HEADER    SIGNALING PROTEIN                       07-DEC-11   3UZC              
TITLE     THERMOSTABILISED ADENOSINE A2A RECEPTOR IN COMPLEX WITH 4-(3-AMINO-5- 
TITLE    2 PHENYL-1,2,4-TRIAZIN-6-YL)-2-CHLOROPHENOL                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADENOSINE A2A RECEPTOR;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1-317;                                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ADORA2A;                                                       
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    7TM, GPCR, G-PROTEIN, MEMBRANE PROTEIN, SIGNALING PROTEIN             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.CONGREVE,S.P.ANDREWS,A.S.DORE,K.HOLLENSTEIN,E.HURRELL,C.J.LANGMEAD, 
AUTHOR   2 J.S.MASON,I.W.NG,A.ZHUKOV,M.WEIR,F.H.MARSHALL                        
REVDAT   2   08-NOV-23 3UZC    1       REMARK SEQADV                            
REVDAT   1   21-MAR-12 3UZC    0                                                
JRNL        AUTH   M.CONGREVE,S.P.ANDREWS,A.S.DORE,K.HOLLENSTEIN,E.HURRELL,     
JRNL        AUTH 2 C.J.LANGMEAD,J.S.MASON,I.W.NG,B.TEHAN,A.ZHUKOV,M.WEIR,       
JRNL        AUTH 3 F.H.MARSHALL                                                 
JRNL        TITL   DISCOVERY OF 1,2,4-TRIAZINE DERIVATIVES AS ADENOSINE A(2A)   
JRNL        TITL 2 ANTAGONISTS USING STRUCTURE BASED DRUG DESIGN                
JRNL        REF    J.MED.CHEM.                   V.  55  1898 2012              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   22220592                                                     
JRNL        DOI    10.1021/JM201376W                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.34 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.4_84)                       
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) : 3.34                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.81                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 10797                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.283                           
REMARK   3   R VALUE            (WORKING SET) : 0.282                           
REMARK   3   FREE R VALUE                     : 0.290                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.730                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 511                             
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 19.8049 -  5.2787    0.91     2608   138  0.2566 0.2355        
REMARK   3     2  5.2787 -  4.2030    0.93     2603   113  0.2420 0.2290        
REMARK   3     3  4.2030 -  3.6756    0.92     2544   132  0.3112 0.3924        
REMARK   3     4  3.6756 -  3.3413    0.93     2531   128  0.4328 0.4763        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.23                                          
REMARK   3   B_SOL              : 56.80                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.420            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 39.970           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 97.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 155.9                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 19.30240                                             
REMARK   3    B22 (A**2) : -61.76260                                            
REMARK   3    B33 (A**2) : 42.46010                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           2333                                  
REMARK   3   ANGLE     :  0.392           3180                                  
REMARK   3   CHIRALITY :  0.027            377                                  
REMARK   3   PLANARITY :  0.002            390                                  
REMARK   3   DIHEDRAL  : 11.047            789                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 15                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 7:33                                 
REMARK   3    ORIGIN FOR THE GROUP (A):  19.8961  26.4223  42.3237              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0231 T22:   0.7021                                     
REMARK   3      T33:   2.0473 T12:  -0.0170                                     
REMARK   3      T13:   0.0798 T23:   0.0619                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7822 L22:   0.3730                                     
REMARK   3      L33:   1.8361 L12:   0.4622                                     
REMARK   3      L13:  -0.2305 L23:   0.3327                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1385 S12:  -0.8816 S13:  -0.2594                       
REMARK   3      S21:   0.9329 S22:   0.8912 S23:   0.0189                       
REMARK   3      S31:   0.0662 S32:  -0.6210 S33:  -0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 34:40                                
REMARK   3    ORIGIN FOR THE GROUP (A):  20.8923  44.5708  30.3390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6675 T22:   1.0670                                     
REMARK   3      T33:   2.9131 T12:   0.2578                                     
REMARK   3      T13:   0.1413 T23:   0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0116 L22:   0.0137                                     
REMARK   3      L33:  -0.0001 L12:  -0.0170                                     
REMARK   3      L13:  -0.0073 L23:   0.0043                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3301 S12:   0.4747 S13:   1.0537                       
REMARK   3      S21:   0.0858 S22:  -0.2420 S23:   0.1653                       
REMARK   3      S31:   0.1167 S32:   0.9460 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 41:68                                
REMARK   3    ORIGIN FOR THE GROUP (A):  17.6095  22.7030  34.0599              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1542 T22:   0.7971                                     
REMARK   3      T33:   1.5095 T12:   0.0186                                     
REMARK   3      T13:   0.5204 T23:   0.1842                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0143 L22:   0.5807                                     
REMARK   3      L33:   1.1947 L12:  -0.1838                                     
REMARK   3      L13:  -0.2603 L23:   0.8284                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9074 S12:  -0.3434 S13:  -0.0174                       
REMARK   3      S21:  -1.3947 S22:  -0.0631 S23:  -0.3487                       
REMARK   3      S31:   0.8982 S32:  -0.2434 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 69:76                                
REMARK   3    ORIGIN FOR THE GROUP (A):   7.5585   4.2447  32.5211              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7182 T22:   1.4188                                     
REMARK   3      T33:   3.2677 T12:  -0.4813                                     
REMARK   3      T13:   0.3004 T23:   0.2640                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2309 L22:   0.1103                                     
REMARK   3      L33:   0.0642 L12:   0.0122                                     
REMARK   3      L13:  -0.1018 L23:   0.0428                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0115 S12:   0.8587 S13:  -0.2868                       
REMARK   3      S21:  -0.8914 S22:   0.6636 S23:   0.0630                       
REMARK   3      S31:   0.7000 S32:   0.1182 S33:   0.0002                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 77:104                               
REMARK   3    ORIGIN FOR THE GROUP (A):  21.1673  23.3909  24.3474              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9384 T22:   0.9372                                     
REMARK   3      T33:   2.0417 T12:  -0.1808                                     
REMARK   3      T13:   0.2600 T23:   0.2833                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4029 L22:   0.0441                                     
REMARK   3      L33:   0.5634 L12:  -0.0232                                     
REMARK   3      L13:   0.5358 L23:  -0.1434                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1828 S12:   1.1155 S13:  -0.2695                       
REMARK   3      S21:  -1.6856 S22:   0.8480 S23:   0.4586                       
REMARK   3      S31:  -0.0157 S32:  -0.8079 S33:   0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 105:118                              
REMARK   3    ORIGIN FOR THE GROUP (A):  26.3813  43.4402  14.5747              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7762 T22:   0.7503                                     
REMARK   3      T33:   2.6562 T12:   0.0874                                     
REMARK   3      T13:   0.4149 T23:   0.0939                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1336 L22:   0.0785                                     
REMARK   3      L33:   0.2243 L12:   0.1002                                     
REMARK   3      L13:   0.1680 L23:   0.1343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8682 S12:   1.2855 S13:   0.6853                       
REMARK   3      S21:  -1.3287 S22:  -0.1364 S23:   0.6300                       
REMARK   3      S31:   0.5142 S32:   0.1701 S33:   0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 119:141                              
REMARK   3    ORIGIN FOR THE GROUP (A):  13.9849  23.3359  20.1521              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0250 T22:   0.7615                                     
REMARK   3      T33:   1.8518 T12:  -0.0383                                     
REMARK   3      T13:  -0.4225 T23:  -0.0596                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8191 L22:   0.1084                                     
REMARK   3      L33:   0.4180 L12:  -0.2908                                     
REMARK   3      L13:   0.2833 L23:  -0.0451                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5249 S12:   1.6907 S13:  -0.5014                       
REMARK   3      S21:  -1.4877 S22:   0.4902 S23:   0.9795                       
REMARK   3      S31:   0.4425 S32:  -0.3060 S33:   0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 142:149                              
REMARK   3    ORIGIN FOR THE GROUP (A):  13.5006  -0.2735  22.2445              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6294 T22:   1.2959                                     
REMARK   3      T33:   2.7567 T12:   0.1160                                     
REMARK   3      T13:   0.1054 T23:   0.0233                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1094 L22:   0.0133                                     
REMARK   3      L33:   0.1208 L12:  -0.0124                                     
REMARK   3      L13:   0.0827 L23:   0.0190                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2306 S12:   0.7374 S13:  -0.1390                       
REMARK   3      S21:  -0.2607 S22:  -0.3527 S23:  -0.1246                       
REMARK   3      S31:   0.2734 S32:  -1.0394 S33:  -0.0002                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 158:175                              
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2924   0.3982  30.1014              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4470 T22:   0.8682                                     
REMARK   3      T33:   2.5388 T12:  -0.0032                                     
REMARK   3      T13:  -0.0409 T23:   0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0866 L22:   0.4035                                     
REMARK   3      L33:   0.5261 L12:  -0.1382                                     
REMARK   3      L13:   0.1249 L23:   0.0616                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.4071 S12:  -0.1516 S13:  -0.4675                       
REMARK   3      S21:  -1.7358 S22:   0.1961 S23:   1.1980                       
REMARK   3      S31:   1.5934 S32:  -0.3512 S33:  -0.0000                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN A AND RESID 176:211                              
REMARK   3    ORIGIN FOR THE GROUP (A):  33.9104  25.9245  17.8107              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4013 T22:   0.8782                                     
REMARK   3      T33:   2.1758 T12:  -0.2641                                     
REMARK   3      T13:   0.0859 T23:   0.1784                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9021 L22:   0.7475                                     
REMARK   3      L33:   0.3133 L12:  -0.8373                                     
REMARK   3      L13:  -0.2824 L23:   0.1251                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3284 S12:   0.1700 S13:   1.3920                       
REMARK   3      S21:  -0.0231 S22:  -0.2569 S23:  -0.5113                       
REMARK   3      S31:  -0.0053 S32:   0.0241 S33:  -0.0000                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN A AND RESID 212:220                              
REMARK   3    ORIGIN FOR THE GROUP (A):  44.9910  54.1652  18.5103              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8685 T22:   1.3127                                     
REMARK   3      T33:   3.2693 T12:  -0.0862                                     
REMARK   3      T13:   0.7543 T23:   0.5088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0374 L22:   0.0068                                     
REMARK   3      L33:   0.1911 L12:  -0.0181                                     
REMARK   3      L13:   0.0850 L23:  -0.0392                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4686 S12:  -0.1936 S13:   0.1141                       
REMARK   3      S21:  -0.3292 S22:   0.7021 S23:  -0.6629                       
REMARK   3      S31:   0.9089 S32:  -0.2057 S33:   0.0000                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN A AND RESID 221:258                              
REMARK   3    ORIGIN FOR THE GROUP (A):  33.6133  24.7887  26.7588              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1445 T22:   0.9679                                     
REMARK   3      T33:   1.1601 T12:  -0.0516                                     
REMARK   3      T13:  -0.1805 T23:  -0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8711 L22:   0.4612                                     
REMARK   3      L33:   1.1230 L12:   0.1736                                     
REMARK   3      L13:  -1.2405 L23:  -0.6113                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5801 S12:   0.7994 S13:  -0.7424                       
REMARK   3      S21:  -1.2940 S22:   1.5760 S23:  -2.6155                       
REMARK   3      S31:  -0.7585 S32:  -0.2122 S33:   0.0001                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN A AND RESID 259:267                              
REMARK   3    ORIGIN FOR THE GROUP (A):  32.4025  -2.0977  30.1301              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0940 T22:   0.7869                                     
REMARK   3      T33:   3.3207 T12:  -0.1292                                     
REMARK   3      T13:   0.0593 T23:   0.0128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2831 L22:   0.0883                                     
REMARK   3      L33:   0.1460 L12:  -0.0222                                     
REMARK   3      L13:   0.2208 L23:  -0.0038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0784 S12:  -0.7130 S13:   0.7774                       
REMARK   3      S21:  -0.9300 S22:   0.9518 S23:   0.3694                       
REMARK   3      S31:  -0.7816 S32:   0.7118 S33:   0.0000                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN A AND RESID 268:292                              
REMARK   3    ORIGIN FOR THE GROUP (A):  29.3387  21.9009  37.3562              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2323 T22:   0.8151                                     
REMARK   3      T33:  -1.4866 T12:   0.0443                                     
REMARK   3      T13:  -1.3396 T23:  -0.2153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0895 L22:   0.4893                                     
REMARK   3      L33:   1.7409 L12:  -0.0542                                     
REMARK   3      L13:   0.1088 L23:  -0.3201                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1174 S12:  -0.9465 S13:   0.1448                       
REMARK   3      S21:   0.9190 S22:  -0.1173 S23:  -0.4923                       
REMARK   3      S31:  -0.6154 S32:   0.6193 S33:   1.3419                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN A AND RESID 293:305                              
REMARK   3    ORIGIN FOR THE GROUP (A):  25.9277  42.7856  42.7276              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0979 T22:   0.8537                                     
REMARK   3      T33:   1.8210 T12:  -0.0171                                     
REMARK   3      T13:  -0.3406 T23:  -0.0022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1290 L22:   0.0934                                     
REMARK   3      L33:   0.1179 L12:  -0.0107                                     
REMARK   3      L13:  -0.0480 L23:  -0.1217                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3614 S12:  -0.5341 S13:   1.1545                       
REMARK   3      S21:   1.6046 S22:  -0.0558 S23:  -1.0137                       
REMARK   3      S31:  -2.2735 S32:   1.7330 S33:   0.0000                       
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 3UZC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-DEC-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000069398.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAY-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 3                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9777                             
REMARK 200  MONOCHROMATOR                  : ACCEL FIXED EXIT DOUBLE CRYSTAL    
REMARK 200                                   SI (111)                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS, SCALA                         
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10975                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.340                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.290                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.09500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.34                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.85100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
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: 3PWH                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 77.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 32-42% PEG1000, 0.25M MGCL2, 0.3% NG,    
REMARK 280  0.1%(W/V) 1-BUTANOL, 0.05% CYMAL-6, PH 8.0, VAPOR DIFFUSION,        
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       55.35000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       56.03200            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       63.45000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       55.35000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.03200            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       63.45000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       55.35000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       56.03200            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       63.45000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       55.35000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       56.03200            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       63.45000            
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     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     ILE A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     LYS A   150                                                      
REMARK 465     GLU A   151                                                      
REMARK 465     GLY A   152                                                      
REMARK 465     LYS A   153                                                      
REMARK 465     ASN A   154                                                      
REMARK 465     HIS A   155                                                      
REMARK 465     SER A   156                                                      
REMARK 465     GLN A   157                                                      
REMARK 465     HIS A   306                                                      
REMARK 465     VAL A   307                                                      
REMARK 465     LEU A   308                                                      
REMARK 465     ARG A   309                                                      
REMARK 465     GLN A   310                                                      
REMARK 465     GLN A   311                                                      
REMARK 465     GLU A   312                                                      
REMARK 465     PRO A   313                                                      
REMARK 465     PHE A   314                                                      
REMARK 465     LYS A   315                                                      
REMARK 465     ALA A   316                                                      
REMARK 465     ALA A   317                                                      
REMARK 465     ALA A   318                                                      
REMARK 465     ALA A   319                                                      
REMARK 465     HIS A   320                                                      
REMARK 465     HIS A   321                                                      
REMARK 465     HIS A   322                                                      
REMARK 465     HIS A   323                                                      
REMARK 465     HIS A   324                                                      
REMARK 465     HIS A   325                                                      
REMARK 465     HIS A   326                                                      
REMARK 465     HIS A   327                                                      
REMARK 465     HIS A   328                                                      
REMARK 465     HIS A   329                                                      
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  58      -53.64   -130.74                                   
REMARK 500    ALA A  73      175.44    -56.11                                   
REMARK 500    VAL A 116       91.81    -68.67                                   
REMARK 500    ALA A 165      101.04    -56.88                                   
REMARK 500    VAL A 178      -66.46    -97.84                                   
REMARK 500    ASN A 181      -70.91    -66.43                                   
REMARK 500    PHE A 182      -71.65    -59.37                                   
REMARK 500    VAL A 186      -58.91   -135.28                                   
REMARK 500    PRO A 217      -74.28    -57.77                                   
REMARK 500    SER A 263      114.40    -39.97                                   
REMARK 500    PRO A 266      170.65    -58.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T4E A 330                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3UZA   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED TO COMPOUND 4G                            
REMARK 900 RELATED ID: 3PWH   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED TO ZM241385                               
REMARK 900 RELATED ID: 3RFM   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED TO CAFFEINE                               
REMARK 900 RELATED ID: 3REY   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED TO XAC                                    
DBREF  3UZC A    1   317  UNP    P29274   AA2AR_HUMAN      1    317             
SEQADV 3UZC LEU A   54  UNP  P29274    ALA    54 ENGINEERED MUTATION            
SEQADV 3UZC ALA A   88  UNP  P29274    THR    88 ENGINEERED MUTATION            
SEQADV 3UZC ALA A  107  UNP  P29274    ARG   107 ENGINEERED MUTATION            
SEQADV 3UZC ALA A  122  UNP  P29274    LYS   122 ENGINEERED MUTATION            
SEQADV 3UZC ALA A  202  UNP  P29274    LEU   202 ENGINEERED MUTATION            
SEQADV 3UZC ALA A  235  UNP  P29274    LEU   235 ENGINEERED MUTATION            
SEQADV 3UZC ALA A  239  UNP  P29274    VAL   239 ENGINEERED MUTATION            
SEQADV 3UZC ALA A  277  UNP  P29274    SER   277 ENGINEERED MUTATION            
SEQADV 3UZC ALA A  318  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZC ALA A  319  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZC HIS A  320  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZC HIS A  321  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZC HIS A  322  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZC HIS A  323  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZC HIS A  324  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZC HIS A  325  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZC HIS A  326  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZC HIS A  327  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZC HIS A  328  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZC HIS A  329  UNP  P29274              EXPRESSION TAG                 
SEQRES   1 A  329  MET PRO ILE MET GLY SER SER VAL TYR ILE THR VAL GLU          
SEQRES   2 A  329  LEU ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU          
SEQRES   3 A  329  VAL CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN ASN          
SEQRES   4 A  329  VAL THR ASN TYR PHE VAL VAL SER LEU ALA ALA ALA ASP          
SEQRES   5 A  329  ILE LEU VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE THR          
SEQRES   6 A  329  ILE SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU          
SEQRES   7 A  329  PHE ILE ALA CYS PHE VAL LEU VAL LEU ALA GLN SER SER          
SEQRES   8 A  329  ILE PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE          
SEQRES   9 A  329  ALA ILE ALA ILE PRO LEU ARG TYR ASN GLY LEU VAL THR          
SEQRES  10 A  329  GLY THR ARG ALA ALA GLY ILE ILE ALA ILE CYS TRP VAL          
SEQRES  11 A  329  LEU SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY TRP          
SEQRES  12 A  329  ASN ASN CYS GLY GLN PRO LYS GLU GLY LYS ASN HIS SER          
SEQRES  13 A  329  GLN GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU          
SEQRES  14 A  329  ASP VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN PHE          
SEQRES  15 A  329  PHE ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU GLY          
