           C  
ANISOU 3460  CG  LEU A 304     6066   4165   2467    810   -504   -674       C  
ATOM   3461  CD1 LEU A 304      -8.315   9.476 -37.108  1.00 38.01           C  
ANISOU 3461  CD1 LEU A 304     6605   4791   3046    803   -493   -730       C  
ATOM   3462  CD2 LEU A 304      -8.439  11.403 -35.515  1.00 27.78           C  
ANISOU 3462  CD2 LEU A 304     5316   3490   1750    873   -560   -749       C  
ATOM   3463  N   LEU A 305      -3.939  11.139 -37.031  1.00 28.61           N  
ANISOU 3463  N   LEU A 305     5655   3373   1845    693   -408   -442       N  
ATOM   3464  CA  LEU A 305      -3.359  12.141 -37.922  1.00 30.60           C  
ANISOU 3464  CA  LEU A 305     6053   3499   2072    710   -443   -404       C  
ATOM   3465  C   LEU A 305      -2.561  11.500 -39.054  1.00 35.14           C  
ANISOU 3465  C   LEU A 305     6700   4015   2636    675   -385   -350       C  
ATOM   3466  O   LEU A 305      -2.773  11.804 -40.236  1.00 38.20           O  
ANISOU 3466  O   LEU A 305     7198   4316   2998    711   -418   -348       O  
ATOM   3467  CB  LEU A 305      -2.468  13.094 -37.123  1.00 32.36           C  
ANISOU 3467  CB  LEU A 305     6315   3701   2280    670   -445   -376       C  
ATOM   3468  CG  LEU A 305      -1.840  14.272 -37.866  1.00 37.78           C  
ANISOU 3468  CG  LEU A 305     7180   4247   2930    673   -476   -343       C  
ATOM   3469  CD1 LEU A 305      -2.915  15.096 -38.555  1.00 42.63           C  
ANISOU 3469  CD1 LEU A 305     7896   4773   3529    779   -569   -382       C  
ATOM   3470  CD2 LEU A 305      -1.032  15.132 -36.905  1.00 33.59           C  
ANISOU 3470  CD2 LEU A 305     6674   3716   2375    615   -477   -333       C  
ATOM   3471  N   VAL A 306      -1.642  10.614 -38.679  1.00 32.07           N  
ANISOU 3471  N   VAL A 306     6259   3672   2254    612   -297   -306       N  
ATOM   3472  CA  VAL A 306      -0.832   9.883 -39.648  1.00 35.91           C  
ANISOU 3472  CA  VAL A 306     6809   4109   2728    581   -221   -258       C  
ATOM   3473  C   VAL A 306      -1.719   9.111 -40.621  1.00 36.68           C  
ANISOU 3473  C   VAL A 306     6915   4197   2824    613   -226   -296       C  
ATOM   3474  O   VAL A 306      -1.456   9.084 -41.827  1.00 32.11           O  
ANISOU 3474  O   VAL A 306     6446   3539   2217    612   -210   -279       O  
ATOM   3475  CB  VAL A 306       0.142   8.911 -38.949  1.00 34.63           C  
ANISOU 3475  CB  VAL A 306     6577   4010   2571    533   -126   -208       C  
ATOM   3476  CG1 VAL A 306       0.770   7.949 -39.951  1.00 32.95           C  
ANISOU 3476  CG1 VAL A 306     6425   3747   2347    519    -33   -172       C  
ATOM   3477  CG2 VAL A 306       1.214   9.690 -38.204  1.00 31.09           C  
ANISOU 3477  CG2 VAL A 306     6134   3578   2099    489   -124   -166       C  
ATOM   3478  N   PHE A 307      -2.775   8.497 -40.094  1.00 40.34           N  
ANISOU 3478  N   PHE A 307     7271   4748   3310    631   -245   -355       N  
ATOM   3479  CA  PHE A 307      -3.736   7.782 -40.929  1.00 37.89           C  
ANISOU 3479  CA  PHE A 307     6957   4452   2989    650   -260   -413       C  
ATOM   3480  C   PHE A 307      -4.336   8.703 -41.991  1.00 37.05           C  
ANISOU 3480  C   PHE A 307     6946   4282   2847    705   -357   -439       C  
ATOM   3481  O   PHE A 307      -4.316   8.389 -43.188  1.00 33.89           O  
ANISOU 3481  O   PHE A 307     6630   3834   2411    704   -352   -438       O  
ATOM   3482  CB  PHE A 307      -4.850   7.179 -40.070  1.00 33.61           C  
ANISOU 3482  CB  PHE A 307     6285   4020   2466    653   -271   -490       C  
ATOM   3483  CG  PHE A 307      -5.794   6.295 -40.836  1.00 32.99           C  
ANISOU 3483  CG  PHE A 307     6191   3974   2371    648   -275   -567       C  
ATOM   3484  CD1 PHE A 307      -6.910   6.825 -41.468  1.00 35.43           C  
ANISOU 3484  CD1 PHE A 307     6507   4300   2657    697   -378   -643       C  
ATOM   3485  CD2 PHE A 307      -5.565   4.932 -40.923  1.00 33.57           C  
ANISOU 3485  CD2 PHE A 307     6250   4059   2445    599   -176   -570       C  
ATOM   3486  CE1 PHE A 307      -7.777   6.012 -42.174  1.00 31.43           C  
ANISOU 3486  CE1 PHE A 307     5979   3837   2125    680   -389   -731       C  
ATOM   3487  CE2 PHE A 307      -6.429   4.114 -41.624  1.00 37.62           C  
ANISOU 3487  CE2 PHE A 307     6753   4603   2939    579   -175   -660       C  
ATOM   3488  CZ  PHE A 307      -7.534   4.654 -42.253  1.00 35.04           C  
ANISOU 3488  CZ  PHE A 307     6418   4310   2585    611   -285   -745       C  
ATOM   3489  N   ALA A 308      -4.867   9.837 -41.540  1.00 37.59           N  
ANISOU 3489  N   ALA A 308     7018   4347   2919    761   -444   -461       N  
ATOM   3490  CA  ALA A 308      -5.493  10.810 -42.430  1.00 39.29           C  
ANISOU 3490  CA  ALA A 308     7343   4491   3093    842   -549   -482       C  
ATOM   3491  C   ALA A 308      -4.538  11.251 -43.532  1.00 38.17           C  
ANISOU 3491  C   ALA A 308     7374   4221   2907    828   -528   -413       C  
ATOM   3492  O   ALA A 308      -4.893  11.243 -44.718  1.00 30.09           O  
ANISOU 3492  O   ALA A 308     6447   3152   1833    861   -569   -423       O  
ATOM   3493  CB  ALA A 308      -5.974  12.015 -41.638  1.00 29.00           C  
ANISOU 3493  CB  ALA A 308     6043   3178   1799    912   -629   -506       C  
ATOM   3494  N   LEU A 309      -3.325  11.627 -43.134  1.00 38.79           N  
ANISOU 3494  N   LEU A 309     7497   4246   2995    773   -464   -348       N  
ATOM   3495  CA  LEU A 309      -2.312  12.060 -44.091  1.00 35.78           C  
ANISOU 3495  CA  LEU A 309     7286   3742   2567    742   -424   -286       C  
ATOM   3496  C   LEU A 309      -1.994  10.967 -45.107  1.00 38.89           C  
ANISOU 3496  C   LEU A 309     7707   4132   2937    702   -349   -274       C  
ATOM   3497  O   LEU A 309      -1.879  11.237 -46.302  1.00 42.76           O  
ANISOU 3497  O   LEU A 309     8347   4533   3367    712   -357   -258       O  
ATOM   3498  CB  LEU A 309      -1.034  12.482 -43.364  1.00 37.16           C  
ANISOU 3498  CB  LEU A 309     7475   3891   2752    670   -356   -234       C  
ATOM   3499  CG  LEU A 309      -1.136  13.725 -42.478  1.00 43.37           C  
ANISOU 3499  CG  LEU A 309     8284   4652   3541    693   -421   -243       C  
ATOM   3500  CD1 LEU A 309       0.184  13.984 -41.771  1.00 43.88           C  
ANISOU 3500  CD1 LEU A 309     8351   4717   3603    600   -352   -201       C  
ATOM   3501  CD2 LEU A 309      -1.555  14.937 -43.297  1.00 42.92           C  
ANISOU 3501  CD2 LEU A 309     8423   4456   3430    763   -506   -244       C  
ATOM   3502  N   CYS A 310      -1.862   9.734 -44.626  1.00 37.32           N  
ANISOU 3502  N   CYS A 310     7380   4023   2778    660   -274   -284       N  
ATOM   3503  CA  CYS A 310      -1.520   8.607 -45.489  1.00 34.28           C  
ANISOU 3503  CA  CYS A 310     7025   3627   2371    623   -188   -277       C  
ATOM   3504  C   CYS A 310      -2.607   8.295 -46.515  1.00 33.75           C  
ANISOU 3504  C   CYS A 310     6991   3572   2259    658   -255   -337       C  
ATOM   3505  O   CYS A 310      -2.308   8.046 -47.683  1.00 36.71           O  
ANISOU 3505  O   CYS A 310     7484   3887   2578    641   -221   -326       O  
ATOM   3506  CB  CYS A 310      -1.236   7.359 -44.652  1.00 29.32           C  
ANISOU 3506  CB  CYS A 310     6271   3078   1792    585    -97   -277       C  
ATOM   3507  SG  CYS A 310       0.408   7.321 -43.904  1.00 43.73           S  
ANISOU 3507  SG  CYS A 310     8091   4886   3636    535     17   -196       S  
ATOM   3508  N   TYR A 311      -3.865   8.309 -46.084  1.00 34.64           N  
ANISOU 3508  N   TYR A 311     7002   3771   2388    703   -347   -409       N  
ATOM   3509  CA  TYR A 311      -4.960   7.943 -46.978  1.00 30.65           C  
ANISOU 3509  CA  TYR A 311     6507   3306   1833    731   -418   -484       C  
ATOM   3510  C   TYR A 311      -5.550   9.135 -47.728  1.00 31.90           C  
ANISOU 3510  C   TYR A 311     6784   3406   1930    816   -547   -492       C  
ATOM   3511  O   TYR A 311      -6.496   8.973 -48.495  1.00 46.49           O  
ANISOU 3511  O   TYR A 311     8648   5291   3723    853   -630   -558       O  
ATOM   3512  CB  TYR A 311      -6.068   7.229 -46.199  1.00 30.36           C  
ANISOU 3512  CB  TYR A 311     6301   3400   1834    729   -445   -577       C  
ATOM   3513  CG  TYR A 311      -5.799   5.761 -45.955  1.00 42.17           C  
ANISOU 3513  CG  TYR A 311     7726   4942   3356    651   -327   -597       C  
ATOM   3514  CD1 TYR A 311      -5.089   5.340 -44.837  1.00 28.67           C  
ANISOU 3514  CD1 TYR A 311     5946   3242   1704    618   -234   -550       C  
ATOM   3515  CD2 TYR A 311      -6.257   4.795 -46.843  1.00 30.62           C  
ANISOU 3515  CD2 TYR A 311     6279   3505   1851    615   -310   -668       C  
ATOM   3516  CE1 TYR A 311      -4.841   3.997 -44.611  1.00 35.94           C  
ANISOU 3516  CE1 TYR A 311     6831   4181   2643    566   -123   -561       C  
ATOM   3517  CE2 TYR A 311      -6.016   3.450 -46.625  1.00 38.34           C  
ANISOU 3517  CE2 TYR A 311     7216   4501   2853    550   -193   -692       C  
ATOM   3518  CZ  TYR A 311      -5.307   3.056 -45.507  1.00 40.75           C  
ANISOU 3518  CZ  TYR A 311     7467   4797   3217    533    -98   -632       C  
ATOM   3519  OH  TYR A 311      -5.060   1.721 -45.281  1.00 44.84           O  
ANISOU 3519  OH  TYR A 311     7972   5309   3756    485     24   -646       O  
ATOM   3520  N   LEU A 312      -5.002  10.328 -47.513  1.00 31.92           N  
ANISOU 3520  N   LEU A 312     6882   3312   1934    850   -568   -431       N  
ATOM   3521  CA  LEU A 312      -5.502  11.519 -48.207  1.00 33.30           C  
ANISOU 3521  CA  LEU A 312     7208   3401   2044    946   -687   -431       C  
ATOM   3522  C   LEU A 312      -5.257  11.534 -49.735  1.00 42.36           C  
ANISOU 3522  C   LEU A 312     8540   4462   3091    945   -690   -408       C  
ATOM   3523  O   LEU A 312      -6.215  11.691 -50.506  1.00 44.74           O  
ANISOU 3523  O   LEU A 312     8895   4778   3325   1020   -802   -458       O  
ATOM   3524  CB  LEU A 312      -4.906  12.784 -47.575  1.00 44.13           C  
ANISOU 3524  CB  LEU A 312     8663   4672   3434    971   -694   -377       C  
ATOM   3525  CG  LEU A 312      -5.378  14.114 -48.164  1.00 44.02           C  
ANISOU 3525  CG  LEU A 312     8837   4537   3352   1085   -814   -374       C  
ATOM   3526  CD1 LEU A 312      -6.889  14.247 -48.046  1.00 35.46           C  
ANISOU 3526  CD1 LEU A 312     7680   3532   2263   1210   -956   -460       C  
ATOM   3527  CD2 LEU A 312      -4.679  15.283 -47.487  1.00 34.58           C  
ANISOU 3527  CD2 LEU A 312     7739   3230   2170   1085   -801   -327       C  
ATOM   3528  N   PRO A 313      -3.990  11.373 -50.186  1.00 40.63           N  
ANISOU 3528  N   PRO A 313     8423   4159   2854    863   -569   -340       N  
ATOM   3529  CA  PRO A 313      -3.737  11.552 -51.624  1.00 40.01           C  
ANISOU 3529  CA  PRO A 313     8549   3986   2668    863   -568   -316       C  
ATOM   3530  C   PRO A 313      -4.477  10.548 -52.502  1.00 42.56           C  
ANISOU 3530  C   PRO A 313     8844   4395   2933    859   -596   -381       C  
ATOM   3531  O   PRO A 313      -5.002  10.914 -53.557  1.00 43.82           O  
ANISOU 3531  O   PRO A 313     9141   4519   2990    913   -685   -398       O  
ATOM   3532  CB  PRO A 313      -2.221  11.349 -51.747  1.00 35.57           C  
ANISOU 3532  CB  PRO A 313     8058   3345   2111    759   -405   -246       C  
ATOM   3533  CG  PRO A 313      -1.686  11.529 -50.368  1.00 47.37           C  
ANISOU 3533  CG  PRO A 313     9426   4867   3704    729   -360   -224       C  
ATOM   3534  CD  PRO A 313      -2.755  11.001 -49.472  1.00 44.47           C  
ANISOU 3534  CD  PRO A 313     8854   4638   3403    771   -430   -287       C  
ATOM   3535  N   ILE A 314      -4.521   9.294 -52.068  1.00 47.60           N  
ANISOU 3535  N   ILE A 314     9319   5140   3627    795   -524   -422       N  
ATOM   3536  CA  ILE A 314      -5.209   8.267 -52.833  1.00 51.86           C  
ANISOU 3536  CA  ILE A 314     9829   5763   4111    772   -541   -501       C  
ATOM   3537  C   ILE A 314      -6.713   8.525 -52.839  1.00 55.85           C  
