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Entry: 3UZA
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HEADER    SIGNALING PROTEIN                       07-DEC-11   3UZA              
TITLE     THERMOSTABILISED ADENOSINE A2A RECEPTOR IN COMPLEX WITH 6-(2,6-       
TITLE    2 DIMETHYLPYRIDIN-4-YL)-5-PHENYL-1,2,4-TRIAZIN-3-AMINE                 
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, SIGNALING PROTEIN, G-PROTEIN, MEMBRANE 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,B.TEHAN,A.ZHUKOV,M.WEIR,F.H.MARSHALL                
REVDAT   1   21-MAR-12 3UZA    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.    3.27 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) : 3.27                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.77                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.510                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 11401                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.295                           
REMARK   3   R VALUE            (WORKING SET) : 0.293                           
REMARK   3   FREE R VALUE                     : 0.335                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.810                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 548                             
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 19.7738 -  5.1716    0.92     2815   136  0.2638 0.3074        
REMARK   3     2  5.1716 -  4.1170    0.93     2736   136  0.2607 0.2966        
REMARK   3     3  4.1170 -  3.6002    0.94     2703   158  0.3316 0.3934        
REMARK   3     4  3.6002 -  3.2726    0.88     2599   118  0.3950 0.4260        
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              : 0.22                                          
REMARK   3   B_SOL              : 60.16                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.460            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 42.610           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 94.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 154.90                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -72.30920                                            
REMARK   3    B22 (A**2) : 7.05460                                              
REMARK   3    B33 (A**2) : 45.66940                                             
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     :  0.466           3180                                  
REMARK   3   CHIRALITY :  0.031            377                                  
REMARK   3   PLANARITY :  0.002            390                                  
REMARK   3   DIHEDRAL  : 11.809            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):  29.8601  19.8787  41.9416              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7974 T22:   1.0542                                     
REMARK   3      T33:   2.2534 T12:  -0.0532                                     
REMARK   3      T13:  -0.1911 T23:   0.0891                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5730 L22:   0.6937                                     
REMARK   3      L33:   3.3859 L12:  -0.4859                                     
REMARK   3      L13:  -1.2981 L23:   0.7333                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.5321 S12:  -0.4203 S13:  -1.1429                       
REMARK   3      S21:   0.9976 S22:   0.2253 S23:  -0.0887                       
REMARK   3      S31:   0.5770 S32:  -0.1862 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain A and resid 34:40                                
REMARK   3    ORIGIN FOR THE GROUP (A):  11.6918  21.2280  29.8354              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0264 T22:   1.4670                                     
REMARK   3      T33:   2.7036 T12:   0.0609                                     
REMARK   3      T13:   0.0490 T23:   0.3644                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0286 L22:   0.0225                                     
REMARK   3      L33:   0.0438 L12:   0.0231                                     
REMARK   3      L13:   0.0268 L23:   0.0321                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4098 S12:   1.6802 S13:  -0.2703                       
REMARK   3      S21:  -1.7773 S22:  -0.0295 S23:   0.7118                       
REMARK   3      S31:   0.7285 S32:   1.2415 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain A and resid 41:68                                
REMARK   3    ORIGIN FOR THE GROUP (A):  33.5546  17.7564  33.5287              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8403 T22:   0.9101                                     
REMARK   3      T33:   2.3669 T12:   0.0610                                     
REMARK   3      T13:  -0.3570 T23:   0.4226                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5788 L22:   0.7159                                     
REMARK   3      L33:   0.9007 L12:   0.2259                                     
REMARK   3      L13:  -0.6952 L23:  -0.0923                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0076 S12:   1.1804 S13:   0.8842                       
REMARK   3      S21:   0.3159 S22:  -0.6586 S23:  -1.0298                       
REMARK   3      S31:  -0.0511 S32:   0.1067 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain A and resid 69:76                                
REMARK   3    ORIGIN FOR THE GROUP (A):  51.8895   7.6703  31.7134              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7163 T22:   1.0993                                     