SEQRES  16 A  329  VAL TYR LEU ARG ILE PHE ALA ALA ALA ARG ARG GLN LEU          
SEQRES  17 A  329  LYS GLN MET GLU SER GLN PRO LEU PRO GLY GLU ARG ALA          
SEQRES  18 A  329  ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS SER          
SEQRES  19 A  329  ALA ALA ILE ILE ALA GLY LEU PHE ALA LEU CYS TRP LEU          
SEQRES  20 A  329  PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS PRO          
SEQRES  21 A  329  ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU ALA          
SEQRES  22 A  329  ILE VAL LEU ALA HIS THR ASN SER VAL VAL ASN PRO PHE          
SEQRES  23 A  329  ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR PHE          
SEQRES  24 A  329  ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN GLN GLU          
SEQRES  25 A  329  PRO PHE LYS ALA ALA ALA ALA HIS HIS HIS HIS HIS HIS          
SEQRES  26 A  329  HIS HIS HIS HIS                                              
HET    T4E  A 330      21                                                       
HETNAM     T4E 4-(3-AMINO-5-PHENYL-1,2,4-TRIAZIN-6-YL)-2-CHLOROPHENOL           
FORMUL   2  T4E    C15 H11 CL N4 O                                              
HELIX    1   1 SER A    7  ASN A   34  1                                  28    
HELIX    2   2 SER A   35  ASN A   39  5                                   5    
HELIX    3   3 VAL A   40  LEU A   58  1                                  19    
HELIX    4   4 LEU A   58  GLY A   69  1                                  12    
HELIX    5   5 ALA A   73  ILE A  108  1                                  36    
HELIX    6   6 ILE A  108  VAL A  116  1                                   9    
HELIX    7   7 THR A  117  LEU A  137  1                                  21    
HELIX    8   8 THR A  138  GLY A  142  5                                   5    
HELIX    9   9 LEU A  167  VAL A  172  1                                   6    
HELIX   10  10 PRO A  173  TYR A  179  1                                   7    
HELIX   11  11 ASN A  181  VAL A  186  1                                   6    
HELIX   12  12 VAL A  186  MET A  211  1                                  26    
HELIX   13  13 GLY A  218  CYS A  259  1                                  42    
HELIX   14  14 PRO A  266  ILE A  292  1                                  27    
HELIX   15  15 ILE A  292  SER A  305  1                                  14    
SHEET    1   A 2 PHE A  70  ALA A  72  0                                        
SHEET    2   A 2 VAL A 164  CYS A 166 -1  O  CYS A 166   N  PHE A  70           
SSBOND   1 CYS A   71    CYS A  159                          1555   1555  2.03  
SSBOND   2 CYS A   74    CYS A  146                          1555   1555  2.03  
SSBOND   3 CYS A   77    CYS A  166                          1555   1555  2.03  
SSBOND   4 CYS A  259    CYS A  262                          1555   1555  2.03  
SITE     1 AC1  9 VAL A  84  LEU A  85  PHE A 168  LEU A 249                    
SITE     2 AC1  9 HIS A 250  ASN A 253  ILE A 274  ALA A 277                    
SITE     3 AC1  9 HIS A 278                                                     
CRYST1  110.700  112.064  126.900  90.00  90.00  90.00 I 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009033  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008923  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007880        0.00000                         
ATOM      1  N   SER A   7      22.399   6.822  51.127  1.00184.85           N  
ATOM      2  CA  SER A   7      21.663   8.071  50.962  1.00183.97           C  
ATOM      3  C   SER A   7      22.606   9.263  50.835  1.00183.85           C  
ATOM      4  O   SER A   7      22.238  10.393  51.156  1.00185.85           O  
ATOM      5  CB  SER A   7      20.699   8.287  52.131  1.00186.19           C  
ATOM      6  OG  SER A   7      19.713   7.270  52.176  1.00187.83           O  
ATOM      7  N   VAL A   8      23.824   9.004  50.368  1.00181.88           N  
ATOM      8  CA  VAL A   8      24.812  10.061  50.173  1.00178.15           C  
ATOM      9  C   VAL A   8      24.660  10.693  48.793  1.00175.02           C  
ATOM     10  O   VAL A   8      24.640  11.918  48.658  1.00169.67           O  
ATOM     11  CB  VAL A   8      26.249   9.534  50.336  1.00172.04           C  
ATOM     12  CG1 VAL A   8      27.256  10.642  50.062  1.00161.34           C  
ATOM     13  CG2 VAL A   8      26.448   8.956  51.728  1.00177.11           C  
ATOM     14  N   TYR A   9      24.556   9.848  47.772  1.00175.20           N  
ATOM     15  CA  TYR A   9      24.317  10.309  46.411  1.00171.48           C  
ATOM     16  C   TYR A   9      23.078  11.195  46.372  1.00183.00           C  
ATOM     17  O   TYR A   9      23.061  12.231  45.708  1.00178.87           O  
ATOM     18  CB  TYR A   9      24.139   9.116  45.470  1.00159.59           C  
ATOM     19  CG  TYR A   9      23.747   9.492  44.059  1.00150.82           C  
ATOM     20  CD1 TYR A   9      24.708   9.847  43.122  1.00153.86           C  
ATOM     21  CD2 TYR A   9      22.416   9.484  43.661  1.00146.92           C  
ATOM     22  CE1 TYR A   9      24.355  10.187  41.830  1.00157.89           C  
ATOM     23  CE2 TYR A   9      22.053   9.822  42.370  1.00150.22           C  
ATOM     24  CZ  TYR A   9      23.027  10.173  41.459  1.00158.93           C  
ATOM     25  OH  TYR A   9      22.673  10.512  40.173  1.00164.43           O  
ATOM     26  N   ILE A  10      22.043  10.776  47.094  1.00197.74           N  
ATOM     27  CA  ILE A  10      20.806  11.539  47.182  1.00195.20           C  
ATOM     28  C   ILE A  10      21.063  12.916  47.785  1.00185.73           C  
ATOM     29  O   ILE A  10      20.606  13.930  47.259  1.00185.37           O  
ATOM     30  CB  ILE A  10      19.756  10.806  48.038  1.00203.64           C  
ATOM     31  CG1 ILE A  10      19.547   9.381  47.521  1.00204.79           C  
ATOM     32  CG2 ILE A  10      18.446  11.580  48.054  1.00202.41           C  
ATOM     33  CD1 ILE A  10      18.588   8.561  48.357  1.00207.13           C  
ATOM     34  N   THR A  11      21.801  12.942  48.890  1.00178.17           N  
ATOM     35  CA  THR A  11      22.113  14.190  49.576  1.00172.88           C  
ATOM     36  C   THR A  11      22.872  15.154  48.668  1.00168.41           C  
ATOM     37  O   THR A  11      22.532  16.333  48.581  1.00170.02           O  
ATOM     38  CB  THR A  11      22.937  13.941  50.855  1.00172.39           C  
ATOM     39  OG1 THR A  11      22.188  13.117  51.755  1.00175.98           O  
ATOM     40  CG2 THR A  11      23.269  15.257  51.540  1.00172.21           C  
ATOM     41  N   VAL A  12      23.897  14.645  47.992  1.00161.43           N  
ATOM     42  CA  VAL A  12      24.697  15.463  47.086  1.00150.38           C  
ATOM     43  C   VAL A  12      23.857  16.006  45.934  1.00147.21           C  
ATOM     44  O   VAL A  12      23.944  17.186  45.596  1.00148.94           O  
ATOM     45  CB  VAL A  12      25.898  14.682  46.521  1.00140.87           C  
ATOM     46  CG1 VAL A  12      26.570  15.470  45.407  1.00122.56           C  
ATOM     47  CG2 VAL A  12      26.889  14.361  47.629  1.00146.64           C  
ATOM     48  N   GLU A  13      23.043  15.142  45.335  1.00147.68           N  
ATOM     49  CA  GLU A  13      22.169  15.553  44.241  1.00148.06           C  
ATOM     50  C   GLU A  13      21.199  16.643  44.686  1.00144.98           C  
ATOM     51  O   GLU A  13      20.927  17.587  43.942  1.00142.23           O  
ATOM     52  CB  GLU A  13      21.400  14.354  43.684  1.00151.87           C  
ATOM     53  CG  GLU A  13      22.249  13.396  42.864  1.00152.84           C  
ATOM     54  CD  GLU A  13      22.790  14.033  41.599  1.00156.16           C  
ATOM     55  OE1 GLU A  13      22.310  13.676  40.502  1.00156.50           O  
ATOM     56  OE2 GLU A  13      23.691  14.893  41.699  1.00158.13           O  
ATOM     57  N   LEU A  14      20.679  16.506  45.901  1.00142.99           N  
ATOM     58  CA  LEU A  14      19.790  17.513  46.468  1.00138.88           C  
ATOM     59  C   LEU A  14      20.534  18.827  46.683  1.00130.97           C  
ATOM     60  O   LEU A  14      19.998  19.903  46.420  1.00126.83           O  
ATOM     61  CB  LEU A  14      19.187  17.022  47.787  1.00141.12           C  
ATOM     62  CG  LEU A  14      17.849  16.282  47.715  1.00140.50           C  
ATOM     63  CD1 LEU A  14      17.871  15.193  46.654  1.00140.85           C  
ATOM     64  CD2 LEU A  14      17.477  15.707  49.075  1.00141.82           C  
ATOM     65  N   ALA A  15      21.771  18.730  47.159  1.00129.85           N  
ATOM     66  CA  ALA A  15      22.600  19.907  47.386  1.00132.64           C  
ATOM     67  C   ALA A  15      22.803  20.688  46.091  1.00141.76           C  
ATOM     68  O   ALA A  15      22.746  21.918  46.080  1.00146.59           O  
ATOM     69  CB  ALA A  15      23.940  19.506  47.982  1.00127.58           C  
ATOM     70  N   ILE A  16      23.037  19.964  45.002  1.00141.07           N  
ATOM     71  CA  ILE A  16      23.222  20.585  43.695  1.00139.07           C  
ATOM     72  C   ILE A  16      21.941  21.262  43.216  1.00141.10           C  
ATOM     73  O   ILE A  16      21.969  22.402  42.749  1.00138.16           O  
ATOM     74  CB  ILE A  16      23.681  19.561  42.640  1.00133.26           C  
ATOM     75  CG1 ILE A  16      25.105  19.092  42.940  1.00134.50           C  
ATOM     76  CG2 ILE A  16      23.613  20.160  41.247  1.00127.18           C  
ATOM     77  CD1 ILE A  16      25.688  18.202  41.866  1.00138.41           C  
ATOM     78  N   ALA A  17      20.822  20.555  43.339  1.00143.25           N  
ATOM     79  CA  ALA A  17      19.529  21.075  42.907  1.00143.10           C  
ATOM     80  C   ALA A  17      19.257  22.460  43.482  1.00142.86           C  
ATOM     81  O   ALA A  17      18.754  23.341  42.787  1.00140.33           O  
ATOM     82  CB  ALA A  17      18.416  20.111  43.293  1.00146.30           C  
ATOM     83  N   VAL A  18      19.594  22.645  44.754  1.00146.44           N  
ATOM     84  CA  VAL A  18      19.379  23.922  45.425  1.00148.20           C  
ATOM     85  C   VAL A  18      20.211  25.033  44.791  1.00144.50           C  
ATOM     86  O   VAL A  18      19.685  26.086  44.431  1.00142.84           O  
ATOM     87  CB  VAL A  18      19.710  23.832  46.927  1.00150.05           C  
ATOM     88  CG1 VAL A  18      19.529  25.187  47.592  1.00155.47           C  
ATOM     89  CG2 VAL A  18      18.838  22.783  47.599  1.00146.68           C  
ATOM     90  N   LEU A  19      21.511  24.791  44.656  1.00141.56           N  
ATOM     91  CA  LEU A  19      22.418  25.768  44.063  1.00139.37           C  
ATOM     92  C   LEU A  19      22.044  26.078  42.618  1.00137.25           C  
ATOM     93  O   LEU A  19      22.095  27.230  42.187  1.00131.55           O  
ATOM     94  CB  LEU A  19      23.866  25.276  44.136  1.00142.49           C  
ATOM     95  CG  LEU A  19      24.608  25.441  45.464  1.00147.13           C  
ATOM     96  CD1 LEU A  19      23.862  24.769  46.608  1.00151.37           C  
ATOM     97  CD2 LEU A  19      26.024  24.895  45.351  1.00145.40           C  
ATOM     98  N   ALA A  20      21.674  25.042  41.872  1.00147.36           N  
ATOM     99  CA  ALA A  20      21.275  25.205  40.479  1.00149.80           C  
ATOM    100  C   ALA A  20      20.089  26.156  40.364  1.00144.75           C  
ATOM    101  O   ALA A  20      20.034  26.991  39.461  1.00137.69           O  
ATOM    102  CB  ALA A  20      20.941  23.857  39.860  1.00152.03           C  
ATOM    103  N   ILE A  21      19.141  26.025  41.286  1.00145.22           N  
ATOM    104  CA  ILE A  21      17.980  26.905  41.313  1.00142.39           C  
ATOM    105  C   ILE A  21      18.380  28.306  41.761  1.00137.31           C  
ATOM    106  O   ILE A  21      18.272  29.262  40.997  1.00137.50           O  
ATOM    107  CB  ILE A  21      16.877  26.365  42.243  1.00145.13           C  
ATOM    108  CG1 ILE A  21      16.414  24.983  41.776  1.00142.26           C  
ATOM    109  CG2 ILE A  21      15.702  27.329  42.288  1.00146.89           C  
ATOM    110  CD1 ILE A  21      15.350  24.364  42.659  1.00142.69           C  
ATOM    111  N   LEU A  22      18.848  28.418  43.001  1.00134.30           N  
ATOM    112  CA  LEU A  22      19.254  29.706  43.558  1.00129.84           C  
ATOM    113  C   LEU A  22      20.137  30.486  42.592  1.00132.71           C  
ATOM    114  O   LEU A  22      19.866  31.645  42.285  1.00133.83           O  
ATOM    115  CB  LEU A  22      19.991  29.510  44.884  1.00120.13           C  
ATOM    116  CG  LEU A  22      19.214  28.844  46.020  1.00118.62           C  
ATOM    117  CD1 LEU A  22      20.077  28.754  47.268  1.00117.45           C  
ATOM    118  CD2 LEU A  22      17.927  29.600  46.307  1.00119.18           C  
ATOM    119  N   GLY A  23      21.193  29.837  42.114  1.00131.04           N  
ATOM    120  CA  GLY A  23      22.154  30.472  41.233  1.00130.39           C  
ATOM    121  C   GLY A  23      21.546  31.087  39.986  1.00126.29           C  
ATOM    122  O   GLY A  23      21.588  32.302  39.803  1.00112.70           O  
ATOM    123  N   ASN A  24      20.982  30.248  39.124  1.00133.94           N  
ATOM    124  CA  ASN A  24      20.436  30.715  37.853  1.00134.06           C  
ATOM    125  C   ASN A  24      19.186  31.579  38.001  1.00130.08           C  
ATOM    126  O   ASN A  24      18.920  32.437  37.162  1.00127.98           O  
ATOM    127  CB  ASN A  24      20.168  29.537  36.914  1.00138.97           C  
ATOM    128  CG  ASN A  24      21.444  28.876  36.431  1.00141.49           C  
ATOM    129  OD1 ASN A  24      22.270  29.505  35.768  1.00135.74           O  
ATOM    130  ND2 ASN A  24      21.611  27.600  36.760  1.00145.16           N  
ATOM    131  N   VAL A  25      18.417  31.348  39.061  1.00129.73           N  
ATOM    132  CA  VAL A  25      17.268  32.197  39.352  1.00130.33           C  
ATOM    133  C   VAL A  25      17.760  33.593  39.712  1.00132.87           C  
ATOM    134  O   VAL A  25      17.184  34.598  39.293  1.00133.04           O  
ATOM    135  CB  VAL A  25      16.418  31.638  40.508  1.00134.75           C  
ATOM    136  CG1 VAL A  25      15.467  32.701  41.036  1.00136.24           C  
ATOM    137  CG2 VAL A  25      15.650  30.406  40.053  1.00138.76           C  
ATOM    138  N   LEU A  26      18.837  33.642  40.487  1.00133.29           N  
ATOM    139  CA  LEU A  26      19.479  34.900  40.840  1.00128.30           C  
ATOM    140  C   LEU A  26      19.937  35.619  39.579  1.00123.50           C  
ATOM    141  O   LEU A  26      19.782  36.832  39.453  1.00128.81           O  
ATOM    142  CB  LEU A  26      20.675  34.641  41.756  1.00124.86           C  
ATOM    143  CG  LEU A  26      21.408  35.867  42.296  1.00118.33           C  
ATOM    144  CD1 LEU A  26      20.463  36.728  43.115  1.00124.55           C  
ATOM    145  CD2 LEU A  26      22.610  35.445  43.126  1.00110.31           C  
ATOM    146  N   VAL A  27      20.501  34.860  38.646  1.00120.89           N  
ATOM    147  CA  VAL A  27      20.952  35.409  37.373  1.00117.02           C  
ATOM    148  C   VAL A  27      19.787  36.009  36.592  1.00115.93           C  
ATOM    149  O   VAL A  27      19.897  37.105  36.044  1.00119.62           O  
ATOM    150  CB  VAL A  27      21.650  34.333  36.513  1.00116.61           C  
ATOM    151  CG1 VAL A  27      21.966  34.876  35.127  1.00105.32           C  
ATOM    152  CG2 VAL A  27      22.915  33.842  37.201  1.00125.17           C  
ATOM    153  N   CYS A  28      18.670  35.289  36.549  1.00115.89           N  
ATOM    154  CA  CYS A  28      17.481  35.763  35.849  1.00120.16           C  
ATOM    155  C   CYS A  28      16.941  37.032  36.497  1.00126.14           C  
ATOM    156  O   CYS A  28      16.511  37.960  35.811  1.00124.69           O  
ATOM    157  CB  CYS A  28      16.396  34.685  35.841  1.00122.60           C  
ATOM    158  SG  CYS A  28      16.869  33.146  35.021  1.00148.77           S  
ATOM    159  N   TRP A  29      16.967  37.062  37.824  1.00133.61           N  
ATOM    160  CA  TRP A  29      16.470  38.203  38.580  1.00143.59           C  
ATOM    161  C   TRP A  29      17.351  39.431  38.358  1.00139.34           C  
ATOM    162  O   TRP A  29      16.851  40.532  38.127  1.00141.15           O  
ATOM    163  CB  TRP A  29      16.403  37.858  40.069  1.00157.67           C  
ATOM    164  CG  TRP A  29      15.693  38.880  40.902  1.00172.09           C  
ATOM    165  CD1 TRP A  29      15.121  40.041  40.468  1.00177.37           C  
ATOM    166  CD2 TRP A  29      15.476  38.832  42.317  1.00180.61           C  
ATOM    167  NE1 TRP A  29      14.563  40.719  41.525  1.00182.11           N  
ATOM    168  CE2 TRP A  29      14.768  39.998  42.672  1.00185.50           C  
ATOM    169  CE3 TRP A  29      15.812  37.916  43.319  1.00182.82           C  
ATOM    170  CZ2 TRP A  29      14.390  40.272  43.986  1.00190.11           C  
ATOM    171  CZ3 TRP A  29      15.436  38.189  44.623  1.00187.04           C  
ATOM    172  CH2 TRP A  29      14.733  39.357  44.945  1.00190.82           C  
ATOM    173  N   ALA A  30      18.663  39.231  38.424  1.00135.14           N  
ATOM    174  CA  ALA A  30      19.618  40.318  38.237  1.00134.49           C  
ATOM    175  C   ALA A  30      19.480  40.954  36.858  1.00140.73           C  
ATOM    176  O   ALA A  30      19.703  42.153  36.693  1.00147.67           O  
ATOM    177  CB  ALA A  30      21.037  39.817  38.451  1.00127.64           C  
ATOM    178  N   VAL A  31      19.115  40.144  35.870  1.00137.16           N  
ATOM    179  CA  VAL A  31      18.918  40.637  34.512  1.00135.57           C  
ATOM    180  C   VAL A  31      17.623  41.433  34.406  1.00143.95           C  
ATOM    181  O   VAL A  31      17.528  42.384  33.631  1.00148.35           O  
ATOM    182  CB  VAL A  31      18.896  39.484  33.489  1.00129.60           C  
ATOM    183  CG1 VAL A  31      18.471  39.992  32.119  1.00127.44           C  
ATOM    184  CG2 VAL A  31      20.259  38.814  33.416  1.00125.62           C  
ATOM    185  N   TRP A  32      16.628  41.044  35.196  1.00146.77           N  
ATOM    186  CA  TRP A  32      15.330  41.708  35.170  1.00149.38           C  
ATOM    187  C   TRP A  32      15.360  43.031  35.934  1.00152.04           C  
ATOM    188  O   TRP A  32      14.565  43.930  35.661  1.00160.99           O  
ATOM    189  CB  TRP A  32      14.243  40.788  35.730  1.00150.22           C  
ATOM    190  CG  TRP A  32      12.849  41.291  35.499  1.00148.99           C  
ATOM    191  CD1 TRP A  32      12.280  41.607  34.299  1.00143.75           C  
ATOM    192  CD2 TRP A  32      11.842  41.519  36.492  1.00154.91           C  
ATOM    193  NE1 TRP A  32      10.985  42.026  34.483  1.00146.43           N  
ATOM    194  CE2 TRP A  32      10.690  41.980  35.822  1.00154.76           C  
ATOM    195  CE3 TRP A  32      11.801  41.383  37.884  1.00160.46           C  
ATOM    196  CZ2 TRP A  32       9.513  42.305  36.493  1.00161.37           C  
ATOM    197  CZ3 TRP A  32      10.631  41.706  38.549  1.00166.24           C  
ATOM    198  CH2 TRP A  32       9.504  42.161  37.854  1.00166.03           C  
ATOM    199  N   LEU A  33      16.280  43.145  36.887  1.00148.01           N  
ATOM    200  CA  LEU A  33      16.422  44.367  37.671  1.00149.50           C  
ATOM    201  C   LEU A  33      17.323  45.376  36.970  1.00143.99           C  
ATOM    202  O   LEU A  33      16.909  46.497  36.671  1.00148.35           O  
ATOM    203  CB  LEU A  33      16.984  44.057  39.060  1.00150.21           C  
ATOM    204  CG  LEU A  33      16.138  43.182  39.984  1.00148.60           C  
ATOM    205  CD1 LEU A  33      16.831  43.006  41.326  1.00144.28           C  
ATOM    206  CD2 LEU A  33      14.751  43.776  40.167  1.00154.81           C  
ATOM    207  N   ASN A  34      18.562  44.969  36.714  1.00181.32           N  
ATOM    208  CA  ASN A  34      19.544  45.839  36.082  1.00172.33           C  
ATOM    209  C   ASN A  34      19.380  45.865  34.565  1.00168.94           C  
ATOM    210  O   ASN A  34      19.624  44.868  33.886  1.00166.01           O  
ATOM    211  CB  ASN A  34      20.959  45.399  36.463  1.00167.42           C  
ATOM    212  CG  ASN A  34      22.008  46.424  36.090  1.00168.48           C  
ATOM    213  OD1 ASN A  34      21.779  47.285  35.242  1.00170.68           O  
ATOM    214  ND2 ASN A  34      23.170  46.338  36.726  1.00168.86           N  
ATOM    215  N   SER A  35      18.965  47.012  34.039  1.00169.20           N  
ATOM    216  CA  SER A  35      18.726  47.160  32.607  1.00163.51           C  
ATOM    217  C   SER A  35      20.028  47.194  31.810  1.00155.75           C  
ATOM    218  O   SER A  35      20.017  47.107  30.582  1.00153.91           O  
ATOM    219  CB  SER A  35      17.898  48.417  32.327  1.00149.09           C  
ATOM    220  OG  SER A  35      18.520  49.569  32.867  1.00181.18           O  
ATOM    221  N   ASN A  36      21.147  47.320  32.516  1.00153.99           N  
ATOM    222  CA  ASN A  36      22.457  47.324  31.878  1.00159.55           C  
ATOM    223  C   ASN A  36      22.907  45.913  31.516  1.00164.37           C  
ATOM    224  O   ASN A  36      23.972  45.720  30.929  1.00163.68           O  
ATOM    225  CB  ASN A  36      23.492  47.995  32.784  1.00160.92           C  
ATOM    226  CG  ASN A  36      23.191  49.462  33.024  1.00160.21           C  
ATOM    227  OD1 ASN A  36      22.773  50.178  32.115  1.00161.82           O  
ATOM    228  ND2 ASN A  36      23.407  49.918  34.253  1.00153.66           N  
ATOM    229  N   LEU A  37      22.083  44.933  31.872  1.00167.11           N  
ATOM    230  CA  LEU A  37      22.368  43.532  31.585  1.00164.57           C  
ATOM    231  C   LEU A  37      21.331  42.955  30.630  1.00158.68           C  
ATOM    232  O   LEU A  37      21.331  41.757  30.353  1.00158.60           O  
ATOM    233  CB  LEU A  37      22.385  42.716  32.879  1.00165.93           C  
ATOM    234  CG  LEU A  37      23.485  43.042  33.889  1.00169.31           C  
ATOM    235  CD1 LEU A  37      23.225  42.349  35.217  1.00146.66           C  
ATOM    236  CD2 LEU A  37      24.848  42.660  33.334  1.00148.76           C  
ATOM    237  N   GLN A  38      20.447  43.812  30.130  1.00156.72           N  
ATOM    238  CA  GLN A  38      19.356  43.367  29.270  1.00156.42           C  
ATOM    239  C   GLN A  38      19.699  43.467  27.786  1.00158.09           C  
ATOM    240  O   GLN A  38      18.815  43.638  26.948  1.00159.46           O  
ATOM    241  CB  GLN A  38      18.082  44.159  29.568  1.00155.23           C  
ATOM    242  CG  GLN A  38      17.576  44.005  30.991  1.00156.72           C  
ATOM    243  CD  GLN A  38      16.286  44.760  31.235  1.00162.64           C  
ATOM    244  OE1 GLN A  38      15.778  45.447  30.348  1.00163.74           O  
ATOM    245  NE2 GLN A  38      15.748  44.637  32.442  1.00165.98           N  
ATOM    246  N   ASN A  39      20.984  43.359  27.465  1.00159.44           N  
ATOM    247  CA  ASN A  39      21.418  43.380  26.073  1.00165.64           C  
ATOM    248  C   ASN A  39      20.996  42.114  25.331  1.00171.04           C  
ATOM    249  O   ASN A  39      20.624  41.117  25.950  1.00169.06           O  
ATOM    250  CB  ASN A  39      22.932  43.589  25.979  1.00168.41           C  
ATOM    251  CG  ASN A  39      23.711  42.606  26.829  1.00170.80           C  
ATOM    252  OD1 ASN A  39      23.290  41.466  27.023  1.00175.58           O  
ATOM    253  ND2 ASN A  39      24.857  43.041  27.337  1.00170.80           N  
ATOM    254  N   VAL A  40      21.049  42.161  24.004  1.00177.20           N  
ATOM    255  CA  VAL A  40      20.623  41.034  23.180  1.00177.73           C  
ATOM    256  C   VAL A  40      21.408  39.768  23.510  1.00177.83           C  
ATOM    257  O   VAL A  40      20.873  38.661  23.448  1.00175.61           O  
ATOM    258  CB  VAL A  40      20.769  41.345  21.678  1.00181.43           C  
ATOM    259  CG1 VAL A  40      20.245  40.188  20.843  1.00174.67           C  
ATOM    260  CG2 VAL A  40      20.033  42.631  21.331  1.00188.76           C  
ATOM    261  N   THR A  41      22.676  39.940  23.867  1.00131.02           N  
ATOM    262  CA  THR A  41      23.546  38.817  24.198  1.00137.79           C  
ATOM    263  C   THR A  41      22.999  38.000  25.362  1.00134.44           C  
ATOM    264  O   THR A  41      22.996  36.771  25.321  1.00139.96           O  
ATOM    265  CB  THR A  41      24.965  39.294  24.563  1.00146.70           C  
ATOM    266  OG1 THR A  41      25.508  40.064  23.483  1.00153.98           O  
ATOM    267  CG2 THR A  41      25.873  38.105  24.847  1.00146.67           C  
ATOM    268  N   ASN A  42      22.536  38.689  26.400  1.00127.65           N  
ATOM    269  CA  ASN A  42      22.072  38.021  27.611  1.00128.31           C  
ATOM    270  C   ASN A  42      20.690  37.386  27.481  1.00133.31           C  
ATOM    271  O   ASN A  42      20.223  36.713  28.400  1.00131.64           O  
ATOM    272  CB  ASN A  42      22.119  38.973  28.808  1.00128.06           C  
ATOM    273  CG  ASN A  42      23.537  39.300  29.232  1.00132.67           C  
ATOM    274  OD1 ASN A  42      24.501  38.842  28.619  1.00137.49           O  
ATOM    275  ND2 ASN A  42      23.672  40.095  30.287  1.00132.20           N  
ATOM    276  N   TYR A  43      20.038  37.599  26.343  1.00138.66           N  
ATOM    277  CA  TYR A  43      18.786  36.910  26.059  1.00137.22           C  
ATOM    278  C   TYR A  43      19.036  35.409  26.008  1.00127.76           C  
ATOM    279  O   TYR A  43      18.210  34.614  26.457  1.00127.15           O  
ATOM    280  CB  TYR A  43      18.180  37.393  24.741  1.00145.07           C  
ATOM    281  CG  TYR A  43      17.384  38.671  24.867  1.00148.84           C  
ATOM    282  CD1 TYR A  43      15.997  38.643  24.935  1.00150.62           C  
ATOM    283  CD2 TYR A  43      18.017  39.904  24.924  1.00145.89           C  
ATOM    284  CE1 TYR A  43      15.264  39.809  25.051  1.00149.66           C  
ATOM    285  CE2 TYR A  43      17.293  41.075  25.041  1.00146.28           C  
ATOM    286  CZ  TYR A  43      15.917  41.022  25.104  1.00148.59           C  
ATOM    287  OH  TYR A  43      15.190  42.184  25.221  1.00150.30           O  
ATOM    288  N   PHE A  44      20.188  35.031  25.464  1.00122.06           N  
ATOM    289  CA  PHE A  44      20.579  33.630  25.389  1.00119.77           C  
ATOM    290  C   PHE A  44      21.023  33.118  26.755  1.00122.00           C  
ATOM    291  O   PHE A  44      20.748  31.975  27.116  1.00127.11           O  
ATOM    292  CB  PHE A  44      21.696  33.437  24.362  1.00119.70           C  
ATOM    293  CG  PHE A  44      21.316  33.851  22.968  1.00128.47           C  