ANISOU 3537  C   ILE A 314    10265   6365   4590    853   -709   -592       C  
ATOM   3538  O   ILE A 314      -7.407   8.128 -53.768  1.00 63.98           O  
ANISOU 3538  O   ILE A 314    11330   7446   5533    857   -775   -661       O  
ATOM   3539  CB  ILE A 314      -4.924   6.853 -52.283  1.00 48.69           C  
ANISOU 3539  CB  ILE A 314     9284   5437   3779    685   -417   -533       C  
ATOM   3540  CG1 ILE A 314      -5.247   5.796 -53.341  1.00 48.28           C  
ANISOU 3540  CG1 ILE A 314     9269   5424   3650    637   -393   -606       C  
ATOM   3541  CG2 ILE A 314      -5.704   6.604 -51.000  1.00 49.71           C  
ANISOU 3541  CG2 ILE A 314     9210   5678   3997    698   -456   -589       C  
ATOM   3542  CD1 ILE A 314      -4.607   6.061 -54.687  1.00 49.67           C  
ANISOU 3542  CD1 ILE A 314     9659   5496   3716    626   -361   -561       C  
ATOM   3543  N   SER A 315      -7.205   9.212 -51.811  1.00 59.53           N  
ANISOU 3543  N   SER A 315    10638   6857   5124    918   -779   -598       N  
ATOM   3544  CA  SER A 315      -8.629   9.496 -51.699  1.00 56.99           C  
ANISOU 3544  CA  SER A 315    10241   6625   4785   1008   -936   -690       C  
ATOM   3545  C   SER A 315      -9.036  10.636 -52.619  1.00 40.48           C  
ANISOU 3545  C   SER A 315     8334   4450   2595   1129  -1077   -675       C  
ATOM   3546  O   SER A 315     -10.062  10.550 -53.295  1.00 46.47           O  
ANISOU 3546  O   SER A 315     9100   5279   3279   1186  -1204   -753       O  
ATOM   3547  CB  SER A 315      -9.007   9.825 -50.254  1.00 37.42           C  
ANISOU 3547  CB  SER A 315     7609   4198   2410   1044   -952   -708       C  
ATOM   3548  OG  SER A 315      -8.928   8.670 -49.437  1.00 36.09           O  
ANISOU 3548  OG  SER A 315     7269   4128   2316    943   -846   -745       O  
ATOM   3549  N   VAL A 316      -8.241  11.703 -52.652  1.00 39.74           N  
ANISOU 3549  N   VAL A 316     8401   4204   2493   1166  -1058   -580       N  
ATOM   3550  CA  VAL A 316      -8.545  12.803 -53.563  1.00 41.73           C  
ANISOU 3550  CA  VAL A 316     8868   4347   2639   1283  -1182   -560       C  
ATOM   3551  C   VAL A 316      -8.358  12.343 -55.011  1.00 55.14           C  
ANISOU 3551  C   VAL A 316    10711   6029   4212   1240  -1173   -555       C  
ATOM   3552  O   VAL A 316      -9.187  12.645 -55.875  1.00 61.67           O  
ANISOU 3552  O   VAL A 316    11631   6869   4932   1330  -1315   -596       O  
ATOM   3553  CB  VAL A 316      -7.685  14.065 -53.274  1.00 41.57           C  
ANISOU 3553  CB  VAL A 316     9017   4148   2630   1316  -1149   -468       C  
ATOM   3554  CG1 VAL A 316      -6.220  13.717 -53.116  1.00 48.40           C  
ANISOU 3554  CG1 VAL A 316     9904   4952   3534   1172   -964   -390       C  
ATOM   3555  CG2 VAL A 316      -7.874  15.111 -54.365  1.00 43.87           C  
ANISOU 3555  CG2 VAL A 316     9576   4302   2792   1423  -1255   -444       C  
ATOM   3556  N   LEU A 317      -7.293  11.587 -55.271  1.00 54.91           N  
ANISOU 3556  N   LEU A 317    10699   5977   4189   1108  -1010   -512       N  
ATOM   3557  CA  LEU A 317      -7.064  11.051 -56.611  1.00 54.36           C  
ANISOU 3557  CA  LEU A 317    10764   5895   3997   1056   -982   -515       C  
ATOM   3558  C   LEU A 317      -8.189  10.111 -57.040  1.00 46.25           C  
ANISOU 3558  C   LEU A 317     9622   5032   2920   1051  -1070   -632       C  
ATOM   3559  O   LEU A 317      -8.612  10.127 -58.196  1.00 60.89           O  
ANISOU 3559  O   LEU A 317    11603   6895   4637   1078  -1155   -661       O  
ATOM   3560  CB  LEU A 317      -5.720  10.324 -56.686  1.00 44.22           C  
ANISOU 3560  CB  LEU A 317     9499   4560   2742    923   -779   -460       C  
ATOM   3561  CG  LEU A 317      -4.477  11.211 -56.754  1.00 44.12           C  
ANISOU 3561  CG  LEU A 317     9662   4376   2725    901   -683   -354       C  
ATOM   3562  CD1 LEU A 317      -3.219  10.367 -56.884  1.00 43.34           C  
ANISOU 3562  CD1 LEU A 317     9568   4248   2650    776   -485   -316       C  
ATOM   3563  CD2 LEU A 317      -4.590  12.193 -57.908  1.00 46.40           C  
ANISOU 3563  CD2 LEU A 317    10215   4546   2867    966   -764   -323       C  
ATOM   3564  N   ASN A 318      -8.673   9.298 -56.105  1.00 51.84           N  
ANISOU 3564  N   ASN A 318    10097   5870   3730   1010  -1051   -705       N  
ATOM   3565  CA  ASN A 318      -9.758   8.364 -56.392  1.00 55.98           C  
ANISOU 3565  CA  ASN A 318    10498   6555   4215    982  -1125   -837       C  
ATOM   3566  C   ASN A 318     -11.065   9.093 -56.678  1.00 60.70           C  
ANISOU 3566  C   ASN A 318    11104   7213   4746   1114  -1343   -902       C  
ATOM   3567  O   ASN A 318     -11.771   8.772 -57.637  1.00 61.01           O  
ANISOU 3567  O   ASN A 318    11181   7330   4669   1117  -1445   -980       O  
ATOM   3568  CB  ASN A 318      -9.953   7.391 -55.227  1.00 55.29           C  
ANISOU 3568  CB  ASN A 318    10175   6575   4255    902  -1042   -902       C  
ATOM   3569  CG  ASN A 318     -10.628   6.100 -55.645  1.00 61.71           C  
ANISOU 3569  CG  ASN A 318    10896   7524   5029    807  -1037  -1040       C  
ATOM   3570  OD1 ASN A 318     -11.347   6.054 -56.641  1.00 67.30           O  
ANISOU 3570  OD1 ASN A 318    11664   8289   5618    823  -1153  -1113       O  
ATOM   3571  ND2 ASN A 318     -10.396   5.040 -54.880  1.00 64.49           N  
ANISOU 3571  ND2 ASN A 318    11107   7923   5475    707   -905  -1081       N  
ATOM   3572  N   ILE A 319     -11.382  10.080 -55.845  1.00 63.06           N  
ANISOU 3572  N   ILE A 319    11372   7475   5115   1229  -1418   -875       N  
ATOM   3573  CA  ILE A 319     -12.637  10.809 -55.984  1.00 63.48           C  
ANISOU 3573  CA  ILE A 319    11422   7578   5120   1385  -1630   -940       C  
ATOM   3574  C   ILE A 319     -12.611  11.708 -57.219  1.00 66.79           C  
ANISOU 3574  C   ILE A 319    12096   7890   5392   1489  -1740   -888       C  
ATOM   3575  O   ILE A 319     -13.659  12.085 -57.742  1.00 70.65           O  
ANISOU 3575  O   ILE A 319    12610   8438   5797   1611  -1930   -952       O  
ATOM   3576  CB  ILE A 319     -12.955  11.650 -54.722  1.00 57.56           C  
ANISOU 3576  CB  ILE A 319    10583   6804   4484   1497  -1673   -933       C  
ATOM   3577  CG1 ILE A 319     -14.455  11.944 -54.640  1.00 60.38           C  
ANISOU 3577  CG1 ILE A 319    10843   7275   4824   1644  -1879  -1051       C  
ATOM   3578  CG2 ILE A 319     -12.141  12.935 -54.695  1.00 57.17           C  
ANISOU 3578  CG2 ILE A 319    10736   6555   4429   1580  -1655   -813       C  
ATOM   3579  CD1 ILE A 319     -15.314  10.703 -54.614  1.00 59.29           C  
ANISOU 3579  CD1 ILE A 319    10502   7334   4692   1547  -1900  -1189       C  
ATOM   3580  N   LEU A 320     -11.412  12.044 -57.688  1.00 64.65           N  
ANISOU 3580  N   LEU A 320    12017   7463   5083   1441  -1623   -775       N  
ATOM   3581  CA  LEU A 320     -11.277  12.774 -58.944  1.00 63.37           C  
ANISOU 3581  CA  LEU A 320    12123   7193   4764   1511  -1699   -723       C  
ATOM   3582  C   LEU A 320     -11.468  11.831 -60.125  1.00 67.48           C  
ANISOU 3582  C   LEU A 320    12678   7811   5152   1426  -1710   -778       C  
ATOM   3583  O   LEU A 320     -12.260  12.098 -61.029  1.00 70.03           O  
ANISOU 3583  O   LEU A 320    13095   8177   5337   1512  -1878   -818       O  
ATOM   3584  CB  LEU A 320      -9.912  13.458 -59.039  1.00 61.48           C  
ANISOU 3584  CB  LEU A 320    12087   6749   4524   1472  -1557   -594       C  
ATOM   3585  CG  LEU A 320      -9.688  14.717 -58.200  1.00 59.45           C  
ANISOU 3585  CG  LEU A 320    11896   6352   4342   1571  -1572   -536       C  
ATOM   3586  CD1 LEU A 320      -8.311  15.303 -58.479  1.00 59.09           C  
ANISOU 3586  CD1 LEU A 320    12069   6112   4271   1499  -1426   -426       C  
ATOM   3587  CD2 LEU A 320     -10.779  15.742 -58.464  1.00 61.08           C  
ANISOU 3587  CD2 LEU A 320    12203   6532   4473   1774  -1788   -572       C  
ATOM   3588  N   LYS A 321     -10.737  10.721 -60.095  1.00 69.43           N  
ANISOU 3588  N   LYS A 321    12852   8092   5437   1261  -1535   -784       N  
ATOM   3589  CA  LYS A 321     -10.727   9.753 -61.187  1.00 67.44           C  
ANISOU 3589  CA  LYS A 321    12648   7913   5061   1162  -1507   -841       C  
ATOM   3590  C   LYS A 321     -12.091   9.110 -61.430  1.00 68.97           C  
ANISOU 3590  C   LYS A 321    12699   8307   5201   1167  -1664   -991       C  
ATOM   3591  O   LYS A 321     -12.487   8.892 -62.575  1.00 77.32           O  
ANISOU 3591  O   LYS A 321    13860   9421   6096   1160  -1754  -1041       O  
ATOM   3592  CB  LYS A 321      -9.684   8.666 -60.904  1.00 65.56           C  
ANISOU 3592  CB  LYS A 321    12342   7664   4903   1002  -1279   -829       C  
ATOM   3593  CG  LYS A 321      -9.591   7.580 -61.961  1.00 60.44           C  
ANISOU 3593  CG  LYS A 321    11746   7079   4138    894  -1223   -901       C  
ATOM   3594  CD  LYS A 321      -8.455   6.617 -61.664  1.00 63.79           C  
ANISOU 3594  CD  LYS A 321    12132   7456   4648    766   -991   -877       C  
ATOM   3595  CE  LYS A 321      -8.276   5.611 -62.788  1.00 69.18           C  
ANISOU 3595  CE  LYS A 321    12906   8172   5208    670   -923   -948       C  
ATOM   3596  NZ  LYS A 321      -9.514   4.822 -63.033  1.00 75.30           N  
ANISOU 3596  NZ  LYS A 321    13553   9130   5928    637  -1041  -1116       N  
ATOM   3597  N   ARG A 322     -12.812   8.818 -60.353  1.00 61.48           N  
ANISOU 3597  N   ARG A 322    11514   7466   4378   1173  -1700  -1069       N  
ATOM   3598  CA  ARG A 322     -14.028   8.017 -60.454  1.00 65.83           C  
ANISOU 3598  CA  ARG A 322    11900   8215   4899   1134  -1815  -1231       C  
ATOM   3599  C   ARG A 322     -15.326   8.824 -60.509  1.00 71.76           C  
ANISOU 3599  C   ARG A 322    12619   9042   5606   1301  -2068  -1286       C  
ATOM   3600  O   ARG A 322     -16.380   8.278 -60.835  1.00 75.00           O  
ANISOU 3600  O   ARG A 322    12921   9617   5958   1279  -2198  -1423       O  
ATOM   3601  CB  ARG A 322     -14.096   7.035 -59.284  1.00 57.52           C  
ANISOU 3601  CB  ARG A 322    10606   7246   4002   1019  -1691  -1306       C  
ATOM   3602  CG  ARG A 322     -13.046   5.940 -59.340  1.00 62.93           C  
ANISOU 3602  CG  ARG A 322    11296   7895   4718    855  -1465  -1296       C  
ATOM   3603  CD  ARG A 322     -13.136   5.159 -60.640  1.00 58.17           C  
ANISOU 3603  CD  ARG A 322    10789   7351   3962    766  -1470  -1380       C  
ATOM   3604  NE  ARG A 322     -12.226   4.017 -60.657  1.00 66.00           N  
ANISOU 3604  NE  ARG A 322    11774   8309   4994    626  -1256  -1395       N  
ATOM   3605  CZ  ARG A 322     -12.094   3.185 -61.684  1.00 72.33           C  
ANISOU 3605  CZ  ARG A 322    12660   9140   5682    535  -1210  -1473       C  
ATOM   3606  NH1 ARG A 322     -12.812   3.367 -62.783  1.00 76.94           N  
ANISOU 3606  NH1 ARG A 322    13336   9802   6094    554  -1368  -1542       N  
ATOM   3607  NH2 ARG A 322     -11.243   2.171 -61.612  1.00 72.58           N  
ANISOU 3607  NH2 ARG A 322    12690   9118   5769    433  -1010  -1484       N  
ATOM   3608  N   VAL A 323     -15.261  10.112 -60.188  1.00 71.98           N  
ANISOU 3608  N   VAL A 323    12739   8948   5662   1470  -2139  -1191       N  
ATOM   3609  CA  VAL A 323     -16.463  10.943 -60.200  1.00 75.89           C  
ANISOU 3609  CA  VAL A 323    13211   9499   6126   1664  -2381  -1244       C  
ATOM   3610  C   VAL A 323     -16.292  12.191 -61.063  1.00 81.55           C  
ANISOU 3610  C   VAL A 323    14201  10071   6715   1826  -2493  -1143       C  
ATOM   3611  O   VAL A 323     -16.857  12.285 -62.154  1.00 85.66           O  
ANISOU 3611  O   VAL A 323    14824  10649   7075   1881  -2651  -1175       O  
ATOM   3612  CB  VAL A 323     -16.866  11.377 -58.775  1.00 72.03           C  
ANISOU 3612  CB  VAL A 323    12545   9015   5808   1757  -2393  -1265       C  
ATOM   3613  CG1 VAL A 323     -18.160  12.179 -58.812  1.00 73.25           C  
ANISOU 3613  CG1 VAL A 323    12660   9238   5934   1978  -2648  -1340       C  
ATOM   3614  CG2 VAL A 323     -17.018  10.166 -57.869  1.00 68.71           C  
ANISOU 3614  CG2 VAL A 323    11872   8726   5508   1594  -2272  -1360       C  
