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Database: PDB
Entry: 3VGA
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Original site: 3VGA 
HEADER    SIGNALING PROTEIN                       04-AUG-11   3VGA              
TITLE     CRYSTAL STRUCTURE OF HUMAN ADENOSINE A2A RECEPTOR WITH AN ALLOSTERIC  
TITLE    2 INVERSE-AGONIST ANTIBODY AT 3.1 A RESOLUTION                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADENOSINE RECEPTOR A2A;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-316;                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: ANTIBODY FAB FRAGMENT LIGHT CHAIN;                         
COMPND   9 CHAIN: B;                                                            
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: ANTIBODY FAB FRAGMENT HEAVY CHAIN;                         
COMPND  12 CHAIN: C                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ADORA2A, ADORA2;                                               
SOURCE   6 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PPIC9K;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  12 ORGANISM_COMMON: MOUSE;                                              
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 MOL_ID: 3;                                                           
SOURCE  15 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  16 ORGANISM_COMMON: MOUSE;                                              
SOURCE  17 ORGANISM_TAXID: 10090                                                
KEYWDS    7 TRANSMEMBRANE RECEPTOR, SIGNAL TRANSDUCTION, SIGNALING PROTEIN      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.HINO,T.ARAKAWA,H.IWANARI,T.YURUGI-KOBAYASHI,C.IKEDA-SUNO,Y.NAKADA-  
AUTHOR   2 NAKURA,O.KUSANO-ARAI,S.WEYAND,T.SHIMAMURA,N.NOMURA,A.D.CAMERON,      
AUTHOR   3 T.KOBAYASHI,T.HAMAKUBO,S.IWATA,T.MURATA                              
REVDAT   2   15-FEB-12 3VGA    1       JRNL                                     
REVDAT   1   01-FEB-12 3VGA    0                                                
JRNL        AUTH   T.HINO,T.ARAKAWA,H.IWANARI,T.YURUGI-KOBAYASHI,C.IKEDA-SUNO,  
JRNL        AUTH 2 Y.NAKADA-NAKURA,O.KUSANO-ARAI,S.WEYAND,T.SHIMAMURA,N.NOMURA, 
JRNL        AUTH 3 A.D.CAMERON,T.KOBAYASHI,T.HAMAKUBO,S.IWATA,T.MURATA          
JRNL        TITL   G-PROTEIN-COUPLED RECEPTOR INACTIVATION BY AN ALLOSTERIC     
JRNL        TITL 2 INVERSE-AGONIST ANTIBODY                                     
JRNL        REF    NATURE                        V. 482   237 2012              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   22286059                                                     
JRNL        DOI    10.1038/NATURE10750                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.1_743)                    
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 : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 17901                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.130                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 968                             
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 19.9969 -  5.8866    0.85     2518   151  0.2252 0.2838        
REMARK   3     2  5.8866 -  4.6922    0.90     2612   135  0.1722 0.2451        
REMARK   3     3  4.6922 -  4.1049    0.86     2498   132  0.1564 0.2259        
REMARK   3     4  4.1049 -  3.7323    0.90     2584   158  0.1779 0.2710        
REMARK   3     5  3.7323 -  3.4662    0.88     2523   137  0.2033 0.2460        
REMARK   3     6  3.4662 -  3.2628    0.89     2575   114  0.2224 0.2869        
REMARK   3     7  3.2628 -  3.1000    0.90     2591   141  0.2614 0.3167        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 0.60                                          
REMARK   3   SHRINKAGE RADIUS   : 0.27                                          
REMARK   3   K_SOL              : 0.30                                          
REMARK   3   B_SOL              : 58.17                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.830            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.760           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 79.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -15.73960                                            
REMARK   3    B22 (A**2) : 6.80060                                              
REMARK   3    B33 (A**2) : 8.93910                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -9.55300                                             
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      :  0.008           5768                                  
