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Database: PDB
Entry: 3PWH
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HEADER    SIGNALING PROTEIN                       08-DEC-10   3PWH              
TITLE     THERMOSTABILISED ADENOSINE A2A RECEPTOR                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADENOSINE RECEPTOR A2A;                                    
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, INVERSE AGONIST, G-PROTEIN, MEMBRANE PROTEIN, SIGNALING    
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.S.DORE,N.ROBERTSON,J.C.ERREY,I.NG,B.TEHAN,E.HURRELL,F.MAGNANI,      
AUTHOR   2 C.G.TATE,M.WEIR,F.H.MARSHALL                                         
REVDAT   2   20-JUN-12 3PWH    1       JRNL                                     
REVDAT   1   07-SEP-11 3PWH    0                                                
JRNL        AUTH   A.S.DORE,N.ROBERTSON,J.C.ERREY,I.NG,K.HOLLENSTEIN,B.TEHAN,   
JRNL        AUTH 2 E.HURRELL,K.BENNETT,M.CONGREVE,F.MAGNANI,C.G.TATE,M.WEIR,    
JRNL        AUTH 3 F.H.MARSHALL                                                 
JRNL        TITL   STRUCTURE OF THE ADENOSINE A(2A) RECEPTOR IN COMPLEX WITH    
JRNL        TITL 2 ZM241385 AND THE XANTHINES XAC AND CAFFEINE                  
JRNL        REF    STRUCTURE                     V.  19  1283 2011              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   21885291                                                     
JRNL        DOI    10.1016/J.STR.2011.06.014                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.4_84)                       
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.84                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 12010                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.278                           
REMARK   3   R VALUE            (WORKING SET) : 0.276                           
REMARK   3   FREE R VALUE                     : 0.316                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 576                             
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 19.8421 -  5.2087    0.99     2993   147  0.2638 0.3165        
REMARK   3     2  5.2087 -  4.1467    0.99     2878   144  0.2295 0.2680        
REMARK   3     3  4.1467 -  3.6261    0.99     2820   151  0.2828 0.2981        
REMARK   3     4  3.6261 -  3.2962    0.95     2743   134  0.3971 0.4875        
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              : 72.89                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.540            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 40.600           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 96.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 139.52                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -60.76360                                            
REMARK   3    B22 (A**2) : 18.45040                                             
REMARK   3    B33 (A**2) : 42.31320                                             
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      :  0.001           2338                                  
REMARK   3   ANGLE     :  0.388           3187                                  
REMARK   3   CHIRALITY :  0.027            377                                  
REMARK   3   PLANARITY :  0.002            390                                  
REMARK   3   DIHEDRAL  : 10.444            791                                  
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):  30.0903  20.0227  41.8459              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9211 T22:   0.7868                                     
REMARK   3      T33:   0.0494 T12:  -0.0079                                     
REMARK   3      T13:  -0.2712 T23:   1.1006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2837 L22:   1.0271                                     
REMARK   3      L33:   1.1611 L12:  -0.0605                                     
REMARK   3      L13:  -0.2252 L23:  -0.9329                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3050 S12:  -1.1647 S13:  -0.6916                       
REMARK   3      S21:   0.6959 S22:   0.3460 S23:   0.3410                       
REMARK   3      S31:   0.0072 S32:  -0.5034 S33:   2.5930                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain A and resid 34:40                                
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9500  21.4088  29.5774              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6181 T22:   1.2560                                     
REMARK   3      T33:   2.4789 T12:  -0.3004                                     
REMARK   3      T13:  -0.0002 T23:   0.0674                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0179 L22:   0.0126                                     
REMARK   3      L33:   0.0072 L12:   0.0188                                     
REMARK   3      L13:   0.0099 L23:   0.0105                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2431 S12:   0.4499 S13:   0.3506                       
REMARK   3      S21:   0.4031 S22:  -0.2015 S23:   0.1379                       
REMARK   3      S31:   0.5653 S32:   0.2159 S33:  -0.0015                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain A and resid 41:68                                
REMARK   3    ORIGIN FOR THE GROUP (A):  33.7968  17.8208  33.2584              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6444 T22:   0.6958                                     
REMARK   3      T33:   2.1995 T12:   0.0104                                     
REMARK   3      T13:  -0.0720 T23:   0.4078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3400 L22:   0.0304                                     
REMARK   3      L33:   0.8841 L12:   0.1162                                     
REMARK   3      L13:  -0.5555 L23:  -0.1762                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0073 S12:   0.9717 S13:  -0.3867                       
REMARK   3      S21:   0.8159 S22:  -0.1882 S23:  -0.0308                       