ATOM    294  CD1 PHE A  44      21.864  34.985  22.394  1.00133.79           C  
ATOM    295  CD2 PHE A  44      20.404  33.109  22.236  1.00132.96           C  
ATOM    296  CE1 PHE A  44      21.516  35.369  21.112  1.00136.33           C  
ATOM    297  CE2 PHE A  44      20.050  33.488  20.954  1.00137.58           C  
ATOM    298  CZ  PHE A  44      20.608  34.620  20.392  1.00138.69           C  
ATOM    299  N   VAL A  45      21.707  33.971  27.512  1.00119.27           N  
ATOM    300  CA  VAL A  45      22.144  33.615  28.857  1.00118.00           C  
ATOM    301  C   VAL A  45      20.948  33.247  29.727  1.00117.06           C  
ATOM    302  O   VAL A  45      21.040  32.375  30.591  1.00120.58           O  
ATOM    303  CB  VAL A  45      22.932  34.759  29.522  1.00114.34           C  
ATOM    304  CG1 VAL A  45      23.267  34.409  30.965  1.00108.27           C  
ATOM    305  CG2 VAL A  45      24.196  35.059  28.733  1.00112.51           C  
ATOM    306  N   VAL A  46      19.824  33.915  29.492  1.00115.54           N  
ATOM    307  CA  VAL A  46      18.590  33.602  30.201  1.00117.06           C  
ATOM    308  C   VAL A  46      18.095  32.213  29.809  1.00125.24           C  
ATOM    309  O   VAL A  46      17.664  31.434  30.659  1.00126.17           O  
ATOM    310  CB  VAL A  46      17.490  34.639  29.911  1.00110.84           C  
ATOM    311  CG1 VAL A  46      16.184  34.227  30.574  1.00109.17           C  
ATOM    312  CG2 VAL A  46      17.923  36.016  30.387  1.00106.92           C  
ATOM    313  N   SER A  47      18.161  31.908  28.516  1.00126.76           N  
ATOM    314  CA  SER A  47      17.787  30.590  28.022  1.00127.68           C  
ATOM    315  C   SER A  47      18.655  29.529  28.687  1.00137.87           C  
ATOM    316  O   SER A  47      18.183  28.442  29.018  1.00143.24           O  
ATOM    317  CB  SER A  47      17.937  30.521  26.502  1.00125.72           C  
ATOM    318  OG  SER A  47      17.581  29.240  26.011  1.00130.31           O  
ATOM    319  N   LEU A  48      19.928  29.858  28.879  1.00140.66           N  
ATOM    320  CA  LEU A  48      20.852  28.980  29.585  1.00142.31           C  
ATOM    321  C   LEU A  48      20.417  28.817  31.035  1.00138.95           C  
ATOM    322  O   LEU A  48      20.463  27.718  31.587  1.00142.49           O  
ATOM    323  CB  LEU A  48      22.274  29.542  29.530  1.00145.61           C  
ATOM    324  CG  LEU A  48      23.316  28.812  30.381  1.00149.75           C  
ATOM    325  CD1 LEU A  48      23.463  27.367  29.925  1.00151.89           C  
ATOM    326  CD2 LEU A  48      24.654  29.533  30.333  1.00151.52           C  
ATOM    327  N   ALA A  49      19.996  29.919  31.644  1.00133.62           N  
ATOM    328  CA  ALA A  49      19.538  29.902  33.027  1.00133.15           C  
ATOM    329  C   ALA A  49      18.302  29.023  33.184  1.00134.37           C  
ATOM    330  O   ALA A  49      18.314  28.057  33.943  1.00139.04           O  
ATOM    331  CB  ALA A  49      19.255  31.313  33.511  1.00134.18           C  
ATOM    332  N   ALA A  50      17.239  29.363  32.461  1.00131.50           N  
ATOM    333  CA  ALA A  50      15.998  28.596  32.509  1.00130.98           C  
ATOM    334  C   ALA A  50      16.269  27.109  32.314  1.00131.50           C  
ATOM    335  O   ALA A  50      15.753  26.270  33.053  1.00128.87           O  
ATOM    336  CB  ALA A  50      15.022  29.099  31.458  1.00130.63           C  
ATOM    337  N   ALA A  51      17.087  26.791  31.316  1.00129.72           N  
ATOM    338  CA  ALA A  51      17.458  25.410  31.040  1.00122.83           C  
ATOM    339  C   ALA A  51      18.167  24.790  32.238  1.00123.23           C  
ATOM    340  O   ALA A  51      17.826  23.692  32.671  1.00129.00           O  
ATOM    341  CB  ALA A  51      18.340  25.335  29.802  1.00117.61           C  
ATOM    342  N   ASP A  52      19.150  25.505  32.775  1.00121.94           N  
ATOM    343  CA  ASP A  52      19.938  25.003  33.896  1.00125.75           C  
ATOM    344  C   ASP A  52      19.198  25.100  35.230  1.00117.59           C  
ATOM    345  O   ASP A  52      19.688  24.623  36.254  1.00117.79           O  
ATOM    346  CB  ASP A  52      21.285  25.727  33.978  1.00133.62           C  
ATOM    347  CG  ASP A  52      22.229  25.333  32.855  1.00141.01           C  
ATOM    348  OD1 ASP A  52      21.798  24.593  31.945  1.00146.58           O  
ATOM    349  OD2 ASP A  52      23.402  25.763  32.882  1.00139.32           O  
ATOM    350  N   ILE A  53      18.023  25.721  35.217  1.00113.47           N  
ATOM    351  CA  ILE A  53      17.177  25.762  36.404  1.00116.07           C  
ATOM    352  C   ILE A  53      16.328  24.501  36.461  1.00117.68           C  
ATOM    353  O   ILE A  53      16.186  23.880  37.515  1.00119.78           O  
ATOM    354  CB  ILE A  53      16.250  26.992  36.414  1.00118.42           C  
ATOM    355  CG1 ILE A  53      17.061  28.272  36.607  1.00107.23           C  
ATOM    356  CG2 ILE A  53      15.214  26.869  37.520  1.00120.29           C  
ATOM    357  CD1 ILE A  53      16.225  29.531  36.591  1.00 94.97           C  
ATOM    358  N   LEU A  54      15.771  24.126  35.314  1.00119.63           N  
ATOM    359  CA  LEU A  54      14.945  22.931  35.212  1.00119.41           C  
ATOM    360  C   LEU A  54      15.745  21.671  35.523  1.00111.56           C  
ATOM    361  O   LEU A  54      15.175  20.603  35.731  1.00103.78           O  
ATOM    362  CB  LEU A  54      14.318  22.829  33.821  1.00119.22           C  
ATOM    363  CG  LEU A  54      13.345  23.947  33.449  1.00107.78           C  
ATOM    364  CD1 LEU A  54      12.836  23.766  32.028  1.00108.39           C  
ATOM    365  CD2 LEU A  54      12.189  23.996  34.437  1.00 97.34           C  
ATOM    366  N   VAL A  55      17.067  21.799  35.546  1.00109.38           N  
ATOM    367  CA  VAL A  55      17.923  20.691  35.942  1.00111.53           C  
ATOM    368  C   VAL A  55      17.713  20.388  37.421  1.00118.78           C  
ATOM    369  O   VAL A  55      17.413  19.255  37.794  1.00130.34           O  
ATOM    370  CB  VAL A  55      19.412  20.988  35.681  1.00107.74           C  
ATOM    371  CG1 VAL A  55      20.287  19.923  36.324  1.00103.81           C  
ATOM    372  CG2 VAL A  55      19.682  21.075  34.186  1.00105.60           C  
ATOM    373  N   GLY A  56      17.860  21.408  38.259  1.00115.33           N  
ATOM    374  CA  GLY A  56      17.653  21.252  39.687  1.00116.27           C  
ATOM    375  C   GLY A  56      16.182  21.164  40.046  1.00119.85           C  
ATOM    376  O   GLY A  56      15.827  20.872  41.189  1.00117.10           O  
ATOM    377  N   VAL A  57      15.324  21.414  39.063  1.00126.63           N  
ATOM    378  CA  VAL A  57      13.882  21.401  39.278  1.00122.94           C  
ATOM    379  C   VAL A  57      13.246  20.089  38.823  1.00124.03           C  
ATOM    380  O   VAL A  57      12.329  19.577  39.467  1.00125.55           O  
ATOM    381  CB  VAL A  57      13.197  22.581  38.555  1.00113.86           C  
ATOM    382  CG1 VAL A  57      11.685  22.438  38.609  1.00111.35           C  
ATOM    383  CG2 VAL A  57      13.634  23.902  39.165  1.00106.84           C  
ATOM    384  N   LEU A  58      13.741  19.543  37.716  1.00117.11           N  
ATOM    385  CA  LEU A  58      13.167  18.331  37.144  1.00107.86           C  
ATOM    386  C   LEU A  58      14.221  17.274  36.826  1.00104.68           C  
ATOM    387  O   LEU A  58      14.112  16.132  37.267  1.00112.34           O  
ATOM    388  CB  LEU A  58      12.365  18.663  35.884  1.00104.84           C  
ATOM    389  CG  LEU A  58      11.180  19.613  36.070  1.00102.99           C  
ATOM    390  CD1 LEU A  58      10.484  19.867  34.743  1.00102.25           C  
ATOM    391  CD2 LEU A  58      10.204  19.055  37.092  1.00101.08           C  
ATOM    392  N   ALA A  59      15.238  17.659  36.062  1.00102.20           N  
ATOM    393  CA  ALA A  59      16.272  16.723  35.626  1.00107.73           C  
ATOM    394  C   ALA A  59      16.896  15.945  36.783  1.00116.08           C  
ATOM    395  O   ALA A  59      16.971  14.719  36.741  1.00123.44           O  
ATOM    396  CB  ALA A  59      17.346  17.446  34.831  1.00106.23           C  
ATOM    397  N   ILE A  60      17.349  16.659  37.809  1.00117.20           N  
ATOM    398  CA  ILE A  60      17.940  16.014  38.978  1.00118.25           C  
ATOM    399  C   ILE A  60      16.918  15.163  39.731  1.00118.45           C  
ATOM    400  O   ILE A  60      17.196  14.011  40.058  1.00125.78           O  
ATOM    401  CB  ILE A  60      18.595  17.028  39.937  1.00118.31           C  
ATOM    402  CG1 ILE A  60      19.783  17.712  39.259  1.00119.23           C  
ATOM    403  CG2 ILE A  60      19.042  16.339  41.217  1.00114.06           C  
ATOM    404  CD1 ILE A  60      20.514  18.693  40.151  1.00118.37           C  
ATOM    405  N   PRO A  61      15.731  15.728  40.012  1.00114.32           N  
ATOM    406  CA  PRO A  61      14.672  14.925  40.633  1.00114.41           C  
ATOM    407  C   PRO A  61      14.401  13.637  39.856  1.00108.39           C  
ATOM    408  O   PRO A  61      14.256  12.576  40.463  1.00 98.67           O  
ATOM    409  CB  PRO A  61      13.456  15.850  40.568  1.00111.15           C  
ATOM    410  CG  PRO A  61      14.036  17.217  40.613  1.00106.24           C  
ATOM    411  CD  PRO A  61      15.337  17.141  39.865  1.00105.88           C  
ATOM    412  N   PHE A  62      14.338  13.735  38.532  1.00113.93           N  
ATOM    413  CA  PHE A  62      14.123  12.566  37.687  1.00120.73           C  
ATOM    414  C   PHE A  62      15.310  11.612  37.750  1.00132.95           C  
ATOM    415  O   PHE A  62      15.136  10.396  37.819  1.00140.32           O  
ATOM    416  CB  PHE A  62      13.872  12.981  36.235  1.00115.65           C  
ATOM    417  CG  PHE A  62      12.560  13.679  36.019  1.00112.26           C  
ATOM    418  CD1 PHE A  62      11.403  13.212  36.618  1.00115.46           C  
ATOM    419  CD2 PHE A  62      12.479  14.791  35.200  1.00106.42           C  
ATOM    420  CE1 PHE A  62      10.192  13.850  36.416  1.00112.51           C  
ATOM    421  CE2 PHE A  62      11.271  15.431  34.995  1.00105.67           C  
ATOM    422  CZ  PHE A  62      10.127  14.960  35.603  1.00108.38           C  
ATOM    423  N   ALA A  63      16.515  12.173  37.722  1.00132.93           N  
ATOM    424  CA  ALA A  63      17.738  11.377  37.743  1.00133.71           C  
ATOM    425  C   ALA A  63      17.837  10.526  39.006  1.00140.95           C  
ATOM    426  O   ALA A  63      18.241   9.365  38.953  1.00144.25           O  
ATOM    427  CB  ALA A  63      18.959  12.275  37.607  1.00125.79           C  
ATOM    428  N   ILE A  64      17.470  11.112  40.141  1.00144.20           N  
ATOM    429  CA  ILE A  64      17.511  10.404  41.414  1.00148.57           C  
ATOM    430  C   ILE A  64      16.439   9.323  41.459  1.00152.17           C  
ATOM    431  O   ILE A  64      16.599   8.303  42.130  1.00157.74           O  
ATOM    432  CB  ILE A  64      17.311  11.366  42.599  1.00154.37           C  
ATOM    433  CG1 ILE A  64      18.283  12.542  42.500  1.00165.88           C  
ATOM    434  CG2 ILE A  64      17.488  10.629  43.919  1.00150.89           C  
ATOM    435  CD1 ILE A  64      18.006  13.650  43.495  1.00169.93           C  
ATOM    436  N   THR A  65      15.345   9.551  40.740  1.00152.15           N  
ATOM    437  CA  THR A  65      14.252   8.589  40.682  1.00157.03           C  
ATOM    438  C   THR A  65      14.609   7.413  39.782  1.00166.15           C  
ATOM    439  O   THR A  65      14.456   6.253  40.165  1.00168.01           O  
ATOM    440  CB  THR A  65      12.958   9.238  40.153  1.00154.30           C  
ATOM    441  OG1 THR A  65      12.577  10.320  41.012  1.00153.32           O  
ATOM    442  CG2 THR A  65      11.833   8.216  40.101  1.00156.93           C  
ATOM    443  N   ILE A  66      15.090   7.724  38.583  1.00169.14           N  
ATOM    444  CA  ILE A  66      15.417   6.705  37.594  1.00173.95           C  
ATOM    445  C   ILE A  66      16.629   5.873  38.013  1.00181.45           C  
ATOM    446  O   ILE A  66      16.836   4.767  37.512  1.00186.42           O  
ATOM    447  CB  ILE A  66      15.677   7.336  36.210  1.00170.20           C  
ATOM    448  CG1 ILE A  66      15.675   6.265  35.118  1.00169.64           C  
ATOM    449  CG2 ILE A  66      16.985   8.113  36.212  1.00170.94           C  
ATOM    450  CD1 ILE A  66      15.878   6.819  33.726  1.00167.09           C  
ATOM    451  N   SER A  67      17.425   6.409  38.933  1.00183.68           N  
ATOM    452  CA  SER A  67      18.613   5.711  39.412  1.00185.75           C  
ATOM    453  C   SER A  67      18.227   4.408  40.099  1.00177.43           C  
ATOM    454  O   SER A  67      18.903   3.392  39.948  1.00179.15           O  
ATOM    455  CB  SER A  67      19.405   6.589  40.382  1.00191.92           C  
ATOM    456  OG  SER A  67      18.775   6.640  41.650  1.00194.16           O  
ATOM    457  N   THR A  68      17.136   4.449  40.857  1.00167.10           N  
ATOM    458  CA  THR A  68      16.642   3.270  41.557  1.00167.90           C  
ATOM    459  C   THR A  68      15.707   2.461  40.662  1.00170.07           C  
ATOM    460  O   THR A  68      15.502   1.267  40.880  1.00175.05           O  
ATOM    461  CB  THR A  68      15.905   3.652  42.855  1.00159.45           C  
ATOM    462  OG1 THR A  68      14.793   4.500  42.544  1.00153.06           O  
ATOM    463  CG2 THR A  68      16.843   4.381  43.805  1.00154.15           C  
ATOM    464  N   GLY A  69      15.145   3.121  39.654  1.00210.86           N  
ATOM    465  CA  GLY A  69      14.250   2.470  38.716  1.00198.92           C  
ATOM    466  C   GLY A  69      12.835   2.348  39.245  1.00184.22           C  
ATOM    467  O   GLY A  69      12.622   2.090  40.429  1.00179.85           O  
ATOM    468  N   PHE A  70      11.862   2.539  38.361  1.00175.13           N  
ATOM    469  CA  PHE A  70      10.457   2.429  38.736  1.00168.10           C  
ATOM    470  C   PHE A  70       9.646   1.761  37.632  1.00164.21           C  
ATOM    471  O   PHE A  70      10.205   1.257  36.659  1.00164.86           O  
ATOM    472  CB  PHE A  70       9.875   3.806  39.068  1.00173.42           C  
ATOM    473  CG  PHE A  70       9.960   4.794  37.937  1.00175.16           C  
ATOM    474  CD1 PHE A  70      11.071   5.609  37.792  1.00173.68           C  
ATOM    475  CD2 PHE A  70       8.925   4.914  37.024  1.00175.28           C  
ATOM    476  CE1 PHE A  70      11.151   6.520  36.755  1.00175.76           C  
ATOM    477  CE2 PHE A  70       8.999   5.823  35.985  1.00177.12           C  
ATOM    478  CZ  PHE A  70      10.113   6.627  35.851  1.00177.90           C  
ATOM    479  N   CYS A  71       8.327   1.760  37.791  1.00164.44           N  
ATOM    480  CA  CYS A  71       7.442   1.143  36.811  1.00172.27           C  
ATOM    481  C   CYS A  71       6.469   2.156  36.220  1.00181.01           C  
ATOM    482  O   CYS A  71       5.747   2.837  36.949  1.00183.89           O  
ATOM    483  CB  CYS A  71       6.672  -0.021  37.439  1.00172.31           C  
ATOM    484  SG  CYS A  71       7.705  -1.406  37.967  1.00284.99           S  
ATOM    485  N   ALA A  72       6.455   2.248  34.895  1.00185.51           N  
ATOM    486  CA  ALA A  72       5.558   3.158  34.193  1.00186.38           C  
ATOM    487  C   ALA A  72       5.534   2.845  32.702  1.00187.70           C  
ATOM    488  O   ALA A  72       6.401   2.132  32.196  1.00189.81           O  
ATOM    489  CB  ALA A  72       5.975   4.601  34.429  1.00183.84           C  
ATOM    490  N   ALA A  73       4.539   3.384  32.003  1.00186.37           N  
ATOM    491  CA  ALA A  73       4.407   3.171  30.567  1.00186.46           C  
ATOM    492  C   ALA A  73       5.673   3.599  29.832  1.00184.62           C  
ATOM    493  O   ALA A  73       6.600   4.132  30.438  1.00177.32           O  
ATOM    494  CB  ALA A  73       3.199   3.925  30.029  1.00186.29           C  
ATOM    495  N   CYS A  74       5.708   3.365  28.524  1.00192.43           N  
ATOM    496  CA  CYS A  74       6.875   3.717  27.723  1.00202.24           C  
ATOM    497  C   CYS A  74       7.016   5.232  27.581  1.00211.62           C  
ATOM    498  O   CYS A  74       8.114   5.775  27.704  1.00213.78           O  
ATOM    499  CB  CYS A  74       6.808   3.056  26.345  1.00205.49           C  
ATOM    500  SG  CYS A  74       8.353   3.142  25.404  1.00242.49           S  
ATOM    501  N   HIS A  75       5.901   5.909  27.324  1.00217.54           N  
ATOM    502  CA  HIS A  75       5.903   7.362  27.193  1.00217.21           C  
ATOM    503  C   HIS A  75       6.372   8.041  28.477  1.00207.51           C  
ATOM    504  O   HIS A  75       7.269   8.883  28.454  1.00203.45           O  
ATOM    505  CB  HIS A  75       4.510   7.871  26.809  1.00225.68           C  
ATOM    506  CG  HIS A  75       4.124   7.573  25.393  1.00234.04           C  
ATOM    507  ND1 HIS A  75       3.624   6.351  24.998  1.00237.93           N  
ATOM    508  CD2 HIS A  75       4.157   8.343  24.279  1.00236.19           C  
ATOM    509  CE1 HIS A  75       3.371   6.379  23.701  1.00240.20           C  
ATOM    510  NE2 HIS A  75       3.686   7.577  23.242  1.00239.96           N  
ATOM    511  N   GLY A  76       5.759   7.667  29.596  1.00205.69           N  
ATOM    512  CA  GLY A  76       6.098   8.245  30.884  1.00205.31           C  
ATOM    513  C   GLY A  76       7.510   7.919  31.328  1.00211.30           C  
ATOM    514  O   GLY A  76       8.154   8.713  32.014  1.00210.90           O  
ATOM    515  N   CYS A  77       7.993   6.745  30.936  1.00159.77           N  
ATOM    516  CA  CYS A  77       9.336   6.307  31.299  1.00160.14           C  
ATOM    517  C   CYS A  77      10.389   7.010  30.450  1.00155.00           C  
ATOM    518  O   CYS A  77      11.466   7.354  30.939  1.00146.16           O  
ATOM    519  CB  CYS A  77       9.462   4.788  31.149  1.00163.54           C  
ATOM    520  SG  CYS A  77      11.045   4.094  31.685  1.00184.82           S  
ATOM    521  N   LEU A  78      10.072   7.223  29.177  1.00157.91           N  
ATOM    522  CA  LEU A  78      10.989   7.889  28.260  1.00159.66           C  
ATOM    523  C   LEU A  78      11.156   9.369  28.591  1.00162.58           C  
ATOM    524  O   LEU A  78      12.271   9.887  28.587  1.00158.61           O  
ATOM    525  CB  LEU A  78      10.522   7.728  26.812  1.00158.62           C  
ATOM    526  CG  LEU A  78      10.709   6.346  26.184  1.00157.15           C  
ATOM    527  CD1 LEU A  78      10.138   6.323  24.777  1.00164.15           C  
ATOM    528  CD2 LEU A  78      12.178   5.957  26.179  1.00151.88           C  
ATOM    529  N   PHE A  79      10.047  10.046  28.873  1.00163.56           N  
ATOM    530  CA  PHE A  79      10.091  11.466  29.201  1.00160.77           C  
ATOM    531  C   PHE A  79      11.022  11.728  30.378  1.00148.86           C  
ATOM    532  O   PHE A  79      11.901  12.586  30.306  1.00152.31           O  
ATOM    533  CB  PHE A  79       8.692  12.001  29.511  1.00171.57           C  
ATOM    534  CG  PHE A  79       8.685  13.421  30.005  1.00181.64           C  
ATOM    535  CD1 PHE A  79       8.755  14.481  29.114  1.00182.18           C  
ATOM    536  CD2 PHE A  79       8.613  13.698  31.362  1.00182.90           C  
ATOM    537  CE1 PHE A  79       8.751  15.788  29.566  1.00176.56           C  
ATOM    538  CE2 PHE A  79       8.609  15.004  31.819  1.00178.39           C  
ATOM    539  CZ  PHE A  79       8.677  16.049  30.920  1.00174.52           C  
ATOM    540  N   ILE A  80      10.823  10.983  31.459  1.00135.69           N  
ATOM    541  CA  ILE A  80      11.640  11.135  32.656  1.00127.23           C  
ATOM    542  C   ILE A  80      13.100  10.772  32.391  1.00131.24           C  
ATOM    543  O   ILE A  80      14.008  11.290  33.043  1.00128.06           O  
ATOM    544  CB  ILE A  80      11.091  10.281  33.819  1.00113.55           C  
ATOM    545  CG1 ILE A  80       9.722  10.805  34.257  1.00109.51           C  
ATOM    546  CG2 ILE A  80      12.058  10.276  34.992  1.00101.92           C  
ATOM    547  CD1 ILE A  80       9.158  10.103  35.472  1.00105.71           C  
ATOM    548  N   ALA A  81      13.321   9.892  31.420  1.00139.52           N  
ATOM    549  CA  ALA A  81      14.666   9.422  31.104  1.00144.90           C  
ATOM    550  C   ALA A  81      15.355  10.281  30.045  1.00147.08           C  
ATOM    551  O   ALA A  81      16.583  10.333  29.981  1.00143.95           O  
ATOM    552  CB  ALA A  81      14.626   7.966  30.659  1.00149.59           C  
ATOM    553  N   CYS A  82      14.562  10.954  29.219  1.00152.20           N  
ATOM    554  CA  CYS A  82      15.104  11.736  28.112  1.00156.57           C  
ATOM    555  C   CYS A  82      14.923  13.237  28.316  1.00155.21           C  
ATOM    556  O   CYS A  82      15.285  14.033  27.450  1.00151.97           O  
ATOM    557  CB  CYS A  82      14.459  11.309  26.792  1.00160.02           C  
ATOM    558  SG  CYS A  82      14.650   9.556  26.394  1.00182.87           S  
ATOM    559  N   PHE A  83      14.362  13.620  29.458  1.00156.74           N  
ATOM    560  CA  PHE A  83      14.137  15.031  29.752  1.00162.51           C  
ATOM    561  C   PHE A  83      15.456  15.774  29.932  1.00160.81           C  
ATOM    562  O   PHE A  83      15.560  16.960  29.618  1.00160.86           O  
ATOM    563  CB  PHE A  83      13.266  15.198  30.998  1.00164.43           C  
ATOM    564  CG  PHE A  83      12.998  16.632  31.359  1.00166.42           C  
ATOM    565  CD1 PHE A  83      11.970  17.333  30.751  1.00164.18           C  
ATOM    566  CD2 PHE A  83      13.778  17.281  32.303  1.00162.63           C  
ATOM    567  CE1 PHE A  83      11.723  18.651  31.080  1.00157.49           C  
ATOM    568  CE2 PHE A  83      13.535  18.599  32.635  1.00154.73           C  
ATOM    569  CZ  PHE A  83      12.507  19.285  32.023  1.00152.91           C  
ATOM    570  N   VAL A  84      16.460  15.068  30.442  1.00154.12           N  
ATOM    571  CA  VAL A  84      17.780  15.652  30.640  1.00145.75           C  
ATOM    572  C   VAL A  84      18.456  15.898  29.295  1.00140.82           C  
ATOM    573  O   VAL A  84      19.322  16.763  29.173  1.00134.29           O  
ATOM    574  CB  VAL A  84      18.671  14.748  31.513  1.00143.12           C  
ATOM    575  CG1 VAL A  84      18.885  13.399  30.840  1.00145.03           C  
ATOM    576  CG2 VAL A  84      20.002  15.428  31.804  1.00138.43           C  
ATOM    577  N   LEU A  85      18.049  15.136  28.285  1.00143.60           N  
ATOM    578  CA  LEU A  85      18.588  15.296  26.940  1.00141.25           C  
ATOM    579  C   LEU A  85      18.076  16.585  26.309  1.00135.80           C  
ATOM    580  O   LEU A  85      18.683  17.116  25.381  1.00132.55           O  
ATOM    581  CB  LEU A  85      18.221  14.095  26.065  1.00145.02           C  
ATOM    582  CG  LEU A  85      18.702  12.724  26.544  1.00138.05           C  
ATOM    583  CD1 LEU A  85      18.248  11.633  25.587  1.00139.82           C  
ATOM    584  CD2 LEU A  85      20.215  12.705  26.703  1.00130.10           C  
ATOM    585  N   VAL A  86      16.953  17.081  26.821  1.00136.37           N  
ATOM    586  CA  VAL A  86      16.370  18.330  26.344  1.00137.29           C  
ATOM    587  C   VAL A  86      17.117  19.533  26.913  1.00134.86           C  
ATOM    588  O   VAL A  86      17.494  20.447  26.179  1.00132.70           O  
ATOM    589  CB  VAL A  86      14.879  18.439  26.723  1.00134.81           C  
ATOM    590  CG1 VAL A  86      14.326  19.799  26.324  1.00141.75           C  
ATOM    591  CG2 VAL A  86      14.081  17.321  26.070  1.00132.84           C  
ATOM    592  N   LEU A  87      17.329  19.524  28.226  1.00130.00           N  
ATOM    593  CA  LEU A  87      18.039  20.605  28.897  1.00118.54           C  
ATOM    594  C   LEU A  87      19.491  20.684  28.437  1.00114.59           C  
ATOM    595  O   LEU A  87      20.067  21.768  28.354  1.00119.81           O  
ATOM    596  CB  LEU A  87      17.977  20.430  30.416  1.00109.93           C  
ATOM    597  CG  LEU A  87      16.584  20.365  31.044  1.00110.18           C  
ATOM    598  CD1 LEU A  87      16.686  20.271  32.557  1.00105.54           C  
ATOM    599  CD2 LEU A  87      15.750  21.569  30.638  1.00110.87           C  
ATOM    600  N   ALA A  88      20.078  19.531  28.139  1.00112.74           N  
ATOM    601  CA  ALA A  88      21.467  19.473  27.700  1.00116.50           C  
ATOM    602  C   ALA A  88      21.611  19.909  26.245  1.00119.02           C  
ATOM    603  O   ALA A  88      22.664  20.397  25.836  1.00108.04           O  
ATOM    604  CB  ALA A  88      22.027  18.072  27.894  1.00121.21           C  
ATOM    605  N   GLN A  89      20.548  19.730  25.468  1.00131.32           N  
ATOM    606  CA  GLN A  89      20.556  20.118  24.062  1.00143.02           C  
ATOM    607  C   GLN A  89      20.273  21.608  23.911  1.00143.39           C  
ATOM    608  O   GLN A  89      20.839  22.272  23.042  1.00145.76           O  
ATOM    609  CB  GLN A  89      19.535  19.298  23.270  1.00153.36           C  
ATOM    610  CG  GLN A  89      19.504  19.606  21.778  1.00161.12           C  
ATOM    611  CD  GLN A  89      20.795  19.232  21.070  1.00162.17           C  
ATOM    612  OE1 GLN A  89      21.686  18.620  21.658  1.00161.94           O  
ATOM    613  NE2 GLN A  89      20.899  19.597  19.797  1.00162.32           N  
ATOM    614  N   SER A  90      19.395  22.129  24.762  1.00142.66           N  
ATOM    615  CA  SER A  90      19.082  23.553  24.756  1.00143.65           C  
ATOM    616  C   SER A  90      20.315  24.371  25.122  1.00134.82           C  
ATOM    617  O   SER A  90      20.516  25.473  24.612  1.00127.04           O  
ATOM    618  CB  SER A  90      17.940  23.860  25.728  1.00142.59           C  
ATOM    619  OG  SER A  90      17.605  25.237  25.705  1.00139.11           O  
ATOM    620  N   SER A  91      21.139  23.822  26.009  1.00130.67           N  
ATOM    621  CA  SER A  91      22.380  24.474  26.405  1.00121.58           C  
ATOM    622  C   SER A  91      23.353  24.529  25.234  1.00119.56           C  
ATOM    623  O   SER A  91      24.123  25.478  25.101  1.00115.34           O  
ATOM    624  CB  SER A  91      23.019  23.745  27.589  1.00116.39           C  
ATOM    625  OG  SER A  91      22.197  23.823  28.741  1.00113.78           O  
ATOM    626  N   ILE A  92      23.311  23.505  24.388  1.00127.20           N  
ATOM    627  CA  ILE A  92      24.166  23.452  23.208  1.00132.00           C  
ATOM    628  C   ILE A  92      23.884  24.622  22.271  1.00130.67           C  
