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Database: PDB
Entry: 6Q60
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Original site: 6Q60 
HEADER    MEMBRANE PROTEIN                        10-DEC-18   6Q60              
TITLE     STRUCTURE OF GLUA2 LIGAND-BINDING DOMAIN (S1S2J) IN COMPLEX WITH THE  
TITLE    2 AGONIST (S)-2-AMINO-3-(2-METHYL-5-HYDROXY-2H-1,2,3-TRIAZOL-4-YL)     
TITLE    3 PROPANOIC ACID AT 1.55 A RESOLUTION                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMATE RECEPTOR 2;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GLUR-2,AMPA-SELECTIVE GLUTAMATE RECEPTOR 2,GLUR-B,GLUR-K2,  
COMPND   5 GLUTAMATE RECEPTOR IONOTROPIC,AMPA 2,GLUA2;                          
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: THE PROTEIN CRYSTALLIZED IS THE EXTRACELLULAR LIGAND- 
COMPND   8 BINDING DOMAIN OF GLUA2. TRANSMEMBRANE REGIONS WERE REPLACED WITH A  
COMPND   9 GLY-THR LINKER (118-119). SEQUENCE MATCHES DISCONTINOUSLY WITH THE   
COMPND  10 REFERENCE DATABASE (413-527, 653-797). RESIDUES 1-2 ARE CLONING      
COMPND  11 REMNANTS.                                                            
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: GRIA2, GLUR2;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: ORIGAMI B;                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
KEYWDS    AMPA RECEPTOR, GLUA2-S1S2, LIGAND BINDING DOMAIN, AGONIST, MEMBRANE   
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.MOELLERUD,P.TEMPERINI,J.S.KASTRUP                                   
REVDAT   2   22-MAY-19 6Q60    1       JRNL                                     
REVDAT   1   17-APR-19 6Q60    0                                                
JRNL        AUTH   S.SAINAS,P.TEMPERINI,J.C.FARNSWORTH,F.YI,S.MOLLERUD,         
JRNL        AUTH 2 A.A.JENSEN,B.NIELSEN,A.PASSONI,J.S.KASTRUP,K.B.HANSEN,       
JRNL        AUTH 3 D.BOSCHI,D.S.PICKERING,R.P.CLAUSEN,M.L.LOLLI                 
JRNL        TITL   USE OF THE 4-HYDROXYTRIAZOLE MOIETY AS A BIOISOSTERIC TOOL   
JRNL        TITL 2 IN THE DEVELOPMENT OF IONOTROPIC GLUTAMATE RECEPTOR LIGANDS. 
JRNL        REF    J.MED.CHEM.                   V.  62  4467 2019              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   30943028                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.8B01986                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.16                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.280                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 83371                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.149                           
REMARK   3   R VALUE            (WORKING SET) : 0.148                           
REMARK   3   FREE R VALUE                     : 0.175                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4173                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 44.1727 -  4.8142    0.99     2849   156  0.1780 0.1757        
REMARK   3     2  4.8142 -  3.8219    1.00     2738   151  0.1239 0.1487        
REMARK   3     3  3.8219 -  3.3390    1.00     2702   151  0.1379 0.1573        
REMARK   3     4  3.3390 -  3.0338    1.00     2673   161  0.1417 0.1520        
REMARK   3     5  3.0338 -  2.8164    1.00     2681   143  0.1465 0.1738        
REMARK   3     6  2.8164 -  2.6503    1.00     2680   131  0.1420 0.1873        
REMARK   3     7  2.6503 -  2.5176    1.00     2646   145  0.1418 0.1710        
REMARK   3     8  2.5176 -  2.4080    1.00     2666   141  0.1441 0.1805        
REMARK   3     9  2.4080 -  2.3153    1.00     2664   127  0.1343 0.1738        
REMARK   3    10  2.3153 -  2.2354    1.00     2640   140  0.1340 0.1666        
REMARK   3    11  2.2354 -  2.1655    1.00     2641   138  0.1332 0.1569        
REMARK   3    12  2.1655 -  2.1036    1.00     2646   134  0.1391 0.1602        
REMARK   3    13  2.1036 -  2.0483    1.00     2617   146  0.1405 0.1737        
REMARK   3    14  2.0483 -  1.9983    1.00     2611   160  0.1502 0.1884        
REMARK   3    15  1.9983 -  1.9529    1.00     2631   135  0.1534 0.1852        
REMARK   3    16  1.9529 -  1.9113    1.00     2620   144  0.1546 0.1972        
REMARK   3    17  1.9113 -  1.8731    1.00     2602   157  0.1559 0.2157        
REMARK   3    18  1.8731 -  1.8377    1.00     2638   131  0.1569 0.2093        
REMARK   3    19  1.8377 -  1.8049    1.00     2634   129  0.1592 0.1713        
REMARK   3    20  1.8049 -  1.7743    0.99     2598   131  0.1526 0.2056        
REMARK   3    21  1.7743 -  1.7457    0.99     2586   139  0.1524 0.1870        
REMARK   3    22  1.7457 -  1.7188    1.00     2644   140  0.1623 0.2064        
REMARK   3    23  1.7188 -  1.6935    0.99     2605   122  0.1745 0.1862        
REMARK   3    24  1.6935 -  1.6697    0.99     2587   158  0.1677 0.2207        
REMARK   3    25  1.6697 -  1.6471    0.99     2622   113  0.1723 0.2218        