REMARK   3      T33:   3.3229 T12:   0.3037                                     
REMARK   3      T13:  -0.0733 T23:   0.1859                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1244 L22:   0.4084                                     
REMARK   3      L33:   0.1322 L12:  -0.0854                                     
REMARK   3      L13:   0.0067 L23:  -0.2117                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0765 S12:  -0.1589 S13:   0.3099                       
REMARK   3      S21:  -1.2246 S22:   0.1678 S23:  -0.4967                       
REMARK   3      S31:  -0.8882 S32:   1.0536 S33:   0.0001                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain A and resid 77:104                               
REMARK   3    ORIGIN FOR THE GROUP (A):  32.8243  21.6182  23.9034              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0013 T22:   0.8443                                     
REMARK   3      T33:   1.0992 T12:   0.3537                                     
REMARK   3      T13:  -0.2194 T23:   0.4823                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2977 L22:   0.4311                                     
REMARK   3      L33:   1.0082 L12:   0.1865                                     
REMARK   3      L13:   0.0356 L23:   0.5991                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.4228 S12:   0.9274 S13:  -0.4301                       
REMARK   3      S21:  -1.5677 S22:  -0.1297 S23:  -0.1154                       
REMARK   3      S31:   1.3687 S32:  -0.1525 S33:  -0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain A and resid 105:118                              
REMARK   3    ORIGIN FOR THE GROUP (A):  12.8547  27.1731  14.2424              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0868 T22:   1.9058                                     
REMARK   3      T33:   3.5319 T12:  -0.0266                                     
REMARK   3      T13:  -0.1959 T23:   0.4545                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1467 L22:   0.1825                                     
REMARK   3      L33:   0.2377 L12:  -0.1602                                     
REMARK   3      L13:  -0.1924 L23:   0.2112                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2507 S12:   2.0818 S13:  -0.5415                       
REMARK   3      S21:  -2.1820 S22:  -0.1503 S23:   0.2694                       
REMARK   3      S31:   0.5972 S32:   0.9899 S33:   0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain A and resid 119:141                              
REMARK   3    ORIGIN FOR THE GROUP (A):  32.8881  14.6050  19.5265              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2026 T22:   1.4771                                     
REMARK   3      T33:   2.1403 T12:   0.0390                                     
REMARK   3      T13:  -0.2414 T23:  -0.1281                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1248 L22:   0.6509                                     
REMARK   3      L33:   0.8149 L12:   0.1442                                     
REMARK   3      L13:  -0.1095 L23:   0.4713                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4854 S12:   2.2377 S13:  -0.3539                       
REMARK   3      S21:  -1.7063 S22:   0.0087 S23:  -0.7588                       
REMARK   3      S31:   0.5235 S32:   0.6693 S33:  -0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain A and resid 142:149                              
REMARK   3    ORIGIN FOR THE GROUP (A):  56.5427  13.9557  21.6676              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3244 T22:   1.3539                                     
REMARK   3      T33:   3.6434 T12:  -0.2437                                     
REMARK   3      T13:   0.1519 T23:   0.1364                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0151 L22:   0.2613                                     
REMARK   3      L33:   0.1510 L12:   0.0474                                     
REMARK   3      L13:   0.0175 L23:   0.1771                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -2.5638 S12:   0.1327 S13:  -0.4075                       
REMARK   3      S21:  -1.5054 S22:  -0.0311 S23:   0.4975                       
REMARK   3      S31:   2.5504 S32:   0.7844 S33:  -0.0002                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain A and resid 158:175                              
REMARK   3    ORIGIN FOR THE GROUP (A):  55.8040  13.4600  29.5073              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9651 T22:   1.4727                                     
REMARK   3      T33:   3.1046 T12:   0.0355                                     
REMARK   3      T13:  -0.2268 T23:  -0.1799                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4984 L22:   0.6921                                     
REMARK   3      L33:   1.0769 L12:  -0.1780                                     
REMARK   3      L13:  -0.2810 L23:   0.8597                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.4255 S12:   1.7188 S13:  -0.1189                       
REMARK   3      S21:  -0.8874 S22:   0.4692 S23:  -0.8777                       
REMARK   3      S31:   1.1928 S32:   2.1782 S33:   0.0000                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain A and resid 176:211                              
REMARK   3    ORIGIN FOR THE GROUP (A):  30.3864  34.6141  17.7844              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8917 T22:   1.3173                                     