REMARK   3   ANGLE     :  1.278           7850                                  
REMARK   3   CHIRALITY :  0.084            902                                  
REMARK   3   PLANARITY :  0.006            980                                  
REMARK   3   DIHEDRAL  : 17.053           2007                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A'                                              
REMARK   3    ORIGIN FOR THE GROUP (A):  62.7650  -8.8708  36.3356              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.4586 T22:   0.8223                                     
REMARK   3      T33:  -0.0638 T12:   0.0402                                     
REMARK   3      T13:  -0.2764 T23:  -0.1037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9795 L22:   1.4776                                     
REMARK   3      L33:   1.7749 L12:   0.0699                                     
REMARK   3      L13:  -0.6019 L23:   0.3411                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0755 S12:  -0.6853 S13:  -0.0693                       
REMARK   3      S21:   0.5246 S22:   0.1228 S23:  -0.6416                       
REMARK   3      S31:  -0.0417 S32:   0.8520 S33:   0.0461                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'C'                                              
REMARK   3    ORIGIN FOR THE GROUP (A):  19.7508   1.4067   0.0609              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3953 T22:   0.2013                                     
REMARK   3      T33:   0.4645 T12:  -0.0364                                     
REMARK   3      T13:   0.0060 T23:   0.0775                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9038 L22:   0.8705                                     
REMARK   3      L33:   1.1396 L12:   0.7196                                     
REMARK   3      L13:   1.6861 L23:   0.2871                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2429 S12:   0.1178 S13:   0.6495                       
REMARK   3      S21:  -0.0755 S22:  -0.0260 S23:   0.0882                       
REMARK   3      S31:  -0.2084 S32:   0.0898 S33:   0.2253                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'B'                                              
REMARK   3    ORIGIN FOR THE GROUP (A):  20.4190 -15.9471  -4.7868              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3184 T22:   0.3262                                     
REMARK   3      T33:   0.3417 T12:   0.0975                                     
REMARK   3      T13:   0.0384 T23:  -0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9493 L22:   1.3228                                     
REMARK   3      L33:   2.8884 L12:   0.2629                                     
REMARK   3      L13:   2.6339 L23:   0.5871                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1956 S12:   0.7483 S13:  -0.0005                       
REMARK   3      S21:  -0.2767 S22:  -0.0522 S23:   0.0071                       
REMARK   3      S31:   0.0717 S32:   0.4044 S33:  -0.1589                       
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 3VGA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-AUG-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB095008.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : 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) : 0.9795                             
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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18451                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 71.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.8                               
REMARK 200  DATA REDUNDANCY                : 2.300                              
REMARK 200  R MERGE                    (I) : 0.10900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.63600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
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: PDB ENTRY 1VGA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 400, 0.1M MES, 0.2M MAGNESIUM    
REMARK 280  CHLORIDE, 0.5% OCTHYL THIOGLUCOSIDE , PH 6.5, VAPOR DIFFUSION,      
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        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       60.15650            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.88300            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       60.15650            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       44.88300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH C 231  LIES ON A SPECIAL POSITION.                          
