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Database: PDB
Entry: 4EIY
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HEADER    MEMBRANE PROTEIN                        06-APR-12   4EIY              
TITLE     CRYSTAL STRUCTURE OF THE CHIMERIC PROTEIN OF A2AAR-BRIL IN COMPLEX    
TITLE    2 WITH ZM241385 AT 1.8A RESOLUTION                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADENOSINE RECEPTOR A2A/SOLUBLE CYTOCHROME B562 CHIMERA;    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CYTOCHROME B-562;                                           
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;                 
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 562;                                           
SOURCE   5 GENE: AA2AR_HUMAN, ADORA2, ADORA2A, CYBC;                            
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC                                  
KEYWDS    NOVEL PROTEIN ENGINEERING, GPCR NETWORK, PSI-BIOLOGY, STRUCTURAL      
KEYWDS   2 GENOMICS, MEMBRANE PROTEIN, GPCR                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.LIU,E.CHUN,A.A.THOMPSON,P.CHUBUKOV,F.XU,V.KATRITCH,G.W.HAN,         
AUTHOR   2 L.H.HEITMAN,A.P.IJZERMAN,V.CHEREZOV,R.C.STEVENS,GPCR NETWORK (GPCR)  
REVDAT   4   13-SEP-23 4EIY    1       REMARK SEQADV LINK                       
REVDAT   3   16-AUG-17 4EIY    1       SOURCE REMARK                            
REVDAT   2   01-AUG-12 4EIY    1       JRNL                                     
REVDAT   1   25-JUL-12 4EIY    0                                                
JRNL        AUTH   W.LIU,E.CHUN,A.A.THOMPSON,P.CHUBUKOV,F.XU,V.KATRITCH,        
JRNL        AUTH 2 G.W.HAN,C.B.ROTH,L.H.HEITMAN,A.P.IJZERMAN,V.CHEREZOV,        
JRNL        AUTH 3 R.C.STEVENS                                                  
JRNL        TITL   STRUCTURAL BASIS FOR ALLOSTERIC REGULATION OF GPCRS BY       
JRNL        TITL 2 SODIUM IONS.                                                 
JRNL        REF    SCIENCE                       V. 337   232 2012              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   22798613                                                     
JRNL        DOI    10.1126/SCIENCE.1219218                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 42032                          
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) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2222                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2809                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.95                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2730                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 147                          
REMARK   3   BIN FREE R VALUE                    : 0.3290                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3012                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 481                                     
REMARK   3   SOLVENT ATOMS            : 177                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.05000                                              
REMARK   3    B22 (A**2) : -0.13000                                             
REMARK   3    B33 (A**2) : 0.09000                                              
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.122         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.119         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.076         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.764         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3653 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2680 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4891 ; 1.584 ; 2.065       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6560 ; 1.098 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   412 ; 4.711 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   124 ;38.746 ;23.548       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   524 ;13.558 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;21.081 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   550 ; 0.105 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3778 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   717 ; 0.001 ; 0.020       
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):  2011 ; 1.481 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   812 ; 0.450 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3253 ; 2.270 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1642 ; 4.026 ; 8.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1638 ; 5.791 ;11.000       
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  : 19                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -1        A    34                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.9918  -3.9454   6.8744              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0567 T22:   0.1036                                     
REMARK   3      T33:   0.0127 T12:   0.0019                                     
REMARK   3      T13:  -0.0020 T23:  -0.0040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3047 L22:  20.5751                                     
REMARK   3      L33:   3.2950 L12:   1.6923                                     
REMARK   3      L13:  -0.5264 L23:  -6.2518                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0484 S12:   0.0377 S13:   0.0063                       
REMARK   3      S21:   0.0644 S22:   0.1134 S23:   0.4664                       
REMARK   3      S31:  -0.1330 S32:  -0.1228 S33:  -0.1617                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    35        A    38                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.3295 -29.8316  14.7622              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2441 T22:   0.0949                                     