REMARK   3      T33:   1.6806 T12:   0.2854                                     
REMARK   3      T13:  -0.1635 T23:   0.1918                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7746 L22:   0.9038                                     
REMARK   3      L33:   1.8450 L12:   0.8354                                     
REMARK   3      L13:   0.4427 L23:   0.2486                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0479 S12:  -0.6906 S13:   0.7535                       
REMARK   3      S21:   0.0033 S22:  -0.2091 S23:   0.4172                       
REMARK   3      S31:   0.2613 S32:  -0.2197 S33:   0.0000                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain A and resid 212:220                              
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2237  45.7382  18.7634              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1082 T22:   1.6025                                     
REMARK   3      T33:   3.4713 T12:  -0.0152                                     
REMARK   3      T13:  -0.4406 T23:   0.5201                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0410 L22:   0.0034                                     
REMARK   3      L33:   0.1100 L12:  -0.0084                                     
REMARK   3      L13:  -0.0677 L23:   0.0167                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7367 S12:   1.3159 S13:   0.4136                       
REMARK   3      S21:  -0.6100 S22:   1.4132 S23:  -0.2355                       
REMARK   3      S31:  -0.7138 S32:   1.0698 S33:   0.0000                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain A and resid 221:258                              
REMARK   3    ORIGIN FOR THE GROUP (A):  31.4883  33.9806  26.7093              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8441 T22:   0.6548                                     
REMARK   3      T33:   1.7843 T12:   0.0149                                     
REMARK   3      T13:  -0.0433 T23:  -0.1770                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4526 L22:   1.8293                                     
REMARK   3      L33:   2.3894 L12:  -0.0272                                     
REMARK   3      L13:   0.9206 L23:  -1.1423                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.5304 S12:   0.9797 S13:   1.9018                       
REMARK   3      S21:  -1.1397 S22:  -0.4916 S23:  -0.4669                       
REMARK   3      S31:   0.1125 S32:  -0.4865 S33:   0.0001                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: chain A and resid 259:267                              
REMARK   3    ORIGIN FOR THE GROUP (A):  58.3201  32.6214  30.1614              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9364 T22:   1.1418                                     
REMARK   3      T33:   2.7737 T12:   0.1130                                     
REMARK   3      T13:  -0.1816 T23:  -0.0347                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3572 L22:   0.4196                                     
REMARK   3      L33:   0.6487 L12:   0.2018                                     
REMARK   3      L13:   0.0750 L23:   0.4769                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.5342 S12:   2.2205 S13:  -0.4853                       
REMARK   3      S21:  -0.0984 S22:  -1.7001 S23:   1.2596                       
REMARK   3      S31:  -1.0689 S32:  -0.4521 S33:   0.0011                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: chain A and resid 268:292                              
REMARK   3    ORIGIN FOR THE GROUP (A):  34.4680  29.2297  37.1336              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0619 T22:   0.1901                                     
REMARK   3      T33:  -0.6292 T12:  -0.1317                                     
REMARK   3      T13:   0.1912 T23:  -1.2089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3439 L22:   0.1461                                     
REMARK   3      L33:   1.6867 L12:  -0.0656                                     
REMARK   3      L13:   0.2472 L23:   0.5952                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0402 S12:  -0.5240 S13:   0.2477                       
REMARK   3      S21:   0.1374 S22:  -0.1282 S23:  -0.2133                       
REMARK   3      S31:  -0.3508 S32:  -0.6276 S33:   0.5979                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: chain A and resid 293:305                              
REMARK   3    ORIGIN FOR THE GROUP (A):  13.5317  25.8910  42.3899              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1135 T22:   1.8098                                     
REMARK   3      T33:   2.0674 T12:   0.0320                                     
REMARK   3      T13:  -0.0760 T23:  -0.1646                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1563 L22:   0.3944                                     
REMARK   3      L33:   0.0408 L12:   0.2101                                     
REMARK   3      L13:   0.0870 L23:   0.1107                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3952 S12:  -0.8974 S13:   0.2206                       
REMARK   3      S21:   0.0266 S22:  -0.1258 S23:   1.8021                       
REMARK   3      S31:  -1.7608 S32:  -3.0972 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 3UZA 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 RCSB ID CODE IS RCSB069396.                                      