REMARK   3      S31:   0.0405 S32:   0.7148 S33:  -0.0003                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain A and resid 69:76                                
REMARK   3    ORIGIN FOR THE GROUP (A):  52.1300   7.7666  31.2759              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7674 T22:   1.4392                                     
REMARK   3      T33:   3.2011 T12:   0.4522                                     
REMARK   3      T13:  -0.0309 T23:  -0.1161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0494 L22:   0.0616                                     
REMARK   3      L33:   0.0010 L12:  -0.0592                                     
REMARK   3      L13:   0.0014 L23:  -0.0014                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4390 S12:  -0.4443 S13:   0.3581                       
REMARK   3      S21:  -0.8761 S22:   0.1256 S23:  -0.0364                       
REMARK   3      S31:  -0.1894 S32:   0.6682 S33:  -0.0035                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain A and resid 77:104                               
REMARK   3    ORIGIN FOR THE GROUP (A):  33.1345  21.9108  23.7102              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9418 T22:   0.6518                                     
REMARK   3      T33:   0.3077 T12:   0.0588                                     
REMARK   3      T13:   0.1172 T23:   0.7339                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9018 L22:   0.1728                                     
REMARK   3      L33:   0.2185 L12:  -0.1748                                     
REMARK   3      L13:   0.0520 L23:   0.0181                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3603 S12:   0.2035 S13:  -0.2160                       
REMARK   3      S21:  -0.8378 S22:   0.6562 S23:   0.0135                       
REMARK   3      S31:   0.0900 S32:  -0.9455 S33:   3.7247                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain A and resid 105:118                              
REMARK   3    ORIGIN FOR THE GROUP (A):  13.1924  27.6597  14.2698              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7109 T22:   1.4749                                     
REMARK   3      T33:   2.5201 T12:  -0.0667                                     
REMARK   3      T13:  -0.3136 T23:   0.3334                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0855 L22:   0.0571                                     
REMARK   3      L33:   0.1330 L12:  -0.0189                                     
REMARK   3      L13:  -0.1159 L23:   0.0225                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1357 S12:   0.7708 S13:   0.0448                       
REMARK   3      S21:   0.2042 S22:  -0.7862 S23:   0.8670                       
REMARK   3      S31:  -0.6183 S32:   0.3015 S33:   0.0016                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain A and resid 119:141                              
REMARK   3    ORIGIN FOR THE GROUP (A):  33.2066  15.0152  19.2255              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9309 T22:   1.2932                                     
REMARK   3      T33:   1.6890 T12:  -0.0492                                     
REMARK   3      T13:  -0.0956 T23:  -0.1547                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1087 L22:   0.3116                                     
REMARK   3      L33:   0.1868 L12:   0.1902                                     
REMARK   3      L13:   0.1455 L23:   0.2566                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1289 S12:   0.9782 S13:  -0.2504                       
REMARK   3      S21:  -1.4147 S22:   0.2723 S23:  -0.1716                       
REMARK   3      S31:   0.0517 S32:   1.5458 S33:   0.0015                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain A and resid 142:151                              
REMARK   3    ORIGIN FOR THE GROUP (A):  56.6014  14.3154  21.3033              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1242 T22:   0.7607                                     
REMARK   3      T33:   3.0569 T12:  -0.2078                                     
REMARK   3      T13:  -0.0809 T23:   0.0185                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0395 L22:   0.0360                                     
REMARK   3      L33:   0.0808 L12:  -0.0348                                     
REMARK   3      L13:  -0.0577 L23:   0.0526                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1638 S12:   0.8039 S13:  -0.2811                       
REMARK   3      S21:  -2.1942 S22:  -0.5167 S23:   0.4101                       
REMARK   3      S31:   0.2744 S32:  -0.0732 S33:   0.0027                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain A and resid 158:175                              
REMARK   3    ORIGIN FOR THE GROUP (A):  56.1127  13.6131  29.0989              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0142 T22:   1.3040                                     
REMARK   3      T33:   2.6543 T12:   0.1886                                     
REMARK   3      T13:   0.0797 T23:   0.0367                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1730 L22:   0.0527                                     
REMARK   3      L33:   0.2845 L12:   0.0423                                     
REMARK   3      L13:  -0.1081 L23:   0.0794                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2575 S12:   1.2049 S13:  -0.6624                       
REMARK   3      S21:   0.5518 S22:   0.5917 S23:  -0.0998                       
REMARK   3      S31:   0.2657 S32:   1.3951 S33:  -0.0007                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain A and resid 176:211                              
REMARK   3    ORIGIN FOR THE GROUP (A):  30.6937  34.9887  17.9274              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7017 T22:   0.8913                                     
REMARK   3      T33:   1.4949 T12:   0.1718                                     
