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Database: PDB
Entry: 4UHR
LinkDB: 4UHR
Original site: 4UHR 
HEADER    SIGNALING PROTEIN                       25-MAR-15   4UHR              
TITLE     THERMOSTABILISED HUMAN A2A RECEPTOR WITH CGS21680 BOUND               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THERMOSTABILISED HUMAN A2A RECEPTOR;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 OTHER_DETAILS: THE CONSTRUCT WAS TRUNCATED AFTER RESIDUE 316 OF THE  
COMPND   7 A2A SEQUENCE, BUT HAS AN 9 RESIDUE SEQUENCE THAT INCLUDES A LINKER   
COMPND   8 AND THE TEV CLEAVAGE SEQUENCE (AAAENLYFQ) AT THE C-TERMINUS          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: BRAIN;                                                       
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PBACPAK8                                  
KEYWDS    SIGNALING PROTEIN, SIGANLING PROTEIN, G PROTEIN COUPLED RECEPTOR,     
KEYWDS   2 SEVEN-HELIX RECEPTOR, INTEGRAL MEMBRANE PROTEIN, AGONIST BOUND FORM, 
KEYWDS   3 THERMOSTABILISING POINT MUTATIONS, GPCR, 7TM RECEPTOR                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.LEBON,P.C.EDWARDS,A.G.W.LESLIE,C.G.TATE                             
REVDAT   3   03-APR-19 4UHR    1       SOURCE                                   
REVDAT   2   13-MAY-15 4UHR    1       JRNL                                     
REVDAT   1   08-APR-15 4UHR    0                                                
JRNL        AUTH   G.LEBON,P.C.EDWARDS,A.G.W.LESLIE,C.G.TATE                    
JRNL        TITL   MOLECULAR DETERMINANTS OF CGS21680 BINDING TO THE HUMAN      
JRNL        TITL 2 ADENOSINE A2A RECEPTOR.                                      
JRNL        REF    MOL.PHARMACOL.                V.  87   907 2015              
JRNL        REFN                   ISSN 0026-895X                               
JRNL        PMID   25762024                                                     
JRNL        DOI    10.1124/MOL.114.097360                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 64.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 12883                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.261                           
REMARK   3   R VALUE            (WORKING SET) : 0.259                           
REMARK   3   FREE R VALUE                     : 0.312                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 679                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 914                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.42                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3220                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 55                           
REMARK   3   BIN FREE R VALUE                    : 0.3310                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2401                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 9                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.77000                                             
REMARK   3    B22 (A**2) : 3.86000                                              
REMARK   3    B33 (A**2) : -2.02000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.80000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.619         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.366         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.282         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.395        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.909                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.871                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2502 ; 0.006 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3412 ; 1.023 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   307 ; 4.473 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    92 ;31.457 ;22.174       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   390 ;15.633 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;16.110 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   402 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1839 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4UHR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1290063446.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8726                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13563                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.340                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.900                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 2YDO                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M ACETATE-HCL (PH4.8), 6%           
REMARK 280  SUCROSE, 21.9% PENTHAETHYLENE GLYCOL                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       29.59350            
REMARK 290   SMTRY3   2  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 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     HIS A   155                                                      
REMARK 465     SER A   156                                                      
REMARK 465     GLN A   157                                                      
REMARK 465     SER A   263                                                      
REMARK 465     GLU A   320                                                      
REMARK 465     ASN A   321                                                      
REMARK 465     LEU A   322                                                      
REMARK 465     TYR A   323                                                      
REMARK 465     PHE A   324                                                      
REMARK 465     GLN A   325                                                      
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     LEU A 216    CG   CD1  CD2                                       
REMARK 470     GLU A 219    CG   CD   OE1  OE2                                  
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    PHE A 180      -63.39    -98.65                                   
REMARK 500    GLN A 214       64.83     38.84                                   
REMARK 500    ASP A 261      -89.79    -69.83                                   
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 NGI A 1320                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4UG2   RELATED DB: PDB                                   