REMARK   3      T33:   0.5072 T12:  -0.0184                                     
REMARK   3      T13:  -0.0766 T23:   0.0845                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  19.5268 L22:  23.9520                                     
REMARK   3      L33:  15.0509 L12:  16.1895                                     
REMARK   3      L13: -12.9421 L23:  -2.7492                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9559 S12:   0.0523 S13:  -0.4134                       
REMARK   3      S21:  -0.1951 S22:   0.6010 S23:   0.4029                       
REMARK   3      S31:   1.1611 S32:   0.3751 S33:   0.3549                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    39        A    73                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1582  -5.0186  17.3034              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0468 T22:   0.0853                                     
REMARK   3      T33:   0.0164 T12:  -0.0017                                     
REMARK   3      T13:   0.0043 T23:   0.0083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7642 L22:   3.6582                                     
REMARK   3      L33:   1.3426 L12:  -1.0193                                     
REMARK   3      L13:   0.5252 L23:  -0.8230                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0068 S12:  -0.0812 S13:  -0.0569                       
REMARK   3      S21:  -0.0716 S22:   0.1231 S23:   0.1718                       
REMARK   3      S31:   0.0548 S32:  -0.1406 S33:  -0.1163                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    74        A   108                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.9496 -10.7814  24.2306              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0518 T22:   0.0923                                     
REMARK   3      T33:   0.0150 T12:  -0.0024                                     
REMARK   3      T13:  -0.0169 T23:   0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8666 L22:  14.9615                                     
REMARK   3      L33:   0.8786 L12:  -6.6088                                     
REMARK   3      L13:  -0.2160 L23:   0.1919                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1526 S12:  -0.1627 S13:   0.1288                       
REMARK   3      S21:   0.3771 S22:   0.1149 S23:  -0.3673                       
REMARK   3      S31:   0.0801 S32:   0.0110 S33:   0.0377                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   109        A   117                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.9067 -33.0684  28.5603              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3188 T22:   0.2568                                     
REMARK   3      T33:   0.1925 T12:  -0.0056                                     
REMARK   3      T13:  -0.0231 T23:   0.0979                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.8029 L22:  21.7072                                     
REMARK   3      L33:  10.3164 L12: -10.1338                                     
REMARK   3      L13:  -9.5771 L23:  -1.2422                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6072 S12:  -0.7783 S13:  -0.4910                       
REMARK   3      S21:  -0.0576 S22:   0.1444 S23:  -0.0296                       
REMARK   3      S31:   0.6201 S32:   0.6694 S33:   0.4628                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   118        A   137                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.8641 -13.8650  29.7137              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1981 T22:   0.1135                                     
REMARK   3      T33:   0.0599 T12:   0.0268                                     
REMARK   3      T13:  -0.0007 T23:   0.0262                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2035 L22:  21.4041                                     
REMARK   3      L33:   0.5095 L12:  -1.2283                                     
REMARK   3      L13:  -0.1009 L23:  -1.9229                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1843 S12:  -0.0734 S13:  -0.2107                       
REMARK   3      S21:   0.6621 S22:   0.2288 S23:   0.2235                       
REMARK   3      S31:   0.1749 S32:   0.0245 S33:  -0.0444                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   138        A   161                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.9818  17.0669  27.1623              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2985 T22:   0.1563                                     
REMARK   3      T33:   0.5053 T12:   0.0409                                     
REMARK   3      T13:   0.0697 T23:   0.0315                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1179 L22:   3.2583                                     
REMARK   3      L33:   3.7961 L12:  -3.8310                                     
REMARK   3      L13:   3.2495 L23:  -1.1023                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3817 S12:   0.1872 S13:   0.9081                       
REMARK   3      S21:   0.1153 S22:  -0.1820 S23:  -0.1317                       
REMARK   3      S31:  -0.8552 S32:  -0.0753 S33:   0.5638                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   162        A   186                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.4102   7.2803  25.4330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0515 T22:   0.0812                                     
REMARK   3      T33:   0.0453 T12:  -0.0136                                     