REMARK   3    26  1.6471 -  1.6257    0.99     2580   144  0.1735 0.2367        
REMARK   3    27  1.6257 -  1.6054    0.99     2599   127  0.1886 0.1995        
REMARK   3    28  1.6054 -  1.5861    0.99     2570   132  0.1939 0.2059        
REMARK   3    29  1.5861 -  1.5676    0.99     2599   129  0.2000 0.2501        
REMARK   3    30  1.5676 -  1.5500    0.99     2629   118  0.2016 0.2296        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.140            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.270           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           4427                                  
REMARK   3   ANGLE     :  1.040           5973                                  
REMARK   3   CHIRALITY :  0.064            652                                  
REMARK   3   PLANARITY :  0.007            741                                  
REMARK   3   DIHEDRAL  : 14.687           2716                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 47 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  29.8353  20.7421 -32.9846              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1171 T22:   0.1086                                     
REMARK   3      T33:   0.1192 T12:   0.0017                                     
REMARK   3      T13:   0.0082 T23:  -0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2972 L22:   2.8936                                     
REMARK   3      L33:   2.1448 L12:   0.0430                                     
REMARK   3      L13:   0.0757 L23:  -0.4709                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0361 S12:   0.0199 S13:  -0.0767                       
REMARK   3      S21:  -0.1166 S22:   0.0345 S23:   0.0094                       
REMARK   3      S31:   0.1138 S32:  -0.0374 S33:  -0.0049                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 48 THROUGH 79 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  42.1295  29.4474 -39.0660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1171 T22:   0.1226                                     
REMARK   3      T33:   0.1222 T12:   0.0508                                     
REMARK   3      T13:   0.0265 T23:  -0.0063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7934 L22:   1.8778                                     
REMARK   3      L33:   2.9922 L12:   0.1885                                     
REMARK   3      L13:   0.7314 L23:   0.0807                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0105 S12:   0.1122 S13:  -0.0586                       
REMARK   3      S21:  -0.0846 S22:   0.0102 S23:  -0.2921                       
REMARK   3      S31:   0.1182 S32:   0.4049 S33:  -0.0207                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 80 THROUGH 123 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  38.5267  37.1569 -28.0792              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1165 T22:   0.1289                                     
REMARK   3      T33:   0.1493 T12:   0.0199                                     
REMARK   3      T13:   0.0154 T23:   0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4265 L22:   0.3273                                     
REMARK   3      L33:   2.2961 L12:   0.1124                                     
REMARK   3      L13:   0.0843 L23:  -0.2259                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0190 S12:  -0.0373 S13:   0.0226                       
REMARK   3      S21:  -0.0059 S22:  -0.0294 S23:   0.0001                       
REMARK   3      S31:  -0.0134 S32:   0.1240 S33:   0.0387                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 124 THROUGH 202 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  49.1637  37.3921 -18.4970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1114 T22:   0.2470                                     
REMARK   3      T33:   0.1493 T12:  -0.0084                                     
REMARK   3      T13:   0.0123 T23:   0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9450 L22:   2.9297                                     
REMARK   3      L33:   2.5785 L12:   0.3156                                     
REMARK   3      L13:  -0.0610 L23:  -0.6327                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0027 S12:  -0.0851 S13:   0.0310                       
REMARK   3      S21:  -0.0174 S22:  -0.0830 S23:  -0.2741                       
REMARK   3      S31:  -0.1073 S32:   0.5275 S33:   0.0527                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 203 THROUGH 217 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  38.4230  34.9326 -12.5154              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1302 T22:   0.1660                                     
REMARK   3      T33:   0.1697 T12:   0.0078                                     
REMARK   3      T13:   0.0340 T23:  -0.0163                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0512 L22:   5.8620                                     