ATOM    629  O   ILE A  92      24.805  25.306  21.824  1.00127.68           O  
ATOM    630  CB  ILE A  92      23.986  22.130  22.439  1.00136.05           C  
ATOM    631  CG1 ILE A  92      24.597  20.971  23.229  1.00124.92           C  
ATOM    632  CG2 ILE A  92      24.630  22.222  21.067  1.00144.02           C  
ATOM    633  CD1 ILE A  92      26.097  21.069  23.391  1.00120.21           C  
ATOM    634  N   PHE A  93      22.607  24.848  21.981  1.00133.88           N  
ATOM    635  CA  PHE A  93      22.203  25.947  21.111  1.00142.81           C  
ATOM    636  C   PHE A  93      22.534  27.300  21.735  1.00142.98           C  
ATOM    637  O   PHE A  93      23.042  28.196  21.061  1.00140.87           O  
ATOM    638  CB  PHE A  93      20.709  25.867  20.798  1.00147.56           C  
ATOM    639  CG  PHE A  93      20.313  24.636  20.033  1.00150.56           C  
ATOM    640  CD1 PHE A  93      20.613  24.514  18.687  1.00151.39           C  
ATOM    641  CD2 PHE A  93      19.629  23.607  20.657  1.00150.20           C  
ATOM    642  CE1 PHE A  93      20.247  23.386  17.979  1.00151.40           C  
ATOM    643  CE2 PHE A  93      19.260  22.477  19.954  1.00152.03           C  
ATOM    644  CZ  PHE A  93      19.569  22.367  18.613  1.00153.80           C  
ATOM    645  N   SER A  94      22.238  27.440  23.024  1.00140.78           N  
ATOM    646  CA  SER A  94      22.527  28.672  23.747  1.00130.83           C  
ATOM    647  C   SER A  94      24.020  28.982  23.724  1.00127.91           C  
ATOM    648  O   SER A  94      24.424  30.108  23.434  1.00126.84           O  
ATOM    649  CB  SER A  94      22.033  28.577  25.193  1.00123.80           C  
ATOM    650  OG  SER A  94      20.629  28.403  25.244  1.00126.42           O  
ATOM    651  N   LEU A  95      24.834  27.976  24.029  1.00128.81           N  
ATOM    652  CA  LEU A  95      26.283  28.142  24.047  1.00125.48           C  
ATOM    653  C   LEU A  95      26.832  28.429  22.653  1.00124.70           C  
ATOM    654  O   LEU A  95      27.828  29.138  22.502  1.00120.36           O  
ATOM    655  CB  LEU A  95      26.963  26.902  24.634  1.00120.16           C  
ATOM    656  CG  LEU A  95      26.741  26.613  26.121  1.00116.10           C  
ATOM    657  CD1 LEU A  95      27.482  25.351  26.527  1.00117.91           C  
ATOM    658  CD2 LEU A  95      27.182  27.791  26.974  1.00115.45           C  
ATOM    659  N   LEU A  96      26.178  27.874  21.637  1.00127.11           N  
ATOM    660  CA  LEU A  96      26.595  28.086  20.256  1.00131.44           C  
ATOM    661  C   LEU A  96      26.214  29.483  19.778  1.00129.57           C  
ATOM    662  O   LEU A  96      26.994  30.149  19.101  1.00129.88           O  
ATOM    663  CB  LEU A  96      25.979  27.029  19.339  1.00139.95           C  
ATOM    664  CG  LEU A  96      26.309  27.153  17.850  1.00145.48           C  
ATOM    665  CD1 LEU A  96      27.814  27.180  17.629  1.00142.32           C  
ATOM    666  CD2 LEU A  96      25.667  26.024  17.058  1.00149.42           C  
ATOM    667  N   ALA A  97      25.009  29.918  20.135  1.00127.22           N  
ATOM    668  CA  ALA A  97      24.531  31.247  19.770  1.00125.23           C  
ATOM    669  C   ALA A  97      25.412  32.329  20.388  1.00119.99           C  
ATOM    670  O   ALA A  97      25.830  33.263  19.706  1.00112.21           O  
ATOM    671  CB  ALA A  97      23.085  31.429  20.196  1.00120.78           C  
ATOM    672  N   ILE A  98      25.687  32.196  21.682  1.00119.93           N  
ATOM    673  CA  ILE A  98      26.560  33.132  22.380  1.00119.34           C  
ATOM    674  C   ILE A  98      27.923  33.217  21.699  1.00123.18           C  
ATOM    675  O   ILE A  98      28.500  34.297  21.579  1.00123.81           O  
ATOM    676  CB  ILE A  98      26.754  32.734  23.855  1.00116.62           C  
ATOM    677  CG1 ILE A  98      25.429  32.833  24.613  1.00112.32           C  
ATOM    678  CG2 ILE A  98      27.805  33.615  24.512  1.00120.67           C  
ATOM    679  CD1 ILE A  98      25.548  32.535  26.091  1.00105.10           C  
ATOM    680  N   ALA A  99      28.432  32.073  21.256  1.00132.63           N  
ATOM    681  CA  ALA A  99      29.708  32.027  20.553  1.00143.30           C  
ATOM    682  C   ALA A  99      29.635  32.828  19.257  1.00154.27           C  
ATOM    683  O   ALA A  99      30.484  33.680  18.993  1.00154.97           O  
ATOM    684  CB  ALA A  99      30.108  30.585  20.268  1.00142.40           C  
ATOM    685  N   ILE A 100      28.613  32.548  18.454  1.00160.27           N  
ATOM    686  CA  ILE A 100      28.394  33.267  17.205  1.00162.05           C  
ATOM    687  C   ILE A 100      28.246  34.759  17.473  1.00159.24           C  
ATOM    688  O   ILE A 100      28.849  35.589  16.793  1.00158.60           O  
ATOM    689  CB  ILE A 100      27.129  32.763  16.482  1.00163.25           C  
ATOM    690  CG1 ILE A 100      27.226  31.258  16.217  1.00158.26           C  
ATOM    691  CG2 ILE A 100      26.917  33.525  15.183  1.00167.88           C  
ATOM    692  CD1 ILE A 100      25.983  30.668  15.585  1.00156.26           C  
ATOM    693  N   ASP A 101      27.438  35.087  18.476  1.00156.74           N  
ATOM    694  CA  ASP A 101      27.196  36.471  18.859  1.00153.26           C  
ATOM    695  C   ASP A 101      28.496  37.204  19.171  1.00149.70           C  
ATOM    696  O   ASP A 101      28.765  38.271  18.621  1.00152.29           O  
ATOM    697  CB  ASP A 101      26.266  36.523  20.071  1.00151.33           C  
ATOM    698  CG  ASP A 101      26.094  37.923  20.613  1.00155.87           C  
ATOM    699  OD1 ASP A 101      25.764  38.833  19.823  1.00165.83           O  
ATOM    700  OD2 ASP A 101      26.287  38.113  21.831  1.00151.56           O  
ATOM    701  N   ARG A 102      29.299  36.623  20.057  1.00145.51           N  
ATOM    702  CA  ARG A 102      30.566  37.226  20.456  1.00143.42           C  
ATOM    703  C   ARG A 102      31.536  37.340  19.285  1.00143.92           C  
ATOM    704  O   ARG A 102      32.510  38.089  19.348  1.00143.82           O  
ATOM    705  CB  ARG A 102      31.204  36.433  21.599  1.00145.08           C  
ATOM    706  CG  ARG A 102      30.434  36.487  22.911  1.00149.77           C  
ATOM    707  CD  ARG A 102      30.424  37.891  23.504  1.00154.58           C  
ATOM    708  NE  ARG A 102      29.576  38.808  22.747  1.00159.75           N  
ATOM    709  CZ  ARG A 102      29.467  40.108  23.001  1.00158.30           C  
ATOM    710  NH1 ARG A 102      30.155  40.651  23.996  1.00157.16           N  
ATOM    711  NH2 ARG A 102      28.671  40.866  22.259  1.00158.42           N  
ATOM    712  N   TYR A 103      31.269  36.591  18.221  1.00147.70           N  
ATOM    713  CA  TYR A 103      32.088  36.666  17.018  1.00150.43           C  
ATOM    714  C   TYR A 103      31.598  37.781  16.103  1.00151.17           C  
ATOM    715  O   TYR A 103      32.396  38.503  15.509  1.00148.61           O  
ATOM    716  CB  TYR A 103      32.082  35.334  16.267  1.00151.69           C  
ATOM    717  CG  TYR A 103      32.805  35.386  14.939  1.00152.89           C  
ATOM    718  CD1 TYR A 103      34.177  35.186  14.864  1.00149.98           C  
ATOM    719  CD2 TYR A 103      32.115  35.639  13.759  1.00156.79           C  
ATOM    720  CE1 TYR A 103      34.842  35.235  13.653  1.00152.73           C  
ATOM    721  CE2 TYR A 103      32.772  35.690  12.544  1.00158.89           C  
ATOM    722  CZ  TYR A 103      34.135  35.487  12.497  1.00156.28           C  
ATOM    723  OH  TYR A 103      34.793  35.536  11.289  1.00156.45           O  
ATOM    724  N   ILE A 104      30.280  37.913  15.997  1.00155.31           N  
ATOM    725  CA  ILE A 104      29.674  38.932  15.149  1.00160.72           C  
ATOM    726  C   ILE A 104      30.068  40.341  15.587  1.00156.21           C  
ATOM    727  O   ILE A 104      30.283  41.222  14.755  1.00158.30           O  
ATOM    728  CB  ILE A 104      28.137  38.811  15.141  1.00166.45           C  
ATOM    729  CG1 ILE A 104      27.717  37.436  14.616  1.00166.77           C  
ATOM    730  CG2 ILE A 104      27.516  39.924  14.307  1.00170.19           C  
ATOM    731  CD1 ILE A 104      26.223  37.197  14.645  1.00166.24           C  
ATOM    732  N   ALA A 105      30.164  40.544  16.897  1.00164.49           N  
ATOM    733  CA  ALA A 105      30.529  41.844  17.449  1.00154.36           C  
ATOM    734  C   ALA A 105      31.957  42.230  17.079  1.00158.53           C  
ATOM    735  O   ALA A 105      32.206  43.337  16.601  1.00164.95           O  
ATOM    736  CB  ALA A 105      30.353  41.845  18.960  1.00140.99           C  
ATOM    737  N   ILE A 106      32.892  41.313  17.301  1.00157.74           N  
ATOM    738  CA  ILE A 106      34.299  41.572  17.017  1.00161.58           C  
ATOM    739  C   ILE A 106      34.586  41.583  15.518  1.00175.20           C  
ATOM    740  O   ILE A 106      35.313  42.445  15.022  1.00181.52           O  
ATOM    741  CB  ILE A 106      35.213  40.543  17.710  1.00153.38           C  
ATOM    742  CG1 ILE A 106      35.036  40.618  19.228  1.00144.04           C  
ATOM    743  CG2 ILE A 106      36.666  40.777  17.331  1.00154.77           C  
ATOM    744  CD1 ILE A 106      35.947  39.689  19.995  1.00144.36           C  
ATOM    745  N   ALA A 107      34.010  40.625  14.799  1.00177.35           N  
ATOM    746  CA  ALA A 107      34.205  40.532  13.356  1.00182.38           C  
ATOM    747  C   ALA A 107      33.586  41.725  12.637  1.00187.01           C  
ATOM    748  O   ALA A 107      34.264  42.434  11.894  1.00188.95           O  
ATOM    749  CB  ALA A 107      33.625  39.230  12.823  1.00184.52           C  
ATOM    750  N   ILE A 108      32.294  41.941  12.864  1.00189.15           N  
ATOM    751  CA  ILE A 108      31.584  43.051  12.241  1.00192.99           C  
ATOM    752  C   ILE A 108      30.813  43.855  13.283  1.00190.33           C  
ATOM    753  O   ILE A 108      29.625  43.618  13.503  1.00194.11           O  
ATOM    754  CB  ILE A 108      30.601  42.558  11.163  1.00195.70           C  
ATOM    755  CG1 ILE A 108      31.256  41.487  10.288  1.00190.38           C  
ATOM    756  CG2 ILE A 108      30.110  43.725  10.319  1.00201.16           C  
ATOM    757  CD1 ILE A 108      30.342  40.929   9.221  1.00189.51           C  
ATOM    758  N   PRO A 109      31.492  44.815  13.929  1.00183.15           N  
ATOM    759  CA  PRO A 109      30.894  45.639  14.986  1.00183.89           C  
ATOM    760  C   PRO A 109      29.757  46.514  14.468  1.00192.27           C  
ATOM    761  O   PRO A 109      28.813  46.795  15.207  1.00193.04           O  
ATOM    762  CB  PRO A 109      32.063  46.514  15.451  1.00178.53           C  
ATOM    763  CG  PRO A 109      33.020  46.516  14.306  1.00178.04           C  
ATOM    764  CD  PRO A 109      32.904  45.160  13.692  1.00178.16           C  
ATOM    765  N   LEU A 110      29.848  46.935  13.210  1.00197.94           N  
ATOM    766  CA  LEU A 110      28.842  47.812  12.623  1.00203.01           C  
ATOM    767  C   LEU A 110      27.529  47.081  12.354  1.00205.85           C  
ATOM    768  O   LEU A 110      26.472  47.489  12.834  1.00203.78           O  
ATOM    769  CB  LEU A 110      29.370  48.447  11.334  1.00206.72           C  
ATOM    770  CG  LEU A 110      30.571  49.382  11.490  1.00204.34           C  
ATOM    771  CD1 LEU A 110      31.053  49.873  10.133  1.00206.74           C  
ATOM    772  CD2 LEU A 110      30.227  50.554  12.398  1.00201.24           C  
ATOM    773  N   ARG A 111      27.603  45.999  11.586  1.00209.64           N  
ATOM    774  CA  ARG A 111      26.415  45.221  11.252  1.00211.31           C  
ATOM    775  C   ARG A 111      25.892  44.447  12.458  1.00204.65           C  
ATOM    776  O   ARG A 111      24.811  43.859  12.405  1.00204.24           O  
ATOM    777  CB  ARG A 111      26.709  44.260  10.098  1.00217.35           C  
ATOM    778  CG  ARG A 111      27.043  44.946   8.784  1.00223.99           C  
ATOM    779  CD  ARG A 111      25.863  45.755   8.270  1.00229.51           C  
ATOM    780  NE  ARG A 111      24.659  44.938   8.140  1.00232.82           N  
ATOM    781  CZ  ARG A 111      24.354  44.222   7.063  1.00236.09           C  
ATOM    782  NH1 ARG A 111      25.166  44.217   6.014  1.00239.60           N  
ATOM    783  NH2 ARG A 111      23.236  43.508   7.033  1.00235.24           N  
ATOM    784  N   TYR A 112      26.663  44.449  13.542  1.00199.74           N  
ATOM    785  CA  TYR A 112      26.283  43.735  14.758  1.00196.48           C  
ATOM    786  C   TYR A 112      24.893  44.138  15.237  1.00193.50           C  
ATOM    787  O   TYR A 112      24.040  43.287  15.484  1.00197.57           O  
ATOM    788  CB  TYR A 112      27.309  43.976  15.868  1.00195.29           C  
ATOM    789  CG  TYR A 112      26.892  43.432  17.218  1.00195.97           C  
ATOM    790  CD1 TYR A 112      26.288  44.252  18.163  1.00193.11           C  
ATOM    791  CD2 TYR A 112      27.100  42.098  17.547  1.00197.67           C  
ATOM    792  CE1 TYR A 112      25.904  43.761  19.398  1.00191.32           C  
ATOM    793  CE2 TYR A 112      26.720  41.597  18.780  1.00193.91           C  
ATOM    794  CZ  TYR A 112      26.122  42.433  19.701  1.00190.72           C  
ATOM    795  OH  TYR A 112      25.741  41.942  20.929  1.00183.95           O  
ATOM    796  N   ASN A 113      24.672  45.441  15.367  1.00186.91           N  
ATOM    797  CA  ASN A 113      23.394  45.953  15.841  1.00180.76           C  
ATOM    798  C   ASN A 113      22.290  45.795  14.801  1.00175.48           C  
ATOM    799  O   ASN A 113      21.105  45.794  15.135  1.00170.20           O  
ATOM    800  CB  ASN A 113      23.532  47.419  16.254  1.00185.00           C  
ATOM    801  CG  ASN A 113      24.631  47.634  17.278  1.00184.93           C  
ATOM    802  OD1 ASN A 113      24.422  47.452  18.477  1.00184.05           O  
ATOM    803  ND2 ASN A 113      25.812  48.020  16.806  1.00184.48           N  
ATOM    804  N   GLY A 114      22.687  45.656  13.540  1.00178.02           N  
ATOM    805  CA  GLY A 114      21.738  45.500  12.453  1.00181.43           C  
ATOM    806  C   GLY A 114      21.253  44.071  12.296  1.00179.60           C  
ATOM    807  O   GLY A 114      20.106  43.833  11.917  1.00178.12           O  
ATOM    808  N   LEU A 115      22.130  43.117  12.588  1.00179.28           N  
ATOM    809  CA  LEU A 115      21.790  41.703  12.485  1.00178.87           C  
ATOM    810  C   LEU A 115      21.339  41.149  13.832  1.00185.14           C  
ATOM    811  O   LEU A 115      20.218  40.662  13.970  1.00189.27           O  
ATOM    812  CB  LEU A 115      22.983  40.903  11.957  1.00168.53           C  
ATOM    813  CG  LEU A 115      23.528  41.339  10.595  1.00165.54           C  
ATOM    814  CD1 LEU A 115      24.743  40.511  10.208  1.00156.46           C  
ATOM    815  CD2 LEU A 115      22.446  41.248   9.528  1.00171.59           C  
ATOM    816  N   VAL A 116      22.221  41.229  14.824  1.00186.85           N  
ATOM    817  CA  VAL A 116      21.906  40.770  16.172  1.00186.09           C  
ATOM    818  C   VAL A 116      20.861  41.675  16.815  1.00193.83           C  
ATOM    819  O   VAL A 116      21.198  42.681  17.441  1.00194.35           O  
ATOM    820  CB  VAL A 116      23.161  40.743  17.064  1.00175.24           C  
ATOM    821  CG1 VAL A 116      22.825  40.187  18.439  1.00167.38           C  
ATOM    822  CG2 VAL A 116      24.263  39.927  16.407  1.00171.16           C  
ATOM    823  N   THR A 117      19.592  41.315  16.658  1.00199.35           N  
ATOM    824  CA  THR A 117      18.502  42.110  17.210  1.00202.07           C  
ATOM    825  C   THR A 117      17.872  41.418  18.414  1.00204.56           C  
ATOM    826  O   THR A 117      17.983  40.202  18.570  1.00204.84           O  
ATOM    827  CB  THR A 117      17.411  42.386  16.156  1.00204.01           C  
ATOM    828  OG1 THR A 117      16.739  41.165  15.827  1.00210.19           O  
ATOM    829  CG2 THR A 117      18.024  42.981  14.897  1.00202.35           C  
ATOM    830  N   GLY A 118      17.214  42.199  19.263  1.00205.81           N  
ATOM    831  CA  GLY A 118      16.555  41.661  20.439  1.00202.68           C  
ATOM    832  C   GLY A 118      15.362  40.798  20.076  1.00200.24           C  
ATOM    833  O   GLY A 118      14.900  39.988  20.880  1.00194.10           O  
ATOM    834  N   THR A 119      14.861  40.976  18.857  1.00161.29           N  
ATOM    835  CA  THR A 119      13.728  40.200  18.372  1.00163.39           C  
ATOM    836  C   THR A 119      14.182  38.845  17.840  1.00162.89           C  
ATOM    837  O   THR A 119      13.631  37.809  18.210  1.00160.50           O  
ATOM    838  CB  THR A 119      12.960  40.948  17.265  1.00166.72           C  
ATOM    839  OG1 THR A 119      12.482  42.199  17.775  1.00166.34           O  
ATOM    840  CG2 THR A 119      11.781  40.119  16.781  1.00167.47           C  
ATOM    841  N   ARG A 120      15.189  38.860  16.971  1.00162.29           N  
ATOM    842  CA  ARG A 120      15.740  37.626  16.420  1.00162.26           C  
ATOM    843  C   ARG A 120      16.235  36.709  17.534  1.00162.00           C  
ATOM    844  O   ARG A 120      16.146  35.487  17.428  1.00164.72           O  
ATOM    845  CB  ARG A 120      16.878  37.927  15.440  1.00159.64           C  
ATOM    846  CG  ARG A 120      16.435  38.588  14.142  1.00163.88           C  
ATOM    847  CD  ARG A 120      17.614  38.797  13.200  1.00168.42           C  
ATOM    848  NE  ARG A 120      17.218  39.442  11.950  1.00174.56           N  
ATOM    849  CZ  ARG A 120      18.053  39.718  10.952  1.00175.99           C  
ATOM    850  NH1 ARG A 120      17.603  40.308   9.852  1.00178.41           N  
ATOM    851  NH2 ARG A 120      19.338  39.406  11.053  1.00174.09           N  
ATOM    852  N   ALA A 121      16.755  37.309  18.601  1.00159.04           N  
ATOM    853  CA  ALA A 121      17.224  36.550  19.753  1.00155.82           C  
ATOM    854  C   ALA A 121      16.110  35.666  20.302  1.00157.34           C  
ATOM    855  O   ALA A 121      16.262  34.448  20.403  1.00159.47           O  
ATOM    856  CB  ALA A 121      17.739  37.488  20.833  1.00152.77           C  
ATOM    857  N   ALA A 122      14.990  36.291  20.650  1.00156.81           N  
ATOM    858  CA  ALA A 122      13.833  35.568  21.167  1.00157.97           C  
ATOM    859  C   ALA A 122      13.331  34.539  20.158  1.00160.07           C  
ATOM    860  O   ALA A 122      12.848  33.470  20.534  1.00158.39           O  
ATOM    861  CB  ALA A 122      12.723  36.540  21.534  1.00157.00           C  
ATOM    862  N   GLY A 123      13.447  34.870  18.876  1.00160.38           N  
ATOM    863  CA  GLY A 123      13.035  33.969  17.816  1.00159.54           C  
ATOM    864  C   GLY A 123      13.909  32.733  17.757  1.00157.01           C  
ATOM    865  O   GLY A 123      13.411  31.608  17.746  1.00162.10           O  
ATOM    866  N   ILE A 124      15.221  32.944  17.721  1.00150.78           N  
ATOM    867  CA  ILE A 124      16.176  31.843  17.689  1.00148.36           C  
ATOM    868  C   ILE A 124      16.002  30.942  18.906  1.00145.64           C  
ATOM    869  O   ILE A 124      15.933  29.720  18.779  1.00146.25           O  
ATOM    870  CB  ILE A 124      17.626  32.354  17.645  1.00143.48           C  
ATOM    871  CG1 ILE A 124      17.843  33.233  16.412  1.00150.14           C  
ATOM    872  CG2 ILE A 124      18.602  31.187  17.650  1.00138.60           C  
ATOM    873  CD1 ILE A 124      19.198  33.909  16.373  1.00150.07           C  
ATOM    874  N   ILE A 125      15.931  31.556  20.083  1.00141.20           N  
ATOM    875  CA  ILE A 125      15.753  30.817  21.328  1.00137.67           C  
ATOM    876  C   ILE A 125      14.563  29.866  21.249  1.00144.05           C  
ATOM    877  O   ILE A 125      14.684  28.680  21.559  1.00148.41           O  
ATOM    878  CB  ILE A 125      15.565  31.769  22.525  1.00126.89           C  
ATOM    879  CG1 ILE A 125      16.840  32.578  22.762  1.00124.54           C  
ATOM    880  CG2 ILE A 125      15.196  30.988  23.774  1.00121.27           C  
ATOM    881  CD1 ILE A 125      16.748  33.527  23.933  1.00125.55           C  
ATOM    882  N   ALA A 126      13.417  30.393  20.831  1.00143.71           N  
ATOM    883  CA  ALA A 126      12.210  29.587  20.689  1.00143.80           C  
ATOM    884  C   ALA A 126      12.456  28.385  19.783  1.00144.45           C  
ATOM    885  O   ALA A 126      12.087  27.259  20.115  1.00142.47           O  
ATOM    886  CB  ALA A 126      11.068  30.434  20.149  1.00145.87           C  
ATOM    887  N   ILE A 127      13.086  28.634  18.639  1.00146.67           N  
ATOM    888  CA  ILE A 127      13.397  27.575  17.687  1.00150.11           C  
ATOM    889  C   ILE A 127      14.310  26.526  18.309  1.00144.09           C  
ATOM    890  O   ILE A 127      14.073  25.325  18.178  1.00141.19           O  
ATOM    891  CB  ILE A 127      14.080  28.135  16.426  1.00155.27           C  
ATOM    892  CG1 ILE A 127      13.186  29.177  15.752  1.00157.25           C  
ATOM    893  CG2 ILE A 127      14.418  27.009  15.459  1.00160.68           C  
ATOM    894  CD1 ILE A 127      13.803  29.801  14.519  1.00160.24           C  
ATOM    895  N   CYS A 128      15.356  26.989  18.985  1.00141.34           N  
ATOM    896  CA  CYS A 128      16.313  26.095  19.623  1.00141.29           C  
ATOM    897  C   CYS A 128      15.621  25.144  20.591  1.00144.04           C  
ATOM    898  O   CYS A 128      15.910  23.949  20.609  1.00147.26           O  
ATOM    899  CB  CYS A 128      17.394  26.897  20.348  1.00136.72           C  
ATOM    900  SG  CYS A 128      18.423  27.902  19.254  1.00153.58           S  
ATOM    901  N   TRP A 129      14.703  25.679  21.390  1.00142.23           N  
ATOM    902  CA  TRP A 129      13.951  24.864  22.337  1.00142.50           C  
ATOM    903  C   TRP A 129      13.102  23.813  21.628  1.00143.59           C  
ATOM    904  O   TRP A 129      13.043  22.660  22.054  1.00142.75           O  
ATOM    905  CB  TRP A 129      13.075  25.741  23.233  1.00140.73           C  
ATOM    906  CG  TRP A 129      13.834  26.395  24.341  1.00139.85           C  
ATOM    907  CD1 TRP A 129      14.279  27.683  24.383  1.00140.09           C  
ATOM    908  CD2 TRP A 129      14.247  25.786  25.571  1.00142.45           C  
ATOM    909  NE1 TRP A 129      14.940  27.917  25.565  1.00138.13           N  
ATOM    910  CE2 TRP A 129      14.935  26.768  26.311  1.00139.89           C  
ATOM    911  CE3 TRP A 129      14.100  24.507  26.117  1.00146.18           C  
ATOM    912  CZ2 TRP A 129      15.475  26.510  27.571  1.00140.41           C  
ATOM    913  CZ3 TRP A 129      14.637  24.254  27.367  1.00144.46           C  
ATOM    914  CH2 TRP A 129      15.315  25.250  28.080  1.00142.53           C  
ATOM    915  N   VAL A 130      12.447  24.218  20.545  1.00141.94           N  
ATOM    916  CA  VAL A 130      11.643  23.298  19.751  1.00140.86           C  
ATOM    917  C   VAL A 130      12.516  22.182  19.187  1.00146.91           C  
ATOM    918  O   VAL A 130      12.142  21.009  19.224  1.00149.86           O  
ATOM    919  CB  VAL A 130      10.921  24.024  18.601  1.00136.47           C  
ATOM    920  CG1 VAL A 130      10.255  23.022  17.673  1.00133.53           C  
ATOM    921  CG2 VAL A 130       9.901  25.009  19.153  1.00137.44           C  
ATOM    922  N   LEU A 131      13.684  22.553  18.673  1.00148.31           N  
ATOM    923  CA  LEU A 131      14.631  21.579  18.143  1.00150.14           C  
ATOM    924  C   LEU A 131      15.200  20.714  19.262  1.00151.73           C  
ATOM    925  O   LEU A 131      15.560  19.557  19.043  1.00155.85           O  
ATOM    926  CB  LEU A 131      15.766  22.281  17.396  1.00145.36           C  
ATOM    927  CG  LEU A 131      15.373  23.084  16.156  1.00144.83           C  
ATOM    928  CD1 LEU A 131      16.593  23.764  15.555  1.00144.81           C  
ATOM    929  CD2 LEU A 131      14.694  22.190  15.131  1.00144.75           C  
ATOM    930  N   SER A 132      15.280  21.284  20.460  1.00147.20           N  
ATOM    931  CA  SER A 132      15.798  20.564  21.618  1.00145.22           C  
ATOM    932  C   SER A 132      14.853  19.445  22.043  1.00151.95           C  
ATOM    933  O   SER A 132      15.294  18.352  22.397  1.00153.60           O  
ATOM    934  CB  SER A 132      16.043  21.522  22.785  1.00135.81           C  
ATOM    935  OG  SER A 132      17.078  22.438  22.481  1.00134.81           O  
ATOM    936  N   PHE A 133      13.554  19.725  22.009  1.00153.71           N  
ATOM    937  CA  PHE A 133      12.553  18.717  22.338  1.00152.54           C  
ATOM    938  C   PHE A 133      12.489  17.641  21.260  1.00156.28           C  
ATOM    939  O   PHE A 133      12.374  16.453  21.561  1.00156.98           O  
ATOM    940  CB  PHE A 133      11.178  19.359  22.533  1.00152.55           C  
ATOM    941  CG  PHE A 133      10.979  19.961  23.894  1.00151.85           C  
ATOM    942  CD1 PHE A 133      10.477  19.199  24.935  1.00147.72           C  
ATOM    943  CD2 PHE A 133      11.295  21.288  24.134  1.00155.48           C  
ATOM    944  CE1 PHE A 133      10.293  19.746  26.191  1.00144.19           C  
ATOM    945  CE2 PHE A 133      11.113  21.842  25.388  1.00152.43           C  
ATOM    946  CZ  PHE A 133      10.611  21.069  26.417  1.00146.72           C  
ATOM    947  N   ALA A 134      12.564  18.066  20.002  1.00158.38           N  
ATOM    948  CA  ALA A 134      12.561  17.134  18.882  1.00161.18           C  
ATOM    949  C   ALA A 134      13.726  16.159  19.003  1.00164.72           C  
ATOM    950  O   ALA A 134      13.546  14.945  18.909  1.00171.48           O  
ATOM    951  CB  ALA A 134      12.633  17.889  17.564  1.00159.39           C  
ATOM    952  N   ILE A 135      14.920  16.701  19.220  1.00161.69           N  
ATOM    953  CA  ILE A 135      16.124  15.888  19.347  1.00160.34           C  
ATOM    954  C   ILE A 135      16.148  15.105  20.657  1.00156.69           C  
ATOM    955  O   ILE A 135      16.252  13.880  20.656  1.00158.15           O  
ATOM    956  CB  ILE A 135      17.397  16.754  19.257  1.00155.17           C  
ATOM    957  CG1 ILE A 135      17.479  17.440  17.891  1.00152.63           C  
ATOM    958  CG2 ILE A 135      18.634  15.907  19.509  1.00152.23           C  
ATOM    959  CD1 ILE A 135      18.678  18.348  17.734  1.00145.40           C  
ATOM    960  N   GLY A 136      16.047  15.823  21.772  1.00152.01           N  
ATOM    961  CA  GLY A 136      16.120  15.217  23.089  1.00148.09           C  
ATOM    962  C   GLY A 136      15.094  14.126  23.337  1.00154.83           C  
ATOM    963  O   GLY A 136      15.330  13.214  24.130  1.00158.90           O  