REMARK   3      T13:   0.0054 T23:  -0.0055                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6764 L22:   5.4095                                     
REMARK   3      L33:   2.3606 L12:  -3.7345                                     
REMARK   3      L13:   1.1163 L23:  -0.4474                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0343 S12:   0.0099 S13:   0.0618                       
REMARK   3      S21:  -0.0091 S22:  -0.0933 S23:   0.1967                       
REMARK   3      S31:  -0.1207 S32:   0.0175 S33:   0.0590                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   187        A   208                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.0473 -20.8720  21.8023              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1107 T22:   0.1176                                     
REMARK   3      T33:   0.1639 T12:   0.0272                                     
REMARK   3      T13:  -0.0205 T23:  -0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0881 L22:  21.8699                                     
REMARK   3      L33:   2.4787 L12:  -5.4485                                     
REMARK   3      L13:  -1.6028 L23:   6.2025                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0124 S12:  -0.0747 S13:   0.0098                       
REMARK   3      S21:   0.2971 S22:   0.1410 S23:  -0.8825                       
REMARK   3      S31:   0.1498 S32:   0.1408 S33:  -0.1286                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   219        A   259                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.6709 -13.3465  15.0381              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0731 T22:   0.0946                                     
REMARK   3      T33:   0.0742 T12:   0.0299                                     
REMARK   3      T13:   0.0115 T23:   0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7200 L22:   6.3930                                     
REMARK   3      L33:   0.8604 L12:   0.5337                                     
REMARK   3      L13:   0.2162 L23:   0.6548                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0305 S12:   0.0484 S13:  -0.1623                       
REMARK   3      S21:  -0.2663 S22:   0.1347 S23:  -0.3255                       
REMARK   3      S31:   0.1498 S32:   0.1210 S33:  -0.1042                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   260        A   265                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.1396  16.2083  17.3125              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2705 T22:   0.1962                                     
REMARK   3      T33:   0.2057 T12:   0.0384                                     
REMARK   3      T13:   0.0381 T23:   0.0520                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0264 L22:   8.2942                                     
REMARK   3      L33:  21.0838 L12:  -4.2003                                     
REMARK   3      L13:  10.9282 L23:  -1.6781                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9217 S12:  -0.0670 S13:   0.4910                       
REMARK   3      S21:   0.4595 S22:   0.5554 S23:  -0.6952                       
REMARK   3      S31:  -1.2802 S32:   0.4163 S33:   0.3662                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   266        A   292                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.4175  -5.0165   8.2951              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0569 T22:   0.1070                                     
REMARK   3      T33:   0.0179 T12:   0.0221                                     
REMARK   3      T13:   0.0004 T23:   0.0165                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9128 L22:  13.7330                                     
REMARK   3      L33:   1.1449 L12:   2.0947                                     
REMARK   3      L13:   0.4242 L23:   1.0745                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0166 S12:   0.0785 S13:   0.0003                       
REMARK   3      S21:  -0.4142 S22:  -0.0077 S23:  -0.0309                       
REMARK   3      S31:   0.0272 S32:   0.0363 S33:   0.0242                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   293        A   307                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.4870 -25.2207   2.7877              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3223 T22:   0.1721                                     
REMARK   3      T33:   0.1214 T12:  -0.0784                                     
REMARK   3      T13:  -0.0227 T23:  -0.0436                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  22.3732 L22:  11.2448                                     
REMARK   3      L33:  13.3027 L12:  -1.2770                                     
REMARK   3      L13:   6.3190 L23:  -0.0488                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2163 S12:   1.1420 S13:  -0.7201                       
REMARK   3      S21:  -0.9830 S22:  -0.0720 S23:   0.5361                       
REMARK   3      S31:   0.6687 S32:  -0.3328 S33:  -0.1443                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1001        A  1021                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.7603 -49.3985  16.1997              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2887 T22:   0.2415                                     
REMARK   3      T33:   0.6371 T12:   0.0665                                     
REMARK   3      T13:   0.1044 T23:   0.0185                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.3514 L22:  38.5212                                     
REMARK   3      L33:   1.7664 L12: -19.9233                                     