REMARK   3      L33:   8.9477 L12:  -1.4255                                     
REMARK   3      L13:   1.0002 L23:  -6.2080                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0863 S12:  -0.1179 S13:  -0.0282                       
REMARK   3      S21:   0.1035 S22:  -0.0455 S23:   0.1389                       
REMARK   3      S31:   0.0697 S32:   0.0995 S33:   0.1341                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 218 THROUGH 243 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  27.1077  37.2395 -38.0450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1057 T22:   0.0534                                     
REMARK   3      T33:   0.1194 T12:   0.0051                                     
REMARK   3      T13:  -0.0074 T23:   0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7684 L22:   1.9225                                     
REMARK   3      L33:   5.9962 L12:  -0.9615                                     
REMARK   3      L13:  -1.4285 L23:   0.3644                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0073 S12:   0.2695 S13:   0.0192                       
REMARK   3      S21:  -0.1180 S22:  -0.0059 S23:   0.0283                       
REMARK   3      S31:  -0.0138 S32:  -0.1538 S33:   0.0152                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 244 THROUGH 264 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  24.3204  28.7416 -17.7927              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1841 T22:   0.1508                                     
REMARK   3      T33:   0.1608 T12:  -0.0063                                     
REMARK   3      T13:   0.0399 T23:  -0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9357 L22:   3.5932                                     
REMARK   3      L33:   8.9168 L12:  -2.5043                                     
REMARK   3      L13:   3.9615 L23:  -4.3489                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0802 S12:  -0.4430 S13:  -0.0387                       
REMARK   3      S21:   0.2195 S22:   0.2530 S23:   0.0829                       
REMARK   3      S31:   0.0638 S32:  -0.5510 S33:  -0.2020                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 47 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  29.6687  68.5266 -32.7952              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1245 T22:   0.0979                                     
REMARK   3      T33:   0.1367 T12:  -0.0092                                     
REMARK   3      T13:   0.0118 T23:  -0.0173                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6561 L22:   1.3440                                     
REMARK   3      L33:   1.7699 L12:  -0.0471                                     
REMARK   3      L13:  -0.3529 L23:  -0.3445                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0386 S12:  -0.0166 S13:   0.1032                       
REMARK   3      S21:  -0.0220 S22:   0.0012 S23:  -0.0664                       
REMARK   3      S31:  -0.1744 S32:   0.0806 S33:  -0.0554                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 48 THROUGH 79 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  17.1955  59.8525 -39.1715              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1351 T22:   0.1238                                     
REMARK   3      T33:   0.1461 T12:   0.0346                                     
REMARK   3      T13:  -0.0116 T23:   0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8271 L22:   1.3041                                     
REMARK   3      L33:   2.5950 L12:  -0.3100                                     
REMARK   3      L13:  -0.7074 L23:  -0.0850                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0662 S12:   0.1228 S13:   0.0378                       
REMARK   3      S21:  -0.1150 S22:   0.0094 S23:   0.1859                       
REMARK   3      S31:  -0.0653 S32:  -0.2978 S33:  -0.0735                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 80 THROUGH 123 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  20.6075  52.2307 -28.1751              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1078 T22:   0.1053                                     
REMARK   3      T33:   0.1342 T12:   0.0125                                     
REMARK   3      T13:  -0.0160 T23:  -0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2529 L22:   0.5864                                     
REMARK   3      L33:   1.9496 L12:   0.1095                                     
REMARK   3      L13:  -0.3964 L23:   0.1087                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0036 S12:  -0.0076 S13:  -0.0113                       
REMARK   3      S21:   0.0073 S22:   0.0100 S23:  -0.0142                       