REMARK   3      T13:  -0.1259 T23:   0.1322                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4578 L22:   0.9302                                     
REMARK   3      L33:   0.4198 L12:   0.5212                                     
REMARK   3      L13:   0.3065 L23:   0.6336                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6245 S12:  -0.8116 S13:   1.3017                       
REMARK   3      S21:   0.8934 S22:  -0.3353 S23:   0.3319                       
REMARK   3      S31:  -0.2005 S32:  -0.1411 S33:  -0.0041                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain A and resid 212:220                              
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2806  46.3634  19.0215              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7062 T22:   1.7584                                     
REMARK   3      T33:   2.1099 T12:  -0.0814                                     
REMARK   3      T13:  -0.2921 T23:   0.6776                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0230 L22:   0.1282                                     
REMARK   3      L33:   0.3368 L12:   0.0027                                     
REMARK   3      L13:   0.0185 L23:   0.2109                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3229 S12:   1.0170 S13:   0.7152                       
REMARK   3      S21:   0.8995 S22:   0.1196 S23:   0.1671                       
REMARK   3      S31:   0.9409 S32:   1.1865 S33:  -0.0012                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain A and resid 221:258                              
REMARK   3    ORIGIN FOR THE GROUP (A):  31.7215  34.2568  26.8291              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3774 T22:   0.1430                                     
REMARK   3      T33:   1.2283 T12:  -0.0882                                     
REMARK   3      T13:  -0.0336 T23:   0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1391 L22:   1.9193                                     
REMARK   3      L33:   2.5122 L12:  -0.6267                                     
REMARK   3      L13:  -3.2333 L23:  -0.3072                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1125 S12:   0.7533 S13:   1.9754                       
REMARK   3      S21:  -0.8069 S22:   0.1149 S23:  -0.0020                       
REMARK   3      S31:   0.1038 S32:  -0.5891 S33:  -0.0703                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: chain A and resid 259:267                              
REMARK   3    ORIGIN FOR THE GROUP (A):  58.6658  33.0067  30.2595              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3917 T22:   0.6275                                     
REMARK   3      T33:   1.5789 T12:   0.2507                                     
REMARK   3      T13:  -0.3550 T23:  -0.2840                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4141 L22:   2.0108                                     
REMARK   3      L33:   1.0883 L12:   7.3105                                     
REMARK   3      L13:   2.4189 L23:   3.3681                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.9678 S12:  -0.0944 S13:  -0.4939                       
REMARK   3      S21:   1.5923 S22:  -0.7472 S23:   0.7135                       
REMARK   3      S31:   0.1913 S32:  -1.0872 S33:  -0.1050                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: chain A and resid 268:292                              
REMARK   3    ORIGIN FOR THE GROUP (A):  34.6152  29.2923  37.1347              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7046 T22:   0.6132                                     
REMARK   3      T33:   1.6036 T12:  -0.0903                                     
REMARK   3      T13:   0.0028 T23:  -0.0645                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2195 L22:   0.3633                                     
REMARK   3      L33:   0.1975 L12:   0.2123                                     
REMARK   3      L13:  -0.1458 L23:  -0.2402                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1603 S12:  -0.2871 S13:   1.0302                       
REMARK   3      S21:   0.7656 S22:   0.5300 S23:   0.4867                       
REMARK   3      S31:  -0.7544 S32:  -0.1844 S33:  -0.0007                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: chain A and resid 293:305                              
REMARK   3    ORIGIN FOR THE GROUP (A):  13.7343  25.7523  41.9297              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6927 T22:   1.6093                                     
REMARK   3      T33:   2.3490 T12:  -0.0336                                     
REMARK   3      T13:   0.0812 T23:   0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2272 L22:   0.6547                                     
REMARK   3      L33:   3.9104 L12:  -0.0647                                     
REMARK   3      L13:  -0.6892 L23:   1.1232                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.3292 S12:   0.2356 S13:  -0.4017                       
REMARK   3      S21:   0.1520 S22:  -1.0580 S23:   1.4699                       
REMARK   3      S31:  -1.9681 S32:  -3.0048 S33:  -0.0150                       
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 3PWH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-DEC-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062896.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-MAY-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 8.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
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          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12191                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.296                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 83.844                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 10.700                             
REMARK 200  R MERGE                    (I) : 0.11900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: 3EML                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 77.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.43                     