REMARK   3      L13:  -1.9101 L23:   1.4838                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2725 S12:   0.1460 S13:   0.4350                       
REMARK   3      S21:  -0.9890 S22:  -0.5419 S23:  -1.6647                       
REMARK   3      S31:   0.1872 S32:   0.1640 S33:   0.2694                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1022        A  1042                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.5547 -53.4454  25.5883              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3548 T22:   0.3251                                     
REMARK   3      T33:   0.8615 T12:   0.0591                                     
REMARK   3      T13:  -0.2118 T23:  -0.2213                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.2785 L22:  24.2101                                     
REMARK   3      L33:   6.7690 L12: -13.6158                                     
REMARK   3      L13:  -2.7492 L23:  -4.7961                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4648 S12:  -1.1799 S13:   1.7658                       
REMARK   3      S21:   1.0732 S22:   0.6136 S23:  -1.4639                       
REMARK   3      S31:  -0.5001 S32:   0.2215 S33:  -0.1488                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1058        A  1081                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.0374 -57.9403  23.7417              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2375 T22:   0.2831                                     
REMARK   3      T33:   0.5244 T12:   0.0551                                     
REMARK   3      T13:   0.0497 T23:   0.0772                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  27.1612 L22:  23.1118                                     
REMARK   3      L33:  13.8851 L12: -17.4107                                     
REMARK   3      L13:   8.3216 L23:  -9.6204                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4466 S12:  -1.3740 S13:   0.1430                       
REMARK   3      S21:   0.6583 S22:   1.3132 S23:   1.4145                       
REMARK   3      S31:  -0.2563 S32:  -1.0919 S33:  -0.8665                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1082        A  1093                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.5360 -65.9659  18.9084              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2893 T22:   0.1325                                     
REMARK   3      T33:   0.4557 T12:   0.0763                                     
REMARK   3      T13:   0.0226 T23:  -0.0142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  24.1901 L22:  18.4892                                     
REMARK   3      L33:  14.5502 L12: -14.5038                                     
REMARK   3      L13:   6.7759 L23:  -2.9948                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3005 S12:  -0.4649 S13:   0.2023                       
REMARK   3      S21:  -0.7867 S22:  -0.0522 S23:  -0.1043                       
REMARK   3      S31:   0.7266 S32:   0.2125 S33:   0.3527                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1094        A  1101                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.9315 -55.6010  12.9640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4562 T22:   0.1950                                     
REMARK   3      T33:   0.6100 T12:   0.0590                                     
REMARK   3      T13:  -0.1223 T23:   0.0722                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.3951 L22:  32.8026                                     
REMARK   3      L33:  15.6122 L12: -14.2936                                     
REMARK   3      L13:   8.2104 L23:   1.7017                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.4333 S12:   0.4974 S13:  -0.6457                       
REMARK   3      S21:  -1.9857 S22:  -0.4732 S23:   0.2107                       
REMARK   3      S31:   0.8320 S32:   0.4045 S33:  -0.9601                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1102        A  1106                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.8641 -47.5550  13.4572              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3548 T22:   0.1207                                     
REMARK   3      T33:   0.5447 T12:   0.0913                                     
REMARK   3      T13:  -0.1500 T23:   0.0082                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  44.0898 L22:  40.5722                                     
REMARK   3      L33:  16.1501 L12:   7.5080                                     
REMARK   3      L13:  -6.9520 L23: -11.0641                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2723 S12:  -0.4155 S13:  -1.6832                       
REMARK   3      S21:  -1.7480 S22:   0.1661 S23:   0.4682                       
REMARK   3      S31:   0.5312 S32:   0.0561 S33:   0.1062                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: 1. A SODIUM ION IS MODELLED BASED ON      
REMARK   3  CRYSTALLIZATION CONDITION AND COORDINATION GEOMETRY. SODIUM ION     
REMARK   3  IS COORDINATED IN AN OCTAHEDRAL GEOMETRY TO OD1 OF ASP52, OG OF     
REMARK   3  SER 91 AND THREE WATER MOLECULES OF HOH2529, HOH2552 AND            
REMARK   3  HOH2579. 2. THERE IS SOME UNKNOWN AND UNMODELLED DENSITY LOCATED    
REMARK   3  NEAR THE PHENOL RING OF THE ZMA LIGAND, WHICH LIKELY REPRESENT      
REMARK   3  AN ALTERNATIVE CONFORMATION OF THIS FLEXIBLE MOIETY. 3.             
REMARK   3  DISORDERED LIPIDS INCLUDING OLA-2417, OLA-2419, OLC-2423, OLC-      
REMARK   3  2427, OLC-2428 COULD REPRESENT FRAGMENTS OF PHOSPHOLIPID,           
REMARK   3  CHOLESTEROL OR 1-OLEOYL-RAC-GLYCEROL.                               