ATOM   3615  N   PHE A 324     -15.515  13.146 -60.564  1.00 82.01           N  
ANISOU 3615  N   PHE A 324    14384   9939   6837   1896  -2412  -1026       N  
ATOM   3616  CA  PHE A 324     -15.305  14.411 -61.260  1.00 82.25           C  
ANISOU 3616  CA  PHE A 324    14696   9800   6755   2047  -2499   -932       C  
ATOM   3617  C   PHE A 324     -14.281  14.268 -62.379  1.00 83.07           C  
ANISOU 3617  C   PHE A 324    15039   9800   6725   1935  -2386   -842       C  
ATOM   3618  O   PHE A 324     -13.099  14.559 -62.195  1.00 84.68           O  
ANISOU 3618  O   PHE A 324    15366   9840   6970   1865  -2210   -740       O  
ATOM   3619  CB  PHE A 324     -14.862  15.493 -60.274  1.00 78.65           C  
ANISOU 3619  CB  PHE A 324    14295   9172   6415   2147  -2448   -860       C  
ATOM   3620  CG  PHE A 324     -15.917  15.865 -59.275  1.00 77.56           C  
ANISOU 3620  CG  PHE A 324    13971   9114   6384   2301  -2580   -949       C  
ATOM   3621  CD1 PHE A 324     -17.244  15.980 -59.657  1.00 81.91           C  
ANISOU 3621  CD1 PHE A 324    14453   9801   6870   2455  -2814  -1051       C  
ATOM   3622  CD2 PHE A 324     -15.583  16.087 -57.950  1.00 74.93           C  
ANISOU 3622  CD2 PHE A 324    13526   8731   6213   2295  -2474   -937       C  
ATOM   3623  CE1 PHE A 324     -18.217  16.319 -58.737  1.00 83.60           C  
ANISOU 3623  CE1 PHE A 324    14486  10092   7185   2609  -2933  -1146       C  
ATOM   3624  CE2 PHE A 324     -16.549  16.425 -57.025  1.00 75.59           C  
ANISOU 3624  CE2 PHE A 324    13443   8889   6387   2443  -2587  -1028       C  
ATOM   3625  CZ  PHE A 324     -17.868  16.542 -57.418  1.00 80.33           C  
ANISOU 3625  CZ  PHE A 324    13973   9620   6930   2605  -2814  -1137       C  
ATOM   3626  N   GLY A 325     -14.744  13.822 -63.542  1.00 89.36           N  
ANISOU 3626  N   GLY A 325    19306   7787   6859   2488   -807    729       N  
ATOM   3627  CA  GLY A 325     -13.864  13.599 -64.675  1.00 90.45           C  
ANISOU 3627  CA  GLY A 325    19815   8212   6340   2551   -493    792       C  
ATOM   3628  C   GLY A 325     -12.907  12.457 -64.406  1.00 86.26           C  
ANISOU 3628  C   GLY A 325    19275   7611   5888   2523   -288    308       C  
ATOM   3629  O   GLY A 325     -13.229  11.544 -63.643  1.00 87.20           O  
ANISOU 3629  O   GLY A 325    19182   7528   6421   2533   -527    -96       O  
ATOM   3630  N   MET A 326     -11.729  12.515 -65.021  1.00 87.24           N  
ANISOU 3630  N   MET A 326    19438   7918   5791   2443    179    306       N  
ATOM   3631  CA  MET A 326     -10.716  11.481 -64.853  1.00 89.86           C  
ANISOU 3631  CA  MET A 326    19563   8211   6367   2362    455   -198       C  
ATOM   3632  C   MET A 326      -9.382  11.929 -65.456  1.00 93.25           C  
ANISOU 3632  C   MET A 326    20064   8791   6577   2262   1005    -36       C  
ATOM   3633  O   MET A 326      -9.305  12.947 -66.143  1.00 98.27           O  
ANISOU 3633  O   MET A 326    20918   9627   6794   2267   1152    441       O  
ATOM   3634  CB  MET A 326     -11.185  10.171 -65.501  1.00 95.79           C  
ANISOU 3634  CB  MET A 326    20285   9283   6827   2436    268   -800       C  
ATOM   3635  CG  MET A 326     -10.407   8.930 -65.097  1.00 96.44           C  
ANISOU 3635  CG  MET A 326    20070   9209   7362   2374    448  -1373       C  
ATOM   3636  SD  MET A 326     -10.867   7.438 -65.997  1.00138.53           S  
ANISOU 3636  SD  MET A 326    25076  14984  12577   2368    289  -2000       S  
ATOM   3637  CE  MET A 326     -12.446   7.063 -65.245  1.00 84.56           C  
ANISOU 3637  CE  MET A 326    17981   8001   6146   2436   -341  -1974       C  
ATOM   3638  N   PHE A 327      -8.333  11.170 -65.162  1.00 89.83           N  
ANISOU 3638  N   PHE A 327    19421   8243   6467   2172   1305   -408       N  
ATOM   3639  CA  PHE A 327      -7.038  11.309 -65.812  1.00 90.82           C  
ANISOU 3639  CA  PHE A 327    19590   8551   6366   2080   1827   -395       C  
ATOM   3640  C   PHE A 327      -6.974  10.271 -66.925  1.00 94.89           C  
ANISOU 3640  C   PHE A 327    20137   9533   6383   2110   1895   -925       C  
ATOM   3641  O   PHE A 327      -6.631   9.118 -66.674  1.00 93.33           O  
ANISOU 3641  O   PHE A 327    19704   9238   6520   2086   1946  -1471       O  
ATOM   3642  CB  PHE A 327      -5.889  11.094 -64.826  1.00 87.92           C  
ANISOU 3642  CB  PHE A 327    18947   7790   6669   1952   2137   -490       C  
ATOM   3643  CG  PHE A 327      -6.160  11.618 -63.433  1.00 84.38           C  
ANISOU 3643  CG  PHE A 327    18325   6874   6864   1908   1954   -224       C  
ATOM   3644  CD1 PHE A 327      -5.583  12.803 -62.994  1.00 84.36           C  
ANISOU 3644  CD1 PHE A 327    18341   6661   7050   1810   2204    249       C  
ATOM   3645  CD2 PHE A 327      -6.966  10.906 -62.552  1.00 82.40           C  
ANISOU 3645  CD2 PHE A 327    17857   6409   7043   1949   1547   -473       C  
ATOM   3646  CE1 PHE A 327      -5.822  13.272 -61.703  1.00 82.80           C  
ANISOU 3646  CE1 PHE A 327    17943   6077   7441   1742   2055    429       C  
ATOM   3647  CE2 PHE A 327      -7.218  11.366 -61.271  1.00 78.53           C  
ANISOU 3647  CE2 PHE A 327    17141   5586   7112   1875   1375   -250       C  
ATOM   3648  CZ  PHE A 327      -6.645  12.549 -60.842  1.00 78.22           C  
ANISOU 3648  CZ  PHE A 327    17025   5460   7236   1738   1617    174       C  
ATOM   3649  N   ARG A 328      -7.307  10.669 -68.147  1.00100.79           N  
ANISOU 3649  N   ARG A 328    21138  10802   6355   2151   1902   -769       N  
ATOM   3650  CA  ARG A 328      -7.475   9.699 -69.227  1.00110.41           C  
ANISOU 3650  CA  ARG A 328    22363  12543   7043   2169   1899  -1314       C  
ATOM   3651  C   ARG A 328      -7.099  10.221 -70.609  1.00117.43           C  
ANISOU 3651  C   ARG A 328    23343  14068   7209   2101   2142  -1095       C  
ATOM   3652  O   ARG A 328      -6.907   9.443 -71.544  1.00118.89           O  
ANISOU 3652  O   ARG A 328    23349  14735   7087   2030   2234  -1559       O  
ATOM   3653  CB  ARG A 328      -8.932   9.220 -69.243  1.00111.11           C  
ANISOU 3653  CB  ARG A 328    22367  12741   7110   2262   1345  -1490       C  
ATOM   3654  CG  ARG A 328      -9.939  10.326 -68.950  1.00109.52           C  
ANISOU 3654  CG  ARG A 328    22401  12431   6781   2361   1010   -868       C  
ATOM   3655  CD  ARG A 328     -11.374   9.857 -69.172  1.00110.29           C  
ANISOU 3655  CD  ARG A 328    22373  12732   6802   2435    490  -1037       C  
ATOM   3656  NE  ARG A 328     -12.331  10.688 -68.447  1.00107.86           N  
ANISOU 3656  NE  ARG A 328    22178  12100   6705   2527    132   -554       N  
ATOM   3657  CZ  ARG A 328     -12.800  11.852 -68.883  1.00110.41           C  
ANISOU 3657  CZ  ARG A 328    22597  12587   6767   2541     60     61       C  
ATOM   3658  NH1 ARG A 328     -12.407  12.334 -70.055  1.00116.68           N  
ANISOU 3658  NH1 ARG A 328    23417  13902   7015   2477    303    303       N  
ATOM   3659  NH2 ARG A 328     -13.663  12.535 -68.144  1.00104.39           N  
ANISOU 3659  NH2 ARG A 328    21811  11475   6378   2596   -249    423       N  
ATOM   3660  N   GLN A 329      -7.003  11.538 -70.738  1.00120.81           N  
ANISOU 3660  N   GLN A 329    23972  14508   7424   2104   2238   -385       N  
ATOM   3661  CA  GLN A 329      -6.819  12.149 -72.048  1.00127.49           C  
ANISOU 3661  CA  GLN A 329    24824  15989   7626   2038   2384    -68       C  
ATOM   3662  C   GLN A 329      -5.353  12.405 -72.400  1.00130.14           C  
ANISOU 3662  C   GLN A 329    25132  16405   7909   1914   2924     -3       C  
ATOM   3663  O   GLN A 329      -4.629  13.069 -71.656  1.00125.79           O  
ANISOU 3663  O   GLN A 329    24641  15382   7772   1890   3172    336       O  
ATOM   3664  CB  GLN A 329      -7.605  13.460 -72.131  1.00127.32           C  
ANISOU 3664  CB  GLN A 329    24890  15982   7505   2092   2150    706       C  
ATOM   3665  CG  GLN A 329      -7.600  14.102 -73.506  1.00133.20           C  
ANISOU 3665  CG  GLN A 329    25566  17441   7603   2017   2226   1085       C  
ATOM   3666  CD  GLN A 329      -8.626  15.208 -73.633  1.00132.30           C  
ANISOU 3666  CD  GLN A 329    25421  17374   7471   2067   1909   1766       C  
ATOM   3667  OE1 GLN A 329      -9.550  15.306 -72.827  1.00127.22           O  
ANISOU 3667  OE1 GLN A 329    24793  16321   7222   2165   1564   1833       O  
ATOM   3668  NE2 GLN A 329      -8.467  16.051 -74.647  1.00134.69           N  
ANISOU 3668  NE2 GLN A 329    25633  18187   7358   1983   2022   2276       N  
ATOM   3669  N   ALA A 330      -4.933  11.857 -73.540  1.00137.30           N  
ANISOU 3669  N   ALA A 330    25908  17936   8324   1818   3099   -355       N  
ATOM   3670  CA  ALA A 330      -3.618  12.118 -74.129  1.00139.76           C  
ANISOU 3670  CA  ALA A 330    26158  18477   8467   1688   3576   -286       C  
ATOM   3671  C   ALA A 330      -2.451  11.833 -73.184  1.00135.10           C  
ANISOU 3671  C   ALA A 330    25523  17287   8521   1645   3933   -485       C  
ATOM   3672  O   ALA A 330      -2.496  10.898 -72.384  1.00128.14           O  
ANISOU 3672  O   ALA A 330    24546  16012   8132   1674   3865   -981       O  
ATOM   3673  CB  ALA A 330      -3.547  13.559 -74.624  1.00141.50           C  
ANISOU 3673  CB  ALA A 330    26456  18901   8406   1665   3639    544       C  
ATOM   3674  N   SER A 331      -1.409  12.654 -73.289  1.00137.48           N  
ANISOU 3674  N   SER A 331    25836  17539   8862   1562   4298    -75       N  
ATOM   3675  CA  SER A 331      -0.193  12.476 -72.502  1.00133.46           C  
ANISOU 3675  CA  SER A 331    25235  16538   8936   1490   4669   -212       C  
ATOM   3676  C   SER A 331      -0.309  13.108 -71.119  1.00128.67           C  
ANISOU 3676  C   SER A 331    24716  15217   8957   1539   4617    160       C  
ATOM   3677  O   SER A 331       0.590  13.818 -70.670  1.00127.64           O  
ANISOU 3677  O   SER A 331    24544  14784   9170   1464   4907    492       O  
ATOM   3678  CB  SER A 331       1.010  13.064 -73.244  1.00135.36           C  
ANISOU 3678  CB  SER A 331    25405  17065   8963   1365   5071     36       C  
ATOM   3679  OG  SER A 331       2.196  12.926 -72.482  1.00129.75           O  
ANISOU 3679  OG  SER A 331    24574  15885   8840   1287   5412    -72       O  
ATOM   3680  N   ASP A 332      -1.426  12.845 -70.451  1.00126.42           N  
ANISOU 3680  N   ASP A 332    24514  14690   8832   1652   4234     79       N  
ATOM   3681  CA  ASP A 332      -1.639  13.315 -69.090  1.00123.95           C  
ANISOU 3681  CA  ASP A 332    24201  13746   9150   1677   4127    346       C  
ATOM   3682  C   ASP A 332      -1.579  12.126 -68.137  1.00121.61           C  
ANISOU 3682  C   ASP A 332    23617  13093   9496   1663   4007   -232       C  
ATOM   3683  O   ASP A 332      -2.074  12.188 -67.014  1.00118.37           O  
ANISOU 3683  O   ASP A 332    23073  12253   9650   1680   3738   -157       O  
ATOM   3684  CB  ASP A 332      -2.984  14.042 -68.975  1.00125.70           C  
ANISOU 3684  CB  ASP A 332    24561  13939   9261   1786   3681    770       C  
ATOM   3685  CG  ASP A 332      -3.114  14.840 -67.691  1.00122.62           C  
ANISOU 3685  CG  ASP A 332    24076  12950   9565   1764   3589   1143       C  
ATOM   3686  OD1 ASP A 332      -2.076  15.284 -67.158  1.00123.64           O  
ANISOU 3686  OD1 ASP A 332    24107  12789  10080   1654   3948   1296       O  
ATOM   3687  OD2 ASP A 332      -4.254  15.022 -67.214  1.00120.27           O  
ANISOU 3687  OD2 ASP A 332    23786  12488   9424   1847   3163   1261       O  
ATOM   3688  N   ARG A 333      -0.963  11.040 -68.595  1.00118.71           N  
ANISOU 3688  N   ARG A 333    23127  12916   9060   1624   4219   -804       N  
ATOM   3689  CA  ARG A 333      -0.961   9.790 -67.843  1.00116.52           C  
ANISOU 3689  CA  ARG A 333    22543  12344   9386   1624   4103  -1364       C  
ATOM   3690  C   ARG A 333       0.392   9.464 -67.211  1.00114.35           C  
ANISOU 3690  C   ARG A 333    22012  11752   9684   1504   4510  -1491       C  
ATOM   3691  O   ARG A 333       0.454   9.023 -66.063  1.00114.49           O  
ANISOU 3691  O   ARG A 333    21741  11348  10413   1478   4398  -1578       O  
ATOM   3692  CB  ARG A 333      -1.396   8.633 -68.747  1.00121.91           C  