ATOM    964  N   LEU A 137      13.952  14.218  22.663  1.00157.90           N  
ATOM    965  CA  LEU A 137      12.891  13.230  22.828  1.00155.83           C  
ATOM    966  C   LEU A 137      12.687  12.393  21.567  1.00163.50           C  
ATOM    967  O   LEU A 137      11.586  11.909  21.304  1.00165.43           O  
ATOM    968  CB  LEU A 137      11.579  13.904  23.238  1.00148.01           C  
ATOM    969  CG  LEU A 137      11.578  14.624  24.589  1.00137.38           C  
ATOM    970  CD1 LEU A 137      10.217  15.244  24.866  1.00135.70           C  
ATOM    971  CD2 LEU A 137      11.973  13.671  25.707  1.00131.66           C  
ATOM    972  N   THR A 138      13.754  12.228  20.791  1.00169.64           N  
ATOM    973  CA  THR A 138      13.714  11.384  19.601  1.00179.54           C  
ATOM    974  C   THR A 138      13.449   9.913  19.941  1.00185.66           C  
ATOM    975  O   THR A 138      12.737   9.226  19.209  1.00189.43           O  
ATOM    976  CB  THR A 138      15.014  11.499  18.773  1.00179.18           C  
ATOM    977  OG1 THR A 138      15.176  12.848  18.318  1.00177.03           O  
ATOM    978  CG2 THR A 138      14.966  10.569  17.570  1.00183.05           C  
ATOM    979  N   PRO A 139      14.030   9.421  21.050  1.00184.45           N  
ATOM    980  CA  PRO A 139      13.734   8.050  21.480  1.00184.30           C  
ATOM    981  C   PRO A 139      12.240   7.819  21.699  1.00184.47           C  
ATOM    982  O   PRO A 139      11.780   6.681  21.620  1.00190.30           O  
ATOM    983  CB  PRO A 139      14.484   7.935  22.809  1.00181.13           C  
ATOM    984  CG  PRO A 139      15.617   8.883  22.674  1.00179.75           C  
ATOM    985  CD  PRO A 139      15.086  10.037  21.874  1.00180.57           C  
ATOM    986  N   MET A 140      11.496   8.886  21.971  1.00181.41           N  
ATOM    987  CA  MET A 140      10.053   8.778  22.157  1.00181.36           C  
ATOM    988  C   MET A 140       9.332   8.650  20.820  1.00186.77           C  
ATOM    989  O   MET A 140       8.167   8.257  20.767  1.00191.05           O  
ATOM    990  CB  MET A 140       9.510   9.981  22.932  1.00178.12           C  
ATOM    991  CG  MET A 140      10.046  10.100  24.348  1.00176.22           C  
ATOM    992  SD  MET A 140       9.124  11.287  25.341  1.00171.45           S  
ATOM    993  CE  MET A 140       7.493  10.548  25.324  1.00134.10           C  
ATOM    994  N   LEU A 141      10.034   8.984  19.742  1.00187.23           N  
ATOM    995  CA  LEU A 141       9.464   8.911  18.402  1.00190.16           C  
ATOM    996  C   LEU A 141       9.418   7.471  17.898  1.00188.18           C  
ATOM    997  O   LEU A 141       8.916   7.202  16.806  1.00191.77           O  
ATOM    998  CB  LEU A 141      10.262   9.786  17.432  1.00192.15           C  
ATOM    999  CG  LEU A 141      10.372  11.268  17.802  1.00188.61           C  
ATOM   1000  CD1 LEU A 141      11.273  12.005  16.822  1.00190.50           C  
ATOM   1001  CD2 LEU A 141       8.995  11.910  17.862  1.00186.98           C  
ATOM   1002  N   GLY A 142       9.942   6.550  18.701  1.00212.91           N  
ATOM   1003  CA  GLY A 142       9.952   5.141  18.349  1.00208.82           C  
ATOM   1004  C   GLY A 142      11.330   4.521  18.473  1.00201.65           C  
ATOM   1005  O   GLY A 142      11.476   3.299  18.472  1.00201.60           O  
ATOM   1006  N   TRP A 143      12.345   5.372  18.582  1.00195.22           N  
ATOM   1007  CA  TRP A 143      13.727   4.921  18.700  1.00187.72           C  
ATOM   1008  C   TRP A 143      14.046   4.551  20.146  1.00181.63           C  
ATOM   1009  O   TRP A 143      14.840   5.221  20.805  1.00178.94           O  
ATOM   1010  CB  TRP A 143      14.677   6.022  18.222  1.00185.79           C  
ATOM   1011  CG  TRP A 143      16.071   5.551  17.935  1.00186.73           C  
ATOM   1012  CD1 TRP A 143      16.952   5.006  18.823  1.00187.68           C  
ATOM   1013  CD2 TRP A 143      16.752   5.603  16.675  1.00188.93           C  
ATOM   1014  NE1 TRP A 143      18.136   4.705  18.193  1.00190.15           N  
ATOM   1015  CE2 TRP A 143      18.039   5.063  16.873  1.00190.86           C  
ATOM   1016  CE3 TRP A 143      16.397   6.050  15.398  1.00189.22           C  
ATOM   1017  CZ2 TRP A 143      18.972   4.958  15.842  1.00190.97           C  
ATOM   1018  CZ3 TRP A 143      17.325   5.944  14.376  1.00189.78           C  
ATOM   1019  CH2 TRP A 143      18.596   5.402  14.604  1.00190.33           C  
ATOM   1020  N   ASN A 144      13.423   3.483  20.637  1.00178.84           N  
ATOM   1021  CA  ASN A 144      13.608   3.070  22.025  1.00173.71           C  
ATOM   1022  C   ASN A 144      13.687   1.554  22.207  1.00173.00           C  
ATOM   1023  O   ASN A 144      13.449   0.789  21.272  1.00170.42           O  
ATOM   1024  CB  ASN A 144      12.499   3.652  22.906  1.00169.47           C  
ATOM   1025  CG  ASN A 144      11.116   3.207  22.473  1.00170.07           C  
ATOM   1026  OD1 ASN A 144      10.845   2.012  22.355  1.00175.22           O  
ATOM   1027  ND2 ASN A 144      10.230   4.168  22.240  1.00167.06           N  
ATOM   1028  N   ASN A 145      14.027   1.130  23.421  1.00172.07           N  
ATOM   1029  CA  ASN A 145      14.122  -0.289  23.742  1.00171.11           C  
ATOM   1030  C   ASN A 145      13.101  -0.715  24.791  1.00173.32           C  
ATOM   1031  O   ASN A 145      13.432  -1.424  25.741  1.00178.92           O  
ATOM   1032  CB  ASN A 145      15.534  -0.643  24.213  1.00169.10           C  
ATOM   1033  CG  ASN A 145      16.560  -0.555  23.102  1.00146.30           C  
ATOM   1034  OD1 ASN A 145      16.211  -0.473  21.924  1.00147.64           O  
ATOM   1035  ND2 ASN A 145      17.835  -0.575  23.471  1.00146.81           N  
ATOM   1036  N   CYS A 146      11.859  -0.277  24.614  1.00170.90           N  
ATOM   1037  CA  CYS A 146      10.790  -0.619  25.544  1.00170.70           C  
ATOM   1038  C   CYS A 146      10.298  -2.046  25.326  1.00174.29           C  
ATOM   1039  O   CYS A 146       9.616  -2.334  24.343  1.00176.80           O  
ATOM   1040  CB  CYS A 146       9.624   0.363  25.407  1.00167.72           C  
ATOM   1041  SG  CYS A 146      10.035   2.076  25.809  1.00222.60           S  
ATOM   1042  N   GLY A 147      10.652  -2.936  26.247  1.00174.05           N  
ATOM   1043  CA  GLY A 147      10.205  -4.315  26.183  1.00177.88           C  
ATOM   1044  C   GLY A 147      11.121  -5.213  25.374  1.00183.77           C  
ATOM   1045  O   GLY A 147      10.738  -6.321  24.996  1.00187.71           O  
ATOM   1046  N   GLN A 148      12.332  -4.737  25.105  1.00184.25           N  
ATOM   1047  CA  GLN A 148      13.314  -5.527  24.372  1.00189.11           C  
ATOM   1048  C   GLN A 148      13.863  -6.652  25.241  1.00195.64           C  
ATOM   1049  O   GLN A 148      14.180  -6.438  26.412  1.00200.27           O  
ATOM   1050  CB  GLN A 148      14.455  -4.641  23.866  1.00182.65           C  
ATOM   1051  CG  GLN A 148      14.029  -3.619  22.826  1.00179.88           C  
ATOM   1052  CD  GLN A 148      13.434  -4.260  21.587  1.00179.95           C  
ATOM   1053  OE1 GLN A 148      13.718  -5.416  21.273  1.00181.29           O  
ATOM   1054  NE2 GLN A 148      12.604  -3.508  20.874  1.00180.15           N  
ATOM   1055  N   PRO A 149      13.975  -7.859  24.665  1.00191.18           N  
ATOM   1056  CA  PRO A 149      14.443  -9.056  25.372  1.00187.70           C  
ATOM   1057  C   PRO A 149      15.711  -8.793  26.178  1.00182.54           C  
ATOM   1058  O   PRO A 149      15.610  -8.597  27.389  1.00179.30           O  
ATOM   1059  CB  PRO A 149      14.734 -10.035  24.234  1.00189.12           C  
ATOM   1060  CG  PRO A 149      13.787  -9.635  23.159  1.00189.01           C  
ATOM   1061  CD  PRO A 149      13.672  -8.138  23.249  1.00189.36           C  
ATOM   1062  N   GLY A 158       7.305  -8.648  37.445  1.00255.41           N  
ATOM   1063  CA  GLY A 158       8.099  -7.453  37.663  1.00250.18           C  
ATOM   1064  C   GLY A 158       7.246  -6.213  37.851  1.00246.52           C  
ATOM   1065  O   GLY A 158       6.969  -5.803  38.979  1.00244.44           O  
ATOM   1066  N   CYS A 159       6.828  -5.614  36.741  1.00245.21           N  
ATOM   1067  CA  CYS A 159       6.003  -4.412  36.780  1.00241.81           C  
ATOM   1068  C   CYS A 159       4.604  -4.682  36.235  1.00240.63           C  
ATOM   1069  O   CYS A 159       3.679  -3.899  36.456  1.00238.23           O  
ATOM   1070  CB  CYS A 159       6.667  -3.279  35.992  1.00240.94           C  
ATOM   1071  SG  CYS A 159       8.300  -2.792  36.604  1.00191.85           S  
ATOM   1072  N   GLY A 160       4.456  -5.794  35.523  1.00241.79           N  
ATOM   1073  CA  GLY A 160       3.178  -6.167  34.945  1.00242.29           C  
ATOM   1074  C   GLY A 160       2.997  -5.623  33.541  1.00236.54           C  
ATOM   1075  O   GLY A 160       3.707  -4.709  33.123  1.00229.89           O  
ATOM   1076  N   GLU A 161       2.042  -6.190  32.810  1.00236.65           N  
ATOM   1077  CA  GLU A 161       1.766  -5.757  31.445  1.00231.20           C  
ATOM   1078  C   GLU A 161       1.363  -4.287  31.413  1.00217.57           C  
ATOM   1079  O   GLU A 161       0.606  -3.822  32.265  1.00211.10           O  
ATOM   1080  CB  GLU A 161       0.675  -6.624  30.812  1.00240.16           C  
ATOM   1081  CG  GLU A 161      -0.666  -6.569  31.528  1.00244.67           C  
ATOM   1082  CD  GLU A 161      -1.690  -7.509  30.919  1.00251.30           C  
ATOM   1083  OE1 GLU A 161      -2.875  -7.431  31.306  1.00253.86           O  
ATOM   1084  OE2 GLU A 161      -1.310  -8.327  30.054  1.00253.56           O  
ATOM   1085  N   GLY A 162       1.876  -3.561  30.426  1.00215.75           N  
ATOM   1086  CA  GLY A 162       1.616  -2.138  30.312  1.00214.28           C  
ATOM   1087  C   GLY A 162       2.759  -1.313  30.869  1.00209.38           C  
ATOM   1088  O   GLY A 162       3.278  -0.420  30.200  1.00205.70           O  
ATOM   1089  N   GLN A 163       3.154  -1.617  32.102  1.00209.46           N  
ATOM   1090  CA  GLN A 163       4.258  -0.919  32.749  1.00205.95           C  
ATOM   1091  C   GLN A 163       5.594  -1.580  32.421  1.00199.31           C  
ATOM   1092  O   GLN A 163       5.690  -2.805  32.346  1.00197.60           O  
ATOM   1093  CB  GLN A 163       4.049  -0.870  34.265  1.00208.54           C  
ATOM   1094  CG  GLN A 163       2.802  -0.112  34.697  1.00208.69           C  
ATOM   1095  CD  GLN A 163       2.650  -0.048  36.205  1.00206.35           C  
ATOM   1096  OE1 GLN A 163       3.419  -0.661  36.945  1.00206.38           O  
ATOM   1097  NE2 GLN A 163       1.653   0.698  36.669  1.00204.21           N  
ATOM   1098  N   VAL A 164       6.622  -0.760  32.226  1.00191.74           N  
ATOM   1099  CA  VAL A 164       7.949  -1.256  31.882  1.00184.47           C  
ATOM   1100  C   VAL A 164       8.986  -0.802  32.903  1.00173.42           C  
ATOM   1101  O   VAL A 164       8.961   0.343  33.355  1.00168.81           O  
ATOM   1102  CB  VAL A 164       8.382  -0.773  30.481  1.00183.00           C  
ATOM   1103  CG1 VAL A 164       9.815  -1.196  30.188  1.00180.49           C  
ATOM   1104  CG2 VAL A 164       7.432  -1.306  29.419  1.00188.46           C  
ATOM   1105  N   ALA A 165       9.891  -1.705  33.270  1.00167.75           N  
ATOM   1106  CA  ALA A 165      10.975  -1.371  34.186  1.00158.25           C  
ATOM   1107  C   ALA A 165      11.780  -0.206  33.628  1.00151.64           C  
ATOM   1108  O   ALA A 165      12.614  -0.384  32.739  1.00143.58           O  
ATOM   1109  CB  ALA A 165      11.869  -2.578  34.415  1.00160.91           C  
ATOM   1110  N   CYS A 166      11.522   0.987  34.155  1.00154.61           N  
ATOM   1111  CA  CYS A 166      12.136   2.207  33.644  1.00148.06           C  
ATOM   1112  C   CYS A 166      13.597   2.334  34.060  1.00139.10           C  
ATOM   1113  O   CYS A 166      13.918   2.969  35.065  1.00119.47           O  
ATOM   1114  CB  CYS A 166      11.348   3.434  34.103  1.00143.39           C  
ATOM   1115  SG  CYS A 166      11.863   4.979  33.322  1.00245.15           S  
ATOM   1116  N   LEU A 167      14.478   1.721  33.277  1.00152.86           N  
ATOM   1117  CA  LEU A 167      15.912   1.801  33.515  1.00157.46           C  
ATOM   1118  C   LEU A 167      16.569   2.464  32.311  1.00155.68           C  
ATOM   1119  O   LEU A 167      16.408   2.008  31.181  1.00160.22           O  
ATOM   1120  CB  LEU A 167      16.495   0.404  33.738  1.00165.70           C  
ATOM   1121  CG  LEU A 167      15.738  -0.502  34.715  1.00167.01           C  
ATOM   1122  CD1 LEU A 167      16.446  -1.839  34.867  1.00164.86           C  
ATOM   1123  CD2 LEU A 167      15.565   0.172  36.068  1.00167.18           C  
ATOM   1124  N   PHE A 168      17.306   3.542  32.558  1.00150.83           N  
ATOM   1125  CA  PHE A 168      17.864   4.355  31.480  1.00157.21           C  
ATOM   1126  C   PHE A 168      18.552   3.533  30.391  1.00161.69           C  
ATOM   1127  O   PHE A 168      18.255   3.691  29.208  1.00166.51           O  
ATOM   1128  CB  PHE A 168      18.828   5.406  32.040  1.00161.27           C  
ATOM   1129  CG  PHE A 168      19.357   6.357  31.002  1.00162.85           C  
ATOM   1130  CD1 PHE A 168      18.542   7.342  30.466  1.00159.41           C  
ATOM   1131  CD2 PHE A 168      20.669   6.270  30.567  1.00161.69           C  
ATOM   1132  CE1 PHE A 168      19.024   8.218  29.512  1.00154.89           C  
ATOM   1133  CE2 PHE A 168      21.158   7.144  29.615  1.00156.37           C  
ATOM   1134  CZ  PHE A 168      20.334   8.119  29.086  1.00153.71           C  
ATOM   1135  N   GLU A 169      19.463   2.654  30.794  1.00162.27           N  
ATOM   1136  CA  GLU A 169      20.230   1.860  29.837  1.00167.37           C  
ATOM   1137  C   GLU A 169      19.370   0.821  29.116  1.00167.14           C  
ATOM   1138  O   GLU A 169      19.699   0.395  28.009  1.00164.75           O  
ATOM   1139  CB  GLU A 169      21.417   1.177  30.525  1.00173.60           C  
ATOM   1140  CG  GLU A 169      21.036   0.086  31.517  1.00182.61           C  
ATOM   1141  CD  GLU A 169      20.443   0.633  32.802  1.00189.02           C  
ATOM   1142  OE1 GLU A 169      20.606   1.844  33.069  1.00190.13           O  
ATOM   1143  OE2 GLU A 169      19.819  -0.150  33.549  1.00190.68           O  
ATOM   1144  N   ASP A 170      18.268   0.423  29.744  1.00169.70           N  
ATOM   1145  CA  ASP A 170      17.402  -0.615  29.193  1.00174.02           C  
ATOM   1146  C   ASP A 170      16.289  -0.063  28.304  1.00171.40           C  
ATOM   1147  O   ASP A 170      15.810  -0.750  27.403  1.00176.09           O  
ATOM   1148  CB  ASP A 170      16.798  -1.463  30.317  1.00180.50           C  
ATOM   1149  CG  ASP A 170      17.828  -2.336  31.010  1.00186.63           C  
ATOM   1150  OD1 ASP A 170      18.997  -2.344  30.570  1.00188.00           O  
ATOM   1151  OD2 ASP A 170      17.467  -3.018  31.992  1.00190.16           O  
ATOM   1152  N   VAL A 171      15.879   1.175  28.559  1.00166.69           N  
ATOM   1153  CA  VAL A 171      14.778   1.777  27.813  1.00169.54           C  
ATOM   1154  C   VAL A 171      15.262   2.766  26.754  1.00168.00           C  
ATOM   1155  O   VAL A 171      14.510   3.140  25.854  1.00167.60           O  
ATOM   1156  CB  VAL A 171      13.778   2.487  28.750  1.00171.32           C  
ATOM   1157  CG1 VAL A 171      13.182   1.496  29.737  1.00175.84           C  
ATOM   1158  CG2 VAL A 171      14.456   3.635  29.481  1.00168.19           C  
ATOM   1159  N   VAL A 172      16.518   3.187  26.866  1.00165.05           N  
ATOM   1160  CA  VAL A 172      17.096   4.128  25.913  1.00157.49           C  
ATOM   1161  C   VAL A 172      18.216   3.478  25.105  1.00161.48           C  
ATOM   1162  O   VAL A 172      19.206   3.014  25.671  1.00164.81           O  
ATOM   1163  CB  VAL A 172      17.643   5.386  26.616  1.00140.86           C  
ATOM   1164  CG1 VAL A 172      18.249   6.339  25.598  1.00137.63           C  
ATOM   1165  CG2 VAL A 172      16.541   6.074  27.407  1.00130.98           C  
ATOM   1166  N   PRO A 173      18.057   3.445  23.774  1.00161.27           N  
ATOM   1167  CA  PRO A 173      19.033   2.845  22.857  1.00163.97           C  
ATOM   1168  C   PRO A 173      20.419   3.465  23.000  1.00166.68           C  
ATOM   1169  O   PRO A 173      20.533   4.645  23.331  1.00164.34           O  
ATOM   1170  CB  PRO A 173      18.458   3.170  21.476  1.00160.82           C  
ATOM   1171  CG  PRO A 173      17.004   3.345  21.706  1.00159.77           C  
ATOM   1172  CD  PRO A 173      16.883   3.972  23.060  1.00158.32           C  
ATOM   1173  N   MET A 174      21.456   2.673  22.748  1.00171.51           N  
ATOM   1174  CA  MET A 174      22.831   3.156  22.832  1.00173.64           C  
ATOM   1175  C   MET A 174      23.305   3.738  21.505  1.00178.72           C  
ATOM   1176  O   MET A 174      24.103   4.675  21.479  1.00181.47           O  
ATOM   1177  CB  MET A 174      23.769   2.036  23.282  1.00177.13           C  
ATOM   1178  CG  MET A 174      23.577   1.611  24.728  1.00178.80           C  
ATOM   1179  SD  MET A 174      23.894   2.954  25.888  1.00214.11           S  
ATOM   1180  CE  MET A 174      25.594   3.358  25.491  1.00112.81           C  
ATOM   1181  N   ASN A 175      22.815   3.174  20.405  1.00182.62           N  
ATOM   1182  CA  ASN A 175      23.141   3.683  19.078  1.00185.86           C  
ATOM   1183  C   ASN A 175      22.689   5.130  18.916  1.00187.72           C  
ATOM   1184  O   ASN A 175      23.288   5.903  18.166  1.00187.02           O  
ATOM   1185  CB  ASN A 175      22.524   2.801  17.989  1.00187.70           C  
ATOM   1186  CG  ASN A 175      21.018   2.669  18.123  1.00189.59           C  
ATOM   1187  OD1 ASN A 175      20.433   3.072  19.128  1.00189.12           O  
ATOM   1188  ND2 ASN A 175      20.382   2.098  17.106  1.00191.34           N  
ATOM   1189  N   TYR A 176      21.627   5.489  19.628  1.00155.63           N  
ATOM   1190  CA  TYR A 176      21.142   6.860  19.646  1.00151.73           C  
ATOM   1191  C   TYR A 176      22.061   7.733  20.493  1.00145.73           C  
ATOM   1192  O   TYR A 176      22.534   8.774  20.042  1.00148.75           O  
ATOM   1193  CB  TYR A 176      19.715   6.916  20.195  1.00156.37           C  
ATOM   1194  CG  TYR A 176      19.244   8.312  20.526  1.00164.14           C  
ATOM   1195  CD1 TYR A 176      18.545   9.070  19.597  1.00166.48           C  
ATOM   1196  CD2 TYR A 176      19.506   8.877  21.769  1.00165.83           C  
ATOM   1197  CE1 TYR A 176      18.116  10.349  19.897  1.00165.82           C  
ATOM   1198  CE2 TYR A 176      19.083  10.155  22.076  1.00165.55           C  
ATOM   1199  CZ  TYR A 176      18.389  10.886  21.138  1.00165.49           C  
ATOM   1200  OH  TYR A 176      17.968  12.159  21.444  1.00167.24           O  
ATOM   1201  N   MET A 177      22.311   7.296  21.722  1.00138.65           N  
ATOM   1202  CA  MET A 177      23.129   8.053  22.662  1.00136.21           C  
ATOM   1203  C   MET A 177      24.526   8.328  22.114  1.00131.23           C  
ATOM   1204  O   MET A 177      25.187   9.281  22.528  1.00129.20           O  
ATOM   1205  CB  MET A 177      23.230   7.310  23.996  1.00141.52           C  
ATOM   1206  CG  MET A 177      21.895   7.101  24.691  1.00145.61           C  
ATOM   1207  SD  MET A 177      21.128   8.654  25.185  1.00130.39           S  
ATOM   1208  CE  MET A 177      22.407   9.330  26.241  1.00114.53           C  
ATOM   1209  N   VAL A 178      24.969   7.492  21.181  1.00130.07           N  
ATOM   1210  CA  VAL A 178      26.319   7.595  20.639  1.00133.01           C  
ATOM   1211  C   VAL A 178      26.364   8.349  19.312  1.00136.87           C  
ATOM   1212  O   VAL A 178      26.929   9.439  19.231  1.00142.20           O  
ATOM   1213  CB  VAL A 178      26.959   6.203  20.460  1.00134.31           C  
ATOM   1214  CG1 VAL A 178      28.286   6.322  19.734  1.00134.27           C  
ATOM   1215  CG2 VAL A 178      27.142   5.525  21.811  1.00134.00           C  
ATOM   1216  N   TYR A 179      25.767   7.767  18.277  1.00140.93           N  
ATOM   1217  CA  TYR A 179      25.795   8.363  16.944  1.00153.48           C  
ATOM   1218  C   TYR A 179      24.983   9.654  16.862  1.00159.54           C  
ATOM   1219  O   TYR A 179      25.542  10.740  16.699  1.00163.70           O  
ATOM   1220  CB  TYR A 179      25.299   7.362  15.898  1.00158.37           C  
ATOM   1221  CG  TYR A 179      26.191   6.151  15.747  1.00164.11           C  
ATOM   1222  CD1 TYR A 179      27.221   6.135  14.816  1.00166.65           C  
ATOM   1223  CD2 TYR A 179      26.007   5.025  16.538  1.00167.45           C  
ATOM   1224  CE1 TYR A 179      28.041   5.032  14.674  1.00168.16           C  
ATOM   1225  CE2 TYR A 179      26.821   3.916  16.405  1.00168.14           C  
ATOM   1226  CZ  TYR A 179      27.837   3.925  15.471  1.00168.19           C  
ATOM   1227  OH  TYR A 179      28.650   2.824  15.335  1.00167.33           O  
ATOM   1228  N   PHE A 180      23.665   9.526  16.974  1.00155.14           N  
ATOM   1229  CA  PHE A 180      22.762  10.665  16.849  1.00148.45           C  
ATOM   1230  C   PHE A 180      23.030  11.728  17.909  1.00143.98           C  
ATOM   1231  O   PHE A 180      23.331  12.878  17.586  1.00144.12           O  
ATOM   1232  CB  PHE A 180      21.307  10.198  16.933  1.00145.14           C  
ATOM   1233  CG  PHE A 180      20.302  11.296  16.719  1.00147.27           C  
ATOM   1234  CD1 PHE A 180      19.852  11.601  15.445  1.00148.08           C  
ATOM   1235  CD2 PHE A 180      19.803  12.017  17.790  1.00149.05           C  
ATOM   1236  CE1 PHE A 180      18.924  12.608  15.245  1.00147.77           C  
ATOM   1237  CE2 PHE A 180      18.875  13.025  17.597  1.00149.76           C  
ATOM   1238  CZ  PHE A 180      18.435  13.321  16.323  1.00148.34           C  
ATOM   1239  N   ASN A 181      22.921  11.337  19.174  1.00136.41           N  
ATOM   1240  CA  ASN A 181      23.056  12.275  20.283  1.00128.64           C  
ATOM   1241  C   ASN A 181      24.461  12.858  20.423  1.00128.70           C  
ATOM   1242  O   ASN A 181      24.680  14.035  20.147  1.00137.58           O  
ATOM   1243  CB  ASN A 181      22.620  11.620  21.597  1.00125.29           C  
ATOM   1244  CG  ASN A 181      22.544  12.608  22.746  1.00122.34           C  
ATOM   1245  OD1 ASN A 181      22.993  13.748  22.631  1.00121.60           O  
ATOM   1246  ND2 ASN A 181      21.971  12.174  23.862  1.00123.46           N  
ATOM   1247  N   PHE A 182      25.407  12.030  20.852  1.00126.28           N  
ATOM   1248  CA  PHE A 182      26.758  12.500  21.141  1.00127.75           C  
ATOM   1249  C   PHE A 182      27.450  13.136  19.933  1.00134.15           C  
ATOM   1250  O   PHE A 182      27.628  14.350  19.885  1.00141.46           O  
ATOM   1251  CB  PHE A 182      27.612  11.370  21.727  1.00129.42           C  
ATOM   1252  CG  PHE A 182      29.037  11.764  21.999  1.00129.41           C  
ATOM   1253  CD1 PHE A 182      29.327  12.879  22.768  1.00133.00           C  
ATOM   1254  CD2 PHE A 182      30.085  11.014  21.495  1.00126.59           C  
ATOM   1255  CE1 PHE A 182      30.637  13.243  23.021  1.00134.62           C  
ATOM   1256  CE2 PHE A 182      31.397  11.372  21.745  1.00126.01           C  
ATOM   1257  CZ  PHE A 182      31.673  12.488  22.510  1.00131.21           C  
ATOM   1258  N   PHE A 183      27.832  12.323  18.957  1.00137.25           N  
ATOM   1259  CA  PHE A 183      28.593  12.825  17.818  1.00146.41           C  
ATOM   1260  C   PHE A 183      27.915  13.979  17.085  1.00150.52           C  
ATOM   1261  O   PHE A 183      28.519  15.033  16.873  1.00151.64           O  
ATOM   1262  CB  PHE A 183      28.898  11.693  16.842  1.00151.96           C  
ATOM   1263  CG  PHE A 183      29.898  10.709  17.362  1.00156.69           C  
ATOM   1264  CD1 PHE A 183      31.236  11.051  17.448  1.00160.43           C  
ATOM   1265  CD2 PHE A 183      29.505   9.445  17.766  1.00154.28           C  
ATOM   1266  CE1 PHE A 183      32.165  10.152  17.927  1.00160.18           C  
ATOM   1267  CE2 PHE A 183      30.429   8.540  18.245  1.00152.59           C  
ATOM   1268  CZ  PHE A 183      31.762   8.893  18.326  1.00156.10           C  
ATOM   1269  N   ALA A 184      26.660  13.778  16.700  1.00151.04           N  
ATOM   1270  CA  ALA A 184      25.961  14.751  15.869  1.00151.36           C  
ATOM   1271  C   ALA A 184      25.436  15.954  16.650  1.00148.17           C  
ATOM   1272  O   ALA A 184      25.587  17.094  16.213  1.00145.94           O  
ATOM   1273  CB  ALA A 184      24.826  14.073  15.106  1.00150.02           C  
ATOM   1274  N   CYS A 185      24.829  15.704  17.805  1.00145.80           N  
ATOM   1275  CA  CYS A 185      24.156  16.766  18.547  1.00143.26           C  
ATOM   1276  C   CYS A 185      25.004  17.366  19.670  1.00142.43           C  
ATOM   1277  O   CYS A 185      24.552  18.263  20.381  1.00151.55           O  
ATOM   1278  CB  CYS A 185      22.821  16.262  19.104  1.00142.95           C  
ATOM   1279  SG  CYS A 185      21.680  15.634  17.848  1.00114.36           S  
ATOM   1280  N   VAL A 186      26.230  16.877  19.826  1.00135.36           N  
ATOM   1281  CA  VAL A 186      27.107  17.375  20.880  1.00136.37           C  
ATOM   1282  C   VAL A 186      28.530  17.630  20.388  1.00131.80           C  
ATOM   1283  O   VAL A 186      29.031  18.751  20.474  1.00124.77           O  
ATOM   1284  CB  VAL A 186      27.147  16.415  22.086  1.00142.69           C  
ATOM   1285  CG1 VAL A 186      28.181  16.880  23.100  1.00146.34           C  
ATOM   1286  CG2 VAL A 186      25.771  16.309  22.728  1.00141.45           C  
ATOM   1287  N   LEU A 187      29.176  16.589  19.874  1.00136.31           N  
ATOM   1288  CA  LEU A 187      30.552  16.700  19.403  1.00140.43           C  
ATOM   1289  C   LEU A 187      30.673  17.706  18.261  1.00140.62           C  
ATOM   1290  O   LEU A 187      31.539  18.580  18.284  1.00136.56           O  
ATOM   1291  CB  LEU A 187      31.088  15.336  18.965  1.00139.91           C  
ATOM   1292  CG  LEU A 187      32.575  15.291  18.605  1.00141.28           C  
ATOM   1293  CD1 LEU A 187      33.428  15.665  19.808  1.00136.76           C  
ATOM   1294  CD2 LEU A 187      32.962  13.921  18.076  1.00143.33           C  
ATOM   1295  N   VAL A 188      29.802  17.578  17.264  1.00142.66           N  
ATOM   1296  CA  VAL A 188      29.801  18.497  16.128  1.00143.31           C  
ATOM   1297  C   VAL A 188      29.635  19.951  16.569  1.00139.71           C  
ATOM   1298  O   VAL A 188      30.435  20.807  16.190  1.00136.00           O  