REMARK   4                                                                      
REMARK   4 4EIY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000071676.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-NOV-11; 10-DEC-11               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 55                                 
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : APS; APS                           
REMARK 200  BEAMLINE                       : 23-ID-D; 23-ID-D                   
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0330; 1.0330                     
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD; MARMOSAIC    
REMARK 200                                   300 MM CCD                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44413                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.730                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.81000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3EML                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25-28% (V/V) PEG 400, 0.04-0.06M         
REMARK 280  SODIUM THIOCYANATE, 2% (V/V) 2,5-HEXANEDIOL, 100MM SODIUM           
REMARK 280  CITRATE, PH 5.0, LIPID CUBIC PHASE (LCP), TEMPERATURE 293K          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
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                                         
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       70.15350            
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       70.15350            
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       19.72100            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       89.75800            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       19.72100            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       89.75800            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       70.15350            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       19.72100            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       89.75800            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       70.15350            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       19.72100            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       89.75800            
REMARK 290   SMTRY3   8  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 300 REMARK: THE SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED      
REMARK 300 BY THE TWO FOLD AXIS:-X,Y,-Z+1/2                                     
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   -24                                                      
REMARK 465     LYS A   -23                                                      
REMARK 465     THR A   -22                                                      
REMARK 465     ILE A   -21                                                      
REMARK 465     ILE A   -20                                                      
REMARK 465     ALA A   -19                                                      
REMARK 465     LEU A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     TYR A   -16                                                      
REMARK 465     ILE A   -15                                                      
REMARK 465     PHE A   -14                                                      
REMARK 465     CYS A   -13                                                      
REMARK 465     LEU A   -12                                                      
REMARK 465     VAL A   -11                                                      
REMARK 465     PHE A   -10                                                      
REMARK 465     ALA A    -9                                                      
REMARK 465     ASP A    -8                                                      
REMARK 465     TYR A    -7                                                      
REMARK 465     LYS A    -6                                                      
REMARK 465     ASP A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     ALA A  1043                                                      
REMARK 465     THR A  1044                                                      
REMARK 465     PRO A  1045                                                      
REMARK 465     PRO A  1046                                                      
REMARK 465     LYS A  1047                                                      
REMARK 465     LEU A  1048                                                      
REMARK 465     GLU A  1049                                                      
REMARK 465     ASP A  1050                                                      
REMARK 465     LYS A  1051                                                      
REMARK 465     SER A  1052                                                      
REMARK 465     PRO A  1053                                                      
REMARK 465     ASP A  1054                                                      
REMARK 465     SER A  1055                                                      
REMARK 465     PRO A  1056                                                      
REMARK 465     GLU A  1057                                                      
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     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 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     GLN A 148    OE1  NE2                                            
REMARK 470     GLU A 161    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1042    CD   CE   NZ                                        
REMARK 470     MET A1058    CG   SD   CE                                        
REMARK 470     LYS A1059    CG   CD   CE   NZ                                   
REMARK 470     ARG A 220    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 293    CZ   NH1  NH2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  58      -53.24   -122.64                                   
REMARK 500    TYR A1101      -54.84   -126.06                                   
REMARK 500    HIS A 306      -71.44   -106.63                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLA A 2407                                                       
REMARK 610     OLA A 2408                                                       
REMARK 610     OLA A 2409                                                       
REMARK 610     OLA A 2410                                                       