REMARK   3      S31:   0.0006 S32:  -0.0081 S33:  -0.0078                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 124 THROUGH 152 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.2354  47.3713 -20.1519              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1001 T22:   0.1464                                     
REMARK   3      T33:   0.1896 T12:  -0.0290                                     
REMARK   3      T13:  -0.0232 T23:  -0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6060 L22:   4.6737                                     
REMARK   3      L33:   3.2724 L12:   0.6978                                     
REMARK   3      L13:  -1.0351 L23:   0.5315                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0930 S12:   0.0863 S13:  -0.0805                       
REMARK   3      S21:   0.0581 S22:  -0.0418 S23:   0.2701                       
REMARK   3      S31:   0.2746 S32:  -0.3044 S33:   0.0813                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 153 THROUGH 173 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.7144  49.8649 -21.2951              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1078 T22:   0.1764                                     
REMARK   3      T33:   0.2337 T12:  -0.0351                                     
REMARK   3      T13:  -0.0195 T23:   0.0151                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9408 L22:   2.3825                                     
REMARK   3      L33:   1.7168 L12:   0.3196                                     
REMARK   3      L13:  -0.4782 L23:   1.1656                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0472 S12:  -0.0055 S13:   0.0210                       
REMARK   3      S21:   0.0194 S22:  -0.0079 S23:   0.7041                       
REMARK   3      S31:   0.1118 S32:  -0.3329 S33:   0.0681                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 174 THROUGH 187 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.2783  61.8092 -13.2119              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1342 T22:   0.1306                                     
REMARK   3      T33:   0.1840 T12:   0.0129                                     
REMARK   3      T13:   0.0223 T23:  -0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6979 L22:   4.5784                                     
REMARK   3      L33:   5.2495 L12:   1.5183                                     
REMARK   3      L13:  -1.6215 L23:  -0.3113                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1220 S12:   0.0408 S13:   0.1806                       
REMARK   3      S21:   0.3482 S22:  -0.0767 S23:   0.4514                       
REMARK   3      S31:  -0.1945 S32:  -0.4246 S33:  -0.1206                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 188 THROUGH 263 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  27.8849  55.6825 -22.9390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1381 T22:   0.1361                                     
REMARK   3      T33:   0.1577 T12:   0.0056                                     
REMARK   3      T13:  -0.0146 T23:  -0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6420 L22:   0.5540                                     
REMARK   3      L33:   1.2993 L12:  -0.2716                                     
REMARK   3      L13:  -0.7469 L23:   0.4165                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0089 S12:  -0.0872 S13:   0.0523                       
REMARK   3      S21:   0.0297 S22:   0.0678 S23:  -0.0859                       
REMARK   3      S31:  -0.0011 S32:   0.1385 S33:  -0.0754                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND (RESID 1 THROUGH 20 OR RESID   
REMARK   3                          22 THROUGH 24 OR RESID 26 THROUGH 42 OR     
REMARK   3                          RESID 44 THROUGH 53 OR RESID 55 THROUGH     
REMARK   3                          76 OR RESID 78 THROUGH 106 OR RESID 108     
REMARK   3                          THROUGH 115 OR RESID 117 THROUGH 155 OR     
REMARK   3                          RESID 157 THROUGH 163 OR RESID 165          
REMARK   3                          THROUGH 200 OR RESID 203 THROUGH 209 OR     
REMARK   3                          RESID 211 THROUGH 221 OR RESID 223          
REMARK   3                          THROUGH 229 OR RESID 231 THROUGH 247 OR     
REMARK   3                          RESID 249 THROUGH 251 OR RESID 254          
REMARK   3                          THROUGH 263))                               
REMARK   3     SELECTION          : (CHAIN B AND (RESID 1 THROUGH 20 OR RESID   
REMARK   3                          22 THROUGH 24 OR RESID 26 THROUGH 42 OR     
REMARK   3                          RESID 44 THROUGH 53 OR RESID 55 THROUGH     
REMARK   3                          76 OR RESID 78 THROUGH 106 OR RESID 108     
REMARK   3                          THROUGH 115 OR RESID 117 THROUGH 155 OR     
REMARK   3                          RESID 157 THROUGH 163 OR RESID 165          
REMARK   3                          THROUGH 200 OR RESID 203 THROUGH 209 OR     