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     PRO A   149                                                      
REMARK 465     LYS A   150                                                      
REMARK 465     GLU A   151                                                      
REMARK 465     GLY A   152                                                      
REMARK 465     LYS A   153                                                      
REMARK 465     GLN A   154                                                      
REMARK 465     HIS A   155                                                      
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     HIS A   317                                                      
REMARK 465     HIS A   318                                                      
REMARK 465     HIS 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     GLU B   213                                                      
REMARK 465     CYS B   214                                                      
REMARK 465     CYS C   139                                                      
REMARK 465     GLY C   140                                                      
REMARK 465     ASP C   141                                                      
REMARK 465     THR C   142                                                      
REMARK 465     SER C   143                                                      
REMARK 465     PRO C   226                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 220    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 222    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 212    O    CG   OD1  ND2                                  
REMARK 470     LYS C  43    CG   CD   CE   NZ                                   
REMARK 470     GLY C 225    O                                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CB   CYS A   259     SG   CYS A   262              1.74            
REMARK 500   O    ILE B    29     O    SER B    31              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  58      -66.94   -107.33                                   
REMARK 500    CYS A 146      -75.80    -91.82                                   
REMARK 500    GLU A 161       66.70     39.13                                   
REMARK 500    PHE A 182      -74.28    -97.37                                   
REMARK 500    VAL A 186      -62.49   -128.54                                   
REMARK 500    LEU A 216      149.82     72.33                                   
REMARK 500    PRO A 260       43.66    -76.92                                   
REMARK 500    ASP A 261      -61.07   -134.66                                   
REMARK 500    PRO A 266     -172.50    -66.33                                   
REMARK 500    SER A 305      -71.71   -117.90                                   
REMARK 500    TYR B  30     -124.64     62.87                                   
REMARK 500    SER B  32        9.31     98.46                                   
REMARK 500    LEU B  47      -64.15   -108.49                                   
REMARK 500    ALA B  51      -26.10     77.37                                   
REMARK 500    SER B  67      166.32    179.98                                   
REMARK 500    ARG B  77       73.91     45.00                                   
REMARK 500    LYS B 169      -70.14    -99.03                                   
REMARK 500    ASN B 190      -61.17    -90.48                                   
REMARK 500    LYS C  43      -73.96   -130.27                                   
REMARK 500    ALA C  92     -177.43   -173.36                                   
REMARK 500    PRO C 137     -166.29    -68.26                                   
REMARK 500    SER C 171      -70.30   -100.31                                   
REMARK 500    SER C 183     -115.27     51.57                                   
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                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3VG9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ADENOSINE A2A RECEPTOR WITH AN            
REMARK 900 ALLOSTERIC INVERSE-AGONIST ANTIBODY AT 2.7 A RESOLUTION              
DBREF  3VGA A    1   316  UNP    P29274   AA2AR_HUMAN      1    316             
DBREF  3VGA B    1   214  PDB    3VGA     3VGA             1    214             