ANISOU 3692  CB  ARG A 333    23102  13437   9782   1651   3949  -1968       C  
ATOM   3693  CG  ARG A 333      -1.572   7.313 -68.016  1.00120.85           C  
ANISOU 3693  CG  ARG A 333    22526  13016  10376   1645   3730  -2481       C  
ATOM   3694  CD  ARG A 333      -2.610   7.440 -66.911  1.00118.15           C  
ANISOU 3694  CD  ARG A 333    22181  12285  10424   1738   3292  -2300       C  
ATOM   3695  NE  ARG A 333      -2.693   6.235 -66.092  1.00116.13           N  
ANISOU 3695  NE  ARG A 333    21376  11778  10971   1698   3067  -2652       N  
ATOM   3696  CZ  ARG A 333      -3.603   5.280 -66.254  1.00116.73           C  
ANISOU 3696  CZ  ARG A 333    21212  11986  11154   1747   2699  -3034       C  
ATOM   3697  NH1 ARG A 333      -4.519   5.388 -67.207  1.00120.00           N  
ANISOU 3697  NH1 ARG A 333    21901  12787  10905   1832   2506  -3144       N  
ATOM   3698  NH2 ARG A 333      -3.600   4.218 -65.461  1.00114.13           N  
ANISOU 3698  NH2 ARG A 333    20316  11444  11603   1700   2520  -3276       N  
ATOM   3699  N   GLU A 334       1.474   9.685 -67.953  1.00112.57           N  
ANISOU 3699  N   GLU A 334    21783  11772   9218   1403   4912  -1443       N  
ATOM   3700  CA  GLU A 334       2.800   9.263 -67.506  1.00107.16           C  
ANISOU 3700  CA  GLU A 334    20769  10862   9086   1268   5250  -1579       C  
ATOM   3701  C   GLU A 334       3.406  10.185 -66.446  1.00102.17           C  
ANISOU 3701  C   GLU A 334    20143   9807   8869   1200   5449  -1106       C  
ATOM   3702  O   GLU A 334       4.589  10.079 -66.126  1.00103.28           O  
ANISOU 3702  O   GLU A 334    20043   9804   9396   1072   5751  -1100       O  
ATOM   3703  CB  GLU A 334       3.749   9.148 -68.702  1.00111.85           C  
ANISOU 3703  CB  GLU A 334    21332  11884   9281   1180   5584  -1729       C  
ATOM   3704  CG  GLU A 334       3.292   8.147 -69.759  1.00118.71           C  
ANISOU 3704  CG  GLU A 334    22102  13223   9780   1209   5443  -2292       C  
ATOM   3705  CD  GLU A 334       3.131   6.736 -69.214  1.00116.34           C  
ANISOU 3705  CD  GLU A 334    21382  12699  10123   1215   5256  -2851       C  
ATOM   3706  OE1 GLU A 334       3.828   6.380 -68.239  1.00110.90           O  
ANISOU 3706  OE1 GLU A 334    20391  11590  10155   1151   5351  -2838       O  
ATOM   3707  OE2 GLU A 334       2.303   5.979 -69.764  1.00118.60           O  
ANISOU 3707  OE2 GLU A 334    21591  13258  10215   1276   4997  -3277       O  
ATOM   3708  N   ALA A 335       2.592  11.087 -65.911  1.00 94.44           N  
ANISOU 3708  N   ALA A 335    19373   8656   7855   1265   5238   -702       N  
ATOM   3709  CA  ALA A 335       2.965  11.870 -64.739  1.00 90.01           C  
ANISOU 3709  CA  ALA A 335    18678   7690   7831   1173   5304   -311       C  
ATOM   3710  C   ALA A 335       1.964  11.573 -63.632  1.00 85.00           C  
ANISOU 3710  C   ALA A 335    17845   6770   7682   1213   4833   -360       C  
ATOM   3711  O   ALA A 335       2.291  11.596 -62.445  1.00 85.12           O  
ANISOU 3711  O   ALA A 335    17578   6461   8303   1117   4842   -290       O  
ATOM   3712  CB  ALA A 335       2.993  13.350 -65.061  1.00 91.71           C  
ANISOU 3712  CB  ALA A 335    19162   7954   7728   1156   5434    282       C  
ATOM   3713  N   VAL A 336       0.736  11.290 -64.049  1.00 85.86           N  
ANISOU 3713  N   VAL A 336    18091   7042   7489   1346   4421   -482       N  
ATOM   3714  CA  VAL A 336      -0.326  10.860 -63.150  1.00 81.63           C  
ANISOU 3714  CA  VAL A 336    17381   6289   7344   1404   3939   -589       C  
ATOM   3715  C   VAL A 336       0.013   9.493 -62.552  1.00 84.94           C  
ANISOU 3715  C   VAL A 336    17368   6586   8321   1360   3896  -1037       C  
ATOM   3716  O   VAL A 336      -0.265   9.217 -61.378  1.00 84.18           O  
ANISOU 3716  O   VAL A 336    16787   6375   8821   1263   3567   -945       O  
ATOM   3717  CB  VAL A 336      -1.680  10.815 -63.897  1.00 83.75           C  
ANISOU 3717  CB  VAL A 336    17901   6819   7102   1558   3527   -636       C  
ATOM   3718  CG1 VAL A 336      -2.619   9.784 -63.297  1.00 80.69           C  
ANISOU 3718  CG1 VAL A 336    17299   6300   7059   1633   3083  -1001       C  
ATOM   3719  CG2 VAL A 336      -2.315  12.195 -63.905  1.00 83.76           C  
ANISOU 3719  CG2 VAL A 336    18146   6800   6879   1585   3388    -68       C  
ATOM   3720  N   TYR A 337       0.636   8.656 -63.375  1.00 83.07           N  
ANISOU 3720  N   TYR A 337    17039   6581   7944   1343   4108  -1394       N  
ATOM   3721  CA  TYR A 337       1.096   7.332 -62.973  1.00 82.07           C  
ANISOU 3721  CA  TYR A 337    16311   6459   8415   1249   4025  -1724       C  
ATOM   3722  C   TYR A 337       1.988   7.386 -61.734  1.00 78.00           C  
ANISOU 3722  C   TYR A 337    15343   5739   8557   1076   4126  -1472       C  
ATOM   3723  O   TYR A 337       1.810   6.606 -60.795  1.00 74.69           O  
ANISOU 3723  O   TYR A 337    14378   5295   8705   1016   3814  -1523       O  
ATOM   3724  CB  TYR A 337       1.837   6.676 -64.141  1.00 87.35           C  
ANISOU 3724  CB  TYR A 337    16992   7390   8806   1239   4343  -2110       C  
ATOM   3725  CG  TYR A 337       2.672   5.473 -63.775  1.00 87.00           C  
ANISOU 3725  CG  TYR A 337    16366   7290   9401   1137   4409  -2396       C  
ATOM   3726  CD1 TYR A 337       2.090   4.226 -63.598  1.00 86.58           C  
ANISOU 3726  CD1 TYR A 337    15902   7258   9737   1184   4059  -2762       C  
ATOM   3727  CD2 TYR A 337       4.051   5.580 -63.629  1.00 87.38           C  
ANISOU 3727  CD2 TYR A 337    16271   7265   9666   1003   4823  -2283       C  
ATOM   3728  CE1 TYR A 337       2.855   3.120 -63.272  1.00 86.65           C  
ANISOU 3728  CE1 TYR A 337    15387   7199  10337   1116   4118  -2984       C  
ATOM   3729  CE2 TYR A 337       4.823   4.481 -63.303  1.00 87.34           C  
ANISOU 3729  CE2 TYR A 337    15749   7202  10234    922   4881  -2507       C  
ATOM   3730  CZ  TYR A 337       4.222   3.253 -63.126  1.00 87.06           C  
ANISOU 3730  CZ  TYR A 337    15326   7174  10578    985   4531  -2845       C  
ATOM   3731  OH  TYR A 337       4.991   2.158 -62.802  1.00 87.35           O  
ANISOU 3731  OH  TYR A 337    14863   7133  11194    921   4594  -3021       O  
ATOM   3732  N   ALA A 338       2.934   8.321 -61.731  1.00 78.45           N  
ANISOU 3732  N   ALA A 338    15599   5709   8500    992   4554  -1186       N  
ATOM   3733  CA  ALA A 338       3.874   8.470 -60.623  1.00 75.09           C  
ANISOU 3733  CA  ALA A 338    14752   5169   8610    804   4696   -942       C  
ATOM   3734  C   ALA A 338       3.164   8.823 -59.318  1.00 69.98           C  
ANISOU 3734  C   ALA A 338    13772   4514   8303    738   4284   -684       C  
ATOM   3735  O   ALA A 338       3.401   8.197 -58.280  1.00 66.78           O  
ANISOU 3735  O   ALA A 338    12772   4195   8406    624   4091   -684       O  
ATOM   3736  CB  ALA A 338       4.914   9.525 -60.958  1.00 76.88           C  
ANISOU 3736  CB  ALA A 338    15299   5313   8599    735   5231   -686       C  
ATOM   3737  N   CYS A 339       2.294   9.827 -59.377  1.00 69.49           N  
ANISOU 3737  N   CYS A 339    14061   4403   7938    811   4136   -469       N  
ATOM   3738  CA  CYS A 339       1.542  10.259 -58.204  1.00 65.00           C  
ANISOU 3738  CA  CYS A 339    13115   3941   7642    737   3705   -271       C  
ATOM   3739  C   CYS A 339       0.642   9.142 -57.684  1.00 62.62           C  
ANISOU 3739  C   CYS A 339    12388   3760   7645    773   3169   -490       C  
ATOM   3740  O   CYS A 339       0.473   8.983 -56.473  1.00 58.61           O  
ANISOU 3740  O   CYS A 339    11325   3401   7543    664   2854   -420       O  
ATOM   3741  CB  CYS A 339       0.709  11.503 -58.525  1.00 65.66           C  
ANISOU 3741  CB  CYS A 339    13640   3956   7351    823   3628    -28       C  
ATOM   3742  SG  CYS A 339       1.678  13.013 -58.772  1.00 75.19           S  
ANISOU 3742  SG  CYS A 339    15132   5073   8367    755   4159    301       S  
ATOM   3743  N   PHE A 340       0.074   8.364 -58.601  1.00 44.89           N  
ANISOU 3743  N   PHE A 340     7705   5875   3478   1019    600   -464       N  
ATOM   3744  CA  PHE A 340      -0.772   7.240 -58.213  1.00 48.21           C  
ANISOU 3744  CA  PHE A 340     8081   6293   3946    976    379   -586       C  
ATOM   3745  C   PHE A 340       0.027   6.155 -57.492  1.00 52.05           C  
ANISOU 3745  C   PHE A 340     8409   6785   4583    938    465   -677       C  
ATOM   3746  O   PHE A 340      -0.391   5.665 -56.438  1.00 54.57           O  
ANISOU 3746  O   PHE A 340     8593   7101   5039    876    370   -753       O  
ATOM   3747  CB  PHE A 340      -1.481   6.652 -59.435  1.00 48.73           C  
ANISOU 3747  CB  PHE A 340     8379   6333   3803    978    193   -583       C  
ATOM   3748  CG  PHE A 340      -2.920   7.070 -59.558  1.00 46.67           C  
ANISOU 3748  CG  PHE A 340     8174   6088   3470    970    -92   -566       C  
ATOM   3749  CD1 PHE A 340      -3.921   6.359 -58.914  1.00 45.24           C  
ANISOU 3749  CD1 PHE A 340     7883   5945   3361    878   -320   -659       C  
ATOM   3750  CD2 PHE A 340      -3.272   8.177 -60.311  1.00 46.20           C  
ANISOU 3750  CD2 PHE A 340     8265   6022   3267   1053   -151   -443       C  
ATOM   3751  CE1 PHE A 340      -5.248   6.745 -59.024  1.00 39.01           C  
ANISOU 3751  CE1 PHE A 340     7024   5225   2573    856   -598   -626       C  
ATOM   3752  CE2 PHE A 340      -4.595   8.567 -60.427  1.00 45.07           C  
ANISOU 3752  CE2 PHE A 340     8057   5909   3157   1053   -447   -405       C  
ATOM   3753  CZ  PHE A 340      -5.584   7.850 -59.782  1.00 40.47           C  
ANISOU 3753  CZ  PHE A 340     7279   5407   2692    960   -666   -502       C  
ATOM   3754  N   THR A 341       1.175   5.785 -58.056  1.00 48.18           N  
ANISOU 3754  N   THR A 341     7941   6316   4050    989    639   -663       N  
ATOM   3755  CA  THR A 341       2.028   4.775 -57.433  1.00 50.30           C  
ANISOU 3755  CA  THR A 341     8081   6593   4439   1001    702   -742       C  
ATOM   3756  C   THR A 341       2.504   5.235 -56.055  1.00 48.13           C  
ANISOU 3756  C   THR A 341     7542   6357   4390    957    779   -755       C  
ATOM   3757  O   THR A 341       2.560   4.443 -55.106  1.00 51.01           O  
ANISOU 3757  O   THR A 341     7808   6697   4877    927    712   -826       O  
ATOM   3758  CB  THR A 341       3.251   4.437 -58.311  1.00 55.33           C  
ANISOU 3758  CB  THR A 341     8762   7288   4972   1105    890   -730       C  
ATOM   3759  OG1 THR A 341       3.988   5.632 -58.596  1.00 57.43           O  
ANISOU 3759  OG1 THR A 341     8947   7652   5221   1107   1107   -624       O  
ATOM   3760  CG2 THR A 341       2.809   3.794 -59.616  1.00 58.72           C  
ANISOU 3760  CG2 THR A 341     9476   7662   5172   1163    800   -744       C  
ATOM   3761  N   PHE A 342       2.833   6.519 -55.949  1.00 42.74           N  
ANISOU 3761  N   PHE A 342     6779   5716   3744    948    913   -678       N  
ATOM   3762  CA  PHE A 342       3.255   7.088 -54.675  1.00 38.59           C  
ANISOU 3762  CA  PHE A 342     6027   5212   3422    904    975   -696       C  
ATOM   3763  C   PHE A 342       2.128   7.033 -53.648  1.00 36.49           C  
ANISOU 3763  C   PHE A 342     5710   4897   3259    853    791   -761       C  
ATOM   3764  O   PHE A 342       2.354   6.693 -52.484  1.00 38.93           O  
ANISOU 3764  O   PHE A 342     5857   5214   3722    811    767   -821       O  
ATOM   3765  CB  PHE A 342       3.728   8.530 -54.853  1.00 36.31           C  
ANISOU 3765  CB  PHE A 342     5731   4938   3127    893   1159   -589       C  
ATOM   3766  CG  PHE A 342       4.076   9.213 -53.562  1.00 40.06           C  
ANISOU 3766  CG  PHE A 342     5983   5399   3838    817   1177   -607       C  
ATOM   3767  CD1 PHE A 342       5.258   8.917 -52.904  1.00 42.12           C  
ANISOU 3767  CD1 PHE A 342     6045   5751   4209    815   1299   -647       C  
ATOM   3768  CD2 PHE A 342       3.219  10.149 -53.003  1.00 42.38           C  
ANISOU 3768  CD2 PHE A 342     6250   5591   4262    749   1034   -588       C  
ATOM   3769  CE1 PHE A 342       5.580   9.542 -51.713  1.00 42.53           C  