REMARK 610     OLA A 2411                                                       
REMARK 610     OLA A 2412                                                       
REMARK 610     OLA A 2413                                                       
REMARK 610     OLA A 2414                                                       
REMARK 610     OLA A 2415                                                       
REMARK 610     OLA A 2416                                                       
REMARK 610     OLA A 2419                                                       
REMARK 610     OLA A 2420                                                       
REMARK 610     OLA A 2421                                                       
REMARK 610     OLC A 2422                                                       
REMARK 610     OLC A 2423                                                       
REMARK 610     OLC A 2424                                                       
REMARK 610     OLC A 2425                                                       
REMARK 610     OLB A 2426                                                       
REMARK 610     OLC A 2427                                                       
REMARK 610     OLC A 2428                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A2402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  52   OD1                                                    
REMARK 620 2 SER A  91   OG  125.5                                              
REMARK 620 3 HOH A2529   O   107.1 122.9                                        
REMARK 620 4 HOH A2552   O    84.9 115.1  87.8                                  
REMARK 620 5 HOH A2579   O    78.1  72.1 102.0 162.2                            
REMARK 620 N                    1     2     3     4                             
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 2401                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 2402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLR A 2403                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLR A 2404                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLR A 2405                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2406                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2407                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2408                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2409                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2410                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2411                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2412                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2413                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2415                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2416                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2417                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2418                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2419                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2420                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 2421                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 2422                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 2423                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 2424                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 2425                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLB A 2426                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 2427                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 2428                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 2430                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3EML   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CHIMERIC PROTEIN OF A2AAR-T4L IN COMPLEX    
REMARK 900 WITH ZM241385                                                        
REMARK 900 RELATED ID: GPCR-6   RELATED DB: TARGETTRACK                         
DBREF  4EIY A    2   208  UNP    P29274   AA2AR_HUMAN      2    208             
DBREF  4EIY A 1001  1106  UNP    P0ABE7   C562_ECOLX      23    128             
DBREF  4EIY A  219   316  UNP    P29274   AA2AR_HUMAN    219    316             
SEQADV 4EIY MET A  -24  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY LYS A  -23  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY THR A  -22  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY ILE A  -21  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY ILE A  -20  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY ALA A  -19  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY LEU A  -18  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY SER A  -17  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY TYR A  -16  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY ILE A  -15  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY PHE A  -14  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY CYS A  -13  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY LEU A  -12  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY VAL A  -11  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY PHE A  -10  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY ALA A   -9  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY ASP A   -8  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY TYR A   -7  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY LYS A   -6  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY ASP A   -5  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY ASP A   -4  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY ASP A   -3  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY ASP A   -2  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY GLY A   -1  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY ALA A    0  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY PRO A    1  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY TRP A 1007  UNP  P0ABE7    MET    29 ENGINEERED MUTATION            
SEQADV 4EIY ILE A 1102  UNP  P0ABE7    HIS   124 ENGINEERED MUTATION            
SEQADV 4EIY LEU A 1106  UNP  P0ABE7    ARG   128 ENGINEERED MUTATION            