DBREF  3VGA C    1   226  PDB    3VGA     3VGA             1    226             
SEQADV 3VGA GLN A  154  UNP  P29274    ASN   154 ENGINEERED MUTATION            
SEQADV 3VGA HIS A  317  UNP  P29274              EXPRESSION TAG                 
SEQADV 3VGA HIS A  318  UNP  P29274              EXPRESSION TAG                 
SEQADV 3VGA HIS A  319  UNP  P29274              EXPRESSION TAG                 
SEQADV 3VGA HIS A  320  UNP  P29274              EXPRESSION TAG                 
SEQADV 3VGA HIS A  321  UNP  P29274              EXPRESSION TAG                 
SEQADV 3VGA HIS A  322  UNP  P29274              EXPRESSION TAG                 
SEQADV 3VGA HIS A  323  UNP  P29274              EXPRESSION TAG                 
SEQADV 3VGA HIS A  324  UNP  P29274              EXPRESSION TAG                 
SEQADV 3VGA HIS A  325  UNP  P29274              EXPRESSION TAG                 
SEQADV 3VGA HIS A  326  UNP  P29274              EXPRESSION TAG                 
SEQRES   1 A  326  MET PRO ILE MET GLY SER SER VAL TYR ILE THR VAL GLU          
SEQRES   2 A  326  LEU ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU          
SEQRES   3 A  326  VAL CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN ASN          
SEQRES   4 A  326  VAL THR ASN TYR PHE VAL VAL SER LEU ALA ALA ALA ASP          
SEQRES   5 A  326  ILE ALA VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE THR          
SEQRES   6 A  326  ILE SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU          
SEQRES   7 A  326  PHE ILE ALA CYS PHE VAL LEU VAL LEU THR GLN SER SER          
SEQRES   8 A  326  ILE PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE          
SEQRES   9 A  326  ALA ILE ARG ILE PRO LEU ARG TYR ASN GLY LEU VAL THR          
SEQRES  10 A  326  GLY THR ARG ALA LYS GLY ILE ILE ALA ILE CYS TRP VAL          
SEQRES  11 A  326  LEU SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY TRP          
SEQRES  12 A  326  ASN ASN CYS GLY GLN PRO LYS GLU GLY LYS GLN HIS SER          
SEQRES  13 A  326  GLN GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU          
SEQRES  14 A  326  ASP VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN PHE          
SEQRES  15 A  326  PHE ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU GLY          
SEQRES  16 A  326  VAL TYR LEU ARG ILE PHE LEU ALA ALA ARG ARG GLN LEU          
SEQRES  17 A  326  LYS GLN MET GLU SER GLN PRO LEU PRO GLY GLU ARG ALA          
SEQRES  18 A  326  ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS SER          
SEQRES  19 A  326  LEU ALA ILE ILE VAL GLY LEU PHE ALA LEU CYS TRP LEU          
SEQRES  20 A  326  PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS PRO          
SEQRES  21 A  326  ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU ALA          
SEQRES  22 A  326  ILE VAL LEU SER HIS THR ASN SER VAL VAL ASN PRO PHE          
SEQRES  23 A  326  ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR PHE          
SEQRES  24 A  326  ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN GLN GLU          
SEQRES  25 A  326  PRO PHE LYS ALA HIS HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES  26 A  326  HIS                                                          
SEQRES   1 B  214  ASP ILE VAL MET THR GLN SER PRO ALA SER LEU SER ALA          
SEQRES   2 B  214  SER VAL GLY ASP THR VAL THR ILE THR CYS ARG ALA SER          
SEQRES   3 B  214  GLU PHE ILE TYR SER SER LEU THR TRP TYR GLN GLN LYS          
SEQRES   4 B  214  GLN GLY GLY SER PRO GLN LEU LEU VAL TYR ALA ALA THR          
SEQRES   5 B  214  ASN LEU ALA ASP ALA VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 B  214  GLY SER GLY THR GLN PHE SER LEU LYS ILE ASN ARG LEU          
SEQRES   7 B  214  GLN PRO GLU ASP PHE GLY THR TYR TYR CYS GLN HIS PHE          
SEQRES   8 B  214  TYR GLY SER THR TRP ALA PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 B  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 B  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 B  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 B  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 B  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 B  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 B  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 B  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 B  214  PHE ASN ARG ASN GLU CYS                                      
SEQRES   1 C  226  GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 C  226  PRO GLY SER SER VAL LYS ILE SER CYS LYS THR SER GLY          