ANISOU 3769  CE1 PHE A 342     5893   5780   4486    712   1259   -665       C  
ATOM   3770  CE2 PHE A 342       3.535  10.779 -51.812  1.00 39.06           C  
ANISOU 3770  CE2 PHE A 342     5650   5135   4055    671   1017   -619       C  
ATOM   3771  CZ  PHE A 342       4.717  10.475 -51.166  1.00 41.05           C  
ANISOU 3771  CZ  PHE A 342     5724   5467   4405    635   1120   -657       C  
ATOM   3772  N   SER A 343       0.916   7.368 -54.084  1.00 33.94           N  
ANISOU 3772  N   SER A 343     5524   4543   2829    865    659   -747       N  
ATOM   3773  CA  SER A 343      -0.251   7.320 -53.208  1.00 38.68           C  
ANISOU 3773  CA  SER A 343     6043   5151   3502    829    490   -808       C  
ATOM   3774  C   SER A 343      -0.500   5.904 -52.696  1.00 40.87           C  
ANISOU 3774  C   SER A 343     6304   5430   3795    750    387   -881       C  
ATOM   3775  O   SER A 343      -0.743   5.700 -51.501  1.00 47.43           O  
ANISOU 3775  O   SER A 343     6994   6286   4743    695    354   -930       O  
ATOM   3776  CB  SER A 343      -1.490   7.845 -53.933  1.00 39.57           C  
ANISOU 3776  CB  SER A 343     6224   5265   3547    832    320   -747       C  
ATOM   3777  OG  SER A 343      -1.358   9.225 -54.227  1.00 42.23           O  
ANISOU 3777  OG  SER A 343     6555   5554   3938    873    373   -645       O  
ATOM   3778  N   HIS A 344      -0.433   4.933 -53.604  1.00 34.50           N  
ANISOU 3778  N   HIS A 344     5666   4581   2860    745    337   -881       N  
ATOM   3779  CA  HIS A 344      -0.567   3.524 -53.239  1.00 34.56           C  
ANISOU 3779  CA  HIS A 344     5728   4539   2866    675    238   -938       C  
ATOM   3780  C   HIS A 344       0.462   3.137 -52.181  1.00 34.60           C  
ANISOU 3780  C   HIS A 344     5590   4535   3021    684    341   -960       C  
ATOM   3781  O   HIS A 344       0.110   2.620 -51.105  1.00 34.61           O  
ANISOU 3781  O   HIS A 344     5539   4526   3084    607    271   -995       O  
ATOM   3782  CB  HIS A 344      -0.410   2.632 -54.473  1.00 30.39           C  
ANISOU 3782  CB  HIS A 344     5428   3938   2181    712    191   -941       C  
ATOM   3783  CG  HIS A 344      -1.455   2.860 -55.521  1.00 40.48           C  
ANISOU 3783  CG  HIS A 344     6870   5216   3293    686     41   -922       C  
ATOM   3784  ND1 HIS A 344      -1.162   2.897 -56.867  1.00 33.54           N  
ANISOU 3784  ND1 HIS A 344     6175   4312   2258    768     70   -889       N  
ATOM   3785  CD2 HIS A 344      -2.791   3.055 -55.421  1.00 40.12           C  
ANISOU 3785  CD2 HIS A 344     6828   5215   3202    588   -161   -930       C  
ATOM   3786  CE1 HIS A 344      -2.272   3.109 -57.552  1.00 34.65           C  
ANISOU 3786  CE1 HIS A 344     6437   4460   2268    720   -120   -873       C  
ATOM   3787  NE2 HIS A 344      -3.275   3.208 -56.698  1.00 40.55           N  
ANISOU 3787  NE2 HIS A 344     7062   5260   3086    610   -273   -897       N  
ATOM   3788  N   TRP A 345       1.731   3.404 -52.482  1.00 24.97           N  
ANISOU 3788  N   TRP A 345     4313   3338   1838    775    499   -936       N  
ATOM   3789  CA  TRP A 345       2.801   3.093 -51.542  1.00 24.52           C  
ANISOU 3789  CA  TRP A 345     4114   3292   1909    803    575   -959       C  
ATOM   3790  C   TRP A 345       2.559   3.730 -50.181  1.00 32.74           C  
ANISOU 3790  C   TRP A 345     4984   4360   3096    725    563   -969       C  
ATOM   3791  O   TRP A 345       2.869   3.132 -49.158  1.00 38.96           O  
ANISOU 3791  O   TRP A 345     5726   5127   3951    711    532   -996       O  
ATOM   3792  CB  TRP A 345       4.164   3.547 -52.066  1.00 25.66           C  
ANISOU 3792  CB  TRP A 345     4172   3510   2068    900    758   -935       C  
ATOM   3793  CG  TRP A 345       5.229   3.367 -51.024  1.00 28.75           C  
ANISOU 3793  CG  TRP A 345     4393   3936   2595    934    816   -963       C  
ATOM   3794  CD1 TRP A 345       5.966   2.244 -50.792  1.00 37.70           C  
ANISOU 3794  CD1 TRP A 345     5556   5046   3724   1038    801  -1001       C  
ATOM   3795  CD2 TRP A 345       5.644   4.328 -50.044  1.00 24.46           C  
ANISOU 3795  CD2 TRP A 345     3651   3445   2198    885    874   -958       C  
ATOM   3796  NE1 TRP A 345       6.823   2.450 -49.739  1.00 42.15           N  
ANISOU 3796  NE1 TRP A 345     5936   5660   4418   1064    843  -1014       N  
ATOM   3797  CE2 TRP A 345       6.646   3.721 -49.262  1.00 41.57           C  
ANISOU 3797  CE2 TRP A 345     5723   5633   4441    960    887   -990       C  
ATOM   3798  CE3 TRP A 345       5.270   5.645 -49.756  1.00 23.64           C  
ANISOU 3798  CE3 TRP A 345     3465   3361   2155    812    905   -935       C  
ATOM   3799  CZ2 TRP A 345       7.281   4.385 -48.215  1.00 37.36           C  
ANISOU 3799  CZ2 TRP A 345     5002   5155   4037    949    920   -996       C  
ATOM   3800  CZ3 TRP A 345       5.900   6.302 -48.716  1.00 23.30           C  
ANISOU 3800  CZ3 TRP A 345     3255   3353   2245    796    947   -953       C  
ATOM   3801  CH2 TRP A 345       6.894   5.671 -47.958  1.00 23.73           C  
ANISOU 3801  CH2 TRP A 345     3203   3444   2368    857    948   -980       C  
ATOM   3802  N   LEU A 346       2.025   4.947 -50.175  1.00 30.56           N  
ANISOU 3802  N   LEU A 346     4643   4120   2849    698    584   -946       N  
ATOM   3803  CA  LEU A 346       1.719   5.645 -48.930  1.00 27.58           C  
ANISOU 3803  CA  LEU A 346     4124   3761   2596    650    570   -964       C  
ATOM   3804  C   LEU A 346       0.669   4.871 -48.134  1.00 35.64           C  
ANISOU 3804  C   LEU A 346     5169   4785   3589    577    444   -998       C  
ATOM   3805  O   LEU A 346       0.828   4.618 -46.922  1.00 39.03           O  
ANISOU 3805  O   LEU A 346     5529   5216   4086    539    433  -1015       O  
ATOM   3806  CB  LEU A 346       1.232   7.065 -49.227  1.00 24.19           C  
ANISOU 3806  CB  LEU A 346     3666   3350   2176    684    596   -945       C  
ATOM   3807  CG  LEU A 346       1.227   8.060 -48.069  1.00 34.25           C  
ANISOU 3807  CG  LEU A 346     4798   4627   3589    674    604   -978       C  
ATOM   3808  CD1 LEU A 346       2.621   8.177 -47.477  1.00 36.58           C  
ANISOU 3808  CD1 LEU A 346     5001   4917   3981    661    694   -989       C  
ATOM   3809  CD2 LEU A 346       0.723   9.416 -48.537  1.00 33.40           C  
ANISOU 3809  CD2 LEU A 346     4711   4483   3499    719    600   -942       C  
ATOM   3810  N   VAL A 347      -0.399   4.493 -48.838  1.00 34.85           N  
ANISOU 3810  N   VAL A 347     5185   4697   3358    556    342  -1008       N  
ATOM   3811  CA  VAL A 347      -1.463   3.676 -48.264  1.00 32.94           C  
ANISOU 3811  CA  VAL A 347     4982   4493   3041    458    211  -1050       C  
ATOM   3812  C   VAL A 347      -0.895   2.457 -47.557  1.00 35.72           C  
ANISOU 3812  C   VAL A 347     5413   4765   3396    404    195  -1060       C  
ATOM   3813  O   VAL A 347      -1.249   2.172 -46.411  1.00 34.43           O  
ANISOU 3813  O   VAL A 347     5207   4641   3235    331    163  -1081       O  
ATOM   3814  CB  VAL A 347      -2.465   3.202 -49.336  1.00 29.94           C  
ANISOU 3814  CB  VAL A 347     4759   4116   2502    406     61  -1053       C  
ATOM   3815  CG1 VAL A 347      -3.417   2.165 -48.757  1.00 27.19           C  
ANISOU 3815  CG1 VAL A 347     4427   3786   2118    204    -87  -1048       C  
ATOM   3816  CG2 VAL A 347      -3.232   4.375 -49.895  1.00 31.36           C  
ANISOU 3816  CG2 VAL A 347     4808   4386   2721    438     34  -1001       C  
ATOM   3817  N   TYR A 348       0.001   1.744 -48.231  1.00 34.24           N  
ANISOU 3817  N   TYR A 348     5339   4481   3190    469    213  -1048       N  
ATOM   3818  CA  TYR A 348       0.594   0.560 -47.609  1.00 32.75           C  
ANISOU 3818  CA  TYR A 348     5244   4203   2996    480    173  -1060       C  
ATOM   3819  C   TYR A 348       1.596   0.920 -46.511  1.00 34.39           C  
ANISOU 3819  C   TYR A 348     5299   4442   3325    541    258  -1059       C  
ATOM   3820  O   TYR A 348       1.854   0.123 -45.609  1.00 35.82           O  
ANISOU 3820  O   TYR A 348     5545   4573   3494    542    201  -1070       O  
ATOM   3821  CB  TYR A 348       1.257  -0.321 -48.668  1.00 29.43           C  
ANISOU 3821  CB  TYR A 348     4998   3676   2506    590    160  -1061       C  
ATOM   3822  CG  TYR A 348       0.267  -0.876 -49.658  1.00 33.87           C  
ANISOU 3822  CG  TYR A 348     5765   4171   2933    512     32  -1065       C  
ATOM   3823  CD1 TYR A 348      -0.591  -1.905 -49.303  1.00 36.44           C  
ANISOU 3823  CD1 TYR A 348     6268   4396   3182    364   -136  -1072       C  
ATOM   3824  CD2 TYR A 348       0.179  -0.362 -50.941  1.00 32.06           C  
ANISOU 3824  CD2 TYR A 348     5570   3971   2639    563     63  -1055       C  
ATOM   3825  CE1 TYR A 348      -1.507  -2.411 -50.202  1.00 39.26           C  
ANISOU 3825  CE1 TYR A 348     6808   4685   3423    253   -286  -1073       C  
ATOM   3826  CE2 TYR A 348      -0.734  -0.856 -51.846  1.00 31.61           C  
ANISOU 3826  CE2 TYR A 348     5709   3851   2448    486    -84  -1062       C  
ATOM   3827  CZ  TYR A 348      -1.574  -1.883 -51.473  1.00 36.14           C  
ANISOU 3827  CZ  TYR A 348     6435   4328   2970    324   -266  -1075       C  
ATOM   3828  OH  TYR A 348      -2.486  -2.385 -52.372  1.00 37.01           O  
ANISOU 3828  OH  TYR A 348     6731   4372   2960    210   -441  -1079       O  
ATOM   3829  N   ALA A 349       2.139   2.131 -46.584  1.00 28.44           N  
ANISOU 3829  N   ALA A 349     4374   3757   2675    584    372  -1042       N  
ATOM   3830  CA  ALA A 349       3.154   2.587 -45.641  1.00 28.43           C  
ANISOU 3830  CA  ALA A 349     4234   3783   2785    632    429  -1043       C  
ATOM   3831  C   ALA A 349       2.553   2.880 -44.272  1.00 36.06           C  
ANISOU 3831  C   ALA A 349     5146   4781   3776    552    381  -1053       C  
ATOM   3832  O   ALA A 349       3.231   2.740 -43.253  1.00 42.05           O  
ANISOU 3832  O   ALA A 349     5863   5545   4568    586    360  -1070       O  
ATOM   3833  CB  ALA A 349       3.866   3.820 -46.179  1.00 22.84           C  
ANISOU 3833  CB  ALA A 349     3393   3125   2160    676    550  -1022       C  
ATOM   3834  N   ASN A 350       1.289   3.299 -44.254  1.00 35.07           N  
ANISOU 3834  N   ASN A 350     5011   4700   3616    470    358  -1051       N  
ATOM   3835  CA  ASN A 350       0.578   3.505 -42.987  1.00 32.01           C  
ANISOU 3835  CA  ASN A 350     4561   4383   3219    408    328  -1067       C  
ATOM   3836  C   ASN A 350       0.647   2.285 -42.053  1.00 36.93           C  
ANISOU 3836  C   ASN A 350     5306   4982   3743    358    261  -1086       C  
ATOM   3837  O   ASN A 350       0.853   2.415 -40.830  1.00 38.07           O  
ANISOU 3837  O   ASN A 350     5412   5162   3891    351    256  -1096       O  
ATOM   3838  CB  ASN A 350      -0.885   3.861 -43.259  1.00 29.74           C  
ANISOU 3838  CB  ASN A 350     4214   4209   2877    350    308  -1085       C  
ATOM   3839  CG  ASN A 350      -1.686   4.051 -41.986  1.00 32.17           C  
ANISOU 3839  CG  ASN A 350     4410   4656   3159    287    317  -1111       C  
ATOM   3840  OD1 ASN A 350      -1.687   5.130 -41.395  1.00 32.27           O  
ANISOU 3840  OD1 ASN A 350     4301   4700   3261    344    364  -1114       O  
ATOM   3841  ND2 ASN A 350      -2.378   3.001 -41.559  1.00 37.41           N  
ANISOU 3841  ND2 ASN A 350     5134   5392   3690    144    271  -1112       N  
ATOM   3842  N   SER A 351       0.477   1.106 -42.649  1.00 37.77           N  
ANISOU 3842  N   SER A 351     5593   5013   3745    324    190  -1090       N  
ATOM   3843  CA  SER A 351       0.520  -0.165 -41.931  1.00 38.39           C  
ANISOU 3843  CA  SER A 351     5862   5012   3712    277     89  -1085       C  
ATOM   3844  C   SER A 351       1.839  -0.346 -41.190  1.00 38.67           C  
ANISOU 3844  C   SER A 351     5890   4996   3805    415     85  -1088       C  
ATOM   3845  O   SER A 351       1.878  -0.916 -40.100  1.00 41.47           O  
ANISOU 3845  O   SER A 351     6355   5325   4076    387     15  -1079       O  
ATOM   3846  CB  SER A 351       0.304  -1.332 -42.898  1.00 38.38           C  
ANISOU 3846  CB  SER A 351     6096   4859   3628    247    -13  -1062       C  