SEQADV 4EIY HIS A  317  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY HIS A  318  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY HIS A  319  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY HIS A  320  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY HIS A  321  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY HIS A  322  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY HIS A  323  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY HIS A  324  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY HIS A  325  UNP  P29274              EXPRESSION TAG                 
SEQADV 4EIY HIS A  326  UNP  P29274              EXPRESSION TAG                 
SEQRES   1 A  447  MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU          
SEQRES   2 A  447  VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO          
SEQRES   3 A  447  PRO ILE MET GLY SER SER VAL TYR ILE THR VAL GLU LEU          
SEQRES   4 A  447  ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL          
SEQRES   5 A  447  CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN ASN VAL          
SEQRES   6 A  447  THR ASN TYR PHE VAL VAL SER LEU ALA ALA ALA ASP ILE          
SEQRES   7 A  447  ALA VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE THR ILE          
SEQRES   8 A  447  SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE          
SEQRES   9 A  447  ILE ALA CYS PHE VAL LEU VAL LEU THR GLN SER SER ILE          
SEQRES  10 A  447  PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA          
SEQRES  11 A  447  ILE ARG ILE PRO LEU ARG TYR ASN GLY LEU VAL THR GLY          
SEQRES  12 A  447  THR ARG ALA LYS GLY ILE ILE ALA ILE CYS TRP VAL LEU          
SEQRES  13 A  447  SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY TRP ASN          
SEQRES  14 A  447  ASN CYS GLY GLN PRO LYS GLU GLY LYS ASN HIS SER GLN          
SEQRES  15 A  447  GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP          
SEQRES  16 A  447  VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN PHE PHE          
SEQRES  17 A  447  ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU GLY VAL          
SEQRES  18 A  447  TYR LEU ARG ILE PHE LEU ALA ALA ARG ARG GLN LEU ALA          
SEQRES  19 A  447  ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU          
SEQRES  20 A  447  LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS          
SEQRES  21 A  447  ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA          
SEQRES  22 A  447  GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO          
SEQRES  23 A  447  ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP          
SEQRES  24 A  447  ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA          
SEQRES  25 A  447  ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU          
SEQRES  26 A  447  GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR          
SEQRES  27 A  447  LEU GLU ARG ALA ARG SER THR LEU GLN LYS GLU VAL HIS          
SEQRES  28 A  447  ALA ALA LYS SER LEU ALA ILE ILE VAL GLY LEU PHE ALA          
SEQRES  29 A  447  LEU CYS TRP LEU PRO LEU HIS ILE ILE ASN CYS PHE THR          
SEQRES  30 A  447  PHE PHE CYS PRO ASP CYS SER HIS ALA PRO LEU TRP LEU          
SEQRES  31 A  447  MET TYR LEU ALA ILE VAL LEU SER HIS THR ASN SER VAL          
SEQRES  32 A  447  VAL ASN PRO PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE          
SEQRES  33 A  447  ARG GLN THR PHE ARG LYS ILE ILE ARG SER HIS VAL LEU          
SEQRES  34 A  447  ARG GLN GLN GLU PRO PHE LYS ALA HIS HIS HIS HIS HIS          
SEQRES  35 A  447  HIS HIS HIS HIS HIS                                          
HET    ZMA  A2401      25                                                       
HET     NA  A2402       1                                                       
HET    CLR  A2403      28                                                       
HET    CLR  A2404      28                                                       
HET    CLR  A2405      28                                                       
HET    OLA  A2406      20                                                       
HET    OLA  A2407      15                                                       
HET    OLA  A2408      11                                                       
HET    OLA  A2409      19                                                       
HET    OLA  A2410      11                                                       
HET    OLA  A2411       9                                                       
HET    OLA  A2412       8                                                       
HET    OLA  A2413      10                                                       
HET    OLA  A2414       9                                                       
HET    OLA  A2415      12                                                       
HET    OLA  A2416      18                                                       
HET    OLA  A2417      20                                                       
HET    OLA  A2418      20                                                       
HET    OLA  A2419      15                                                       
HET    OLA  A2420      15                                                       
HET    OLA  A2421      19                                                       
HET    OLC  A2422      17                                                       
HET    OLC  A2423      15                                                       
HET    OLC  A2424      22                                                       
HET    OLC  A2425      17                                                       
HET    OLB  A2426      18                                                       
HET    OLC  A2427      16                                                       
HET    OLC  A2428      21                                                       
HET    PEG  A2429       7                                                       
HET    PEG  A2430       7                                                       
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                               
HETNAM      NA SODIUM ION                                                       
HETNAM     CLR CHOLESTEROL                                                      
HETNAM     OLA OLEIC ACID                                                       
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     OLB (2S)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
FORMUL   2  ZMA    C16 H15 N7 O2                                                
FORMUL   3   NA    NA 1+                                                        