SEQRES   3 C  226  ASP SER PHE THR ALA TYR ASN MET ASN TRP VAL LYS GLN          
SEQRES   4 C  226  SER HIS GLY LYS SER LEU GLU TRP ILE GLY ASN ILE ASN          
SEQRES   5 C  226  PRO TYR TYR GLY SER THR ARG TYR ASN GLN LYS PHE LYS          
SEQRES   6 C  226  GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR          
SEQRES   7 C  226  ALA TYR ILE GLN LEU ASN SER LEU THR SER GLU ASP SER          
SEQRES   8 C  226  ALA VAL TYR TYR CYS ALA ARG GLU GLY ASN TYR TYR ASP          
SEQRES   9 C  226  GLY GLY SER VAL ARG TYR PHE ASP TYR TRP GLY GLN GLY          
SEQRES  10 C  226  THR THR LEU THR VAL SER SER ALA LYS THR THR ALA PRO          
SEQRES  11 C  226  SER VAL TYR PRO LEU ALA PRO VAL CYS GLY ASP THR SER          
SEQRES  12 C  226  GLY SER SER VAL THR LEU GLY CYS LEU VAL LYS GLY TYR          
SEQRES  13 C  226  PHE PRO GLU PRO VAL THR LEU THR TRP ASN SER GLY SER          
SEQRES  14 C  226  LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN          
SEQRES  15 C  226  SER ASP LEU TYR THR LEU SER SER SER VAL THR VAL THR          
SEQRES  16 C  226  SER SER THR TRP PRO SER GLN SER ILE THR CYS ASN VAL          
SEQRES  17 C  226  ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE          
SEQRES  18 C  226  GLU PRO ARG GLY PRO                                          
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   4  ZMA    C16 H15 N7 O2                                                
FORMUL   5  HOH   *14(H2 O)                                                     
HELIX    1   1 SER A    6  ASN A   34  1                                  29    
HELIX    2   2 SER A   35  GLN A   38  5                                   4    
HELIX    3   3 ASN A   39  LEU A   58  1                                  20    
HELIX    4   4 LEU A   58  ILE A   66  1                                   9    
HELIX    5   5 ALA A   73  CYS A   82  1                                  10    
HELIX    6   6 CYS A   82  ILE A  108  1                                  27    
HELIX    7   7 ILE A  108  VAL A  116  1                                   9    
HELIX    8   8 THR A  117  LEU A  137  1                                  21    
HELIX    9   9 THR A  138  LEU A  141  5                                   4    
HELIX   10  10 LEU A  167  VAL A  172  1                                   6    
HELIX   11  11 PRO A  173  TYR A  179  1                                   7    
HELIX   12  12 VAL A  186  SER A  213  1                                  28    
HELIX   13  13 ALA A  221  PHE A  258  1                                  38    
HELIX   14  14 PRO A  266  THR A  279  1                                  14    
HELIX   15  15 VAL A  282  ILE A  292  1                                  11    
HELIX   16  16 ILE A  292  VAL A  307  1                                  16    
HELIX   17  17 GLN B   79  PHE B   83  5                                   5    
HELIX   18  18 SER B  121  THR B  126  1                                   6    
HELIX   19  19 LYS B  183  GLU B  187  1                                   5    
HELIX   20  20 SER C   28  TYR C   32  5                                   5    
HELIX   21  21 GLN C   62  LYS C   65  5                                   4    
HELIX   22  22 THR C   87  SER C   91  5                                   5    
HELIX   23  23 SER C  167  SER C  169  5                                   3    
HELIX   24  24 PRO C  211  SER C  214  5                                   4    
SHEET    1   A 2 CYS A  71  ALA A  72  0                                        
SHEET    2   A 2 VAL A 164  ALA A 165 -1  O  VAL A 164   N  ALA A  72           
SHEET    1   B 4 MET B   4  SER B   7  0                                        
SHEET    2   B 4 VAL B  19  ALA B  25 -1  O  THR B  22   N  SER B   7           
SHEET    3   B 4 GLN B  70  ILE B  75 -1  O  ILE B  75   N  VAL B  19           
SHEET    4   B 4 PHE B  62  SER B  67 -1  N  SER B  63   O  LYS B  74           
SHEET    1   C 6 SER B  10  ALA B  13  0                                        
SHEET    2   C 6 THR B 102  ILE B 106  1  O  GLU B 105   N  LEU B  11           
SHEET    3   C 6 GLY B  84  HIS B  90 -1  N  TYR B  86   O  THR B 102           
SHEET    4   C 6 LEU B  33  GLN B  38 -1  N  TYR B  36   O  TYR B  87           
SHEET    5   C 6 GLN B  45  TYR B  49 -1  O  LEU B  47   N  TRP B  35           