ATOM   3847  OG  SER A 351      -0.914  -1.190 -43.607  1.00 44.18           O  
ANISOU 3847  OG  SER A 351     6849   5641   4294    100    -51  -1059       O  
ATOM   3848  N   ALA A 352       2.917   0.139 -41.794  1.00 34.04           N  
ANISOU 3848  N   ALA A 352     5189   4409   3336    560    148  -1096       N  
ATOM   3849  CA  ALA A 352       4.229   0.096 -41.165  1.00 34.03           C  
ANISOU 3849  CA  ALA A 352     5135   4409   3385    714    130  -1117       C  
ATOM   3850  C   ALA A 352       4.392   1.263 -40.200  1.00 35.58           C  
ANISOU 3850  C   ALA A 352     5148   4715   3657    679    158  -1140       C  
ATOM   3851  O   ALA A 352       5.227   1.223 -39.296  1.00 34.81           O  
ANISOU 3851  O   ALA A 352     5021   4643   3564    769     93  -1179       O  
ATOM   3852  CB  ALA A 352       5.324   0.120 -42.218  1.00 30.78           C  
ANISOU 3852  CB  ALA A 352     4656   3998   3041    877    192  -1122       C  
ATOM   3853  N   ALA A 353       3.582   2.300 -40.394  1.00 39.44           N  
ANISOU 3853  N   ALA A 353     5534   5257   4193    572    230  -1125       N  
ATOM   3854  CA  ALA A 353       3.686   3.511 -39.589  1.00 24.52           C  
ANISOU 3854  CA  ALA A 353     3503   3437   2378    552    246  -1150       C  
ATOM   3855  C   ALA A 353       3.133   3.323 -38.180  1.00 32.20           C  
ANISOU 3855  C   ALA A 353     4532   4449   3252    488    196  -1168       C  
ATOM   3856  O   ALA A 353       3.748   3.767 -37.211  1.00 25.28           O  
ANISOU 3856  O   ALA A 353     3613   3605   2390    519    149  -1216       O  
ATOM   3857  CB  ALA A 353       2.977   4.668 -40.281  1.00 23.88           C  
ANISOU 3857  CB  ALA A 353     3335   3372   2368    507    320  -1125       C  
ATOM   3858  N   ASN A 354       1.978   2.671 -38.064  1.00 29.73           N  
ANISOU 3858  N   ASN A 354     4323   4157   2817    390    203  -1141       N  
ATOM   3859  CA  ASN A 354       1.345   2.502 -36.747  1.00 29.62           C  
ANISOU 3859  CA  ASN A 354     4365   4224   2667    313    192  -1147       C  
ATOM   3860  C   ASN A 354       2.224   1.867 -35.640  1.00 31.31           C  
ANISOU 3860  C   ASN A 354     4701   4406   2789    355     91  -1165       C  
ATOM   3861  O   ASN A 354       2.302   2.417 -34.532  1.00 29.07           O  
ANISOU 3861  O   ASN A 354     4397   4183   2467    352     85  -1191       O  
ATOM   3862  CB  ASN A 354       0.049   1.693 -36.888  1.00 33.58           C  
ANISOU 3862  CB  ASN A 354     4952   4800   3006    175    207  -1119       C  
ATOM   3863  CG  ASN A 354      -1.053   2.472 -37.578  1.00 37.10           C  
ANISOU 3863  CG  ASN A 354     5218   5362   3515    136    291  -1118       C  
ATOM   3864  OD1 ASN A 354      -1.110   3.698 -37.493  1.00 36.00           O  
ANISOU 3864  OD1 ASN A 354     4929   5253   3495    218    346  -1133       O  
ATOM   3865  ND2 ASN A 354      -1.940   1.759 -38.261  1.00 42.23           N  
ANISOU 3865  ND2 ASN A 354     5900   6051   4095     -5    274  -1077       N  
ATOM   3866  N   PRO A 355       2.885   0.721 -35.921  1.00 33.50           N  
ANISOU 3866  N   PRO A 355     5133   4574   3022    423     -8  -1146       N  
ATOM   3867  CA  PRO A 355       3.677   0.096 -34.850  1.00 34.15           C  
ANISOU 3867  CA  PRO A 355     5360   4612   3004    502   -141  -1144       C  
ATOM   3868  C   PRO A 355       4.830   0.967 -34.348  1.00 32.45           C  
ANISOU 3868  C   PRO A 355     4986   4452   2892    631   -195  -1223       C  
ATOM   3869  O   PRO A 355       5.179   0.903 -33.168  1.00 35.79           O  
ANISOU 3869  O   PRO A 355     5487   4899   3214    651   -299  -1237       O  
ATOM   3870  CB  PRO A 355       4.218  -1.178 -35.512  1.00 35.16           C  
ANISOU 3870  CB  PRO A 355     5684   4569   3105    613   -240  -1108       C  
ATOM   3871  CG  PRO A 355       3.287  -1.450 -36.633  1.00 36.00           C  
ANISOU 3871  CG  PRO A 355     5825   4634   3221    498   -165  -1074       C  
ATOM   3872  CD  PRO A 355       2.910  -0.099 -37.146  1.00 35.15           C  
ANISOU 3872  CD  PRO A 355     5438   4668   3248    454    -24  -1118       C  
ATOM   3873  N   ILE A 356       5.412   1.764 -35.239  1.00 26.27           N  
ANISOU 3873  N   ILE A 356     3999   3694   2289    700   -141  -1273       N  
ATOM   3874  CA  ILE A 356       6.489   2.675 -34.867  1.00 34.32           C  
ANISOU 3874  CA  ILE A 356     4849   4787   3405    785   -206  -1373       C  
ATOM   3875  C   ILE A 356       5.961   3.750 -33.921  1.00 31.67           C  
ANISOU 3875  C   ILE A 356     4483   4497   3051    665   -190  -1401       C  
ATOM   3876  O   ILE A 356       6.597   4.084 -32.914  1.00 31.37           O  
ANISOU 3876  O   ILE A 356     4448   4496   2975    694   -318  -1475       O  
ATOM   3877  CB  ILE A 356       7.122   3.335 -36.110  1.00 33.49           C  
ANISOU 3877  CB  ILE A 356     4537   4713   3477    844   -121  -1413       C  
ATOM   3878  CG1 ILE A 356       7.651   2.265 -37.069  1.00 26.65           C  
ANISOU 3878  CG1 ILE A 356     3711   3804   2611    997   -108  -1380       C  
ATOM   3879  CG2 ILE A 356       8.232   4.293 -35.704  1.00 27.16           C  
ANISOU 3879  CG2 ILE A 356     3529   3987   2803    855   -198  -1489       C  
ATOM   3880  CD1 ILE A 356       8.204   2.819 -38.363  1.00 26.52           C  
ANISOU 3880  CD1 ILE A 356     3504   3839   2735   1042     21  -1381       C  
ATOM   3881  N   ILE A 357       4.786   4.280 -34.251  1.00 25.93           N  
ANISOU 3881  N   ILE A 357     3743   3769   2342    554    -49  -1349       N  
ATOM   3882  CA  ILE A 357       4.111   5.253 -33.402  1.00 34.15           C  
ANISOU 3882  CA  ILE A 357     4786   4842   3346    490     -9  -1373       C  
ATOM   3883  C   ILE A 357       3.876   4.675 -32.014  1.00 37.27           C  
ANISOU 3883  C   ILE A 357     5342   5280   3540    461    -61  -1367       C  
ATOM   3884  O   ILE A 357       4.155   5.328 -31.003  1.00 34.93           O  
ANISOU 3884  O   ILE A 357     5078   5001   3194    468   -121  -1431       O  
ATOM   3885  CB  ILE A 357       2.766   5.692 -34.007  1.00 25.52           C  
ANISOU 3885  CB  ILE A 357     3655   3764   2278    436    137  -1317       C  
ATOM   3886  CG1 ILE A 357       2.988   6.394 -35.347  1.00 34.14           C  
ANISOU 3886  CG1 ILE A 357     4626   4804   3542    462    176  -1311       C  
ATOM   3887  CG2 ILE A 357       2.020   6.604 -33.046  1.00 26.43           C  
ANISOU 3887  CG2 ILE A 357     3790   3924   2330    431    184  -1355       C  
ATOM   3888  CD1 ILE A 357       1.705   6.798 -36.040  1.00 37.63           C  
ANISOU 3888  CD1 ILE A 357     5030   5265   4004    442    275  -1260       C  
ATOM   3889  N   TYR A 358       3.367   3.445 -31.972  1.00 40.20           N  
ANISOU 3889  N   TYR A 358     5844   5660   3772    414    -48  -1291       N  
ATOM   3890  CA  TYR A 358       3.182   2.743 -30.704  1.00 38.71           C  
ANISOU 3890  CA  TYR A 358     5844   5514   3351    368   -101  -1261       C  
ATOM   3891  C   TYR A 358       4.503   2.633 -29.949  1.00 42.52           C  
ANISOU 3891  C   TYR A 358     6384   5958   3814    475   -300  -1304       C  
ATOM   3892  O   TYR A 358       4.549   2.784 -28.728  1.00 44.48           O  
ANISOU 3892  O   TYR A 358     6736   6250   3916    455   -356  -1317       O  
ATOM   3893  CB  TYR A 358       2.605   1.345 -30.930  1.00 36.43           C  
ANISOU 3893  CB  TYR A 358     5724   5208   2909    290   -100  -1161       C  
ATOM   3894  CG  TYR A 358       1.265   1.323 -31.623  1.00 36.39           C  
ANISOU 3894  CG  TYR A 358     5665   5282   2877    168     58  -1126       C  
ATOM   3895  CD1 TYR A 358       0.326   2.321 -31.400  1.00 34.12           C  
ANISOU 3895  CD1 TYR A 358     5243   5114   2607    148    205  -1143       C  
ATOM   3896  CD2 TYR A 358       0.940   0.302 -32.503  1.00 39.21           C  
ANISOU 3896  CD2 TYR A 358     6133   5565   3201    109     31  -1060       C  
ATOM   3897  CE1 TYR A 358      -0.900   2.298 -32.035  1.00 36.71           C  
ANISOU 3897  CE1 TYR A 358     5449   5562   2936     66    325  -1102       C  
ATOM   3898  CE2 TYR A 358      -0.280   0.271 -33.143  1.00 39.84           C  
ANISOU 3898  CE2 TYR A 358     6117   5730   3289    -43    146  -1006       C  
ATOM   3899  CZ  TYR A 358      -1.197   1.270 -32.907  1.00 38.14           C  
ANISOU 3899  CZ  TYR A 358     5690   5722   3081    -64    297  -1046       C  
ATOM   3900  OH  TYR A 358      -2.415   1.236 -33.547  1.00 41.24           O  
ANISOU 3900  OH  TYR A 358     5941   6243   3486   -204    395   -994       O  
ATOM   3901  N   ASN A 359       5.577   2.373 -30.689  1.00 42.21           N  
ANISOU 3901  N   ASN A 359     6272   5857   3908    605   -413  -1334       N  
ATOM   3902  CA  ASN A 359       6.897   2.212 -30.093  1.00 44.98           C  
ANISOU 3902  CA  ASN A 359     6640   6202   4247    745   -639  -1392       C  
ATOM   3903  C   ASN A 359       7.456   3.509 -29.517  1.00 49.87           C  
ANISOU 3903  C   ASN A 359     7127   6883   4940    731   -713  -1510       C  
ATOM   3904  O   ASN A 359       8.263   3.484 -28.590  1.00 48.42           O  
ANISOU 3904  O   ASN A 359     6992   6718   4686    785   -918  -1550       O  
ATOM   3905  CB  ASN A 359       7.880   1.648 -31.123  1.00 42.75           C  
ANISOU 3905  CB  ASN A 359     6268   5886   4088    922   -721  -1422       C  
ATOM   3906  CG  ASN A 359       9.295   1.533 -30.580  1.00 41.91           C  
ANISOU 3906  CG  ASN A 359     6076   5812   4035   1072   -955  -1454       C  
ATOM   3907  OD1 ASN A 359       9.645   0.547 -29.933  1.00 42.92           O  
ANISOU 3907  OD1 ASN A 359     6394   5886   4027   1181  -1121  -1394       O  
ATOM   3908  ND2 ASN A 359      10.115   2.547 -30.840  1.00 31.34           N  
ANISOU 3908  ND2 ASN A 359     4451   4563   2895   1067   -985  -1536       N  
ATOM   3909  N   PHE A 360       7.038   4.645 -30.065  1.00 49.11           N  
ANISOU 3909  N   PHE A 360     6888   6794   4979    655   -575  -1559       N  
ATOM   3910  CA  PHE A 360       7.594   5.917 -29.613  1.00 52.23           C  
ANISOU 3910  CA  PHE A 360     7201   7196   5449    625   -668  -1680       C  
ATOM   3911  C   PHE A 360       6.681   6.704 -28.676  1.00 52.05           C  
ANISOU 3911  C   PHE A 360     7310   7157   5311    542   -579  -1685       C  
ATOM   3912  O   PHE A 360       7.123   7.670 -28.058  1.00 54.61           O  
ANISOU 3912  O   PHE A 360     7651   7453   5644    517   -687  -1786       O  
ATOM   3913  CB  PHE A 360       7.962   6.791 -30.813  1.00 54.19           C  
ANISOU 3913  CB  PHE A 360     7237   7433   5921    611   -619  -1758       C  
ATOM   3914  CG  PHE A 360       9.354   6.556 -31.324  1.00 62.03           C  
ANISOU 3914  CG  PHE A 360     8021   8472   7075    664   -754  -1774       C  
ATOM   3915  CD1 PHE A 360       9.595   5.611 -32.307  1.00 62.76           C  
ANISOU 3915  CD1 PHE A 360     8028   8582   7237    759   -671  -1675       C  
ATOM   3916  CD2 PHE A 360      10.424   7.275 -30.814  1.00 67.68           C  
ANISOU 3916  CD2 PHE A 360     8610   9214   7891    605   -952  -1846       C  
ATOM   3917  CE1 PHE A 360      10.879   5.389 -32.777  1.00 64.67           C  
ANISOU 3917  CE1 PHE A 360     8035   8896   7640    835   -748  -1649       C  
ATOM   3918  CE2 PHE A 360      11.710   7.060 -31.279  1.00 69.35           C  
ANISOU 3918  CE2 PHE A 360     8551   9513   8287    635  -1047  -1803       C  
ATOM   3919  CZ  PHE A 360      11.938   6.115 -32.262  1.00 67.21           C  
ANISOU 3919  CZ  PHE A 360     8169   9289   8078    770   -927  -1705       C  
ATOM   3920  N   LEU A 361       5.420   6.299 -28.557  1.00 49.90           N  
ANISOU 3920  N   LEU A 361     7132   6910   4919    499   -394  -1594       N  
ATOM   3921  CA  LEU A 361       4.480   7.070 -27.744  1.00 45.55           C  
ANISOU 3921  CA  LEU A 361     6674   6381   4253    461   -282  -1624       C  
ATOM   3922  C   LEU A 361       3.740   6.252 -26.682  1.00 48.44           C  
ANISOU 3922  C   LEU A 361     7212   6838   4354    416   -216  -1561       C  
ATOM   3923  O   LEU A 361       2.866   6.778 -25.991  1.00 52.15           O  
ANISOU 3923  O   LEU A 361     7751   7365   4698    403    -90  -1590       O  
ATOM   3924  CB  LEU A 361       3.465   7.767 -28.652  1.00 39.30           C  