REMARK   3                          RESID 211 THROUGH 221 OR RESID 223          
REMARK   3                          THROUGH 229 OR RESID 231 THROUGH 247 OR     
REMARK   3                          RESID 249 THROUGH 251 OR RESID 254          
REMARK   3                          THROUGH 263))                               
REMARK   3     ATOM PAIRS NUMBER  : 2804                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6Q60 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-DEC-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200013304.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX IV                             
REMARK 200  BEAMLINE                       : BIOMAX                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979988                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.22                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 83759                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.150                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.36800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1M5B                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG4000, 0.1 M LITHIUM SULFATE,      
REMARK 280  0.1 M PHOSPHATE-CITRATE, PH 4.5, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 279K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       49.17200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.12700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.17200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       61.12700            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 737  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY B   264                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   HZ2  LYS A    52     O    HOH A   402              1.47            
REMARK 500  HH22  ARG A   182     O    HOH A   403              1.49            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 140       37.51     71.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 771        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH A 772        DISTANCE =  6.53 ANGSTROMS                       
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                              LI A 312  LI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  97   O                                                      
REMARK 620 2 GLU A  97   OE2 117.7                                              
REMARK 620 3 ILE A 100   O   104.0 109.7                                        
REMARK 620 4 HOH A 436   O   110.8 108.1 106.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              LI B 311  LI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  97   O                                                      
REMARK 620 2 GLU B  97   OE2 113.5                                              
REMARK 620 3 ILE B 100   O   104.3 114.9                                        
REMARK 620 4 HOH B 457   O   108.6 106.6 108.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HJH A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 309                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 310                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 311                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LI A 312                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HJH B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 309                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 310                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LI B 311                  
DBREF  6Q60 A    3   117  UNP    P19491   GRIA2_RAT      413    527             
DBREF  6Q60 A  120   264  UNP    P19491   GRIA2_RAT      653    797             
DBREF  6Q60 B    3   117  UNP    P19491   GRIA2_RAT      413    527             
DBREF  6Q60 B  120   264  UNP    P19491   GRIA2_RAT      653    797             
SEQADV 6Q60 GLY A    1  UNP  P19491              CLONING ARTIFACT               
SEQADV 6Q60 ALA A    2  UNP  P19491              CLONING ARTIFACT               
SEQADV 6Q60 GLY A  118  UNP  P19491              LINKER                         
SEQADV 6Q60 THR A  119  UNP  P19491              LINKER                         
SEQADV 6Q60 GLY B    1  UNP  P19491              CLONING ARTIFACT               
SEQADV 6Q60 ALA B    2  UNP  P19491              CLONING ARTIFACT               
SEQADV 6Q60 GLY B  118  UNP  P19491              LINKER                         
SEQADV 6Q60 THR B  119  UNP  P19491              LINKER                         
SEQRES   1 A  264  GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU          
SEQRES   2 A  264  SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU          
SEQRES   3 A  264  GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU          
SEQRES   4 A  264  ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS          