FORMUL   4  CLR    3(C27 H46 O)                                                 
FORMUL   7  OLA    16(C18 H34 O2)                                               
FORMUL  23  OLC    6(C21 H40 O4)                                                
FORMUL  27  OLB    C21 H40 O4                                                   
FORMUL  30  PEG    2(C4 H10 O3)                                                 
FORMUL  32  HOH   *177(H2 O)                                                    
HELIX    1   1 PRO A    1  ASN A   34  1                                  34    
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  THR A   68  1                                  11    
HELIX    5   5 CYS A   74  ILE A  108  1                                  35    
HELIX    6   6 ILE A  108  VAL A  116  1                                   9    
HELIX    7   7 THR A  117  LEU A  137  1                                  21    
HELIX    8   8 THR A  138  GLY A  142  5                                   5    
HELIX    9   9 LYS A  150  GLN A  157  1                                   8    
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 VAL A  186  LYS A 1019  1                                  42    
HELIX   13  13 ASN A 1022  LYS A 1042  1                                  21    
HELIX   14  14 LYS A 1059  GLU A 1081  1                                  23    
HELIX   15  15 LYS A 1083  GLN A 1093  1                                  11    
HELIX   16  16 GLN A 1093  TYR A 1101  1                                   9    
HELIX   17  17 TYR A 1101  CYS A  259  1                                  47    
HELIX   18  18 PRO A  266  ILE A  292  1                                  27    
HELIX   19  19 ILE A  292  HIS A  306  1                                  15    
SHEET    1   A 2 CYS A  71  ALA A  73  0                                        
SHEET    2   A 2 GLN A 163  ALA A 165 -1  O  VAL A 164   N  ALA A  72           
SSBOND   1 CYS A   71    CYS A  159                          1555   1555  2.10  
SSBOND   2 CYS A   74    CYS A  146                          1555   1555  2.03  
SSBOND   3 CYS A   77    CYS A  166                          1555   1555  2.00  
SSBOND   4 CYS A  259    CYS A  262                          1555   1555  2.05  
LINK         OD1 ASP A  52                NA    NA A2402     1555   1555  2.45  
LINK         OG  SER A  91                NA    NA A2402     1555   1555  2.54  
LINK        NA    NA A2402                 O   HOH A2529     1555   1555  2.44  
LINK        NA    NA A2402                 O   HOH A2552     1555   1555  2.20  
LINK        NA    NA A2402                 O   HOH A2579     1555   1555  2.60  
SITE     1 AC1 13 LEU A  85  PHE A 168  GLU A 169  MET A 177                    
SITE     2 AC1 13 TRP A 246  LEU A 249  HIS A 250  ASN A 253                    
SITE     3 AC1 13 MET A 270  HOH A2521  HOH A2524  HOH A2585                    
SITE     4 AC1 13 HOH A2668                                                     
SITE     1 AC2  5 ASP A  52  SER A  91  HOH A2529  HOH A2552                    
SITE     2 AC2  5 HOH A2579                                                     
SITE     1 AC3  7 ALA A  72  ALA A  73  GLY A  76  ILE A  80                    
SITE     2 AC3  7 CLR A2405  OLC A2424  OLC A2427                               
SITE     1 AC4  5 LEU A 247  PRO A 248  CYS A 262  SER A 263                    
SITE     2 AC4  5 OLA A2409                                                     
SITE     1 AC5  9 LEU A 187  CYS A 254  PHE A 255  PHE A 258                    
SITE     2 AC5  9 CLR A2403  OLA A2409  OLC A2424  OLC A2427                    
SITE     3 AC5  9 HOH A2603                                                     
SITE     1 AC6  5 THR A  65  THR A  68  OLA A2408  OLC A2424                    
SITE     2 AC6  5 HOH A2657                                                     
SITE     1 AC7  1 HIS A 264                                                     
SITE     1 AC8  3 ILE A  10  OLA A2406  OLA A2420                               
SITE     1 AC9  5 PHE A 255  CYS A 262  CLR A2404  CLR A2405                    
SITE     2 AC9  5 OLC A2424                                                     
SITE     1 BC1  4 ILE A   3  SER A   7  THR A  11  HOH A2667                    
SITE     1 BC2  3 PHE A  44  ALA A  97  HOH A2671                               
SITE     1 BC3  1 HOH A2611                                                     
SITE     1 BC4  3 LEU A 198  ARG A 199  LEU A 202                               
SITE     1 BC5  4 LEU A  19  LEU A  22  TRP A  29  VAL A 307                    
SITE     1 BC6  5 GLY A   5  SER A   6  TYR A 271  VAL A 275                    
SITE     2 BC6  5 HOH A2504                                                     
SITE     1 BC7  1 LEU A 192                                                     
SITE     1 BC8  3 PHE A 133  MET A 140  OLC A2425                               
SITE     1 BC9  2 TYR A 290  ARG A 291                                          
SITE     1 CC1  2 OLA A2408  HOH A2605                                          
SITE     1 CC2  4 TRP A  32  VAL A 229  LYS A 233  HOH A2673                    
SITE     1 CC3  6 TYR A 179  PHE A 258  OLC A2423  OLC A2425                    
SITE     2 CC3  6 OLC A2427  HOH A2600                                          
SITE     1 CC4  2 OLC A2422  OLC A2427                                          
SITE     1 CC5  9 PRO A  61  THR A  65  PHE A  70  CLR A2403                    
SITE     2 CC5  9 CLR A2405  OLA A2406  OLA A2409  HOH A2657                    
SITE     3 CC5  9 HOH A2674                                                     
SITE     1 CC6  6 MET A 140  LEU A 141  TYR A 179  ALA A 184                    
SITE     2 CC6  6 OLA A2418  OLC A2422                                          
SITE     1 CC7  4 CYS A  28  VAL A  31  TRP A  32  ARG A 205                    
SITE     1 CC8  5 PHE A 258  CLR A2403  CLR A2405  OLC A2422                    
SITE     2 CC8  5 OLC A2423                                                     
SITE     1 CC9  4 TYR A  43  VAL A  46  PHE A  83  TRP A 129                    
SITE     1 DC1  1 ARG A 120                                                     
CRYST1   39.442  179.516  140.307  90.00  90.00  90.00 C 2 2 21      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      0.025354  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005571  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007127        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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