ANISOU 3924  CB  LEU A 361     5779   5575   3580    463    -95  -1607       C  
ATOM   3925  CG  LEU A 361       4.051   8.797 -29.620  1.00 30.55           C  
ANISOU 3925  CG  LEU A 361     4540   4371   2695    486   -140  -1670       C  
ATOM   3926  CD1 LEU A 361       2.970   9.371 -30.518  1.00 26.91           C  
ANISOU 3926  CD1 LEU A 361     4005   3896   2323    507     24  -1628       C  
ATOM   3927  CD2 LEU A 361       4.763   9.904 -28.857  1.00 29.66           C  
ANISOU 3927  CD2 LEU A 361     4501   4186   2582    485   -282  -1805       C  
ATOM   3928  N   SER A 362       4.091   4.978 -26.542  1.00 48.95           N  
ANISOU 3928  N   SER A 362     7358   6922   4319    403   -301  -1478       N  
ATOM   3929  CA  SER A 362       3.446   4.123 -25.547  1.00 47.00           C  
ANISOU 3929  CA  SER A 362     7293   6771   3792    330   -252  -1400       C  
ATOM   3930  C   SER A 362       4.453   3.257 -24.800  1.00 50.26           C  
ANISOU 3930  C   SER A 362     7860   7151   4085    378   -483  -1355       C  
ATOM   3931  O   SER A 362       4.918   2.249 -25.327  1.00 50.50           O  
ANISOU 3931  O   SER A 362     7930   7108   4152    424   -586  -1274       O  
ATOM   3932  CB  SER A 362       2.392   3.233 -26.207  1.00 43.46           C  
ANISOU 3932  CB  SER A 362     6843   6381   3287    237    -93  -1289       C  
ATOM   3933  OG  SER A 362       1.767   2.394 -25.253  1.00 46.32           O  
ANISOU 3933  OG  SER A 362     7365   6878   3357    142    -47  -1198       O  
ATOM   3934  N   GLY A 363       4.761   3.646 -23.565  1.00 54.14           N  
ANISOU 3934  N   GLY A 363     8466   7680   4424    388   -573  -1405       N  
ATOM   3935  CA  GLY A 363       5.777   2.986 -22.762  1.00 43.39           C  
ANISOU 3935  CA  GLY A 363     7258   6277   2953    457   -827  -1365       C  
ATOM   3936  C   GLY A 363       5.649   1.479 -22.632  1.00 51.19           C  
ANISOU 3936  C   GLY A 363     8433   7231   3785    452   -872  -1192       C  
ATOM   3937  O   GLY A 363       6.645   0.758 -22.714  1.00 52.55           O  
ANISOU 3937  O   GLY A 363     8676   7292   4000    569  -1100  -1143       O  
ATOM   3938  N   LYS A 364       4.426   1.000 -22.429  1.00 46.35           N  
ANISOU 3938  N   LYS A 364     7907   6714   2990    326   -668  -1094       N  
ATOM   3939  CA  LYS A 364       4.187  -0.431 -22.274  1.00 50.49           C  
ANISOU 3939  CA  LYS A 364     8664   7169   3350    279   -706   -901       C  
ATOM   3940  C   LYS A 364       4.523  -1.185 -23.560  1.00 53.26           C  
ANISOU 3940  C   LYS A 364     9003   7343   3891    328   -775   -847       C  
ATOM   3941  O   LYS A 364       5.128  -2.262 -23.523  1.00 60.47           O  
ANISOU 3941  O   LYS A 364    10130   8082   4766    400   -960   -738       O  
ATOM   3942  CB  LYS A 364       2.736  -0.688 -21.864  1.00 49.95           C  
ANISOU 3942  CB  LYS A 364     8652   7273   3053    110   -456   -798       C  
ATOM   3943  CG  LYS A 364       2.359  -0.088 -20.516  1.00 56.79           C  
ANISOU 3943  CG  LYS A 364     9562   8338   3677     96   -372   -843       C  
ATOM   3944  CD  LYS A 364       0.922  -0.413 -20.138  1.00 61.42           C  
ANISOU 3944  CD  LYS A 364    10171   9139   4027    -32   -107   -717       C  
ATOM   3945  CE  LYS A 364       0.552   0.204 -18.796  1.00 65.38           C  
ANISOU 3945  CE  LYS A 364    10709   9870   4264     -4     -6   -776       C  
ATOM   3946  NZ  LYS A 364      -0.853  -0.102 -18.410  1.00 68.13           N  
ANISOU 3946  NZ  LYS A 364    11056  10456   4376    -78    278   -632       N  
ATOM   3947  N   PHE A 365       4.138  -0.610 -24.695  1.00 47.93           N  
ANISOU 3947  N   PHE A 365     8096   6701   3414    308   -633   -930       N  
ATOM   3948  CA  PHE A 365       4.470  -1.191 -25.989  1.00 46.39           C  
ANISOU 3948  CA  PHE A 365     7873   6354   3398    372   -684   -910       C  
ATOM   3949  C   PHE A 365       5.976  -1.156 -26.231  1.00 46.14           C  
ANISOU 3949  C   PHE A 365     7786   6220   3524    601   -921   -987       C  
ATOM   3950  O   PHE A 365       6.519  -2.033 -26.898  1.00 50.15           O  
ANISOU 3950  O   PHE A 365     8384   6581   4089    727  -1039   -945       O  
ATOM   3951  CB  PHE A 365       3.735  -0.466 -27.119  1.00 45.75           C  
ANISOU 3951  CB  PHE A 365     7545   6351   3488    308   -481   -987       C  
ATOM   3952  CG  PHE A 365       2.318  -0.931 -27.321  1.00 47.23           C  
ANISOU 3952  CG  PHE A 365     7788   6613   3544    114   -298   -883       C  
ATOM   3953  CD1 PHE A 365       2.047  -2.064 -28.071  1.00 45.41           C  
ANISOU 3953  CD1 PHE A 365     7725   6228   3303     32   -331   -763       C  
ATOM   3954  CD2 PHE A 365       1.257  -0.233 -26.767  1.00 49.35           C  
ANISOU 3954  CD2 PHE A 365     7945   7108   3696     20   -103   -906       C  
ATOM   3955  CE1 PHE A 365       0.746  -2.494 -28.261  1.00 43.53           C  
ANISOU 3955  CE1 PHE A 365     7535   6056   2949   -209   -182   -648       C  
ATOM   3956  CE2 PHE A 365      -0.045  -0.657 -26.954  1.00 48.71           C  
ANISOU 3956  CE2 PHE A 365     7878   7127   3502   -156     68   -790       C  
ATOM   3957  CZ  PHE A 365      -0.301  -1.790 -27.702  1.00 45.93           C  
ANISOU 3957  CZ  PHE A 365     7680   6621   3150   -316     26   -653       C  
ATOM   3958  N   ARG A 366       6.646  -0.141 -25.690  1.00 58.89           N  
ANISOU 3958  N   ARG A 366    10107   5123   7147    163  -1865  -2978       N  
ATOM   3959  CA  ARG A 366       8.102  -0.065 -25.767  1.00 60.70           C  
ANISOU 3959  CA  ARG A 366    10137   5959   6965    350  -2001  -3107       C  
ATOM   3960  C   ARG A 366       8.715  -1.241 -25.026  1.00 62.01           C  
ANISOU 3960  C   ARG A 366    10541   6644   6377    718  -2178  -3058       C  
ATOM   3961  O   ARG A 366       9.552  -1.968 -25.569  1.00 62.50           O  
ANISOU 3961  O   ARG A 366    10699   7004   6043   1166  -2317  -2783       O  
ATOM   3962  CB  ARG A 366       8.624   1.246 -25.172  1.00 64.38           C  
ANISOU 3962  CB  ARG A 366    10076   6673   7712   -107  -1798  -3510       C  
ATOM   3963  CG  ARG A 366       7.954   2.495 -25.703  1.00 72.14           C  
ANISOU 3963  CG  ARG A 366    10776   7094   9540   -503  -1532  -3578       C  
ATOM   3964  CD  ARG A 366       8.561   3.753 -25.100  1.00 81.93           C  
ANISOU 3964  CD  ARG A 366    11553   8547  11029   -965  -1315  -4016       C  
ATOM   3965  NE  ARG A 366       9.893   4.030 -25.631  1.00 85.13           N  
ANISOU 3965  NE  ARG A 366    11586   9476  11284   -868  -1480  -3921       N  
ATOM   3966  CZ  ARG A 366      10.300   5.230 -26.035  1.00 85.94           C  
ANISOU 3966  CZ  ARG A 366    11215   9518  11919  -1180  -1331  -4019       C  
ATOM   3967  NH1 ARG A 366       9.477   6.268 -25.964  1.00 84.61           N  
ANISOU 3967  NH1 ARG A 366    10907   8761  12480  -1600   -983  -4235       N  
ATOM   3968  NH2 ARG A 366      11.529   5.394 -26.506  1.00 87.11           N  
ANISOU 3968  NH2 ARG A 366    11004  10170  11924  -1055  -1492  -3855       N  
ATOM   3969  N   GLU A 367       8.287  -1.413 -23.777  1.00 63.10           N  
ANISOU 3969  N   GLU A 367    10768   6871   6336    539  -2123  -3292       N  
ATOM   3970  CA  GLU A 367       8.754  -2.509 -22.938  1.00 64.75           C  
ANISOU 3970  CA  GLU A 367    11145   7580   5877    834  -2270  -3184       C  
ATOM   3971  C   GLU A 367       8.536  -3.855 -23.618  1.00 62.96           C  
ANISOU 3971  C   GLU A 367    11343   7128   5452   1358  -2396  -2714       C  
ATOM   3972  O   GLU A 367       9.418  -4.713 -23.610  1.00 64.53           O  
ANISOU 3972  O   GLU A 367    11626   7737   5156   1796  -2531  -2504       O  
ATOM   3973  CB  GLU A 367       8.043  -2.486 -21.584  1.00 66.06           C  
ANISOU 3973  CB  GLU A 367    11325   7774   6003    499  -2070  -3370       C  
ATOM   3974  CG  GLU A 367       8.283  -1.222 -20.776  1.00 76.20           C  
ANISOU 3974  CG  GLU A 367    12301   9267   7385    -74  -1873  -3867       C  
ATOM   3975  CD  GLU A 367       7.403  -1.143 -19.545  1.00 84.71           C  
ANISOU 3975  CD  GLU A 367    13518  10231   8436   -403  -1565  -4075       C  
ATOM   3976  OE1 GLU A 367       6.659  -2.112 -19.285  1.00 84.55           O  
ANISOU 3976  OE1 GLU A 367    13758  10042   8325   -142  -1573  -3819       O  
ATOM   3977  OE2 GLU A 367       7.452  -0.112 -18.841  1.00 88.46           O  
ANISOU 3977  OE2 GLU A 367    13945  10711   8953   -914  -1321  -4455       O  
ATOM   3978  N   GLN A 368       7.364  -4.027 -24.222  1.00 60.81           N  
ANISOU 3978  N   GLN A 368    11311   6201   5593   1294  -2339  -2505       N  
ATOM   3979  CA  GLN A 368       7.028  -5.293 -24.867  1.00 59.63           C  
ANISOU 3979  CA  GLN A 368    11620   5757   5279   1682  -2475  -2083       C  
ATOM   3980  C   GLN A 368       7.832  -5.539 -26.144  1.00 62.93           C  
ANISOU 3980  C   GLN A 368    12238   6163   5508   2042  -2567  -1912       C  
ATOM   3981  O   GLN A 368       8.261  -6.665 -26.404  1.00 65.65           O  
ANISOU 3981  O   GLN A 368    12928   6539   5479   2499  -2610  -1665       O  
ATOM   3982  CB  GLN A 368       5.532  -5.348 -25.175  1.00 57.20           C  
ANISOU 3982  CB  GLN A 368    11459   4842   5432   1424  -2463  -1850       C  
ATOM   3983  CG  GLN A 368       4.658  -5.489 -23.942  1.00 61.95           C  
ANISOU 3983  CG  GLN A 368    12027   5386   6127   1235  -2350  -1920       C  
ATOM   3984  CD  GLN A 368       5.010  -6.711 -23.115  1.00 68.42           C  
ANISOU 3984  CD  GLN A 368    13117   6473   6408   1596  -2458  -1841       C  
ATOM   3985  OE1 GLN A 368       5.367  -7.760 -23.653  1.00 66.39           O  
ANISOU 3985  OE1 GLN A 368    13192   6158   5874   1995  -2617  -1566       O  
ATOM   3986  NE2 GLN A 368       4.916  -6.580 -21.797  1.00 75.55           N  
ANISOU 3986  NE2 GLN A 368    13885   7655   7166   1453  -2329  -2073       N  
ATOM   3987  N   PHE A 369       8.028  -4.492 -26.940  1.00 58.84           N  
ANISOU 3987  N   PHE A 369    11528   5556   5274   1853  -2546  -2044       N  
ATOM   3988  CA  PHE A 369       8.822  -4.601 -28.161  1.00 59.54           C  
ANISOU 3988  CA  PHE A 369    11825   5655   5142   2199  -2588  -1915       C  
ATOM   3989  C   PHE A 369      10.259  -4.968 -27.824  1.00 62.39           C  
ANISOU 3989  C   PHE A 369    11948   6699   5058   2624  -2504  -1843       C  
ATOM   3990  O   PHE A 369      10.856  -5.835 -28.463  1.00 63.90           O  
ANISOU 3990  O   PHE A 369    12487   6910   4880   3137  -2451  -1579       O  
ATOM   3991  CB  PHE A 369       8.795  -3.294 -28.958  1.00 58.76           C  
ANISOU 3991  CB  PHE A 369    11331   5425   5572   1850  -2504  -1958       C  
ATOM   3992  CG  PHE A 369       7.464  -2.988 -29.587  1.00 56.70           C  
ANISOU 3992  CG  PHE A 369    11249   4504   5789   1482  -2583  -1824       C  
ATOM   3993  CD1 PHE A 369       6.482  -3.960 -29.680  1.00 55.87           C  
ANISOU 3993  CD1 PHE A 369    11476   4147   5606   1464  -2667  -1470       C  
ATOM   3994  CD2 PHE A 369       7.199  -1.724 -30.089  1.00 56.10           C  
ANISOU 3994  CD2 PHE A 369    10764   4229   6322   1094  -2502  -1856       C  
ATOM   3995  CE1 PHE A 369       5.258  -3.675 -30.258  1.00 54.66           C  
ANISOU 3995  CE1 PHE A 369    11232   3665   5872   1066  -2709  -1183       C  
ATOM   3996  CE2 PHE A 369       5.979  -1.434 -30.668  1.00 54.83           C  
ANISOU 3996  CE2 PHE A 369    10535   3654   6644    730  -2503  -1531       C  
ATOM   3997  CZ  PHE A 369       5.008  -2.410 -30.753  1.00 54.20           C  
ANISOU 3997  CZ  PHE A 369    10742   3458   6393    715  -2608  -1190       C  
ATOM   3998  N   LYS A 370      10.807  -4.297 -26.816  1.00 63.79           N  
ANISOU 3998  N   LYS A 370    11541   7416   5280   2385  -2476  -2052       N  
ATOM   3999  CA  LYS A 370      12.167  -4.561 -26.364  1.00 67.23           C  
ANISOU 3999  CA  LYS A 370    11619   8577   5348   2691  -2462  -1901       C  
ATOM   4000  C   LYS A 370      12.296  -5.976 -25.805  1.00 68.68           C  
ANISOU 4000  C   LYS A 370    12165   8900   5029   3159  -2514  -1662       C  
ATOM   4001  O   LYS A 370      13.298  -6.654 -26.033  1.00 71.46           O  