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        : 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   : 11568                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.273                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.6                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.27                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.96000                            
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): 5.40                     
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, 0.1M TRIS-HCL, PH 8.0, VAPOR    
REMARK 280  DIFFUSION, 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       55.90700            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       55.94800            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       62.92050            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       55.90700            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       55.94800            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       62.92050            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       55.90700            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       55.94800            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       62.92050            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       55.90700            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       55.94800            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       62.92050            
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      -56.42   -130.12                                   
REMARK 500    ALA A 165      105.73    -54.51                                   
REMARK 500    VAL A 178      -61.87   -103.32                                   
REMARK 500    PHE A 182      -74.24    -76.79                                   
REMARK 500    VAL A 186      -57.54   -125.38                                   
REMARK 500    PRO A 215       20.22    -72.39                                   
REMARK 500    PRO A 217      -71.94    -57.57                                   
REMARK 500    SER A 263      112.66    -38.45                                   
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 T4G A 330                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3UZC   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH COMPOUND 4E                          
REMARK 900 RELATED ID: 3PWH   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ZM241385                             
REMARK 900 RELATED ID: 3REY   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH XAC                                  
REMARK 900 RELATED ID: 3RFM   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH CAFFEINE                             
DBREF  3UZA A    1   317  UNP    P29274   AA2AR_HUMAN      1    317             
SEQADV 3UZA LEU A   54  UNP  P29274    ALA    54 ENGINEERED MUTATION            
SEQADV 3UZA ALA A   88  UNP  P29274    THR    88 ENGINEERED MUTATION            
SEQADV 3UZA ALA A  107  UNP  P29274    ARG   107 ENGINEERED MUTATION            
SEQADV 3UZA ALA A  122  UNP  P29274    LYS   122 ENGINEERED MUTATION            
SEQADV 3UZA ALA A  202  UNP  P29274    LEU   202 ENGINEERED MUTATION            
SEQADV 3UZA ALA A  235  UNP  P29274    LEU   235 ENGINEERED MUTATION            
SEQADV 3UZA ALA A  239  UNP  P29274    VAL   239 ENGINEERED MUTATION            
SEQADV 3UZA ALA A  277  UNP  P29274    SER   277 ENGINEERED MUTATION            
SEQADV 3UZA ALA A  318  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZA ALA A  319  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZA HIS A  320  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZA HIS A  321  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZA HIS A  322  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZA HIS A  323  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZA HIS A  324  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZA HIS A  325  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZA HIS A  326  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZA HIS A  327  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZA HIS A  328  UNP  P29274              EXPRESSION TAG                 
SEQADV 3UZA 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    T4G  A 330      21                                                       
HETNAM     T4G 6-(2,6-DIMETHYLPYRIDIN-4-YL)-5-PHENYL-1,2,4-TRIAZIN-3-           
HETNAM   2 T4G  AMINE                                                           
FORMUL   2  T4G    C16 H15 N5                                                   
HELIX    1   1 SER A    7  ASN A   34  1                                  28    
HELIX    2   2 THR A   41  LEU A   58  1                                  18    
HELIX    3   3 LEU A   58  GLY A   69  1                                  12    
HELIX    4   4 ALA A   73  ILE A  108  1                                  36    
HELIX    5   5 ILE A  108  VAL A  116  1                                   9    
HELIX    6   6 THR A  117  LEU A  137  1                                  21    
HELIX    7   7 THR A  138  GLY A  142  5                                   5    
HELIX    8   8 LEU A  167  VAL A  172  1                                   6    
HELIX    9   9 PRO A  173  TYR A  179  1                                   7    
HELIX   10  10 VAL A  186  MET A  211  1                                  26    
HELIX   11  11 GLU A  212  GLN A  214  5                                   3    
HELIX   12  12 GLY A  218  CYS A  259  1                                  42    
HELIX   13  13 PRO A  266  ILE A  292  1                                  27    
HELIX   14  14 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  6 PHE A 168  MET A 177  LEU A 249  HIS A 250                    
SITE     2 AC1  6 ASN A 253  ILE A 274                                          
CRYST1  111.814  111.896  125.841  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      0.008943  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008937  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007947        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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