SEQRES   5 A  264  LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP          
SEQRES   6 A  264  ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU          
SEQRES   7 A  264  VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR          
SEQRES   8 A  264  ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS          
SEQRES   9 A  264  PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS          
SEQRES  10 A  264  GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN          
SEQRES  11 A  264  THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR          
SEQRES  12 A  264  LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP          
SEQRES  13 A  264  LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL          
SEQRES  14 A  264  PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG          
SEQRES  15 A  264  LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR          
SEQRES  16 A  264  MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR          
SEQRES  17 A  264  MET LYS VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY          
SEQRES  18 A  264  ILE ALA THR PRO LYS GLY SER SER LEU GLY ASN ALA VAL          
SEQRES  19 A  264  ASN LEU ALA VAL LEU LYS LEU ASN GLU GLN GLY LEU LEU          
SEQRES  20 A  264  ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU          
SEQRES  21 A  264  CYS GLY SER GLY                                              
SEQRES   1 B  264  GLY ALA ASN LYS THR VAL VAL VAL THR THR ILE LEU GLU          
SEQRES   2 B  264  SER PRO TYR VAL MET MET LYS LYS ASN HIS GLU MET LEU          
SEQRES   3 B  264  GLU GLY ASN GLU ARG TYR GLU GLY TYR CYS VAL ASP LEU          
SEQRES   4 B  264  ALA ALA GLU ILE ALA LYS HIS CYS GLY PHE LYS TYR LYS          
SEQRES   5 B  264  LEU THR ILE VAL GLY ASP GLY LYS TYR GLY ALA ARG ASP          
SEQRES   6 B  264  ALA ASP THR LYS ILE TRP ASN GLY MET VAL GLY GLU LEU          
SEQRES   7 B  264  VAL TYR GLY LYS ALA ASP ILE ALA ILE ALA PRO LEU THR          
SEQRES   8 B  264  ILE THR LEU VAL ARG GLU GLU VAL ILE ASP PHE SER LYS          
SEQRES   9 B  264  PRO PHE MET SER LEU GLY ILE SER ILE MET ILE LYS LYS          
SEQRES  10 B  264  GLY THR PRO ILE GLU SER ALA GLU ASP LEU SER LYS GLN          
SEQRES  11 B  264  THR GLU ILE ALA TYR GLY THR LEU ASP SER GLY SER THR          
SEQRES  12 B  264  LYS GLU PHE PHE ARG ARG SER LYS ILE ALA VAL PHE ASP          
SEQRES  13 B  264  LYS MET TRP THR TYR MET ARG SER ALA GLU PRO SER VAL          
SEQRES  14 B  264  PHE VAL ARG THR THR ALA GLU GLY VAL ALA ARG VAL ARG          
SEQRES  15 B  264  LYS SER LYS GLY LYS TYR ALA TYR LEU LEU GLU SER THR          
SEQRES  16 B  264  MET ASN GLU TYR ILE GLU GLN ARG LYS PRO CYS ASP THR          
SEQRES  17 B  264  MET LYS VAL GLY GLY ASN LEU ASP SER LYS GLY TYR GLY          
SEQRES  18 B  264  ILE ALA THR PRO LYS GLY SER SER LEU GLY ASN ALA VAL          
SEQRES  19 B  264  ASN LEU ALA VAL LEU LYS LEU ASN GLU GLN GLY LEU LEU          
SEQRES  20 B  264  ASP LYS LEU LYS ASN LYS TRP TRP TYR ASP LYS GLY GLU          
SEQRES  21 B  264  CYS GLY SER GLY                                              
HET    HJH  A 301      22                                                       
HET    SO4  A 302       5                                                       
HET    SO4  A 303       5                                                       
HET    GOL  A 304      14                                                       
HET    GOL  A 305      14                                                       
HET    GOL  A 306      14                                                       
HET    GOL  A 307      14                                                       
HET    GOL  A 308      14                                                       
HET    GOL  A 309      13                                                       
HET     CL  A 310       1                                                       
HET     CL  A 311       1                                                       
HET     LI  A 312       1                                                       
HET    HJH  B 301      22                                                       
HET    SO4  B 302       5                                                       
HET    SO4  B 303       5                                                       
HET    GOL  B 304      14                                                       
HET    GOL  B 305      14                                                       
HET    GOL  B 306      14                                                       
HET    GOL  B 307      14                                                       
HET    GOL  B 308      14                                                       
HET    GOL  B 309      14                                                       
HET     CL  B 310       1                                                       
HET     LI  B 311       1                                                       