ATOM   1299  CB  VAL A 188      28.717  18.135  15.089  1.00145.21           C  
ATOM   1300  CG1 VAL A 188      28.542  19.269  14.087  1.00147.20           C  
ATOM   1301  CG2 VAL A 188      29.069  16.833  14.383  1.00143.74           C  
ATOM   1302  N   PRO A 189      28.595  20.237  17.371  1.00139.05           N  
ATOM   1303  CA  PRO A 189      28.415  21.601  17.878  1.00135.60           C  
ATOM   1304  C   PRO A 189      29.653  22.105  18.614  1.00124.97           C  
ATOM   1305  O   PRO A 189      30.098  23.222  18.361  1.00115.47           O  
ATOM   1306  CB  PRO A 189      27.243  21.457  18.851  1.00136.47           C  
ATOM   1307  CG  PRO A 189      26.472  20.298  18.332  1.00134.07           C  
ATOM   1308  CD  PRO A 189      27.496  19.347  17.788  1.00135.19           C  
ATOM   1309  N   LEU A 190      30.201  21.287  19.508  1.00125.97           N  
ATOM   1310  CA  LEU A 190      31.388  21.671  20.266  1.00125.49           C  
ATOM   1311  C   LEU A 190      32.597  21.887  19.361  1.00131.98           C  
ATOM   1312  O   LEU A 190      33.537  22.592  19.728  1.00138.30           O  
ATOM   1313  CB  LEU A 190      31.710  20.626  21.338  1.00122.53           C  
ATOM   1314  CG  LEU A 190      30.748  20.554  22.526  1.00122.75           C  
ATOM   1315  CD1 LEU A 190      31.081  19.367  23.414  1.00128.78           C  
ATOM   1316  CD2 LEU A 190      30.779  21.848  23.323  1.00110.29           C  
ATOM   1317  N   LEU A 191      32.573  21.277  18.181  1.00133.48           N  
ATOM   1318  CA  LEU A 191      33.637  21.474  17.204  1.00138.28           C  
ATOM   1319  C   LEU A 191      33.419  22.772  16.434  1.00143.63           C  
ATOM   1320  O   LEU A 191      34.374  23.467  16.085  1.00143.93           O  
ATOM   1321  CB  LEU A 191      33.723  20.287  16.244  1.00137.20           C  
ATOM   1322  CG  LEU A 191      34.244  18.983  16.849  1.00136.92           C  
ATOM   1323  CD1 LEU A 191      34.180  17.855  15.831  1.00140.75           C  
ATOM   1324  CD2 LEU A 191      35.662  19.160  17.373  1.00131.03           C  
ATOM   1325  N   LEU A 192      32.155  23.092  16.174  1.00144.31           N  
ATOM   1326  CA  LEU A 192      31.804  24.359  15.545  1.00142.63           C  
ATOM   1327  C   LEU A 192      32.114  25.507  16.495  1.00141.17           C  
ATOM   1328  O   LEU A 192      32.748  26.488  16.110  1.00144.73           O  
ATOM   1329  CB  LEU A 192      30.322  24.383  15.164  1.00142.94           C  
ATOM   1330  CG  LEU A 192      29.874  23.425  14.058  1.00142.13           C  
ATOM   1331  CD1 LEU A 192      28.367  23.500  13.865  1.00139.78           C  
ATOM   1332  CD2 LEU A 192      30.600  23.731  12.757  1.00141.66           C  
ATOM   1333  N   MET A 193      31.665  25.373  17.739  1.00135.98           N  
ATOM   1334  CA  MET A 193      31.916  26.378  18.763  1.00133.10           C  
ATOM   1335  C   MET A 193      33.407  26.656  18.898  1.00140.26           C  
ATOM   1336  O   MET A 193      33.844  27.802  18.799  1.00146.92           O  
ATOM   1337  CB  MET A 193      31.346  25.927  20.108  1.00127.92           C  
ATOM   1338  CG  MET A 193      29.847  25.687  20.098  1.00130.81           C  
ATOM   1339  SD  MET A 193      29.218  25.221  21.721  1.00176.58           S  
ATOM   1340  CE  MET A 193      29.772  26.616  22.692  1.00189.18           C  
ATOM   1341  N   LEU A 194      34.184  25.603  19.124  1.00140.16           N  
ATOM   1342  CA  LEU A 194      35.631  25.736  19.236  1.00144.63           C  
ATOM   1343  C   LEU A 194      36.203  26.403  17.990  1.00144.03           C  
ATOM   1344  O   LEU A 194      37.070  27.271  18.083  1.00139.82           O  
ATOM   1345  CB  LEU A 194      36.284  24.370  19.449  1.00145.01           C  
ATOM   1346  CG  LEU A 194      37.804  24.384  19.622  1.00149.04           C  
ATOM   1347  CD1 LEU A 194      38.206  25.341  20.736  1.00156.06           C  
ATOM   1348  CD2 LEU A 194      38.334  22.984  19.892  1.00145.61           C  
ATOM   1349  N   GLY A 195      35.708  25.994  16.826  1.00143.77           N  
ATOM   1350  CA  GLY A 195      36.139  26.570  15.566  1.00141.02           C  
ATOM   1351  C   GLY A 195      35.807  28.046  15.474  1.00134.81           C  
ATOM   1352  O   GLY A 195      36.544  28.822  14.867  1.00134.60           O  
ATOM   1353  N   VAL A 196      34.687  28.432  16.077  1.00132.66           N  
ATOM   1354  CA  VAL A 196      34.279  29.830  16.114  1.00135.06           C  
ATOM   1355  C   VAL A 196      35.268  30.654  16.929  1.00139.51           C  
ATOM   1356  O   VAL A 196      35.810  31.645  16.442  1.00138.81           O  
ATOM   1357  CB  VAL A 196      32.868  29.996  16.710  1.00131.73           C  
ATOM   1358  CG1 VAL A 196      32.596  31.455  17.032  1.00133.60           C  
ATOM   1359  CG2 VAL A 196      31.819  29.451  15.754  1.00131.36           C  
ATOM   1360  N   TYR A 197      35.502  30.236  18.169  1.00144.44           N  
ATOM   1361  CA  TYR A 197      36.435  30.934  19.046  1.00154.41           C  
ATOM   1362  C   TYR A 197      37.817  31.048  18.413  1.00157.11           C  
ATOM   1363  O   TYR A 197      38.577  31.966  18.721  1.00155.42           O  
ATOM   1364  CB  TYR A 197      36.533  30.236  20.404  1.00161.93           C  
ATOM   1365  CG  TYR A 197      35.264  30.302  21.223  1.00165.33           C  
ATOM   1366  CD1 TYR A 197      34.930  31.449  21.932  1.00165.60           C  
ATOM   1367  CD2 TYR A 197      34.402  29.216  21.292  1.00167.75           C  
ATOM   1368  CE1 TYR A 197      33.771  31.512  22.683  1.00166.29           C  
ATOM   1369  CE2 TYR A 197      33.242  29.270  22.040  1.00169.92           C  
ATOM   1370  CZ  TYR A 197      32.932  30.420  22.734  1.00169.79           C  
ATOM   1371  OH  TYR A 197      31.776  30.477  23.480  1.00171.60           O  
ATOM   1372  N   LEU A 198      38.140  30.110  17.529  1.00160.36           N  
ATOM   1373  CA  LEU A 198      39.416  30.139  16.824  1.00162.83           C  
ATOM   1374  C   LEU A 198      39.527  31.389  15.961  1.00166.55           C  
ATOM   1375  O   LEU A 198      40.567  32.044  15.933  1.00168.10           O  
ATOM   1376  CB  LEU A 198      39.586  28.890  15.957  1.00156.83           C  
ATOM   1377  CG  LEU A 198      39.790  27.561  16.687  1.00149.24           C  
ATOM   1378  CD1 LEU A 198      39.835  26.413  15.691  1.00152.85           C  
ATOM   1379  CD2 LEU A 198      41.056  27.597  17.529  1.00142.46           C  
ATOM   1380  N   ARG A 199      38.446  31.713  15.259  1.00168.27           N  
ATOM   1381  CA  ARG A 199      38.418  32.886  14.395  1.00174.89           C  
ATOM   1382  C   ARG A 199      38.264  34.164  15.217  1.00174.55           C  
ATOM   1383  O   ARG A 199      38.786  35.216  14.847  1.00172.27           O  
ATOM   1384  CB  ARG A 199      37.280  32.777  13.377  1.00179.04           C  
ATOM   1385  CG  ARG A 199      37.239  31.461  12.614  1.00181.33           C  
ATOM   1386  CD  ARG A 199      38.534  31.202  11.859  1.00189.49           C  
ATOM   1387  NE  ARG A 199      38.447  30.005  11.024  1.00196.56           N  
ATOM   1388  CZ  ARG A 199      38.749  28.777  11.438  1.00195.73           C  
ATOM   1389  NH1 ARG A 199      39.160  28.574  12.682  1.00196.58           N  
ATOM   1390  NH2 ARG A 199      38.639  27.749  10.606  1.00190.33           N  
ATOM   1391  N   ILE A 200      37.547  34.064  16.332  1.00173.32           N  
ATOM   1392  CA  ILE A 200      37.317  35.211  17.206  1.00171.66           C  
ATOM   1393  C   ILE A 200      38.622  35.822  17.702  1.00181.80           C  
ATOM   1394  O   ILE A 200      38.920  36.982  17.421  1.00187.80           O  
ATOM   1395  CB  ILE A 200      36.452  34.837  18.427  1.00160.20           C  
ATOM   1396  CG1 ILE A 200      35.035  34.465  17.989  1.00152.93           C  
ATOM   1397  CG2 ILE A 200      36.407  35.986  19.420  1.00159.17           C  
ATOM   1398  CD1 ILE A 200      34.095  34.188  19.141  1.00149.20           C  
ATOM   1399  N   PHE A 201      39.397  35.036  18.442  1.00184.47           N  
ATOM   1400  CA  PHE A 201      40.639  35.523  19.031  1.00190.07           C  
ATOM   1401  C   PHE A 201      41.723  35.754  17.983  1.00193.50           C  
ATOM   1402  O   PHE A 201      42.590  36.610  18.156  1.00196.91           O  
ATOM   1403  CB  PHE A 201      41.137  34.561  20.111  1.00190.16           C  
ATOM   1404  CG  PHE A 201      40.194  34.415  21.269  1.00190.13           C  
ATOM   1405  CD1 PHE A 201      40.236  35.304  22.331  1.00192.29           C  
ATOM   1406  CD2 PHE A 201      39.262  33.391  21.296  1.00186.37           C  
ATOM   1407  CE1 PHE A 201      39.368  35.173  23.397  1.00192.01           C  
ATOM   1408  CE2 PHE A 201      38.391  33.254  22.359  1.00185.19           C  
ATOM   1409  CZ  PHE A 201      38.444  34.147  23.411  1.00189.29           C  
ATOM   1410  N   ALA A 202      41.673  34.989  16.898  1.00193.05           N  
ATOM   1411  CA  ALA A 202      42.628  35.166  15.812  1.00196.17           C  
ATOM   1412  C   ALA A 202      42.438  36.528  15.155  1.00199.07           C  
ATOM   1413  O   ALA A 202      43.408  37.194  14.796  1.00202.49           O  
ATOM   1414  CB  ALA A 202      42.487  34.054  14.787  1.00194.86           C  
ATOM   1415  N   ALA A 203      41.182  36.938  15.007  1.00196.81           N  
ATOM   1416  CA  ALA A 203      40.862  38.230  14.410  1.00195.36           C  
ATOM   1417  C   ALA A 203      40.984  39.361  15.426  1.00194.64           C  
ATOM   1418  O   ALA A 203      41.428  40.459  15.093  1.00197.13           O  
ATOM   1419  CB  ALA A 203      39.467  38.208  13.801  1.00193.82           C  
ATOM   1420  N   ALA A 204      40.588  39.087  16.666  1.00192.61           N  
ATOM   1421  CA  ALA A 204      40.657  40.083  17.730  1.00194.92           C  
ATOM   1422  C   ALA A 204      42.078  40.608  17.914  1.00200.66           C  
ATOM   1423  O   ALA A 204      42.282  41.797  18.161  1.00205.94           O  
ATOM   1424  CB  ALA A 204      40.130  39.506  19.035  1.00191.16           C  
ATOM   1425  N   ARG A 205      43.056  39.717  17.793  1.00198.70           N  
ATOM   1426  CA  ARG A 205      44.457  40.099  17.927  1.00197.77           C  
ATOM   1427  C   ARG A 205      44.956  40.820  16.678  1.00194.95           C  
ATOM   1428  O   ARG A 205      45.925  41.577  16.735  1.00194.15           O  
ATOM   1429  CB  ARG A 205      45.331  38.879  18.232  1.00198.52           C  
ATOM   1430  CG  ARG A 205      45.391  38.501  19.709  1.00200.92           C  
ATOM   1431  CD  ARG A 205      44.006  38.248  20.286  1.00203.67           C  
ATOM   1432  NE  ARG A 205      44.052  37.844  21.689  1.00206.02           N  
ATOM   1433  CZ  ARG A 205      44.072  36.581  22.104  1.00204.64           C  
ATOM   1434  NH1 ARG A 205      44.049  35.591  21.222  1.00201.07           N  
ATOM   1435  NH2 ARG A 205      44.113  36.308  23.401  1.00204.61           N  
ATOM   1436  N   ARG A 206      44.289  40.582  15.553  1.00194.58           N  
ATOM   1437  CA  ARG A 206      44.605  41.292  14.319  1.00197.77           C  
ATOM   1438  C   ARG A 206      44.069  42.718  14.379  1.00198.39           C  
ATOM   1439  O   ARG A 206      44.675  43.643  13.837  1.00202.41           O  
ATOM   1440  CB  ARG A 206      44.033  40.560  13.102  1.00202.25           C  
ATOM   1441  CG  ARG A 206      44.681  39.212  12.826  1.00208.34           C  
ATOM   1442  CD  ARG A 206      44.347  38.709  11.427  1.00212.45           C  
ATOM   1443  NE  ARG A 206      42.920  38.455  11.249  1.00212.19           N  
ATOM   1444  CZ  ARG A 206      42.352  37.260  11.377  1.00206.22           C  
ATOM   1445  NH1 ARG A 206      43.089  36.202  11.684  1.00203.43           N  
ATOM   1446  NH2 ARG A 206      41.045  37.122  11.195  1.00203.48           N  
ATOM   1447  N   GLN A 207      42.930  42.888  15.043  1.00193.58           N  
ATOM   1448  CA  GLN A 207      42.355  44.210  15.248  1.00188.81           C  
ATOM   1449  C   GLN A 207      43.319  45.067  16.055  1.00189.76           C  
ATOM   1450  O   GLN A 207      43.534  46.238  15.746  1.00191.84           O  
ATOM   1451  CB  GLN A 207      41.015  44.108  15.981  1.00183.33           C  
ATOM   1452  CG  GLN A 207      39.971  43.266  15.266  1.00180.06           C  
ATOM   1453  CD  GLN A 207      39.531  43.872  13.949  1.00184.35           C  
ATOM   1454  OE1 GLN A 207      39.783  45.046  13.677  1.00193.99           O  
ATOM   1455  NE2 GLN A 207      38.864  43.073  13.124  1.00178.38           N  
ATOM   1456  N   LEU A 208      43.899  44.469  17.090  1.00192.27           N  
ATOM   1457  CA  LEU A 208      44.845  45.167  17.952  1.00200.32           C  
ATOM   1458  C   LEU A 208      46.141  45.492  17.217  1.00211.24           C  
ATOM   1459  O   LEU A 208      46.825  46.458  17.553  1.00218.83           O  
ATOM   1460  CB  LEU A 208      45.145  44.336  19.201  1.00198.53           C  
ATOM   1461  CG  LEU A 208      43.960  44.050  20.126  1.00197.25           C  
ATOM   1462  CD1 LEU A 208      44.372  43.119  21.255  1.00196.03           C  
ATOM   1463  CD2 LEU A 208      43.382  45.345  20.676  1.00199.19           C  
ATOM   1464  N   LYS A 209      46.476  44.684  16.216  1.00215.87           N  
ATOM   1465  CA  LYS A 209      47.685  44.910  15.432  1.00225.71           C  
ATOM   1466  C   LYS A 209      47.500  46.074  14.463  1.00235.29           C  
ATOM   1467  O   LYS A 209      48.408  46.881  14.268  1.00240.28           O  
ATOM   1468  CB  LYS A 209      48.090  43.645  14.672  1.00225.09           C  
ATOM   1469  CG  LYS A 209      49.388  43.788  13.890  1.00229.15           C  
ATOM   1470  CD  LYS A 209      49.767  42.493  13.190  1.00229.61           C  
ATOM   1471  CE  LYS A 209      51.071  42.645  12.421  1.00234.18           C  
ATOM   1472  NZ  LYS A 209      51.461  41.386  11.728  1.00233.19           N  
ATOM   1473  N   GLN A 210      46.320  46.153  13.855  1.00236.74           N  
ATOM   1474  CA  GLN A 210      45.994  47.265  12.971  1.00239.00           C  
ATOM   1475  C   GLN A 210      45.900  48.552  13.780  1.00238.71           C  
ATOM   1476  O   GLN A 210      46.233  49.632  13.293  1.00242.13           O  
ATOM   1477  CB  GLN A 210      44.678  47.005  12.239  1.00240.41           C  
ATOM   1478  CG  GLN A 210      44.685  45.757  11.374  1.00242.98           C  
ATOM   1479  CD  GLN A 210      43.381  45.563  10.627  1.00245.03           C  
ATOM   1480  OE1 GLN A 210      42.533  46.455  10.592  1.00246.46           O  
ATOM   1481  NE2 GLN A 210      43.214  44.392  10.021  1.00243.40           N  
ATOM   1482  N   MET A 211      45.442  48.424  15.021  1.00235.35           N  
ATOM   1483  CA  MET A 211      45.360  49.558  15.930  1.00236.27           C  
ATOM   1484  C   MET A 211      46.711  49.808  16.589  1.00240.96           C  
ATOM   1485  O   MET A 211      46.888  50.784  17.317  1.00248.24           O  
ATOM   1486  CB  MET A 211      44.292  49.315  16.996  1.00231.79           C  
ATOM   1487  CG  MET A 211      42.888  49.151  16.441  1.00230.39           C  
ATOM   1488  SD  MET A 211      41.664  48.952  17.747  1.00180.01           S  
ATOM   1489  CE  MET A 211      41.939  50.452  18.683  1.00277.84           C  
ATOM   1490  N   GLU A 212      47.660  48.915  16.333  1.00249.15           N  
ATOM   1491  CA  GLU A 212      49.016  49.067  16.846  1.00250.65           C  
ATOM   1492  C   GLU A 212      49.834  49.925  15.888  1.00245.50           C  
ATOM   1493  O   GLU A 212      50.862  50.490  16.262  1.00244.25           O  
ATOM   1494  CB  GLU A 212      49.674  47.698  17.030  1.00260.06           C  
ATOM   1495  CG  GLU A 212      51.069  47.744  17.630  1.00266.21           C  
ATOM   1496  CD  GLU A 212      51.667  46.362  17.819  1.00271.01           C  
ATOM   1497  OE1 GLU A 212      50.977  45.366  17.513  1.00272.06           O  
ATOM   1498  OE2 GLU A 212      52.827  46.271  18.275  1.00273.06           O  
ATOM   1499  N   SER A 213      49.361  50.022  14.650  1.00241.99           N  
ATOM   1500  CA  SER A 213      50.029  50.816  13.628  1.00239.03           C  
ATOM   1501  C   SER A 213      49.141  51.967  13.164  1.00232.84           C  
ATOM   1502  O   SER A 213      49.125  52.312  11.983  1.00230.52           O  
ATOM   1503  CB  SER A 213      50.414  49.938  12.435  1.00242.83           C  
ATOM   1504  OG  SER A 213      51.244  48.863  12.837  1.00246.36           O  
ATOM   1505  N   GLN A 214      48.400  52.553  14.099  1.00231.59           N  
ATOM   1506  CA  GLN A 214      47.520  53.674  13.785  1.00232.47           C  
ATOM   1507  C   GLN A 214      48.135  55.001  14.225  1.00238.36           C  
ATOM   1508  O   GLN A 214      48.694  55.100  15.318  1.00239.49           O  
ATOM   1509  CB  GLN A 214      46.147  53.483  14.433  1.00228.47           C  
ATOM   1510  CG  GLN A 214      46.183  53.372  15.947  1.00225.49           C  
ATOM   1511  CD  GLN A 214      44.805  53.184  16.552  1.00222.96           C  
ATOM   1512  OE1 GLN A 214      43.797  53.198  15.846  1.00223.93           O  
ATOM   1513  NE2 GLN A 214      44.756  53.007  17.868  1.00220.10           N  
ATOM   1514  N   PRO A 215      48.037  56.024  13.363  1.00240.99           N  
ATOM   1515  CA  PRO A 215      48.596  57.358  13.614  1.00241.65           C  
ATOM   1516  C   PRO A 215      47.840  58.127  14.697  1.00244.75           C  
ATOM   1517  O   PRO A 215      47.977  59.347  14.783  1.00242.99           O  
ATOM   1518  CB  PRO A 215      48.430  58.068  12.263  1.00238.23           C  
ATOM   1519  CG  PRO A 215      48.205  56.976  11.264  1.00238.47           C  
ATOM   1520  CD  PRO A 215      47.469  55.916  12.010  1.00240.89           C  
ATOM   1521  N   LEU A 216      47.055  57.425  15.508  1.00250.29           N  
ATOM   1522  CA  LEU A 216      46.281  58.071  16.564  1.00250.66           C  
ATOM   1523  C   LEU A 216      46.066  57.152  17.766  1.00246.77           C  
ATOM   1524  O   LEU A 216      46.070  55.929  17.626  1.00248.80           O  
ATOM   1525  CB  LEU A 216      44.939  58.574  16.017  1.00252.60           C  
ATOM   1526  CG  LEU A 216      44.109  57.631  15.139  1.00254.64           C  
ATOM   1527  CD1 LEU A 216      43.536  56.475  15.947  1.00255.62           C  
ATOM   1528  CD2 LEU A 216      42.992  58.399  14.448  1.00253.27           C  
ATOM   1529  N   PRO A 217      45.888  57.745  18.957  1.00239.45           N  
ATOM   1530  CA  PRO A 217      45.632  56.984  20.185  1.00236.74           C  
ATOM   1531  C   PRO A 217      44.389  56.105  20.065  1.00235.97           C  
ATOM   1532  O   PRO A 217      44.508  54.886  19.932  1.00242.06           O  
ATOM   1533  CB  PRO A 217      45.404  58.079  21.231  1.00231.56           C  
ATOM   1534  CG  PRO A 217      46.147  59.256  20.707  1.00230.72           C  
ATOM   1535  CD  PRO A 217      46.001  59.190  19.218  1.00233.14           C  
ATOM   1536  N   GLY A 218      43.213  56.723  20.114  1.00225.51           N  
ATOM   1537  CA  GLY A 218      41.961  55.999  19.987  1.00215.50           C  
ATOM   1538  C   GLY A 218      41.824  54.860  20.979  1.00207.94           C  
ATOM   1539  O   GLY A 218      41.648  53.705  20.591  1.00208.84           O  
ATOM   1540  N   GLU A 219      41.906  55.185  22.265  1.00199.16           N  
ATOM   1541  CA  GLU A 219      41.772  54.183  23.316  1.00192.41           C  
ATOM   1542  C   GLU A 219      40.315  53.783  23.512  1.00197.58           C  
ATOM   1543  O   GLU A 219      40.016  52.823  24.219  1.00201.07           O  
ATOM   1544  CB  GLU A 219      42.370  54.691  24.630  1.00184.55           C  
ATOM   1545  CG  GLU A 219      43.870  54.917  24.569  1.00182.92           C  
ATOM   1546  CD  GLU A 219      44.627  53.674  24.142  1.00180.71           C  
ATOM   1547  OE1 GLU A 219      45.598  53.803  23.367  1.00175.88           O  
ATOM   1548  OE2 GLU A 219      44.245  52.567  24.575  1.00184.82           O  
ATOM   1549  N   ARG A 220      39.413  54.529  22.883  1.00200.97           N  
ATOM   1550  CA  ARG A 220      37.995  54.193  22.908  1.00205.76           C  
ATOM   1551  C   ARG A 220      37.754  52.873  22.191  1.00207.22           C  
ATOM   1552  O   ARG A 220      37.010  52.019  22.671  1.00203.84           O  
ATOM   1553  CB  ARG A 220      37.171  55.303  22.255  1.00209.47           C  
ATOM   1554  CG  ARG A 220      36.845  56.454  23.185  1.00212.71           C  
ATOM   1555  CD  ARG A 220      35.766  56.064  24.180  1.00218.86           C  
ATOM   1556  NE  ARG A 220      35.548  57.102  25.182  1.00225.38           N  
ATOM   1557  CZ  ARG A 220      36.026  57.055  26.421  1.00232.37           C  
ATOM   1558  NH1 ARG A 220      36.744  56.012  26.816  1.00235.28           N  
ATOM   1559  NH2 ARG A 220      35.780  58.046  27.268  1.00233.75           N  
ATOM   1560  N   ALA A 221      38.393  52.713  21.037  1.00169.00           N  
ATOM   1561  CA  ALA A 221      38.268  51.490  20.257  1.00170.80           C  
ATOM   1562  C   ALA A 221      39.006  50.335  20.927  1.00170.01           C  
ATOM   1563  O   ALA A 221      38.528  49.203  20.926  1.00165.82           O  
ATOM   1564  CB  ALA A 221      38.778  51.706  18.843  1.00172.24           C  
ATOM   1565  N   ARG A 222      40.172  50.627  21.498  1.00174.09           N  
ATOM   1566  CA  ARG A 222      40.947  49.614  22.207  1.00174.46           C  
ATOM   1567  C   ARG A 222      40.218  49.131  23.454  1.00171.53           C  
ATOM   1568  O   ARG A 222      40.085  47.929  23.678  1.00176.26           O  
ATOM   1569  CB  ARG A 222      42.328  50.148  22.592  1.00180.10           C  
ATOM   1570  CG  ARG A 222      43.450  49.711  21.665  1.00186.35           C  
ATOM   1571  CD  ARG A 222      44.806  49.930  22.314  1.00193.36           C  
ATOM   1572  NE  ARG A 222      45.908  49.541  21.438  1.00204.43           N  
ATOM   1573  CZ  ARG A 222      46.617  50.394  20.706  1.00218.28           C  
ATOM   1574  NH1 ARG A 222      46.343  51.692  20.745  1.00223.03           N  
ATOM   1575  NH2 ARG A 222      47.603  49.951  19.938  1.00223.38           N  
ATOM   1576  N   SER A 223      39.749  50.074  24.265  1.00165.76           N  
ATOM   1577  CA  SER A 223      39.039  49.738  25.493  1.00166.52           C  
ATOM   1578  C   SER A 223      37.787  48.918  25.200  1.00167.20           C  
ATOM   1579  O   SER A 223      37.481  47.964  25.913  1.00165.20           O  
ATOM   1580  CB  SER A 223      38.672  51.005  26.268  1.00167.53           C  
ATOM   1581  OG  SER A 223      38.024  50.687  27.487  1.00166.82           O  
ATOM   1582  N   THR A 224      37.068  49.294  24.147  1.00170.06           N  
ATOM   1583  CA  THR A 224      35.863  48.576  23.744  1.00162.80           C  
ATOM   1584  C   THR A 224      36.208  47.191  23.207  1.00155.70           C  
ATOM   1585  O   THR A 224      35.539  46.205  23.518  1.00145.30           O  
ATOM   1586  CB  THR A 224      35.075  49.351  22.672  1.00162.65           C  
ATOM   1587  OG1 THR A 224      34.657  50.615  23.203  1.00158.92           O  
ATOM   1588  CG2 THR A 224      33.850  48.562  22.234  1.00160.86           C  
ATOM   1589  N   LEU A 225      37.259  47.128  22.397  1.00153.62           N  
ATOM   1590  CA  LEU A 225      37.719  45.870  21.825  1.00139.19           C  
ATOM   1591  C   LEU A 225      38.116  44.900  22.931  1.00134.05           C  
ATOM   1592  O   LEU A 225      37.722  43.736  22.915  1.00139.52           O  
ATOM   1593  CB  LEU A 225      38.901  46.123  20.884  1.00139.76           C  
ATOM   1594  CG  LEU A 225      39.330  45.020  19.912  1.00143.73           C  
ATOM   1595  CD1 LEU A 225      40.035  43.885  20.637  1.00151.24           C  
ATOM   1596  CD2 LEU A 225      38.132  44.506  19.128  1.00141.24           C  
ATOM   1597  N   GLN A 226      38.891  45.388  23.895  1.00137.11           N  
ATOM   1598  CA  GLN A 226      39.351  44.559  25.004  1.00147.97           C  
ATOM   1599  C   GLN A 226      38.195  44.098  25.886  1.00149.96           C  
ATOM   1600  O   GLN A 226      38.275  43.050  26.526  1.00152.95           O  
ATOM   1601  CB  GLN A 226      40.386  45.308  25.845  1.00158.35           C  
ATOM   1602  CG  GLN A 226      41.655  45.674  25.092  1.00166.07           C  
ATOM   1603  CD  GLN A 226      42.668  46.385  25.968  1.00166.45           C  
ATOM   1604  OE1 GLN A 226      42.611  46.301  27.195  1.00166.45           O  
ATOM   1605  NE2 GLN A 226      43.605  47.089  25.342  1.00166.09           N  
ATOM   1606  N   LYS A 227      37.125  44.886  25.922  1.00150.75           N  
ATOM   1607  CA  LYS A 227      35.942  44.526  26.697  1.00154.21           C  
ATOM   1608  C   LYS A 227      35.056  43.554  25.924  1.00153.79           C  
ATOM   1609  O   LYS A 227      34.343  42.743  26.517  1.00145.62           O  
ATOM   1610  CB  LYS A 227      35.150  45.774  27.095  1.00159.41           C  
ATOM   1611  CG  LYS A 227      35.854  46.650  28.119  1.00166.55           C  
ATOM   1612  CD  LYS A 227      35.026  47.878  28.468  1.00168.67           C  
ATOM   1613  CE  LYS A 227      35.754  48.767  29.466  1.00170.31           C  
ATOM   1614  NZ  LYS A 227      34.974  49.991  29.798  1.00168.20           N  
ATOM   1615  N   GLU A 228      35.106  43.642  24.599  1.00160.71           N  
ATOM   1616  CA  GLU A 228      34.395  42.702  23.741  1.00160.17           C  
ATOM   1617  C   GLU A 228      35.106  41.353  23.741  1.00155.03           C  
ATOM   1618  O   GLU A 228      34.475  40.305  23.608  1.00155.11           O  
ATOM   1619  CB  GLU A 228      34.294  43.244  22.314  1.00166.76           C  
ATOM   1620  CG  GLU A 228      33.354  44.428  22.163  1.00167.63           C  
ATOM   1621  CD  GLU A 228      31.900  44.043  22.352  1.00164.97           C  
ATOM   1622  OE1 GLU A 228      31.581  42.841  22.235  1.00164.42           O  
ATOM   1623  OE2 GLU A 228      31.074  44.943  22.612  1.00163.21           O  
ATOM   1624  N   VAL A 229      36.426  41.390  23.893  1.00149.83           N  
ATOM   1625  CA  VAL A 229      37.225  40.174  23.967  1.00145.85           C  
ATOM   1626  C   VAL A 229      37.084  39.521  25.338  1.00142.39           C  
ATOM   1627  O   VAL A 229      37.049  38.296  25.451  1.00147.63           O  
ATOM   1628  CB  VAL A 229      38.712  40.455  23.681  1.00147.75           C  
ATOM   1629  CG1 VAL A 229      39.556  39.226  23.983  1.00153.76           C  
ATOM   1630  CG2 VAL A 229      38.899  40.892  22.237  1.00146.65           C  
ATOM   1631  N   HIS A 230      37.000  40.345  26.378  1.00133.99           N  
ATOM   1632  CA  HIS A 230      36.816  39.843  27.735  1.00132.00           C  
ATOM   1633  C   HIS A 230      35.492  39.096  27.853  1.00131.82           C  