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 8.1, 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       55.96750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       56.27550            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       62.83900            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       55.96750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.27550            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       62.83900            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       55.96750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       56.27550            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       62.83900            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       55.96750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       56.27550            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       62.83900            
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    GLN A  38       49.47    -84.02                                   
REMARK 500    LEU A  58      -54.04   -126.55                                   
REMARK 500    ALA A  73      175.65    -58.63                                   
REMARK 500    ALA A 165       93.64    -59.77                                   
REMARK 500    CYS A 166       91.26    -67.42                                   
REMARK 500    VAL A 178      -69.02   -100.69                                   
REMARK 500    PHE A 180      -71.78    -85.35                                   
REMARK 500    ASN A 181      -76.05    -52.68                                   
REMARK 500    PHE A 182      -72.32    -57.22                                   
REMARK 500    VAL A 186      -52.70   -138.08                                   
REMARK 500    SER A 213       41.06   -107.21                                   
REMARK 500    PRO A 215       23.83    -71.62                                   
REMARK 500    PRO A 217      -71.05    -57.13                                   
REMARK 500    TRP A 246      -34.58   -138.98                                   
REMARK 500    SER A 263      108.97    -45.22                                   
REMARK 500    ALA A 289        0.32    -65.58                                   
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 ZMA A 401                 
DBREF  3PWH A    1   317  UNP    P29274   AA2AR_HUMAN      1    317             
SEQADV 3PWH LEU A   54  UNP  P29274    ALA    54 ENGINEERED MUTATION            
SEQADV 3PWH ALA A   88  UNP  P29274    THR    88 ENGINEERED MUTATION            
SEQADV 3PWH ALA A  107  UNP  P29274    ARG   107 ENGINEERED MUTATION            
SEQADV 3PWH ALA A  122  UNP  P29274    LYS   122 ENGINEERED MUTATION            
SEQADV 3PWH ALA A  202  UNP  P29274    LEU   202 ENGINEERED MUTATION            
SEQADV 3PWH ALA A  235  UNP  P29274    LEU   235 ENGINEERED MUTATION            
SEQADV 3PWH ALA A  239  UNP  P29274    VAL   239 ENGINEERED MUTATION            
SEQADV 3PWH ALA A  277  UNP  P29274    SER   277 ENGINEERED MUTATION            
SEQADV 3PWH ALA A  318  UNP  P29274              EXPRESSION TAG                 
SEQADV 3PWH ALA A  319  UNP  P29274              EXPRESSION TAG                 
SEQADV 3PWH HIS A  320  UNP  P29274              EXPRESSION TAG                 
SEQADV 3PWH HIS A  321  UNP  P29274              EXPRESSION TAG                 
SEQADV 3PWH HIS A  322  UNP  P29274              EXPRESSION TAG                 
SEQADV 3PWH HIS A  323  UNP  P29274              EXPRESSION TAG                 
SEQADV 3PWH HIS A  324  UNP  P29274              EXPRESSION TAG                 
SEQADV 3PWH HIS A  325  UNP  P29274              EXPRESSION TAG                 
SEQADV 3PWH HIS A  326  UNP  P29274              EXPRESSION TAG                 
SEQADV 3PWH HIS A  327  UNP  P29274              EXPRESSION TAG                 
SEQADV 3PWH HIS A  328  UNP  P29274              EXPRESSION TAG                 
SEQADV 3PWH 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    ZMA  A 401      25                                                       
HETNAM     ZMA 4-{2-[(7-AMINO-2-FURAN-2-YL[1,2,4]TRIAZOLO[1,5-A][1,3,           
HETNAM   2 ZMA  5]TRIAZIN-5-YL)AMINO]ETHYL}PHENOL                               
FORMUL   2  ZMA    C16 H15 N7 O2                                                
HELIX    1   1 TYR A    9  ASN A   34  1                                  26    
HELIX    2   2 ASN A   39  LEU A   58  1                                  20    
HELIX    3   3 LEU A   58  ILE A   64  1                                   7    
HELIX    4   4 ILE A   64  GLY A   69  1                                   6    
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  PHE A  180  1                                   8    
HELIX   11  11 PHE A  180  VAL A  186  1                                   7    
HELIX   12  12 VAL A  186  MET A  211  1                                  26    
HELIX   13  13 GLY A  218  CYS A  245  1                                  28    
HELIX   14  14 TRP A  246  CYS A  259  1                                  14    
HELIX   15  15 PRO A  266  ASN A  280  1                                  15    
HELIX   16  16 VAL A  282  ILE A  292  1                                  11    
HELIX   17  17 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  VAL A 164   N  ALA A  72           
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 ALA A  63  SER A  67  PHE A 168  GLU A 169                    
SITE     2 AC1  9 MET A 177  LEU A 249  ASN A 253  TYR A 271                    
SITE     3 AC1  9 ILE A 274                                                     
CRYST1  111.935  112.551  125.678  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      0.008934  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008885  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007957        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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