HETNAM     HJH (2~{S})-2-AZANYL-3-(2-METHYL-5-OXIDANYL-1,2,3-TRIAZOL-           
HETNAM   2 HJH  4-YL)PROPANOIC ACID                                             
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM      LI LITHIUM ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  HJH    2(C6 H10 N4 O3)                                              
FORMUL   4  SO4    4(O4 S 2-)                                                   
FORMUL   6  GOL    12(C3 H8 O3)                                                 
FORMUL  12   CL    3(CL 1-)                                                     
FORMUL  14   LI    2(LI 1+)                                                     
FORMUL  26  HOH   *735(H2 O)                                                    
HELIX    1 AA1 ASN A   22  LEU A   26  5                                   5    
HELIX    2 AA2 GLU A   27  GLU A   30  5                                   4    
HELIX    3 AA3 GLY A   34  GLY A   48  1                                  15    
HELIX    4 AA4 ASN A   72  TYR A   80  1                                   9    
HELIX    5 AA5 THR A   93  GLU A   98  1                                   6    
HELIX    6 AA6 SER A  123  LYS A  129  1                                   7    
HELIX    7 AA7 GLY A  141  SER A  150  1                                  10    
HELIX    8 AA8 ILE A  152  ALA A  165  1                                  14    
HELIX    9 AA9 THR A  173  SER A  184  1                                  12    
HELIX   10 AB1 SER A  194  GLN A  202  1                                   9    
HELIX   11 AB2 LEU A  230  GLN A  244  1                                  15    
HELIX   12 AB3 GLY A  245  TRP A  255  1                                  11    
HELIX   13 AB4 ASN B   22  LEU B   26  5                                   5    
HELIX   14 AB5 GLU B   27  GLU B   30  5                                   4    
HELIX   15 AB6 GLY B   34  GLY B   48  1                                  15    
HELIX   16 AB7 ASN B   72  TYR B   80  1                                   9    
HELIX   17 AB8 THR B   93  GLU B   98  1                                   6    
HELIX   18 AB9 SER B  123  LYS B  129  1                                   7    
HELIX   19 AC1 GLY B  141  SER B  150  1                                  10    
HELIX   20 AC2 ILE B  152  ALA B  165  1                                  14    
HELIX   21 AC3 THR B  173  SER B  184  1                                  12    
HELIX   22 AC4 SER B  194  GLN B  202  1                                   9    
HELIX   23 AC5 LEU B  230  GLN B  244  1                                  15    
HELIX   24 AC6 GLY B  245  TYR B  256  1                                  12    
SHEET    1 AA1 3 LYS A  50  ILE A  55  0                                        
SHEET    2 AA1 3 THR A   5  THR A  10  1  N  VAL A   6   O  LYS A  50           
SHEET    3 AA1 3 ILE A  85  ALA A  86  1  O  ILE A  85   N  THR A   9           
SHEET    1 AA2 2 MET A  18  MET A  19  0                                        
SHEET    2 AA2 2 TYR A  32  GLU A  33 -1  O  GLU A  33   N  MET A  18           
SHEET    1 AA3 2 ILE A 100  PHE A 102  0                                        
SHEET    2 AA3 2 ALA A 223  PRO A 225 -1  O  THR A 224   N  ASP A 101           
SHEET    1 AA4 2 MET A 107  LEU A 109  0                                        
SHEET    2 AA4 2 LYS A 218  TYR A 220 -1  O  LYS A 218   N  LEU A 109           
SHEET    1 AA5 4 ALA A 134  THR A 137  0                                        
SHEET    2 AA5 4 TYR A 188  GLU A 193  1  O  LEU A 191   N  GLY A 136           
SHEET    3 AA5 4 ILE A 111  LYS A 116 -1  N  MET A 114   O  TYR A 190           
SHEET    4 AA5 4 THR A 208  VAL A 211 -1  O  MET A 209   N  ILE A 115           
SHEET    1 AA6 3 TYR B  51  ILE B  55  0                                        
SHEET    2 AA6 3 VAL B   6  THR B  10  1  N  VAL B   8   O  THR B  54           
SHEET    3 AA6 3 ILE B  85  ALA B  86  1  O  ILE B  85   N  THR B   9           
SHEET    1 AA7 2 MET B  18  MET B  19  0                                        
SHEET    2 AA7 2 TYR B  32  GLU B  33 -1  O  GLU B  33   N  MET B  18           
SHEET    1 AA8 2 ILE B 100  PHE B 102  0                                        
SHEET    2 AA8 2 ALA B 223  PRO B 225 -1  O  THR B 224   N  ASP B 101           
SHEET    1 AA9 2 MET B 107  LEU B 109  0                                        
SHEET    2 AA9 2 LYS B 218  TYR B 220 -1  O  LYS B 218   N  LEU B 109           
SHEET    1 AB1 4 ALA B 134  THR B 137  0                                        
SHEET    2 AB1 4 TYR B 188  GLU B 193  1  O  LEU B 191   N  GLY B 136           
SHEET    3 AB1 4 ILE B 111  LYS B 116 -1  N  MET B 114   O  TYR B 190           
SHEET    4 AB1 4 THR B 208  VAL B 211 -1  O  MET B 209   N  ILE B 115           
SSBOND   1 CYS A  206    CYS A  261                          1555   1555  1.98  
SSBOND   2 CYS B  206    CYS B  261                          1555   1555  2.04  