ATOM   1634  O   HIS A 230      35.385  38.115  28.590  1.00128.96           O  
ATOM   1635  CB  HIS A 230      36.868  40.988  28.748  1.00133.90           C  
ATOM   1636  CG  HIS A 230      36.727  40.545  30.172  1.00132.26           C  
ATOM   1637  ND1 HIS A 230      37.809  40.310  30.989  1.00131.90           N  
ATOM   1638  CD2 HIS A 230      35.626  40.295  30.922  1.00126.25           C  
ATOM   1639  CE1 HIS A 230      37.384  39.934  32.184  1.00124.59           C  
ATOM   1640  NE2 HIS A 230      36.064  39.917  32.168  1.00121.46           N  
ATOM   1641  N   ALA A 231      34.486  39.565  27.122  1.00136.61           N  
ATOM   1642  CA  ALA A 231      33.186  38.908  27.100  1.00130.85           C  
ATOM   1643  C   ALA A 231      33.249  37.631  26.271  1.00132.76           C  
ATOM   1644  O   ALA A 231      32.650  36.618  26.628  1.00137.70           O  
ATOM   1645  CB  ALA A 231      32.123  39.847  26.553  1.00127.42           C  
ATOM   1646  N   ALA A 232      33.982  37.688  25.163  1.00135.32           N  
ATOM   1647  CA  ALA A 232      34.152  36.529  24.295  1.00133.56           C  
ATOM   1648  C   ALA A 232      34.939  35.431  25.004  1.00131.90           C  
ATOM   1649  O   ALA A 232      34.679  34.243  24.812  1.00128.65           O  
ATOM   1650  CB  ALA A 232      34.843  36.931  23.002  1.00132.55           C  
ATOM   1651  N   LYS A 233      35.903  35.838  25.825  1.00134.12           N  
ATOM   1652  CA  LYS A 233      36.703  34.892  26.591  1.00134.56           C  
ATOM   1653  C   LYS A 233      35.870  34.259  27.699  1.00127.84           C  
ATOM   1654  O   LYS A 233      35.945  33.053  27.932  1.00133.56           O  
ATOM   1655  CB  LYS A 233      37.936  35.577  27.184  1.00143.28           C  
ATOM   1656  CG  LYS A 233      38.827  34.642  27.986  1.00151.51           C  
ATOM   1657  CD  LYS A 233      40.096  35.334  28.459  1.00159.66           C  
ATOM   1658  CE  LYS A 233      41.000  34.361  29.207  1.00163.49           C  
ATOM   1659  NZ  LYS A 233      42.279  34.989  29.641  1.00168.80           N  
ATOM   1660  N   SER A 234      35.076  35.080  28.378  1.00120.84           N  
ATOM   1661  CA  SER A 234      34.192  34.592  29.429  1.00119.17           C  
ATOM   1662  C   SER A 234      33.210  33.572  28.865  1.00115.50           C  
ATOM   1663  O   SER A 234      32.908  32.566  29.507  1.00110.27           O  
ATOM   1664  CB  SER A 234      33.434  35.752  30.075  1.00125.13           C  
ATOM   1665  OG  SER A 234      34.325  36.672  30.680  1.00131.38           O  
ATOM   1666  N   ALA A 235      32.716  33.840  27.661  1.00116.49           N  
ATOM   1667  CA  ALA A 235      31.798  32.931  26.987  1.00113.50           C  
ATOM   1668  C   ALA A 235      32.503  31.628  26.630  1.00113.04           C  
ATOM   1669  O   ALA A 235      31.899  30.556  26.654  1.00113.20           O  
ATOM   1670  CB  ALA A 235      31.227  33.585  25.739  1.00113.31           C  
ATOM   1671  N   ALA A 236      33.786  31.731  26.298  1.00113.39           N  
ATOM   1672  CA  ALA A 236      34.588  30.561  25.966  1.00110.67           C  
ATOM   1673  C   ALA A 236      34.780  29.678  27.192  1.00107.77           C  
ATOM   1674  O   ALA A 236      34.817  28.453  27.085  1.00113.94           O  
ATOM   1675  CB  ALA A 236      35.932  30.981  25.397  1.00115.20           C  
ATOM   1676  N   ILE A 237      34.902  30.308  28.356  1.00102.90           N  
ATOM   1677  CA  ILE A 237      35.078  29.575  29.603  1.00107.26           C  
ATOM   1678  C   ILE A 237      33.797  28.840  29.988  1.00112.80           C  
ATOM   1679  O   ILE A 237      33.844  27.734  30.525  1.00109.89           O  
ATOM   1680  CB  ILE A 237      35.506  30.502  30.755  1.00107.47           C  
ATOM   1681  CG1 ILE A 237      36.760  31.288  30.370  1.00109.35           C  
ATOM   1682  CG2 ILE A 237      35.756  29.699  32.020  1.00106.94           C  
ATOM   1683  CD1 ILE A 237      37.292  32.168  31.480  1.00103.92           C  
ATOM   1684  N   ILE A 238      32.655  29.459  29.707  1.00125.29           N  
ATOM   1685  CA  ILE A 238      31.364  28.838  29.978  1.00128.13           C  
ATOM   1686  C   ILE A 238      31.187  27.590  29.119  1.00129.60           C  
ATOM   1687  O   ILE A 238      30.773  26.539  29.610  1.00130.27           O  
ATOM   1688  CB  ILE A 238      30.200  29.809  29.704  1.00130.56           C  
ATOM   1689  CG1 ILE A 238      30.378  31.096  30.511  1.00140.40           C  
ATOM   1690  CG2 ILE A 238      28.869  29.152  30.035  1.00120.32           C  
ATOM   1691  CD1 ILE A 238      29.323  32.147  30.230  1.00147.43           C  
ATOM   1692  N   ALA A 239      31.507  27.713  27.835  1.00129.27           N  
ATOM   1693  CA  ALA A 239      31.392  26.598  26.904  1.00128.30           C  
ATOM   1694  C   ALA A 239      32.401  25.504  27.228  1.00135.04           C  
ATOM   1695  O   ALA A 239      32.083  24.316  27.174  1.00136.19           O  
ATOM   1696  CB  ALA A 239      31.579  27.082  25.478  1.00125.05           C  
ATOM   1697  N   GLY A 240      33.621  25.913  27.564  1.00137.30           N  
ATOM   1698  CA  GLY A 240      34.675  24.975  27.901  1.00135.50           C  
ATOM   1699  C   GLY A 240      34.288  24.065  29.049  1.00128.74           C  
ATOM   1700  O   GLY A 240      34.568  22.866  29.024  1.00126.74           O  
ATOM   1701  N   LEU A 241      33.639  24.636  30.058  1.00126.60           N  
ATOM   1702  CA  LEU A 241      33.216  23.871  31.224  1.00127.29           C  
ATOM   1703  C   LEU A 241      32.081  22.910  30.885  1.00128.24           C  
ATOM   1704  O   LEU A 241      31.845  21.942  31.604  1.00131.88           O  
ATOM   1705  CB  LEU A 241      32.793  24.804  32.360  1.00127.74           C  
ATOM   1706  CG  LEU A 241      33.885  25.702  32.944  1.00133.61           C  
ATOM   1707  CD1 LEU A 241      33.326  26.557  34.070  1.00137.71           C  
ATOM   1708  CD2 LEU A 241      35.061  24.872  33.431  1.00128.39           C  
ATOM   1709  N   PHE A 242      31.377  23.182  29.791  1.00123.37           N  
ATOM   1710  CA  PHE A 242      30.293  22.309  29.358  1.00119.91           C  
ATOM   1711  C   PHE A 242      30.849  20.979  28.861  1.00126.38           C  
ATOM   1712  O   PHE A 242      30.508  19.917  29.383  1.00125.26           O  
ATOM   1713  CB  PHE A 242      29.458  22.977  28.265  1.00116.58           C  
ATOM   1714  CG  PHE A 242      28.252  22.179  27.852  1.00121.86           C  
ATOM   1715  CD1 PHE A 242      27.015  22.419  28.428  1.00122.17           C  
ATOM   1716  CD2 PHE A 242      28.356  21.185  26.892  1.00129.37           C  
ATOM   1717  CE1 PHE A 242      25.904  21.685  28.052  1.00123.87           C  
ATOM   1718  CE2 PHE A 242      27.250  20.448  26.513  1.00131.53           C  
ATOM   1719  CZ  PHE A 242      26.022  20.699  27.093  1.00127.79           C  
ATOM   1720  N   ALA A 243      31.708  21.043  27.850  1.00128.37           N  
ATOM   1721  CA  ALA A 243      32.347  19.847  27.316  1.00124.17           C  
ATOM   1722  C   ALA A 243      33.148  19.137  28.402  1.00120.48           C  
ATOM   1723  O   ALA A 243      33.219  17.911  28.437  1.00121.68           O  
ATOM   1724  CB  ALA A 243      33.243  20.204  26.140  1.00126.82           C  
ATOM   1725  N   LEU A 244      33.745  19.921  29.293  1.00119.45           N  
ATOM   1726  CA  LEU A 244      34.566  19.379  30.369  1.00119.91           C  
ATOM   1727  C   LEU A 244      33.738  18.575  31.370  1.00115.57           C  
ATOM   1728  O   LEU A 244      34.265  17.708  32.066  1.00106.77           O  
ATOM   1729  CB  LEU A 244      35.310  20.510  31.086  1.00121.41           C  
ATOM   1730  CG  LEU A 244      36.309  20.115  32.175  1.00123.39           C  
ATOM   1731  CD1 LEU A 244      37.374  19.187  31.615  1.00132.19           C  
ATOM   1732  CD2 LEU A 244      36.942  21.351  32.795  1.00120.35           C  
ATOM   1733  N   CYS A 245      32.442  18.862  31.435  1.00125.61           N  
ATOM   1734  CA  CYS A 245      31.563  18.204  32.397  1.00137.27           C  
ATOM   1735  C   CYS A 245      30.669  17.156  31.743  1.00142.79           C  
ATOM   1736  O   CYS A 245      29.972  16.411  32.432  1.00141.91           O  
ATOM   1737  CB  CYS A 245      30.699  19.234  33.128  1.00138.37           C  
ATOM   1738  SG  CYS A 245      31.617  20.371  34.193  1.00176.92           S  
ATOM   1739  N   TRP A 246      30.691  17.100  30.416  1.00146.08           N  
ATOM   1740  CA  TRP A 246      29.850  16.156  29.687  1.00143.10           C  
ATOM   1741  C   TRP A 246      30.653  15.099  28.930  1.00137.14           C  
ATOM   1742  O   TRP A 246      30.192  13.971  28.763  1.00138.12           O  
ATOM   1743  CB  TRP A 246      28.901  16.897  28.740  1.00147.50           C  
ATOM   1744  CG  TRP A 246      27.799  17.615  29.459  1.00151.99           C  
ATOM   1745  CD1 TRP A 246      27.843  18.874  29.981  1.00157.26           C  
ATOM   1746  CD2 TRP A 246      26.489  17.109  29.741  1.00154.21           C  
ATOM   1747  NE1 TRP A 246      26.639  19.185  30.568  1.00158.12           N  
ATOM   1748  CE2 TRP A 246      25.791  18.118  30.435  1.00156.70           C  
ATOM   1749  CE3 TRP A 246      25.837  15.901  29.473  1.00154.99           C  
ATOM   1750  CZ2 TRP A 246      24.475  17.955  30.863  1.00158.62           C  
ATOM   1751  CZ3 TRP A 246      24.531  15.742  29.899  1.00153.31           C  
ATOM   1752  CH2 TRP A 246      23.864  16.763  30.587  1.00156.57           C  
ATOM   1753  N   LEU A 247      31.849  15.462  28.479  1.00132.93           N  
ATOM   1754  CA  LEU A 247      32.708  14.517  27.770  1.00132.69           C  
ATOM   1755  C   LEU A 247      32.928  13.226  28.558  1.00134.78           C  
ATOM   1756  O   LEU A 247      32.721  12.139  28.025  1.00135.27           O  
ATOM   1757  CB  LEU A 247      34.051  15.151  27.393  1.00129.35           C  
ATOM   1758  CG  LEU A 247      34.059  16.061  26.164  1.00125.22           C  
ATOM   1759  CD1 LEU A 247      35.470  16.546  25.872  1.00124.44           C  
ATOM   1760  CD2 LEU A 247      33.480  15.336  24.960  1.00125.60           C  
ATOM   1761  N   PRO A 248      33.344  13.341  29.831  1.00130.41           N  
ATOM   1762  CA  PRO A 248      33.573  12.143  30.646  1.00129.49           C  
ATOM   1763  C   PRO A 248      32.386  11.189  30.599  1.00125.60           C  
ATOM   1764  O   PRO A 248      32.570   9.985  30.428  1.00127.46           O  
ATOM   1765  CB  PRO A 248      33.725  12.709  32.059  1.00124.35           C  
ATOM   1766  CG  PRO A 248      34.240  14.080  31.852  1.00123.26           C  
ATOM   1767  CD  PRO A 248      33.592  14.577  30.594  1.00123.93           C  
ATOM   1768  N   LEU A 249      31.181  11.730  30.745  1.00122.20           N  
ATOM   1769  CA  LEU A 249      29.971  10.917  30.716  1.00115.71           C  
ATOM   1770  C   LEU A 249      29.750  10.265  29.350  1.00112.69           C  
ATOM   1771  O   LEU A 249      29.326   9.113  29.272  1.00106.70           O  
ATOM   1772  CB  LEU A 249      28.753  11.751  31.123  1.00109.57           C  
ATOM   1773  CG  LEU A 249      27.421  11.009  31.253  1.00 98.50           C  
ATOM   1774  CD1 LEU A 249      27.568   9.770  32.124  1.00107.79           C  
ATOM   1775  CD2 LEU A 249      26.345  11.931  31.803  1.00 74.21           C  
ATOM   1776  N   HIS A 250      30.037  10.999  28.278  1.00119.14           N  
ATOM   1777  CA  HIS A 250      29.911  10.455  26.929  1.00124.01           C  
ATOM   1778  C   HIS A 250      31.050   9.488  26.631  1.00126.88           C  
ATOM   1779  O   HIS A 250      30.841   8.437  26.029  1.00132.04           O  
ATOM   1780  CB  HIS A 250      29.885  11.573  25.885  1.00136.97           C  
ATOM   1781  CG  HIS A 250      28.634  12.398  25.909  1.00144.19           C  
ATOM   1782  ND1 HIS A 250      27.483  12.022  25.248  1.00147.27           N  
ATOM   1783  CD2 HIS A 250      28.358  13.581  26.504  1.00143.34           C  
ATOM   1784  CE1 HIS A 250      26.551  12.938  25.441  1.00143.79           C  
ATOM   1785  NE2 HIS A 250      27.054  13.894  26.200  1.00141.82           N  
ATOM   1786  N   ILE A 251      32.254   9.856  27.057  1.00125.02           N  
ATOM   1787  CA  ILE A 251      33.426   9.005  26.897  1.00126.48           C  
ATOM   1788  C   ILE A 251      33.160   7.621  27.475  1.00125.20           C  
ATOM   1789  O   ILE A 251      33.551   6.608  26.896  1.00127.52           O  
ATOM   1790  CB  ILE A 251      34.661   9.618  27.580  1.00125.33           C  
ATOM   1791  CG1 ILE A 251      35.125  10.860  26.817  1.00129.80           C  
ATOM   1792  CG2 ILE A 251      35.786   8.602  27.665  1.00125.44           C  
ATOM   1793  CD1 ILE A 251      36.342  11.531  27.416  1.00133.38           C  
ATOM   1794  N   ILE A 252      32.486   7.591  28.620  1.00122.62           N  
ATOM   1795  CA  ILE A 252      32.098   6.337  29.253  1.00118.15           C  
ATOM   1796  C   ILE A 252      31.208   5.503  28.333  1.00117.74           C  
ATOM   1797  O   ILE A 252      31.416   4.300  28.177  1.00124.89           O  
ATOM   1798  CB  ILE A 252      31.366   6.586  30.587  1.00111.67           C  
ATOM   1799  CG1 ILE A 252      32.361   7.026  31.662  1.00112.45           C  
ATOM   1800  CG2 ILE A 252      30.622   5.339  31.031  1.00105.94           C  
ATOM   1801  CD1 ILE A 252      31.751   7.169  33.040  1.00111.44           C  
ATOM   1802  N   ASN A 253      30.223   6.152  27.722  1.00115.52           N  
ATOM   1803  CA  ASN A 253      29.294   5.472  26.826  1.00123.32           C  
ATOM   1804  C   ASN A 253      29.945   5.031  25.519  1.00130.50           C  
ATOM   1805  O   ASN A 253      29.493   4.080  24.884  1.00133.12           O  
ATOM   1806  CB  ASN A 253      28.078   6.356  26.540  1.00126.49           C  
ATOM   1807  CG  ASN A 253      27.268   6.653  27.786  1.00126.31           C  
ATOM   1808  OD1 ASN A 253      27.505   6.075  28.847  1.00130.45           O  
ATOM   1809  ND2 ASN A 253      26.304   7.559  27.662  1.00120.60           N  
ATOM   1810  N   CYS A 254      31.005   5.726  25.120  1.00137.30           N  
ATOM   1811  CA  CYS A 254      31.742   5.363  23.916  1.00145.22           C  
ATOM   1812  C   CYS A 254      32.518   4.069  24.132  1.00146.80           C  
ATOM   1813  O   CYS A 254      32.667   3.262  23.214  1.00147.63           O  
ATOM   1814  CB  CYS A 254      32.693   6.488  23.504  1.00146.96           C  
ATOM   1815  SG  CYS A 254      31.862   7.996  22.962  1.00162.90           S  
ATOM   1816  N   PHE A 255      33.012   3.879  25.352  1.00143.93           N  
ATOM   1817  CA  PHE A 255      33.720   2.657  25.716  1.00143.26           C  
ATOM   1818  C   PHE A 255      32.761   1.472  25.767  1.00142.90           C  
ATOM   1819  O   PHE A 255      33.049   0.402  25.230  1.00146.73           O  
ATOM   1820  CB  PHE A 255      34.416   2.825  27.070  1.00138.56           C  
ATOM   1821  CG  PHE A 255      35.774   3.467  26.985  1.00143.48           C  
ATOM   1822  CD1 PHE A 255      35.971   4.617  26.237  1.00146.46           C  
ATOM   1823  CD2 PHE A 255      36.852   2.927  27.669  1.00144.93           C  
ATOM   1824  CE1 PHE A 255      37.220   5.208  26.162  1.00147.69           C  
ATOM   1825  CE2 PHE A 255      38.102   3.514  27.600  1.00145.85           C  
ATOM   1826  CZ  PHE A 255      38.286   4.655  26.846  1.00146.70           C  
ATOM   1827  N   THR A 256      31.618   1.673  26.415  1.00136.70           N  
ATOM   1828  CA  THR A 256      30.623   0.618  26.570  1.00134.06           C  
ATOM   1829  C   THR A 256      30.082   0.144  25.222  1.00136.92           C  
ATOM   1830  O   THR A 256      29.950  -1.056  24.984  1.00145.85           O  
ATOM   1831  CB  THR A 256      29.450   1.076  27.461  1.00125.15           C  
ATOM   1832  OG1 THR A 256      29.939   1.407  28.767  1.00116.66           O  
ATOM   1833  CG2 THR A 256      28.406  -0.024  27.579  1.00125.64           C  
ATOM   1834  N   PHE A 257      29.777   1.092  24.343  1.00130.95           N  
ATOM   1835  CA  PHE A 257      29.199   0.781  23.040  1.00130.46           C  
ATOM   1836  C   PHE A 257      30.225   0.214  22.064  1.00142.13           C  
ATOM   1837  O   PHE A 257      30.156  -0.955  21.689  1.00147.39           O  
ATOM   1838  CB  PHE A 257      28.550   2.030  22.438  1.00124.12           C  
ATOM   1839  CG  PHE A 257      27.933   1.804  21.085  1.00115.55           C  
ATOM   1840  CD1 PHE A 257      26.595   1.471  20.966  1.00105.40           C  
ATOM   1841  CD2 PHE A 257      28.689   1.933  19.931  1.00118.70           C  
ATOM   1842  CE1 PHE A 257      26.023   1.267  19.723  1.00106.52           C  
ATOM   1843  CE2 PHE A 257      28.123   1.729  18.686  1.00117.95           C  
ATOM   1844  CZ  PHE A 257      26.789   1.395  18.582  1.00112.25           C  
ATOM   1845  N   PHE A 258      31.170   1.051  21.649  1.00150.16           N  
ATOM   1846  CA  PHE A 258      32.159   0.658  20.648  1.00159.58           C  
ATOM   1847  C   PHE A 258      32.988  -0.546  21.086  1.00159.06           C  
ATOM   1848  O   PHE A 258      33.503  -1.292  20.251  1.00162.10           O  
ATOM   1849  CB  PHE A 258      33.078   1.832  20.301  1.00163.80           C  
ATOM   1850  CG  PHE A 258      32.393   2.937  19.551  1.00164.08           C  
ATOM   1851  CD1 PHE A 258      31.948   4.069  20.212  1.00166.10           C  
ATOM   1852  CD2 PHE A 258      32.193   2.841  18.184  1.00166.57           C  
ATOM   1853  CE1 PHE A 258      31.318   5.086  19.526  1.00171.22           C  
ATOM   1854  CE2 PHE A 258      31.562   3.854  17.490  1.00170.34           C  
ATOM   1855  CZ  PHE A 258      31.124   4.979  18.162  1.00173.96           C  
ATOM   1856  N   CYS A 259      33.116  -0.731  22.395  1.00183.67           N  
ATOM   1857  CA  CYS A 259      33.891  -1.843  22.927  1.00182.90           C  
ATOM   1858  C   CYS A 259      33.096  -2.635  23.962  1.00181.67           C  
ATOM   1859  O   CYS A 259      33.209  -2.385  25.163  1.00183.87           O  
ATOM   1860  CB  CYS A 259      35.201  -1.339  23.538  1.00179.67           C  
ATOM   1861  SG  CYS A 259      36.336  -2.651  24.049  1.00389.77           S  
ATOM   1862  N   PRO A 260      32.283  -3.594  23.493  1.00174.25           N  
ATOM   1863  CA  PRO A 260      31.481  -4.442  24.381  1.00176.00           C  
ATOM   1864  C   PRO A 260      32.371  -5.242  25.322  1.00178.56           C  
ATOM   1865  O   PRO A 260      31.936  -5.622  26.409  1.00178.90           O  
ATOM   1866  CB  PRO A 260      30.761  -5.382  23.410  1.00175.65           C  
ATOM   1867  CG  PRO A 260      30.757  -4.658  22.107  1.00173.67           C  
ATOM   1868  CD  PRO A 260      32.050  -3.907  22.074  1.00171.12           C  
ATOM   1869  N   ASP A 261      33.606  -5.494  24.902  1.00179.09           N  
ATOM   1870  CA  ASP A 261      34.565  -6.207  25.737  1.00178.07           C  
ATOM   1871  C   ASP A 261      35.035  -5.333  26.894  1.00177.38           C  
ATOM   1872  O   ASP A 261      35.178  -5.805  28.023  1.00177.66           O  
ATOM   1873  CB  ASP A 261      35.762  -6.676  24.908  1.00177.38           C  
ATOM   1874  CG  ASP A 261      35.416  -7.829  23.984  1.00174.38           C  
ATOM   1875  OD1 ASP A 261      34.294  -8.368  24.095  1.00171.36           O  
ATOM   1876  OD2 ASP A 261      36.269  -8.199  23.149  1.00172.12           O  
ATOM   1877  N   CYS A 262      35.270  -4.057  26.605  1.00175.08           N  
ATOM   1878  CA  CYS A 262      35.731  -3.112  27.615  1.00172.43           C  
ATOM   1879  C   CYS A 262      34.802  -3.112  28.823  1.00166.89           C  
ATOM   1880  O   CYS A 262      33.621  -2.780  28.708  1.00167.12           O  
ATOM   1881  CB  CYS A 262      35.832  -1.703  27.025  1.00177.74           C  
ATOM   1882  SG  CYS A 262      36.984  -1.557  25.636  1.00147.05           S  
ATOM   1883  N   SER A 263      35.346  -3.492  29.977  1.00159.19           N  
ATOM   1884  CA  SER A 263      34.573  -3.585  31.211  1.00156.00           C  
ATOM   1885  C   SER A 263      33.584  -2.434  31.352  1.00161.74           C  
ATOM   1886  O   SER A 263      33.979  -1.275  31.479  1.00165.79           O  
ATOM   1887  CB  SER A 263      35.503  -3.635  32.427  1.00155.86           C  
ATOM   1888  OG  SER A 263      36.343  -2.495  32.476  1.00166.61           O  
ATOM   1889  N   HIS A 264      32.296  -2.761  31.320  1.00160.66           N  
ATOM   1890  CA  HIS A 264      31.250  -1.756  31.454  1.00164.43           C  
ATOM   1891  C   HIS A 264      31.487  -0.919  32.706  1.00164.69           C  
ATOM   1892  O   HIS A 264      31.689  -1.459  33.795  1.00161.90           O  
ATOM   1893  CB  HIS A 264      29.867  -2.412  31.506  1.00166.22           C  
ATOM   1894  CG  HIS A 264      29.572  -3.299  30.336  1.00166.05           C  
ATOM   1895  ND1 HIS A 264      29.256  -2.807  29.088  1.00170.71           N  
ATOM   1896  CD2 HIS A 264      29.534  -4.649  30.228  1.00162.59           C  
ATOM   1897  CE1 HIS A 264      29.043  -3.814  28.259  1.00133.78           C  
ATOM   1898  NE2 HIS A 264      29.205  -4.943  28.927  1.00132.10           N  
ATOM   1899  N   ALA A 265      31.468   0.400  32.542  1.00168.78           N  
ATOM   1900  CA  ALA A 265      31.747   1.320  33.639  1.00169.28           C  
ATOM   1901  C   ALA A 265      30.933   0.994  34.888  1.00159.61           C  
ATOM   1902  O   ALA A 265      29.715   0.826  34.816  1.00150.38           O  
ATOM   1903  CB  ALA A 265      31.494   2.754  33.200  1.00173.53           C  
ATOM   1904  N   PRO A 266      31.613   0.901  36.042  1.00157.98           N  
ATOM   1905  CA  PRO A 266      30.975   0.622  37.333  1.00161.29           C  
ATOM   1906  C   PRO A 266      29.928   1.676  37.678  1.00180.46           C  
ATOM   1907  O   PRO A 266      29.837   2.696  36.996  1.00189.81           O  
ATOM   1908  CB  PRO A 266      32.141   0.695  38.330  1.00152.21           C  
ATOM   1909  CG  PRO A 266      33.255   1.379  37.599  1.00149.48           C  
ATOM   1910  CD  PRO A 266      33.074   1.026  36.164  1.00152.74           C  
ATOM   1911  N   LEU A 267      29.150   1.429  38.727  1.00189.53           N  
ATOM   1912  CA  LEU A 267      28.103   2.361  39.134  1.00200.17           C  
ATOM   1913  C   LEU A 267      28.671   3.542  39.917  1.00215.96           C  
ATOM   1914  O   LEU A 267      28.220   4.678  39.760  1.00217.61           O  
ATOM   1915  CB  LEU A 267      27.031   1.642  39.955  1.00196.11           C  
ATOM   1916  CG  LEU A 267      26.305   0.499  39.241  1.00196.42           C  
ATOM   1917  CD1 LEU A 267      25.303  -0.170  40.170  1.00199.57           C  
ATOM   1918  CD2 LEU A 267      25.620   1.002  37.978  1.00191.69           C  
ATOM   1919  N   TRP A 268      29.664   3.271  40.758  1.00132.33           N  
ATOM   1920  CA  TRP A 268      30.290   4.315  41.560  1.00143.68           C  
ATOM   1921  C   TRP A 268      31.035   5.305  40.670  1.00144.38           C  
ATOM   1922  O   TRP A 268      31.291   6.440  41.066  1.00148.56           O  
ATOM   1923  CB  TRP A 268      31.247   3.702  42.581  1.00154.56           C  
ATOM   1924  CG  TRP A 268      32.413   3.011  41.953  1.00164.74           C  
ATOM   1925  CD1 TRP A 268      32.492   1.698  41.592  1.00169.78           C  
ATOM   1926  CD2 TRP A 268      33.669   3.601  41.603  1.00168.86           C  
ATOM   1927  NE1 TRP A 268      33.723   1.433  41.041  1.00173.60           N  
ATOM   1928  CE2 TRP A 268      34.464   2.586  41.036  1.00173.88           C  
ATOM   1929  CE3 TRP A 268      34.200   4.890  41.716  1.00166.71           C  
ATOM   1930  CZ2 TRP A 268      35.760   2.819  40.584  1.00175.33           C  
ATOM   1931  CZ3 TRP A 268      35.486   5.119  41.266  1.00168.05           C  
ATOM   1932  CH2 TRP A 268      36.252   4.089  40.707  1.00172.53           C  
ATOM   1933  N   LEU A 269      31.388   4.861  39.468  1.00139.90           N  
ATOM   1934  CA  LEU A 269      32.045   5.722  38.493  1.00134.19           C  
ATOM   1935  C   LEU A 269      31.011   6.300  37.539  1.00126.53           C  
ATOM   1936  O   LEU A 269      31.230   7.344  36.922  1.00128.24           O  
ATOM   1937  CB  LEU A 269      33.098   4.942  37.709  1.00133.86           C  
ATOM   1938  CG  LEU A 269      33.874   5.743  36.665  1.00133.60           C  
ATOM   1939  CD1 LEU A 269      34.627   6.889  37.323  1.00136.70           C  
ATOM   1940  CD2 LEU A 269      34.826   4.844  35.895  1.00136.22           C  
ATOM   1941  N   MET A 270      29.881   5.611  37.420  1.00120.56           N  
ATOM   1942  CA  MET A 270      28.803   6.060  36.551  1.00122.83           C  
ATOM   1943  C   MET A 270      28.127   7.311  37.104  1.00128.12           C  
ATOM   1944  O   MET A 270      27.944   8.295  36.386  1.00129.52           O  
ATOM   1945  CB  MET A 270      27.773   4.948  36.355  1.00124.24           C  
ATOM   1946  CG  MET A 270      26.678   5.293  35.361  1.00125.59           C  
ATOM   1947  SD  MET A 270      27.318   5.596  33.701  1.00169.15           S  
ATOM   1948  CE  MET A 270      28.076   4.015  33.336  1.00105.89           C  
ATOM   1949  N   TYR A 271      27.760   7.273  38.381  1.00130.59           N  
ATOM   1950  CA  TYR A 271      27.087   8.404  39.006  1.00134.40           C  
ATOM   1951  C   TYR A 271      27.991   9.635  39.005  1.00130.97           C  
ATOM   1952  O   TYR A 271      27.518  10.760  38.847  1.00132.42           O  
ATOM   1953  CB  TYR A 271      26.655   8.063  40.436  1.00145.27           C  
ATOM   1954  CG  TYR A 271      27.709   8.344  41.482  1.00156.71           C  
ATOM   1955  CD1 TYR A 271      27.924   9.638  41.950  1.00160.79           C  
ATOM   1956  CD2 TYR A 271      28.483   7.319  42.009  1.00162.28           C  
ATOM   1957  CE1 TYR A 271      28.888   9.901  42.905  1.00165.06           C  
ATOM   1958  CE2 TYR A 271      29.445   7.574  42.966  1.00169.31           C  
ATOM   1959  CZ  TYR A 271      29.644   8.865  43.410  1.00171.04           C  
ATOM   1960  OH  TYR A 271      30.604   9.117  44.364  1.00176.44           O  
ATOM   1961  N   LEU A 272      29.291   9.413  39.184  1.00120.71           N  
ATOM   1962  CA  LEU A 272      30.256  10.504  39.229  1.00108.63           C  
ATOM   1963  C   LEU A 272      30.211  11.306  37.937  1.00103.16           C  
ATOM   1964  O   LEU A 272      30.326  12.533  37.952  1.00111.02           O  
ATOM   1965  CB  LEU A 272      31.664   9.961  39.472  1.00108.13           C  
ATOM   1966  CG  LEU A 272      32.785  10.979  39.692  1.00109.92           C  
ATOM   1967  CD1 LEU A 272      33.907  10.365  40.514  1.00108.09           C  
ATOM   1968  CD2 LEU A 272      33.320  11.532  38.374  1.00109.92           C  