REMARK 900 THERMOSTABILISED HUMAN A2A RECEPTOR WITH CGS21680 BOUND              
DBREF  4UHR A    1   317  UNP    P29274   AA2AR_HUMAN      1    317             
SEQADV 4UHR ALA A  318  UNP  P29274              EXPRESSION TAG                 
SEQADV 4UHR ALA A  319  UNP  P29274              EXPRESSION TAG                 
SEQADV 4UHR GLU A  320  UNP  P29274              EXPRESSION TAG                 
SEQADV 4UHR ASN A  321  UNP  P29274              EXPRESSION TAG                 
SEQADV 4UHR LEU A  322  UNP  P29274              EXPRESSION TAG                 
SEQADV 4UHR TYR A  323  UNP  P29274              EXPRESSION TAG                 
SEQADV 4UHR PHE A  324  UNP  P29274              EXPRESSION TAG                 
SEQADV 4UHR GLN A  325  UNP  P29274              EXPRESSION TAG                 
SEQADV 4UHR ALA A   48  UNP  P29274    LEU    48 ENGINEERED MUTATION            
SEQADV 4UHR LEU A   54  UNP  P29274    ALA    54 ENGINEERED MUTATION            
SEQADV 4UHR ALA A   65  UNP  P29274    THR    65 ENGINEERED MUTATION            
SEQADV 4UHR ALA A   89  UNP  P29274    GLN    89 ENGINEERED MUTATION            
SEQADV 4UHR ALA A  154  UNP  P29274    ASN   154 ENGINEERED MUTATION            
SEQRES   1 A  325  MET PRO ILE MET GLY SER SER VAL TYR ILE THR VAL GLU          
SEQRES   2 A  325  LEU ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU          
SEQRES   3 A  325  VAL CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN ASN          
SEQRES   4 A  325  VAL THR ASN TYR PHE VAL VAL SER ALA ALA ALA ALA ASP          
SEQRES   5 A  325  ILE LEU VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE ALA          
SEQRES   6 A  325  ILE SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU          
SEQRES   7 A  325  PHE ILE ALA CYS PHE VAL LEU VAL LEU THR ALA SER SER          
SEQRES   8 A  325  ILE PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE          
SEQRES   9 A  325  ALA ILE ARG ILE PRO LEU ARG TYR ASN GLY LEU VAL THR          
SEQRES  10 A  325  GLY THR ARG ALA LYS GLY ILE ILE ALA ILE CYS TRP VAL          
SEQRES  11 A  325  LEU SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY TRP          
SEQRES  12 A  325  ASN ASN CYS GLY GLN PRO LYS GLU GLY LYS ALA HIS SER          
SEQRES  13 A  325  GLN GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU          
SEQRES  14 A  325  ASP VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN PHE          
SEQRES  15 A  325  PHE ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU GLY          
SEQRES  16 A  325  VAL TYR LEU ARG ILE PHE LEU ALA ALA ARG ARG GLN LEU          
SEQRES  17 A  325  LYS GLN MET GLU SER GLN PRO LEU PRO GLY GLU ARG ALA          
SEQRES  18 A  325  ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS SER          
SEQRES  19 A  325  LEU ALA ILE ILE VAL GLY LEU PHE ALA LEU CYS TRP LEU          
SEQRES  20 A  325  PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS PRO          
SEQRES  21 A  325  ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU ALA          
SEQRES  22 A  325  ILE VAL LEU SER HIS THR ASN SER VAL VAL ASN PRO PHE          
SEQRES  23 A  325  ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR PHE          
SEQRES  24 A  325  ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN GLN GLU          
SEQRES  25 A  325  PRO PHE LYS ALA ALA ALA ALA GLU ASN LEU TYR PHE GLN          
HET    NGI  A1320      36                                                       
HETNAM     NGI 2-[P-(2-CARBOXYETHYL)PHENYLETHYL-AMINO]-5'-N-                    
HETNAM   2 NGI  ETHYLCARBOXAMIDO ADENOSINE                                      
FORMUL   2  NGI    C23 H29 N7 O6                                                
FORMUL   3  HOH   *9(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  GLY A   69  1                                  12    
HELIX    5   5 ALA A   73  ILE A  108  1                                  36    
HELIX    6   6 ARG A  111  VAL A  116  1                                   6    
HELIX    7   7 THR A  117  LEU A  137  1                                  21    
HELIX    8   8 THR A  138  GLY A  142  5                                   5    
HELIX    9   9 LYS A  150  ALA A  154  5                                   5    
HELIX   10  10 LEU A  167  VAL A  172  1                                   6    
HELIX   11  11 PRO A  173  PHE A  180  1                                   8    
HELIX   12  12 PHE A  180  VAL A  186  1                                   7    
HELIX   13  13 VAL A  186  SER A  213  1                                  28    
HELIX   14  14 GLU A  219  CYS A  259  1                                  41    
HELIX   15  15 PRO A  266  THR A  279  1                                  14    
HELIX   16  16 THR A  279  ASN A  284  1                                   6    
HELIX   17  17 PRO A  285  ILE A  292  1                                   8    
HELIX   18  18 ILE A  292  GLU A  312  1                                  21    
HELIX   19  19 PRO A  313  LYS A  315  5                                   3    
SHEET    1  AA 2 CYS A  71  ALA A  72  0                                        
SHEET    2  AA 2 VAL A 164  ALA A 165 -1  O  VAL A 164   N  ALA A  72           
SSBOND   1 CYS A   71    CYS A  159                          1555   1555  2.04  
SSBOND   2 CYS A   74    CYS A  146                          1555   1555  2.04  
SSBOND   3 CYS A   77    CYS A  166                          1555   1555  2.03  
SSBOND   4 CYS A  259    CYS A  262                          1555   1555  2.04  
CISPEP   1 LEU A  216    PRO A  217          0        -2.95                     
CISPEP   2 ASN A  284    PRO A  285          0         4.69                     
SITE     1 AC1 16 VAL A  84  LEU A  85  THR A  88  PHE A 168                    
SITE     2 AC1 16 GLU A 169  MET A 177  ASN A 181  TRP A 246                    
SITE     3 AC1 16 LEU A 249  HIS A 250  ASN A 253  LEU A 267                    
SITE     4 AC1 16 MET A 270  ILE A 274  SER A 277  HIS A 278                    
CRYST1   60.407   59.187   65.058  90.00  92.83  90.00 P 1 21 1      2          
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      0.016554  0.000000  0.000818        0.00000                         
SCALE2      0.000000  0.016896  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015390        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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