LINK         O   GLU A  97                LI    LI A 312     1555   1555  1.90  
LINK         OE2 GLU A  97                LI    LI A 312     1555   1555  1.92  
LINK         O   ILE A 100                LI    LI A 312     1555   1555  1.95  
LINK         O   GLU B  97                LI    LI B 311     1555   1555  1.92  
LINK         OE2 GLU B  97                LI    LI B 311     1555   1555  1.96  
LINK         O   ILE B 100                LI    LI B 311     1555   1555  1.87  
LINK        LI    LI A 312                 O   HOH A 436     1555   1555  1.93  
LINK        LI    LI B 311                 O   HOH B 457     1555   1555  1.92  
CISPEP   1 SER A   14    PRO A   15          0         2.08                     
CISPEP   2 GLU A  166    PRO A  167          0        -4.89                     
CISPEP   3 LYS A  204    PRO A  205          0         4.85                     
CISPEP   4 SER B   14    PRO B   15          0         2.95                     
CISPEP   5 GLU B  166    PRO B  167          0        -5.17                     
CISPEP   6 LYS B  204    PRO B  205          0         3.34                     
SITE     1 AC1 14 TYR A  61  PRO A  89  THR A  91  ARG A  96                    
SITE     2 AC1 14 GLY A 141  SER A 142  THR A 143  LEU A 192                    
SITE     3 AC1 14 GLU A 193  MET A 196  TYR A 220  HOH A 413                    
SITE     4 AC1 14 HOH A 540  HOH A 542                                          
SITE     1 AC2  7 SER A 140  LYS A 144  ARG A 148  HOH A 407                    
SITE     2 AC2  7 HOH A 418  HOH A 470  HOH A 566                               
SITE     1 AC3  6 ARG A  31  HOH A 409  HOH A 444  HOH A 463                    
SITE     2 AC3  6 HOH A 594  LYS B 183                                          
SITE     1 AC4  7 ASP A 248  HOH A 458  HOH A 571  HOH A 626                    
SITE     2 AC4  7 ASN B 214  ASP B 216  SER B 217                               
SITE     1 AC5  5 SER A 194  THR A 195  GLU A 198  ASN A 214                    
SITE     2 AC5  5 HOH A 401                                                     
SITE     1 AC6  9 ILE A 113  SER A 123  ALA A 124  GLY A 212                    
SITE     2 AC6  9 GLY A 213  LEU A 215  HOH A 434  HOH A 489                    
SITE     3 AC6  9 HOH A 638                                                     
SITE     1 AC7  4 ARG A 148  TRP A 159  ARG A 163  HOH A 584                    
SITE     1 AC8  6 GLU A  97  ASP A 101  PHE A 102  HOH A 436                    
SITE     2 AC8  6 HOH A 500  LYS B 104                                          
SITE     1 AC9  5 ASN A 214  ASP A 216  SER A 217  HOH A 551                    
SITE     2 AC9  5 ASP B 248                                                     
SITE     1 AD1  2 ASN A  22  HOH A 744                                          
SITE     1 AD2  1 ALA A 153                                                     
SITE     1 AD3  3 GLU A  97  ILE A 100  HOH A 436                               
SITE     1 AD4 13 TYR B  61  PRO B  89  LEU B  90  THR B  91                    
SITE     2 AD4 13 ARG B  96  GLY B 141  SER B 142  THR B 143                    
SITE     3 AD4 13 GLU B 193  MET B 196  HOH B 412  HOH B 514                    
SITE     4 AD4 13 HOH B 526                                                     
SITE     1 AD5  5 LYS B  82  LYS B 116  HOH B 407  HOH B 515                    
SITE     2 AD5  5 HOH B 539                                                     
SITE     1 AD6  7 SER B 140  LYS B 144  ARG B 148  HOH B 406                    
SITE     2 AD6  7 HOH B 476  HOH B 536  HOH B 620                               
SITE     1 AD7  5 LYS A 258  MET B  19  HIS B  23  HOH B 458                    
SITE     2 AD7  5 HOH B 566                                                     
SITE     1 AD8  5 ASN A   3  HOH A 648  ARG B  31  LYS B  52                    
SITE     2 AD8  5 HOH B 410                                                     
SITE     1 AD9  8 LYS A 104  GLU B  97  ASP B 101  PHE B 102                    
SITE     2 AD9  8  LI B 311  HOH B 440  HOH B 457  HOH B 628                    
SITE     1 AE1  4 HIS B  46  LYS B 240  GLN B 244  HOH B 610                    
SITE     1 AE2  3 ARG B 148  TRP B 159  ARG B 163                               
SITE     1 AE3  8 LEU A  94  GLU A  98  HIS B  46  LEU B 236                    
SITE     2 AE3  8 ALA B 237  LYS B 240  HOH B 401  HOH B 610                    
SITE     1 AE4  2 LYS B   4  THR B   5                                          
SITE     1 AE5  5 GLU B  97  ILE B 100  ASP B 101  GOL B 306                    
SITE     2 AE5  5 HOH B 457                                                     
CRYST1   98.344  122.254   47.351  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010168  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008180  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021119        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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