ANISOU 4001  O   LYS A 370    12485   9580   5088   3679  -2433  -1313       O  
ATOM   4002  CB  LYS A 370      12.583  -3.536 -25.307  1.00 69.08           C  
ANISOU 4002  CB  LYS A 370    11218   9333   5695   2186  -2506  -2199       C  
ATOM   4003  CG  LYS A 370      14.001  -3.705 -24.788  1.00 73.43           C  
ANISOU 4003  CG  LYS A 370    11293  10702   5903   2381  -2582  -1967       C  
ATOM   4004  CD  LYS A 370      14.331  -2.641 -23.754  1.00 75.93           C  
ANISOU 4004  CD  LYS A 370    11072  11492   6286   1741  -2692  -2310       C  
ATOM   4005  CE  LYS A 370      15.752  -2.789 -23.238  1.00 81.03           C  
ANISOU 4005  CE  LYS A 370    11183  13002   6603   1849  -2860  -1986       C  
ATOM   4006  NZ  LYS A 370      16.087  -1.736 -22.241  1.00 84.35           N  
ANISOU 4006  NZ  LYS A 370    11150  13879   7021   1118  -3030  -2346       N  
ATOM   4007  N   ALA A 371      11.271  -6.417 -25.081  1.00 69.60           N  
ANISOU 4007  N   ALA A 371    12601   8741   5101   2996  -2608  -1799       N  
ATOM   4008  CA  ALA A 371      11.288  -7.732 -24.446  1.00 69.74           C  
ANISOU 4008  CA  ALA A 371    12829   8834   4837   3333  -2588  -1522       C  
ATOM   4009  C   ALA A 371      11.230  -8.870 -25.462  1.00 73.73           C  
ANISOU 4009  C   ALA A 371    13883   8827   5303   3834  -2457  -1205       C  
ATOM   4010  O   ALA A 371      11.735  -9.963 -25.207  1.00 79.64           O  
ANISOU 4010  O   ALA A 371    14736   9705   5818   4270  -2348   -934       O  
ATOM   4011  CB  ALA A 371      10.134  -7.853 -23.460  1.00 67.16           C  
ANISOU 4011  CB  ALA A 371    12558   8272   4689   2947  -2602  -1661       C  
ATOM   4012  N   ALA A 372      10.624  -8.607 -26.617  1.00 75.21           N  
ANISOU 4012  N   ALA A 372    14420   8423   5734   3732  -2448  -1243       N  
ATOM   4013  CA  ALA A 372      10.408  -9.640 -27.627  1.00 74.11           C  
ANISOU 4013  CA  ALA A 372    14905   7695   5559   4066  -2334  -1030       C  
ATOM   4014  C   ALA A 372      11.705 -10.126 -28.273  1.00 77.09           C  
ANISOU 4014  C   ALA A 372    15389   8316   5585   4676  -2072   -836       C  
ATOM   4015  O   ALA A 372      11.697 -11.082 -29.051  1.00 77.70           O  
ANISOU 4015  O   ALA A 372    16034   7938   5549   4984  -1865   -755       O  
ATOM   4016  CB  ALA A 372       9.455  -9.131 -28.694  1.00 70.34           C  
ANISOU 4016  CB  ALA A 372    14716   6621   5387   3704  -2452  -1036       C  
ATOM   4017  N   PHE A 373      12.814  -9.468 -27.953  1.00 76.81           N  
ANISOU 4017  N   PHE A 373    14808   9005   5370   4832  -2058   -760       N  
ATOM   4018  CA  PHE A 373      14.115  -9.854 -28.485  1.00 77.65           C  
ANISOU 4018  CA  PHE A 373    14862   9423   5219   5462  -1765   -411       C  
ATOM   4019  C   PHE A 373      15.133 -10.043 -27.368  1.00 80.23           C  
ANISOU 4019  C   PHE A 373    14546  10549   5389   5695  -1777   -123       C  
ATOM   4020  O   PHE A 373      15.356 -11.161 -26.905  1.00 85.00           O  
ANISOU 4020  O   PHE A 373    15234  11164   5898   6007  -1605    104       O  
ATOM   4021  CB  PHE A 373      14.616  -8.811 -29.485  1.00 76.28           C  
ANISOU 4021  CB  PHE A 373    14483   9342   5157   5430  -1684   -402       C  
ATOM   4022  CG  PHE A 373      13.747  -8.675 -30.702  1.00 74.04           C  
ANISOU 4022  CG  PHE A 373    14868   8342   4922   5254  -1693   -564       C  
ATOM   4023  CD1 PHE A 373      13.934  -9.500 -31.799  1.00 83.76           C  
ANISOU 4023  CD1 PHE A 373    16754   9125   5947   5651  -1360   -431       C  
ATOM   4024  CD2 PHE A 373      12.742  -7.724 -30.750  1.00 70.19           C  
ANISOU 4024  CD2 PHE A 373    14260   7607   4801   4586  -1960   -864       C  
ATOM   4025  CE1 PHE A 373      13.136  -9.378 -32.923  1.00 79.84           C  
ANISOU 4025  CE1 PHE A 373    16821   8003   5511   5361  -1399   -582       C  
ATOM   4026  CE2 PHE A 373      11.942  -7.596 -31.871  1.00 73.11           C  
ANISOU 4026  CE2 PHE A 373    15184   7368   5224   4376  -2028   -910       C  
ATOM   4027  CZ  PHE A 373      12.138  -8.425 -32.959  1.00 74.58           C  
ANISOU 4027  CZ  PHE A 373    16007   7149   5180   4727  -1778   -740       C  
TER    4028      PHE A 373                                                      
HETATM 4029  C1  4OT A2001      -9.883  -1.056 -53.995  1.00 40.40           C  
HETATM 4030  C2  4OT A2001      -8.927  -1.398 -55.079  1.00 42.36           C  
HETATM 4031  N3  4OT A2001      -8.950  -1.159 -56.339  1.00 40.06           N  
HETATM 4032  N4  4OT A2001      -7.785  -1.729 -56.871  1.00 39.96           N  
HETATM 4033  C5  4OT A2001      -7.157  -2.265 -55.881  1.00 38.28           C  
HETATM 4034  O6  4OT A2001      -7.818  -2.100 -54.700  1.00 44.21           O  
HETATM 4035  C7  4OT A2001      -5.882  -2.982 -55.883  1.00 32.53           C  
HETATM 4036  C8  4OT A2001      -9.692   0.378 -53.498  1.00 40.69           C  
HETATM 4037  C11 4OT A2001      -8.512   1.823 -55.118  1.00 37.64           C  
HETATM 4038  C12 4OT A2001      -7.198   1.456 -54.509  1.00 45.56           C  
HETATM 4039  N12 4OT A2001      -9.655   1.334 -54.611  1.00 39.48           N  
HETATM 4040  C13 4OT A2001     -11.015   1.730 -54.993  1.00 43.91           C  
HETATM 4041  C14 4OT A2001     -11.785   1.628 -53.679  1.00 42.99           C  
HETATM 4042  O23 4OT A2001      -8.508   2.571 -56.089  1.00 35.69           O  
HETATM 4043  C24 4OT A2001     -10.865   0.899 -52.667  1.00 42.98           C  
HETATM 4044  C25 4OT A2001      -3.983  -0.227 -54.884  1.00 42.40           C  
HETATM 4045  C26 4OT A2001      -5.178   0.553 -54.443  1.00 45.18           C  
HETATM 4046  N27 4OT A2001      -6.263   0.669 -55.156  1.00 45.90           N  
HETATM 4047  C28 4OT A2001      -6.826   1.945 -53.280  1.00 53.70           C  
HETATM 4048  S29 4OT A2001      -5.217   1.394 -52.920  1.00 44.45           S  
HETATM 4049  C30 4OT A2001      -7.538   2.793 -52.301  1.00 57.55           C  
HETATM 4050  C34 4OT A2001      -8.116   3.988 -52.731  1.00 58.46           C  
HETATM 4051  C35 4OT A2001      -8.790   4.809 -51.845  1.00 59.61           C  
HETATM 4052  C36 4OT A2001      -8.902   4.456 -50.519  1.00 58.06           C  
HETATM 4053  C37 4OT A2001      -8.341   3.278 -50.061  1.00 55.57           C  
HETATM 4054  C38 4OT A2001      -7.677   2.477 -50.958  1.00 57.09           C  
HETATM 4055  F39 4OT A2001      -7.138   1.324 -50.502  1.00 60.99           F  
HETATM 4056  C44 4OT A2001      -5.168  -3.157 -57.063  1.00 34.98           C  
HETATM 4057  C45 4OT A2001      -3.954  -3.822 -57.056  1.00 33.88           C  
HETATM 4058  C46 4OT A2001      -3.442  -4.321 -55.877  1.00 34.53           C  
HETATM 4059  C47 4OT A2001      -4.143  -4.157 -54.701  1.00 34.42           C  
HETATM 4060  C48 4OT A2001      -5.357  -3.493 -54.700  1.00 32.29           C  
HETATM 4061  C1  OLA A2002       8.086  -6.559 -66.864  1.00 49.37           C  
HETATM 4062  O1  OLA A2002       7.418  -5.776 -67.574  1.00 48.00           O  
HETATM 4063  O2  OLA A2002       9.258  -6.250 -66.555  1.00 52.16           O  
HETATM 4064  C2  OLA A2002       7.486  -7.859 -66.385  1.00 45.51           C  
HETATM 4065  C3  OLA A2002       8.591  -8.872 -66.109  1.00 44.09           C  
HETATM 4066  C4  OLA A2002       8.538  -9.376 -64.671  1.00 44.24           C  
HETATM 4067  C5  OLA A2002       7.554 -10.531 -64.527  1.00 42.66           C  
HETATM 4068  C6  OLA A2002       7.078 -10.665 -63.085  1.00 41.37           C  
HETATM 4069  C7  OLA A2002       7.856 -11.752 -62.353  1.00 39.70           C  
HETATM 4070  C1  OLA A2003     -21.393   3.544 -23.716  1.00 68.43           C  
HETATM 4071  O1  OLA A2003     -20.303   3.807 -24.268  1.00 72.37           O  
HETATM 4072  O2  OLA A2003     -21.384   3.024 -22.580  1.00 70.31           O  
HETATM 4073  C2  OLA A2003     -22.702   3.845 -24.408  1.00 60.07           C  
HETATM 4074  C3  OLA A2003     -22.559   3.593 -25.905  1.00 55.57           C  
HETATM 4075  C4  OLA A2003     -23.283   4.666 -26.709  1.00 51.50           C  
HETATM 4076  C5  OLA A2003     -23.238   4.366 -28.202  1.00 48.18           C  
HETATM 4077  C6  OLA A2003     -23.276   5.654 -29.016  1.00 46.50           C  
CONECT  773 1410                                                                
CONECT 1410  773                                                                
CONECT 4029 4030 4036                                                           
CONECT 4030 4029 4031 4034                                                      
CONECT 4031 4030 4032                                                           
CONECT 4032 4031 4033                                                           
CONECT 4033 4032 4034 4035                                                      
CONECT 4034 4030 4033                                                           
CONECT 4035 4033 4056 4060                                                      
CONECT 4036 4029 4039 4043                                                      
CONECT 4037 4038 4039 4042                                                      
CONECT 4038 4037 4046 4047                                                      
CONECT 4039 4036 4037 4040                                                      
CONECT 4040 4039 4041                                                           
CONECT 4041 4040 4043                                                           
CONECT 4042 4037                                                                
CONECT 4043 4036 4041                                                           
CONECT 4044 4045                                                                
CONECT 4045 4044 4046 4048                                                      
CONECT 4046 4038 4045                                                           
CONECT 4047 4038 4048 4049                                                      
CONECT 4048 4045 4047                                                           
CONECT 4049 4047 4050 4054                                                      
CONECT 4050 4049 4051                                                           
CONECT 4051 4050 4052                                                           
CONECT 4052 4051 4053                                                           
CONECT 4053 4052 4054                                                           
CONECT 4054 4049 4053 4055                                                      
CONECT 4055 4054                                                                
CONECT 4056 4035 4057                                                           
CONECT 4057 4056 4058                                                           
CONECT 4058 4057 4059                                                           
CONECT 4059 4058 4060                                                           
CONECT 4060 4035 4059                                                           
CONECT 4061 4062 4063 4064                                                      
CONECT 4062 4061                                                                
CONECT 4063 4061                                                                
CONECT 4064 4061 4065                                                           
CONECT 4065 4064 4066                                                           
CONECT 4066 4065 4067                                                           
CONECT 4067 4066 4068                                                           
CONECT 4068 4067 4069                                                           
CONECT 4069 4068                                                                
CONECT 4070 4071 4072 4073                                                      
CONECT 4071 4070                                                                
CONECT 4072 4070                                                                
CONECT 4073 4070 4074                                                           
CONECT 4074 4073 4075                                                           
CONECT 4075 4074 4076                                                           
CONECT 4076 4075 4077                                                           
CONECT 4077 4076                                                                
MASTER      612    0    3   21    8    0    5    6 4076    1   51   43          
END