ATOM   1969  N   ALA A 273      30.045  10.607  36.820  1.00 96.07           N  
ATOM   1970  CA  ALA A 273      29.948  11.257  35.522  1.00 94.79           C  
ATOM   1971  C   ALA A 273      28.581  11.911  35.362  1.00101.22           C  
ATOM   1972  O   ALA A 273      28.436  12.900  34.644  1.00102.45           O  
ATOM   1973  CB  ALA A 273      30.193  10.254  34.411  1.00 87.63           C  
ATOM   1974  N   ILE A 274      27.584  11.351  36.041  1.00104.98           N  
ATOM   1975  CA  ILE A 274      26.231  11.893  36.017  1.00107.27           C  
ATOM   1976  C   ILE A 274      26.142  13.137  36.897  1.00111.65           C  
ATOM   1977  O   ILE A 274      25.553  14.147  36.505  1.00115.98           O  
ATOM   1978  CB  ILE A 274      25.203  10.855  36.492  1.00109.22           C  
ATOM   1979  CG1 ILE A 274      25.280   9.594  35.628  1.00115.73           C  
ATOM   1980  CG2 ILE A 274      23.801  11.438  36.461  1.00 98.49           C  
ATOM   1981  CD1 ILE A 274      24.333   8.496  36.062  1.00117.19           C  
ATOM   1982  N   VAL A 275      26.726  13.056  38.089  1.00109.51           N  
ATOM   1983  CA  VAL A 275      26.772  14.191  39.000  1.00107.49           C  
ATOM   1984  C   VAL A 275      27.594  15.317  38.388  1.00111.84           C  
ATOM   1985  O   VAL A 275      27.260  16.493  38.536  1.00119.66           O  
ATOM   1986  CB  VAL A 275      27.381  13.799  40.359  1.00100.85           C  
ATOM   1987  CG1 VAL A 275      27.567  15.027  41.238  1.00 93.79           C  
ATOM   1988  CG2 VAL A 275      26.505  12.769  41.054  1.00 99.01           C  
ATOM   1989  N   LEU A 276      28.667  14.949  37.693  1.00107.67           N  
ATOM   1990  CA  LEU A 276      29.524  15.928  37.037  1.00110.71           C  
ATOM   1991  C   LEU A 276      28.733  16.763  36.034  1.00118.38           C  
ATOM   1992  O   LEU A 276      28.941  17.971  35.916  1.00127.20           O  
ATOM   1993  CB  LEU A 276      30.694  15.234  36.339  1.00106.64           C  
ATOM   1994  CG  LEU A 276      31.735  16.158  35.706  1.00106.99           C  
ATOM   1995  CD1 LEU A 276      32.301  17.115  36.744  1.00109.93           C  
ATOM   1996  CD2 LEU A 276      32.847  15.350  35.056  1.00109.20           C  
ATOM   1997  N   ALA A 277      27.823  16.112  35.317  1.00114.39           N  
ATOM   1998  CA  ALA A 277      26.990  16.795  34.333  1.00112.14           C  
ATOM   1999  C   ALA A 277      25.989  17.729  35.007  1.00116.51           C  
ATOM   2000  O   ALA A 277      25.683  18.803  34.489  1.00111.46           O  
ATOM   2001  CB  ALA A 277      26.268  15.784  33.457  1.00107.27           C  
ATOM   2002  N   HIS A 278      25.481  17.310  36.162  1.00125.49           N  
ATOM   2003  CA  HIS A 278      24.516  18.107  36.908  1.00129.79           C  
ATOM   2004  C   HIS A 278      25.181  19.308  37.566  1.00128.93           C  
ATOM   2005  O   HIS A 278      24.511  20.262  37.958  1.00134.14           O  
ATOM   2006  CB  HIS A 278      23.819  17.257  37.971  1.00132.54           C  
ATOM   2007  CG  HIS A 278      23.001  16.137  37.409  1.00123.80           C  
ATOM   2008  ND1 HIS A 278      22.792  14.956  38.088  1.00118.61           N  
ATOM   2009  CD2 HIS A 278      22.344  16.016  36.231  1.00116.96           C  
ATOM   2010  CE1 HIS A 278      22.036  14.158  37.355  1.00115.88           C  
ATOM   2011  NE2 HIS A 278      21.753  14.776  36.223  1.00113.05           N  
ATOM   2012  N   THR A 279      26.503  19.253  37.687  1.00124.70           N  
ATOM   2013  CA  THR A 279      27.264  20.331  38.306  1.00127.70           C  
ATOM   2014  C   THR A 279      27.410  21.522  37.361  1.00126.67           C  
ATOM   2015  O   THR A 279      27.526  22.667  37.800  1.00123.54           O  
ATOM   2016  CB  THR A 279      28.659  19.847  38.745  1.00128.54           C  
ATOM   2017  OG1 THR A 279      28.518  18.801  39.714  1.00134.44           O  
ATOM   2018  CG2 THR A 279      29.460  20.987  39.355  1.00128.79           C  
ATOM   2019  N   ASN A 280      27.394  21.242  36.062  1.00127.32           N  
ATOM   2020  CA  ASN A 280      27.568  22.273  35.046  1.00130.02           C  
ATOM   2021  C   ASN A 280      26.578  23.428  35.190  1.00136.08           C  
ATOM   2022  O   ASN A 280      26.926  24.587  34.960  1.00146.92           O  
ATOM   2023  CB  ASN A 280      27.459  21.660  33.649  1.00131.15           C  
ATOM   2024  CG  ASN A 280      27.873  22.621  32.553  1.00132.96           C  
ATOM   2025  OD1 ASN A 280      28.333  23.731  32.823  1.00138.15           O  
ATOM   2026  ND2 ASN A 280      27.717  22.197  31.306  1.00128.20           N  
ATOM   2027  N   SER A 281      25.346  23.110  35.573  1.00132.16           N  
ATOM   2028  CA  SER A 281      24.306  24.124  35.711  1.00130.18           C  
ATOM   2029  C   SER A 281      24.616  25.104  36.841  1.00128.57           C  
ATOM   2030  O   SER A 281      24.065  26.204  36.890  1.00127.76           O  
ATOM   2031  CB  SER A 281      22.947  23.464  35.953  1.00128.15           C  
ATOM   2032  OG  SER A 281      22.932  22.780  37.193  1.00131.62           O  
ATOM   2033  N   VAL A 282      25.509  24.700  37.739  1.00126.42           N  
ATOM   2034  CA  VAL A 282      25.818  25.486  38.930  1.00129.98           C  
ATOM   2035  C   VAL A 282      26.967  26.476  38.719  1.00139.74           C  
ATOM   2036  O   VAL A 282      26.975  27.561  39.305  1.00146.70           O  
ATOM   2037  CB  VAL A 282      26.140  24.566  40.131  1.00123.38           C  
ATOM   2038  CG1 VAL A 282      26.638  25.378  41.315  1.00123.96           C  
ATOM   2039  CG2 VAL A 282      24.915  23.749  40.515  1.00120.07           C  
ATOM   2040  N   VAL A 283      27.926  26.107  37.877  1.00140.22           N  
ATOM   2041  CA  VAL A 283      29.132  26.911  37.692  1.00142.47           C  
ATOM   2042  C   VAL A 283      28.869  28.266  37.037  1.00143.04           C  
ATOM   2043  O   VAL A 283      29.623  29.217  37.244  1.00147.02           O  
ATOM   2044  CB  VAL A 283      30.192  26.157  36.865  1.00140.65           C  
ATOM   2045  CG1 VAL A 283      30.547  24.841  37.536  1.00140.72           C  
ATOM   2046  CG2 VAL A 283      29.693  25.924  35.448  1.00137.41           C  
ATOM   2047  N   ASN A 284      27.802  28.353  36.250  1.00136.96           N  
ATOM   2048  CA  ASN A 284      27.491  29.579  35.518  1.00133.72           C  
ATOM   2049  C   ASN A 284      27.268  30.802  36.411  1.00131.24           C  
ATOM   2050  O   ASN A 284      27.936  31.820  36.245  1.00124.30           O  
ATOM   2051  CB  ASN A 284      26.298  29.366  34.582  1.00129.72           C  
ATOM   2052  CG  ASN A 284      26.575  28.328  33.516  1.00127.22           C  
ATOM   2053  OD1 ASN A 284      27.725  28.101  33.139  1.00124.16           O  
ATOM   2054  ND2 ASN A 284      25.520  27.691  33.021  1.00130.31           N  
ATOM   2055  N   PRO A 285      26.328  30.706  37.364  1.00134.70           N  
ATOM   2056  CA  PRO A 285      26.067  31.847  38.248  1.00132.28           C  
ATOM   2057  C   PRO A 285      27.341  32.356  38.915  1.00128.61           C  
ATOM   2058  O   PRO A 285      27.478  33.557  39.145  1.00136.81           O  
ATOM   2059  CB  PRO A 285      25.121  31.263  39.300  1.00137.98           C  
ATOM   2060  CG  PRO A 285      24.438  30.140  38.603  1.00141.30           C  
ATOM   2061  CD  PRO A 285      25.460  29.556  37.675  1.00140.52           C  
ATOM   2062  N   PHE A 286      28.262  31.446  39.216  1.00118.82           N  
ATOM   2063  CA  PHE A 286      29.515  31.811  39.866  1.00116.90           C  
ATOM   2064  C   PHE A 286      30.542  32.331  38.867  1.00104.72           C  
ATOM   2065  O   PHE A 286      31.408  33.132  39.217  1.00 84.12           O  
ATOM   2066  CB  PHE A 286      30.090  30.619  40.634  1.00124.32           C  
ATOM   2067  CG  PHE A 286      29.245  30.180  41.793  1.00130.59           C  
ATOM   2068  CD1 PHE A 286      28.272  29.210  41.629  1.00133.16           C  
ATOM   2069  CD2 PHE A 286      29.424  30.738  43.048  1.00132.20           C  
ATOM   2070  CE1 PHE A 286      27.493  28.804  42.696  1.00137.71           C  
ATOM   2071  CE2 PHE A 286      28.648  30.336  44.118  1.00135.61           C  
ATOM   2072  CZ  PHE A 286      27.681  29.368  43.942  1.00139.40           C  
ATOM   2073  N   ILE A 287      30.443  31.872  37.624  1.00114.23           N  
ATOM   2074  CA  ILE A 287      31.371  32.305  36.587  1.00125.81           C  
ATOM   2075  C   ILE A 287      31.011  33.704  36.101  1.00130.10           C  
ATOM   2076  O   ILE A 287      31.837  34.392  35.505  1.00140.51           O  
ATOM   2077  CB  ILE A 287      31.395  31.335  35.392  1.00132.86           C  
ATOM   2078  CG1 ILE A 287      32.698  31.488  34.605  1.00135.36           C  
ATOM   2079  CG2 ILE A 287      30.199  31.566  34.485  1.00134.96           C  
ATOM   2080  CD1 ILE A 287      32.773  30.599  33.386  1.00134.97           C  
ATOM   2081  N   TYR A 288      29.773  34.117  36.357  1.00119.56           N  
ATOM   2082  CA  TYR A 288      29.333  35.466  36.021  1.00103.52           C  
ATOM   2083  C   TYR A 288      29.769  36.447  37.100  1.00 93.39           C  
ATOM   2084  O   TYR A 288      30.289  37.522  36.802  1.00 91.10           O  
ATOM   2085  CB  TYR A 288      27.814  35.517  35.849  1.00103.68           C  
ATOM   2086  CG  TYR A 288      27.305  34.725  34.668  1.00110.95           C  
ATOM   2087  CD1 TYR A 288      27.761  34.990  33.385  1.00113.56           C  
ATOM   2088  CD2 TYR A 288      26.361  33.721  34.834  1.00115.65           C  
ATOM   2089  CE1 TYR A 288      27.299  34.272  32.300  1.00115.03           C  
ATOM   2090  CE2 TYR A 288      25.893  32.997  33.755  1.00117.62           C  
ATOM   2091  CZ  TYR A 288      26.365  33.277  32.490  1.00117.95           C  
ATOM   2092  OH  TYR A 288      25.902  32.561  31.410  1.00118.27           O  
ATOM   2093  N   ALA A 289      29.555  36.066  38.354  1.00 90.51           N  
ATOM   2094  CA  ALA A 289      29.939  36.896  39.488  1.00 93.41           C  
ATOM   2095  C   ALA A 289      31.449  37.119  39.535  1.00111.29           C  
ATOM   2096  O   ALA A 289      31.922  38.103  40.101  1.00121.85           O  
ATOM   2097  CB  ALA A 289      29.452  36.273  40.788  1.00 85.59           C  
ATOM   2098  N   TYR A 290      32.204  36.205  38.938  1.00121.86           N  
ATOM   2099  CA  TYR A 290      33.659  36.307  38.947  1.00132.33           C  
ATOM   2100  C   TYR A 290      34.198  37.038  37.719  1.00123.11           C  
ATOM   2101  O   TYR A 290      35.006  37.959  37.841  1.00122.80           O  
ATOM   2102  CB  TYR A 290      34.299  34.919  39.057  1.00146.11           C  
ATOM   2103  CG  TYR A 290      35.806  34.937  38.915  1.00158.58           C  
ATOM   2104  CD1 TYR A 290      36.627  35.108  40.023  1.00164.17           C  
ATOM   2105  CD2 TYR A 290      36.406  34.791  37.671  1.00160.20           C  
ATOM   2106  CE1 TYR A 290      38.005  35.129  39.894  1.00165.28           C  
ATOM   2107  CE2 TYR A 290      37.781  34.812  37.533  1.00161.80           C  
ATOM   2108  CZ  TYR A 290      38.576  34.980  38.647  1.00164.12           C  
ATOM   2109  OH  TYR A 290      39.946  35.000  38.512  1.00164.28           O  
ATOM   2110  N   ARG A 291      33.751  36.621  36.539  1.00117.19           N  
ATOM   2111  CA  ARG A 291      34.246  37.183  35.286  1.00121.21           C  
ATOM   2112  C   ARG A 291      33.697  38.577  35.008  1.00131.28           C  
ATOM   2113  O   ARG A 291      34.440  39.481  34.627  1.00145.81           O  
ATOM   2114  CB  ARG A 291      33.921  36.252  34.117  1.00122.40           C  
ATOM   2115  CG  ARG A 291      34.746  34.978  34.097  1.00129.98           C  
ATOM   2116  CD  ARG A 291      36.205  35.282  33.802  1.00132.34           C  
ATOM   2117  NE  ARG A 291      36.375  35.864  32.474  1.00129.38           N  
ATOM   2118  CZ  ARG A 291      37.549  36.199  31.949  1.00129.52           C  
ATOM   2119  NH1 ARG A 291      38.664  36.013  32.642  1.00132.75           N  
ATOM   2120  NH2 ARG A 291      37.609  36.722  30.732  1.00124.91           N  
ATOM   2121  N   ILE A 292      32.393  38.748  35.195  1.00122.63           N  
ATOM   2122  CA  ILE A 292      31.756  40.028  34.911  1.00113.66           C  
ATOM   2123  C   ILE A 292      31.602  40.890  36.162  1.00116.97           C  
ATOM   2124  O   ILE A 292      30.837  40.561  37.069  1.00107.69           O  
ATOM   2125  CB  ILE A 292      30.389  39.844  34.230  1.00100.78           C  
ATOM   2126  CG1 ILE A 292      30.551  39.046  32.934  1.00 96.52           C  
ATOM   2127  CG2 ILE A 292      29.751  41.193  33.949  1.00107.85           C  
ATOM   2128  CD1 ILE A 292      29.280  38.920  32.125  1.00 99.50           C  
ATOM   2129  N   ARG A 293      32.338  41.997  36.195  1.00161.66           N  
ATOM   2130  CA  ARG A 293      32.290  42.930  37.315  1.00171.53           C  
ATOM   2131  C   ARG A 293      30.930  43.618  37.409  1.00163.85           C  
ATOM   2132  O   ARG A 293      30.568  44.160  38.454  1.00165.98           O  
ATOM   2133  CB  ARG A 293      33.396  43.979  37.178  1.00181.37           C  
ATOM   2134  CG  ARG A 293      34.806  43.407  37.205  1.00185.83           C  
ATOM   2135  CD  ARG A 293      35.833  44.471  36.854  1.00193.47           C  
ATOM   2136  NE  ARG A 293      35.705  44.912  35.467  1.00194.82           N  
ATOM   2137  CZ  ARG A 293      36.365  45.940  34.945  1.00198.71           C  
ATOM   2138  NH1 ARG A 293      37.198  46.645  35.696  1.00204.61           N  
ATOM   2139  NH2 ARG A 293      36.187  46.268  33.672  1.00196.24           N  
ATOM   2140  N   GLU A 294      30.183  43.596  36.311  1.00143.02           N  
ATOM   2141  CA  GLU A 294      28.850  44.183  36.284  1.00131.56           C  
ATOM   2142  C   GLU A 294      27.844  43.274  36.982  1.00121.83           C  
ATOM   2143  O   GLU A 294      26.911  43.746  37.632  1.00110.52           O  
ATOM   2144  CB  GLU A 294      28.411  44.452  34.844  1.00139.61           C  
ATOM   2145  CG  GLU A 294      26.994  44.991  34.712  1.00155.72           C  
ATOM   2146  CD  GLU A 294      26.814  46.356  35.357  1.00175.25           C  
ATOM   2147  OE1 GLU A 294      25.653  46.780  35.534  1.00175.38           O  
ATOM   2148  OE2 GLU A 294      27.830  47.005  35.686  1.00186.27           O  
ATOM   2149  N   PHE A 295      28.044  41.967  36.847  1.00129.70           N  
ATOM   2150  CA  PHE A 295      27.146  40.986  37.447  1.00121.92           C  
ATOM   2151  C   PHE A 295      27.312  40.887  38.960  1.00120.58           C  
ATOM   2152  O   PHE A 295      26.333  40.958  39.702  1.00122.88           O  
ATOM   2153  CB  PHE A 295      27.344  39.609  36.807  1.00115.20           C  
ATOM   2154  CG  PHE A 295      26.431  39.342  35.644  1.00112.51           C  
ATOM   2155  CD1 PHE A 295      25.151  38.860  35.849  1.00109.66           C  
ATOM   2156  CD2 PHE A 295      26.854  39.567  34.345  1.00111.39           C  
ATOM   2157  CE1 PHE A 295      24.309  38.611  34.782  1.00102.61           C  
ATOM   2158  CE2 PHE A 295      26.015  39.319  33.273  1.00105.55           C  
ATOM   2159  CZ  PHE A 295      24.742  38.841  33.493  1.00100.90           C  
ATOM   2160  N   ARG A 296      28.551  40.721  39.413  1.00114.01           N  
ATOM   2161  CA  ARG A 296      28.826  40.539  40.835  1.00113.84           C  
ATOM   2162  C   ARG A 296      28.267  41.674  41.690  1.00131.95           C  
ATOM   2163  O   ARG A 296      27.812  41.451  42.811  1.00139.79           O  
ATOM   2164  CB  ARG A 296      30.328  40.374  41.083  1.00104.54           C  
ATOM   2165  CG  ARG A 296      31.180  41.541  40.619  1.00104.53           C  
ATOM   2166  CD  ARG A 296      32.646  41.323  40.962  1.00117.42           C  
ATOM   2167  NE  ARG A 296      33.438  42.530  40.748  1.00143.43           N  
ATOM   2168  CZ  ARG A 296      34.733  42.637  41.029  1.00163.79           C  
ATOM   2169  NH1 ARG A 296      35.372  43.779  40.802  1.00170.57           N  
ATOM   2170  NH2 ARG A 296      35.391  41.603  41.537  1.00169.60           N  
ATOM   2171  N   GLN A 297      28.303  42.890  41.156  1.00140.69           N  
ATOM   2172  CA  GLN A 297      27.801  44.051  41.878  1.00149.63           C  
ATOM   2173  C   GLN A 297      26.277  44.064  41.902  1.00144.85           C  
ATOM   2174  O   GLN A 297      25.666  44.529  42.863  1.00149.32           O  
ATOM   2175  CB  GLN A 297      28.335  45.337  41.251  1.00162.21           C  
ATOM   2176  CG  GLN A 297      29.850  45.400  41.201  1.00173.98           C  
ATOM   2177  CD  GLN A 297      30.358  46.633  40.486  1.00186.34           C  
ATOM   2178  OE1 GLN A 297      29.597  47.561  40.206  1.00190.09           O  
ATOM   2179  NE2 GLN A 297      31.653  46.651  40.185  1.00190.08           N  
ATOM   2180  N   THR A 298      25.670  43.549  40.838  1.00138.24           N  
ATOM   2181  CA  THR A 298      24.218  43.455  40.765  1.00138.95           C  
ATOM   2182  C   THR A 298      23.699  42.485  41.820  1.00143.75           C  
ATOM   2183  O   THR A 298      22.779  42.806  42.572  1.00139.11           O  
ATOM   2184  CB  THR A 298      23.748  42.989  39.376  1.00134.66           C  
ATOM   2185  OG1 THR A 298      24.299  43.846  38.369  1.00139.15           O  
ATOM   2186  CG2 THR A 298      22.231  43.023  39.289  1.00130.18           C  
ATOM   2187  N   PHE A 299      24.298  41.297  41.868  1.00154.88           N  
ATOM   2188  CA  PHE A 299      23.930  40.289  42.857  1.00160.34           C  
ATOM   2189  C   PHE A 299      24.138  40.826  44.268  1.00167.51           C  
ATOM   2190  O   PHE A 299      23.272  40.687  45.132  1.00174.21           O  
ATOM   2191  CB  PHE A 299      24.761  39.016  42.674  1.00160.49           C  
ATOM   2192  CG  PHE A 299      24.697  38.438  41.290  1.00159.12           C  
ATOM   2193  CD1 PHE A 299      23.487  38.051  40.740  1.00157.91           C  
ATOM   2194  CD2 PHE A 299      25.853  38.259  40.548  1.00158.83           C  
ATOM   2195  CE1 PHE A 299      23.428  37.511  39.470  1.00153.19           C  
ATOM   2196  CE2 PHE A 299      25.801  37.720  39.278  1.00155.39           C  
ATOM   2197  CZ  PHE A 299      24.586  37.346  38.738  1.00152.35           C  
ATOM   2198  N   ARG A 300      25.298  41.439  44.489  1.00161.77           N  
ATOM   2199  CA  ARG A 300      25.668  41.976  45.793  1.00153.61           C  
ATOM   2200  C   ARG A 300      24.574  42.882  46.351  1.00149.03           C  
ATOM   2201  O   ARG A 300      24.330  42.913  47.556  1.00143.02           O  
ATOM   2202  CB  ARG A 300      26.993  42.734  45.686  1.00154.44           C  
ATOM   2203  CG  ARG A 300      27.556  43.227  47.006  1.00160.97           C  
ATOM   2204  CD  ARG A 300      28.925  43.854  46.798  1.00172.90           C  
ATOM   2205  NE  ARG A 300      29.435  44.493  48.007  1.00189.06           N  
ATOM   2206  CZ  ARG A 300      30.588  45.153  48.072  1.00201.06           C  
ATOM   2207  NH1 ARG A 300      31.354  45.260  46.995  1.00203.80           N  
ATOM   2208  NH2 ARG A 300      30.976  45.707  49.213  1.00207.03           N  
ATOM   2209  N   LYS A 301      23.912  43.609  45.460  1.00155.80           N  
ATOM   2210  CA  LYS A 301      22.827  44.500  45.846  1.00164.47           C  
ATOM   2211  C   LYS A 301      21.557  43.732  46.211  1.00164.10           C  
ATOM   2212  O   LYS A 301      20.916  44.016  47.223  1.00166.83           O  
ATOM   2213  CB  LYS A 301      22.541  45.477  44.708  1.00165.18           C  
ATOM   2214  CG  LYS A 301      21.304  46.327  44.900  1.00164.15           C  
ATOM   2215  CD  LYS A 301      20.395  46.222  43.683  1.00157.89           C  
ATOM   2216  CE  LYS A 301      21.169  46.416  42.382  1.00156.12           C  
ATOM   2217  NZ  LYS A 301      20.474  45.800  41.213  1.00149.81           N  
ATOM   2218  N   ILE A 302      21.197  42.762  45.377  1.00160.43           N  
ATOM   2219  CA  ILE A 302      19.994  41.966  45.598  1.00157.29           C  
ATOM   2220  C   ILE A 302      20.024  41.259  46.951  1.00157.34           C  
ATOM   2221  O   ILE A 302      19.049  41.293  47.702  1.00157.21           O  
ATOM   2222  CB  ILE A 302      19.801  40.911  44.490  1.00152.02           C  
ATOM   2223  CG1 ILE A 302      19.798  41.572  43.109  1.00153.23           C  
ATOM   2224  CG2 ILE A 302      18.515  40.133  44.716  1.00145.38           C  
ATOM   2225  CD1 ILE A 302      19.630  40.591  41.964  1.00144.30           C  
ATOM   2226  N   ILE A 303      21.149  40.619  47.255  1.00159.91           N  
ATOM   2227  CA  ILE A 303      21.305  39.881  48.506  1.00161.79           C  
ATOM   2228  C   ILE A 303      21.128  40.785  49.723  1.00167.98           C  
ATOM   2229  O   ILE A 303      20.322  40.498  50.609  1.00165.59           O  
ATOM   2230  CB  ILE A 303      22.682  39.189  48.587  1.00157.95           C  
ATOM   2231  CG1 ILE A 303      22.877  38.249  47.396  1.00143.36           C  
ATOM   2232  CG2 ILE A 303      22.826  38.431  49.900  1.00157.41           C  
ATOM   2233  CD1 ILE A 303      24.226  37.569  47.372  1.00140.23           C  
ATOM   2234  N   ARG A 304      21.887  41.875  49.759  1.00175.65           N  
ATOM   2235  CA  ARG A 304      21.813  42.823  50.864  1.00186.43           C  
ATOM   2236  C   ARG A 304      20.399  43.362  51.044  1.00185.55           C  
ATOM   2237  O   ARG A 304      19.851  43.339  52.146  1.00186.25           O  
ATOM   2238  CB  ARG A 304      22.790  43.979  50.643  1.00197.78           C  
ATOM   2239  CG  ARG A 304      24.252  43.575  50.704  1.00205.44           C  
ATOM   2240  CD  ARG A 304      25.159  44.778  50.499  1.00213.97           C  
ATOM   2241  NE  ARG A 304      26.558  44.463  50.776  1.00218.44           N  
ATOM   2242  CZ  ARG A 304      27.554  45.336  50.674  1.00222.23           C  
ATOM   2243  NH1 ARG A 304      28.797  44.961  50.948  1.00224.87           N  
ATOM   2244  NH2 ARG A 304      27.309  46.584  50.298  1.00223.23           N  
ATOM   2245  N   SER A 305      19.813  43.846  49.954  1.00183.73           N  
ATOM   2246  CA  SER A 305      18.464  44.400  49.990  1.00181.17           C  
ATOM   2247  C   SER A 305      17.429  43.360  49.573  1.00174.05           C  
ATOM   2248  O   SER A 305      17.003  42.533  50.380  1.00172.15           O  
ATOM   2249  CB  SER A 305      18.366  45.634  49.090  1.00181.50           C  
ATOM   2250  OG  SER A 305      17.075  46.213  49.155  1.00179.40           O  
TER    2251      SER A 305                                                      
HETATM 2252  N2  T4E A 330      23.684   6.666  32.080  1.00119.27           N  
HETATM 2253  N1  T4E A 330      23.105   7.781  32.548  1.00118.43           N  
HETATM 2254  C6  T4E A 330      23.167   8.937  31.828  1.00118.04           C  
HETATM 2255  C5  T4E A 330      23.852   8.945  30.571  1.00117.97           C  
HETATM 2256  N4  T4E A 330      24.432   7.799  30.123  1.00118.08           N  
HETATM 2257  C3  T4E A 330      24.308   6.738  30.908  1.00118.73           C  
HETATM 2258  C10 T4E A 330      21.114  12.259  33.687  1.00114.66           C  
HETATM 2259  C11 T4E A 330      20.430  11.061  33.407  1.00115.14           C  
HETATM 2260  C12 T4E A 330      21.110   9.987  32.803  1.00117.02           C  
HETATM 2261  C7  T4E A 330      22.480  10.083  32.466  1.00116.84           C  
HETATM 2262  C8  T4E A 330      23.155  11.292  32.750  1.00115.62           C  
HETATM 2263  C9  T4E A 330      22.484  12.376  33.356  1.00115.01           C  
HETATM 2264  C16 T4E A 330      24.362  12.344  27.927  1.00115.74           C  
HETATM 2265  C17 T4E A 330      23.174  12.204  28.663  1.00115.36           C  
HETATM 2266  C18 T4E A 330      23.004  11.102  29.521  1.00116.32           C  
HETATM 2267  C13 T4E A 330      24.011  10.116  29.668  1.00117.31           C  
HETATM 2268  C14 T4E A 330      25.200  10.281  28.914  1.00116.86           C  
HETATM 2269  C15 T4E A 330      25.380  11.381  28.053  1.00116.02           C  
HETATM 2270  N3  T4E A 330      24.883   5.599  30.462  1.00118.82           N  
HETATM 2271 CL1  T4E A 330      23.352  13.836  33.683  1.00114.91          CL  
HETATM 2272  O1  T4E A 330      20.443  13.293  34.273  1.00114.91           O  
CONECT  484 1071                                                                
CONECT  500 1041                                                                
CONECT  520 1115                                                                
CONECT 1041  500                                                                
CONECT 1071  484                                                                
CONECT 1115  520                                                                
CONECT 1861 1882                                                                
CONECT 1882 1861                                                                
CONECT 2252 2253 2257                                                           
CONECT 2253 2252 2254                                                           
CONECT 2254 2253 2255 2261                                                      
CONECT 2255 2254 2256 2267                                                      
CONECT 2256 2255 2257                                                           
CONECT 2257 2252 2256 2270                                                      
CONECT 2258 2259 2263 2272                                                      
CONECT 2259 2258 2260                                                           
CONECT 2260 2259 2261                                                           
CONECT 2261 2254 2260 2262                                                      
CONECT 2262 2261 2263                                                           
CONECT 2263 2258 2262 2271                                                      
CONECT 2264 2265 2269                                                           
CONECT 2265 2264 2266                                                           
CONECT 2266 2265 2267                                                           
CONECT 2267 2255 2266 2268                                                      
CONECT 2268 2267 2269                                                           
CONECT 2269 2264 2268                                                           
CONECT 2270 2257                                                                
CONECT 2271 2263                                                                
CONECT 2272 2258                                                                
MASTER      523    0    1   15    2    0    3    6 2271    1   29   26          
END                                                                             