SHEET    6   C 6 ASN B  53  LEU B  54 -1  O  ASN B  53   N  TYR B  49           
SHEET    1   D 4 SER B  10  ALA B  13  0                                        
SHEET    2   D 4 THR B 102  ILE B 106  1  O  GLU B 105   N  LEU B  11           
SHEET    3   D 4 GLY B  84  HIS B  90 -1  N  TYR B  86   O  THR B 102           
SHEET    4   D 4 ALA B  97  PHE B  98 -1  O  ALA B  97   N  HIS B  90           
SHEET    1   E 4 THR B 114  PHE B 118  0                                        
SHEET    2   E 4 GLY B 129  PHE B 139 -1  O  ASN B 137   N  THR B 114           
SHEET    3   E 4 TYR B 173  THR B 182 -1  O  TYR B 173   N  PHE B 139           
SHEET    4   E 4 VAL B 159  TRP B 163 -1  N  SER B 162   O  SER B 176           
SHEET    1   F 4 SER B 153  ARG B 155  0                                        
SHEET    2   F 4 ASN B 145  ILE B 150 -1  N  ILE B 150   O  SER B 153           
SHEET    3   F 4 SER B 191  HIS B 198 -1  O  THR B 193   N  LYS B 149           
SHEET    4   F 4 SER B 201  ASN B 210 -1  O  ILE B 205   N  ALA B 196           
SHEET    1   G 4 GLN C   3  GLN C   6  0                                        
SHEET    2   G 4 VAL C  18  SER C  25 -1  O  LYS C  23   N  GLN C   5           
SHEET    3   G 4 THR C  78  LEU C  83 -1  O  ILE C  81   N  ILE C  20           
SHEET    4   G 4 ALA C  68  ASP C  73 -1  N  THR C  71   O  TYR C  80           
SHEET    1   H 6 GLU C  10  VAL C  12  0                                        
SHEET    2   H 6 THR C 118  VAL C 122  1  O  THR C 119   N  GLU C  10           
SHEET    3   H 6 ALA C  92  TYR C 103 -1  N  ALA C  92   O  LEU C 120           
SHEET    4   H 6 MET C  34  SER C  40 -1  N  GLN C  39   O  VAL C  93           
SHEET    5   H 6 SER C  44  ILE C  51 -1  O  ILE C  51   N  MET C  34           
SHEET    6   H 6 THR C  58  TYR C  60 -1  O  ARG C  59   N  ASN C  50           
SHEET    1   I 4 GLU C  10  VAL C  12  0                                        
SHEET    2   I 4 THR C 118  VAL C 122  1  O  THR C 119   N  GLU C  10           
SHEET    3   I 4 ALA C  92  TYR C 103 -1  N  ALA C  92   O  LEU C 120           
SHEET    4   I 4 SER C 107  TRP C 114 -1  O  TYR C 113   N  ARG C  98           
SHEET    1   J 4 SER C 131  LEU C 135  0                                        
SHEET    2   J 4 SER C 146  TYR C 156 -1  O  GLY C 150   N  LEU C 135           
SHEET    3   J 4 LEU C 185  THR C 195 -1  O  LEU C 188   N  VAL C 153           
SHEET    4   J 4 VAL C 174  THR C 176 -1  N  HIS C 175   O  SER C 191           
SHEET    1   K 4 SER C 131  LEU C 135  0                                        
SHEET    2   K 4 SER C 146  TYR C 156 -1  O  GLY C 150   N  LEU C 135           
SHEET    3   K 4 LEU C 185  THR C 195 -1  O  LEU C 188   N  VAL C 153           
SHEET    4   K 4 VAL C 180  GLN C 182 -1  N  GLN C 182   O  LEU C 185           
SHEET    1   L 3 THR C 162  TRP C 165  0                                        
SHEET    2   L 3 THR C 205  HIS C 210 -1  O  ASN C 207   N  THR C 164           
SHEET    3   L 3 THR C 215  LYS C 220 -1  O  LYS C 219   N  CYS C 206           
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  2.04  
SSBOND   5 CYS B   23    CYS B   88                          1555   1555  2.04  
SSBOND   6 CYS B  134    CYS B  194                          1555   1555  2.04  
SSBOND   7 CYS C   22    CYS C   96                          1555   1555  2.03  
SSBOND   8 CYS C  151    CYS C  206                          1555   1555  2.03  
CISPEP   1 GLY A  218    GLU A  219          0         3.64                     
CISPEP   2 SER B    7    PRO B    8          0        -6.28                     
CISPEP   3 TYR B  140    PRO B  141          0         1.62                     
CISPEP   4 PHE C  157    PRO C  158          0        -7.32                     
CISPEP   5 GLU C  159    PRO C  160          0        -9.31                     
CISPEP   6 TRP C  199    PRO C  200          0         0.22                     
SITE     1 AC1  7 LEU A  85  PHE A 168  GLU A 169  MET A 177                    
SITE     2 AC1  7 LEU A 249  HIS A 250  MET A 270                               
CRYST1  120.313   89.766  110.682  90.00  96.14  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008312  0.000000  0.000894        0.00000                         
SCALE2      0.000000  0.011140  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009087        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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